data_9BM7
# 
_entry.id   9BM7 
# 
_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   9BM7         pdb_00009bm7 10.2210/pdb9bm7/pdb 
WWPDB D_1000283521 ?            ?                   
EMDB  EMD-44690    ?            ?                   
# 
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 ? 
11 'Structure model' 1 2 2025-05-14 ? 
12 'EM metadata'     1 1 2025-05-14 ? 
# 
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'  
3 11 'Structure model' 'Data collection'      
4 12 'EM metadata'     'Data processing'      
5 12 'EM metadata'     'Experimental summary' 
# 
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        
4 11 'Structure model' em_admin        
5 11 'Structure model' em_software     
6 12 'EM metadata'     em_admin        
7 12 'EM metadata'     em_software     
# 
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'             
10 11 'Structure model' '_em_admin.last_update'             
11 11 'Structure model' '_em_software.name'                 
12 12 'EM metadata'     '_em_admin.last_update'             
13 12 'EM metadata'     '_em_software.name'                 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BM7 
_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-7b of motor domain from full-length human dynein-1 in 5 mM ATP' 
_pdbx_database_related.db_id          EMD-44690 
_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 ?    ?   ?   A . n 
A 1 1328 ASP 1328 1328 ?    ?   ?   A . n 
A 1 1329 LEU 1329 1329 ?    ?   ?   A . n 
A 1 1330 LYS 1330 1330 ?    ?   ?   A . n 
A 1 1331 GLY 1331 1331 ?    ?   ?   A . n 
A 1 1332 VAL 1332 1332 ?    ?   ?   A . n 
A 1 1333 TRP 1333 1333 ?    ?   ?   A . n 
A 1 1334 SER 1334 1334 ?    ?   ?   A . n 
A 1 1335 GLU 1335 1335 ?    ?   ?   A . n 
A 1 1336 LEU 1336 1336 ?    ?   ?   A . n 
A 1 1337 SER 1337 1337 ?    ?   ?   A . n 
A 1 1338 LYS 1338 1338 ?    ?   ?   A . n 
A 1 1339 VAL 1339 1339 ?    ?   ?   A . n 
A 1 1340 TRP 1340 1340 ?    ?   ?   A . n 
A 1 1341 GLU 1341 1341 ?    ?   ?   A . n 
A 1 1342 GLN 1342 1342 ?    ?   ?   A . n 
A 1 1343 ILE 1343 1343 ?    ?   ?   A . n 
A 1 1344 ASP 1344 1344 ?    ?   ?   A . n 
A 1 1345 GLN 1345 1345 ?    ?   ?   A . n 
A 1 1346 MET 1346 1346 ?    ?   ?   A . n 
A 1 1347 LYS 1347 1347 ?    ?   ?   A . n 
A 1 1348 GLU 1348 1348 ?    ?   ?   A . n 
A 1 1349 GLN 1349 1349 ?    ?   ?   A . n 
A 1 1350 PRO 1350 1350 ?    ?   ?   A . n 
A 1 1351 TRP 1351 1351 ?    ?   ?   A . n 
A 1 1352 VAL 1352 1352 ?    ?   ?   A . n 
A 1 1353 SER 1353 1353 ?    ?   ?   A . n 
A 1 1354 VAL 1354 1354 ?    ?   ?   A . n 
A 1 1355 GLN 1355 1355 ?    ?   ?   A . n 
A 1 1356 PRO 1356 1356 ?    ?   ?   A . n 
A 1 1357 ARG 1357 1357 ?    ?   ?   A . n 
A 1 1358 LYS 1358 1358 ?    ?   ?   A . n 
A 1 1359 LEU 1359 1359 ?    ?   ?   A . n 
A 1 1360 ARG 1360 1360 ?    ?   ?   A . n 
A 1 1361 GLN 1361 1361 ?    ?   ?   A . n 
A 1 1362 ASN 1362 1362 ?    ?   ?   A . n 
A 1 1363 LEU 1363 1363 ?    ?   ?   A . n 
A 1 1364 ASP 1364 1364 ?    ?   ?   A . n 
A 1 1365 ALA 1365 1365 ?    ?   ?   A . n 
A 1 1366 LEU 1366 1366 ?    ?   ?   A . n 
A 1 1367 LEU 1367 1367 ?    ?   ?   A . n 
A 1 1368 ASN 1368 1368 ?    ?   ?   A . n 
A 1 1369 GLN 1369 1369 ?    ?   ?   A . n 
A 1 1370 LEU 1370 1370 ?    ?   ?   A . n 
A 1 1371 LYS 1371 1371 ?    ?   ?   A . n 
A 1 1372 SER 1372 1372 ?    ?   ?   A . n 
A 1 1373 PHE 1373 1373 ?    ?   ?   A . n 
A 1 1374 PRO 1374 1374 ?    ?   ?   A . n 
A 1 1375 ALA 1375 1375 ?    ?   ?   A . n 
A 1 1376 ARG 1376 1376 ?    ?   ?   A . n 
A 1 1377 LEU 1377 1377 ?    ?   ?   A . n 
A 1 1378 ARG 1378 1378 ?    ?   ?   A . n 
A 1 1379 GLN 1379 1379 ?    ?   ?   A . n 
A 1 1380 TYR 1380 1380 ?    ?   ?   A . n 
A 1 1381 ALA 1381 1381 ?    ?   ?   A . n 
A 1 1382 SER 1382 1382 ?    ?   ?   A . n 
A 1 1383 TYR 1383 1383 ?    ?   ?   A . n 
A 1 1384 GLU 1384 1384 ?    ?   ?   A . n 
A 1 1385 PHE 1385 1385 ?    ?   ?   A . n 
A 1 1386 VAL 1386 1386 ?    ?   ?   A . n 
A 1 1387 GLN 1387 1387 ?    ?   ?   A . n 
A 1 1388 ARG 1388 1388 ?    ?   ?   A . n 
A 1 1389 LEU 1389 1389 ?    ?   ?   A . n 
A 1 1390 LEU 1390 1390 ?    ?   ?   A . n 
A 1 1391 LYS 1391 1391 ?    ?   ?   A . n 
A 1 1392 GLY 1392 1392 ?    ?   ?   A . n 
A 1 1393 TYR 1393 1393 ?    ?   ?   A . n 
A 1 1394 MET 1394 1394 ?    ?   ?   A . n 
A 1 1395 LYS 1395 1395 ?    ?   ?   A . n 
A 1 1396 ILE 1396 1396 ?    ?   ?   A . n 
A 1 1397 ASN 1397 1397 ?    ?   ?   A . n 
A 1 1398 MET 1398 1398 ?    ?   ?   A . n 
A 1 1399 LEU 1399 1399 ?    ?   ?   A . n 
A 1 1400 VAL 1400 1400 ?    ?   ?   A . n 
A 1 1401 ILE 1401 1401 ?    ?   ?   A . n 
A 1 1402 GLU 1402 1402 ?    ?   ?   A . n 
A 1 1403 LEU 1403 1403 ?    ?   ?   A . n 
A 1 1404 LYS 1404 1404 ?    ?   ?   A . n 
A 1 1405 SER 1405 1405 ?    ?   ?   A . n 
A 1 1406 GLU 1406 1406 ?    ?   ?   A . n 
A 1 1407 ALA 1407 1407 ?    ?   ?   A . n 
A 1 1408 LEU 1408 1408 ?    ?   ?   A . n 
A 1 1409 LYS 1409 1409 ?    ?   ?   A . n 
A 1 1410 ASP 1410 1410 ?    ?   ?   A . n 
A 1 1411 ARG 1411 1411 ?    ?   ?   A . n 
A 1 1412 HIS 1412 1412 ?    ?   ?   A . n 
A 1 1413 TRP 1413 1413 ?    ?   ?   A . n 
A 1 1414 LYS 1414 1414 ?    ?   ?   A . n 
A 1 1415 GLN 1415 1415 ?    ?   ?   A . n 
A 1 1416 LEU 1416 1416 ?    ?   ?   A . n 
A 1 1417 MET 1417 1417 ?    ?   ?   A . n 
A 1 1418 LYS 1418 1418 ?    ?   ?   A . n 
A 1 1419 ARG 1419 1419 ?    ?   ?   A . n 
A 1 1420 LEU 1420 1420 ?    ?   ?   A . n 
A 1 1421 HIS 1421 1421 ?    ?   ?   A . n 
A 1 1422 VAL 1422 1422 ?    ?   ?   A . n 
A 1 1423 ASN 1423 1423 ?    ?   ?   A . n 
A 1 1424 TRP 1424 1424 ?    ?   ?   A . n 
A 1 1425 VAL 1425 1425 ?    ?   ?   A . n 
A 1 1426 VAL 1426 1426 ?    ?   ?   A . n 
A 1 1427 SER 1427 1427 ?    ?   ?   A . n 
A 1 1428 GLU 1428 1428 ?    ?   ?   A . n 
A 1 1429 LEU 1429 1429 ?    ?   ?   A . n 
A 1 1430 THR 1430 1430 ?    ?   ?   A . n 
A 1 1431 LEU 1431 1431 ?    ?   ?   A . n 
A 1 1432 GLY 1432 1432 ?    ?   ?   A . n 
A 1 1433 GLN 1433 1433 ?    ?   ?   A . n 
A 1 1434 ILE 1434 1434 ?    ?   ?   A . n 
A 1 1435 TRP 1435 1435 ?    ?   ?   A . n 
A 1 1436 ASP 1436 1436 ?    ?   ?   A . n 
A 1 1437 VAL 1437 1437 ?    ?   ?   A . n 
A 1 1438 ASP 1438 1438 ?    ?   ?   A . n 
A 1 1439 LEU 1439 1439 ?    ?   ?   A . n 
A 1 1440 GLN 1440 1440 ?    ?   ?   A . n 
A 1 1441 LYS 1441 1441 ?    ?   ?   A . n 
A 1 1442 ASN 1442 1442 ?    ?   ?   A . n 
A 1 1443 GLU 1443 1443 ?    ?   ?   A . n 
A 1 1444 ALA 1444 1444 ?    ?   ?   A . n 
A 1 1445 ILE 1445 1445 ?    ?   ?   A . n 
A 1 1446 VAL 1446 1446 ?    ?   ?   A . n 
A 1 1447 LYS 1447 1447 ?    ?   ?   A . n 
A 1 1448 ASP 1448 1448 ?    ?   ?   A . n 
A 1 1449 VAL 1449 1449 ?    ?   ?   A . n 
A 1 1450 LEU 1450 1450 ?    ?   ?   A . n 
A 1 1451 LEU 1451 1451 ?    ?   ?   A . n 
A 1 1452 VAL 1452 1452 ?    ?   ?   A . n 
A 1 1453 ALA 1453 1453 ?    ?   ?   A . n 
A 1 1454 GLN 1454 1454 ?    ?   ?   A . n 
A 1 1455 GLY 1455 1455 ?    ?   ?   A . n 
A 1 1456 GLU 1456 1456 ?    ?   ?   A . n 
A 1 1457 MET 1457 1457 ?    ?   ?   A . n 
A 1 1458 ALA 1458 1458 ?    ?   ?   A . n 
A 1 1459 LEU 1459 1459 ?    ?   ?   A . n 
A 1 1460 GLU 1460 1460 ?    ?   ?   A . n 
A 1 1461 GLU 1461 1461 ?    ?   ?   A . n 
A 1 1462 PHE 1462 1462 ?    ?   ?   A . n 
A 1 1463 LEU 1463 1463 ?    ?   ?   A . n 
A 1 1464 LYS 1464 1464 ?    ?   ?   A . n 
A 1 1465 GLN 1465 1465 ?    ?   ?   A . n 
A 1 1466 ILE 1466 1466 ?    ?   ?   A . n 
A 1 1467 ARG 1467 1467 ?    ?   ?   A . n 
A 1 1468 GLU 1468 1468 ?    ?   ?   A . n 
A 1 1469 VAL 1469 1469 ?    ?   ?   A . n 
A 1 1470 TRP 1470 1470 ?    ?   ?   A . n 
A 1 1471 ASN 1471 1471 ?    ?   ?   A . n 
A 1 1472 THR 1472 1472 ?    ?   ?   A . n 
A 1 1473 TYR 1473 1473 ?    ?   ?   A . n 
A 1 1474 GLU 1474 1474 ?    ?   ?   A . n 
A 1 1475 LEU 1475 1475 ?    ?   ?   A . n 
A 1 1476 ASP 1476 1476 ?    ?   ?   A . n 
A 1 1477 LEU 1477 1477 ?    ?   ?   A . n 
A 1 1478 VAL 1478 1478 ?    ?   ?   A . n 
A 1 1479 ASN 1479 1479 ?    ?   ?   A . n 
A 1 1480 TYR 1480 1480 ?    ?   ?   A . n 
A 1 1481 GLN 1481 1481 ?    ?   ?   A . n 
A 1 1482 ASN 1482 1482 ?    ?   ?   A . n 
A 1 1483 LYS 1483 1483 ?    ?   ?   A . n 
A 1 1484 CYS 1484 1484 ?    ?   ?   A . n 
A 1 1485 ARG 1485 1485 ?    ?   ?   A . n 
A 1 1486 LEU 1486 1486 ?    ?   ?   A . n 
A 1 1487 ILE 1487 1487 ?    ?   ?   A . n 
A 1 1488 ARG 1488 1488 ?    ?   ?   A . n 
A 1 1489 GLY 1489 1489 ?    ?   ?   A . n 
A 1 1490 TRP 1490 1490 ?    ?   ?   A . n 
A 1 1491 ASP 1491 1491 ?    ?   ?   A . n 
A 1 1492 ASP 1492 1492 ?    ?   ?   A . n 
A 1 1493 LEU 1493 1493 ?    ?   ?   A . n 
A 1 1494 PHE 1494 1494 ?    ?   ?   A . n 
A 1 1495 ASN 1495 1495 ?    ?   ?   A . n 
A 1 1496 LYS 1496 1496 ?    ?   ?   A . n 
A 1 1497 VAL 1497 1497 ?    ?   ?   A . n 
A 1 1498 LYS 1498 1498 ?    ?   ?   A . n 
A 1 1499 GLU 1499 1499 ?    ?   ?   A . n 
A 1 1500 HIS 1500 1500 ?    ?   ?   A . n 
A 1 1501 ILE 1501 1501 ?    ?   ?   A . n 
A 1 1502 ASN 1502 1502 ?    ?   ?   A . n 
A 1 1503 SER 1503 1503 ?    ?   ?   A . n 
A 1 1504 VAL 1504 1504 ?    ?   ?   A . n 
A 1 1505 SER 1505 1505 ?    ?   ?   A . n 
A 1 1506 ALA 1506 1506 ?    ?   ?   A . n 
A 1 1507 MET 1507 1507 ?    ?   ?   A . n 
A 1 1508 LYS 1508 1508 ?    ?   ?   A . n 
A 1 1509 LEU 1509 1509 ?    ?   ?   A . n 
A 1 1510 SER 1510 1510 ?    ?   ?   A . n 
A 1 1511 PRO 1511 1511 ?    ?   ?   A . n 
A 1 1512 TYR 1512 1512 ?    ?   ?   A . n 
A 1 1513 TYR 1513 1513 ?    ?   ?   A . n 
A 1 1514 LYS 1514 1514 ?    ?   ?   A . n 
A 1 1515 VAL 1515 1515 ?    ?   ?   A . n 
A 1 1516 PHE 1516 1516 ?    ?   ?   A . n 
A 1 1517 GLU 1517 1517 ?    ?   ?   A . n 
A 1 1518 GLU 1518 1518 ?    ?   ?   A . n 
A 1 1519 ASP 1519 1519 ?    ?   ?   A . n 
A 1 1520 ALA 1520 1520 ?    ?   ?   A . n 
A 1 1521 LEU 1521 1521 ?    ?   ?   A . n 
A 1 1522 SER 1522 1522 ?    ?   ?   A . n 
A 1 1523 TRP 1523 1523 ?    ?   ?   A . n 
A 1 1524 GLU 1524 1524 ?    ?   ?   A . n 
A 1 1525 ASP 1525 1525 ?    ?   ?   A . n 
A 1 1526 LYS 1526 1526 ?    ?   ?   A . n 
A 1 1527 LEU 1527 1527 ?    ?   ?   A . n 
A 1 1528 ASN 1528 1528 ?    ?   ?   A . n 
A 1 1529 ARG 1529 1529 ?    ?   ?   A . n 
A 1 1530 ILE 1530 1530 ?    ?   ?   A . n 
A 1 1531 MET 1531 1531 ?    ?   ?   A . n 
A 1 1532 ALA 1532 1532 ?    ?   ?   A . n 
A 1 1533 LEU 1533 1533 ?    ?   ?   A . n 
A 1 1534 PHE 1534 1534 ?    ?   ?   A . n 
A 1 1535 ASP 1535 1535 ?    ?   ?   A . n 
A 1 1536 VAL 1536 1536 ?    ?   ?   A . n 
A 1 1537 TRP 1537 1537 ?    ?   ?   A . n 
A 1 1538 ILE 1538 1538 ?    ?   ?   A . n 
A 1 1539 ASP 1539 1539 ?    ?   ?   A . n 
A 1 1540 VAL 1540 1540 ?    ?   ?   A . n 
A 1 1541 GLN 1541 1541 ?    ?   ?   A . n 
A 1 1542 ARG 1542 1542 ?    ?   ?   A . n 
A 1 1543 ARG 1543 1543 ?    ?   ?   A . n 
A 1 1544 TRP 1544 1544 ?    ?   ?   A . n 
A 1 1545 VAL 1545 1545 ?    ?   ?   A . n 
A 1 1546 TYR 1546 1546 ?    ?   ?   A . n 
A 1 1547 LEU 1547 1547 ?    ?   ?   A . n 
A 1 1548 GLU 1548 1548 ?    ?   ?   A . n 
A 1 1549 GLY 1549 1549 ?    ?   ?   A . n 
A 1 1550 ILE 1550 1550 ?    ?   ?   A . n 
A 1 1551 PHE 1551 1551 ?    ?   ?   A . n 
A 1 1552 THR 1552 1552 ?    ?   ?   A . n 
A 1 1553 GLY 1553 1553 ?    ?   ?   A . n 
A 1 1554 SER 1554 1554 ?    ?   ?   A . n 
A 1 1555 ALA 1555 1555 ?    ?   ?   A . n 
A 1 1556 ASP 1556 1556 ?    ?   ?   A . n 
A 1 1557 ILE 1557 1557 ?    ?   ?   A . n 
A 1 1558 LYS 1558 1558 ?    ?   ?   A . n 
A 1 1559 HIS 1559 1559 ?    ?   ?   A . n 
A 1 1560 LEU 1560 1560 ?    ?   ?   A . n 
A 1 1561 LEU 1561 1561 ?    ?   ?   A . n 
A 1 1562 PRO 1562 1562 ?    ?   ?   A . n 
A 1 1563 VAL 1563 1563 ?    ?   ?   A . n 
A 1 1564 GLU 1564 1564 ?    ?   ?   A . n 
A 1 1565 THR 1565 1565 ?    ?   ?   A . n 
A 1 1566 GLN 1566 1566 ?    ?   ?   A . n 
A 1 1567 ARG 1567 1567 ?    ?   ?   A . n 
A 1 1568 PHE 1568 1568 ?    ?   ?   A . n 
A 1 1569 GLN 1569 1569 ?    ?   ?   A . n 
A 1 1570 SER 1570 1570 ?    ?   ?   A . n 
A 1 1571 ILE 1571 1571 ?    ?   ?   A . n 
A 1 1572 SER 1572 1572 ?    ?   ?   A . n 
A 1 1573 THR 1573 1573 ?    ?   ?   A . n 
A 1 1574 GLU 1574 1574 ?    ?   ?   A . n 
A 1 1575 PHE 1575 1575 ?    ?   ?   A . n 
A 1 1576 LEU 1576 1576 ?    ?   ?   A . n 
A 1 1577 ALA 1577 1577 ?    ?   ?   A . n 
A 1 1578 LEU 1578 1578 ?    ?   ?   A . n 
A 1 1579 MET 1579 1579 ?    ?   ?   A . n 
A 1 1580 LYS 1580 1580 ?    ?   ?   A . n 
A 1 1581 LYS 1581 1581 ?    ?   ?   A . n 
A 1 1582 VAL 1582 1582 ?    ?   ?   A . n 
A 1 1583 SER 1583 1583 ?    ?   ?   A . n 
A 1 1584 LYS 1584 1584 ?    ?   ?   A . n 
A 1 1585 SER 1585 1585 ?    ?   ?   A . n 
A 1 1586 PRO 1586 1586 ?    ?   ?   A . n 
A 1 1587 LEU 1587 1587 ?    ?   ?   A . n 
A 1 1588 VAL 1588 1588 ?    ?   ?   A . n 
A 1 1589 MET 1589 1589 ?    ?   ?   A . n 
A 1 1590 ASP 1590 1590 ?    ?   ?   A . n 
A 1 1591 VAL 1591 1591 ?    ?   ?   A . n 
A 1 1592 LEU 1592 1592 ?    ?   ?   A . n 
A 1 1593 ASN 1593 1593 ?    ?   ?   A . n 
A 1 1594 ILE 1594 1594 ?    ?   ?   A . n 
A 1 1595 GLN 1595 1595 ?    ?   ?   A . n 
A 1 1596 GLY 1596 1596 ?    ?   ?   A . n 
A 1 1597 VAL 1597 1597 ?    ?   ?   A . n 
A 1 1598 GLN 1598 1598 ?    ?   ?   A . n 
A 1 1599 ARG 1599 1599 ?    ?   ?   A . n 
A 1 1600 SER 1600 1600 ?    ?   ?   A . n 
A 1 1601 LEU 1601 1601 ?    ?   ?   A . n 
A 1 1602 GLU 1602 1602 ?    ?   ?   A . n 
A 1 1603 ARG 1603 1603 ?    ?   ?   A . n 
A 1 1604 LEU 1604 1604 ?    ?   ?   A . n 
A 1 1605 ALA 1605 1605 ?    ?   ?   A . n 
A 1 1606 ASP 1606 1606 ?    ?   ?   A . n 
A 1 1607 LEU 1607 1607 ?    ?   ?   A . n 
A 1 1608 LEU 1608 1608 ?    ?   ?   A . n 
A 1 1609 GLY 1609 1609 ?    ?   ?   A . n 
A 1 1610 LYS 1610 1610 ?    ?   ?   A . n 
A 1 1611 ILE 1611 1611 ?    ?   ?   A . n 
A 1 1612 GLN 1612 1612 ?    ?   ?   A . n 
A 1 1613 LYS 1613 1613 ?    ?   ?   A . n 
A 1 1614 ALA 1614 1614 ?    ?   ?   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 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BM7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BM7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BM7 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9BM7 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.004 ? 22303 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.639 ? 30267 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 4.496 ? 2972  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.042 ? 3407  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005 ? 3878  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9BM7 
_struct.title                        'State-7b 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        9BM7 
_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              9BM7 
_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 LEU A 1615 ? PHE A 1626 ? LEU A 1615 PHE A 1626 1 ? 12 
HELX_P HELX_P2   AA2 PRO A 1627 ? PHE A 1631 ? PRO A 1627 PHE A 1631 5 ? 5  
HELX_P HELX_P3   AA3 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P4   AA4 ASN A 1646 ? LEU A 1650 ? ASN A 1646 LEU A 1650 5 ? 5  
HELX_P HELX_P5   AA5 HIS A 1653 ? PHE A 1658 ? HIS A 1653 PHE A 1658 1 ? 6  
HELX_P HELX_P6   AA6 LYS A 1697 ? LYS A 1729 ? LYS A 1697 LYS A 1729 1 ? 33 
HELX_P HELX_P7   AA7 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P8   AA8 GLN A 1746 ? SER A 1768 ? GLN A 1746 SER A 1768 1 ? 23 
HELX_P HELX_P9   AA9 PRO A 1777 ? MET A 1798 ? PRO A 1777 MET A 1798 1 ? 22 
HELX_P HELX_P10  AB1 PRO A 1801 ? SER A 1824 ? PRO A 1801 SER A 1824 1 ? 24 
HELX_P HELX_P11  AB2 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P12  AB3 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P13  AB4 LYS A 1912 ? GLY A 1924 ? LYS A 1912 GLY A 1924 1 ? 13 
HELX_P HELX_P14  AB5 ALA A 1940 ? GLY A 1952 ? ALA A 1940 GLY A 1952 1 ? 13 
HELX_P HELX_P15  AB6 GLU A 1959 ? LEU A 1963 ? GLU A 1959 LEU A 1963 5 ? 5  
HELX_P HELX_P16  AB7 GLU A 1964 ? HIS A 1985 ? GLU A 1964 HIS A 1985 1 ? 22 
HELX_P HELX_P17  AB8 ASP A 2045 ? GLY A 2058 ? ASP A 2045 GLY A 2058 1 ? 14 
HELX_P HELX_P18  AB9 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P19  AC1 GLY A 2089 ? ARG A 2113 ? GLY A 2089 ARG A 2113 1 ? 25 
HELX_P HELX_P20  AC2 PRO A 2132 ? VAL A 2146 ? PRO A 2132 VAL A 2146 1 ? 15 
HELX_P HELX_P21  AC3 PRO A 2147 ? LEU A 2149 ? PRO A 2147 LEU A 2149 5 ? 3  
HELX_P HELX_P22  AC4 VAL A 2150 ? ALA A 2151 ? VAL A 2150 ALA A 2151 5 ? 2  
HELX_P HELX_P23  AC5 GLU A 2152 ? PHE A 2165 ? GLU A 2152 PHE A 2165 1 ? 14 
HELX_P HELX_P24  AC6 MET A 2175 ? MET A 2189 ? MET A 2175 MET A 2189 1 ? 15 
HELX_P HELX_P25  AC7 GLY A 2200 ? ASN A 2217 ? GLY A 2200 ASN A 2217 1 ? 18 
HELX_P HELX_P26  AC8 LYS A 2230 ? GLY A 2246 ? LYS A 2230 GLY A 2246 1 ? 17 
HELX_P HELX_P27  AC9 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P28  AD1 GLY A 2278 ? SER A 2290 ? GLY A 2278 SER A 2290 1 ? 13 
HELX_P HELX_P29  AD2 LEU A 2315 ? ASP A 2320 ? LEU A 2315 ASP A 2320 1 ? 6  
HELX_P HELX_P30  AD3 THR A 2352 ? ARG A 2358 ? THR A 2352 ARG A 2358 1 ? 7  
HELX_P HELX_P31  AD4 SER A 2365 ? LEU A 2369 ? SER A 2365 LEU A 2369 5 ? 5  
HELX_P HELX_P32  AD5 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P33  AD6 PRO A 2411 ? GLN A 2424 ? PRO A 2411 GLN A 2424 1 ? 14 
HELX_P HELX_P34  AD7 PRO A 2425 ? PHE A 2427 ? PRO A 2425 PHE A 2427 5 ? 3  
HELX_P HELX_P35  AD8 GLY A 2431 ? LEU A 2443 ? GLY A 2431 LEU A 2443 1 ? 13 
HELX_P HELX_P36  AD9 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P37  AE1 GLN A 2482 ? LEU A 2502 ? GLN A 2482 LEU A 2502 1 ? 21 
HELX_P HELX_P38  AE2 ARG A 2507 ? THR A 2522 ? ARG A 2507 THR A 2522 1 ? 16 
HELX_P HELX_P39  AE3 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P40  AE4 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P41  AE5 GLU A 2558 ? VAL A 2562 ? GLU A 2558 VAL A 2562 5 ? 5  
HELX_P HELX_P42  AE6 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P43  AE7 GLY A 2600 ? LEU A 2612 ? GLY A 2600 LEU A 2612 1 ? 13 
HELX_P HELX_P44  AE8 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P45  AE9 GLN A 2677 ? GLY A 2690 ? GLN A 2677 GLY A 2690 1 ? 14 
HELX_P HELX_P46  AF1 SER A 2724 ? ARG A 2729 ? SER A 2724 ARG A 2729 1 ? 6  
HELX_P HELX_P47  AF2 GLY A 2740 ? LEU A 2756 ? GLY A 2740 LEU A 2756 1 ? 17 
HELX_P HELX_P48  AF3 ARG A 2757 ? LEU A 2758 ? ARG A 2757 LEU A 2758 5 ? 2  
HELX_P HELX_P49  AF4 ILE A 2759 ? THR A 2764 ? ILE A 2759 THR A 2764 5 ? 6  
HELX_P HELX_P50  AF5 TYR A 2765 ? ARG A 2783 ? TYR A 2765 ARG A 2783 1 ? 19 
HELX_P HELX_P51  AF6 SER A 2795 ? ARG A 2811 ? SER A 2795 ARG A 2811 1 ? 17 
HELX_P HELX_P52  AF7 PRO A 2817 ? GLN A 2834 ? PRO A 2817 GLN A 2834 1 ? 18 
HELX_P HELX_P53  AF8 ASP A 2835 ? LEU A 2837 ? ASP A 2835 LEU A 2837 5 ? 3  
HELX_P HELX_P54  AF9 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P55  AG1 ASP A 2885 ? GLU A 2904 ? ASP A 2885 GLU A 2904 1 ? 20 
HELX_P HELX_P56  AG2 PHE A 2912 ? GLN A 2928 ? PHE A 2912 GLN A 2928 1 ? 17 
HELX_P HELX_P57  AG3 GLY A 2942 ? ASN A 2954 ? GLY A 2942 ASN A 2954 1 ? 13 
HELX_P HELX_P58  AG4 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P59  AG5 ASP A 3001 ? GLY A 3015 ? ASP A 3001 GLY A 3015 1 ? 15 
HELX_P HELX_P60  AG6 GLY A 3023 ? GLY A 3041 ? GLY A 3023 GLY A 3041 1 ? 19 
HELX_P HELX_P61  AG7 SER A 3046 ? ASN A 3061 ? SER A 3046 ASN A 3061 1 ? 16 
HELX_P HELX_P62  AG8 PRO A 3083 ? ASN A 3087 ? PRO A 3083 ASN A 3087 1 ? 5  
HELX_P HELX_P63  AG9 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P64  AH1 SER A 3138 ? ARG A 3164 ? SER A 3138 ARG A 3164 1 ? 27 
HELX_P HELX_P65  AH2 THR A 3172 ? ARG A 3220 ? THR A 3172 ARG A 3220 1 ? 49 
HELX_P HELX_P66  AH3 VAL A 3472 ? THR A 3502 ? VAL A 3472 THR A 3502 1 ? 31 
HELX_P HELX_P67  AH4 ILE A 3503 ? TYR A 3516 ? ILE A 3503 TYR A 3516 1 ? 14 
HELX_P HELX_P68  AH5 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P69  AH6 ALA A 3548 ? LEU A 3553 ? ALA A 3548 LEU A 3553 1 ? 6  
HELX_P HELX_P70  AH7 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P71  AH8 ASP A 3570 ? ARG A 3582 ? ASP A 3570 ARG A 3582 1 ? 13 
HELX_P HELX_P72  AH9 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P73  AI1 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P74  AI2 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P75  AI3 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P76  AI4 LEU A 3645 ? ASN A 3650 ? LEU A 3645 ASN A 3650 1 ? 6  
HELX_P HELX_P77  AI5 PRO A 3689 ? VAL A 3696 ? PRO A 3689 VAL A 3696 1 ? 8  
HELX_P HELX_P78  AI6 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P79  AI7 ARG A 3721 ? GLN A 3735 ? ARG A 3721 GLN A 3735 1 ? 15 
HELX_P HELX_P80  AI8 GLY A 3736 ? LYS A 3757 ? GLY A 3736 LYS A 3757 1 ? 22 
HELX_P HELX_P81  AI9 ASP A 3762 ? GLU A 3786 ? ASP A 3762 GLU A 3786 1 ? 25 
HELX_P HELX_P82  AJ1 GLU A 3786 ? LEU A 3818 ? GLU A 3786 LEU A 3818 1 ? 33 
HELX_P HELX_P83  AJ2 LYS A 3819 ? ILE A 3821 ? LYS A 3819 ILE A 3821 5 ? 3  
HELX_P HELX_P84  AJ3 SER A 3828 ? TYR A 3841 ? SER A 3828 TYR A 3841 1 ? 14 
HELX_P HELX_P85  AJ4 ASN A 3843 ? LYS A 3847 ? ASN A 3843 LYS A 3847 5 ? 5  
HELX_P HELX_P86  AJ5 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P87  AJ6 GLY A 3874 ? MET A 3875 ? GLY A 3874 MET A 3875 5 ? 2  
HELX_P HELX_P88  AJ7 LEU A 3876 ? GLN A 3878 ? LEU A 3876 GLN A 3878 5 ? 3  
HELX_P HELX_P89  AJ8 ASP A 3879 ? THR A 3895 ? ASP A 3879 THR A 3895 1 ? 17 
HELX_P HELX_P90  AJ9 TYR A 3901 ? ARG A 3910 ? TYR A 3901 ARG A 3910 1 ? 10 
HELX_P HELX_P91  AK1 THR A 3928 ? SER A 3939 ? THR A 3928 SER A 3939 1 ? 12 
HELX_P HELX_P92  AK2 CYS A 3940 ? LYS A 3945 ? CYS A 3940 LYS A 3945 5 ? 6  
HELX_P HELX_P93  AK3 ASP A 3946 ? ASP A 3954 ? ASP A 3946 ASP A 3954 1 ? 9  
HELX_P HELX_P94  AK4 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P95  AK5 SER A 3965 ? VAL A 3970 ? SER A 3965 VAL A 3970 5 ? 6  
HELX_P HELX_P96  AK6 THR A 3981 ? PHE A 3996 ? THR A 3981 PHE A 3996 1 ? 16 
HELX_P HELX_P97  AK7 ARG A 3997 ? ASP A 3999 ? ARG A 3997 ASP A 3999 5 ? 3  
HELX_P HELX_P98  AK8 ARG A 4000 ? GLY A 4014 ? ARG A 4000 GLY A 4014 1 ? 15 
HELX_P HELX_P99  AK9 MET A 4018 ? GLN A 4023 ? MET A 4018 GLN A 4023 1 ? 6  
HELX_P HELX_P100 AL1 ASP A 4026 ? GLY A 4032 ? ASP A 4026 GLY A 4032 1 ? 7  
HELX_P HELX_P101 AL2 ALA A 4051 ? GLN A 4062 ? ALA A 4051 GLN A 4062 1 ? 12 
HELX_P HELX_P102 AL3 ALA A 4074 ? GLY A 4091 ? ALA A 4074 GLY A 4091 1 ? 18 
HELX_P HELX_P103 AL4 VAL A 4099 ? LEU A 4101 ? VAL A 4099 LEU A 4101 5 ? 3  
HELX_P HELX_P104 AL5 ALA A 4102 ? HIS A 4114 ? ALA A 4102 HIS A 4114 1 ? 13 
HELX_P HELX_P105 AL6 PRO A 4135 ? GLY A 4142 ? PRO A 4135 GLY A 4142 1 ? 8  
HELX_P HELX_P106 AL7 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P107 AL8 PRO A 4165 ? CYS A 4170 ? PRO A 4165 CYS A 4170 1 ? 6  
HELX_P HELX_P108 AL9 ASN A 4174 ? ARG A 4193 ? ASN A 4174 ARG A 4193 1 ? 20 
HELX_P HELX_P109 AM1 ALA A 4197 ? SER A 4202 ? ALA A 4197 SER A 4202 1 ? 6  
HELX_P HELX_P110 AM2 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P111 AM3 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P112 AM4 ILE A 4251 ? ARG A 4255 ? ILE A 4251 ARG A 4255 5 ? 5  
HELX_P HELX_P113 AM5 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P114 AM6 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P115 AM7 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P116 AM8 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
HELX_P HELX_P117 AM9 ASN A 4325 ? MET A 4346 ? ASN A 4325 MET A 4346 1 ? 22 
HELX_P HELX_P118 AN1 TRP A 4376 ? ILE A 4391 ? TRP A 4376 ILE A 4391 1 ? 16 
HELX_P HELX_P119 AN2 ASP A 4407 ? GLU A 4439 ? ASP A 4407 GLU A 4439 1 ? 33 
HELX_P HELX_P120 AN3 THR A 4445 ? LYS A 4457 ? THR A 4445 LYS A 4457 1 ? 13 
HELX_P HELX_P121 AN4 THR A 4474 ? GLY A 4500 ? THR A 4474 GLY A 4500 1 ? 27 
HELX_P HELX_P122 AN5 ALA A 4501 ? ASN A 4506 ? ALA A 4501 ASN A 4506 1 ? 6  
HELX_P HELX_P123 AN6 VAL A 4516 ? ALA A 4531 ? VAL A 4516 ALA A 4531 1 ? 16 
HELX_P HELX_P124 AN7 SER A 4535 ? GLU A 4537 ? SER A 4535 GLU A 4537 5 ? 3  
HELX_P HELX_P125 AN8 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 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 5 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 5 ? 
AB2 ? 4 ? 
AB3 ? 5 ? 
AB4 ? 5 ? 
AB5 ? 2 ? 
AB6 ? 5 ? 
AB7 ? 2 ? 
AB8 ? 4 ? 
AB9 ? 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 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB1 4 5 ? parallel      
AB2 1 2 ? anti-parallel 
AB2 2 3 ? parallel      
AB2 3 4 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? parallel      
AB3 4 5 ? parallel      
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB4 4 5 ? parallel      
AB5 1 2 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB6 4 5 ? parallel      
AB7 1 2 ? anti-parallel 
AB8 1 2 ? parallel      
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? parallel      
AB9 3 4 ? anti-parallel 
AB9 4 5 ? parallel      
AB9 5 6 ? anti-parallel 
AB9 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 VAL A 1661 ? LEU A 1666 ? VAL A 1661 LEU A 1666 
AA1 2 VAL A 1672 ? SER A 1678 ? VAL A 1672 SER A 1678 
AA1 3 GLU A 1683 ? SER A 1691 ? GLU A 1683 SER A 1691 
AA2 1 ARG A 1843 ? PHE A 1846 ? ARG A 1843 PHE A 1846 
AA2 2 LEU A 1857 ? MET A 1861 ? LEU A 1857 MET A 1861 
AA2 3 ALA A 1864 ? ASN A 1867 ? ALA A 1864 ASN A 1867 
AA3 1 GLY A 1901 ? SER A 1903 ? GLY A 1901 SER A 1903 
AA3 2 PHE A 2036 ? SER A 2038 ? PHE A 2036 SER A 2038 
AA4 1 VAL A 1927 ? PHE A 1930 ? VAL A 1927 PHE A 1930 
AA4 2 TRP A 1954 ? PHE A 1957 ? TRP A 1954 PHE A 1957 
AA4 3 ALA A 2013 ? ILE A 2016 ? ALA A 2013 ILE A 2016 
AA5 1 THR A 1998 ? LEU A 2001 ? THR A 1998 LEU A 2001 
AA5 2 LYS A 2004 ? LYS A 2007 ? LYS A 2004 LYS A 2007 
AA6 1 GLY A 2249 ? ILE A 2253 ? GLY A 2249 ILE A 2253 
AA6 2 ARG A 2298 ? GLY A 2305 ? ARG A 2298 GLY A 2305 
AA6 3 VAL A 2339 ? VAL A 2345 ? VAL A 2339 VAL A 2345 
AA6 4 LEU A 2220 ? VAL A 2223 ? LEU A 2220 VAL A 2223 
AA6 5 GLY A 2360 ? TRP A 2363 ? GLY A 2360 TRP A 2363 
AA7 1 GLY A 2266 ? LEU A 2268 ? GLY A 2266 LEU A 2268 
AA7 2 TRP A 2275 ? ASP A 2277 ? TRP A 2275 ASP A 2277 
AA8 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AA8 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AA9 1 TYR A 2537 ? VAL A 2539 ? TYR A 2537 VAL A 2539 
AA9 2 TRP A 2545 ? PRO A 2547 ? TRP A 2545 PRO A 2547 
AB1 1 MET A 2615 ? ASN A 2621 ? MET A 2615 ASN A 2621 
AB1 2 TRP A 2658 ? ASP A 2664 ? TRP A 2658 ASP A 2664 
AB1 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB1 4 LEU A 2591 ? CYS A 2594 ? LEU A 2591 CYS A 2594 
AB1 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB2 1 CYS A 2639 ? ARG A 2642 ? CYS A 2639 ARG A 2642 
AB2 2 VAL A 2649 ? PRO A 2652 ? VAL A 2649 PRO A 2652 
AB2 3 THR A 2699 ? LEU A 2703 ? THR A 2699 LEU A 2703 
AB2 4 GLY A 2691 ? ARG A 2694 ? GLY A 2691 ARG A 2694 
AB3 1 SER A 2957 ? GLN A 2960 ? SER A 2957 GLN A 2960 
AB3 2 ILE A 2990 ? ASP A 2995 ? ILE A 2990 ASP A 2995 
AB3 3 LEU A 3062 ? MET A 3068 ? LEU A 3062 MET A 3068 
AB3 4 HIS A 2932 ? GLY A 2937 ? HIS A 2932 GLY A 2937 
AB3 5 VAL A 3090 ? PHE A 3094 ? VAL A 3090 PHE A 3094 
AB4 1 THR A 3610 ? SER A 3613 ? THR A 3610 SER A 3613 
AB4 2 LEU A 3633 ? GLN A 3636 ? LEU A 3633 GLN A 3636 
AB4 3 ILE A 3677 ? THR A 3681 ? ILE A 3677 THR A 3681 
AB4 4 PRO A 3587 ? ILE A 3590 ? PRO A 3587 ILE A 3590 
AB4 5 THR A 3697 ? ASN A 3700 ? THR A 3697 ASN A 3700 
AB5 1 LEU A 3661 ? LEU A 3664 ? LEU A 3661 LEU A 3664 
AB5 2 GLN A 3667 ? ASP A 3670 ? GLN A 3667 ASP A 3670 
AB6 1 ILE A 4066 ? ALA A 4070 ? ILE A 4066 ALA A 4070 
AB6 2 TRP A 4093 ? LYS A 4097 ? TRP A 4093 LYS A 4097 
AB6 3 LEU A 4124 ? GLU A 4129 ? LEU A 4124 GLU A 4129 
AB6 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB6 5 ARG A 4143 ? PHE A 4147 ? ARG A 4143 PHE A 4147 
AB7 1 LYS A 4283 ? VAL A 4288 ? LYS A 4283 VAL A 4288 
AB7 2 LYS A 4292 ? GLN A 4295 ? LYS A 4292 GLN A 4295 
AB8 1 HIS A 4508 ? CYS A 4510 ? HIS A 4508 CYS A 4510 
AB8 2 SER A 4557 ? THR A 4561 ? SER A 4557 THR A 4561 
AB8 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AB8 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AB9 1 ALA A 4568 ? ASN A 4571 ? ALA A 4568 ASN A 4571 
AB9 2 LYS A 4574 ? LEU A 4577 ? LYS A 4574 LEU A 4577 
AB9 3 LEU A 4618 ? ILE A 4626 ? LEU A 4618 ILE A 4626 
AB9 4 VAL A 4604 ? TYR A 4610 ? VAL A 4604 TYR A 4610 
AB9 5 ALA A 4641 ? LEU A 4643 ? ALA A 4641 LEU A 4643 
AB9 6 LYS A 4564 ? GLN A 4566 ? LYS A 4564 GLN A 4566 
AB9 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 SER A 1663 ? N SER A 1663 O SER A 1677 ? O SER A 1677 
AA1 2 3 N ILE A 1676 ? N ILE A 1676 O VAL A 1684 ? O VAL A 1684 
AA2 1 2 N TYR A 1845 ? N TYR A 1845 O SER A 1858 ? O SER A 1858 
AA2 2 3 N MET A 1861 ? N MET A 1861 O ALA A 1864 ? O ALA A 1864 
AA3 1 2 N GLY A 1901 ? N GLY A 1901 O ARG A 2037 ? O ARG A 2037 
AA4 1 2 N LEU A 1928 ? N LEU A 1928 O TRP A 1954 ? O TRP A 1954 
AA4 2 3 N GLY A 1955 ? N GLY A 1955 O PHE A 2015 ? O PHE A 2015 
AA5 1 2 N CYS A 1999 ? N CYS A 1999 O VAL A 2006 ? O VAL A 2006 
AA6 1 2 N HIS A 2252 ? N HIS A 2252 O TRP A 2300 ? O TRP A 2300 
AA6 2 3 N PHE A 2303 ? N PHE A 2303 O MET A 2342 ? O MET A 2342 
AA6 3 4 O PHE A 2343 ? O PHE A 2343 N MET A 2222 ? N MET A 2222 
AA6 4 5 N MET A 2221 ? N MET A 2221 O VAL A 2362 ? O VAL A 2362 
AA7 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA8 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AA9 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB1 1 2 N LEU A 2620 ? N LEU A 2620 O PHE A 2662 ? O PHE A 2662 
AB1 2 3 N CYS A 2663 ? N CYS A 2663 O VAL A 2709 ? O VAL A 2709 
AB1 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 2591 ? N LEU A 2591 
AB1 4 5 N CYS A 2594 ? N CYS A 2594 O VAL A 2734 ? O VAL A 2734 
AB2 1 2 N GLU A 2640 ? N GLU A 2640 O ALA A 2651 ? O ALA A 2651 
AB2 2 3 N LEU A 2650 ? N LEU A 2650 O LYS A 2702 ? O LYS A 2702 
AB2 3 4 O THR A 2699 ? O THR A 2699 N ARG A 2694 ? N ARG A 2694 
AB3 1 2 N SER A 2957 ? N SER A 2957 O ALA A 2991 ? O ALA A 2991 
AB3 2 3 N PHE A 2992 ? N PHE A 2992 O VAL A 3065 ? O VAL A 3065 
AB3 3 4 O PHE A 3066 ? O PHE A 3066 N LEU A 2935 ? N LEU A 2935 
AB3 4 5 N LEU A 2934 ? N LEU A 2934 O VAL A 3090 ? O VAL A 3090 
AB4 1 2 N THR A 3612 ? N THR A 3612 O GLN A 3636 ? O GLN A 3636 
AB4 2 3 N LEU A 3633 ? N LEU A 3633 O PHE A 3678 ? O PHE A 3678 
AB4 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB4 4 5 N ILE A 3590 ? N ILE A 3590 O VAL A 3699 ? O VAL A 3699 
AB5 1 2 N LEU A 3664 ? N LEU A 3664 O GLN A 3667 ? O GLN A 3667 
AB6 1 2 N ILE A 4069 ? N ILE A 4069 O LYS A 4097 ? O LYS A 4097 
AB6 2 3 N LEU A 4096 ? N LEU A 4096 O THR A 4127 ? O THR A 4127 
AB6 3 4 O LEU A 4126 ? O LEU A 4126 N MET A 4043 ? N MET A 4043 
AB6 4 5 N LEU A 4042 ? N LEU A 4042 O ARG A 4143 ? O ARG A 4143 
AB7 1 2 N LEU A 4284 ? N LEU A 4284 O ILE A 4294 ? O ILE A 4294 
AB8 1 2 N VAL A 4509 ? N VAL A 4509 O GLY A 4559 ? O GLY A 4559 
AB8 2 3 N VAL A 4560 ? N VAL A 4560 O THR A 4588 ? O THR A 4588 
AB8 3 4 O GLN A 4589 ? O GLN A 4589 N ASN A 4544 ? N ASN A 4544 
AB9 1 2 N THR A 4569 ? N THR A 4569 O SER A 4576 ? O SER A 4576 
AB9 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AB9 3 4 O PHE A 4624 ? O PHE A 4624 N VAL A 4605 ? N VAL A 4605 
AB9 4 5 N PRO A 4608 ? N PRO A 4608 O VAL A 4642 ? O VAL A 4642 
AB9 5 6 O LEU A 4643 ? O LEU A 4643 N LYS A 4564 ? N LYS A 4564 
AB9 6 7 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
# 
_pdbx_entry_details.entry_id                   9BM7 
_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 OH  A TYR 2426 ? ? OE1 A GLN 2491 ? ? 2.12 
2 1 OD1 A ASP 2995 ? ? OG1 A THR 3067 ? ? 2.15 
3 1 OG  A SER 2983 ? ? O   A ASN 3061 ? ? 2.15 
4 1 OG  A SER 2542 ? ? OE1 A GLU 2544 ? ? 2.16 
5 1 OH  A TYR 2265 ? ? O   A TRP 2311 ? ? 2.19 
# 
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 MET A 1769 ? ? -97.03  33.81   
2  1 ALA A 1862 ? ? 56.75   -116.77 
3  1 GLU A 1934 ? ? 67.11   -4.16   
4  1 MET A 2041 ? ? -100.30 75.11   
5  1 LYS A 2230 ? ? -101.48 -60.78  
6  1 PRO A 2309 ? ? -69.96  8.24    
7  1 ASP A 2320 ? ? -77.91  -166.50 
8  1 LYS A 2349 ? ? -130.23 -30.64  
9  1 LEU A 2387 ? ? -69.45  22.55   
10 1 PHE A 2427 ? ? -94.31  54.11   
11 1 PHE A 2479 ? ? 52.37   71.59   
12 1 VAL A 2838 ? ? -106.34 -62.28  
13 1 ILE A 2871 ? ? 52.24   71.93   
14 1 SER A 2878 ? ? -125.86 -168.36 
15 1 ASP A 3045 ? ? 58.21   -117.73 
16 1 ARG A 3088 ? ? 53.83   17.33   
17 1 TYR A 3125 ? ? 71.96   -126.03 
18 1 VAL A 3128 ? ? -130.39 -55.29  
19 1 ASP A 3131 ? ? -95.69  58.76   
20 1 TYR A 3519 ? ? 71.00   -9.25   
21 1 ASP A 3546 ? ? 36.62   45.29   
22 1 LYS A 3608 ? ? 60.93   61.21   
23 1 SER A 3640 ? ? -93.48  59.10   
24 1 TYR A 3825 ? ? -98.92  38.75   
25 1 LEU A 3916 ? ? -144.02 32.44   
26 1 ARG A 3923 ? ? 56.51   -114.31 
27 1 GLU A 4034 ? ? 57.57   7.58    
28 1 SER A 4172 ? ? 62.80   -167.05 
29 1 SER A 4202 ? ? 61.23   -66.29  
30 1 PRO A 4239 ? ? -69.35  77.26   
31 1 ILE A 4251 ? ? 55.77   -104.01 
32 1 ASN A 4532 ? ? 66.27   -2.87   
33 1 ALA A 4555 ? ? 53.91   -96.40  
34 1 ASN A 4597 ? ? 33.74   52.38   
35 1 ILE A 4619 ? ? -94.77  -61.78  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BM7 
_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                    9BM7 
_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                  3.58 
_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               66008 
_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-7b 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                        9BM7 
_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              9BM7 
_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                9BM7 
_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 GLN 1327 ? A GLN 1327 
1328 1 Y 1 A ASP 1328 ? A ASP 1328 
1329 1 Y 1 A LEU 1329 ? A LEU 1329 
1330 1 Y 1 A LYS 1330 ? A LYS 1330 
1331 1 Y 1 A GLY 1331 ? A GLY 1331 
1332 1 Y 1 A VAL 1332 ? A VAL 1332 
1333 1 Y 1 A TRP 1333 ? A TRP 1333 
1334 1 Y 1 A SER 1334 ? A SER 1334 
1335 1 Y 1 A GLU 1335 ? A GLU 1335 
1336 1 Y 1 A LEU 1336 ? A LEU 1336 
1337 1 Y 1 A SER 1337 ? A SER 1337 
1338 1 Y 1 A LYS 1338 ? A LYS 1338 
1339 1 Y 1 A VAL 1339 ? A VAL 1339 
1340 1 Y 1 A TRP 1340 ? A TRP 1340 
1341 1 Y 1 A GLU 1341 ? A GLU 1341 
1342 1 Y 1 A GLN 1342 ? A GLN 1342 
1343 1 Y 1 A ILE 1343 ? A ILE 1343 
1344 1 Y 1 A ASP 1344 ? A ASP 1344 
1345 1 Y 1 A GLN 1345 ? A GLN 1345 
1346 1 Y 1 A MET 1346 ? A MET 1346 
1347 1 Y 1 A LYS 1347 ? A LYS 1347 
1348 1 Y 1 A GLU 1348 ? A GLU 1348 
1349 1 Y 1 A GLN 1349 ? A GLN 1349 
1350 1 Y 1 A PRO 1350 ? A PRO 1350 
1351 1 Y 1 A TRP 1351 ? A TRP 1351 
1352 1 Y 1 A VAL 1352 ? A VAL 1352 
1353 1 Y 1 A SER 1353 ? A SER 1353 
1354 1 Y 1 A VAL 1354 ? A VAL 1354 
1355 1 Y 1 A GLN 1355 ? A GLN 1355 
1356 1 Y 1 A PRO 1356 ? A PRO 1356 
1357 1 Y 1 A ARG 1357 ? A ARG 1357 
1358 1 Y 1 A LYS 1358 ? A LYS 1358 
1359 1 Y 1 A LEU 1359 ? A LEU 1359 
1360 1 Y 1 A ARG 1360 ? A ARG 1360 
1361 1 Y 1 A GLN 1361 ? A GLN 1361 
1362 1 Y 1 A ASN 1362 ? A ASN 1362 
1363 1 Y 1 A LEU 1363 ? A LEU 1363 
1364 1 Y 1 A ASP 1364 ? A ASP 1364 
1365 1 Y 1 A ALA 1365 ? A ALA 1365 
1366 1 Y 1 A LEU 1366 ? A LEU 1366 
1367 1 Y 1 A LEU 1367 ? A LEU 1367 
1368 1 Y 1 A ASN 1368 ? A ASN 1368 
1369 1 Y 1 A GLN 1369 ? A GLN 1369 
1370 1 Y 1 A LEU 1370 ? A LEU 1370 
1371 1 Y 1 A LYS 1371 ? A LYS 1371 
1372 1 Y 1 A SER 1372 ? A SER 1372 
1373 1 Y 1 A PHE 1373 ? A PHE 1373 
1374 1 Y 1 A PRO 1374 ? A PRO 1374 
1375 1 Y 1 A ALA 1375 ? A ALA 1375 
1376 1 Y 1 A ARG 1376 ? A ARG 1376 
1377 1 Y 1 A LEU 1377 ? A LEU 1377 
1378 1 Y 1 A ARG 1378 ? A ARG 1378 
1379 1 Y 1 A GLN 1379 ? A GLN 1379 
1380 1 Y 1 A TYR 1380 ? A TYR 1380 
1381 1 Y 1 A ALA 1381 ? A ALA 1381 
1382 1 Y 1 A SER 1382 ? A SER 1382 
1383 1 Y 1 A TYR 1383 ? A TYR 1383 
1384 1 Y 1 A GLU 1384 ? A GLU 1384 
1385 1 Y 1 A PHE 1385 ? A PHE 1385 
1386 1 Y 1 A VAL 1386 ? A VAL 1386 
1387 1 Y 1 A GLN 1387 ? A GLN 1387 
1388 1 Y 1 A ARG 1388 ? A ARG 1388 
1389 1 Y 1 A LEU 1389 ? A LEU 1389 
1390 1 Y 1 A LEU 1390 ? A LEU 1390 
1391 1 Y 1 A LYS 1391 ? A LYS 1391 
1392 1 Y 1 A GLY 1392 ? A GLY 1392 
1393 1 Y 1 A TYR 1393 ? A TYR 1393 
1394 1 Y 1 A MET 1394 ? A MET 1394 
1395 1 Y 1 A LYS 1395 ? A LYS 1395 
1396 1 Y 1 A ILE 1396 ? A ILE 1396 
1397 1 Y 1 A ASN 1397 ? A ASN 1397 
1398 1 Y 1 A MET 1398 ? A MET 1398 
1399 1 Y 1 A LEU 1399 ? A LEU 1399 
1400 1 Y 1 A VAL 1400 ? A VAL 1400 
1401 1 Y 1 A ILE 1401 ? A ILE 1401 
1402 1 Y 1 A GLU 1402 ? A GLU 1402 
1403 1 Y 1 A LEU 1403 ? A LEU 1403 
1404 1 Y 1 A LYS 1404 ? A LYS 1404 
1405 1 Y 1 A SER 1405 ? A SER 1405 
1406 1 Y 1 A GLU 1406 ? A GLU 1406 
1407 1 Y 1 A ALA 1407 ? A ALA 1407 
1408 1 Y 1 A LEU 1408 ? A LEU 1408 
1409 1 Y 1 A LYS 1409 ? A LYS 1409 
1410 1 Y 1 A ASP 1410 ? A ASP 1410 
1411 1 Y 1 A ARG 1411 ? A ARG 1411 
1412 1 Y 1 A HIS 1412 ? A HIS 1412 
1413 1 Y 1 A TRP 1413 ? A TRP 1413 
1414 1 Y 1 A LYS 1414 ? A LYS 1414 
1415 1 Y 1 A GLN 1415 ? A GLN 1415 
1416 1 Y 1 A LEU 1416 ? A LEU 1416 
1417 1 Y 1 A MET 1417 ? A MET 1417 
1418 1 Y 1 A LYS 1418 ? A LYS 1418 
1419 1 Y 1 A ARG 1419 ? A ARG 1419 
1420 1 Y 1 A LEU 1420 ? A LEU 1420 
1421 1 Y 1 A HIS 1421 ? A HIS 1421 
1422 1 Y 1 A VAL 1422 ? A VAL 1422 
1423 1 Y 1 A ASN 1423 ? A ASN 1423 
1424 1 Y 1 A TRP 1424 ? A TRP 1424 
1425 1 Y 1 A VAL 1425 ? A VAL 1425 
1426 1 Y 1 A VAL 1426 ? A VAL 1426 
1427 1 Y 1 A SER 1427 ? A SER 1427 
1428 1 Y 1 A GLU 1428 ? A GLU 1428 
1429 1 Y 1 A LEU 1429 ? A LEU 1429 
1430 1 Y 1 A THR 1430 ? A THR 1430 
1431 1 Y 1 A LEU 1431 ? A LEU 1431 
1432 1 Y 1 A GLY 1432 ? A GLY 1432 
1433 1 Y 1 A GLN 1433 ? A GLN 1433 
1434 1 Y 1 A ILE 1434 ? A ILE 1434 
1435 1 Y 1 A TRP 1435 ? A TRP 1435 
1436 1 Y 1 A ASP 1436 ? A ASP 1436 
1437 1 Y 1 A VAL 1437 ? A VAL 1437 
1438 1 Y 1 A ASP 1438 ? A ASP 1438 
1439 1 Y 1 A LEU 1439 ? A LEU 1439 
1440 1 Y 1 A GLN 1440 ? A GLN 1440 
1441 1 Y 1 A LYS 1441 ? A LYS 1441 
1442 1 Y 1 A ASN 1442 ? A ASN 1442 
1443 1 Y 1 A GLU 1443 ? A GLU 1443 
1444 1 Y 1 A ALA 1444 ? A ALA 1444 
1445 1 Y 1 A ILE 1445 ? A ILE 1445 
1446 1 Y 1 A VAL 1446 ? A VAL 1446 
1447 1 Y 1 A LYS 1447 ? A LYS 1447 
1448 1 Y 1 A ASP 1448 ? A ASP 1448 
1449 1 Y 1 A VAL 1449 ? A VAL 1449 
1450 1 Y 1 A LEU 1450 ? A LEU 1450 
1451 1 Y 1 A LEU 1451 ? A LEU 1451 
1452 1 Y 1 A VAL 1452 ? A VAL 1452 
1453 1 Y 1 A ALA 1453 ? A ALA 1453 
1454 1 Y 1 A GLN 1454 ? A GLN 1454 
1455 1 Y 1 A GLY 1455 ? A GLY 1455 
1456 1 Y 1 A GLU 1456 ? A GLU 1456 
1457 1 Y 1 A MET 1457 ? A MET 1457 
1458 1 Y 1 A ALA 1458 ? A ALA 1458 
1459 1 Y 1 A LEU 1459 ? A LEU 1459 
1460 1 Y 1 A GLU 1460 ? A GLU 1460 
1461 1 Y 1 A GLU 1461 ? A GLU 1461 
1462 1 Y 1 A PHE 1462 ? A PHE 1462 
1463 1 Y 1 A LEU 1463 ? A LEU 1463 
1464 1 Y 1 A LYS 1464 ? A LYS 1464 
1465 1 Y 1 A GLN 1465 ? A GLN 1465 
1466 1 Y 1 A ILE 1466 ? A ILE 1466 
1467 1 Y 1 A ARG 1467 ? A ARG 1467 
1468 1 Y 1 A GLU 1468 ? A GLU 1468 
1469 1 Y 1 A VAL 1469 ? A VAL 1469 
1470 1 Y 1 A TRP 1470 ? A TRP 1470 
1471 1 Y 1 A ASN 1471 ? A ASN 1471 
1472 1 Y 1 A THR 1472 ? A THR 1472 
1473 1 Y 1 A TYR 1473 ? A TYR 1473 
1474 1 Y 1 A GLU 1474 ? A GLU 1474 
1475 1 Y 1 A LEU 1475 ? A LEU 1475 
1476 1 Y 1 A ASP 1476 ? A ASP 1476 
1477 1 Y 1 A LEU 1477 ? A LEU 1477 
1478 1 Y 1 A VAL 1478 ? A VAL 1478 
1479 1 Y 1 A ASN 1479 ? A ASN 1479 
1480 1 Y 1 A TYR 1480 ? A TYR 1480 
1481 1 Y 1 A GLN 1481 ? A GLN 1481 
1482 1 Y 1 A ASN 1482 ? A ASN 1482 
1483 1 Y 1 A LYS 1483 ? A LYS 1483 
1484 1 Y 1 A CYS 1484 ? A CYS 1484 
1485 1 Y 1 A ARG 1485 ? A ARG 1485 
1486 1 Y 1 A LEU 1486 ? A LEU 1486 
1487 1 Y 1 A ILE 1487 ? A ILE 1487 
1488 1 Y 1 A ARG 1488 ? A ARG 1488 
1489 1 Y 1 A GLY 1489 ? A GLY 1489 
1490 1 Y 1 A TRP 1490 ? A TRP 1490 
1491 1 Y 1 A ASP 1491 ? A ASP 1491 
1492 1 Y 1 A ASP 1492 ? A ASP 1492 
1493 1 Y 1 A LEU 1493 ? A LEU 1493 
1494 1 Y 1 A PHE 1494 ? A PHE 1494 
1495 1 Y 1 A ASN 1495 ? A ASN 1495 
1496 1 Y 1 A LYS 1496 ? A LYS 1496 
1497 1 Y 1 A VAL 1497 ? A VAL 1497 
1498 1 Y 1 A LYS 1498 ? A LYS 1498 
1499 1 Y 1 A GLU 1499 ? A GLU 1499 
1500 1 Y 1 A HIS 1500 ? A HIS 1500 
1501 1 Y 1 A ILE 1501 ? A ILE 1501 
1502 1 Y 1 A ASN 1502 ? A ASN 1502 
1503 1 Y 1 A SER 1503 ? A SER 1503 
1504 1 Y 1 A VAL 1504 ? A VAL 1504 
1505 1 Y 1 A SER 1505 ? A SER 1505 
1506 1 Y 1 A ALA 1506 ? A ALA 1506 
1507 1 Y 1 A MET 1507 ? A MET 1507 
1508 1 Y 1 A LYS 1508 ? A LYS 1508 
1509 1 Y 1 A LEU 1509 ? A LEU 1509 
1510 1 Y 1 A SER 1510 ? A SER 1510 
1511 1 Y 1 A PRO 1511 ? A PRO 1511 
1512 1 Y 1 A TYR 1512 ? A TYR 1512 
1513 1 Y 1 A TYR 1513 ? A TYR 1513 
1514 1 Y 1 A LYS 1514 ? A LYS 1514 
1515 1 Y 1 A VAL 1515 ? A VAL 1515 
1516 1 Y 1 A PHE 1516 ? A PHE 1516 
1517 1 Y 1 A GLU 1517 ? A GLU 1517 
1518 1 Y 1 A GLU 1518 ? A GLU 1518 
1519 1 Y 1 A ASP 1519 ? A ASP 1519 
1520 1 Y 1 A ALA 1520 ? A ALA 1520 
1521 1 Y 1 A LEU 1521 ? A LEU 1521 
1522 1 Y 1 A SER 1522 ? A SER 1522 
1523 1 Y 1 A TRP 1523 ? A TRP 1523 
1524 1 Y 1 A GLU 1524 ? A GLU 1524 
1525 1 Y 1 A ASP 1525 ? A ASP 1525 
1526 1 Y 1 A LYS 1526 ? A LYS 1526 
1527 1 Y 1 A LEU 1527 ? A LEU 1527 
1528 1 Y 1 A ASN 1528 ? A ASN 1528 
1529 1 Y 1 A ARG 1529 ? A ARG 1529 
1530 1 Y 1 A ILE 1530 ? A ILE 1530 
1531 1 Y 1 A MET 1531 ? A MET 1531 
1532 1 Y 1 A ALA 1532 ? A ALA 1532 
1533 1 Y 1 A LEU 1533 ? A LEU 1533 
1534 1 Y 1 A PHE 1534 ? A PHE 1534 
1535 1 Y 1 A ASP 1535 ? A ASP 1535 
1536 1 Y 1 A VAL 1536 ? A VAL 1536 
1537 1 Y 1 A TRP 1537 ? A TRP 1537 
1538 1 Y 1 A ILE 1538 ? A ILE 1538 
1539 1 Y 1 A ASP 1539 ? A ASP 1539 
1540 1 Y 1 A VAL 1540 ? A VAL 1540 
1541 1 Y 1 A GLN 1541 ? A GLN 1541 
1542 1 Y 1 A ARG 1542 ? A ARG 1542 
1543 1 Y 1 A ARG 1543 ? A ARG 1543 
1544 1 Y 1 A TRP 1544 ? A TRP 1544 
1545 1 Y 1 A VAL 1545 ? A VAL 1545 
1546 1 Y 1 A TYR 1546 ? A TYR 1546 
1547 1 Y 1 A LEU 1547 ? A LEU 1547 
1548 1 Y 1 A GLU 1548 ? A GLU 1548 
1549 1 Y 1 A GLY 1549 ? A GLY 1549 
1550 1 Y 1 A ILE 1550 ? A ILE 1550 
1551 1 Y 1 A PHE 1551 ? A PHE 1551 
1552 1 Y 1 A THR 1552 ? A THR 1552 
1553 1 Y 1 A GLY 1553 ? A GLY 1553 
1554 1 Y 1 A SER 1554 ? A SER 1554 
1555 1 Y 1 A ALA 1555 ? A ALA 1555 
1556 1 Y 1 A ASP 1556 ? A ASP 1556 
1557 1 Y 1 A ILE 1557 ? A ILE 1557 
1558 1 Y 1 A LYS 1558 ? A LYS 1558 
1559 1 Y 1 A HIS 1559 ? A HIS 1559 
1560 1 Y 1 A LEU 1560 ? A LEU 1560 
1561 1 Y 1 A LEU 1561 ? A LEU 1561 
1562 1 Y 1 A PRO 1562 ? A PRO 1562 
1563 1 Y 1 A VAL 1563 ? A VAL 1563 
1564 1 Y 1 A GLU 1564 ? A GLU 1564 
1565 1 Y 1 A THR 1565 ? A THR 1565 
1566 1 Y 1 A GLN 1566 ? A GLN 1566 
1567 1 Y 1 A ARG 1567 ? A ARG 1567 
1568 1 Y 1 A PHE 1568 ? A PHE 1568 
1569 1 Y 1 A GLN 1569 ? A GLN 1569 
1570 1 Y 1 A SER 1570 ? A SER 1570 
1571 1 Y 1 A ILE 1571 ? A ILE 1571 
1572 1 Y 1 A SER 1572 ? A SER 1572 
1573 1 Y 1 A THR 1573 ? A THR 1573 
1574 1 Y 1 A GLU 1574 ? A GLU 1574 
1575 1 Y 1 A PHE 1575 ? A PHE 1575 
1576 1 Y 1 A LEU 1576 ? A LEU 1576 
1577 1 Y 1 A ALA 1577 ? A ALA 1577 
1578 1 Y 1 A LEU 1578 ? A LEU 1578 
1579 1 Y 1 A MET 1579 ? A MET 1579 
1580 1 Y 1 A LYS 1580 ? A LYS 1580 
1581 1 Y 1 A LYS 1581 ? A LYS 1581 
1582 1 Y 1 A VAL 1582 ? A VAL 1582 
1583 1 Y 1 A SER 1583 ? A SER 1583 
1584 1 Y 1 A LYS 1584 ? A LYS 1584 
1585 1 Y 1 A SER 1585 ? A SER 1585 
1586 1 Y 1 A PRO 1586 ? A PRO 1586 
1587 1 Y 1 A LEU 1587 ? A LEU 1587 
1588 1 Y 1 A VAL 1588 ? A VAL 1588 
1589 1 Y 1 A MET 1589 ? A MET 1589 
1590 1 Y 1 A ASP 1590 ? A ASP 1590 
1591 1 Y 1 A VAL 1591 ? A VAL 1591 
1592 1 Y 1 A LEU 1592 ? A LEU 1592 
1593 1 Y 1 A ASN 1593 ? A ASN 1593 
1594 1 Y 1 A ILE 1594 ? A ILE 1594 
1595 1 Y 1 A GLN 1595 ? A GLN 1595 
1596 1 Y 1 A GLY 1596 ? A GLY 1596 
1597 1 Y 1 A VAL 1597 ? A VAL 1597 
1598 1 Y 1 A GLN 1598 ? A GLN 1598 
1599 1 Y 1 A ARG 1599 ? A ARG 1599 
1600 1 Y 1 A SER 1600 ? A SER 1600 
1601 1 Y 1 A LEU 1601 ? A LEU 1601 
1602 1 Y 1 A GLU 1602 ? A GLU 1602 
1603 1 Y 1 A ARG 1603 ? A ARG 1603 
1604 1 Y 1 A LEU 1604 ? A LEU 1604 
1605 1 Y 1 A ALA 1605 ? A ALA 1605 
1606 1 Y 1 A ASP 1606 ? A ASP 1606 
1607 1 Y 1 A LEU 1607 ? A LEU 1607 
1608 1 Y 1 A LEU 1608 ? A LEU 1608 
1609 1 Y 1 A GLY 1609 ? A GLY 1609 
1610 1 Y 1 A LYS 1610 ? A LYS 1610 
1611 1 Y 1 A ILE 1611 ? A ILE 1611 
1612 1 Y 1 A GLN 1612 ? A GLN 1612 
1613 1 Y 1 A LYS 1613 ? A LYS 1613 
1614 1 Y 1 A ALA 1614 ? A ALA 1614 
1615 1 Y 1 A PRO 2020 ? A PRO 2020 
1616 1 Y 1 A GLY 2021 ? A GLY 2021 
1617 1 Y 1 A TYR 2022 ? A TYR 2022 
1618 1 Y 1 A ALA 2023 ? A ALA 2023 
1619 1 Y 1 A GLY 2024 ? A GLY 2024 
1620 1 Y 1 A ARG 2025 ? A ARG 2025 
1621 1 Y 1 A SER 2026 ? A SER 2026 
1622 1 Y 1 A LYS 2115 ? A LYS 2115 
1623 1 Y 1 A GLU 2116 ? A GLU 2116 
1624 1 Y 1 A GLU 2117 ? A GLU 2117 
1625 1 Y 1 A ARG 2118 ? A ARG 2118 
1626 1 Y 1 A GLY 2119 ? A GLY 2119 
1627 1 Y 1 A GLU 2120 ? A GLU 2120 
1628 1 Y 1 A ALA 2121 ? A ALA 2121 
1629 1 Y 1 A VAL 2122 ? A VAL 2122 
1630 1 Y 1 A ASP 2123 ? A ASP 2123 
1631 1 Y 1 A GLU 2124 ? A GLU 2124 
1632 1 Y 1 A GLY 2125 ? A GLY 2125 
1633 1 Y 1 A GLU 2126 ? A GLU 2126 
1634 1 Y 1 A GLU 2389 ? A GLU 2389 
1635 1 Y 1 A GLY 2390 ? A GLY 2390 
1636 1 Y 1 A GLU 2391 ? A GLU 2391 
1637 1 Y 1 A ASP 2392 ? A ASP 2392 
1638 1 Y 1 A GLU 2393 ? A GLU 2393 
1639 1 Y 1 A ALA 2394 ? A ALA 2394 
1640 1 Y 1 A GLN 2395 ? A GLN 2395 
1641 1 Y 1 A ARG 2396 ? A ARG 2396 
1642 1 Y 1 A ARG 2397 ? A ARG 2397 
1643 1 Y 1 A ARG 2398 ? A ARG 2398 
1644 1 Y 1 A LYS 2399 ? A LYS 2399 
1645 1 Y 1 A GLY 2400 ? A GLY 2400 
1646 1 Y 1 A LYS 2401 ? A LYS 2401 
1647 1 Y 1 A GLU 2402 ? A GLU 2402 
1648 1 Y 1 A ASP 2403 ? A ASP 2403 
1649 1 Y 1 A GLU 2404 ? A GLU 2404 
1650 1 Y 1 A GLY 2405 ? A GLY 2405 
1651 1 Y 1 A GLU 2406 ? A GLU 2406 
1652 1 Y 1 A GLU 2407 ? A GLU 2407 
1653 1 Y 1 A ALA 2408 ? A ALA 2408 
1654 1 Y 1 A ALA 2409 ? A ALA 2409 
1655 1 Y 1 A SER 3071 ? A SER 3071 
1656 1 Y 1 A SER 3072 ? A SER 3072 
1657 1 Y 1 A GLU 3073 ? A GLU 3073 
1658 1 Y 1 A GLY 3074 ? A GLY 3074 
1659 1 Y 1 A LEU 3075 ? A LEU 3075 
1660 1 Y 1 A LYS 3076 ? A LYS 3076 
1661 1 Y 1 A ASP 3077 ? A ASP 3077 
1662 1 Y 1 A ARG 3078 ? A ARG 3078 
1663 1 Y 1 A ALA 3079 ? A ALA 3079 
1664 1 Y 1 A ALA 3080 ? A ALA 3080 
1665 1 Y 1 A THR 3081 ? A THR 3081 
1666 1 Y 1 A ASP 3221 ? A ASP 3221 
1667 1 Y 1 A LEU 3222 ? A LEU 3222 
1668 1 Y 1 A ARG 3223 ? A ARG 3223 
1669 1 Y 1 A ILE 3224 ? A ILE 3224 
1670 1 Y 1 A LYS 3225 ? A LYS 3225 
1671 1 Y 1 A SER 3226 ? A SER 3226 
1672 1 Y 1 A GLN 3227 ? A GLN 3227 
1673 1 Y 1 A GLU 3228 ? A GLU 3228 
1674 1 Y 1 A LEU 3229 ? A LEU 3229 
1675 1 Y 1 A GLU 3230 ? A GLU 3230 
1676 1 Y 1 A VAL 3231 ? A VAL 3231 
1677 1 Y 1 A LYS 3232 ? A LYS 3232 
1678 1 Y 1 A ASN 3233 ? A ASN 3233 
1679 1 Y 1 A ALA 3234 ? A ALA 3234 
1680 1 Y 1 A ALA 3235 ? A ALA 3235 
1681 1 Y 1 A ALA 3236 ? A ALA 3236 
1682 1 Y 1 A ASN 3237 ? A ASN 3237 
1683 1 Y 1 A ASP 3238 ? A ASP 3238 
1684 1 Y 1 A LYS 3239 ? A LYS 3239 
1685 1 Y 1 A LEU 3240 ? A LEU 3240 
1686 1 Y 1 A LYS 3241 ? A LYS 3241 
1687 1 Y 1 A LYS 3242 ? A LYS 3242 
1688 1 Y 1 A MET 3243 ? A MET 3243 
1689 1 Y 1 A VAL 3244 ? A VAL 3244 
1690 1 Y 1 A LYS 3245 ? A LYS 3245 
1691 1 Y 1 A ASP 3246 ? A ASP 3246 
1692 1 Y 1 A GLN 3247 ? A GLN 3247 
1693 1 Y 1 A GLN 3248 ? A GLN 3248 
1694 1 Y 1 A GLU 3249 ? A GLU 3249 
1695 1 Y 1 A ALA 3250 ? A ALA 3250 
1696 1 Y 1 A GLU 3251 ? A GLU 3251 
1697 1 Y 1 A LYS 3252 ? A LYS 3252 
1698 1 Y 1 A LYS 3253 ? A LYS 3253 
1699 1 Y 1 A LYS 3254 ? A LYS 3254 
1700 1 Y 1 A VAL 3255 ? A VAL 3255 
1701 1 Y 1 A MET 3256 ? A MET 3256 
1702 1 Y 1 A SER 3257 ? A SER 3257 
1703 1 Y 1 A GLN 3258 ? A GLN 3258 
1704 1 Y 1 A GLU 3259 ? A GLU 3259 
1705 1 Y 1 A ILE 3260 ? A ILE 3260 
1706 1 Y 1 A GLN 3261 ? A GLN 3261 
1707 1 Y 1 A GLU 3262 ? A GLU 3262 
1708 1 Y 1 A GLN 3263 ? A GLN 3263 
1709 1 Y 1 A LEU 3264 ? A LEU 3264 
1710 1 Y 1 A HIS 3265 ? A HIS 3265 
1711 1 Y 1 A LYS 3266 ? A LYS 3266 
1712 1 Y 1 A GLN 3267 ? A GLN 3267 
1713 1 Y 1 A GLN 3268 ? A GLN 3268 
1714 1 Y 1 A GLU 3269 ? A GLU 3269 
1715 1 Y 1 A VAL 3270 ? A VAL 3270 
1716 1 Y 1 A ILE 3271 ? A ILE 3271 
1717 1 Y 1 A ALA 3272 ? A ALA 3272 
1718 1 Y 1 A ASP 3273 ? A ASP 3273 
1719 1 Y 1 A LYS 3274 ? A LYS 3274 
1720 1 Y 1 A GLN 3275 ? A GLN 3275 
1721 1 Y 1 A MET 3276 ? A MET 3276 
1722 1 Y 1 A SER 3277 ? A SER 3277 
1723 1 Y 1 A VAL 3278 ? A VAL 3278 
1724 1 Y 1 A LYS 3279 ? A LYS 3279 
1725 1 Y 1 A GLU 3280 ? A GLU 3280 
1726 1 Y 1 A ASP 3281 ? A ASP 3281 
1727 1 Y 1 A LEU 3282 ? A LEU 3282 
1728 1 Y 1 A ASP 3283 ? A ASP 3283 
1729 1 Y 1 A LYS 3284 ? A LYS 3284 
1730 1 Y 1 A VAL 3285 ? A VAL 3285 
1731 1 Y 1 A GLU 3286 ? A GLU 3286 
1732 1 Y 1 A PRO 3287 ? A PRO 3287 
1733 1 Y 1 A ALA 3288 ? A ALA 3288 
1734 1 Y 1 A VAL 3289 ? A VAL 3289 
1735 1 Y 1 A ILE 3290 ? A ILE 3290 
1736 1 Y 1 A GLU 3291 ? A GLU 3291 
1737 1 Y 1 A ALA 3292 ? A ALA 3292 
1738 1 Y 1 A GLN 3293 ? A GLN 3293 
1739 1 Y 1 A ASN 3294 ? A ASN 3294 
1740 1 Y 1 A ALA 3295 ? A ALA 3295 
1741 1 Y 1 A VAL 3296 ? A VAL 3296 
1742 1 Y 1 A LYS 3297 ? A LYS 3297 
1743 1 Y 1 A SER 3298 ? A SER 3298 
1744 1 Y 1 A ILE 3299 ? A ILE 3299 
1745 1 Y 1 A LYS 3300 ? A LYS 3300 
1746 1 Y 1 A LYS 3301 ? A LYS 3301 
1747 1 Y 1 A GLN 3302 ? A GLN 3302 
1748 1 Y 1 A HIS 3303 ? A HIS 3303 
1749 1 Y 1 A LEU 3304 ? A LEU 3304 
1750 1 Y 1 A VAL 3305 ? A VAL 3305 
1751 1 Y 1 A GLU 3306 ? A GLU 3306 
1752 1 Y 1 A VAL 3307 ? A VAL 3307 
1753 1 Y 1 A ARG 3308 ? A ARG 3308 
1754 1 Y 1 A SER 3309 ? A SER 3309 
1755 1 Y 1 A MET 3310 ? A MET 3310 
1756 1 Y 1 A ALA 3311 ? A ALA 3311 
1757 1 Y 1 A ASN 3312 ? A ASN 3312 
1758 1 Y 1 A PRO 3313 ? A PRO 3313 
1759 1 Y 1 A PRO 3314 ? A PRO 3314 
1760 1 Y 1 A ALA 3315 ? A ALA 3315 
1761 1 Y 1 A ALA 3316 ? A ALA 3316 
1762 1 Y 1 A VAL 3317 ? A VAL 3317 
1763 1 Y 1 A LYS 3318 ? A LYS 3318 
1764 1 Y 1 A LEU 3319 ? A LEU 3319 
1765 1 Y 1 A ALA 3320 ? A ALA 3320 
1766 1 Y 1 A LEU 3321 ? A LEU 3321 
1767 1 Y 1 A GLU 3322 ? A GLU 3322 
1768 1 Y 1 A SER 3323 ? A SER 3323 
1769 1 Y 1 A ILE 3324 ? A ILE 3324 
1770 1 Y 1 A CYS 3325 ? A CYS 3325 
1771 1 Y 1 A LEU 3326 ? A LEU 3326 
1772 1 Y 1 A LEU 3327 ? A LEU 3327 
1773 1 Y 1 A LEU 3328 ? A LEU 3328 
1774 1 Y 1 A GLY 3329 ? A GLY 3329 
1775 1 Y 1 A GLU 3330 ? A GLU 3330 
1776 1 Y 1 A SER 3331 ? A SER 3331 
1777 1 Y 1 A THR 3332 ? A THR 3332 
1778 1 Y 1 A THR 3333 ? A THR 3333 
1779 1 Y 1 A ASP 3334 ? A ASP 3334 
1780 1 Y 1 A TRP 3335 ? A TRP 3335 
1781 1 Y 1 A LYS 3336 ? A LYS 3336 
1782 1 Y 1 A GLN 3337 ? A GLN 3337 
1783 1 Y 1 A ILE 3338 ? A ILE 3338 
1784 1 Y 1 A ARG 3339 ? A ARG 3339 
1785 1 Y 1 A SER 3340 ? A SER 3340 
1786 1 Y 1 A ILE 3341 ? A ILE 3341 
1787 1 Y 1 A ILE 3342 ? A ILE 3342 
1788 1 Y 1 A MET 3343 ? A MET 3343 
1789 1 Y 1 A ARG 3344 ? A ARG 3344 
1790 1 Y 1 A GLU 3345 ? A GLU 3345 
1791 1 Y 1 A ASN 3346 ? A ASN 3346 
1792 1 Y 1 A PHE 3347 ? A PHE 3347 
1793 1 Y 1 A ILE 3348 ? A ILE 3348 
1794 1 Y 1 A PRO 3349 ? A PRO 3349 
1795 1 Y 1 A THR 3350 ? A THR 3350 
1796 1 Y 1 A ILE 3351 ? A ILE 3351 
1797 1 Y 1 A VAL 3352 ? A VAL 3352 
1798 1 Y 1 A ASN 3353 ? A ASN 3353 
1799 1 Y 1 A PHE 3354 ? A PHE 3354 
1800 1 Y 1 A SER 3355 ? A SER 3355 
1801 1 Y 1 A ALA 3356 ? A ALA 3356 
1802 1 Y 1 A GLU 3357 ? A GLU 3357 
1803 1 Y 1 A GLU 3358 ? A GLU 3358 
1804 1 Y 1 A ILE 3359 ? A ILE 3359 
1805 1 Y 1 A SER 3360 ? A SER 3360 
1806 1 Y 1 A ASP 3361 ? A ASP 3361 
1807 1 Y 1 A ALA 3362 ? A ALA 3362 
1808 1 Y 1 A ILE 3363 ? A ILE 3363 
1809 1 Y 1 A ARG 3364 ? A ARG 3364 
1810 1 Y 1 A GLU 3365 ? A GLU 3365 
1811 1 Y 1 A LYS 3366 ? A LYS 3366 
1812 1 Y 1 A MET 3367 ? A MET 3367 
1813 1 Y 1 A LYS 3368 ? A LYS 3368 
1814 1 Y 1 A LYS 3369 ? A LYS 3369 
1815 1 Y 1 A ASN 3370 ? A ASN 3370 
1816 1 Y 1 A TYR 3371 ? A TYR 3371 
1817 1 Y 1 A MET 3372 ? A MET 3372 
1818 1 Y 1 A SER 3373 ? A SER 3373 
1819 1 Y 1 A ASN 3374 ? A ASN 3374 
1820 1 Y 1 A PRO 3375 ? A PRO 3375 
1821 1 Y 1 A SER 3376 ? A SER 3376 
1822 1 Y 1 A TYR 3377 ? A TYR 3377 
1823 1 Y 1 A ASN 3378 ? A ASN 3378 
1824 1 Y 1 A TYR 3379 ? A TYR 3379 
1825 1 Y 1 A GLU 3380 ? A GLU 3380 
1826 1 Y 1 A ILE 3381 ? A ILE 3381 
1827 1 Y 1 A VAL 3382 ? A VAL 3382 
1828 1 Y 1 A ASN 3383 ? A ASN 3383 
1829 1 Y 1 A ARG 3384 ? A ARG 3384 
1830 1 Y 1 A ALA 3385 ? A ALA 3385 
1831 1 Y 1 A SER 3386 ? A SER 3386 
1832 1 Y 1 A LEU 3387 ? A LEU 3387 
1833 1 Y 1 A ALA 3388 ? A ALA 3388 
1834 1 Y 1 A CYS 3389 ? A CYS 3389 
1835 1 Y 1 A GLY 3390 ? A GLY 3390 
1836 1 Y 1 A PRO 3391 ? A PRO 3391 
1837 1 Y 1 A MET 3392 ? A MET 3392 
1838 1 Y 1 A VAL 3393 ? A VAL 3393 
1839 1 Y 1 A LYS 3394 ? A LYS 3394 
1840 1 Y 1 A TRP 3395 ? A TRP 3395 
1841 1 Y 1 A ALA 3396 ? A ALA 3396 
1842 1 Y 1 A ILE 3397 ? A ILE 3397 
1843 1 Y 1 A ALA 3398 ? A ALA 3398 
1844 1 Y 1 A GLN 3399 ? A GLN 3399 
1845 1 Y 1 A LEU 3400 ? A LEU 3400 
1846 1 Y 1 A ASN 3401 ? A ASN 3401 
1847 1 Y 1 A TYR 3402 ? A TYR 3402 
1848 1 Y 1 A ALA 3403 ? A ALA 3403 
1849 1 Y 1 A ASP 3404 ? A ASP 3404 
1850 1 Y 1 A MET 3405 ? A MET 3405 
1851 1 Y 1 A LEU 3406 ? A LEU 3406 
1852 1 Y 1 A LYS 3407 ? A LYS 3407 
1853 1 Y 1 A ARG 3408 ? A ARG 3408 
1854 1 Y 1 A VAL 3409 ? A VAL 3409 
1855 1 Y 1 A GLU 3410 ? A GLU 3410 
1856 1 Y 1 A PRO 3411 ? A PRO 3411 
1857 1 Y 1 A LEU 3412 ? A LEU 3412 
1858 1 Y 1 A ARG 3413 ? A ARG 3413 
1859 1 Y 1 A ASN 3414 ? A ASN 3414 
1860 1 Y 1 A GLU 3415 ? A GLU 3415 
1861 1 Y 1 A LEU 3416 ? A LEU 3416 
1862 1 Y 1 A GLN 3417 ? A GLN 3417 
1863 1 Y 1 A LYS 3418 ? A LYS 3418 
1864 1 Y 1 A LEU 3419 ? A LEU 3419 
1865 1 Y 1 A GLU 3420 ? A GLU 3420 
1866 1 Y 1 A ASP 3421 ? A ASP 3421 
1867 1 Y 1 A ASP 3422 ? A ASP 3422 
1868 1 Y 1 A ALA 3423 ? A ALA 3423 
1869 1 Y 1 A LYS 3424 ? A LYS 3424 
1870 1 Y 1 A ASP 3425 ? A ASP 3425 
1871 1 Y 1 A ASN 3426 ? A ASN 3426 
1872 1 Y 1 A GLN 3427 ? A GLN 3427 
1873 1 Y 1 A GLN 3428 ? A GLN 3428 
1874 1 Y 1 A LYS 3429 ? A LYS 3429 
1875 1 Y 1 A ALA 3430 ? A ALA 3430 
1876 1 Y 1 A ASN 3431 ? A ASN 3431 
1877 1 Y 1 A GLU 3432 ? A GLU 3432 
1878 1 Y 1 A VAL 3433 ? A VAL 3433 
1879 1 Y 1 A GLU 3434 ? A GLU 3434 
1880 1 Y 1 A GLN 3435 ? A GLN 3435 
1881 1 Y 1 A MET 3436 ? A MET 3436 
1882 1 Y 1 A ILE 3437 ? A ILE 3437 
1883 1 Y 1 A ARG 3438 ? A ARG 3438 
1884 1 Y 1 A ASP 3439 ? A ASP 3439 
1885 1 Y 1 A LEU 3440 ? A LEU 3440 
1886 1 Y 1 A GLU 3441 ? A GLU 3441 
1887 1 Y 1 A ALA 3442 ? A ALA 3442 
1888 1 Y 1 A SER 3443 ? A SER 3443 
1889 1 Y 1 A ILE 3444 ? A ILE 3444 
1890 1 Y 1 A ALA 3445 ? A ALA 3445 
1891 1 Y 1 A ARG 3446 ? A ARG 3446 
1892 1 Y 1 A TYR 3447 ? A TYR 3447 
1893 1 Y 1 A LYS 3448 ? A LYS 3448 
1894 1 Y 1 A GLU 3449 ? A GLU 3449 
1895 1 Y 1 A GLU 3450 ? A GLU 3450 
1896 1 Y 1 A TYR 3451 ? A TYR 3451 
1897 1 Y 1 A ALA 3452 ? A ALA 3452 
1898 1 Y 1 A VAL 3453 ? A VAL 3453 
1899 1 Y 1 A LEU 3454 ? A LEU 3454 
1900 1 Y 1 A ILE 3455 ? A ILE 3455 
1901 1 Y 1 A SER 3456 ? A SER 3456 
1902 1 Y 1 A GLU 3457 ? A GLU 3457 
1903 1 Y 1 A ALA 3458 ? A ALA 3458 
1904 1 Y 1 A GLN 3459 ? A GLN 3459 
1905 1 Y 1 A ALA 3460 ? A ALA 3460 
1906 1 Y 1 A ILE 3461 ? A ILE 3461 
1907 1 Y 1 A LYS 3462 ? A LYS 3462 
1908 1 Y 1 A ALA 3463 ? A ALA 3463 
1909 1 Y 1 A ASP 3464 ? A ASP 3464 
1910 1 Y 1 A LEU 3465 ? A LEU 3465 
1911 1 Y 1 A ALA 3466 ? A ALA 3466 
1912 1 Y 1 A ALA 3467 ? A ALA 3467 
1913 1 Y 1 A VAL 3468 ? A VAL 3468 
1914 1 Y 1 A GLU 3469 ? A GLU 3469 
1915 1 Y 1 A ALA 3470 ? A ALA 3470 
1916 1 Y 1 A MET 4348 ? A MET 4348 
1917 1 Y 1 A LEU 4349 ? A LEU 4349 
1918 1 Y 1 A GLU 4350 ? A GLU 4350 
1919 1 Y 1 A ASP 4351 ? A ASP 4351 
1920 1 Y 1 A GLU 4352 ? A GLU 4352 
1921 1 Y 1 A ASP 4353 ? A ASP 4353 
1922 1 Y 1 A ASP 4354 ? A ASP 4354 
1923 1 Y 1 A LEU 4355 ? A LEU 4355 
1924 1 Y 1 A ALA 4356 ? A ALA 4356 
1925 1 Y 1 A TYR 4357 ? A TYR 4357 
1926 1 Y 1 A ALA 4358 ? A ALA 4358 
1927 1 Y 1 A GLU 4359 ? A GLU 4359 
1928 1 Y 1 A THR 4360 ? A THR 4360 
1929 1 Y 1 A GLU 4361 ? A GLU 4361 
1930 1 Y 1 A LYS 4362 ? A LYS 4362 
1931 1 Y 1 A LYS 4363 ? A LYS 4363 
1932 1 Y 1 A THR 4364 ? A THR 4364 
1933 1 Y 1 A ARG 4365 ? A ARG 4365 
1934 1 Y 1 A THR 4366 ? A THR 4366 
1935 1 Y 1 A ASP 4367 ? A ASP 4367 
1936 1 Y 1 A SER 4368 ? A SER 4368 
1937 1 Y 1 A THR 4369 ? A THR 4369 
1938 1 Y 1 A SER 4370 ? A SER 4370 
1939 1 Y 1 A ASP 4371 ? A ASP 4371 
1940 1 Y 1 A GLY 4372 ? A GLY 4372 
1941 1 Y 1 A ARG 4373 ? A ARG 4373 
1942 1 Y 1 A PRO 4374 ? A PRO 4374 
1943 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           9BM7 
_em_admin.last_update        2025-05-14 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-7b 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  ? ? ? PHENIX    ? 
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                    9BM7 
_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     . LEU A 1 1615 ? 187.077 186.153 131.482 1.00 191.73 ? 1615 LEU A N     1 
ATOM   2     C CA    . LEU A 1 1615 ? 187.033 187.041 132.638 1.00 191.73 ? 1615 LEU A CA    1 
ATOM   3     C C     . LEU A 1 1615 ? 187.591 186.350 133.878 1.00 191.73 ? 1615 LEU A C     1 
ATOM   4     O O     . LEU A 1 1615 ? 188.413 186.918 134.597 1.00 191.73 ? 1615 LEU A O     1 
ATOM   5     C CB    . LEU A 1 1615 ? 185.602 187.517 132.897 1.00 191.73 ? 1615 LEU A CB    1 
ATOM   6     C CG    . LEU A 1 1615 ? 185.382 188.336 134.170 1.00 191.73 ? 1615 LEU A CG    1 
ATOM   7     C CD1   . LEU A 1 1615 ? 185.899 189.755 133.991 1.00 191.73 ? 1615 LEU A CD1   1 
ATOM   8     C CD2   . LEU A 1 1615 ? 183.912 188.344 134.556 1.00 191.73 ? 1615 LEU A CD2   1 
ATOM   9     N N     . GLY A 1 1616 ? 187.133 185.121 134.126 1.00 190.36 ? 1616 GLY A N     1 
ATOM   10    C CA    . GLY A 1 1616 ? 187.655 184.361 135.251 1.00 190.36 ? 1616 GLY A CA    1 
ATOM   11    C C     . GLY A 1 1616 ? 189.137 184.071 135.115 1.00 190.36 ? 1616 GLY A C     1 
ATOM   12    O O     . GLY A 1 1616 ? 189.876 184.076 136.104 1.00 190.36 ? 1616 GLY A O     1 
ATOM   13    N N     . GLU A 1 1617 ? 189.592 183.817 133.887 1.00 187.81 ? 1617 GLU A N     1 
ATOM   14    C CA    . GLU A 1 1617 ? 191.021 183.638 133.658 1.00 187.81 ? 1617 GLU A CA    1 
ATOM   15    C C     . GLU A 1 1617 ? 191.789 184.912 133.983 1.00 187.81 ? 1617 GLU A C     1 
ATOM   16    O O     . GLU A 1 1617 ? 192.878 184.858 134.568 1.00 187.81 ? 1617 GLU A O     1 
ATOM   17    C CB    . GLU A 1 1617 ? 191.274 183.208 132.213 1.00 187.81 ? 1617 GLU A CB    1 
ATOM   18    C CG    . GLU A 1 1617 ? 192.707 182.782 131.944 1.00 187.81 ? 1617 GLU A CG    1 
ATOM   19    C CD    . GLU A 1 1617 ? 193.317 182.022 133.107 1.00 187.81 ? 1617 GLU A CD    1 
ATOM   20    O OE1   . GLU A 1 1617 ? 192.781 180.953 133.471 1.00 187.81 ? 1617 GLU A OE1   1 
ATOM   21    O OE2   . GLU A 1 1617 ? 194.332 182.497 133.659 1.00 187.81 ? 1617 GLU A OE2   1 
ATOM   22    N N     . TYR A 1 1618 ? 191.238 186.070 133.612 1.00 185.52 ? 1618 TYR A N     1 
ATOM   23    C CA    . TYR A 1 1618 ? 191.891 187.331 133.947 1.00 185.52 ? 1618 TYR A CA    1 
ATOM   24    C C     . TYR A 1 1618 ? 191.923 187.544 135.455 1.00 185.52 ? 1618 TYR A C     1 
ATOM   25    O O     . TYR A 1 1618 ? 192.909 188.056 135.996 1.00 185.52 ? 1618 TYR A O     1 
ATOM   26    C CB    . TYR A 1 1618 ? 191.185 188.495 133.254 1.00 185.52 ? 1618 TYR A CB    1 
ATOM   27    C CG    . TYR A 1 1618 ? 191.838 189.831 133.524 1.00 185.52 ? 1618 TYR A CG    1 
ATOM   28    C CD1   . TYR A 1 1618 ? 193.012 190.191 132.875 1.00 185.52 ? 1618 TYR A CD1   1 
ATOM   29    C CD2   . TYR A 1 1618 ? 191.291 190.724 134.436 1.00 185.52 ? 1618 TYR A CD2   1 
ATOM   30    C CE1   . TYR A 1 1618 ? 193.619 191.407 133.119 1.00 185.52 ? 1618 TYR A CE1   1 
ATOM   31    C CE2   . TYR A 1 1618 ? 191.892 191.944 134.687 1.00 185.52 ? 1618 TYR A CE2   1 
ATOM   32    C CZ    . TYR A 1 1618 ? 193.056 192.279 134.025 1.00 185.52 ? 1618 TYR A CZ    1 
ATOM   33    O OH    . TYR A 1 1618 ? 193.660 193.491 134.271 1.00 185.52 ? 1618 TYR A OH    1 
ATOM   34    N N     . LEU A 1 1619 ? 190.847 187.163 136.149 1.00 180.89 ? 1619 LEU A N     1 
ATOM   35    C CA    . LEU A 1 1619 ? 190.836 187.258 137.605 1.00 180.89 ? 1619 LEU A CA    1 
ATOM   36    C C     . LEU A 1 1619 ? 191.910 186.370 138.219 1.00 180.89 ? 1619 LEU A C     1 
ATOM   37    O O     . LEU A 1 1619 ? 192.604 186.778 139.158 1.00 180.89 ? 1619 LEU A O     1 
ATOM   38    C CB    . LEU A 1 1619 ? 189.457 186.882 138.151 1.00 180.89 ? 1619 LEU A CB    1 
ATOM   39    C CG    . LEU A 1 1619 ? 188.333 187.915 138.034 1.00 180.89 ? 1619 LEU A CG    1 
ATOM   40    C CD1   . LEU A 1 1619 ? 187.121 187.477 138.840 1.00 180.89 ? 1619 LEU A CD1   1 
ATOM   41    C CD2   . LEU A 1 1619 ? 188.805 189.289 138.479 1.00 180.89 ? 1619 LEU A CD2   1 
ATOM   42    N N     . GLU A 1 1620 ? 192.063 185.150 137.700 1.00 177.88 ? 1620 GLU A N     1 
ATOM   43    C CA    . GLU A 1 1620 ? 193.098 184.257 138.212 1.00 177.88 ? 1620 GLU A CA    1 
ATOM   44    C C     . GLU A 1 1620 ? 194.490 184.814 137.936 1.00 177.88 ? 1620 GLU A C     1 
ATOM   45    O O     . GLU A 1 1620 ? 195.393 184.694 138.771 1.00 177.88 ? 1620 GLU A O     1 
ATOM   46    C CB    . GLU A 1 1620 ? 192.946 182.863 137.606 1.00 177.88 ? 1620 GLU A CB    1 
ATOM   47    C CG    . GLU A 1 1620 ? 193.677 181.778 138.382 1.00 177.88 ? 1620 GLU A CG    1 
ATOM   48    C CD    . GLU A 1 1620 ? 195.074 181.517 137.855 1.00 177.88 ? 1620 GLU A CD    1 
ATOM   49    O OE1   . GLU A 1 1620 ? 195.447 182.115 136.824 1.00 177.88 ? 1620 GLU A OE1   1 
ATOM   50    O OE2   . GLU A 1 1620 ? 195.803 180.715 138.476 1.00 177.88 ? 1620 GLU A OE2   1 
ATOM   51    N N     . ARG A 1 1621 ? 194.686 185.418 136.761 1.00 178.88 ? 1621 ARG A N     1 
ATOM   52    C CA    . ARG A 1 1621 ? 195.976 186.026 136.451 1.00 178.88 ? 1621 ARG A CA    1 
ATOM   53    C C     . ARG A 1 1621 ? 196.272 187.197 137.381 1.00 178.88 ? 1621 ARG A C     1 
ATOM   54    O O     . ARG A 1 1621 ? 197.412 187.378 137.823 1.00 178.88 ? 1621 ARG A O     1 
ATOM   55    C CB    . ARG A 1 1621 ? 196.009 186.480 134.992 1.00 178.88 ? 1621 ARG A CB    1 
ATOM   56    C CG    . ARG A 1 1621 ? 196.061 185.343 133.987 1.00 178.88 ? 1621 ARG A CG    1 
ATOM   57    C CD    . ARG A 1 1621 ? 196.639 185.810 132.662 1.00 178.88 ? 1621 ARG A CD    1 
ATOM   58    N NE    . ARG A 1 1621 ? 195.727 186.697 131.950 1.00 178.88 ? 1621 ARG A NE    1 
ATOM   59    C CZ    . ARG A 1 1621 ? 194.883 186.302 131.006 1.00 178.88 ? 1621 ARG A CZ    1 
ATOM   60    N NH1   . ARG A 1 1621 ? 194.802 185.034 130.639 1.00 178.88 ? 1621 ARG A NH1   1 
ATOM   61    N NH2   . ARG A 1 1621 ? 194.101 187.202 130.418 1.00 178.88 ? 1621 ARG A NH2   1 
ATOM   62    N N     . GLU A 1 1622 ? 195.256 188.011 137.676 1.00 168.05 ? 1622 GLU A N     1 
ATOM   63    C CA    . GLU A 1 1622 ? 195.434 189.104 138.626 1.00 168.05 ? 1622 GLU A CA    1 
ATOM   64    C C     . GLU A 1 1622 ? 195.765 188.571 140.015 1.00 168.05 ? 1622 GLU A C     1 
ATOM   65    O O     . GLU A 1 1622 ? 196.593 189.148 140.731 1.00 168.05 ? 1622 GLU A O     1 
ATOM   66    C CB    . GLU A 1 1622 ? 194.178 189.972 138.666 1.00 168.05 ? 1622 GLU A CB    1 
ATOM   67    C CG    . GLU A 1 1622 ? 193.925 190.761 137.392 1.00 168.05 ? 1622 GLU A CG    1 
ATOM   68    C CD    . GLU A 1 1622 ? 195.036 191.749 137.084 1.00 168.05 ? 1622 GLU A CD    1 
ATOM   69    O OE1   . GLU A 1 1622 ? 195.192 192.728 137.843 1.00 168.05 ? 1622 GLU A OE1   1 
ATOM   70    O OE2   . GLU A 1 1622 ? 195.750 191.549 136.080 1.00 168.05 ? 1622 GLU A OE2   1 
ATOM   71    N N     . ARG A 1 1623 ? 195.120 187.472 140.415 1.00 151.32 ? 1623 ARG A N     1 
ATOM   72    C CA    . ARG A 1 1623 ? 195.448 186.840 141.688 1.00 151.32 ? 1623 ARG A CA    1 
ATOM   73    C C     . ARG A 1 1623 ? 196.892 186.354 141.701 1.00 151.32 ? 1623 ARG A C     1 
ATOM   74    O O     . ARG A 1 1623 ? 197.591 186.482 142.711 1.00 151.32 ? 1623 ARG A O     1 
ATOM   75    C CB    . ARG A 1 1623 ? 194.498 185.672 141.957 1.00 151.32 ? 1623 ARG A CB    1 
ATOM   76    C CG    . ARG A 1 1623 ? 193.100 186.062 142.411 1.00 151.32 ? 1623 ARG A CG    1 
ATOM   77    C CD    . ARG A 1 1623 ? 192.073 185.056 141.906 1.00 151.32 ? 1623 ARG A CD    1 
ATOM   78    N NE    . ARG A 1 1623 ? 191.189 184.579 142.963 1.00 151.32 ? 1623 ARG A NE    1 
ATOM   79    C CZ    . ARG A 1 1623 ? 189.977 185.059 143.202 1.00 151.32 ? 1623 ARG A CZ    1 
ATOM   80    N NH1   . ARG A 1 1623 ? 189.461 186.031 142.470 1.00 151.32 ? 1623 ARG A NH1   1 
ATOM   81    N NH2   . ARG A 1 1623 ? 189.262 184.546 144.199 1.00 151.32 ? 1623 ARG A NH2   1 
ATOM   82    N N     . SER A 1 1624 ? 197.349 185.780 140.588 1.00 155.96 ? 1624 SER A N     1 
ATOM   83    C CA    . SER A 1 1624 ? 198.720 185.286 140.516 1.00 155.96 ? 1624 SER A CA    1 
ATOM   84    C C     . SER A 1 1624 ? 199.726 186.430 140.555 1.00 155.96 ? 1624 SER A C     1 
ATOM   85    O O     . SER A 1 1624 ? 200.815 186.285 141.120 1.00 155.96 ? 1624 SER A O     1 
ATOM   86    C CB    . SER A 1 1624 ? 198.909 184.445 139.256 1.00 155.96 ? 1624 SER A CB    1 
ATOM   87    O OG    . SER A 1 1624 ? 200.059 183.625 139.367 1.00 155.96 ? 1624 SER A OG    1 
ATOM   88    N N     . SER A 1 1625 ? 199.390 187.567 139.941 1.00 144.01 ? 1625 SER A N     1 
ATOM   89    C CA    . SER A 1 1625 ? 200.284 188.721 139.992 1.00 144.01 ? 1625 SER A CA    1 
ATOM   90    C C     . SER A 1 1625 ? 200.448 189.228 141.420 1.00 144.01 ? 1625 SER A C     1 
ATOM   91    O O     . SER A 1 1625 ? 201.563 189.546 141.851 1.00 144.01 ? 1625 SER A O     1 
ATOM   92    C CB    . SER A 1 1625 ? 199.759 189.835 139.086 1.00 144.01 ? 1625 SER A CB    1 
ATOM   93    O OG    . SER A 1 1625 ? 200.768 190.794 138.823 1.00 144.01 ? 1625 SER A OG    1 
ATOM   94    N N     . PHE A 1 1626 ? 199.350 189.314 142.164 1.00 130.49 ? 1626 PHE A N     1 
ATOM   95    C CA    . PHE A 1 1626 ? 199.371 189.737 143.564 1.00 130.49 ? 1626 PHE A CA    1 
ATOM   96    C C     . PHE A 1 1626 ? 198.766 188.637 144.421 1.00 130.49 ? 1626 PHE A C     1 
ATOM   97    O O     . PHE A 1 1626 ? 197.530 188.529 144.510 1.00 130.49 ? 1626 PHE A O     1 
ATOM   98    C CB    . PHE A 1 1626 ? 198.608 191.043 143.749 1.00 130.49 ? 1626 PHE A CB    1 
ATOM   99    C CG    . PHE A 1 1626 ? 198.901 191.731 145.044 1.00 130.49 ? 1626 PHE A CG    1 
ATOM   100   C CD1   . PHE A 1 1626 ? 200.194 192.089 145.371 1.00 130.49 ? 1626 PHE A CD1   1 
ATOM   101   C CD2   . PHE A 1 1626 ? 197.883 192.021 145.934 1.00 130.49 ? 1626 PHE A CD2   1 
ATOM   102   C CE1   . PHE A 1 1626 ? 200.470 192.726 146.561 1.00 130.49 ? 1626 PHE A CE1   1 
ATOM   103   C CE2   . PHE A 1 1626 ? 198.152 192.657 147.126 1.00 130.49 ? 1626 PHE A CE2   1 
ATOM   104   C CZ    . PHE A 1 1626 ? 199.447 193.010 147.440 1.00 130.49 ? 1626 PHE A CZ    1 
ATOM   105   N N     . PRO A 1 1627 ? 199.582 187.810 145.075 1.00 115.97 ? 1627 PRO A N     1 
ATOM   106   C CA    . PRO A 1 1627 ? 199.034 186.628 145.759 1.00 115.97 ? 1627 PRO A CA    1 
ATOM   107   C C     . PRO A 1 1627 ? 198.012 186.959 146.826 1.00 115.97 ? 1627 PRO A C     1 
ATOM   108   O O     . PRO A 1 1627 ? 197.112 186.151 147.082 1.00 115.97 ? 1627 PRO A O     1 
ATOM   109   C CB    . PRO A 1 1627 ? 200.280 185.967 146.365 1.00 115.97 ? 1627 PRO A CB    1 
ATOM   110   C CG    . PRO A 1 1627 ? 201.433 186.531 145.602 1.00 115.97 ? 1627 PRO A CG    1 
ATOM   111   C CD    . PRO A 1 1627 ? 201.037 187.924 145.248 1.00 115.97 ? 1627 PRO A CD    1 
ATOM   112   N N     . ARG A 1 1628 ? 198.114 188.132 147.451 1.00 112.82 ? 1628 ARG A N     1 
ATOM   113   C CA    . ARG A 1 1628 ? 197.192 188.487 148.521 1.00 112.82 ? 1628 ARG A CA    1 
ATOM   114   C C     . ARG A 1 1628 ? 195.763 188.652 148.031 1.00 112.82 ? 1628 ARG A C     1 
ATOM   115   O O     . ARG A 1 1628 ? 194.838 188.661 148.850 1.00 112.82 ? 1628 ARG A O     1 
ATOM   116   C CB    . ARG A 1 1628 ? 197.661 189.767 149.203 1.00 112.82 ? 1628 ARG A CB    1 
ATOM   117   C CG    . ARG A 1 1628 ? 198.919 189.584 150.017 1.00 112.82 ? 1628 ARG A CG    1 
ATOM   118   C CD    . ARG A 1 1628 ? 198.965 190.562 151.164 1.00 112.82 ? 1628 ARG A CD    1 
ATOM   119   N NE    . ARG A 1 1628 ? 200.322 190.751 151.656 1.00 112.82 ? 1628 ARG A NE    1 
ATOM   120   C CZ    . ARG A 1 1628 ? 200.737 190.376 152.856 1.00 112.82 ? 1628 ARG A CZ    1 
ATOM   121   N NH1   . ARG A 1 1628 ? 199.916 189.809 153.724 1.00 112.82 ? 1628 ARG A NH1   1 
ATOM   122   N NH2   . ARG A 1 1628 ? 202.006 190.577 153.196 1.00 112.82 ? 1628 ARG A NH2   1 
ATOM   123   N N     . PHE A 1 1629 ? 195.557 188.776 146.720 1.00 126.47 ? 1629 PHE A N     1 
ATOM   124   C CA    . PHE A 1 1629 ? 194.204 188.877 146.194 1.00 126.47 ? 1629 PHE A CA    1 
ATOM   125   C C     . PHE A 1 1629 ? 193.406 187.599 146.399 1.00 126.47 ? 1629 PHE A C     1 
ATOM   126   O O     . PHE A 1 1629 ? 192.179 187.624 146.275 1.00 126.47 ? 1629 PHE A O     1 
ATOM   127   C CB    . PHE A 1 1629 ? 194.241 189.223 144.707 1.00 126.47 ? 1629 PHE A CB    1 
ATOM   128   C CG    . PHE A 1 1629 ? 194.343 190.691 144.431 1.00 126.47 ? 1629 PHE A CG    1 
ATOM   129   C CD1   . PHE A 1 1629 ? 193.816 191.613 145.314 1.00 126.47 ? 1629 PHE A CD1   1 
ATOM   130   C CD2   . PHE A 1 1629 ? 194.967 191.148 143.285 1.00 126.47 ? 1629 PHE A CD2   1 
ATOM   131   C CE1   . PHE A 1 1629 ? 193.909 192.965 145.060 1.00 126.47 ? 1629 PHE A CE1   1 
ATOM   132   C CE2   . PHE A 1 1629 ? 195.064 192.498 143.026 1.00 126.47 ? 1629 PHE A CE2   1 
ATOM   133   C CZ    . PHE A 1 1629 ? 194.533 193.407 143.914 1.00 126.47 ? 1629 PHE A CZ    1 
ATOM   134   N N     . TYR A 1 1630 ? 194.068 186.483 146.703 1.00 124.25 ? 1630 TYR A N     1 
ATOM   135   C CA    . TYR A 1 1630 ? 193.340 185.238 146.900 1.00 124.25 ? 1630 TYR A CA    1 
ATOM   136   C C     . TYR A 1 1630 ? 192.447 185.280 148.130 1.00 124.25 ? 1630 TYR A C     1 
ATOM   137   O O     . TYR A 1 1630 ? 191.516 184.474 148.231 1.00 124.25 ? 1630 TYR A O     1 
ATOM   138   C CB    . TYR A 1 1630 ? 194.316 184.070 147.004 1.00 124.25 ? 1630 TYR A CB    1 
ATOM   139   C CG    . TYR A 1 1630 ? 194.779 183.561 145.665 1.00 124.25 ? 1630 TYR A CG    1 
ATOM   140   C CD1   . TYR A 1 1630 ? 193.899 182.919 144.808 1.00 124.25 ? 1630 TYR A CD1   1 
ATOM   141   C CD2   . TYR A 1 1630 ? 196.092 183.727 145.254 1.00 124.25 ? 1630 TYR A CD2   1 
ATOM   142   C CE1   . TYR A 1 1630 ? 194.315 182.452 143.581 1.00 124.25 ? 1630 TYR A CE1   1 
ATOM   143   C CE2   . TYR A 1 1630 ? 196.518 183.264 144.028 1.00 124.25 ? 1630 TYR A CE2   1 
ATOM   144   C CZ    . TYR A 1 1630 ? 195.626 182.627 143.195 1.00 124.25 ? 1630 TYR A CZ    1 
ATOM   145   O OH    . TYR A 1 1630 ? 196.045 182.163 141.969 1.00 124.25 ? 1630 TYR A OH    1 
ATOM   146   N N     . PHE A 1 1631 ? 192.703 186.197 149.061 1.00 115.28 ? 1631 PHE A N     1 
ATOM   147   C CA    . PHE A 1 1631 ? 191.868 186.290 150.250 1.00 115.28 ? 1631 PHE A CA    1 
ATOM   148   C C     . PHE A 1 1631 ? 190.516 186.919 149.938 1.00 115.28 ? 1631 PHE A C     1 
ATOM   149   O O     . PHE A 1 1631 ? 189.496 186.510 150.503 1.00 115.28 ? 1631 PHE A O     1 
ATOM   150   C CB    . PHE A 1 1631 ? 192.592 187.082 151.336 1.00 115.28 ? 1631 PHE A CB    1 
ATOM   151   C CG    . PHE A 1 1631 ? 193.936 186.523 151.693 1.00 115.28 ? 1631 PHE A CG    1 
ATOM   152   C CD1   . PHE A 1 1631 ? 194.090 185.174 151.959 1.00 115.28 ? 1631 PHE A CD1   1 
ATOM   153   C CD2   . PHE A 1 1631 ? 195.046 187.343 151.758 1.00 115.28 ? 1631 PHE A CD2   1 
ATOM   154   C CE1   . PHE A 1 1631 ? 195.328 184.656 152.287 1.00 115.28 ? 1631 PHE A CE1   1 
ATOM   155   C CE2   . PHE A 1 1631 ? 196.286 186.830 152.086 1.00 115.28 ? 1631 PHE A CE2   1 
ATOM   156   C CZ    . PHE A 1 1631 ? 196.427 185.485 152.350 1.00 115.28 ? 1631 PHE A CZ    1 
ATOM   157   N N     . VAL A 1 1632 ? 190.484 187.907 149.043 1.00 128.40 ? 1632 VAL A N     1 
ATOM   158   C CA    . VAL A 1 1632 ? 189.230 188.574 148.719 1.00 128.40 ? 1632 VAL A CA    1 
ATOM   159   C C     . VAL A 1 1632 ? 188.468 187.771 147.669 1.00 128.40 ? 1632 VAL A C     1 
ATOM   160   O O     . VAL A 1 1632 ? 189.035 186.977 146.916 1.00 128.40 ? 1632 VAL A O     1 
ATOM   161   C CB    . VAL A 1 1632 ? 189.471 190.020 148.254 1.00 128.40 ? 1632 VAL A CB    1 
ATOM   162   C CG1   . VAL A 1 1632 ? 189.754 190.910 149.444 1.00 128.40 ? 1632 VAL A CG1   1 
ATOM   163   C CG2   . VAL A 1 1632 ? 190.619 190.079 147.272 1.00 128.40 ? 1632 VAL A CG2   1 
ATOM   164   N N     . GLY A 1 1633 ? 187.153 187.992 147.624 1.00 144.31 ? 1633 GLY A N     1 
ATOM   165   C CA    . GLY A 1 1633 ? 186.284 187.201 146.781 1.00 144.31 ? 1633 GLY A CA    1 
ATOM   166   C C     . GLY A 1 1633 ? 186.379 187.546 145.308 1.00 144.31 ? 1633 GLY A C     1 
ATOM   167   O O     . GLY A 1 1633 ? 186.928 188.571 144.904 1.00 144.31 ? 1633 GLY A O     1 
ATOM   168   N N     . ASP A 1 1634 ? 185.823 186.648 144.491 1.00 152.15 ? 1634 ASP A N     1 
ATOM   169   C CA    . ASP A 1 1634 ? 185.835 186.851 143.046 1.00 152.15 ? 1634 ASP A CA    1 
ATOM   170   C C     . ASP A 1 1634 ? 185.049 188.097 142.664 1.00 152.15 ? 1634 ASP A C     1 
ATOM   171   O O     . ASP A 1 1634 ? 185.517 188.919 141.870 1.00 152.15 ? 1634 ASP A O     1 
ATOM   172   C CB    . ASP A 1 1634 ? 185.277 185.616 142.339 1.00 152.15 ? 1634 ASP A CB    1 
ATOM   173   C CG    . ASP A 1 1634 ? 184.082 185.024 143.056 1.00 152.15 ? 1634 ASP A CG    1 
ATOM   174   O OD1   . ASP A 1 1634 ? 183.720 185.541 144.134 1.00 152.15 ? 1634 ASP A OD1   1 
ATOM   175   O OD2   . ASP A 1 1634 ? 183.507 184.042 142.543 1.00 152.15 ? 1634 ASP A OD2   1 
ATOM   176   N N     . GLU A 1 1635 ? 183.850 188.263 143.227 1.00 150.67 ? 1635 GLU A N     1 
ATOM   177   C CA    . GLU A 1 1635 ? 183.121 189.506 143.006 1.00 150.67 ? 1635 GLU A CA    1 
ATOM   178   C C     . GLU A 1 1635 ? 183.837 190.669 143.677 1.00 150.67 ? 1635 GLU A C     1 
ATOM   179   O O     . GLU A 1 1635 ? 183.818 191.798 143.173 1.00 150.67 ? 1635 GLU A O     1 
ATOM   180   C CB    . GLU A 1 1635 ? 181.677 189.381 143.503 1.00 150.67 ? 1635 GLU A CB    1 
ATOM   181   C CG    . GLU A 1 1635 ? 181.452 189.665 144.987 1.00 150.67 ? 1635 GLU A CG    1 
ATOM   182   C CD    . GLU A 1 1635 ? 182.277 188.780 145.897 1.00 150.67 ? 1635 GLU A CD    1 
ATOM   183   O OE1   . GLU A 1 1635 ? 182.723 189.272 146.955 1.00 150.67 ? 1635 GLU A OE1   1 
ATOM   184   O OE2   . GLU A 1 1635 ? 182.479 187.595 145.560 1.00 150.67 ? 1635 GLU A OE2   1 
ATOM   185   N N     . ASP A 1 1636 ? 184.498 190.407 144.805 1.00 149.88 ? 1636 ASP A N     1 
ATOM   186   C CA    . ASP A 1 1636 ? 185.299 191.441 145.444 1.00 149.88 ? 1636 ASP A CA    1 
ATOM   187   C C     . ASP A 1 1636 ? 186.472 191.837 144.559 1.00 149.88 ? 1636 ASP A C     1 
ATOM   188   O O     . ASP A 1 1636 ? 186.776 193.024 144.411 1.00 149.88 ? 1636 ASP A O     1 
ATOM   189   C CB    . ASP A 1 1636 ? 185.782 190.961 146.812 1.00 149.88 ? 1636 ASP A CB    1 
ATOM   190   C CG    . ASP A 1 1636 ? 185.915 192.093 147.809 1.00 149.88 ? 1636 ASP A CG    1 
ATOM   191   O OD1   . ASP A 1 1636 ? 186.246 193.218 147.384 1.00 149.88 ? 1636 ASP A OD1   1 
ATOM   192   O OD2   . ASP A 1 1636 ? 185.686 191.862 149.014 1.00 149.88 ? 1636 ASP A OD2   1 
ATOM   193   N N     . LEU A 1 1637 ? 187.135 190.854 143.947 1.00 151.33 ? 1637 LEU A N     1 
ATOM   194   C CA    . LEU A 1 1637 ? 188.225 191.175 143.033 1.00 151.33 ? 1637 LEU A CA    1 
ATOM   195   C C     . LEU A 1 1637 ? 187.714 191.913 141.803 1.00 151.33 ? 1637 LEU A C     1 
ATOM   196   O O     . LEU A 1 1637 ? 188.408 192.789 141.272 1.00 151.33 ? 1637 LEU A O     1 
ATOM   197   C CB    . LEU A 1 1637 ? 188.967 189.904 142.625 1.00 151.33 ? 1637 LEU A CB    1 
ATOM   198   C CG    . LEU A 1 1637 ? 190.290 190.133 141.895 1.00 151.33 ? 1637 LEU A CG    1 
ATOM   199   C CD1   . LEU A 1 1637 ? 191.262 190.881 142.788 1.00 151.33 ? 1637 LEU A CD1   1 
ATOM   200   C CD2   . LEU A 1 1637 ? 190.894 188.820 141.435 1.00 151.33 ? 1637 LEU A CD2   1 
ATOM   201   N N     . LEU A 1 1638 ? 186.512 191.570 141.336 1.00 154.31 ? 1638 LEU A N     1 
ATOM   202   C CA    . LEU A 1 1638 ? 185.899 192.320 140.246 1.00 154.31 ? 1638 LEU A CA    1 
ATOM   203   C C     . LEU A 1 1638 ? 185.661 193.766 140.652 1.00 154.31 ? 1638 LEU A C     1 
ATOM   204   O O     . LEU A 1 1638 ? 185.881 194.688 139.860 1.00 154.31 ? 1638 LEU A O     1 
ATOM   205   C CB    . LEU A 1 1638 ? 184.587 191.659 139.828 1.00 154.31 ? 1638 LEU A CB    1 
ATOM   206   C CG    . LEU A 1 1638 ? 184.712 190.357 139.039 1.00 154.31 ? 1638 LEU A CG    1 
ATOM   207   C CD1   . LEU A 1 1638 ? 183.345 189.722 138.837 1.00 154.31 ? 1638 LEU A CD1   1 
ATOM   208   C CD2   . LEU A 1 1638 ? 185.396 190.606 137.705 1.00 154.31 ? 1638 LEU A CD2   1 
ATOM   209   N N     . GLU A 1 1639 ? 185.206 193.982 141.885 1.00 153.51 ? 1639 GLU A N     1 
ATOM   210   C CA    . GLU A 1 1639 ? 185.046 195.342 142.382 1.00 153.51 ? 1639 GLU A CA    1 
ATOM   211   C C     . GLU A 1 1639 ? 186.385 196.067 142.425 1.00 153.51 ? 1639 GLU A C     1 
ATOM   212   O O     . GLU A 1 1639 ? 186.473 197.241 142.050 1.00 153.51 ? 1639 GLU A O     1 
ATOM   213   C CB    . GLU A 1 1639 ? 184.392 195.316 143.765 1.00 153.51 ? 1639 GLU A CB    1 
ATOM   214   C CG    . GLU A 1 1639 ? 184.054 196.683 144.357 1.00 153.51 ? 1639 GLU A CG    1 
ATOM   215   C CD    . GLU A 1 1639 ? 185.253 197.384 144.970 1.00 153.51 ? 1639 GLU A CD    1 
ATOM   216   O OE1   . GLU A 1 1639 ? 186.185 196.686 145.417 1.00 153.51 ? 1639 GLU A OE1   1 
ATOM   217   O OE2   . GLU A 1 1639 ? 185.266 198.632 145.006 1.00 153.51 ? 1639 GLU A OE2   1 
ATOM   218   N N     . ILE A 1 1640 ? 187.438 195.381 142.878 1.00 154.66 ? 1640 ILE A N     1 
ATOM   219   C CA    . ILE A 1 1640 ? 188.753 196.013 142.969 1.00 154.66 ? 1640 ILE A CA    1 
ATOM   220   C C     . ILE A 1 1640 ? 189.244 196.425 141.587 1.00 154.66 ? 1640 ILE A C     1 
ATOM   221   O O     . ILE A 1 1640 ? 189.713 197.550 141.384 1.00 154.66 ? 1640 ILE A O     1 
ATOM   222   C CB    . ILE A 1 1640 ? 189.764 195.081 143.664 1.00 154.66 ? 1640 ILE A CB    1 
ATOM   223   C CG1   . ILE A 1 1640 ? 189.238 194.595 145.014 1.00 154.66 ? 1640 ILE A CG1   1 
ATOM   224   C CG2   . ILE A 1 1640 ? 191.096 195.790 143.853 1.00 154.66 ? 1640 ILE A CG2   1 
ATOM   225   C CD1   . ILE A 1 1640 ? 189.096 195.680 146.045 1.00 154.66 ? 1640 ILE A CD1   1 
ATOM   226   N N     . ILE A 1 1641 ? 189.140 195.520 140.613 1.00 155.13 ? 1641 ILE A N     1 
ATOM   227   C CA    . ILE A 1 1641 ? 189.662 195.825 139.285 1.00 155.13 ? 1641 ILE A CA    1 
ATOM   228   C C     . ILE A 1 1641 ? 188.809 196.888 138.602 1.00 155.13 ? 1641 ILE A C     1 
ATOM   229   O O     . ILE A 1 1641 ? 189.331 197.772 137.913 1.00 155.13 ? 1641 ILE A O     1 
ATOM   230   C CB    . ILE A 1 1641 ? 189.780 194.545 138.435 1.00 155.13 ? 1641 ILE A CB    1 
ATOM   231   C CG1   . ILE A 1 1641 ? 188.416 193.886 138.232 1.00 155.13 ? 1641 ILE A CG1   1 
ATOM   232   C CG2   . ILE A 1 1641 ? 190.747 193.567 139.084 1.00 155.13 ? 1641 ILE A CG2   1 
ATOM   233   C CD1   . ILE A 1 1641 ? 188.429 192.755 137.234 1.00 155.13 ? 1641 ILE A CD1   1 
ATOM   234   N N     . GLY A 1 1642 ? 187.488 196.825 138.781 1.00 151.17 ? 1642 GLY A N     1 
ATOM   235   C CA    . GLY A 1 1642 ? 186.623 197.818 138.171 1.00 151.17 ? 1642 GLY A CA    1 
ATOM   236   C C     . GLY A 1 1642 ? 186.807 199.200 138.765 1.00 151.17 ? 1642 GLY A C     1 
ATOM   237   O O     . GLY A 1 1642 ? 186.748 200.205 138.052 1.00 151.17 ? 1642 GLY A O     1 
ATOM   238   N N     . ASN A 1 1643 ? 187.036 199.273 140.074 1.00 151.14 ? 1643 ASN A N     1 
ATOM   239   C CA    . ASN A 1 1643 ? 187.162 200.544 140.784 1.00 151.14 ? 1643 ASN A CA    1 
ATOM   240   C C     . ASN A 1 1643 ? 188.603 200.844 141.164 1.00 151.14 ? 1643 ASN A C     1 
ATOM   241   O O     . ASN A 1 1643 ? 188.871 201.412 142.225 1.00 151.14 ? 1643 ASN A O     1 
ATOM   242   C CB    . ASN A 1 1643 ? 186.268 200.545 142.018 1.00 151.14 ? 1643 ASN A CB    1 
ATOM   243   C CG    . ASN A 1 1643 ? 184.876 200.036 141.721 1.00 151.14 ? 1643 ASN A CG    1 
ATOM   244   O OD1   . ASN A 1 1643 ? 184.384 199.120 142.375 1.00 151.14 ? 1643 ASN A OD1   1 
ATOM   245   N ND2   . ASN A 1 1643 ? 184.233 200.625 140.722 1.00 151.14 ? 1643 ASN A ND2   1 
ATOM   246   N N     . SER A 1 1644 ? 189.553 200.471 140.307 1.00 150.82 ? 1644 SER A N     1 
ATOM   247   C CA    . SER A 1 1644 ? 190.954 200.749 140.598 1.00 150.82 ? 1644 SER A CA    1 
ATOM   248   C C     . SER A 1 1644 ? 191.239 202.244 140.562 1.00 150.82 ? 1644 SER A C     1 
ATOM   249   O O     . SER A 1 1644 ? 192.083 202.739 141.318 1.00 150.82 ? 1644 SER A O     1 
ATOM   250   C CB    . SER A 1 1644 ? 191.848 200.010 139.604 1.00 150.82 ? 1644 SER A CB    1 
ATOM   251   O OG    . SER A 1 1644 ? 191.349 198.709 139.346 1.00 150.82 ? 1644 SER A OG    1 
ATOM   252   N N     . LYS A 1 1645 ? 190.544 202.978 139.690 1.00 147.47 ? 1645 LYS A N     1 
ATOM   253   C CA    . LYS A 1 1645 ? 190.835 204.397 139.514 1.00 147.47 ? 1645 LYS A CA    1 
ATOM   254   C C     . LYS A 1 1645 ? 190.571 205.187 140.789 1.00 147.47 ? 1645 LYS A C     1 
ATOM   255   O O     . LYS A 1 1645 ? 191.363 206.061 141.159 1.00 147.47 ? 1645 LYS A O     1 
ATOM   256   C CB    . LYS A 1 1645 ? 190.022 204.963 138.349 1.00 147.47 ? 1645 LYS A CB    1 
ATOM   257   C CG    . LYS A 1 1645 ? 190.453 204.461 136.972 1.00 147.47 ? 1645 LYS A CG    1 
ATOM   258   C CD    . LYS A 1 1645 ? 189.836 203.117 136.609 1.00 147.47 ? 1645 LYS A CD    1 
ATOM   259   C CE    . LYS A 1 1645 ? 188.320 203.171 136.636 1.00 147.47 ? 1645 LYS A CE    1 
ATOM   260   N NZ    . LYS A 1 1645 ? 187.720 201.844 136.330 1.00 147.47 ? 1645 LYS A NZ    1 
ATOM   261   N N     . ASN A 1 1646 ? 189.468 204.901 141.475 1.00 148.92 ? 1646 ASN A N     1 
ATOM   262   C CA    . ASN A 1 1646 ? 189.130 205.586 142.718 1.00 148.92 ? 1646 ASN A CA    1 
ATOM   263   C C     . ASN A 1 1646 ? 189.423 204.649 143.886 1.00 148.92 ? 1646 ASN A C     1 
ATOM   264   O O     . ASN A 1 1646 ? 188.875 203.546 143.965 1.00 148.92 ? 1646 ASN A O     1 
ATOM   265   C CB    . ASN A 1 1646 ? 187.674 206.046 142.717 1.00 148.92 ? 1646 ASN A CB    1 
ATOM   266   C CG    . ASN A 1 1646 ? 186.698 204.898 142.632 1.00 148.92 ? 1646 ASN A CG    1 
ATOM   267   O OD1   . ASN A 1 1646 ? 186.910 203.937 141.892 1.00 148.92 ? 1646 ASN A OD1   1 
ATOM   268   N ND2   . ASN A 1 1646 ? 185.617 204.990 143.393 1.00 148.92 ? 1646 ASN A ND2   1 
ATOM   269   N N     . VAL A 1 1647 ? 190.295 205.096 144.792 1.00 144.75 ? 1647 VAL A N     1 
ATOM   270   C CA    . VAL A 1 1647 ? 190.730 204.252 145.901 1.00 144.75 ? 1647 VAL A CA    1 
ATOM   271   C C     . VAL A 1 1647 ? 189.770 204.274 147.076 1.00 144.75 ? 1647 VAL A C     1 
ATOM   272   O O     . VAL A 1 1647 ? 189.950 203.495 148.019 1.00 144.75 ? 1647 VAL A O     1 
ATOM   273   C CB    . VAL A 1 1647 ? 192.129 204.683 146.375 1.00 144.75 ? 1647 VAL A CB    1 
ATOM   274   C CG1   . VAL A 1 1647 ? 193.177 204.285 145.350 1.00 144.75 ? 1647 VAL A CG1   1 
ATOM   275   C CG2   . VAL A 1 1647 ? 192.162 206.180 146.619 1.00 144.75 ? 1647 VAL A CG2   1 
ATOM   276   N N     . ALA A 1 1648 ? 188.750 205.134 147.043 1.00 142.27 ? 1648 ALA A N     1 
ATOM   277   C CA    . ALA A 1 1648 ? 187.868 205.285 148.196 1.00 142.27 ? 1648 ALA A CA    1 
ATOM   278   C C     . ALA A 1 1648 ? 187.103 204.001 148.491 1.00 142.27 ? 1648 ALA A C     1 
ATOM   279   O O     . ALA A 1 1648 ? 186.620 203.802 149.612 1.00 142.27 ? 1648 ALA A O     1 
ATOM   280   C CB    . ALA A 1 1648 ? 186.899 206.445 147.968 1.00 142.27 ? 1648 ALA A CB    1 
ATOM   281   N N     . LYS A 1 1649 ? 186.965 203.123 147.497 1.00 141.34 ? 1649 LYS A N     1 
ATOM   282   C CA    . LYS A 1 1649 ? 186.290 201.855 147.739 1.00 141.34 ? 1649 LYS A CA    1 
ATOM   283   C C     . LYS A 1 1649 ? 187.260 200.733 148.080 1.00 141.34 ? 1649 LYS A C     1 
ATOM   284   O O     . LYS A 1 1649 ? 186.816 199.630 148.413 1.00 141.34 ? 1649 LYS A O     1 
ATOM   285   C CB    . LYS A 1 1649 ? 185.451 201.461 146.525 1.00 141.34 ? 1649 LYS A CB    1 
ATOM   286   C CG    . LYS A 1 1649 ? 184.715 202.617 145.877 1.00 141.34 ? 1649 LYS A CG    1 
ATOM   287   C CD    . LYS A 1 1649 ? 184.289 202.267 144.464 1.00 141.34 ? 1649 LYS A CD    1 
ATOM   288   C CE    . LYS A 1 1649 ? 183.026 203.012 144.070 1.00 141.34 ? 1649 LYS A CE    1 
ATOM   289   N NZ    . LYS A 1 1649 ? 182.998 204.389 144.632 1.00 141.34 ? 1649 LYS A NZ    1 
ATOM   290   N N     . LEU A 1 1650 ? 188.567 200.984 148.006 1.00 138.28 ? 1650 LEU A N     1 
ATOM   291   C CA    . LEU A 1 1650 ? 189.530 199.920 148.271 1.00 138.28 ? 1650 LEU A CA    1 
ATOM   292   C C     . LEU A 1 1650 ? 189.667 199.642 149.763 1.00 138.28 ? 1650 LEU A C     1 
ATOM   293   O O     . LEU A 1 1650 ? 189.766 198.481 150.176 1.00 138.28 ? 1650 LEU A O     1 
ATOM   294   C CB    . LEU A 1 1650 ? 190.886 200.277 147.668 1.00 138.28 ? 1650 LEU A CB    1 
ATOM   295   C CG    . LEU A 1 1650 ? 190.977 200.222 146.145 1.00 138.28 ? 1650 LEU A CG    1 
ATOM   296   C CD1   . LEU A 1 1650 ? 192.418 200.017 145.717 1.00 138.28 ? 1650 LEU A CD1   1 
ATOM   297   C CD2   . LEU A 1 1650 ? 190.087 199.125 145.592 1.00 138.28 ? 1650 LEU A CD2   1 
ATOM   298   N N     . GLN A 1 1651 ? 189.667 200.691 150.590 1.00 138.50 ? 1651 GLN A N     1 
ATOM   299   C CA    . GLN A 1 1651 ? 189.937 200.507 152.011 1.00 138.50 ? 1651 GLN A CA    1 
ATOM   300   C C     . GLN A 1 1651 ? 188.831 199.740 152.719 1.00 138.50 ? 1651 GLN A C     1 
ATOM   301   O O     . GLN A 1 1651 ? 189.022 199.319 153.864 1.00 138.50 ? 1651 GLN A O     1 
ATOM   302   C CB    . GLN A 1 1651 ? 190.161 201.857 152.694 1.00 138.50 ? 1651 GLN A CB    1 
ATOM   303   C CG    . GLN A 1 1651 ? 191.063 202.807 151.924 1.00 138.50 ? 1651 GLN A CG    1 
ATOM   304   C CD    . GLN A 1 1651 ? 190.293 203.682 150.966 1.00 138.50 ? 1651 GLN A CD    1 
ATOM   305   O OE1   . GLN A 1 1651 ? 189.138 203.404 150.653 1.00 138.50 ? 1651 GLN A OE1   1 
ATOM   306   N NE2   . GLN A 1 1651 ? 190.929 204.743 150.488 1.00 138.50 ? 1651 GLN A NE2   1 
ATOM   307   N N     . LYS A 1 1652 ? 187.679 199.554 152.075 1.00 134.91 ? 1652 LYS A N     1 
ATOM   308   C CA    . LYS A 1 1652 ? 186.663 198.681 152.651 1.00 134.91 ? 1652 LYS A CA    1 
ATOM   309   C C     . LYS A 1 1652 ? 187.152 197.240 152.699 1.00 134.91 ? 1652 LYS A C     1 
ATOM   310   O O     . LYS A 1 1652 ? 186.809 196.490 153.620 1.00 134.91 ? 1652 LYS A O     1 
ATOM   311   C CB    . LYS A 1 1652 ? 185.365 198.777 151.852 1.00 134.91 ? 1652 LYS A CB    1 
ATOM   312   C CG    . LYS A 1 1652 ? 185.157 200.109 151.159 1.00 134.91 ? 1652 LYS A CG    1 
ATOM   313   C CD    . LYS A 1 1652 ? 183.765 200.193 150.558 1.00 134.91 ? 1652 LYS A CD    1 
ATOM   314   C CE    . LYS A 1 1652 ? 183.497 199.021 149.629 1.00 134.91 ? 1652 LYS A CE    1 
ATOM   315   N NZ    . LYS A 1 1652 ? 184.495 198.942 148.529 1.00 134.91 ? 1652 LYS A NZ    1 
ATOM   316   N N     . HIS A 1 1653 ? 187.952 196.837 151.716 1.00 133.06 ? 1653 HIS A N     1 
ATOM   317   C CA    . HIS A 1 1653 ? 188.465 195.478 151.627 1.00 133.06 ? 1653 HIS A CA    1 
ATOM   318   C C     . HIS A 1 1653 ? 189.935 195.364 152.001 1.00 133.06 ? 1653 HIS A C     1 
ATOM   319   O O     . HIS A 1 1653 ? 190.470 194.252 152.013 1.00 133.06 ? 1653 HIS A O     1 
ATOM   320   C CB    . HIS A 1 1653 ? 188.247 194.934 150.214 1.00 133.06 ? 1653 HIS A CB    1 
ATOM   321   C CG    . HIS A 1 1653 ? 186.873 195.189 149.682 1.00 133.06 ? 1653 HIS A CG    1 
ATOM   322   N ND1   . HIS A 1 1653 ? 185.737 194.719 150.306 1.00 133.06 ? 1653 HIS A ND1   1 
ATOM   323   C CD2   . HIS A 1 1653 ? 186.449 195.884 148.601 1.00 133.06 ? 1653 HIS A CD2   1 
ATOM   324   C CE1   . HIS A 1 1653 ? 184.673 195.101 149.623 1.00 133.06 ? 1653 HIS A CE1   1 
ATOM   325   N NE2   . HIS A 1 1653 ? 185.077 195.809 148.584 1.00 133.06 ? 1653 HIS A NE2   1 
ATOM   326   N N     . PHE A 1 1654 ? 190.598 196.476 152.321 1.00 123.37 ? 1654 PHE A N     1 
ATOM   327   C CA    . PHE A 1 1654 ? 192.020 196.433 152.639 1.00 123.37 ? 1654 PHE A CA    1 
ATOM   328   C C     . PHE A 1 1654 ? 192.321 195.737 153.957 1.00 123.37 ? 1654 PHE A C     1 
ATOM   329   O O     . PHE A 1 1654 ? 193.491 195.450 154.227 1.00 123.37 ? 1654 PHE A O     1 
ATOM   330   C CB    . PHE A 1 1654 ? 192.596 197.845 152.667 1.00 123.37 ? 1654 PHE A CB    1 
ATOM   331   C CG    . PHE A 1 1654 ? 193.369 198.197 151.439 1.00 123.37 ? 1654 PHE A CG    1 
ATOM   332   C CD1   . PHE A 1 1654 ? 194.299 197.314 150.921 1.00 123.37 ? 1654 PHE A CD1   1 
ATOM   333   C CD2   . PHE A 1 1654 ? 193.166 199.401 150.796 1.00 123.37 ? 1654 PHE A CD2   1 
ATOM   334   C CE1   . PHE A 1 1654 ? 195.016 197.627 149.786 1.00 123.37 ? 1654 PHE A CE1   1 
ATOM   335   C CE2   . PHE A 1 1654 ? 193.878 199.721 149.659 1.00 123.37 ? 1654 PHE A CE2   1 
ATOM   336   C CZ    . PHE A 1 1654 ? 194.806 198.833 149.154 1.00 123.37 ? 1654 PHE A CZ    1 
ATOM   337   N N     . LYS A 1 1655 ? 191.312 195.461 154.778 1.00 122.36 ? 1655 LYS A N     1 
ATOM   338   C CA    . LYS A 1 1655 ? 191.526 194.733 156.021 1.00 122.36 ? 1655 LYS A CA    1 
ATOM   339   C C     . LYS A 1 1655 ? 191.509 193.225 155.829 1.00 122.36 ? 1655 LYS A C     1 
ATOM   340   O O     . LYS A 1 1655 ? 191.645 192.490 156.812 1.00 122.36 ? 1655 LYS A O     1 
ATOM   341   C CB    . LYS A 1 1655 ? 190.470 195.123 157.055 1.00 122.36 ? 1655 LYS A CB    1 
ATOM   342   C CG    . LYS A 1 1655 ? 189.051 194.998 156.552 1.00 122.36 ? 1655 LYS A CG    1 
ATOM   343   C CD    . LYS A 1 1655 ? 188.117 194.623 157.679 1.00 122.36 ? 1655 LYS A CD    1 
ATOM   344   C CE    . LYS A 1 1655 ? 188.402 193.213 158.155 1.00 122.36 ? 1655 LYS A CE    1 
ATOM   345   N NZ    . LYS A 1 1655 ? 188.040 192.206 157.125 1.00 122.36 ? 1655 LYS A NZ    1 
ATOM   346   N N     . LYS A 1 1656 ? 191.338 192.749 154.597 1.00 120.19 ? 1656 LYS A N     1 
ATOM   347   C CA    . LYS A 1 1656 ? 191.259 191.319 154.339 1.00 120.19 ? 1656 LYS A CA    1 
ATOM   348   C C     . LYS A 1 1656 ? 192.623 190.703 154.065 1.00 120.19 ? 1656 LYS A C     1 
ATOM   349   O O     . LYS A 1 1656 ? 192.994 189.721 154.715 1.00 120.19 ? 1656 LYS A O     1 
ATOM   350   C CB    . LYS A 1 1656 ? 190.324 191.053 153.160 1.00 120.19 ? 1656 LYS A CB    1 
ATOM   351   C CG    . LYS A 1 1656 ? 188.855 191.190 153.505 1.00 120.19 ? 1656 LYS A CG    1 
ATOM   352   C CD    . LYS A 1 1656 ? 187.982 190.393 152.553 1.00 120.19 ? 1656 LYS A CD    1 
ATOM   353   C CE    . LYS A 1 1656 ? 188.470 188.964 152.416 1.00 120.19 ? 1656 LYS A CE    1 
ATOM   354   N NZ    . LYS A 1 1656 ? 187.542 188.146 151.588 1.00 120.19 ? 1656 LYS A NZ    1 
ATOM   355   N N     . MET A 1 1657 ? 193.384 191.259 153.124 1.00 119.81 ? 1657 MET A N     1 
ATOM   356   C CA    . MET A 1 1657 ? 194.671 190.681 152.762 1.00 119.81 ? 1657 MET A CA    1 
ATOM   357   C C     . MET A 1 1657 ? 195.815 191.125 153.659 1.00 119.81 ? 1657 MET A C     1 
ATOM   358   O O     . MET A 1 1657 ? 196.909 190.561 153.560 1.00 119.81 ? 1657 MET A O     1 
ATOM   359   C CB    . MET A 1 1657 ? 195.023 191.015 151.308 1.00 119.81 ? 1657 MET A CB    1 
ATOM   360   C CG    . MET A 1 1657 ? 195.378 192.465 151.074 1.00 119.81 ? 1657 MET A CG    1 
ATOM   361   S SD    . MET A 1 1657 ? 194.047 193.563 151.575 1.00 119.81 ? 1657 MET A SD    1 
ATOM   362   C CE    . MET A 1 1657 ? 192.844 193.177 150.308 1.00 119.81 ? 1657 MET A CE    1 
ATOM   363   N N     . PHE A 1 1658 ? 195.603 192.109 154.521 1.00 112.69 ? 1658 PHE A N     1 
ATOM   364   C CA    . PHE A 1 1658 ? 196.640 192.568 155.430 1.00 112.69 ? 1658 PHE A CA    1 
ATOM   365   C C     . PHE A 1 1658 ? 196.275 192.255 156.875 1.00 112.69 ? 1658 PHE A C     1 
ATOM   366   O O     . PHE A 1 1658 ? 195.101 192.188 157.248 1.00 112.69 ? 1658 PHE A O     1 
ATOM   367   C CB    . PHE A 1 1658 ? 196.886 194.065 155.254 1.00 112.69 ? 1658 PHE A CB    1 
ATOM   368   C CG    . PHE A 1 1658 ? 197.285 194.446 153.863 1.00 112.69 ? 1658 PHE A CG    1 
ATOM   369   C CD1   . PHE A 1 1658 ? 196.883 195.648 153.316 1.00 112.69 ? 1658 PHE A CD1   1 
ATOM   370   C CD2   . PHE A 1 1658 ? 198.072 193.601 153.104 1.00 112.69 ? 1658 PHE A CD2   1 
ATOM   371   C CE1   . PHE A 1 1658 ? 197.254 195.998 152.034 1.00 112.69 ? 1658 PHE A CE1   1 
ATOM   372   C CE2   . PHE A 1 1658 ? 198.446 193.948 151.824 1.00 112.69 ? 1658 PHE A CE2   1 
ATOM   373   C CZ    . PHE A 1 1658 ? 198.035 195.147 151.288 1.00 112.69 ? 1658 PHE A CZ    1 
ATOM   374   N N     . ALA A 1 1659 ? 197.312 192.056 157.689 1.00 106.79 ? 1659 ALA A N     1 
ATOM   375   C CA    . ALA A 1 1659 ? 197.106 191.667 159.079 1.00 106.79 ? 1659 ALA A CA    1 
ATOM   376   C C     . ALA A 1 1659 ? 196.377 192.753 159.855 1.00 106.79 ? 1659 ALA A C     1 
ATOM   377   O O     . ALA A 1 1659 ? 195.394 192.478 160.552 1.00 106.79 ? 1659 ALA A O     1 
ATOM   378   C CB    . ALA A 1 1659 ? 198.447 191.345 159.735 1.00 106.79 ? 1659 ALA A CB    1 
ATOM   379   N N     . GLY A 1 1660 ? 196.838 193.994 159.744 1.00 114.35 ? 1660 GLY A N     1 
ATOM   380   C CA    . GLY A 1 1660 ? 196.244 195.073 160.505 1.00 114.35 ? 1660 GLY A CA    1 
ATOM   381   C C     . GLY A 1 1660 ? 195.989 196.329 159.700 1.00 114.35 ? 1660 GLY A C     1 
ATOM   382   O O     . GLY A 1 1660 ? 195.398 197.284 160.210 1.00 114.35 ? 1660 GLY A O     1 
ATOM   383   N N     . VAL A 1 1661 ? 196.424 196.344 158.443 1.00 118.34 ? 1661 VAL A N     1 
ATOM   384   C CA    . VAL A 1 1661 ? 196.273 197.538 157.620 1.00 118.34 ? 1661 VAL A CA    1 
ATOM   385   C C     . VAL A 1 1661 ? 194.803 197.711 157.267 1.00 118.34 ? 1661 VAL A C     1 
ATOM   386   O O     . VAL A 1 1661 ? 194.207 196.864 156.593 1.00 118.34 ? 1661 VAL A O     1 
ATOM   387   C CB    . VAL A 1 1661 ? 197.141 197.453 156.360 1.00 118.34 ? 1661 VAL A CB    1 
ATOM   388   C CG1   . VAL A 1 1661 ? 196.970 198.705 155.523 1.00 118.34 ? 1661 VAL A CG1   1 
ATOM   389   C CG2   . VAL A 1 1661 ? 198.597 197.255 156.734 1.00 118.34 ? 1661 VAL A CG2   1 
ATOM   390   N N     . SER A 1 1662 ? 194.214 198.820 157.717 1.00 124.41 ? 1662 SER A N     1 
ATOM   391   C CA    . SER A 1 1662 ? 192.811 199.111 157.468 1.00 124.41 ? 1662 SER A CA    1 
ATOM   392   C C     . SER A 1 1662 ? 192.588 200.217 156.450 1.00 124.41 ? 1662 SER A C     1 
ATOM   393   O O     . SER A 1 1662 ? 191.500 200.287 155.873 1.00 124.41 ? 1662 SER A O     1 
ATOM   394   C CB    . SER A 1 1662 ? 192.106 199.500 158.775 1.00 124.41 ? 1662 SER A CB    1 
ATOM   395   O OG    . SER A 1 1662 ? 190.745 199.816 158.544 1.00 124.41 ? 1662 SER A OG    1 
ATOM   396   N N     . SER A 1 1663 ? 193.576 201.076 156.221 1.00 125.73 ? 1663 SER A N     1 
ATOM   397   C CA    . SER A 1 1663 ? 193.451 202.137 155.233 1.00 125.73 ? 1663 SER A CA    1 
ATOM   398   C C     . SER A 1 1663 ? 194.846 202.562 154.805 1.00 125.73 ? 1663 SER A C     1 
ATOM   399   O O     . SER A 1 1663 ? 195.834 202.293 155.493 1.00 125.73 ? 1663 SER A O     1 
ATOM   400   C CB    . SER A 1 1663 ? 192.664 203.329 155.783 1.00 125.73 ? 1663 SER A CB    1 
ATOM   401   O OG    . SER A 1 1663 ? 191.309 202.983 156.008 1.00 125.73 ? 1663 SER A OG    1 
ATOM   402   N N     . ILE A 1 1664 ? 194.912 203.233 153.658 1.00 123.67 ? 1664 ILE A N     1 
ATOM   403   C CA    . ILE A 1 1664 ? 196.168 203.706 153.089 1.00 123.67 ? 1664 ILE A CA    1 
ATOM   404   C C     . ILE A 1 1664 ? 196.157 205.227 153.097 1.00 123.67 ? 1664 ILE A C     1 
ATOM   405   O O     . ILE A 1 1664 ? 195.174 205.849 152.679 1.00 123.67 ? 1664 ILE A O     1 
ATOM   406   C CB    . ILE A 1 1664 ? 196.388 203.168 151.664 1.00 123.67 ? 1664 ILE A CB    1 
ATOM   407   C CG1   . ILE A 1 1664 ? 195.070 203.132 150.897 1.00 123.67 ? 1664 ILE A CG1   1 
ATOM   408   C CG2   . ILE A 1 1664 ? 196.994 201.784 151.711 1.00 123.67 ? 1664 ILE A CG2   1 
ATOM   409   C CD1   . ILE A 1 1664 ? 195.245 202.880 149.421 1.00 123.67 ? 1664 ILE A CD1   1 
ATOM   410   N N     . ILE A 1 1665 ? 197.247 205.821 153.577 1.00 123.92 ? 1665 ILE A N     1 
ATOM   411   C CA    . ILE A 1 1665 ? 197.372 207.275 153.645 1.00 123.92 ? 1665 ILE A CA    1 
ATOM   412   C C     . ILE A 1 1665 ? 197.771 207.763 152.257 1.00 123.92 ? 1665 ILE A C     1 
ATOM   413   O O     . ILE A 1 1665 ? 198.932 207.662 151.859 1.00 123.92 ? 1665 ILE A O     1 
ATOM   414   C CB    . ILE A 1 1665 ? 198.381 207.712 154.709 1.00 123.92 ? 1665 ILE A CB    1 
ATOM   415   C CG1   . ILE A 1 1665 ? 198.048 207.075 156.061 1.00 123.92 ? 1665 ILE A CG1   1 
ATOM   416   C CG2   . ILE A 1 1665 ? 198.409 209.226 154.822 1.00 123.92 ? 1665 ILE A CG2   1 
ATOM   417   C CD1   . ILE A 1 1665 ? 196.581 207.164 156.439 1.00 123.92 ? 1665 ILE A CD1   1 
ATOM   418   N N     . LEU A 1 1666 ? 196.809 208.301 151.518 1.00 129.09 ? 1666 LEU A N     1 
ATOM   419   C CA    . LEU A 1 1666 ? 197.046 208.789 150.169 1.00 129.09 ? 1666 LEU A CA    1 
ATOM   420   C C     . LEU A 1 1666 ? 197.210 210.304 150.169 1.00 129.09 ? 1666 LEU A C     1 
ATOM   421   O O     . LEU A 1 1666 ? 196.965 210.987 151.165 1.00 129.09 ? 1666 LEU A O     1 
ATOM   422   C CB    . LEU A 1 1666 ? 195.903 208.378 149.237 1.00 129.09 ? 1666 LEU A CB    1 
ATOM   423   C CG    . LEU A 1 1666 ? 195.679 206.878 149.061 1.00 129.09 ? 1666 LEU A CG    1 
ATOM   424   C CD1   . LEU A 1 1666 ? 194.320 206.489 149.604 1.00 129.09 ? 1666 LEU A CD1   1 
ATOM   425   C CD2   . LEU A 1 1666 ? 195.808 206.485 147.601 1.00 129.09 ? 1666 LEU A CD2   1 
ATOM   426   N N     . ASN A 1 1667 ? 197.637 210.825 149.023 1.00 135.93 ? 1667 ASN A N     1 
ATOM   427   C CA    . ASN A 1 1667 ? 197.869 212.253 148.864 1.00 135.93 ? 1667 ASN A CA    1 
ATOM   428   C C     . ASN A 1 1667 ? 196.534 212.976 148.705 1.00 135.93 ? 1667 ASN A C     1 
ATOM   429   O O     . ASN A 1 1667 ? 195.457 212.382 148.804 1.00 135.93 ? 1667 ASN A O     1 
ATOM   430   C CB    . ASN A 1 1667 ? 198.799 212.506 147.682 1.00 135.93 ? 1667 ASN A CB    1 
ATOM   431   C CG    . ASN A 1 1667 ? 199.933 213.445 148.027 1.00 135.93 ? 1667 ASN A CG    1 
ATOM   432   O OD1   . ASN A 1 1667 ? 200.056 213.892 149.166 1.00 135.93 ? 1667 ASN A OD1   1 
ATOM   433   N ND2   . ASN A 1 1667 ? 200.771 213.748 147.045 1.00 135.93 ? 1667 ASN A ND2   1 
ATOM   434   N N     . GLU A 1 1668 ? 196.595 214.285 148.455 1.00 139.16 ? 1668 GLU A N     1 
ATOM   435   C CA    . GLU A 1 1668 ? 195.374 215.060 148.268 1.00 139.16 ? 1668 GLU A CA    1 
ATOM   436   C C     . GLU A 1 1668 ? 194.635 214.646 147.002 1.00 139.16 ? 1668 GLU A C     1 
ATOM   437   O O     . GLU A 1 1668 ? 193.414 214.817 146.916 1.00 139.16 ? 1668 GLU A O     1 
ATOM   438   C CB    . GLU A 1 1668 ? 195.707 216.552 148.230 1.00 139.16 ? 1668 GLU A CB    1 
ATOM   439   C CG    . GLU A 1 1668 ? 196.169 217.060 146.872 1.00 139.16 ? 1668 GLU A CG    1 
ATOM   440   C CD    . GLU A 1 1668 ? 197.485 216.446 146.428 1.00 139.16 ? 1668 GLU A CD    1 
ATOM   441   O OE1   . GLU A 1 1668 ? 198.233 215.939 147.291 1.00 139.16 ? 1668 GLU A OE1   1 
ATOM   442   O OE2   . GLU A 1 1668 ? 197.770 216.468 145.213 1.00 139.16 ? 1668 GLU A OE2   1 
ATOM   443   N N     . ASP A 1 1669 ? 195.350 214.101 146.019 1.00 138.34 ? 1669 ASP A N     1 
ATOM   444   C CA    . ASP A 1 1669 ? 194.764 213.682 144.754 1.00 138.34 ? 1669 ASP A CA    1 
ATOM   445   C C     . ASP A 1 1669 ? 194.733 212.169 144.599 1.00 138.34 ? 1669 ASP A C     1 
ATOM   446   O O     . ASP A 1 1669 ? 194.418 211.676 143.512 1.00 138.34 ? 1669 ASP A O     1 
ATOM   447   C CB    . ASP A 1 1669 ? 195.532 214.306 143.590 1.00 138.34 ? 1669 ASP A CB    1 
ATOM   448   C CG    . ASP A 1 1669 ? 197.006 213.970 143.627 1.00 138.34 ? 1669 ASP A CG    1 
ATOM   449   O OD1   . ASP A 1 1669 ? 197.486 213.515 144.687 1.00 138.34 ? 1669 ASP A OD1   1 
ATOM   450   O OD2   . ASP A 1 1669 ? 197.686 214.163 142.598 1.00 138.34 ? 1669 ASP A OD2   1 
ATOM   451   N N     . ASN A 1 1670 ? 195.054 211.425 145.659 1.00 134.42 ? 1670 ASN A N     1 
ATOM   452   C CA    . ASN A 1 1670 ? 195.106 209.964 145.617 1.00 134.42 ? 1670 ASN A CA    1 
ATOM   453   C C     . ASN A 1 1670 ? 196.063 209.477 144.533 1.00 134.42 ? 1670 ASN A C     1 
ATOM   454   O O     . ASN A 1 1670 ? 195.801 208.491 143.844 1.00 134.42 ? 1670 ASN A O     1 
ATOM   455   C CB    . ASN A 1 1670 ? 193.713 209.366 145.414 1.00 134.42 ? 1670 ASN A CB    1 
ATOM   456   C CG    . ASN A 1 1670 ? 192.629 210.191 146.065 1.00 134.42 ? 1670 ASN A CG    1 
ATOM   457   O OD1   . ASN A 1 1670 ? 192.601 210.350 147.285 1.00 134.42 ? 1670 ASN A OD1   1 
ATOM   458   N ND2   . ASN A 1 1670 ? 191.731 210.730 145.252 1.00 134.42 ? 1670 ASN A ND2   1 
ATOM   459   N N     . SER A 1 1671 ? 197.183 210.179 144.377 1.00 133.89 ? 1671 SER A N     1 
ATOM   460   C CA    . SER A 1 1671 ? 198.186 209.823 143.382 1.00 133.89 ? 1671 SER A CA    1 
ATOM   461   C C     . SER A 1 1671 ? 199.325 208.997 143.958 1.00 133.89 ? 1671 SER A C     1 
ATOM   462   O O     . SER A 1 1671 ? 199.820 208.083 143.292 1.00 133.89 ? 1671 SER A O     1 
ATOM   463   C CB    . SER A 1 1671 ? 198.757 211.087 142.735 1.00 133.89 ? 1671 SER A CB    1 
ATOM   464   O OG    . SER A 1 1671 ? 199.596 211.784 143.639 1.00 133.89 ? 1671 SER A OG    1 
ATOM   465   N N     . VAL A 1 1672 ? 199.751 209.298 145.180 1.00 130.17 ? 1672 VAL A N     1 
ATOM   466   C CA    . VAL A 1 1672 ? 200.830 208.575 145.838 1.00 130.17 ? 1672 VAL A CA    1 
ATOM   467   C C     . VAL A 1 1672 ? 200.308 208.022 147.155 1.00 130.17 ? 1672 VAL A C     1 
ATOM   468   O O     . VAL A 1 1672 ? 199.313 208.505 147.706 1.00 130.17 ? 1672 VAL A O     1 
ATOM   469   C CB    . VAL A 1 1672 ? 202.068 209.468 146.071 1.00 130.17 ? 1672 VAL A CB    1 
ATOM   470   C CG1   . VAL A 1 1672 ? 202.452 210.187 144.792 1.00 130.17 ? 1672 VAL A CG1   1 
ATOM   471   C CG2   . VAL A 1 1672 ? 201.803 210.465 147.182 1.00 130.17 ? 1672 VAL A CG2   1 
ATOM   472   N N     . VAL A 1 1673 ? 200.980 206.991 147.652 1.00 124.20 ? 1673 VAL A N     1 
ATOM   473   C CA    . VAL A 1 1673 ? 200.623 206.344 148.907 1.00 124.20 ? 1673 VAL A CA    1 
ATOM   474   C C     . VAL A 1 1673 ? 201.730 206.666 149.900 1.00 124.20 ? 1673 VAL A C     1 
ATOM   475   O O     . VAL A 1 1673 ? 202.774 206.006 149.918 1.00 124.20 ? 1673 VAL A O     1 
ATOM   476   C CB    . VAL A 1 1673 ? 200.439 204.834 148.741 1.00 124.20 ? 1673 VAL A CB    1 
ATOM   477   C CG1   . VAL A 1 1673 ? 199.808 204.247 149.987 1.00 124.20 ? 1673 VAL A CG1   1 
ATOM   478   C CG2   . VAL A 1 1673 ? 199.591 204.543 147.521 1.00 124.20 ? 1673 VAL A CG2   1 
ATOM   479   N N     . LEU A 1 1674 ? 201.508 207.685 150.733 1.00 123.23 ? 1674 LEU A N     1 
ATOM   480   C CA    . LEU A 1 1674 ? 202.532 208.082 151.691 1.00 123.23 ? 1674 LEU A CA    1 
ATOM   481   C C     . LEU A 1 1674 ? 202.665 207.078 152.826 1.00 123.23 ? 1674 LEU A C     1 
ATOM   482   O O     . LEU A 1 1674 ? 203.747 206.943 153.408 1.00 123.23 ? 1674 LEU A O     1 
ATOM   483   C CB    . LEU A 1 1674 ? 202.231 209.469 152.254 1.00 123.23 ? 1674 LEU A CB    1 
ATOM   484   C CG    . LEU A 1 1674 ? 201.892 210.578 151.260 1.00 123.23 ? 1674 LEU A CG    1 
ATOM   485   C CD1   . LEU A 1 1674 ? 200.393 210.792 151.201 1.00 123.23 ? 1674 LEU A CD1   1 
ATOM   486   C CD2   . LEU A 1 1674 ? 202.606 211.865 151.638 1.00 123.23 ? 1674 LEU A CD2   1 
ATOM   487   N N     . GLY A 1 1675 ? 201.591 206.374 153.163 1.00 122.70 ? 1675 GLY A N     1 
ATOM   488   C CA    . GLY A 1 1675 ? 201.684 205.427 154.256 1.00 122.70 ? 1675 GLY A CA    1 
ATOM   489   C C     . GLY A 1 1675 ? 200.407 204.636 154.415 1.00 122.70 ? 1675 GLY A C     1 
ATOM   490   O O     . GLY A 1 1675 ? 199.469 204.748 153.621 1.00 122.70 ? 1675 GLY A O     1 
ATOM   491   N N     . ILE A 1 1676 ? 200.392 203.826 155.471 1.00 120.53 ? 1676 ILE A N     1 
ATOM   492   C CA    . ILE A 1 1676 ? 199.278 202.948 155.788 1.00 120.53 ? 1676 ILE A CA    1 
ATOM   493   C C     . ILE A 1 1676 ? 198.815 203.249 157.205 1.00 120.53 ? 1676 ILE A C     1 
ATOM   494   O O     . ILE A 1 1676 ? 199.567 203.763 158.036 1.00 120.53 ? 1676 ILE A O     1 
ATOM   495   C CB    . ILE A 1 1676 ? 199.663 201.466 155.646 1.00 120.53 ? 1676 ILE A CB    1 
ATOM   496   C CG1   . ILE A 1 1676 ? 201.085 201.250 156.162 1.00 120.53 ? 1676 ILE A CG1   1 
ATOM   497   C CG2   . ILE A 1 1676 ? 199.556 201.031 154.201 1.00 120.53 ? 1676 ILE A CG2   1 
ATOM   498   C CD1   . ILE A 1 1676 ? 201.596 199.847 155.970 1.00 120.53 ? 1676 ILE A CD1   1 
ATOM   499   N N     . SER A 1 1677 ? 197.557 202.920 157.475 1.00 119.94 ? 1677 SER A N     1 
ATOM   500   C CA    . SER A 1 1677 ? 196.956 203.153 158.778 1.00 119.94 ? 1677 SER A CA    1 
ATOM   501   C C     . SER A 1 1677 ? 196.225 201.902 159.229 1.00 119.94 ? 1677 SER A C     1 
ATOM   502   O O     . SER A 1 1677 ? 195.620 201.198 158.416 1.00 119.94 ? 1677 SER A O     1 
ATOM   503   C CB    . SER A 1 1677 ? 195.989 204.333 158.739 1.00 119.94 ? 1677 SER A CB    1 
ATOM   504   O OG    . SER A 1 1677 ? 194.979 204.119 157.771 1.00 119.94 ? 1677 SER A OG    1 
ATOM   505   N N     . SER A 1 1678 ? 196.278 201.635 160.529 1.00 119.28 ? 1678 SER A N     1 
ATOM   506   C CA    . SER A 1 1678 ? 195.674 200.442 161.093 1.00 119.28 ? 1678 SER A CA    1 
ATOM   507   C C     . SER A 1 1678 ? 194.221 200.708 161.477 1.00 119.28 ? 1678 SER A C     1 
ATOM   508   O O     . SER A 1 1678 ? 193.708 201.823 161.359 1.00 119.28 ? 1678 SER A O     1 
ATOM   509   C CB    . SER A 1 1678 ? 196.478 199.965 162.299 1.00 119.28 ? 1678 SER A CB    1 
ATOM   510   O OG    . SER A 1 1678 ? 196.554 200.980 163.283 1.00 119.28 ? 1678 SER A OG    1 
ATOM   511   N N     . ARG A 1 1679 ? 193.547 199.658 161.949 1.00 124.59 ? 1679 ARG A N     1 
ATOM   512   C CA    . ARG A 1 1679 ? 192.159 199.793 162.371 1.00 124.59 ? 1679 ARG A CA    1 
ATOM   513   C C     . ARG A 1 1679 ? 192.030 200.672 163.606 1.00 124.59 ? 1679 ARG A C     1 
ATOM   514   O O     . ARG A 1 1679 ? 191.011 201.348 163.783 1.00 124.59 ? 1679 ARG A O     1 
ATOM   515   C CB    . ARG A 1 1679 ? 191.558 198.413 162.634 1.00 124.59 ? 1679 ARG A CB    1 
ATOM   516   C CG    . ARG A 1 1679 ? 190.043 198.389 162.706 1.00 124.59 ? 1679 ARG A CG    1 
ATOM   517   C CD    . ARG A 1 1679 ? 189.566 197.558 163.886 1.00 124.59 ? 1679 ARG A CD    1 
ATOM   518   N NE    . ARG A 1 1679 ? 190.025 198.097 165.161 1.00 124.59 ? 1679 ARG A NE    1 
ATOM   519   C CZ    . ARG A 1 1679 ? 189.564 199.209 165.719 1.00 124.59 ? 1679 ARG A CZ    1 
ATOM   520   N NH1   . ARG A 1 1679 ? 188.598 199.916 165.157 1.00 124.59 ? 1679 ARG A NH1   1 
ATOM   521   N NH2   . ARG A 1 1679 ? 190.081 199.617 166.874 1.00 124.59 ? 1679 ARG A NH2   1 
ATOM   522   N N     . GLU A 1 1680 ? 193.044 200.682 164.464 1.00 122.16 ? 1680 GLU A N     1 
ATOM   523   C CA    . GLU A 1 1680 ? 193.009 201.478 165.682 1.00 122.16 ? 1680 GLU A CA    1 
ATOM   524   C C     . GLU A 1 1680 ? 193.468 202.912 165.464 1.00 122.16 ? 1680 GLU A C     1 
ATOM   525   O O     . GLU A 1 1680 ? 193.553 203.671 166.434 1.00 122.16 ? 1680 GLU A O     1 
ATOM   526   C CB    . GLU A 1 1680 ? 193.865 200.819 166.765 1.00 122.16 ? 1680 GLU A CB    1 
ATOM   527   C CG    . GLU A 1 1680 ? 193.467 199.384 167.071 1.00 122.16 ? 1680 GLU A CG    1 
ATOM   528   C CD    . GLU A 1 1680 ? 194.337 198.368 166.355 1.00 122.16 ? 1680 GLU A CD    1 
ATOM   529   O OE1   . GLU A 1 1680 ? 195.365 198.767 165.770 1.00 122.16 ? 1680 GLU A OE1   1 
ATOM   530   O OE2   . GLU A 1 1680 ? 193.988 197.169 166.371 1.00 122.16 ? 1680 GLU A OE2   1 
ATOM   531   N N     . GLY A 1 1681 ? 193.772 203.297 164.230 1.00 115.21 ? 1681 GLY A N     1 
ATOM   532   C CA    . GLY A 1 1681 ? 194.197 204.644 163.928 1.00 115.21 ? 1681 GLY A CA    1 
ATOM   533   C C     . GLY A 1 1681 ? 195.695 204.838 163.879 1.00 115.21 ? 1681 GLY A C     1 
ATOM   534   O O     . GLY A 1 1681 ? 196.149 205.886 163.408 1.00 115.21 ? 1681 GLY A O     1 
ATOM   535   N N     . GLU A 1 1682 ? 196.471 203.868 164.352 1.00 115.41 ? 1682 GLU A N     1 
ATOM   536   C CA    . GLU A 1 1682 ? 197.920 203.960 164.258 1.00 115.41 ? 1682 GLU A CA    1 
ATOM   537   C C     . GLU A 1 1682 ? 198.346 203.902 162.796 1.00 115.41 ? 1682 GLU A C     1 
ATOM   538   O O     . GLU A 1 1682 ? 197.851 203.072 162.028 1.00 115.41 ? 1682 GLU A O     1 
ATOM   539   C CB    . GLU A 1 1682 ? 198.572 202.829 165.049 1.00 115.41 ? 1682 GLU A CB    1 
ATOM   540   C CG    . GLU A 1 1682 ? 200.058 202.688 164.808 1.00 115.41 ? 1682 GLU A CG    1 
ATOM   541   C CD    . GLU A 1 1682 ? 200.813 203.952 165.147 1.00 115.41 ? 1682 GLU A CD    1 
ATOM   542   O OE1   . GLU A 1 1682 ? 200.480 204.588 166.168 1.00 115.41 ? 1682 GLU A OE1   1 
ATOM   543   O OE2   . GLU A 1 1682 ? 201.733 204.316 164.389 1.00 115.41 ? 1682 GLU A OE2   1 
ATOM   544   N N     . GLU A 1 1683 ? 199.264 204.781 162.408 1.00 115.24 ? 1683 GLU A N     1 
ATOM   545   C CA    . GLU A 1 1683 ? 199.673 204.909 161.019 1.00 115.24 ? 1683 GLU A CA    1 
ATOM   546   C C     . GLU A 1 1683 ? 201.183 204.778 160.894 1.00 115.24 ? 1683 GLU A C     1 
ATOM   547   O O     . GLU A 1 1683 ? 201.930 205.189 161.786 1.00 115.24 ? 1683 GLU A O     1 
ATOM   548   C CB    . GLU A 1 1683 ? 199.218 206.248 160.428 1.00 115.24 ? 1683 GLU A CB    1 
ATOM   549   C CG    . GLU A 1 1683 ? 199.851 207.476 161.068 1.00 115.24 ? 1683 GLU A CG    1 
ATOM   550   C CD    . GLU A 1 1683 ? 199.127 207.931 162.320 1.00 115.24 ? 1683 GLU A CD    1 
ATOM   551   O OE1   . GLU A 1 1683 ? 198.635 207.068 163.077 1.00 115.24 ? 1683 GLU A OE1   1 
ATOM   552   O OE2   . GLU A 1 1683 ? 199.048 209.156 162.547 1.00 115.24 ? 1683 GLU A OE2   1 
ATOM   553   N N     . VAL A 1 1684 ? 201.624 204.204 159.780 1.00 113.93 ? 1684 VAL A N     1 
ATOM   554   C CA    . VAL A 1 1684 ? 203.038 204.050 159.463 1.00 113.93 ? 1684 VAL A CA    1 
ATOM   555   C C     . VAL A 1 1684 ? 203.341 204.906 158.245 1.00 113.93 ? 1684 VAL A C     1 
ATOM   556   O O     . VAL A 1 1684 ? 202.656 204.803 157.221 1.00 113.93 ? 1684 VAL A O     1 
ATOM   557   C CB    . VAL A 1 1684 ? 203.402 202.578 159.208 1.00 113.93 ? 1684 VAL A CB    1 
ATOM   558   C CG1   . VAL A 1 1684 ? 204.579 202.476 158.258 1.00 113.93 ? 1684 VAL A CG1   1 
ATOM   559   C CG2   . VAL A 1 1684 ? 203.711 201.881 160.516 1.00 113.93 ? 1684 VAL A CG2   1 
ATOM   560   N N     . MET A 1 1685 ? 204.357 205.754 158.356 1.00 116.09 ? 1685 MET A N     1 
ATOM   561   C CA    . MET A 1 1685 ? 204.755 206.644 157.275 1.00 116.09 ? 1685 MET A CA    1 
ATOM   562   C C     . MET A 1 1685 ? 205.884 205.990 156.490 1.00 116.09 ? 1685 MET A C     1 
ATOM   563   O O     . MET A 1 1685 ? 206.938 205.681 157.056 1.00 116.09 ? 1685 MET A O     1 
ATOM   564   C CB    . MET A 1 1685 ? 205.197 208.000 157.821 1.00 116.09 ? 1685 MET A CB    1 
ATOM   565   C CG    . MET A 1 1685 ? 204.145 209.115 157.798 1.00 116.09 ? 1685 MET A CG    1 
ATOM   566   S SD    . MET A 1 1685 ? 203.239 209.380 156.256 1.00 116.09 ? 1685 MET A SD    1 
ATOM   567   C CE    . MET A 1 1685 ? 201.853 208.255 156.421 1.00 116.09 ? 1685 MET A CE    1 
ATOM   568   N N     . PHE A 1 1686 ? 205.665 205.787 155.194 1.00 116.12 ? 1686 PHE A N     1 
ATOM   569   C CA    . PHE A 1 1686 ? 206.689 205.185 154.354 1.00 116.12 ? 1686 PHE A CA    1 
ATOM   570   C C     . PHE A 1 1686 ? 207.921 206.074 154.289 1.00 116.12 ? 1686 PHE A C     1 
ATOM   571   O O     . PHE A 1 1686 ? 207.819 207.298 154.172 1.00 116.12 ? 1686 PHE A O     1 
ATOM   572   C CB    . PHE A 1 1686 ? 206.151 204.950 152.947 1.00 116.12 ? 1686 PHE A CB    1 
ATOM   573   C CG    . PHE A 1 1686 ? 205.107 203.886 152.869 1.00 116.12 ? 1686 PHE A CG    1 
ATOM   574   C CD1   . PHE A 1 1686 ? 205.236 202.722 153.598 1.00 116.12 ? 1686 PHE A CD1   1 
ATOM   575   C CD2   . PHE A 1 1686 ? 203.997 204.047 152.064 1.00 116.12 ? 1686 PHE A CD2   1 
ATOM   576   C CE1   . PHE A 1 1686 ? 204.277 201.739 153.524 1.00 116.12 ? 1686 PHE A CE1   1 
ATOM   577   C CE2   . PHE A 1 1686 ? 203.035 203.068 151.988 1.00 116.12 ? 1686 PHE A CE2   1 
ATOM   578   C CZ    . PHE A 1 1686 ? 203.175 201.913 152.719 1.00 116.12 ? 1686 PHE A CZ    1 
ATOM   579   N N     . LYS A 1 1687 ? 209.095 205.450 154.376 1.00 115.59 ? 1687 LYS A N     1 
ATOM   580   C CA    . LYS A 1 1687 ? 210.333 206.200 154.201 1.00 115.59 ? 1687 LYS A CA    1 
ATOM   581   C C     . LYS A 1 1687 ? 210.449 206.740 152.782 1.00 115.59 ? 1687 LYS A C     1 
ATOM   582   O O     . LYS A 1 1687 ? 210.832 207.898 152.580 1.00 115.59 ? 1687 LYS A O     1 
ATOM   583   C CB    . LYS A 1 1687 ? 211.531 205.320 154.547 1.00 115.59 ? 1687 LYS A CB    1 
ATOM   584   C CG    . LYS A 1 1687 ? 212.771 206.099 154.939 1.00 115.59 ? 1687 LYS A CG    1 
ATOM   585   C CD    . LYS A 1 1687 ? 212.767 206.409 156.424 1.00 115.59 ? 1687 LYS A CD    1 
ATOM   586   C CE    . LYS A 1 1687 ? 212.697 205.140 157.255 1.00 115.59 ? 1687 LYS A CE    1 
ATOM   587   N NZ    . LYS A 1 1687 ? 212.612 205.436 158.711 1.00 115.59 ? 1687 LYS A NZ    1 
ATOM   588   N N     . THR A 1 1688 ? 210.125 205.918 151.788 1.00 119.99 ? 1688 THR A N     1 
ATOM   589   C CA    . THR A 1 1688 ? 210.102 206.338 150.387 1.00 119.99 ? 1688 THR A CA    1 
ATOM   590   C C     . THR A 1 1688 ? 208.724 206.048 149.813 1.00 119.99 ? 1688 THR A C     1 
ATOM   591   O O     . THR A 1 1688 ? 208.449 204.907 149.399 1.00 119.99 ? 1688 THR A O     1 
ATOM   592   C CB    . THR A 1 1688 ? 211.182 205.625 149.576 1.00 119.99 ? 1688 THR A CB    1 
ATOM   593   O OG1   . THR A 1 1688 ? 210.691 204.355 149.134 1.00 119.99 ? 1688 THR A OG1   1 
ATOM   594   C CG2   . THR A 1 1688 ? 212.437 205.414 150.410 1.00 119.99 ? 1688 THR A CG2   1 
ATOM   595   N N     . PRO A 1 1689 ? 207.825 207.028 149.772 1.00 117.42 ? 1689 PRO A N     1 
ATOM   596   C CA    . PRO A 1 1689 ? 206.473 206.766 149.265 1.00 117.42 ? 1689 PRO A CA    1 
ATOM   597   C C     . PRO A 1 1689 ? 206.495 206.364 147.798 1.00 117.42 ? 1689 PRO A C     1 
ATOM   598   O O     . PRO A 1 1689 ? 207.368 206.778 147.033 1.00 117.42 ? 1689 PRO A O     1 
ATOM   599   C CB    . PRO A 1 1689 ? 205.751 208.104 149.469 1.00 117.42 ? 1689 PRO A CB    1 
ATOM   600   C CG    . PRO A 1 1689 ? 206.574 208.844 150.474 1.00 117.42 ? 1689 PRO A CG    1 
ATOM   601   C CD    . PRO A 1 1689 ? 207.984 208.413 150.239 1.00 117.42 ? 1689 PRO A CD    1 
ATOM   602   N N     . VAL A 1 1690 ? 205.527 205.542 147.413 1.00 122.88 ? 1690 VAL A N     1 
ATOM   603   C CA    . VAL A 1 1690 ? 205.373 205.120 146.033 1.00 122.88 ? 1690 VAL A CA    1 
ATOM   604   C C     . VAL A 1 1690 ? 204.251 205.927 145.397 1.00 122.88 ? 1690 VAL A C     1 
ATOM   605   O O     . VAL A 1 1690 ? 203.420 206.533 146.078 1.00 122.88 ? 1690 VAL A O     1 
ATOM   606   C CB    . VAL A 1 1690 ? 205.098 203.607 145.919 1.00 122.88 ? 1690 VAL A CB    1 
ATOM   607   C CG1   . VAL A 1 1690 ? 206.185 202.825 146.625 1.00 122.88 ? 1690 VAL A CG1   1 
ATOM   608   C CG2   . VAL A 1 1690 ? 203.732 203.276 146.492 1.00 122.88 ? 1690 VAL A CG2   1 
ATOM   609   N N     . SER A 1 1691 ? 204.222 205.932 144.067 1.00 123.86 ? 1691 SER A N     1 
ATOM   610   C CA    . SER A 1 1691 ? 203.256 206.707 143.301 1.00 123.86 ? 1691 SER A CA    1 
ATOM   611   C C     . SER A 1 1691 ? 202.375 205.773 142.487 1.00 123.86 ? 1691 SER A C     1 
ATOM   612   O O     . SER A 1 1691 ? 202.881 204.891 141.786 1.00 123.86 ? 1691 SER A O     1 
ATOM   613   C CB    . SER A 1 1691 ? 203.965 207.698 142.376 1.00 123.86 ? 1691 SER A CB    1 
ATOM   614   O OG    . SER A 1 1691 ? 205.076 207.089 141.747 1.00 123.86 ? 1691 SER A OG    1 
ATOM   615   N N     . ILE A 1 1692 ? 201.060 205.973 142.576 1.00 124.90 ? 1692 ILE A N     1 
ATOM   616   C CA    . ILE A 1 1692 ? 200.145 205.174 141.769 1.00 124.90 ? 1692 ILE A CA    1 
ATOM   617   C C     . ILE A 1 1692 ? 200.146 205.646 140.321 1.00 124.90 ? 1692 ILE A C     1 
ATOM   618   O O     . ILE A 1 1692 ? 199.843 204.868 139.410 1.00 124.90 ? 1692 ILE A O     1 
ATOM   619   C CB    . ILE A 1 1692 ? 198.733 205.207 142.374 1.00 124.90 ? 1692 ILE A CB    1 
ATOM   620   C CG1   . ILE A 1 1692 ? 198.792 204.869 143.863 1.00 124.90 ? 1692 ILE A CG1   1 
ATOM   621   C CG2   . ILE A 1 1692 ? 197.815 204.238 141.649 1.00 124.90 ? 1692 ILE A CG2   1 
ATOM   622   C CD1   . ILE A 1 1692 ? 197.490 204.339 144.425 1.00 124.90 ? 1692 ILE A CD1   1 
ATOM   623   N N     . THR A 1 1693 ? 200.483 206.914 140.079 1.00 126.47 ? 1693 THR A N     1 
ATOM   624   C CA    . THR A 1 1693 ? 200.567 207.403 138.706 1.00 126.47 ? 1693 THR A CA    1 
ATOM   625   C C     . THR A 1 1693 ? 201.670 206.690 137.935 1.00 126.47 ? 1693 THR A C     1 
ATOM   626   O O     . THR A 1 1693 ? 201.492 206.339 136.763 1.00 126.47 ? 1693 THR A O     1 
ATOM   627   C CB    . THR A 1 1693 ? 200.799 208.912 138.697 1.00 126.47 ? 1693 THR A CB    1 
ATOM   628   O OG1   . THR A 1 1693 ? 202.050 209.208 139.330 1.00 126.47 ? 1693 THR A OG1   1 
ATOM   629   C CG2   . THR A 1 1693 ? 199.680 209.625 139.438 1.00 126.47 ? 1693 THR A CG2   1 
ATOM   630   N N     . GLU A 1 1694 ? 202.819 206.465 138.576 1.00 127.23 ? 1694 GLU A N     1 
ATOM   631   C CA    . GLU A 1 1694 ? 203.919 205.792 137.896 1.00 127.23 ? 1694 GLU A CA    1 
ATOM   632   C C     . GLU A 1 1694 ? 203.631 204.309 137.697 1.00 127.23 ? 1694 GLU A C     1 
ATOM   633   O O     . GLU A 1 1694 ? 204.095 203.713 136.720 1.00 127.23 ? 1694 GLU A O     1 
ATOM   634   C CB    . GLU A 1 1694 ? 205.218 206.004 138.675 1.00 127.23 ? 1694 GLU A CB    1 
ATOM   635   C CG    . GLU A 1 1694 ? 206.265 204.917 138.505 1.00 127.23 ? 1694 GLU A CG    1 
ATOM   636   C CD    . GLU A 1 1694 ? 207.512 205.181 139.326 1.00 127.23 ? 1694 GLU A CD    1 
ATOM   637   O OE1   . GLU A 1 1694 ? 208.044 206.307 139.250 1.00 127.23 ? 1694 GLU A OE1   1 
ATOM   638   O OE2   . GLU A 1 1694 ? 207.961 204.266 140.047 1.00 127.23 ? 1694 GLU A OE2   1 
ATOM   639   N N     . HIS A 1 1695 ? 202.847 203.704 138.588 1.00 125.89 ? 1695 HIS A N     1 
ATOM   640   C CA    . HIS A 1 1695 ? 202.437 202.307 138.467 1.00 125.89 ? 1695 HIS A CA    1 
ATOM   641   C C     . HIS A 1 1695 ? 200.916 202.267 138.455 1.00 125.89 ? 1695 HIS A C     1 
ATOM   642   O O     . HIS A 1 1695 ? 200.281 202.094 139.506 1.00 125.89 ? 1695 HIS A O     1 
ATOM   643   C CB    . HIS A 1 1695 ? 203.001 201.461 139.605 1.00 125.89 ? 1695 HIS A CB    1 
ATOM   644   C CG    . HIS A 1 1695 ? 204.473 201.213 139.503 1.00 125.89 ? 1695 HIS A CG    1 
ATOM   645   N ND1   . HIS A 1 1695 ? 205.413 202.123 139.935 1.00 125.89 ? 1695 HIS A ND1   1 
ATOM   646   C CD2   . HIS A 1 1695 ? 205.166 200.155 139.022 1.00 125.89 ? 1695 HIS A CD2   1 
ATOM   647   C CE1   . HIS A 1 1695 ? 206.622 201.636 139.724 1.00 125.89 ? 1695 HIS A CE1   1 
ATOM   648   N NE2   . HIS A 1 1695 ? 206.500 200.443 139.170 1.00 125.89 ? 1695 HIS A NE2   1 
ATOM   649   N N     . PRO A 1 1696 ? 200.289 202.420 137.288 1.00 126.73 ? 1696 PRO A N     1 
ATOM   650   C CA    . PRO A 1 1696 ? 198.822 202.504 137.261 1.00 126.73 ? 1696 PRO A CA    1 
ATOM   651   C C     . PRO A 1 1696 ? 198.131 201.184 137.546 1.00 126.73 ? 1696 PRO A C     1 
ATOM   652   O O     . PRO A 1 1696 ? 197.065 201.186 138.173 1.00 126.73 ? 1696 PRO A O     1 
ATOM   653   C CB    . PRO A 1 1696 ? 198.527 203.000 135.841 1.00 126.73 ? 1696 PRO A CB    1 
ATOM   654   C CG    . PRO A 1 1696 ? 199.683 202.527 135.031 1.00 126.73 ? 1696 PRO A CG    1 
ATOM   655   C CD    . PRO A 1 1696 ? 200.882 202.474 135.941 1.00 126.73 ? 1696 PRO A CD    1 
ATOM   656   N N     . LYS A 1 1697 ? 198.694 200.060 137.108 1.00 126.87 ? 1697 LYS A N     1 
ATOM   657   C CA    . LYS A 1 1697 ? 198.052 198.774 137.343 1.00 126.87 ? 1697 LYS A CA    1 
ATOM   658   C C     . LYS A 1 1697 ? 198.004 198.463 138.832 1.00 126.87 ? 1697 LYS A C     1 
ATOM   659   O O     . LYS A 1 1697 ? 198.944 198.754 139.576 1.00 126.87 ? 1697 LYS A O     1 
ATOM   660   C CB    . LYS A 1 1697 ? 198.783 197.662 136.593 1.00 126.87 ? 1697 LYS A CB    1 
ATOM   661   C CG    . LYS A 1 1697 ? 199.021 197.957 135.127 1.00 126.87 ? 1697 LYS A CG    1 
ATOM   662   C CD    . LYS A 1 1697 ? 199.360 196.687 134.370 1.00 126.87 ? 1697 LYS A CD    1 
ATOM   663   C CE    . LYS A 1 1697 ? 198.102 196.009 133.854 1.00 126.87 ? 1697 LYS A CE    1 
ATOM   664   N NZ    . LYS A 1 1697 ? 197.294 196.920 132.997 1.00 126.87 ? 1697 LYS A NZ    1 
ATOM   665   N N     . ILE A 1 1698 ? 196.898 197.853 139.257 1.00 128.52 ? 1698 ILE A N     1 
ATOM   666   C CA    . ILE A 1 1698 ? 196.645 197.639 140.680 1.00 128.52 ? 1698 ILE A CA    1 
ATOM   667   C C     . ILE A 1 1698 ? 197.721 196.746 141.294 1.00 128.52 ? 1698 ILE A C     1 
ATOM   668   O O     . ILE A 1 1698 ? 198.262 197.045 142.368 1.00 128.52 ? 1698 ILE A O     1 
ATOM   669   C CB    . ILE A 1 1698 ? 195.227 197.064 140.878 1.00 128.52 ? 1698 ILE A CB    1 
ATOM   670   C CG1   . ILE A 1 1698 ? 194.876 196.893 142.359 1.00 128.52 ? 1698 ILE A CG1   1 
ATOM   671   C CG2   . ILE A 1 1698 ? 195.027 195.773 140.084 1.00 128.52 ? 1698 ILE A CG2   1 
ATOM   672   C CD1   . ILE A 1 1698 ? 195.229 198.062 143.218 1.00 128.52 ? 1698 ILE A CD1   1 
ATOM   673   N N     . ASN A 1 1699 ? 198.067 195.653 140.610 1.00 131.90 ? 1699 ASN A N     1 
ATOM   674   C CA    . ASN A 1 1699 ? 198.901 194.628 141.229 1.00 131.90 ? 1699 ASN A CA    1 
ATOM   675   C C     . ASN A 1 1699 ? 200.321 195.122 141.467 1.00 131.90 ? 1699 ASN A C     1 
ATOM   676   O O     . ASN A 1 1699 ? 200.899 194.875 142.532 1.00 131.90 ? 1699 ASN A O     1 
ATOM   677   C CB    . ASN A 1 1699 ? 198.911 193.370 140.364 1.00 131.90 ? 1699 ASN A CB    1 
ATOM   678   C CG    . ASN A 1 1699 ? 199.158 193.674 138.906 1.00 131.90 ? 1699 ASN A CG    1 
ATOM   679   O OD1   . ASN A 1 1699 ? 200.195 194.229 138.545 1.00 131.90 ? 1699 ASN A OD1   1 
ATOM   680   N ND2   . ASN A 1 1699 ? 198.204 193.314 138.056 1.00 131.90 ? 1699 ASN A ND2   1 
ATOM   681   N N     . GLU A 1 1700 ? 200.905 195.814 140.488 1.00 129.24 ? 1700 GLU A N     1 
ATOM   682   C CA    . GLU A 1 1700 ? 202.295 196.234 140.625 1.00 129.24 ? 1700 GLU A CA    1 
ATOM   683   C C     . GLU A 1 1700 ? 202.458 197.217 141.778 1.00 129.24 ? 1700 GLU A C     1 
ATOM   684   O O     . GLU A 1 1700 ? 203.351 197.061 142.619 1.00 129.24 ? 1700 GLU A O     1 
ATOM   685   C CB    . GLU A 1 1700 ? 202.799 196.844 139.316 1.00 129.24 ? 1700 GLU A CB    1 
ATOM   686   C CG    . GLU A 1 1700 ? 201.780 197.689 138.574 1.00 129.24 ? 1700 GLU A CG    1 
ATOM   687   C CD    . GLU A 1 1700 ? 202.382 198.416 137.384 1.00 129.24 ? 1700 GLU A CD    1 
ATOM   688   O OE1   . GLU A 1 1700 ? 203.611 198.318 137.184 1.00 129.24 ? 1700 GLU A OE1   1 
ATOM   689   O OE2   . GLU A 1 1700 ? 201.630 199.094 136.653 1.00 129.24 ? 1700 GLU A OE2   1 
ATOM   690   N N     . TRP A 1 1701 ? 201.588 198.227 141.851 1.00 126.98 ? 1701 TRP A N     1 
ATOM   691   C CA    . TRP A 1 1701 ? 201.739 199.208 142.917 1.00 126.98 ? 1701 TRP A CA    1 
ATOM   692   C C     . TRP A 1 1701 ? 201.321 198.633 144.262 1.00 126.98 ? 1701 TRP A C     1 
ATOM   693   O O     . TRP A 1 1701 ? 201.846 199.053 145.296 1.00 126.98 ? 1701 TRP A O     1 
ATOM   694   C CB    . TRP A 1 1701 ? 200.971 200.492 142.588 1.00 126.98 ? 1701 TRP A CB    1 
ATOM   695   C CG    . TRP A 1 1701 ? 199.495 200.483 142.848 1.00 126.98 ? 1701 TRP A CG    1 
ATOM   696   C CD1   . TRP A 1 1701 ? 198.507 200.336 141.925 1.00 126.98 ? 1701 TRP A CD1   1 
ATOM   697   C CD2   . TRP A 1 1701 ? 198.839 200.700 144.103 1.00 126.98 ? 1701 TRP A CD2   1 
ATOM   698   N NE1   . TRP A 1 1701 ? 197.277 200.414 142.527 1.00 126.98 ? 1701 TRP A NE1   1 
ATOM   699   C CE2   . TRP A 1 1701 ? 197.453 200.638 143.865 1.00 126.98 ? 1701 TRP A CE2   1 
ATOM   700   C CE3   . TRP A 1 1701 ? 199.288 200.924 145.406 1.00 126.98 ? 1701 TRP A CE3   1 
ATOM   701   C CZ2   . TRP A 1 1701 ? 196.515 200.791 144.880 1.00 126.98 ? 1701 TRP A CZ2   1 
ATOM   702   C CZ3   . TRP A 1 1701 ? 198.354 201.074 146.412 1.00 126.98 ? 1701 TRP A CZ3   1 
ATOM   703   C CH2   . TRP A 1 1701 ? 196.984 201.007 146.143 1.00 126.98 ? 1701 TRP A CH2   1 
ATOM   704   N N     . LEU A 1 1702 ? 200.416 197.652 144.278 1.00 122.70 ? 1702 LEU A N     1 
ATOM   705   C CA    . LEU A 1 1702 ? 200.120 196.970 145.534 1.00 122.70 ? 1702 LEU A CA    1 
ATOM   706   C C     . LEU A 1 1702 ? 201.334 196.203 146.044 1.00 122.70 ? 1702 LEU A C     1 
ATOM   707   O O     . LEU A 1 1702 ? 201.648 196.241 147.241 1.00 122.70 ? 1702 LEU A O     1 
ATOM   708   C CB    . LEU A 1 1702 ? 198.932 196.031 145.350 1.00 122.70 ? 1702 LEU A CB    1 
ATOM   709   C CG    . LEU A 1 1702 ? 197.567 196.664 145.601 1.00 122.70 ? 1702 LEU A CG    1 
ATOM   710   C CD1   . LEU A 1 1702 ? 196.510 195.589 145.739 1.00 122.70 ? 1702 LEU A CD1   1 
ATOM   711   C CD2   . LEU A 1 1702 ? 197.607 197.546 146.836 1.00 122.70 ? 1702 LEU A CD2   1 
ATOM   712   N N     . THR A 1 1703 ? 202.030 195.499 145.149 1.00 123.40 ? 1703 THR A N     1 
ATOM   713   C CA    . THR A 1 1703 ? 203.242 194.792 145.550 1.00 123.40 ? 1703 THR A CA    1 
ATOM   714   C C     . THR A 1 1703 ? 204.308 195.771 146.022 1.00 123.40 ? 1703 THR A C     1 
ATOM   715   O O     . THR A 1 1703 ? 205.027 195.502 146.994 1.00 123.40 ? 1703 THR A O     1 
ATOM   716   C CB    . THR A 1 1703 ? 203.770 193.944 144.393 1.00 123.40 ? 1703 THR A CB    1 
ATOM   717   O OG1   . THR A 1 1703 ? 202.749 193.041 143.953 1.00 123.40 ? 1703 THR A OG1   1 
ATOM   718   C CG2   . THR A 1 1703 ? 204.984 193.141 144.830 1.00 123.40 ? 1703 THR A CG2   1 
ATOM   719   N N     . LEU A 1 1704 ? 204.429 196.909 145.338 1.00 121.94 ? 1704 LEU A N     1 
ATOM   720   C CA    . LEU A 1 1704 ? 205.366 197.935 145.782 1.00 121.94 ? 1704 LEU A CA    1 
ATOM   721   C C     . LEU A 1 1704 ? 205.001 198.449 147.167 1.00 121.94 ? 1704 LEU A C     1 
ATOM   722   O O     . LEU A 1 1704 ? 205.881 198.668 148.005 1.00 121.94 ? 1704 LEU A O     1 
ATOM   723   C CB    . LEU A 1 1704 ? 205.414 199.080 144.775 1.00 121.94 ? 1704 LEU A CB    1 
ATOM   724   C CG    . LEU A 1 1704 ? 206.576 199.008 143.784 1.00 121.94 ? 1704 LEU A CG    1 
ATOM   725   C CD1   . LEU A 1 1704 ? 207.890 198.890 144.538 1.00 121.94 ? 1704 LEU A CD1   1 
ATOM   726   C CD2   . LEU A 1 1704 ? 206.409 197.846 142.820 1.00 121.94 ? 1704 LEU A CD2   1 
ATOM   727   N N     . VAL A 1 1705 ? 203.708 198.644 147.428 1.00 119.42 ? 1705 VAL A N     1 
ATOM   728   C CA    . VAL A 1 1705 ? 203.273 199.083 148.750 1.00 119.42 ? 1705 VAL A CA    1 
ATOM   729   C C     . VAL A 1 1705 ? 203.650 198.052 149.802 1.00 119.42 ? 1705 VAL A C     1 
ATOM   730   O O     . VAL A 1 1705 ? 204.134 198.399 150.883 1.00 119.42 ? 1705 VAL A O     1 
ATOM   731   C CB    . VAL A 1 1705 ? 201.760 199.365 148.751 1.00 119.42 ? 1705 VAL A CB    1 
ATOM   732   C CG1   . VAL A 1 1705 ? 201.171 199.135 150.133 1.00 119.42 ? 1705 VAL A CG1   1 
ATOM   733   C CG2   . VAL A 1 1705 ? 201.497 200.785 148.294 1.00 119.42 ? 1705 VAL A CG2   1 
ATOM   734   N N     . GLU A 1 1706 ? 203.437 196.770 149.503 1.00 116.97 ? 1706 GLU A N     1 
ATOM   735   C CA    . GLU A 1 1706 ? 203.786 195.718 150.456 1.00 116.97 ? 1706 GLU A CA    1 
ATOM   736   C C     . GLU A 1 1706 ? 205.282 195.722 150.758 1.00 116.97 ? 1706 GLU A C     1 
ATOM   737   O O     . GLU A 1 1706 ? 205.699 195.705 151.927 1.00 116.97 ? 1706 GLU A O     1 
ATOM   738   C CB    . GLU A 1 1706 ? 203.352 194.359 149.908 1.00 116.97 ? 1706 GLU A CB    1 
ATOM   739   C CG    . GLU A 1 1706 ? 204.184 193.189 150.408 1.00 116.97 ? 1706 GLU A CG    1 
ATOM   740   C CD    . GLU A 1 1706 ? 203.770 191.868 149.789 1.00 116.97 ? 1706 GLU A CD    1 
ATOM   741   O OE1   . GLU A 1 1706 ? 203.642 191.805 148.550 1.00 116.97 ? 1706 GLU A OE1   1 
ATOM   742   O OE2   . GLU A 1 1706 ? 203.577 190.890 150.540 1.00 116.97 ? 1706 GLU A OE2   1 
ATOM   743   N N     . LYS A 1 1707 ? 206.105 195.748 149.709 1.00 114.83 ? 1707 LYS A N     1 
ATOM   744   C CA    . LYS A 1 1707 ? 207.549 195.708 149.908 1.00 114.83 ? 1707 LYS A CA    1 
ATOM   745   C C     . LYS A 1 1707 ? 208.029 196.934 150.668 1.00 114.83 ? 1707 LYS A C     1 
ATOM   746   O O     . LYS A 1 1707 ? 208.876 196.830 151.564 1.00 114.83 ? 1707 LYS A O     1 
ATOM   747   C CB    . LYS A 1 1707 ? 208.262 195.594 148.564 1.00 114.83 ? 1707 LYS A CB    1 
ATOM   748   C CG    . LYS A 1 1707 ? 209.716 195.171 148.668 1.00 114.83 ? 1707 LYS A CG    1 
ATOM   749   C CD    . LYS A 1 1707 ? 210.181 194.481 147.394 1.00 114.83 ? 1707 LYS A CD    1 
ATOM   750   C CE    . LYS A 1 1707 ? 209.188 193.420 146.946 1.00 114.83 ? 1707 LYS A CE    1 
ATOM   751   N NZ    . LYS A 1 1707 ? 209.539 192.848 145.618 1.00 114.83 ? 1707 LYS A NZ    1 
ATOM   752   N N     . GLU A 1 1708 ? 207.488 198.106 150.337 1.00 118.50 ? 1708 GLU A N     1 
ATOM   753   C CA    . GLU A 1 1708 ? 207.879 199.313 151.049 1.00 118.50 ? 1708 GLU A CA    1 
ATOM   754   C C     . GLU A 1 1708 ? 207.422 199.279 152.497 1.00 118.50 ? 1708 GLU A C     1 
ATOM   755   O O     . GLU A 1 1708 ? 208.146 199.751 153.375 1.00 118.50 ? 1708 GLU A O     1 
ATOM   756   C CB    . GLU A 1 1708 ? 207.329 200.545 150.339 1.00 118.50 ? 1708 GLU A CB    1 
ATOM   757   C CG    . GLU A 1 1708 ? 207.979 200.798 148.991 1.00 118.50 ? 1708 GLU A CG    1 
ATOM   758   C CD    . GLU A 1 1708 ? 209.023 201.892 149.041 1.00 118.50 ? 1708 GLU A CD    1 
ATOM   759   O OE1   . GLU A 1 1708 ? 209.653 202.069 150.104 1.00 118.50 ? 1708 GLU A OE1   1 
ATOM   760   O OE2   . GLU A 1 1708 ? 209.216 202.576 148.015 1.00 118.50 ? 1708 GLU A OE2   1 
ATOM   761   N N     . MET A 1 1709 ? 206.236 198.735 152.773 1.00 114.38 ? 1709 MET A N     1 
ATOM   762   C CA    . MET A 1 1709 ? 205.801 198.595 154.156 1.00 114.38 ? 1709 MET A CA    1 
ATOM   763   C C     . MET A 1 1709 ? 206.791 197.753 154.941 1.00 114.38 ? 1709 MET A C     1 
ATOM   764   O O     . MET A 1 1709 ? 207.213 198.130 156.039 1.00 114.38 ? 1709 MET A O     1 
ATOM   765   C CB    . MET A 1 1709 ? 204.406 197.973 154.215 1.00 114.38 ? 1709 MET A CB    1 
ATOM   766   C CG    . MET A 1 1709 ? 204.149 197.167 155.480 1.00 114.38 ? 1709 MET A CG    1 
ATOM   767   S SD    . MET A 1 1709 ? 202.547 196.342 155.497 1.00 114.38 ? 1709 MET A SD    1 
ATOM   768   C CE    . MET A 1 1709 ? 202.584 195.491 153.925 1.00 114.38 ? 1709 MET A CE    1 
ATOM   769   N N     . ARG A 1 1710 ? 207.201 196.620 154.371 1.00 109.23 ? 1710 ARG A N     1 
ATOM   770   C CA    . ARG A 1 1710 ? 208.185 195.784 155.050 1.00 109.23 ? 1710 ARG A CA    1 
ATOM   771   C C     . ARG A 1 1710 ? 209.490 196.542 155.269 1.00 109.23 ? 1710 ARG A C     1 
ATOM   772   O O     . ARG A 1 1710 ? 210.097 196.457 156.345 1.00 109.23 ? 1710 ARG A O     1 
ATOM   773   C CB    . ARG A 1 1710 ? 208.431 194.509 154.248 1.00 109.23 ? 1710 ARG A CB    1 
ATOM   774   C CG    . ARG A 1 1710 ? 207.202 193.635 154.091 1.00 109.23 ? 1710 ARG A CG    1 
ATOM   775   C CD    . ARG A 1 1710 ? 207.553 192.169 154.224 1.00 109.23 ? 1710 ARG A CD    1 
ATOM   776   N NE    . ARG A 1 1710 ? 206.527 191.317 153.639 1.00 109.23 ? 1710 ARG A NE    1 
ATOM   777   C CZ    . ARG A 1 1710 ? 206.459 191.013 152.351 1.00 109.23 ? 1710 ARG A CZ    1 
ATOM   778   N NH1   . ARG A 1 1710 ? 207.339 191.483 151.483 1.00 109.23 ? 1710 ARG A NH1   1 
ATOM   779   N NH2   . ARG A 1 1710 ? 205.484 190.218 151.922 1.00 109.23 ? 1710 ARG A NH2   1 
ATOM   780   N N     . VAL A 1 1711 ? 209.929 197.302 154.264 1.00 110.48 ? 1711 VAL A N     1 
ATOM   781   C CA    . VAL A 1 1711 ? 211.206 198.001 154.370 1.00 110.48 ? 1711 VAL A CA    1 
ATOM   782   C C     . VAL A 1 1711 ? 211.161 199.063 155.463 1.00 110.48 ? 1711 VAL A C     1 
ATOM   783   O O     . VAL A 1 1711 ? 212.082 199.163 156.282 1.00 110.48 ? 1711 VAL A O     1 
ATOM   784   C CB    . VAL A 1 1711 ? 211.598 198.603 153.011 1.00 110.48 ? 1711 VAL A CB    1 
ATOM   785   C CG1   . VAL A 1 1711 ? 212.752 199.577 153.178 1.00 110.48 ? 1711 VAL A CG1   1 
ATOM   786   C CG2   . VAL A 1 1711 ? 211.973 197.498 152.039 1.00 110.48 ? 1711 VAL A CG2   1 
ATOM   787   N N     . THR A 1 1712 ? 210.105 199.879 155.492 1.00 113.34 ? 1712 THR A N     1 
ATOM   788   C CA    . THR A 1 1712 ? 210.013 200.899 156.536 1.00 113.34 ? 1712 THR A CA    1 
ATOM   789   C C     . THR A 1 1712 ? 209.829 200.273 157.907 1.00 113.34 ? 1712 THR A C     1 
ATOM   790   O O     . THR A 1 1712 ? 210.310 200.814 158.906 1.00 113.34 ? 1712 THR A O     1 
ATOM   791   C CB    . THR A 1 1712 ? 208.885 201.894 156.261 1.00 113.34 ? 1712 THR A CB    1 
ATOM   792   O OG1   . THR A 1 1712 ? 207.658 201.405 156.821 1.00 113.34 ? 1712 THR A OG1   1 
ATOM   793   C CG2   . THR A 1 1712 ? 208.744 202.208 154.785 1.00 113.34 ? 1712 THR A CG2   1 
ATOM   794   N N     . LEU A 1 1713 ? 209.135 199.138 157.983 1.00 106.76 ? 1713 LEU A N     1 
ATOM   795   C CA    . LEU A 1 1713 ? 209.060 198.429 159.253 1.00 106.76 ? 1713 LEU A CA    1 
ATOM   796   C C     . LEU A 1 1713 ? 210.453 198.041 159.733 1.00 106.76 ? 1713 LEU A C     1 
ATOM   797   O O     . LEU A 1 1713 ? 210.799 198.252 160.901 1.00 106.76 ? 1713 LEU A O     1 
ATOM   798   C CB    . LEU A 1 1713 ? 208.166 197.198 159.107 1.00 106.76 ? 1713 LEU A CB    1 
ATOM   799   C CG    . LEU A 1 1713 ? 206.685 197.315 159.482 1.00 106.76 ? 1713 LEU A CG    1 
ATOM   800   C CD1   . LEU A 1 1713 ? 206.535 197.386 160.969 1.00 106.76 ? 1713 LEU A CD1   1 
ATOM   801   C CD2   . LEU A 1 1713 ? 206.040 198.534 158.860 1.00 106.76 ? 1713 LEU A CD2   1 
ATOM   802   N N     . ALA A 1 1714 ? 211.280 197.511 158.831 1.00 106.33 ? 1714 ALA A N     1 
ATOM   803   C CA    . ALA A 1 1714 ? 212.639 197.130 159.205 1.00 106.33 ? 1714 ALA A CA    1 
ATOM   804   C C     . ALA A 1 1714 ? 213.461 198.342 159.631 1.00 106.33 ? 1714 ALA A C     1 
ATOM   805   O O     . ALA A 1 1714 ? 214.211 198.285 160.612 1.00 106.33 ? 1714 ALA A O     1 
ATOM   806   C CB    . ALA A 1 1714 ? 213.318 196.403 158.045 1.00 106.33 ? 1714 ALA A CB    1 
ATOM   807   N N     . LYS A 1 1715 ? 213.347 199.446 158.892 1.00 110.27 ? 1715 LYS A N     1 
ATOM   808   C CA    . LYS A 1 1715 ? 214.150 200.622 159.217 1.00 110.27 ? 1715 LYS A CA    1 
ATOM   809   C C     . LYS A 1 1715 ? 213.715 201.244 160.539 1.00 110.27 ? 1715 LYS A C     1 
ATOM   810   O O     . LYS A 1 1715 ? 214.557 201.681 161.336 1.00 110.27 ? 1715 LYS A O     1 
ATOM   811   C CB    . LYS A 1 1715 ? 214.080 201.642 158.081 1.00 110.27 ? 1715 LYS A CB    1 
ATOM   812   C CG    . LYS A 1 1715 ? 214.483 201.073 156.728 1.00 110.27 ? 1715 LYS A CG    1 
ATOM   813   C CD    . LYS A 1 1715 ? 214.351 202.099 155.614 1.00 110.27 ? 1715 LYS A CD    1 
ATOM   814   C CE    . LYS A 1 1715 ? 215.350 203.231 155.778 1.00 110.27 ? 1715 LYS A CE    1 
ATOM   815   N NZ    . LYS A 1 1715 ? 216.733 202.724 155.985 1.00 110.27 ? 1715 LYS A NZ    1 
ATOM   816   N N     . LEU A 1 1716 ? 212.405 201.288 160.793 1.00 104.53 ? 1716 LEU A N     1 
ATOM   817   C CA    . LEU A 1 1716 ? 211.923 201.752 162.086 1.00 104.53 ? 1716 LEU A CA    1 
ATOM   818   C C     . LEU A 1 1716 ? 212.408 200.841 163.198 1.00 104.53 ? 1716 LEU A C     1 
ATOM   819   O O     . LEU A 1 1716 ? 212.759 201.311 164.285 1.00 104.53 ? 1716 LEU A O     1 
ATOM   820   C CB    . LEU A 1 1716 ? 210.398 201.828 162.087 1.00 104.53 ? 1716 LEU A CB    1 
ATOM   821   C CG    . LEU A 1 1716 ? 209.760 202.990 161.330 1.00 104.53 ? 1716 LEU A CG    1 
ATOM   822   C CD1   . LEU A 1 1716 ? 208.305 203.146 161.736 1.00 104.53 ? 1716 LEU A CD1   1 
ATOM   823   C CD2   . LEU A 1 1716 ? 210.528 204.277 161.568 1.00 104.53 ? 1716 LEU A CD2   1 
ATOM   824   N N     . LEU A 1 1717 ? 212.434 199.531 162.947 1.00 104.60 ? 1717 LEU A N     1 
ATOM   825   C CA    . LEU A 1 1717 ? 212.965 198.609 163.941 1.00 104.60 ? 1717 LEU A CA    1 
ATOM   826   C C     . LEU A 1 1717 ? 214.425 198.905 164.235 1.00 104.60 ? 1717 LEU A C     1 
ATOM   827   O O     . LEU A 1 1717 ? 214.845 198.899 165.395 1.00 104.60 ? 1717 LEU A O     1 
ATOM   828   C CB    . LEU A 1 1717 ? 212.807 197.167 163.465 1.00 104.60 ? 1717 LEU A CB    1 
ATOM   829   C CG    . LEU A 1 1717 ? 213.088 196.123 164.543 1.00 104.60 ? 1717 LEU A CG    1 
ATOM   830   C CD1   . LEU A 1 1717 ? 212.078 196.246 165.672 1.00 104.60 ? 1717 LEU A CD1   1 
ATOM   831   C CD2   . LEU A 1 1717 ? 213.091 194.723 163.959 1.00 104.60 ? 1717 LEU A CD2   1 
ATOM   832   N N     . ALA A 1 1718 ? 215.213 199.166 163.194 1.00 107.75 ? 1718 ALA A N     1 
ATOM   833   C CA    . ALA A 1 1718 ? 216.625 199.468 163.400 1.00 107.75 ? 1718 ALA A CA    1 
ATOM   834   C C     . ALA A 1 1718 ? 216.794 200.735 164.228 1.00 107.75 ? 1718 ALA A C     1 
ATOM   835   O O     . ALA A 1 1718 ? 217.581 200.770 165.182 1.00 107.75 ? 1718 ALA A O     1 
ATOM   836   C CB    . ALA A 1 1718 ? 217.335 199.601 162.054 1.00 107.75 ? 1718 ALA A CB    1 
ATOM   837   N N     . GLU A 1 1719 ? 216.048 201.785 163.882 1.00 111.50 ? 1719 GLU A N     1 
ATOM   838   C CA    . GLU A 1 1719 ? 216.152 203.037 164.625 1.00 111.50 ? 1719 GLU A CA    1 
ATOM   839   C C     . GLU A 1 1719 ? 215.738 202.848 166.080 1.00 111.50 ? 1719 GLU A C     1 
ATOM   840   O O     . GLU A 1 1719 ? 216.420 203.320 167.002 1.00 111.50 ? 1719 GLU A O     1 
ATOM   841   C CB    . GLU A 1 1719 ? 215.293 204.107 163.952 1.00 111.50 ? 1719 GLU A CB    1 
ATOM   842   C CG    . GLU A 1 1719 ? 215.622 205.531 164.357 1.00 111.50 ? 1719 GLU A CG    1 
ATOM   843   C CD    . GLU A 1 1719 ? 214.630 206.533 163.799 1.00 111.50 ? 1719 GLU A CD    1 
ATOM   844   O OE1   . GLU A 1 1719 ? 214.689 207.716 164.194 1.00 111.50 ? 1719 GLU A OE1   1 
ATOM   845   O OE2   . GLU A 1 1719 ? 213.789 206.137 162.965 1.00 111.50 ? 1719 GLU A OE2   1 
ATOM   846   N N     . SER A 1 1720 ? 214.634 202.135 166.306 1.00 107.71 ? 1720 SER A N     1 
ATOM   847   C CA    . SER A 1 1720 ? 214.170 201.905 167.666 1.00 107.71 ? 1720 SER A CA    1 
ATOM   848   C C     . SER A 1 1720 ? 215.170 201.074 168.451 1.00 107.71 ? 1720 SER A C     1 
ATOM   849   O O     . SER A 1 1720 ? 215.357 201.296 169.649 1.00 107.71 ? 1720 SER A O     1 
ATOM   850   C CB    . SER A 1 1720 ? 212.803 201.226 167.650 1.00 107.71 ? 1720 SER A CB    1 
ATOM   851   O OG    . SER A 1 1720 ? 212.165 201.355 168.907 1.00 107.71 ? 1720 SER A OG    1 
ATOM   852   N N     . VAL A 1 1721 ? 215.817 200.108 167.794 1.00 107.67 ? 1721 VAL A N     1 
ATOM   853   C CA    . VAL A 1 1721 ? 216.837 199.306 168.462 1.00 107.67 ? 1721 VAL A CA    1 
ATOM   854   C C     . VAL A 1 1721 ? 218.008 200.182 168.872 1.00 107.67 ? 1721 VAL A C     1 
ATOM   855   O O     . VAL A 1 1721 ? 218.531 200.064 169.988 1.00 107.67 ? 1721 VAL A O     1 
ATOM   856   C CB    . VAL A 1 1721 ? 217.285 198.144 167.557 1.00 107.67 ? 1721 VAL A CB    1 
ATOM   857   C CG1   . VAL A 1 1721 ? 218.700 197.712 167.904 1.00 107.67 ? 1721 VAL A CG1   1 
ATOM   858   C CG2   . VAL A 1 1721 ? 216.329 196.977 167.689 1.00 107.67 ? 1721 VAL A CG2   1 
ATOM   859   N N     . THR A 1 1722 ? 218.438 201.077 167.979 1.00 111.77 ? 1722 THR A N     1 
ATOM   860   C CA    . THR A 1 1722 ? 219.500 202.011 168.337 1.00 111.77 ? 1722 THR A CA    1 
ATOM   861   C C     . THR A 1 1722 ? 219.114 202.841 169.552 1.00 111.77 ? 1722 THR A C     1 
ATOM   862   O O     . THR A 1 1722 ? 219.950 203.109 170.422 1.00 111.77 ? 1722 THR A O     1 
ATOM   863   C CB    . THR A 1 1722 ? 219.835 202.923 167.157 1.00 111.77 ? 1722 THR A CB    1 
ATOM   864   O OG1   . THR A 1 1722 ? 218.715 203.770 166.870 1.00 111.77 ? 1722 THR A OG1   1 
ATOM   865   C CG2   . THR A 1 1722 ? 220.213 202.112 165.929 1.00 111.77 ? 1722 THR A CG2   1 
ATOM   866   N N     . GLU A 1 1723 ? 217.849 203.257 169.631 1.00 112.20 ? 1723 GLU A N     1 
ATOM   867   C CA    . GLU A 1 1723 ? 217.425 204.038 170.791 1.00 112.20 ? 1723 GLU A CA    1 
ATOM   868   C C     . GLU A 1 1723 ? 217.406 203.195 172.065 1.00 112.20 ? 1723 GLU A C     1 
ATOM   869   O O     . GLU A 1 1723 ? 217.919 203.619 173.110 1.00 112.20 ? 1723 GLU A O     1 
ATOM   870   C CB    . GLU A 1 1723 ? 216.053 204.660 170.540 1.00 112.20 ? 1723 GLU A CB    1 
ATOM   871   C CG    . GLU A 1 1723 ? 215.961 205.465 169.256 1.00 112.20 ? 1723 GLU A CG    1 
ATOM   872   C CD    . GLU A 1 1723 ? 215.055 206.673 169.390 1.00 112.20 ? 1723 GLU A CD    1 
ATOM   873   O OE1   . GLU A 1 1723 ? 214.485 206.870 170.482 1.00 112.20 ? 1723 GLU A OE1   1 
ATOM   874   O OE2   . GLU A 1 1723 ? 214.913 207.425 168.404 1.00 112.20 ? 1723 GLU A OE2   1 
ATOM   875   N N     . VAL A 1 1724 ? 216.827 201.996 172.005 1.00 109.90 ? 1724 VAL A N     1 
ATOM   876   C CA    . VAL A 1 1724 ? 216.646 201.236 173.237 1.00 109.90 ? 1724 VAL A CA    1 
ATOM   877   C C     . VAL A 1 1724 ? 217.972 200.655 173.709 1.00 109.90 ? 1724 VAL A C     1 
ATOM   878   O O     . VAL A 1 1724 ? 218.115 200.333 174.891 1.00 109.90 ? 1724 VAL A O     1 
ATOM   879   C CB    . VAL A 1 1724 ? 215.584 200.130 173.074 1.00 109.90 ? 1724 VAL A CB    1 
ATOM   880   C CG1   . VAL A 1 1724 ? 215.812 199.325 171.817 1.00 109.90 ? 1724 VAL A CG1   1 
ATOM   881   C CG2   . VAL A 1 1724 ? 215.463 199.245 174.312 1.00 109.90 ? 1724 VAL A CG2   1 
ATOM   882   N N     . GLU A 1 1725 ? 218.967 200.536 172.828 1.00 110.76 ? 1725 GLU A N     1 
ATOM   883   C CA    . GLU A 1 1725 ? 220.293 200.149 173.298 1.00 110.76 ? 1725 GLU A CA    1 
ATOM   884   C C     . GLU A 1 1725 ? 220.849 201.184 174.266 1.00 110.76 ? 1725 GLU A C     1 
ATOM   885   O O     . GLU A 1 1725 ? 221.426 200.830 175.300 1.00 110.76 ? 1725 GLU A O     1 
ATOM   886   C CB    . GLU A 1 1725 ? 221.241 199.951 172.116 1.00 110.76 ? 1725 GLU A CB    1 
ATOM   887   C CG    . GLU A 1 1725 ? 220.986 198.680 171.329 1.00 110.76 ? 1725 GLU A CG    1 
ATOM   888   C CD    . GLU A 1 1725 ? 221.816 197.518 171.825 1.00 110.76 ? 1725 GLU A CD    1 
ATOM   889   O OE1   . GLU A 1 1725 ? 222.348 197.602 172.952 1.00 110.76 ? 1725 GLU A OE1   1 
ATOM   890   O OE2   . GLU A 1 1725 ? 221.934 196.517 171.090 1.00 110.76 ? 1725 GLU A OE2   1 
ATOM   891   N N     . ILE A 1 1726 ? 220.680 202.467 173.949 1.00 112.92 ? 1726 ILE A N     1 
ATOM   892   C CA    . ILE A 1 1726 ? 221.056 203.517 174.887 1.00 112.92 ? 1726 ILE A CA    1 
ATOM   893   C C     . ILE A 1 1726 ? 220.153 203.480 176.110 1.00 112.92 ? 1726 ILE A C     1 
ATOM   894   O O     . ILE A 1 1726 ? 220.603 203.699 177.241 1.00 112.92 ? 1726 ILE A O     1 
ATOM   895   C CB    . ILE A 1 1726 ? 221.010 204.891 174.196 1.00 112.92 ? 1726 ILE A CB    1 
ATOM   896   C CG1   . ILE A 1 1726 ? 221.680 204.823 172.823 1.00 112.92 ? 1726 ILE A CG1   1 
ATOM   897   C CG2   . ILE A 1 1726 ? 221.677 205.943 175.062 1.00 112.92 ? 1726 ILE A CG2   1 
ATOM   898   C CD1   . ILE A 1 1726 ? 223.156 204.506 172.881 1.00 112.92 ? 1726 ILE A CD1   1 
ATOM   899   N N     . PHE A 1 1727 ? 218.861 203.214 175.902 1.00 114.05 ? 1727 PHE A N     1 
ATOM   900   C CA    . PHE A 1 1727 ? 217.913 203.223 177.014 1.00 114.05 ? 1727 PHE A CA    1 
ATOM   901   C C     . PHE A 1 1727 ? 218.270 202.177 178.066 1.00 114.05 ? 1727 PHE A C     1 
ATOM   902   O O     . PHE A 1 1727 ? 218.404 202.494 179.253 1.00 114.05 ? 1727 PHE A O     1 
ATOM   903   C CB    . PHE A 1 1727 ? 216.499 202.979 176.491 1.00 114.05 ? 1727 PHE A CB    1 
ATOM   904   C CG    . PHE A 1 1727 ? 215.777 204.226 176.096 1.00 114.05 ? 1727 PHE A CG    1 
ATOM   905   C CD1   . PHE A 1 1727 ? 215.477 205.195 177.036 1.00 114.05 ? 1727 PHE A CD1   1 
ATOM   906   C CD2   . PHE A 1 1727 ? 215.397 204.431 174.784 1.00 114.05 ? 1727 PHE A CD2   1 
ATOM   907   C CE1   . PHE A 1 1727 ? 214.809 206.346 176.672 1.00 114.05 ? 1727 PHE A CE1   1 
ATOM   908   C CE2   . PHE A 1 1727 ? 214.733 205.578 174.413 1.00 114.05 ? 1727 PHE A CE2   1 
ATOM   909   C CZ    . PHE A 1 1727 ? 214.437 206.537 175.358 1.00 114.05 ? 1727 PHE A CZ    1 
ATOM   910   N N     . GLY A 1 1728 ? 218.427 200.922 177.643 1.00 122.17 ? 1728 GLY A N     1 
ATOM   911   C CA    . GLY A 1 1728 ? 218.646 199.844 178.594 1.00 122.17 ? 1728 GLY A CA    1 
ATOM   912   C C     . GLY A 1 1728 ? 219.996 199.916 179.278 1.00 122.17 ? 1728 GLY A C     1 
ATOM   913   O O     . GLY A 1 1728 ? 220.097 199.718 180.491 1.00 122.17 ? 1728 GLY A O     1 
ATOM   914   N N     . LYS A 1 1729 ? 221.051 200.206 178.518 1.00 125.11 ? 1729 LYS A N     1 
ATOM   915   C CA    . LYS A 1 1729 ? 222.397 200.299 179.080 1.00 125.11 ? 1729 LYS A CA    1 
ATOM   916   C C     . LYS A 1 1729 ? 222.523 201.625 179.834 1.00 125.11 ? 1729 LYS A C     1 
ATOM   917   O O     . LYS A 1 1729 ? 223.264 202.538 179.463 1.00 125.11 ? 1729 LYS A O     1 
ATOM   918   C CB    . LYS A 1 1729 ? 223.445 200.152 177.985 1.00 125.11 ? 1729 LYS A CB    1 
ATOM   919   C CG    . LYS A 1 1729 ? 224.879 200.131 178.488 1.00 125.11 ? 1729 LYS A CG    1 
ATOM   920   C CD    . LYS A 1 1729 ? 225.011 199.289 179.743 1.00 125.11 ? 1729 LYS A CD    1 
ATOM   921   C CE    . LYS A 1 1729 ? 225.912 199.971 180.760 1.00 125.11 ? 1729 LYS A CE    1 
ATOM   922   N NZ    . LYS A 1 1729 ? 225.186 201.028 181.520 1.00 125.11 ? 1729 LYS A NZ    1 
ATOM   923   N N     . ALA A 1 1730 ? 221.763 201.714 180.921 1.00 125.13 ? 1730 ALA A N     1 
ATOM   924   C CA    . ALA A 1 1730 ? 221.718 202.897 181.770 1.00 125.13 ? 1730 ALA A CA    1 
ATOM   925   C C     . ALA A 1 1730 ? 220.928 202.543 183.020 1.00 125.13 ? 1730 ALA A C     1 
ATOM   926   O O     . ALA A 1 1730 ? 220.325 201.471 183.116 1.00 125.13 ? 1730 ALA A O     1 
ATOM   927   C CB    . ALA A 1 1730 ? 221.093 204.096 181.052 1.00 125.13 ? 1730 ALA A CB    1 
ATOM   928   N N     . THR A 1 1731 ? 220.937 203.462 183.979 1.00 133.86 ? 1731 THR A N     1 
ATOM   929   C CA    . THR A 1 1731 ? 220.198 203.306 185.220 1.00 133.86 ? 1731 THR A CA    1 
ATOM   930   C C     . THR A 1 1731 ? 219.404 204.574 185.494 1.00 133.86 ? 1731 THR A C     1 
ATOM   931   O O     . THR A 1 1731 ? 219.803 205.672 185.096 1.00 133.86 ? 1731 THR A O     1 
ATOM   932   C CB    . THR A 1 1731 ? 221.131 203.008 186.400 1.00 133.86 ? 1731 THR A CB    1 
ATOM   933   O OG1   . THR A 1 1731 ? 220.395 203.095 187.627 1.00 133.86 ? 1731 THR A OG1   1 
ATOM   934   C CG2   . THR A 1 1731 ? 222.284 203.999 186.430 1.00 133.86 ? 1731 THR A CG2   1 
ATOM   935   N N     . SER A 1 1732 ? 218.272 204.408 186.179 1.00 134.05 ? 1732 SER A N     1 
ATOM   936   C CA    . SER A 1 1732 ? 217.368 205.510 186.508 1.00 134.05 ? 1732 SER A CA    1 
ATOM   937   C C     . SER A 1 1732 ? 216.945 206.263 185.244 1.00 134.05 ? 1732 SER A C     1 
ATOM   938   O O     . SER A 1 1732 ? 217.241 207.444 185.056 1.00 134.05 ? 1732 SER A O     1 
ATOM   939   C CB    . SER A 1 1732 ? 218.005 206.454 187.534 1.00 134.05 ? 1732 SER A CB    1 
ATOM   940   O OG    . SER A 1 1732 ? 219.025 207.240 186.942 1.00 134.05 ? 1732 SER A OG    1 
ATOM   941   N N     . ILE A 1 1733 ? 216.244 205.542 184.369 1.00 123.02 ? 1733 ILE A N     1 
ATOM   942   C CA    . ILE A 1 1733 ? 215.825 206.103 183.092 1.00 123.02 ? 1733 ILE A CA    1 
ATOM   943   C C     . ILE A 1 1733 ? 214.806 207.210 183.324 1.00 123.02 ? 1733 ILE A C     1 
ATOM   944   O O     . ILE A 1 1733 ? 213.860 207.056 184.107 1.00 123.02 ? 1733 ILE A O     1 
ATOM   945   C CB    . ILE A 1 1733 ? 215.254 205.005 182.185 1.00 123.02 ? 1733 ILE A CB    1 
ATOM   946   C CG1   . ILE A 1 1733 ? 216.217 203.820 182.121 1.00 123.02 ? 1733 ILE A CG1   1 
ATOM   947   C CG2   . ILE A 1 1733 ? 214.980 205.549 180.794 1.00 123.02 ? 1733 ILE A CG2   1 
ATOM   948   C CD1   . ILE A 1 1733 ? 215.668 202.632 181.366 1.00 123.02 ? 1733 ILE A CD1   1 
ATOM   949   N N     . ASP A 1 1734 ? 215.001 208.333 182.647 1.00 122.50 ? 1734 ASP A N     1 
ATOM   950   C CA    . ASP A 1 1734 ? 214.047 209.431 182.721 1.00 122.50 ? 1734 ASP A CA    1 
ATOM   951   C C     . ASP A 1 1734 ? 212.727 209.009 182.087 1.00 122.50 ? 1734 ASP A C     1 
ATOM   952   O O     . ASP A 1 1734 ? 212.721 208.508 180.958 1.00 122.50 ? 1734 ASP A O     1 
ATOM   953   C CB    . ASP A 1 1734 ? 214.607 210.663 182.012 1.00 122.50 ? 1734 ASP A CB    1 
ATOM   954   C CG    . ASP A 1 1734 ? 213.525 211.635 181.578 1.00 122.50 ? 1734 ASP A CG    1 
ATOM   955   O OD1   . ASP A 1 1734 ? 212.612 211.921 182.381 1.00 122.50 ? 1734 ASP A OD1   1 
ATOM   956   O OD2   . ASP A 1 1734 ? 213.585 212.111 180.425 1.00 122.50 ? 1734 ASP A OD2   1 
ATOM   957   N N     . PRO A 1 1735 ? 211.599 209.178 182.777 1.00 115.35 ? 1735 PRO A N     1 
ATOM   958   C CA    . PRO A 1 1735 ? 210.311 208.820 182.162 1.00 115.35 ? 1735 PRO A CA    1 
ATOM   959   C C     . PRO A 1 1735 ? 210.005 209.592 180.891 1.00 115.35 ? 1735 PRO A C     1 
ATOM   960   O O     . PRO A 1 1735 ? 209.349 209.049 179.994 1.00 115.35 ? 1735 PRO A O     1 
ATOM   961   C CB    . PRO A 1 1735 ? 209.299 209.137 183.271 1.00 115.35 ? 1735 PRO A CB    1 
ATOM   962   C CG    . PRO A 1 1735 ? 210.083 209.041 184.531 1.00 115.35 ? 1735 PRO A CG    1 
ATOM   963   C CD    . PRO A 1 1735 ? 211.455 209.539 184.195 1.00 115.35 ? 1735 PRO A CD    1 
ATOM   964   N N     . ASN A 1 1736 ? 210.462 210.840 180.780 1.00 117.72 ? 1736 ASN A N     1 
ATOM   965   C CA    . ASN A 1 1736 ? 210.078 211.670 179.642 1.00 117.72 ? 1736 ASN A CA    1 
ATOM   966   C C     . ASN A 1 1736 ? 210.678 211.150 178.341 1.00 117.72 ? 1736 ASN A C     1 
ATOM   967   O O     . ASN A 1 1736 ? 209.981 211.042 177.325 1.00 117.72 ? 1736 ASN A O     1 
ATOM   968   C CB    . ASN A 1 1736 ? 210.495 213.118 179.891 1.00 117.72 ? 1736 ASN A CB    1 
ATOM   969   C CG    . ASN A 1 1736 ? 209.693 213.770 181.000 1.00 117.72 ? 1736 ASN A CG    1 
ATOM   970   O OD1   . ASN A 1 1736 ? 208.513 213.470 181.187 1.00 117.72 ? 1736 ASN A OD1   1 
ATOM   971   N ND2   . ASN A 1 1736 ? 210.330 214.667 181.743 1.00 117.72 ? 1736 ASN A ND2   1 
ATOM   972   N N     . THR A 1 1737 ? 211.974 210.833 178.345 1.00 113.17 ? 1737 THR A N     1 
ATOM   973   C CA    . THR A 1 1737 ? 212.594 210.330 177.123 1.00 113.17 ? 1737 THR A CA    1 
ATOM   974   C C     . THR A 1 1737 ? 212.012 208.978 176.733 1.00 113.17 ? 1737 THR A C     1 
ATOM   975   O O     . THR A 1 1737 ? 211.810 208.700 175.545 1.00 113.17 ? 1737 THR A O     1 
ATOM   976   C CB    . THR A 1 1737 ? 214.112 210.244 177.285 1.00 113.17 ? 1737 THR A CB    1 
ATOM   977   O OG1   . THR A 1 1737 ? 214.672 209.545 176.166 1.00 113.17 ? 1737 THR A OG1   1 
ATOM   978   C CG2   . THR A 1 1737 ? 214.486 209.522 178.565 1.00 113.17 ? 1737 THR A CG2   1 
ATOM   979   N N     . TYR A 1 1738 ? 211.718 208.133 177.722 1.00 108.75 ? 1738 TYR A N     1 
ATOM   980   C CA    . TYR A 1 1738 ? 211.085 206.853 177.434 1.00 108.75 ? 1738 TYR A CA    1 
ATOM   981   C C     . TYR A 1 1738 ? 209.710 207.052 176.813 1.00 108.75 ? 1738 TYR A C     1 
ATOM   982   O O     . TYR A 1 1738 ? 209.327 206.330 175.885 1.00 108.75 ? 1738 TYR A O     1 
ATOM   983   C CB    . TYR A 1 1738 ? 210.975 206.026 178.712 1.00 108.75 ? 1738 TYR A CB    1 
ATOM   984   C CG    . TYR A 1 1738 ? 211.106 204.541 178.492 1.00 108.75 ? 1738 TYR A CG    1 
ATOM   985   C CD1   . TYR A 1 1738 ? 212.352 203.935 178.460 1.00 108.75 ? 1738 TYR A CD1   1 
ATOM   986   C CD2   . TYR A 1 1738 ? 209.988 203.749 178.289 1.00 108.75 ? 1738 TYR A CD2   1 
ATOM   987   C CE1   . TYR A 1 1738 ? 212.477 202.580 178.255 1.00 108.75 ? 1738 TYR A CE1   1 
ATOM   988   C CE2   . TYR A 1 1738 ? 210.103 202.395 178.079 1.00 108.75 ? 1738 TYR A CE2   1 
ATOM   989   C CZ    . TYR A 1 1738 ? 211.349 201.815 178.065 1.00 108.75 ? 1738 TYR A CZ    1 
ATOM   990   O OH    . TYR A 1 1738 ? 211.465 200.462 177.855 1.00 108.75 ? 1738 TYR A OH    1 
ATOM   991   N N     . ILE A 1 1739 ? 208.945 208.019 177.325 1.00 108.72 ? 1739 ILE A N     1 
ATOM   992   C CA    . ILE A 1 1739 ? 207.608 208.258 176.792 1.00 108.72 ? 1739 ILE A CA    1 
ATOM   993   C C     . ILE A 1 1739 ? 207.695 208.790 175.367 1.00 108.72 ? 1739 ILE A C     1 
ATOM   994   O O     . ILE A 1 1739 ? 206.900 208.409 174.498 1.00 108.72 ? 1739 ILE A O     1 
ATOM   995   C CB    . ILE A 1 1739 ? 206.808 209.186 177.730 1.00 108.72 ? 1739 ILE A CB    1 
ATOM   996   C CG1   . ILE A 1 1739 ? 205.359 208.710 177.827 1.00 108.72 ? 1739 ILE A CG1   1 
ATOM   997   C CG2   . ILE A 1 1739 ? 206.841 210.642 177.278 1.00 108.72 ? 1739 ILE A CG2   1 
ATOM   998   C CD1   . ILE A 1 1739 ? 205.186 207.500 178.708 1.00 108.72 ? 1739 ILE A CD1   1 
ATOM   999   N N     . THR A 1 1740 ? 208.676 209.653 175.092 1.00 108.37 ? 1740 THR A N     1 
ATOM   1000  C CA    . THR A 1 1740 ? 208.869 210.108 173.719 1.00 108.37 ? 1740 THR A CA    1 
ATOM   1001  C C     . THR A 1 1740 ? 209.224 208.939 172.814 1.00 108.37 ? 1740 THR A C     1 
ATOM   1002  O O     . THR A 1 1740 ? 208.716 208.833 171.692 1.00 108.37 ? 1740 THR A O     1 
ATOM   1003  C CB    . THR A 1 1740 ? 209.956 211.179 173.651 1.00 108.37 ? 1740 THR A CB    1 
ATOM   1004  O OG1   . THR A 1 1740 ? 211.179 210.654 174.179 1.00 108.37 ? 1740 THR A OG1   1 
ATOM   1005  C CG2   . THR A 1 1740 ? 209.547 212.411 174.441 1.00 108.37 ? 1740 THR A CG2   1 
ATOM   1006  N N     . TRP A 1 1741 ? 210.084 208.041 173.296 1.00 105.85 ? 1741 TRP A N     1 
ATOM   1007  C CA    . TRP A 1 1741 ? 210.487 206.894 172.493 1.00 105.85 ? 1741 TRP A CA    1 
ATOM   1008  C C     . TRP A 1 1741 ? 209.299 206.003 172.164 1.00 105.85 ? 1741 TRP A C     1 
ATOM   1009  O O     . TRP A 1 1741 ? 209.110 205.601 171.011 1.00 105.85 ? 1741 TRP A O     1 
ATOM   1010  C CB    . TRP A 1 1741 ? 211.559 206.097 173.228 1.00 105.85 ? 1741 TRP A CB    1 
ATOM   1011  C CG    . TRP A 1 1741 ? 211.804 204.763 172.620 1.00 105.85 ? 1741 TRP A CG    1 
ATOM   1012  C CD1   . TRP A 1 1741 ? 212.251 204.517 171.363 1.00 105.85 ? 1741 TRP A CD1   1 
ATOM   1013  C CD2   . TRP A 1 1741 ? 211.624 203.486 173.240 1.00 105.85 ? 1741 TRP A CD2   1 
ATOM   1014  N NE1   . TRP A 1 1741 ? 212.357 203.165 171.152 1.00 105.85 ? 1741 TRP A NE1   1 
ATOM   1015  C CE2   . TRP A 1 1741 ? 211.980 202.509 172.292 1.00 105.85 ? 1741 TRP A CE2   1 
ATOM   1016  C CE3   . TRP A 1 1741 ? 211.198 203.073 174.504 1.00 105.85 ? 1741 TRP A CE3   1 
ATOM   1017  C CZ2   . TRP A 1 1741 ? 211.923 201.149 172.566 1.00 105.85 ? 1741 TRP A CZ2   1 
ATOM   1018  C CZ3   . TRP A 1 1741 ? 211.140 201.721 174.773 1.00 105.85 ? 1741 TRP A CZ3   1 
ATOM   1019  C CH2   . TRP A 1 1741 ? 211.505 200.775 173.811 1.00 105.85 ? 1741 TRP A CH2   1 
ATOM   1020  N N     . ILE A 1 1742 ? 208.484 205.683 173.169 1.00 104.92 ? 1742 ILE A N     1 
ATOM   1021  C CA    . ILE A 1 1742 ? 207.366 204.775 172.934 1.00 104.92 ? 1742 ILE A CA    1 
ATOM   1022  C C     . ILE A 1 1742 ? 206.311 205.438 172.056 1.00 104.92 ? 1742 ILE A C     1 
ATOM   1023  O O     . ILE A 1 1742 ? 205.695 204.782 171.209 1.00 104.92 ? 1742 ILE A O     1 
ATOM   1024  C CB    . ILE A 1 1742 ? 206.774 204.272 174.263 1.00 104.92 ? 1742 ILE A CB    1 
ATOM   1025  C CG1   . ILE A 1 1742 ? 206.319 205.440 175.124 1.00 104.92 ? 1742 ILE A CG1   1 
ATOM   1026  C CG2   . ILE A 1 1742 ? 207.789 203.436 175.016 1.00 104.92 ? 1742 ILE A CG2   1 
ATOM   1027  C CD1   . ILE A 1 1742 ? 204.950 205.272 175.684 1.00 104.92 ? 1742 ILE A CD1   1 
ATOM   1028  N N     . ASP A 1 1743 ? 206.085 206.744 172.232 1.00 103.25 ? 1743 ASP A N     1 
ATOM   1029  C CA    . ASP A 1 1743 ? 205.138 207.432 171.364 1.00 103.25 ? 1743 ASP A CA    1 
ATOM   1030  C C     . ASP A 1 1743 ? 205.641 207.499 169.930 1.00 103.25 ? 1743 ASP A C     1 
ATOM   1031  O O     . ASP A 1 1743 ? 204.836 207.479 168.992 1.00 103.25 ? 1743 ASP A O     1 
ATOM   1032  C CB    . ASP A 1 1743 ? 204.865 208.839 171.891 1.00 103.25 ? 1743 ASP A CB    1 
ATOM   1033  C CG    . ASP A 1 1743 ? 203.737 208.874 172.896 1.00 103.25 ? 1743 ASP A CG    1 
ATOM   1034  O OD1   . ASP A 1 1743 ? 202.597 208.529 172.522 1.00 103.25 ? 1743 ASP A OD1   1 
ATOM   1035  O OD2   . ASP A 1 1743 ? 203.988 209.248 174.060 1.00 103.25 ? 1743 ASP A OD2   1 
ATOM   1036  N N     . LYS A 1 1744 ? 206.959 207.580 169.740 1.00 104.63 ? 1744 LYS A N     1 
ATOM   1037  C CA    . LYS A 1 1744 ? 207.507 207.731 168.397 1.00 104.63 ? 1744 LYS A CA    1 
ATOM   1038  C C     . LYS A 1 1744 ? 207.224 206.506 167.537 1.00 104.63 ? 1744 LYS A C     1 
ATOM   1039  O O     . LYS A 1 1744 ? 206.908 206.633 166.348 1.00 104.63 ? 1744 LYS A O     1 
ATOM   1040  C CB    . LYS A 1 1744 ? 209.008 208.002 168.477 1.00 104.63 ? 1744 LYS A CB    1 
ATOM   1041  C CG    . LYS A 1 1744 ? 209.792 207.589 167.244 1.00 104.63 ? 1744 LYS A CG    1 
ATOM   1042  C CD    . LYS A 1 1744 ? 211.232 208.066 167.324 1.00 104.63 ? 1744 LYS A CD    1 
ATOM   1043  C CE    . LYS A 1 1744 ? 211.323 209.577 167.201 1.00 104.63 ? 1744 LYS A CE    1 
ATOM   1044  N NZ    . LYS A 1 1744 ? 210.516 210.086 166.058 1.00 104.63 ? 1744 LYS A NZ    1 
ATOM   1045  N N     . TYR A 1 1745 ? 207.322 205.315 168.116 1.00 104.67 ? 1745 TYR A N     1 
ATOM   1046  C CA    . TYR A 1 1745 ? 207.187 204.074 167.370 1.00 104.67 ? 1745 TYR A CA    1 
ATOM   1047  C C     . TYR A 1 1745 ? 205.852 203.405 167.667 1.00 104.67 ? 1745 TYR A C     1 
ATOM   1048  O O     . TYR A 1 1745 ? 205.087 203.830 168.535 1.00 104.67 ? 1745 TYR A O     1 
ATOM   1049  C CB    . TYR A 1 1745 ? 208.339 203.122 167.695 1.00 104.67 ? 1745 TYR A CB    1 
ATOM   1050  C CG    . TYR A 1 1745 ? 209.695 203.710 167.409 1.00 104.67 ? 1745 TYR A CG    1 
ATOM   1051  C CD1   . TYR A 1 1745 ? 210.102 203.959 166.109 1.00 104.67 ? 1745 TYR A CD1   1 
ATOM   1052  C CD2   . TYR A 1 1745 ? 210.567 204.018 168.438 1.00 104.67 ? 1745 TYR A CD2   1 
ATOM   1053  C CE1   . TYR A 1 1745 ? 211.342 204.496 165.844 1.00 104.67 ? 1745 TYR A CE1   1 
ATOM   1054  C CE2   . TYR A 1 1745 ? 211.806 204.554 168.182 1.00 104.67 ? 1745 TYR A CE2   1 
ATOM   1055  C CZ    . TYR A 1 1745 ? 212.190 204.790 166.885 1.00 104.67 ? 1745 TYR A CZ    1 
ATOM   1056  O OH    . TYR A 1 1745 ? 213.430 205.327 166.635 1.00 104.67 ? 1745 TYR A OH    1 
ATOM   1057  N N     . GLN A 1 1746 ? 205.584 202.338 166.921 1.00 101.58 ? 1746 GLN A N     1 
ATOM   1058  C CA    . GLN A 1 1746 ? 204.345 201.594 167.053 1.00 101.58 ? 1746 GLN A CA    1 
ATOM   1059  C C     . GLN A 1 1746 ? 204.447 200.591 168.198 1.00 101.58 ? 1746 GLN A C     1 
ATOM   1060  O O     . GLN A 1 1746 ? 205.530 200.307 168.717 1.00 101.58 ? 1746 GLN A O     1 
ATOM   1061  C CB    . GLN A 1 1746 ? 204.014 200.870 165.749 1.00 101.58 ? 1746 GLN A CB    1 
ATOM   1062  C CG    . GLN A 1 1746 ? 203.696 201.792 164.589 1.00 101.58 ? 1746 GLN A CG    1 
ATOM   1063  C CD    . GLN A 1 1746 ? 204.935 202.456 164.023 1.00 101.58 ? 1746 GLN A CD    1 
ATOM   1064  O OE1   . GLN A 1 1746 ? 206.056 202.018 164.278 1.00 101.58 ? 1746 GLN A OE1   1 
ATOM   1065  N NE2   . GLN A 1 1746 ? 204.741 203.522 163.257 1.00 101.58 ? 1746 GLN A NE2   1 
ATOM   1066  N N     . ALA A 1 1747 ? 203.292 200.046 168.586 1.00 98.07  ? 1747 ALA A N     1 
ATOM   1067  C CA    . ALA A 1 1747 ? 203.257 199.098 169.695 1.00 98.07  ? 1747 ALA A CA    1 
ATOM   1068  C C     . ALA A 1 1747 ? 204.081 197.856 169.382 1.00 98.07  ? 1747 ALA A C     1 
ATOM   1069  O O     . ALA A 1 1747 ? 204.960 197.461 170.161 1.00 98.07  ? 1747 ALA A O     1 
ATOM   1070  C CB    . ALA A 1 1747 ? 201.810 198.723 170.010 1.00 98.07  ? 1747 ALA A CB    1 
ATOM   1071  N N     . GLN A 1 1748 ? 203.818 197.233 168.232 1.00 92.76  ? 1748 GLN A N     1 
ATOM   1072  C CA    . GLN A 1 1748 ? 204.592 196.065 167.832 1.00 92.76  ? 1748 GLN A CA    1 
ATOM   1073  C C     . GLN A 1 1748 ? 206.072 196.401 167.759 1.00 92.76  ? 1748 GLN A C     1 
ATOM   1074  O O     . GLN A 1 1748 ? 206.924 195.624 168.208 1.00 92.76  ? 1748 GLN A O     1 
ATOM   1075  C CB    . GLN A 1 1748 ? 204.088 195.548 166.485 1.00 92.76  ? 1748 GLN A CB    1 
ATOM   1076  C CG    . GLN A 1 1748 ? 205.186 195.109 165.536 1.00 92.76  ? 1748 GLN A CG    1 
ATOM   1077  C CD    . GLN A 1 1748 ? 204.654 194.672 164.191 1.00 92.76  ? 1748 GLN A CD    1 
ATOM   1078  O OE1   . GLN A 1 1748 ? 203.601 195.129 163.748 1.00 92.76  ? 1748 GLN A OE1   1 
ATOM   1079  N NE2   . GLN A 1 1748 ? 205.381 193.782 163.530 1.00 92.76  ? 1748 GLN A NE2   1 
ATOM   1080  N N     . LEU A 1 1749 ? 206.392 197.573 167.216 1.00 92.20  ? 1749 LEU A N     1 
ATOM   1081  C CA    . LEU A 1 1749 ? 207.785 197.969 167.080 1.00 92.20  ? 1749 LEU A CA    1 
ATOM   1082  C C     . LEU A 1 1749 ? 208.443 198.125 168.439 1.00 92.20  ? 1749 LEU A C     1 
ATOM   1083  O O     . LEU A 1 1749 ? 209.583 197.690 168.636 1.00 92.20  ? 1749 LEU A O     1 
ATOM   1084  C CB    . LEU A 1 1749 ? 207.883 199.271 166.291 1.00 92.20  ? 1749 LEU A CB    1 
ATOM   1085  C CG    . LEU A 1 1749 ? 208.039 199.128 164.781 1.00 92.20  ? 1749 LEU A CG    1 
ATOM   1086  C CD1   . LEU A 1 1749 ? 209.467 198.787 164.448 1.00 92.20  ? 1749 LEU A CD1   1 
ATOM   1087  C CD2   . LEU A 1 1749 ? 207.112 198.065 164.254 1.00 92.20  ? 1749 LEU A CD2   1 
ATOM   1088  N N     . VAL A 1 1750 ? 207.741 198.740 169.390 1.00 93.19  ? 1750 VAL A N     1 
ATOM   1089  C CA    . VAL A 1 1750 ? 208.349 198.991 170.688 1.00 93.19  ? 1750 VAL A CA    1 
ATOM   1090  C C     . VAL A 1 1750 ? 208.551 197.681 171.442 1.00 93.19  ? 1750 VAL A C     1 
ATOM   1091  O O     . VAL A 1 1750 ? 209.586 197.478 172.090 1.00 93.19  ? 1750 VAL A O     1 
ATOM   1092  C CB    . VAL A 1 1750 ? 207.517 200.017 171.482 1.00 93.19  ? 1750 VAL A CB    1 
ATOM   1093  C CG1   . VAL A 1 1750 ? 206.330 199.380 172.174 1.00 93.19  ? 1750 VAL A CG1   1 
ATOM   1094  C CG2   . VAL A 1 1750 ? 208.391 200.744 172.477 1.00 93.19  ? 1750 VAL A CG2   1 
ATOM   1095  N N     . VAL A 1 1751 ? 207.596 196.753 171.334 1.00 89.46  ? 1751 VAL A N     1 
ATOM   1096  C CA    . VAL A 1 1751 ? 207.765 195.462 171.993 1.00 89.46  ? 1751 VAL A CA    1 
ATOM   1097  C C     . VAL A 1 1751 ? 208.928 194.693 171.376 1.00 89.46  ? 1751 VAL A C     1 
ATOM   1098  O O     . VAL A 1 1751 ? 209.739 194.089 172.092 1.00 89.46  ? 1751 VAL A O     1 
ATOM   1099  C CB    . VAL A 1 1751 ? 206.457 194.655 171.942 1.00 89.46  ? 1751 VAL A CB    1 
ATOM   1100  C CG1   . VAL A 1 1751 ? 206.687 193.253 172.456 1.00 89.46  ? 1751 VAL A CG1   1 
ATOM   1101  C CG2   . VAL A 1 1751 ? 205.394 195.344 172.765 1.00 89.46  ? 1751 VAL A CG2   1 
ATOM   1102  N N     . LEU A 1 1752 ? 209.030 194.698 170.043 1.00 88.24  ? 1752 LEU A N     1 
ATOM   1103  C CA    . LEU A 1 1752 ? 210.134 194.001 169.387 1.00 88.24  ? 1752 LEU A CA    1 
ATOM   1104  C C     . LEU A 1 1752 ? 211.475 194.609 169.764 1.00 88.24  ? 1752 LEU A C     1 
ATOM   1105  O O     . LEU A 1 1752 ? 212.453 193.885 169.978 1.00 88.24  ? 1752 LEU A O     1 
ATOM   1106  C CB    . LEU A 1 1752 ? 209.950 194.018 167.873 1.00 88.24  ? 1752 LEU A CB    1 
ATOM   1107  C CG    . LEU A 1 1752 ? 209.213 192.827 167.267 1.00 88.24  ? 1752 LEU A CG    1 
ATOM   1108  C CD1   . LEU A 1 1752 ? 210.153 191.642 167.199 1.00 88.24  ? 1752 LEU A CD1   1 
ATOM   1109  C CD2   . LEU A 1 1752 ? 207.965 192.470 168.057 1.00 88.24  ? 1752 LEU A CD2   1 
ATOM   1110  N N     . SER A 1 1753 ? 211.545 195.938 169.841 1.00 92.24  ? 1753 SER A N     1 
ATOM   1111  C CA    . SER A 1 1753 ? 212.786 196.579 170.254 1.00 92.24  ? 1753 SER A CA    1 
ATOM   1112  C C     . SER A 1 1753 ? 213.152 196.189 171.677 1.00 92.24  ? 1753 SER A C     1 
ATOM   1113  O O     . SER A 1 1753 ? 214.322 195.912 171.970 1.00 92.24  ? 1753 SER A O     1 
ATOM   1114  C CB    . SER A 1 1753 ? 212.662 198.095 170.132 1.00 92.24  ? 1753 SER A CB    1 
ATOM   1115  O OG    . SER A 1 1753 ? 211.470 198.550 170.742 1.00 92.24  ? 1753 SER A OG    1 
ATOM   1116  N N     . ALA A 1 1754 ? 212.166 196.161 172.576 1.00 87.12  ? 1754 ALA A N     1 
ATOM   1117  C CA    . ALA A 1 1754 ? 212.445 195.762 173.951 1.00 87.12  ? 1754 ALA A CA    1 
ATOM   1118  C C     . ALA A 1 1754 ? 212.970 194.335 174.013 1.00 87.12  ? 1754 ALA A C     1 
ATOM   1119  O O     . ALA A 1 1754 ? 213.961 194.056 174.702 1.00 87.12  ? 1754 ALA A O     1 
ATOM   1120  C CB    . ALA A 1 1754 ? 211.188 195.905 174.805 1.00 87.12  ? 1754 ALA A CB    1 
ATOM   1121  N N     . GLN A 1 1755 ? 212.327 193.420 173.285 1.00 84.14  ? 1755 GLN A N     1 
ATOM   1122  C CA    . GLN A 1 1755 ? 212.777 192.034 173.287 1.00 84.14  ? 1755 GLN A CA    1 
ATOM   1123  C C     . GLN A 1 1755 ? 214.185 191.912 172.727 1.00 84.14  ? 1755 GLN A C     1 
ATOM   1124  O O     . GLN A 1 1755 ? 215.020 191.191 173.282 1.00 84.14  ? 1755 GLN A O     1 
ATOM   1125  C CB    . GLN A 1 1755 ? 211.817 191.164 172.482 1.00 84.14  ? 1755 GLN A CB    1 
ATOM   1126  C CG    . GLN A 1 1755 ? 210.429 191.081 173.060 1.00 84.14  ? 1755 GLN A CG    1 
ATOM   1127  C CD    . GLN A 1 1755 ? 209.763 189.759 172.765 1.00 84.14  ? 1755 GLN A CD    1 
ATOM   1128  O OE1   . GLN A 1 1755 ? 210.243 188.704 173.176 1.00 84.14  ? 1755 GLN A OE1   1 
ATOM   1129  N NE2   . GLN A 1 1755 ? 208.653 189.805 172.040 1.00 84.14  ? 1755 GLN A NE2   1 
ATOM   1130  N N     . ILE A 1 1756 ? 214.467 192.609 171.624 1.00 85.15  ? 1756 ILE A N     1 
ATOM   1131  C CA    . ILE A 1 1756 ? 215.782 192.511 171.001 1.00 85.15  ? 1756 ILE A CA    1 
ATOM   1132  C C     . ILE A 1 1756 ? 216.855 193.037 171.939 1.00 85.15  ? 1756 ILE A C     1 
ATOM   1133  O O     . ILE A 1 1756 ? 217.907 192.411 172.119 1.00 85.15  ? 1756 ILE A O     1 
ATOM   1134  C CB    . ILE A 1 1756 ? 215.789 193.259 169.657 1.00 85.15  ? 1756 ILE A CB    1 
ATOM   1135  C CG1   . ILE A 1 1756 ? 215.104 192.422 168.584 1.00 85.15  ? 1756 ILE A CG1   1 
ATOM   1136  C CG2   . ILE A 1 1756 ? 217.203 193.582 169.237 1.00 85.15  ? 1756 ILE A CG2   1 
ATOM   1137  C CD1   . ILE A 1 1756 ? 214.996 193.125 167.264 1.00 85.15  ? 1756 ILE A CD1   1 
ATOM   1138  N N     . ALA A 1 1757 ? 216.605 194.190 172.560 1.00 89.94  ? 1757 ALA A N     1 
ATOM   1139  C CA    . ALA A 1 1757 ? 217.589 194.756 173.471 1.00 89.94  ? 1757 ALA A CA    1 
ATOM   1140  C C     . ALA A 1 1757 ? 217.831 193.836 174.657 1.00 89.94  ? 1757 ALA A C     1 
ATOM   1141  O O     . ALA A 1 1757 ? 218.983 193.596 175.038 1.00 89.94  ? 1757 ALA A O     1 
ATOM   1142  C CB    . ALA A 1 1757 ? 217.138 196.133 173.945 1.00 89.94  ? 1757 ALA A CB    1 
ATOM   1143  N N     . TRP A 1 1758 ? 216.760 193.302 175.250 1.00 84.50  ? 1758 TRP A N     1 
ATOM   1144  C CA    . TRP A 1 1758 ? 216.932 192.413 176.393 1.00 84.50  ? 1758 TRP A CA    1 
ATOM   1145  C C     . TRP A 1 1758 ? 217.694 191.154 176.008 1.00 84.50  ? 1758 TRP A C     1 
ATOM   1146  O O     . TRP A 1 1758 ? 218.591 190.715 176.737 1.00 84.50  ? 1758 TRP A O     1 
ATOM   1147  C CB    . TRP A 1 1758 ? 215.576 192.047 176.988 1.00 84.50  ? 1758 TRP A CB    1 
ATOM   1148  C CG    . TRP A 1 1758 ? 215.656 190.900 177.932 1.00 84.50  ? 1758 TRP A CG    1 
ATOM   1149  C CD1   . TRP A 1 1758 ? 216.146 190.921 179.198 1.00 84.50  ? 1758 TRP A CD1   1 
ATOM   1150  C CD2   . TRP A 1 1758 ? 215.243 189.554 177.682 1.00 84.50  ? 1758 TRP A CD2   1 
ATOM   1151  N NE1   . TRP A 1 1758 ? 216.061 189.672 179.759 1.00 84.50  ? 1758 TRP A NE1   1 
ATOM   1152  C CE2   . TRP A 1 1758 ? 215.509 188.815 178.846 1.00 84.50  ? 1758 TRP A CE2   1 
ATOM   1153  C CE3   . TRP A 1 1758 ? 214.670 188.904 176.588 1.00 84.50  ? 1758 TRP A CE3   1 
ATOM   1154  C CZ2   . TRP A 1 1758 ? 215.224 187.459 178.949 1.00 84.50  ? 1758 TRP A CZ2   1 
ATOM   1155  C CZ3   . TRP A 1 1758 ? 214.387 187.557 176.692 1.00 84.50  ? 1758 TRP A CZ3   1 
ATOM   1156  C CH2   . TRP A 1 1758 ? 214.664 186.849 177.862 1.00 84.50  ? 1758 TRP A CH2   1 
ATOM   1157  N N     . SER A 1 1759 ? 217.351 190.557 174.864 1.00 87.24  ? 1759 SER A N     1 
ATOM   1158  C CA    . SER A 1 1759 ? 218.015 189.328 174.452 1.00 87.24  ? 1759 SER A CA    1 
ATOM   1159  C C     . SER A 1 1759 ? 219.488 189.571 174.171 1.00 87.24  ? 1759 SER A C     1 
ATOM   1160  O O     . SER A 1 1759 ? 220.339 188.759 174.547 1.00 87.24  ? 1759 SER A O     1 
ATOM   1161  C CB    . SER A 1 1759 ? 217.324 188.740 173.225 1.00 87.24  ? 1759 SER A CB    1 
ATOM   1162  O OG    . SER A 1 1759 ? 217.968 189.154 172.037 1.00 87.24  ? 1759 SER A OG    1 
ATOM   1163  N N     . GLU A 1 1760 ? 219.815 190.688 173.520 1.00 97.78  ? 1760 GLU A N     1 
ATOM   1164  C CA    . GLU A 1 1760 ? 221.218 190.974 173.240 1.00 97.78  ? 1760 GLU A CA    1 
ATOM   1165  C C     . GLU A 1 1760 ? 221.987 191.270 174.520 1.00 97.78  ? 1760 GLU A C     1 
ATOM   1166  O O     . GLU A 1 1760 ? 223.144 190.854 174.665 1.00 97.78  ? 1760 GLU A O     1 
ATOM   1167  C CB    . GLU A 1 1760 ? 221.331 192.130 172.249 1.00 97.78  ? 1760 GLU A CB    1 
ATOM   1168  C CG    . GLU A 1 1760 ? 221.650 191.674 170.834 1.00 97.78  ? 1760 GLU A CG    1 
ATOM   1169  C CD    . GLU A 1 1760 ? 221.271 192.697 169.785 1.00 97.78  ? 1760 GLU A CD    1 
ATOM   1170  O OE1   . GLU A 1 1760 ? 221.582 193.890 169.978 1.00 97.78  ? 1760 GLU A OE1   1 
ATOM   1171  O OE2   . GLU A 1 1760 ? 220.668 192.307 168.763 1.00 97.78  ? 1760 GLU A OE2   1 
ATOM   1172  N N     . ASN A 1 1761 ? 221.364 191.976 175.466 1.00 95.42  ? 1761 ASN A N     1 
ATOM   1173  C CA    . ASN A 1 1761 ? 222.027 192.231 176.739 1.00 95.42  ? 1761 ASN A CA    1 
ATOM   1174  C C     . ASN A 1 1761 ? 222.306 190.930 177.480 1.00 95.42  ? 1761 ASN A C     1 
ATOM   1175  O O     . ASN A 1 1761 ? 223.405 190.731 178.012 1.00 95.42  ? 1761 ASN A O     1 
ATOM   1176  C CB    . ASN A 1 1761 ? 221.172 193.163 177.594 1.00 95.42  ? 1761 ASN A CB    1 
ATOM   1177  C CG    . ASN A 1 1761 ? 221.307 194.611 177.182 1.00 95.42  ? 1761 ASN A CG    1 
ATOM   1178  O OD1   . ASN A 1 1761 ? 221.996 194.928 176.213 1.00 95.42  ? 1761 ASN A OD1   1 
ATOM   1179  N ND2   . ASN A 1 1761 ? 220.646 195.499 177.912 1.00 95.42  ? 1761 ASN A ND2   1 
ATOM   1180  N N     . VAL A 1 1762 ? 221.328 190.024 177.508 1.00 97.69  ? 1762 VAL A N     1 
ATOM   1181  C CA    . VAL A 1 1762 ? 221.530 188.744 178.179 1.00 97.69  ? 1762 VAL A CA    1 
ATOM   1182  C C     . VAL A 1 1762 ? 222.602 187.932 177.467 1.00 97.69  ? 1762 VAL A C     1 
ATOM   1183  O O     . VAL A 1 1762 ? 223.431 187.276 178.108 1.00 97.69  ? 1762 VAL A O     1 
ATOM   1184  C CB    . VAL A 1 1762 ? 220.201 187.974 178.273 1.00 97.69  ? 1762 VAL A CB    1 
ATOM   1185  C CG1   . VAL A 1 1762 ? 220.445 186.554 178.737 1.00 97.69  ? 1762 VAL A CG1   1 
ATOM   1186  C CG2   . VAL A 1 1762 ? 219.254 188.685 179.217 1.00 97.69  ? 1762 VAL A CG2   1 
ATOM   1187  N N     . GLU A 1 1763 ? 222.599 187.952 176.132 1.00 98.47  ? 1763 GLU A N     1 
ATOM   1188  C CA    . GLU A 1 1763 ? 223.615 187.227 175.379 1.00 98.47  ? 1763 GLU A CA    1 
ATOM   1189  C C     . GLU A 1 1763 ? 225.008 187.738 175.710 1.00 98.47  ? 1763 GLU A C     1 
ATOM   1190  O O     . GLU A 1 1763 ? 225.933 186.946 175.921 1.00 98.47  ? 1763 GLU A O     1 
ATOM   1191  C CB    . GLU A 1 1763 ? 223.346 187.356 173.881 1.00 98.47  ? 1763 GLU A CB    1 
ATOM   1192  C CG    . GLU A 1 1763 ? 222.470 186.264 173.312 1.00 98.47  ? 1763 GLU A CG    1 
ATOM   1193  C CD    . GLU A 1 1763 ? 223.278 185.123 172.740 1.00 98.47  ? 1763 GLU A CD    1 
ATOM   1194  O OE1   . GLU A 1 1763 ? 224.521 185.234 172.712 1.00 98.47  ? 1763 GLU A OE1   1 
ATOM   1195  O OE2   . GLU A 1 1763 ? 222.674 184.117 172.317 1.00 98.47  ? 1763 GLU A OE2   1 
ATOM   1196  N N     . THR A 1 1764 ? 225.172 189.060 175.768 1.00 101.89 ? 1764 THR A N     1 
ATOM   1197  C CA    . THR A 1 1764 ? 226.459 189.625 176.155 1.00 101.89 ? 1764 THR A CA    1 
ATOM   1198  C C     . THR A 1 1764 ? 226.830 189.214 177.573 1.00 101.89 ? 1764 THR A C     1 
ATOM   1199  O O     . THR A 1 1764 ? 227.990 188.877 177.849 1.00 101.89 ? 1764 THR A O     1 
ATOM   1200  C CB    . THR A 1 1764 ? 226.423 191.147 176.030 1.00 101.89 ? 1764 THR A CB    1 
ATOM   1201  O OG1   . THR A 1 1764 ? 226.009 191.508 174.707 1.00 101.89 ? 1764 THR A OG1   1 
ATOM   1202  C CG2   . THR A 1 1764 ? 227.795 191.736 176.304 1.00 101.89 ? 1764 THR A CG2   1 
ATOM   1203  N N     . ALA A 1 1765 ? 225.855 189.223 178.483 1.00 106.61 ? 1765 ALA A N     1 
ATOM   1204  C CA    . ALA A 1 1765 ? 226.129 188.842 179.863 1.00 106.61 ? 1765 ALA A CA    1 
ATOM   1205  C C     . ALA A 1 1765 ? 226.651 187.412 179.947 1.00 106.61 ? 1765 ALA A C     1 
ATOM   1206  O O     . ALA A 1 1765 ? 227.690 187.156 180.564 1.00 106.61 ? 1765 ALA A O     1 
ATOM   1207  C CB    . ALA A 1 1765 ? 224.870 189.010 180.712 1.00 106.61 ? 1765 ALA A CB    1 
ATOM   1208  N N     . LEU A 1 1766 ? 225.948 186.467 179.320 1.00 112.90 ? 1766 LEU A N     1 
ATOM   1209  C CA    . LEU A 1 1766 ? 226.402 185.078 179.365 1.00 112.90 ? 1766 LEU A CA    1 
ATOM   1210  C C     . LEU A 1 1766 ? 227.721 184.887 178.632 1.00 112.90 ? 1766 LEU A C     1 
ATOM   1211  O O     . LEU A 1 1766 ? 228.548 184.075 179.061 1.00 112.90 ? 1766 LEU A O     1 
ATOM   1212  C CB    . LEU A 1 1766 ? 225.353 184.123 178.795 1.00 112.90 ? 1766 LEU A CB    1 
ATOM   1213  C CG    . LEU A 1 1766 ? 223.864 184.416 178.941 1.00 112.90 ? 1766 LEU A CG    1 
ATOM   1214  C CD1   . LEU A 1 1766 ? 223.053 183.275 178.355 1.00 112.90 ? 1766 LEU A CD1   1 
ATOM   1215  C CD2   . LEU A 1 1766 ? 223.502 184.629 180.401 1.00 112.90 ? 1766 LEU A CD2   1 
ATOM   1216  N N     . SER A 1 1767 ? 227.937 185.608 177.530 1.00 114.91 ? 1767 SER A N     1 
ATOM   1217  C CA    . SER A 1 1767 ? 229.228 185.536 176.857 1.00 114.91 ? 1767 SER A CA    1 
ATOM   1218  C C     . SER A 1 1767 ? 230.345 185.965 177.795 1.00 114.91 ? 1767 SER A C     1 
ATOM   1219  O O     . SER A 1 1767 ? 231.439 185.390 177.778 1.00 114.91 ? 1767 SER A O     1 
ATOM   1220  C CB    . SER A 1 1767 ? 229.216 186.406 175.603 1.00 114.91 ? 1767 SER A CB    1 
ATOM   1221  O OG    . SER A 1 1767 ? 229.638 187.724 175.902 1.00 114.91 ? 1767 SER A OG    1 
ATOM   1222  N N     . SER A 1 1768 ? 230.082 186.969 178.631 1.00 115.39 ? 1768 SER A N     1 
ATOM   1223  C CA    . SER A 1 1768 ? 231.050 187.365 179.643 1.00 115.39 ? 1768 SER A CA    1 
ATOM   1224  C C     . SER A 1 1768 ? 231.149 186.365 180.787 1.00 115.39 ? 1768 SER A C     1 
ATOM   1225  O O     . SER A 1 1768 ? 232.060 186.488 181.611 1.00 115.39 ? 1768 SER A O     1 
ATOM   1226  C CB    . SER A 1 1768 ? 230.695 188.745 180.191 1.00 115.39 ? 1768 SER A CB    1 
ATOM   1227  O OG    . SER A 1 1768 ? 230.331 189.624 179.142 1.00 115.39 ? 1768 SER A OG    1 
ATOM   1228  N N     . MET A 1 1769 ? 230.247 185.385 180.859 1.00 125.07 ? 1769 MET A N     1 
ATOM   1229  C CA    . MET A 1 1769 ? 230.224 184.417 181.949 1.00 125.07 ? 1769 MET A CA    1 
ATOM   1230  C C     . MET A 1 1769 ? 230.929 183.115 181.591 1.00 125.07 ? 1769 MET A C     1 
ATOM   1231  O O     . MET A 1 1769 ? 230.512 182.043 182.043 1.00 125.07 ? 1769 MET A O     1 
ATOM   1232  C CB    . MET A 1 1769 ? 228.787 184.129 182.387 1.00 125.07 ? 1769 MET A CB    1 
ATOM   1233  C CG    . MET A 1 1769 ? 227.996 185.282 183.022 1.00 125.07 ? 1769 MET A CG    1 
ATOM   1234  S SD    . MET A 1 1769 ? 228.766 186.674 183.899 1.00 125.07 ? 1769 MET A SD    1 
ATOM   1235  C CE    . MET A 1 1769 ? 230.137 185.972 184.819 1.00 125.07 ? 1769 MET A CE    1 
ATOM   1236  N N     . GLY A 1 1770 ? 231.987 183.182 180.784 1.00 133.45 ? 1770 GLY A N     1 
ATOM   1237  C CA    . GLY A 1 1770 ? 232.741 181.977 180.483 1.00 133.45 ? 1770 GLY A CA    1 
ATOM   1238  C C     . GLY A 1 1770 ? 233.346 181.346 181.723 1.00 133.45 ? 1770 GLY A C     1 
ATOM   1239  O O     . GLY A 1 1770 ? 233.316 180.124 181.889 1.00 133.45 ? 1770 GLY A O     1 
ATOM   1240  N N     . GLY A 1 1771 ? 233.897 182.172 182.615 1.00 134.02 ? 1771 GLY A N     1 
ATOM   1241  C CA    . GLY A 1 1771 ? 234.520 181.639 183.815 1.00 134.02 ? 1771 GLY A CA    1 
ATOM   1242  C C     . GLY A 1 1771 ? 233.529 180.989 184.761 1.00 134.02 ? 1771 GLY A C     1 
ATOM   1243  O O     . GLY A 1 1771 ? 233.794 179.915 185.308 1.00 134.02 ? 1771 GLY A O     1 
ATOM   1244  N N     . GLY A 1 1772 ? 232.378 181.623 184.966 1.00 136.10 ? 1772 GLY A N     1 
ATOM   1245  C CA    . GLY A 1 1772 ? 231.389 181.105 185.891 1.00 136.10 ? 1772 GLY A CA    1 
ATOM   1246  C C     . GLY A 1 1772 ? 230.438 182.168 186.401 1.00 136.10 ? 1772 GLY A C     1 
ATOM   1247  O O     . GLY A 1 1772 ? 229.857 182.916 185.611 1.00 136.10 ? 1772 GLY A O     1 
ATOM   1248  N N     . GLY A 1 1773 ? 230.261 182.240 187.718 1.00 135.74 ? 1773 GLY A N     1 
ATOM   1249  C CA    . GLY A 1 1773 ? 229.422 183.262 188.306 1.00 135.74 ? 1773 GLY A CA    1 
ATOM   1250  C C     . GLY A 1 1773 ? 230.143 184.500 188.781 1.00 135.74 ? 1773 GLY A C     1 
ATOM   1251  O O     . GLY A 1 1773 ? 229.509 185.400 189.339 1.00 135.74 ? 1773 GLY A O     1 
ATOM   1252  N N     . ASP A 1 1774 ? 231.454 184.579 188.567 1.00 148.98 ? 1774 ASP A N     1 
ATOM   1253  C CA    . ASP A 1 1774 ? 232.237 185.694 189.080 1.00 148.98 ? 1774 ASP A CA    1 
ATOM   1254  C C     . ASP A 1 1774 ? 231.903 186.975 188.328 1.00 148.98 ? 1774 ASP A C     1 
ATOM   1255  O O     . ASP A 1 1774 ? 232.002 187.028 187.099 1.00 148.98 ? 1774 ASP A O     1 
ATOM   1256  C CB    . ASP A 1 1774 ? 233.729 185.387 188.959 1.00 148.98 ? 1774 ASP A CB    1 
ATOM   1257  C CG    . ASP A 1 1774 ? 234.109 184.874 187.580 1.00 148.98 ? 1774 ASP A CG    1 
ATOM   1258  O OD1   . ASP A 1 1774 ? 233.508 183.877 187.128 1.00 148.98 ? 1774 ASP A OD1   1 
ATOM   1259  O OD2   . ASP A 1 1774 ? 235.009 185.467 186.948 1.00 148.98 ? 1774 ASP A OD2   1 
ATOM   1260  N N     . ALA A 1 1775 ? 231.519 188.009 189.073 1.00 147.71 ? 1775 ALA A N     1 
ATOM   1261  C CA    . ALA A 1 1775 ? 231.189 189.318 188.514 1.00 147.71 ? 1775 ALA A CA    1 
ATOM   1262  C C     . ALA A 1 1775 ? 230.112 189.193 187.436 1.00 147.71 ? 1775 ALA A C     1 
ATOM   1263  O O     . ALA A 1 1775 ? 230.335 189.462 186.255 1.00 147.71 ? 1775 ALA A O     1 
ATOM   1264  C CB    . ALA A 1 1775 ? 232.441 190.013 187.971 1.00 147.71 ? 1775 ALA A CB    1 
ATOM   1265  N N     . ALA A 1 1776 ? 228.929 188.765 187.869 1.00 124.85 ? 1776 ALA A N     1 
ATOM   1266  C CA    . ALA A 1 1776 ? 227.833 188.499 186.948 1.00 124.85 ? 1776 ALA A CA    1 
ATOM   1267  C C     . ALA A 1 1776 ? 227.041 189.774 186.693 1.00 124.85 ? 1776 ALA A C     1 
ATOM   1268  O O     . ALA A 1 1776 ? 226.426 190.303 187.629 1.00 124.85 ? 1776 ALA A O     1 
ATOM   1269  C CB    . ALA A 1 1776 ? 226.917 187.425 187.506 1.00 124.85 ? 1776 ALA A CB    1 
ATOM   1270  N N     . PRO A 1 1777 ? 227.018 190.293 185.463 1.00 115.42 ? 1777 PRO A N     1 
ATOM   1271  C CA    . PRO A 1 1777 ? 226.115 191.402 185.136 1.00 115.42 ? 1777 PRO A CA    1 
ATOM   1272  C C     . PRO A 1 1777 ? 224.692 190.961 184.845 1.00 115.42 ? 1777 PRO A C     1 
ATOM   1273  O O     . PRO A 1 1777 ? 223.873 191.795 184.443 1.00 115.42 ? 1777 PRO A O     1 
ATOM   1274  C CB    . PRO A 1 1777 ? 226.761 192.026 183.886 1.00 115.42 ? 1777 PRO A CB    1 
ATOM   1275  C CG    . PRO A 1 1777 ? 227.999 191.215 183.597 1.00 115.42 ? 1777 PRO A CG    1 
ATOM   1276  C CD    . PRO A 1 1777 ? 227.854 189.925 184.315 1.00 115.42 ? 1777 PRO A CD    1 
ATOM   1277  N N     . LEU A 1 1778 ? 224.382 189.675 185.017 1.00 110.43 ? 1778 LEU A N     1 
ATOM   1278  C CA    . LEU A 1 1778 ? 222.996 189.235 184.929 1.00 110.43 ? 1778 LEU A CA    1 
ATOM   1279  C C     . LEU A 1 1778 ? 222.150 189.916 185.992 1.00 110.43 ? 1778 LEU A C     1 
ATOM   1280  O O     . LEU A 1 1778 ? 220.999 190.290 185.739 1.00 110.43 ? 1778 LEU A O     1 
ATOM   1281  C CB    . LEU A 1 1778 ? 222.919 187.717 185.070 1.00 110.43 ? 1778 LEU A CB    1 
ATOM   1282  C CG    . LEU A 1 1778 ? 222.902 186.927 183.765 1.00 110.43 ? 1778 LEU A CG    1 
ATOM   1283  C CD1   . LEU A 1 1778 ? 222.959 185.438 184.043 1.00 110.43 ? 1778 LEU A CD1   1 
ATOM   1284  C CD2   . LEU A 1 1778 ? 221.663 187.275 182.968 1.00 110.43 ? 1778 LEU A CD2   1 
ATOM   1285  N N     . HIS A 1 1779 ? 222.709 190.093 187.190 1.00 112.67 ? 1779 HIS A N     1 
ATOM   1286  C CA    . HIS A 1 1779 ? 222.029 190.886 188.205 1.00 112.67 ? 1779 HIS A CA    1 
ATOM   1287  C C     . HIS A 1 1779 ? 221.842 192.319 187.731 1.00 112.67 ? 1779 HIS A C     1 
ATOM   1288  O O     . HIS A 1 1779 ? 220.817 192.949 188.017 1.00 112.67 ? 1779 HIS A O     1 
ATOM   1289  C CB    . HIS A 1 1779 ? 222.817 190.851 189.512 1.00 112.67 ? 1779 HIS A CB    1 
ATOM   1290  C CG    . HIS A 1 1779 ? 222.875 189.497 190.144 1.00 112.67 ? 1779 HIS A CG    1 
ATOM   1291  N ND1   . HIS A 1 1779 ? 223.852 188.575 189.838 1.00 112.67 ? 1779 HIS A ND1   1 
ATOM   1292  C CD2   . HIS A 1 1779 ? 222.074 188.906 191.062 1.00 112.67 ? 1779 HIS A CD2   1 
ATOM   1293  C CE1   . HIS A 1 1779 ? 223.654 187.476 190.543 1.00 112.67 ? 1779 HIS A CE1   1 
ATOM   1294  N NE2   . HIS A 1 1779 ? 222.581 187.651 191.293 1.00 112.67 ? 1779 HIS A NE2   1 
ATOM   1295  N N     . SER A 1 1780 ? 222.823 192.851 187.000 1.00 111.04 ? 1780 SER A N     1 
ATOM   1296  C CA    . SER A 1 1780 ? 222.676 194.186 186.434 1.00 111.04 ? 1780 SER A CA    1 
ATOM   1297  C C     . SER A 1 1780 ? 221.526 194.235 185.437 1.00 111.04 ? 1780 SER A C     1 
ATOM   1298  O O     . SER A 1 1780 ? 220.745 195.195 185.425 1.00 111.04 ? 1780 SER A O     1 
ATOM   1299  C CB    . SER A 1 1780 ? 223.984 194.621 185.775 1.00 111.04 ? 1780 SER A CB    1 
ATOM   1300  O OG    . SER A 1 1780 ? 223.984 194.297 184.396 1.00 111.04 ? 1780 SER A OG    1 
ATOM   1301  N N     . VAL A 1 1781 ? 221.400 193.206 184.596 1.00 103.52 ? 1781 VAL A N     1 
ATOM   1302  C CA    . VAL A 1 1781 ? 220.298 193.159 183.638 1.00 103.52 ? 1781 VAL A CA    1 
ATOM   1303  C C     . VAL A 1 1781 ? 218.964 193.078 184.369 1.00 103.52 ? 1781 VAL A C     1 
ATOM   1304  O O     . VAL A 1 1781 ? 217.985 193.733 183.988 1.00 103.52 ? 1781 VAL A O     1 
ATOM   1305  C CB    . VAL A 1 1781 ? 220.488 191.980 182.666 1.00 103.52 ? 1781 VAL A CB    1 
ATOM   1306  C CG1   . VAL A 1 1781 ? 219.151 191.519 182.117 1.00 103.52 ? 1781 VAL A CG1   1 
ATOM   1307  C CG2   . VAL A 1 1781 ? 221.420 192.376 181.537 1.00 103.52 ? 1781 VAL A CG2   1 
ATOM   1308  N N     . LEU A 1 1782 ? 218.905 192.274 185.430 1.00 104.14 ? 1782 LEU A N     1 
ATOM   1309  C CA    . LEU A 1 1782 ? 217.675 192.163 186.203 1.00 104.14 ? 1782 LEU A CA    1 
ATOM   1310  C C     . LEU A 1 1782 ? 217.315 193.502 186.836 1.00 104.14 ? 1782 LEU A C     1 
ATOM   1311  O O     . LEU A 1 1782 ? 216.145 193.898 186.841 1.00 104.14 ? 1782 LEU A O     1 
ATOM   1312  C CB    . LEU A 1 1782 ? 217.831 191.068 187.260 1.00 104.14 ? 1782 LEU A CB    1 
ATOM   1313  C CG    . LEU A 1 1782 ? 216.647 190.394 187.971 1.00 104.14 ? 1782 LEU A CG    1 
ATOM   1314  C CD1   . LEU A 1 1782 ? 217.179 189.465 189.049 1.00 104.14 ? 1782 LEU A CD1   1 
ATOM   1315  C CD2   . LEU A 1 1782 ? 215.636 191.349 188.579 1.00 104.14 ? 1782 LEU A CD2   1 
ATOM   1316  N N     . SER A 1 1783 ? 218.308 194.221 187.362 1.00 103.31 ? 1783 SER A N     1 
ATOM   1317  C CA    . SER A 1 1783 ? 218.033 195.525 187.958 1.00 103.31 ? 1783 SER A CA    1 
ATOM   1318  C C     . SER A 1 1783 ? 217.568 196.524 186.906 1.00 103.31 ? 1783 SER A C     1 
ATOM   1319  O O     . SER A 1 1783 ? 216.699 197.363 187.174 1.00 103.31 ? 1783 SER A O     1 
ATOM   1320  C CB    . SER A 1 1783 ? 219.273 196.046 188.679 1.00 103.31 ? 1783 SER A CB    1 
ATOM   1321  O OG    . SER A 1 1783 ? 220.447 195.699 187.975 1.00 103.31 ? 1783 SER A OG    1 
ATOM   1322  N N     . ASN A 1 1784 ? 218.148 196.462 185.707 1.00 102.04 ? 1784 ASN A N     1 
ATOM   1323  C CA    . ASN A 1 1784 ? 217.684 197.319 184.623 1.00 102.04 ? 1784 ASN A CA    1 
ATOM   1324  C C     . ASN A 1 1784 ? 216.234 197.019 184.271 1.00 102.04 ? 1784 ASN A C     1 
ATOM   1325  O O     . ASN A 1 1784 ? 215.428 197.934 184.061 1.00 102.04 ? 1784 ASN A O     1 
ATOM   1326  C CB    . ASN A 1 1784 ? 218.578 197.142 183.400 1.00 102.04 ? 1784 ASN A CB    1 
ATOM   1327  C CG    . ASN A 1 1784 ? 217.925 197.635 182.131 1.00 102.04 ? 1784 ASN A CG    1 
ATOM   1328  O OD1   . ASN A 1 1784 ? 217.839 198.837 181.891 1.00 102.04 ? 1784 ASN A OD1   1 
ATOM   1329  N ND2   . ASN A 1 1784 ? 217.457 196.705 181.309 1.00 102.04 ? 1784 ASN A ND2   1 
ATOM   1330  N N     . VAL A 1 1785 ? 215.882 195.737 184.208 1.00 97.75  ? 1785 VAL A N     1 
ATOM   1331  C CA    . VAL A 1 1785 ? 214.496 195.369 183.941 1.00 97.75  ? 1785 VAL A CA    1 
ATOM   1332  C C     . VAL A 1 1785 ? 213.593 195.866 185.061 1.00 97.75  ? 1785 VAL A C     1 
ATOM   1333  O O     . VAL A 1 1785 ? 212.467 196.310 184.819 1.00 97.75  ? 1785 VAL A O     1 
ATOM   1334  C CB    . VAL A 1 1785 ? 214.378 193.848 183.742 1.00 97.75  ? 1785 VAL A CB    1 
ATOM   1335  C CG1   . VAL A 1 1785 ? 212.924 193.432 183.693 1.00 97.75  ? 1785 VAL A CG1   1 
ATOM   1336  C CG2   . VAL A 1 1785 ? 215.092 193.431 182.472 1.00 97.75  ? 1785 VAL A CG2   1 
ATOM   1337  N N     . GLU A 1 1786 ? 214.077 195.815 186.302 1.00 97.34  ? 1786 GLU A N     1 
ATOM   1338  C CA    . GLU A 1 1786 ? 213.274 196.279 187.428 1.00 97.34  ? 1786 GLU A CA    1 
ATOM   1339  C C     . GLU A 1 1786 ? 213.025 197.780 187.358 1.00 97.34  ? 1786 GLU A C     1 
ATOM   1340  O O     . GLU A 1 1786 ? 211.912 198.244 187.632 1.00 97.34  ? 1786 GLU A O     1 
ATOM   1341  C CB    . GLU A 1 1786 ? 213.953 195.914 188.745 1.00 97.34  ? 1786 GLU A CB    1 
ATOM   1342  C CG    . GLU A 1 1786 ? 213.952 194.430 189.046 1.00 97.34  ? 1786 GLU A CG    1 
ATOM   1343  C CD    . GLU A 1 1786 ? 212.678 193.965 189.722 1.00 97.34  ? 1786 GLU A CD    1 
ATOM   1344  O OE1   . GLU A 1 1786 ? 211.743 194.781 189.864 1.00 97.34  ? 1786 GLU A OE1   1 
ATOM   1345  O OE2   . GLU A 1 1786 ? 212.611 192.780 190.112 1.00 97.34  ? 1786 GLU A OE2   1 
ATOM   1346  N N     . VAL A 1 1787 ? 214.048 198.563 187.012 1.00 97.68  ? 1787 VAL A N     1 
ATOM   1347  C CA    . VAL A 1 1787 ? 213.853 200.010 186.930 1.00 97.68  ? 1787 VAL A CA    1 
ATOM   1348  C C     . VAL A 1 1787 ? 212.947 200.353 185.752 1.00 97.68  ? 1787 VAL A C     1 
ATOM   1349  O O     . VAL A 1 1787 ? 212.126 201.278 185.824 1.00 97.68  ? 1787 VAL A O     1 
ATOM   1350  C CB    . VAL A 1 1787 ? 215.202 200.753 186.866 1.00 97.68  ? 1787 VAL A CB    1 
ATOM   1351  C CG1   . VAL A 1 1787 ? 216.053 200.414 188.081 1.00 97.68  ? 1787 VAL A CG1   1 
ATOM   1352  C CG2   . VAL A 1 1787 ? 215.950 200.461 185.585 1.00 97.68  ? 1787 VAL A CG2   1 
ATOM   1353  N N     . THR A 1 1788 ? 213.063 199.598 184.656 1.00 92.71  ? 1788 THR A N     1 
ATOM   1354  C CA    . THR A 1 1788 ? 212.128 199.780 183.552 1.00 92.71  ? 1788 THR A CA    1 
ATOM   1355  C C     . THR A 1 1788 ? 210.703 199.466 183.989 1.00 92.71  ? 1788 THR A C     1 
ATOM   1356  O O     . THR A 1 1788 ? 209.760 200.181 183.631 1.00 92.71  ? 1788 THR A O     1 
ATOM   1357  C CB    . THR A 1 1788 ? 212.537 198.901 182.372 1.00 92.71  ? 1788 THR A CB    1 
ATOM   1358  O OG1   . THR A 1 1788 ? 213.901 199.173 182.029 1.00 92.71  ? 1788 THR A OG1   1 
ATOM   1359  C CG2   . THR A 1 1788 ? 211.661 199.187 181.167 1.00 92.71  ? 1788 THR A CG2   1 
ATOM   1360  N N     . LEU A 1 1789 ? 210.532 198.402 184.775 1.00 95.80  ? 1789 LEU A N     1 
ATOM   1361  C CA    . LEU A 1 1789 ? 209.218 198.070 185.311 1.00 95.80  ? 1789 LEU A CA    1 
ATOM   1362  C C     . LEU A 1 1789 ? 208.683 199.194 186.181 1.00 95.80  ? 1789 LEU A C     1 
ATOM   1363  O O     . LEU A 1 1789 ? 207.496 199.525 186.119 1.00 95.80  ? 1789 LEU A O     1 
ATOM   1364  C CB    . LEU A 1 1789 ? 209.291 196.777 186.121 1.00 95.80  ? 1789 LEU A CB    1 
ATOM   1365  C CG    . LEU A 1 1789 ? 208.725 195.506 185.495 1.00 95.80  ? 1789 LEU A CG    1 
ATOM   1366  C CD1   . LEU A 1 1789 ? 207.225 195.634 185.310 1.00 95.80  ? 1789 LEU A CD1   1 
ATOM   1367  C CD2   . LEU A 1 1789 ? 209.412 195.216 184.182 1.00 95.80  ? 1789 LEU A CD2   1 
ATOM   1368  N N     . ASN A 1 1790 ? 209.542 199.774 187.018 1.00 93.82  ? 1790 ASN A N     1 
ATOM   1369  C CA    . ASN A 1 1790 ? 209.110 200.876 187.869 1.00 93.82  ? 1790 ASN A CA    1 
ATOM   1370  C C     . ASN A 1 1790 ? 208.652 202.059 187.031 1.00 93.82  ? 1790 ASN A C     1 
ATOM   1371  O O     . ASN A 1 1790 ? 207.613 202.669 187.316 1.00 93.82  ? 1790 ASN A O     1 
ATOM   1372  C CB    . ASN A 1 1790 ? 210.245 201.289 188.800 1.00 93.82  ? 1790 ASN A CB    1 
ATOM   1373  C CG    . ASN A 1 1790 ? 210.560 200.232 189.827 1.00 93.82  ? 1790 ASN A CG    1 
ATOM   1374  O OD1   . ASN A 1 1790 ? 209.990 199.143 189.802 1.00 93.82  ? 1790 ASN A OD1   1 
ATOM   1375  N ND2   . ASN A 1 1790 ? 211.472 200.544 190.739 1.00 93.82  ? 1790 ASN A ND2   1 
ATOM   1376  N N     . VAL A 1 1791 ? 209.407 202.385 185.982 1.00 96.80  ? 1791 VAL A N     1 
ATOM   1377  C CA    . VAL A 1 1791 ? 209.039 203.506 185.123 1.00 96.80  ? 1791 VAL A CA    1 
ATOM   1378  C C     . VAL A 1 1791 ? 207.696 203.243 184.454 1.00 96.80  ? 1791 VAL A C     1 
ATOM   1379  O O     . VAL A 1 1791 ? 206.816 204.111 184.424 1.00 96.80  ? 1791 VAL A O     1 
ATOM   1380  C CB    . VAL A 1 1791 ? 210.144 203.773 184.088 1.00 96.80  ? 1791 VAL A CB    1 
ATOM   1381  C CG1   . VAL A 1 1791 ? 209.617 204.647 182.965 1.00 96.80  ? 1791 VAL A CG1   1 
ATOM   1382  C CG2   . VAL A 1 1791 ? 211.340 204.422 184.757 1.00 96.80  ? 1791 VAL A CG2   1 
ATOM   1383  N N     . LEU A 1 1792 ? 207.516 202.037 183.913 1.00 93.71  ? 1792 LEU A N     1 
ATOM   1384  C CA    . LEU A 1 1792 ? 206.259 201.715 183.244 1.00 93.71  ? 1792 LEU A CA    1 
ATOM   1385  C C     . LEU A 1 1792 ? 205.084 201.724 184.215 1.00 93.71  ? 1792 LEU A C     1 
ATOM   1386  O O     . LEU A 1 1792 ? 204.001 202.218 183.880 1.00 93.71  ? 1792 LEU A O     1 
ATOM   1387  C CB    . LEU A 1 1792 ? 206.362 200.366 182.536 1.00 93.71  ? 1792 LEU A CB    1 
ATOM   1388  C CG    . LEU A 1 1792 ? 206.843 200.390 181.084 1.00 93.71  ? 1792 LEU A CG    1 
ATOM   1389  C CD1   . LEU A 1 1792 ? 206.020 201.382 180.296 1.00 93.71  ? 1792 LEU A CD1   1 
ATOM   1390  C CD2   . LEU A 1 1792 ? 208.310 200.728 180.973 1.00 93.71  ? 1792 LEU A CD2   1 
ATOM   1391  N N     . ALA A 1 1793 ? 205.274 201.181 185.418 1.00 94.76  ? 1793 ALA A N     1 
ATOM   1392  C CA    . ALA A 1 1793 ? 204.197 201.169 186.402 1.00 94.76  ? 1793 ALA A CA    1 
ATOM   1393  C C     . ALA A 1 1793 ? 203.819 202.582 186.817 1.00 94.76  ? 1793 ALA A C     1 
ATOM   1394  O O     . ALA A 1 1793 ? 202.634 202.890 186.995 1.00 94.76  ? 1793 ALA A O     1 
ATOM   1395  C CB    . ALA A 1 1793 ? 204.606 200.343 187.620 1.00 94.76  ? 1793 ALA A CB    1 
ATOM   1396  N N     . ASP A 1 1794 ? 204.812 203.454 186.988 1.00 98.66  ? 1794 ASP A N     1 
ATOM   1397  C CA    . ASP A 1 1794 ? 204.509 204.847 187.289 1.00 98.66  ? 1794 ASP A CA    1 
ATOM   1398  C C     . ASP A 1 1794 ? 203.750 205.500 186.143 1.00 98.66  ? 1794 ASP A C     1 
ATOM   1399  O O     . ASP A 1 1794 ? 202.761 206.208 186.366 1.00 98.66  ? 1794 ASP A O     1 
ATOM   1400  C CB    . ASP A 1 1794 ? 205.799 205.608 187.581 1.00 98.66  ? 1794 ASP A CB    1 
ATOM   1401  C CG    . ASP A 1 1794 ? 206.454 205.162 188.866 1.00 98.66  ? 1794 ASP A CG    1 
ATOM   1402  O OD1   . ASP A 1 1794 ? 205.882 204.286 189.548 1.00 98.66  ? 1794 ASP A OD1   1 
ATOM   1403  O OD2   . ASP A 1 1794 ? 207.540 205.683 189.195 1.00 98.66  ? 1794 ASP A OD2   1 
ATOM   1404  N N     . SER A 1 1795 ? 204.189 205.259 184.906 1.00 96.92  ? 1795 SER A N     1 
ATOM   1405  C CA    . SER A 1 1795 ? 203.580 205.933 183.765 1.00 96.92  ? 1795 SER A CA    1 
ATOM   1406  C C     . SER A 1 1795 ? 202.140 205.490 183.552 1.00 96.92  ? 1795 SER A C     1 
ATOM   1407  O O     . SER A 1 1795 ? 201.263 206.323 183.298 1.00 96.92  ? 1795 SER A O     1 
ATOM   1408  C CB    . SER A 1 1795 ? 204.401 205.679 182.505 1.00 96.92  ? 1795 SER A CB    1 
ATOM   1409  O OG    . SER A 1 1795 ? 203.835 206.361 181.402 1.00 96.92  ? 1795 SER A OG    1 
ATOM   1410  N N     . VAL A 1 1796 ? 201.873 204.187 183.651 1.00 93.11  ? 1796 VAL A N     1 
ATOM   1411  C CA    . VAL A 1 1796 ? 200.537 203.684 183.347 1.00 93.11  ? 1796 VAL A CA    1 
ATOM   1412  C C     . VAL A 1 1796 ? 199.522 204.192 184.361 1.00 93.11  ? 1796 VAL A C     1 
ATOM   1413  O O     . VAL A 1 1796 ? 198.324 204.282 184.064 1.00 93.11  ? 1796 VAL A O     1 
ATOM   1414  C CB    . VAL A 1 1796 ? 200.552 202.144 183.274 1.00 93.11  ? 1796 VAL A CB    1 
ATOM   1415  C CG1   . VAL A 1 1796 ? 200.885 201.546 184.627 1.00 93.11  ? 1796 VAL A CG1   1 
ATOM   1416  C CG2   . VAL A 1 1796 ? 199.225 201.615 182.754 1.00 93.11  ? 1796 VAL A CG2   1 
ATOM   1417  N N     . LEU A 1 1797 ? 199.975 204.546 185.564 1.00 91.28  ? 1797 LEU A N     1 
ATOM   1418  C CA    . LEU A 1 1797 ? 199.059 205.058 186.573 1.00 91.28  ? 1797 LEU A CA    1 
ATOM   1419  C C     . LEU A 1 1797 ? 198.468 206.408 186.193 1.00 91.28  ? 1797 LEU A C     1 
ATOM   1420  O O     . LEU A 1 1797 ? 197.362 206.731 186.637 1.00 91.28  ? 1797 LEU A O     1 
ATOM   1421  C CB    . LEU A 1 1797 ? 199.771 205.168 187.919 1.00 91.28  ? 1797 LEU A CB    1 
ATOM   1422  C CG    . LEU A 1 1797 ? 199.662 203.938 188.816 1.00 91.28  ? 1797 LEU A CG    1 
ATOM   1423  C CD1   . LEU A 1 1797 ? 200.251 204.220 190.185 1.00 91.28  ? 1797 LEU A CD1   1 
ATOM   1424  C CD2   . LEU A 1 1797 ? 198.213 203.514 188.932 1.00 91.28  ? 1797 LEU A CD2   1 
ATOM   1425  N N     . MET A 1 1798 ? 199.166 207.196 185.383 1.00 97.98  ? 1798 MET A N     1 
ATOM   1426  C CA    . MET A 1 1798 ? 198.723 208.539 185.047 1.00 97.98  ? 1798 MET A CA    1 
ATOM   1427  C C     . MET A 1 1798 ? 197.720 208.489 183.895 1.00 97.98  ? 1798 MET A C     1 
ATOM   1428  O O     . MET A 1 1798 ? 197.224 207.426 183.514 1.00 97.98  ? 1798 MET A O     1 
ATOM   1429  C CB    . MET A 1 1798 ? 199.923 209.422 184.716 1.00 97.98  ? 1798 MET A CB    1 
ATOM   1430  C CG    . MET A 1 1798 ? 201.126 209.182 185.605 1.00 97.98  ? 1798 MET A CG    1 
ATOM   1431  S SD    . MET A 1 1798 ? 202.633 209.896 184.926 1.00 97.98  ? 1798 MET A SD    1 
ATOM   1432  C CE    . MET A 1 1798 ? 202.133 211.603 184.733 1.00 97.98  ? 1798 MET A CE    1 
ATOM   1433  N N     . GLU A 1 1799 ? 197.409 209.653 183.333 1.00 106.57 ? 1799 GLU A N     1 
ATOM   1434  C CA    . GLU A 1 1799 ? 196.453 209.768 182.239 1.00 106.57 ? 1799 GLU A CA    1 
ATOM   1435  C C     . GLU A 1 1799 ? 197.204 209.719 180.914 1.00 106.57 ? 1799 GLU A C     1 
ATOM   1436  O O     . GLU A 1 1799 ? 198.018 210.602 180.624 1.00 106.57 ? 1799 GLU A O     1 
ATOM   1437  C CB    . GLU A 1 1799 ? 195.659 211.068 182.370 1.00 106.57 ? 1799 GLU A CB    1 
ATOM   1438  C CG    . GLU A 1 1799 ? 194.641 211.331 181.270 1.00 106.57 ? 1799 GLU A CG    1 
ATOM   1439  C CD    . GLU A 1 1799 ? 194.117 210.066 180.626 1.00 106.57 ? 1799 GLU A CD    1 
ATOM   1440  O OE1   . GLU A 1 1799 ? 194.430 209.834 179.441 1.00 106.57 ? 1799 GLU A OE1   1 
ATOM   1441  O OE2   . GLU A 1 1799 ? 193.395 209.304 181.302 1.00 106.57 ? 1799 GLU A OE2   1 
ATOM   1442  N N     . GLN A 1 1800 ? 196.926 208.696 180.111 1.00 98.74  ? 1800 GLN A N     1 
ATOM   1443  C CA    . GLN A 1 1800 ? 197.603 208.494 178.842 1.00 98.74  ? 1800 GLN A CA    1 
ATOM   1444  C C     . GLN A 1 1800 ? 196.591 208.291 177.725 1.00 98.74  ? 1800 GLN A C     1 
ATOM   1445  O O     . GLN A 1 1800 ? 195.477 207.819 177.966 1.00 98.74  ? 1800 GLN A O     1 
ATOM   1446  C CB    . GLN A 1 1800 ? 198.538 207.278 178.899 1.00 98.74  ? 1800 GLN A CB    1 
ATOM   1447  C CG    . GLN A 1 1800 ? 199.309 207.129 180.194 1.00 98.74  ? 1800 GLN A CG    1 
ATOM   1448  C CD    . GLN A 1 1800 ? 200.204 208.312 180.476 1.00 98.74  ? 1800 GLN A CD    1 
ATOM   1449  O OE1   . GLN A 1 1800 ? 200.073 208.972 181.504 1.00 98.74  ? 1800 GLN A OE1   1 
ATOM   1450  N NE2   . GLN A 1 1800 ? 201.122 208.588 179.561 1.00 98.74  ? 1800 GLN A NE2   1 
ATOM   1451  N N     . PRO A 1 1801 ? 196.953 208.638 176.492 1.00 93.07  ? 1801 PRO A N     1 
ATOM   1452  C CA    . PRO A 1 1801 ? 196.067 208.357 175.370 1.00 93.07  ? 1801 PRO A CA    1 
ATOM   1453  C C     . PRO A 1 1801 ? 195.891 206.862 175.195 1.00 93.07  ? 1801 PRO A C     1 
ATOM   1454  O O     . PRO A 1 1801 ? 196.774 206.068 175.566 1.00 93.07  ? 1801 PRO A O     1 
ATOM   1455  C CB    . PRO A 1 1801 ? 196.802 208.981 174.175 1.00 93.07  ? 1801 PRO A CB    1 
ATOM   1456  C CG    . PRO A 1 1801 ? 197.714 209.994 174.774 1.00 93.07  ? 1801 PRO A CG    1 
ATOM   1457  C CD    . PRO A 1 1801 ? 198.132 209.420 176.086 1.00 93.07  ? 1801 PRO A CD    1 
ATOM   1458  N N     . PRO A 1 1802 ? 194.754 206.430 174.642 1.00 89.72  ? 1802 PRO A N     1 
ATOM   1459  C CA    . PRO A 1 1802 ? 194.499 204.982 174.533 1.00 89.72  ? 1802 PRO A CA    1 
ATOM   1460  C C     . PRO A 1 1802 ? 195.560 204.223 173.755 1.00 89.72  ? 1802 PRO A C     1 
ATOM   1461  O O     . PRO A 1 1802 ? 195.902 203.095 174.130 1.00 89.72  ? 1802 PRO A O     1 
ATOM   1462  C CB    . PRO A 1 1802 ? 193.132 204.921 173.838 1.00 89.72  ? 1802 PRO A CB    1 
ATOM   1463  C CG    . PRO A 1 1802 ? 192.965 206.252 173.186 1.00 89.72  ? 1802 PRO A CG    1 
ATOM   1464  C CD    . PRO A 1 1802 ? 193.655 207.229 174.079 1.00 89.72  ? 1802 PRO A CD    1 
ATOM   1465  N N     . LEU A 1 1803 ? 196.095 204.802 172.680 1.00 89.41  ? 1803 LEU A N     1 
ATOM   1466  C CA    . LEU A 1 1803 ? 197.158 204.129 171.940 1.00 89.41  ? 1803 LEU A CA    1 
ATOM   1467  C C     . LEU A 1 1803 ? 198.406 203.981 172.798 1.00 89.41  ? 1803 LEU A C     1 
ATOM   1468  O O     . LEU A 1 1803 ? 199.016 202.905 172.856 1.00 89.41  ? 1803 LEU A O     1 
ATOM   1469  C CB    . LEU A 1 1803 ? 197.473 204.897 170.658 1.00 89.41  ? 1803 LEU A CB    1 
ATOM   1470  C CG    . LEU A 1 1803 ? 196.740 204.451 169.392 1.00 89.41  ? 1803 LEU A CG    1 
ATOM   1471  C CD1   . LEU A 1 1803 ? 197.200 203.064 168.985 1.00 89.41  ? 1803 LEU A CD1   1 
ATOM   1472  C CD2   . LEU A 1 1803 ? 195.233 204.484 169.580 1.00 89.41  ? 1803 LEU A CD2   1 
ATOM   1473  N N     . ARG A 1 1804 ? 198.794 205.055 173.485 1.00 92.11  ? 1804 ARG A N     1 
ATOM   1474  C CA    . ARG A 1 1804 ? 199.926 204.973 174.398 1.00 92.11  ? 1804 ARG A CA    1 
ATOM   1475  C C     . ARG A 1 1804 ? 199.632 204.030 175.554 1.00 92.11  ? 1804 ARG A C     1 
ATOM   1476  O O     . ARG A 1 1804 ? 200.536 203.349 176.044 1.00 92.11  ? 1804 ARG A O     1 
ATOM   1477  C CB    . ARG A 1 1804 ? 200.284 206.361 174.922 1.00 92.11  ? 1804 ARG A CB    1 
ATOM   1478  C CG    . ARG A 1 1804 ? 201.619 206.415 175.627 1.00 92.11  ? 1804 ARG A CG    1 
ATOM   1479  C CD    . ARG A 1 1804 ? 201.804 207.725 176.361 1.00 92.11  ? 1804 ARG A CD    1 
ATOM   1480  N NE    . ARG A 1 1804 ? 201.507 208.873 175.515 1.00 92.11  ? 1804 ARG A NE    1 
ATOM   1481  C CZ    . ARG A 1 1804 ? 201.528 210.132 175.930 1.00 92.11  ? 1804 ARG A CZ    1 
ATOM   1482  N NH1   . ARG A 1 1804 ? 201.848 210.443 177.175 1.00 92.11  ? 1804 ARG A NH1   1 
ATOM   1483  N NH2   . ARG A 1 1804 ? 201.219 211.102 175.076 1.00 92.11  ? 1804 ARG A NH2   1 
ATOM   1484  N N     . ARG A 1 1805 ? 198.375 203.971 175.997 1.00 87.62  ? 1805 ARG A N     1 
ATOM   1485  C CA    . ARG A 1 1805 ? 198.006 203.028 177.046 1.00 87.62  ? 1805 ARG A CA    1 
ATOM   1486  C C     . ARG A 1 1805 ? 198.208 201.588 176.593 1.00 87.62  ? 1805 ARG A C     1 
ATOM   1487  O O     . ARG A 1 1805 ? 198.754 200.766 177.336 1.00 87.62  ? 1805 ARG A O     1 
ATOM   1488  C CB    . ARG A 1 1805 ? 196.558 203.263 177.467 1.00 87.62  ? 1805 ARG A CB    1 
ATOM   1489  C CG    . ARG A 1 1805 ? 195.919 202.089 178.171 1.00 87.62  ? 1805 ARG A CG    1 
ATOM   1490  C CD    . ARG A 1 1805 ? 195.224 202.533 179.437 1.00 87.62  ? 1805 ARG A CD    1 
ATOM   1491  N NE    . ARG A 1 1805 ? 196.185 202.857 180.482 1.00 87.62  ? 1805 ARG A NE    1 
ATOM   1492  C CZ    . ARG A 1 1805 ? 196.279 204.040 181.071 1.00 87.62  ? 1805 ARG A CZ    1 
ATOM   1493  N NH1   . ARG A 1 1805 ? 195.479 205.040 180.743 1.00 87.62  ? 1805 ARG A NH1   1 
ATOM   1494  N NH2   . ARG A 1 1805 ? 197.198 204.223 182.015 1.00 87.62  ? 1805 ARG A NH2   1 
ATOM   1495  N N     . ARG A 1 1806 ? 197.777 201.264 175.373 1.00 88.86  ? 1806 ARG A N     1 
ATOM   1496  C CA    . ARG A 1 1806 ? 197.967 199.911 174.862 1.00 88.86  ? 1806 ARG A CA    1 
ATOM   1497  C C     . ARG A 1 1806 ? 199.445 199.596 174.677 1.00 88.86  ? 1806 ARG A C     1 
ATOM   1498  O O     . ARG A 1 1806 ? 199.891 198.473 174.952 1.00 88.86  ? 1806 ARG A O     1 
ATOM   1499  C CB    . ARG A 1 1806 ? 197.211 199.738 173.549 1.00 88.86  ? 1806 ARG A CB    1 
ATOM   1500  C CG    . ARG A 1 1806 ? 195.710 199.864 173.689 1.00 88.86  ? 1806 ARG A CG    1 
ATOM   1501  C CD    . ARG A 1 1806 ? 195.081 198.528 174.010 1.00 88.86  ? 1806 ARG A CD    1 
ATOM   1502  N NE    . ARG A 1 1806 ? 195.128 197.623 172.869 1.00 88.86  ? 1806 ARG A NE    1 
ATOM   1503  C CZ    . ARG A 1 1806 ? 194.274 197.653 171.855 1.00 88.86  ? 1806 ARG A CZ    1 
ATOM   1504  N NH1   . ARG A 1 1806 ? 193.286 198.531 171.808 1.00 88.86  ? 1806 ARG A NH1   1 
ATOM   1505  N NH2   . ARG A 1 1806 ? 194.416 196.779 170.863 1.00 88.86  ? 1806 ARG A NH2   1 
ATOM   1506  N N     . LYS A 1 1807 ? 200.220 200.570 174.197 1.00 91.56  ? 1807 LYS A N     1 
ATOM   1507  C CA    . LYS A 1 1807 ? 201.657 200.356 174.074 1.00 91.56  ? 1807 LYS A CA    1 
ATOM   1508  C C     . LYS A 1 1807 ? 202.283 200.082 175.433 1.00 91.56  ? 1807 LYS A C     1 
ATOM   1509  O O     . LYS A 1 1807 ? 203.110 199.173 175.573 1.00 91.56  ? 1807 LYS A O     1 
ATOM   1510  C CB    . LYS A 1 1807 ? 202.320 201.563 173.413 1.00 91.56  ? 1807 LYS A CB    1 
ATOM   1511  C CG    . LYS A 1 1807 ? 201.900 201.793 171.976 1.00 91.56  ? 1807 LYS A CG    1 
ATOM   1512  C CD    . LYS A 1 1807 ? 202.968 202.549 171.210 1.00 91.56  ? 1807 LYS A CD    1 
ATOM   1513  C CE    . LYS A 1 1807 ? 202.577 203.999 171.007 1.00 91.56  ? 1807 LYS A CE    1 
ATOM   1514  N NZ    . LYS A 1 1807 ? 203.288 204.605 169.847 1.00 91.56  ? 1807 LYS A NZ    1 
ATOM   1515  N N     . LEU A 1 1808 ? 201.886 200.848 176.451 1.00 85.16  ? 1808 LEU A N     1 
ATOM   1516  C CA    . LEU A 1 1808 ? 202.383 200.610 177.799 1.00 85.16  ? 1808 LEU A CA    1 
ATOM   1517  C C     . LEU A 1 1808 ? 202.009 199.219 178.278 1.00 85.16  ? 1808 LEU A C     1 
ATOM   1518  O O     . LEU A 1 1808 ? 202.829 198.524 178.883 1.00 85.16  ? 1808 LEU A O     1 
ATOM   1519  C CB    . LEU A 1 1808 ? 201.830 201.660 178.760 1.00 85.16  ? 1808 LEU A CB    1 
ATOM   1520  C CG    . LEU A 1 1808 ? 202.353 203.087 178.642 1.00 85.16  ? 1808 LEU A CG    1 
ATOM   1521  C CD1   . LEU A 1 1808 ? 202.291 203.780 179.990 1.00 85.16  ? 1808 LEU A CD1   1 
ATOM   1522  C CD2   . LEU A 1 1808 ? 203.767 203.071 178.123 1.00 85.16  ? 1808 LEU A CD2   1 
ATOM   1523  N N     . GLU A 1 1809 ? 200.769 198.805 178.022 1.00 85.10  ? 1809 GLU A N     1 
ATOM   1524  C CA    . GLU A 1 1809 ? 200.310 197.486 178.442 1.00 85.10  ? 1809 GLU A CA    1 
ATOM   1525  C C     . GLU A 1 1809 ? 201.165 196.384 177.831 1.00 85.10  ? 1809 GLU A C     1 
ATOM   1526  O O     . GLU A 1 1809 ? 201.662 195.501 178.545 1.00 85.10  ? 1809 GLU A O     1 
ATOM   1527  C CB    . GLU A 1 1809 ? 198.848 197.311 178.041 1.00 85.10  ? 1809 GLU A CB    1 
ATOM   1528  C CG    . GLU A 1 1809 ? 197.857 197.768 179.085 1.00 85.10  ? 1809 GLU A CG    1 
ATOM   1529  C CD    . GLU A 1 1809 ? 197.762 196.803 180.236 1.00 85.10  ? 1809 GLU A CD    1 
ATOM   1530  O OE1   . GLU A 1 1809 ? 197.472 197.243 181.368 1.00 85.10  ? 1809 GLU A OE1   1 
ATOM   1531  O OE2   . GLU A 1 1809 ? 197.969 195.594 180.004 1.00 85.10  ? 1809 GLU A OE2   1 
ATOM   1532  N N     . HIS A 1 1810 ? 201.351 196.428 176.512 1.00 84.70  ? 1810 HIS A N     1 
ATOM   1533  C CA    . HIS A 1 1810 ? 202.170 195.418 175.853 1.00 84.70  ? 1810 HIS A CA    1 
ATOM   1534  C C     . HIS A 1 1810 ? 203.591 195.435 176.394 1.00 84.70  ? 1810 HIS A C     1 
ATOM   1535  O O     . HIS A 1 1810 ? 204.184 194.378 176.653 1.00 84.70  ? 1810 HIS A O     1 
ATOM   1536  C CB    . HIS A 1 1810 ? 202.172 195.649 174.345 1.00 84.70  ? 1810 HIS A CB    1 
ATOM   1537  C CG    . HIS A 1 1810 ? 200.852 195.393 173.695 1.00 84.70  ? 1810 HIS A CG    1 
ATOM   1538  N ND1   . HIS A 1 1810 ? 199.716 195.089 174.413 1.00 84.70  ? 1810 HIS A ND1   1 
ATOM   1539  C CD2   . HIS A 1 1810 ? 200.483 195.402 172.393 1.00 84.70  ? 1810 HIS A CD2   1 
ATOM   1540  C CE1   . HIS A 1 1810 ? 198.705 194.916 173.581 1.00 84.70  ? 1810 HIS A CE1   1 
ATOM   1541  N NE2   . HIS A 1 1810 ? 199.144 195.101 172.349 1.00 84.70  ? 1810 HIS A NE2   1 
ATOM   1542  N N     . LEU A 1 1811 ? 204.148 196.632 176.581 1.00 83.78  ? 1811 LEU A N     1 
ATOM   1543  C CA    . LEU A 1 1811 ? 205.523 196.740 177.043 1.00 83.78  ? 1811 LEU A CA    1 
ATOM   1544  C C     . LEU A 1 1811 ? 205.684 196.136 178.429 1.00 83.78  ? 1811 LEU A C     1 
ATOM   1545  O O     . LEU A 1 1811 ? 206.645 195.405 178.687 1.00 83.78  ? 1811 LEU A O     1 
ATOM   1546  C CB    . LEU A 1 1811 ? 205.962 198.202 177.035 1.00 83.78  ? 1811 LEU A CB    1 
ATOM   1547  C CG    . LEU A 1 1811 ? 207.153 198.514 176.134 1.00 83.78  ? 1811 LEU A CG    1 
ATOM   1548  C CD1   . LEU A 1 1811 ? 207.645 199.927 176.373 1.00 83.78  ? 1811 LEU A CD1   1 
ATOM   1549  C CD2   . LEU A 1 1811 ? 208.261 197.514 176.377 1.00 83.78  ? 1811 LEU A CD2   1 
ATOM   1550  N N     . ILE A 1 1812 ? 204.751 196.424 179.340 1.00 78.99  ? 1812 ILE A N     1 
ATOM   1551  C CA    . ILE A 1 1812 ? 204.939 195.926 180.696 1.00 78.99  ? 1812 ILE A CA    1 
ATOM   1552  C C     . ILE A 1 1812 ? 204.694 194.428 180.736 1.00 78.99  ? 1812 ILE A C     1 
ATOM   1553  O O     . ILE A 1 1812 ? 205.353 193.712 181.494 1.00 78.99  ? 1812 ILE A O     1 
ATOM   1554  C CB    . ILE A 1 1812 ? 204.057 196.667 181.717 1.00 78.99  ? 1812 ILE A CB    1 
ATOM   1555  C CG1   . ILE A 1 1812 ? 204.012 195.895 183.031 1.00 78.99  ? 1812 ILE A CG1   1 
ATOM   1556  C CG2   . ILE A 1 1812 ? 202.642 196.741 181.240 1.00 78.99  ? 1812 ILE A CG2   1 
ATOM   1557  C CD1   . ILE A 1 1812 ? 203.247 196.594 184.114 1.00 78.99  ? 1812 ILE A CD1   1 
ATOM   1558  N N     . THR A 1 1813 ? 203.775 193.914 179.914 1.00 78.08  ? 1813 THR A N     1 
ATOM   1559  C CA    . THR A 1 1813 ? 203.606 192.465 179.843 1.00 78.08  ? 1813 THR A CA    1 
ATOM   1560  C C     . THR A 1 1813 ? 204.899 191.788 179.403 1.00 78.08  ? 1813 THR A C     1 
ATOM   1561  O O     . THR A 1 1813 ? 205.383 190.847 180.052 1.00 78.08  ? 1813 THR A O     1 
ATOM   1562  C CB    . THR A 1 1813 ? 202.470 192.114 178.885 1.00 78.08  ? 1813 THR A CB    1 
ATOM   1563  O OG1   . THR A 1 1813 ? 201.215 192.466 179.479 1.00 78.08  ? 1813 THR A OG1   1 
ATOM   1564  C CG2   . THR A 1 1813 ? 202.481 190.631 178.574 1.00 78.08  ? 1813 THR A CG2   1 
ATOM   1565  N N     . GLU A 1 1814 ? 205.485 192.271 178.307 1.00 83.34  ? 1814 GLU A N     1 
ATOM   1566  C CA    . GLU A 1 1814 ? 206.710 191.658 177.810 1.00 83.34  ? 1814 GLU A CA    1 
ATOM   1567  C C     . GLU A 1 1814 ? 207.844 191.801 178.815 1.00 83.34  ? 1814 GLU A C     1 
ATOM   1568  O O     . GLU A 1 1814 ? 208.626 190.866 179.019 1.00 83.34  ? 1814 GLU A O     1 
ATOM   1569  C CB    . GLU A 1 1814 ? 207.097 192.275 176.472 1.00 83.34  ? 1814 GLU A CB    1 
ATOM   1570  C CG    . GLU A 1 1814 ? 208.079 191.441 175.681 1.00 83.34  ? 1814 GLU A CG    1 
ATOM   1571  C CD    . GLU A 1 1814 ? 207.976 189.963 175.993 1.00 83.34  ? 1814 GLU A CD    1 
ATOM   1572  O OE1   . GLU A 1 1814 ? 206.971 189.337 175.598 1.00 83.34  ? 1814 GLU A OE1   1 
ATOM   1573  O OE2   . GLU A 1 1814 ? 208.907 189.425 176.626 1.00 83.34  ? 1814 GLU A OE2   1 
ATOM   1574  N N     . LEU A 1 1815 ? 207.947 192.962 179.459 1.00 81.36  ? 1815 LEU A N     1 
ATOM   1575  C CA    . LEU A 1 1815 ? 209.021 193.176 180.417 1.00 81.36  ? 1815 LEU A CA    1 
ATOM   1576  C C     . LEU A 1 1815 ? 208.839 192.327 181.668 1.00 81.36  ? 1815 LEU A C     1 
ATOM   1577  O O     . LEU A 1 1815 ? 209.826 191.879 182.257 1.00 81.36  ? 1815 LEU A O     1 
ATOM   1578  C CB    . LEU A 1 1815 ? 209.108 194.656 180.772 1.00 81.36  ? 1815 LEU A CB    1 
ATOM   1579  C CG    . LEU A 1 1815 ? 210.247 195.401 180.082 1.00 81.36  ? 1815 LEU A CG    1 
ATOM   1580  C CD1   . LEU A 1 1815 ? 211.586 194.890 180.571 1.00 81.36  ? 1815 LEU A CD1   1 
ATOM   1581  C CD2   . LEU A 1 1815 ? 210.135 195.238 178.582 1.00 81.36  ? 1815 LEU A CD2   1 
ATOM   1582  N N     . VAL A 1 1816 ? 207.597 192.087 182.086 1.00 78.00  ? 1816 VAL A N     1 
ATOM   1583  C CA    . VAL A 1 1816 ? 207.356 191.180 183.200 1.00 78.00  ? 1816 VAL A CA    1 
ATOM   1584  C C     . VAL A 1 1816 ? 207.788 189.773 182.830 1.00 78.00  ? 1816 VAL A C     1 
ATOM   1585  O O     . VAL A 1 1816 ? 208.396 189.063 183.640 1.00 78.00  ? 1816 VAL A O     1 
ATOM   1586  C CB    . VAL A 1 1816 ? 205.876 191.227 183.621 1.00 78.00  ? 1816 VAL A CB    1 
ATOM   1587  C CG1   . VAL A 1 1816 ? 205.480 189.940 184.320 1.00 78.00  ? 1816 VAL A CG1   1 
ATOM   1588  C CG2   . VAL A 1 1816 ? 205.623 192.415 184.525 1.00 78.00  ? 1816 VAL A CG2   1 
ATOM   1589  N N     . HIS A 1 1817 ? 207.480 189.343 181.606 1.00 77.42  ? 1817 HIS A N     1 
ATOM   1590  C CA    . HIS A 1 1817 ? 207.945 188.027 181.178 1.00 77.42  ? 1817 HIS A CA    1 
ATOM   1591  C C     . HIS A 1 1817 ? 209.466 187.960 181.186 1.00 77.42  ? 1817 HIS A C     1 
ATOM   1592  O O     . HIS A 1 1817 ? 210.051 186.960 181.620 1.00 77.42  ? 1817 HIS A O     1 
ATOM   1593  C CB    . HIS A 1 1817 ? 207.410 187.689 179.791 1.00 77.42  ? 1817 HIS A CB    1 
ATOM   1594  C CG    . HIS A 1 1817 ? 208.157 186.582 179.117 1.00 77.42  ? 1817 HIS A CG    1 
ATOM   1595  N ND1   . HIS A 1 1817 ? 208.675 186.697 177.846 1.00 77.42  ? 1817 HIS A ND1   1 
ATOM   1596  C CD2   . HIS A 1 1817 ? 208.477 185.337 179.542 1.00 77.42  ? 1817 HIS A CD2   1 
ATOM   1597  C CE1   . HIS A 1 1817 ? 209.279 185.570 177.515 1.00 77.42  ? 1817 HIS A CE1   1 
ATOM   1598  N NE2   . HIS A 1 1817 ? 209.173 184.728 178.526 1.00 77.42  ? 1817 HIS A NE2   1 
ATOM   1599  N N     . GLN A 1 1818 ? 210.123 189.018 180.709 1.00 82.15  ? 1818 GLN A N     1 
ATOM   1600  C CA    . GLN A 1 1818 ? 211.582 189.049 180.726 1.00 82.15  ? 1818 GLN A CA    1 
ATOM   1601  C C     . GLN A 1 1818 ? 212.115 188.963 182.147 1.00 82.15  ? 1818 GLN A C     1 
ATOM   1602  O O     . GLN A 1 1818 ? 213.087 188.249 182.413 1.00 82.15  ? 1818 GLN A O     1 
ATOM   1603  C CB    . GLN A 1 1818 ? 212.089 190.322 180.057 1.00 82.15  ? 1818 GLN A CB    1 
ATOM   1604  C CG    . GLN A 1 1818 ? 211.952 190.344 178.557 1.00 82.15  ? 1818 GLN A CG    1 
ATOM   1605  C CD    . GLN A 1 1818 ? 211.689 191.739 178.040 1.00 82.15  ? 1818 GLN A CD    1 
ATOM   1606  O OE1   . GLN A 1 1818 ? 210.622 192.021 177.499 1.00 82.15  ? 1818 GLN A OE1   1 
ATOM   1607  N NE2   . GLN A 1 1818 ? 212.656 192.628 178.223 1.00 82.15  ? 1818 GLN A NE2   1 
ATOM   1608  N N     . ARG A 1 1819 ? 211.499 189.701 183.069 1.00 88.05  ? 1819 ARG A N     1 
ATOM   1609  C CA    . ARG A 1 1819 ? 211.943 189.673 184.456 1.00 88.05  ? 1819 ARG A CA    1 
ATOM   1610  C C     . ARG A 1 1819 ? 211.791 188.282 185.047 1.00 88.05  ? 1819 ARG A C     1 
ATOM   1611  O O     . ARG A 1 1819 ? 212.694 187.787 185.729 1.00 88.05  ? 1819 ARG A O     1 
ATOM   1612  C CB    . ARG A 1 1819 ? 211.154 190.687 185.280 1.00 88.05  ? 1819 ARG A CB    1 
ATOM   1613  C CG    . ARG A 1 1819 ? 211.787 191.016 186.619 1.00 88.05  ? 1819 ARG A CG    1 
ATOM   1614  C CD    . ARG A 1 1819 ? 210.757 191.522 187.611 1.00 88.05  ? 1819 ARG A CD    1 
ATOM   1615  N NE    . ARG A 1 1819 ? 209.609 190.630 187.698 1.00 88.05  ? 1819 ARG A NE    1 
ATOM   1616  C CZ    . ARG A 1 1819 ? 208.477 190.928 188.318 1.00 88.05  ? 1819 ARG A CZ    1 
ATOM   1617  N NH1   . ARG A 1 1819 ? 208.307 192.090 188.925 1.00 88.05  ? 1819 ARG A NH1   1 
ATOM   1618  N NH2   . ARG A 1 1819 ? 207.492 190.035 188.333 1.00 88.05  ? 1819 ARG A NH2   1 
ATOM   1619  N N     . ASP A 1 1820 ? 210.653 187.636 184.794 1.00 95.30  ? 1820 ASP A N     1 
ATOM   1620  C CA    . ASP A 1 1820 ? 210.431 186.302 185.341 1.00 95.30  ? 1820 ASP A CA    1 
ATOM   1621  C C     . ASP A 1 1820 ? 211.415 185.300 184.759 1.00 95.30  ? 1820 ASP A C     1 
ATOM   1622  O O     . ASP A 1 1820 ? 211.896 184.409 185.468 1.00 95.30  ? 1820 ASP A O     1 
ATOM   1623  C CB    . ASP A 1 1820 ? 208.992 185.859 185.086 1.00 95.30  ? 1820 ASP A CB    1 
ATOM   1624  C CG    . ASP A 1 1820 ? 208.021 186.426 186.103 1.00 95.30  ? 1820 ASP A CG    1 
ATOM   1625  O OD1   . ASP A 1 1820 ? 207.947 185.881 187.224 1.00 95.30  ? 1820 ASP A OD1   1 
ATOM   1626  O OD2   . ASP A 1 1820 ? 207.332 187.417 185.784 1.00 95.30  ? 1820 ASP A OD2   1 
ATOM   1627  N N     . VAL A 1 1821 ? 211.726 185.424 183.469 1.00 88.78  ? 1821 VAL A N     1 
ATOM   1628  C CA    . VAL A 1 1821 ? 212.686 184.512 182.856 1.00 88.78  ? 1821 VAL A CA    1 
ATOM   1629  C C     . VAL A 1 1821 ? 214.075 184.727 183.440 1.00 88.78  ? 1821 VAL A C     1 
ATOM   1630  O O     . VAL A 1 1821 ? 214.752 183.774 183.844 1.00 88.78  ? 1821 VAL A O     1 
ATOM   1631  C CB    . VAL A 1 1821 ? 212.686 184.684 181.329 1.00 88.78  ? 1821 VAL A CB    1 
ATOM   1632  C CG1   . VAL A 1 1821 ? 213.982 184.161 180.737 1.00 88.78  ? 1821 VAL A CG1   1 
ATOM   1633  C CG2   . VAL A 1 1821 ? 211.499 183.966 180.727 1.00 88.78  ? 1821 VAL A CG2   1 
ATOM   1634  N N     . THR A 1 1822 ? 214.517 185.983 183.507 1.00 91.25  ? 1822 THR A N     1 
ATOM   1635  C CA    . THR A 1 1822 ? 215.881 186.264 183.938 1.00 91.25  ? 1822 THR A CA    1 
ATOM   1636  C C     . THR A 1 1822 ? 216.078 185.948 185.413 1.00 91.25  ? 1822 THR A C     1 
ATOM   1637  O O     . THR A 1 1822 ? 217.135 185.445 185.809 1.00 91.25  ? 1822 THR A O     1 
ATOM   1638  C CB    . THR A 1 1822 ? 216.227 187.723 183.656 1.00 91.25  ? 1822 THR A CB    1 
ATOM   1639  O OG1   . THR A 1 1822 ? 215.820 188.060 182.325 1.00 91.25  ? 1822 THR A OG1   1 
ATOM   1640  C CG2   . THR A 1 1822 ? 217.717 187.947 183.790 1.00 91.25  ? 1822 THR A CG2   1 
ATOM   1641  N N     . ARG A 1 1823 ? 215.071 186.233 186.240 1.00 98.90  ? 1823 ARG A N     1 
ATOM   1642  C CA    . ARG A 1 1823 ? 215.231 186.083 187.681 1.00 98.90  ? 1823 ARG A CA    1 
ATOM   1643  C C     . ARG A 1 1823 ? 215.471 184.632 188.068 1.00 98.90  ? 1823 ARG A C     1 
ATOM   1644  O O     . ARG A 1 1823 ? 216.321 184.341 188.917 1.00 98.90  ? 1823 ARG A O     1 
ATOM   1645  C CB    . ARG A 1 1823 ? 214.003 186.631 188.403 1.00 98.90  ? 1823 ARG A CB    1 
ATOM   1646  C CG    . ARG A 1 1823 ? 213.751 185.996 189.755 1.00 98.90  ? 1823 ARG A CG    1 
ATOM   1647  C CD    . ARG A 1 1823 ? 212.418 186.430 190.328 1.00 98.90  ? 1823 ARG A CD    1 
ATOM   1648  N NE    . ARG A 1 1823 ? 212.422 187.846 190.673 1.00 98.90  ? 1823 ARG A NE    1 
ATOM   1649  C CZ    . ARG A 1 1823 ? 211.849 188.792 189.942 1.00 98.90  ? 1823 ARG A CZ    1 
ATOM   1650  N NH1   . ARG A 1 1823 ? 211.204 188.503 188.825 1.00 98.90  ? 1823 ARG A NH1   1 
ATOM   1651  N NH2   . ARG A 1 1823 ? 211.928 190.057 190.341 1.00 98.90  ? 1823 ARG A NH2   1 
ATOM   1652  N N     . SER A 1 1824 ? 214.740 183.705 187.456 1.00 101.59 ? 1824 SER A N     1 
ATOM   1653  C CA    . SER A 1 1824 ? 214.826 182.300 187.824 1.00 101.59 ? 1824 SER A CA    1 
ATOM   1654  C C     . SER A 1 1824 ? 215.426 181.431 186.732 1.00 101.59 ? 1824 SER A C     1 
ATOM   1655  O O     . SER A 1 1824 ? 216.439 180.764 186.960 1.00 101.59 ? 1824 SER A O     1 
ATOM   1656  C CB    . SER A 1 1824 ? 213.433 181.774 188.197 1.00 101.59 ? 1824 SER A CB    1 
ATOM   1657  O OG    . SER A 1 1824 ? 212.526 181.930 187.122 1.00 101.59 ? 1824 SER A OG    1 
ATOM   1658  N N     . LEU A 1 1825 ? 214.836 181.438 185.536 1.00 103.35 ? 1825 LEU A N     1 
ATOM   1659  C CA    . LEU A 1 1825 ? 215.241 180.491 184.504 1.00 103.35 ? 1825 LEU A CA    1 
ATOM   1660  C C     . LEU A 1 1825 ? 216.656 180.739 184.002 1.00 103.35 ? 1825 LEU A C     1 
ATOM   1661  O O     . LEU A 1 1825 ? 217.217 179.872 183.325 1.00 103.35 ? 1825 LEU A O     1 
ATOM   1662  C CB    . LEU A 1 1825 ? 214.257 180.534 183.335 1.00 103.35 ? 1825 LEU A CB    1 
ATOM   1663  C CG    . LEU A 1 1825 ? 213.051 179.598 183.444 1.00 103.35 ? 1825 LEU A CG    1 
ATOM   1664  C CD1   . LEU A 1 1825 ? 212.331 179.491 182.112 1.00 103.35 ? 1825 LEU A CD1   1 
ATOM   1665  C CD2   . LEU A 1 1825 ? 213.476 178.222 183.937 1.00 103.35 ? 1825 LEU A CD2   1 
ATOM   1666  N N     . ILE A 1 1826 ? 217.244 181.890 184.308 1.00 100.68 ? 1826 ILE A N     1 
ATOM   1667  C CA    . ILE A 1 1826 ? 218.615 182.168 183.912 1.00 100.68 ? 1826 ILE A CA    1 
ATOM   1668  C C     . ILE A 1 1826 ? 219.560 182.276 185.098 1.00 100.68 ? 1826 ILE A C     1 
ATOM   1669  O O     . ILE A 1 1826 ? 220.755 181.980 184.942 1.00 100.68 ? 1826 ILE A O     1 
ATOM   1670  C CB    . ILE A 1 1826 ? 218.703 183.440 183.046 1.00 100.68 ? 1826 ILE A CB    1 
ATOM   1671  C CG1   . ILE A 1 1826 ? 217.483 183.550 182.135 1.00 100.68 ? 1826 ILE A CG1   1 
ATOM   1672  C CG2   . ILE A 1 1826 ? 219.973 183.427 182.214 1.00 100.68 ? 1826 ILE A CG2   1 
ATOM   1673  C CD1   . ILE A 1 1826 ? 217.411 182.466 181.088 1.00 100.68 ? 1826 ILE A CD1   1 
ATOM   1674  N N     . LYS A 1 1827 ? 219.080 182.668 186.271 1.00 97.15  ? 1827 LYS A N     1 
ATOM   1675  C CA    . LYS A 1 1827 ? 219.951 182.846 187.420 1.00 97.15  ? 1827 LYS A CA    1 
ATOM   1676  C C     . LYS A 1 1827 ? 220.059 181.594 188.276 1.00 97.15  ? 1827 LYS A C     1 
ATOM   1677  O O     . LYS A 1 1827 ? 220.501 181.681 189.424 1.00 97.15  ? 1827 LYS A O     1 
ATOM   1678  C CB    . LYS A 1 1827 ? 219.471 184.019 188.270 1.00 97.15  ? 1827 LYS A CB    1 
ATOM   1679  C CG    . LYS A 1 1827 ? 220.599 184.864 188.822 1.00 97.15  ? 1827 LYS A CG    1 
ATOM   1680  C CD    . LYS A 1 1827 ? 220.125 186.271 189.117 1.00 97.15  ? 1827 LYS A CD    1 
ATOM   1681  C CE    . LYS A 1 1827 ? 219.454 186.880 187.899 1.00 97.15  ? 1827 LYS A CE    1 
ATOM   1682  N NZ    . LYS A 1 1827 ? 220.276 186.714 186.673 1.00 97.15  ? 1827 LYS A NZ    1 
ATOM   1683  N N     . SER A 1 1828 ? 219.660 180.436 187.752 1.00 95.89  ? 1828 SER A N     1 
ATOM   1684  C CA    . SER A 1 1828 ? 219.841 179.170 188.459 1.00 95.89  ? 1828 SER A CA    1 
ATOM   1685  C C     . SER A 1 1828 ? 221.229 178.597 188.166 1.00 95.89  ? 1828 SER A C     1 
ATOM   1686  O O     . SER A 1 1828 ? 221.389 177.491 187.652 1.00 95.89  ? 1828 SER A O     1 
ATOM   1687  C CB    . SER A 1 1828 ? 218.740 178.190 188.081 1.00 95.89  ? 1828 SER A CB    1 
ATOM   1688  O OG    . SER A 1 1828 ? 217.507 178.573 188.661 1.00 95.89  ? 1828 SER A OG    1 
ATOM   1689  N N     . LYS A 1 1829 ? 222.242 179.389 188.516 1.00 101.44 ? 1829 LYS A N     1 
ATOM   1690  C CA    . LYS A 1 1829 ? 223.646 179.024 188.334 1.00 101.44 ? 1829 LYS A CA    1 
ATOM   1691  C C     . LYS A 1 1829 ? 223.933 178.639 186.886 1.00 101.44 ? 1829 LYS A C     1 
ATOM   1692  O O     . LYS A 1 1829 ? 224.575 177.628 186.596 1.00 101.44 ? 1829 LYS A O     1 
ATOM   1693  C CB    . LYS A 1 1829 ? 224.050 177.903 189.291 1.00 101.44 ? 1829 LYS A CB    1 
ATOM   1694  C CG    . LYS A 1 1829 ? 223.936 178.276 190.756 1.00 101.44 ? 1829 LYS A CG    1 
ATOM   1695  C CD    . LYS A 1 1829 ? 224.602 179.611 191.033 1.00 101.44 ? 1829 LYS A CD    1 
ATOM   1696  C CE    . LYS A 1 1829 ? 224.368 180.045 192.466 1.00 101.44 ? 1829 LYS A CE    1 
ATOM   1697  N NZ    . LYS A 1 1829 ? 222.923 180.002 192.816 1.00 101.44 ? 1829 LYS A NZ    1 
ATOM   1698  N N     . ILE A 1 1830 ? 223.446 179.463 185.967 1.00 99.40  ? 1830 ILE A N     1 
ATOM   1699  C CA    . ILE A 1 1830 ? 223.641 179.256 184.540 1.00 99.40  ? 1830 ILE A CA    1 
ATOM   1700  C C     . ILE A 1 1830 ? 224.622 180.307 184.050 1.00 99.40  ? 1830 ILE A C     1 
ATOM   1701  O O     . ILE A 1 1830 ? 224.386 181.510 184.212 1.00 99.40  ? 1830 ILE A O     1 
ATOM   1702  C CB    . ILE A 1 1830 ? 222.317 179.332 183.770 1.00 99.40  ? 1830 ILE A CB    1 
ATOM   1703  C CG1   . ILE A 1 1830 ? 221.442 178.128 184.118 1.00 99.40  ? 1830 ILE A CG1   1 
ATOM   1704  C CG2   . ILE A 1 1830 ? 222.579 179.399 182.279 1.00 99.40  ? 1830 ILE A CG2   1 
ATOM   1705  C CD1   . ILE A 1 1830 ? 220.029 178.495 184.510 1.00 99.40  ? 1830 ILE A CD1   1 
ATOM   1706  N N     . ASP A 1 1831 ? 225.722 179.855 183.453 1.00 116.65 ? 1831 ASP A N     1 
ATOM   1707  C CA    . ASP A 1 1831 ? 226.761 180.755 182.980 1.00 116.65 ? 1831 ASP A CA    1 
ATOM   1708  C C     . ASP A 1 1831 ? 227.174 180.520 181.537 1.00 116.65 ? 1831 ASP A C     1 
ATOM   1709  O O     . ASP A 1 1831 ? 227.976 181.300 181.015 1.00 116.65 ? 1831 ASP A O     1 
ATOM   1710  C CB    . ASP A 1 1831 ? 228.006 180.651 183.872 1.00 116.65 ? 1831 ASP A CB    1 
ATOM   1711  C CG    . ASP A 1 1831 ? 228.342 179.221 184.235 1.00 116.65 ? 1831 ASP A CG    1 
ATOM   1712  O OD1   . ASP A 1 1831 ? 228.572 178.412 183.313 1.00 116.65 ? 1831 ASP A OD1   1 
ATOM   1713  O OD2   . ASP A 1 1831 ? 228.375 178.905 185.443 1.00 116.65 ? 1831 ASP A OD2   1 
ATOM   1714  N N     . ASN A 1 1832 ? 226.665 179.485 180.879 1.00 106.57 ? 1832 ASN A N     1 
ATOM   1715  C CA    . ASN A 1 1832 ? 227.012 179.200 179.496 1.00 106.57 ? 1832 ASN A CA    1 
ATOM   1716  C C     . ASN A 1 1832 ? 225.915 179.717 178.578 1.00 106.57 ? 1832 ASN A C     1 
ATOM   1717  O O     . ASN A 1 1832 ? 224.739 179.385 178.758 1.00 106.57 ? 1832 ASN A O     1 
ATOM   1718  C CB    . ASN A 1 1832 ? 227.217 177.701 179.280 1.00 106.57 ? 1832 ASN A CB    1 
ATOM   1719  C CG    . ASN A 1 1832 ? 227.787 177.385 177.912 1.00 106.57 ? 1832 ASN A CG    1 
ATOM   1720  O OD1   . ASN A 1 1832 ? 228.124 178.286 177.143 1.00 106.57 ? 1832 ASN A OD1   1 
ATOM   1721  N ND2   . ASN A 1 1832 ? 227.894 176.099 177.599 1.00 106.57 ? 1832 ASN A ND2   1 
ATOM   1722  N N     . ALA A 1 1833 ? 226.305 180.526 177.592 1.00 104.68 ? 1833 ALA A N     1 
ATOM   1723  C CA    . ALA A 1 1833 ? 225.346 181.030 176.618 1.00 104.68 ? 1833 ALA A CA    1 
ATOM   1724  C C     . ALA A 1 1833 ? 224.798 179.928 175.726 1.00 104.68 ? 1833 ALA A C     1 
ATOM   1725  O O     . ALA A 1 1833 ? 223.786 180.140 175.050 1.00 104.68 ? 1833 ALA A O     1 
ATOM   1726  C CB    . ALA A 1 1833 ? 225.986 182.121 175.761 1.00 104.68 ? 1833 ALA A CB    1 
ATOM   1727  N N     . LYS A 1 1834 ? 225.447 178.768 175.696 1.00 103.27 ? 1834 LYS A N     1 
ATOM   1728  C CA    . LYS A 1 1834 ? 224.983 177.632 174.916 1.00 103.27 ? 1834 LYS A CA    1 
ATOM   1729  C C     . LYS A 1 1834 ? 224.232 176.609 175.754 1.00 103.27 ? 1834 LYS A C     1 
ATOM   1730  O O     . LYS A 1 1834 ? 223.803 175.584 175.216 1.00 103.27 ? 1834 LYS A O     1 
ATOM   1731  C CB    . LYS A 1 1834 ? 226.164 176.956 174.215 1.00 103.27 ? 1834 LYS A CB    1 
ATOM   1732  C CG    . LYS A 1 1834 ? 227.198 177.921 173.651 1.00 103.27 ? 1834 LYS A CG    1 
ATOM   1733  C CD    . LYS A 1 1834 ? 226.566 178.953 172.726 1.00 103.27 ? 1834 LYS A CD    1 
ATOM   1734  C CE    . LYS A 1 1834 ? 226.022 178.304 171.463 1.00 103.27 ? 1834 LYS A CE    1 
ATOM   1735  N NZ    . LYS A 1 1834 ? 225.261 179.269 170.624 1.00 103.27 ? 1834 LYS A NZ    1 
ATOM   1736  N N     . SER A 1 1835 ? 224.069 176.854 177.050 1.00 95.33  ? 1835 SER A N     1 
ATOM   1737  C CA    . SER A 1 1835 ? 223.300 175.948 177.890 1.00 95.33  ? 1835 SER A CA    1 
ATOM   1738  C C     . SER A 1 1835 ? 221.841 175.949 177.461 1.00 95.33  ? 1835 SER A C     1 
ATOM   1739  O O     . SER A 1 1835 ? 221.287 176.987 177.091 1.00 95.33  ? 1835 SER A O     1 
ATOM   1740  C CB    . SER A 1 1835 ? 223.414 176.354 179.356 1.00 95.33  ? 1835 SER A CB    1 
ATOM   1741  O OG    . SER A 1 1835 ? 222.800 177.610 179.575 1.00 95.33  ? 1835 SER A OG    1 
ATOM   1742  N N     . PHE A 1 1836 ? 221.212 174.773 177.517 1.00 83.92  ? 1836 PHE A N     1 
ATOM   1743  C CA    . PHE A 1 1836 ? 219.849 174.648 177.017 1.00 83.92  ? 1836 PHE A CA    1 
ATOM   1744  C C     . PHE A 1 1836 ? 218.859 175.486 177.807 1.00 83.92  ? 1836 PHE A C     1 
ATOM   1745  O O     . PHE A 1 1836 ? 217.817 175.865 177.262 1.00 83.92  ? 1836 PHE A O     1 
ATOM   1746  C CB    . PHE A 1 1836 ? 219.400 173.190 177.031 1.00 83.92  ? 1836 PHE A CB    1 
ATOM   1747  C CG    . PHE A 1 1836 ? 218.076 172.972 176.370 1.00 83.92  ? 1836 PHE A CG    1 
ATOM   1748  C CD1   . PHE A 1 1836 ? 217.963 173.009 174.996 1.00 83.92  ? 1836 PHE A CD1   1 
ATOM   1749  C CD2   . PHE A 1 1836 ? 216.941 172.757 177.122 1.00 83.92  ? 1836 PHE A CD2   1 
ATOM   1750  C CE1   . PHE A 1 1836 ? 216.748 172.817 174.386 1.00 83.92  ? 1836 PHE A CE1   1 
ATOM   1751  C CE2   . PHE A 1 1836 ? 215.723 172.569 176.515 1.00 83.92  ? 1836 PHE A CE2   1 
ATOM   1752  C CZ    . PHE A 1 1836 ? 215.627 172.598 175.147 1.00 83.92  ? 1836 PHE A CZ    1 
ATOM   1753  N N     . GLU A 1 1837 ? 219.157 175.786 179.071 1.00 89.21  ? 1837 GLU A N     1 
ATOM   1754  C CA    . GLU A 1 1837 ? 218.247 176.605 179.862 1.00 89.21  ? 1837 GLU A CA    1 
ATOM   1755  C C     . GLU A 1 1837 ? 218.054 177.976 179.236 1.00 89.21  ? 1837 GLU A C     1 
ATOM   1756  O O     . GLU A 1 1837 ? 216.994 178.590 179.396 1.00 89.21  ? 1837 GLU A O     1 
ATOM   1757  C CB    . GLU A 1 1837 ? 218.771 176.740 181.288 1.00 89.21  ? 1837 GLU A CB    1 
ATOM   1758  C CG    . GLU A 1 1837 ? 218.563 175.500 182.133 1.00 89.21  ? 1837 GLU A CG    1 
ATOM   1759  C CD    . GLU A 1 1837 ? 219.458 174.355 181.705 1.00 89.21  ? 1837 GLU A CD    1 
ATOM   1760  O OE1   . GLU A 1 1837 ? 220.694 174.533 181.700 1.00 89.21  ? 1837 GLU A OE1   1 
ATOM   1761  O OE2   . GLU A 1 1837 ? 218.926 173.278 181.368 1.00 89.21  ? 1837 GLU A OE2   1 
ATOM   1762  N N     . TRP A 1 1838 ? 219.062 178.470 178.521 1.00 86.76  ? 1838 TRP A N     1 
ATOM   1763  C CA    . TRP A 1 1838 ? 218.924 179.710 177.775 1.00 86.76  ? 1838 TRP A CA    1 
ATOM   1764  C C     . TRP A 1 1838 ? 218.483 179.480 176.340 1.00 86.76  ? 1838 TRP A C     1 
ATOM   1765  O O     . TRP A 1 1838 ? 217.759 180.310 175.782 1.00 86.76  ? 1838 TRP A O     1 
ATOM   1766  C CB    . TRP A 1 1838 ? 220.243 180.483 177.780 1.00 86.76  ? 1838 TRP A CB    1 
ATOM   1767  C CG    . TRP A 1 1838 ? 220.237 181.639 176.849 1.00 86.76  ? 1838 TRP A CG    1 
ATOM   1768  C CD1   . TRP A 1 1838 ? 221.058 181.834 175.783 1.00 86.76  ? 1838 TRP A CD1   1 
ATOM   1769  C CD2   . TRP A 1 1838 ? 219.354 182.761 176.887 1.00 86.76  ? 1838 TRP A CD2   1 
ATOM   1770  N NE1   . TRP A 1 1838 ? 220.746 183.012 175.156 1.00 86.76  ? 1838 TRP A NE1   1 
ATOM   1771  C CE2   . TRP A 1 1838 ? 219.702 183.601 175.816 1.00 86.76  ? 1838 TRP A CE2   1 
ATOM   1772  C CE3   . TRP A 1 1838 ? 218.305 183.140 177.726 1.00 86.76  ? 1838 TRP A CE3   1 
ATOM   1773  C CZ2   . TRP A 1 1838 ? 219.042 184.795 175.562 1.00 86.76  ? 1838 TRP A CZ2   1 
ATOM   1774  C CZ3   . TRP A 1 1838 ? 217.650 184.323 177.472 1.00 86.76  ? 1838 TRP A CZ3   1 
ATOM   1775  C CH2   . TRP A 1 1838 ? 218.020 185.137 176.398 1.00 86.76  ? 1838 TRP A CH2   1 
ATOM   1776  N N     . LEU A 1 1839 ? 218.903 178.373 175.728 1.00 82.04  ? 1839 LEU A N     1 
ATOM   1777  C CA    . LEU A 1 1839 ? 218.464 178.081 174.370 1.00 82.04  ? 1839 LEU A CA    1 
ATOM   1778  C C     . LEU A 1 1839 ? 216.967 177.829 174.311 1.00 82.04  ? 1839 LEU A C     1 
ATOM   1779  O O     . LEU A 1 1839 ? 216.331 178.124 173.295 1.00 82.04  ? 1839 LEU A O     1 
ATOM   1780  C CB    . LEU A 1 1839 ? 219.225 176.880 173.819 1.00 82.04  ? 1839 LEU A CB    1 
ATOM   1781  C CG    . LEU A 1 1839 ? 220.640 177.170 173.325 1.00 82.04  ? 1839 LEU A CG    1 
ATOM   1782  C CD1   . LEU A 1 1839 ? 221.220 175.955 172.627 1.00 82.04  ? 1839 LEU A CD1   1 
ATOM   1783  C CD2   . LEU A 1 1839 ? 220.631 178.368 172.394 1.00 82.04  ? 1839 LEU A CD2   1 
ATOM   1784  N N     . SER A 1 1840 ? 216.389 177.292 175.386 1.00 85.87  ? 1840 SER A N     1 
ATOM   1785  C CA    . SER A 1 1840 ? 214.961 177.003 175.387 1.00 85.87  ? 1840 SER A CA    1 
ATOM   1786  C C     . SER A 1 1840 ? 214.136 178.274 175.266 1.00 85.87  ? 1840 SER A C     1 
ATOM   1787  O O     . SER A 1 1840 ? 213.096 178.282 174.603 1.00 85.87  ? 1840 SER A O     1 
ATOM   1788  C CB    . SER A 1 1840 ? 214.577 176.243 176.653 1.00 85.87  ? 1840 SER A CB    1 
ATOM   1789  O OG    . SER A 1 1840 ? 213.176 176.285 176.853 1.00 85.87  ? 1840 SER A OG    1 
ATOM   1790  N N     . GLN A 1 1841 ? 214.572 179.351 175.908 1.00 84.17  ? 1841 GLN A N     1 
ATOM   1791  C CA    . GLN A 1 1841 ? 213.816 180.589 175.853 1.00 84.17  ? 1841 GLN A CA    1 
ATOM   1792  C C     . GLN A 1 1841 ? 213.918 181.221 174.471 1.00 84.17  ? 1841 GLN A C     1 
ATOM   1793  O O     . GLN A 1 1841 ? 214.846 180.959 173.703 1.00 84.17  ? 1841 GLN A O     1 
ATOM   1794  C CB    . GLN A 1 1841 ? 214.310 181.566 176.918 1.00 84.17  ? 1841 GLN A CB    1 
ATOM   1795  C CG    . GLN A 1 1841 ? 213.648 181.404 178.273 1.00 84.17  ? 1841 GLN A CG    1 
ATOM   1796  C CD    . GLN A 1 1841 ? 212.130 181.425 178.210 1.00 84.17  ? 1841 GLN A CD    1 
ATOM   1797  O OE1   . GLN A 1 1841 ? 211.534 181.919 177.252 1.00 84.17  ? 1841 GLN A OE1   1 
ATOM   1798  N NE2   . GLN A 1 1841 ? 211.495 180.878 179.237 1.00 84.17  ? 1841 GLN A NE2   1 
ATOM   1799  N N     . MET A 1 1842 ? 212.938 182.063 174.156 1.00 78.46  ? 1842 MET A N     1 
ATOM   1800  C CA    . MET A 1 1842 ? 212.917 182.767 172.880 1.00 78.46  ? 1842 MET A CA    1 
ATOM   1801  C C     . MET A 1 1842 ? 214.004 183.830 172.891 1.00 78.46  ? 1842 MET A C     1 
ATOM   1802  O O     . MET A 1 1842 ? 213.979 184.746 173.718 1.00 78.46  ? 1842 MET A O     1 
ATOM   1803  C CB    . MET A 1 1842 ? 211.547 183.385 172.626 1.00 78.46  ? 1842 MET A CB    1 
ATOM   1804  C CG    . MET A 1 1842 ? 211.392 183.959 171.230 1.00 78.46  ? 1842 MET A CG    1 
ATOM   1805  S SD    . MET A 1 1842 ? 210.644 182.821 170.054 1.00 78.46  ? 1842 MET A SD    1 
ATOM   1806  C CE    . MET A 1 1842 ? 208.911 183.149 170.336 1.00 78.46  ? 1842 MET A CE    1 
ATOM   1807  N N     . ARG A 1 1843 ? 214.955 183.712 171.973 1.00 86.64  ? 1843 ARG A N     1 
ATOM   1808  C CA    . ARG A 1 1843 ? 216.079 184.630 171.870 1.00 86.64  ? 1843 ARG A CA    1 
ATOM   1809  C C     . ARG A 1 1843 ? 215.945 185.443 170.591 1.00 86.64  ? 1843 ARG A C     1 
ATOM   1810  O O     . ARG A 1 1843 ? 215.496 184.925 169.565 1.00 86.64  ? 1843 ARG A O     1 
ATOM   1811  C CB    . ARG A 1 1843 ? 217.406 183.872 171.880 1.00 86.64  ? 1843 ARG A CB    1 
ATOM   1812  C CG    . ARG A 1 1843 ? 217.578 182.950 173.069 1.00 86.64  ? 1843 ARG A CG    1 
ATOM   1813  C CD    . ARG A 1 1843 ? 218.542 181.828 172.745 1.00 86.64  ? 1843 ARG A CD    1 
ATOM   1814  N NE    . ARG A 1 1843 ? 217.898 180.762 171.989 1.00 86.64  ? 1843 ARG A NE    1 
ATOM   1815  C CZ    . ARG A 1 1843 ? 218.242 180.408 170.759 1.00 86.64  ? 1843 ARG A CZ    1 
ATOM   1816  N NH1   . ARG A 1 1843 ? 219.216 181.022 170.109 1.00 86.64  ? 1843 ARG A NH1   1 
ATOM   1817  N NH2   . ARG A 1 1843 ? 217.591 179.412 170.164 1.00 86.64  ? 1843 ARG A NH2   1 
ATOM   1818  N N     . PHE A 1 1844 ? 216.325 186.713 170.658 1.00 85.54  ? 1844 PHE A N     1 
ATOM   1819  C CA    . PHE A 1 1844 ? 216.244 187.622 169.526 1.00 85.54  ? 1844 PHE A CA    1 
ATOM   1820  C C     . PHE A 1 1844 ? 217.649 188.014 169.100 1.00 85.54  ? 1844 PHE A C     1 
ATOM   1821  O O     . PHE A 1 1844 ? 218.480 188.361 169.943 1.00 85.54  ? 1844 PHE A O     1 
ATOM   1822  C CB    . PHE A 1 1844 ? 215.442 188.870 169.884 1.00 85.54  ? 1844 PHE A CB    1 
ATOM   1823  C CG    . PHE A 1 1844 ? 213.969 188.636 169.988 1.00 85.54  ? 1844 PHE A CG    1 
ATOM   1824  C CD1   . PHE A 1 1844 ? 213.461 187.723 170.889 1.00 85.54  ? 1844 PHE A CD1   1 
ATOM   1825  C CD2   . PHE A 1 1844 ? 213.086 189.355 169.206 1.00 85.54  ? 1844 PHE A CD2   1 
ATOM   1826  C CE1   . PHE A 1 1844 ? 212.107 187.516 170.994 1.00 85.54  ? 1844 PHE A CE1   1 
ATOM   1827  C CE2   . PHE A 1 1844 ? 211.726 189.154 169.310 1.00 85.54  ? 1844 PHE A CE2   1 
ATOM   1828  C CZ    . PHE A 1 1844 ? 211.238 188.232 170.205 1.00 85.54  ? 1844 PHE A CZ    1 
ATOM   1829  N N     . TYR A 1 1845 ? 217.910 187.961 167.797 1.00 89.23  ? 1845 TYR A N     1 
ATOM   1830  C CA    . TYR A 1 1845 ? 219.204 188.336 167.240 1.00 89.23  ? 1845 TYR A CA    1 
ATOM   1831  C C     . TYR A 1 1845 ? 218.976 189.284 166.075 1.00 89.23  ? 1845 TYR A C     1 
ATOM   1832  O O     . TYR A 1 1845 ? 218.319 188.918 165.096 1.00 89.23  ? 1845 TYR A O     1 
ATOM   1833  C CB    . TYR A 1 1845 ? 219.986 187.102 166.792 1.00 89.23  ? 1845 TYR A CB    1 
ATOM   1834  C CG    . TYR A 1 1845 ? 220.238 186.127 167.914 1.00 89.23  ? 1845 TYR A CG    1 
ATOM   1835  C CD1   . TYR A 1 1845 ? 220.783 186.554 169.114 1.00 89.23  ? 1845 TYR A CD1   1 
ATOM   1836  C CD2   . TYR A 1 1845 ? 219.923 184.785 167.780 1.00 89.23  ? 1845 TYR A CD2   1 
ATOM   1837  C CE1   . TYR A 1 1845 ? 221.012 185.675 170.145 1.00 89.23  ? 1845 TYR A CE1   1 
ATOM   1838  C CE2   . TYR A 1 1845 ? 220.150 183.898 168.808 1.00 89.23  ? 1845 TYR A CE2   1 
ATOM   1839  C CZ    . TYR A 1 1845 ? 220.694 184.348 169.987 1.00 89.23  ? 1845 TYR A CZ    1 
ATOM   1840  O OH    . TYR A 1 1845 ? 220.922 183.467 171.016 1.00 89.23  ? 1845 TYR A OH    1 
ATOM   1841  N N     . PHE A 1 1846 ? 219.517 190.493 166.180 1.00 100.50 ? 1846 PHE A N     1 
ATOM   1842  C CA    . PHE A 1 1846 ? 219.346 191.521 165.164 1.00 100.50 ? 1846 PHE A CA    1 
ATOM   1843  C C     . PHE A 1 1846 ? 220.691 191.849 164.534 1.00 100.50 ? 1846 PHE A C     1 
ATOM   1844  O O     . PHE A 1 1846 ? 221.659 192.136 165.245 1.00 100.50 ? 1846 PHE A O     1 
ATOM   1845  C CB    . PHE A 1 1846 ? 218.734 192.787 165.757 1.00 100.50 ? 1846 PHE A CB    1 
ATOM   1846  C CG    . PHE A 1 1846 ? 218.433 193.841 164.737 1.00 100.50 ? 1846 PHE A CG    1 
ATOM   1847  C CD1   . PHE A 1 1846 ? 217.702 193.533 163.605 1.00 100.50 ? 1846 PHE A CD1   1 
ATOM   1848  C CD2   . PHE A 1 1846 ? 218.891 195.134 164.901 1.00 100.50 ? 1846 PHE A CD2   1 
ATOM   1849  C CE1   . PHE A 1 1846 ? 217.422 194.496 162.663 1.00 100.50 ? 1846 PHE A CE1   1 
ATOM   1850  C CE2   . PHE A 1 1846 ? 218.616 196.102 163.960 1.00 100.50 ? 1846 PHE A CE2   1 
ATOM   1851  C CZ    . PHE A 1 1846 ? 217.880 195.782 162.840 1.00 100.50 ? 1846 PHE A CZ    1 
ATOM   1852  N N     . ASP A 1 1847 ? 220.744 191.808 163.204 1.00 116.46 ? 1847 ASP A N     1 
ATOM   1853  C CA    . ASP A 1 1847 ? 221.938 192.173 162.444 1.00 116.46 ? 1847 ASP A CA    1 
ATOM   1854  C C     . ASP A 1 1847 ? 221.500 193.137 161.350 1.00 116.46 ? 1847 ASP A C     1 
ATOM   1855  O O     . ASP A 1 1847 ? 221.123 192.717 160.247 1.00 116.46 ? 1847 ASP A O     1 
ATOM   1856  C CB    . ASP A 1 1847 ? 222.637 190.938 161.878 1.00 116.46 ? 1847 ASP A CB    1 
ATOM   1857  C CG    . ASP A 1 1847 ? 223.670 191.282 160.824 1.00 116.46 ? 1847 ASP A CG    1 
ATOM   1858  O OD1   . ASP A 1 1847 ? 224.359 192.310 160.979 1.00 116.46 ? 1847 ASP A OD1   1 
ATOM   1859  O OD2   . ASP A 1 1847 ? 223.804 190.515 159.849 1.00 116.46 ? 1847 ASP A OD2   1 
ATOM   1860  N N     . PRO A 1 1848 ? 221.518 194.443 161.627 1.00 111.84 ? 1848 PRO A N     1 
ATOM   1861  C CA    . PRO A 1 1848 ? 221.003 195.412 160.647 1.00 111.84 ? 1848 PRO A CA    1 
ATOM   1862  C C     . PRO A 1 1848 ? 221.802 195.478 159.358 1.00 111.84 ? 1848 PRO A C     1 
ATOM   1863  O O     . PRO A 1 1848 ? 221.276 195.974 158.355 1.00 111.84 ? 1848 PRO A O     1 
ATOM   1864  C CB    . PRO A 1 1848 ? 221.067 196.744 161.404 1.00 111.84 ? 1848 PRO A CB    1 
ATOM   1865  C CG    . PRO A 1 1848 ? 222.128 196.539 162.432 1.00 111.84 ? 1848 PRO A CG    1 
ATOM   1866  C CD    . PRO A 1 1848 ? 222.045 195.097 162.836 1.00 111.84 ? 1848 PRO A CD    1 
ATOM   1867  N N     . LYS A 1 1849 ? 223.048 195.001 159.346 1.00 115.02 ? 1849 LYS A N     1 
ATOM   1868  C CA    . LYS A 1 1849 ? 223.894 195.141 158.166 1.00 115.02 ? 1849 LYS A CA    1 
ATOM   1869  C C     . LYS A 1 1849 ? 223.402 194.329 156.976 1.00 115.02 ? 1849 LYS A C     1 
ATOM   1870  O O     . LYS A 1 1849 ? 223.878 194.559 155.859 1.00 115.02 ? 1849 LYS A O     1 
ATOM   1871  C CB    . LYS A 1 1849 ? 225.338 194.745 158.491 1.00 115.02 ? 1849 LYS A CB    1 
ATOM   1872  C CG    . LYS A 1 1849 ? 226.119 195.783 159.292 1.00 115.02 ? 1849 LYS A CG    1 
ATOM   1873  C CD    . LYS A 1 1849 ? 225.760 195.764 160.768 1.00 115.02 ? 1849 LYS A CD    1 
ATOM   1874  C CE    . LYS A 1 1849 ? 226.420 194.595 161.478 1.00 115.02 ? 1849 LYS A CE    1 
ATOM   1875  N NZ    . LYS A 1 1849 ? 226.017 194.512 162.909 1.00 115.02 ? 1849 LYS A NZ    1 
ATOM   1876  N N     . GLN A 1 1850 ? 222.475 193.398 157.176 1.00 117.18 ? 1850 GLN A N     1 
ATOM   1877  C CA    . GLN A 1 1850 ? 221.942 192.630 156.059 1.00 117.18 ? 1850 GLN A CA    1 
ATOM   1878  C C     . GLN A 1 1850 ? 221.141 193.535 155.135 1.00 117.18 ? 1850 GLN A C     1 
ATOM   1879  O O     . GLN A 1 1850 ? 220.236 194.249 155.578 1.00 117.18 ? 1850 GLN A O     1 
ATOM   1880  C CB    . GLN A 1 1850 ? 221.063 191.490 156.566 1.00 117.18 ? 1850 GLN A CB    1 
ATOM   1881  C CG    . GLN A 1 1850 ? 221.773 190.483 157.450 1.00 117.18 ? 1850 GLN A CG    1 
ATOM   1882  C CD    . GLN A 1 1850 ? 223.075 189.989 156.856 1.00 117.18 ? 1850 GLN A CD    1 
ATOM   1883  O OE1   . GLN A 1 1850 ? 224.126 190.607 157.026 1.00 117.18 ? 1850 GLN A OE1   1 
ATOM   1884  N NE2   . GLN A 1 1850 ? 223.012 188.867 156.150 1.00 117.18 ? 1850 GLN A NE2   1 
ATOM   1885  N N     . THR A 1 1851 ? 221.473 193.500 153.844 1.00 123.94 ? 1851 THR A N     1 
ATOM   1886  C CA    . THR A 1 1851 ? 220.726 194.289 152.872 1.00 123.94 ? 1851 THR A CA    1 
ATOM   1887  C C     . THR A 1 1851 ? 219.288 193.804 152.762 1.00 123.94 ? 1851 THR A C     1 
ATOM   1888  O O     . THR A 1 1851 ? 218.358 194.614 152.676 1.00 123.94 ? 1851 THR A O     1 
ATOM   1889  C CB    . THR A 1 1851 ? 221.411 194.233 151.509 1.00 123.94 ? 1851 THR A CB    1 
ATOM   1890  O OG1   . THR A 1 1851 ? 222.832 194.190 151.690 1.00 123.94 ? 1851 THR A OG1   1 
ATOM   1891  C CG2   . THR A 1 1851 ? 221.045 195.454 150.682 1.00 123.94 ? 1851 THR A CG2   1 
ATOM   1892  N N     . ASP A 1 1852 ? 219.087 192.490 152.765 1.00 120.54 ? 1852 ASP A N     1 
ATOM   1893  C CA    . ASP A 1 1852 ? 217.744 191.941 152.664 1.00 120.54 ? 1852 ASP A CA    1 
ATOM   1894  C C     . ASP A 1 1852 ? 216.939 192.271 153.913 1.00 120.54 ? 1852 ASP A C     1 
ATOM   1895  O O     . ASP A 1 1852 ? 217.434 192.168 155.038 1.00 120.54 ? 1852 ASP A O     1 
ATOM   1896  C CB    . ASP A 1 1852 ? 217.799 190.429 152.456 1.00 120.54 ? 1852 ASP A CB    1 
ATOM   1897  C CG    . ASP A 1 1852 ? 216.629 189.910 151.645 1.00 120.54 ? 1852 ASP A CG    1 
ATOM   1898  O OD1   . ASP A 1 1852 ? 215.570 190.571 151.638 1.00 120.54 ? 1852 ASP A OD1   1 
ATOM   1899  O OD2   . ASP A 1 1852 ? 216.767 188.841 151.016 1.00 120.54 ? 1852 ASP A OD2   1 
ATOM   1900  N N     . VAL A 1 1853 ? 215.687 192.675 153.705 1.00 110.44 ? 1853 VAL A N     1 
ATOM   1901  C CA    . VAL A 1 1853 ? 214.827 193.029 154.827 1.00 110.44 ? 1853 VAL A CA    1 
ATOM   1902  C C     . VAL A 1 1853 ? 214.484 191.795 155.649 1.00 110.44 ? 1853 VAL A C     1 
ATOM   1903  O O     . VAL A 1 1853 ? 214.437 191.848 156.883 1.00 110.44 ? 1853 VAL A O     1 
ATOM   1904  C CB    . VAL A 1 1853 ? 213.565 193.747 154.320 1.00 110.44 ? 1853 VAL A CB    1 
ATOM   1905  C CG1   . VAL A 1 1853 ? 212.932 192.967 153.180 1.00 110.44 ? 1853 VAL A CG1   1 
ATOM   1906  C CG2   . VAL A 1 1853 ? 212.570 193.937 155.449 1.00 110.44 ? 1853 VAL A CG2   1 
ATOM   1907  N N     . LEU A 1 1854 ? 214.254 190.661 154.986 1.00 110.88 ? 1854 LEU A N     1 
ATOM   1908  C CA    . LEU A 1 1854 ? 213.806 189.471 155.696 1.00 110.88 ? 1854 LEU A CA    1 
ATOM   1909  C C     . LEU A 1 1854 ? 214.896 188.861 156.568 1.00 110.88 ? 1854 LEU A C     1 
ATOM   1910  O O     . LEU A 1 1854 ? 214.586 188.044 157.440 1.00 110.88 ? 1854 LEU A O     1 
ATOM   1911  C CB    . LEU A 1 1854 ? 213.289 188.426 154.706 1.00 110.88 ? 1854 LEU A CB    1 
ATOM   1912  C CG    . LEU A 1 1854 ? 212.053 188.805 153.886 1.00 110.88 ? 1854 LEU A CG    1 
ATOM   1913  C CD1   . LEU A 1 1854 ? 212.444 189.423 152.554 1.00 110.88 ? 1854 LEU A CD1   1 
ATOM   1914  C CD2   . LEU A 1 1854 ? 211.160 187.594 153.674 1.00 110.88 ? 1854 LEU A CD2   1 
ATOM   1915  N N     . GLN A 1 1855 ? 216.155 189.233 156.362 1.00 110.55 ? 1855 GLN A N     1 
ATOM   1916  C CA    . GLN A 1 1855 ? 217.256 188.662 157.121 1.00 110.55 ? 1855 GLN A CA    1 
ATOM   1917  C C     . GLN A 1 1855 ? 217.788 189.602 158.195 1.00 110.55 ? 1855 GLN A C     1 
ATOM   1918  O O     . GLN A 1 1855 ? 218.778 189.272 158.855 1.00 110.55 ? 1855 GLN A O     1 
ATOM   1919  C CB    . GLN A 1 1855 ? 218.382 188.255 156.171 1.00 110.55 ? 1855 GLN A CB    1 
ATOM   1920  C CG    . GLN A 1 1855 ? 217.888 187.658 154.867 1.00 110.55 ? 1855 GLN A CG    1 
ATOM   1921  C CD    . GLN A 1 1855 ? 217.997 186.150 154.841 1.00 110.55 ? 1855 GLN A CD    1 
ATOM   1922  O OE1   . GLN A 1 1855 ? 218.524 185.539 155.770 1.00 110.55 ? 1855 GLN A OE1   1 
ATOM   1923  N NE2   . GLN A 1 1855 ? 217.500 185.539 153.773 1.00 110.55 ? 1855 GLN A NE2   1 
ATOM   1924  N N     . GLN A 1 1856 ? 217.158 190.762 158.387 1.00 105.27 ? 1856 GLN A N     1 
ATOM   1925  C CA    . GLN A 1 1856 ? 217.654 191.709 159.381 1.00 105.27 ? 1856 GLN A CA    1 
ATOM   1926  C C     . GLN A 1 1856 ? 217.472 191.177 160.796 1.00 105.27 ? 1856 GLN A C     1 
ATOM   1927  O O     . GLN A 1 1856 ? 218.403 191.228 161.608 1.00 105.27 ? 1856 GLN A O     1 
ATOM   1928  C CB    . GLN A 1 1856 ? 216.949 193.056 159.225 1.00 105.27 ? 1856 GLN A CB    1 
ATOM   1929  C CG    . GLN A 1 1856 ? 216.910 193.577 157.805 1.00 105.27 ? 1856 GLN A CG    1 
ATOM   1930  C CD    . GLN A 1 1856 ? 217.513 194.957 157.675 1.00 105.27 ? 1856 GLN A CD    1 
ATOM   1931  O OE1   . GLN A 1 1856 ? 218.477 195.294 158.363 1.00 105.27 ? 1856 GLN A OE1   1 
ATOM   1932  N NE2   . GLN A 1 1856 ? 216.949 195.767 156.789 1.00 105.27 ? 1856 GLN A NE2   1 
ATOM   1933  N N     . LEU A 1 1857 ? 216.290 190.661 161.109 1.00 90.39  ? 1857 LEU A N     1 
ATOM   1934  C CA    . LEU A 1 1857 ? 215.985 190.140 162.432 1.00 90.39  ? 1857 LEU A CA    1 
ATOM   1935  C C     . LEU A 1 1857 ? 215.926 188.623 162.372 1.00 90.39  ? 1857 LEU A C     1 
ATOM   1936  O O     . LEU A 1 1857 ? 215.217 188.058 161.534 1.00 90.39  ? 1857 LEU A O     1 
ATOM   1937  C CB    . LEU A 1 1857 ? 214.660 190.699 162.952 1.00 90.39  ? 1857 LEU A CB    1 
ATOM   1938  C CG    . LEU A 1 1857 ? 214.095 190.014 164.195 1.00 90.39  ? 1857 LEU A CG    1 
ATOM   1939  C CD1   . LEU A 1 1857 ? 215.092 190.068 165.333 1.00 90.39  ? 1857 LEU A CD1   1 
ATOM   1940  C CD2   . LEU A 1 1857 ? 212.792 190.659 164.610 1.00 90.39  ? 1857 LEU A CD2   1 
ATOM   1941  N N     . SER A 1 1858 ? 216.665 187.970 163.261 1.00 87.65  ? 1858 SER A N     1 
ATOM   1942  C CA    . SER A 1 1858 ? 216.696 186.519 163.347 1.00 87.65  ? 1858 SER A CA    1 
ATOM   1943  C C     . SER A 1 1858 ? 216.050 186.082 164.651 1.00 87.65  ? 1858 SER A C     1 
ATOM   1944  O O     . SER A 1 1858 ? 216.442 186.544 165.726 1.00 87.65  ? 1858 SER A O     1 
ATOM   1945  C CB    . SER A 1 1858 ? 218.128 185.991 163.267 1.00 87.65  ? 1858 SER A CB    1 
ATOM   1946  O OG    . SER A 1 1858 ? 218.217 184.692 163.824 1.00 87.65  ? 1858 SER A OG    1 
ATOM   1947  N N     . ILE A 1 1859 ? 215.070 185.192 164.552 1.00 81.42  ? 1859 ILE A N     1 
ATOM   1948  C CA    . ILE A 1 1859 ? 214.358 184.666 165.706 1.00 81.42  ? 1859 ILE A CA    1 
ATOM   1949  C C     . ILE A 1 1859 ? 214.694 183.189 165.847 1.00 81.42  ? 1859 ILE A C     1 
ATOM   1950  O O     . ILE A 1 1859 ? 214.817 182.472 164.847 1.00 81.42  ? 1859 ILE A O     1 
ATOM   1951  C CB    . ILE A 1 1859 ? 212.837 184.900 165.586 1.00 81.42  ? 1859 ILE A CB    1 
ATOM   1952  C CG1   . ILE A 1 1859 ? 212.223 185.048 166.970 1.00 81.42  ? 1859 ILE A CG1   1 
ATOM   1953  C CG2   . ILE A 1 1859 ? 212.154 183.798 164.809 1.00 81.42  ? 1859 ILE A CG2   1 
ATOM   1954  C CD1   . ILE A 1 1859 ? 212.503 186.368 167.580 1.00 81.42  ? 1859 ILE A CD1   1 
ATOM   1955  N N     . GLN A 1 1860 ? 214.905 182.748 167.085 1.00 81.77  ? 1860 GLN A N     1 
ATOM   1956  C CA    . GLN A 1 1860 ? 215.319 181.379 167.355 1.00 81.77  ? 1860 GLN A CA    1 
ATOM   1957  C C     . GLN A 1 1860 ? 214.567 180.821 168.552 1.00 81.77  ? 1860 GLN A C     1 
ATOM   1958  O O     . GLN A 1 1860 ? 214.276 181.543 169.509 1.00 81.77  ? 1860 GLN A O     1 
ATOM   1959  C CB    . GLN A 1 1860 ? 216.827 181.286 167.601 1.00 81.77  ? 1860 GLN A CB    1 
ATOM   1960  C CG    . GLN A 1 1860 ? 217.673 181.875 166.487 1.00 81.77  ? 1860 GLN A CG    1 
ATOM   1961  C CD    . GLN A 1 1860 ? 219.148 181.621 166.682 1.00 81.77  ? 1860 GLN A CD    1 
ATOM   1962  O OE1   . GLN A 1 1860 ? 219.557 181.004 167.664 1.00 81.77  ? 1860 GLN A OE1   1 
ATOM   1963  N NE2   . GLN A 1 1860 ? 219.959 182.101 165.749 1.00 81.77  ? 1860 GLN A NE2   1 
ATOM   1964  N N     . MET A 1 1861 ? 214.256 179.529 168.483 1.00 79.00  ? 1861 MET A N     1 
ATOM   1965  C CA    . MET A 1 1861 ? 213.557 178.810 169.542 1.00 79.00  ? 1861 MET A CA    1 
ATOM   1966  C C     . MET A 1 1861 ? 214.115 177.394 169.577 1.00 79.00  ? 1861 MET A C     1 
ATOM   1967  O O     . MET A 1 1861 ? 213.864 176.607 168.660 1.00 79.00  ? 1861 MET A O     1 
ATOM   1968  C CB    . MET A 1 1861 ? 212.051 178.794 169.294 1.00 79.00  ? 1861 MET A CB    1 
ATOM   1969  C CG    . MET A 1 1861 ? 211.230 178.324 170.470 1.00 79.00  ? 1861 MET A CG    1 
ATOM   1970  S SD    . MET A 1 1861 ? 211.754 179.089 172.007 1.00 79.00  ? 1861 MET A SD    1 
ATOM   1971  C CE    . MET A 1 1861 ? 210.271 178.899 172.990 1.00 79.00  ? 1861 MET A CE    1 
ATOM   1972  N N     . ALA A 1 1862 ? 214.868 177.074 170.628 1.00 78.06  ? 1862 ALA A N     1 
ATOM   1973  C CA    . ALA A 1 1862 ? 215.574 175.796 170.754 1.00 78.06  ? 1862 ALA A CA    1 
ATOM   1974  C C     . ALA A 1 1862 ? 216.479 175.651 169.537 1.00 78.06  ? 1862 ALA A C     1 
ATOM   1975  O O     . ALA A 1 1862 ? 217.395 176.475 169.373 1.00 78.06  ? 1862 ALA A O     1 
ATOM   1976  C CB    . ALA A 1 1862 ? 214.561 174.672 170.968 1.00 78.06  ? 1862 ALA A CB    1 
ATOM   1977  N N     . ASN A 1 1863 ? 216.280 174.660 168.674 1.00 78.05  ? 1863 ASN A N     1 
ATOM   1978  C CA    . ASN A 1 1863 ? 217.093 174.501 167.479 1.00 78.05  ? 1863 ASN A CA    1 
ATOM   1979  C C     . ASN A 1 1863 ? 216.402 175.005 166.223 1.00 78.05  ? 1863 ASN A C     1 
ATOM   1980  O O     . ASN A 1 1863 ? 216.882 174.736 165.119 1.00 78.05  ? 1863 ASN A O     1 
ATOM   1981  C CB    . ASN A 1 1863 ? 217.482 173.033 167.293 1.00 78.05  ? 1863 ASN A CB    1 
ATOM   1982  C CG    . ASN A 1 1863 ? 216.321 172.180 166.839 1.00 78.05  ? 1863 ASN A CG    1 
ATOM   1983  O OD1   . ASN A 1 1863 ? 215.408 171.893 167.610 1.00 78.05  ? 1863 ASN A OD1   1 
ATOM   1984  N ND2   . ASN A 1 1863 ? 216.347 171.770 165.578 1.00 78.05  ? 1863 ASN A ND2   1 
ATOM   1985  N N     . ALA A 1 1864 ? 215.290 175.718 166.358 1.00 80.49  ? 1864 ALA A N     1 
ATOM   1986  C CA    . ALA A 1 1864 ? 214.523 176.198 165.218 1.00 80.49  ? 1864 ALA A CA    1 
ATOM   1987  C C     . ALA A 1 1864 ? 214.762 177.688 165.021 1.00 80.49  ? 1864 ALA A C     1 
ATOM   1988  O O     . ALA A 1 1864 ? 214.651 178.470 165.970 1.00 80.49  ? 1864 ALA A O     1 
ATOM   1989  C CB    . ALA A 1 1864 ? 213.032 175.927 165.415 1.00 80.49  ? 1864 ALA A CB    1 
ATOM   1990  N N     . LYS A 1 1865 ? 215.078 178.075 163.790 1.00 82.87  ? 1865 LYS A N     1 
ATOM   1991  C CA    . LYS A 1 1865 ? 215.339 179.461 163.437 1.00 82.87  ? 1865 LYS A CA    1 
ATOM   1992  C C     . LYS A 1 1865 ? 214.334 179.916 162.392 1.00 82.87  ? 1865 LYS A C     1 
ATOM   1993  O O     . LYS A 1 1865 ? 213.982 179.156 161.485 1.00 82.87  ? 1865 LYS A O     1 
ATOM   1994  C CB    . LYS A 1 1865 ? 216.757 179.639 162.894 1.00 82.87  ? 1865 LYS A CB    1 
ATOM   1995  C CG    . LYS A 1 1865 ? 217.853 179.216 163.850 1.00 82.87  ? 1865 LYS A CG    1 
ATOM   1996  C CD    . LYS A 1 1865 ? 218.960 178.491 163.104 1.00 82.87  ? 1865 LYS A CD    1 
ATOM   1997  C CE    . LYS A 1 1865 ? 220.233 178.416 163.927 1.00 82.87  ? 1865 LYS A CE    1 
ATOM   1998  N NZ    . LYS A 1 1865 ? 220.964 179.712 163.931 1.00 82.87  ? 1865 LYS A NZ    1 
ATOM   1999  N N     . PHE A 1 1866 ? 213.873 181.156 162.519 1.00 82.79  ? 1866 PHE A N     1 
ATOM   2000  C CA    . PHE A 1 1866 ? 212.963 181.739 161.548 1.00 82.79  ? 1866 PHE A CA    1 
ATOM   2001  C C     . PHE A 1 1866 ? 213.355 183.183 161.290 1.00 82.79  ? 1866 PHE A C     1 
ATOM   2002  O O     . PHE A 1 1866 ? 214.088 183.801 162.064 1.00 82.79  ? 1866 PHE A O     1 
ATOM   2003  C CB    . PHE A 1 1866 ? 211.499 181.689 161.999 1.00 82.79  ? 1866 PHE A CB    1 
ATOM   2004  C CG    . PHE A 1 1866 ? 211.149 180.485 162.813 1.00 82.79  ? 1866 PHE A CG    1 
ATOM   2005  C CD1   . PHE A 1 1866 ? 211.454 180.425 164.158 1.00 82.79  ? 1866 PHE A CD1   1 
ATOM   2006  C CD2   . PHE A 1 1866 ? 210.499 179.416 162.229 1.00 82.79  ? 1866 PHE A CD2   1 
ATOM   2007  C CE1   . PHE A 1 1866 ? 211.128 179.319 164.901 1.00 82.79  ? 1866 PHE A CE1   1 
ATOM   2008  C CE2   . PHE A 1 1866 ? 210.169 178.309 162.968 1.00 82.79  ? 1866 PHE A CE2   1 
ATOM   2009  C CZ    . PHE A 1 1866 ? 210.484 178.259 164.306 1.00 82.79  ? 1866 PHE A CZ    1 
ATOM   2010  N N     . ASN A 1 1867 ? 212.849 183.713 160.184 1.00 91.80  ? 1867 ASN A N     1 
ATOM   2011  C CA    . ASN A 1 1867 ? 213.052 185.100 159.806 1.00 91.80  ? 1867 ASN A CA    1 
ATOM   2012  C C     . ASN A 1 1867 ? 211.772 185.874 160.074 1.00 91.80  ? 1867 ASN A C     1 
ATOM   2013  O O     . ASN A 1 1867 ? 210.682 185.421 159.714 1.00 91.80  ? 1867 ASN A O     1 
ATOM   2014  C CB    . ASN A 1 1867 ? 213.444 185.212 158.333 1.00 91.80  ? 1867 ASN A CB    1 
ATOM   2015  C CG    . ASN A 1 1867 ? 214.911 184.931 158.101 1.00 91.80  ? 1867 ASN A CG    1 
ATOM   2016  O OD1   . ASN A 1 1867 ? 215.442 183.925 158.568 1.00 91.80  ? 1867 ASN A OD1   1 
ATOM   2017  N ND2   . ASN A 1 1867 ? 215.575 185.818 157.371 1.00 91.80  ? 1867 ASN A ND2   1 
ATOM   2018  N N     . TYR A 1 1868 ? 211.908 187.029 160.714 1.00 89.13  ? 1868 TYR A N     1 
ATOM   2019  C CA    . TYR A 1 1868 ? 210.754 187.867 161.004 1.00 89.13  ? 1868 TYR A CA    1 
ATOM   2020  C C     . TYR A 1 1868 ? 210.107 188.325 159.706 1.00 89.13  ? 1868 TYR A C     1 
ATOM   2021  O O     . TYR A 1 1868 ? 210.760 188.946 158.863 1.00 89.13  ? 1868 TYR A O     1 
ATOM   2022  C CB    . TYR A 1 1868 ? 211.191 189.064 161.844 1.00 89.13  ? 1868 TYR A CB    1 
ATOM   2023  C CG    . TYR A 1 1868 ? 210.071 189.806 162.536 1.00 89.13  ? 1868 TYR A CG    1 
ATOM   2024  C CD1   . TYR A 1 1868 ? 209.295 189.191 163.505 1.00 89.13  ? 1868 TYR A CD1   1 
ATOM   2025  C CD2   . TYR A 1 1868 ? 209.805 191.133 162.234 1.00 89.13  ? 1868 TYR A CD2   1 
ATOM   2026  C CE1   . TYR A 1 1868 ? 208.279 189.873 164.141 1.00 89.13  ? 1868 TYR A CE1   1 
ATOM   2027  C CE2   . TYR A 1 1868 ? 208.792 191.821 162.866 1.00 89.13  ? 1868 TYR A CE2   1 
ATOM   2028  C CZ    . TYR A 1 1868 ? 208.033 191.186 163.818 1.00 89.13  ? 1868 TYR A CZ    1 
ATOM   2029  O OH    . TYR A 1 1868 ? 207.023 191.871 164.448 1.00 89.13  ? 1868 TYR A OH    1 
ATOM   2030  N N     . GLY A 1 1869 ? 208.821 188.014 159.543 1.00 91.16  ? 1869 GLY A N     1 
ATOM   2031  C CA    . GLY A 1 1869 ? 208.124 188.383 158.325 1.00 91.16  ? 1869 GLY A CA    1 
ATOM   2032  C C     . GLY A 1 1869 ? 207.901 189.870 158.171 1.00 91.16  ? 1869 GLY A C     1 
ATOM   2033  O O     . GLY A 1 1869 ? 207.647 190.335 157.055 1.00 91.16  ? 1869 GLY A O     1 
ATOM   2034  N N     . PHE A 1 1870 ? 207.970 190.620 159.270 1.00 88.99  ? 1870 PHE A N     1 
ATOM   2035  C CA    . PHE A 1 1870 ? 207.867 192.077 159.275 1.00 88.99  ? 1870 PHE A CA    1 
ATOM   2036  C C     . PHE A 1 1870 ? 206.527 192.571 158.755 1.00 88.99  ? 1870 PHE A C     1 
ATOM   2037  O O     . PHE A 1 1870 ? 206.400 193.738 158.378 1.00 88.99  ? 1870 PHE A O     1 
ATOM   2038  C CB    . PHE A 1 1870 ? 209.005 192.714 158.476 1.00 88.99  ? 1870 PHE A CB    1 
ATOM   2039  C CG    . PHE A 1 1870 ? 210.280 192.828 159.242 1.00 88.99  ? 1870 PHE A CG    1 
ATOM   2040  C CD1   . PHE A 1 1870 ? 210.425 193.787 160.222 1.00 88.99  ? 1870 PHE A CD1   1 
ATOM   2041  C CD2   . PHE A 1 1870 ? 211.330 191.970 158.989 1.00 88.99  ? 1870 PHE A CD2   1 
ATOM   2042  C CE1   . PHE A 1 1870 ? 211.594 193.892 160.931 1.00 88.99  ? 1870 PHE A CE1   1 
ATOM   2043  C CE2   . PHE A 1 1870 ? 212.503 192.070 159.696 1.00 88.99  ? 1870 PHE A CE2   1 
ATOM   2044  C CZ    . PHE A 1 1870 ? 212.635 193.032 160.670 1.00 88.99  ? 1870 PHE A CZ    1 
ATOM   2045  N N     . GLU A 1 1871 ? 205.520 191.708 158.724 1.00 96.38  ? 1871 GLU A N     1 
ATOM   2046  C CA    . GLU A 1 1871 ? 204.186 192.147 158.355 1.00 96.38  ? 1871 GLU A CA    1 
ATOM   2047  C C     . GLU A 1 1871 ? 203.666 193.140 159.384 1.00 96.38  ? 1871 GLU A C     1 
ATOM   2048  O O     . GLU A 1 1871 ? 203.983 193.056 160.571 1.00 96.38  ? 1871 GLU A O     1 
ATOM   2049  C CB    . GLU A 1 1871 ? 203.245 190.951 158.252 1.00 96.38  ? 1871 GLU A CB    1 
ATOM   2050  C CG    . GLU A 1 1871 ? 201.884 191.283 157.691 1.00 96.38  ? 1871 GLU A CG    1 
ATOM   2051  C CD    . GLU A 1 1871 ? 201.702 190.758 156.287 1.00 96.38  ? 1871 GLU A CD    1 
ATOM   2052  O OE1   . GLU A 1 1871 ? 202.719 190.463 155.626 1.00 96.38  ? 1871 GLU A OE1   1 
ATOM   2053  O OE2   . GLU A 1 1871 ? 200.541 190.640 155.844 1.00 96.38  ? 1871 GLU A OE2   1 
ATOM   2054  N N     . TYR A 1 1872 ? 202.885 194.110 158.920 1.00 105.71 ? 1872 TYR A N     1 
ATOM   2055  C CA    . TYR A 1 1872 ? 202.313 195.112 159.807 1.00 105.71 ? 1872 TYR A CA    1 
ATOM   2056  C C     . TYR A 1 1872 ? 201.008 194.594 160.394 1.00 105.71 ? 1872 TYR A C     1 
ATOM   2057  O O     . TYR A 1 1872 ? 200.102 194.201 159.654 1.00 105.71 ? 1872 TYR A O     1 
ATOM   2058  C CB    . TYR A 1 1872 ? 202.067 196.426 159.072 1.00 105.71 ? 1872 TYR A CB    1 
ATOM   2059  C CG    . TYR A 1 1872 ? 201.502 197.493 159.973 1.00 105.71 ? 1872 TYR A CG    1 
ATOM   2060  C CD1   . TYR A 1 1872 ? 202.202 197.921 161.090 1.00 105.71 ? 1872 TYR A CD1   1 
ATOM   2061  C CD2   . TYR A 1 1872 ? 200.263 198.056 159.722 1.00 105.71 ? 1872 TYR A CD2   1 
ATOM   2062  C CE1   . TYR A 1 1872 ? 201.690 198.891 161.924 1.00 105.71 ? 1872 TYR A CE1   1 
ATOM   2063  C CE2   . TYR A 1 1872 ? 199.742 199.026 160.550 1.00 105.71 ? 1872 TYR A CE2   1 
ATOM   2064  C CZ    . TYR A 1 1872 ? 200.459 199.440 161.649 1.00 105.71 ? 1872 TYR A CZ    1 
ATOM   2065  O OH    . TYR A 1 1872 ? 199.942 200.407 162.478 1.00 105.71 ? 1872 TYR A OH    1 
ATOM   2066  N N     . LEU A 1 1873 ? 200.911 194.604 161.721 1.00 95.83  ? 1873 LEU A N     1 
ATOM   2067  C CA    . LEU A 1 1873 ? 199.733 194.086 162.396 1.00 95.83  ? 1873 LEU A CA    1 
ATOM   2068  C C     . LEU A 1 1873 ? 199.015 195.125 163.240 1.00 95.83  ? 1873 LEU A C     1 
ATOM   2069  O O     . LEU A 1 1873 ? 198.060 194.773 163.942 1.00 95.83  ? 1873 LEU A O     1 
ATOM   2070  C CB    . LEU A 1 1873 ? 200.099 192.887 163.281 1.00 95.83  ? 1873 LEU A CB    1 
ATOM   2071  C CG    . LEU A 1 1873 ? 201.074 191.852 162.720 1.00 95.83  ? 1873 LEU A CG    1 
ATOM   2072  C CD1   . LEU A 1 1873 ? 202.494 192.203 163.096 1.00 95.83  ? 1873 LEU A CD1   1 
ATOM   2073  C CD2   . LEU A 1 1873 ? 200.730 190.459 163.186 1.00 95.83  ? 1873 LEU A CD2   1 
ATOM   2074  N N     . GLY A 1 1874 ? 199.435 196.385 163.196 1.00 103.40 ? 1874 GLY A N     1 
ATOM   2075  C CA    . GLY A 1 1874 ? 198.763 197.398 163.989 1.00 103.40 ? 1874 GLY A CA    1 
ATOM   2076  C C     . GLY A 1 1874 ? 198.926 197.138 165.471 1.00 103.40 ? 1874 GLY A C     1 
ATOM   2077  O O     . GLY A 1 1874 ? 199.973 196.674 165.935 1.00 103.40 ? 1874 GLY A O     1 
ATOM   2078  N N     . VAL A 1 1875 ? 197.878 197.435 166.230 1.00 103.15 ? 1875 VAL A N     1 
ATOM   2079  C CA    . VAL A 1 1875 ? 197.881 197.245 167.678 1.00 103.15 ? 1875 VAL A CA    1 
ATOM   2080  C C     . VAL A 1 1875 ? 197.073 195.983 167.952 1.00 103.15 ? 1875 VAL A C     1 
ATOM   2081  O O     . VAL A 1 1875 ? 195.847 196.008 168.051 1.00 103.15 ? 1875 VAL A O     1 
ATOM   2082  C CB    . VAL A 1 1875 ? 197.325 198.459 168.416 1.00 103.15 ? 1875 VAL A CB    1 
ATOM   2083  C CG1   . VAL A 1 1875 ? 197.376 198.228 169.912 1.00 103.15 ? 1875 VAL A CG1   1 
ATOM   2084  C CG2   . VAL A 1 1875 ? 198.114 199.698 168.048 1.00 103.15 ? 1875 VAL A CG2   1 
ATOM   2085  N N     . GLN A 1 1876 ? 197.772 194.863 168.077 1.00 98.89  ? 1876 GLN A N     1 
ATOM   2086  C CA    . GLN A 1 1876 ? 197.139 193.600 168.410 1.00 98.89  ? 1876 GLN A CA    1 
ATOM   2087  C C     . GLN A 1 1876 ? 197.217 193.347 169.911 1.00 98.89  ? 1876 GLN A C     1 
ATOM   2088  O O     . GLN A 1 1876 ? 198.056 193.908 170.619 1.00 98.89  ? 1876 GLN A O     1 
ATOM   2089  C CB    . GLN A 1 1876 ? 197.796 192.450 167.649 1.00 98.89  ? 1876 GLN A CB    1 
ATOM   2090  C CG    . GLN A 1 1876 ? 197.383 192.369 166.196 1.00 98.89  ? 1876 GLN A CG    1 
ATOM   2091  C CD    . GLN A 1 1876 ? 196.116 191.567 165.999 1.00 98.89  ? 1876 GLN A CD    1 
ATOM   2092  O OE1   . GLN A 1 1876 ? 196.157 190.416 165.568 1.00 98.89  ? 1876 GLN A OE1   1 
ATOM   2093  N NE2   . GLN A 1 1876 ? 194.979 192.171 166.317 1.00 98.89  ? 1876 GLN A NE2   1 
ATOM   2094  N N     . ASP A 1 1877 ? 196.321 192.493 170.393 1.00 98.17  ? 1877 ASP A N     1 
ATOM   2095  C CA    . ASP A 1 1877 ? 196.320 192.121 171.800 1.00 98.17  ? 1877 ASP A CA    1 
ATOM   2096  C C     . ASP A 1 1877 ? 197.512 191.216 172.084 1.00 98.17  ? 1877 ASP A C     1 
ATOM   2097  O O     . ASP A 1 1877 ? 197.556 190.072 171.622 1.00 98.17  ? 1877 ASP A O     1 
ATOM   2098  C CB    . ASP A 1 1877 ? 195.010 191.422 172.156 1.00 98.17  ? 1877 ASP A CB    1 
ATOM   2099  C CG    . ASP A 1 1877 ? 194.825 191.236 173.653 1.00 98.17  ? 1877 ASP A CG    1 
ATOM   2100  O OD1   . ASP A 1 1877 ? 195.829 191.097 174.382 1.00 98.17  ? 1877 ASP A OD1   1 
ATOM   2101  O OD2   . ASP A 1 1877 ? 193.661 191.224 174.103 1.00 98.17  ? 1877 ASP A OD2   1 
ATOM   2102  N N     . LYS A 1 1878 ? 198.464 191.718 172.877 1.00 84.90  ? 1878 LYS A N     1 
ATOM   2103  C CA    . LYS A 1 1878 ? 199.638 190.893 173.270 1.00 84.90  ? 1878 LYS A CA    1 
ATOM   2104  C C     . LYS A 1 1878 ? 199.180 189.825 174.269 1.00 84.90  ? 1878 LYS A C     1 
ATOM   2105  O O     . LYS A 1 1878 ? 198.809 190.199 175.399 1.00 84.90  ? 1878 LYS A O     1 
ATOM   2106  C CB    . LYS A 1 1878 ? 200.731 191.780 173.872 1.00 84.90  ? 1878 LYS A CB    1 
ATOM   2107  C CG    . LYS A 1 1878 ? 201.833 191.044 174.623 1.00 84.90  ? 1878 LYS A CG    1 
ATOM   2108  C CD    . LYS A 1 1878 ? 202.558 190.017 173.781 1.00 84.90  ? 1878 LYS A CD    1 
ATOM   2109  C CE    . LYS A 1 1878 ? 203.686 189.336 174.525 1.00 84.90  ? 1878 LYS A CE    1 
ATOM   2110  N NZ    . LYS A 1 1878 ? 203.209 188.677 175.763 1.00 84.90  ? 1878 LYS A NZ    1 
ATOM   2111  N N     . LEU A 1 1879 ? 199.204 188.552 173.865 1.00 80.66  ? 1879 LEU A N     1 
ATOM   2112  C CA    . LEU A 1 1879 ? 198.741 187.449 174.749 1.00 80.66  ? 1879 LEU A CA    1 
ATOM   2113  C C     . LEU A 1 1879 ? 199.720 187.293 175.918 1.00 80.66  ? 1879 LEU A C     1 
ATOM   2114  O O     . LEU A 1 1879 ? 200.940 187.314 175.668 1.00 80.66  ? 1879 LEU A O     1 
ATOM   2115  C CB    . LEU A 1 1879 ? 198.658 186.163 173.922 1.00 80.66  ? 1879 LEU A CB    1 
ATOM   2116  C CG    . LEU A 1 1879 ? 197.637 185.135 174.405 1.00 80.66  ? 1879 LEU A CG    1 
ATOM   2117  C CD1   . LEU A 1 1879 ? 196.219 185.609 174.123 1.00 80.66  ? 1879 LEU A CD1   1 
ATOM   2118  C CD2   . LEU A 1 1879 ? 197.882 183.781 173.756 1.00 80.66  ? 1879 LEU A CD2   1 
ATOM   2119  N N     . VAL A 1 1880 ? 199.201 187.137 177.139 1.00 75.17  ? 1880 VAL A N     1 
ATOM   2120  C CA    . VAL A 1 1880 ? 200.072 186.993 178.345 1.00 75.17  ? 1880 VAL A CA    1 
ATOM   2121  C C     . VAL A 1 1880 ? 200.926 185.732 178.184 1.00 75.17  ? 1880 VAL A C     1 
ATOM   2122  O O     . VAL A 1 1880 ? 200.378 184.701 177.748 1.00 75.17  ? 1880 VAL A O     1 
ATOM   2123  C CB    . VAL A 1 1880 ? 199.239 186.941 179.640 1.00 75.17  ? 1880 VAL A CB    1 
ATOM   2124  C CG1   . VAL A 1 1880 ? 200.096 186.608 180.852 1.00 75.17  ? 1880 VAL A CG1   1 
ATOM   2125  C CG2   . VAL A 1 1880 ? 198.462 188.228 179.866 1.00 75.17  ? 1880 VAL A CG2   1 
ATOM   2126  N N     . GLN A 1 1881 ? 202.214 185.817 178.526 1.00 69.84  ? 1881 GLN A N     1 
ATOM   2127  C CA    . GLN A 1 1881 ? 203.118 184.641 178.424 1.00 69.84  ? 1881 GLN A CA    1 
ATOM   2128  C C     . GLN A 1 1881 ? 202.994 183.797 179.696 1.00 69.84  ? 1881 GLN A C     1 
ATOM   2129  O O     . GLN A 1 1881 ? 203.151 184.364 180.794 1.00 69.84  ? 1881 GLN A O     1 
ATOM   2130  C CB    . GLN A 1 1881 ? 204.564 185.089 178.208 1.00 69.84  ? 1881 GLN A CB    1 
ATOM   2131  C CG    . GLN A 1 1881 ? 205.577 183.959 178.337 1.00 69.84  ? 1881 GLN A CG    1 
ATOM   2132  C CD    . GLN A 1 1881 ? 205.418 182.901 177.273 1.00 69.84  ? 1881 GLN A CD    1 
ATOM   2133  O OE1   . GLN A 1 1881 ? 204.574 183.001 176.386 1.00 69.84  ? 1881 GLN A OE1   1 
ATOM   2134  N NE2   . GLN A 1 1881 ? 206.247 181.872 177.350 1.00 69.84  ? 1881 GLN A NE2   1 
ATOM   2135  N N     . THR A 1 1882 ? 202.723 182.498 179.545 1.00 68.34  ? 1882 THR A N     1 
ATOM   2136  C CA    . THR A 1 1882 ? 202.595 181.589 180.716 1.00 68.34  ? 1882 THR A CA    1 
ATOM   2137  C C     . THR A 1 1882 ? 203.323 180.274 180.417 1.00 68.34  ? 1882 THR A C     1 
ATOM   2138  O O     . THR A 1 1882 ? 203.723 180.073 179.254 1.00 68.34  ? 1882 THR A O     1 
ATOM   2139  C CB    . THR A 1 1882 ? 201.123 181.342 181.068 1.00 68.34  ? 1882 THR A CB    1 
ATOM   2140  O OG1   . THR A 1 1882 ? 200.465 180.860 179.897 1.00 68.34  ? 1882 THR A OG1   1 
ATOM   2141  C CG2   . THR A 1 1882 ? 200.424 182.583 181.576 1.00 68.34  ? 1882 THR A CG2   1 
ATOM   2142  N N     . PRO A 1 1883 ? 203.504 179.373 181.406 1.00 66.90  ? 1883 PRO A N     1 
ATOM   2143  C CA    . PRO A 1 1883 ? 204.245 178.131 181.189 1.00 66.90  ? 1883 PRO A CA    1 
ATOM   2144  C C     . PRO A 1 1883 ? 203.585 177.315 180.069 1.00 66.90  ? 1883 PRO A C     1 
ATOM   2145  O O     . PRO A 1 1883 ? 204.296 176.808 179.223 1.00 66.90  ? 1883 PRO A O     1 
ATOM   2146  C CB    . PRO A 1 1883 ? 204.131 177.391 182.529 1.00 66.90  ? 1883 PRO A CB    1 
ATOM   2147  C CG    . PRO A 1 1883 ? 202.953 178.041 183.223 1.00 66.90  ? 1883 PRO A CG    1 
ATOM   2148  C CD    . PRO A 1 1883 ? 202.984 179.484 182.768 1.00 66.90  ? 1883 PRO A CD    1 
ATOM   2149  N N     . LEU A 1 1884 ? 202.253 177.219 180.088 1.00 66.25  ? 1884 LEU A N     1 
ATOM   2150  C CA    . LEU A 1 1884 ? 201.525 176.487 179.018 1.00 66.25  ? 1884 LEU A CA    1 
ATOM   2151  C C     . LEU A 1 1884 ? 201.795 177.183 177.682 1.00 66.25  ? 1884 LEU A C     1 
ATOM   2152  O O     . LEU A 1 1884 ? 202.093 176.478 176.699 1.00 66.25  ? 1884 LEU A O     1 
ATOM   2153  C CB    . LEU A 1 1884 ? 200.029 176.483 179.343 1.00 66.25  ? 1884 LEU A CB    1 
ATOM   2154  C CG    . LEU A 1 1884 ? 199.143 175.753 178.335 1.00 66.25  ? 1884 LEU A CG    1 
ATOM   2155  C CD1   . LEU A 1 1884 ? 199.362 174.250 178.417 1.00 66.25  ? 1884 LEU A CD1   1 
ATOM   2156  C CD2   . LEU A 1 1884 ? 197.677 176.090 178.559 1.00 66.25  ? 1884 LEU A CD2   1 
ATOM   2157  N N     . THR A 1 1885 ? 201.708 178.516 177.660 1.00 66.41  ? 1885 THR A N     1 
ATOM   2158  C CA    . THR A 1 1885 ? 201.984 179.282 176.417 1.00 66.41  ? 1885 THR A CA    1 
ATOM   2159  C C     . THR A 1 1885 ? 203.423 178.997 175.979 1.00 66.41  ? 1885 THR A C     1 
ATOM   2160  O O     . THR A 1 1885 ? 203.651 178.846 174.763 1.00 66.41  ? 1885 THR A O     1 
ATOM   2161  C CB    . THR A 1 1885 ? 201.738 180.782 176.621 1.00 66.41  ? 1885 THR A CB    1 
ATOM   2162  O OG1   . THR A 1 1885 ? 200.420 180.949 177.145 1.00 66.41  ? 1885 THR A OG1   1 
ATOM   2163  C CG2   . THR A 1 1885 ? 201.888 181.582 175.346 1.00 66.41  ? 1885 THR A CG2   1 
ATOM   2164  N N     . ASP A 1 1886 ? 204.348 178.921 176.940 1.00 70.27  ? 1886 ASP A N     1 
ATOM   2165  C CA    . ASP A 1 1886 ? 205.766 178.619 176.615 1.00 70.27  ? 1886 ASP A CA    1 
ATOM   2166  C C     . ASP A 1 1886 ? 205.837 177.231 175.972 1.00 70.27  ? 1886 ASP A C     1 
ATOM   2167  O O     . ASP A 1 1886 ? 206.239 177.150 174.796 1.00 70.27  ? 1886 ASP A O     1 
ATOM   2168  C CB    . ASP A 1 1886 ? 206.662 178.727 177.851 1.00 70.27  ? 1886 ASP A CB    1 
ATOM   2169  C CG    . ASP A 1 1886 ? 208.142 178.774 177.513 1.00 70.27  ? 1886 ASP A CG    1 
ATOM   2170  O OD1   . ASP A 1 1886 ? 208.470 178.707 176.311 1.00 70.27  ? 1886 ASP A OD1   1 
ATOM   2171  O OD2   . ASP A 1 1886 ? 208.954 178.886 178.452 1.00 70.27  ? 1886 ASP A OD2   1 
ATOM   2172  N N     . ARG A 1 1887 ? 205.458 176.185 176.713 1.00 67.27  ? 1887 ARG A N     1 
ATOM   2173  C CA    . ARG A 1 1887 ? 205.445 174.849 176.134 1.00 67.27  ? 1887 ARG A CA    1 
ATOM   2174  C C     . ARG A 1 1887 ? 204.792 174.856 174.761 1.00 67.27  ? 1887 ARG A C     1 
ATOM   2175  O O     . ARG A 1 1887 ? 205.238 174.152 173.849 1.00 67.27  ? 1887 ARG A O     1 
ATOM   2176  C CB    . ARG A 1 1887 ? 204.719 173.886 177.069 1.00 67.27  ? 1887 ARG A CB    1 
ATOM   2177  C CG    . ARG A 1 1887 ? 204.487 172.512 176.486 1.00 67.27  ? 1887 ARG A CG    1 
ATOM   2178  C CD    . ARG A 1 1887 ? 203.443 171.764 177.282 1.00 67.27  ? 1887 ARG A CD    1 
ATOM   2179  N NE    . ARG A 1 1887 ? 203.736 170.340 177.362 1.00 67.27  ? 1887 ARG A NE    1 
ATOM   2180  C CZ    . ARG A 1 1887 ? 203.106 169.495 178.165 1.00 67.27  ? 1887 ARG A CZ    1 
ATOM   2181  N NH1   . ARG A 1 1887 ? 202.141 169.901 178.973 1.00 67.27  ? 1887 ARG A NH1   1 
ATOM   2182  N NH2   . ARG A 1 1887 ? 203.451 168.212 178.157 1.00 67.27  ? 1887 ARG A NH2   1 
ATOM   2183  N N     . CYS A 1 1888 ? 203.726 175.639 174.597 1.00 70.14  ? 1888 CYS A N     1 
ATOM   2184  C CA    . CYS A 1 1888 ? 203.055 175.712 173.305 1.00 70.14  ? 1888 CYS A CA    1 
ATOM   2185  C C     . CYS A 1 1888 ? 203.984 176.274 172.241 1.00 70.14  ? 1888 CYS A C     1 
ATOM   2186  O O     . CYS A 1 1888 ? 204.063 175.744 171.129 1.00 70.14  ? 1888 CYS A O     1 
ATOM   2187  C CB    . CYS A 1 1888 ? 201.795 176.564 173.412 1.00 70.14  ? 1888 CYS A CB    1 
ATOM   2188  S SG    . CYS A 1 1888 ? 201.067 176.974 171.818 1.00 70.14  ? 1888 CYS A SG    1 
ATOM   2189  N N     . TYR A 1 1889 ? 204.698 177.350 172.568 1.00 69.60  ? 1889 TYR A N     1 
ATOM   2190  C CA    . TYR A 1 1889 ? 205.642 177.930 171.621 1.00 69.60  ? 1889 TYR A CA    1 
ATOM   2191  C C     . TYR A 1 1889 ? 206.731 176.931 171.268 1.00 69.60  ? 1889 TYR A C     1 
ATOM   2192  O O     . TYR A 1 1889 ? 207.086 176.769 170.096 1.00 69.60  ? 1889 TYR A O     1 
ATOM   2193  C CB    . TYR A 1 1889 ? 206.253 179.203 172.204 1.00 69.60  ? 1889 TYR A CB    1 
ATOM   2194  C CG    . TYR A 1 1889 ? 205.409 180.440 172.018 1.00 69.60  ? 1889 TYR A CG    1 
ATOM   2195  C CD1   . TYR A 1 1889 ? 204.102 180.352 171.574 1.00 69.60  ? 1889 TYR A CD1   1 
ATOM   2196  C CD2   . TYR A 1 1889 ? 205.920 181.697 172.302 1.00 69.60  ? 1889 TYR A CD2   1 
ATOM   2197  C CE1   . TYR A 1 1889 ? 203.329 181.480 171.409 1.00 69.60  ? 1889 TYR A CE1   1 
ATOM   2198  C CE2   . TYR A 1 1889 ? 205.155 182.830 172.141 1.00 69.60  ? 1889 TYR A CE2   1 
ATOM   2199  C CZ    . TYR A 1 1889 ? 203.860 182.716 171.693 1.00 69.60  ? 1889 TYR A CZ    1 
ATOM   2200  O OH    . TYR A 1 1889 ? 203.089 183.844 171.528 1.00 69.60  ? 1889 TYR A OH    1 
ATOM   2201  N N     . LEU A 1 1890 ? 207.269 176.244 172.276 1.00 67.05  ? 1890 LEU A N     1 
ATOM   2202  C CA    . LEU A 1 1890 ? 208.336 175.281 172.024 1.00 67.05  ? 1890 LEU A CA    1 
ATOM   2203  C C     . LEU A 1 1890 ? 207.854 174.159 171.115 1.00 67.05  ? 1890 LEU A C     1 
ATOM   2204  O O     . LEU A 1 1890 ? 208.514 173.815 170.127 1.00 67.05  ? 1890 LEU A O     1 
ATOM   2205  C CB    . LEU A 1 1890 ? 208.852 174.722 173.347 1.00 67.05  ? 1890 LEU A CB    1 
ATOM   2206  C CG    . LEU A 1 1890 ? 209.940 173.662 173.256 1.00 67.05  ? 1890 LEU A CG    1 
ATOM   2207  C CD1   . LEU A 1 1890 ? 211.232 174.295 172.807 1.00 67.05  ? 1890 LEU A CD1   1 
ATOM   2208  C CD2   . LEU A 1 1890 ? 210.117 172.989 174.598 1.00 67.05  ? 1890 LEU A CD2   1 
ATOM   2209  N N     . THR A 1 1891 ? 206.687 173.592 171.423 1.00 64.06  ? 1891 THR A N     1 
ATOM   2210  C CA    . THR A 1 1891 ? 206.152 172.503 170.616 1.00 64.06  ? 1891 THR A CA    1 
ATOM   2211  C C     . THR A 1 1891 ? 205.852 172.964 169.199 1.00 64.06  ? 1891 THR A C     1 
ATOM   2212  O O     . THR A 1 1891 ? 206.158 172.260 168.230 1.00 64.06  ? 1891 THR A O     1 
ATOM   2213  C CB    . THR A 1 1891 ? 204.890 171.945 171.267 1.00 64.06  ? 1891 THR A CB    1 
ATOM   2214  O OG1   . THR A 1 1891 ? 205.210 171.423 172.560 1.00 64.06  ? 1891 THR A OG1   1 
ATOM   2215  C CG2   . THR A 1 1891 ? 204.298 170.843 170.417 1.00 64.06  ? 1891 THR A CG2   1 
ATOM   2216  N N     . MET A 1 1892 ? 205.252 174.146 169.057 1.00 63.13  ? 1892 MET A N     1 
ATOM   2217  C CA    . MET A 1 1892 ? 204.881 174.626 167.736 1.00 63.13  ? 1892 MET A CA    1 
ATOM   2218  C C     . MET A 1 1892 ? 206.115 174.897 166.889 1.00 63.13  ? 1892 MET A C     1 
ATOM   2219  O O     . MET A 1 1892 ? 206.150 174.548 165.704 1.00 63.13  ? 1892 MET A O     1 
ATOM   2220  C CB    . MET A 1 1892 ? 204.030 175.887 167.863 1.00 63.13  ? 1892 MET A CB    1 
ATOM   2221  C CG    . MET A 1 1892 ? 202.551 175.697 168.237 1.00 63.13  ? 1892 MET A CG    1 
ATOM   2222  S SD    . MET A 1 1892 ? 201.493 174.610 167.257 1.00 63.13  ? 1892 MET A SD    1 
ATOM   2223  C CE    . MET A 1 1892 ? 201.960 172.979 167.833 1.00 63.13  ? 1892 MET A CE    1 
ATOM   2224  N N     . THR A 1 1893 ? 207.141 175.515 167.478 1.00 70.84  ? 1893 THR A N     1 
ATOM   2225  C CA    . THR A 1 1893 ? 208.366 175.774 166.732 1.00 70.84  ? 1893 THR A CA    1 
ATOM   2226  C C     . THR A 1 1893 ? 209.073 174.477 166.367 1.00 70.84  ? 1893 THR A C     1 
ATOM   2227  O O     . THR A 1 1893 ? 209.631 174.357 165.271 1.00 70.84  ? 1893 THR A O     1 
ATOM   2228  C CB    . THR A 1 1893 ? 209.289 176.682 167.536 1.00 70.84  ? 1893 THR A CB    1 
ATOM   2229  O OG1   . THR A 1 1893 ? 209.269 176.282 168.910 1.00 70.84  ? 1893 THR A OG1   1 
ATOM   2230  C CG2   . THR A 1 1893 ? 208.826 178.121 167.433 1.00 70.84  ? 1893 THR A CG2   1 
ATOM   2231  N N     . GLN A 1 1894 ? 209.068 173.493 167.269 1.00 74.71  ? 1894 GLN A N     1 
ATOM   2232  C CA    . GLN A 1 1894 ? 209.644 172.196 166.931 1.00 74.71  ? 1894 GLN A CA    1 
ATOM   2233  C C     . GLN A 1 1894 ? 208.907 171.557 165.765 1.00 74.71  ? 1894 GLN A C     1 
ATOM   2234  O O     . GLN A 1 1894 ? 209.530 170.998 164.857 1.00 74.71  ? 1894 GLN A O     1 
ATOM   2235  C CB    . GLN A 1 1894 ? 209.614 171.275 168.146 1.00 74.71  ? 1894 GLN A CB    1 
ATOM   2236  C CG    . GLN A 1 1894 ? 210.687 171.577 169.152 1.00 74.71  ? 1894 GLN A CG    1 
ATOM   2237  C CD    . GLN A 1 1894 ? 212.047 171.660 168.512 1.00 74.71  ? 1894 GLN A CD    1 
ATOM   2238  O OE1   . GLN A 1 1894 ? 212.501 170.712 167.877 1.00 74.71  ? 1894 GLN A OE1   1 
ATOM   2239  N NE2   . GLN A 1 1894 ? 212.709 172.796 168.674 1.00 74.71  ? 1894 GLN A NE2   1 
ATOM   2240  N N     . ALA A 1 1895 ? 207.576 171.629 165.774 1.00 76.30  ? 1895 ALA A N     1 
ATOM   2241  C CA    . ALA A 1 1895 ? 206.803 171.069 164.674 1.00 76.30  ? 1895 ALA A CA    1 
ATOM   2242  C C     . ALA A 1 1895 ? 207.099 171.797 163.371 1.00 76.30  ? 1895 ALA A C     1 
ATOM   2243  O O     . ALA A 1 1895 ? 207.207 171.172 162.310 1.00 76.30  ? 1895 ALA A O     1 
ATOM   2244  C CB    . ALA A 1 1895 ? 205.313 171.128 164.999 1.00 76.30  ? 1895 ALA A CB    1 
ATOM   2245  N N     . LEU A 1 1896 ? 207.229 173.122 163.431 1.00 71.32  ? 1896 LEU A N     1 
ATOM   2246  C CA    . LEU A 1 1896 ? 207.516 173.889 162.226 1.00 71.32  ? 1896 LEU A CA    1 
ATOM   2247  C C     . LEU A 1 1896 ? 208.902 173.569 161.682 1.00 71.32  ? 1896 LEU A C     1 
ATOM   2248  O O     . LEU A 1 1896 ? 209.093 173.502 160.464 1.00 71.32  ? 1896 LEU A O     1 
ATOM   2249  C CB    . LEU A 1 1896 ? 207.380 175.381 162.513 1.00 71.32  ? 1896 LEU A CB    1 
ATOM   2250  C CG    . LEU A 1 1896 ? 205.947 175.857 162.734 1.00 71.32  ? 1896 LEU A CG    1 
ATOM   2251  C CD1   . LEU A 1 1896 ? 205.892 177.367 162.800 1.00 71.32  ? 1896 LEU A CD1   1 
ATOM   2252  C CD2   . LEU A 1 1896 ? 205.045 175.334 161.635 1.00 71.32  ? 1896 LEU A CD2   1 
ATOM   2253  N N     . GLU A 1 1897 ? 209.880 173.372 162.569 1.00 82.02  ? 1897 GLU A N     1 
ATOM   2254  C CA    . GLU A 1 1897 ? 211.234 173.066 162.122 1.00 82.02  ? 1897 GLU A CA    1 
ATOM   2255  C C     . GLU A 1 1897 ? 211.282 171.750 161.361 1.00 82.02  ? 1897 GLU A C     1 
ATOM   2256  O O     . GLU A 1 1897 ? 211.971 171.637 160.342 1.00 82.02  ? 1897 GLU A O     1 
ATOM   2257  C CB    . GLU A 1 1897 ? 212.185 173.025 163.314 1.00 82.02  ? 1897 GLU A CB    1 
ATOM   2258  C CG    . GLU A 1 1897 ? 213.568 172.493 162.987 1.00 82.02  ? 1897 GLU A CG    1 
ATOM   2259  C CD    . GLU A 1 1897 ? 214.316 173.369 162.007 1.00 82.02  ? 1897 GLU A CD    1 
ATOM   2260  O OE1   . GLU A 1 1897 ? 214.018 174.579 161.938 1.00 82.02  ? 1897 GLU A OE1   1 
ATOM   2261  O OE2   . GLU A 1 1897 ? 215.211 172.847 161.310 1.00 82.02  ? 1897 GLU A OE2   1 
ATOM   2262  N N     . ALA A 1 1898 ? 210.561 170.744 161.838 1.00 82.06  ? 1898 ALA A N     1 
ATOM   2263  C CA    . ALA A 1 1898 ? 210.438 169.489 161.113 1.00 82.06  ? 1898 ALA A CA    1 
ATOM   2264  C C     . ALA A 1 1898 ? 209.403 169.560 160.003 1.00 82.06  ? 1898 ALA A C     1 
ATOM   2265  O O     . ALA A 1 1898 ? 209.065 168.522 159.426 1.00 82.06  ? 1898 ALA A O     1 
ATOM   2266  C CB    . ALA A 1 1898 ? 210.094 168.352 162.076 1.00 82.06  ? 1898 ALA A CB    1 
ATOM   2267  N N     . ARG A 1 1899 ? 208.897 170.757 159.702 1.00 86.35  ? 1899 ARG A N     1 
ATOM   2268  C CA    . ARG A 1 1899 ? 207.900 170.957 158.653 1.00 86.35  ? 1899 ARG A CA    1 
ATOM   2269  C C     . ARG A 1 1899 ? 206.665 170.098 158.897 1.00 86.35  ? 1899 ARG A C     1 
ATOM   2270  O O     . ARG A 1 1899 ? 206.186 169.396 158.006 1.00 86.35  ? 1899 ARG A O     1 
ATOM   2271  C CB    . ARG A 1 1899 ? 208.493 170.686 157.272 1.00 86.35  ? 1899 ARG A CB    1 
ATOM   2272  C CG    . ARG A 1 1899 ? 209.724 171.511 156.977 1.00 86.35  ? 1899 ARG A CG    1 
ATOM   2273  C CD    . ARG A 1 1899 ? 209.351 172.914 156.540 1.00 86.35  ? 1899 ARG A CD    1 
ATOM   2274  N NE    . ARG A 1 1899 ? 210.400 173.877 156.848 1.00 86.35  ? 1899 ARG A NE    1 
ATOM   2275  C CZ    . ARG A 1 1899 ? 210.211 175.186 156.941 1.00 86.35  ? 1899 ARG A CZ    1 
ATOM   2276  N NH1   . ARG A 1 1899 ? 209.019 175.727 156.748 1.00 86.35  ? 1899 ARG A NH1   1 
ATOM   2277  N NH2   . ARG A 1 1899 ? 211.242 175.971 157.236 1.00 86.35  ? 1899 ARG A NH2   1 
ATOM   2278  N N     . LEU A 1 1900 ? 206.150 170.152 160.117 1.00 82.77  ? 1900 LEU A N     1 
ATOM   2279  C CA    . LEU A 1 1900 ? 204.988 169.377 160.513 1.00 82.77  ? 1900 LEU A CA    1 
ATOM   2280  C C     . LEU A 1 1900 ? 203.878 170.313 160.969 1.00 82.77  ? 1900 LEU A C     1 
ATOM   2281  O O     . LEU A 1 1900 ? 204.104 171.486 161.272 1.00 82.77  ? 1900 LEU A O     1 
ATOM   2282  C CB    . LEU A 1 1900 ? 205.358 168.395 161.627 1.00 82.77  ? 1900 LEU A CB    1 
ATOM   2283  C CG    . LEU A 1 1900 ? 205.892 167.053 161.128 1.00 82.77  ? 1900 LEU A CG    1 
ATOM   2284  C CD1   . LEU A 1 1900 ? 206.607 166.327 162.240 1.00 82.77  ? 1900 LEU A CD1   1 
ATOM   2285  C CD2   . LEU A 1 1900 ? 204.786 166.194 160.568 1.00 82.77  ? 1900 LEU A CD2   1 
ATOM   2286  N N     . GLY A 1 1901 ? 202.665 169.780 161.014 1.00 84.37  ? 1901 GLY A N     1 
ATOM   2287  C CA    . GLY A 1 1901 ? 201.517 170.535 161.455 1.00 84.37  ? 1901 GLY A CA    1 
ATOM   2288  C C     . GLY A 1 1901 ? 201.402 170.543 162.966 1.00 84.37  ? 1901 GLY A C     1 
ATOM   2289  O O     . GLY A 1 1901 ? 201.911 169.662 163.652 1.00 84.37  ? 1901 GLY A O     1 
ATOM   2290  N N     . GLY A 1 1902 ? 200.723 171.562 163.482 1.00 76.00  ? 1902 GLY A N     1 
ATOM   2291  C CA    . GLY A 1 1902 ? 200.512 171.719 164.909 1.00 76.00  ? 1902 GLY A CA    1 
ATOM   2292  C C     . GLY A 1 1902 ? 199.031 171.643 165.238 1.00 76.00  ? 1902 GLY A C     1 
ATOM   2293  O O     . GLY A 1 1902 ? 198.218 172.352 164.643 1.00 76.00  ? 1902 GLY A O     1 
ATOM   2294  N N     . SER A 1 1903 ? 198.698 170.778 166.190 1.00 76.83  ? 1903 SER A N     1 
ATOM   2295  C CA    . SER A 1 1903 ? 197.312 170.528 166.580 1.00 76.83  ? 1903 SER A CA    1 
ATOM   2296  C C     . SER A 1 1903 ? 197.185 170.659 168.089 1.00 76.83  ? 1903 SER A C     1 
ATOM   2297  O O     . SER A 1 1903 ? 197.159 169.657 168.814 1.00 76.83  ? 1903 SER A O     1 
ATOM   2298  C CB    . SER A 1 1903 ? 196.845 169.152 166.108 1.00 76.83  ? 1903 SER A CB    1 
ATOM   2299  O OG    . SER A 1 1903 ? 196.902 168.212 167.162 1.00 76.83  ? 1903 SER A OG    1 
ATOM   2300  N N     . PRO A 1 1904 ? 197.102 171.876 168.595 1.00 73.22  ? 1904 PRO A N     1 
ATOM   2301  C CA    . PRO A 1 1904 ? 196.964 172.080 170.047 1.00 73.22  ? 1904 PRO A CA    1 
ATOM   2302  C C     . PRO A 1 1904 ? 195.548 171.799 170.539 1.00 73.22  ? 1904 PRO A C     1 
ATOM   2303  O O     . PRO A 1 1904 ? 194.760 172.685 170.848 1.00 73.22  ? 1904 PRO A O     1 
ATOM   2304  C CB    . PRO A 1 1904 ? 197.350 173.550 170.213 1.00 73.22  ? 1904 PRO A CB    1 
ATOM   2305  C CG    . PRO A 1 1904 ? 196.946 174.176 168.933 1.00 73.22  ? 1904 PRO A CG    1 
ATOM   2306  C CD    . PRO A 1 1904 ? 197.158 173.149 167.860 1.00 73.22  ? 1904 PRO A CD    1 
ATOM   2307  N N     . PHE A 1 1905 ? 195.212 170.516 170.623 1.00 77.33  ? 1905 PHE A N     1 
ATOM   2308  C CA    . PHE A 1 1905 ? 193.874 170.128 171.032 1.00 77.33  ? 1905 PHE A CA    1 
ATOM   2309  C C     . PHE A 1 1905 ? 193.652 170.426 172.510 1.00 77.33  ? 1905 PHE A C     1 
ATOM   2310  O O     . PHE A 1 1905 ? 194.592 170.524 173.301 1.00 77.33  ? 1905 PHE A O     1 
ATOM   2311  C CB    . PHE A 1 1905 ? 193.637 168.644 170.762 1.00 77.33  ? 1905 PHE A CB    1 
ATOM   2312  C CG    . PHE A 1 1905 ? 194.398 167.729 171.680 1.00 77.33  ? 1905 PHE A CG    1 
ATOM   2313  C CD1   . PHE A 1 1905 ? 195.689 167.344 171.378 1.00 77.33  ? 1905 PHE A CD1   1 
ATOM   2314  C CD2   . PHE A 1 1905 ? 193.815 167.240 172.837 1.00 77.33  ? 1905 PHE A CD2   1 
ATOM   2315  C CE1   . PHE A 1 1905 ? 196.386 166.500 172.214 1.00 77.33  ? 1905 PHE A CE1   1 
ATOM   2316  C CE2   . PHE A 1 1905 ? 194.510 166.397 173.675 1.00 77.33  ? 1905 PHE A CE2   1 
ATOM   2317  C CZ    . PHE A 1 1905 ? 195.793 166.025 173.361 1.00 77.33  ? 1905 PHE A CZ    1 
ATOM   2318  N N     . GLY A 1 1906 ? 192.379 170.569 172.890 1.00 83.33  ? 1906 GLY A N     1 
ATOM   2319  C CA    . GLY A 1 1906 ? 192.051 170.847 174.302 1.00 83.33  ? 1906 GLY A CA    1 
ATOM   2320  C C     . GLY A 1 1906 ? 190.643 171.393 174.462 1.00 83.33  ? 1906 GLY A C     1 
ATOM   2321  O O     . GLY A 1 1906 ? 190.016 171.728 173.439 1.00 83.33  ? 1906 GLY A O     1 
ATOM   2322  N N     . PRO A 1 1907 ? 190.118 171.505 175.701 1.00 88.89  ? 1907 PRO A N     1 
ATOM   2323  C CA    . PRO A 1 1907 ? 188.784 172.061 175.935 1.00 88.89  ? 1907 PRO A CA    1 
ATOM   2324  C C     . PRO A 1 1907 ? 188.707 173.505 175.424 1.00 88.89  ? 1907 PRO A C     1 
ATOM   2325  O O     . PRO A 1 1907 ? 189.674 174.224 175.573 1.00 88.89  ? 1907 PRO A O     1 
ATOM   2326  C CB    . PRO A 1 1907 ? 188.642 172.052 177.463 1.00 88.89  ? 1907 PRO A CB    1 
ATOM   2327  C CG    . PRO A 1 1907 ? 189.637 171.012 177.928 1.00 88.89  ? 1907 PRO A CG    1 
ATOM   2328  C CD    . PRO A 1 1907 ? 190.782 171.104 176.942 1.00 88.89  ? 1907 PRO A CD    1 
ATOM   2329  N N     . ALA A 1 1908 ? 187.567 173.892 174.847 1.00 92.46  ? 1908 ALA A N     1 
ATOM   2330  C CA    . ALA A 1 1908 ? 187.413 175.260 174.299 1.00 92.46  ? 1908 ALA A CA    1 
ATOM   2331  C C     . ALA A 1 1908 ? 187.602 176.289 175.418 1.00 92.46  ? 1908 ALA A C     1 
ATOM   2332  O O     . ALA A 1 1908 ? 187.164 176.014 176.552 1.00 92.46  ? 1908 ALA A O     1 
ATOM   2333  C CB    . ALA A 1 1908 ? 186.063 175.400 173.644 1.00 92.46  ? 1908 ALA A CB    1 
ATOM   2334  N N     . GLY A 1 1909 ? 188.229 177.428 175.107 1.00 86.24  ? 1909 GLY A N     1 
ATOM   2335  C CA    . GLY A 1 1909 ? 188.421 178.495 176.109 1.00 86.24  ? 1909 GLY A CA    1 
ATOM   2336  C C     . GLY A 1 1909 ? 189.705 178.314 176.901 1.00 86.24  ? 1909 GLY A C     1 
ATOM   2337  O O     . GLY A 1 1909 ? 189.931 179.100 177.840 1.00 86.24  ? 1909 GLY A O     1 
ATOM   2338  N N     . THR A 1 1910 ? 190.517 177.317 176.537 1.00 82.07  ? 1910 THR A N     1 
ATOM   2339  C CA    . THR A 1 1910 ? 191.785 177.047 177.264 1.00 82.07  ? 1910 THR A CA    1 
ATOM   2340  C C     . THR A 1 1910 ? 192.912 177.888 176.657 1.00 82.07  ? 1910 THR A C     1 
ATOM   2341  O O     . THR A 1 1910 ? 194.048 177.795 177.161 1.00 82.07  ? 1910 THR A O     1 
ATOM   2342  C CB    . THR A 1 1910 ? 192.145 175.558 177.214 1.00 82.07  ? 1910 THR A CB    1 
ATOM   2343  O OG1   . THR A 1 1910 ? 193.256 175.343 178.084 1.00 82.07  ? 1910 THR A OG1   1 
ATOM   2344  C CG2   . THR A 1 1910 ? 192.483 175.091 175.816 1.00 82.07  ? 1910 THR A CG2   1 
ATOM   2345  N N     . GLY A 1 1911 ? 192.605 178.674 175.622 1.00 80.41  ? 1911 GLY A N     1 
ATOM   2346  C CA    . GLY A 1 1911 ? 193.638 179.481 174.944 1.00 80.41  ? 1911 GLY A CA    1 
ATOM   2347  C C     . GLY A 1 1911 ? 194.396 178.660 173.917 1.00 80.41  ? 1911 GLY A C     1 
ATOM   2348  O O     . GLY A 1 1911 ? 195.552 178.291 174.196 1.00 80.41  ? 1911 GLY A O     1 
ATOM   2349  N N     . LYS A 1 1912 ? 193.766 178.379 172.772 1.00 84.60  ? 1912 LYS A N     1 
ATOM   2350  C CA    . LYS A 1 1912 ? 194.413 177.563 171.711 1.00 84.60  ? 1912 LYS A CA    1 
ATOM   2351  C C     . LYS A 1 1912 ? 194.593 178.416 170.451 1.00 84.60  ? 1912 LYS A C     1 
ATOM   2352  O O     . LYS A 1 1912 ? 195.752 178.639 170.054 1.00 84.60  ? 1912 LYS A O     1 
ATOM   2353  C CB    . LYS A 1 1912 ? 193.568 176.321 171.409 1.00 84.60  ? 1912 LYS A CB    1 
ATOM   2354  C CG    . LYS A 1 1912 ? 193.404 175.347 172.568 1.00 84.60  ? 1912 LYS A CG    1 
ATOM   2355  C CD    . LYS A 1 1912 ? 192.551 174.142 172.234 1.00 84.60  ? 1912 LYS A CD    1 
ATOM   2356  C CE    . LYS A 1 1912 ? 191.113 174.492 171.916 1.00 84.60  ? 1912 LYS A CE    1 
ATOM   2357  N NZ    . LYS A 1 1912 ? 190.400 175.017 173.104 1.00 84.60  ? 1912 LYS A NZ    1 
ATOM   2358  N N     . THR A 1 1913 ? 193.490 178.880 169.856 1.00 87.29  ? 1913 THR A N     1 
ATOM   2359  C CA    . THR A 1 1913 ? 193.571 179.654 168.588 1.00 87.29  ? 1913 THR A CA    1 
ATOM   2360  C C     . THR A 1 1913 ? 194.389 180.931 168.808 1.00 87.29  ? 1913 THR A C     1 
ATOM   2361  O O     . THR A 1 1913 ? 195.305 181.187 168.004 1.00 87.29  ? 1913 THR A O     1 
ATOM   2362  C CB    . THR A 1 1913 ? 192.171 179.973 168.049 1.00 87.29  ? 1913 THR A CB    1 
ATOM   2363  O OG1   . THR A 1 1913 ? 191.485 178.737 167.847 1.00 87.29  ? 1913 THR A OG1   1 
ATOM   2364  C CG2   . THR A 1 1913 ? 192.203 180.759 166.758 1.00 87.29  ? 1913 THR A CG2   1 
ATOM   2365  N N     . GLU A 1 1914 ? 194.075 181.689 169.862 1.00 83.55  ? 1914 GLU A N     1 
ATOM   2366  C CA    . GLU A 1 1914 ? 194.815 182.943 170.159 1.00 83.55  ? 1914 GLU A CA    1 
ATOM   2367  C C     . GLU A 1 1914 ? 196.292 182.597 170.356 1.00 83.55  ? 1914 GLU A C     1 
ATOM   2368  O O     . GLU A 1 1914 ? 197.146 183.332 169.827 1.00 83.55  ? 1914 GLU A O     1 
ATOM   2369  C CB    . GLU A 1 1914 ? 194.259 183.625 171.410 1.00 83.55  ? 1914 GLU A CB    1 
ATOM   2370  C CG    . GLU A 1 1914 ? 192.868 183.157 171.798 1.00 83.55  ? 1914 GLU A CG    1 
ATOM   2371  C CD    . GLU A 1 1914 ? 192.829 181.855 172.579 1.00 83.55  ? 1914 GLU A CD    1 
ATOM   2372  O OE1   . GLU A 1 1914 ? 192.370 181.879 173.734 1.00 83.55  ? 1914 GLU A OE1   1 
ATOM   2373  O OE2   . GLU A 1 1914 ? 193.250 180.820 172.028 1.00 83.55  ? 1914 GLU A OE2   1 
ATOM   2374  N N     . SER A 1 1915 ? 196.571 181.515 171.087 1.00 76.70  ? 1915 SER A N     1 
ATOM   2375  C CA    . SER A 1 1915 ? 197.976 181.073 171.283 1.00 76.70  ? 1915 SER A CA    1 
ATOM   2376  C C     . SER A 1 1915 ? 198.677 181.019 169.923 1.00 76.70  ? 1915 SER A C     1 
ATOM   2377  O O     . SER A 1 1915 ? 199.728 181.673 169.775 1.00 76.70  ? 1915 SER A O     1 
ATOM   2378  C CB    . SER A 1 1915 ? 198.030 179.744 171.986 1.00 76.70  ? 1915 SER A CB    1 
ATOM   2379  O OG    . SER A 1 1915 ? 197.376 179.815 173.243 1.00 76.70  ? 1915 SER A OG    1 
ATOM   2380  N N     . VAL A 1 1916 ? 198.105 180.279 168.968 1.00 73.37  ? 1916 VAL A N     1 
ATOM   2381  C CA    . VAL A 1 1916 ? 198.698 180.196 167.635 1.00 73.37  ? 1916 VAL A CA    1 
ATOM   2382  C C     . VAL A 1 1916 ? 198.803 181.582 167.013 1.00 73.37  ? 1916 VAL A C     1 
ATOM   2383  O O     . VAL A 1 1916 ? 199.812 181.927 166.384 1.00 73.37  ? 1916 VAL A O     1 
ATOM   2384  C CB    . VAL A 1 1916 ? 197.883 179.240 166.748 1.00 73.37  ? 1916 VAL A CB    1 
ATOM   2385  C CG1   . VAL A 1 1916 ? 198.396 179.278 165.326 1.00 73.37  ? 1916 VAL A CG1   1 
ATOM   2386  C CG2   . VAL A 1 1916 ? 197.950 177.835 167.297 1.00 73.37  ? 1916 VAL A CG2   1 
ATOM   2387  N N     . LYS A 1 1917 ? 197.762 182.396 167.180 1.00 78.63  ? 1917 LYS A N     1 
ATOM   2388  C CA    . LYS A 1 1917 ? 197.755 183.739 166.614 1.00 78.63  ? 1917 LYS A CA    1 
ATOM   2389  C C     . LYS A 1 1917 ? 198.862 184.596 167.210 1.00 78.63  ? 1917 LYS A C     1 
ATOM   2390  O O     . LYS A 1 1917 ? 199.518 185.360 166.497 1.00 78.63  ? 1917 LYS A O     1 
ATOM   2391  C CB    . LYS A 1 1917 ? 196.388 184.379 166.845 1.00 78.63  ? 1917 LYS A CB    1 
ATOM   2392  C CG    . LYS A 1 1917 ? 196.289 185.832 166.449 1.00 78.63  ? 1917 LYS A CG    1 
ATOM   2393  C CD    . LYS A 1 1917 ? 194.956 186.411 166.887 1.00 78.63  ? 1917 LYS A CD    1 
ATOM   2394  C CE    . LYS A 1 1917 ? 193.795 185.675 166.243 1.00 78.63  ? 1917 LYS A CE    1 
ATOM   2395  N NZ    . LYS A 1 1917 ? 194.024 185.441 164.794 1.00 78.63  ? 1917 LYS A NZ    1 
ATOM   2396  N N     . ALA A 1 1918 ? 199.086 184.485 168.518 1.00 77.91  ? 1918 ALA A N     1 
ATOM   2397  C CA    . ALA A 1 1918 ? 200.142 185.254 169.158 1.00 77.91  ? 1918 ALA A CA    1 
ATOM   2398  C C     . ALA A 1 1918 ? 201.516 184.737 168.777 1.00 77.91  ? 1918 ALA A C     1 
ATOM   2399  O O     . ALA A 1 1918 ? 202.464 185.522 168.689 1.00 77.91  ? 1918 ALA A O     1 
ATOM   2400  C CB    . ALA A 1 1918 ? 199.974 185.224 170.671 1.00 77.91  ? 1918 ALA A CB    1 
ATOM   2401  N N     . LEU A 1 1919 ? 201.653 183.429 168.564 1.00 74.28  ? 1919 LEU A N     1 
ATOM   2402  C CA    . LEU A 1 1919 ? 202.910 182.922 168.028 1.00 74.28  ? 1919 LEU A CA    1 
ATOM   2403  C C     . LEU A 1 1919 ? 203.185 183.514 166.654 1.00 74.28  ? 1919 LEU A C     1 
ATOM   2404  O O     . LEU A 1 1919 ? 204.310 183.932 166.361 1.00 74.28  ? 1919 LEU A O     1 
ATOM   2405  C CB    . LEU A 1 1919 ? 202.885 181.400 167.956 1.00 74.28  ? 1919 LEU A CB    1 
ATOM   2406  C CG    . LEU A 1 1919 ? 204.081 180.807 167.220 1.00 74.28  ? 1919 LEU A CG    1 
ATOM   2407  C CD1   . LEU A 1 1919 ? 205.336 180.979 168.045 1.00 74.28  ? 1919 LEU A CD1   1 
ATOM   2408  C CD2   . LEU A 1 1919 ? 203.842 179.350 166.911 1.00 74.28  ? 1919 LEU A CD2   1 
ATOM   2409  N N     . GLY A 1 1920 ? 202.160 183.571 165.805 1.00 79.93  ? 1920 GLY A N     1 
ATOM   2410  C CA    . GLY A 1 1920 ? 202.330 184.188 164.500 1.00 79.93  ? 1920 GLY A CA    1 
ATOM   2411  C C     . GLY A 1 1920 ? 202.667 185.664 164.596 1.00 79.93  ? 1920 GLY A C     1 
ATOM   2412  O O     . GLY A 1 1920 ? 203.527 186.164 163.869 1.00 79.93  ? 1920 GLY A O     1 
ATOM   2413  N N     . HIS A 1 1921 ? 201.995 186.378 165.499 1.00 84.03  ? 1921 HIS A N     1 
ATOM   2414  C CA    . HIS A 1 1921 ? 202.301 187.786 165.709 1.00 84.03  ? 1921 HIS A CA    1 
ATOM   2415  C C     . HIS A 1 1921 ? 203.728 187.972 166.191 1.00 84.03  ? 1921 HIS A C     1 
ATOM   2416  O O     . HIS A 1 1921 ? 204.380 188.963 165.844 1.00 84.03  ? 1921 HIS A O     1 
ATOM   2417  C CB    . HIS A 1 1921 ? 201.331 188.394 166.719 1.00 84.03  ? 1921 HIS A CB    1 
ATOM   2418  C CG    . HIS A 1 1921 ? 199.919 188.473 166.232 1.00 84.03  ? 1921 HIS A CG    1 
ATOM   2419  N ND1   . HIS A 1 1921 ? 199.548 188.098 164.960 1.00 84.03  ? 1921 HIS A ND1   1 
ATOM   2420  C CD2   . HIS A 1 1921 ? 198.790 188.898 166.844 1.00 84.03  ? 1921 HIS A CD2   1 
ATOM   2421  C CE1   . HIS A 1 1921 ? 198.249 188.286 164.810 1.00 84.03  ? 1921 HIS A CE1   1 
ATOM   2422  N NE2   . HIS A 1 1921 ? 197.765 188.770 165.939 1.00 84.03  ? 1921 HIS A NE2   1 
ATOM   2423  N N     . GLN A 1 1922 ? 204.224 187.038 167.000 1.00 85.14  ? 1922 GLN A N     1 
ATOM   2424  C CA    . GLN A 1 1922 ? 205.595 187.129 167.478 1.00 85.14  ? 1922 GLN A CA    1 
ATOM   2425  C C     . GLN A 1 1922 ? 206.583 187.034 166.326 1.00 85.14  ? 1922 GLN A C     1 
ATOM   2426  O O     . GLN A 1 1922 ? 207.584 187.757 166.297 1.00 85.14  ? 1922 GLN A O     1 
ATOM   2427  C CB    . GLN A 1 1922 ? 205.863 186.034 168.503 1.00 85.14  ? 1922 GLN A CB    1 
ATOM   2428  C CG    . GLN A 1 1922 ? 207.192 186.178 169.197 1.00 85.14  ? 1922 GLN A CG    1 
ATOM   2429  C CD    . GLN A 1 1922 ? 207.536 187.622 169.472 1.00 85.14  ? 1922 GLN A CD    1 
ATOM   2430  O OE1   . GLN A 1 1922 ? 208.468 188.172 168.888 1.00 85.14  ? 1922 GLN A OE1   1 
ATOM   2431  N NE2   . GLN A 1 1922 ? 206.782 188.247 170.365 1.00 85.14  ? 1922 GLN A NE2   1 
ATOM   2432  N N     . LEU A 1 1923 ? 206.321 186.152 165.369 1.00 81.73  ? 1923 LEU A N     1 
ATOM   2433  C CA    . LEU A 1 1923 ? 207.194 185.989 164.217 1.00 81.73  ? 1923 LEU A CA    1 
ATOM   2434  C C     . LEU A 1 1923 ? 206.883 186.970 163.097 1.00 81.73  ? 1923 LEU A C     1 
ATOM   2435  O O     . LEU A 1 1923 ? 207.566 186.951 162.069 1.00 81.73  ? 1923 LEU A O     1 
ATOM   2436  C CB    . LEU A 1 1923 ? 207.108 184.557 163.686 1.00 81.73  ? 1923 LEU A CB    1 
ATOM   2437  C CG    . LEU A 1 1923 ? 207.985 183.525 164.393 1.00 81.73  ? 1923 LEU A CG    1 
ATOM   2438  C CD1   . LEU A 1 1923 ? 207.345 183.072 165.686 1.00 81.73  ? 1923 LEU A CD1   1 
ATOM   2439  C CD2   . LEU A 1 1923 ? 208.242 182.340 163.489 1.00 81.73  ? 1923 LEU A CD2   1 
ATOM   2440  N N     . GLY A 1 1924 ? 205.887 187.830 163.273 1.00 85.28  ? 1924 GLY A N     1 
ATOM   2441  C CA    . GLY A 1 1924 ? 205.537 188.781 162.235 1.00 85.28  ? 1924 GLY A CA    1 
ATOM   2442  C C     . GLY A 1 1924 ? 204.971 188.147 160.985 1.00 85.28  ? 1924 GLY A C     1 
ATOM   2443  O O     . GLY A 1 1924 ? 205.306 188.571 159.874 1.00 85.28  ? 1924 GLY A O     1 
ATOM   2444  N N     . ARG A 1 1925 ? 204.121 187.138 161.138 1.00 83.60  ? 1925 ARG A N     1 
ATOM   2445  C CA    . ARG A 1 1925 ? 203.481 186.468 160.018 1.00 83.60  ? 1925 ARG A CA    1 
ATOM   2446  C C     . ARG A 1 1925 ? 201.982 186.714 160.072 1.00 83.60  ? 1925 ARG A C     1 
ATOM   2447  O O     . ARG A 1 1925 ? 201.368 186.621 161.138 1.00 83.60  ? 1925 ARG A O     1 
ATOM   2448  C CB    . ARG A 1 1925 ? 203.755 184.966 160.045 1.00 83.60  ? 1925 ARG A CB    1 
ATOM   2449  C CG    . ARG A 1 1925 ? 205.221 184.611 160.085 1.00 83.60  ? 1925 ARG A CG    1 
ATOM   2450  C CD    . ARG A 1 1925 ? 205.950 185.171 158.883 1.00 83.60  ? 1925 ARG A CD    1 
ATOM   2451  N NE    . ARG A 1 1925 ? 207.379 184.885 158.924 1.00 83.60  ? 1925 ARG A NE    1 
ATOM   2452  C CZ    . ARG A 1 1925 ? 207.911 183.673 158.851 1.00 83.60  ? 1925 ARG A CZ    1 
ATOM   2453  N NH1   . ARG A 1 1925 ? 207.161 182.592 158.715 1.00 83.60  ? 1925 ARG A NH1   1 
ATOM   2454  N NH2   . ARG A 1 1925 ? 209.233 183.541 158.912 1.00 83.60  ? 1925 ARG A NH2   1 
ATOM   2455  N N     . PHE A 1 1926 ? 201.400 187.036 158.922 1.00 89.53  ? 1926 PHE A N     1 
ATOM   2456  C CA    . PHE A 1 1926 ? 199.954 187.170 158.837 1.00 89.53  ? 1926 PHE A CA    1 
ATOM   2457  C C     . PHE A 1 1926 ? 199.296 185.851 159.211 1.00 89.53  ? 1926 PHE A C     1 
ATOM   2458  O O     . PHE A 1 1926 ? 199.682 184.790 158.716 1.00 89.53  ? 1926 PHE A O     1 
ATOM   2459  C CB    . PHE A 1 1926 ? 199.553 187.588 157.424 1.00 89.53  ? 1926 PHE A CB    1 
ATOM   2460  C CG    . PHE A 1 1926 ? 198.084 187.829 157.251 1.00 89.53  ? 1926 PHE A CG    1 
ATOM   2461  C CD1   . PHE A 1 1926 ? 197.314 188.294 158.298 1.00 89.53  ? 1926 PHE A CD1   1 
ATOM   2462  C CD2   . PHE A 1 1926 ? 197.475 187.594 156.034 1.00 89.53  ? 1926 PHE A CD2   1 
ATOM   2463  C CE1   . PHE A 1 1926 ? 195.964 188.517 158.135 1.00 89.53  ? 1926 PHE A CE1   1 
ATOM   2464  C CE2   . PHE A 1 1926 ? 196.127 187.816 155.866 1.00 89.53  ? 1926 PHE A CE2   1 
ATOM   2465  C CZ    . PHE A 1 1926 ? 195.371 188.278 156.918 1.00 89.53  ? 1926 PHE A CZ    1 
ATOM   2466  N N     . VAL A 1 1927 ? 198.305 185.915 160.093 1.00 79.43  ? 1927 VAL A N     1 
ATOM   2467  C CA    . VAL A 1 1927 ? 197.601 184.732 160.566 1.00 79.43  ? 1927 VAL A CA    1 
ATOM   2468  C C     . VAL A 1 1927 ? 196.124 184.884 160.234 1.00 79.43  ? 1927 VAL A C     1 
ATOM   2469  O O     . VAL A 1 1927 ? 195.536 185.949 160.453 1.00 79.43  ? 1927 VAL A O     1 
ATOM   2470  C CB    . VAL A 1 1927 ? 197.814 184.506 162.074 1.00 79.43  ? 1927 VAL A CB    1 
ATOM   2471  C CG1   . VAL A 1 1927 ? 197.362 185.712 162.865 1.00 79.43  ? 1927 VAL A CG1   1 
ATOM   2472  C CG2   . VAL A 1 1927 ? 197.082 183.261 162.529 1.00 79.43  ? 1927 VAL A CG2   1 
ATOM   2473  N N     . LEU A 1 1928 ? 195.538 183.829 159.681 1.00 84.96  ? 1928 LEU A N     1 
ATOM   2474  C CA    . LEU A 1 1928 ? 194.132 183.805 159.313 1.00 84.96  ? 1928 LEU A CA    1 
ATOM   2475  C C     . LEU A 1 1928 ? 193.418 182.759 160.152 1.00 84.96  ? 1928 LEU A C     1 
ATOM   2476  O O     . LEU A 1 1928 ? 193.964 181.684 160.412 1.00 84.96  ? 1928 LEU A O     1 
ATOM   2477  C CB    . LEU A 1 1928 ? 193.960 183.497 157.826 1.00 84.96  ? 1928 LEU A CB    1 
ATOM   2478  C CG    . LEU A 1 1928 ? 193.839 184.701 156.896 1.00 84.96  ? 1928 LEU A CG    1 
ATOM   2479  C CD1   . LEU A 1 1928 ? 193.286 184.276 155.553 1.00 84.96  ? 1928 LEU A CD1   1 
ATOM   2480  C CD2   . LEU A 1 1928 ? 192.957 185.764 157.518 1.00 84.96  ? 1928 LEU A CD2   1 
ATOM   2481  N N     . VAL A 1 1929 ? 192.203 183.076 160.584 1.00 87.18  ? 1929 VAL A N     1 
ATOM   2482  C CA    . VAL A 1 1929 ? 191.410 182.182 161.417 1.00 87.18  ? 1929 VAL A CA    1 
ATOM   2483  C C     . VAL A 1 1929 ? 190.145 181.824 160.654 1.00 87.18  ? 1929 VAL A C     1 
ATOM   2484  O O     . VAL A 1 1929 ? 189.431 182.712 160.173 1.00 87.18  ? 1929 VAL A O     1 
ATOM   2485  C CB    . VAL A 1 1929 ? 191.076 182.820 162.772 1.00 87.18  ? 1929 VAL A CB    1 
ATOM   2486  C CG1   . VAL A 1 1929 ? 190.011 182.012 163.486 1.00 87.18  ? 1929 VAL A CG1   1 
ATOM   2487  C CG2   . VAL A 1 1929 ? 192.322 182.922 163.618 1.00 87.18  ? 1929 VAL A CG2   1 
ATOM   2488  N N     . PHE A 1 1930 ? 189.870 180.529 160.536 1.00 92.13  ? 1930 PHE A N     1 
ATOM   2489  C CA    . PHE A 1 1930 ? 188.674 180.030 159.861 1.00 92.13  ? 1930 PHE A CA    1 
ATOM   2490  C C     . PHE A 1 1930 ? 187.793 179.354 160.907 1.00 92.13  ? 1930 PHE A C     1 
ATOM   2491  O O     . PHE A 1 1930 ? 188.002 178.193 161.257 1.00 92.13  ? 1930 PHE A O     1 
ATOM   2492  C CB    . PHE A 1 1930 ? 189.023 179.061 158.738 1.00 92.13  ? 1930 PHE A CB    1 
ATOM   2493  C CG    . PHE A 1 1930 ? 190.288 179.396 158.015 1.00 92.13  ? 1930 PHE A CG    1 
ATOM   2494  C CD1   . PHE A 1 1930 ? 190.499 180.661 157.508 1.00 92.13  ? 1930 PHE A CD1   1 
ATOM   2495  C CD2   . PHE A 1 1930 ? 191.263 178.436 157.832 1.00 92.13  ? 1930 PHE A CD2   1 
ATOM   2496  C CE1   . PHE A 1 1930 ? 191.663 180.963 156.844 1.00 92.13  ? 1930 PHE A CE1   1 
ATOM   2497  C CE2   . PHE A 1 1930 ? 192.428 178.732 157.166 1.00 92.13  ? 1930 PHE A CE2   1 
ATOM   2498  C CZ    . PHE A 1 1930 ? 192.628 179.997 156.670 1.00 92.13  ? 1930 PHE A CZ    1 
ATOM   2499  N N     . ASN A 1 1931 ? 186.803 180.087 161.403 1.00 112.52 ? 1931 ASN A N     1 
ATOM   2500  C CA    . ASN A 1 1931 ? 185.827 179.485 162.296 1.00 112.52 ? 1931 ASN A CA    1 
ATOM   2501  C C     . ASN A 1 1931 ? 184.976 178.482 161.527 1.00 112.52 ? 1931 ASN A C     1 
ATOM   2502  O O     . ASN A 1 1931 ? 184.777 178.602 160.316 1.00 112.52 ? 1931 ASN A O     1 
ATOM   2503  C CB    . ASN A 1 1931 ? 184.946 180.559 162.929 1.00 112.52 ? 1931 ASN A CB    1 
ATOM   2504  C CG    . ASN A 1 1931 ? 184.196 180.055 164.147 1.00 112.52 ? 1931 ASN A CG    1 
ATOM   2505  O OD1   . ASN A 1 1931 ? 183.821 178.886 164.221 1.00 112.52 ? 1931 ASN A OD1   1 
ATOM   2506  N ND2   . ASN A 1 1931 ? 183.976 180.939 165.112 1.00 112.52 ? 1931 ASN A ND2   1 
ATOM   2507  N N     . CYS A 1 1932 ? 184.477 177.474 162.242 1.00 115.35 ? 1932 CYS A N     1 
ATOM   2508  C CA    . CYS A 1 1932 ? 183.745 176.377 161.620 1.00 115.35 ? 1932 CYS A CA    1 
ATOM   2509  C C     . CYS A 1 1932 ? 182.283 176.333 162.050 1.00 115.35 ? 1932 CYS A C     1 
ATOM   2510  O O     . CYS A 1 1932 ? 181.629 175.297 161.900 1.00 115.35 ? 1932 CYS A O     1 
ATOM   2511  C CB    . CYS A 1 1932 ? 184.429 175.047 161.931 1.00 115.35 ? 1932 CYS A CB    1 
ATOM   2512  S SG    . CYS A 1 1932 ? 186.142 174.956 161.372 1.00 115.35 ? 1932 CYS A SG    1 
ATOM   2513  N N     . ASP A 1 1933 ? 181.751 177.438 162.571 1.00 127.26 ? 1933 ASP A N     1 
ATOM   2514  C CA    . ASP A 1 1933 ? 180.384 177.478 163.090 1.00 127.26 ? 1933 ASP A CA    1 
ATOM   2515  C C     . ASP A 1 1933 ? 179.376 177.701 161.960 1.00 127.26 ? 1933 ASP A C     1 
ATOM   2516  O O     . ASP A 1 1933 ? 178.633 178.682 161.927 1.00 127.26 ? 1933 ASP A O     1 
ATOM   2517  C CB    . ASP A 1 1933 ? 180.268 178.556 164.158 1.00 127.26 ? 1933 ASP A CB    1 
ATOM   2518  C CG    . ASP A 1 1933 ? 180.905 179.865 163.736 1.00 127.26 ? 1933 ASP A CG    1 
ATOM   2519  O OD1   . ASP A 1 1933 ? 181.187 180.031 162.530 1.00 127.26 ? 1933 ASP A OD1   1 
ATOM   2520  O OD2   . ASP A 1 1933 ? 181.134 180.726 164.611 1.00 127.26 ? 1933 ASP A OD2   1 
ATOM   2521  N N     . GLU A 1 1934 ? 179.381 176.766 161.009 1.00 130.89 ? 1934 GLU A N     1 
ATOM   2522  C CA    . GLU A 1 1934 ? 178.525 176.740 159.825 1.00 130.89 ? 1934 GLU A CA    1 
ATOM   2523  C C     . GLU A 1 1934 ? 178.831 177.867 158.850 1.00 130.89 ? 1934 GLU A C     1 
ATOM   2524  O O     . GLU A 1 1934 ? 178.235 177.908 157.767 1.00 130.89 ? 1934 GLU A O     1 
ATOM   2525  C CB    . GLU A 1 1934 ? 177.031 176.775 160.175 1.00 130.89 ? 1934 GLU A CB    1 
ATOM   2526  C CG    . GLU A 1 1934 ? 176.537 175.515 160.851 1.00 130.89 ? 1934 GLU A CG    1 
ATOM   2527  C CD    . GLU A 1 1934 ? 176.961 174.267 160.105 1.00 130.89 ? 1934 GLU A CD    1 
ATOM   2528  O OE1   . GLU A 1 1934 ? 176.619 174.144 158.911 1.00 130.89 ? 1934 GLU A OE1   1 
ATOM   2529  O OE2   . GLU A 1 1934 ? 177.642 173.414 160.709 1.00 130.89 ? 1934 GLU A OE2   1 
ATOM   2530  N N     . THR A 1 1935 ? 179.741 178.777 159.186 1.00 129.82 ? 1935 THR A N     1 
ATOM   2531  C CA    . THR A 1 1935 ? 180.185 179.814 158.258 1.00 129.82 ? 1935 THR A CA    1 
ATOM   2532  C C     . THR A 1 1935 ? 181.336 179.272 157.410 1.00 129.82 ? 1935 THR A C     1 
ATOM   2533  O O     . THR A 1 1935 ? 182.450 179.794 157.385 1.00 129.82 ? 1935 THR A O     1 
ATOM   2534  C CB    . THR A 1 1935 ? 180.589 181.069 159.023 1.00 129.82 ? 1935 THR A CB    1 
ATOM   2535  O OG1   . THR A 1 1935 ? 179.627 181.330 160.054 1.00 129.82 ? 1935 THR A OG1   1 
ATOM   2536  C CG2   . THR A 1 1935 ? 180.647 182.271 158.090 1.00 129.82 ? 1935 THR A CG2   1 
ATOM   2537  N N     . PHE A 1 1936 ? 181.036 178.184 156.708 1.00 126.87 ? 1936 PHE A N     1 
ATOM   2538  C CA    . PHE A 1 1936 ? 182.048 177.368 156.061 1.00 126.87 ? 1936 PHE A CA    1 
ATOM   2539  C C     . PHE A 1 1936 ? 181.717 177.200 154.587 1.00 126.87 ? 1936 PHE A C     1 
ATOM   2540  O O     . PHE A 1 1936 ? 180.558 177.015 154.210 1.00 126.87 ? 1936 PHE A O     1 
ATOM   2541  C CB    . PHE A 1 1936 ? 182.142 175.998 156.732 1.00 126.87 ? 1936 PHE A CB    1 
ATOM   2542  C CG    . PHE A 1 1936 ? 183.538 175.490 156.876 1.00 126.87 ? 1936 PHE A CG    1 
ATOM   2543  C CD1   . PHE A 1 1936 ? 184.359 175.976 157.876 1.00 126.87 ? 1936 PHE A CD1   1 
ATOM   2544  C CD2   . PHE A 1 1936 ? 184.028 174.518 156.025 1.00 126.87 ? 1936 PHE A CD2   1 
ATOM   2545  C CE1   . PHE A 1 1936 ? 185.645 175.511 158.021 1.00 126.87 ? 1936 PHE A CE1   1 
ATOM   2546  C CE2   . PHE A 1 1936 ? 185.314 174.046 156.166 1.00 126.87 ? 1936 PHE A CE2   1 
ATOM   2547  C CZ    . PHE A 1 1936 ? 186.123 174.542 157.168 1.00 126.87 ? 1936 PHE A CZ    1 
ATOM   2548  N N     . ASP A 1 1937 ? 182.752 177.258 153.755 1.00 119.55 ? 1937 ASP A N     1 
ATOM   2549  C CA    . ASP A 1 1937 ? 182.575 177.088 152.322 1.00 119.55 ? 1937 ASP A CA    1 
ATOM   2550  C C     . ASP A 1 1937 ? 183.879 176.592 151.723 1.00 119.55 ? 1937 ASP A C     1 
ATOM   2551  O O     . ASP A 1 1937 ? 184.950 176.735 152.316 1.00 119.55 ? 1937 ASP A O     1 
ATOM   2552  C CB    . ASP A 1 1937 ? 182.123 178.390 151.654 1.00 119.55 ? 1937 ASP A CB    1 
ATOM   2553  C CG    . ASP A 1 1937 ? 183.101 179.529 151.869 1.00 119.55 ? 1937 ASP A CG    1 
ATOM   2554  O OD1   . ASP A 1 1937 ? 184.070 179.358 152.636 1.00 119.55 ? 1937 ASP A OD1   1 
ATOM   2555  O OD2   . ASP A 1 1937 ? 182.896 180.604 151.268 1.00 119.55 ? 1937 ASP A OD2   1 
ATOM   2556  N N     . PHE A 1 1938 ? 183.772 176.002 150.535 1.00 123.58 ? 1938 PHE A N     1 
ATOM   2557  C CA    . PHE A 1 1938 ? 184.925 175.480 149.814 1.00 123.58 ? 1938 PHE A CA    1 
ATOM   2558  C C     . PHE A 1 1938 ? 185.401 176.406 148.707 1.00 123.58 ? 1938 PHE A C     1 
ATOM   2559  O O     . PHE A 1 1938 ? 186.611 176.519 148.475 1.00 123.58 ? 1938 PHE A O     1 
ATOM   2560  C CB    . PHE A 1 1938 ? 184.596 174.108 149.220 1.00 123.58 ? 1938 PHE A CB    1 
ATOM   2561  C CG    . PHE A 1 1938 ? 185.694 173.104 149.383 1.00 123.58 ? 1938 PHE A CG    1 
ATOM   2562  C CD1   . PHE A 1 1938 ? 185.938 172.519 150.610 1.00 123.58 ? 1938 PHE A CD1   1 
ATOM   2563  C CD2   . PHE A 1 1938 ? 186.483 172.747 148.305 1.00 123.58 ? 1938 PHE A CD2   1 
ATOM   2564  C CE1   . PHE A 1 1938 ? 186.951 171.599 150.761 1.00 123.58 ? 1938 PHE A CE1   1 
ATOM   2565  C CE2   . PHE A 1 1938 ? 187.496 171.825 148.449 1.00 123.58 ? 1938 PHE A CE2   1 
ATOM   2566  C CZ    . PHE A 1 1938 ? 187.731 171.250 149.679 1.00 123.58 ? 1938 PHE A CZ    1 
ATOM   2567  N N     . GLN A 1 1939 ? 184.467 177.078 148.030 1.00 129.14 ? 1939 GLN A N     1 
ATOM   2568  C CA    . GLN A 1 1939 ? 184.821 177.965 146.928 1.00 129.14 ? 1939 GLN A CA    1 
ATOM   2569  C C     . GLN A 1 1939 ? 185.767 179.066 147.379 1.00 129.14 ? 1939 GLN A C     1 
ATOM   2570  O O     . GLN A 1 1939 ? 186.585 179.547 146.587 1.00 129.14 ? 1939 GLN A O     1 
ATOM   2571  C CB    . GLN A 1 1939 ? 183.555 178.569 146.319 1.00 129.14 ? 1939 GLN A CB    1 
ATOM   2572  C CG    . GLN A 1 1939 ? 182.348 177.636 146.317 1.00 129.14 ? 1939 GLN A CG    1 
ATOM   2573  C CD    . GLN A 1 1939 ? 181.600 177.635 147.639 1.00 129.14 ? 1939 GLN A CD    1 
ATOM   2574  O OE1   . GLN A 1 1939 ? 181.669 178.596 148.404 1.00 129.14 ? 1939 GLN A OE1   1 
ATOM   2575  N NE2   . GLN A 1 1939 ? 180.889 176.549 147.916 1.00 129.14 ? 1939 GLN A NE2   1 
ATOM   2576  N N     . ALA A 1 1940 ? 185.671 179.478 148.641 1.00 121.67 ? 1940 ALA A N     1 
ATOM   2577  C CA    . ALA A 1 1940 ? 186.598 180.447 149.206 1.00 121.67 ? 1940 ALA A CA    1 
ATOM   2578  C C     . ALA A 1 1940 ? 187.779 179.799 149.903 1.00 121.67 ? 1940 ALA A C     1 
ATOM   2579  O O     . ALA A 1 1940 ? 188.878 180.364 149.894 1.00 121.67 ? 1940 ALA A O     1 
ATOM   2580  C CB    . ALA A 1 1940 ? 185.872 181.361 150.198 1.00 121.67 ? 1940 ALA A CB    1 
ATOM   2581  N N     . MET A 1 1941 ? 187.585 178.624 150.502 1.00 117.66 ? 1941 MET A N     1 
ATOM   2582  C CA    . MET A 1 1941 ? 188.674 178.017 151.252 1.00 117.66 ? 1941 MET A CA    1 
ATOM   2583  C C     . MET A 1 1941 ? 189.776 177.505 150.339 1.00 117.66 ? 1941 MET A C     1 
ATOM   2584  O O     . MET A 1 1941 ? 190.955 177.593 150.696 1.00 117.66 ? 1941 MET A O     1 
ATOM   2585  C CB    . MET A 1 1941 ? 188.150 176.910 152.155 1.00 117.66 ? 1941 MET A CB    1 
ATOM   2586  C CG    . MET A 1 1941 ? 188.814 176.929 153.512 1.00 117.66 ? 1941 MET A CG    1 
ATOM   2587  S SD    . MET A 1 1941 ? 187.896 175.983 154.720 1.00 117.66 ? 1941 MET A SD    1 
ATOM   2588  C CE    . MET A 1 1941 ? 186.674 177.215 155.169 1.00 117.66 ? 1941 MET A CE    1 
ATOM   2589  N N     . GLY A 1 1942 ? 189.426 176.990 149.160 1.00 116.21 ? 1942 GLY A N     1 
ATOM   2590  C CA    . GLY A 1 1942 ? 190.462 176.598 148.218 1.00 116.21 ? 1942 GLY A CA    1 
ATOM   2591  C C     . GLY A 1 1942 ? 191.356 177.761 147.835 1.00 116.21 ? 1942 GLY A C     1 
ATOM   2592  O O     . GLY A 1 1942 ? 192.587 177.654 147.844 1.00 116.21 ? 1942 GLY A O     1 
ATOM   2593  N N     . ARG A 1 1943 ? 190.748 178.905 147.520 1.00 121.98 ? 1943 ARG A N     1 
ATOM   2594  C CA    . ARG A 1 1943 ? 191.549 180.047 147.105 1.00 121.98 ? 1943 ARG A CA    1 
ATOM   2595  C C     . ARG A 1 1943 ? 192.338 180.638 148.267 1.00 121.98 ? 1943 ARG A C     1 
ATOM   2596  O O     . ARG A 1 1943 ? 193.462 181.106 148.062 1.00 121.98 ? 1943 ARG A O     1 
ATOM   2597  C CB    . ARG A 1 1943 ? 190.672 181.109 146.441 1.00 121.98 ? 1943 ARG A CB    1 
ATOM   2598  C CG    . ARG A 1 1943 ? 189.662 181.750 147.351 1.00 121.98 ? 1943 ARG A CG    1 
ATOM   2599  C CD    . ARG A 1 1943 ? 188.511 182.361 146.577 1.00 121.98 ? 1943 ARG A CD    1 
ATOM   2600  N NE    . ARG A 1 1943 ? 187.648 183.153 147.444 1.00 121.98 ? 1943 ARG A NE    1 
ATOM   2601  C CZ    . ARG A 1 1943 ? 188.012 184.276 148.050 1.00 121.98 ? 1943 ARG A CZ    1 
ATOM   2602  N NH1   . ARG A 1 1943 ? 189.215 184.799 147.877 1.00 121.98 ? 1943 ARG A NH1   1 
ATOM   2603  N NH2   . ARG A 1 1943 ? 187.146 184.890 148.851 1.00 121.98 ? 1943 ARG A NH2   1 
ATOM   2604  N N     . ILE A 1 1944 ? 191.802 180.616 149.492 1.00 113.48 ? 1944 ILE A N     1 
ATOM   2605  C CA    . ILE A 1 1944 ? 192.624 181.159 150.572 1.00 113.48 ? 1944 ILE A CA    1 
ATOM   2606  C C     . ILE A 1 1944 ? 193.745 180.193 150.919 1.00 113.48 ? 1944 ILE A C     1 
ATOM   2607  O O     . ILE A 1 1944 ? 194.806 180.614 151.383 1.00 113.48 ? 1944 ILE A O     1 
ATOM   2608  C CB    . ILE A 1 1944 ? 191.808 181.514 151.827 1.00 113.48 ? 1944 ILE A CB    1 
ATOM   2609  C CG1   . ILE A 1 1944 ? 190.815 180.417 152.162 1.00 113.48 ? 1944 ILE A CG1   1 
ATOM   2610  C CG2   . ILE A 1 1944 ? 191.088 182.835 151.630 1.00 113.48 ? 1944 ILE A CG2   1 
ATOM   2611  C CD1   . ILE A 1 1944 ? 190.434 180.361 153.614 1.00 113.48 ? 1944 ILE A CD1   1 
ATOM   2612  N N     . PHE A 1 1945 ? 193.542 178.890 150.712 1.00 110.09 ? 1945 PHE A N     1 
ATOM   2613  C CA    . PHE A 1 1945 ? 194.648 177.952 150.869 1.00 110.09 ? 1945 PHE A CA    1 
ATOM   2614  C C     . PHE A 1 1945 ? 195.731 178.225 149.838 1.00 110.09 ? 1945 PHE A C     1 
ATOM   2615  O O     . PHE A 1 1945 ? 196.929 178.185 150.149 1.00 110.09 ? 1945 PHE A O     1 
ATOM   2616  C CB    . PHE A 1 1945 ? 194.142 176.517 150.751 1.00 110.09 ? 1945 PHE A CB    1 
ATOM   2617  C CG    . PHE A 1 1945 ? 193.735 175.912 152.058 1.00 110.09 ? 1945 PHE A CG    1 
ATOM   2618  C CD1   . PHE A 1 1945 ? 194.506 176.092 153.188 1.00 110.09 ? 1945 PHE A CD1   1 
ATOM   2619  C CD2   . PHE A 1 1945 ? 192.573 175.172 152.159 1.00 110.09 ? 1945 PHE A CD2   1 
ATOM   2620  C CE1   . PHE A 1 1945 ? 194.130 175.538 154.393 1.00 110.09 ? 1945 PHE A CE1   1 
ATOM   2621  C CE2   . PHE A 1 1945 ? 192.192 174.617 153.362 1.00 110.09 ? 1945 PHE A CE2   1 
ATOM   2622  C CZ    . PHE A 1 1945 ? 192.972 174.800 154.479 1.00 110.09 ? 1945 PHE A CZ    1 
ATOM   2623  N N     . VAL A 1 1946 ? 195.323 178.506 148.600 1.00 112.10 ? 1946 VAL A N     1 
ATOM   2624  C CA    . VAL A 1 1946 ? 196.287 178.913 147.583 1.00 112.10 ? 1946 VAL A CA    1 
ATOM   2625  C C     . VAL A 1 1946 ? 197.029 180.163 148.035 1.00 112.10 ? 1946 VAL A C     1 
ATOM   2626  O O     . VAL A 1 1946 ? 198.255 180.258 147.908 1.00 112.10 ? 1946 VAL A O     1 
ATOM   2627  C CB    . VAL A 1 1946 ? 195.580 179.125 146.233 1.00 112.10 ? 1946 VAL A CB    1 
ATOM   2628  C CG1   . VAL A 1 1946 ? 196.497 179.841 145.259 1.00 112.10 ? 1946 VAL A CG1   1 
ATOM   2629  C CG2   . VAL A 1 1946 ? 195.129 177.791 145.661 1.00 112.10 ? 1946 VAL A CG2   1 
ATOM   2630  N N     . GLY A 1 1947 ? 196.298 181.132 148.585 1.00 107.46 ? 1947 GLY A N     1 
ATOM   2631  C CA    . GLY A 1 1947 ? 196.937 182.346 149.066 1.00 107.46 ? 1947 GLY A CA    1 
ATOM   2632  C C     . GLY A 1 1947 ? 197.920 182.085 150.190 1.00 107.46 ? 1947 GLY A C     1 
ATOM   2633  O O     . GLY A 1 1947 ? 198.992 182.689 150.242 1.00 107.46 ? 1947 GLY A O     1 
ATOM   2634  N N     . LEU A 1 1948 ? 197.563 181.191 151.111 1.00 99.98  ? 1948 LEU A N     1 
ATOM   2635  C CA    . LEU A 1 1948 ? 198.475 180.830 152.189 1.00 99.98  ? 1948 LEU A CA    1 
ATOM   2636  C C     . LEU A 1 1948 ? 199.747 180.207 151.638 1.00 99.98  ? 1948 LEU A C     1 
ATOM   2637  O O     . LEU A 1 1948 ? 200.853 180.547 152.070 1.00 99.98  ? 1948 LEU A O     1 
ATOM   2638  C CB    . LEU A 1 1948 ? 197.792 179.870 153.160 1.00 99.98  ? 1948 LEU A CB    1 
ATOM   2639  C CG    . LEU A 1 1948 ? 196.752 180.476 154.097 1.00 99.98  ? 1948 LEU A CG    1 
ATOM   2640  C CD1   . LEU A 1 1948 ? 196.079 179.392 154.909 1.00 99.98  ? 1948 LEU A CD1   1 
ATOM   2641  C CD2   . LEU A 1 1948 ? 197.414 181.481 155.009 1.00 99.98  ? 1948 LEU A CD2   1 
ATOM   2642  N N     . CYS A 1 1949 ? 199.609 179.300 150.670 1.00 106.49 ? 1949 CYS A N     1 
ATOM   2643  C CA    . CYS A 1 1949 ? 200.792 178.703 150.064 1.00 106.49 ? 1949 CYS A CA    1 
ATOM   2644  C C     . CYS A 1 1949 ? 201.624 179.741 149.325 1.00 106.49 ? 1949 CYS A C     1 
ATOM   2645  O O     . CYS A 1 1949 ? 202.851 179.613 149.246 1.00 106.49 ? 1949 CYS A O     1 
ATOM   2646  C CB    . CYS A 1 1949 ? 200.390 177.576 149.114 1.00 106.49 ? 1949 CYS A CB    1 
ATOM   2647  S SG    . CYS A 1 1949 ? 199.687 176.130 149.929 1.00 106.49 ? 1949 CYS A SG    1 
ATOM   2648  N N     . GLN A 1 1950 ? 200.980 180.773 148.781 1.00 106.80 ? 1950 GLN A N     1 
ATOM   2649  C CA    . GLN A 1 1950 ? 201.699 181.740 147.958 1.00 106.80 ? 1950 GLN A CA    1 
ATOM   2650  C C     . GLN A 1 1950 ? 202.399 182.799 148.803 1.00 106.80 ? 1950 GLN A C     1 
ATOM   2651  O O     . GLN A 1 1950 ? 203.629 182.903 148.790 1.00 106.80 ? 1950 GLN A O     1 
ATOM   2652  C CB    . GLN A 1 1950 ? 200.733 182.398 146.972 1.00 106.80 ? 1950 GLN A CB    1 
ATOM   2653  C CG    . GLN A 1 1950 ? 200.261 181.482 145.862 1.00 106.80 ? 1950 GLN A CG    1 
ATOM   2654  C CD    . GLN A 1 1950 ? 200.987 181.724 144.564 1.00 106.80 ? 1950 GLN A CD    1 
ATOM   2655  O OE1   . GLN A 1 1950 ? 201.318 182.860 144.229 1.00 106.80 ? 1950 GLN A OE1   1 
ATOM   2656  N NE2   . GLN A 1 1950 ? 201.240 180.655 143.820 1.00 106.80 ? 1950 GLN A NE2   1 
ATOM   2657  N N     . VAL A 1 1951 ? 201.628 183.596 149.546 1.00 99.57  ? 1951 VAL A N     1 
ATOM   2658  C CA    . VAL A 1 1951 ? 202.201 184.755 150.225 1.00 99.57  ? 1951 VAL A CA    1 
ATOM   2659  C C     . VAL A 1 1951 ? 203.079 184.338 151.397 1.00 99.57  ? 1951 VAL A C     1 
ATOM   2660  O O     . VAL A 1 1951 ? 204.096 184.983 151.675 1.00 99.57  ? 1951 VAL A O     1 
ATOM   2661  C CB    . VAL A 1 1951 ? 201.093 185.730 150.669 1.00 99.57  ? 1951 VAL A CB    1 
ATOM   2662  C CG1   . VAL A 1 1951 ? 200.228 185.122 151.756 1.00 99.57  ? 1951 VAL A CG1   1 
ATOM   2663  C CG2   . VAL A 1 1951 ? 201.703 187.033 151.146 1.00 99.57  ? 1951 VAL A CG2   1 
ATOM   2664  N N     . GLY A 1 1952 ? 202.716 183.267 152.097 1.00 95.52  ? 1952 GLY A N     1 
ATOM   2665  C CA    . GLY A 1 1952 ? 203.468 182.846 153.262 1.00 95.52  ? 1952 GLY A CA    1 
ATOM   2666  C C     . GLY A 1 1952 ? 202.851 183.304 154.566 1.00 95.52  ? 1952 GLY A C     1 
ATOM   2667  O O     . GLY A 1 1952 ? 203.550 183.805 155.451 1.00 95.52  ? 1952 GLY A O     1 
ATOM   2668  N N     . ALA A 1 1953 ? 201.540 183.143 154.692 1.00 87.46  ? 1953 ALA A N     1 
ATOM   2669  C CA    . ALA A 1 1953 ? 200.819 183.500 155.900 1.00 87.46  ? 1953 ALA A CA    1 
ATOM   2670  C C     . ALA A 1 1953 ? 200.429 182.237 156.660 1.00 87.46  ? 1953 ALA A C     1 
ATOM   2671  O O     . ALA A 1 1953 ? 200.697 181.114 156.232 1.00 87.46  ? 1953 ALA A O     1 
ATOM   2672  C CB    . ALA A 1 1953 ? 199.592 184.344 155.556 1.00 87.46  ? 1953 ALA A CB    1 
ATOM   2673  N N     . TRP A 1 1954 ? 199.783 182.423 157.804 1.00 77.03  ? 1954 TRP A N     1 
ATOM   2674  C CA    . TRP A 1 1954 ? 199.406 181.320 158.673 1.00 77.03  ? 1954 TRP A CA    1 
ATOM   2675  C C     . TRP A 1 1954 ? 197.893 181.176 158.725 1.00 77.03  ? 1954 TRP A C     1 
ATOM   2676  O O     . TRP A 1 1954 ? 197.153 182.157 158.615 1.00 77.03  ? 1954 TRP A O     1 
ATOM   2677  C CB    . TRP A 1 1954 ? 199.941 181.525 160.089 1.00 77.03  ? 1954 TRP A CB    1 
ATOM   2678  C CG    . TRP A 1 1954 ? 201.391 181.238 160.232 1.00 77.03  ? 1954 TRP A CG    1 
ATOM   2679  C CD1   . TRP A 1 1954 ? 202.312 181.166 159.236 1.00 77.03  ? 1954 TRP A CD1   1 
ATOM   2680  C CD2   . TRP A 1 1954 ? 202.096 180.989 161.449 1.00 77.03  ? 1954 TRP A CD2   1 
ATOM   2681  N NE1   . TRP A 1 1954 ? 203.550 180.887 159.756 1.00 77.03  ? 1954 TRP A NE1   1 
ATOM   2682  C CE2   . TRP A 1 1954 ? 203.441 180.773 161.115 1.00 77.03  ? 1954 TRP A CE2   1 
ATOM   2683  C CE3   . TRP A 1 1954 ? 201.717 180.928 162.790 1.00 77.03  ? 1954 TRP A CE3   1 
ATOM   2684  C CZ2   . TRP A 1 1954 ? 204.408 180.498 162.069 1.00 77.03  ? 1954 TRP A CZ2   1 
ATOM   2685  C CZ3   . TRP A 1 1954 ? 202.677 180.655 163.734 1.00 77.03  ? 1954 TRP A CZ3   1 
ATOM   2686  C CH2   . TRP A 1 1954 ? 204.007 180.443 163.372 1.00 77.03  ? 1954 TRP A CH2   1 
ATOM   2687  N N     . GLY A 1 1955 ? 197.441 179.939 158.903 1.00 78.78  ? 1955 GLY A N     1 
ATOM   2688  C CA    . GLY A 1 1955 ? 196.024 179.661 159.016 1.00 78.78  ? 1955 GLY A CA    1 
ATOM   2689  C C     . GLY A 1 1955 ? 195.707 178.703 160.143 1.00 78.78  ? 1955 GLY A C     1 
ATOM   2690  O O     . GLY A 1 1955 ? 196.322 177.639 160.249 1.00 78.78  ? 1955 GLY A O     1 
ATOM   2691  N N     . CYS A 1 1956 ? 194.753 179.064 160.993 1.00 79.66  ? 1956 CYS A N     1 
ATOM   2692  C CA    . CYS A 1 1956 ? 194.366 178.235 162.123 1.00 79.66  ? 1956 CYS A CA    1 
ATOM   2693  C C     . CYS A 1 1956 ? 192.863 178.010 162.112 1.00 79.66  ? 1956 CYS A C     1 
ATOM   2694  O O     . CYS A 1 1956 ? 192.087 178.959 161.976 1.00 79.66  ? 1956 CYS A O     1 
ATOM   2695  C CB    . CYS A 1 1956 ? 194.782 178.878 163.440 1.00 79.66  ? 1956 CYS A CB    1 
ATOM   2696  S SG    . CYS A 1 1956 ? 194.081 178.084 164.897 1.00 79.66  ? 1956 CYS A SG    1 
ATOM   2697  N N     . PHE A 1 1957 ? 192.458 176.754 162.266 1.00 84.42  ? 1957 PHE A N     1 
ATOM   2698  C CA    . PHE A 1 1957 ? 191.052 176.384 162.344 1.00 84.42  ? 1957 PHE A CA    1 
ATOM   2699  C C     . PHE A 1 1957 ? 190.625 176.418 163.802 1.00 84.42  ? 1957 PHE A C     1 
ATOM   2700  O O     . PHE A 1 1957 ? 191.306 175.851 164.660 1.00 84.42  ? 1957 PHE A O     1 
ATOM   2701  C CB    . PHE A 1 1957 ? 190.810 174.990 161.766 1.00 84.42  ? 1957 PHE A CB    1 
ATOM   2702  C CG    . PHE A 1 1957 ? 191.009 174.900 160.283 1.00 84.42  ? 1957 PHE A CG    1 
ATOM   2703  C CD1   . PHE A 1 1957 ? 192.271 174.997 159.733 1.00 84.42  ? 1957 PHE A CD1   1 
ATOM   2704  C CD2   . PHE A 1 1957 ? 189.933 174.709 159.442 1.00 84.42  ? 1957 PHE A CD2   1 
ATOM   2705  C CE1   . PHE A 1 1957 ? 192.454 174.910 158.375 1.00 84.42  ? 1957 PHE A CE1   1 
ATOM   2706  C CE2   . PHE A 1 1957 ? 190.112 174.623 158.082 1.00 84.42  ? 1957 PHE A CE2   1 
ATOM   2707  C CZ    . PHE A 1 1957 ? 191.374 174.723 157.548 1.00 84.42  ? 1957 PHE A CZ    1 
ATOM   2708  N N     . ASP A 1 1958 ? 189.506 177.084 164.085 1.00 96.55  ? 1958 ASP A N     1 
ATOM   2709  C CA    . ASP A 1 1958 ? 189.096 177.254 165.475 1.00 96.55  ? 1958 ASP A CA    1 
ATOM   2710  C C     . ASP A 1 1958 ? 188.766 175.917 166.123 1.00 96.55  ? 1958 ASP A C     1 
ATOM   2711  O O     . ASP A 1 1958 ? 189.308 175.577 167.180 1.00 96.55  ? 1958 ASP A O     1 
ATOM   2712  C CB    . ASP A 1 1958 ? 187.899 178.199 165.563 1.00 96.55  ? 1958 ASP A CB    1 
ATOM   2713  C CG    . ASP A 1 1958 ? 187.669 178.712 166.969 1.00 96.55  ? 1958 ASP A CG    1 
ATOM   2714  O OD1   . ASP A 1 1958 ? 188.557 178.514 167.825 1.00 96.55  ? 1958 ASP A OD1   1 
ATOM   2715  O OD2   . ASP A 1 1958 ? 186.601 179.306 167.221 1.00 96.55  ? 1958 ASP A OD2   1 
ATOM   2716  N N     . GLU A 1 1959 ? 187.885 175.137 165.500 1.00 100.53 ? 1959 GLU A N     1 
ATOM   2717  C CA    . GLU A 1 1959 ? 187.493 173.834 166.036 1.00 100.53 ? 1959 GLU A CA    1 
ATOM   2718  C C     . GLU A 1 1959 ? 187.209 172.916 164.858 1.00 100.53 ? 1959 GLU A C     1 
ATOM   2719  O O     . GLU A 1 1959 ? 186.192 173.076 164.179 1.00 100.53 ? 1959 GLU A O     1 
ATOM   2720  C CB    . GLU A 1 1959 ? 186.270 173.940 166.943 1.00 100.53 ? 1959 GLU A CB    1 
ATOM   2721  C CG    . GLU A 1 1959 ? 186.452 174.787 168.188 1.00 100.53 ? 1959 GLU A CG    1 
ATOM   2722  C CD    . GLU A 1 1959 ? 186.630 173.950 169.436 1.00 100.53 ? 1959 GLU A CD    1 
ATOM   2723  O OE1   . GLU A 1 1959 ? 187.206 172.847 169.337 1.00 100.53 ? 1959 GLU A OE1   1 
ATOM   2724  O OE2   . GLU A 1 1959 ? 186.190 174.394 170.517 1.00 100.53 ? 1959 GLU A OE2   1 
ATOM   2725  N N     . PHE A 1 1960 ? 188.096 171.950 164.627 1.00 95.04  ? 1960 PHE A N     1 
ATOM   2726  C CA    . PHE A 1 1960 ? 187.953 171.100 163.455 1.00 95.04  ? 1960 PHE A CA    1 
ATOM   2727  C C     . PHE A 1 1960 ? 186.834 170.082 163.621 1.00 95.04  ? 1960 PHE A C     1 
ATOM   2728  O O     . PHE A 1 1960 ? 186.323 169.564 162.623 1.00 95.04  ? 1960 PHE A O     1 
ATOM   2729  C CB    . PHE A 1 1960 ? 189.266 170.387 163.161 1.00 95.04  ? 1960 PHE A CB    1 
ATOM   2730  C CG    . PHE A 1 1960 ? 189.497 170.133 161.708 1.00 95.04  ? 1960 PHE A CG    1 
ATOM   2731  C CD1   . PHE A 1 1960 ? 189.546 171.183 160.814 1.00 95.04  ? 1960 PHE A CD1   1 
ATOM   2732  C CD2   . PHE A 1 1960 ? 189.657 168.847 161.233 1.00 95.04  ? 1960 PHE A CD2   1 
ATOM   2733  C CE1   . PHE A 1 1960 ? 189.759 170.956 159.474 1.00 95.04  ? 1960 PHE A CE1   1 
ATOM   2734  C CE2   . PHE A 1 1960 ? 189.869 168.614 159.893 1.00 95.04  ? 1960 PHE A CE2   1 
ATOM   2735  C CZ    . PHE A 1 1960 ? 189.919 169.671 159.013 1.00 95.04  ? 1960 PHE A CZ    1 
ATOM   2736  N N     . ASN A 1 1961 ? 186.444 169.775 164.858 1.00 100.71 ? 1961 ASN A N     1 
ATOM   2737  C CA    . ASN A 1 1961 ? 185.422 168.754 165.059 1.00 100.71 ? 1961 ASN A CA    1 
ATOM   2738  C C     . ASN A 1 1961 ? 184.053 169.213 164.572 1.00 100.71 ? 1961 ASN A C     1 
ATOM   2739  O O     . ASN A 1 1961 ? 183.207 168.381 164.224 1.00 100.71 ? 1961 ASN A O     1 
ATOM   2740  C CB    . ASN A 1 1961 ? 185.393 168.319 166.533 1.00 100.71 ? 1961 ASN A CB    1 
ATOM   2741  C CG    . ASN A 1 1961 ? 184.383 169.089 167.388 1.00 100.71 ? 1961 ASN A CG    1 
ATOM   2742  O OD1   . ASN A 1 1961 ? 183.952 170.193 167.057 1.00 100.71 ? 1961 ASN A OD1   1 
ATOM   2743  N ND2   . ASN A 1 1961 ? 184.000 168.485 168.507 1.00 100.71 ? 1961 ASN A ND2   1 
ATOM   2744  N N     . ARG A 1 1962 ? 183.816 170.524 164.536 1.00 107.43 ? 1962 ARG A N     1 
ATOM   2745  C CA    . ARG A 1 1962 ? 182.520 171.047 164.123 1.00 107.43 ? 1962 ARG A CA    1 
ATOM   2746  C C     . ARG A 1 1962 ? 182.221 170.804 162.651 1.00 107.43 ? 1962 ARG A C     1 
ATOM   2747  O O     . ARG A 1 1962 ? 181.067 170.957 162.240 1.00 107.43 ? 1962 ARG A O     1 
ATOM   2748  C CB    . ARG A 1 1962 ? 182.446 172.547 164.410 1.00 107.43 ? 1962 ARG A CB    1 
ATOM   2749  C CG    . ARG A 1 1962 ? 183.070 172.956 165.725 1.00 107.43 ? 1962 ARG A CG    1 
ATOM   2750  C CD    . ARG A 1 1962 ? 182.796 174.416 166.043 1.00 107.43 ? 1962 ARG A CD    1 
ATOM   2751  N NE    . ARG A 1 1962 ? 181.393 174.767 165.867 1.00 107.43 ? 1962 ARG A NE    1 
ATOM   2752  C CZ    . ARG A 1 1962 ? 180.822 175.841 166.392 1.00 107.43 ? 1962 ARG A CZ    1 
ATOM   2753  N NH1   . ARG A 1 1962 ? 181.506 176.692 167.140 1.00 107.43 ? 1962 ARG A NH1   1 
ATOM   2754  N NH2   . ARG A 1 1962 ? 179.531 176.066 166.165 1.00 107.43 ? 1962 ARG A NH2   1 
ATOM   2755  N N     . LEU A 1 1963 ? 183.216 170.434 161.856 1.00 111.03 ? 1963 LEU A N     1 
ATOM   2756  C CA    . LEU A 1 1963 ? 183.019 170.328 160.421 1.00 111.03 ? 1963 LEU A CA    1 
ATOM   2757  C C     . LEU A 1 1963 ? 182.131 169.143 160.066 1.00 111.03 ? 1963 LEU A C     1 
ATOM   2758  O O     . LEU A 1 1963 ? 182.111 168.120 160.754 1.00 111.03 ? 1963 LEU A O     1 
ATOM   2759  C CB    . LEU A 1 1963 ? 184.363 170.193 159.714 1.00 111.03 ? 1963 LEU A CB    1 
ATOM   2760  C CG    . LEU A 1 1963 ? 185.123 171.509 159.616 1.00 111.03 ? 1963 LEU A CG    1 
ATOM   2761  C CD1   . LEU A 1 1963 ? 186.255 171.394 158.615 1.00 111.03 ? 1963 LEU A CD1   1 
ATOM   2762  C CD2   . LEU A 1 1963 ? 184.164 172.618 159.242 1.00 111.03 ? 1963 LEU A CD2   1 
ATOM   2763  N N     . GLU A 1 1964 ? 181.386 169.297 158.976 1.00 121.31 ? 1964 GLU A N     1 
ATOM   2764  C CA    . GLU A 1 1964 ? 180.599 168.198 158.442 1.00 121.31 ? 1964 GLU A CA    1 
ATOM   2765  C C     . GLU A 1 1964 ? 181.528 167.130 157.877 1.00 121.31 ? 1964 GLU A C     1 
ATOM   2766  O O     . GLU A 1 1964 ? 182.645 167.418 157.444 1.00 121.31 ? 1964 GLU A O     1 
ATOM   2767  C CB    . GLU A 1 1964 ? 179.641 168.709 157.365 1.00 121.31 ? 1964 GLU A CB    1 
ATOM   2768  C CG    . GLU A 1 1964 ? 178.576 167.716 156.933 1.00 121.31 ? 1964 GLU A CG    1 
ATOM   2769  C CD    . GLU A 1 1964 ? 179.057 166.780 155.846 1.00 121.31 ? 1964 GLU A CD    1 
ATOM   2770  O OE1   . GLU A 1 1964 ? 179.893 167.206 155.023 1.00 121.31 ? 1964 GLU A OE1   1 
ATOM   2771  O OE2   . GLU A 1 1964 ? 178.605 165.616 155.822 1.00 121.31 ? 1964 GLU A OE2   1 
ATOM   2772  N N     . GLU A 1 1965 ? 181.050 165.884 157.884 1.00 117.74 ? 1965 GLU A N     1 
ATOM   2773  C CA    . GLU A 1 1965 ? 181.906 164.749 157.549 1.00 117.74 ? 1965 GLU A CA    1 
ATOM   2774  C C     . GLU A 1 1965 ? 182.529 164.896 156.164 1.00 117.74 ? 1965 GLU A C     1 
ATOM   2775  O O     . GLU A 1 1965 ? 183.751 164.789 156.010 1.00 117.74 ? 1965 GLU A O     1 
ATOM   2776  C CB    . GLU A 1 1965 ? 181.104 163.451 157.643 1.00 117.74 ? 1965 GLU A CB    1 
ATOM   2777  C CG    . GLU A 1 1965 ? 181.917 162.200 157.368 1.00 117.74 ? 1965 GLU A CG    1 
ATOM   2778  C CD    . GLU A 1 1965 ? 183.323 162.285 157.927 1.00 117.74 ? 1965 GLU A CD    1 
ATOM   2779  O OE1   . GLU A 1 1965 ? 183.468 162.384 159.163 1.00 117.74 ? 1965 GLU A OE1   1 
ATOM   2780  O OE2   . GLU A 1 1965 ? 184.283 162.253 157.130 1.00 117.74 ? 1965 GLU A OE2   1 
ATOM   2781  N N     . ARG A 1 1966 ? 181.709 165.140 155.140 1.00 119.31 ? 1966 ARG A N     1 
ATOM   2782  C CA    . ARG A 1 1966 ? 182.254 165.282 153.792 1.00 119.31 ? 1966 ARG A CA    1 
ATOM   2783  C C     . ARG A 1 1966 ? 183.125 166.526 153.678 1.00 119.31 ? 1966 ARG A C     1 
ATOM   2784  O O     . ARG A 1 1966 ? 184.205 166.488 153.072 1.00 119.31 ? 1966 ARG A O     1 
ATOM   2785  C CB    . ARG A 1 1966 ? 181.126 165.326 152.764 1.00 119.31 ? 1966 ARG A CB    1 
ATOM   2786  C CG    . ARG A 1 1966 ? 179.891 164.545 153.160 1.00 119.31 ? 1966 ARG A CG    1 
ATOM   2787  C CD    . ARG A 1 1966 ? 178.678 165.055 152.406 1.00 119.31 ? 1966 ARG A CD    1 
ATOM   2788  N NE    . ARG A 1 1966 ? 178.501 166.491 152.584 1.00 119.31 ? 1966 ARG A NE    1 
ATOM   2789  C CZ    . ARG A 1 1966 ? 178.189 167.333 151.608 1.00 119.31 ? 1966 ARG A CZ    1 
ATOM   2790  N NH1   . ARG A 1 1966 ? 178.010 166.916 150.366 1.00 119.31 ? 1966 ARG A NH1   1 
ATOM   2791  N NH2   . ARG A 1 1966 ? 178.055 168.627 151.886 1.00 119.31 ? 1966 ARG A NH2   1 
ATOM   2792  N N     . MET A 1 1967 ? 182.670 167.640 154.253 1.00 116.53 ? 1967 MET A N     1 
ATOM   2793  C CA    . MET A 1 1967 ? 183.472 168.858 154.251 1.00 116.53 ? 1967 MET A CA    1 
ATOM   2794  C C     . MET A 1 1967 ? 184.795 168.629 154.964 1.00 116.53 ? 1967 MET A C     1 
ATOM   2795  O O     . MET A 1 1967 ? 185.855 169.050 154.484 1.00 116.53 ? 1967 MET A O     1 
ATOM   2796  C CB    . MET A 1 1967 ? 182.692 169.992 154.915 1.00 116.53 ? 1967 MET A CB    1 
ATOM   2797  C CG    . MET A 1 1967 ? 183.049 171.381 154.427 1.00 116.53 ? 1967 MET A CG    1 
ATOM   2798  S SD    . MET A 1 1967 ? 183.068 171.519 152.632 1.00 116.53 ? 1967 MET A SD    1 
ATOM   2799  C CE    . MET A 1 1967 ? 183.077 173.300 152.445 1.00 116.53 ? 1967 MET A CE    1 
ATOM   2800  N N     . LEU A 1 1968 ? 184.746 167.954 156.116 1.00 109.91 ? 1968 LEU A N     1 
ATOM   2801  C CA    . LEU A 1 1968 ? 185.964 167.662 156.861 1.00 109.91 ? 1968 LEU A CA    1 
ATOM   2802  C C     . LEU A 1 1968 ? 186.910 166.805 156.039 1.00 109.91 ? 1968 LEU A C     1 
ATOM   2803  O O     . LEU A 1 1968 ? 188.116 167.062 156.007 1.00 109.91 ? 1968 LEU A O     1 
ATOM   2804  C CB    . LEU A 1 1968 ? 185.627 166.968 158.180 1.00 109.91 ? 1968 LEU A CB    1 
ATOM   2805  C CG    . LEU A 1 1968 ? 186.802 166.531 159.054 1.00 109.91 ? 1968 LEU A CG    1 
ATOM   2806  C CD1   . LEU A 1 1968 ? 186.580 166.962 160.491 1.00 109.91 ? 1968 LEU A CD1   1 
ATOM   2807  C CD2   . LEU A 1 1968 ? 187.002 165.029 158.977 1.00 109.91 ? 1968 LEU A CD2   1 
ATOM   2808  N N     . SER A 1 1969 ? 186.382 165.789 155.356 1.00 108.59 ? 1969 SER A N     1 
ATOM   2809  C CA    . SER A 1 1969 ? 187.235 164.939 154.534 1.00 108.59 ? 1969 SER A CA    1 
ATOM   2810  C C     . SER A 1 1969 ? 187.876 165.730 153.403 1.00 108.59 ? 1969 SER A C     1 
ATOM   2811  O O     . SER A 1 1969 ? 189.056 165.537 153.091 1.00 108.59 ? 1969 SER A O     1 
ATOM   2812  C CB    . SER A 1 1969 ? 186.432 163.768 153.975 1.00 108.59 ? 1969 SER A CB    1 
ATOM   2813  O OG    . SER A 1 1969 ? 187.111 163.168 152.885 1.00 108.59 ? 1969 SER A OG    1 
ATOM   2814  N N     . ALA A 1 1970 ? 187.115 166.627 152.777 1.00 109.87 ? 1970 ALA A N     1 
ATOM   2815  C CA    . ALA A 1 1970 ? 187.658 167.395 151.660 1.00 109.87 ? 1970 ALA A CA    1 
ATOM   2816  C C     . ALA A 1 1970 ? 188.767 168.337 152.121 1.00 109.87 ? 1970 ALA A C     1 
ATOM   2817  O O     . ALA A 1 1970 ? 189.845 168.397 151.508 1.00 109.87 ? 1970 ALA A O     1 
ATOM   2818  C CB    . ALA A 1 1970 ? 186.538 168.167 150.969 1.00 109.87 ? 1970 ALA A CB    1 
ATOM   2819  N N     . VAL A 1 1971 ? 188.526 169.082 153.203 1.00 105.97 ? 1971 VAL A N     1 
ATOM   2820  C CA    . VAL A 1 1971 ? 189.583 169.970 153.675 1.00 105.97 ? 1971 VAL A CA    1 
ATOM   2821  C C     . VAL A 1 1971 ? 190.750 169.153 154.199 1.00 105.97 ? 1971 VAL A C     1 
ATOM   2822  O O     . VAL A 1 1971 ? 191.897 169.598 154.142 1.00 105.97 ? 1971 VAL A O     1 
ATOM   2823  C CB    . VAL A 1 1971 ? 189.086 170.959 154.745 1.00 105.97 ? 1971 VAL A CB    1 
ATOM   2824  C CG1   . VAL A 1 1971 ? 188.365 172.131 154.096 1.00 105.97 ? 1971 VAL A CG1   1 
ATOM   2825  C CG2   . VAL A 1 1971 ? 188.248 170.267 155.791 1.00 105.97 ? 1971 VAL A CG2   1 
ATOM   2826  N N     . SER A 1 1972 ? 190.487 167.950 154.712 1.00 106.78 ? 1972 SER A N     1 
ATOM   2827  C CA    . SER A 1 1972 ? 191.573 167.080 155.137 1.00 106.78 ? 1972 SER A CA    1 
ATOM   2828  C C     . SER A 1 1972 ? 192.436 166.670 153.957 1.00 106.78 ? 1972 SER A C     1 
ATOM   2829  O O     . SER A 1 1972 ? 193.662 166.632 154.068 1.00 106.78 ? 1972 SER A O     1 
ATOM   2830  C CB    . SER A 1 1972 ? 191.011 165.852 155.846 1.00 106.78 ? 1972 SER A CB    1 
ATOM   2831  O OG    . SER A 1 1972 ? 190.035 166.227 156.800 1.00 106.78 ? 1972 SER A OG    1 
ATOM   2832  N N     . GLN A 1 1973 ? 191.816 166.359 152.820 1.00 106.87 ? 1973 GLN A N     1 
ATOM   2833  C CA    . GLN A 1 1973 ? 192.592 166.027 151.629 1.00 106.87 ? 1973 GLN A CA    1 
ATOM   2834  C C     . GLN A 1 1973 ? 193.431 167.216 151.176 1.00 106.87 ? 1973 GLN A C     1 
ATOM   2835  O O     . GLN A 1 1973 ? 194.615 167.070 150.843 1.00 106.87 ? 1973 GLN A O     1 
ATOM   2836  C CB    . GLN A 1 1973 ? 191.666 165.562 150.507 1.00 106.87 ? 1973 GLN A CB    1 
ATOM   2837  C CG    . GLN A 1 1973 ? 190.854 164.332 150.851 1.00 106.87 ? 1973 GLN A CG    1 
ATOM   2838  C CD    . GLN A 1 1973 ? 191.506 163.052 150.373 1.00 106.87 ? 1973 GLN A CD    1 
ATOM   2839  O OE1   . GLN A 1 1973 ? 192.725 162.898 150.449 1.00 106.87 ? 1973 GLN A OE1   1 
ATOM   2840  N NE2   . GLN A 1 1973 ? 190.696 162.123 149.881 1.00 106.87 ? 1973 GLN A NE2   1 
ATOM   2841  N N     . GLN A 1 1974 ? 192.832 168.408 151.161 1.00 105.12 ? 1974 GLN A N     1 
ATOM   2842  C CA    . GLN A 1 1974 ? 193.593 169.586 150.751 1.00 105.12 ? 1974 GLN A CA    1 
ATOM   2843  C C     . GLN A 1 1974 ? 194.754 169.852 151.705 1.00 105.12 ? 1974 GLN A C     1 
ATOM   2844  O O     . GLN A 1 1974 ? 195.881 170.131 151.269 1.00 105.12 ? 1974 GLN A O     1 
ATOM   2845  C CB    . GLN A 1 1974 ? 192.680 170.806 150.663 1.00 105.12 ? 1974 GLN A CB    1 
ATOM   2846  C CG    . GLN A 1 1974 ? 191.822 170.841 149.412 1.00 105.12 ? 1974 GLN A CG    1 
ATOM   2847  C CD    . GLN A 1 1974 ? 191.323 172.234 149.085 1.00 105.12 ? 1974 GLN A CD    1 
ATOM   2848  O OE1   . GLN A 1 1974 ? 190.990 173.013 149.976 1.00 105.12 ? 1974 GLN A OE1   1 
ATOM   2849  N NE2   . GLN A 1 1974 ? 191.267 172.554 147.799 1.00 105.12 ? 1974 GLN A NE2   1 
ATOM   2850  N N     . VAL A 1 1975 ? 194.499 169.757 153.010 1.00 99.55  ? 1975 VAL A N     1 
ATOM   2851  C CA    . VAL A 1 1975 ? 195.539 169.988 154.005 1.00 99.55  ? 1975 VAL A CA    1 
ATOM   2852  C C     . VAL A 1 1975 ? 196.619 168.926 153.891 1.00 99.55  ? 1975 VAL A C     1 
ATOM   2853  O O     . VAL A 1 1975 ? 197.805 169.205 154.083 1.00 99.55  ? 1975 VAL A O     1 
ATOM   2854  C CB    . VAL A 1 1975 ? 194.921 170.026 155.414 1.00 99.55  ? 1975 VAL A CB    1 
ATOM   2855  C CG1   . VAL A 1 1975 ? 195.985 169.843 156.475 1.00 99.55  ? 1975 VAL A CG1   1 
ATOM   2856  C CG2   . VAL A 1 1975 ? 194.185 171.331 155.625 1.00 99.55  ? 1975 VAL A CG2   1 
ATOM   2857  N N     . GLN A 1 1976 ? 196.228 167.695 153.569 1.00 103.99 ? 1976 GLN A N     1 
ATOM   2858  C CA    . GLN A 1 1976 ? 197.205 166.637 153.361 1.00 103.99 ? 1976 GLN A CA    1 
ATOM   2859  C C     . GLN A 1 1976 ? 198.114 166.963 152.190 1.00 103.99 ? 1976 GLN A C     1 
ATOM   2860  O O     . GLN A 1 1976 ? 199.334 166.797 152.280 1.00 103.99 ? 1976 GLN A O     1 
ATOM   2861  C CB    . GLN A 1 1976 ? 196.490 165.308 153.134 1.00 103.99 ? 1976 GLN A CB    1 
ATOM   2862  C CG    . GLN A 1 1976 ? 197.270 164.096 153.593 1.00 103.99 ? 1976 GLN A CG    1 
ATOM   2863  C CD    . GLN A 1 1976 ? 196.421 162.846 153.621 1.00 103.99 ? 1976 GLN A CD    1 
ATOM   2864  O OE1   . GLN A 1 1976 ? 195.315 162.823 153.083 1.00 103.99 ? 1976 GLN A OE1   1 
ATOM   2865  N NE2   . GLN A 1 1976 ? 196.928 161.799 154.261 1.00 103.99 ? 1976 GLN A NE2   1 
ATOM   2866  N N     . CYS A 1 1977 ? 197.541 167.440 151.085 1.00 103.09 ? 1977 CYS A N     1 
ATOM   2867  C CA    . CYS A 1 1977 ? 198.368 167.815 149.942 1.00 103.09 ? 1977 CYS A CA    1 
ATOM   2868  C C     . CYS A 1 1977 ? 199.336 168.932 150.315 1.00 103.09 ? 1977 CYS A C     1 
ATOM   2869  O O     . CYS A 1 1977 ? 200.537 168.865 150.013 1.00 103.09 ? 1977 CYS A O     1 
ATOM   2870  C CB    . CYS A 1 1977 ? 197.480 168.237 148.774 1.00 103.09 ? 1977 CYS A CB    1 
ATOM   2871  S SG    . CYS A 1 1977 ? 196.342 166.955 148.208 1.00 103.09 ? 1977 CYS A SG    1 
ATOM   2872  N N     . ILE A 1 1978 ? 198.831 169.957 151.002 1.00 100.57 ? 1978 ILE A N     1 
ATOM   2873  C CA    . ILE A 1 1978 ? 199.676 171.089 151.374 1.00 100.57 ? 1978 ILE A CA    1 
ATOM   2874  C C     . ILE A 1 1978 ? 200.792 170.641 152.309 1.00 100.57 ? 1978 ILE A C     1 
ATOM   2875  O O     . ILE A 1 1978 ? 201.951 171.048 152.161 1.00 100.57 ? 1978 ILE A O     1 
ATOM   2876  C CB    . ILE A 1 1978 ? 198.824 172.204 152.002 1.00 100.57 ? 1978 ILE A CB    1 
ATOM   2877  C CG1   . ILE A 1 1978 ? 197.771 172.685 151.007 1.00 100.57 ? 1978 ILE A CG1   1 
ATOM   2878  C CG2   . ILE A 1 1978 ? 199.700 173.355 152.429 1.00 100.57 ? 1978 ILE A CG2   1 
ATOM   2879  C CD1   . ILE A 1 1978 ? 197.052 173.940 151.438 1.00 100.57 ? 1978 ILE A CD1   1 
ATOM   2880  N N     . GLN A 1 1979 ? 200.466 169.793 153.283 1.00 97.49  ? 1979 GLN A N     1 
ATOM   2881  C CA    . GLN A 1 1979 ? 201.467 169.362 154.246 1.00 97.49  ? 1979 GLN A CA    1 
ATOM   2882  C C     . GLN A 1 1979 ? 202.485 168.425 153.619 1.00 97.49  ? 1979 GLN A C     1 
ATOM   2883  O O     . GLN A 1 1979 ? 203.651 168.433 154.019 1.00 97.49  ? 1979 GLN A O     1 
ATOM   2884  C CB    . GLN A 1 1979 ? 200.798 168.692 155.442 1.00 97.49  ? 1979 GLN A CB    1 
ATOM   2885  C CG    . GLN A 1 1979 ? 201.642 168.729 156.693 1.00 97.49  ? 1979 GLN A CG    1 
ATOM   2886  C CD    . GLN A 1 1979 ? 202.025 170.137 157.087 1.00 97.49  ? 1979 GLN A CD    1 
ATOM   2887  O OE1   . GLN A 1 1979 ? 201.220 171.060 156.986 1.00 97.49  ? 1979 GLN A OE1   1 
ATOM   2888  N NE2   . GLN A 1 1979 ? 203.261 170.313 157.535 1.00 97.49  ? 1979 GLN A NE2   1 
ATOM   2889  N N     . GLU A 1 1980 ? 202.075 167.606 152.650 1.00 106.73 ? 1980 GLU A N     1 
ATOM   2890  C CA    . GLU A 1 1980 ? 203.053 166.801 151.928 1.00 106.73 ? 1980 GLU A CA    1 
ATOM   2891  C C     . GLU A 1 1980 ? 203.998 167.689 151.135 1.00 106.73 ? 1980 GLU A C     1 
ATOM   2892  O O     . GLU A 1 1980 ? 205.205 167.424 151.071 1.00 106.73 ? 1980 GLU A O     1 
ATOM   2893  C CB    . GLU A 1 1980 ? 202.353 165.799 151.013 1.00 106.73 ? 1980 GLU A CB    1 
ATOM   2894  C CG    . GLU A 1 1980 ? 201.544 164.755 151.758 1.00 106.73 ? 1980 GLU A CG    1 
ATOM   2895  C CD    . GLU A 1 1980 ? 202.337 163.501 152.052 1.00 106.73 ? 1980 GLU A CD    1 
ATOM   2896  O OE1   . GLU A 1 1980 ? 203.583 163.563 152.020 1.00 106.73 ? 1980 GLU A OE1   1 
ATOM   2897  O OE2   . GLU A 1 1980 ? 201.712 162.454 152.322 1.00 106.73 ? 1980 GLU A OE2   1 
ATOM   2898  N N     . ALA A 1 1981 ? 203.470 168.758 150.535 1.00 110.32 ? 1981 ALA A N     1 
ATOM   2899  C CA    . ALA A 1 1981 ? 204.347 169.720 149.877 1.00 110.32 ? 1981 ALA A CA    1 
ATOM   2900  C C     . ALA A 1 1981 ? 205.330 170.324 150.871 1.00 110.32 ? 1981 ALA A C     1 
ATOM   2901  O O     . ALA A 1 1981 ? 206.528 170.438 150.587 1.00 110.32 ? 1981 ALA A O     1 
ATOM   2902  C CB    . ALA A 1 1981 ? 203.520 170.815 149.208 1.00 110.32 ? 1981 ALA A CB    1 
ATOM   2903  N N     . LEU A 1 1982 ? 204.842 170.696 152.053 1.00 107.31 ? 1982 LEU A N     1 
ATOM   2904  C CA    . LEU A 1 1982 ? 205.722 171.273 153.064 1.00 107.31 ? 1982 LEU A CA    1 
ATOM   2905  C C     . LEU A 1 1982 ? 206.793 170.280 153.500 1.00 107.31 ? 1982 LEU A C     1 
ATOM   2906  O O     . LEU A 1 1982 ? 207.957 170.653 153.685 1.00 107.31 ? 1982 LEU A O     1 
ATOM   2907  C CB    . LEU A 1 1982 ? 204.905 171.737 154.266 1.00 107.31 ? 1982 LEU A CB    1 
ATOM   2908  C CG    . LEU A 1 1982 ? 205.385 173.024 154.934 1.00 107.31 ? 1982 LEU A CG    1 
ATOM   2909  C CD1   . LEU A 1 1982 ? 205.729 174.074 153.896 1.00 107.31 ? 1982 LEU A CD1   1 
ATOM   2910  C CD2   . LEU A 1 1982 ? 204.342 173.536 155.907 1.00 107.31 ? 1982 LEU A CD2   1 
ATOM   2911  N N     . ARG A 1 1983 ? 206.416 169.015 153.684 1.00 109.43 ? 1983 ARG A N     1 
ATOM   2912  C CA    . ARG A 1 1983 ? 207.386 168.004 154.088 1.00 109.43 ? 1983 ARG A CA    1 
ATOM   2913  C C     . ARG A 1 1983 ? 208.445 167.803 153.016 1.00 109.43 ? 1983 ARG A C     1 
ATOM   2914  O O     . ARG A 1 1983 ? 209.638 167.698 153.321 1.00 109.43 ? 1983 ARG A O     1 
ATOM   2915  C CB    . ARG A 1 1983 ? 206.679 166.685 154.391 1.00 109.43 ? 1983 ARG A CB    1 
ATOM   2916  C CG    . ARG A 1 1983 ? 205.898 166.680 155.688 1.00 109.43 ? 1983 ARG A CG    1 
ATOM   2917  C CD    . ARG A 1 1983 ? 206.302 165.513 156.569 1.00 109.43 ? 1983 ARG A CD    1 
ATOM   2918  N NE    . ARG A 1 1983 ? 207.701 165.592 156.968 1.00 109.43 ? 1983 ARG A NE    1 
ATOM   2919  C CZ    . ARG A 1 1983 ? 208.219 164.951 158.005 1.00 109.43 ? 1983 ARG A CZ    1 
ATOM   2920  N NH1   . ARG A 1 1983 ? 207.481 164.164 158.770 1.00 109.43 ? 1983 ARG A NH1   1 
ATOM   2921  N NH2   . ARG A 1 1983 ? 209.510 165.105 158.284 1.00 109.43 ? 1983 ARG A NH2   1 
ATOM   2922  N N     . GLU A 1 1984 ? 208.027 167.749 151.750 1.00 129.54 ? 1984 GLU A N     1 
ATOM   2923  C CA    . GLU A 1 1984 ? 208.987 167.649 150.658 1.00 129.54 ? 1984 GLU A CA    1 
ATOM   2924  C C     . GLU A 1 1984 ? 209.867 168.886 150.559 1.00 129.54 ? 1984 GLU A C     1 
ATOM   2925  O O     . GLU A 1 1984 ? 210.985 168.798 150.043 1.00 129.54 ? 1984 GLU A O     1 
ATOM   2926  C CB    . GLU A 1 1984 ? 208.257 167.417 149.335 1.00 129.54 ? 1984 GLU A CB    1 
ATOM   2927  C CG    . GLU A 1 1984 ? 207.897 165.963 149.076 1.00 129.54 ? 1984 GLU A CG    1 
ATOM   2928  C CD    . GLU A 1 1984 ? 207.022 165.790 147.851 1.00 129.54 ? 1984 GLU A CD    1 
ATOM   2929  O OE1   . GLU A 1 1984 ? 206.698 164.634 147.506 1.00 129.54 ? 1984 GLU A OE1   1 
ATOM   2930  O OE2   . GLU A 1 1984 ? 206.655 166.811 147.235 1.00 129.54 ? 1984 GLU A OE2   1 
ATOM   2931  N N     . HIS A 1 1985 ? 209.387 170.031 151.049 1.00 129.94 ? 1985 HIS A N     1 
ATOM   2932  C CA    . HIS A 1 1985 ? 210.191 171.247 151.026 1.00 129.94 ? 1985 HIS A CA    1 
ATOM   2933  C C     . HIS A 1 1985 ? 211.452 171.129 151.873 1.00 129.94 ? 1985 HIS A C     1 
ATOM   2934  O O     . HIS A 1 1985 ? 212.368 171.942 151.712 1.00 129.94 ? 1985 HIS A O     1 
ATOM   2935  C CB    . HIS A 1 1985 ? 209.354 172.433 151.503 1.00 129.94 ? 1985 HIS A CB    1 
ATOM   2936  C CG    . HIS A 1 1985 ? 209.794 173.749 150.943 1.00 129.94 ? 1985 HIS A CG    1 
ATOM   2937  N ND1   . HIS A 1 1985 ? 209.059 174.441 150.005 1.00 129.94 ? 1985 HIS A ND1   1 
ATOM   2938  C CD2   . HIS A 1 1985 ? 210.888 174.505 151.197 1.00 129.94 ? 1985 HIS A CD2   1 
ATOM   2939  C CE1   . HIS A 1 1985 ? 209.685 175.563 149.699 1.00 129.94 ? 1985 HIS A CE1   1 
ATOM   2940  N NE2   . HIS A 1 1985 ? 210.797 175.627 150.409 1.00 129.94 ? 1985 HIS A NE2   1 
ATOM   2941  N N     . SER A 1 1986 ? 211.525 170.149 152.769 1.00 135.39 ? 1986 SER A N     1 
ATOM   2942  C CA    . SER A 1 1986 ? 212.694 169.942 153.613 1.00 135.39 ? 1986 SER A CA    1 
ATOM   2943  C C     . SER A 1 1986 ? 213.245 168.531 153.458 1.00 135.39 ? 1986 SER A C     1 
ATOM   2944  O O     . SER A 1 1986 ? 213.570 167.861 154.440 1.00 135.39 ? 1986 SER A O     1 
ATOM   2945  C CB    . SER A 1 1986 ? 212.373 170.223 155.077 1.00 135.39 ? 1986 SER A CB    1 
ATOM   2946  O OG    . SER A 1 1986 ? 211.928 169.047 155.729 1.00 135.39 ? 1986 SER A OG    1 
ATOM   2947  N N     . ASN A 1 1987 ? 213.347 168.061 152.225 1.00 158.85 ? 1987 ASN A N     1 
ATOM   2948  C CA    . ASN A 1 1987 ? 213.978 166.772 151.980 1.00 158.85 ? 1987 ASN A CA    1 
ATOM   2949  C C     . ASN A 1 1987 ? 215.469 166.874 152.278 1.00 158.85 ? 1987 ASN A C     1 
ATOM   2950  O O     . ASN A 1 1987 ? 216.139 167.770 151.753 1.00 158.85 ? 1987 ASN A O     1 
ATOM   2951  C CB    . ASN A 1 1987 ? 213.755 166.330 150.538 1.00 158.85 ? 1987 ASN A CB    1 
ATOM   2952  C CG    . ASN A 1 1987 ? 212.362 165.791 150.306 1.00 158.85 ? 1987 ASN A CG    1 
ATOM   2953  O OD1   . ASN A 1 1987 ? 211.626 165.516 151.252 1.00 158.85 ? 1987 ASN A OD1   1 
ATOM   2954  N ND2   . ASN A 1 1987 ? 211.991 165.635 149.041 1.00 158.85 ? 1987 ASN A ND2   1 
ATOM   2955  N N     . PRO A 1 1988 ? 216.019 165.995 153.119 1.00 174.66 ? 1988 PRO A N     1 
ATOM   2956  C CA    . PRO A 1 1988 ? 217.462 166.074 153.408 1.00 174.66 ? 1988 PRO A CA    1 
ATOM   2957  C C     . PRO A 1 1988 ? 218.326 165.923 152.170 1.00 174.66 ? 1988 PRO A C     1 
ATOM   2958  O O     . PRO A 1 1988 ? 219.382 166.560 152.072 1.00 174.66 ? 1988 PRO A O     1 
ATOM   2959  C CB    . PRO A 1 1988 ? 217.682 164.926 154.404 1.00 174.66 ? 1988 PRO A CB    1 
ATOM   2960  C CG    . PRO A 1 1988 ? 216.537 163.992 154.170 1.00 174.66 ? 1988 PRO A CG    1 
ATOM   2961  C CD    . PRO A 1 1988 ? 215.375 164.858 153.796 1.00 174.66 ? 1988 PRO A CD    1 
ATOM   2962  N N     . ASN A 1 1989 ? 217.901 165.092 151.217 1.00 176.75 ? 1989 ASN A N     1 
ATOM   2963  C CA    . ASN A 1 1989 ? 218.628 164.955 149.961 1.00 176.75 ? 1989 ASN A CA    1 
ATOM   2964  C C     . ASN A 1 1989 ? 218.416 166.154 149.046 1.00 176.75 ? 1989 ASN A C     1 
ATOM   2965  O O     . ASN A 1 1989 ? 219.300 166.482 148.247 1.00 176.75 ? 1989 ASN A O     1 
ATOM   2966  C CB    . ASN A 1 1989 ? 218.201 163.670 149.251 1.00 176.75 ? 1989 ASN A CB    1 
ATOM   2967  C CG    . ASN A 1 1989 ? 216.700 163.461 149.280 1.00 176.75 ? 1989 ASN A CG    1 
ATOM   2968  O OD1   . ASN A 1 1989 ? 216.096 163.365 150.349 1.00 176.75 ? 1989 ASN A OD1   1 
ATOM   2969  N ND2   . ASN A 1 1989 ? 216.088 163.388 148.104 1.00 176.75 ? 1989 ASN A ND2   1 
ATOM   2970  N N     . TYR A 1 1990 ? 217.267 166.813 149.149 1.00 180.09 ? 1990 TYR A N     1 
ATOM   2971  C CA    . TYR A 1 1990 ? 216.908 167.937 148.296 1.00 180.09 ? 1990 TYR A CA    1 
ATOM   2972  C C     . TYR A 1 1990 ? 216.723 169.206 149.118 1.00 180.09 ? 1990 TYR A C     1 
ATOM   2973  O O     . TYR A 1 1990 ? 215.772 169.964 148.918 1.00 180.09 ? 1990 TYR A O     1 
ATOM   2974  C CB    . TYR A 1 1990 ? 215.647 167.625 147.494 1.00 180.09 ? 1990 TYR A CB    1 
ATOM   2975  C CG    . TYR A 1 1990 ? 215.487 168.449 146.236 1.00 180.09 ? 1990 TYR A CG    1 
ATOM   2976  C CD1   . TYR A 1 1990 ? 216.595 168.920 145.545 1.00 180.09 ? 1990 TYR A CD1   1 
ATOM   2977  C CD2   . TYR A 1 1990 ? 214.227 168.749 145.737 1.00 180.09 ? 1990 TYR A CD2   1 
ATOM   2978  C CE1   . TYR A 1 1990 ? 216.452 169.671 144.393 1.00 180.09 ? 1990 TYR A CE1   1 
ATOM   2979  C CE2   . TYR A 1 1990 ? 214.074 169.499 144.587 1.00 180.09 ? 1990 TYR A CE2   1 
ATOM   2980  C CZ    . TYR A 1 1990 ? 215.189 169.958 143.919 1.00 180.09 ? 1990 TYR A CZ    1 
ATOM   2981  O OH    . TYR A 1 1990 ? 215.039 170.705 142.774 1.00 180.09 ? 1990 TYR A OH    1 
ATOM   2982  N N     . ASP A 1 1991 ? 217.630 169.442 150.069 1.00 181.41 ? 1991 ASP A N     1 
ATOM   2983  C CA    . ASP A 1 1991 ? 217.568 170.672 150.851 1.00 181.41 ? 1991 ASP A CA    1 
ATOM   2984  C C     . ASP A 1 1991 ? 217.752 171.895 149.963 1.00 181.41 ? 1991 ASP A C     1 
ATOM   2985  O O     . ASP A 1 1991 ? 217.060 172.906 150.134 1.00 181.41 ? 1991 ASP A O     1 
ATOM   2986  C CB    . ASP A 1 1991 ? 218.620 170.650 151.959 1.00 181.41 ? 1991 ASP A CB    1 
ATOM   2987  C CG    . ASP A 1 1991 ? 218.135 171.311 153.233 1.00 181.41 ? 1991 ASP A CG    1 
ATOM   2988  O OD1   . ASP A 1 1991 ? 216.921 171.582 153.339 1.00 181.41 ? 1991 ASP A OD1   1 
ATOM   2989  O OD2   . ASP A 1 1991 ? 218.969 171.564 154.128 1.00 181.41 ? 1991 ASP A OD2   1 
ATOM   2990  N N     . LYS A 1 1992 ? 218.678 171.822 149.008 1.00 188.24 ? 1992 LYS A N     1 
ATOM   2991  C CA    . LYS A 1 1992 ? 218.853 172.878 148.014 1.00 188.24 ? 1992 LYS A CA    1 
ATOM   2992  C C     . LYS A 1 1992 ? 217.712 172.755 147.014 1.00 188.24 ? 1992 LYS A C     1 
ATOM   2993  O O     . LYS A 1 1992 ? 217.809 172.060 146.002 1.00 188.24 ? 1992 LYS A O     1 
ATOM   2994  C CB    . LYS A 1 1992 ? 220.212 172.770 147.333 1.00 188.24 ? 1992 LYS A CB    1 
ATOM   2995  C CG    . LYS A 1 1992 ? 220.454 173.835 146.277 1.00 188.24 ? 1992 LYS A CG    1 
ATOM   2996  C CD    . LYS A 1 1992 ? 220.167 175.223 146.825 1.00 188.24 ? 1992 LYS A CD    1 
ATOM   2997  C CE    . LYS A 1 1992 ? 219.772 176.185 145.720 1.00 188.24 ? 1992 LYS A CE    1 
ATOM   2998  N NZ    . LYS A 1 1992 ? 218.512 175.759 145.052 1.00 188.24 ? 1992 LYS A NZ    1 
ATOM   2999  N N     . THR A 1 1993 ? 216.611 173.437 147.310 1.00 185.41 ? 1993 THR A N     1 
ATOM   3000  C CA    . THR A 1 1993 ? 215.394 173.327 146.512 1.00 185.41 ? 1993 THR A CA    1 
ATOM   3001  C C     . THR A 1 1993 ? 215.594 174.065 145.195 1.00 185.41 ? 1993 THR A C     1 
ATOM   3002  O O     . THR A 1 1993 ? 215.427 175.283 145.116 1.00 185.41 ? 1993 THR A O     1 
ATOM   3003  C CB    . THR A 1 1993 ? 214.204 173.884 147.284 1.00 185.41 ? 1993 THR A CB    1 
ATOM   3004  O OG1   . THR A 1 1993 ? 214.023 173.129 148.489 1.00 185.41 ? 1993 THR A OG1   1 
ATOM   3005  C CG2   . THR A 1 1993 ? 212.937 173.796 146.450 1.00 185.41 ? 1993 THR A CG2   1 
ATOM   3006  N N     . SER A 1 1994 ? 215.963 173.323 144.151 1.00 191.03 ? 1994 SER A N     1 
ATOM   3007  C CA    . SER A 1 1994 ? 216.109 173.897 142.817 1.00 191.03 ? 1994 SER A CA    1 
ATOM   3008  C C     . SER A 1 1994 ? 214.761 173.967 142.107 1.00 191.03 ? 1994 SER A C     1 
ATOM   3009  O O     . SER A 1 1994 ? 214.305 175.052 141.729 1.00 191.03 ? 1994 SER A O     1 
ATOM   3010  C CB    . SER A 1 1994 ? 217.114 173.080 141.998 1.00 191.03 ? 1994 SER A CB    1 
ATOM   3011  O OG    . SER A 1 1994 ? 217.105 173.480 140.639 1.00 191.03 ? 1994 SER A OG    1 
ATOM   3012  N N     . ALA A 1 1995 ? 214.114 172.824 141.926 1.00 183.87 ? 1995 ALA A N     1 
ATOM   3013  C CA    . ALA A 1 1995 ? 212.753 172.819 141.411 1.00 183.87 ? 1995 ALA A CA    1 
ATOM   3014  C C     . ALA A 1 1995 ? 211.811 173.338 142.491 1.00 183.87 ? 1995 ALA A C     1 
ATOM   3015  O O     . ALA A 1 1995 ? 211.832 172.827 143.616 1.00 183.87 ? 1995 ALA A O     1 
ATOM   3016  C CB    . ALA A 1 1995 ? 212.344 171.415 140.977 1.00 183.87 ? 1995 ALA A CB    1 
ATOM   3017  N N     . PRO A 1 1996 ? 210.989 174.345 142.202 1.00 168.66 ? 1996 PRO A N     1 
ATOM   3018  C CA    . PRO A 1 1996 ? 210.116 174.896 143.245 1.00 168.66 ? 1996 PRO A CA    1 
ATOM   3019  C C     . PRO A 1 1996 ? 209.132 173.850 143.746 1.00 168.66 ? 1996 PRO A C     1 
ATOM   3020  O O     . PRO A 1 1996 ? 208.621 173.033 142.979 1.00 168.66 ? 1996 PRO A O     1 
ATOM   3021  C CB    . PRO A 1 1996 ? 209.402 176.061 142.549 1.00 168.66 ? 1996 PRO A CB    1 
ATOM   3022  C CG    . PRO A 1 1996 ? 209.657 175.912 141.093 1.00 168.66 ? 1996 PRO A CG    1 
ATOM   3023  C CD    . PRO A 1 1996 ? 210.657 174.830 140.853 1.00 168.66 ? 1996 PRO A CD    1 
ATOM   3024  N N     . ILE A 1 1997 ? 208.874 173.879 145.050 1.00 145.48 ? 1997 ILE A N     1 
ATOM   3025  C CA    . ILE A 1 1997 ? 208.002 172.891 145.673 1.00 145.48 ? 1997 ILE A CA    1 
ATOM   3026  C C     . ILE A 1 1997 ? 206.558 173.278 145.387 1.00 145.48 ? 1997 ILE A C     1 
ATOM   3027  O O     . ILE A 1 1997 ? 206.122 174.384 145.722 1.00 145.48 ? 1997 ILE A O     1 
ATOM   3028  C CB    . ILE A 1 1997 ? 208.261 172.791 147.181 1.00 145.48 ? 1997 ILE A CB    1 
ATOM   3029  C CG1   . ILE A 1 1997 ? 209.688 172.309 147.451 1.00 145.48 ? 1997 ILE A CG1   1 
ATOM   3030  C CG2   . ILE A 1 1997 ? 207.269 171.843 147.814 1.00 145.48 ? 1997 ILE A CG2   1 
ATOM   3031  C CD1   . ILE A 1 1997 ? 210.111 171.125 146.610 1.00 145.48 ? 1997 ILE A CD1   1 
ATOM   3032  N N     . THR A 1 1998 ? 205.815 172.370 144.768 1.00 145.34 ? 1998 THR A N     1 
ATOM   3033  C CA    . THR A 1 1998 ? 204.476 172.658 144.285 1.00 145.34 ? 1998 THR A CA    1 
ATOM   3034  C C     . THR A 1 1998 ? 203.471 171.687 144.886 1.00 145.34 ? 1998 THR A C     1 
ATOM   3035  O O     . THR A 1 1998 ? 203.824 170.615 145.385 1.00 145.34 ? 1998 THR A O     1 
ATOM   3036  C CB    . THR A 1 1998 ? 204.412 172.583 142.757 1.00 145.34 ? 1998 THR A CB    1 
ATOM   3037  O OG1   . THR A 1 1998 ? 204.522 171.216 142.344 1.00 145.34 ? 1998 THR A OG1   1 
ATOM   3038  C CG2   . THR A 1 1998 ? 205.542 173.388 142.135 1.00 145.34 ? 1998 THR A CG2   1 
ATOM   3039  N N     . CYS A 1 1999 ? 202.203 172.081 144.823 1.00 144.56 ? 1999 CYS A N     1 
ATOM   3040  C CA    . CYS A 1 1999 ? 201.102 171.324 145.396 1.00 144.56 ? 1999 CYS A CA    1 
ATOM   3041  C C     . CYS A 1 1999 ? 199.881 171.416 144.486 1.00 144.56 ? 1999 CYS A C     1 
ATOM   3042  O O     . CYS A 1 1999 ? 199.831 172.222 143.552 1.00 144.56 ? 1999 CYS A O     1 
ATOM   3043  C CB    . CYS A 1 1999 ? 200.789 171.826 146.809 1.00 144.56 ? 1999 CYS A CB    1 
ATOM   3044  S SG    . CYS A 1 1999 ? 200.204 173.527 146.853 1.00 144.56 ? 1999 CYS A SG    1 
ATOM   3045  N N     . GLU A 1 2000 ? 198.888 170.572 144.768 1.00 145.46 ? 2000 GLU A N     1 
ATOM   3046  C CA    . GLU A 1 2000 ? 197.700 170.432 143.924 1.00 145.46 ? 2000 GLU A CA    1 
ATOM   3047  C C     . GLU A 1 2000 ? 196.475 170.957 144.669 1.00 145.46 ? 2000 GLU A C     1 
ATOM   3048  O O     . GLU A 1 2000 ? 195.831 170.239 145.433 1.00 145.46 ? 2000 GLU A O     1 
ATOM   3049  C CB    . GLU A 1 2000 ? 197.514 168.977 143.507 1.00 145.46 ? 2000 GLU A CB    1 
ATOM   3050  C CG    . GLU A 1 2000 ? 197.080 168.786 142.063 1.00 145.46 ? 2000 GLU A CG    1 
ATOM   3051  C CD    . GLU A 1 2000 ? 197.144 167.335 141.625 1.00 145.46 ? 2000 GLU A CD    1 
ATOM   3052  O OE1   . GLU A 1 2000 ? 196.273 166.909 140.840 1.00 145.46 ? 2000 GLU A OE1   1 
ATOM   3053  O OE2   . GLU A 1 2000 ? 198.073 166.622 142.058 1.00 145.46 ? 2000 GLU A OE2   1 
ATOM   3054  N N     . LEU A 1 2001 ? 196.148 172.224 144.432 1.00 138.99 ? 2001 LEU A N     1 
ATOM   3055  C CA    . LEU A 1 2001 ? 194.894 172.820 144.874 1.00 138.99 ? 2001 LEU A CA    1 
ATOM   3056  C C     . LEU A 1 2001 ? 194.175 173.433 143.683 1.00 138.99 ? 2001 LEU A C     1 
ATOM   3057  O O     . LEU A 1 2001 ? 194.811 173.982 142.778 1.00 138.99 ? 2001 LEU A O     1 
ATOM   3058  C CB    . LEU A 1 2001 ? 195.094 173.889 145.963 1.00 138.99 ? 2001 LEU A CB    1 
ATOM   3059  C CG    . LEU A 1 2001 ? 195.614 173.569 147.372 1.00 138.99 ? 2001 LEU A CG    1 
ATOM   3060  C CD1   . LEU A 1 2001 ? 194.589 172.734 148.117 1.00 138.99 ? 2001 LEU A CD1   1 
ATOM   3061  C CD2   . LEU A 1 2001 ? 196.957 172.877 147.391 1.00 138.99 ? 2001 LEU A CD2   1 
ATOM   3062  N N     . LEU A 1 2002 ? 192.846 173.324 143.688 1.00 139.86 ? 2002 LEU A N     1 
ATOM   3063  C CA    . LEU A 1 2002 ? 192.006 173.838 142.606 1.00 139.86 ? 2002 LEU A CA    1 
ATOM   3064  C C     . LEU A 1 2002 ? 192.406 173.233 141.264 1.00 139.86 ? 2002 LEU A C     1 
ATOM   3065  O O     . LEU A 1 2002 ? 192.318 173.881 140.218 1.00 139.86 ? 2002 LEU A O     1 
ATOM   3066  C CB    . LEU A 1 2002 ? 192.047 175.366 142.549 1.00 139.86 ? 2002 LEU A CB    1 
ATOM   3067  C CG    . LEU A 1 2002 ? 191.377 176.088 143.717 1.00 139.86 ? 2002 LEU A CG    1 
ATOM   3068  C CD1   . LEU A 1 2002 ? 191.232 177.567 143.407 1.00 139.86 ? 2002 LEU A CD1   1 
ATOM   3069  C CD2   . LEU A 1 2002 ? 190.027 175.461 144.039 1.00 139.86 ? 2002 LEU A CD2   1 
ATOM   3070  N N     . ASN A 1 2003 ? 192.851 171.977 141.303 1.00 145.54 ? 2003 ASN A N     1 
ATOM   3071  C CA    . ASN A 1 2003 ? 193.254 171.236 140.109 1.00 145.54 ? 2003 ASN A CA    1 
ATOM   3072  C C     . ASN A 1 2003 ? 194.327 171.984 139.323 1.00 145.54 ? 2003 ASN A C     1 
ATOM   3073  O O     . ASN A 1 2003 ? 194.313 172.007 138.091 1.00 145.54 ? 2003 ASN A O     1 
ATOM   3074  C CB    . ASN A 1 2003 ? 192.047 170.929 139.222 1.00 145.54 ? 2003 ASN A CB    1 
ATOM   3075  C CG    . ASN A 1 2003 ? 190.861 170.422 140.012 1.00 145.54 ? 2003 ASN A CG    1 
ATOM   3076  O OD1   . ASN A 1 2003 ? 190.940 169.395 140.685 1.00 145.54 ? 2003 ASN A OD1   1 
ATOM   3077  N ND2   . ASN A 1 2003 ? 189.751 171.147 139.940 1.00 145.54 ? 2003 ASN A ND2   1 
ATOM   3078  N N     . LYS A 1 2004 ? 195.263 172.607 140.034 1.00 140.20 ? 2004 LYS A N     1 
ATOM   3079  C CA    . LYS A 1 2004 ? 196.326 173.343 139.366 1.00 140.20 ? 2004 LYS A CA    1 
ATOM   3080  C C     . LYS A 1 2004 ? 197.549 173.394 140.269 1.00 140.20 ? 2004 LYS A C     1 
ATOM   3081  O O     . LYS A 1 2004 ? 197.458 173.218 141.486 1.00 140.20 ? 2004 LYS A O     1 
ATOM   3082  C CB    . LYS A 1 2004 ? 195.877 174.756 138.980 1.00 140.20 ? 2004 LYS A CB    1 
ATOM   3083  C CG    . LYS A 1 2004 ? 195.972 175.769 140.102 1.00 140.20 ? 2004 LYS A CG    1 
ATOM   3084  C CD    . LYS A 1 2004 ? 195.707 177.172 139.586 1.00 140.20 ? 2004 LYS A CD    1 
ATOM   3085  C CE    . LYS A 1 2004 ? 196.906 177.712 138.825 1.00 140.20 ? 2004 LYS A CE    1 
ATOM   3086  N NZ    . LYS A 1 2004 ? 198.070 177.968 139.717 1.00 140.20 ? 2004 LYS A NZ    1 
ATOM   3087  N N     . GLN A 1 2005 ? 198.697 173.642 139.645 1.00 140.68 ? 2005 GLN A N     1 
ATOM   3088  C CA    . GLN A 1 2005 ? 199.959 173.719 140.367 1.00 140.68 ? 2005 GLN A CA    1 
ATOM   3089  C C     . GLN A 1 2005 ? 200.052 175.024 141.148 1.00 140.68 ? 2005 GLN A C     1 
ATOM   3090  O O     . GLN A 1 2005 ? 199.815 176.106 140.601 1.00 140.68 ? 2005 GLN A O     1 
ATOM   3091  C CB    . GLN A 1 2005 ? 201.122 173.597 139.384 1.00 140.68 ? 2005 GLN A CB    1 
ATOM   3092  C CG    . GLN A 1 2005 ? 202.495 173.864 139.968 1.00 140.68 ? 2005 GLN A CG    1 
ATOM   3093  C CD    . GLN A 1 2005 ? 202.953 175.286 139.716 1.00 140.68 ? 2005 GLN A CD    1 
ATOM   3094  O OE1   . GLN A 1 2005 ? 202.238 176.077 139.100 1.00 140.68 ? 2005 GLN A OE1   1 
ATOM   3095  N NE2   . GLN A 1 2005 ? 204.152 175.616 140.177 1.00 140.68 ? 2005 GLN A NE2   1 
ATOM   3096  N N     . VAL A 1 2006 ? 200.391 174.922 142.432 1.00 134.86 ? 2006 VAL A N     1 
ATOM   3097  C CA    . VAL A 1 2006 ? 200.548 176.078 143.307 1.00 134.86 ? 2006 VAL A CA    1 
ATOM   3098  C C     . VAL A 1 2006 ? 201.887 175.977 144.020 1.00 134.86 ? 2006 VAL A C     1 
ATOM   3099  O O     . VAL A 1 2006 ? 202.221 174.926 144.579 1.00 134.86 ? 2006 VAL A O     1 
ATOM   3100  C CB    . VAL A 1 2006 ? 199.406 176.190 144.333 1.00 134.86 ? 2006 VAL A CB    1 
ATOM   3101  C CG1   . VAL A 1 2006 ? 199.310 177.613 144.844 1.00 134.86 ? 2006 VAL A CG1   1 
ATOM   3102  C CG2   . VAL A 1 2006 ? 198.085 175.748 143.723 1.00 134.86 ? 2006 VAL A CG2   1 
ATOM   3103  N N     . LYS A 1 2007 ? 202.649 177.067 144.003 1.00 127.09 ? 2007 LYS A N     1 
ATOM   3104  C CA    . LYS A 1 2007 ? 203.923 177.108 144.704 1.00 127.09 ? 2007 LYS A CA    1 
ATOM   3105  C C     . LYS A 1 2007 ? 203.701 177.346 146.193 1.00 127.09 ? 2007 LYS A C     1 
ATOM   3106  O O     . LYS A 1 2007 ? 202.857 178.154 146.588 1.00 127.09 ? 2007 LYS A O     1 
ATOM   3107  C CB    . LYS A 1 2007 ? 204.809 178.205 144.115 1.00 127.09 ? 2007 LYS A CB    1 
ATOM   3108  C CG    . LYS A 1 2007 ? 206.050 178.521 144.927 1.00 127.09 ? 2007 LYS A CG    1 
ATOM   3109  C CD    . LYS A 1 2007 ? 207.019 177.354 144.916 1.00 127.09 ? 2007 LYS A CD    1 
ATOM   3110  C CE    . LYS A 1 2007 ? 208.058 177.486 146.014 1.00 127.09 ? 2007 LYS A CE    1 
ATOM   3111  N NZ    . LYS A 1 2007 ? 208.669 178.843 146.031 1.00 127.09 ? 2007 LYS A NZ    1 
ATOM   3112  N N     . VAL A 1 2008 ? 204.465 176.641 147.022 1.00 116.66 ? 2008 VAL A N     1 
ATOM   3113  C CA    . VAL A 1 2008 ? 204.341 176.722 148.473 1.00 116.66 ? 2008 VAL A CA    1 
ATOM   3114  C C     . VAL A 1 2008 ? 205.560 177.452 149.013 1.00 116.66 ? 2008 VAL A C     1 
ATOM   3115  O O     . VAL A 1 2008 ? 206.690 176.966 148.892 1.00 116.66 ? 2008 VAL A O     1 
ATOM   3116  C CB    . VAL A 1 2008 ? 204.214 175.336 149.115 1.00 116.66 ? 2008 VAL A CB    1 
ATOM   3117  C CG1   . VAL A 1 2008 ? 204.279 175.458 150.620 1.00 116.66 ? 2008 VAL A CG1   1 
ATOM   3118  C CG2   . VAL A 1 2008 ? 202.923 174.681 148.696 1.00 116.66 ? 2008 VAL A CG2   1 
ATOM   3119  N N     . SER A 1 2009 ? 205.335 178.611 149.617 1.00 106.98 ? 2009 SER A N     1 
ATOM   3120  C CA    . SER A 1 2009 ? 206.419 179.312 150.282 1.00 106.98 ? 2009 SER A CA    1 
ATOM   3121  C C     . SER A 1 2009 ? 206.803 178.570 151.561 1.00 106.98 ? 2009 SER A C     1 
ATOM   3122  O O     . SER A 1 2009 ? 205.927 178.069 152.273 1.00 106.98 ? 2009 SER A O     1 
ATOM   3123  C CB    . SER A 1 2009 ? 206.010 180.747 150.604 1.00 106.98 ? 2009 SER A CB    1 
ATOM   3124  O OG    . SER A 1 2009 ? 207.132 181.534 150.959 1.00 106.98 ? 2009 SER A OG    1 
ATOM   3125  N N     . PRO A 1 2010 ? 208.097 178.478 151.880 1.00 102.24 ? 2010 PRO A N     1 
ATOM   3126  C CA    . PRO A 1 2010 ? 208.505 177.708 153.065 1.00 102.24 ? 2010 PRO A CA    1 
ATOM   3127  C C     . PRO A 1 2010 ? 207.997 178.287 154.369 1.00 102.24 ? 2010 PRO A C     1 
ATOM   3128  O O     . PRO A 1 2010 ? 207.923 177.556 155.364 1.00 102.24 ? 2010 PRO A O     1 
ATOM   3129  C CB    . PRO A 1 2010 ? 210.036 177.749 153.000 1.00 102.24 ? 2010 PRO A CB    1 
ATOM   3130  C CG    . PRO A 1 2010 ? 210.336 178.997 152.257 1.00 102.24 ? 2010 PRO A CG    1 
ATOM   3131  C CD    . PRO A 1 2010 ? 209.243 179.141 151.236 1.00 102.24 ? 2010 PRO A CD    1 
ATOM   3132  N N     . ASP A 1 2011 ? 207.646 179.569 154.400 1.00 98.12  ? 2011 ASP A N     1 
ATOM   3133  C CA    . ASP A 1 2011 ? 207.200 180.201 155.631 1.00 98.12  ? 2011 ASP A CA    1 
ATOM   3134  C C     . ASP A 1 2011 ? 205.755 179.878 155.974 1.00 98.12  ? 2011 ASP A C     1 
ATOM   3135  O O     . ASP A 1 2011 ? 205.344 180.102 157.117 1.00 98.12  ? 2011 ASP A O     1 
ATOM   3136  C CB    . ASP A 1 2011 ? 207.374 181.716 155.526 1.00 98.12  ? 2011 ASP A CB    1 
ATOM   3137  C CG    . ASP A 1 2011 ? 208.750 182.109 155.028 1.00 98.12  ? 2011 ASP A CG    1 
ATOM   3138  O OD1   . ASP A 1 2011 ? 209.751 181.611 155.583 1.00 98.12  ? 2011 ASP A OD1   1 
ATOM   3139  O OD2   . ASP A 1 2011 ? 208.831 182.916 154.078 1.00 98.12  ? 2011 ASP A OD2   1 
ATOM   3140  N N     . MET A 1 2012 ? 204.988 179.349 155.028 1.00 91.79  ? 2012 MET A N     1 
ATOM   3141  C CA    . MET A 1 2012 ? 203.581 179.070 155.262 1.00 91.79  ? 2012 MET A CA    1 
ATOM   3142  C C     . MET A 1 2012 ? 203.431 178.001 156.338 1.00 91.79  ? 2012 MET A C     1 
ATOM   3143  O O     . MET A 1 2012 ? 204.246 177.084 156.451 1.00 91.79  ? 2012 MET A O     1 
ATOM   3144  C CB    . MET A 1 2012 ? 202.916 178.651 153.945 1.00 91.79  ? 2012 MET A CB    1 
ATOM   3145  C CG    . MET A 1 2012 ? 201.477 178.114 153.989 1.00 91.79  ? 2012 MET A CG    1 
ATOM   3146  S SD    . MET A 1 2012 ? 201.174 176.559 154.845 1.00 91.79  ? 2012 MET A SD    1 
ATOM   3147  C CE    . MET A 1 2012 ? 202.174 175.466 153.846 1.00 91.79  ? 2012 MET A CE    1 
ATOM   3148  N N     . ALA A 1 2013 ? 202.376 178.131 157.139 1.00 77.86  ? 2013 ALA A N     1 
ATOM   3149  C CA    . ALA A 1 2013 ? 202.118 177.191 158.218 1.00 77.86  ? 2013 ALA A CA    1 
ATOM   3150  C C     . ALA A 1 2013 ? 200.619 176.999 158.379 1.00 77.86  ? 2013 ALA A C     1 
ATOM   3151  O O     . ALA A 1 2013 ? 199.842 177.938 158.191 1.00 77.86  ? 2013 ALA A O     1 
ATOM   3152  C CB    . ALA A 1 2013 ? 202.731 177.671 159.534 1.00 77.86  ? 2013 ALA A CB    1 
ATOM   3153  N N     . ILE A 1 2014 ? 200.225 175.780 158.735 1.00 72.40  ? 2014 ILE A N     1 
ATOM   3154  C CA    . ILE A 1 2014 ? 198.828 175.406 158.910 1.00 72.40  ? 2014 ILE A CA    1 
ATOM   3155  C C     . ILE A 1 2014 ? 198.669 174.785 160.288 1.00 72.40  ? 2014 ILE A C     1 
ATOM   3156  O O     . ILE A 1 2014 ? 199.451 173.908 160.669 1.00 72.40  ? 2014 ILE A O     1 
ATOM   3157  C CB    . ILE A 1 2014 ? 198.365 174.429 157.817 1.00 72.40  ? 2014 ILE A CB    1 
ATOM   3158  C CG1   . ILE A 1 2014 ? 198.097 175.181 156.516 1.00 72.40  ? 2014 ILE A CG1   1 
ATOM   3159  C CG2   . ILE A 1 2014 ? 197.130 173.676 158.262 1.00 72.40  ? 2014 ILE A CG2   1 
ATOM   3160  C CD1   . ILE A 1 2014 ? 197.332 174.376 155.498 1.00 72.40  ? 2014 ILE A CD1   1 
ATOM   3161  N N     . PHE A 1 2015 ? 197.663 175.237 161.032 1.00 70.46  ? 2015 PHE A N     1 
ATOM   3162  C CA    . PHE A 1 2015 ? 197.386 174.726 162.367 1.00 70.46  ? 2015 PHE A CA    1 
ATOM   3163  C C     . PHE A 1 2015 ? 195.927 174.317 162.452 1.00 70.46  ? 2015 PHE A C     1 
ATOM   3164  O O     . PHE A 1 2015 ? 195.044 175.070 162.034 1.00 70.46  ? 2015 PHE A O     1 
ATOM   3165  C CB    . PHE A 1 2015 ? 197.701 175.772 163.432 1.00 70.46  ? 2015 PHE A CB    1 
ATOM   3166  C CG    . PHE A 1 2015 ? 199.120 176.241 163.414 1.00 70.46  ? 2015 PHE A CG    1 
ATOM   3167  C CD1   . PHE A 1 2015 ? 199.509 177.266 162.580 1.00 70.46  ? 2015 PHE A CD1   1 
ATOM   3168  C CD2   . PHE A 1 2015 ? 200.064 175.659 164.231 1.00 70.46  ? 2015 PHE A CD2   1 
ATOM   3169  C CE1   . PHE A 1 2015 ? 200.811 177.700 162.560 1.00 70.46  ? 2015 PHE A CE1   1 
ATOM   3170  C CE2   . PHE A 1 2015 ? 201.369 176.092 164.213 1.00 70.46  ? 2015 PHE A CE2   1 
ATOM   3171  C CZ    . PHE A 1 2015 ? 201.742 177.113 163.377 1.00 70.46  ? 2015 PHE A CZ    1 
ATOM   3172  N N     . ILE A 1 2016 ? 195.676 173.134 162.997 1.00 76.99  ? 2016 ILE A N     1 
ATOM   3173  C CA    . ILE A 1 2016 ? 194.327 172.611 163.171 1.00 76.99  ? 2016 ILE A CA    1 
ATOM   3174  C C     . ILE A 1 2016 ? 194.102 172.476 164.669 1.00 76.99  ? 2016 ILE A C     1 
ATOM   3175  O O     . ILE A 1 2016 ? 194.823 171.741 165.348 1.00 76.99  ? 2016 ILE A O     1 
ATOM   3176  C CB    . ILE A 1 2016 ? 194.126 171.273 162.456 1.00 76.99  ? 2016 ILE A CB    1 
ATOM   3177  C CG1   . ILE A 1 2016 ? 193.874 171.498 160.967 1.00 76.99  ? 2016 ILE A CG1   1 
ATOM   3178  C CG2   . ILE A 1 2016 ? 192.970 170.512 163.072 1.00 76.99  ? 2016 ILE A CG2   1 
ATOM   3179  C CD1   . ILE A 1 2016 ? 193.663 170.223 160.190 1.00 76.99  ? 2016 ILE A CD1   1 
ATOM   3180  N N     . THR A 1 2017 ? 193.106 173.178 165.193 1.00 83.91  ? 2017 THR A N     1 
ATOM   3181  C CA    . THR A 1 2017 ? 192.811 173.136 166.616 1.00 83.91  ? 2017 THR A CA    1 
ATOM   3182  C C     . THR A 1 2017 ? 191.582 172.271 166.858 1.00 83.91  ? 2017 THR A C     1 
ATOM   3183  O O     . THR A 1 2017 ? 190.552 172.450 166.202 1.00 83.91  ? 2017 THR A O     1 
ATOM   3184  C CB    . THR A 1 2017 ? 192.590 174.544 167.158 1.00 83.91  ? 2017 THR A CB    1 
ATOM   3185  O OG1   . THR A 1 2017 ? 193.849 175.219 167.249 1.00 83.91  ? 2017 THR A OG1   1 
ATOM   3186  C CG2   . THR A 1 2017 ? 191.963 174.489 168.523 1.00 83.91  ? 2017 THR A CG2   1 
ATOM   3187  N N     . MET A 1 2018 ? 191.691 171.342 167.799 1.00 92.06  ? 2018 MET A N     1 
ATOM   3188  C CA    . MET A 1 2018 ? 190.664 170.347 168.063 1.00 92.06  ? 2018 MET A CA    1 
ATOM   3189  C C     . MET A 1 2018 ? 190.187 170.465 169.506 1.00 92.06  ? 2018 MET A C     1 
ATOM   3190  O O     . MET A 1 2018 ? 190.526 171.410 170.220 1.00 92.06  ? 2018 MET A O     1 
ATOM   3191  C CB    . MET A 1 2018 ? 191.200 168.945 167.775 1.00 92.06  ? 2018 MET A CB    1 
ATOM   3192  C CG    . MET A 1 2018 ? 191.312 168.636 166.300 1.00 92.06  ? 2018 MET A CG    1 
ATOM   3193  S SD    . MET A 1 2018 ? 190.517 167.087 165.853 1.00 92.06  ? 2018 MET A SD    1 
ATOM   3194  C CE    . MET A 1 2018 ? 188.802 167.500 166.134 1.00 92.06  ? 2018 MET A CE    1 
ATOM   3195  N N     . ASN A 1 2019 ? 189.386 169.493 169.930 1.00 92.86  ? 2019 ASN A N     1 
ATOM   3196  C CA    . ASN A 1 2019 ? 188.912 169.446 171.310 1.00 92.86  ? 2019 ASN A CA    1 
ATOM   3197  C C     . ASN A 1 2019 ? 188.671 168.017 171.787 1.00 92.86  ? 2019 ASN A C     1 
ATOM   3198  O O     . ASN A 1 2019 ? 188.788 167.060 171.026 0.00 92.86  ? 2019 ASN A O     1 
ATOM   3199  C CB    . ASN A 1 2019 ? 187.634 170.266 171.464 1.00 92.86  ? 2019 ASN A CB    1 
ATOM   3200  C CG    . ASN A 1 2019 ? 186.483 169.704 170.663 1.00 92.86  ? 2019 ASN A CG    1 
ATOM   3201  O OD1   . ASN A 1 2019 ? 186.659 168.801 169.846 1.00 92.86  ? 2019 ASN A OD1   1 
ATOM   3202  N ND2   . ASN A 1 2019 ? 185.292 170.239 170.892 1.00 92.86  ? 2019 ASN A ND2   1 
ATOM   3203  N N     . ASN A 1 2027 ? 188.806 163.381 167.446 1.00 83.61  ? 2027 ASN A N     1 
ATOM   3204  C CA    . ASN A 1 2027 ? 190.248 163.378 167.234 1.00 83.61  ? 2027 ASN A CA    1 
ATOM   3205  C C     . ASN A 1 2027 ? 190.589 163.775 165.806 1.00 83.61  ? 2027 ASN A C     1 
ATOM   3206  O O     . ASN A 1 2027 ? 189.701 163.975 164.981 1.00 83.61  ? 2027 ASN A O     1 
ATOM   3207  C CB    . ASN A 1 2027 ? 190.833 162.004 167.549 1.00 83.61  ? 2027 ASN A CB    1 
ATOM   3208  C CG    . ASN A 1 2027 ? 192.291 162.071 167.935 1.00 83.61  ? 2027 ASN A CG    1 
ATOM   3209  O OD1   . ASN A 1 2027 ? 192.894 163.144 167.938 1.00 83.61  ? 2027 ASN A OD1   1 
ATOM   3210  N ND2   . ASN A 1 2027 ? 192.871 160.923 168.258 1.00 83.61  ? 2027 ASN A ND2   1 
ATOM   3211  N N     . LEU A 1 2028 ? 191.883 163.895 165.522 1.00 88.03  ? 2028 LEU A N     1 
ATOM   3212  C CA    . LEU A 1 2028 ? 192.321 164.234 164.180 1.00 88.03  ? 2028 LEU A CA    1 
ATOM   3213  C C     . LEU A 1 2028 ? 191.941 163.129 163.199 1.00 88.03  ? 2028 LEU A C     1 
ATOM   3214  O O     . LEU A 1 2028 ? 191.938 161.947 163.550 1.00 88.03  ? 2028 LEU A O     1 
ATOM   3215  C CB    . LEU A 1 2028 ? 193.830 164.447 164.144 1.00 88.03  ? 2028 LEU A CB    1 
ATOM   3216  C CG    . LEU A 1 2028 ? 194.350 165.817 164.562 1.00 88.03  ? 2028 LEU A CG    1 
ATOM   3217  C CD1   . LEU A 1 2028 ? 195.798 165.973 164.146 1.00 88.03  ? 2028 LEU A CD1   1 
ATOM   3218  C CD2   . LEU A 1 2028 ? 193.502 166.895 163.929 1.00 88.03  ? 2028 LEU A CD2   1 
ATOM   3219  N N     . PRO A 1 2029 ? 191.606 163.490 161.965 1.00 94.74  ? 2029 PRO A N     1 
ATOM   3220  C CA    . PRO A 1 2029 ? 191.361 162.467 160.947 1.00 94.74  ? 2029 PRO A CA    1 
ATOM   3221  C C     . PRO A 1 2029 ? 192.626 161.671 160.675 1.00 94.74  ? 2029 PRO A C     1 
ATOM   3222  O O     . PRO A 1 2029 ? 193.744 162.166 160.826 1.00 94.74  ? 2029 PRO A O     1 
ATOM   3223  C CB    . PRO A 1 2029 ? 190.932 163.279 159.720 1.00 94.74  ? 2029 PRO A CB    1 
ATOM   3224  C CG    . PRO A 1 2029 ? 190.500 164.601 160.267 1.00 94.74  ? 2029 PRO A CG    1 
ATOM   3225  C CD    . PRO A 1 2029 ? 191.375 164.847 161.451 1.00 94.74  ? 2029 PRO A CD    1 
ATOM   3226  N N     . ASP A 1 2030 ? 192.434 160.415 160.273 1.00 100.23 ? 2030 ASP A N     1 
ATOM   3227  C CA    . ASP A 1 2030 ? 193.559 159.514 160.058 1.00 100.23 ? 2030 ASP A CA    1 
ATOM   3228  C C     . ASP A 1 2030 ? 194.506 160.005 158.972 1.00 100.23 ? 2030 ASP A C     1 
ATOM   3229  O O     . ASP A 1 2030 ? 195.656 159.559 158.924 1.00 100.23 ? 2030 ASP A O     1 
ATOM   3230  C CB    . ASP A 1 2030 ? 193.040 158.121 159.714 1.00 100.23 ? 2030 ASP A CB    1 
ATOM   3231  C CG    . ASP A 1 2030 ? 191.883 158.162 158.740 1.00 100.23 ? 2030 ASP A CG    1 
ATOM   3232  O OD1   . ASP A 1 2030 ? 191.465 159.278 158.369 1.00 100.23 ? 2030 ASP A OD1   1 
ATOM   3233  O OD2   . ASP A 1 2030 ? 191.389 157.084 158.350 1.00 100.23 ? 2030 ASP A OD2   1 
ATOM   3234  N N     . ASN A 1 2031 ? 194.051 160.903 158.099 1.00 98.83  ? 2031 ASN A N     1 
ATOM   3235  C CA    . ASN A 1 2031 ? 194.918 161.407 157.040 1.00 98.83  ? 2031 ASN A CA    1 
ATOM   3236  C C     . ASN A 1 2031 ? 196.091 162.196 157.604 1.00 98.83  ? 2031 ASN A C     1 
ATOM   3237  O O     . ASN A 1 2031 ? 197.221 162.068 157.120 1.00 98.83  ? 2031 ASN A O     1 
ATOM   3238  C CB    . ASN A 1 2031 ? 194.114 162.273 156.076 1.00 98.83  ? 2031 ASN A CB    1 
ATOM   3239  C CG    . ASN A 1 2031 ? 192.791 161.650 155.707 1.00 98.83  ? 2031 ASN A CG    1 
ATOM   3240  O OD1   . ASN A 1 2031 ? 191.917 161.478 156.556 1.00 98.83  ? 2031 ASN A OD1   1 
ATOM   3241  N ND2   . ASN A 1 2031 ? 192.632 161.308 154.435 1.00 98.83  ? 2031 ASN A ND2   1 
ATOM   3242  N N     . LEU A 1 2032 ? 195.846 163.018 158.622 1.00 94.20  ? 2032 LEU A N     1 
ATOM   3243  C CA    . LEU A 1 2032 ? 196.843 163.946 159.134 1.00 94.20  ? 2032 LEU A CA    1 
ATOM   3244  C C     . LEU A 1 2032 ? 197.468 163.496 160.450 1.00 94.20  ? 2032 LEU A C     1 
ATOM   3245  O O     . LEU A 1 2032 ? 198.200 164.274 161.068 1.00 94.20  ? 2032 LEU A O     1 
ATOM   3246  C CB    . LEU A 1 2032 ? 196.223 165.332 159.303 1.00 94.20  ? 2032 LEU A CB    1 
ATOM   3247  C CG    . LEU A 1 2032 ? 195.246 165.737 158.204 1.00 94.20  ? 2032 LEU A CG    1 
ATOM   3248  C CD1   . LEU A 1 2032 ? 194.519 167.007 158.586 1.00 94.20  ? 2032 LEU A CD1   1 
ATOM   3249  C CD2   . LEU A 1 2032 ? 195.983 165.915 156.896 1.00 94.20  ? 2032 LEU A CD2   1 
ATOM   3250  N N     . LYS A 1 2033 ? 197.205 162.263 160.889 1.00 88.35  ? 2033 LYS A N     1 
ATOM   3251  C CA    . LYS A 1 2033 ? 197.780 161.797 162.147 1.00 88.35  ? 2033 LYS A CA    1 
ATOM   3252  C C     . LYS A 1 2033 ? 199.300 161.794 162.091 1.00 88.35  ? 2033 LYS A C     1 
ATOM   3253  O O     . LYS A 1 2033 ? 199.966 162.189 163.054 1.00 88.35  ? 2033 LYS A O     1 
ATOM   3254  C CB    . LYS A 1 2033 ? 197.262 160.400 162.478 1.00 88.35  ? 2033 LYS A CB    1 
ATOM   3255  C CG    . LYS A 1 2033 ? 195.784 160.345 162.775 1.00 88.35  ? 2033 LYS A CG    1 
ATOM   3256  C CD    . LYS A 1 2033 ? 195.439 161.260 163.927 1.00 88.35  ? 2033 LYS A CD    1 
ATOM   3257  C CE    . LYS A 1 2033 ? 196.126 160.805 165.201 1.00 88.35  ? 2033 LYS A CE    1 
ATOM   3258  N NZ    . LYS A 1 2033 ? 195.939 159.346 165.423 1.00 88.35  ? 2033 LYS A NZ    1 
ATOM   3259  N N     . LYS A 1 2034 ? 199.866 161.357 160.976 1.00 81.65  ? 2034 LYS A N     1 
ATOM   3260  C CA    . LYS A 1 2034 ? 201.311 161.316 160.836 1.00 81.65  ? 2034 LYS A CA    1 
ATOM   3261  C C     . LYS A 1 2034 ? 201.897 162.659 160.437 1.00 81.65  ? 2034 LYS A C     1 
ATOM   3262  O O     . LYS A 1 2034 ? 203.123 162.780 160.348 1.00 81.65  ? 2034 LYS A O     1 
ATOM   3263  C CB    . LYS A 1 2034 ? 201.710 160.251 159.811 1.00 81.65  ? 2034 LYS A CB    1 
ATOM   3264  C CG    . LYS A 1 2034 ? 201.274 158.841 160.176 1.00 81.65  ? 2034 LYS A CG    1 
ATOM   3265  C CD    . LYS A 1 2034 ? 199.904 158.509 159.606 1.00 81.65  ? 2034 LYS A CD    1 
ATOM   3266  C CE    . LYS A 1 2034 ? 199.611 157.023 159.696 1.00 81.65  ? 2034 LYS A CE    1 
ATOM   3267  N NZ    . LYS A 1 2034 ? 198.151 156.747 159.631 1.00 81.65  ? 2034 LYS A NZ    1 
ATOM   3268  N N     . LEU A 1 2035 ? 201.062 163.667 160.201 1.00 86.13  ? 2035 LEU A N     1 
ATOM   3269  C CA    . LEU A 1 2035 ? 201.533 164.957 159.728 1.00 86.13  ? 2035 LEU A CA    1 
ATOM   3270  C C     . LEU A 1 2035 ? 201.358 166.084 160.731 1.00 86.13  ? 2035 LEU A C     1 
ATOM   3271  O O     . LEU A 1 2035 ? 201.821 167.197 160.464 1.00 86.13  ? 2035 LEU A O     1 
ATOM   3272  C CB    . LEU A 1 2035 ? 200.815 165.341 158.429 1.00 86.13  ? 2035 LEU A CB    1 
ATOM   3273  C CG    . LEU A 1 2035 ? 201.125 164.444 157.239 1.00 86.13  ? 2035 LEU A CG    1 
ATOM   3274  C CD1   . LEU A 1 2035 ? 200.136 164.697 156.125 1.00 86.13  ? 2035 LEU A CD1   1 
ATOM   3275  C CD2   . LEU A 1 2035 ? 202.542 164.690 156.767 1.00 86.13  ? 2035 LEU A CD2   1 
ATOM   3276  N N     . PHE A 1 2036 ? 200.699 165.849 161.859 1.00 83.35  ? 2036 PHE A N     1 
ATOM   3277  C CA    . PHE A 1 2036 ? 200.419 166.922 162.800 1.00 83.35  ? 2036 PHE A CA    1 
ATOM   3278  C C     . PHE A 1 2036 ? 200.824 166.516 164.207 1.00 83.35  ? 2036 PHE A C     1 
ATOM   3279  O O     . PHE A 1 2036 ? 200.467 165.432 164.676 1.00 83.35  ? 2036 PHE A O     1 
ATOM   3280  C CB    . PHE A 1 2036 ? 198.943 167.312 162.757 1.00 83.35  ? 2036 PHE A CB    1 
ATOM   3281  C CG    . PHE A 1 2036 ? 198.608 168.246 161.638 1.00 83.35  ? 2036 PHE A CG    1 
ATOM   3282  C CD1   . PHE A 1 2036 ? 198.669 167.821 160.327 1.00 83.35  ? 2036 PHE A CD1   1 
ATOM   3283  C CD2   . PHE A 1 2036 ? 198.249 169.551 161.893 1.00 83.35  ? 2036 PHE A CD2   1 
ATOM   3284  C CE1   . PHE A 1 2036 ? 198.370 168.675 159.296 1.00 83.35  ? 2036 PHE A CE1   1 
ATOM   3285  C CE2   . PHE A 1 2036 ? 197.951 170.409 160.863 1.00 83.35  ? 2036 PHE A CE2   1 
ATOM   3286  C CZ    . PHE A 1 2036 ? 198.012 169.970 159.563 1.00 83.35  ? 2036 PHE A CZ    1 
ATOM   3287  N N     . ARG A 1 2037 ? 201.565 167.395 164.870 1.00 81.80  ? 2037 ARG A N     1 
ATOM   3288  C CA    . ARG A 1 2037 ? 201.986 167.188 166.245 1.00 81.80  ? 2037 ARG A CA    1 
ATOM   3289  C C     . ARG A 1 2037 ? 200.893 167.674 167.185 1.00 81.80  ? 2037 ARG A C     1 
ATOM   3290  O O     . ARG A 1 2037 ? 200.448 168.821 167.087 1.00 81.80  ? 2037 ARG A O     1 
ATOM   3291  C CB    . ARG A 1 2037 ? 203.290 167.936 166.514 1.00 81.80  ? 2037 ARG A CB    1 
ATOM   3292  C CG    . ARG A 1 2037 ? 203.988 167.547 167.796 1.00 81.80  ? 2037 ARG A CG    1 
ATOM   3293  C CD    . ARG A 1 2037 ? 204.170 166.042 167.903 1.00 81.80  ? 2037 ARG A CD    1 
ATOM   3294  N NE    . ARG A 1 2037 ? 204.713 165.447 166.686 1.00 81.80  ? 2037 ARG A NE    1 
ATOM   3295  C CZ    . ARG A 1 2037 ? 205.930 165.670 166.208 1.00 81.80  ? 2037 ARG A CZ    1 
ATOM   3296  N NH1   . ARG A 1 2037 ? 206.770 166.499 166.806 1.00 81.80  ? 2037 ARG A NH1   1 
ATOM   3297  N NH2   . ARG A 1 2037 ? 206.318 165.037 165.107 1.00 81.80  ? 2037 ARG A NH2   1 
ATOM   3298  N N     . SER A 1 2038 ? 200.468 166.806 168.093 1.00 73.84  ? 2038 SER A N     1 
ATOM   3299  C CA    . SER A 1 2038 ? 199.381 167.110 169.010 1.00 73.84  ? 2038 SER A CA    1 
ATOM   3300  C C     . SER A 1 2038 ? 199.933 167.651 170.318 1.00 73.84  ? 2038 SER A C     1 
ATOM   3301  O O     . SER A 1 2038 ? 200.943 167.161 170.829 1.00 73.84  ? 2038 SER A O     1 
ATOM   3302  C CB    . SER A 1 2038 ? 198.533 165.869 169.281 1.00 73.84  ? 2038 SER A CB    1 
ATOM   3303  O OG    . SER A 1 2038 ? 197.976 165.361 168.083 1.00 73.84  ? 2038 SER A OG    1 
ATOM   3304  N N     . LEU A 1 2039 ? 199.266 168.667 170.852 1.00 73.48  ? 2039 LEU A N     1 
ATOM   3305  C CA    . LEU A 1 2039 ? 199.626 169.264 172.128 1.00 73.48  ? 2039 LEU A CA    1 
ATOM   3306  C C     . LEU A 1 2039 ? 198.369 169.445 172.964 1.00 73.48  ? 2039 LEU A C     1 
ATOM   3307  O O     . LEU A 1 2039 ? 197.324 169.847 172.446 1.00 73.48  ? 2039 LEU A O     1 
ATOM   3308  C CB    . LEU A 1 2039 ? 200.331 170.601 171.927 1.00 73.48  ? 2039 LEU A CB    1 
ATOM   3309  C CG    . LEU A 1 2039 ? 200.756 171.332 173.193 1.00 73.48  ? 2039 LEU A CG    1 
ATOM   3310  C CD1   . LEU A 1 2039 ? 201.964 170.660 173.804 1.00 73.48  ? 2039 LEU A CD1   1 
ATOM   3311  C CD2   . LEU A 1 2039 ? 201.065 172.768 172.858 1.00 73.48  ? 2039 LEU A CD2   1 
ATOM   3312  N N     . ALA A 1 2040 ? 198.469 169.148 174.252 1.00 75.65  ? 2040 ALA A N     1 
ATOM   3313  C CA    . ALA A 1 2040 ? 197.314 169.127 175.145 1.00 75.65  ? 2040 ALA A CA    1 
ATOM   3314  C C     . ALA A 1 2040 ? 197.408 170.303 176.110 1.00 75.65  ? 2040 ALA A C     1 
ATOM   3315  O O     . ALA A 1 2040 ? 198.064 170.220 177.148 1.00 75.65  ? 2040 ALA A O     1 
ATOM   3316  C CB    . ALA A 1 2040 ? 197.238 167.806 175.896 1.00 75.65  ? 2040 ALA A CB    1 
ATOM   3317  N N     . MET A 1 2041 ? 196.745 171.401 175.763 1.00 78.61  ? 2041 MET A N     1 
ATOM   3318  C CA    . MET A 1 2041 ? 196.630 172.540 176.668 1.00 78.61  ? 2041 MET A CA    1 
ATOM   3319  C C     . MET A 1 2041 ? 195.261 172.514 177.345 1.00 78.61  ? 2041 MET A C     1 
ATOM   3320  O O     . MET A 1 2041 ? 194.358 173.283 177.030 1.00 78.61  ? 2041 MET A O     1 
ATOM   3321  C CB    . MET A 1 2041 ? 196.856 173.843 175.913 1.00 78.61  ? 2041 MET A CB    1 
ATOM   3322  C CG    . MET A 1 2041 ? 196.368 173.809 174.486 1.00 78.61  ? 2041 MET A CG    1 
ATOM   3323  S SD    . MET A 1 2041 ? 196.694 175.359 173.635 1.00 78.61  ? 2041 MET A SD    1 
ATOM   3324  C CE    . MET A 1 2041 ? 198.477 175.319 173.580 1.00 78.61  ? 2041 MET A CE    1 
ATOM   3325  N N     . THR A 1 2042 ? 195.124 171.603 178.305 1.00 78.53  ? 2042 THR A N     1 
ATOM   3326  C CA    . THR A 1 2042 ? 193.842 171.452 178.980 1.00 78.53  ? 2042 THR A CA    1 
ATOM   3327  C C     . THR A 1 2042 ? 193.581 172.560 179.988 1.00 78.53  ? 2042 THR A C     1 
ATOM   3328  O O     . THR A 1 2042 ? 192.434 172.991 180.139 1.00 78.53  ? 2042 THR A O     1 
ATOM   3329  C CB    . THR A 1 2042 ? 193.767 170.103 179.688 1.00 78.53  ? 2042 THR A CB    1 
ATOM   3330  O OG1   . THR A 1 2042 ? 194.755 170.054 180.724 1.00 78.53  ? 2042 THR A OG1   1 
ATOM   3331  C CG2   . THR A 1 2042 ? 194.011 168.977 178.704 1.00 78.53  ? 2042 THR A CG2   1 
ATOM   3332  N N     . LYS A 1 2043 ? 194.610 173.031 180.682 1.00 77.66  ? 2043 LYS A N     1 
ATOM   3333  C CA    . LYS A 1 2043 ? 194.434 173.973 181.786 1.00 77.66  ? 2043 LYS A CA    1 
ATOM   3334  C C     . LYS A 1 2043 ? 195.411 175.131 181.644 1.00 77.66  ? 2043 LYS A C     1 
ATOM   3335  O O     . LYS A 1 2043 ? 196.634 174.923 181.773 1.00 77.66  ? 2043 LYS A O     1 
ATOM   3336  C CB    . LYS A 1 2043 ? 194.626 173.258 183.122 1.00 77.66  ? 2043 LYS A CB    1 
ATOM   3337  C CG    . LYS A 1 2043 ? 194.586 174.135 184.379 1.00 77.66  ? 2043 LYS A CG    1 
ATOM   3338  C CD    . LYS A 1 2043 ? 193.533 175.246 184.349 1.00 77.66  ? 2043 LYS A CD    1 
ATOM   3339  C CE    . LYS A 1 2043 ? 192.117 174.719 184.126 1.00 77.66  ? 2043 LYS A CE    1 
ATOM   3340  N NZ    . LYS A 1 2043 ? 191.129 175.829 184.034 1.00 77.66  ? 2043 LYS A NZ    1 
ATOM   3341  N N     . PRO A 1 2044 ? 194.936 176.346 181.391 1.00 74.84  ? 2044 PRO A N     1 
ATOM   3342  C CA    . PRO A 1 2044 ? 195.829 177.504 181.363 1.00 74.84  ? 2044 PRO A CA    1 
ATOM   3343  C C     . PRO A 1 2044 ? 196.096 178.037 182.759 1.00 74.84  ? 2044 PRO A C     1 
ATOM   3344  O O     . PRO A 1 2044 ? 195.254 177.973 183.655 1.00 74.84  ? 2044 PRO A O     1 
ATOM   3345  C CB    . PRO A 1 2044 ? 195.039 178.519 180.528 1.00 74.84  ? 2044 PRO A CB    1 
ATOM   3346  C CG    . PRO A 1 2044 ? 193.625 178.206 180.841 1.00 74.84  ? 2044 PRO A CG    1 
ATOM   3347  C CD    . PRO A 1 2044 ? 193.542 176.722 181.103 1.00 74.84  ? 2044 PRO A CD    1 
ATOM   3348  N N     . ASP A 1 2045 ? 197.297 178.576 182.935 1.00 75.17  ? 2045 ASP A N     1 
ATOM   3349  C CA    . ASP A 1 2045 ? 197.710 179.083 184.240 1.00 75.17  ? 2045 ASP A CA    1 
ATOM   3350  C C     . ASP A 1 2045 ? 196.996 180.403 184.494 1.00 75.17  ? 2045 ASP A C     1 
ATOM   3351  O O     . ASP A 1 2045 ? 197.514 181.475 184.182 1.00 75.17  ? 2045 ASP A O     1 
ATOM   3352  C CB    . ASP A 1 2045 ? 199.224 179.247 184.291 1.00 75.17  ? 2045 ASP A CB    1 
ATOM   3353  C CG    . ASP A 1 2045 ? 199.733 179.536 185.690 1.00 75.17  ? 2045 ASP A CG    1 
ATOM   3354  O OD1   . ASP A 1 2045 ? 198.908 179.606 186.623 1.00 75.17  ? 2045 ASP A OD1   1 
ATOM   3355  O OD2   . ASP A 1 2045 ? 200.960 179.686 185.862 1.00 75.17  ? 2045 ASP A OD2   1 
ATOM   3356  N N     . ARG A 1 2046 ? 195.795 180.325 185.070 1.00 69.28  ? 2046 ARG A N     1 
ATOM   3357  C CA    . ARG A 1 2046 ? 194.994 181.520 185.308 1.00 69.28  ? 2046 ARG A CA    1 
ATOM   3358  C C     . ARG A 1 2046 ? 195.649 182.473 186.294 1.00 69.28  ? 2046 ARG A C     1 
ATOM   3359  O O     . ARG A 1 2046 ? 195.533 183.693 186.138 1.00 69.28  ? 2046 ARG A O     1 
ATOM   3360  C CB    . ARG A 1 2046 ? 193.612 181.132 185.824 1.00 69.28  ? 2046 ARG A CB    1 
ATOM   3361  C CG    . ARG A 1 2046 ? 192.761 180.381 184.831 1.00 69.28  ? 2046 ARG A CG    1 
ATOM   3362  C CD    . ARG A 1 2046 ? 191.601 179.702 185.531 1.00 69.28  ? 2046 ARG A CD    1 
ATOM   3363  N NE    . ARG A 1 2046 ? 190.690 179.075 184.584 1.00 69.28  ? 2046 ARG A NE    1 
ATOM   3364  C CZ    . ARG A 1 2046 ? 189.785 179.732 183.874 1.00 69.28  ? 2046 ARG A CZ    1 
ATOM   3365  N NH1   . ARG A 1 2046 ? 189.614 181.036 184.012 1.00 69.28  ? 2046 ARG A NH1   1 
ATOM   3366  N NH2   . ARG A 1 2046 ? 189.029 179.064 183.009 1.00 69.28  ? 2046 ARG A NH2   1 
ATOM   3367  N N     . GLN A 1 2047 ? 196.317 181.943 187.318 1.00 67.41  ? 2047 GLN A N     1 
ATOM   3368  C CA    . GLN A 1 2047 ? 196.900 182.804 188.339 1.00 67.41  ? 2047 GLN A CA    1 
ATOM   3369  C C     . GLN A 1 2047 ? 197.926 183.749 187.735 1.00 67.41  ? 2047 GLN A C     1 
ATOM   3370  O O     . GLN A 1 2047 ? 197.926 184.949 188.024 1.00 67.41  ? 2047 GLN A O     1 
ATOM   3371  C CB    . GLN A 1 2047 ? 197.529 181.953 189.439 1.00 67.41  ? 2047 GLN A CB    1 
ATOM   3372  C CG    . GLN A 1 2047 ? 197.905 182.730 190.681 1.00 67.41  ? 2047 GLN A CG    1 
ATOM   3373  C CD    . GLN A 1 2047 ? 199.356 183.161 190.679 1.00 67.41  ? 2047 GLN A CD    1 
ATOM   3374  O OE1   . GLN A 1 2047 ? 200.057 183.013 189.681 1.00 67.41  ? 2047 GLN A OE1   1 
ATOM   3375  N NE2   . GLN A 1 2047 ? 199.818 183.689 191.805 1.00 67.41  ? 2047 GLN A NE2   1 
ATOM   3376  N N     . LEU A 1 2048 ? 198.777 183.215 186.855 1.00 68.16  ? 2048 LEU A N     1 
ATOM   3377  C CA    . LEU A 1 2048 ? 199.800 184.063 186.184 1.00 68.16  ? 2048 LEU A CA    1 
ATOM   3378  C C     . LEU A 1 2048 ? 199.106 185.021 185.209 1.00 68.16  ? 2048 LEU A C     1 
ATOM   3379  O O     . LEU A 1 2048 ? 199.504 186.201 185.161 1.00 68.16  ? 2048 LEU A O     1 
ATOM   3380  C CB    . LEU A 1 2048 ? 200.804 183.164 185.456 1.00 68.16  ? 2048 LEU A CB    1 
ATOM   3381  C CG    . LEU A 1 2048 ? 201.931 183.903 184.737 1.00 68.16  ? 2048 LEU A CG    1 
ATOM   3382  C CD1   . LEU A 1 2048 ? 202.696 184.790 185.707 1.00 68.16  ? 2048 LEU A CD1   1 
ATOM   3383  C CD2   . LEU A 1 2048 ? 202.876 182.920 184.064 1.00 68.16  ? 2048 LEU A CD2   1 
ATOM   3384  N N     . ILE A 1 2049 ? 198.103 184.531 184.474 1.00 68.27  ? 2049 ILE A N     1 
ATOM   3385  C CA    . ILE A 1 2049 ? 197.365 185.389 183.499 1.00 68.27  ? 2049 ILE A CA    1 
ATOM   3386  C C     . ILE A 1 2049 ? 196.839 186.617 184.245 1.00 68.27  ? 2049 ILE A C     1 
ATOM   3387  O O     . ILE A 1 2049 ? 197.001 187.738 183.726 1.00 68.27  ? 2049 ILE A O     1 
ATOM   3388  C CB    . ILE A 1 2049 ? 196.215 184.606 182.835 1.00 68.27  ? 2049 ILE A CB    1 
ATOM   3389  C CG1   . ILE A 1 2049 ? 196.730 183.422 182.013 1.00 68.27  ? 2049 ILE A CG1   1 
ATOM   3390  C CG2   . ILE A 1 2049 ? 195.350 185.534 181.996 1.00 68.27  ? 2049 ILE A CG2   1 
ATOM   3391  C CD1   . ILE A 1 2049 ? 197.488 183.826 180.774 1.00 68.27  ? 2049 ILE A CD1   1 
ATOM   3392  N N     . ALA A 1 2050 ? 196.242 186.404 185.421 1.00 68.37  ? 2050 ALA A N     1 
ATOM   3393  C CA    . ALA A 1 2050 ? 195.688 187.526 186.212 1.00 68.37  ? 2050 ALA A CA    1 
ATOM   3394  C C     . ALA A 1 2050 ? 196.832 188.394 186.744 1.00 68.37  ? 2050 ALA A C     1 
ATOM   3395  O O     . ALA A 1 2050 ? 196.813 189.613 186.490 1.00 68.37  ? 2050 ALA A O     1 
ATOM   3396  C CB    . ALA A 1 2050 ? 194.835 186.990 187.334 1.00 68.37  ? 2050 ALA A CB    1 
ATOM   3397  N N     . GLN A 1 2051 ? 197.788 187.786 187.453 1.00 68.37  ? 2051 GLN A N     1 
ATOM   3398  C CA    . GLN A 1 2051 ? 198.882 188.557 188.029 1.00 68.37  ? 2051 GLN A CA    1 
ATOM   3399  C C     . GLN A 1 2051 ? 199.438 189.547 187.019 1.00 68.37  ? 2051 GLN A C     1 
ATOM   3400  O O     . GLN A 1 2051 ? 199.605 190.735 187.321 1.00 68.37  ? 2051 GLN A O     1 
ATOM   3401  C CB    . GLN A 1 2051 ? 199.984 187.624 188.523 1.00 68.37  ? 2051 GLN A CB    1 
ATOM   3402  C CG    . GLN A 1 2051 ? 201.281 188.337 188.838 1.00 68.37  ? 2051 GLN A CG    1 
ATOM   3403  C CD    . GLN A 1 2051 ? 202.430 187.381 189.055 1.00 68.37  ? 2051 GLN A CD    1 
ATOM   3404  O OE1   . GLN A 1 2051 ? 202.231 186.237 189.459 1.00 68.37  ? 2051 GLN A OE1   1 
ATOM   3405  N NE2   . GLN A 1 2051 ? 203.644 187.846 188.793 1.00 68.37  ? 2051 GLN A NE2   1 
ATOM   3406  N N     . VAL A 1 2052 ? 199.715 189.078 185.803 1.00 65.77  ? 2052 VAL A N     1 
ATOM   3407  C CA    . VAL A 1 2052 ? 200.277 189.961 184.789 1.00 65.77  ? 2052 VAL A CA    1 
ATOM   3408  C C     . VAL A 1 2052 ? 199.283 191.051 184.414 1.00 65.77  ? 2052 VAL A C     1 
ATOM   3409  O O     . VAL A 1 2052 ? 199.656 192.221 184.277 1.00 65.77  ? 2052 VAL A O     1 
ATOM   3410  C CB    . VAL A 1 2052 ? 200.724 189.155 183.560 1.00 65.77  ? 2052 VAL A CB    1 
ATOM   3411  C CG1   . VAL A 1 2052 ? 200.814 190.055 182.349 1.00 65.77  ? 2052 VAL A CG1   1 
ATOM   3412  C CG2   . VAL A 1 2052 ? 202.060 188.501 183.828 1.00 65.77  ? 2052 VAL A CG2   1 
ATOM   3413  N N     . MET A 1 2053 ? 198.007 190.697 184.243 1.00 69.11  ? 2053 MET A N     1 
ATOM   3414  C CA    . MET A 1 2053 ? 197.027 191.713 183.872 1.00 69.11  ? 2053 MET A CA    1 
ATOM   3415  C C     . MET A 1 2053 ? 196.867 192.764 184.964 1.00 69.11  ? 2053 MET A C     1 
ATOM   3416  O O     . MET A 1 2053 ? 196.802 193.963 184.669 1.00 69.11  ? 2053 MET A O     1 
ATOM   3417  C CB    . MET A 1 2053 ? 195.685 191.066 183.545 1.00 69.11  ? 2053 MET A CB    1 
ATOM   3418  C CG    . MET A 1 2053 ? 195.564 190.677 182.092 1.00 69.11  ? 2053 MET A CG    1 
ATOM   3419  S SD    . MET A 1 2053 ? 196.168 192.014 181.048 1.00 69.11  ? 2053 MET A SD    1 
ATOM   3420  C CE    . MET A 1 2053 ? 195.451 191.581 179.469 1.00 69.11  ? 2053 MET A CE    1 
ATOM   3421  N N     . LEU A 1 2054 ? 196.805 192.343 186.228 1.00 70.36  ? 2054 LEU A N     1 
ATOM   3422  C CA    . LEU A 1 2054 ? 196.683 193.303 187.317 1.00 70.36  ? 2054 LEU A CA    1 
ATOM   3423  C C     . LEU A 1 2054 ? 197.906 194.202 187.395 1.00 70.36  ? 2054 LEU A C     1 
ATOM   3424  O O     . LEU A 1 2054 ? 197.779 195.419 187.569 1.00 70.36  ? 2054 LEU A O     1 
ATOM   3425  C CB    . LEU A 1 2054 ? 196.477 192.578 188.643 1.00 70.36  ? 2054 LEU A CB    1 
ATOM   3426  C CG    . LEU A 1 2054 ? 195.039 192.377 189.101 1.00 70.36  ? 2054 LEU A CG    1 
ATOM   3427  C CD1   . LEU A 1 2054 ? 194.338 193.702 189.211 1.00 70.36  ? 2054 LEU A CD1   1 
ATOM   3428  C CD2   . LEU A 1 2054 ? 194.317 191.496 188.134 1.00 70.36  ? 2054 LEU A CD2   1 
ATOM   3429  N N     . TYR A 1 2055 ? 199.101 193.625 187.268 1.00 71.18  ? 2055 TYR A N     1 
ATOM   3430  C CA    . TYR A 1 2055 ? 200.302 194.446 187.328 1.00 71.18  ? 2055 TYR A CA    1 
ATOM   3431  C C     . TYR A 1 2055 ? 200.336 195.428 186.169 1.00 71.18  ? 2055 TYR A C     1 
ATOM   3432  O O     . TYR A 1 2055 ? 200.740 196.583 186.341 1.00 71.18  ? 2055 TYR A O     1 
ATOM   3433  C CB    . TYR A 1 2055 ? 201.541 193.554 187.321 1.00 71.18  ? 2055 TYR A CB    1 
ATOM   3434  C CG    . TYR A 1 2055 ? 202.789 194.196 187.878 1.00 71.18  ? 2055 TYR A CG    1 
ATOM   3435  C CD1   . TYR A 1 2055 ? 203.883 193.426 188.226 1.00 71.18  ? 2055 TYR A CD1   1 
ATOM   3436  C CD2   . TYR A 1 2055 ? 202.859 195.562 188.093 1.00 71.18  ? 2055 TYR A CD2   1 
ATOM   3437  C CE1   . TYR A 1 2055 ? 205.019 194.001 188.744 1.00 71.18  ? 2055 TYR A CE1   1 
ATOM   3438  C CE2   . TYR A 1 2055 ? 203.987 196.145 188.608 1.00 71.18  ? 2055 TYR A CE2   1 
ATOM   3439  C CZ    . TYR A 1 2055 ? 205.065 195.362 188.934 1.00 71.18  ? 2055 TYR A CZ    1 
ATOM   3440  O OH    . TYR A 1 2055 ? 206.197 195.944 189.453 1.00 71.18  ? 2055 TYR A OH    1 
ATOM   3441  N N     . SER A 1 2056 ? 199.888 194.999 184.993 1.00 71.14  ? 2056 SER A N     1 
ATOM   3442  C CA    . SER A 1 2056 ? 199.872 195.887 183.840 1.00 71.14  ? 2056 SER A CA    1 
ATOM   3443  C C     . SER A 1 2056 ? 198.875 197.019 184.031 1.00 71.14  ? 2056 SER A C     1 
ATOM   3444  O O     . SER A 1 2056 ? 199.101 198.137 183.558 1.00 71.14  ? 2056 SER A O     1 
ATOM   3445  C CB    . SER A 1 2056 ? 199.554 195.088 182.584 1.00 71.14  ? 2056 SER A CB    1 
ATOM   3446  O OG    . SER A 1 2056 ? 198.159 194.884 182.465 1.00 71.14  ? 2056 SER A OG    1 
ATOM   3447  N N     . GLN A 1 2057 ? 197.768 196.752 184.721 1.00 73.15  ? 2057 GLN A N     1 
ATOM   3448  C CA    . GLN A 1 2057 ? 196.779 197.796 184.947 1.00 73.15  ? 2057 GLN A CA    1 
ATOM   3449  C C     . GLN A 1 2057 ? 197.278 198.865 185.907 1.00 73.15  ? 2057 GLN A C     1 
ATOM   3450  O O     . GLN A 1 2057 ? 196.720 199.966 185.930 1.00 73.15  ? 2057 GLN A O     1 
ATOM   3451  C CB    . GLN A 1 2057 ? 195.485 197.184 185.477 1.00 73.15  ? 2057 GLN A CB    1 
ATOM   3452  C CG    . GLN A 1 2057 ? 194.672 196.469 184.421 1.00 73.15  ? 2057 GLN A CG    1 
ATOM   3453  C CD    . GLN A 1 2057 ? 194.584 197.250 183.131 1.00 73.15  ? 2057 GLN A CD    1 
ATOM   3454  O OE1   . GLN A 1 2057 ? 194.236 198.428 183.130 1.00 73.15  ? 2057 GLN A OE1   1 
ATOM   3455  N NE2   . GLN A 1 2057 ? 194.899 196.597 182.023 1.00 73.15  ? 2057 GLN A NE2   1 
ATOM   3456  N N     . GLY A 1 2058 ? 198.314 198.574 186.690 1.00 78.46  ? 2058 GLY A N     1 
ATOM   3457  C CA    . GLY A 1 2058 ? 198.885 199.535 187.612 1.00 78.46  ? 2058 GLY A CA    1 
ATOM   3458  C C     . GLY A 1 2058 ? 198.856 199.128 189.067 1.00 78.46  ? 2058 GLY A C     1 
ATOM   3459  O O     . GLY A 1 2058 ? 199.448 199.828 189.897 1.00 78.46  ? 2058 GLY A O     1 
ATOM   3460  N N     . PHE A 1 2059 ? 198.200 198.023 189.407 1.00 74.40  ? 2059 PHE A N     1 
ATOM   3461  C CA    . PHE A 1 2059 ? 198.142 197.573 190.789 1.00 74.40  ? 2059 PHE A CA    1 
ATOM   3462  C C     . PHE A 1 2059 ? 199.530 197.171 191.271 1.00 74.40  ? 2059 PHE A C     1 
ATOM   3463  O O     . PHE A 1 2059 ? 200.327 196.613 190.514 1.00 74.40  ? 2059 PHE A O     1 
ATOM   3464  C CB    . PHE A 1 2059 ? 197.178 196.397 190.916 1.00 74.40  ? 2059 PHE A CB    1 
ATOM   3465  C CG    . PHE A 1 2059 ? 195.750 196.748 190.617 1.00 74.40  ? 2059 PHE A CG    1 
ATOM   3466  C CD1   . PHE A 1 2059 ? 195.326 196.943 189.316 1.00 74.40  ? 2059 PHE A CD1   1 
ATOM   3467  C CD2   . PHE A 1 2059 ? 194.827 196.858 191.634 1.00 74.40  ? 2059 PHE A CD2   1 
ATOM   3468  C CE1   . PHE A 1 2059 ? 194.016 197.256 189.041 1.00 74.40  ? 2059 PHE A CE1   1 
ATOM   3469  C CE2   . PHE A 1 2059 ? 193.516 197.170 191.362 1.00 74.40  ? 2059 PHE A CE2   1 
ATOM   3470  C CZ    . PHE A 1 2059 ? 193.110 197.369 190.064 1.00 74.40  ? 2059 PHE A CZ    1 
ATOM   3471  N N     . ARG A 1 2060 ? 199.824 197.468 192.534 1.00 88.08  ? 2060 ARG A N     1 
ATOM   3472  C CA    . ARG A 1 2060 ? 201.136 197.179 193.101 1.00 88.08  ? 2060 ARG A CA    1 
ATOM   3473  C C     . ARG A 1 2060 ? 201.168 195.907 193.937 1.00 88.08  ? 2060 ARG A C     1 
ATOM   3474  O O     . ARG A 1 2060 ? 202.227 195.564 194.470 1.00 88.08  ? 2060 ARG A O     1 
ATOM   3475  C CB    . ARG A 1 2060 ? 201.619 198.362 193.943 1.00 88.08  ? 2060 ARG A CB    1 
ATOM   3476  C CG    . ARG A 1 2060 ? 200.524 199.033 194.736 1.00 88.08  ? 2060 ARG A CG    1 
ATOM   3477  C CD    . ARG A 1 2060 ? 201.076 199.805 195.917 1.00 88.08  ? 2060 ARG A CD    1 
ATOM   3478  N NE    . ARG A 1 2060 ? 201.151 198.982 197.118 1.00 88.08  ? 2060 ARG A NE    1 
ATOM   3479  C CZ    . ARG A 1 2060 ? 200.171 198.857 198.004 1.00 88.08  ? 2060 ARG A CZ    1 
ATOM   3480  N NH1   . ARG A 1 2060 ? 199.019 199.490 197.854 1.00 88.08  ? 2060 ARG A NH1   1 
ATOM   3481  N NH2   . ARG A 1 2060 ? 200.353 198.078 199.066 1.00 88.08  ? 2060 ARG A NH2   1 
ATOM   3482  N N     . THR A 1 2061 ? 200.048 195.203 194.068 1.00 81.39  ? 2061 THR A N     1 
ATOM   3483  C CA    . THR A 1 2061 ? 199.991 193.914 194.754 1.00 81.39  ? 2061 THR A CA    1 
ATOM   3484  C C     . THR A 1 2061 ? 199.261 192.902 193.888 1.00 81.39  ? 2061 THR A C     1 
ATOM   3485  O O     . THR A 1 2061 ? 198.329 192.221 194.318 1.00 81.39  ? 2061 THR A O     1 
ATOM   3486  C CB    . THR A 1 2061 ? 199.334 194.028 196.126 1.00 81.39  ? 2061 THR A CB    1 
ATOM   3487  O OG1   . THR A 1 2061 ? 198.999 192.720 196.606 1.00 81.39  ? 2061 THR A OG1   1 
ATOM   3488  C CG2   . THR A 1 2061 ? 198.082 194.867 196.056 1.00 81.39  ? 2061 THR A CG2   1 
ATOM   3489  N N     . ALA A 1 2062 ? 199.697 192.802 192.632 1.00 79.38  ? 2062 ALA A N     1 
ATOM   3490  C CA    . ALA A 1 2062 ? 198.959 192.033 191.636 1.00 79.38  ? 2062 ALA A CA    1 
ATOM   3491  C C     . ALA A 1 2062 ? 198.834 190.565 192.023 1.00 79.38  ? 2062 ALA A C     1 
ATOM   3492  O O     . ALA A 1 2062 ? 197.789 189.947 191.794 1.00 79.38  ? 2062 ALA A O     1 
ATOM   3493  C CB    . ALA A 1 2062 ? 199.636 192.169 190.275 1.00 79.38  ? 2062 ALA A CB    1 
ATOM   3494  N N     . GLU A 1 2063 ? 199.888 189.982 192.595 1.00 78.97  ? 2063 GLU A N     1 
ATOM   3495  C CA    . GLU A 1 2063 ? 199.880 188.543 192.847 1.00 78.97  ? 2063 GLU A CA    1 
ATOM   3496  C C     . GLU A 1 2063 ? 198.798 188.155 193.850 1.00 78.97  ? 2063 GLU A C     1 
ATOM   3497  O O     . GLU A 1 2063 ? 198.094 187.155 193.658 1.00 78.97  ? 2063 GLU A O     1 
ATOM   3498  C CB    . GLU A 1 2063 ? 201.264 188.084 193.316 1.00 78.97  ? 2063 GLU A CB    1 
ATOM   3499  C CG    . GLU A 1 2063 ? 201.679 188.519 194.719 1.00 78.97  ? 2063 GLU A CG    1 
ATOM   3500  C CD    . GLU A 1 2063 ? 201.763 190.027 194.887 1.00 78.97  ? 2063 GLU A CD    1 
ATOM   3501  O OE1   . GLU A 1 2063 ? 201.839 190.743 193.867 1.00 78.97  ? 2063 GLU A OE1   1 
ATOM   3502  O OE2   . GLU A 1 2063 ? 201.751 190.497 196.044 1.00 78.97  ? 2063 GLU A OE2   1 
ATOM   3503  N N     . VAL A 1 2064 ? 198.636 188.940 194.917 1.00 74.94  ? 2064 VAL A N     1 
ATOM   3504  C CA    . VAL A 1 2064 ? 197.617 188.628 195.912 1.00 74.94  ? 2064 VAL A CA    1 
ATOM   3505  C C     . VAL A 1 2064 ? 196.228 188.778 195.312 1.00 74.94  ? 2064 VAL A C     1 
ATOM   3506  O O     . VAL A 1 2064 ? 195.340 187.947 195.542 1.00 74.94  ? 2064 VAL A O     1 
ATOM   3507  C CB    . VAL A 1 2064 ? 197.797 189.514 197.155 1.00 74.94  ? 2064 VAL A CB    1 
ATOM   3508  C CG1   . VAL A 1 2064 ? 196.738 189.187 198.188 1.00 74.94  ? 2064 VAL A CG1   1 
ATOM   3509  C CG2   . VAL A 1 2064 ? 199.184 189.327 197.734 1.00 74.94  ? 2064 VAL A CG2   1 
ATOM   3510  N N     . LEU A 1 2065 ? 196.016 189.835 194.528 1.00 76.76  ? 2065 LEU A N     1 
ATOM   3511  C CA    . LEU A 1 2065 ? 194.715 190.029 193.904 1.00 76.76  ? 2065 LEU A CA    1 
ATOM   3512  C C     . LEU A 1 2065 ? 194.398 188.895 192.941 1.00 76.76  ? 2065 LEU A C     1 
ATOM   3513  O O     . LEU A 1 2065 ? 193.243 188.478 192.826 1.00 76.76  ? 2065 LEU A O     1 
ATOM   3514  C CB    . LEU A 1 2065 ? 194.667 191.376 193.189 1.00 76.76  ? 2065 LEU A CB    1 
ATOM   3515  C CG    . LEU A 1 2065 ? 194.256 192.575 194.045 1.00 76.76  ? 2065 LEU A CG    1 
ATOM   3516  C CD1   . LEU A 1 2065 ? 192.861 192.379 194.601 1.00 76.76  ? 2065 LEU A CD1   1 
ATOM   3517  C CD2   . LEU A 1 2065 ? 195.244 192.831 195.167 1.00 76.76  ? 2065 LEU A CD2   1 
ATOM   3518  N N     . ALA A 1 2066 ? 195.409 188.378 192.246 1.00 75.11  ? 2066 ALA A N     1 
ATOM   3519  C CA    . ALA A 1 2066 ? 195.187 187.243 191.357 1.00 75.11  ? 2066 ALA A CA    1 
ATOM   3520  C C     . ALA A 1 2066 ? 194.824 185.994 192.146 1.00 75.11  ? 2066 ALA A C     1 
ATOM   3521  O O     . ALA A 1 2066 ? 193.871 185.279 191.803 1.00 75.11  ? 2066 ALA A O     1 
ATOM   3522  C CB    . ALA A 1 2066 ? 196.432 187.000 190.509 1.00 75.11  ? 2066 ALA A CB    1 
ATOM   3523  N N     . ASN A 1 2067 ? 195.586 185.711 193.207 1.00 77.63  ? 2067 ASN A N     1 
ATOM   3524  C CA    . ASN A 1 2067 ? 195.295 184.562 194.055 1.00 77.63  ? 2067 ASN A CA    1 
ATOM   3525  C C     . ASN A 1 2067 ? 193.921 184.660 194.689 1.00 77.63  ? 2067 ASN A C     1 
ATOM   3526  O O     . ASN A 1 2067 ? 193.355 183.637 195.081 1.00 77.63  ? 2067 ASN A O     1 
ATOM   3527  C CB    . ASN A 1 2067 ? 196.347 184.426 195.154 1.00 77.63  ? 2067 ASN A CB    1 
ATOM   3528  C CG    . ASN A 1 2067 ? 197.719 184.124 194.610 1.00 77.63  ? 2067 ASN A CG    1 
ATOM   3529  O OD1   . ASN A 1 2067 ? 197.986 184.323 193.427 1.00 77.63  ? 2067 ASN A OD1   1 
ATOM   3530  N ND2   . ASN A 1 2067 ? 198.604 183.642 195.473 1.00 77.63  ? 2067 ASN A ND2   1 
ATOM   3531  N N     . LYS A 1 2068 ? 193.389 185.870 194.831 1.00 74.89  ? 2068 LYS A N     1 
ATOM   3532  C CA    . LYS A 1 2068 ? 192.026 186.001 195.324 1.00 74.89  ? 2068 LYS A CA    1 
ATOM   3533  C C     . LYS A 1 2068 ? 191.007 185.829 194.205 1.00 74.89  ? 2068 LYS A C     1 
ATOM   3534  O O     . LYS A 1 2068 ? 190.004 185.130 194.379 1.00 74.89  ? 2068 LYS A O     1 
ATOM   3535  C CB    . LYS A 1 2068 ? 191.843 187.352 196.012 1.00 74.89  ? 2068 LYS A CB    1 
ATOM   3536  C CG    . LYS A 1 2068 ? 192.707 187.523 197.242 1.00 74.89  ? 2068 LYS A CG    1 
ATOM   3537  C CD    . LYS A 1 2068 ? 192.687 188.933 197.780 1.00 74.89  ? 2068 LYS A CD    1 
ATOM   3538  C CE    . LYS A 1 2068 ? 193.071 188.938 199.246 1.00 74.89  ? 2068 LYS A CE    1 
ATOM   3539  N NZ    . LYS A 1 2068 ? 192.805 187.615 199.873 1.00 74.89  ? 2068 LYS A NZ    1 
ATOM   3540  N N     . ILE A 1 2069 ? 191.252 186.440 193.048 1.00 68.35  ? 2069 ILE A N     1 
ATOM   3541  C CA    . ILE A 1 2069 ? 190.227 186.502 192.015 1.00 68.35  ? 2069 ILE A CA    1 
ATOM   3542  C C     . ILE A 1 2069 ? 190.040 185.165 191.303 1.00 68.35  ? 2069 ILE A C     1 
ATOM   3543  O O     . ILE A 1 2069 ? 188.904 184.787 190.998 1.00 68.35  ? 2069 ILE A O     1 
ATOM   3544  C CB    . ILE A 1 2069 ? 190.541 187.637 191.025 1.00 68.35  ? 2069 ILE A CB    1 
ATOM   3545  C CG1   . ILE A 1 2069 ? 189.302 187.986 190.206 1.00 68.35  ? 2069 ILE A CG1   1 
ATOM   3546  C CG2   . ILE A 1 2069 ? 191.709 187.288 190.126 1.00 68.35  ? 2069 ILE A CG2   1 
ATOM   3547  C CD1   . ILE A 1 2069 ? 188.199 188.593 191.022 1.00 68.35  ? 2069 ILE A CD1   1 
ATOM   3548  N N     . VAL A 1 2070 ? 191.113 184.431 191.020 1.00 68.14  ? 2070 VAL A N     1 
ATOM   3549  C CA    . VAL A 1 2070 ? 190.977 183.216 190.213 1.00 68.14  ? 2070 VAL A CA    1 
ATOM   3550  C C     . VAL A 1 2070 ? 190.137 182.161 190.932 1.00 68.14  ? 2070 VAL A C     1 
ATOM   3551  O O     . VAL A 1 2070 ? 189.157 181.664 190.349 1.00 68.14  ? 2070 VAL A O     1 
ATOM   3552  C CB    . VAL A 1 2070 ? 192.349 182.656 189.812 1.00 68.14  ? 2070 VAL A CB    1 
ATOM   3553  C CG1   . VAL A 1 2070 ? 192.192 181.273 189.222 1.00 68.14  ? 2070 VAL A CG1   1 
ATOM   3554  C CG2   . VAL A 1 2070 ? 193.018 183.583 188.825 1.00 68.14  ? 2070 VAL A CG2   1 
ATOM   3555  N N     . PRO A 1 2071 ? 190.449 181.785 192.179 1.00 74.91  ? 2071 PRO A N     1 
ATOM   3556  C CA    . PRO A 1 2071 ? 189.562 180.844 192.872 1.00 74.91  ? 2071 PRO A CA    1 
ATOM   3557  C C     . PRO A 1 2071 ? 188.161 181.383 193.032 1.00 74.91  ? 2071 PRO A C     1 
ATOM   3558  O O     . PRO A 1 2071 ? 187.207 180.600 193.061 1.00 74.91  ? 2071 PRO A O     1 
ATOM   3559  C CB    . PRO A 1 2071 ? 190.250 180.636 194.227 1.00 74.91  ? 2071 PRO A CB    1 
ATOM   3560  C CG    . PRO A 1 2071 ? 191.651 181.019 194.000 1.00 74.91  ? 2071 PRO A CG    1 
ATOM   3561  C CD    . PRO A 1 2071 ? 191.584 182.155 193.038 1.00 74.91  ? 2071 PRO A CD    1 
ATOM   3562  N N     . PHE A 1 2072 ? 188.004 182.703 193.136 1.00 72.05  ? 2072 PHE A N     1 
ATOM   3563  C CA    . PHE A 1 2072 ? 186.665 183.272 193.199 1.00 72.05  ? 2072 PHE A CA    1 
ATOM   3564  C C     . PHE A 1 2072 ? 185.888 182.982 191.925 1.00 72.05  ? 2072 PHE A C     1 
ATOM   3565  O O     . PHE A 1 2072 ? 184.700 182.646 191.976 1.00 72.05  ? 2072 PHE A O     1 
ATOM   3566  C CB    . PHE A 1 2072 ? 186.738 184.775 193.441 1.00 72.05  ? 2072 PHE A CB    1 
ATOM   3567  C CG    . PHE A 1 2072 ? 185.454 185.484 193.164 1.00 72.05  ? 2072 PHE A CG    1 
ATOM   3568  C CD1   . PHE A 1 2072 ? 184.373 185.324 194.002 1.00 72.05  ? 2072 PHE A CD1   1 
ATOM   3569  C CD2   . PHE A 1 2072 ? 185.324 186.300 192.061 1.00 72.05  ? 2072 PHE A CD2   1 
ATOM   3570  C CE1   . PHE A 1 2072 ? 183.190 185.970 193.750 1.00 72.05  ? 2072 PHE A CE1   1 
ATOM   3571  C CE2   . PHE A 1 2072 ? 184.142 186.948 191.806 1.00 72.05  ? 2072 PHE A CE2   1 
ATOM   3572  C CZ    . PHE A 1 2072 ? 183.075 186.785 192.652 1.00 72.05  ? 2072 PHE A CZ    1 
ATOM   3573  N N     . PHE A 1 2073 ? 186.541 183.111 190.769 1.00 73.04  ? 2073 PHE A N     1 
ATOM   3574  C CA    . PHE A 1 2073 ? 185.880 182.775 189.514 1.00 73.04  ? 2073 PHE A CA    1 
ATOM   3575  C C     . PHE A 1 2073 ? 185.563 181.289 189.440 1.00 73.04  ? 2073 PHE A C     1 
ATOM   3576  O O     . PHE A 1 2073 ? 184.503 180.900 188.937 1.00 73.04  ? 2073 PHE A O     1 
ATOM   3577  C CB    . PHE A 1 2073 ? 186.742 183.202 188.332 1.00 73.04  ? 2073 PHE A CB    1 
ATOM   3578  C CG    . PHE A 1 2073 ? 186.263 184.448 187.660 1.00 73.04  ? 2073 PHE A CG    1 
ATOM   3579  C CD1   . PHE A 1 2073 ? 186.206 185.640 188.352 1.00 73.04  ? 2073 PHE A CD1   1 
ATOM   3580  C CD2   . PHE A 1 2073 ? 185.869 184.430 186.338 1.00 73.04  ? 2073 PHE A CD2   1 
ATOM   3581  C CE1   . PHE A 1 2073 ? 185.766 186.788 187.740 1.00 73.04  ? 2073 PHE A CE1   1 
ATOM   3582  C CE2   . PHE A 1 2073 ? 185.430 185.578 185.721 1.00 73.04  ? 2073 PHE A CE2   1 
ATOM   3583  C CZ    . PHE A 1 2073 ? 185.378 186.758 186.423 1.00 73.04  ? 2073 PHE A CZ    1 
ATOM   3584  N N     . LYS A 1 2074 ? 186.467 180.441 189.934 1.00 81.15  ? 2074 LYS A N     1 
ATOM   3585  C CA    . LYS A 1 2074 ? 186.175 179.010 189.970 1.00 81.15  ? 2074 LYS A CA    1 
ATOM   3586  C C     . LYS A 1 2074 ? 184.930 178.728 190.806 1.00 81.15  ? 2074 LYS A C     1 
ATOM   3587  O O     . LYS A 1 2074 ? 184.037 177.978 190.389 1.00 81.15  ? 2074 LYS A O     1 
ATOM   3588  C CB    . LYS A 1 2074 ? 187.377 178.247 190.524 1.00 81.15  ? 2074 LYS A CB    1 
ATOM   3589  C CG    . LYS A 1 2074 ? 187.339 176.757 190.261 1.00 81.15  ? 2074 LYS A CG    1 
ATOM   3590  C CD    . LYS A 1 2074 ? 187.399 176.467 188.773 1.00 81.15  ? 2074 LYS A CD    1 
ATOM   3591  C CE    . LYS A 1 2074 ? 188.664 177.038 188.151 1.00 81.15  ? 2074 LYS A CE    1 
ATOM   3592  N NZ    . LYS A 1 2074 ? 189.887 176.657 188.911 1.00 81.15  ? 2074 LYS A NZ    1 
ATOM   3593  N N     . LEU A 1 2075 ? 184.850 179.338 191.988 1.00 77.20  ? 2075 LEU A N     1 
ATOM   3594  C CA    . LEU A 1 2075 ? 183.693 179.141 192.852 1.00 77.20  ? 2075 LEU A CA    1 
ATOM   3595  C C     . LEU A 1 2075 ? 182.422 179.635 192.179 1.00 77.20  ? 2075 LEU A C     1 
ATOM   3596  O O     . LEU A 1 2075 ? 181.389 178.957 192.204 1.00 77.20  ? 2075 LEU A O     1 
ATOM   3597  C CB    . LEU A 1 2075 ? 183.903 179.856 194.185 1.00 77.20  ? 2075 LEU A CB    1 
ATOM   3598  C CG    . LEU A 1 2075 ? 185.111 179.471 195.033 1.00 77.20  ? 2075 LEU A CG    1 
ATOM   3599  C CD1   . LEU A 1 2075 ? 184.844 179.783 196.490 1.00 77.20  ? 2075 LEU A CD1   1 
ATOM   3600  C CD2   . LEU A 1 2075 ? 185.454 178.008 194.854 1.00 77.20  ? 2075 LEU A CD2   1 
ATOM   3601  N N     . CYS A 1 2076 ? 182.481 180.818 191.563 1.00 81.74  ? 2076 CYS A N     1 
ATOM   3602  C CA    . CYS A 1 2076 ? 181.311 181.346 190.873 1.00 81.74  ? 2076 CYS A CA    1 
ATOM   3603  C C     . CYS A 1 2076 ? 180.872 180.430 189.744 1.00 81.74  ? 2076 CYS A C     1 
ATOM   3604  O O     . CYS A 1 2076 ? 179.672 180.305 189.477 1.00 81.74  ? 2076 CYS A O     1 
ATOM   3605  C CB    . CYS A 1 2076 ? 181.598 182.744 190.335 1.00 81.74  ? 2076 CYS A CB    1 
ATOM   3606  S SG    . CYS A 1 2076 ? 181.318 184.063 191.526 1.00 81.74  ? 2076 CYS A SG    1 
ATOM   3607  N N     . ASP A 1 2077 ? 181.821 179.784 189.068 1.00 88.35  ? 2077 ASP A N     1 
ATOM   3608  C CA    . ASP A 1 2077 ? 181.445 178.807 188.056 1.00 88.35  ? 2077 ASP A CA    1 
ATOM   3609  C C     . ASP A 1 2077 ? 180.818 177.569 188.674 1.00 88.35  ? 2077 ASP A C     1 
ATOM   3610  O O     . ASP A 1 2077 ? 179.969 176.930 188.045 1.00 88.35  ? 2077 ASP A O     1 
ATOM   3611  C CB    . ASP A 1 2077 ? 182.653 178.413 187.213 1.00 88.35  ? 2077 ASP A CB    1 
ATOM   3612  C CG    . ASP A 1 2077 ? 182.256 177.720 185.931 1.00 88.35  ? 2077 ASP A CG    1 
ATOM   3613  O OD1   . ASP A 1 2077 ? 181.116 177.937 185.472 1.00 88.35  ? 2077 ASP A OD1   1 
ATOM   3614  O OD2   . ASP A 1 2077 ? 183.079 176.961 185.381 1.00 88.35  ? 2077 ASP A OD2   1 
ATOM   3615  N N     . GLU A 1 2078 ? 181.220 177.209 189.891 1.00 89.47  ? 2078 GLU A N     1 
ATOM   3616  C CA    . GLU A 1 2078 ? 180.670 176.019 190.527 1.00 89.47  ? 2078 GLU A CA    1 
ATOM   3617  C C     . GLU A 1 2078 ? 179.516 176.319 191.475 1.00 89.47  ? 2078 GLU A C     1 
ATOM   3618  O O     . GLU A 1 2078 ? 178.433 175.753 191.313 1.00 89.47  ? 2078 GLU A O     1 
ATOM   3619  C CB    . GLU A 1 2078 ? 181.767 175.267 191.290 1.00 89.47  ? 2078 GLU A CB    1 
ATOM   3620  C CG    . GLU A 1 2078 ? 181.293 174.263 192.360 1.00 89.47  ? 2078 GLU A CG    1 
ATOM   3621  C CD    . GLU A 1 2078 ? 180.160 173.325 191.928 1.00 89.47  ? 2078 GLU A CD    1 
ATOM   3622  O OE1   . GLU A 1 2078 ? 179.617 172.630 192.811 1.00 89.47  ? 2078 GLU A OE1   1 
ATOM   3623  O OE2   . GLU A 1 2078 ? 179.838 173.228 190.725 1.00 89.47  ? 2078 GLU A OE2   1 
ATOM   3624  N N     . GLN A 1 2079 ? 179.722 177.195 192.461 1.00 82.34  ? 2079 GLN A N     1 
ATOM   3625  C CA    . GLN A 1 2079 ? 178.719 177.391 193.504 1.00 82.34  ? 2079 GLN A CA    1 
ATOM   3626  C C     . GLN A 1 2079 ? 177.412 177.923 192.931 1.00 82.34  ? 2079 GLN A C     1 
ATOM   3627  O O     . GLN A 1 2079 ? 176.327 177.527 193.371 1.00 82.34  ? 2079 GLN A O     1 
ATOM   3628  C CB    . GLN A 1 2079 ? 179.257 178.341 194.571 1.00 82.34  ? 2079 GLN A CB    1 
ATOM   3629  C CG    . GLN A 1 2079 ? 180.441 177.796 195.342 1.00 82.34  ? 2079 GLN A CG    1 
ATOM   3630  C CD    . GLN A 1 2079 ? 180.031 176.937 196.516 1.00 82.34  ? 2079 GLN A CD    1 
ATOM   3631  O OE1   . GLN A 1 2079 ? 179.414 177.418 197.464 1.00 82.34  ? 2079 GLN A OE1   1 
ATOM   3632  N NE2   . GLN A 1 2079 ? 180.373 175.657 196.459 1.00 82.34  ? 2079 GLN A NE2   1 
ATOM   3633  N N     . LEU A 1 2080 ? 177.493 178.823 191.959 1.00 81.96  ? 2080 LEU A N     1 
ATOM   3634  C CA    . LEU A 1 2080 ? 176.299 179.411 191.377 1.00 81.96  ? 2080 LEU A CA    1 
ATOM   3635  C C     . LEU A 1 2080 ? 175.559 178.394 190.515 1.00 81.96  ? 2080 LEU A C     1 
ATOM   3636  O O     . LEU A 1 2080 ? 176.140 177.440 189.991 1.00 81.96  ? 2080 LEU A O     1 
ATOM   3637  C CB    . LEU A 1 2080 ? 176.663 180.633 190.540 1.00 81.96  ? 2080 LEU A CB    1 
ATOM   3638  C CG    . LEU A 1 2080 ? 177.248 181.790 191.343 1.00 81.96  ? 2080 LEU A CG    1 
ATOM   3639  C CD1   . LEU A 1 2080 ? 177.378 183.017 190.474 1.00 81.96  ? 2080 LEU A CD1   1 
ATOM   3640  C CD2   . LEU A 1 2080 ? 176.384 182.077 192.553 1.00 81.96  ? 2080 LEU A CD2   1 
ATOM   3641  N N     . SER A 1 2081 ? 174.255 178.612 190.372 1.00 84.75  ? 2081 SER A N     1 
ATOM   3642  C CA    . SER A 1 2081 ? 173.437 177.741 189.545 1.00 84.75  ? 2081 SER A CA    1 
ATOM   3643  C C     . SER A 1 2081 ? 173.832 177.874 188.080 1.00 84.75  ? 2081 SER A C     1 
ATOM   3644  O O     . SER A 1 2081 ? 174.266 178.931 187.618 1.00 84.75  ? 2081 SER A O     1 
ATOM   3645  C CB    . SER A 1 2081 ? 171.957 178.077 189.709 1.00 84.75  ? 2081 SER A CB    1 
ATOM   3646  O OG    . SER A 1 2081 ? 171.629 179.250 188.988 1.00 84.75  ? 2081 SER A OG    1 
ATOM   3647  N N     . SER A 1 2082 ? 173.675 176.780 187.344 1.00 82.71  ? 2082 SER A N     1 
ATOM   3648  C CA    . SER A 1 2082 ? 174.037 176.768 185.935 1.00 82.71  ? 2082 SER A CA    1 
ATOM   3649  C C     . SER A 1 2082 ? 173.009 177.546 185.128 1.00 82.71  ? 2082 SER A C     1 
ATOM   3650  O O     . SER A 1 2082 ? 171.802 177.335 185.272 1.00 82.71  ? 2082 SER A O     1 
ATOM   3651  C CB    . SER A 1 2082 ? 174.139 175.336 185.415 1.00 82.71  ? 2082 SER A CB    1 
ATOM   3652  O OG    . SER A 1 2082 ? 173.819 175.279 184.036 1.00 82.71  ? 2082 SER A OG    1 
ATOM   3653  N N     . GLN A 1 2083 ? 173.492 178.452 184.285 1.00 86.21  ? 2083 GLN A N     1 
ATOM   3654  C CA    . GLN A 1 2083 ? 172.634 179.229 183.409 1.00 86.21  ? 2083 GLN A CA    1 
ATOM   3655  C C     . GLN A 1 2083 ? 173.293 179.342 182.046 1.00 86.21  ? 2083 GLN A C     1 
ATOM   3656  O O     . GLN A 1 2083 ? 174.520 179.324 181.930 1.00 86.21  ? 2083 GLN A O     1 
ATOM   3657  C CB    . GLN A 1 2083 ? 172.362 180.626 183.969 1.00 86.21  ? 2083 GLN A CB    1 
ATOM   3658  C CG    . GLN A 1 2083 ? 171.478 180.643 185.196 1.00 86.21  ? 2083 GLN A CG    1 
ATOM   3659  C CD    . GLN A 1 2083 ? 170.011 180.544 184.847 1.00 86.21  ? 2083 GLN A CD    1 
ATOM   3660  O OE1   . GLN A 1 2083 ? 169.645 180.488 183.674 1.00 86.21  ? 2083 GLN A OE1   1 
ATOM   3661  N NE2   . GLN A 1 2083 ? 169.160 180.526 185.865 1.00 86.21  ? 2083 GLN A NE2   1 
ATOM   3662  N N     . SER A 1 2084 ? 172.461 179.455 181.012 1.00 92.47  ? 2084 SER A N     1 
ATOM   3663  C CA    . SER A 1 2084 ? 172.992 179.636 179.667 1.00 92.47  ? 2084 SER A CA    1 
ATOM   3664  C C     . SER A 1 2084 ? 173.720 180.966 179.543 1.00 92.47  ? 2084 SER A C     1 
ATOM   3665  O O     . SER A 1 2084 ? 174.759 181.056 178.879 1.00 92.47  ? 2084 SER A O     1 
ATOM   3666  C CB    . SER A 1 2084 ? 171.864 179.545 178.641 1.00 92.47  ? 2084 SER A CB    1 
ATOM   3667  O OG    . SER A 1 2084 ? 172.342 179.817 177.336 1.00 92.47  ? 2084 SER A OG    1 
ATOM   3668  N N     . HIS A 1 2085 ? 173.191 182.009 180.175 1.00 89.09  ? 2085 HIS A N     1 
ATOM   3669  C CA    . HIS A 1 2085 ? 173.754 183.343 180.038 1.00 89.09  ? 2085 HIS A CA    1 
ATOM   3670  C C     . HIS A 1 2085 ? 174.943 183.594 180.956 1.00 89.09  ? 2085 HIS A C     1 
ATOM   3671  O O     . HIS A 1 2085 ? 175.670 184.569 180.740 1.00 89.09  ? 2085 HIS A O     1 
ATOM   3672  C CB    . HIS A 1 2085 ? 172.672 184.387 180.302 1.00 89.09  ? 2085 HIS A CB    1 
ATOM   3673  C CG    . HIS A 1 2085 ? 172.124 184.356 181.694 1.00 89.09  ? 2085 HIS A CG    1 
ATOM   3674  N ND1   . HIS A 1 2085 ? 171.231 183.399 182.122 1.00 89.09  ? 2085 HIS A ND1   1 
ATOM   3675  C CD2   . HIS A 1 2085 ? 172.336 185.171 182.753 1.00 89.09  ? 2085 HIS A CD2   1 
ATOM   3676  C CE1   . HIS A 1 2085 ? 170.919 183.624 183.385 1.00 89.09  ? 2085 HIS A CE1   1 
ATOM   3677  N NE2   . HIS A 1 2085 ? 171.576 184.694 183.791 1.00 89.09  ? 2085 HIS A NE2   1 
ATOM   3678  N N     . TYR A 1 2086 ? 175.157 182.755 181.965 1.00 86.15  ? 2086 TYR A N     1 
ATOM   3679  C CA    . TYR A 1 2086 ? 176.313 182.919 182.834 1.00 86.15  ? 2086 TYR A CA    1 
ATOM   3680  C C     . TYR A 1 2086 ? 177.591 182.634 182.062 1.00 86.15  ? 2086 TYR A C     1 
ATOM   3681  O O     . TYR A 1 2086 ? 177.631 181.750 181.204 1.00 86.15  ? 2086 TYR A O     1 
ATOM   3682  C CB    . TYR A 1 2086 ? 176.224 181.981 184.035 1.00 86.15  ? 2086 TYR A CB    1 
ATOM   3683  C CG    . TYR A 1 2086 ? 175.278 182.436 185.116 1.00 86.15  ? 2086 TYR A CG    1 
ATOM   3684  C CD1   . TYR A 1 2086 ? 174.638 183.659 185.037 1.00 86.15  ? 2086 TYR A CD1   1 
ATOM   3685  C CD2   . TYR A 1 2086 ? 175.025 181.637 186.216 1.00 86.15  ? 2086 TYR A CD2   1 
ATOM   3686  C CE1   . TYR A 1 2086 ? 173.774 184.071 186.024 1.00 86.15  ? 2086 TYR A CE1   1 
ATOM   3687  C CE2   . TYR A 1 2086 ? 174.163 182.042 187.206 1.00 86.15  ? 2086 TYR A CE2   1 
ATOM   3688  C CZ    . TYR A 1 2086 ? 173.541 183.259 187.105 1.00 86.15  ? 2086 TYR A CZ    1 
ATOM   3689  O OH    . TYR A 1 2086 ? 172.679 183.666 188.093 1.00 86.15  ? 2086 TYR A OH    1 
ATOM   3690  N N     . ASP A 1 2087 ? 178.641 183.389 182.368 1.00 87.74  ? 2087 ASP A N     1 
ATOM   3691  C CA    . ASP A 1 2087 ? 179.942 183.153 181.748 1.00 87.74  ? 2087 ASP A CA    1 
ATOM   3692  C C     . ASP A 1 2087 ? 181.025 183.489 182.760 1.00 87.74  ? 2087 ASP A C     1 
ATOM   3693  O O     . ASP A 1 2087 ? 181.057 184.603 183.291 1.00 87.74  ? 2087 ASP A O     1 
ATOM   3694  C CB    . ASP A 1 2087 ? 180.110 183.972 180.475 1.00 87.74  ? 2087 ASP A CB    1 
ATOM   3695  C CG    . ASP A 1 2087 ? 181.367 183.608 179.717 1.00 87.74  ? 2087 ASP A CG    1 
ATOM   3696  O OD1   . ASP A 1 2087 ? 181.830 182.458 179.858 1.00 87.74  ? 2087 ASP A OD1   1 
ATOM   3697  O OD2   . ASP A 1 2087 ? 181.889 184.467 178.980 1.00 87.74  ? 2087 ASP A OD2   1 
ATOM   3698  N N     . PHE A 1 2088 ? 181.900 182.525 183.030 1.00 79.52  ? 2088 PHE A N     1 
ATOM   3699  C CA    . PHE A 1 2088 ? 183.014 182.704 183.948 1.00 79.52  ? 2088 PHE A CA    1 
ATOM   3700  C C     . PHE A 1 2088 ? 184.317 182.211 183.336 1.00 79.52  ? 2088 PHE A C     1 
ATOM   3701  O O     . PHE A 1 2088 ? 185.222 181.774 184.047 1.00 79.52  ? 2088 PHE A O     1 
ATOM   3702  C CB    . PHE A 1 2088 ? 182.735 181.997 185.269 1.00 79.52  ? 2088 PHE A CB    1 
ATOM   3703  C CG    . PHE A 1 2088 ? 181.559 182.549 186.003 1.00 79.52  ? 2088 PHE A CG    1 
ATOM   3704  C CD1   . PHE A 1 2088 ? 181.628 183.788 186.607 1.00 79.52  ? 2088 PHE A CD1   1 
ATOM   3705  C CD2   . PHE A 1 2088 ? 180.382 181.838 186.078 1.00 79.52  ? 2088 PHE A CD2   1 
ATOM   3706  C CE1   . PHE A 1 2088 ? 180.548 184.303 187.282 1.00 79.52  ? 2088 PHE A CE1   1 
ATOM   3707  C CE2   . PHE A 1 2088 ? 179.299 182.349 186.750 1.00 79.52  ? 2088 PHE A CE2   1 
ATOM   3708  C CZ    . PHE A 1 2088 ? 179.383 183.584 187.354 1.00 79.52  ? 2088 PHE A CZ    1 
ATOM   3709  N N     . GLY A 1 2089 ? 184.418 182.299 182.006 1.00 81.02  ? 2089 GLY A N     1 
ATOM   3710  C CA    . GLY A 1 2089 ? 185.635 181.840 181.309 1.00 81.02  ? 2089 GLY A CA    1 
ATOM   3711  C C     . GLY A 1 2089 ? 186.813 182.770 181.544 1.00 81.02  ? 2089 GLY A C     1 
ATOM   3712  O O     . GLY A 1 2089 ? 186.616 183.822 182.184 1.00 81.02  ? 2089 GLY A O     1 
ATOM   3713  N N     . LEU A 1 2090 ? 187.993 182.402 181.038 1.00 77.47  ? 2090 LEU A N     1 
ATOM   3714  C CA    . LEU A 1 2090 ? 189.207 183.243 181.214 1.00 77.47  ? 2090 LEU A CA    1 
ATOM   3715  C C     . LEU A 1 2090 ? 188.939 184.627 180.619 1.00 77.47  ? 2090 LEU A C     1 
ATOM   3716  O O     . LEU A 1 2090 ? 189.361 185.624 181.233 1.00 77.47  ? 2090 LEU A O     1 
ATOM   3717  C CB    . LEU A 1 2090 ? 190.391 182.569 180.515 1.00 77.47  ? 2090 LEU A CB    1 
ATOM   3718  C CG    . LEU A 1 2090 ? 191.698 183.360 180.536 1.00 77.47  ? 2090 LEU A CG    1 
ATOM   3719  C CD1   . LEU A 1 2090 ? 192.282 183.399 181.939 1.00 77.47  ? 2090 LEU A CD1   1 
ATOM   3720  C CD2   . LEU A 1 2090 ? 192.703 182.773 179.557 1.00 77.47  ? 2090 LEU A CD2   1 
ATOM   3721  N N     . ARG A 1 2091 ? 188.254 184.676 179.473 1.00 84.99  ? 2091 ARG A N     1 
ATOM   3722  C CA    . ARG A 1 2091 ? 187.947 185.973 178.814 1.00 84.99  ? 2091 ARG A CA    1 
ATOM   3723  C C     . ARG A 1 2091 ? 187.152 186.848 179.787 1.00 84.99  ? 2091 ARG A C     1 
ATOM   3724  O O     . ARG A 1 2091 ? 187.480 188.044 179.909 1.00 84.99  ? 2091 ARG A O     1 
ATOM   3725  C CB    . ARG A 1 2091 ? 187.159 185.735 177.523 1.00 84.99  ? 2091 ARG A CB    1 
ATOM   3726  C CG    . ARG A 1 2091 ? 186.835 187.005 176.749 1.00 84.99  ? 2091 ARG A CG    1 
ATOM   3727  C CD    . ARG A 1 2091 ? 186.200 186.696 175.407 1.00 84.99  ? 2091 ARG A CD    1 
ATOM   3728  N NE    . ARG A 1 2091 ? 187.070 185.887 174.565 1.00 84.99  ? 2091 ARG A NE    1 
ATOM   3729  C CZ    . ARG A 1 2091 ? 186.757 185.471 173.343 1.00 84.99  ? 2091 ARG A CZ    1 
ATOM   3730  N NH1   . ARG A 1 2091 ? 185.562 185.726 172.843 1.00 84.99  ? 2091 ARG A NH1   1 
ATOM   3731  N NH2   . ARG A 1 2091 ? 187.641 184.799 172.626 1.00 84.99  ? 2091 ARG A NH2   1 
ATOM   3732  N N     . ALA A 1 2092 ? 186.159 186.261 180.461 1.00 81.71  ? 2092 ALA A N     1 
ATOM   3733  C CA    . ALA A 1 2092 ? 185.342 187.023 181.432 1.00 81.71  ? 2092 ALA A CA    1 
ATOM   3734  C C     . ALA A 1 2092 ? 186.258 187.600 182.515 1.00 81.71  ? 2092 ALA A C     1 
ATOM   3735  O O     . ALA A 1 2092 ? 186.139 188.803 182.816 1.00 81.71  ? 2092 ALA A O     1 
ATOM   3736  C CB    . ALA A 1 2092 ? 184.285 186.125 182.026 1.00 81.71  ? 2092 ALA A CB    1 
ATOM   3737  N N     . LEU A 1 2093 ? 187.153 186.772 183.059 1.00 72.81  ? 2093 LEU A N     1 
ATOM   3738  C CA    . LEU A 1 2093 ? 188.088 187.244 184.112 1.00 72.81  ? 2093 LEU A CA    1 
ATOM   3739  C C     . LEU A 1 2093 ? 188.927 188.392 183.547 1.00 72.81  ? 2093 LEU A C     1 
ATOM   3740  O O     . LEU A 1 2093 ? 188.988 189.448 184.201 1.00 72.81  ? 2093 LEU A O     1 
ATOM   3741  C CB    . LEU A 1 2093 ? 188.984 186.080 184.542 1.00 72.81  ? 2093 LEU A CB    1 
ATOM   3742  C CG    . LEU A 1 2093 ? 190.075 186.437 185.550 1.00 72.81  ? 2093 LEU A CG    1 
ATOM   3743  C CD1   . LEU A 1 2093 ? 189.488 186.621 186.940 1.00 72.81  ? 2093 LEU A CD1   1 
ATOM   3744  C CD2   . LEU A 1 2093 ? 191.166 185.377 185.568 1.00 72.81  ? 2093 LEU A CD2   1 
ATOM   3745  N N     . LYS A 1 2094 ? 189.510 188.203 182.360 1.00 74.98  ? 2094 LYS A N     1 
ATOM   3746  C CA    . LYS A 1 2094 ? 190.404 189.238 181.777 1.00 74.98  ? 2094 LYS A CA    1 
ATOM   3747  C C     . LYS A 1 2094 ? 189.646 190.566 181.678 1.00 74.98  ? 2094 LYS A C     1 
ATOM   3748  O O     . LYS A 1 2094 ? 190.196 191.593 182.120 1.00 74.98  ? 2094 LYS A O     1 
ATOM   3749  C CB    . LYS A 1 2094 ? 190.908 188.787 180.403 1.00 74.98  ? 2094 LYS A CB    1 
ATOM   3750  C CG    . LYS A 1 2094 ? 191.664 187.465 180.395 1.00 74.98  ? 2094 LYS A CG    1 
ATOM   3751  C CD    . LYS A 1 2094 ? 192.150 187.065 179.021 1.00 74.98  ? 2094 LYS A CD    1 
ATOM   3752  C CE    . LYS A 1 2094 ? 193.075 188.094 178.406 1.00 74.98  ? 2094 LYS A CE    1 
ATOM   3753  N NZ    . LYS A 1 2094 ? 194.291 188.297 179.227 1.00 74.98  ? 2094 LYS A NZ    1 
ATOM   3754  N N     . SER A 1 2095 ? 188.429 190.536 181.129 1.00 79.08  ? 2095 SER A N     1 
ATOM   3755  C CA    . SER A 1 2095 ? 187.619 191.775 180.998 1.00 79.08  ? 2095 SER A CA    1 
ATOM   3756  C C     . SER A 1 2095 ? 187.451 192.412 182.379 1.00 79.08  ? 2095 SER A C     1 
ATOM   3757  O O     . SER A 1 2095 ? 187.921 193.547 182.569 1.00 79.08  ? 2095 SER A O     1 
ATOM   3758  C CB    . SER A 1 2095 ? 186.287 191.488 180.357 1.00 79.08  ? 2095 SER A CB    1 
ATOM   3759  O OG    . SER A 1 2095 ? 185.548 190.551 181.125 1.00 79.08  ? 2095 SER A OG    1 
ATOM   3760  N N     . VAL A 1 2096 ? 186.808 191.702 183.307 1.00 71.88  ? 2096 VAL A N     1 
ATOM   3761  C CA    . VAL A 1 2096 ? 186.642 192.217 184.661 1.00 71.88  ? 2096 VAL A CA    1 
ATOM   3762  C C     . VAL A 1 2096 ? 187.904 192.938 185.113 1.00 71.88  ? 2096 VAL A C     1 
ATOM   3763  O O     . VAL A 1 2096 ? 187.839 194.008 185.728 1.00 71.88  ? 2096 VAL A O     1 
ATOM   3764  C CB    . VAL A 1 2096 ? 186.263 191.079 185.623 1.00 71.88  ? 2096 VAL A CB    1 
ATOM   3765  C CG1   . VAL A 1 2096 ? 186.502 191.496 187.059 1.00 71.88  ? 2096 VAL A CG1   1 
ATOM   3766  C CG2   . VAL A 1 2096 ? 184.818 190.688 185.415 1.00 71.88  ? 2096 VAL A CG2   1 
ATOM   3767  N N     . LEU A 1 2097 ? 189.072 192.370 184.813 1.00 72.37  ? 2097 LEU A N     1 
ATOM   3768  C CA    . LEU A 1 2097 ? 190.312 192.998 185.261 1.00 72.37  ? 2097 LEU A CA    1 
ATOM   3769  C C     . LEU A 1 2097 ? 190.539 194.340 184.576 1.00 72.37  ? 2097 LEU A C     1 
ATOM   3770  O O     . LEU A 1 2097 ? 190.960 195.307 185.222 1.00 72.37  ? 2097 LEU A O     1 
ATOM   3771  C CB    . LEU A 1 2097 ? 191.501 192.073 185.026 1.00 72.37  ? 2097 LEU A CB    1 
ATOM   3772  C CG    . LEU A 1 2097 ? 191.296 190.638 185.502 1.00 72.37  ? 2097 LEU A CG    1 
ATOM   3773  C CD1   . LEU A 1 2097 ? 192.342 189.709 184.911 1.00 72.37  ? 2097 LEU A CD1   1 
ATOM   3774  C CD2   . LEU A 1 2097 ? 191.227 190.531 187.012 1.00 72.37  ? 2097 LEU A CD2   1 
ATOM   3775  N N     . VAL A 1 2098 ? 190.283 194.424 183.269 1.00 73.15  ? 2098 VAL A N     1 
ATOM   3776  C CA    . VAL A 1 2098 ? 190.477 195.704 182.592 1.00 73.15  ? 2098 VAL A CA    1 
ATOM   3777  C C     . VAL A 1 2098 ? 189.458 196.725 183.085 1.00 73.15  ? 2098 VAL A C     1 
ATOM   3778  O O     . VAL A 1 2098 ? 189.760 197.921 183.192 1.00 73.15  ? 2098 VAL A O     1 
ATOM   3779  C CB    . VAL A 1 2098 ? 190.444 195.540 181.060 1.00 73.15  ? 2098 VAL A CB    1 
ATOM   3780  C CG1   . VAL A 1 2098 ? 191.427 194.473 180.624 1.00 73.15  ? 2098 VAL A CG1   1 
ATOM   3781  C CG2   . VAL A 1 2098 ? 189.050 195.224 180.559 1.00 73.15  ? 2098 VAL A CG2   1 
ATOM   3782  N N     . SER A 1 2099 ? 188.245 196.276 183.412 1.00 73.84  ? 2099 SER A N     1 
ATOM   3783  C CA    . SER A 1 2099 ? 187.280 197.184 184.019 1.00 73.84  ? 2099 SER A CA    1 
ATOM   3784  C C     . SER A 1 2099 ? 187.775 197.677 185.372 1.00 73.84  ? 2099 SER A C     1 
ATOM   3785  O O     . SER A 1 2099 ? 187.583 198.845 185.725 1.00 73.84  ? 2099 SER A O     1 
ATOM   3786  C CB    . SER A 1 2099 ? 185.925 196.496 184.155 1.00 73.84  ? 2099 SER A CB    1 
ATOM   3787  O OG    . SER A 1 2099 ? 185.307 196.352 182.890 1.00 73.84  ? 2099 SER A OG    1 
ATOM   3788  N N     . ALA A 1 2100 ? 188.414 196.799 186.145 1.00 72.35  ? 2100 ALA A N     1 
ATOM   3789  C CA    . ALA A 1 2100 ? 188.977 197.216 187.424 1.00 72.35  ? 2100 ALA A CA    1 
ATOM   3790  C C     . ALA A 1 2100 ? 190.073 198.250 187.229 1.00 72.35  ? 2100 ALA A C     1 
ATOM   3791  O O     . ALA A 1 2100 ? 190.173 199.214 187.995 1.00 72.35  ? 2100 ALA A O     1 
ATOM   3792  C CB    . ALA A 1 2100 ? 189.520 196.007 188.180 1.00 72.35  ? 2100 ALA A CB    1 
ATOM   3793  N N     . GLY A 1 2101 ? 190.919 198.051 186.222 1.00 76.29  ? 2101 GLY A N     1 
ATOM   3794  C CA    . GLY A 1 2101 ? 191.941 199.041 185.927 1.00 76.29  ? 2101 GLY A CA    1 
ATOM   3795  C C     . GLY A 1 2101 ? 191.348 200.385 185.553 1.00 76.29  ? 2101 GLY A C     1 
ATOM   3796  O O     . GLY A 1 2101 ? 191.816 201.434 186.006 1.00 76.29  ? 2101 GLY A O     1 
ATOM   3797  N N     . ASN A 1 2102 ? 190.300 200.370 184.726 1.00 80.60  ? 2102 ASN A N     1 
ATOM   3798  C CA    . ASN A 1 2102 ? 189.620 201.613 184.378 1.00 80.60  ? 2102 ASN A CA    1 
ATOM   3799  C C     . ASN A 1 2102 ? 189.030 202.278 185.614 1.00 80.60  ? 2102 ASN A C     1 
ATOM   3800  O O     . ASN A 1 2102 ? 189.098 203.503 185.760 1.00 80.60  ? 2102 ASN A O     1 
ATOM   3801  C CB    . ASN A 1 2102 ? 188.529 201.344 183.345 1.00 80.60  ? 2102 ASN A CB    1 
ATOM   3802  C CG    . ASN A 1 2102 ? 189.089 201.088 181.966 1.00 80.60  ? 2102 ASN A CG    1 
ATOM   3803  O OD1   . ASN A 1 2102 ? 190.272 201.308 181.717 1.00 80.60  ? 2102 ASN A OD1   1 
ATOM   3804  N ND2   . ASN A 1 2102 ? 188.241 200.620 181.059 1.00 80.60  ? 2102 ASN A ND2   1 
ATOM   3805  N N     . VAL A 1 2103 ? 188.447 201.484 186.513 1.00 75.41  ? 2103 VAL A N     1 
ATOM   3806  C CA    . VAL A 1 2103 ? 187.853 202.038 187.726 1.00 75.41  ? 2103 VAL A CA    1 
ATOM   3807  C C     . VAL A 1 2103 ? 188.923 202.669 188.605 1.00 75.41  ? 2103 VAL A C     1 
ATOM   3808  O O     . VAL A 1 2103 ? 188.731 203.758 189.160 1.00 75.41  ? 2103 VAL A O     1 
ATOM   3809  C CB    . VAL A 1 2103 ? 187.073 200.948 188.481 1.00 75.41  ? 2103 VAL A CB    1 
ATOM   3810  C CG1   . VAL A 1 2103 ? 186.746 201.413 189.881 1.00 75.41  ? 2103 VAL A CG1   1 
ATOM   3811  C CG2   . VAL A 1 2103 ? 185.807 200.603 187.731 1.00 75.41  ? 2103 VAL A CG2   1 
ATOM   3812  N N     . LYS A 1 2104 ? 190.063 201.994 188.753 1.00 77.32  ? 2104 LYS A N     1 
ATOM   3813  C CA    . LYS A 1 2104 ? 191.145 202.551 189.555 1.00 77.32  ? 2104 LYS A CA    1 
ATOM   3814  C C     . LYS A 1 2104 ? 191.665 203.845 188.950 1.00 77.32  ? 2104 LYS A C     1 
ATOM   3815  O O     . LYS A 1 2104 ? 191.933 204.811 189.671 1.00 77.32  ? 2104 LYS A O     1 
ATOM   3816  C CB    . LYS A 1 2104 ? 192.280 201.541 189.696 1.00 77.32  ? 2104 LYS A CB    1 
ATOM   3817  C CG    . LYS A 1 2104 ? 193.502 202.099 190.401 1.00 77.32  ? 2104 LYS A CG    1 
ATOM   3818  C CD    . LYS A 1 2104 ? 194.323 200.995 191.030 1.00 77.32  ? 2104 LYS A CD    1 
ATOM   3819  C CE    . LYS A 1 2104 ? 195.383 201.558 191.955 1.00 77.32  ? 2104 LYS A CE    1 
ATOM   3820  N NZ    . LYS A 1 2104 ? 196.690 201.692 191.268 1.00 77.32  ? 2104 LYS A NZ    1 
ATOM   3821  N N     . ARG A 1 2105 ? 191.813 203.885 187.626 1.00 84.44  ? 2105 ARG A N     1 
ATOM   3822  C CA    . ARG A 1 2105 ? 192.268 205.112 186.983 1.00 84.44  ? 2105 ARG A CA    1 
ATOM   3823  C C     . ARG A 1 2105 ? 191.264 206.239 187.178 1.00 84.44  ? 2105 ARG A C     1 
ATOM   3824  O O     . ARG A 1 2105 ? 191.648 207.390 187.419 1.00 84.44  ? 2105 ARG A O     1 
ATOM   3825  C CB    . ARG A 1 2105 ? 192.519 204.861 185.499 1.00 84.44  ? 2105 ARG A CB    1 
ATOM   3826  C CG    . ARG A 1 2105 ? 193.878 204.260 185.216 1.00 84.44  ? 2105 ARG A CG    1 
ATOM   3827  C CD    . ARG A 1 2105 ? 194.110 204.107 183.730 1.00 84.44  ? 2105 ARG A CD    1 
ATOM   3828  N NE    . ARG A 1 2105 ? 193.195 203.141 183.137 1.00 84.44  ? 2105 ARG A NE    1 
ATOM   3829  C CZ    . ARG A 1 2105 ? 193.323 201.827 183.245 1.00 84.44  ? 2105 ARG A CZ    1 
ATOM   3830  N NH1   . ARG A 1 2105 ? 194.316 201.282 183.928 1.00 84.44  ? 2105 ARG A NH1   1 
ATOM   3831  N NH2   . ARG A 1 2105 ? 192.432 201.039 182.652 1.00 84.44  ? 2105 ARG A NH2   1 
ATOM   3832  N N     . GLU A 1 2106 ? 189.972 205.929 187.075 1.00 86.87  ? 2106 GLU A N     1 
ATOM   3833  C CA    . GLU A 1 2106 ? 188.952 206.951 187.270 1.00 86.87  ? 2106 GLU A CA    1 
ATOM   3834  C C     . GLU A 1 2106 ? 188.963 207.475 188.700 1.00 86.87  ? 2106 GLU A C     1 
ATOM   3835  O O     . GLU A 1 2106 ? 188.834 208.684 188.925 1.00 86.87  ? 2106 GLU A O     1 
ATOM   3836  C CB    . GLU A 1 2106 ? 187.582 206.385 186.902 1.00 86.87  ? 2106 GLU A CB    1 
ATOM   3837  C CG    . GLU A 1 2106 ? 186.419 207.322 187.155 1.00 86.87  ? 2106 GLU A CG    1 
ATOM   3838  C CD    . GLU A 1 2106 ? 185.760 207.079 188.493 1.00 86.87  ? 2106 GLU A CD    1 
ATOM   3839  O OE1   . GLU A 1 2106 ? 186.228 206.187 189.231 1.00 86.87  ? 2106 GLU A OE1   1 
ATOM   3840  O OE2   . GLU A 1 2106 ? 184.769 207.773 188.803 1.00 86.87  ? 2106 GLU A OE2   1 
ATOM   3841  N N     . ARG A 1 2107 ? 189.120 206.582 189.679 1.00 81.02  ? 2107 ARG A N     1 
ATOM   3842  C CA    . ARG A 1 2107 ? 189.211 207.022 191.067 1.00 81.02  ? 2107 ARG A CA    1 
ATOM   3843  C C     . ARG A 1 2107 ? 190.461 207.860 191.297 1.00 81.02  ? 2107 ARG A C     1 
ATOM   3844  O O     . ARG A 1 2107 ? 190.437 208.827 192.069 1.00 81.02  ? 2107 ARG A O     1 
ATOM   3845  C CB    . ARG A 1 2107 ? 189.194 205.819 192.005 1.00 81.02  ? 2107 ARG A CB    1 
ATOM   3846  C CG    . ARG A 1 2107 ? 188.763 206.153 193.417 1.00 81.02  ? 2107 ARG A CG    1 
ATOM   3847  C CD    . ARG A 1 2107 ? 188.708 204.908 194.279 1.00 81.02  ? 2107 ARG A CD    1 
ATOM   3848  N NE    . ARG A 1 2107 ? 187.507 204.121 194.032 1.00 81.02  ? 2107 ARG A NE    1 
ATOM   3849  C CZ    . ARG A 1 2107 ? 186.921 203.351 194.938 1.00 81.02  ? 2107 ARG A CZ    1 
ATOM   3850  N NH1   . ARG A 1 2107 ? 187.403 203.237 196.164 1.00 81.02  ? 2107 ARG A NH1   1 
ATOM   3851  N NH2   . ARG A 1 2107 ? 185.823 202.679 194.605 1.00 81.02  ? 2107 ARG A NH2   1 
ATOM   3852  N N     . ILE A 1 2108 ? 191.566 207.498 190.643 1.00 88.93  ? 2108 ILE A N     1 
ATOM   3853  C CA    . ILE A 1 2108 ? 192.782 208.297 190.730 1.00 88.93  ? 2108 ILE A CA    1 
ATOM   3854  C C     . ILE A 1 2108 ? 192.527 209.697 190.194 1.00 88.93  ? 2108 ILE A C     1 
ATOM   3855  O O     . ILE A 1 2108 ? 192.925 210.695 190.805 1.00 88.93  ? 2108 ILE A O     1 
ATOM   3856  C CB    . ILE A 1 2108 ? 193.929 207.601 189.975 1.00 88.93  ? 2108 ILE A CB    1 
ATOM   3857  C CG1   . ILE A 1 2108 ? 194.546 206.501 190.838 1.00 88.93  ? 2108 ILE A CG1   1 
ATOM   3858  C CG2   . ILE A 1 2108 ? 194.988 208.606 189.556 1.00 88.93  ? 2108 ILE A CG2   1 
ATOM   3859  C CD1   . ILE A 1 2108 ? 195.144 207.005 192.128 1.00 88.93  ? 2108 ILE A CD1   1 
ATOM   3860  N N     . GLN A 1 2109 ? 191.850 209.790 189.049 1.00 93.34  ? 2109 GLN A N     1 
ATOM   3861  C CA    . GLN A 1 2109 ? 191.529 211.096 188.486 1.00 93.34  ? 2109 GLN A CA    1 
ATOM   3862  C C     . GLN A 1 2109 ? 190.646 211.897 189.430 1.00 93.34  ? 2109 GLN A C     1 
ATOM   3863  O O     . GLN A 1 2109 ? 190.857 213.100 189.622 1.00 93.34  ? 2109 GLN A O     1 
ATOM   3864  C CB    . GLN A 1 2109 ? 190.844 210.933 187.131 1.00 93.34  ? 2109 GLN A CB    1 
ATOM   3865  C CG    . GLN A 1 2109 ? 191.739 210.364 186.053 1.00 93.34  ? 2109 GLN A CG    1 
ATOM   3866  C CD    . GLN A 1 2109 ? 193.088 211.044 186.005 1.00 93.34  ? 2109 GLN A CD    1 
ATOM   3867  O OE1   . GLN A 1 2109 ? 193.177 212.270 185.975 1.00 93.34  ? 2109 GLN A OE1   1 
ATOM   3868  N NE2   . GLN A 1 2109 ? 194.150 210.249 186.005 1.00 93.34  ? 2109 GLN A NE2   1 
ATOM   3869  N N     . LYS A 1 2110 ? 189.650 211.245 190.029 1.00 93.81  ? 2110 LYS A N     1 
ATOM   3870  C CA    . LYS A 1 2110 ? 188.745 211.950 190.928 1.00 93.81  ? 2110 LYS A CA    1 
ATOM   3871  C C     . LYS A 1 2110 ? 189.477 212.482 192.153 1.00 93.81  ? 2110 LYS A C     1 
ATOM   3872  O O     . LYS A 1 2110 ? 189.285 213.639 192.544 1.00 93.81  ? 2110 LYS A O     1 
ATOM   3873  C CB    . LYS A 1 2110 ? 187.605 211.027 191.349 1.00 93.81  ? 2110 LYS A CB    1 
ATOM   3874  C CG    . LYS A 1 2110 ? 186.445 211.746 191.999 1.00 93.81  ? 2110 LYS A CG    1 
ATOM   3875  C CD    . LYS A 1 2110 ? 185.308 210.788 192.274 1.00 93.81  ? 2110 LYS A CD    1 
ATOM   3876  C CE    . LYS A 1 2110 ? 184.789 210.181 190.983 1.00 93.81  ? 2110 LYS A CE    1 
ATOM   3877  N NZ    . LYS A 1 2110 ? 184.702 211.186 189.888 1.00 93.81  ? 2110 LYS A NZ    1 
ATOM   3878  N N     . ILE A 1 2111 ? 190.322 211.656 192.769 1.00 93.48  ? 2111 ILE A N     1 
ATOM   3879  C CA    . ILE A 1 2111 ? 191.033 212.094 193.966 1.00 93.48  ? 2111 ILE A CA    1 
ATOM   3880  C C     . ILE A 1 2111 ? 192.047 213.175 193.617 1.00 93.48  ? 2111 ILE A C     1 
ATOM   3881  O O     . ILE A 1 2111 ? 192.255 214.121 194.386 1.00 93.48  ? 2111 ILE A O     1 
ATOM   3882  C CB    . ILE A 1 2111 ? 191.693 210.893 194.665 1.00 93.48  ? 2111 ILE A CB    1 
ATOM   3883  C CG1   . ILE A 1 2111 ? 190.626 209.913 195.152 1.00 93.48  ? 2111 ILE A CG1   1 
ATOM   3884  C CG2   . ILE A 1 2111 ? 192.537 211.354 195.839 1.00 93.48  ? 2111 ILE A CG2   1 
ATOM   3885  C CD1   . ILE A 1 2111 ? 189.676 210.502 196.168 1.00 93.48  ? 2111 ILE A CD1   1 
ATOM   3886  N N     . LYS A 1 2112 ? 192.688 213.058 192.453 1.00 104.15 ? 2112 LYS A N     1 
ATOM   3887  C CA    . LYS A 1 2112 ? 193.640 214.078 192.026 1.00 104.15 ? 2112 LYS A CA    1 
ATOM   3888  C C     . LYS A 1 2112 ? 192.956 215.425 191.851 1.00 104.15 ? 2112 LYS A C     1 
ATOM   3889  O O     . LYS A 1 2112 ? 193.512 216.466 192.219 1.00 104.15 ? 2112 LYS A O     1 
ATOM   3890  C CB    . LYS A 1 2112 ? 194.320 213.648 190.726 1.00 104.15 ? 2112 LYS A CB    1 
ATOM   3891  C CG    . LYS A 1 2112 ? 195.423 214.582 190.256 1.00 104.15 ? 2112 LYS A CG    1 
ATOM   3892  C CD    . LYS A 1 2112 ? 196.471 213.835 189.444 1.00 104.15 ? 2112 LYS A CD    1 
ATOM   3893  C CE    . LYS A 1 2112 ? 197.706 213.530 190.279 1.00 104.15 ? 2112 LYS A CE    1 
ATOM   3894  N NZ    . LYS A 1 2112 ? 198.562 212.482 189.656 1.00 104.15 ? 2112 LYS A NZ    1 
ATOM   3895  N N     . ARG A 1 2113 ? 191.748 215.426 191.297 1.00 103.04 ? 2113 ARG A N     1 
ATOM   3896  C CA    . ARG A 1 2113 ? 190.980 216.658 191.129 1.00 103.04 ? 2113 ARG A CA    1 
ATOM   3897  C C     . ARG A 1 2113 ? 190.278 217.013 192.441 1.00 103.04 ? 2113 ARG A C     1 
ATOM   3898  O O     . ARG A 1 2113 ? 189.069 216.872 192.608 1.00 103.04 ? 2113 ARG A O     1 
ATOM   3899  C CB    . ARG A 1 2113 ? 189.995 216.506 189.975 1.00 103.04 ? 2113 ARG A CB    1 
ATOM   3900  C CG    . ARG A 1 2113 ? 189.154 217.737 189.685 1.00 103.04 ? 2113 ARG A CG    1 
ATOM   3901  C CD    . ARG A 1 2113 ? 187.779 217.350 189.163 1.00 103.04 ? 2113 ARG A CD    1 
ATOM   3902  N NE    . ARG A 1 2113 ? 187.082 216.424 190.048 1.00 103.04 ? 2113 ARG A NE    1 
ATOM   3903  C CZ    . ARG A 1 2113 ? 186.532 216.760 191.207 1.00 103.04 ? 2113 ARG A CZ    1 
ATOM   3904  N NH1   . ARG A 1 2113 ? 186.573 218.003 191.658 1.00 103.04 ? 2113 ARG A NH1   1 
ATOM   3905  N NH2   . ARG A 1 2113 ? 185.929 215.824 191.934 1.00 103.04 ? 2113 ARG A NH2   1 
ATOM   3906  N N     . GLU A 1 2114 ? 191.086 217.465 193.395 1.00 103.53 ? 2114 GLU A N     1 
ATOM   3907  C CA    . GLU A 1 2114 ? 190.596 217.809 194.724 1.00 103.53 ? 2114 GLU A CA    1 
ATOM   3908  C C     . GLU A 1 2114 ? 191.662 218.571 195.503 1.00 103.53 ? 2114 GLU A C     1 
ATOM   3909  O O     . GLU A 1 2114 ? 191.357 219.479 196.275 0.00 103.53 ? 2114 GLU A O     1 
ATOM   3910  C CB    . GLU A 1 2114 ? 190.179 216.548 195.487 1.00 103.53 ? 2114 GLU A CB    1 
ATOM   3911  C CG    . GLU A 1 2114 ? 189.381 216.810 196.752 1.00 103.53 ? 2114 GLU A CG    1 
ATOM   3912  C CD    . GLU A 1 2114 ? 190.263 216.974 197.973 1.00 103.53 ? 2114 GLU A CD    1 
ATOM   3913  O OE1   . GLU A 1 2114 ? 191.431 216.535 197.926 1.00 103.53 ? 2114 GLU A OE1   1 
ATOM   3914  O OE2   . GLU A 1 2114 ? 189.790 217.541 198.980 1.00 103.53 ? 2114 GLU A OE2   1 
ATOM   3915  N N     . ILE A 1 2127 ? 202.528 208.620 195.381 1.00 88.83  ? 2127 ILE A N     1 
ATOM   3916  C CA    . ILE A 1 2127 ? 201.443 209.584 195.267 1.00 88.83  ? 2127 ILE A CA    1 
ATOM   3917  C C     . ILE A 1 2127 ? 200.142 208.869 194.923 1.00 88.83  ? 2127 ILE A C     1 
ATOM   3918  O O     . ILE A 1 2127 ? 200.034 208.228 193.877 1.00 88.83  ? 2127 ILE A O     1 
ATOM   3919  C CB    . ILE A 1 2127 ? 201.771 210.669 194.223 1.00 88.83  ? 2127 ILE A CB    1 
ATOM   3920  C CG1   . ILE A 1 2127 ? 200.505 211.423 193.812 1.00 88.83  ? 2127 ILE A CG1   1 
ATOM   3921  C CG2   . ILE A 1 2127 ? 202.454 210.059 193.008 1.00 88.83  ? 2127 ILE A CG2   1 
ATOM   3922  C CD1   . ILE A 1 2127 ? 200.780 212.727 193.093 1.00 88.83  ? 2127 ILE A CD1   1 
ATOM   3923  N N     . ALA A 1 2128 ? 199.160 208.980 195.819 1.00 86.15  ? 2128 ALA A N     1 
ATOM   3924  C CA    . ALA A 1 2128 ? 197.847 208.363 195.633 1.00 86.15  ? 2128 ALA A CA    1 
ATOM   3925  C C     . ALA A 1 2128 ? 197.967 206.863 195.375 1.00 86.15  ? 2128 ALA A C     1 
ATOM   3926  O O     . ALA A 1 2128 ? 197.284 206.304 194.515 1.00 86.15  ? 2128 ALA A O     1 
ATOM   3927  C CB    . ALA A 1 2128 ? 197.067 209.050 194.510 1.00 86.15  ? 2128 ALA A CB    1 
ATOM   3928  N N     . GLU A 1 2129 ? 198.857 206.207 196.117 1.00 91.68  ? 2129 GLU A N     1 
ATOM   3929  C CA    . GLU A 1 2129 ? 199.042 204.766 196.030 1.00 91.68  ? 2129 GLU A CA    1 
ATOM   3930  C C     . GLU A 1 2129 ? 198.357 204.010 197.160 1.00 91.68  ? 2129 GLU A C     1 
ATOM   3931  O O     . GLU A 1 2129 ? 198.366 202.776 197.157 1.00 91.68  ? 2129 GLU A O     1 
ATOM   3932  C CB    . GLU A 1 2129 ? 200.537 204.431 196.015 1.00 91.68  ? 2129 GLU A CB    1 
ATOM   3933  C CG    . GLU A 1 2129 ? 201.126 204.141 197.386 1.00 91.68  ? 2129 GLU A CG    1 
ATOM   3934  C CD    . GLU A 1 2129 ? 202.457 203.422 197.307 1.00 91.68  ? 2129 GLU A CD    1 
ATOM   3935  O OE1   . GLU A 1 2129 ? 202.614 202.558 196.420 1.00 91.68  ? 2129 GLU A OE1   1 
ATOM   3936  O OE2   . GLU A 1 2129 ? 203.345 203.716 198.132 1.00 91.68  ? 2129 GLU A OE2   1 
ATOM   3937  N N     . ASN A 1 2130 ? 197.749 204.715 198.111 1.00 96.99  ? 2130 ASN A N     1 
ATOM   3938  C CA    . ASN A 1 2130 ? 197.148 204.099 199.284 1.00 96.99  ? 2130 ASN A CA    1 
ATOM   3939  C C     . ASN A 1 2130 ? 195.724 203.616 199.038 1.00 96.99  ? 2130 ASN A C     1 
ATOM   3940  O O     . ASN A 1 2130 ? 194.988 203.372 200.002 1.00 96.99  ? 2130 ASN A O     1 
ATOM   3941  C CB    . ASN A 1 2130 ? 197.166 205.084 200.453 1.00 96.99  ? 2130 ASN A CB    1 
ATOM   3942  C CG    . ASN A 1 2130 ? 196.866 206.503 200.018 1.00 96.99  ? 2130 ASN A CG    1 
ATOM   3943  O OD1   . ASN A 1 2130 ? 195.794 206.786 199.483 1.00 96.99  ? 2130 ASN A OD1   1 
ATOM   3944  N ND2   . ASN A 1 2130 ? 197.816 207.404 200.241 1.00 96.99  ? 2130 ASN A ND2   1 
ATOM   3945  N N     . LEU A 1 2131 ? 195.318 203.477 197.781 1.00 91.72  ? 2131 LEU A N     1 
ATOM   3946  C CA    . LEU A 1 2131 ? 193.958 203.064 197.487 1.00 91.72  ? 2131 LEU A CA    1 
ATOM   3947  C C     . LEU A 1 2131 ? 193.731 201.611 197.900 1.00 91.72  ? 2131 LEU A C     1 
ATOM   3948  O O     . LEU A 1 2131 ? 194.609 200.761 197.731 1.00 91.72  ? 2131 LEU A O     1 
ATOM   3949  C CB    . LEU A 1 2131 ? 193.658 203.234 196.002 1.00 91.72  ? 2131 LEU A CB    1 
ATOM   3950  C CG    . LEU A 1 2131 ? 193.608 204.679 195.510 1.00 91.72  ? 2131 LEU A CG    1 
ATOM   3951  C CD1   . LEU A 1 2131 ? 192.802 204.780 194.232 1.00 91.72  ? 2131 LEU A CD1   1 
ATOM   3952  C CD2   . LEU A 1 2131 ? 193.026 205.587 196.576 1.00 91.72  ? 2131 LEU A CD2   1 
ATOM   3953  N N     . PRO A 1 2132 ? 192.563 201.302 198.449 1.00 88.49  ? 2132 PRO A N     1 
ATOM   3954  C CA    . PRO A 1 2132 ? 192.252 199.910 198.795 1.00 88.49  ? 2132 PRO A CA    1 
ATOM   3955  C C     . PRO A 1 2132 ? 191.905 199.092 197.565 1.00 88.49  ? 2132 PRO A C     1 
ATOM   3956  O O     . PRO A 1 2132 ? 190.726 198.912 197.245 1.00 88.49  ? 2132 PRO A O     1 
ATOM   3957  C CB    . PRO A 1 2132 ? 191.054 200.044 199.740 1.00 88.49  ? 2132 PRO A CB    1 
ATOM   3958  C CG    . PRO A 1 2132 ? 190.414 201.327 199.349 1.00 88.49  ? 2132 PRO A CG    1 
ATOM   3959  C CD    . PRO A 1 2132 ? 191.495 202.234 198.845 1.00 88.49  ? 2132 PRO A CD    1 
ATOM   3960  N N     . GLU A 1 2133 ? 192.928 198.584 196.874 1.00 86.45  ? 2133 GLU A N     1 
ATOM   3961  C CA    . GLU A 1 2133 ? 192.712 198.001 195.554 1.00 86.45  ? 2133 GLU A CA    1 
ATOM   3962  C C     . GLU A 1 2133 ? 191.808 196.779 195.615 1.00 86.45  ? 2133 GLU A C     1 
ATOM   3963  O O     . GLU A 1 2133 ? 191.151 196.438 194.625 1.00 86.45  ? 2133 GLU A O     1 
ATOM   3964  C CB    . GLU A 1 2133 ? 194.048 197.642 194.916 1.00 86.45  ? 2133 GLU A CB    1 
ATOM   3965  C CG    . GLU A 1 2133 ? 195.210 198.413 195.479 1.00 86.45  ? 2133 GLU A CG    1 
ATOM   3966  C CD    . GLU A 1 2133 ? 196.525 197.940 194.917 1.00 86.45  ? 2133 GLU A CD    1 
ATOM   3967  O OE1   . GLU A 1 2133 ? 197.517 198.683 195.035 1.00 86.45  ? 2133 GLU A OE1   1 
ATOM   3968  O OE2   . GLU A 1 2133 ? 196.555 196.847 194.318 1.00 86.45  ? 2133 GLU A OE2   1 
ATOM   3969  N N     . GLN A 1 2134 ? 191.764 196.099 196.761 1.00 78.30  ? 2134 GLN A N     1 
ATOM   3970  C CA    . GLN A 1 2134 ? 190.815 195.003 196.905 1.00 78.30  ? 2134 GLN A CA    1 
ATOM   3971  C C     . GLN A 1 2134 ? 189.388 195.506 196.754 1.00 78.30  ? 2134 GLN A C     1 
ATOM   3972  O O     . GLN A 1 2134 ? 188.566 194.874 196.082 1.00 78.30  ? 2134 GLN A O     1 
ATOM   3973  C CB    . GLN A 1 2134 ? 191.002 194.312 198.253 1.00 78.30  ? 2134 GLN A CB    1 
ATOM   3974  C CG    . GLN A 1 2134 ? 192.396 193.773 198.481 1.00 78.30  ? 2134 GLN A CG    1 
ATOM   3975  C CD    . GLN A 1 2134 ? 192.425 192.687 199.531 1.00 78.30  ? 2134 GLN A CD    1 
ATOM   3976  O OE1   . GLN A 1 2134 ? 191.383 192.240 200.007 1.00 78.30  ? 2134 GLN A OE1   1 
ATOM   3977  N NE2   . GLN A 1 2134 ? 193.624 192.255 199.903 1.00 78.30  ? 2134 GLN A NE2   1 
ATOM   3978  N N     . GLU A 1 2135 ? 189.080 196.654 197.359 1.00 82.12  ? 2135 GLU A N     1 
ATOM   3979  C CA    . GLU A 1 2135 ? 187.755 197.234 197.189 1.00 82.12  ? 2135 GLU A CA    1 
ATOM   3980  C C     . GLU A 1 2135 ? 187.506 197.601 195.735 1.00 82.12  ? 2135 GLU A C     1 
ATOM   3981  O O     . GLU A 1 2135 ? 186.392 197.439 195.232 1.00 82.12  ? 2135 GLU A O     1 
ATOM   3982  C CB    . GLU A 1 2135 ? 187.588 198.460 198.083 1.00 82.12  ? 2135 GLU A CB    1 
ATOM   3983  C CG    . GLU A 1 2135 ? 186.314 199.237 197.801 1.00 82.12  ? 2135 GLU A CG    1 
ATOM   3984  C CD    . GLU A 1 2135 ? 186.412 200.690 198.203 1.00 82.12  ? 2135 GLU A CD    1 
ATOM   3985  O OE1   . GLU A 1 2135 ? 187.316 201.026 198.992 1.00 82.12  ? 2135 GLU A OE1   1 
ATOM   3986  O OE2   . GLU A 1 2135 ? 185.586 201.498 197.730 1.00 82.12  ? 2135 GLU A OE2   1 
ATOM   3987  N N     . ILE A 1 2136 ? 188.531 198.097 195.043 1.00 76.10  ? 2136 ILE A N     1 
ATOM   3988  C CA    . ILE A 1 2136 ? 188.369 198.449 193.636 1.00 76.10  ? 2136 ILE A CA    1 
ATOM   3989  C C     . ILE A 1 2136 ? 188.024 197.216 192.816 1.00 76.10  ? 2136 ILE A C     1 
ATOM   3990  O O     . ILE A 1 2136 ? 187.112 197.241 191.980 1.00 76.10  ? 2136 ILE A O     1 
ATOM   3991  C CB    . ILE A 1 2136 ? 189.637 199.139 193.107 1.00 76.10  ? 2136 ILE A CB    1 
ATOM   3992  C CG1   . ILE A 1 2136 ? 189.828 200.494 193.782 1.00 76.10  ? 2136 ILE A CG1   1 
ATOM   3993  C CG2   . ILE A 1 2136 ? 189.559 199.310 191.612 1.00 76.10  ? 2136 ILE A CG2   1 
ATOM   3994  C CD1   . ILE A 1 2136 ? 191.268 200.924 193.867 1.00 76.10  ? 2136 ILE A CD1   1 
ATOM   3995  N N     . LEU A 1 2137 ? 188.744 196.118 193.041 1.00 74.25  ? 2137 LEU A N     1 
ATOM   3996  C CA    . LEU A 1 2137 ? 188.474 194.899 192.288 1.00 74.25  ? 2137 LEU A CA    1 
ATOM   3997  C C     . LEU A 1 2137 ? 187.093 194.345 192.614 1.00 74.25  ? 2137 LEU A C     1 
ATOM   3998  O O     . LEU A 1 2137 ? 186.381 193.869 191.721 1.00 74.25  ? 2137 LEU A O     1 
ATOM   3999  C CB    . LEU A 1 2137 ? 189.560 193.862 192.564 1.00 74.25  ? 2137 LEU A CB    1 
ATOM   4000  C CG    . LEU A 1 2137 ? 189.607 192.668 191.612 1.00 74.25  ? 2137 LEU A CG    1 
ATOM   4001  C CD1   . LEU A 1 2137 ? 189.197 193.074 190.215 1.00 74.25  ? 2137 LEU A CD1   1 
ATOM   4002  C CD2   . LEU A 1 2137 ? 190.994 192.066 191.588 1.00 74.25  ? 2137 LEU A CD2   1 
ATOM   4003  N N     . ILE A 1 2138 ? 186.693 194.401 193.886 1.00 73.16  ? 2138 ILE A N     1 
ATOM   4004  C CA    . ILE A 1 2138 ? 185.353 193.953 194.252 1.00 73.16  ? 2138 ILE A CA    1 
ATOM   4005  C C     . ILE A 1 2138 ? 184.300 194.813 193.573 1.00 73.16  ? 2138 ILE A C     1 
ATOM   4006  O O     . ILE A 1 2138 ? 183.285 194.305 193.086 1.00 73.16  ? 2138 ILE A O     1 
ATOM   4007  C CB    . ILE A 1 2138 ? 185.180 193.958 195.779 1.00 73.16  ? 2138 ILE A CB    1 
ATOM   4008  C CG1   . ILE A 1 2138 ? 186.115 192.938 196.414 1.00 73.16  ? 2138 ILE A CG1   1 
ATOM   4009  C CG2   . ILE A 1 2138 ? 183.746 193.653 196.146 1.00 73.16  ? 2138 ILE A CG2   1 
ATOM   4010  C CD1   . ILE A 1 2138 ? 186.188 191.646 195.654 1.00 73.16  ? 2138 ILE A CD1   1 
ATOM   4011  N N     . GLN A 1 2139 ? 184.516 196.126 193.539 1.00 78.06  ? 2139 GLN A N     1 
ATOM   4012  C CA    . GLN A 1 2139 ? 183.572 197.015 192.878 1.00 78.06  ? 2139 GLN A CA    1 
ATOM   4013  C C     . GLN A 1 2139 ? 183.459 196.687 191.400 1.00 78.06  ? 2139 GLN A C     1 
ATOM   4014  O O     . GLN A 1 2139 ? 182.355 196.637 190.852 1.00 78.06  ? 2139 GLN A O     1 
ATOM   4015  C CB    . GLN A 1 2139 ? 183.998 198.467 193.074 1.00 78.06  ? 2139 GLN A CB    1 
ATOM   4016  C CG    . GLN A 1 2139 ? 183.286 199.441 192.169 1.00 78.06  ? 2139 GLN A CG    1 
ATOM   4017  C CD    . GLN A 1 2139 ? 183.663 200.871 192.459 1.00 78.06  ? 2139 GLN A CD    1 
ATOM   4018  O OE1   . GLN A 1 2139 ? 184.087 201.200 193.566 1.00 78.06  ? 2139 GLN A OE1   1 
ATOM   4019  N NE2   . GLN A 1 2139 ? 183.507 201.737 191.467 1.00 78.06  ? 2139 GLN A NE2   1 
ATOM   4020  N N     . SER A 1 2140 ? 184.588 196.440 190.742 1.00 73.77  ? 2140 SER A N     1 
ATOM   4021  C CA    . SER A 1 2140 ? 184.543 196.102 189.326 1.00 73.77  ? 2140 SER A CA    1 
ATOM   4022  C C     . SER A 1 2140 ? 183.790 194.800 189.097 1.00 73.77  ? 2140 SER A C     1 
ATOM   4023  O O     . SER A 1 2140 ? 182.913 194.718 188.227 1.00 73.77  ? 2140 SER A O     1 
ATOM   4024  C CB    . SER A 1 2140 ? 185.957 196.002 188.768 1.00 73.77  ? 2140 SER A CB    1 
ATOM   4025  O OG    . SER A 1 2140 ? 185.926 195.825 187.366 1.00 73.77  ? 2140 SER A OG    1 
ATOM   4026  N N     . VAL A 1 2141 ? 184.109 193.771 189.884 1.00 76.47  ? 2141 VAL A N     1 
ATOM   4027  C CA    . VAL A 1 2141 ? 183.504 192.465 189.649 1.00 76.47  ? 2141 VAL A CA    1 
ATOM   4028  C C     . VAL A 1 2141 ? 182.014 192.498 189.960 1.00 76.47  ? 2141 VAL A C     1 
ATOM   4029  O O     . VAL A 1 2141 ? 181.214 191.869 189.261 1.00 76.47  ? 2141 VAL A O     1 
ATOM   4030  C CB    . VAL A 1 2141 ? 184.237 191.365 190.439 1.00 76.47  ? 2141 VAL A CB    1 
ATOM   4031  C CG1   . VAL A 1 2141 ? 183.906 191.429 191.910 1.00 76.47  ? 2141 VAL A CG1   1 
ATOM   4032  C CG2   . VAL A 1 2141 ? 183.875 190.004 189.882 1.00 76.47  ? 2141 VAL A CG2   1 
ATOM   4033  N N     . CYS A 1 2142 ? 181.605 193.247 190.986 1.00 79.50  ? 2142 CYS A N     1 
ATOM   4034  C CA    . CYS A 1 2142 ? 180.181 193.334 191.281 1.00 79.50  ? 2142 CYS A CA    1 
ATOM   4035  C C     . CYS A 1 2142 ? 179.457 194.151 190.221 1.00 79.50  ? 2142 CYS A C     1 
ATOM   4036  O O     . CYS A 1 2142 ? 178.405 193.734 189.730 1.00 79.50  ? 2142 CYS A O     1 
ATOM   4037  C CB    . CYS A 1 2142 ? 179.956 193.923 192.671 1.00 79.50  ? 2142 CYS A CB    1 
ATOM   4038  S SG    . CYS A 1 2142 ? 180.118 195.709 192.774 1.00 79.50  ? 2142 CYS A SG    1 
ATOM   4039  N N     . GLU A 1 2143 ? 180.031 195.287 189.822 1.00 78.23  ? 2143 GLU A N     1 
ATOM   4040  C CA    . GLU A 1 2143 ? 179.421 196.122 188.796 1.00 78.23  ? 2143 GLU A CA    1 
ATOM   4041  C C     . GLU A 1 2143 ? 179.271 195.378 187.478 1.00 78.23  ? 2143 GLU A C     1 
ATOM   4042  O O     . GLU A 1 2143 ? 178.358 195.675 186.702 1.00 78.23  ? 2143 GLU A O     1 
ATOM   4043  C CB    . GLU A 1 2143 ? 180.264 197.380 188.600 1.00 78.23  ? 2143 GLU A CB    1 
ATOM   4044  C CG    . GLU A 1 2143 ? 179.478 198.655 188.393 1.00 78.23  ? 2143 GLU A CG    1 
ATOM   4045  C CD    . GLU A 1 2143 ? 180.343 199.892 188.552 1.00 78.23  ? 2143 GLU A CD    1 
ATOM   4046  O OE1   . GLU A 1 2143 ? 181.418 199.950 187.921 1.00 78.23  ? 2143 GLU A OE1   1 
ATOM   4047  O OE2   . GLU A 1 2143 ? 179.952 200.805 189.310 1.00 78.23  ? 2143 GLU A OE2   1 
ATOM   4048  N N     . THR A 1 2144 ? 180.157 194.424 187.197 1.00 76.40  ? 2144 THR A N     1 
ATOM   4049  C CA    . THR A 1 2144 ? 180.066 193.674 185.950 1.00 76.40  ? 2144 THR A CA    1 
ATOM   4050  C C     . THR A 1 2144 ? 179.239 192.399 186.053 1.00 76.40  ? 2144 THR A C     1 
ATOM   4051  O O     . THR A 1 2144 ? 178.637 191.991 185.056 1.00 76.40  ? 2144 THR A O     1 
ATOM   4052  C CB    . THR A 1 2144 ? 181.464 193.320 185.442 1.00 76.40  ? 2144 THR A CB    1 
ATOM   4053  O OG1   . THR A 1 2144 ? 182.344 194.425 185.669 1.00 76.40  ? 2144 THR A OG1   1 
ATOM   4054  C CG2   . THR A 1 2144 ? 181.424 193.023 183.956 1.00 76.40  ? 2144 THR A CG2   1 
ATOM   4055  N N     . MET A 1 2145 ? 179.191 191.752 187.218 1.00 80.22  ? 2145 MET A N     1 
ATOM   4056  C CA    . MET A 1 2145 ? 178.419 190.527 187.388 1.00 80.22  ? 2145 MET A CA    1 
ATOM   4057  C C     . MET A 1 2145 ? 176.998 190.789 187.873 1.00 80.22  ? 2145 MET A C     1 
ATOM   4058  O O     . MET A 1 2145 ? 176.038 190.443 187.182 1.00 80.22  ? 2145 MET A O     1 
ATOM   4059  C CB    . MET A 1 2145 ? 179.123 189.589 188.373 1.00 80.22  ? 2145 MET A CB    1 
ATOM   4060  C CG    . MET A 1 2145 ? 180.340 188.783 187.888 1.00 80.22  ? 2145 MET A CG    1 
ATOM   4061  S SD    . MET A 1 2145 ? 180.457 188.222 186.169 1.00 80.22  ? 2145 MET A SD    1 
ATOM   4062  C CE    . MET A 1 2145 ? 180.966 189.685 185.274 1.00 80.22  ? 2145 MET A CE    1 
ATOM   4063  N N     . VAL A 1 2146 ? 176.858 191.411 189.040 1.00 79.45  ? 2146 VAL A N     1 
ATOM   4064  C CA    . VAL A 1 2146 ? 175.598 191.524 189.773 1.00 79.45  ? 2146 VAL A CA    1 
ATOM   4065  C C     . VAL A 1 2146 ? 174.414 191.826 188.857 1.00 79.45  ? 2146 VAL A C     1 
ATOM   4066  O O     . VAL A 1 2146 ? 173.345 191.225 189.039 1.00 79.45  ? 2146 VAL A O     1 
ATOM   4067  C CB    . VAL A 1 2146 ? 175.727 192.577 190.886 1.00 79.45  ? 2146 VAL A CB    1 
ATOM   4068  C CG1   . VAL A 1 2146 ? 174.373 193.154 191.254 1.00 79.45  ? 2146 VAL A CG1   1 
ATOM   4069  C CG2   . VAL A 1 2146 ? 176.400 191.969 192.102 1.00 79.45  ? 2146 VAL A CG2   1 
ATOM   4070  N N     . PRO A 1 2147 ? 174.535 192.710 187.861 1.00 82.54  ? 2147 PRO A N     1 
ATOM   4071  C CA    . PRO A 1 2147 ? 173.419 192.868 186.917 1.00 82.54  ? 2147 PRO A CA    1 
ATOM   4072  C C     . PRO A 1 2147 ? 173.046 191.595 186.179 1.00 82.54  ? 2147 PRO A C     1 
ATOM   4073  O O     . PRO A 1 2147 ? 171.892 191.461 185.757 1.00 82.54  ? 2147 PRO A O     1 
ATOM   4074  C CB    . PRO A 1 2147 ? 173.932 193.944 185.957 1.00 82.54  ? 2147 PRO A CB    1 
ATOM   4075  C CG    . PRO A 1 2147 ? 174.821 194.759 186.786 1.00 82.54  ? 2147 PRO A CG    1 
ATOM   4076  C CD    . PRO A 1 2147 ? 175.525 193.787 187.685 1.00 82.54  ? 2147 PRO A CD    1 
ATOM   4077  N N     . LYS A 1 2148 ? 173.972 190.654 186.001 1.00 80.40  ? 2148 LYS A N     1 
ATOM   4078  C CA    . LYS A 1 2148 ? 173.684 189.443 185.245 1.00 80.40  ? 2148 LYS A CA    1 
ATOM   4079  C C     . LYS A 1 2148 ? 173.406 188.238 186.137 1.00 80.40  ? 2148 LYS A C     1 
ATOM   4080  O O     . LYS A 1 2148 ? 173.447 187.101 185.659 1.00 80.40  ? 2148 LYS A O     1 
ATOM   4081  C CB    . LYS A 1 2148 ? 174.822 189.133 184.270 1.00 80.40  ? 2148 LYS A CB    1 
ATOM   4082  C CG    . LYS A 1 2148 ? 176.077 188.524 184.846 1.00 80.40  ? 2148 LYS A CG    1 
ATOM   4083  C CD    . LYS A 1 2148 ? 177.131 188.406 183.760 1.00 80.40  ? 2148 LYS A CD    1 
ATOM   4084  C CE    . LYS A 1 2148 ? 177.386 189.750 183.097 1.00 80.40  ? 2148 LYS A CE    1 
ATOM   4085  N NZ    . LYS A 1 2148 ? 178.397 189.654 182.012 1.00 80.40  ? 2148 LYS A NZ    1 
ATOM   4086  N N     . LEU A 1 2149 ? 173.100 188.459 187.410 1.00 80.02  ? 2149 LEU A N     1 
ATOM   4087  C CA    . LEU A 1 2149 ? 172.834 187.377 188.348 1.00 80.02  ? 2149 LEU A CA    1 
ATOM   4088  C C     . LEU A 1 2149 ? 171.348 187.318 188.667 1.00 80.02  ? 2149 LEU A C     1 
ATOM   4089  O O     . LEU A 1 2149 ? 170.721 188.350 188.921 1.00 80.02  ? 2149 LEU A O     1 
ATOM   4090  C CB    . LEU A 1 2149 ? 173.637 187.551 189.638 1.00 80.02  ? 2149 LEU A CB    1 
ATOM   4091  C CG    . LEU A 1 2149 ? 175.052 186.974 189.661 1.00 80.02  ? 2149 LEU A CG    1 
ATOM   4092  C CD1   . LEU A 1 2149 ? 174.993 185.481 189.447 1.00 80.02  ? 2149 LEU A CD1   1 
ATOM   4093  C CD2   . LEU A 1 2149 ? 175.951 187.616 188.634 1.00 80.02  ? 2149 LEU A CD2   1 
ATOM   4094  N N     . VAL A 1 2150 ? 170.792 186.107 188.653 1.00 81.00  ? 2150 VAL A N     1 
ATOM   4095  C CA    . VAL A 1 2150 ? 169.407 185.912 189.052 1.00 81.00  ? 2150 VAL A CA    1 
ATOM   4096  C C     . VAL A 1 2150 ? 169.286 186.139 190.555 1.00 81.00  ? 2150 VAL A C     1 
ATOM   4097  O O     . VAL A 1 2150 ? 170.269 186.038 191.301 1.00 81.00  ? 2150 VAL A O     1 
ATOM   4098  C CB    . VAL A 1 2150 ? 168.935 184.505 188.642 1.00 81.00  ? 2150 VAL A CB    1 
ATOM   4099  C CG1   . VAL A 1 2150 ? 167.452 184.320 188.904 1.00 81.00  ? 2150 VAL A CG1   1 
ATOM   4100  C CG2   . VAL A 1 2150 ? 169.256 184.254 187.182 1.00 81.00  ? 2150 VAL A CG2   1 
ATOM   4101  N N     . ALA A 1 2151 ? 168.067 186.450 191.007 1.00 83.00  ? 2151 ALA A N     1 
ATOM   4102  C CA    . ALA A 1 2151 ? 167.862 186.937 192.369 1.00 83.00  ? 2151 ALA A CA    1 
ATOM   4103  C C     . ALA A 1 2151 ? 168.392 185.970 193.419 1.00 83.00  ? 2151 ALA A C     1 
ATOM   4104  O O     . ALA A 1 2151 ? 168.922 186.396 194.451 1.00 83.00  ? 2151 ALA A O     1 
ATOM   4105  C CB    . ALA A 1 2151 ? 166.378 187.209 192.607 1.00 83.00  ? 2151 ALA A CB    1 
ATOM   4106  N N     . GLU A 1 2152 ? 168.254 184.666 193.183 1.00 83.70  ? 2152 GLU A N     1 
ATOM   4107  C CA    . GLU A 1 2152 ? 168.708 183.705 194.182 1.00 83.70  ? 2152 GLU A CA    1 
ATOM   4108  C C     . GLU A 1 2152 ? 170.226 183.676 194.290 1.00 83.70  ? 2152 GLU A C     1 
ATOM   4109  O O     . GLU A 1 2152 ? 170.762 183.322 195.345 1.00 83.70  ? 2152 GLU A O     1 
ATOM   4110  C CB    . GLU A 1 2152 ? 168.178 182.310 193.858 1.00 83.70  ? 2152 GLU A CB    1 
ATOM   4111  C CG    . GLU A 1 2152 ? 168.256 181.936 192.392 1.00 83.70  ? 2152 GLU A CG    1 
ATOM   4112  C CD    . GLU A 1 2152 ? 166.997 182.294 191.634 1.00 83.70  ? 2152 GLU A CD    1 
ATOM   4113  O OE1   . GLU A 1 2152 ? 166.445 183.385 191.883 1.00 83.70  ? 2152 GLU A OE1   1 
ATOM   4114  O OE2   . GLU A 1 2152 ? 166.559 181.485 190.789 1.00 83.70  ? 2152 GLU A OE2   1 
ATOM   4115  N N     . ASP A 1 2153 ? 170.935 184.045 193.222 1.00 83.40  ? 2153 ASP A N     1 
ATOM   4116  C CA    . ASP A 1 2153 ? 172.386 183.914 193.206 1.00 83.40  ? 2153 ASP A CA    1 
ATOM   4117  C C     . ASP A 1 2153 ? 173.110 185.119 193.789 1.00 83.40  ? 2153 ASP A C     1 
ATOM   4118  O O     . ASP A 1 2153 ? 174.303 185.014 194.091 1.00 83.40  ? 2153 ASP A O     1 
ATOM   4119  C CB    . ASP A 1 2153 ? 172.873 183.669 191.779 1.00 83.40  ? 2153 ASP A CB    1 
ATOM   4120  C CG    . ASP A 1 2153 ? 172.225 182.459 191.148 1.00 83.40  ? 2153 ASP A CG    1 
ATOM   4121  O OD1   . ASP A 1 2153 ? 171.602 181.669 191.886 1.00 83.40  ? 2153 ASP A OD1   1 
ATOM   4122  O OD2   . ASP A 1 2153 ? 172.344 182.291 189.917 1.00 83.40  ? 2153 ASP A OD2   1 
ATOM   4123  N N     . ILE A 1 2154 ? 172.433 186.255 193.952 1.00 73.52  ? 2154 ILE A N     1 
ATOM   4124  C CA    . ILE A 1 2154 ? 173.096 187.435 194.510 1.00 73.52  ? 2154 ILE A CA    1 
ATOM   4125  C C     . ILE A 1 2154 ? 173.619 187.181 195.920 1.00 73.52  ? 2154 ILE A C     1 
ATOM   4126  O O     . ILE A 1 2154 ? 174.803 187.458 196.175 1.00 73.52  ? 2154 ILE A O     1 
ATOM   4127  C CB    . ILE A 1 2154 ? 172.164 188.653 194.432 1.00 73.52  ? 2154 ILE A CB    1 
ATOM   4128  C CG1   . ILE A 1 2154 ? 171.345 188.613 193.144 1.00 73.52  ? 2154 ILE A CG1   1 
ATOM   4129  C CG2   . ILE A 1 2154 ? 172.964 189.936 194.510 1.00 73.52  ? 2154 ILE A CG2   1 
ATOM   4130  C CD1   . ILE A 1 2154 ? 170.556 189.873 192.886 1.00 73.52  ? 2154 ILE A CD1   1 
ATOM   4131  N N     . PRO A 1 2155 ? 172.824 186.670 196.868 1.00 77.43  ? 2155 PRO A N     1 
ATOM   4132  C CA    . PRO A 1 2155 ? 173.402 186.354 198.181 1.00 77.43  ? 2155 PRO A CA    1 
ATOM   4133  C C     . PRO A 1 2155 ? 174.516 185.331 198.103 1.00 77.43  ? 2155 PRO A C     1 
ATOM   4134  O O     . PRO A 1 2155 ? 175.489 185.429 198.859 1.00 77.43  ? 2155 PRO A O     1 
ATOM   4135  C CB    . PRO A 1 2155 ? 172.201 185.829 198.978 1.00 77.43  ? 2155 PRO A CB    1 
ATOM   4136  C CG    . PRO A 1 2155 ? 171.235 185.375 197.951 1.00 77.43  ? 2155 PRO A CG    1 
ATOM   4137  C CD    . PRO A 1 2155 ? 171.389 186.337 196.822 1.00 77.43  ? 2155 PRO A CD    1 
ATOM   4138  N N     . LEU A 1 2156 ? 174.412 184.357 197.197 1.00 79.75  ? 2156 LEU A N     1 
ATOM   4139  C CA    . LEU A 1 2156 ? 175.491 183.391 197.036 1.00 79.75  ? 2156 LEU A CA    1 
ATOM   4140  C C     . LEU A 1 2156 ? 176.770 184.071 196.572 1.00 79.75  ? 2156 LEU A C     1 
ATOM   4141  O O     . LEU A 1 2156 ? 177.855 183.788 197.092 1.00 79.75  ? 2156 LEU A O     1 
ATOM   4142  C CB    . LEU A 1 2156 ? 175.083 182.301 196.050 1.00 79.75  ? 2156 LEU A CB    1 
ATOM   4143  C CG    . LEU A 1 2156 ? 174.745 180.942 196.657 1.00 79.75  ? 2156 LEU A CG    1 
ATOM   4144  C CD1   . LEU A 1 2156 ? 173.423 181.009 197.395 1.00 79.75  ? 2156 LEU A CD1   1 
ATOM   4145  C CD2   . LEU A 1 2156 ? 174.709 179.875 195.581 1.00 79.75  ? 2156 LEU A CD2   1 
ATOM   4146  N N     . LEU A 1 2157 ? 176.664 184.974 195.596 1.00 74.68  ? 2157 LEU A N     1 
ATOM   4147  C CA    . LEU A 1 2157 ? 177.854 185.665 195.118 1.00 74.68  ? 2157 LEU A CA    1 
ATOM   4148  C C     . LEU A 1 2157 ? 178.467 186.519 196.215 1.00 74.68  ? 2157 LEU A C     1 
ATOM   4149  O O     . LEU A 1 2157 ? 179.695 186.575 196.353 1.00 74.68  ? 2157 LEU A O     1 
ATOM   4150  C CB    . LEU A 1 2157 ? 177.520 186.519 193.897 1.00 74.68  ? 2157 LEU A CB    1 
ATOM   4151  C CG    . LEU A 1 2157 ? 178.714 187.076 193.117 1.00 74.68  ? 2157 LEU A CG    1 
ATOM   4152  C CD1   . LEU A 1 2157 ? 178.410 187.098 191.634 1.00 74.68  ? 2157 LEU A CD1   1 
ATOM   4153  C CD2   . LEU A 1 2157 ? 179.073 188.470 193.593 1.00 74.68  ? 2157 LEU A CD2   1 
ATOM   4154  N N     . PHE A 1 2158 ? 177.637 187.195 197.006 1.00 71.43  ? 2158 PHE A N     1 
ATOM   4155  C CA    . PHE A 1 2158 ? 178.198 188.034 198.057 1.00 71.43  ? 2158 PHE A CA    1 
ATOM   4156  C C     . PHE A 1 2158 ? 178.828 187.191 199.159 1.00 71.43  ? 2158 PHE A C     1 
ATOM   4157  O O     . PHE A 1 2158 ? 179.850 187.581 199.735 1.00 71.43  ? 2158 PHE A O     1 
ATOM   4158  C CB    . PHE A 1 2158 ? 177.130 188.971 198.608 1.00 71.43  ? 2158 PHE A CB    1 
ATOM   4159  C CG    . PHE A 1 2158 ? 176.953 190.209 197.783 1.00 71.43  ? 2158 PHE A CG    1 
ATOM   4160  C CD1   . PHE A 1 2158 ? 178.006 191.086 197.600 1.00 71.43  ? 2158 PHE A CD1   1 
ATOM   4161  C CD2   . PHE A 1 2158 ? 175.746 190.485 197.173 1.00 71.43  ? 2158 PHE A CD2   1 
ATOM   4162  C CE1   . PHE A 1 2158 ? 177.854 192.218 196.837 1.00 71.43  ? 2158 PHE A CE1   1 
ATOM   4163  C CE2   . PHE A 1 2158 ? 175.590 191.617 196.407 1.00 71.43  ? 2158 PHE A CE2   1 
ATOM   4164  C CZ    . PHE A 1 2158 ? 176.645 192.484 196.239 1.00 71.43  ? 2158 PHE A CZ    1 
ATOM   4165  N N     . SER A 1 2159 ? 178.253 186.024 199.453 1.00 78.48  ? 2159 SER A N     1 
ATOM   4166  C CA    . SER A 1 2159 ? 178.890 185.121 200.405 1.00 78.48  ? 2159 SER A CA    1 
ATOM   4167  C C     . SER A 1 2159 ? 180.226 184.625 199.871 1.00 78.48  ? 2159 SER A C     1 
ATOM   4168  O O     . SER A 1 2159 ? 181.198 184.502 200.625 1.00 78.48  ? 2159 SER A O     1 
ATOM   4169  C CB    . SER A 1 2159 ? 177.967 183.945 200.720 1.00 78.48  ? 2159 SER A CB    1 
ATOM   4170  O OG    . SER A 1 2159 ? 178.051 182.950 199.717 1.00 78.48  ? 2159 SER A OG    1 
ATOM   4171  N N     . LEU A 1 2160 ? 180.293 184.334 198.570 1.00 74.96  ? 2160 LEU A N     1 
ATOM   4172  C CA    . LEU A 1 2160 ? 181.556 183.931 197.959 1.00 74.96  ? 2160 LEU A CA    1 
ATOM   4173  C C     . LEU A 1 2160 ? 182.599 185.031 198.082 1.00 74.96  ? 2160 LEU A C     1 
ATOM   4174  O O     . LEU A 1 2160 ? 183.761 184.766 198.415 1.00 74.96  ? 2160 LEU A O     1 
ATOM   4175  C CB    . LEU A 1 2160 ? 181.336 183.581 196.491 1.00 74.96  ? 2160 LEU A CB    1 
ATOM   4176  C CG    . LEU A 1 2160 ? 181.253 182.108 196.114 1.00 74.96  ? 2160 LEU A CG    1 
ATOM   4177  C CD1   . LEU A 1 2160 ? 180.127 181.428 196.860 1.00 74.96  ? 2160 LEU A CD1   1 
ATOM   4178  C CD2   . LEU A 1 2160 ? 181.049 181.986 194.619 1.00 74.96  ? 2160 LEU A CD2   1 
ATOM   4179  N N     . LEU A 1 2161 ? 182.200 186.273 197.812 1.00 72.36  ? 2161 LEU A N     1 
ATOM   4180  C CA    . LEU A 1 2161 ? 183.128 187.390 197.935 1.00 72.36  ? 2161 LEU A CA    1 
ATOM   4181  C C     . LEU A 1 2161 ? 183.596 187.553 199.373 1.00 72.36  ? 2161 LEU A C     1 
ATOM   4182  O O     . LEU A 1 2161 ? 184.775 187.826 199.623 1.00 72.36  ? 2161 LEU A O     1 
ATOM   4183  C CB    . LEU A 1 2161 ? 182.472 188.674 197.434 1.00 72.36  ? 2161 LEU A CB    1 
ATOM   4184  C CG    . LEU A 1 2161 ? 182.649 188.949 195.944 1.00 72.36  ? 2161 LEU A CG    1 
ATOM   4185  C CD1   . LEU A 1 2161 ? 182.198 190.353 195.606 1.00 72.36  ? 2161 LEU A CD1   1 
ATOM   4186  C CD2   . LEU A 1 2161 ? 184.090 188.741 195.551 1.00 72.36  ? 2161 LEU A CD2   1 
ATOM   4187  N N     . SER A 1 2162 ? 182.685 187.388 200.332 1.00 77.93  ? 2162 SER A N     1 
ATOM   4188  C CA    . SER A 1 2162 ? 183.064 187.467 201.737 1.00 77.93  ? 2162 SER A CA    1 
ATOM   4189  C C     . SER A 1 2162 ? 184.071 186.383 202.093 1.00 77.93  ? 2162 SER A C     1 
ATOM   4190  O O     . SER A 1 2162 ? 185.044 186.633 202.813 1.00 77.93  ? 2162 SER A O     1 
ATOM   4191  C CB    . SER A 1 2162 ? 181.822 187.355 202.618 1.00 77.93  ? 2162 SER A CB    1 
ATOM   4192  O OG    . SER A 1 2162 ? 182.171 187.388 203.989 1.00 77.93  ? 2162 SER A OG    1 
ATOM   4193  N N     . ASP A 1 2163 ? 183.847 185.164 201.601 1.00 85.95  ? 2163 ASP A N     1 
ATOM   4194  C CA    . ASP A 1 2163 ? 184.753 184.065 201.915 1.00 85.95  ? 2163 ASP A CA    1 
ATOM   4195  C C     . ASP A 1 2163 ? 186.129 184.279 201.298 1.00 85.95  ? 2163 ASP A C     1 
ATOM   4196  O O     . ASP A 1 2163 ? 187.148 184.024 201.947 1.00 85.95  ? 2163 ASP A O     1 
ATOM   4197  C CB    . ASP A 1 2163 ? 184.153 182.741 201.448 1.00 85.95  ? 2163 ASP A CB    1 
ATOM   4198  C CG    . ASP A 1 2163 ? 182.914 182.357 202.234 1.00 85.95  ? 2163 ASP A CG    1 
ATOM   4199  O OD1   . ASP A 1 2163 ? 182.526 181.171 202.197 1.00 85.95  ? 2163 ASP A OD1   1 
ATOM   4200  O OD2   . ASP A 1 2163 ? 182.333 183.242 202.896 1.00 85.95  ? 2163 ASP A OD2   1 
ATOM   4201  N N     . VAL A 1 2164 ? 186.184 184.740 200.050 1.00 72.18  ? 2164 VAL A N     1 
ATOM   4202  C CA    . VAL A 1 2164 ? 187.479 184.963 199.413 1.00 72.18  ? 2164 VAL A CA    1 
ATOM   4203  C C     . VAL A 1 2164 ? 188.109 186.256 199.909 1.00 72.18  ? 2164 VAL A C     1 
ATOM   4204  O O     . VAL A 1 2164 ? 189.283 186.284 200.295 1.00 72.18  ? 2164 VAL A O     1 
ATOM   4205  C CB    . VAL A 1 2164 ? 187.336 184.958 197.882 1.00 72.18  ? 2164 VAL A CB    1 
ATOM   4206  C CG1   . VAL A 1 2164 ? 188.675 185.222 197.243 1.00 72.18  ? 2164 VAL A CG1   1 
ATOM   4207  C CG2   . VAL A 1 2164 ? 186.789 183.631 197.414 1.00 72.18  ? 2164 VAL A CG2   1 
ATOM   4208  N N     . PHE A 1 2165 ? 187.344 187.346 199.908 1.00 70.38  ? 2165 PHE A N     1 
ATOM   4209  C CA    . PHE A 1 2165 ? 187.829 188.624 200.407 1.00 70.38  ? 2165 PHE A CA    1 
ATOM   4210  C C     . PHE A 1 2165 ? 187.225 188.851 201.782 1.00 70.38  ? 2165 PHE A C     1 
ATOM   4211  O O     . PHE A 1 2165 ? 186.018 189.116 201.888 1.00 70.38  ? 2165 PHE A O     1 
ATOM   4212  C CB    . PHE A 1 2165 ? 187.450 189.764 199.459 1.00 70.38  ? 2165 PHE A CB    1 
ATOM   4213  C CG    . PHE A 1 2165 ? 188.023 189.630 198.081 1.00 70.38  ? 2165 PHE A CG    1 
ATOM   4214  C CD1   . PHE A 1 2165 ? 187.468 188.759 197.165 1.00 70.38  ? 2165 PHE A CD1   1 
ATOM   4215  C CD2   . PHE A 1 2165 ? 189.107 190.391 197.694 1.00 70.38  ? 2165 PHE A CD2   1 
ATOM   4216  C CE1   . PHE A 1 2165 ? 187.990 188.642 195.896 1.00 70.38  ? 2165 PHE A CE1   1 
ATOM   4217  C CE2   . PHE A 1 2165 ? 189.630 190.276 196.424 1.00 70.38  ? 2165 PHE A CE2   1 
ATOM   4218  C CZ    . PHE A 1 2165 ? 189.069 189.402 195.525 1.00 70.38  ? 2165 PHE A CZ    1 
ATOM   4219  N N     . PRO A 1 2166 ? 188.001 188.763 202.863 1.00 76.55  ? 2166 PRO A N     1 
ATOM   4220  C CA    . PRO A 1 2166 ? 187.421 188.878 204.207 1.00 76.55  ? 2166 PRO A CA    1 
ATOM   4221  C C     . PRO A 1 2166 ? 187.241 190.337 204.601 1.00 76.55  ? 2166 PRO A C     1 
ATOM   4222  O O     . PRO A 1 2166 ? 188.202 191.107 204.636 1.00 76.55  ? 2166 PRO A O     1 
ATOM   4223  C CB    . PRO A 1 2166 ? 188.455 188.178 205.095 1.00 76.55  ? 2166 PRO A CB    1 
ATOM   4224  C CG    . PRO A 1 2166 ? 189.748 188.370 204.373 1.00 76.55  ? 2166 PRO A CG    1 
ATOM   4225  C CD    . PRO A 1 2166 ? 189.446 188.484 202.899 1.00 76.55  ? 2166 PRO A CD    1 
ATOM   4226  N N     . GLY A 1 2167 ? 185.998 190.716 204.887 1.00 81.85  ? 2167 GLY A N     1 
ATOM   4227  C CA    . GLY A 1 2167 ? 185.722 192.027 205.435 1.00 81.85  ? 2167 GLY A CA    1 
ATOM   4228  C C     . GLY A 1 2167 ? 185.852 193.184 204.474 1.00 81.85  ? 2167 GLY A C     1 
ATOM   4229  O O     . GLY A 1 2167 ? 185.850 194.335 204.917 1.00 81.85  ? 2167 GLY A O     1 
ATOM   4230  N N     . VAL A 1 2168 ? 185.964 192.923 203.175 1.00 82.57  ? 2168 VAL A N     1 
ATOM   4231  C CA    . VAL A 1 2168 ? 186.053 193.967 202.161 1.00 82.57  ? 2168 VAL A CA    1 
ATOM   4232  C C     . VAL A 1 2168 ? 184.683 194.103 201.518 1.00 82.57  ? 2168 VAL A C     1 
ATOM   4233  O O     . VAL A 1 2168 ? 184.209 193.177 200.850 1.00 82.57  ? 2168 VAL A O     1 
ATOM   4234  C CB    . VAL A 1 2168 ? 187.125 193.652 201.109 1.00 82.57  ? 2168 VAL A CB    1 
ATOM   4235  C CG1   . VAL A 1 2168 ? 187.199 194.768 200.091 1.00 82.57  ? 2168 VAL A CG1   1 
ATOM   4236  C CG2   . VAL A 1 2168 ? 188.469 193.453 201.776 1.00 82.57  ? 2168 VAL A CG2   1 
ATOM   4237  N N     . GLN A 1 2169 ? 184.053 195.254 201.709 1.00 94.23  ? 2169 GLN A N     1 
ATOM   4238  C CA    . GLN A 1 2169 ? 182.683 195.470 201.275 1.00 94.23  ? 2169 GLN A CA    1 
ATOM   4239  C C     . GLN A 1 2169 ? 182.644 196.426 200.092 1.00 94.23  ? 2169 GLN A C     1 
ATOM   4240  O O     . GLN A 1 2169 ? 183.560 197.220 199.864 1.00 94.23  ? 2169 GLN A O     1 
ATOM   4241  C CB    . GLN A 1 2169 ? 181.834 196.018 202.427 1.00 94.23  ? 2169 GLN A CB    1 
ATOM   4242  C CG    . GLN A 1 2169 ? 181.915 197.527 202.587 1.00 94.23  ? 2169 GLN A CG    1 
ATOM   4243  C CD    . GLN A 1 2169 ? 183.173 197.987 203.300 1.00 94.23  ? 2169 GLN A CD    1 
ATOM   4244  O OE1   . GLN A 1 2169 ? 184.237 197.383 203.166 1.00 94.23  ? 2169 GLN A OE1   1 
ATOM   4245  N NE2   . GLN A 1 2169 ? 183.057 199.072 204.056 1.00 94.23  ? 2169 GLN A NE2   1 
ATOM   4246  N N     . TYR A 1 2170 ? 181.556 196.337 199.339 1.00 93.96  ? 2170 TYR A N     1 
ATOM   4247  C CA    . TYR A 1 2170 ? 181.294 197.208 198.206 1.00 93.96  ? 2170 TYR A CA    1 
ATOM   4248  C C     . TYR A 1 2170 ? 180.467 198.414 198.633 1.00 93.96  ? 2170 TYR A C     1 
ATOM   4249  O O     . TYR A 1 2170 ? 179.747 198.377 199.634 1.00 93.96  ? 2170 TYR A O     1 
ATOM   4250  C CB    . TYR A 1 2170 ? 180.566 196.445 197.098 1.00 93.96  ? 2170 TYR A CB    1 
ATOM   4251  C CG    . TYR A 1 2170 ? 180.117 197.328 195.964 1.00 93.96  ? 2170 TYR A CG    1 
ATOM   4252  C CD1   . TYR A 1 2170 ? 181.030 198.057 195.218 1.00 93.96  ? 2170 TYR A CD1   1 
ATOM   4253  C CD2   . TYR A 1 2170 ? 178.770 197.461 195.664 1.00 93.96  ? 2170 TYR A CD2   1 
ATOM   4254  C CE1   . TYR A 1 2170 ? 180.614 198.881 194.196 1.00 93.96  ? 2170 TYR A CE1   1 
ATOM   4255  C CE2   . TYR A 1 2170 ? 178.346 198.278 194.640 1.00 93.96  ? 2170 TYR A CE2   1 
ATOM   4256  C CZ    . TYR A 1 2170 ? 179.272 198.986 193.908 1.00 93.96  ? 2170 TYR A CZ    1 
ATOM   4257  O OH    . TYR A 1 2170 ? 178.852 199.804 192.886 1.00 93.96  ? 2170 TYR A OH    1 
ATOM   4258  N N     . HIS A 1 2171 ? 180.573 199.488 197.854 1.00 97.60  ? 2171 HIS A N     1 
ATOM   4259  C CA    . HIS A 1 2171 ? 179.816 200.714 198.081 1.00 97.60  ? 2171 HIS A CA    1 
ATOM   4260  C C     . HIS A 1 2171 ? 179.284 201.202 196.741 1.00 97.60  ? 2171 HIS A C     1 
ATOM   4261  O O     . HIS A 1 2171 ? 180.051 201.679 195.900 1.00 97.60  ? 2171 HIS A O     1 
ATOM   4262  C CB    . HIS A 1 2171 ? 180.686 201.778 198.745 1.00 97.60  ? 2171 HIS A CB    1 
ATOM   4263  C CG    . HIS A 1 2171 ? 180.891 201.557 200.209 1.00 97.60  ? 2171 HIS A CG    1 
ATOM   4264  N ND1   . HIS A 1 2171 ? 180.139 200.661 200.937 1.00 97.60  ? 2171 HIS A ND1   1 
ATOM   4265  C CD2   . HIS A 1 2171 ? 181.770 202.106 201.080 1.00 97.60  ? 2171 HIS A CD2   1 
ATOM   4266  C CE1   . HIS A 1 2171 ? 180.540 200.672 202.195 1.00 97.60  ? 2171 HIS A CE1   1 
ATOM   4267  N NE2   . HIS A 1 2171 ? 181.530 201.540 202.309 1.00 97.60  ? 2171 HIS A NE2   1 
ATOM   4268  N N     . ARG A 1 2172 ? 177.977 201.073 196.542 1.00 99.09  ? 2172 ARG A N     1 
ATOM   4269  C CA    . ARG A 1 2172 ? 177.350 201.561 195.324 1.00 99.09  ? 2172 ARG A CA    1 
ATOM   4270  C C     . ARG A 1 2172 ? 177.390 203.084 195.289 1.00 99.09  ? 2172 ARG A C     1 
ATOM   4271  O O     . ARG A 1 2172 ? 177.192 203.747 196.310 1.00 99.09  ? 2172 ARG A O     1 
ATOM   4272  C CB    . ARG A 1 2172 ? 175.908 201.054 195.245 1.00 99.09  ? 2172 ARG A CB    1 
ATOM   4273  C CG    . ARG A 1 2172 ? 174.912 202.004 194.598 1.00 99.09  ? 2172 ARG A CG    1 
ATOM   4274  C CD    . ARG A 1 2172 ? 175.007 201.980 193.081 1.00 99.09  ? 2172 ARG A CD    1 
ATOM   4275  N NE    . ARG A 1 2172 ? 174.744 200.650 192.545 1.00 99.09  ? 2172 ARG A NE    1 
ATOM   4276  C CZ    . ARG A 1 2172 ? 174.934 200.301 191.281 1.00 99.09  ? 2172 ARG A CZ    1 
ATOM   4277  N NH1   . ARG A 1 2172 ? 175.379 201.166 190.384 1.00 99.09  ? 2172 ARG A NH1   1 
ATOM   4278  N NH2   . ARG A 1 2172 ? 174.671 199.053 190.907 1.00 99.09  ? 2172 ARG A NH2   1 
ATOM   4279  N N     . GLY A 1 2173 ? 177.670 203.636 194.112 1.00 106.56 ? 2173 GLY A N     1 
ATOM   4280  C CA    . GLY A 1 2173 ? 177.662 205.082 193.969 1.00 106.56 ? 2173 GLY A CA    1 
ATOM   4281  C C     . GLY A 1 2173 ? 176.291 205.657 194.279 1.00 106.56 ? 2173 GLY A C     1 
ATOM   4282  O O     . GLY A 1 2173 ? 175.260 205.089 193.914 1.00 106.56 ? 2173 GLY A O     1 
ATOM   4283  N N     . GLU A 1 2174 ? 176.285 206.799 194.969 1.00 106.92 ? 2174 GLU A N     1 
ATOM   4284  C CA    . GLU A 1 2174 ? 175.027 207.365 195.448 1.00 106.92 ? 2174 GLU A CA    1 
ATOM   4285  C C     . GLU A 1 2174 ? 174.114 207.758 194.293 1.00 106.92 ? 2174 GLU A C     1 
ATOM   4286  O O     . GLU A 1 2174 ? 172.917 207.451 194.305 1.00 106.92 ? 2174 GLU A O     1 
ATOM   4287  C CB    . GLU A 1 2174 ? 175.304 208.563 196.355 1.00 106.92 ? 2174 GLU A CB    1 
ATOM   4288  C CG    . GLU A 1 2174 ? 176.025 208.197 197.640 1.00 106.92 ? 2174 GLU A CG    1 
ATOM   4289  C CD    . GLU A 1 2174 ? 175.139 207.438 198.611 1.00 106.92 ? 2174 GLU A CD    1 
ATOM   4290  O OE1   . GLU A 1 2174 ? 173.910 207.390 198.393 1.00 106.92 ? 2174 GLU A OE1   1 
ATOM   4291  O OE2   . GLU A 1 2174 ? 175.674 206.886 199.594 1.00 106.92 ? 2174 GLU A OE2   1 
ATOM   4292  N N     . MET A 1 2175 ? 174.668 208.425 193.280 1.00 102.55 ? 2175 MET A N     1 
ATOM   4293  C CA    . MET A 1 2175 ? 173.902 208.857 192.111 1.00 102.55 ? 2175 MET A CA    1 
ATOM   4294  C C     . MET A 1 2175 ? 172.682 209.676 192.526 1.00 102.55 ? 2175 MET A C     1 
ATOM   4295  O O     . MET A 1 2175 ? 171.570 209.463 192.041 1.00 102.55 ? 2175 MET A O     1 
ATOM   4296  C CB    . MET A 1 2175 ? 173.485 207.656 191.259 1.00 102.55 ? 2175 MET A CB    1 
ATOM   4297  C CG    . MET A 1 2175 ? 174.531 206.561 191.162 1.00 102.55 ? 2175 MET A CG    1 
ATOM   4298  S SD    . MET A 1 2175 ? 175.748 206.865 189.876 1.00 102.55 ? 2175 MET A SD    1 
ATOM   4299  C CE    . MET A 1 2175 ? 174.669 207.165 188.488 1.00 102.55 ? 2175 MET A CE    1 
ATOM   4300  N N     . THR A 1 2176 ? 172.895 210.626 193.439 1.00 95.47  ? 2176 THR A N     1 
ATOM   4301  C CA    . THR A 1 2176 ? 171.770 211.324 194.056 1.00 95.47  ? 2176 THR A CA    1 
ATOM   4302  C C     . THR A 1 2176 ? 170.965 212.119 193.034 1.00 95.47  ? 2176 THR A C     1 
ATOM   4303  O O     . THR A 1 2176 ? 169.730 212.135 193.087 1.00 95.47  ? 2176 THR A O     1 
ATOM   4304  C CB    . THR A 1 2176 ? 172.267 212.232 195.180 1.00 95.47  ? 2176 THR A CB    1 
ATOM   4305  O OG1   . THR A 1 2176 ? 171.192 213.058 195.640 1.00 95.47  ? 2176 THR A OG1   1 
ATOM   4306  C CG2   . THR A 1 2176 ? 173.422 213.103 194.709 1.00 95.47  ? 2176 THR A CG2   1 
ATOM   4307  N N     . ALA A 1 2177 ? 171.640 212.791 192.100 1.00 95.44  ? 2177 ALA A N     1 
ATOM   4308  C CA    . ALA A 1 2177 ? 170.916 213.552 191.088 1.00 95.44  ? 2177 ALA A CA    1 
ATOM   4309  C C     . ALA A 1 2177 ? 170.094 212.634 190.192 1.00 95.44  ? 2177 ALA A C     1 
ATOM   4310  O O     . ALA A 1 2177 ? 168.926 212.925 189.893 1.00 95.44  ? 2177 ALA A O     1 
ATOM   4311  C CB    . ALA A 1 2177 ? 171.891 214.384 190.258 1.00 95.44  ? 2177 ALA A CB    1 
ATOM   4312  N N     . LEU A 1 2178 ? 170.682 211.519 189.758 1.00 90.39  ? 2178 LEU A N     1 
ATOM   4313  C CA    . LEU A 1 2178 ? 169.920 210.576 188.952 1.00 90.39  ? 2178 LEU A CA    1 
ATOM   4314  C C     . LEU A 1 2178 ? 168.790 209.961 189.759 1.00 90.39  ? 2178 LEU A C     1 
ATOM   4315  O O     . LEU A 1 2178 ? 167.720 209.678 189.218 1.00 90.39  ? 2178 LEU A O     1 
ATOM   4316  C CB    . LEU A 1 2178 ? 170.824 209.483 188.395 1.00 90.39  ? 2178 LEU A CB    1 
ATOM   4317  C CG    . LEU A 1 2178 ? 170.087 208.678 187.326 1.00 90.39  ? 2178 LEU A CG    1 
ATOM   4318  C CD1   . LEU A 1 2178 ? 169.997 209.470 186.033 1.00 90.39  ? 2178 LEU A CD1   1 
ATOM   4319  C CD2   . LEU A 1 2178 ? 170.732 207.334 187.100 1.00 90.39  ? 2178 LEU A CD2   1 
ATOM   4320  N N     . ARG A 1 2179 ? 169.004 209.743 191.057 1.00 96.49  ? 2179 ARG A N     1 
ATOM   4321  C CA    . ARG A 1 2179 ? 167.924 209.231 191.892 1.00 96.49  ? 2179 ARG A CA    1 
ATOM   4322  C C     . ARG A 1 2179 ? 166.767 210.217 191.949 1.00 96.49  ? 2179 ARG A C     1 
ATOM   4323  O O     . ARG A 1 2179 ? 165.597 209.823 191.866 1.00 96.49  ? 2179 ARG A O     1 
ATOM   4324  C CB    . ARG A 1 2179 ? 168.441 208.929 193.295 1.00 96.49  ? 2179 ARG A CB    1 
ATOM   4325  C CG    . ARG A 1 2179 ? 169.177 207.614 193.400 1.00 96.49  ? 2179 ARG A CG    1 
ATOM   4326  C CD    . ARG A 1 2179 ? 169.233 207.127 194.831 1.00 96.49  ? 2179 ARG A CD    1 
ATOM   4327  N NE    . ARG A 1 2179 ? 169.721 205.757 194.911 1.00 96.49  ? 2179 ARG A NE    1 
ATOM   4328  C CZ    . ARG A 1 2179 ? 169.003 204.733 195.349 1.00 96.49  ? 2179 ARG A CZ    1 
ATOM   4329  N NH1   . ARG A 1 2179 ? 167.755 204.888 195.755 1.00 96.49  ? 2179 ARG A NH1   1 
ATOM   4330  N NH2   . ARG A 1 2179 ? 169.551 203.521 195.376 1.00 96.49  ? 2179 ARG A NH2   1 
ATOM   4331  N N     . GLU A 1 2180 ? 167.074 211.506 192.088 1.00 91.16  ? 2180 GLU A N     1 
ATOM   4332  C CA    . GLU A 1 2180 ? 166.020 212.513 192.108 1.00 91.16  ? 2180 GLU A CA    1 
ATOM   4333  C C     . GLU A 1 2180 ? 165.268 212.547 190.785 1.00 91.16  ? 2180 GLU A C     1 
ATOM   4334  O O     . GLU A 1 2180 ? 164.031 212.614 190.763 1.00 91.16  ? 2180 GLU A O     1 
ATOM   4335  C CB    . GLU A 1 2180 ? 166.617 213.882 192.422 1.00 91.16  ? 2180 GLU A CB    1 
ATOM   4336  C CG    . GLU A 1 2180 ? 165.606 214.884 192.924 1.00 91.16  ? 2180 GLU A CG    1 
ATOM   4337  C CD    . GLU A 1 2180 ? 164.933 214.426 194.196 1.00 91.16  ? 2180 GLU A CD    1 
ATOM   4338  O OE1   . GLU A 1 2180 ? 165.605 213.774 195.022 1.00 91.16  ? 2180 GLU A OE1   1 
ATOM   4339  O OE2   . GLU A 1 2180 ? 163.729 214.711 194.370 1.00 91.16  ? 2180 GLU A OE2   1 
ATOM   4340  N N     . GLU A 1 2181 ? 165.997 212.494 189.668 1.00 88.16  ? 2181 GLU A N     1 
ATOM   4341  C CA    . GLU A 1 2181 ? 165.333 212.490 188.368 1.00 88.16  ? 2181 GLU A CA    1 
ATOM   4342  C C     . GLU A 1 2181 ? 164.482 211.238 188.185 1.00 88.16  ? 2181 GLU A C     1 
ATOM   4343  O O     . GLU A 1 2181 ? 163.385 211.301 187.618 1.00 88.16  ? 2181 GLU A O     1 
ATOM   4344  C CB    . GLU A 1 2181 ? 166.362 212.610 187.247 1.00 88.16  ? 2181 GLU A CB    1 
ATOM   4345  C CG    . GLU A 1 2181 ? 166.873 214.023 187.022 1.00 88.16  ? 2181 GLU A CG    1 
ATOM   4346  C CD    . GLU A 1 2181 ? 165.899 214.885 186.239 1.00 88.16  ? 2181 GLU A CD    1 
ATOM   4347  O OE1   . GLU A 1 2181 ? 164.769 214.427 185.976 1.00 88.16  ? 2181 GLU A OE1   1 
ATOM   4348  O OE2   . GLU A 1 2181 ? 166.267 216.022 185.877 1.00 88.16  ? 2181 GLU A OE2   1 
ATOM   4349  N N     . LEU A 1 2182 ? 164.976 210.092 188.656 1.00 88.04  ? 2182 LEU A N     1 
ATOM   4350  C CA    . LEU A 1 2182 ? 164.205 208.858 188.590 1.00 88.04  ? 2182 LEU A CA    1 
ATOM   4351  C C     . LEU A 1 2182 ? 162.911 208.984 189.375 1.00 88.04  ? 2182 LEU A C     1 
ATOM   4352  O O     . LEU A 1 2182 ? 161.844 208.583 188.897 1.00 88.04  ? 2182 LEU A O     1 
ATOM   4353  C CB    . LEU A 1 2182 ? 165.037 207.698 189.133 1.00 88.04  ? 2182 LEU A CB    1 
ATOM   4354  C CG    . LEU A 1 2182 ? 165.661 206.717 188.146 1.00 88.04  ? 2182 LEU A CG    1 
ATOM   4355  C CD1   . LEU A 1 2182 ? 164.588 205.992 187.386 1.00 88.04  ? 2182 LEU A CD1   1 
ATOM   4356  C CD2   . LEU A 1 2182 ? 166.586 207.435 187.192 1.00 88.04  ? 2182 LEU A CD2   1 
ATOM   4357  N N     . LYS A 1 2183 ? 162.985 209.539 190.584 1.00 87.36  ? 2183 LYS A N     1 
ATOM   4358  C CA    . LYS A 1 2183 ? 161.778 209.706 191.382 1.00 87.36  ? 2183 LYS A CA    1 
ATOM   4359  C C     . LYS A 1 2183 ? 160.793 210.638 190.692 1.00 87.36  ? 2183 LYS A C     1 
ATOM   4360  O O     . LYS A 1 2183 ? 159.587 210.367 190.664 1.00 87.36  ? 2183 LYS A O     1 
ATOM   4361  C CB    . LYS A 1 2183 ? 162.131 210.230 192.771 1.00 87.36  ? 2183 LYS A CB    1 
ATOM   4362  C CG    . LYS A 1 2183 ? 160.921 210.500 193.650 1.00 87.36  ? 2183 LYS A CG    1 
ATOM   4363  C CD    . LYS A 1 2183 ? 161.258 210.422 195.135 1.00 87.36  ? 2183 LYS A CD    1 
ATOM   4364  C CE    . LYS A 1 2183 ? 162.711 210.772 195.416 1.00 87.36  ? 2183 LYS A CE    1 
ATOM   4365  N NZ    . LYS A 1 2183 ? 162.995 212.208 195.156 1.00 87.36  ? 2183 LYS A NZ    1 
ATOM   4366  N N     . LYS A 1 2184 ? 161.289 211.738 190.123 1.00 85.31  ? 2184 LYS A N     1 
ATOM   4367  C CA    . LYS A 1 2184 ? 160.397 212.679 189.452 1.00 85.31  ? 2184 LYS A CA    1 
ATOM   4368  C C     . LYS A 1 2184 ? 159.710 212.030 188.257 1.00 85.31  ? 2184 LYS A C     1 
ATOM   4369  O O     . LYS A 1 2184 ? 158.491 212.155 188.082 1.00 85.31  ? 2184 LYS A O     1 
ATOM   4370  C CB    . LYS A 1 2184 ? 161.173 213.921 189.021 1.00 85.31  ? 2184 LYS A CB    1 
ATOM   4371  C CG    . LYS A 1 2184 ? 161.182 215.019 190.065 1.00 85.31  ? 2184 LYS A CG    1 
ATOM   4372  C CD    . LYS A 1 2184 ? 162.372 215.943 189.890 1.00 85.31  ? 2184 LYS A CD    1 
ATOM   4373  C CE    . LYS A 1 2184 ? 162.714 216.648 191.193 1.00 85.31  ? 2184 LYS A CE    1 
ATOM   4374  N NZ    . LYS A 1 2184 ? 162.338 215.836 192.383 1.00 85.31  ? 2184 LYS A NZ    1 
ATOM   4375  N N     . VAL A 1 2185 ? 160.473 211.311 187.432 1.00 80.18  ? 2185 VAL A N     1 
ATOM   4376  C CA    . VAL A 1 2185 ? 159.877 210.669 186.265 1.00 80.18  ? 2185 VAL A CA    1 
ATOM   4377  C C     . VAL A 1 2185 ? 158.871 209.612 186.694 1.00 80.18  ? 2185 VAL A C     1 
ATOM   4378  O O     . VAL A 1 2185 ? 157.773 209.518 186.133 1.00 80.18  ? 2185 VAL A O     1 
ATOM   4379  C CB    . VAL A 1 2185 ? 160.967 210.074 185.358 1.00 80.18  ? 2185 VAL A CB    1 
ATOM   4380  C CG1   . VAL A 1 2185 ? 160.332 209.305 184.219 1.00 80.18  ? 2185 VAL A CG1   1 
ATOM   4381  C CG2   . VAL A 1 2185 ? 161.857 211.171 184.815 1.00 80.18  ? 2185 VAL A CG2   1 
ATOM   4382  N N     . CYS A 1 2186 ? 159.219 208.806 187.697 1.00 86.07  ? 2186 CYS A N     1 
ATOM   4383  C CA    . CYS A 1 2186 ? 158.318 207.750 188.135 1.00 86.07  ? 2186 CYS A CA    1 
ATOM   4384  C C     . CYS A 1 2186 ? 157.019 208.324 188.679 1.00 86.07  ? 2186 CYS A C     1 
ATOM   4385  O O     . CYS A 1 2186 ? 155.934 207.820 188.370 1.00 86.07  ? 2186 CYS A O     1 
ATOM   4386  C CB    . CYS A 1 2186 ? 159.005 206.884 189.187 1.00 86.07  ? 2186 CYS A CB    1 
ATOM   4387  S SG    . CYS A 1 2186 ? 160.171 205.692 188.502 1.00 86.07  ? 2186 CYS A SG    1 
ATOM   4388  N N     . GLN A 1 2187 ? 157.104 209.384 189.484 1.00 86.18  ? 2187 GLN A N     1 
ATOM   4389  C CA    . GLN A 1 2187 ? 155.884 210.005 189.984 1.00 86.18  ? 2187 GLN A CA    1 
ATOM   4390  C C     . GLN A 1 2187 ? 155.094 210.632 188.845 1.00 86.18  ? 2187 GLN A C     1 
ATOM   4391  O O     . GLN A 1 2187 ? 153.867 210.751 188.923 1.00 86.18  ? 2187 GLN A O     1 
ATOM   4392  C CB    . GLN A 1 2187 ? 156.221 211.033 191.070 1.00 86.18  ? 2187 GLN A CB    1 
ATOM   4393  C CG    . GLN A 1 2187 ? 156.479 212.455 190.590 1.00 86.18  ? 2187 GLN A CG    1 
ATOM   4394  C CD    . GLN A 1 2187 ? 155.209 213.254 190.390 1.00 86.18  ? 2187 GLN A CD    1 
ATOM   4395  O OE1   . GLN A 1 2187 ? 154.158 212.908 190.926 1.00 86.18  ? 2187 GLN A OE1   1 
ATOM   4396  N NE2   . GLN A 1 2187 ? 155.298 214.325 189.610 1.00 86.18  ? 2187 GLN A NE2   1 
ATOM   4397  N N     . GLU A 1 2188 ? 155.780 211.043 187.777 1.00 87.42  ? 2188 GLU A N     1 
ATOM   4398  C CA    . GLU A 1 2188 ? 155.057 211.545 186.616 1.00 87.42  ? 2188 GLU A CA    1 
ATOM   4399  C C     . GLU A 1 2188 ? 154.391 210.417 185.842 1.00 87.42  ? 2188 GLU A C     1 
ATOM   4400  O O     . GLU A 1 2188 ? 153.269 210.583 185.355 1.00 87.42  ? 2188 GLU A O     1 
ATOM   4401  C CB    . GLU A 1 2188 ? 155.996 212.328 185.700 1.00 87.42  ? 2188 GLU A CB    1 
ATOM   4402  C CG    . GLU A 1 2188 ? 155.278 213.232 184.710 1.00 87.42  ? 2188 GLU A CG    1 
ATOM   4403  C CD    . GLU A 1 2188 ? 154.713 212.481 183.520 1.00 87.42  ? 2188 GLU A CD    1 
ATOM   4404  O OE1   . GLU A 1 2188 ? 155.219 211.382 183.211 1.00 87.42  ? 2188 GLU A OE1   1 
ATOM   4405  O OE2   . GLU A 1 2188 ? 153.753 212.984 182.901 1.00 87.42  ? 2188 GLU A OE2   1 
ATOM   4406  N N     . MET A 1 2189 ? 155.060 209.274 185.711 1.00 77.70  ? 2189 MET A N     1 
ATOM   4407  C CA    . MET A 1 2189 ? 154.568 208.171 184.899 1.00 77.70  ? 2189 MET A CA    1 
ATOM   4408  C C     . MET A 1 2189 ? 153.736 207.178 185.702 1.00 77.70  ? 2189 MET A C     1 
ATOM   4409  O O     . MET A 1 2189 ? 153.543 206.041 185.259 1.00 77.70  ? 2189 MET A O     1 
ATOM   4410  C CB    . MET A 1 2189 ? 155.738 207.454 184.226 1.00 77.70  ? 2189 MET A CB    1 
ATOM   4411  C CG    . MET A 1 2189 ? 156.305 208.182 183.026 1.00 77.70  ? 2189 MET A CG    1 
ATOM   4412  S SD    . MET A 1 2189 ? 157.225 207.083 181.940 1.00 77.70  ? 2189 MET A SD    1 
ATOM   4413  C CE    . MET A 1 2189 ? 155.885 206.308 181.047 1.00 77.70  ? 2189 MET A CE    1 
ATOM   4414  N N     . TYR A 1 2190 ? 153.241 207.584 186.872 1.00 78.61  ? 2190 TYR A N     1 
ATOM   4415  C CA    . TYR A 1 2190 ? 152.412 206.732 187.723 1.00 78.61  ? 2190 TYR A CA    1 
ATOM   4416  C C     . TYR A 1 2190 ? 153.134 205.452 188.124 1.00 78.61  ? 2190 TYR A C     1 
ATOM   4417  O O     . TYR A 1 2190 ? 152.586 204.356 187.999 1.00 78.61  ? 2190 TYR A O     1 
ATOM   4418  C CB    . TYR A 1 2190 ? 151.086 206.396 187.043 1.00 78.61  ? 2190 TYR A CB    1 
ATOM   4419  C CG    . TYR A 1 2190 ? 150.400 207.593 186.448 1.00 78.61  ? 2190 TYR A CG    1 
ATOM   4420  C CD1   . TYR A 1 2190 ? 149.879 208.589 187.258 1.00 78.61  ? 2190 TYR A CD1   1 
ATOM   4421  C CD2   . TYR A 1 2190 ? 150.290 207.739 185.076 1.00 78.61  ? 2190 TYR A CD2   1 
ATOM   4422  C CE1   . TYR A 1 2190 ? 149.253 209.690 186.719 1.00 78.61  ? 2190 TYR A CE1   1 
ATOM   4423  C CE2   . TYR A 1 2190 ? 149.667 208.836 184.525 1.00 78.61  ? 2190 TYR A CE2   1 
ATOM   4424  C CZ    . TYR A 1 2190 ? 149.149 209.808 185.352 1.00 78.61  ? 2190 TYR A CZ    1 
ATOM   4425  O OH    . TYR A 1 2190 ? 148.527 210.905 184.809 1.00 78.61  ? 2190 TYR A OH    1 
ATOM   4426  N N     . LEU A 1 2191 ? 154.366 205.583 188.604 1.00 77.16  ? 2191 LEU A N     1 
ATOM   4427  C CA    . LEU A 1 2191 ? 155.185 204.449 189.004 1.00 77.16  ? 2191 LEU A CA    1 
ATOM   4428  C C     . LEU A 1 2191 ? 155.590 204.582 190.463 1.00 77.16  ? 2191 LEU A C     1 
ATOM   4429  O O     . LEU A 1 2191 ? 155.706 205.694 190.986 1.00 77.16  ? 2191 LEU A O     1 
ATOM   4430  C CB    . LEU A 1 2191 ? 156.441 204.349 188.146 1.00 77.16  ? 2191 LEU A CB    1 
ATOM   4431  C CG    . LEU A 1 2191 ? 156.223 204.214 186.648 1.00 77.16  ? 2191 LEU A CG    1 
ATOM   4432  C CD1   . LEU A 1 2191 ? 157.488 203.722 186.008 1.00 77.16  ? 2191 LEU A CD1   1 
ATOM   4433  C CD2   . LEU A 1 2191 ? 155.094 203.263 186.376 1.00 77.16  ? 2191 LEU A CD2   1 
ATOM   4434  N N     . THR A 1 2192 ? 155.812 203.445 191.113 1.00 77.25  ? 2192 THR A N     1 
ATOM   4435  C CA    . THR A 1 2192 ? 156.314 203.459 192.478 1.00 77.25  ? 2192 THR A CA    1 
ATOM   4436  C C     . THR A 1 2192 ? 157.830 203.603 192.483 1.00 77.25  ? 2192 THR A C     1 
ATOM   4437  O O     . THR A 1 2192 ? 158.532 202.970 191.691 1.00 77.25  ? 2192 THR A O     1 
ATOM   4438  C CB    . THR A 1 2192 ? 155.909 202.183 193.209 1.00 77.25  ? 2192 THR A CB    1 
ATOM   4439  O OG1   . THR A 1 2192 ? 154.538 201.884 192.926 1.00 77.25  ? 2192 THR A OG1   1 
ATOM   4440  C CG2   . THR A 1 2192 ? 156.087 202.356 194.707 1.00 77.25  ? 2192 THR A CG2   1 
ATOM   4441  N N     . TYR A 1 2193 ? 158.336 204.443 193.381 1.00 88.00  ? 2193 TYR A N     1 
ATOM   4442  C CA    . TYR A 1 2193 ? 159.769 204.654 193.533 1.00 88.00  ? 2193 TYR A CA    1 
ATOM   4443  C C     . TYR A 1 2193 ? 160.154 204.438 194.986 1.00 88.00  ? 2193 TYR A C     1 
ATOM   4444  O O     . TYR A 1 2193 ? 159.438 204.873 195.893 1.00 88.00  ? 2193 TYR A O     1 
ATOM   4445  C CB    . TYR A 1 2193 ? 160.176 206.058 193.076 1.00 88.00  ? 2193 TYR A CB    1 
ATOM   4446  C CG    . TYR A 1 2193 ? 161.618 206.407 193.364 1.00 88.00  ? 2193 TYR A CG    1 
ATOM   4447  C CD1   . TYR A 1 2193 ? 161.988 207.002 194.563 1.00 88.00  ? 2193 TYR A CD1   1 
ATOM   4448  C CD2   . TYR A 1 2193 ? 162.611 206.136 192.438 1.00 88.00  ? 2193 TYR A CD2   1 
ATOM   4449  C CE1   . TYR A 1 2193 ? 163.306 207.319 194.826 1.00 88.00  ? 2193 TYR A CE1   1 
ATOM   4450  C CE2   . TYR A 1 2193 ? 163.930 206.451 192.693 1.00 88.00  ? 2193 TYR A CE2   1 
ATOM   4451  C CZ    . TYR A 1 2193 ? 164.273 207.040 193.888 1.00 88.00  ? 2193 TYR A CZ    1 
ATOM   4452  O OH    . TYR A 1 2193 ? 165.587 207.354 194.144 1.00 88.00  ? 2193 TYR A OH    1 
ATOM   4453  N N     . GLY A 1 2194 ? 161.284 203.773 195.202 1.00 96.58  ? 2194 GLY A N     1 
ATOM   4454  C CA    . GLY A 1 2194 ? 161.772 203.525 196.546 1.00 96.58  ? 2194 GLY A CA    1 
ATOM   4455  C C     . GLY A 1 2194 ? 163.262 203.267 196.518 1.00 96.58  ? 2194 GLY A C     1 
ATOM   4456  O O     . GLY A 1 2194 ? 163.850 203.030 195.461 1.00 96.58  ? 2194 GLY A O     1 
ATOM   4457  N N     . ASP A 1 2195 ? 163.871 203.321 197.697 1.00 103.10 ? 2195 ASP A N     1 
ATOM   4458  C CA    . ASP A 1 2195 ? 165.308 203.141 197.843 1.00 103.10 ? 2195 ASP A CA    1 
ATOM   4459  C C     . ASP A 1 2195 ? 165.594 201.950 198.743 1.00 103.10 ? 2195 ASP A C     1 
ATOM   4460  O O     . ASP A 1 2195 ? 165.082 201.878 199.865 1.00 103.10 ? 2195 ASP A O     1 
ATOM   4461  C CB    . ASP A 1 2195 ? 165.957 204.399 198.417 1.00 103.10 ? 2195 ASP A CB    1 
ATOM   4462  C CG    . ASP A 1 2195 ? 165.439 205.664 197.772 1.00 103.10 ? 2195 ASP A CG    1 
ATOM   4463  O OD1   . ASP A 1 2195 ? 165.633 205.828 196.549 1.00 103.10 ? 2195 ASP A OD1   1 
ATOM   4464  O OD2   . ASP A 1 2195 ? 164.830 206.490 198.484 1.00 103.10 ? 2195 ASP A OD2   1 
ATOM   4465  N N     . GLY A 1 2196 ? 166.416 201.031 198.256 1.00 105.01 ? 2196 GLY A N     1 
ATOM   4466  C CA    . GLY A 1 2196 ? 166.822 199.900 199.073 1.00 105.01 ? 2196 GLY A CA    1 
ATOM   4467  C C     . GLY A 1 2196 ? 165.648 199.007 199.422 1.00 105.01 ? 2196 GLY A C     1 
ATOM   4468  O O     . GLY A 1 2196 ? 164.961 198.468 198.547 1.00 105.01 ? 2196 GLY A O     1 
ATOM   4469  N N     . GLU A 1 2197 ? 165.408 198.842 200.722 1.00 109.54 ? 2197 GLU A N     1 
ATOM   4470  C CA    . GLU A 1 2197 ? 164.388 197.917 201.195 1.00 109.54 ? 2197 GLU A CA    1 
ATOM   4471  C C     . GLU A 1 2197 ? 162.971 198.367 200.872 1.00 109.54 ? 2197 GLU A C     1 
ATOM   4472  O O     . GLU A 1 2197 ? 162.051 197.548 200.965 1.00 109.54 ? 2197 GLU A O     1 
ATOM   4473  C CB    . GLU A 1 2197 ? 164.530 197.717 202.704 1.00 109.54 ? 2197 GLU A CB    1 
ATOM   4474  C CG    . GLU A 1 2197 ? 165.653 196.774 203.099 1.00 109.54 ? 2197 GLU A CG    1 
ATOM   4475  C CD    . GLU A 1 2197 ? 166.323 197.176 204.397 1.00 109.54 ? 2197 GLU A CD    1 
ATOM   4476  O OE1   . GLU A 1 2197 ? 166.196 198.354 204.792 1.00 109.54 ? 2197 GLU A OE1   1 
ATOM   4477  O OE2   . GLU A 1 2197 ? 166.977 196.315 205.021 1.00 109.54 ? 2197 GLU A OE2   1 
ATOM   4478  N N     . GLU A 1 2198 ? 162.766 199.627 200.498 1.00 101.52 ? 2198 GLU A N     1 
ATOM   4479  C CA    . GLU A 1 2198 ? 161.418 200.092 200.212 1.00 101.52 ? 2198 GLU A CA    1 
ATOM   4480  C C     . GLU A 1 2198 ? 160.851 199.385 198.986 1.00 101.52 ? 2198 GLU A C     1 
ATOM   4481  O O     . GLU A 1 2198 ? 161.568 198.747 198.209 1.00 101.52 ? 2198 GLU A O     1 
ATOM   4482  C CB    . GLU A 1 2198 ? 161.393 201.603 199.984 1.00 101.52 ? 2198 GLU A CB    1 
ATOM   4483  C CG    . GLU A 1 2198 ? 162.168 202.417 200.994 1.00 101.52 ? 2198 GLU A CG    1 
ATOM   4484  C CD    . GLU A 1 2198 ? 162.452 203.820 200.496 1.00 101.52 ? 2198 GLU A CD    1 
ATOM   4485  O OE1   . GLU A 1 2198 ? 161.523 204.462 199.964 1.00 101.52 ? 2198 GLU A OE1   1 
ATOM   4486  O OE2   . GLU A 1 2198 ? 163.603 204.282 200.635 1.00 101.52 ? 2198 GLU A OE2   1 
ATOM   4487  N N     . VAL A 1 2199 ? 159.532 199.505 198.824 1.00 90.64  ? 2199 VAL A N     1 
ATOM   4488  C CA    . VAL A 1 2199 ? 158.859 198.887 197.691 1.00 90.64  ? 2199 VAL A CA    1 
ATOM   4489  C C     . VAL A 1 2199 ? 159.398 199.487 196.404 1.00 90.64  ? 2199 VAL A C     1 
ATOM   4490  O O     . VAL A 1 2199 ? 159.481 200.712 196.254 1.00 90.64  ? 2199 VAL A O     1 
ATOM   4491  C CB    . VAL A 1 2199 ? 157.340 199.072 197.812 1.00 90.64  ? 2199 VAL A CB    1 
ATOM   4492  C CG1   . VAL A 1 2199 ? 156.691 199.057 196.448 1.00 90.64  ? 2199 VAL A CG1   1 
ATOM   4493  C CG2   . VAL A 1 2199 ? 156.747 197.988 198.691 1.00 90.64  ? 2199 VAL A CG2   1 
ATOM   4494  N N     . GLY A 1 2200 ? 159.781 198.622 195.470 1.00 85.61  ? 2200 GLY A N     1 
ATOM   4495  C CA    . GLY A 1 2200 ? 160.397 199.052 194.237 1.00 85.61  ? 2200 GLY A CA    1 
ATOM   4496  C C     . GLY A 1 2200 ? 161.885 199.285 194.323 1.00 85.61  ? 2200 GLY A C     1 
ATOM   4497  O O     . GLY A 1 2200 ? 162.490 199.682 193.320 1.00 85.61  ? 2200 GLY A O     1 
ATOM   4498  N N     . GLY A 1 2201 ? 162.494 199.054 195.486 1.00 89.21  ? 2201 GLY A N     1 
ATOM   4499  C CA    . GLY A 1 2201 ? 163.925 199.262 195.610 1.00 89.21  ? 2201 GLY A CA    1 
ATOM   4500  C C     . GLY A 1 2201 ? 164.723 198.382 194.670 1.00 89.21  ? 2201 GLY A C     1 
ATOM   4501  O O     . GLY A 1 2201 ? 165.702 198.828 194.066 1.00 89.21  ? 2201 GLY A O     1 
ATOM   4502  N N     . MET A 1 2202 ? 164.311 197.123 194.527 1.00 82.97  ? 2202 MET A N     1 
ATOM   4503  C CA    . MET A 1 2202 ? 164.984 196.240 193.585 1.00 82.97  ? 2202 MET A CA    1 
ATOM   4504  C C     . MET A 1 2202 ? 164.872 196.775 192.166 1.00 82.97  ? 2202 MET A C     1 
ATOM   4505  O O     . MET A 1 2202 ? 165.845 196.750 191.403 1.00 82.97  ? 2202 MET A O     1 
ATOM   4506  C CB    . MET A 1 2202 ? 164.400 194.833 193.682 1.00 82.97  ? 2202 MET A CB    1 
ATOM   4507  C CG    . MET A 1 2202 ? 164.512 194.221 195.066 1.00 82.97  ? 2202 MET A CG    1 
ATOM   4508  S SD    . MET A 1 2202 ? 162.987 193.417 195.583 1.00 82.97  ? 2202 MET A SD    1 
ATOM   4509  C CE    . MET A 1 2202 ? 161.870 194.815 195.599 1.00 82.97  ? 2202 MET A CE    1 
ATOM   4510  N N     . TRP A 1 2203 ? 163.694 197.280 191.798 1.00 74.07  ? 2203 TRP A N     1 
ATOM   4511  C CA    . TRP A 1 2203 ? 163.525 197.825 190.458 1.00 74.07  ? 2203 TRP A CA    1 
ATOM   4512  C C     . TRP A 1 2203 ? 164.441 199.015 190.220 1.00 74.07  ? 2203 TRP A C     1 
ATOM   4513  O O     . TRP A 1 2203 ? 165.122 199.081 189.192 1.00 74.07  ? 2203 TRP A O     1 
ATOM   4514  C CB    . TRP A 1 2203 ? 162.070 198.217 190.223 1.00 74.07  ? 2203 TRP A CB    1 
ATOM   4515  C CG    . TRP A 1 2203 ? 161.827 198.683 188.832 1.00 74.07  ? 2203 TRP A CG    1 
ATOM   4516  C CD1   . TRP A 1 2203 ? 161.872 197.934 187.699 1.00 74.07  ? 2203 TRP A CD1   1 
ATOM   4517  C CD2   . TRP A 1 2203 ? 161.508 200.013 188.422 1.00 74.07  ? 2203 TRP A CD2   1 
ATOM   4518  N NE1   . TRP A 1 2203 ? 161.600 198.714 186.604 1.00 74.07  ? 2203 TRP A NE1   1 
ATOM   4519  C CE2   . TRP A 1 2203 ? 161.373 199.997 187.024 1.00 74.07  ? 2203 TRP A CE2   1 
ATOM   4520  C CE3   . TRP A 1 2203 ? 161.325 201.217 189.102 1.00 74.07  ? 2203 TRP A CE3   1 
ATOM   4521  C CZ2   . TRP A 1 2203 ? 161.062 201.136 186.295 1.00 74.07  ? 2203 TRP A CZ2   1 
ATOM   4522  C CZ3   . TRP A 1 2203 ? 161.017 202.345 188.378 1.00 74.07  ? 2203 TRP A CZ3   1 
ATOM   4523  C CH2   . TRP A 1 2203 ? 160.889 202.299 186.989 1.00 74.07  ? 2203 TRP A CH2   1 
ATOM   4524  N N     . VAL A 1 2204 ? 164.485 199.960 191.159 1.00 82.71  ? 2204 VAL A N     1 
ATOM   4525  C CA    . VAL A 1 2204 ? 165.313 201.136 190.930 1.00 82.71  ? 2204 VAL A CA    1 
ATOM   4526  C C     . VAL A 1 2204 ? 166.786 200.759 190.933 1.00 82.71  ? 2204 VAL A C     1 
ATOM   4527  O O     . VAL A 1 2204 ? 167.587 201.361 190.208 1.00 82.71  ? 2204 VAL A O     1 
ATOM   4528  C CB    . VAL A 1 2204 ? 165.000 202.237 191.958 1.00 82.71  ? 2204 VAL A CB    1 
ATOM   4529  C CG1   . VAL A 1 2204 ? 165.695 201.960 193.273 1.00 82.71  ? 2204 VAL A CG1   1 
ATOM   4530  C CG2   . VAL A 1 2204 ? 165.412 203.587 191.409 1.00 82.71  ? 2204 VAL A CG2   1 
ATOM   4531  N N     . GLU A 1 2205 ? 167.173 199.759 191.728 1.00 85.33  ? 2205 GLU A N     1 
ATOM   4532  C CA    . GLU A 1 2205 ? 168.549 199.286 191.667 1.00 85.33  ? 2205 GLU A CA    1 
ATOM   4533  C C     . GLU A 1 2205 ? 168.851 198.688 190.304 1.00 85.33  ? 2205 GLU A C     1 
ATOM   4534  O O     . GLU A 1 2205 ? 169.956 198.852 189.775 1.00 85.33  ? 2205 GLU A O     1 
ATOM   4535  C CB    . GLU A 1 2205 ? 168.811 198.269 192.772 1.00 85.33  ? 2205 GLU A CB    1 
ATOM   4536  C CG    . GLU A 1 2205 ? 170.283 198.048 193.040 1.00 85.33  ? 2205 GLU A CG    1 
ATOM   4537  C CD    . GLU A 1 2205 ? 170.928 199.234 193.726 1.00 85.33  ? 2205 GLU A CD    1 
ATOM   4538  O OE1   . GLU A 1 2205 ? 170.191 200.069 194.288 1.00 85.33  ? 2205 GLU A OE1   1 
ATOM   4539  O OE2   . GLU A 1 2205 ? 172.172 199.336 193.698 1.00 85.33  ? 2205 GLU A OE2   1 
ATOM   4540  N N     . LYS A 1 2206 ? 167.877 197.995 189.717 1.00 80.55  ? 2206 LYS A N     1 
ATOM   4541  C CA    . LYS A 1 2206 ? 168.063 197.481 188.368 1.00 80.55  ? 2206 LYS A CA    1 
ATOM   4542  C C     . LYS A 1 2206 ? 168.217 198.616 187.365 1.00 80.55  ? 2206 LYS A C     1 
ATOM   4543  O O     . LYS A 1 2206 ? 169.028 198.526 186.439 1.00 80.55  ? 2206 LYS A O     1 
ATOM   4544  C CB    . LYS A 1 2206 ? 166.900 196.572 187.989 1.00 80.55  ? 2206 LYS A CB    1 
ATOM   4545  C CG    . LYS A 1 2206 ? 166.943 195.213 188.663 1.00 80.55  ? 2206 LYS A CG    1 
ATOM   4546  C CD    . LYS A 1 2206 ? 168.212 194.460 188.307 1.00 80.55  ? 2206 LYS A CD    1 
ATOM   4547  C CE    . LYS A 1 2206 ? 168.423 193.277 189.232 1.00 80.55  ? 2206 LYS A CE    1 
ATOM   4548  N NZ    . LYS A 1 2206 ? 169.675 192.544 188.916 1.00 80.55  ? 2206 LYS A NZ    1 
ATOM   4549  N N     . VAL A 1 2207 ? 167.450 199.696 187.532 1.00 79.81  ? 2207 VAL A N     1 
ATOM   4550  C CA    . VAL A 1 2207 ? 167.611 200.846 186.640 1.00 79.81  ? 2207 VAL A CA    1 
ATOM   4551  C C     . VAL A 1 2207 ? 169.006 201.436 186.778 1.00 79.81  ? 2207 VAL A C     1 
ATOM   4552  O O     . VAL A 1 2207 ? 169.643 201.807 185.785 1.00 79.81  ? 2207 VAL A O     1 
ATOM   4553  C CB    . VAL A 1 2207 ? 166.537 201.917 186.899 1.00 79.81  ? 2207 VAL A CB    1 
ATOM   4554  C CG1   . VAL A 1 2207 ? 166.413 202.818 185.689 1.00 79.81  ? 2207 VAL A CG1   1 
ATOM   4555  C CG2   . VAL A 1 2207 ? 165.211 201.286 187.183 1.00 79.81  ? 2207 VAL A CG2   1 
ATOM   4556  N N     . LEU A 1 2208 ? 169.492 201.558 188.011 1.00 84.99  ? 2208 LEU A N     1 
ATOM   4557  C CA    . LEU A 1 2208 ? 170.822 202.116 188.220 1.00 84.99  ? 2208 LEU A CA    1 
ATOM   4558  C C     . LEU A 1 2208 ? 171.891 201.222 187.606 1.00 84.99  ? 2208 LEU A C     1 
ATOM   4559  O O     . LEU A 1 2208 ? 172.853 201.714 187.004 1.00 84.99  ? 2208 LEU A O     1 
ATOM   4560  C CB    . LEU A 1 2208 ? 171.069 202.321 189.712 1.00 84.99  ? 2208 LEU A CB    1 
ATOM   4561  C CG    . LEU A 1 2208 ? 170.172 203.386 190.344 1.00 84.99  ? 2208 LEU A CG    1 
ATOM   4562  C CD1   . LEU A 1 2208 ? 170.579 203.680 191.776 1.00 84.99  ? 2208 LEU A CD1   1 
ATOM   4563  C CD2   . LEU A 1 2208 ? 170.199 204.651 189.514 1.00 84.99  ? 2208 LEU A CD2   1 
ATOM   4564  N N     . GLN A 1 2209 ? 171.735 199.904 187.742 1.00 86.66  ? 2209 GLN A N     1 
ATOM   4565  C CA    . GLN A 1 2209 ? 172.666 198.980 187.102 1.00 86.66  ? 2209 GLN A CA    1 
ATOM   4566  C C     . GLN A 1 2209 ? 172.613 199.118 185.589 1.00 86.66  ? 2209 GLN A C     1 
ATOM   4567  O O     . GLN A 1 2209 ? 173.646 199.057 184.913 1.00 86.66  ? 2209 GLN A O     1 
ATOM   4568  C CB    . GLN A 1 2209 ? 172.357 197.545 187.523 1.00 86.66  ? 2209 GLN A CB    1 
ATOM   4569  C CG    . GLN A 1 2209 ? 172.659 197.261 188.981 1.00 86.66  ? 2209 GLN A CG    1 
ATOM   4570  C CD    . GLN A 1 2209 ? 172.102 195.935 189.450 1.00 86.66  ? 2209 GLN A CD    1 
ATOM   4571  O OE1   . GLN A 1 2209 ? 171.659 195.115 188.649 1.00 86.66  ? 2209 GLN A OE1   1 
ATOM   4572  N NE2   . GLN A 1 2209 ? 172.124 195.717 190.759 1.00 86.66  ? 2209 GLN A NE2   1 
ATOM   4573  N N     . LEU A 1 2210 ? 171.413 199.310 185.040 1.00 81.74  ? 2210 LEU A N     1 
ATOM   4574  C CA    . LEU A 1 2210 ? 171.278 199.539 183.609 1.00 81.74  ? 2210 LEU A CA    1 
ATOM   4575  C C     . LEU A 1 2210 ? 172.028 200.793 183.191 1.00 81.74  ? 2210 LEU A C     1 
ATOM   4576  O O     . LEU A 1 2210 ? 172.705 200.806 182.160 1.00 81.74  ? 2210 LEU A O     1 
ATOM   4577  C CB    . LEU A 1 2210 ? 169.801 199.660 183.240 1.00 81.74  ? 2210 LEU A CB    1 
ATOM   4578  C CG    . LEU A 1 2210 ? 169.418 199.727 181.762 1.00 81.74  ? 2210 LEU A CG    1 
ATOM   4579  C CD1   . LEU A 1 2210 ? 170.389 198.948 180.896 1.00 81.74  ? 2210 LEU A CD1   1 
ATOM   4580  C CD2   . LEU A 1 2210 ? 168.001 199.228 181.562 1.00 81.74  ? 2210 LEU A CD2   1 
ATOM   4581  N N     . TYR A 1 2211 ? 171.914 201.859 183.980 1.00 85.84  ? 2211 TYR A N     1 
ATOM   4582  C CA    . TYR A 1 2211 ? 172.594 203.105 183.640 1.00 85.84  ? 2211 TYR A CA    1 
ATOM   4583  C C     . TYR A 1 2211 ? 174.106 202.943 183.708 1.00 85.84  ? 2211 TYR A C     1 
ATOM   4584  O O     . TYR A 1 2211 ? 174.837 203.455 182.850 1.00 85.84  ? 2211 TYR A O     1 
ATOM   4585  C CB    . TYR A 1 2211 ? 172.119 204.225 184.563 1.00 85.84  ? 2211 TYR A CB    1 
ATOM   4586  C CG    . TYR A 1 2211 ? 172.789 205.556 184.329 1.00 85.84  ? 2211 TYR A CG    1 
ATOM   4587  C CD1   . TYR A 1 2211 ? 172.736 206.164 183.087 1.00 85.84  ? 2211 TYR A CD1   1 
ATOM   4588  C CD2   . TYR A 1 2211 ? 173.413 206.235 185.361 1.00 85.84  ? 2211 TYR A CD2   1 
ATOM   4589  C CE1   . TYR A 1 2211 ? 173.330 207.383 182.864 1.00 85.84  ? 2211 TYR A CE1   1 
ATOM   4590  C CE2   . TYR A 1 2211 ? 173.988 207.471 185.154 1.00 85.84  ? 2211 TYR A CE2   1 
ATOM   4591  C CZ    . TYR A 1 2211 ? 173.951 208.036 183.901 1.00 85.84  ? 2211 TYR A CZ    1 
ATOM   4592  O OH    . TYR A 1 2211 ? 174.533 209.262 183.677 1.00 85.84  ? 2211 TYR A OH    1 
ATOM   4593  N N     . GLN A 1 2212 ? 174.594 202.229 184.721 1.00 87.20  ? 2212 GLN A N     1 
ATOM   4594  C CA    . GLN A 1 2212 ? 176.026 201.968 184.816 1.00 87.20  ? 2212 GLN A CA    1 
ATOM   4595  C C     . GLN A 1 2212 ? 176.518 201.156 183.626 1.00 87.20  ? 2212 GLN A C     1 
ATOM   4596  O O     . GLN A 1 2212 ? 177.579 201.446 183.060 1.00 87.20  ? 2212 GLN A O     1 
ATOM   4597  C CB    . GLN A 1 2212 ? 176.339 201.248 186.126 1.00 87.20  ? 2212 GLN A CB    1 
ATOM   4598  C CG    . GLN A 1 2212 ? 177.782 201.358 186.577 1.00 87.20  ? 2212 GLN A CG    1 
ATOM   4599  C CD    . GLN A 1 2212 ? 178.108 202.695 187.215 1.00 87.20  ? 2212 GLN A CD    1 
ATOM   4600  O OE1   . GLN A 1 2212 ? 177.355 203.659 187.090 1.00 87.20  ? 2212 GLN A OE1   1 
ATOM   4601  N NE2   . GLN A 1 2212 ? 179.235 202.755 187.914 1.00 87.20  ? 2212 GLN A NE2   1 
ATOM   4602  N N     . ILE A 1 2213 ? 175.756 200.136 183.229 1.00 85.76  ? 2213 ILE A N     1 
ATOM   4603  C CA    . ILE A 1 2213 ? 176.145 199.333 182.077 1.00 85.76  ? 2213 ILE A CA    1 
ATOM   4604  C C     . ILE A 1 2213 ? 176.102 200.177 180.812 1.00 85.76  ? 2213 ILE A C     1 
ATOM   4605  O O     . ILE A 1 2213 ? 176.927 200.003 179.908 1.00 85.76  ? 2213 ILE A O     1 
ATOM   4606  C CB    . ILE A 1 2213 ? 175.243 198.092 181.977 1.00 85.76  ? 2213 ILE A CB    1 
ATOM   4607  C CG1   . ILE A 1 2213 ? 175.497 197.159 183.163 1.00 85.76  ? 2213 ILE A CG1   1 
ATOM   4608  C CG2   . ILE A 1 2213 ? 175.492 197.354 180.683 1.00 85.76  ? 2213 ILE A CG2   1 
ATOM   4609  C CD1   . ILE A 1 2213 ? 176.453 196.028 182.872 1.00 85.76  ? 2213 ILE A CD1   1 
ATOM   4610  N N     . THR A 1 2214 ? 175.153 201.111 180.734 1.00 86.59  ? 2214 THR A N     1 
ATOM   4611  C CA    . THR A 1 2214 ? 175.109 202.044 179.617 1.00 86.59  ? 2214 THR A CA    1 
ATOM   4612  C C     . THR A 1 2214 ? 176.377 202.882 179.564 1.00 86.59  ? 2214 THR A C     1 
ATOM   4613  O O     . THR A 1 2214 ? 176.940 203.104 178.486 1.00 86.59  ? 2214 THR A O     1 
ATOM   4614  C CB    . THR A 1 2214 ? 173.882 202.946 179.737 1.00 86.59  ? 2214 THR A CB    1 
ATOM   4615  O OG1   . THR A 1 2214 ? 172.696 202.148 179.762 1.00 86.59  ? 2214 THR A OG1   1 
ATOM   4616  C CG2   . THR A 1 2214 ? 173.803 203.876 178.557 1.00 86.59  ? 2214 THR A CG2   1 
ATOM   4617  N N     . GLN A 1 2215 ? 176.844 203.352 180.721 1.00 90.52  ? 2215 GLN A N     1 
ATOM   4618  C CA    . GLN A 1 2215 ? 178.115 204.068 180.751 1.00 90.52  ? 2215 GLN A CA    1 
ATOM   4619  C C     . GLN A 1 2215 ? 179.256 203.183 180.270 1.00 90.52  ? 2215 GLN A C     1 
ATOM   4620  O O     . GLN A 1 2215 ? 180.070 203.600 179.437 1.00 90.52  ? 2215 GLN A O     1 
ATOM   4621  C CB    . GLN A 1 2215 ? 178.415 204.566 182.164 1.00 90.52  ? 2215 GLN A CB    1 
ATOM   4622  C CG    . GLN A 1 2215 ? 178.032 206.003 182.421 1.00 90.52  ? 2215 GLN A CG    1 
ATOM   4623  C CD    . GLN A 1 2215 ? 177.657 206.235 183.858 1.00 90.52  ? 2215 GLN A CD    1 
ATOM   4624  O OE1   . GLN A 1 2215 ? 176.481 206.286 184.192 1.00 90.52  ? 2215 GLN A OE1   1 
ATOM   4625  N NE2   . GLN A 1 2215 ? 178.658 206.373 184.723 1.00 90.52  ? 2215 GLN A NE2   1 
ATOM   4626  N N     . ILE A 1 2216 ? 179.314 201.946 180.766 1.00 93.80  ? 2216 ILE A N     1 
ATOM   4627  C CA    . ILE A 1 2216 ? 180.491 201.109 180.549 1.00 93.80  ? 2216 ILE A CA    1 
ATOM   4628  C C     . ILE A 1 2216 ? 180.648 200.765 179.075 1.00 93.80  ? 2216 ILE A C     1 
ATOM   4629  O O     . ILE A 1 2216 ? 181.739 200.886 178.507 1.00 93.80  ? 2216 ILE A O     1 
ATOM   4630  C CB    . ILE A 1 2216 ? 180.416 199.840 181.416 1.00 93.80  ? 2216 ILE A CB    1 
ATOM   4631  C CG1   . ILE A 1 2216 ? 180.678 200.186 182.878 1.00 93.80  ? 2216 ILE A CG1   1 
ATOM   4632  C CG2   . ILE A 1 2216 ? 181.409 198.798 180.928 1.00 93.80  ? 2216 ILE A CG2   1 
ATOM   4633  C CD1   . ILE A 1 2216 ? 181.988 200.905 183.102 1.00 93.80  ? 2216 ILE A CD1   1 
ATOM   4634  N N     . ASN A 1 2217 ? 179.567 200.342 178.429 1.00 95.14  ? 2217 ASN A N     1 
ATOM   4635  C CA    . ASN A 1 2217 ? 179.662 199.853 177.062 1.00 95.14  ? 2217 ASN A CA    1 
ATOM   4636  C C     . ASN A 1 2217 ? 178.339 200.068 176.349 1.00 95.14  ? 2217 ASN A C     1 
ATOM   4637  O O     . ASN A 1 2217 ? 177.320 200.384 176.962 1.00 95.14  ? 2217 ASN A O     1 
ATOM   4638  C CB    . ASN A 1 2217 ? 180.053 198.371 177.024 1.00 95.14  ? 2217 ASN A CB    1 
ATOM   4639  C CG    . ASN A 1 2217 ? 179.160 197.507 177.894 1.00 95.14  ? 2217 ASN A CG    1 
ATOM   4640  O OD1   . ASN A 1 2217 ? 178.056 197.904 178.255 1.00 95.14  ? 2217 ASN A OD1   1 
ATOM   4641  N ND2   . ASN A 1 2217 ? 179.636 196.316 178.234 1.00 95.14  ? 2217 ASN A ND2   1 
ATOM   4642  N N     . HIS A 1 2218 ? 178.372 199.898 175.036 1.00 101.62 ? 2218 HIS A N     1 
ATOM   4643  C CA    . HIS A 1 2218 ? 177.168 199.888 174.227 1.00 101.62 ? 2218 HIS A CA    1 
ATOM   4644  C C     . HIS A 1 2218 ? 176.666 198.458 174.071 1.00 101.62 ? 2218 HIS A C     1 
ATOM   4645  O O     . HIS A 1 2218 ? 177.340 197.492 174.435 1.00 101.62 ? 2218 HIS A O     1 
ATOM   4646  C CB    . HIS A 1 2218 ? 177.442 200.511 172.860 1.00 101.62 ? 2218 HIS A CB    1 
ATOM   4647  C CG    . HIS A 1 2218 ? 178.348 199.689 171.997 1.00 101.62 ? 2218 HIS A CG    1 
ATOM   4648  N ND1   . HIS A 1 2218 ? 179.595 199.274 172.410 1.00 101.62 ? 2218 HIS A ND1   1 
ATOM   4649  C CD2   . HIS A 1 2218 ? 178.177 199.183 170.753 1.00 101.62 ? 2218 HIS A CD2   1 
ATOM   4650  C CE1   . HIS A 1 2218 ? 180.159 198.557 171.454 1.00 101.62 ? 2218 HIS A CE1   1 
ATOM   4651  N NE2   . HIS A 1 2218 ? 179.318 198.485 170.438 1.00 101.62 ? 2218 HIS A NE2   1 
ATOM   4652  N N     . GLY A 1 2219 ? 175.463 198.329 173.517 1.00 100.35 ? 2219 GLY A N     1 
ATOM   4653  C CA    . GLY A 1 2219 ? 174.913 197.024 173.214 1.00 100.35 ? 2219 GLY A CA    1 
ATOM   4654  C C     . GLY A 1 2219 ? 174.590 196.225 174.456 1.00 100.35 ? 2219 GLY A C     1 
ATOM   4655  O O     . GLY A 1 2219 ? 175.256 195.230 174.746 1.00 100.35 ? 2219 GLY A O     1 
ATOM   4656  N N     . LEU A 1 2220 ? 173.584 196.648 175.206 1.00 95.42  ? 2220 LEU A N     1 
ATOM   4657  C CA    . LEU A 1 2220 ? 173.263 196.001 176.465 1.00 95.42  ? 2220 LEU A CA    1 
ATOM   4658  C C     . LEU A 1 2220 ? 172.121 195.021 176.262 1.00 95.42  ? 2220 LEU A C     1 
ATOM   4659  O O     . LEU A 1 2220 ? 171.373 195.094 175.285 1.00 95.42  ? 2220 LEU A O     1 
ATOM   4660  C CB    . LEU A 1 2220 ? 172.902 197.033 177.534 1.00 95.42  ? 2220 LEU A CB    1 
ATOM   4661  C CG    . LEU A 1 2220 ? 173.575 198.396 177.392 1.00 95.42  ? 2220 LEU A CG    1 
ATOM   4662  C CD1   . LEU A 1 2220 ? 173.119 199.311 178.512 1.00 95.42  ? 2220 LEU A CD1   1 
ATOM   4663  C CD2   . LEU A 1 2220 ? 175.076 198.284 177.367 1.00 95.42  ? 2220 LEU A CD2   1 
ATOM   4664  N N     . MET A 1 2221 ? 172.014 194.070 177.187 1.00 94.02  ? 2221 MET A N     1 
ATOM   4665  C CA    . MET A 1 2221 ? 170.992 193.031 177.128 1.00 94.02  ? 2221 MET A CA    1 
ATOM   4666  C C     . MET A 1 2221 ? 170.056 193.301 178.302 1.00 94.02  ? 2221 MET A C     1 
ATOM   4667  O O     . MET A 1 2221 ? 170.498 193.288 179.454 1.00 94.02  ? 2221 MET A O     1 
ATOM   4668  C CB    . MET A 1 2221 ? 171.596 191.630 177.280 1.00 94.02  ? 2221 MET A CB    1 
ATOM   4669  C CG    . MET A 1 2221 ? 171.937 190.763 176.057 1.00 94.02  ? 2221 MET A CG    1 
ATOM   4670  S SD    . MET A 1 2221 ? 170.772 190.559 174.739 1.00 94.02  ? 2221 MET A SD    1 
ATOM   4671  C CE    . MET A 1 2221 ? 171.332 191.993 173.834 1.00 94.02  ? 2221 MET A CE    1 
ATOM   4672  N N     . MET A 1 2222 ? 168.769 193.522 178.043 1.00 85.50  ? 2222 MET A N     1 
ATOM   4673  C CA    . MET A 1 2222 ? 167.779 193.590 179.116 1.00 85.50  ? 2222 MET A CA    1 
ATOM   4674  C C     . MET A 1 2222 ? 166.937 192.324 179.041 1.00 85.50  ? 2222 MET A C     1 
ATOM   4675  O O     . MET A 1 2222 ? 166.226 192.102 178.057 1.00 85.50  ? 2222 MET A O     1 
ATOM   4676  C CB    . MET A 1 2222 ? 166.914 194.844 179.022 1.00 85.50  ? 2222 MET A CB    1 
ATOM   4677  C CG    . MET A 1 2222 ? 167.702 196.130 178.883 1.00 85.50  ? 2222 MET A CG    1 
ATOM   4678  S SD    . MET A 1 2222 ? 166.765 197.440 178.080 1.00 85.50  ? 2222 MET A SD    1 
ATOM   4679  C CE    . MET A 1 2222 ? 166.327 196.650 176.541 1.00 85.50  ? 2222 MET A CE    1 
ATOM   4680  N N     . VAL A 1 2223 ? 167.027 191.485 180.070 1.00 79.89  ? 2223 VAL A N     1 
ATOM   4681  C CA    . VAL A 1 2223 ? 166.449 190.149 180.032 1.00 79.89  ? 2223 VAL A CA    1 
ATOM   4682  C C     . VAL A 1 2223 ? 165.695 189.887 181.328 1.00 79.89  ? 2223 VAL A C     1 
ATOM   4683  O O     . VAL A 1 2223 ? 166.163 190.246 182.414 1.00 79.89  ? 2223 VAL A O     1 
ATOM   4684  C CB    . VAL A 1 2223 ? 167.536 189.079 179.808 1.00 79.89  ? 2223 VAL A CB    1 
ATOM   4685  C CG1   . VAL A 1 2223 ? 166.994 187.692 180.092 1.00 79.89  ? 2223 VAL A CG1   1 
ATOM   4686  C CG2   . VAL A 1 2223 ? 168.078 189.170 178.406 1.00 79.89  ? 2223 VAL A CG2   1 
ATOM   4687  N N     . GLY A 1 2224 ? 164.523 189.265 181.210 1.00 79.56  ? 2224 GLY A N     1 
ATOM   4688  C CA    . GLY A 1 2224 ? 163.751 188.845 182.355 1.00 79.56  ? 2224 GLY A CA    1 
ATOM   4689  C C     . GLY A 1 2224 ? 162.516 188.066 181.951 1.00 79.56  ? 2224 GLY A C     1 
ATOM   4690  O O     . GLY A 1 2224 ? 162.135 188.034 180.778 1.00 79.56  ? 2224 GLY A O     1 
ATOM   4691  N N     . PRO A 1 2225 ? 161.869 187.415 182.916 1.00 78.77  ? 2225 PRO A N     1 
ATOM   4692  C CA    . PRO A 1 2225 ? 160.610 186.730 182.616 1.00 78.77  ? 2225 PRO A CA    1 
ATOM   4693  C C     . PRO A 1 2225 ? 159.578 187.718 182.104 1.00 78.77  ? 2225 PRO A C     1 
ATOM   4694  O O     . PRO A 1 2225 ? 159.570 188.891 182.480 1.00 78.77  ? 2225 PRO A O     1 
ATOM   4695  C CB    . PRO A 1 2225 ? 160.193 186.139 183.966 1.00 78.77  ? 2225 PRO A CB    1 
ATOM   4696  C CG    . PRO A 1 2225 ? 161.447 186.042 184.738 1.00 78.77  ? 2225 PRO A CG    1 
ATOM   4697  C CD    . PRO A 1 2225 ? 162.285 187.207 184.310 1.00 78.77  ? 2225 PRO A CD    1 
ATOM   4698  N N     . SER A 1 2226 ? 158.716 187.234 181.215 1.00 81.25  ? 2226 SER A N     1 
ATOM   4699  C CA    . SER A 1 2226 ? 157.691 188.090 180.639 1.00 81.25  ? 2226 SER A CA    1 
ATOM   4700  C C     . SER A 1 2226 ? 156.805 188.658 181.736 1.00 81.25  ? 2226 SER A C     1 
ATOM   4701  O O     . SER A 1 2226 ? 156.342 187.930 182.618 1.00 81.25  ? 2226 SER A O     1 
ATOM   4702  C CB    . SER A 1 2226 ? 156.853 187.309 179.632 1.00 81.25  ? 2226 SER A CB    1 
ATOM   4703  O OG    . SER A 1 2226 ? 155.645 187.992 179.350 1.00 81.25  ? 2226 SER A OG    1 
ATOM   4704  N N     . GLY A 1 2227 ? 156.570 189.963 181.680 1.00 78.80  ? 2227 GLY A N     1 
ATOM   4705  C CA    . GLY A 1 2227 ? 155.823 190.649 182.707 1.00 78.80  ? 2227 GLY A CA    1 
ATOM   4706  C C     . GLY A 1 2227 ? 156.670 191.401 183.710 1.00 78.80  ? 2227 GLY A C     1 
ATOM   4707  O O     . GLY A 1 2227 ? 156.114 192.099 184.564 1.00 78.80  ? 2227 GLY A O     1 
ATOM   4708  N N     . SER A 1 2228 ? 157.991 191.275 183.640 1.00 76.93  ? 2228 SER A N     1 
ATOM   4709  C CA    . SER A 1 2228 ? 158.850 192.048 184.519 1.00 76.93  ? 2228 SER A CA    1 
ATOM   4710  C C     . SER A 1 2228 ? 159.009 193.470 183.995 1.00 76.93  ? 2228 SER A C     1 
ATOM   4711  O O     . SER A 1 2228 ? 158.629 193.797 182.867 1.00 76.93  ? 2228 SER A O     1 
ATOM   4712  C CB    . SER A 1 2228 ? 160.220 191.394 184.653 1.00 76.93  ? 2228 SER A CB    1 
ATOM   4713  O OG    . SER A 1 2228 ? 161.163 192.327 185.147 1.00 76.93  ? 2228 SER A OG    1 
ATOM   4714  N N     . GLY A 1 2229 ? 159.593 194.318 184.832 1.00 76.24  ? 2229 GLY A N     1 
ATOM   4715  C CA    . GLY A 1 2229 ? 159.750 195.714 184.485 1.00 76.24  ? 2229 GLY A CA    1 
ATOM   4716  C C     . GLY A 1 2229 ? 160.949 195.975 183.603 1.00 76.24  ? 2229 GLY A C     1 
ATOM   4717  O O     . GLY A 1 2229 ? 161.958 196.503 184.075 1.00 76.24  ? 2229 GLY A O     1 
ATOM   4718  N N     . LYS A 1 2230 ? 160.865 195.606 182.325 1.00 77.74  ? 2230 LYS A N     1 
ATOM   4719  C CA    . LYS A 1 2230 ? 161.975 195.801 181.401 1.00 77.74  ? 2230 LYS A CA    1 
ATOM   4720  C C     . LYS A 1 2230 ? 161.787 197.008 180.493 1.00 77.74  ? 2230 LYS A C     1 
ATOM   4721  O O     . LYS A 1 2230 ? 162.598 197.936 180.533 1.00 77.74  ? 2230 LYS A O     1 
ATOM   4722  C CB    . LYS A 1 2230 ? 162.182 194.548 180.547 1.00 77.74  ? 2230 LYS A CB    1 
ATOM   4723  C CG    . LYS A 1 2230 ? 162.658 193.349 181.326 1.00 77.74  ? 2230 LYS A CG    1 
ATOM   4724  C CD    . LYS A 1 2230 ? 162.981 192.200 180.398 1.00 77.74  ? 2230 LYS A CD    1 
ATOM   4725  C CE    . LYS A 1 2230 ? 161.729 191.661 179.751 1.00 77.74  ? 2230 LYS A CE    1 
ATOM   4726  N NZ    . LYS A 1 2230 ? 160.738 191.238 180.773 1.00 77.74  ? 2230 LYS A NZ    1 
ATOM   4727  N N     . SER A 1 2231 ? 160.729 197.015 179.678 1.00 75.26  ? 2231 SER A N     1 
ATOM   4728  C CA    . SER A 1 2231 ? 160.527 198.109 178.733 1.00 75.26  ? 2231 SER A CA    1 
ATOM   4729  C C     . SER A 1 2231 ? 160.488 199.444 179.455 1.00 75.26  ? 2231 SER A C     1 
ATOM   4730  O O     . SER A 1 2231 ? 161.244 200.370 179.135 1.00 75.26  ? 2231 SER A O     1 
ATOM   4731  C CB    . SER A 1 2231 ? 159.222 197.906 177.963 1.00 75.26  ? 2231 SER A CB    1 
ATOM   4732  O OG    . SER A 1 2231 ? 159.064 196.576 177.516 1.00 75.26  ? 2231 SER A OG    1 
ATOM   4733  N N     . MET A 1 2232 ? 159.633 199.544 180.460 1.00 75.26  ? 2232 MET A N     1 
ATOM   4734  C CA    . MET A 1 2232 ? 159.416 200.809 181.128 1.00 75.26  ? 2232 MET A CA    1 
ATOM   4735  C C     . MET A 1 2232 ? 160.563 201.174 182.060 1.00 75.26  ? 2232 MET A C     1 
ATOM   4736  O O     . MET A 1 2232 ? 160.760 202.361 182.332 1.00 75.26  ? 2232 MET A O     1 
ATOM   4737  C CB    . MET A 1 2232 ? 158.064 200.748 181.840 1.00 75.26  ? 2232 MET A CB    1 
ATOM   4738  C CG    . MET A 1 2232 ? 157.875 201.614 183.041 1.00 75.26  ? 2232 MET A CG    1 
ATOM   4739  S SD    . MET A 1 2232 ? 156.164 201.450 183.569 1.00 75.26  ? 2232 MET A SD    1 
ATOM   4740  C CE    . MET A 1 2232 ? 155.327 201.560 181.982 1.00 75.26  ? 2232 MET A CE    1 
ATOM   4741  N N     . ALA A 1 2233 ? 161.380 200.207 182.480 1.00 71.32  ? 2233 ALA A N     1 
ATOM   4742  C CA    . ALA A 1 2233 ? 162.599 200.556 183.200 1.00 71.32  ? 2233 ALA A CA    1 
ATOM   4743  C C     . ALA A 1 2233 ? 163.511 201.418 182.336 1.00 71.32  ? 2233 ALA A C     1 
ATOM   4744  O O     . ALA A 1 2233 ? 163.911 202.517 182.741 1.00 71.32  ? 2233 ALA A O     1 
ATOM   4745  C CB    . ALA A 1 2233 ? 163.326 199.294 183.655 1.00 71.32  ? 2233 ALA A CB    1 
ATOM   4746  N N     . TRP A 1 2234 ? 163.822 200.960 181.120 1.00 69.93  ? 2234 TRP A N     1 
ATOM   4747  C CA    . TRP A 1 2234 ? 164.681 201.772 180.268 1.00 69.93  ? 2234 TRP A CA    1 
ATOM   4748  C C     . TRP A 1 2234 ? 163.956 203.006 179.753 1.00 69.93  ? 2234 TRP A C     1 
ATOM   4749  O O     . TRP A 1 2234 ? 164.599 204.023 179.487 1.00 69.93  ? 2234 TRP A O     1 
ATOM   4750  C CB    . TRP A 1 2234 ? 165.253 200.956 179.106 1.00 69.93  ? 2234 TRP A CB    1 
ATOM   4751  C CG    . TRP A 1 2234 ? 164.276 200.481 178.086 1.00 69.93  ? 2234 TRP A CG    1 
ATOM   4752  C CD1   . TRP A 1 2234 ? 163.808 199.214 177.944 1.00 69.93  ? 2234 TRP A CD1   1 
ATOM   4753  C CD2   . TRP A 1 2234 ? 163.673 201.250 177.039 1.00 69.93  ? 2234 TRP A CD2   1 
ATOM   4754  N NE1   . TRP A 1 2234 ? 162.942 199.144 176.884 1.00 69.93  ? 2234 TRP A NE1   1 
ATOM   4755  C CE2   . TRP A 1 2234 ? 162.841 200.383 176.313 1.00 69.93  ? 2234 TRP A CE2   1 
ATOM   4756  C CE3   . TRP A 1 2234 ? 163.751 202.587 176.649 1.00 69.93  ? 2234 TRP A CE3   1 
ATOM   4757  C CZ2   . TRP A 1 2234 ? 162.091 200.809 175.225 1.00 69.93  ? 2234 TRP A CZ2   1 
ATOM   4758  C CZ3   . TRP A 1 2234 ? 163.004 203.007 175.574 1.00 69.93  ? 2234 TRP A CZ3   1 
ATOM   4759  C CH2   . TRP A 1 2234 ? 162.187 202.122 174.871 1.00 69.93  ? 2234 TRP A CH2   1 
ATOM   4760  N N     . ARG A 1 2235 ? 162.630 202.952 179.608 1.00 71.96  ? 2235 ARG A N     1 
ATOM   4761  C CA    . ARG A 1 2235 ? 161.897 204.161 179.241 1.00 71.96  ? 2235 ARG A CA    1 
ATOM   4762  C C     . ARG A 1 2235 ? 162.082 205.250 180.291 1.00 71.96  ? 2235 ARG A C     1 
ATOM   4763  O O     . ARG A 1 2235 ? 162.398 206.405 179.969 1.00 71.96  ? 2235 ARG A O     1 
ATOM   4764  C CB    . ARG A 1 2235 ? 160.414 203.844 179.065 1.00 71.96  ? 2235 ARG A CB    1 
ATOM   4765  C CG    . ARG A 1 2235 ? 160.060 203.224 177.733 1.00 71.96  ? 2235 ARG A CG    1 
ATOM   4766  C CD    . ARG A 1 2235 ? 158.736 203.756 177.220 1.00 71.96  ? 2235 ARG A CD    1 
ATOM   4767  N NE    . ARG A 1 2235 ? 158.294 203.038 176.033 1.00 71.96  ? 2235 ARG A NE    1 
ATOM   4768  C CZ    . ARG A 1 2235 ? 157.690 201.859 176.058 1.00 71.96  ? 2235 ARG A CZ    1 
ATOM   4769  N NH1   . ARG A 1 2235 ? 157.422 201.246 177.197 1.00 71.96  ? 2235 ARG A NH1   1 
ATOM   4770  N NH2   . ARG A 1 2235 ? 157.346 201.282 174.911 1.00 71.96  ? 2235 ARG A NH2   1 
ATOM   4771  N N     . VAL A 1 2236 ? 161.898 204.892 181.560 1.00 69.00  ? 2236 VAL A N     1 
ATOM   4772  C CA    . VAL A 1 2236 ? 162.059 205.855 182.638 1.00 69.00  ? 2236 VAL A CA    1 
ATOM   4773  C C     . VAL A 1 2236 ? 163.504 206.314 182.724 1.00 69.00  ? 2236 VAL A C     1 
ATOM   4774  O O     . VAL A 1 2236 ? 163.779 207.490 182.982 1.00 69.00  ? 2236 VAL A O     1 
ATOM   4775  C CB    . VAL A 1 2236 ? 161.570 205.248 183.961 1.00 69.00  ? 2236 VAL A CB    1 
ATOM   4776  C CG1   . VAL A 1 2236 ? 161.917 206.147 185.112 1.00 69.00  ? 2236 VAL A CG1   1 
ATOM   4777  C CG2   . VAL A 1 2236 ? 160.080 205.044 183.905 1.00 69.00  ? 2236 VAL A CG2   1 
ATOM   4778  N N     . LEU A 1 2237 ? 164.451 205.402 182.500 1.00 74.95  ? 2237 LEU A N     1 
ATOM   4779  C CA    . LEU A 1 2237 ? 165.852 205.803 182.514 1.00 74.95  ? 2237 LEU A CA    1 
ATOM   4780  C C     . LEU A 1 2237 ? 166.142 206.814 181.415 1.00 74.95  ? 2237 LEU A C     1 
ATOM   4781  O O     . LEU A 1 2237 ? 166.855 207.797 181.640 1.00 74.95  ? 2237 LEU A O     1 
ATOM   4782  C CB    . LEU A 1 2237 ? 166.756 204.581 182.367 1.00 74.95  ? 2237 LEU A CB    1 
ATOM   4783  C CG    . LEU A 1 2237 ? 168.115 204.840 181.722 1.00 74.95  ? 2237 LEU A CG    1 
ATOM   4784  C CD1   . LEU A 1 2237 ? 169.026 205.538 182.712 1.00 74.95  ? 2237 LEU A CD1   1 
ATOM   4785  C CD2   . LEU A 1 2237 ? 168.735 203.544 181.251 1.00 74.95  ? 2237 LEU A CD2   1 
ATOM   4786  N N     . LEU A 1 2238 ? 165.597 206.591 180.219 1.00 74.68  ? 2238 LEU A N     1 
ATOM   4787  C CA    . LEU A 1 2238 ? 165.821 207.518 179.117 1.00 74.68  ? 2238 LEU A CA    1 
ATOM   4788  C C     . LEU A 1 2238 ? 165.232 208.887 179.419 1.00 74.68  ? 2238 LEU A C     1 
ATOM   4789  O O     . LEU A 1 2238 ? 165.871 209.916 179.169 1.00 74.68  ? 2238 LEU A O     1 
ATOM   4790  C CB    . LEU A 1 2238 ? 165.225 206.957 177.830 1.00 74.68  ? 2238 LEU A CB    1 
ATOM   4791  C CG    . LEU A 1 2238 ? 165.481 207.801 176.587 1.00 74.68  ? 2238 LEU A CG    1 
ATOM   4792  C CD1   . LEU A 1 2238 ? 166.964 207.860 176.313 1.00 74.68  ? 2238 LEU A CD1   1 
ATOM   4793  C CD2   . LEU A 1 2238 ? 164.740 207.228 175.399 1.00 74.68  ? 2238 LEU A CD2   1 
ATOM   4794  N N     . LYS A 1 2239 ? 164.014 208.924 179.961 1.00 71.09  ? 2239 LYS A N     1 
ATOM   4795  C CA    . LYS A 1 2239 ? 163.424 210.219 180.282 1.00 71.09  ? 2239 LYS A CA    1 
ATOM   4796  C C     . LYS A 1 2239 ? 164.196 210.921 181.392 1.00 71.09  ? 2239 LYS A C     1 
ATOM   4797  O O     . LYS A 1 2239 ? 164.377 212.144 181.354 1.00 71.09  ? 2239 LYS A O     1 
ATOM   4798  C CB    . LYS A 1 2239 ? 161.953 210.060 180.654 1.00 71.09  ? 2239 LYS A CB    1 
ATOM   4799  C CG    . LYS A 1 2239 ? 161.037 210.155 179.452 1.00 71.09  ? 2239 LYS A CG    1 
ATOM   4800  C CD    . LYS A 1 2239 ? 159.579 210.133 179.846 1.00 71.09  ? 2239 LYS A CD    1 
ATOM   4801  C CE    . LYS A 1 2239 ? 158.720 209.724 178.665 1.00 71.09  ? 2239 LYS A CE    1 
ATOM   4802  N NZ    . LYS A 1 2239 ? 159.449 208.782 177.770 1.00 71.09  ? 2239 LYS A NZ    1 
ATOM   4803  N N     . ALA A 1 2240 ? 164.668 210.165 182.385 1.00 78.07  ? 2240 ALA A N     1 
ATOM   4804  C CA    . ALA A 1 2240 ? 165.463 210.767 183.447 1.00 78.07  ? 2240 ALA A CA    1 
ATOM   4805  C C     . ALA A 1 2240 ? 166.774 211.318 182.907 1.00 78.07  ? 2240 ALA A C     1 
ATOM   4806  O O     . ALA A 1 2240 ? 167.222 212.388 183.330 1.00 78.07  ? 2240 ALA A O     1 
ATOM   4807  C CB    . ALA A 1 2240 ? 165.723 209.748 184.553 1.00 78.07  ? 2240 ALA A CB    1 
ATOM   4808  N N     . LEU A 1 2241 ? 167.407 210.600 181.978 1.00 79.38  ? 2241 LEU A N     1 
ATOM   4809  C CA    . LEU A 1 2241 ? 168.619 211.117 181.355 1.00 79.38  ? 2241 LEU A CA    1 
ATOM   4810  C C     . LEU A 1 2241 ? 168.334 212.390 180.579 1.00 79.38  ? 2241 LEU A C     1 
ATOM   4811  O O     . LEU A 1 2241 ? 169.112 213.350 180.636 1.00 79.38  ? 2241 LEU A O     1 
ATOM   4812  C CB    . LEU A 1 2241 ? 169.236 210.066 180.438 1.00 79.38  ? 2241 LEU A CB    1 
ATOM   4813  C CG    . LEU A 1 2241 ? 170.112 209.043 181.146 1.00 79.38  ? 2241 LEU A CG    1 
ATOM   4814  C CD1   . LEU A 1 2241 ? 171.058 208.397 180.159 1.00 79.38  ? 2241 LEU A CD1   1 
ATOM   4815  C CD2   . LEU A 1 2241 ? 170.879 209.724 182.257 1.00 79.38  ? 2241 LEU A CD2   1 
ATOM   4816  N N     . GLU A 1 2242 ? 167.223 212.418 179.846 1.00 87.56  ? 2242 GLU A N     1 
ATOM   4817  C CA    . GLU A 1 2242 ? 166.885 213.613 179.085 1.00 87.56  ? 2242 GLU A CA    1 
ATOM   4818  C C     . GLU A 1 2242 ? 166.669 214.804 180.005 1.00 87.56  ? 2242 GLU A C     1 
ATOM   4819  O O     . GLU A 1 2242 ? 167.128 215.914 179.716 1.00 87.56  ? 2242 GLU A O     1 
ATOM   4820  C CB    . GLU A 1 2242 ? 165.645 213.358 178.232 1.00 87.56  ? 2242 GLU A CB    1 
ATOM   4821  C CG    . GLU A 1 2242 ? 165.128 214.582 177.508 1.00 87.56  ? 2242 GLU A CG    1 
ATOM   4822  C CD    . GLU A 1 2242 ? 163.753 214.361 176.917 1.00 87.56  ? 2242 GLU A CD    1 
ATOM   4823  O OE1   . GLU A 1 2242 ? 163.596 213.417 176.116 1.00 87.56  ? 2242 GLU A OE1   1 
ATOM   4824  O OE2   . GLU A 1 2242 ? 162.827 215.127 177.257 1.00 87.56  ? 2242 GLU A OE2   1 
ATOM   4825  N N     . ARG A 1 2243 ? 165.981 214.593 181.126 1.00 85.84  ? 2243 ARG A N     1 
ATOM   4826  C CA    . ARG A 1 2243 ? 165.716 215.705 182.030 1.00 85.84  ? 2243 ARG A CA    1 
ATOM   4827  C C     . ARG A 1 2243 ? 166.955 216.111 182.817 1.00 85.84  ? 2243 ARG A C     1 
ATOM   4828  O O     . ARG A 1 2243 ? 167.085 217.277 183.204 1.00 85.84  ? 2243 ARG A O     1 
ATOM   4829  C CB    . ARG A 1 2243 ? 164.576 215.352 182.981 1.00 85.84  ? 2243 ARG A CB    1 
ATOM   4830  C CG    . ARG A 1 2243 ? 163.206 215.343 182.331 1.00 85.84  ? 2243 ARG A CG    1 
ATOM   4831  C CD    . ARG A 1 2243 ? 162.190 214.694 183.243 1.00 85.84  ? 2243 ARG A CD    1 
ATOM   4832  N NE    . ARG A 1 2243 ? 162.269 215.237 184.593 1.00 85.84  ? 2243 ARG A NE    1 
ATOM   4833  C CZ    . ARG A 1 2243 ? 161.240 215.742 185.257 1.00 85.84  ? 2243 ARG A CZ    1 
ATOM   4834  N NH1   . ARG A 1 2243 ? 160.027 215.778 184.729 1.00 85.84  ? 2243 ARG A NH1   1 
ATOM   4835  N NH2   . ARG A 1 2243 ? 161.431 216.221 186.483 1.00 85.84  ? 2243 ARG A NH2   1 
ATOM   4836  N N     . LEU A 1 2244 ? 167.871 215.176 183.068 1.00 85.46  ? 2244 LEU A N     1 
ATOM   4837  C CA    . LEU A 1 2244 ? 169.047 215.481 183.875 1.00 85.46  ? 2244 LEU A CA    1 
ATOM   4838  C C     . LEU A 1 2244 ? 170.145 216.133 183.045 1.00 85.46  ? 2244 LEU A C     1 
ATOM   4839  O O     . LEU A 1 2244 ? 170.551 217.268 183.313 1.00 85.46  ? 2244 LEU A O     1 
ATOM   4840  C CB    . LEU A 1 2244 ? 169.571 214.207 184.537 1.00 85.46  ? 2244 LEU A CB    1 
ATOM   4841  C CG    . LEU A 1 2244 ? 170.938 214.347 185.199 1.00 85.46  ? 2244 LEU A CG    1 
ATOM   4842  C CD1   . LEU A 1 2244 ? 170.804 215.024 186.547 1.00 85.46  ? 2244 LEU A CD1   1 
ATOM   4843  C CD2   . LEU A 1 2244 ? 171.590 212.988 185.341 1.00 85.46  ? 2244 LEU A CD2   1 
ATOM   4844  N N     . GLU A 1 2245 ? 170.642 215.424 182.033 1.00 95.95  ? 2245 GLU A N     1 
ATOM   4845  C CA    . GLU A 1 2245 ? 171.717 215.945 181.201 1.00 95.95  ? 2245 GLU A CA    1 
ATOM   4846  C C     . GLU A 1 2245 ? 171.241 216.971 180.186 1.00 95.95  ? 2245 GLU A C     1 
ATOM   4847  O O     . GLU A 1 2245 ? 172.076 217.644 179.575 1.00 95.95  ? 2245 GLU A O     1 
ATOM   4848  C CB    . GLU A 1 2245 ? 172.422 214.799 180.472 1.00 95.95  ? 2245 GLU A CB    1 
ATOM   4849  C CG    . GLU A 1 2245 ? 173.083 213.797 181.401 1.00 95.95  ? 2245 GLU A CG    1 
ATOM   4850  C CD    . GLU A 1 2245 ? 173.861 212.733 180.653 1.00 95.95  ? 2245 GLU A CD    1 
ATOM   4851  O OE1   . GLU A 1 2245 ? 173.812 212.727 179.405 1.00 95.95  ? 2245 GLU A OE1   1 
ATOM   4852  O OE2   . GLU A 1 2245 ? 174.522 211.905 181.314 1.00 95.95  ? 2245 GLU A OE2   1 
ATOM   4853  N N     . GLY A 1 2246 ? 169.934 217.110 179.993 1.00 96.75  ? 2246 GLY A N     1 
ATOM   4854  C CA    . GLY A 1 2246 ? 169.423 218.033 179.006 1.00 96.75  ? 2246 GLY A CA    1 
ATOM   4855  C C     . GLY A 1 2246 ? 169.512 217.545 177.581 1.00 96.75  ? 2246 GLY A C     1 
ATOM   4856  O O     . GLY A 1 2246 ? 169.159 218.293 176.663 1.00 96.75  ? 2246 GLY A O     1 
ATOM   4857  N N     . VAL A 1 2247 ? 169.964 216.315 177.365 1.00 99.54  ? 2247 VAL A N     1 
ATOM   4858  C CA    . VAL A 1 2247 ? 170.098 215.748 176.030 1.00 99.54  ? 2247 VAL A CA    1 
ATOM   4859  C C     . VAL A 1 2247 ? 168.802 215.028 175.695 1.00 99.54  ? 2247 VAL A C     1 
ATOM   4860  O O     . VAL A 1 2247 ? 168.408 214.086 176.393 1.00 99.54  ? 2247 VAL A O     1 
ATOM   4861  C CB    . VAL A 1 2247 ? 171.297 214.793 175.941 1.00 99.54  ? 2247 VAL A CB    1 
ATOM   4862  C CG1   . VAL A 1 2247 ? 171.493 214.322 174.509 1.00 99.54  ? 2247 VAL A CG1   1 
ATOM   4863  C CG2   . VAL A 1 2247 ? 172.551 215.468 176.467 1.00 99.54  ? 2247 VAL A CG2   1 
ATOM   4864  N N     . GLU A 1 2248 ? 168.138 215.470 174.632 1.00 101.28 ? 2248 GLU A N     1 
ATOM   4865  C CA    . GLU A 1 2248 ? 166.904 214.827 174.210 1.00 101.28 ? 2248 GLU A CA    1 
ATOM   4866  C C     . GLU A 1 2248 ? 167.163 213.367 173.872 1.00 101.28 ? 2248 GLU A C     1 
ATOM   4867  O O     . GLU A 1 2248 ? 168.111 213.040 173.154 1.00 101.28 ? 2248 GLU A O     1 
ATOM   4868  C CB    . GLU A 1 2248 ? 166.320 215.558 173.003 1.00 101.28 ? 2248 GLU A CB    1 
ATOM   4869  C CG    . GLU A 1 2248 ? 165.404 214.707 172.148 1.00 101.28 ? 2248 GLU A CG    1 
ATOM   4870  C CD    . GLU A 1 2248 ? 164.411 215.536 171.366 1.00 101.28 ? 2248 GLU A CD    1 
ATOM   4871  O OE1   . GLU A 1 2248 ? 164.743 216.687 171.018 1.00 101.28 ? 2248 GLU A OE1   1 
ATOM   4872  O OE2   . GLU A 1 2248 ? 163.300 215.036 171.095 1.00 101.28 ? 2248 GLU A OE2   1 
ATOM   4873  N N     . GLY A 1 2249 ? 166.320 212.486 174.403 1.00 97.18  ? 2249 GLY A N     1 
ATOM   4874  C CA    . GLY A 1 2249 ? 166.429 211.058 174.171 1.00 97.18  ? 2249 GLY A CA    1 
ATOM   4875  C C     . GLY A 1 2249 ? 165.320 210.583 173.248 1.00 97.18  ? 2249 GLY A C     1 
ATOM   4876  O O     . GLY A 1 2249 ? 164.155 210.939 173.428 1.00 97.18  ? 2249 GLY A O     1 
ATOM   4877  N N     . VAL A 1 2250 ? 165.703 209.790 172.255 1.00 91.89  ? 2250 VAL A N     1 
ATOM   4878  C CA    . VAL A 1 2250 ? 164.767 209.209 171.305 1.00 91.89  ? 2250 VAL A CA    1 
ATOM   4879  C C     . VAL A 1 2250 ? 165.049 207.719 171.215 1.00 91.89  ? 2250 VAL A C     1 
ATOM   4880  O O     . VAL A 1 2250 ? 166.196 207.314 170.994 1.00 91.89  ? 2250 VAL A O     1 
ATOM   4881  C CB    . VAL A 1 2250 ? 164.875 209.879 169.925 1.00 91.89  ? 2250 VAL A CB    1 
ATOM   4882  C CG1   . VAL A 1 2250 ? 164.321 208.969 168.846 1.00 91.89  ? 2250 VAL A CG1   1 
ATOM   4883  C CG2   . VAL A 1 2250 ? 164.142 211.208 169.936 1.00 91.89  ? 2250 VAL A CG2   1 
ATOM   4884  N N     . ALA A 1 2251 ? 164.009 206.909 171.386 1.00 85.32  ? 2251 ALA A N     1 
ATOM   4885  C CA    . ALA A 1 2251 ? 164.124 205.458 171.359 1.00 85.32  ? 2251 ALA A CA    1 
ATOM   4886  C C     . ALA A 1 2251 ? 163.354 204.912 170.168 1.00 85.32  ? 2251 ALA A C     1 
ATOM   4887  O O     . ALA A 1 2251 ? 162.214 205.317 169.922 1.00 85.32  ? 2251 ALA A O     1 
ATOM   4888  C CB    . ALA A 1 2251 ? 163.599 204.843 172.654 1.00 85.32  ? 2251 ALA A CB    1 
ATOM   4889  N N     . HIS A 1 2252 ? 163.976 203.998 169.434 1.00 88.91  ? 2252 HIS A N     1 
ATOM   4890  C CA    . HIS A 1 2252 ? 163.360 203.350 168.283 1.00 88.91  ? 2252 HIS A CA    1 
ATOM   4891  C C     . HIS A 1 2252 ? 163.161 201.880 168.620 1.00 88.91  ? 2252 HIS A C     1 
ATOM   4892  O O     . HIS A 1 2252 ? 164.134 201.126 168.725 1.00 88.91  ? 2252 HIS A O     1 
ATOM   4893  C CB    . HIS A 1 2252 ? 164.224 203.517 167.037 1.00 88.91  ? 2252 HIS A CB    1 
ATOM   4894  C CG    . HIS A 1 2252 ? 164.564 204.940 166.728 1.00 88.91  ? 2252 HIS A CG    1 
ATOM   4895  N ND1   . HIS A 1 2252 ? 163.706 205.780 166.052 1.00 88.91  ? 2252 HIS A ND1   1 
ATOM   4896  C CD2   . HIS A 1 2252 ? 165.665 205.675 167.009 1.00 88.91  ? 2252 HIS A CD2   1 
ATOM   4897  C CE1   . HIS A 1 2252 ? 164.267 206.969 165.926 1.00 88.91  ? 2252 HIS A CE1   1 
ATOM   4898  N NE2   . HIS A 1 2252 ? 165.456 206.932 166.498 1.00 88.91  ? 2252 HIS A NE2   1 
ATOM   4899  N N     . ILE A 1 2253 ? 161.908 201.473 168.782 1.00 89.49  ? 2253 ILE A N     1 
ATOM   4900  C CA    . ILE A 1 2253 ? 161.563 200.104 169.141 1.00 89.49  ? 2253 ILE A CA    1 
ATOM   4901  C C     . ILE A 1 2253 ? 161.266 199.340 167.861 1.00 89.49  ? 2253 ILE A C     1 
ATOM   4902  O O     . ILE A 1 2253 ? 160.437 199.767 167.049 1.00 89.49  ? 2253 ILE A O     1 
ATOM   4903  C CB    . ILE A 1 2253 ? 160.369 200.059 170.104 1.00 89.49  ? 2253 ILE A CB    1 
ATOM   4904  C CG1   . ILE A 1 2253 ? 160.461 201.204 171.110 1.00 89.49  ? 2253 ILE A CG1   1 
ATOM   4905  C CG2   . ILE A 1 2253 ? 160.326 198.731 170.823 1.00 89.49  ? 2253 ILE A CG2   1 
ATOM   4906  C CD1   . ILE A 1 2253 ? 159.271 201.297 172.032 1.00 89.49  ? 2253 ILE A CD1   1 
ATOM   4907  N N     . ILE A 1 2254 ? 161.946 198.214 167.676 1.00 88.03  ? 2254 ILE A N     1 
ATOM   4908  C CA    . ILE A 1 2254 ? 161.842 197.417 166.463 1.00 88.03  ? 2254 ILE A CA    1 
ATOM   4909  C C     . ILE A 1 2254 ? 161.782 195.946 166.848 1.00 88.03  ? 2254 ILE A C     1 
ATOM   4910  O O     . ILE A 1 2254 ? 162.572 195.485 167.678 1.00 88.03  ? 2254 ILE A O     1 
ATOM   4911  C CB    . ILE A 1 2254 ? 163.022 197.694 165.514 1.00 88.03  ? 2254 ILE A CB    1 
ATOM   4912  C CG1   . ILE A 1 2254 ? 163.014 196.726 164.335 1.00 88.03  ? 2254 ILE A CG1   1 
ATOM   4913  C CG2   . ILE A 1 2254 ? 164.336 197.665 166.266 1.00 88.03  ? 2254 ILE A CG2   1 
ATOM   4914  C CD1   . ILE A 1 2254 ? 164.086 197.020 163.324 1.00 88.03  ? 2254 ILE A CD1   1 
ATOM   4915  N N     . ASP A 1 2255 ? 160.841 195.213 166.253 1.00 90.49  ? 2255 ASP A N     1 
ATOM   4916  C CA    . ASP A 1 2255 ? 160.678 193.796 166.540 1.00 90.49  ? 2255 ASP A CA    1 
ATOM   4917  C C     . ASP A 1 2255 ? 161.328 192.978 165.440 1.00 90.49  ? 2255 ASP A C     1 
ATOM   4918  O O     . ASP A 1 2255 ? 160.881 193.048 164.285 1.00 90.49  ? 2255 ASP A O     1 
ATOM   4919  C CB    . ASP A 1 2255 ? 159.203 193.436 166.663 1.00 90.49  ? 2255 ASP A CB    1 
ATOM   4920  C CG    . ASP A 1 2255 ? 158.974 192.203 167.514 1.00 90.49  ? 2255 ASP A CG    1 
ATOM   4921  O OD1   . ASP A 1 2255 ? 159.538 191.140 167.184 1.00 90.49  ? 2255 ASP A OD1   1 
ATOM   4922  O OD2   . ASP A 1 2255 ? 158.228 192.297 168.511 1.00 90.49  ? 2255 ASP A OD2   1 
ATOM   4923  N N     . PRO A 1 2256 ? 162.356 192.197 165.735 1.00 90.97  ? 2256 PRO A N     1 
ATOM   4924  C CA    . PRO A 1 2256 ? 163.055 191.468 164.672 1.00 90.97  ? 2256 PRO A CA    1 
ATOM   4925  C C     . PRO A 1 2256 ? 162.219 190.360 164.060 1.00 90.97  ? 2256 PRO A C     1 
ATOM   4926  O O     . PRO A 1 2256 ? 162.126 190.257 162.834 1.00 90.97  ? 2256 PRO A O     1 
ATOM   4927  C CB    . PRO A 1 2256 ? 164.286 190.906 165.389 1.00 90.97  ? 2256 PRO A CB    1 
ATOM   4928  C CG    . PRO A 1 2256 ? 163.871 190.794 166.805 1.00 90.97  ? 2256 PRO A CG    1 
ATOM   4929  C CD    . PRO A 1 2256 ? 162.932 191.932 167.062 1.00 90.97  ? 2256 PRO A CD    1 
ATOM   4930  N N     . LYS A 1 2257 ? 161.598 189.527 164.896 1.00 89.43  ? 2257 LYS A N     1 
ATOM   4931  C CA    . LYS A 1 2257 ? 160.849 188.390 164.377 1.00 89.43  ? 2257 LYS A CA    1 
ATOM   4932  C C     . LYS A 1 2257 ? 159.589 188.810 163.638 1.00 89.43  ? 2257 LYS A C     1 
ATOM   4933  O O     . LYS A 1 2257 ? 159.046 188.013 162.867 1.00 89.43  ? 2257 LYS A O     1 
ATOM   4934  C CB    . LYS A 1 2257 ? 160.490 187.429 165.509 1.00 89.43  ? 2257 LYS A CB    1 
ATOM   4935  C CG    . LYS A 1 2257 ? 161.672 186.993 166.345 1.00 89.43  ? 2257 LYS A CG    1 
ATOM   4936  C CD    . LYS A 1 2257 ? 162.783 186.461 165.463 1.00 89.43  ? 2257 LYS A CD    1 
ATOM   4937  C CE    . LYS A 1 2257 ? 162.541 185.013 165.091 1.00 89.43  ? 2257 LYS A CE    1 
ATOM   4938  N NZ    . LYS A 1 2257 ? 162.971 184.090 166.171 1.00 89.43  ? 2257 LYS A NZ    1 
ATOM   4939  N N     . ALA A 1 2258 ? 159.114 190.037 163.852 1.00 90.90  ? 2258 ALA A N     1 
ATOM   4940  C CA    . ALA A 1 2258 ? 157.913 190.488 163.160 1.00 90.90  ? 2258 ALA A CA    1 
ATOM   4941  C C     . ALA A 1 2258 ? 158.136 190.549 161.657 1.00 90.90  ? 2258 ALA A C     1 
ATOM   4942  O O     . ALA A 1 2258 ? 157.246 190.202 160.874 1.00 90.90  ? 2258 ALA A O     1 
ATOM   4943  C CB    . ALA A 1 2258 ? 157.480 191.851 163.693 1.00 90.90  ? 2258 ALA A CB    1 
ATOM   4944  N N     . ILE A 1 2259 ? 159.317 190.984 161.237 1.00 96.55  ? 2259 ILE A N     1 
ATOM   4945  C CA    . ILE A 1 2259 ? 159.634 191.133 159.828 1.00 96.55  ? 2259 ILE A CA    1 
ATOM   4946  C C     . ILE A 1 2259 ? 160.719 190.129 159.452 1.00 96.55  ? 2259 ILE A C     1 
ATOM   4947  O O     . ILE A 1 2259 ? 161.354 189.510 160.305 1.00 96.55  ? 2259 ILE A O     1 
ATOM   4948  C CB    . ILE A 1 2259 ? 160.062 192.571 159.485 1.00 96.55  ? 2259 ILE A CB    1 
ATOM   4949  C CG1   . ILE A 1 2259 ? 161.296 192.958 160.295 1.00 96.55  ? 2259 ILE A CG1   1 
ATOM   4950  C CG2   . ILE A 1 2259 ? 158.926 193.539 159.754 1.00 96.55  ? 2259 ILE A CG2   1 
ATOM   4951  C CD1   . ILE A 1 2259 ? 161.714 194.388 160.105 1.00 96.55  ? 2259 ILE A CD1   1 
ATOM   4952  N N     . SER A 1 2260 ? 160.918 189.963 158.150 1.00 108.25 ? 2260 SER A N     1 
ATOM   4953  C CA    . SER A 1 2260 ? 161.946 189.070 157.648 1.00 108.25 ? 2260 SER A CA    1 
ATOM   4954  C C     . SER A 1 2260 ? 163.331 189.681 157.842 1.00 108.25 ? 2260 SER A C     1 
ATOM   4955  O O     . SER A 1 2260 ? 163.492 190.899 157.955 1.00 108.25 ? 2260 SER A O     1 
ATOM   4956  C CB    . SER A 1 2260 ? 161.707 188.762 156.171 1.00 108.25 ? 2260 SER A CB    1 
ATOM   4957  O OG    . SER A 1 2260 ? 161.661 189.956 155.411 1.00 108.25 ? 2260 SER A OG    1 
ATOM   4958  N N     . LYS A 1 2261 ? 164.342 188.808 157.881 1.00 114.08 ? 2261 LYS A N     1 
ATOM   4959  C CA    . LYS A 1 2261 ? 165.717 189.274 158.027 1.00 114.08 ? 2261 LYS A CA    1 
ATOM   4960  C C     . LYS A 1 2261 ? 166.122 190.170 156.866 1.00 114.08 ? 2261 LYS A C     1 
ATOM   4961  O O     . LYS A 1 2261 ? 166.755 191.217 157.064 1.00 114.08 ? 2261 LYS A O     1 
ATOM   4962  C CB    . LYS A 1 2261 ? 166.669 188.083 158.126 1.00 114.08 ? 2261 LYS A CB    1 
ATOM   4963  C CG    . LYS A 1 2261 ? 168.030 188.360 157.514 1.00 114.08 ? 2261 LYS A CG    1 
ATOM   4964  C CD    . LYS A 1 2261 ? 169.130 187.550 158.156 1.00 114.08 ? 2261 LYS A CD    1 
ATOM   4965  C CE    . LYS A 1 2261 ? 170.397 187.635 157.326 1.00 114.08 ? 2261 LYS A CE    1 
ATOM   4966  N NZ    . LYS A 1 2261 ? 170.606 186.421 156.492 1.00 114.08 ? 2261 LYS A NZ    1 
ATOM   4967  N N     . ASP A 1 2262 ? 165.763 189.772 155.644 1.00 121.83 ? 2262 ASP A N     1 
ATOM   4968  C CA    . ASP A 1 2262 ? 166.099 190.576 154.477 1.00 121.83 ? 2262 ASP A CA    1 
ATOM   4969  C C     . ASP A 1 2262 ? 165.516 191.974 154.598 1.00 121.83 ? 2262 ASP A C     1 
ATOM   4970  O O     . ASP A 1 2262 ? 166.201 192.967 154.333 1.00 121.83 ? 2262 ASP A O     1 
ATOM   4971  C CB    . ASP A 1 2262 ? 165.588 189.892 153.210 1.00 121.83 ? 2262 ASP A CB    1 
ATOM   4972  C CG    . ASP A 1 2262 ? 165.987 190.629 151.952 1.00 121.83 ? 2262 ASP A CG    1 
ATOM   4973  O OD1   . ASP A 1 2262 ? 165.107 190.869 151.098 1.00 121.83 ? 2262 ASP A OD1   1 
ATOM   4974  O OD2   . ASP A 1 2262 ? 167.181 190.964 151.816 1.00 121.83 ? 2262 ASP A OD2   1 
ATOM   4975  N N     . HIS A 1 2263 ? 164.258 192.071 155.020 1.00 118.68 ? 2263 HIS A N     1 
ATOM   4976  C CA    . HIS A 1 2263 ? 163.639 193.378 155.167 1.00 118.68 ? 2263 HIS A CA    1 
ATOM   4977  C C     . HIS A 1 2263 ? 164.216 194.126 156.359 1.00 118.68 ? 2263 HIS A C     1 
ATOM   4978  O O     . HIS A 1 2263 ? 164.226 195.361 156.370 1.00 118.68 ? 2263 HIS A O     1 
ATOM   4979  C CB    . HIS A 1 2263 ? 162.130 193.214 155.307 1.00 118.68 ? 2263 HIS A CB    1 
ATOM   4980  C CG    . HIS A 1 2263 ? 161.389 193.382 154.019 1.00 118.68 ? 2263 HIS A CG    1 
ATOM   4981  N ND1   . HIS A 1 2263 ? 160.234 194.124 153.913 1.00 118.68 ? 2263 HIS A ND1   1 
ATOM   4982  C CD2   . HIS A 1 2263 ? 161.636 192.893 152.781 1.00 118.68 ? 2263 HIS A CD2   1 
ATOM   4983  C CE1   . HIS A 1 2263 ? 159.803 194.090 152.665 1.00 118.68 ? 2263 HIS A CE1   1 
ATOM   4984  N NE2   . HIS A 1 2263 ? 160.636 193.350 151.957 1.00 118.68 ? 2263 HIS A NE2   1 
ATOM   4985  N N     . LEU A 1 2264 ? 164.693 193.396 157.369 1.00 112.28 ? 2264 LEU A N     1 
ATOM   4986  C CA    . LEU A 1 2264 ? 165.322 194.034 158.520 1.00 112.28 ? 2264 LEU A CA    1 
ATOM   4987  C C     . LEU A 1 2264 ? 166.616 194.730 158.121 1.00 112.28 ? 2264 LEU A C     1 
ATOM   4988  O O     . LEU A 1 2264 ? 166.889 195.855 158.557 1.00 112.28 ? 2264 LEU A O     1 
ATOM   4989  C CB    . LEU A 1 2264 ? 165.582 192.996 159.613 1.00 112.28 ? 2264 LEU A CB    1 
ATOM   4990  C CG    . LEU A 1 2264 ? 166.577 193.368 160.713 1.00 112.28 ? 2264 LEU A CG    1 
ATOM   4991  C CD1   . LEU A 1 2264 ? 166.020 194.470 161.588 1.00 112.28 ? 2264 LEU A CD1   1 
ATOM   4992  C CD2   . LEU A 1 2264 ? 166.926 192.151 161.549 1.00 112.28 ? 2264 LEU A CD2   1 
ATOM   4993  N N     . TYR A 1 2265 ? 167.422 194.079 157.285 1.00 117.09 ? 2265 TYR A N     1 
ATOM   4994  C CA    . TYR A 1 2265 ? 168.711 194.624 156.875 1.00 117.09 ? 2265 TYR A CA    1 
ATOM   4995  C C     . TYR A 1 2265 ? 168.664 195.325 155.528 1.00 117.09 ? 2265 TYR A C     1 
ATOM   4996  O O     . TYR A 1 2265 ? 169.306 196.364 155.353 1.00 117.09 ? 2265 TYR A O     1 
ATOM   4997  C CB    . TYR A 1 2265 ? 169.761 193.515 156.819 1.00 117.09 ? 2265 TYR A CB    1 
ATOM   4998  C CG    . TYR A 1 2265 ? 170.129 192.963 158.168 1.00 117.09 ? 2265 TYR A CG    1 
ATOM   4999  C CD1   . TYR A 1 2265 ? 170.014 193.739 159.311 1.00 117.09 ? 2265 TYR A CD1   1 
ATOM   5000  C CD2   . TYR A 1 2265 ? 170.580 191.662 158.300 1.00 117.09 ? 2265 TYR A CD2   1 
ATOM   5001  C CE1   . TYR A 1 2265 ? 170.348 193.233 160.548 1.00 117.09 ? 2265 TYR A CE1   1 
ATOM   5002  C CE2   . TYR A 1 2265 ? 170.911 191.147 159.529 1.00 117.09 ? 2265 TYR A CE2   1 
ATOM   5003  C CZ    . TYR A 1 2265 ? 170.796 191.935 160.650 1.00 117.09 ? 2265 TYR A CZ    1 
ATOM   5004  O OH    . TYR A 1 2265 ? 171.131 191.413 161.875 1.00 117.09 ? 2265 TYR A OH    1 
ATOM   5005  N N     . GLY A 1 2266 ? 167.913 194.785 154.576 1.00 130.34 ? 2266 GLY A N     1 
ATOM   5006  C CA    . GLY A 1 2266 ? 167.915 195.304 153.225 1.00 130.34 ? 2266 GLY A CA    1 
ATOM   5007  C C     . GLY A 1 2266 ? 168.256 194.220 152.226 1.00 130.34 ? 2266 GLY A C     1 
ATOM   5008  O O     . GLY A 1 2266 ? 168.752 193.156 152.607 1.00 130.34 ? 2266 GLY A O     1 
ATOM   5009  N N     . THR A 1 2267 ? 168.004 194.474 150.945 1.00 145.32 ? 2267 THR A N     1 
ATOM   5010  C CA    . THR A 1 2267 ? 168.216 193.479 149.908 1.00 145.32 ? 2267 THR A CA    1 
ATOM   5011  C C     . THR A 1 2267 ? 169.047 194.065 148.778 1.00 145.32 ? 2267 THR A C     1 
ATOM   5012  O O     . THR A 1 2267 ? 168.998 195.266 148.502 1.00 145.32 ? 2267 THR A O     1 
ATOM   5013  C CB    . THR A 1 2267 ? 166.890 192.956 149.343 1.00 145.32 ? 2267 THR A CB    1 
ATOM   5014  O OG1   . THR A 1 2267 ? 167.152 192.080 148.240 1.00 145.32 ? 2267 THR A OG1   1 
ATOM   5015  C CG2   . THR A 1 2267 ? 166.020 194.106 148.872 1.00 145.32 ? 2267 THR A CG2   1 
ATOM   5016  N N     . LEU A 1 2268 ? 169.818 193.194 148.135 1.00 161.03 ? 2268 LEU A N     1 
ATOM   5017  C CA    . LEU A 1 2268 ? 170.576 193.533 146.940 1.00 161.03 ? 2268 LEU A CA    1 
ATOM   5018  C C     . LEU A 1 2268 ? 169.957 192.800 145.756 1.00 161.03 ? 2268 LEU A C     1 
ATOM   5019  O O     . LEU A 1 2268 ? 169.911 191.565 145.744 1.00 161.03 ? 2268 LEU A O     1 
ATOM   5020  C CB    . LEU A 1 2268 ? 172.046 193.152 147.106 1.00 161.03 ? 2268 LEU A CB    1 
ATOM   5021  C CG    . LEU A 1 2268 ? 173.067 193.923 146.271 1.00 161.03 ? 2268 LEU A CG    1 
ATOM   5022  C CD1   . LEU A 1 2268 ? 172.667 195.382 146.135 1.00 161.03 ? 2268 LEU A CD1   1 
ATOM   5023  C CD2   . LEU A 1 2268 ? 174.446 193.795 146.892 1.00 161.03 ? 2268 LEU A CD2   1 
ATOM   5024  N N     . ASP A 1 2269 ? 169.482 193.555 144.773 1.00 173.70 ? 2269 ASP A N     1 
ATOM   5025  C CA    . ASP A 1 2269 ? 168.824 192.942 143.629 1.00 173.70 ? 2269 ASP A CA    1 
ATOM   5026  C C     . ASP A 1 2269 ? 169.825 192.104 142.839 1.00 173.70 ? 2269 ASP A C     1 
ATOM   5027  O O     . ASP A 1 2269 ? 170.928 192.581 142.540 1.00 173.70 ? 2269 ASP A O     1 
ATOM   5028  C CB    . ASP A 1 2269 ? 168.197 194.005 142.730 1.00 173.70 ? 2269 ASP A CB    1 
ATOM   5029  C CG    . ASP A 1 2269 ? 167.526 195.107 143.518 1.00 173.70 ? 2269 ASP A CG    1 
ATOM   5030  O OD1   . ASP A 1 2269 ? 167.671 196.286 143.135 1.00 173.70 ? 2269 ASP A OD1   1 
ATOM   5031  O OD2   . ASP A 1 2269 ? 166.857 194.795 144.524 1.00 173.70 ? 2269 ASP A OD2   1 
ATOM   5032  N N     . PRO A 1 2270 ? 169.487 190.860 142.489 1.00 182.32 ? 2270 PRO A N     1 
ATOM   5033  C CA    . PRO A 1 2270 ? 170.453 190.012 141.774 1.00 182.32 ? 2270 PRO A CA    1 
ATOM   5034  C C     . PRO A 1 2270 ? 170.761 190.490 140.368 1.00 182.32 ? 2270 PRO A C     1 
ATOM   5035  O O     . PRO A 1 2270 ? 171.799 190.103 139.817 1.00 182.32 ? 2270 PRO A O     1 
ATOM   5036  C CB    . PRO A 1 2270 ? 169.771 188.633 141.756 1.00 182.32 ? 2270 PRO A CB    1 
ATOM   5037  C CG    . PRO A 1 2270 ? 168.563 188.759 142.665 1.00 182.32 ? 2270 PRO A CG    1 
ATOM   5038  C CD    . PRO A 1 2270 ? 168.184 190.198 142.634 1.00 182.32 ? 2270 PRO A CD    1 
ATOM   5039  N N     . ASN A 1 2271 ? 169.903 191.315 139.769 1.00 186.74 ? 2271 ASN A N     1 
ATOM   5040  C CA    . ASN A 1 2271 ? 170.086 191.754 138.390 1.00 186.74 ? 2271 ASN A CA    1 
ATOM   5041  C C     . ASN A 1 2271 ? 170.582 193.194 138.299 1.00 186.74 ? 2271 ASN A C     1 
ATOM   5042  O O     . ASN A 1 2271 ? 171.635 193.451 137.709 1.00 186.74 ? 2271 ASN A O     1 
ATOM   5043  C CB    . ASN A 1 2271 ? 168.773 191.580 137.615 1.00 186.74 ? 2271 ASN A CB    1 
ATOM   5044  C CG    . ASN A 1 2271 ? 167.556 191.943 138.443 1.00 186.74 ? 2271 ASN A CG    1 
ATOM   5045  O OD1   . ASN A 1 2271 ? 167.534 192.969 139.120 1.00 186.74 ? 2271 ASN A OD1   1 
ATOM   5046  N ND2   . ASN A 1 2271 ? 166.533 191.099 138.389 1.00 186.74 ? 2271 ASN A ND2   1 
ATOM   5047  N N     . THR A 1 2272 ? 169.848 194.142 138.881 1.00 181.61 ? 2272 THR A N     1 
ATOM   5048  C CA    . THR A 1 2272 ? 170.264 195.537 138.821 1.00 181.61 ? 2272 THR A CA    1 
ATOM   5049  C C     . THR A 1 2272 ? 171.355 195.877 139.825 1.00 181.61 ? 2272 THR A C     1 
ATOM   5050  O O     . THR A 1 2272 ? 171.960 196.949 139.710 1.00 181.61 ? 2272 THR A O     1 
ATOM   5051  C CB    . THR A 1 2272 ? 169.068 196.468 139.045 1.00 181.61 ? 2272 THR A CB    1 
ATOM   5052  O OG1   . THR A 1 2272 ? 168.766 196.538 140.444 1.00 181.61 ? 2272 THR A OG1   1 
ATOM   5053  C CG2   . THR A 1 2272 ? 167.850 195.979 138.280 1.00 181.61 ? 2272 THR A CG2   1 
ATOM   5054  N N     . ARG A 1 2273 ? 171.615 195.002 140.798 1.00 179.68 ? 2273 ARG A N     1 
ATOM   5055  C CA    . ARG A 1 2273 ? 172.633 195.235 141.823 1.00 179.68 ? 2273 ARG A CA    1 
ATOM   5056  C C     . ARG A 1 2273 ? 172.378 196.542 142.570 1.00 179.68 ? 2273 ARG A C     1 
ATOM   5057  O O     . ARG A 1 2273 ? 173.305 197.205 143.038 1.00 179.68 ? 2273 ARG A O     1 
ATOM   5058  C CB    . ARG A 1 2273 ? 174.041 195.214 141.224 1.00 179.68 ? 2273 ARG A CB    1 
ATOM   5059  C CG    . ARG A 1 2273 ? 174.318 194.024 140.320 1.00 179.68 ? 2273 ARG A CG    1 
ATOM   5060  C CD    . ARG A 1 2273 ? 173.958 192.708 141.000 1.00 179.68 ? 2273 ARG A CD    1 
ATOM   5061  N NE    . ARG A 1 2273 ? 174.512 192.590 142.345 1.00 179.68 ? 2273 ARG A NE    1 
ATOM   5062  C CZ    . ARG A 1 2273 ? 175.806 192.561 142.637 1.00 179.68 ? 2273 ARG A CZ    1 
ATOM   5063  N NH1   . ARG A 1 2273 ? 176.732 192.600 141.692 1.00 179.68 ? 2273 ARG A NH1   1 
ATOM   5064  N NH2   . ARG A 1 2273 ? 176.182 192.479 143.910 1.00 179.68 ? 2273 ARG A NH2   1 
ATOM   5065  N N     . GLU A 1 2274 ? 171.107 196.914 142.681 1.00 171.25 ? 2274 GLU A N     1 
ATOM   5066  C CA    . GLU A 1 2274 ? 170.699 198.107 143.407 1.00 171.25 ? 2274 GLU A CA    1 
ATOM   5067  C C     . GLU A 1 2274 ? 170.331 197.712 144.830 1.00 171.25 ? 2274 GLU A C     1 
ATOM   5068  O O     . GLU A 1 2274 ? 169.698 196.674 145.048 1.00 171.25 ? 2274 GLU A O     1 
ATOM   5069  C CB    . GLU A 1 2274 ? 169.519 198.793 142.716 1.00 171.25 ? 2274 GLU A CB    1 
ATOM   5070  C CG    . GLU A 1 2274 ? 169.299 200.235 143.141 1.00 171.25 ? 2274 GLU A CG    1 
ATOM   5071  C CD    . GLU A 1 2274 ? 168.497 200.350 144.422 1.00 171.25 ? 2274 GLU A CD    1 
ATOM   5072  O OE1   . GLU A 1 2274 ? 167.734 199.412 144.732 1.00 171.25 ? 2274 GLU A OE1   1 
ATOM   5073  O OE2   . GLU A 1 2274 ? 168.629 201.379 145.118 1.00 171.25 ? 2274 GLU A OE2   1 
ATOM   5074  N N     . TRP A 1 2275 ? 170.736 198.533 145.793 1.00 149.55 ? 2275 TRP A N     1 
ATOM   5075  C CA    . TRP A 1 2275 ? 170.543 198.233 147.203 1.00 149.55 ? 2275 TRP A CA    1 
ATOM   5076  C C     . TRP A 1 2275 ? 169.435 199.095 147.787 1.00 149.55 ? 2275 TRP A C     1 
ATOM   5077  O O     . TRP A 1 2275 ? 169.434 200.318 147.614 1.00 149.55 ? 2275 TRP A O     1 
ATOM   5078  C CB    . TRP A 1 2275 ? 171.834 198.451 147.989 1.00 149.55 ? 2275 TRP A CB    1 
ATOM   5079  C CG    . TRP A 1 2275 ? 171.625 198.365 149.461 1.00 149.55 ? 2275 TRP A CG    1 
ATOM   5080  C CD1   . TRP A 1 2275 ? 171.424 199.401 150.323 1.00 149.55 ? 2275 TRP A CD1   1 
ATOM   5081  C CD2   . TRP A 1 2275 ? 171.563 197.172 150.244 1.00 149.55 ? 2275 TRP A CD2   1 
ATOM   5082  N NE1   . TRP A 1 2275 ? 171.256 198.926 151.599 1.00 149.55 ? 2275 TRP A NE1   1 
ATOM   5083  C CE2   . TRP A 1 2275 ? 171.338 197.559 151.577 1.00 149.55 ? 2275 TRP A CE2   1 
ATOM   5084  C CE3   . TRP A 1 2275 ? 171.687 195.812 149.949 1.00 149.55 ? 2275 TRP A CE3   1 
ATOM   5085  C CZ2   . TRP A 1 2275 ? 171.228 196.639 152.610 1.00 149.55 ? 2275 TRP A CZ2   1 
ATOM   5086  C CZ3   . TRP A 1 2275 ? 171.578 194.900 150.977 1.00 149.55 ? 2275 TRP A CZ3   1 
ATOM   5087  C CH2   . TRP A 1 2275 ? 171.356 195.316 152.292 1.00 149.55 ? 2275 TRP A CH2   1 
ATOM   5088  N N     . THR A 1 2276 ? 168.503 198.455 148.484 1.00 144.86 ? 2276 THR A N     1 
ATOM   5089  C CA    . THR A 1 2276 ? 167.480 199.139 149.262 1.00 144.86 ? 2276 THR A CA    1 
ATOM   5090  C C     . THR A 1 2276 ? 167.703 198.804 150.729 1.00 144.86 ? 2276 THR A C     1 
ATOM   5091  O O     . THR A 1 2276 ? 167.756 197.627 151.097 1.00 144.86 ? 2276 THR A O     1 
ATOM   5092  C CB    . THR A 1 2276 ? 166.078 198.727 148.817 1.00 144.86 ? 2276 THR A CB    1 
ATOM   5093  O OG1   . THR A 1 2276 ? 166.027 197.305 148.660 1.00 144.86 ? 2276 THR A OG1   1 
ATOM   5094  C CG2   . THR A 1 2276 ? 165.723 199.390 147.498 1.00 144.86 ? 2276 THR A CG2   1 
ATOM   5095  N N     . ASP A 1 2277 ? 167.837 199.833 151.558 1.00 134.49 ? 2277 ASP A N     1 
ATOM   5096  C CA    . ASP A 1 2277 ? 168.162 199.630 152.961 1.00 134.49 ? 2277 ASP A CA    1 
ATOM   5097  C C     . ASP A 1 2277 ? 166.984 199.025 153.718 1.00 134.49 ? 2277 ASP A C     1 
ATOM   5098  O O     . ASP A 1 2277 ? 165.818 199.277 153.407 1.00 134.49 ? 2277 ASP A O     1 
ATOM   5099  C CB    . ASP A 1 2277 ? 168.568 200.954 153.602 1.00 134.49 ? 2277 ASP A CB    1 
ATOM   5100  C CG    . ASP A 1 2277 ? 167.786 202.126 153.049 1.00 134.49 ? 2277 ASP A CG    1 
ATOM   5101  O OD1   . ASP A 1 2277 ? 166.854 201.892 152.252 1.00 134.49 ? 2277 ASP A OD1   1 
ATOM   5102  O OD2   . ASP A 1 2277 ? 168.101 203.279 153.410 1.00 134.49 ? 2277 ASP A OD2   1 
ATOM   5103  N N     . GLY A 1 2278 ? 167.305 198.214 154.726 1.00 118.41 ? 2278 GLY A N     1 
ATOM   5104  C CA    . GLY A 1 2278 ? 166.310 197.643 155.607 1.00 118.41 ? 2278 GLY A CA    1 
ATOM   5105  C C     . GLY A 1 2278 ? 165.996 198.557 156.775 1.00 118.41 ? 2278 GLY A C     1 
ATOM   5106  O O     . GLY A 1 2278 ? 166.492 199.680 156.878 1.00 118.41 ? 2278 GLY A O     1 
ATOM   5107  N N     . LEU A 1 2279 ? 165.156 198.050 157.679 1.00 105.41 ? 2279 LEU A N     1 
ATOM   5108  C CA    . LEU A 1 2279 ? 164.678 198.870 158.789 1.00 105.41 ? 2279 LEU A CA    1 
ATOM   5109  C C     . LEU A 1 2279 ? 165.828 199.307 159.686 1.00 105.41 ? 2279 LEU A C     1 
ATOM   5110  O O     . LEU A 1 2279 ? 166.006 200.500 159.958 1.00 105.41 ? 2279 LEU A O     1 
ATOM   5111  C CB    . LEU A 1 2279 ? 163.630 198.098 159.591 1.00 105.41 ? 2279 LEU A CB    1 
ATOM   5112  C CG    . LEU A 1 2279 ? 162.459 198.882 160.190 1.00 105.41 ? 2279 LEU A CG    1 
ATOM   5113  C CD1   . LEU A 1 2279 ? 161.519 197.932 160.898 1.00 105.41 ? 2279 LEU A CD1   1 
ATOM   5114  C CD2   . LEU A 1 2279 ? 162.921 199.972 161.144 1.00 105.41 ? 2279 LEU A CD2   1 
ATOM   5115  N N     . PHE A 1 2280 ? 166.630 198.349 160.151 1.00 104.52 ? 2280 PHE A N     1 
ATOM   5116  C CA    . PHE A 1 2280 ? 167.770 198.699 160.988 1.00 104.52 ? 2280 PHE A CA    1 
ATOM   5117  C C     . PHE A 1 2280 ? 168.779 199.525 160.207 1.00 104.52 ? 2280 PHE A C     1 
ATOM   5118  O O     . PHE A 1 2280 ? 169.333 200.502 160.726 1.00 104.52 ? 2280 PHE A O     1 
ATOM   5119  C CB    . PHE A 1 2280 ? 168.418 197.435 161.543 1.00 104.52 ? 2280 PHE A CB    1 
ATOM   5120  C CG    . PHE A 1 2280 ? 169.620 197.697 162.391 1.00 104.52 ? 2280 PHE A CG    1 
ATOM   5121  C CD1   . PHE A 1 2280 ? 169.545 198.559 163.466 1.00 104.52 ? 2280 PHE A CD1   1 
ATOM   5122  C CD2   . PHE A 1 2280 ? 170.819 197.065 162.128 1.00 104.52 ? 2280 PHE A CD2   1 
ATOM   5123  C CE1   . PHE A 1 2280 ? 170.647 198.798 164.255 1.00 104.52 ? 2280 PHE A CE1   1 
ATOM   5124  C CE2   . PHE A 1 2280 ? 171.924 197.298 162.915 1.00 104.52 ? 2280 PHE A CE2   1 
ATOM   5125  C CZ    . PHE A 1 2280 ? 171.838 198.166 163.979 1.00 104.52 ? 2280 PHE A CZ    1 
ATOM   5126  N N     . THR A 1 2281 ? 169.016 199.152 158.948 1.00 115.92 ? 2281 THR A N     1 
ATOM   5127  C CA    . THR A 1 2281 ? 169.927 199.912 158.100 1.00 115.92 ? 2281 THR A CA    1 
ATOM   5128  C C     . THR A 1 2281 ? 169.421 201.332 157.892 1.00 115.92 ? 2281 THR A C     1 
ATOM   5129  O O     . THR A 1 2281 ? 170.190 202.295 157.979 1.00 115.92 ? 2281 THR A O     1 
ATOM   5130  C CB    . THR A 1 2281 ? 170.098 199.205 156.756 1.00 115.92 ? 2281 THR A CB    1 
ATOM   5131  O OG1   . THR A 1 2281 ? 170.397 197.821 156.974 1.00 115.92 ? 2281 THR A OG1   1 
ATOM   5132  C CG2   . THR A 1 2281 ? 171.225 199.841 155.965 1.00 115.92 ? 2281 THR A CG2   1 
ATOM   5133  N N     . HIS A 1 2282 ? 168.122 201.481 157.618 1.00 112.77 ? 2282 HIS A N     1 
ATOM   5134  C CA    . HIS A 1 2282 ? 167.561 202.812 157.414 1.00 112.77 ? 2282 HIS A CA    1 
ATOM   5135  C C     . HIS A 1 2282 ? 167.671 203.658 158.674 1.00 112.77 ? 2282 HIS A C     1 
ATOM   5136  O O     . HIS A 1 2282 ? 168.030 204.840 158.606 1.00 112.77 ? 2282 HIS A O     1 
ATOM   5137  C CB    . HIS A 1 2282 ? 166.104 202.710 156.974 1.00 112.77 ? 2282 HIS A CB    1 
ATOM   5138  C CG    . HIS A 1 2282 ? 165.327 203.970 157.182 1.00 112.77 ? 2282 HIS A CG    1 
ATOM   5139  N ND1   . HIS A 1 2282 ? 165.549 205.110 156.443 1.00 112.77 ? 2282 HIS A ND1   1 
ATOM   5140  C CD2   . HIS A 1 2282 ? 164.335 204.272 158.052 1.00 112.77 ? 2282 HIS A CD2   1 
ATOM   5141  C CE1   . HIS A 1 2282 ? 164.723 206.060 156.844 1.00 112.77 ? 2282 HIS A CE1   1 
ATOM   5142  N NE2   . HIS A 1 2282 ? 163.976 205.577 157.820 1.00 112.77 ? 2282 HIS A NE2   1 
ATOM   5143  N N     . VAL A 1 2283 ? 167.365 203.072 159.833 1.00 111.29 ? 2283 VAL A N     1 
ATOM   5144  C CA    . VAL A 1 2283 ? 167.437 203.823 161.083 1.00 111.29 ? 2283 VAL A CA    1 
ATOM   5145  C C     . VAL A 1 2283 ? 168.870 204.258 161.357 1.00 111.29 ? 2283 VAL A C     1 
ATOM   5146  O O     . VAL A 1 2283 ? 169.131 205.414 161.717 1.00 111.29 ? 2283 VAL A O     1 
ATOM   5147  C CB    . VAL A 1 2283 ? 166.867 202.991 162.244 1.00 111.29 ? 2283 VAL A CB    1 
ATOM   5148  C CG1   . VAL A 1 2283 ? 167.228 203.626 163.574 1.00 111.29 ? 2283 VAL A CG1   1 
ATOM   5149  C CG2   . VAL A 1 2283 ? 165.364 202.862 162.107 1.00 111.29 ? 2283 VAL A CG2   1 
ATOM   5150  N N     . LEU A 1 2284 ? 169.824 203.341 161.181 1.00 111.68 ? 2284 LEU A N     1 
ATOM   5151  C CA    . LEU A 1 2284 ? 171.219 203.684 161.429 1.00 111.68 ? 2284 LEU A CA    1 
ATOM   5152  C C     . LEU A 1 2284 ? 171.702 204.755 160.463 1.00 111.68 ? 2284 LEU A C     1 
ATOM   5153  O O     . LEU A 1 2284 ? 172.436 205.669 160.858 1.00 111.68 ? 2284 LEU A O     1 
ATOM   5154  C CB    . LEU A 1 2284 ? 172.095 202.439 161.331 1.00 111.68 ? 2284 LEU A CB    1 
ATOM   5155  C CG    . LEU A 1 2284 ? 173.438 202.566 162.046 1.00 111.68 ? 2284 LEU A CG    1 
ATOM   5156  C CD1   . LEU A 1 2284 ? 173.260 203.268 163.377 1.00 111.68 ? 2284 LEU A CD1   1 
ATOM   5157  C CD2   . LEU A 1 2284 ? 174.071 201.203 162.244 1.00 111.68 ? 2284 LEU A CD2   1 
ATOM   5158  N N     . ARG A 1 2285 ? 171.309 204.658 159.192 1.00 117.63 ? 2285 ARG A N     1 
ATOM   5159  C CA    . ARG A 1 2285 ? 171.712 205.664 158.217 1.00 117.63 ? 2285 ARG A CA    1 
ATOM   5160  C C     . ARG A 1 2285 ? 171.136 207.028 158.567 1.00 117.63 ? 2285 ARG A C     1 
ATOM   5161  O O     . ARG A 1 2285 ? 171.832 208.046 158.477 1.00 117.63 ? 2285 ARG A O     1 
ATOM   5162  C CB    . ARG A 1 2285 ? 171.281 205.237 156.815 1.00 117.63 ? 2285 ARG A CB    1 
ATOM   5163  C CG    . ARG A 1 2285 ? 171.425 206.322 155.763 1.00 117.63 ? 2285 ARG A CG    1 
ATOM   5164  C CD    . ARG A 1 2285 ? 171.561 205.723 154.373 1.00 117.63 ? 2285 ARG A CD    1 
ATOM   5165  N NE    . ARG A 1 2285 ? 172.788 204.949 154.239 1.00 117.63 ? 2285 ARG A NE    1 
ATOM   5166  C CZ    . ARG A 1 2285 ? 172.845 203.708 153.776 1.00 117.63 ? 2285 ARG A CZ    1 
ATOM   5167  N NH1   . ARG A 1 2285 ? 171.758 203.069 153.377 1.00 117.63 ? 2285 ARG A NH1   1 
ATOM   5168  N NH2   . ARG A 1 2285 ? 174.022 203.093 153.712 1.00 117.63 ? 2285 ARG A NH2   1 
ATOM   5169  N N     . LYS A 1 2286 ? 169.867 207.067 158.975 1.00 116.60 ? 2286 LYS A N     1 
ATOM   5170  C CA    . LYS A 1 2286 ? 169.264 208.335 159.368 1.00 116.60 ? 2286 LYS A CA    1 
ATOM   5171  C C     . LYS A 1 2286 ? 169.973 208.927 160.578 1.00 116.60 ? 2286 LYS A C     1 
ATOM   5172  O O     . LYS A 1 2286 ? 170.189 210.143 160.645 1.00 116.60 ? 2286 LYS A O     1 
ATOM   5173  C CB    . LYS A 1 2286 ? 167.776 208.147 159.657 1.00 116.60 ? 2286 LYS A CB    1 
ATOM   5174  C CG    . LYS A 1 2286 ? 166.868 208.817 158.643 1.00 116.60 ? 2286 LYS A CG    1 
ATOM   5175  C CD    . LYS A 1 2286 ? 165.409 208.717 159.055 1.00 116.60 ? 2286 LYS A CD    1 
ATOM   5176  C CE    . LYS A 1 2286 ? 164.564 209.745 158.323 1.00 116.60 ? 2286 LYS A CE    1 
ATOM   5177  N NZ    . LYS A 1 2286 ? 163.158 209.757 158.809 1.00 116.60 ? 2286 LYS A NZ    1 
ATOM   5178  N N     . ILE A 1 2287 ? 170.339 208.087 161.547 1.00 113.67 ? 2287 ILE A N     1 
ATOM   5179  C CA    . ILE A 1 2287 ? 171.062 208.591 162.710 1.00 113.67 ? 2287 ILE A CA    1 
ATOM   5180  C C     . ILE A 1 2287 ? 172.426 209.136 162.304 1.00 113.67 ? 2287 ILE A C     1 
ATOM   5181  O O     . ILE A 1 2287 ? 172.825 210.224 162.737 1.00 113.67 ? 2287 ILE A O     1 
ATOM   5182  C CB    . ILE A 1 2287 ? 171.188 207.499 163.785 1.00 113.67 ? 2287 ILE A CB    1 
ATOM   5183  C CG1   . ILE A 1 2287 ? 169.805 207.054 164.250 1.00 113.67 ? 2287 ILE A CG1   1 
ATOM   5184  C CG2   . ILE A 1 2287 ? 171.985 208.013 164.966 1.00 113.67 ? 2287 ILE A CG2   1 
ATOM   5185  C CD1   . ILE A 1 2287 ? 168.938 208.194 164.715 1.00 113.67 ? 2287 ILE A CD1   1 
ATOM   5186  N N     . ILE A 1 2288 ? 173.158 208.401 161.465 1.00 119.66 ? 2288 ILE A N     1 
ATOM   5187  C CA    . ILE A 1 2288 ? 174.504 208.826 161.085 1.00 119.66 ? 2288 ILE A CA    1 
ATOM   5188  C C     . ILE A 1 2288 ? 174.451 210.142 160.320 1.00 119.66 ? 2288 ILE A C     1 
ATOM   5189  O O     . ILE A 1 2288 ? 175.208 211.077 160.607 1.00 119.66 ? 2288 ILE A O     1 
ATOM   5190  C CB    . ILE A 1 2288 ? 175.207 207.728 160.267 1.00 119.66 ? 2288 ILE A CB    1 
ATOM   5191  C CG1   . ILE A 1 2288 ? 175.843 206.693 161.193 1.00 119.66 ? 2288 ILE A CG1   1 
ATOM   5192  C CG2   . ILE A 1 2288 ? 176.258 208.326 159.347 1.00 119.66 ? 2288 ILE A CG2   1 
ATOM   5193  C CD1   . ILE A 1 2288 ? 176.170 205.390 160.500 1.00 119.66 ? 2288 ILE A CD1   1 
ATOM   5194  N N     . ASP A 1 2289 ? 173.550 210.239 159.340 1.00 125.41 ? 2289 ASP A N     1 
ATOM   5195  C CA    . ASP A 1 2289 ? 173.475 211.456 158.538 1.00 125.41 ? 2289 ASP A CA    1 
ATOM   5196  C C     . ASP A 1 2289 ? 173.077 212.654 159.389 1.00 125.41 ? 2289 ASP A C     1 
ATOM   5197  O O     . ASP A 1 2289 ? 173.640 213.744 159.238 1.00 125.41 ? 2289 ASP A O     1 
ATOM   5198  C CB    . ASP A 1 2289 ? 172.497 211.270 157.379 1.00 125.41 ? 2289 ASP A CB    1 
ATOM   5199  C CG    . ASP A 1 2289 ? 172.892 210.132 156.462 1.00 125.41 ? 2289 ASP A CG    1 
ATOM   5200  O OD1   . ASP A 1 2289 ? 173.908 209.465 156.746 1.00 125.41 ? 2289 ASP A OD1   1 
ATOM   5201  O OD2   . ASP A 1 2289 ? 172.192 209.910 155.452 1.00 125.41 ? 2289 ASP A OD2   1 
ATOM   5202  N N     . SER A 1 2290 ? 172.118 212.466 160.294 1.00 125.49 ? 2290 SER A N     1 
ATOM   5203  C CA    . SER A 1 2290 ? 171.652 213.524 161.188 1.00 125.49 ? 2290 SER A CA    1 
ATOM   5204  C C     . SER A 1 2290 ? 171.197 214.751 160.403 1.00 125.49 ? 2290 SER A C     1 
ATOM   5205  O O     . SER A 1 2290 ? 171.603 215.883 160.674 1.00 125.49 ? 2290 SER A O     1 
ATOM   5206  C CB    . SER A 1 2290 ? 172.731 213.898 162.203 1.00 125.49 ? 2290 SER A CB    1 
ATOM   5207  O OG    . SER A 1 2290 ? 173.799 214.587 161.579 1.00 125.49 ? 2290 SER A OG    1 
ATOM   5208  N N     . VAL A 1 2291 ? 170.343 214.512 159.407 1.00 127.97 ? 2291 VAL A N     1 
ATOM   5209  C CA    . VAL A 1 2291 ? 169.846 215.613 158.592 1.00 127.97 ? 2291 VAL A CA    1 
ATOM   5210  C C     . VAL A 1 2291 ? 168.963 216.545 159.414 1.00 127.97 ? 2291 VAL A C     1 
ATOM   5211  O O     . VAL A 1 2291 ? 168.941 217.758 159.175 1.00 127.97 ? 2291 VAL A O     1 
ATOM   5212  C CB    . VAL A 1 2291 ? 169.119 215.068 157.348 1.00 127.97 ? 2291 VAL A CB    1 
ATOM   5213  C CG1   . VAL A 1 2291 ? 170.047 214.159 156.561 1.00 127.97 ? 2291 VAL A CG1   1 
ATOM   5214  C CG2   . VAL A 1 2291 ? 167.872 214.308 157.745 1.00 127.97 ? 2291 VAL A CG2   1 
ATOM   5215  N N     . ARG A 1 2292 ? 168.229 216.011 160.384 1.00 125.98 ? 2292 ARG A N     1 
ATOM   5216  C CA    . ARG A 1 2292 ? 167.453 216.830 161.305 1.00 125.98 ? 2292 ARG A CA    1 
ATOM   5217  C C     . ARG A 1 2292 ? 168.193 217.112 162.604 1.00 125.98 ? 2292 ARG A C     1 
ATOM   5218  O O     . ARG A 1 2292 ? 167.618 217.728 163.507 1.00 125.98 ? 2292 ARG A O     1 
ATOM   5219  C CB    . ARG A 1 2292 ? 166.114 216.156 161.617 1.00 125.98 ? 2292 ARG A CB    1 
ATOM   5220  C CG    . ARG A 1 2292 ? 164.984 216.533 160.674 1.00 125.98 ? 2292 ARG A CG    1 
ATOM   5221  C CD    . ARG A 1 2292 ? 164.977 215.643 159.446 1.00 125.98 ? 2292 ARG A CD    1 
ATOM   5222  N NE    . ARG A 1 2292 ? 165.269 214.253 159.777 1.00 125.98 ? 2292 ARG A NE    1 
ATOM   5223  C CZ    . ARG A 1 2292 ? 164.420 213.421 160.365 1.00 125.98 ? 2292 ARG A CZ    1 
ATOM   5224  N NH1   . ARG A 1 2292 ? 163.195 213.799 160.691 1.00 125.98 ? 2292 ARG A NH1   1 
ATOM   5225  N NH2   . ARG A 1 2292 ? 164.809 212.177 160.630 1.00 125.98 ? 2292 ARG A NH2   1 
ATOM   5226  N N     . GLY A 1 2293 ? 169.443 216.676 162.724 1.00 123.47 ? 2293 GLY A N     1 
ATOM   5227  C CA    . GLY A 1 2293 ? 170.179 216.830 163.961 1.00 123.47 ? 2293 GLY A CA    1 
ATOM   5228  C C     . GLY A 1 2293 ? 170.051 215.612 164.850 1.00 123.47 ? 2293 GLY A C     1 
ATOM   5229  O O     . GLY A 1 2293 ? 169.798 215.733 166.052 1.00 123.47 ? 2293 GLY A O     1 
ATOM   5230  N N     . GLU A 1 2294 ? 170.219 214.427 164.260 1.00 124.15 ? 2294 GLU A N     1 
ATOM   5231  C CA    . GLU A 1 2294 ? 170.088 213.192 165.025 1.00 124.15 ? 2294 GLU A CA    1 
ATOM   5232  C C     . GLU A 1 2294 ? 171.163 213.088 166.098 1.00 124.15 ? 2294 GLU A C     1 
ATOM   5233  O O     . GLU A 1 2294 ? 170.885 212.656 167.223 1.00 124.15 ? 2294 GLU A O     1 
ATOM   5234  C CB    . GLU A 1 2294 ? 170.139 211.988 164.085 1.00 124.15 ? 2294 GLU A CB    1 
ATOM   5235  C CG    . GLU A 1 2294 ? 168.795 211.623 163.464 1.00 124.15 ? 2294 GLU A CG    1 
ATOM   5236  C CD    . GLU A 1 2294 ? 168.437 212.480 162.260 1.00 124.15 ? 2294 GLU A CD    1 
ATOM   5237  O OE1   . GLU A 1 2294 ? 168.534 213.722 162.350 1.00 124.15 ? 2294 GLU A OE1   1 
ATOM   5238  O OE2   . GLU A 1 2294 ? 168.051 211.906 161.220 1.00 124.15 ? 2294 GLU A OE2   1 
ATOM   5239  N N     . LEU A 1 2295 ? 172.394 213.480 165.776 1.00 116.07 ? 2295 LEU A N     1 
ATOM   5240  C CA    . LEU A 1 2295 ? 173.432 213.543 166.792 1.00 116.07 ? 2295 LEU A CA    1 
ATOM   5241  C C     . LEU A 1 2295 ? 173.083 214.592 167.845 1.00 116.07 ? 2295 LEU A C     1 
ATOM   5242  O O     . LEU A 1 2295 ? 172.126 215.361 167.709 1.00 116.07 ? 2295 LEU A O     1 
ATOM   5243  C CB    . LEU A 1 2295 ? 174.797 213.844 166.171 1.00 116.07 ? 2295 LEU A CB    1 
ATOM   5244  C CG    . LEU A 1 2295 ? 175.586 212.718 165.493 1.00 116.07 ? 2295 LEU A CG    1 
ATOM   5245  C CD1   . LEU A 1 2295 ? 175.900 211.629 166.506 1.00 116.07 ? 2295 LEU A CD1   1 
ATOM   5246  C CD2   . LEU A 1 2295 ? 174.878 212.133 164.290 1.00 116.07 ? 2295 LEU A CD2   1 
ATOM   5247  N N     . GLN A 1 2296 ? 173.878 214.606 168.915 1.00 114.96 ? 2296 GLN A N     1 
ATOM   5248  C CA    . GLN A 1 2296 ? 173.600 215.386 170.119 1.00 114.96 ? 2296 GLN A CA    1 
ATOM   5249  C C     . GLN A 1 2296 ? 172.290 214.969 170.774 1.00 114.96 ? 2296 GLN A C     1 
ATOM   5250  O O     . GLN A 1 2296 ? 171.732 215.711 171.586 1.00 114.96 ? 2296 GLN A O     1 
ATOM   5251  C CB    . GLN A 1 2296 ? 173.594 216.893 169.832 1.00 114.96 ? 2296 GLN A CB    1 
ATOM   5252  C CG    . GLN A 1 2296 ? 174.904 217.431 169.279 1.00 114.96 ? 2296 GLN A CG    1 
ATOM   5253  C CD    . GLN A 1 2296 ? 175.000 217.304 167.772 1.00 114.96 ? 2296 GLN A CD    1 
ATOM   5254  O OE1   . GLN A 1 2296 ? 175.916 216.672 167.249 1.00 114.96 ? 2296 GLN A OE1   1 
ATOM   5255  N NE2   . GLN A 1 2296 ? 174.047 217.900 167.066 1.00 114.96 ? 2296 GLN A NE2   1 
ATOM   5256  N N     . LYS A 1 2297 ? 171.787 213.787 170.424 1.00 105.76 ? 2297 LYS A N     1 
ATOM   5257  C CA    . LYS A 1 2297 ? 170.578 213.234 171.015 1.00 105.76 ? 2297 LYS A CA    1 
ATOM   5258  C C     . LYS A 1 2297 ? 170.802 211.756 171.282 1.00 105.76 ? 2297 LYS A C     1 
ATOM   5259  O O     . LYS A 1 2297 ? 171.269 211.030 170.401 1.00 105.76 ? 2297 LYS A O     1 
ATOM   5260  C CB    . LYS A 1 2297 ? 169.367 213.422 170.098 1.00 105.76 ? 2297 LYS A CB    1 
ATOM   5261  C CG    . LYS A 1 2297 ? 168.723 214.789 170.185 1.00 105.76 ? 2297 LYS A CG    1 
ATOM   5262  C CD    . LYS A 1 2297 ? 167.851 215.059 168.972 1.00 105.76 ? 2297 LYS A CD    1 
ATOM   5263  C CE    . LYS A 1 2297 ? 167.044 213.830 168.588 1.00 105.76 ? 2297 LYS A CE    1 
ATOM   5264  N NZ    . LYS A 1 2297 ? 166.302 214.024 167.314 1.00 105.76 ? 2297 LYS A NZ    1 
ATOM   5265  N N     . ARG A 1 2298 ? 170.461 211.315 172.488 1.00 95.70  ? 2298 ARG A N     1 
ATOM   5266  C CA    . ARG A 1 2298 ? 170.644 209.918 172.864 1.00 95.70  ? 2298 ARG A CA    1 
ATOM   5267  C C     . ARG A 1 2298 ? 169.701 209.047 172.047 1.00 95.70  ? 2298 ARG A C     1 
ATOM   5268  O O     . ARG A 1 2298 ? 168.480 209.107 172.219 1.00 95.70  ? 2298 ARG A O     1 
ATOM   5269  C CB    . ARG A 1 2298 ? 170.398 209.742 174.358 1.00 95.70  ? 2298 ARG A CB    1 
ATOM   5270  C CG    . ARG A 1 2298 ? 170.789 208.381 174.895 1.00 95.70  ? 2298 ARG A CG    1 
ATOM   5271  C CD    . ARG A 1 2298 ? 170.922 208.423 176.402 1.00 95.70  ? 2298 ARG A CD    1 
ATOM   5272  N NE    . ARG A 1 2298 ? 171.188 209.777 176.868 1.00 95.70  ? 2298 ARG A NE    1 
ATOM   5273  C CZ    . ARG A 1 2298 ? 172.400 210.253 177.116 1.00 95.70  ? 2298 ARG A CZ    1 
ATOM   5274  N NH1   . ARG A 1 2298 ? 173.480 209.507 176.956 1.00 95.70  ? 2298 ARG A NH1   1 
ATOM   5275  N NH2   . ARG A 1 2298 ? 172.532 211.510 177.528 1.00 95.70  ? 2298 ARG A NH2   1 
ATOM   5276  N N     . GLN A 1 2299 ? 170.260 208.243 171.151 1.00 96.28  ? 2299 GLN A N     1 
ATOM   5277  C CA    . GLN A 1 2299 ? 169.478 207.330 170.332 1.00 96.28  ? 2299 GLN A CA    1 
ATOM   5278  C C     . GLN A 1 2299 ? 169.665 205.909 170.842 1.00 96.28  ? 2299 GLN A C     1 
ATOM   5279  O O     . GLN A 1 2299 ? 170.797 205.440 170.990 1.00 96.28  ? 2299 GLN A O     1 
ATOM   5280  C CB    . GLN A 1 2299 ? 169.887 207.418 168.863 1.00 96.28  ? 2299 GLN A CB    1 
ATOM   5281  C CG    . GLN A 1 2299 ? 170.011 208.830 168.349 1.00 96.28  ? 2299 GLN A CG    1 
ATOM   5282  C CD    . GLN A 1 2299 ? 168.679 209.538 168.298 1.00 96.28  ? 2299 GLN A CD    1 
ATOM   5283  O OE1   . GLN A 1 2299 ? 168.558 210.686 168.721 1.00 96.28  ? 2299 GLN A OE1   1 
ATOM   5284  N NE2   . GLN A 1 2299 ? 167.663 208.850 167.791 1.00 96.28  ? 2299 GLN A NE2   1 
ATOM   5285  N N     . TRP A 1 2300 ? 168.554 205.232 171.109 1.00 85.80  ? 2300 TRP A N     1 
ATOM   5286  C CA    . TRP A 1 2300 ? 168.564 203.850 171.567 1.00 85.80  ? 2300 TRP A CA    1 
ATOM   5287  C C     . TRP A 1 2300 ? 167.735 203.019 170.603 1.00 85.80  ? 2300 TRP A C     1 
ATOM   5288  O O     . TRP A 1 2300 ? 166.571 203.341 170.345 1.00 85.80  ? 2300 TRP A O     1 
ATOM   5289  C CB    . TRP A 1 2300 ? 168.010 203.743 172.985 1.00 85.80  ? 2300 TRP A CB    1 
ATOM   5290  C CG    . TRP A 1 2300 ? 168.970 204.197 174.017 1.00 85.80  ? 2300 TRP A CG    1 
ATOM   5291  C CD1   . TRP A 1 2300 ? 170.272 204.535 173.825 1.00 85.80  ? 2300 TRP A CD1   1 
ATOM   5292  C CD2   . TRP A 1 2300 ? 168.709 204.375 175.409 1.00 85.80  ? 2300 TRP A CD2   1 
ATOM   5293  N NE1   . TRP A 1 2300 ? 170.844 204.909 175.013 1.00 85.80  ? 2300 TRP A NE1   1 
ATOM   5294  C CE2   . TRP A 1 2300 ? 169.902 204.819 176.002 1.00 85.80  ? 2300 TRP A CE2   1 
ATOM   5295  C CE3   . TRP A 1 2300 ? 167.582 204.202 176.211 1.00 85.80  ? 2300 TRP A CE3   1 
ATOM   5296  C CZ2   . TRP A 1 2300 ? 170.002 205.091 177.359 1.00 85.80  ? 2300 TRP A CZ2   1 
ATOM   5297  C CZ3   . TRP A 1 2300 ? 167.683 204.472 177.557 1.00 85.80  ? 2300 TRP A CZ3   1 
ATOM   5298  C CH2   . TRP A 1 2300 ? 168.882 204.913 178.118 1.00 85.80  ? 2300 TRP A CH2   1 
ATOM   5299  N N     . ILE A 1 2301 ? 168.332 201.962 170.070 1.00 90.08  ? 2301 ILE A N     1 
ATOM   5300  C CA    . ILE A 1 2301 ? 167.643 201.037 169.180 1.00 90.08  ? 2301 ILE A CA    1 
ATOM   5301  C C     . ILE A 1 2301 ? 167.234 199.841 170.030 1.00 90.08  ? 2301 ILE A C     1 
ATOM   5302  O O     . ILE A 1 2301 ? 168.052 198.970 170.334 1.00 90.08  ? 2301 ILE A O     1 
ATOM   5303  C CB    . ILE A 1 2301 ? 168.518 200.622 167.995 1.00 90.08  ? 2301 ILE A CB    1 
ATOM   5304  C CG1   . ILE A 1 2301 ? 168.900 201.825 167.126 1.00 90.08  ? 2301 ILE A CG1   1 
ATOM   5305  C CG2   . ILE A 1 2301 ? 167.800 199.592 167.149 1.00 90.08  ? 2301 ILE A CG2   1 
ATOM   5306  C CD1   . ILE A 1 2301 ? 167.914 202.973 167.148 1.00 90.08  ? 2301 ILE A CD1   1 
ATOM   5307  N N     . VAL A 1 2302 ? 165.967 199.797 170.424 1.00 87.41  ? 2302 VAL A N     1 
ATOM   5308  C CA    . VAL A 1 2302 ? 165.468 198.747 171.301 1.00 87.41  ? 2302 VAL A CA    1 
ATOM   5309  C C     . VAL A 1 2302 ? 164.935 197.618 170.431 1.00 87.41  ? 2302 VAL A C     1 
ATOM   5310  O O     . VAL A 1 2302 ? 164.003 197.812 169.648 1.00 87.41  ? 2302 VAL A O     1 
ATOM   5311  C CB    . VAL A 1 2302 ? 164.387 199.270 172.251 1.00 87.41  ? 2302 VAL A CB    1 
ATOM   5312  C CG1   . VAL A 1 2302 ? 163.874 198.145 173.120 1.00 87.41  ? 2302 VAL A CG1   1 
ATOM   5313  C CG2   . VAL A 1 2302 ? 164.932 200.395 173.102 1.00 87.41  ? 2302 VAL A CG2   1 
ATOM   5314  N N     . PHE A 1 2303 ? 165.525 196.435 170.570 1.00 92.57  ? 2303 PHE A N     1 
ATOM   5315  C CA    . PHE A 1 2303 ? 165.095 195.267 169.808 1.00 92.57  ? 2303 PHE A CA    1 
ATOM   5316  C C     . PHE A 1 2303 ? 164.169 194.408 170.667 1.00 92.57  ? 2303 PHE A C     1 
ATOM   5317  O O     . PHE A 1 2303 ? 164.534 193.351 171.180 1.00 92.57  ? 2303 PHE A O     1 
ATOM   5318  C CB    . PHE A 1 2303 ? 166.304 194.481 169.319 1.00 92.57  ? 2303 PHE A CB    1 
ATOM   5319  C CG    . PHE A 1 2303 ? 166.805 194.921 167.979 1.00 92.57  ? 2303 PHE A CG    1 
ATOM   5320  C CD1   . PHE A 1 2303 ? 166.071 194.672 166.835 1.00 92.57  ? 2303 PHE A CD1   1 
ATOM   5321  C CD2   . PHE A 1 2303 ? 168.009 195.587 167.863 1.00 92.57  ? 2303 PHE A CD2   1 
ATOM   5322  C CE1   . PHE A 1 2303 ? 166.532 195.076 165.600 1.00 92.57  ? 2303 PHE A CE1   1 
ATOM   5323  C CE2   . PHE A 1 2303 ? 168.473 195.993 166.634 1.00 92.57  ? 2303 PHE A CE2   1 
ATOM   5324  C CZ    . PHE A 1 2303 ? 167.733 195.738 165.501 1.00 92.57  ? 2303 PHE A CZ    1 
ATOM   5325  N N     . ASP A 1 2304 ? 162.944 194.899 170.824 1.00 91.89  ? 2304 ASP A N     1 
ATOM   5326  C CA    . ASP A 1 2304 ? 161.924 194.153 171.544 1.00 91.89  ? 2304 ASP A CA    1 
ATOM   5327  C C     . ASP A 1 2304 ? 161.566 192.892 170.770 1.00 91.89  ? 2304 ASP A C     1 
ATOM   5328  O O     . ASP A 1 2304 ? 161.274 192.951 169.573 1.00 91.89  ? 2304 ASP A O     1 
ATOM   5329  C CB    . ASP A 1 2304 ? 160.684 195.019 171.749 1.00 91.89  ? 2304 ASP A CB    1 
ATOM   5330  C CG    . ASP A 1 2304 ? 159.820 194.540 172.893 1.00 91.89  ? 2304 ASP A CG    1 
ATOM   5331  O OD1   . ASP A 1 2304 ? 159.529 193.327 172.955 1.00 91.89  ? 2304 ASP A OD1   1 
ATOM   5332  O OD2   . ASP A 1 2304 ? 159.423 195.379 173.728 1.00 91.89  ? 2304 ASP A OD2   1 
ATOM   5333  N N     . GLY A 1 2305 ? 161.577 191.753 171.453 1.00 90.74  ? 2305 GLY A N     1 
ATOM   5334  C CA    . GLY A 1 2305 ? 161.304 190.493 170.792 1.00 90.74  ? 2305 GLY A CA    1 
ATOM   5335  C C     . GLY A 1 2305 ? 162.204 189.374 171.269 1.00 90.74  ? 2305 GLY A C     1 
ATOM   5336  O O     . GLY A 1 2305 ? 162.588 189.338 172.440 1.00 90.74  ? 2305 GLY A O     1 
ATOM   5337  N N     . ASP A 1 2306 ? 162.546 188.454 170.374 1.00 95.54  ? 2306 ASP A N     1 
ATOM   5338  C CA    . ASP A 1 2306 ? 163.408 187.328 170.694 1.00 95.54  ? 2306 ASP A CA    1 
ATOM   5339  C C     . ASP A 1 2306 ? 164.693 187.403 169.882 1.00 95.54  ? 2306 ASP A C     1 
ATOM   5340  O O     . ASP A 1 2306 ? 164.776 188.104 168.871 1.00 95.54  ? 2306 ASP A O     1 
ATOM   5341  C CB    . ASP A 1 2306 ? 162.695 186.002 170.428 1.00 95.54  ? 2306 ASP A CB    1 
ATOM   5342  C CG    . ASP A 1 2306 ? 161.313 185.955 171.041 1.00 95.54  ? 2306 ASP A CG    1 
ATOM   5343  O OD1   . ASP A 1 2306 ? 160.335 186.252 170.326 1.00 95.54  ? 2306 ASP A OD1   1 
ATOM   5344  O OD2   . ASP A 1 2306 ? 161.204 185.616 172.239 1.00 95.54  ? 2306 ASP A OD2   1 
ATOM   5345  N N     . VAL A 1 2307 ? 165.704 186.672 170.340 1.00 93.01  ? 2307 VAL A N     1 
ATOM   5346  C CA    . VAL A 1 2307 ? 167.012 186.652 169.699 1.00 93.01  ? 2307 VAL A CA    1 
ATOM   5347  C C     . VAL A 1 2307 ? 167.343 185.222 169.296 1.00 93.01  ? 2307 VAL A C     1 
ATOM   5348  O O     . VAL A 1 2307 ? 167.284 184.305 170.123 1.00 93.01  ? 2307 VAL A O     1 
ATOM   5349  C CB    . VAL A 1 2307 ? 168.101 187.237 170.616 1.00 93.01  ? 2307 VAL A CB    1 
ATOM   5350  C CG1   . VAL A 1 2307 ? 168.008 186.642 172.004 1.00 93.01  ? 2307 VAL A CG1   1 
ATOM   5351  C CG2   . VAL A 1 2307 ? 169.473 186.985 170.026 1.00 93.01  ? 2307 VAL A CG2   1 
ATOM   5352  N N     . ASP A 1 2308 ? 167.673 185.037 168.026 1.00 97.39  ? 2308 ASP A N     1 
ATOM   5353  C CA    . ASP A 1 2308 ? 168.136 183.771 167.482 1.00 97.39  ? 2308 ASP A CA    1 
ATOM   5354  C C     . ASP A 1 2308 ? 169.251 184.067 166.493 1.00 97.39  ? 2308 ASP A C     1 
ATOM   5355  O O     . ASP A 1 2308 ? 169.326 185.173 165.948 1.00 97.39  ? 2308 ASP A O     1 
ATOM   5356  C CB    . ASP A 1 2308 ? 166.992 182.992 166.820 1.00 97.39  ? 2308 ASP A CB    1 
ATOM   5357  C CG    . ASP A 1 2308 ? 166.452 183.678 165.594 1.00 97.39  ? 2308 ASP A CG    1 
ATOM   5358  O OD1   . ASP A 1 2308 ? 166.459 184.919 165.565 1.00 97.39  ? 2308 ASP A OD1   1 
ATOM   5359  O OD2   . ASP A 1 2308 ? 166.010 182.977 164.662 1.00 97.39  ? 2308 ASP A OD2   1 
ATOM   5360  N N     . PRO A 1 2309 ? 170.136 183.096 166.234 1.00 104.72 ? 2309 PRO A N     1 
ATOM   5361  C CA    . PRO A 1 2309 ? 171.394 183.418 165.544 1.00 104.72 ? 2309 PRO A CA    1 
ATOM   5362  C C     . PRO A 1 2309 ? 171.239 183.796 164.080 1.00 104.72 ? 2309 PRO A C     1 
ATOM   5363  O O     . PRO A 1 2309 ? 172.242 183.931 163.374 1.00 104.72 ? 2309 PRO A O     1 
ATOM   5364  C CB    . PRO A 1 2309 ? 172.213 182.126 165.688 1.00 104.72 ? 2309 PRO A CB    1 
ATOM   5365  C CG    . PRO A 1 2309 ? 171.532 181.337 166.750 1.00 104.72 ? 2309 PRO A CG    1 
ATOM   5366  C CD    . PRO A 1 2309 ? 170.092 181.682 166.634 1.00 104.72 ? 2309 PRO A CD    1 
ATOM   5367  N N     . GLU A 1 2310 ? 170.009 183.967 163.602 1.00 107.06 ? 2310 GLU A N     1 
ATOM   5368  C CA    . GLU A 1 2310 ? 169.801 184.314 162.200 1.00 107.06 ? 2310 GLU A CA    1 
ATOM   5369  C C     . GLU A 1 2310 ? 169.823 185.824 161.980 1.00 107.06 ? 2310 GLU A C     1 
ATOM   5370  O O     . GLU A 1 2310 ? 170.566 186.322 161.129 1.00 107.06 ? 2310 GLU A O     1 
ATOM   5371  C CB    . GLU A 1 2310 ? 168.485 183.712 161.699 1.00 107.06 ? 2310 GLU A CB    1 
ATOM   5372  C CG    . GLU A 1 2310 ? 168.266 182.272 162.128 1.00 107.06 ? 2310 GLU A CG    1 
ATOM   5373  C CD    . GLU A 1 2310 ? 169.022 181.269 161.275 1.00 107.06 ? 2310 GLU A CD    1 
ATOM   5374  O OE1   . GLU A 1 2310 ? 170.073 181.626 160.704 1.00 107.06 ? 2310 GLU A OE1   1 
ATOM   5375  O OE2   . GLU A 1 2310 ? 168.561 180.112 161.179 1.00 107.06 ? 2310 GLU A OE2   1 
ATOM   5376  N N     . TRP A 1 2311 ? 169.022 186.565 162.740 1.00 100.56 ? 2311 TRP A N     1 
ATOM   5377  C CA    . TRP A 1 2311 ? 168.942 188.006 162.547 1.00 100.56 ? 2311 TRP A CA    1 
ATOM   5378  C C     . TRP A 1 2311 ? 170.027 188.769 163.291 1.00 100.56 ? 2311 TRP A C     1 
ATOM   5379  O O     . TRP A 1 2311 ? 170.082 189.997 163.179 1.00 100.56 ? 2311 TRP A O     1 
ATOM   5380  C CB    . TRP A 1 2311 ? 167.563 188.523 162.969 1.00 100.56 ? 2311 TRP A CB    1 
ATOM   5381  C CG    . TRP A 1 2311 ? 167.366 188.647 164.451 1.00 100.56 ? 2311 TRP A CG    1 
ATOM   5382  C CD1   . TRP A 1 2311 ? 166.966 187.667 165.303 1.00 100.56 ? 2311 TRP A CD1   1 
ATOM   5383  C CD2   . TRP A 1 2311 ? 167.527 189.826 165.247 1.00 100.56 ? 2311 TRP A CD2   1 
ATOM   5384  N NE1   . TRP A 1 2311 ? 166.881 188.152 166.583 1.00 100.56 ? 2311 TRP A NE1   1 
ATOM   5385  C CE2   . TRP A 1 2311 ? 167.220 189.478 166.575 1.00 100.56 ? 2311 TRP A CE2   1 
ATOM   5386  C CE3   . TRP A 1 2311 ? 167.905 191.140 164.967 1.00 100.56 ? 2311 TRP A CE3   1 
ATOM   5387  C CZ2   . TRP A 1 2311 ? 167.282 190.392 167.618 1.00 100.56 ? 2311 TRP A CZ2   1 
ATOM   5388  C CZ3   . TRP A 1 2311 ? 167.968 192.044 166.004 1.00 100.56 ? 2311 TRP A CZ3   1 
ATOM   5389  C CH2   . TRP A 1 2311 ? 167.655 191.669 167.312 1.00 100.56 ? 2311 TRP A CH2   1 
ATOM   5390  N N     . VAL A 1 2312 ? 170.894 188.084 164.035 1.00 106.04 ? 2312 VAL A N     1 
ATOM   5391  C CA    . VAL A 1 2312 ? 171.951 188.740 164.792 1.00 106.04 ? 2312 VAL A CA    1 
ATOM   5392  C C     . VAL A 1 2312 ? 173.327 188.498 164.203 1.00 106.04 ? 2312 VAL A C     1 
ATOM   5393  O O     . VAL A 1 2312 ? 174.323 188.945 164.789 1.00 106.04 ? 2312 VAL A O     1 
ATOM   5394  C CB    . VAL A 1 2312 ? 171.927 188.316 166.270 1.00 106.04 ? 2312 VAL A CB    1 
ATOM   5395  C CG1   . VAL A 1 2312 ? 170.570 188.607 166.876 1.00 106.04 ? 2312 VAL A CG1   1 
ATOM   5396  C CG2   . VAL A 1 2312 ? 172.274 186.847 166.399 1.00 106.04 ? 2312 VAL A CG2   1 
ATOM   5397  N N     . GLU A 1 2313 ? 173.424 187.807 163.067 1.00 113.35 ? 2313 GLU A N     1 
ATOM   5398  C CA    . GLU A 1 2313 ? 174.737 187.547 162.492 1.00 113.35 ? 2313 GLU A CA    1 
ATOM   5399  C C     . GLU A 1 2313 ? 175.394 188.811 161.955 1.00 113.35 ? 2313 GLU A C     1 
ATOM   5400  O O     . GLU A 1 2313 ? 176.625 188.873 161.893 1.00 113.35 ? 2313 GLU A O     1 
ATOM   5401  C CB    . GLU A 1 2313 ? 174.639 186.486 161.394 1.00 113.35 ? 2313 GLU A CB    1 
ATOM   5402  C CG    . GLU A 1 2313 ? 174.206 187.002 160.038 1.00 113.35 ? 2313 GLU A CG    1 
ATOM   5403  C CD    . GLU A 1 2313 ? 173.876 185.879 159.076 1.00 113.35 ? 2313 GLU A CD    1 
ATOM   5404  O OE1   . GLU A 1 2313 ? 174.699 184.949 158.941 1.00 113.35 ? 2313 GLU A OE1   1 
ATOM   5405  O OE2   . GLU A 1 2313 ? 172.794 185.922 158.457 1.00 113.35 ? 2313 GLU A OE2   1 
ATOM   5406  N N     . ASN A 1 2314 ? 174.611 189.818 161.570 1.00 113.62 ? 2314 ASN A N     1 
ATOM   5407  C CA    . ASN A 1 2314 ? 175.194 191.099 161.199 1.00 113.62 ? 2314 ASN A CA    1 
ATOM   5408  C C     . ASN A 1 2314 ? 175.447 191.991 162.403 1.00 113.62 ? 2314 ASN A C     1 
ATOM   5409  O O     . ASN A 1 2314 ? 176.201 192.962 162.290 1.00 113.62 ? 2314 ASN A O     1 
ATOM   5410  C CB    . ASN A 1 2314 ? 174.291 191.833 160.207 1.00 113.62 ? 2314 ASN A CB    1 
ATOM   5411  C CG    . ASN A 1 2314 ? 174.168 191.106 158.886 1.00 113.62 ? 2314 ASN A CG    1 
ATOM   5412  O OD1   . ASN A 1 2314 ? 173.841 189.922 158.845 1.00 113.62 ? 2314 ASN A OD1   1 
ATOM   5413  N ND2   . ASN A 1 2314 ? 174.426 191.814 157.793 1.00 113.62 ? 2314 ASN A ND2   1 
ATOM   5414  N N     . LEU A 1 2315 ? 174.841 191.684 163.547 1.00 115.82 ? 2315 LEU A N     1 
ATOM   5415  C CA    . LEU A 1 2315 ? 174.989 192.509 164.737 1.00 115.82 ? 2315 LEU A CA    1 
ATOM   5416  C C     . LEU A 1 2315 ? 176.232 192.184 165.549 1.00 115.82 ? 2315 LEU A C     1 
ATOM   5417  O O     . LEU A 1 2315 ? 176.555 192.938 166.470 1.00 115.82 ? 2315 LEU A O     1 
ATOM   5418  C CB    . LEU A 1 2315 ? 173.757 192.384 165.637 1.00 115.82 ? 2315 LEU A CB    1 
ATOM   5419  C CG    . LEU A 1 2315 ? 172.650 193.417 165.426 1.00 115.82 ? 2315 LEU A CG    1 
ATOM   5420  C CD1   . LEU A 1 2315 ? 173.153 194.792 165.821 1.00 115.82 ? 2315 LEU A CD1   1 
ATOM   5421  C CD2   . LEU A 1 2315 ? 172.159 193.430 163.995 1.00 115.82 ? 2315 LEU A CD2   1 
ATOM   5422  N N     . ASN A 1 2316 ? 176.932 191.091 165.247 1.00 115.32 ? 2316 ASN A N     1 
ATOM   5423  C CA    . ASN A 1 2316 ? 178.176 190.817 165.957 1.00 115.32 ? 2316 ASN A CA    1 
ATOM   5424  C C     . ASN A 1 2316 ? 179.234 191.863 165.634 1.00 115.32 ? 2316 ASN A C     1 
ATOM   5425  O O     . ASN A 1 2316 ? 179.985 192.289 166.518 1.00 115.32 ? 2316 ASN A O     1 
ATOM   5426  C CB    . ASN A 1 2316 ? 178.680 189.415 165.624 1.00 115.32 ? 2316 ASN A CB    1 
ATOM   5427  C CG    . ASN A 1 2316 ? 177.564 188.396 165.571 1.00 115.32 ? 2316 ASN A CG    1 
ATOM   5428  O OD1   . ASN A 1 2316 ? 177.163 187.952 164.498 1.00 115.32 ? 2316 ASN A OD1   1 
ATOM   5429  N ND2   . ASN A 1 2316 ? 177.056 188.018 166.737 1.00 115.32 ? 2316 ASN A ND2   1 
ATOM   5430  N N     . SER A 1 2317 ? 179.300 192.295 164.374 1.00 118.75 ? 2317 SER A N     1 
ATOM   5431  C CA    . SER A 1 2317 ? 180.282 193.300 163.989 1.00 118.75 ? 2317 SER A CA    1 
ATOM   5432  C C     . SER A 1 2317 ? 179.984 194.653 164.620 1.00 118.75 ? 2317 SER A C     1 
ATOM   5433  O O     . SER A 1 2317 ? 180.902 195.455 164.826 1.00 118.75 ? 2317 SER A O     1 
ATOM   5434  C CB    . SER A 1 2317 ? 180.328 193.425 162.467 1.00 118.75 ? 2317 SER A CB    1 
ATOM   5435  O OG    . SER A 1 2317 ? 179.148 194.037 161.976 1.00 118.75 ? 2317 SER A OG    1 
ATOM   5436  N N     . VAL A 1 2318 ? 178.721 194.925 164.930 1.00 114.32 ? 2318 VAL A N     1 
ATOM   5437  C CA    . VAL A 1 2318 ? 178.336 196.219 165.483 1.00 114.32 ? 2318 VAL A CA    1 
ATOM   5438  C C     . VAL A 1 2318 ? 178.377 196.206 167.004 1.00 114.32 ? 2318 VAL A C     1 
ATOM   5439  O O     . VAL A 1 2318 ? 178.650 197.229 167.637 1.00 114.32 ? 2318 VAL A O     1 
ATOM   5440  C CB    . VAL A 1 2318 ? 176.937 196.599 164.958 1.00 114.32 ? 2318 VAL A CB    1 
ATOM   5441  C CG1   . VAL A 1 2318 ? 176.500 197.946 165.506 1.00 114.32 ? 2318 VAL A CG1   1 
ATOM   5442  C CG2   . VAL A 1 2318 ? 176.928 196.599 163.440 1.00 114.32 ? 2318 VAL A CG2   1 
ATOM   5443  N N     . LEU A 1 2319 ? 178.122 195.049 167.606 1.00 114.73 ? 2319 LEU A N     1 
ATOM   5444  C CA    . LEU A 1 2319 ? 177.959 194.962 169.049 1.00 114.73 ? 2319 LEU A CA    1 
ATOM   5445  C C     . LEU A 1 2319 ? 179.287 195.007 169.795 1.00 114.73 ? 2319 LEU A C     1 
ATOM   5446  O O     . LEU A 1 2319 ? 179.361 195.598 170.878 1.00 114.73 ? 2319 LEU A O     1 
ATOM   5447  C CB    . LEU A 1 2319 ? 177.190 193.686 169.386 1.00 114.73 ? 2319 LEU A CB    1 
ATOM   5448  C CG    . LEU A 1 2319 ? 177.136 193.225 170.835 1.00 114.73 ? 2319 LEU A CG    1 
ATOM   5449  C CD1   . LEU A 1 2319 ? 176.337 194.217 171.636 1.00 114.73 ? 2319 LEU A CD1   1 
ATOM   5450  C CD2   . LEU A 1 2319 ? 176.493 191.855 170.890 1.00 114.73 ? 2319 LEU A CD2   1 
ATOM   5451  N N     . ASP A 1 2320 ? 180.339 194.417 169.239 1.00 119.74 ? 2320 ASP A N     1 
ATOM   5452  C CA    . ASP A 1 2320 ? 181.628 194.364 169.914 1.00 119.74 ? 2320 ASP A CA    1 
ATOM   5453  C C     . ASP A 1 2320 ? 182.325 195.716 169.780 1.00 119.74 ? 2320 ASP A C     1 
ATOM   5454  O O     . ASP A 1 2320 ? 181.716 196.722 169.407 1.00 119.74 ? 2320 ASP A O     1 
ATOM   5455  C CB    . ASP A 1 2320 ? 182.477 193.229 169.351 1.00 119.74 ? 2320 ASP A CB    1 
ATOM   5456  C CG    . ASP A 1 2320 ? 182.595 193.284 167.842 1.00 119.74 ? 2320 ASP A CG    1 
ATOM   5457  O OD1   . ASP A 1 2320 ? 181.924 194.135 167.221 1.00 119.74 ? 2320 ASP A OD1   1 
ATOM   5458  O OD2   . ASP A 1 2320 ? 183.360 192.477 167.275 1.00 119.74 ? 2320 ASP A OD2   1 
ATOM   5459  N N     . ASP A 1 2321 ? 183.619 195.757 170.096 1.00 122.14 ? 2321 ASP A N     1 
ATOM   5460  C CA    . ASP A 1 2321 ? 184.386 196.987 169.948 1.00 122.14 ? 2321 ASP A CA    1 
ATOM   5461  C C     . ASP A 1 2321 ? 184.562 197.401 168.494 1.00 122.14 ? 2321 ASP A C     1 
ATOM   5462  O O     . ASP A 1 2321 ? 185.003 198.526 168.240 1.00 122.14 ? 2321 ASP A O     1 
ATOM   5463  C CB    . ASP A 1 2321 ? 185.753 196.831 170.610 1.00 122.14 ? 2321 ASP A CB    1 
ATOM   5464  C CG    . ASP A 1 2321 ? 185.674 196.106 171.934 1.00 122.14 ? 2321 ASP A CG    1 
ATOM   5465  O OD1   . ASP A 1 2321 ? 185.193 196.711 172.913 1.00 122.14 ? 2321 ASP A OD1   1 
ATOM   5466  O OD2   . ASP A 1 2321 ? 186.086 194.930 171.996 1.00 122.14 ? 2321 ASP A OD2   1 
ATOM   5467  N N     . ASN A 1 2322 ? 184.241 196.522 167.543 1.00 123.58 ? 2322 ASN A N     1 
ATOM   5468  C CA    . ASN A 1 2322 ? 184.354 196.873 166.132 1.00 123.58 ? 2322 ASN A CA    1 
ATOM   5469  C C     . ASN A 1 2322 ? 183.415 198.025 165.785 1.00 123.58 ? 2322 ASN A C     1 
ATOM   5470  O O     . ASN A 1 2322 ? 183.826 199.007 165.156 1.00 123.58 ? 2322 ASN A O     1 
ATOM   5471  C CB    . ASN A 1 2322 ? 184.084 195.622 165.285 1.00 123.58 ? 2322 ASN A CB    1 
ATOM   5472  C CG    . ASN A 1 2322 ? 183.922 195.911 163.797 1.00 123.58 ? 2322 ASN A CG    1 
ATOM   5473  O OD1   . ASN A 1 2322 ? 183.182 196.800 163.387 1.00 123.58 ? 2322 ASN A OD1   1 
ATOM   5474  N ND2   . ASN A 1 2322 ? 184.632 195.144 162.978 1.00 123.58 ? 2322 ASN A ND2   1 
ATOM   5475  N N     . LYS A 1 2323 ? 182.147 197.918 166.185 1.00 118.86 ? 2323 LYS A N     1 
ATOM   5476  C CA    . LYS A 1 2323 ? 181.174 199.010 166.085 1.00 118.86 ? 2323 LYS A CA    1 
ATOM   5477  C C     . LYS A 1 2323 ? 181.024 199.523 164.654 1.00 118.86 ? 2323 LYS A C     1 
ATOM   5478  O O     . LYS A 1 2323 ? 180.899 200.724 164.407 1.00 118.86 ? 2323 LYS A O     1 
ATOM   5479  C CB    . LYS A 1 2323 ? 181.544 200.157 167.024 1.00 118.86 ? 2323 LYS A CB    1 
ATOM   5480  C CG    . LYS A 1 2323 ? 181.919 199.726 168.424 1.00 118.86 ? 2323 LYS A CG    1 
ATOM   5481  C CD    . LYS A 1 2323 ? 182.582 200.859 169.186 1.00 118.86 ? 2323 LYS A CD    1 
ATOM   5482  C CE    . LYS A 1 2323 ? 183.548 201.636 168.304 1.00 118.86 ? 2323 LYS A CE    1 
ATOM   5483  N NZ    . LYS A 1 2323 ? 184.670 200.781 167.825 1.00 118.86 ? 2323 LYS A NZ    1 
ATOM   5484  N N     . LEU A 1 2324 ? 181.044 198.601 163.698 1.00 124.52 ? 2324 LEU A N     1 
ATOM   5485  C CA    . LEU A 1 2324 ? 180.874 198.971 162.301 1.00 124.52 ? 2324 LEU A CA    1 
ATOM   5486  C C     . LEU A 1 2324 ? 179.956 197.946 161.652 1.00 124.52 ? 2324 LEU A C     1 
ATOM   5487  O O     . LEU A 1 2324 ? 180.081 196.747 161.911 1.00 124.52 ? 2324 LEU A O     1 
ATOM   5488  C CB    . LEU A 1 2324 ? 182.232 199.035 161.588 1.00 124.52 ? 2324 LEU A CB    1 
ATOM   5489  C CG    . LEU A 1 2324 ? 182.385 198.857 160.077 1.00 124.52 ? 2324 LEU A CG    1 
ATOM   5490  C CD1   . LEU A 1 2324 ? 181.475 199.811 159.320 1.00 124.52 ? 2324 LEU A CD1   1 
ATOM   5491  C CD2   . LEU A 1 2324 ? 183.835 199.044 159.661 1.00 124.52 ? 2324 LEU A CD2   1 
ATOM   5492  N N     . LEU A 1 2325 ? 179.043 198.417 160.806 1.00 129.81 ? 2325 LEU A N     1 
ATOM   5493  C CA    . LEU A 1 2325 ? 178.084 197.548 160.139 1.00 129.81 ? 2325 LEU A CA    1 
ATOM   5494  C C     . LEU A 1 2325 ? 178.614 197.211 158.754 1.00 129.81 ? 2325 LEU A C     1 
ATOM   5495  O O     . LEU A 1 2325 ? 179.035 198.103 158.011 1.00 129.81 ? 2325 LEU A O     1 
ATOM   5496  C CB    . LEU A 1 2325 ? 176.706 198.217 160.053 1.00 129.81 ? 2325 LEU A CB    1 
ATOM   5497  C CG    . LEU A 1 2325 ? 175.431 197.528 159.525 1.00 129.81 ? 2325 LEU A CG    1 
ATOM   5498  C CD1   . LEU A 1 2325 ? 174.278 198.514 159.583 1.00 129.81 ? 2325 LEU A CD1   1 
ATOM   5499  C CD2   . LEU A 1 2325 ? 175.523 196.949 158.113 1.00 129.81 ? 2325 LEU A CD2   1 
ATOM   5500  N N     . THR A 1 2326 ? 178.583 195.929 158.411 1.00 136.69 ? 2326 THR A N     1 
ATOM   5501  C CA    . THR A 1 2326 ? 179.076 195.445 157.126 1.00 136.69 ? 2326 THR A CA    1 
ATOM   5502  C C     . THR A 1 2326 ? 177.880 195.161 156.223 1.00 136.69 ? 2326 THR A C     1 
ATOM   5503  O O     . THR A 1 2326 ? 177.263 194.096 156.301 1.00 136.69 ? 2326 THR A O     1 
ATOM   5504  C CB    . THR A 1 2326 ? 179.938 194.203 157.316 1.00 136.69 ? 2326 THR A CB    1 
ATOM   5505  O OG1   . THR A 1 2326 ? 180.689 194.330 158.530 1.00 136.69 ? 2326 THR A OG1   1 
ATOM   5506  C CG2   . THR A 1 2326 ? 180.892 194.030 156.144 1.00 136.69 ? 2326 THR A CG2   1 
ATOM   5507  N N     . LEU A 1 2327 ? 177.554 196.119 155.368 1.00 144.24 ? 2327 LEU A N     1 
ATOM   5508  C CA    . LEU A 1 2327 ? 176.513 195.907 154.375 1.00 144.24 ? 2327 LEU A CA    1 
ATOM   5509  C C     . LEU A 1 2327 ? 177.026 194.947 153.301 1.00 144.24 ? 2327 LEU A C     1 
ATOM   5510  O O     . LEU A 1 2327 ? 178.214 194.969 152.969 1.00 144.24 ? 2327 LEU A O     1 
ATOM   5511  C CB    . LEU A 1 2327 ? 176.110 197.241 153.744 1.00 144.24 ? 2327 LEU A CB    1 
ATOM   5512  C CG    . LEU A 1 2327 ? 174.621 197.512 153.525 1.00 144.24 ? 2327 LEU A CG    1 
ATOM   5513  C CD1   . LEU A 1 2327 ? 173.846 197.066 154.746 1.00 144.24 ? 2327 LEU A CD1   1 
ATOM   5514  C CD2   . LEU A 1 2327 ? 174.373 198.981 153.237 1.00 144.24 ? 2327 LEU A CD2   1 
ATOM   5515  N N     . PRO A 1 2328 ? 176.170 194.083 152.749 1.00 149.90 ? 2328 PRO A N     1 
ATOM   5516  C CA    . PRO A 1 2328 ? 176.661 193.149 151.727 1.00 149.90 ? 2328 PRO A CA    1 
ATOM   5517  C C     . PRO A 1 2328 ? 177.041 193.816 150.416 1.00 149.90 ? 2328 PRO A C     1 
ATOM   5518  O O     . PRO A 1 2328 ? 177.877 193.275 149.681 1.00 149.90 ? 2328 PRO A O     1 
ATOM   5519  C CB    . PRO A 1 2328 ? 175.494 192.163 151.559 1.00 149.90 ? 2328 PRO A CB    1 
ATOM   5520  C CG    . PRO A 1 2328 ? 174.286 192.849 152.134 1.00 149.90 ? 2328 PRO A CG    1 
ATOM   5521  C CD    . PRO A 1 2328 ? 174.701 194.148 152.756 1.00 149.90 ? 2328 PRO A CD    1 
ATOM   5522  N N     . ASN A 1 2329 ? 176.459 194.974 150.091 1.00 150.60 ? 2329 ASN A N     1 
ATOM   5523  C CA    . ASN A 1 2329 ? 176.867 195.667 148.876 1.00 150.60 ? 2329 ASN A CA    1 
ATOM   5524  C C     . ASN A 1 2329 ? 178.254 196.278 149.006 1.00 150.60 ? 2329 ASN A C     1 
ATOM   5525  O O     . ASN A 1 2329 ? 178.984 196.345 148.012 1.00 150.60 ? 2329 ASN A O     1 
ATOM   5526  C CB    . ASN A 1 2329 ? 175.849 196.748 148.504 1.00 150.60 ? 2329 ASN A CB    1 
ATOM   5527  C CG    . ASN A 1 2329 ? 175.815 197.896 149.495 1.00 150.60 ? 2329 ASN A CG    1 
ATOM   5528  O OD1   . ASN A 1 2329 ? 176.388 197.820 150.582 1.00 150.60 ? 2329 ASN A OD1   1 
ATOM   5529  N ND2   . ASN A 1 2329 ? 175.133 198.971 149.120 1.00 150.60 ? 2329 ASN A ND2   1 
ATOM   5530  N N     . GLY A 1 2330 ? 178.634 196.716 150.203 1.00 149.61 ? 2330 GLY A N     1 
ATOM   5531  C CA    . GLY A 1 2330 ? 179.949 197.282 150.412 1.00 149.61 ? 2330 GLY A CA    1 
ATOM   5532  C C     . GLY A 1 2330 ? 179.955 198.510 151.298 1.00 149.61 ? 2330 GLY A C     1 
ATOM   5533  O O     . GLY A 1 2330 ? 181.013 198.925 151.778 1.00 149.61 ? 2330 GLY A O     1 
ATOM   5534  N N     . GLU A 1 2331 ? 178.786 199.102 151.523 1.00 145.74 ? 2331 GLU A N     1 
ATOM   5535  C CA    . GLU A 1 2331 ? 178.711 200.296 152.352 1.00 145.74 ? 2331 GLU A CA    1 
ATOM   5536  C C     . GLU A 1 2331 ? 179.055 199.969 153.799 1.00 145.74 ? 2331 GLU A C     1 
ATOM   5537  O O     . GLU A 1 2331 ? 178.696 198.911 154.320 1.00 145.74 ? 2331 GLU A O     1 
ATOM   5538  C CB    . GLU A 1 2331 ? 177.319 200.918 152.267 1.00 145.74 ? 2331 GLU A CB    1 
ATOM   5539  C CG    . GLU A 1 2331 ? 176.829 201.127 150.847 1.00 145.74 ? 2331 GLU A CG    1 
ATOM   5540  C CD    . GLU A 1 2331 ? 175.410 201.656 150.791 1.00 145.74 ? 2331 GLU A CD    1 
ATOM   5541  O OE1   . GLU A 1 2331 ? 174.991 202.341 151.747 1.00 145.74 ? 2331 GLU A OE1   1 
ATOM   5542  O OE2   . GLU A 1 2331 ? 174.711 201.384 149.793 1.00 145.74 ? 2331 GLU A OE2   1 
ATOM   5543  N N     . ARG A 1 2332 ? 179.767 200.886 154.445 1.00 139.00 ? 2332 ARG A N     1 
ATOM   5544  C CA    . ARG A 1 2332 ? 180.203 200.724 155.823 1.00 139.00 ? 2332 ARG A CA    1 
ATOM   5545  C C     . ARG A 1 2332 ? 179.505 201.759 156.692 1.00 139.00 ? 2332 ARG A C     1 
ATOM   5546  O O     . ARG A 1 2332 ? 179.550 202.957 156.392 1.00 139.00 ? 2332 ARG A O     1 
ATOM   5547  C CB    . ARG A 1 2332 ? 181.721 200.873 155.934 1.00 139.00 ? 2332 ARG A CB    1 
ATOM   5548  C CG    . ARG A 1 2332 ? 182.508 199.651 155.485 1.00 139.00 ? 2332 ARG A CG    1 
ATOM   5549  C CD    . ARG A 1 2332 ? 182.052 198.373 156.179 1.00 139.00 ? 2332 ARG A CD    1 
ATOM   5550  N NE    . ARG A 1 2332 ? 181.012 197.662 155.444 1.00 139.00 ? 2332 ARG A NE    1 
ATOM   5551  C CZ    . ARG A 1 2332 ? 181.173 197.106 154.251 1.00 139.00 ? 2332 ARG A CZ    1 
ATOM   5552  N NH1   . ARG A 1 2332 ? 182.335 197.142 153.619 1.00 139.00 ? 2332 ARG A NH1   1 
ATOM   5553  N NH2   . ARG A 1 2332 ? 180.142 196.492 153.679 1.00 139.00 ? 2332 ARG A NH2   1 
ATOM   5554  N N     . LEU A 1 2333 ? 178.861 201.298 157.760 1.00 123.74 ? 2333 LEU A N     1 
ATOM   5555  C CA    . LEU A 1 2333 ? 178.152 202.171 158.687 1.00 123.74 ? 2333 LEU A CA    1 
ATOM   5556  C C     . LEU A 1 2333 ? 178.728 201.965 160.079 1.00 123.74 ? 2333 LEU A C     1 
ATOM   5557  O O     . LEU A 1 2333 ? 178.768 200.834 160.575 1.00 123.74 ? 2333 LEU A O     1 
ATOM   5558  C CB    . LEU A 1 2333 ? 176.649 201.888 158.673 1.00 123.74 ? 2333 LEU A CB    1 
ATOM   5559  C CG    . LEU A 1 2333 ? 175.862 202.420 157.470 1.00 123.74 ? 2333 LEU A CG    1 
ATOM   5560  C CD1   . LEU A 1 2333 ? 176.268 203.849 157.140 1.00 123.74 ? 2333 LEU A CD1   1 
ATOM   5561  C CD2   . LEU A 1 2333 ? 176.011 201.516 156.252 1.00 123.74 ? 2333 LEU A CD2   1 
ATOM   5562  N N     . SER A 1 2334 ? 179.163 203.051 160.705 1.00 117.69 ? 2334 SER A N     1 
ATOM   5563  C CA    . SER A 1 2334 ? 179.806 202.998 162.009 1.00 117.69 ? 2334 SER A CA    1 
ATOM   5564  C C     . SER A 1 2334 ? 178.880 203.560 163.078 1.00 117.69 ? 2334 SER A C     1 
ATOM   5565  O O     . SER A 1 2334 ? 178.165 204.538 162.846 1.00 117.69 ? 2334 SER A O     1 
ATOM   5566  C CB    . SER A 1 2334 ? 181.123 203.774 162.001 1.00 117.69 ? 2334 SER A CB    1 
ATOM   5567  O OG    . SER A 1 2334 ? 181.738 203.749 163.277 1.00 117.69 ? 2334 SER A OG    1 
ATOM   5568  N N     . LEU A 1 2335 ? 178.905 202.938 164.247 1.00 108.57 ? 2335 LEU A N     1 
ATOM   5569  C CA    . LEU A 1 2335 ? 178.039 203.350 165.341 1.00 108.57 ? 2335 LEU A CA    1 
ATOM   5570  C C     . LEU A 1 2335 ? 178.589 204.611 165.995 1.00 108.57 ? 2335 LEU A C     1 
ATOM   5571  O O     . LEU A 1 2335 ? 179.707 204.586 166.520 1.00 108.57 ? 2335 LEU A O     1 
ATOM   5572  C CB    . LEU A 1 2335 ? 177.918 202.213 166.353 1.00 108.57 ? 2335 LEU A CB    1 
ATOM   5573  C CG    . LEU A 1 2335 ? 177.251 202.364 167.723 1.00 108.57 ? 2335 LEU A CG    1 
ATOM   5574  C CD1   . LEU A 1 2335 ? 176.674 201.028 168.144 1.00 108.57 ? 2335 LEU A CD1   1 
ATOM   5575  C CD2   . LEU A 1 2335 ? 178.252 202.818 168.767 1.00 108.57 ? 2335 LEU A CD2   1 
ATOM   5576  N N     . PRO A 1 2336 ? 177.855 205.726 165.979 1.00 100.71 ? 2336 PRO A N     1 
ATOM   5577  C CA    . PRO A 1 2336 ? 178.311 206.905 166.708 1.00 100.71 ? 2336 PRO A CA    1 
ATOM   5578  C C     . PRO A 1 2336 ? 178.275 206.653 168.204 1.00 100.71 ? 2336 PRO A C     1 
ATOM   5579  O O     . PRO A 1 2336 ? 177.481 205.829 168.688 1.00 100.71 ? 2336 PRO A O     1 
ATOM   5580  C CB    . PRO A 1 2336 ? 177.300 207.990 166.296 1.00 100.71 ? 2336 PRO A CB    1 
ATOM   5581  C CG    . PRO A 1 2336 ? 176.109 207.244 165.822 1.00 100.71 ? 2336 PRO A CG    1 
ATOM   5582  C CD    . PRO A 1 2336 ? 176.622 205.979 165.219 1.00 100.71 ? 2336 PRO A CD    1 
ATOM   5583  N N     . PRO A 1 2337 ? 179.112 207.345 168.979 1.00 102.29 ? 2337 PRO A N     1 
ATOM   5584  C CA    . PRO A 1 2337 ? 179.221 207.027 170.413 1.00 102.29 ? 2337 PRO A CA    1 
ATOM   5585  C C     . PRO A 1 2337 ? 177.934 207.209 171.199 1.00 102.29 ? 2337 PRO A C     1 
ATOM   5586  O O     . PRO A 1 2337 ? 177.765 206.553 172.234 1.00 102.29 ? 2337 PRO A O     1 
ATOM   5587  C CB    . PRO A 1 2337 ? 180.310 207.992 170.902 1.00 102.29 ? 2337 PRO A CB    1 
ATOM   5588  C CG    . PRO A 1 2337 ? 180.291 209.109 169.920 1.00 102.29 ? 2337 PRO A CG    1 
ATOM   5589  C CD    . PRO A 1 2337 ? 179.962 208.484 168.600 1.00 102.29 ? 2337 PRO A CD    1 
ATOM   5590  N N     . ASN A 1 2338 ? 177.021 208.070 170.752 1.00 101.94 ? 2338 ASN A N     1 
ATOM   5591  C CA    . ASN A 1 2338 ? 175.801 208.352 171.493 1.00 101.94 ? 2338 ASN A CA    1 
ATOM   5592  C C     . ASN A 1 2338 ? 174.675 207.381 171.166 1.00 101.94 ? 2338 ASN A C     1 
ATOM   5593  O O     . ASN A 1 2338 ? 173.521 207.647 171.518 1.00 101.94 ? 2338 ASN A O     1 
ATOM   5594  C CB    . ASN A 1 2338 ? 175.341 209.783 171.223 1.00 101.94 ? 2338 ASN A CB    1 
ATOM   5595  C CG    . ASN A 1 2338 ? 174.659 209.926 169.883 1.00 101.94 ? 2338 ASN A CG    1 
ATOM   5596  O OD1   . ASN A 1 2338 ? 175.149 209.434 168.869 1.00 101.94 ? 2338 ASN A OD1   1 
ATOM   5597  N ND2   . ASN A 1 2338 ? 173.524 210.612 169.868 1.00 101.94 ? 2338 ASN A ND2   1 
ATOM   5598  N N     . VAL A 1 2339 ? 174.976 206.269 170.500 1.00 98.17  ? 2339 VAL A N     1 
ATOM   5599  C CA    . VAL A 1 2339 ? 173.971 205.294 170.095 1.00 98.17  ? 2339 VAL A CA    1 
ATOM   5600  C C     . VAL A 1 2339 ? 174.239 203.989 170.829 1.00 98.17  ? 2339 VAL A C     1 
ATOM   5601  O O     . VAL A 1 2339 ? 175.367 203.483 170.815 1.00 98.17  ? 2339 VAL A O     1 
ATOM   5602  C CB    . VAL A 1 2339 ? 173.973 205.075 168.571 1.00 98.17  ? 2339 VAL A CB    1 
ATOM   5603  C CG1   . VAL A 1 2339 ? 173.434 203.700 168.228 1.00 98.17  ? 2339 VAL A CG1   1 
ATOM   5604  C CG2   . VAL A 1 2339 ? 173.153 206.148 167.888 1.00 98.17  ? 2339 VAL A CG2   1 
ATOM   5605  N N     . ARG A 1 2340 ? 173.208 203.453 171.473 1.00 96.02  ? 2340 ARG A N     1 
ATOM   5606  C CA    . ARG A 1 2340 ? 173.299 202.193 172.193 1.00 96.02  ? 2340 ARG A CA    1 
ATOM   5607  C C     . ARG A 1 2340 ? 172.257 201.231 171.648 1.00 96.02  ? 2340 ARG A C     1 
ATOM   5608  O O     . ARG A 1 2340 ? 171.161 201.643 171.259 1.00 96.02  ? 2340 ARG A O     1 
ATOM   5609  C CB    . ARG A 1 2340 ? 173.101 202.396 173.694 1.00 96.02  ? 2340 ARG A CB    1 
ATOM   5610  C CG    . ARG A 1 2340 ? 173.947 203.511 174.254 1.00 96.02  ? 2340 ARG A CG    1 
ATOM   5611  C CD    . ARG A 1 2340 ? 175.419 203.226 174.059 1.00 96.02  ? 2340 ARG A CD    1 
ATOM   5612  N NE    . ARG A 1 2340 ? 176.222 203.990 175.001 1.00 96.02  ? 2340 ARG A NE    1 
ATOM   5613  C CZ    . ARG A 1 2340 ? 176.534 205.267 174.836 1.00 96.02  ? 2340 ARG A CZ    1 
ATOM   5614  N NH1   . ARG A 1 2340 ? 176.137 205.943 173.771 1.00 96.02  ? 2340 ARG A NH1   1 
ATOM   5615  N NH2   . ARG A 1 2340 ? 177.259 205.883 175.765 1.00 96.02  ? 2340 ARG A NH2   1 
ATOM   5616  N N     . ILE A 1 2341 ? 172.612 199.955 171.599 1.00 93.30  ? 2341 ILE A N     1 
ATOM   5617  C CA    . ILE A 1 2341 ? 171.736 198.925 171.058 1.00 93.30  ? 2341 ILE A CA    1 
ATOM   5618  C C     . ILE A 1 2341 ? 171.055 198.201 172.210 1.00 93.30  ? 2341 ILE A C     1 
ATOM   5619  O O     . ILE A 1 2341 ? 171.712 197.774 173.167 1.00 93.30  ? 2341 ILE A O     1 
ATOM   5620  C CB    . ILE A 1 2341 ? 172.523 197.944 170.179 1.00 93.30  ? 2341 ILE A CB    1 
ATOM   5621  C CG1   . ILE A 1 2341 ? 173.114 198.653 168.961 1.00 93.30  ? 2341 ILE A CG1   1 
ATOM   5622  C CG2   . ILE A 1 2341 ? 171.616 196.844 169.709 1.00 93.30  ? 2341 ILE A CG2   1 
ATOM   5623  C CD1   . ILE A 1 2341 ? 172.078 199.227 168.024 1.00 93.30  ? 2341 ILE A CD1   1 
ATOM   5624  N N     . MET A 1 2342 ? 169.741 198.053 172.119 1.00 97.06  ? 2342 MET A N     1 
ATOM   5625  C CA    . MET A 1 2342 ? 168.956 197.467 173.190 1.00 97.06  ? 2342 MET A CA    1 
ATOM   5626  C C     . MET A 1 2342 ? 168.260 196.234 172.635 1.00 97.06  ? 2342 MET A C     1 
ATOM   5627  O O     . MET A 1 2342 ? 167.693 196.284 171.540 1.00 97.06  ? 2342 MET A O     1 
ATOM   5628  C CB    . MET A 1 2342 ? 167.918 198.468 173.709 1.00 97.06  ? 2342 MET A CB    1 
ATOM   5629  C CG    . MET A 1 2342 ? 168.437 199.708 174.461 1.00 97.06  ? 2342 MET A CG    1 
ATOM   5630  S SD    . MET A 1 2342 ? 170.109 199.731 175.126 1.00 97.06  ? 2342 MET A SD    1 
ATOM   5631  C CE    . MET A 1 2342 ? 169.999 198.398 176.304 1.00 97.06  ? 2342 MET A CE    1 
ATOM   5632  N N     . PHE A 1 2343 ? 168.339 195.122 173.359 1.00 91.31  ? 2343 PHE A N     1 
ATOM   5633  C CA    . PHE A 1 2343 ? 167.496 193.960 173.096 1.00 91.31  ? 2343 PHE A CA    1 
ATOM   5634  C C     . PHE A 1 2343 ? 166.603 193.787 174.314 1.00 91.31  ? 2343 PHE A C     1 
ATOM   5635  O O     . PHE A 1 2343 ? 167.096 193.736 175.445 1.00 91.31  ? 2343 PHE A O     1 
ATOM   5636  C CB    . PHE A 1 2343 ? 168.299 192.685 172.856 1.00 91.31  ? 2343 PHE A CB    1 
ATOM   5637  C CG    . PHE A 1 2343 ? 169.034 192.632 171.543 1.00 91.31  ? 2343 PHE A CG    1 
ATOM   5638  C CD1   . PHE A 1 2343 ? 169.491 193.775 170.922 1.00 91.31  ? 2343 PHE A CD1   1 
ATOM   5639  C CD2   . PHE A 1 2343 ? 169.296 191.409 170.951 1.00 91.31  ? 2343 PHE A CD2   1 
ATOM   5640  C CE1   . PHE A 1 2343 ? 170.181 193.696 169.726 1.00 91.31  ? 2343 PHE A CE1   1 
ATOM   5641  C CE2   . PHE A 1 2343 ? 169.979 191.332 169.756 1.00 91.31  ? 2343 PHE A CE2   1 
ATOM   5642  C CZ    . PHE A 1 2343 ? 170.419 192.473 169.146 1.00 91.31  ? 2343 PHE A CZ    1 
ATOM   5643  N N     . GLU A 1 2344 ? 165.296 193.693 174.093 1.00 87.82  ? 2344 GLU A N     1 
ATOM   5644  C CA    . GLU A 1 2344 ? 164.360 193.365 175.165 1.00 87.82  ? 2344 GLU A CA    1 
ATOM   5645  C C     . GLU A 1 2344 ? 163.864 191.950 174.913 1.00 87.82  ? 2344 GLU A C     1 
ATOM   5646  O O     . GLU A 1 2344 ? 162.827 191.730 174.287 1.00 87.82  ? 2344 GLU A O     1 
ATOM   5647  C CB    . GLU A 1 2344 ? 163.223 194.370 175.212 1.00 87.82  ? 2344 GLU A CB    1 
ATOM   5648  C CG    . GLU A 1 2344 ? 162.327 194.208 176.404 1.00 87.82  ? 2344 GLU A CG    1 
ATOM   5649  C CD    . GLU A 1 2344 ? 161.129 195.112 176.329 1.00 87.82  ? 2344 GLU A CD    1 
ATOM   5650  O OE1   . GLU A 1 2344 ? 161.315 196.330 176.131 1.00 87.82  ? 2344 GLU A OE1   1 
ATOM   5651  O OE2   . GLU A 1 2344 ? 159.994 194.610 176.471 1.00 87.82  ? 2344 GLU A OE2   1 
ATOM   5652  N N     . VAL A 1 2345 ? 164.621 190.975 175.405 1.00 83.06  ? 2345 VAL A N     1 
ATOM   5653  C CA    . VAL A 1 2345 ? 164.350 189.573 175.134 1.00 83.06  ? 2345 VAL A CA    1 
ATOM   5654  C C     . VAL A 1 2345 ? 164.015 188.868 176.439 1.00 83.06  ? 2345 VAL A C     1 
ATOM   5655  O O     . VAL A 1 2345 ? 164.671 189.049 177.466 1.00 83.06  ? 2345 VAL A O     1 
ATOM   5656  C CB    . VAL A 1 2345 ? 165.531 188.890 174.418 1.00 83.06  ? 2345 VAL A CB    1 
ATOM   5657  C CG1   . VAL A 1 2345 ? 166.829 189.249 175.093 1.00 83.06  ? 2345 VAL A CG1   1 
ATOM   5658  C CG2   . VAL A 1 2345 ? 165.347 187.386 174.408 1.00 83.06  ? 2345 VAL A CG2   1 
ATOM   5659  N N     . GLN A 1 2346 ? 162.968 188.047 176.381 1.00 86.64  ? 2346 GLN A N     1 
ATOM   5660  C CA    . GLN A 1 2346 ? 162.417 187.377 177.550 1.00 86.64  ? 2346 GLN A CA    1 
ATOM   5661  C C     . GLN A 1 2346 ? 163.334 186.298 178.109 1.00 86.64  ? 2346 GLN A C     1 
ATOM   5662  O O     . GLN A 1 2346 ? 163.754 186.386 179.264 1.00 86.64  ? 2346 GLN A O     1 
ATOM   5663  C CB    . GLN A 1 2346 ? 161.056 186.766 177.203 1.00 86.64  ? 2346 GLN A CB    1 
ATOM   5664  C CG    . GLN A 1 2346 ? 160.410 186.005 178.345 1.00 86.64  ? 2346 GLN A CG    1 
ATOM   5665  C CD    . GLN A 1 2346 ? 159.331 185.053 177.869 1.00 86.64  ? 2346 GLN A CD    1 
ATOM   5666  O OE1   . GLN A 1 2346 ? 159.038 184.977 176.676 1.00 86.64  ? 2346 GLN A OE1   1 
ATOM   5667  N NE2   . GLN A 1 2346 ? 158.736 184.317 178.801 1.00 86.64  ? 2346 GLN A NE2   1 
ATOM   5668  N N     . ASP A 1 2347 ? 163.656 185.279 177.316 1.00 98.48  ? 2347 ASP A N     1 
ATOM   5669  C CA    . ASP A 1 2347 ? 164.344 184.105 177.836 1.00 98.48  ? 2347 ASP A CA    1 
ATOM   5670  C C     . ASP A 1 2347 ? 165.837 184.076 177.556 1.00 98.48  ? 2347 ASP A C     1 
ATOM   5671  O O     . ASP A 1 2347 ? 166.597 183.645 178.425 1.00 98.48  ? 2347 ASP A O     1 
ATOM   5672  C CB    . ASP A 1 2347 ? 163.715 182.826 177.271 1.00 98.48  ? 2347 ASP A CB    1 
ATOM   5673  C CG    . ASP A 1 2347 ? 162.766 182.160 178.250 1.00 98.48  ? 2347 ASP A CG    1 
ATOM   5674  O OD1   . ASP A 1 2347 ? 162.639 182.657 179.389 1.00 98.48  ? 2347 ASP A OD1   1 
ATOM   5675  O OD2   . ASP A 1 2347 ? 162.146 181.140 177.881 1.00 98.48  ? 2347 ASP A OD2   1 
ATOM   5676  N N     . LEU A 1 2348 ? 166.276 184.519 176.377 1.00 92.14  ? 2348 LEU A N     1 
ATOM   5677  C CA    . LEU A 1 2348 ? 167.680 184.420 175.975 1.00 92.14  ? 2348 LEU A CA    1 
ATOM   5678  C C     . LEU A 1 2348 ? 168.150 182.973 176.090 1.00 92.14  ? 2348 LEU A C     1 
ATOM   5679  O O     . LEU A 1 2348 ? 168.956 182.621 176.953 1.00 92.14  ? 2348 LEU A O     1 
ATOM   5680  C CB    . LEU A 1 2348 ? 168.567 185.361 176.796 1.00 92.14  ? 2348 LEU A CB    1 
ATOM   5681  C CG    . LEU A 1 2348 ? 169.940 185.821 176.279 1.00 92.14  ? 2348 LEU A CG    1 
ATOM   5682  C CD1   . LEU A 1 2348 ? 170.503 186.870 177.218 1.00 92.14  ? 2348 LEU A CD1   1 
ATOM   5683  C CD2   . LEU A 1 2348 ? 170.965 184.714 176.086 1.00 92.14  ? 2348 LEU A CD2   1 
ATOM   5684  N N     . LYS A 1 2349 ? 167.587 182.113 175.247 1.00 95.88  ? 2349 LYS A N     1 
ATOM   5685  C CA    . LYS A 1 2349 ? 167.956 180.708 175.235 1.00 95.88  ? 2349 LYS A CA    1 
ATOM   5686  C C     . LYS A 1 2349 ? 168.281 180.180 173.848 1.00 95.88  ? 2349 LYS A C     1 
ATOM   5687  O O     . LYS A 1 2349 ? 169.135 179.294 173.730 1.00 95.88  ? 2349 LYS A O     1 
ATOM   5688  C CB    . LYS A 1 2349 ? 166.837 179.862 175.866 1.00 95.88  ? 2349 LYS A CB    1 
ATOM   5689  C CG    . LYS A 1 2349 ? 166.972 178.369 175.678 1.00 95.88  ? 2349 LYS A CG    1 
ATOM   5690  C CD    . LYS A 1 2349 ? 165.618 177.697 175.736 1.00 95.88  ? 2349 LYS A CD    1 
ATOM   5691  C CE    . LYS A 1 2349 ? 164.979 177.677 174.369 1.00 95.88  ? 2349 LYS A CE    1 
ATOM   5692  N NZ    . LYS A 1 2349 ? 165.800 176.927 173.381 1.00 95.88  ? 2349 LYS A NZ    1 
ATOM   5693  N N     . TYR A 1 2350 ? 167.662 180.716 172.798 1.00 102.57 ? 2350 TYR A N     1 
ATOM   5694  C CA    . TYR A 1 2350 ? 168.004 180.359 171.429 1.00 102.57 ? 2350 TYR A CA    1 
ATOM   5695  C C     . TYR A 1 2350 ? 169.136 181.212 170.872 1.00 102.57 ? 2350 TYR A C     1 
ATOM   5696  O O     . TYR A 1 2350 ? 169.272 181.329 169.648 1.00 102.57 ? 2350 TYR A O     1 
ATOM   5697  C CB    . TYR A 1 2350 ? 166.772 180.474 170.531 1.00 102.57 ? 2350 TYR A CB    1 
ATOM   5698  C CG    . TYR A 1 2350 ? 165.824 179.301 170.615 1.00 102.57 ? 2350 TYR A CG    1 
ATOM   5699  C CD1   . TYR A 1 2350 ? 166.139 178.083 170.032 1.00 102.57 ? 2350 TYR A CD1   1 
ATOM   5700  C CD2   . TYR A 1 2350 ? 164.601 179.422 171.256 1.00 102.57 ? 2350 TYR A CD2   1 
ATOM   5701  C CE1   . TYR A 1 2350 ? 165.270 177.013 170.103 1.00 102.57 ? 2350 TYR A CE1   1 
ATOM   5702  C CE2   . TYR A 1 2350 ? 163.723 178.360 171.325 1.00 102.57 ? 2350 TYR A CE2   1 
ATOM   5703  C CZ    . TYR A 1 2350 ? 164.063 177.158 170.751 1.00 102.57 ? 2350 TYR A CZ    1 
ATOM   5704  O OH    . TYR A 1 2350 ? 163.189 176.100 170.825 1.00 102.57 ? 2350 TYR A OH    1 
ATOM   5705  N N     . ALA A 1 2351 ? 169.952 181.814 171.732 1.00 102.74 ? 2351 ALA A N     1 
ATOM   5706  C CA    . ALA A 1 2351 ? 170.991 182.744 171.312 1.00 102.74 ? 2351 ALA A CA    1 
ATOM   5707  C C     . ALA A 1 2351 ? 172.363 182.118 171.514 1.00 102.74 ? 2351 ALA A C     1 
ATOM   5708  O O     . ALA A 1 2351 ? 172.599 181.438 172.518 1.00 102.74 ? 2351 ALA A O     1 
ATOM   5709  C CB    . ALA A 1 2351 ? 170.894 184.058 172.088 1.00 102.74 ? 2351 ALA A CB    1 
ATOM   5710  N N     . THR A 1 2352 ? 173.261 182.357 170.564 1.00 108.40 ? 2352 THR A N     1 
ATOM   5711  C CA    . THR A 1 2352 ? 174.602 181.803 170.630 1.00 108.40 ? 2352 THR A CA    1 
ATOM   5712  C C     . THR A 1 2352 ? 175.420 182.496 171.715 1.00 108.40 ? 2352 THR A C     1 
ATOM   5713  O O     . THR A 1 2352 ? 175.106 183.604 172.157 1.00 108.40 ? 2352 THR A O     1 
ATOM   5714  C CB    . THR A 1 2352 ? 175.306 181.947 169.283 1.00 108.40 ? 2352 THR A CB    1 
ATOM   5715  O OG1   . THR A 1 2352 ? 175.034 183.245 168.740 1.00 108.40 ? 2352 THR A OG1   1 
ATOM   5716  C CG2   . THR A 1 2352 ? 174.814 180.889 168.312 1.00 108.40 ? 2352 THR A CG2   1 
ATOM   5717  N N     . LEU A 1 2353 ? 176.489 181.822 172.144 1.00 105.58 ? 2353 LEU A N     1 
ATOM   5718  C CA    . LEU A 1 2353 ? 177.371 182.408 173.147 1.00 105.58 ? 2353 LEU A CA    1 
ATOM   5719  C C     . LEU A 1 2353 ? 178.084 183.643 172.618 1.00 105.58 ? 2353 LEU A C     1 
ATOM   5720  O O     . LEU A 1 2353 ? 178.449 184.527 173.401 1.00 105.58 ? 2353 LEU A O     1 
ATOM   5721  C CB    . LEU A 1 2353 ? 178.389 181.376 173.626 1.00 105.58 ? 2353 LEU A CB    1 
ATOM   5722  C CG    . LEU A 1 2353 ? 178.090 180.725 174.977 1.00 105.58 ? 2353 LEU A CG    1 
ATOM   5723  C CD1   . LEU A 1 2353 ? 178.162 181.755 176.090 1.00 105.58 ? 2353 LEU A CD1   1 
ATOM   5724  C CD2   . LEU A 1 2353 ? 176.732 180.049 174.957 1.00 105.58 ? 2353 LEU A CD2   1 
ATOM   5725  N N     . ALA A 1 2354 ? 178.290 183.725 171.303 1.00 109.09 ? 2354 ALA A N     1 
ATOM   5726  C CA    . ALA A 1 2354 ? 178.972 184.881 170.734 1.00 109.09 ? 2354 ALA A CA    1 
ATOM   5727  C C     . ALA A 1 2354 ? 178.182 186.160 170.967 1.00 109.09 ? 2354 ALA A C     1 
ATOM   5728  O O     . ALA A 1 2354 ? 178.761 187.214 171.251 1.00 109.09 ? 2354 ALA A O     1 
ATOM   5729  C CB    . ALA A 1 2354 ? 179.212 184.666 169.241 1.00 109.09 ? 2354 ALA A CB    1 
ATOM   5730  N N     . THR A 1 2355 ? 176.856 186.088 170.846 1.00 105.81 ? 2355 THR A N     1 
ATOM   5731  C CA    . THR A 1 2355 ? 176.034 187.281 171.011 1.00 105.81 ? 2355 THR A CA    1 
ATOM   5732  C C     . THR A 1 2355 ? 176.024 187.755 172.459 1.00 105.81 ? 2355 THR A C     1 
ATOM   5733  O O     . THR A 1 2355 ? 176.193 188.948 172.733 1.00 105.81 ? 2355 THR A O     1 
ATOM   5734  C CB    . THR A 1 2355 ? 174.612 187.005 170.532 1.00 105.81 ? 2355 THR A CB    1 
ATOM   5735  O OG1   . THR A 1 2355 ? 174.655 186.427 169.222 1.00 105.81 ? 2355 THR A OG1   1 
ATOM   5736  C CG2   . THR A 1 2355 ? 173.817 188.294 170.482 1.00 105.81 ? 2355 THR A CG2   1 
ATOM   5737  N N     . VAL A 1 2356 ? 175.820 186.834 173.403 1.00 107.29 ? 2356 VAL A N     1 
ATOM   5738  C CA    . VAL A 1 2356 ? 175.722 187.224 174.806 1.00 107.29 ? 2356 VAL A CA    1 
ATOM   5739  C C     . VAL A 1 2356 ? 177.081 187.654 175.349 1.00 107.29 ? 2356 VAL A C     1 
ATOM   5740  O O     . VAL A 1 2356 ? 177.174 188.598 176.142 1.00 107.29 ? 2356 VAL A O     1 
ATOM   5741  C CB    . VAL A 1 2356 ? 175.107 186.082 175.635 1.00 107.29 ? 2356 VAL A CB    1 
ATOM   5742  C CG1   . VAL A 1 2356 ? 175.858 184.788 175.405 1.00 107.29 ? 2356 VAL A CG1   1 
ATOM   5743  C CG2   . VAL A 1 2356 ? 175.091 186.442 177.110 1.00 107.29 ? 2356 VAL A CG2   1 
ATOM   5744  N N     . SER A 1 2357 ? 178.156 186.978 174.933 1.00 108.85 ? 2357 SER A N     1 
ATOM   5745  C CA    . SER A 1 2357 ? 179.477 187.282 175.473 1.00 108.85 ? 2357 SER A CA    1 
ATOM   5746  C C     . SER A 1 2357 ? 179.934 188.687 175.105 1.00 108.85 ? 2357 SER A C     1 
ATOM   5747  O O     . SER A 1 2357 ? 180.812 189.246 175.770 1.00 108.85 ? 2357 SER A O     1 
ATOM   5748  C CB    . SER A 1 2357 ? 180.492 186.253 174.980 1.00 108.85 ? 2357 SER A CB    1 
ATOM   5749  O OG    . SER A 1 2357 ? 180.337 186.015 173.592 1.00 108.85 ? 2357 SER A OG    1 
ATOM   5750  N N     . ARG A 1 2358 ? 179.365 189.268 174.055 1.00 111.32 ? 2358 ARG A N     1 
ATOM   5751  C CA    . ARG A 1 2358 ? 179.702 190.627 173.659 1.00 111.32 ? 2358 ARG A CA    1 
ATOM   5752  C C     . ARG A 1 2358 ? 178.822 191.674 174.327 1.00 111.32 ? 2358 ARG A C     1 
ATOM   5753  O O     . ARG A 1 2358 ? 178.917 192.853 173.974 1.00 111.32 ? 2358 ARG A O     1 
ATOM   5754  C CB    . ARG A 1 2358 ? 179.591 190.774 172.142 1.00 111.32 ? 2358 ARG A CB    1 
ATOM   5755  C CG    . ARG A 1 2358 ? 180.627 190.007 171.355 1.00 111.32 ? 2358 ARG A CG    1 
ATOM   5756  C CD    . ARG A 1 2358 ? 180.433 190.226 169.865 1.00 111.32 ? 2358 ARG A CD    1 
ATOM   5757  N NE    . ARG A 1 2358 ? 180.406 188.972 169.124 1.00 111.32 ? 2358 ARG A NE    1 
ATOM   5758  C CZ    . ARG A 1 2358 ? 181.488 188.312 168.736 1.00 111.32 ? 2358 ARG A CZ    1 
ATOM   5759  N NH1   . ARG A 1 2358 ? 182.703 188.755 169.011 1.00 111.32 ? 2358 ARG A NH1   1 
ATOM   5760  N NH2   . ARG A 1 2358 ? 181.347 187.176 168.059 1.00 111.32 ? 2358 ARG A NH2   1 
ATOM   5761  N N     . CYS A 1 2359 ? 177.974 191.279 175.272 1.00 112.69 ? 2359 CYS A N     1 
ATOM   5762  C CA    . CYS A 1 2359 ? 176.937 192.147 175.815 1.00 112.69 ? 2359 CYS A CA    1 
ATOM   5763  C C     . CYS A 1 2359 ? 177.099 192.274 177.320 1.00 112.69 ? 2359 CYS A C     1 
ATOM   5764  O O     . CYS A 1 2359 ? 177.152 191.264 178.029 1.00 112.69 ? 2359 CYS A O     1 
ATOM   5765  C CB    . CYS A 1 2359 ? 175.549 191.593 175.495 1.00 112.69 ? 2359 CYS A CB    1 
ATOM   5766  S SG    . CYS A 1 2359 ? 174.812 192.205 173.979 1.00 112.69 ? 2359 CYS A SG    1 
ATOM   5767  N N     . GLY A 1 2360 ? 177.172 193.510 177.805 1.00 101.37 ? 2360 GLY A N     1 
ATOM   5768  C CA    . GLY A 1 2360 ? 176.934 193.755 179.217 1.00 101.37 ? 2360 GLY A CA    1 
ATOM   5769  C C     . GLY A 1 2360 ? 175.445 193.676 179.490 1.00 101.37 ? 2360 GLY A C     1 
ATOM   5770  O O     . GLY A 1 2360 ? 174.657 194.444 178.926 1.00 101.37 ? 2360 GLY A O     1 
ATOM   5771  N N     . MET A 1 2361 ? 175.044 192.738 180.341 1.00 94.39  ? 2361 MET A N     1 
ATOM   5772  C CA    . MET A 1 2361 ? 173.650 192.333 180.354 1.00 94.39  ? 2361 MET A CA    1 
ATOM   5773  C C     . MET A 1 2361 ? 173.081 192.441 181.758 1.00 94.39  ? 2361 MET A C     1 
ATOM   5774  O O     . MET A 1 2361 ? 173.734 192.062 182.733 1.00 94.39  ? 2361 MET A O     1 
ATOM   5775  C CB    . MET A 1 2361 ? 173.515 190.906 179.825 1.00 94.39  ? 2361 MET A CB    1 
ATOM   5776  C CG    . MET A 1 2361 ? 172.357 190.110 180.364 1.00 94.39  ? 2361 MET A CG    1 
ATOM   5777  S SD    . MET A 1 2361 ? 172.819 189.054 181.716 1.00 94.39  ? 2361 MET A SD    1 
ATOM   5778  C CE    . MET A 1 2361 ? 173.391 187.645 180.795 1.00 94.39  ? 2361 MET A CE    1 
ATOM   5779  N N     . VAL A 1 2362 ? 171.858 192.957 181.850 1.00 85.42  ? 2362 VAL A N     1 
ATOM   5780  C CA    . VAL A 1 2362 ? 171.149 193.118 183.112 1.00 85.42  ? 2362 VAL A CA    1 
ATOM   5781  C C     . VAL A 1 2362 ? 169.979 192.150 183.133 1.00 85.42  ? 2362 VAL A C     1 
ATOM   5782  O O     . VAL A 1 2362 ? 169.191 192.102 182.182 1.00 85.42  ? 2362 VAL A O     1 
ATOM   5783  C CB    . VAL A 1 2362 ? 170.652 194.560 183.309 1.00 85.42  ? 2362 VAL A CB    1 
ATOM   5784  C CG1   . VAL A 1 2362 ? 169.867 194.667 184.598 1.00 85.42  ? 2362 VAL A CG1   1 
ATOM   5785  C CG2   . VAL A 1 2362 ? 171.819 195.522 183.318 1.00 85.42  ? 2362 VAL A CG2   1 
ATOM   5786  N N     . TRP A 1 2363 ? 169.866 191.383 184.209 1.00 80.92  ? 2363 TRP A N     1 
ATOM   5787  C CA    . TRP A 1 2363 ? 168.769 190.445 184.384 1.00 80.92  ? 2363 TRP A CA    1 
ATOM   5788  C C     . TRP A 1 2363 ? 167.694 191.066 185.262 1.00 80.92  ? 2363 TRP A C     1 
ATOM   5789  O O     . TRP A 1 2363 ? 167.990 191.618 186.324 1.00 80.92  ? 2363 TRP A O     1 
ATOM   5790  C CB    . TRP A 1 2363 ? 169.258 189.142 185.010 1.00 80.92  ? 2363 TRP A CB    1 
ATOM   5791  C CG    . TRP A 1 2363 ? 168.221 188.075 185.045 1.00 80.92  ? 2363 TRP A CG    1 
ATOM   5792  C CD1   . TRP A 1 2363 ? 167.220 187.935 185.959 1.00 80.92  ? 2363 TRP A CD1   1 
ATOM   5793  C CD2   . TRP A 1 2363 ? 168.081 186.988 184.126 1.00 80.92  ? 2363 TRP A CD2   1 
ATOM   5794  N NE1   . TRP A 1 2363 ? 166.464 186.827 185.667 1.00 80.92  ? 2363 TRP A NE1   1 
ATOM   5795  C CE2   . TRP A 1 2363 ? 166.973 186.228 184.545 1.00 80.92  ? 2363 TRP A CE2   1 
ATOM   5796  C CE3   . TRP A 1 2363 ? 168.785 186.582 182.992 1.00 80.92  ? 2363 TRP A CE3   1 
ATOM   5797  C CZ2   . TRP A 1 2363 ? 166.552 185.090 183.868 1.00 80.92  ? 2363 TRP A CZ2   1 
ATOM   5798  C CZ3   . TRP A 1 2363 ? 168.367 185.452 182.323 1.00 80.92  ? 2363 TRP A CZ3   1 
ATOM   5799  C CH2   . TRP A 1 2363 ? 167.261 184.720 182.761 1.00 80.92  ? 2363 TRP A CH2   1 
ATOM   5800  N N     . PHE A 1 2364 ? 166.447 190.973 184.812 1.00 77.70  ? 2364 PHE A N     1 
ATOM   5801  C CA    . PHE A 1 2364 ? 165.296 191.497 185.543 1.00 77.70  ? 2364 PHE A CA    1 
ATOM   5802  C C     . PHE A 1 2364 ? 164.482 190.308 186.035 1.00 77.70  ? 2364 PHE A C     1 
ATOM   5803  O O     . PHE A 1 2364 ? 163.527 189.890 185.379 1.00 77.70  ? 2364 PHE A O     1 
ATOM   5804  C CB    . PHE A 1 2364 ? 164.450 192.403 184.671 1.00 77.70  ? 2364 PHE A CB    1 
ATOM   5805  C CG    . PHE A 1 2364 ? 165.057 193.745 184.418 1.00 77.70  ? 2364 PHE A CG    1 
ATOM   5806  C CD1   . PHE A 1 2364 ? 165.879 193.948 183.329 1.00 77.70  ? 2364 PHE A CD1   1 
ATOM   5807  C CD2   . PHE A 1 2364 ? 164.798 194.805 185.260 1.00 77.70  ? 2364 PHE A CD2   1 
ATOM   5808  C CE1   . PHE A 1 2364 ? 166.434 195.182 183.088 1.00 77.70  ? 2364 PHE A CE1   1 
ATOM   5809  C CE2   . PHE A 1 2364 ? 165.350 196.040 185.022 1.00 77.70  ? 2364 PHE A CE2   1 
ATOM   5810  C CZ    . PHE A 1 2364 ? 166.171 196.229 183.937 1.00 77.70  ? 2364 PHE A CZ    1 
ATOM   5811  N N     . SER A 1 2365 ? 164.848 189.773 187.194 1.00 80.12  ? 2365 SER A N     1 
ATOM   5812  C CA    . SER A 1 2365 ? 164.096 188.665 187.757 1.00 80.12  ? 2365 SER A CA    1 
ATOM   5813  C C     . SER A 1 2365 ? 162.682 189.113 188.106 1.00 80.12  ? 2365 SER A C     1 
ATOM   5814  O O     . SER A 1 2365 ? 162.438 190.277 188.428 1.00 80.12  ? 2365 SER A O     1 
ATOM   5815  C CB    . SER A 1 2365 ? 164.795 188.122 188.998 1.00 80.12  ? 2365 SER A CB    1 
ATOM   5816  O OG    . SER A 1 2365 ? 165.318 189.178 189.781 1.00 80.12  ? 2365 SER A OG    1 
ATOM   5817  N N     . GLU A 1 2366 ? 161.742 188.170 188.027 1.00 85.18  ? 2366 GLU A N     1 
ATOM   5818  C CA    . GLU A 1 2366 ? 160.348 188.496 188.308 1.00 85.18  ? 2366 GLU A CA    1 
ATOM   5819  C C     . GLU A 1 2366 ? 160.171 189.019 189.725 1.00 85.18  ? 2366 GLU A C     1 
ATOM   5820  O O     . GLU A 1 2366 ? 159.296 189.856 189.972 1.00 85.18  ? 2366 GLU A O     1 
ATOM   5821  C CB    . GLU A 1 2366 ? 159.469 187.267 188.075 1.00 85.18  ? 2366 GLU A CB    1 
ATOM   5822  C CG    . GLU A 1 2366 ? 158.071 187.351 188.675 1.00 85.18  ? 2366 GLU A CG    1 
ATOM   5823  C CD    . GLU A 1 2366 ? 157.086 188.089 187.788 1.00 85.18  ? 2366 GLU A CD    1 
ATOM   5824  O OE1   . GLU A 1 2366 ? 157.526 188.878 186.926 1.00 85.18  ? 2366 GLU A OE1   1 
ATOM   5825  O OE2   . GLU A 1 2366 ? 155.866 187.883 187.955 1.00 85.18  ? 2366 GLU A OE2   1 
ATOM   5826  N N     . ASP A 1 2367 ? 161.008 188.566 190.660 1.00 85.01  ? 2367 ASP A N     1 
ATOM   5827  C CA    . ASP A 1 2367 ? 160.915 189.040 192.034 1.00 85.01  ? 2367 ASP A CA    1 
ATOM   5828  C C     . ASP A 1 2367 ? 161.124 190.543 192.137 1.00 85.01  ? 2367 ASP A C     1 
ATOM   5829  O O     . ASP A 1 2367 ? 160.702 191.150 193.126 1.00 85.01  ? 2367 ASP A O     1 
ATOM   5830  C CB    . ASP A 1 2367 ? 161.936 188.315 192.910 1.00 85.01  ? 2367 ASP A CB    1 
ATOM   5831  C CG    . ASP A 1 2367 ? 162.072 186.853 192.552 1.00 85.01  ? 2367 ASP A CG    1 
ATOM   5832  O OD1   . ASP A 1 2367 ? 163.177 186.299 192.717 1.00 85.01  ? 2367 ASP A OD1   1 
ATOM   5833  O OD2   . ASP A 1 2367 ? 161.074 186.259 192.095 1.00 85.01  ? 2367 ASP A OD2   1 
ATOM   5834  N N     . VAL A 1 2368 ? 161.769 191.153 191.142 1.00 82.81  ? 2368 VAL A N     1 
ATOM   5835  C CA    . VAL A 1 2368 ? 161.947 192.600 191.148 1.00 82.81  ? 2368 VAL A CA    1 
ATOM   5836  C C     . VAL A 1 2368 ? 160.598 193.300 191.112 1.00 82.81  ? 2368 VAL A C     1 
ATOM   5837  O O     . VAL A 1 2368 ? 160.349 194.245 191.871 1.00 82.81  ? 2368 VAL A O     1 
ATOM   5838  C CB    . VAL A 1 2368 ? 162.839 193.031 189.971 1.00 82.81  ? 2368 VAL A CB    1 
ATOM   5839  C CG1   . VAL A 1 2368 ? 162.587 194.476 189.619 1.00 82.81  ? 2368 VAL A CG1   1 
ATOM   5840  C CG2   . VAL A 1 2368 ? 164.298 192.821 190.320 1.00 82.81  ? 2368 VAL A CG2   1 
ATOM   5841  N N     . LEU A 1 2369 ? 159.701 192.842 190.248 1.00 80.43  ? 2369 LEU A N     1 
ATOM   5842  C CA    . LEU A 1 2369 ? 158.408 193.493 190.065 1.00 80.43  ? 2369 LEU A CA    1 
ATOM   5843  C C     . LEU A 1 2369 ? 157.397 192.826 190.988 1.00 80.43  ? 2369 LEU A C     1 
ATOM   5844  O O     . LEU A 1 2369 ? 156.882 191.747 190.691 1.00 80.43  ? 2369 LEU A O     1 
ATOM   5845  C CB    . LEU A 1 2369 ? 157.982 193.430 188.605 1.00 80.43  ? 2369 LEU A CB    1 
ATOM   5846  C CG    . LEU A 1 2369 ? 156.893 194.403 188.169 1.00 80.43  ? 2369 LEU A CG    1 
ATOM   5847  C CD1   . LEU A 1 2369 ? 156.974 194.635 186.682 1.00 80.43  ? 2369 LEU A CD1   1 
ATOM   5848  C CD2   . LEU A 1 2369 ? 155.543 193.846 188.519 1.00 80.43  ? 2369 LEU A CD2   1 
ATOM   5849  N N     . SER A 1 2370 ? 157.100 193.478 192.106 1.00 81.23  ? 2370 SER A N     1 
ATOM   5850  C CA    . SER A 1 2370 ? 156.132 192.953 193.050 1.00 81.23  ? 2370 SER A CA    1 
ATOM   5851  C C     . SER A 1 2370 ? 154.720 193.380 192.660 1.00 81.23  ? 2370 SER A C     1 
ATOM   5852  O O     . SER A 1 2370 ? 154.511 194.359 191.940 1.00 81.23  ? 2370 SER A O     1 
ATOM   5853  C CB    . SER A 1 2370 ? 156.453 193.429 194.463 1.00 81.23  ? 2370 SER A CB    1 
ATOM   5854  O OG    . SER A 1 2370 ? 156.324 194.836 194.556 1.00 81.23  ? 2370 SER A OG    1 
ATOM   5855  N N     . THR A 1 2371 ? 153.735 192.633 193.161 1.00 79.65  ? 2371 THR A N     1 
ATOM   5856  C CA    . THR A 1 2371 ? 152.347 192.939 192.840 1.00 79.65  ? 2371 THR A CA    1 
ATOM   5857  C C     . THR A 1 2371 ? 151.907 194.263 193.446 1.00 79.65  ? 2371 THR A C     1 
ATOM   5858  O O     . THR A 1 2371 ? 150.961 194.889 192.952 1.00 79.65  ? 2371 THR A O     1 
ATOM   5859  C CB    . THR A 1 2371 ? 151.436 191.818 193.329 1.00 79.65  ? 2371 THR A CB    1 
ATOM   5860  O OG1   . THR A 1 2371 ? 151.294 191.913 194.749 1.00 79.65  ? 2371 THR A OG1   1 
ATOM   5861  C CG2   . THR A 1 2371 ? 152.030 190.468 192.983 1.00 79.65  ? 2371 THR A CG2   1 
ATOM   5862  N N     . ASP A 1 2372 ? 152.570 194.701 194.515 1.00 83.99  ? 2372 ASP A N     1 
ATOM   5863  C CA    . ASP A 1 2372 ? 152.161 195.935 195.172 1.00 83.99  ? 2372 ASP A CA    1 
ATOM   5864  C C     . ASP A 1 2372 ? 152.315 197.132 194.245 1.00 83.99  ? 2372 ASP A C     1 
ATOM   5865  O O     . ASP A 1 2372 ? 151.436 198.000 194.194 1.00 83.99  ? 2372 ASP A O     1 
ATOM   5866  C CB    . ASP A 1 2372 ? 152.961 196.132 196.455 1.00 83.99  ? 2372 ASP A CB    1 
ATOM   5867  C CG    . ASP A 1 2372 ? 152.707 195.035 197.467 1.00 83.99  ? 2372 ASP A CG    1 
ATOM   5868  O OD1   . ASP A 1 2372 ? 151.542 194.871 197.886 1.00 83.99  ? 2372 ASP A OD1   1 
ATOM   5869  O OD2   . ASP A 1 2372 ? 153.669 194.333 197.840 1.00 83.99  ? 2372 ASP A OD2   1 
ATOM   5870  N N     . MET A 1 2373 ? 153.419 197.199 193.497 1.00 79.03  ? 2373 MET A N     1 
ATOM   5871  C CA    . MET A 1 2373 ? 153.573 198.329 192.590 1.00 79.03  ? 2373 MET A CA    1 
ATOM   5872  C C     . MET A 1 2373 ? 152.621 198.232 191.409 1.00 79.03  ? 2373 MET A C     1 
ATOM   5873  O O     . MET A 1 2373 ? 152.184 199.263 190.895 1.00 79.03  ? 2373 MET A O     1 
ATOM   5874  C CB    . MET A 1 2373 ? 155.013 198.469 192.101 1.00 79.03  ? 2373 MET A CB    1 
ATOM   5875  C CG    . MET A 1 2373 ? 156.064 197.965 193.053 1.00 79.03  ? 2373 MET A CG    1 
ATOM   5876  S SD    . MET A 1 2373 ? 157.696 198.079 192.306 1.00 79.03  ? 2373 MET A SD    1 
ATOM   5877  C CE    . MET A 1 2373 ? 157.724 196.598 191.327 1.00 79.03  ? 2373 MET A CE    1 
ATOM   5878  N N     . ILE A 1 2374 ? 152.274 197.021 190.975 1.00 67.56  ? 2374 ILE A N     1 
ATOM   5879  C CA    . ILE A 1 2374 ? 151.242 196.887 189.950 1.00 67.56  ? 2374 ILE A CA    1 
ATOM   5880  C C     . ILE A 1 2374 ? 149.934 197.479 190.449 1.00 67.56  ? 2374 ILE A C     1 
ATOM   5881  O O     . ILE A 1 2374 ? 149.265 198.244 189.745 1.00 67.56  ? 2374 ILE A O     1 
ATOM   5882  C CB    . ILE A 1 2374 ? 151.060 195.415 189.551 1.00 67.56  ? 2374 ILE A CB    1 
ATOM   5883  C CG1   . ILE A 1 2374 ? 152.296 194.900 188.831 1.00 67.56  ? 2374 ILE A CG1   1 
ATOM   5884  C CG2   . ILE A 1 2374 ? 149.838 195.267 188.675 1.00 67.56  ? 2374 ILE A CG2   1 
ATOM   5885  C CD1   . ILE A 1 2374 ? 152.272 195.125 187.346 1.00 67.56  ? 2374 ILE A CD1   1 
ATOM   5886  N N     . PHE A 1 2375 ? 149.554 197.135 191.679 1.00 75.20  ? 2375 PHE A N     1 
ATOM   5887  C CA    . PHE A 1 2375 ? 148.309 197.651 192.232 1.00 75.20  ? 2375 PHE A CA    1 
ATOM   5888  C C     . PHE A 1 2375 ? 148.353 199.166 192.362 1.00 75.20  ? 2375 PHE A C     1 
ATOM   5889  O O     . PHE A 1 2375 ? 147.388 199.855 192.013 1.00 75.20  ? 2375 PHE A O     1 
ATOM   5890  C CB    . PHE A 1 2375 ? 148.031 197.010 193.590 1.00 75.20  ? 2375 PHE A CB    1 
ATOM   5891  C CG    . PHE A 1 2375 ? 147.731 195.544 193.519 1.00 75.20  ? 2375 PHE A CG    1 
ATOM   5892  C CD1   . PHE A 1 2375 ? 147.527 194.920 192.304 1.00 75.20  ? 2375 PHE A CD1   1 
ATOM   5893  C CD2   . PHE A 1 2375 ? 147.659 194.789 194.671 1.00 75.20  ? 2375 PHE A CD2   1 
ATOM   5894  C CE1   . PHE A 1 2375 ? 147.256 193.575 192.243 1.00 75.20  ? 2375 PHE A CE1   1 
ATOM   5895  C CE2   . PHE A 1 2375 ? 147.388 193.443 194.614 1.00 75.20  ? 2375 PHE A CE2   1 
ATOM   5896  C CZ    . PHE A 1 2375 ? 147.186 192.836 193.399 1.00 75.20  ? 2375 PHE A CZ    1 
ATOM   5897  N N     . ASN A 1 2376 ? 149.465 199.703 192.866 1.00 76.89  ? 2376 ASN A N     1 
ATOM   5898  C CA    . ASN A 1 2376 ? 149.567 201.149 193.035 1.00 76.89  ? 2376 ASN A CA    1 
ATOM   5899  C C     . ASN A 1 2376 ? 149.546 201.867 191.692 1.00 76.89  ? 2376 ASN A C     1 
ATOM   5900  O O     . ASN A 1 2376 ? 148.930 202.930 191.564 1.00 76.89  ? 2376 ASN A O     1 
ATOM   5901  C CB    . ASN A 1 2376 ? 150.826 201.499 193.823 1.00 76.89  ? 2376 ASN A CB    1 
ATOM   5902  C CG    . ASN A 1 2376 ? 150.730 201.084 195.274 1.00 76.89  ? 2376 ASN A CG    1 
ATOM   5903  O OD1   . ASN A 1 2376 ? 149.718 200.537 195.704 1.00 76.89  ? 2376 ASN A OD1   1 
ATOM   5904  N ND2   . ASN A 1 2376 ? 151.782 201.345 196.037 1.00 76.89  ? 2376 ASN A ND2   1 
ATOM   5905  N N     . ASN A 1 2377 ? 150.208 201.303 190.681 1.00 78.45  ? 2377 ASN A N     1 
ATOM   5906  C CA    . ASN A 1 2377 ? 150.167 201.891 189.349 1.00 78.45  ? 2377 ASN A CA    1 
ATOM   5907  C C     . ASN A 1 2377 ? 148.756 201.880 188.784 1.00 78.45  ? 2377 ASN A C     1 
ATOM   5908  O O     . ASN A 1 2377 ? 148.305 202.875 188.203 1.00 78.45  ? 2377 ASN A O     1 
ATOM   5909  C CB    . ASN A 1 2377 ? 151.113 201.138 188.421 1.00 78.45  ? 2377 ASN A CB    1 
ATOM   5910  C CG    . ASN A 1 2377 ? 150.837 201.413 186.962 1.00 78.45  ? 2377 ASN A CG    1 
ATOM   5911  O OD1   . ASN A 1 2377 ? 150.568 200.498 186.188 1.00 78.45  ? 2377 ASN A OD1   1 
ATOM   5912  N ND2   . ASN A 1 2377 ? 150.900 202.679 186.577 1.00 78.45  ? 2377 ASN A ND2   1 
ATOM   5913  N N     . PHE A 1 2378 ? 148.045 200.763 188.937 1.00 76.69  ? 2378 PHE A N     1 
ATOM   5914  C CA    . PHE A 1 2378 ? 146.675 200.707 188.444 1.00 76.69  ? 2378 PHE A CA    1 
ATOM   5915  C C     . PHE A 1 2378 ? 145.803 201.729 189.152 1.00 76.69  ? 2378 PHE A C     1 
ATOM   5916  O O     . PHE A 1 2378 ? 144.999 202.418 188.516 1.00 76.69  ? 2378 PHE A O     1 
ATOM   5917  C CB    . PHE A 1 2378 ? 146.102 199.306 188.627 1.00 76.69  ? 2378 PHE A CB    1 
ATOM   5918  C CG    . PHE A 1 2378 ? 144.611 199.245 188.498 1.00 76.69  ? 2378 PHE A CG    1 
ATOM   5919  C CD1   . PHE A 1 2378 ? 143.994 199.559 187.303 1.00 76.69  ? 2378 PHE A CD1   1 
ATOM   5920  C CD2   . PHE A 1 2378 ? 143.826 198.885 189.575 1.00 76.69  ? 2378 PHE A CD2   1 
ATOM   5921  C CE1   . PHE A 1 2378 ? 142.624 199.506 187.183 1.00 76.69  ? 2378 PHE A CE1   1 
ATOM   5922  C CE2   . PHE A 1 2378 ? 142.455 198.832 189.460 1.00 76.69  ? 2378 PHE A CE2   1 
ATOM   5923  C CZ    . PHE A 1 2378 ? 141.854 199.142 188.263 1.00 76.69  ? 2378 PHE A CZ    1 
ATOM   5924  N N     . LEU A 1 2379 ? 145.956 201.849 190.470 1.00 77.95  ? 2379 LEU A N     1 
ATOM   5925  C CA    . LEU A 1 2379 ? 145.152 202.805 191.220 1.00 77.95  ? 2379 LEU A CA    1 
ATOM   5926  C C     . LEU A 1 2379 ? 145.464 204.235 190.803 1.00 77.95  ? 2379 LEU A C     1 
ATOM   5927  O O     . LEU A 1 2379 ? 144.554 205.057 190.659 1.00 77.95  ? 2379 LEU A O     1 
ATOM   5928  C CB    . LEU A 1 2379 ? 145.379 202.619 192.718 1.00 77.95  ? 2379 LEU A CB    1 
ATOM   5929  C CG    . LEU A 1 2379 ? 144.787 201.356 193.344 1.00 77.95  ? 2379 LEU A CG    1 
ATOM   5930  C CD1   . LEU A 1 2379 ? 144.387 201.619 194.783 1.00 77.95  ? 2379 LEU A CD1   1 
ATOM   5931  C CD2   . LEU A 1 2379 ? 143.600 200.853 192.547 1.00 77.95  ? 2379 LEU A CD2   1 
ATOM   5932  N N     . ALA A 1 2380 ? 146.743 204.553 190.602 1.00 80.24  ? 2380 ALA A N     1 
ATOM   5933  C CA    . ALA A 1 2380 ? 147.105 205.903 190.185 1.00 80.24  ? 2380 ALA A CA    1 
ATOM   5934  C C     . ALA A 1 2380 ? 146.560 206.219 188.798 1.00 80.24  ? 2380 ALA A C     1 
ATOM   5935  O O     . ALA A 1 2380 ? 146.028 207.311 188.565 1.00 80.24  ? 2380 ALA A O     1 
ATOM   5936  C CB    . ALA A 1 2380 ? 148.621 206.075 190.217 1.00 80.24  ? 2380 ALA A CB    1 
ATOM   5937  N N     . ARG A 1 2381 ? 146.679 205.274 187.864 1.00 79.35  ? 2381 ARG A N     1 
ATOM   5938  C CA    . ARG A 1 2381 ? 146.140 205.498 186.528 1.00 79.35  ? 2381 ARG A CA    1 
ATOM   5939  C C     . ARG A 1 2381 ? 144.629 205.667 186.571 1.00 79.35  ? 2381 ARG A C     1 
ATOM   5940  O O     . ARG A 1 2381 ? 144.069 206.509 185.860 1.00 79.35  ? 2381 ARG A O     1 
ATOM   5941  C CB    . ARG A 1 2381 ? 146.526 204.347 185.605 1.00 79.35  ? 2381 ARG A CB    1 
ATOM   5942  C CG    . ARG A 1 2381 ? 147.999 204.300 185.276 1.00 79.35  ? 2381 ARG A CG    1 
ATOM   5943  C CD    . ARG A 1 2381 ? 148.297 203.177 184.312 1.00 79.35  ? 2381 ARG A CD    1 
ATOM   5944  N NE    . ARG A 1 2381 ? 147.445 203.249 183.133 1.00 79.35  ? 2381 ARG A NE    1 
ATOM   5945  C CZ    . ARG A 1 2381 ? 147.653 204.065 182.111 1.00 79.35  ? 2381 ARG A CZ    1 
ATOM   5946  N NH1   . ARG A 1 2381 ? 148.676 204.902 182.093 1.00 79.35  ? 2381 ARG A NH1   1 
ATOM   5947  N NH2   . ARG A 1 2381 ? 146.814 204.040 181.081 1.00 79.35  ? 2381 ARG A NH2   1 
ATOM   5948  N N     . LEU A 1 2382 ? 143.953 204.876 187.403 1.00 83.90  ? 2382 LEU A N     1 
ATOM   5949  C CA    . LEU A 1 2382 ? 142.511 205.017 187.552 1.00 83.90  ? 2382 LEU A CA    1 
ATOM   5950  C C     . LEU A 1 2382 ? 142.153 206.376 188.135 1.00 83.90  ? 2382 LEU A C     1 
ATOM   5951  O O     . LEU A 1 2382 ? 141.167 206.998 187.724 1.00 83.90  ? 2382 LEU A O     1 
ATOM   5952  C CB    . LEU A 1 2382 ? 141.974 203.889 188.431 1.00 83.90  ? 2382 LEU A CB    1 
ATOM   5953  C CG    . LEU A 1 2382 ? 140.533 203.980 188.920 1.00 83.90  ? 2382 LEU A CG    1 
ATOM   5954  C CD1   . LEU A 1 2382 ? 139.597 204.022 187.736 1.00 83.90  ? 2382 LEU A CD1   1 
ATOM   5955  C CD2   . LEU A 1 2382 ? 140.207 202.806 189.816 1.00 83.90  ? 2382 LEU A CD2   1 
ATOM   5956  N N     . ARG A 1 2383 ? 142.945 206.856 189.093 1.00 84.58  ? 2383 ARG A N     1 
ATOM   5957  C CA    . ARG A 1 2383 ? 142.662 208.126 189.742 1.00 84.58  ? 2383 ARG A CA    1 
ATOM   5958  C C     . ARG A 1 2383 ? 143.021 209.325 188.882 1.00 84.58  ? 2383 ARG A C     1 
ATOM   5959  O O     . ARG A 1 2383 ? 142.533 210.426 189.150 1.00 84.58  ? 2383 ARG A O     1 
ATOM   5960  C CB    . ARG A 1 2383 ? 143.413 208.221 191.070 1.00 84.58  ? 2383 ARG A CB    1 
ATOM   5961  C CG    . ARG A 1 2383 ? 142.765 207.455 192.203 1.00 84.58  ? 2383 ARG A CG    1 
ATOM   5962  C CD    . ARG A 1 2383 ? 143.085 208.085 193.542 1.00 84.58  ? 2383 ARG A CD    1 
ATOM   5963  N NE    . ARG A 1 2383 ? 142.748 207.200 194.649 1.00 84.58  ? 2383 ARG A NE    1 
ATOM   5964  C CZ    . ARG A 1 2383 ? 143.617 206.411 195.263 1.00 84.58  ? 2383 ARG A CZ    1 
ATOM   5965  N NH1   . ARG A 1 2383 ? 144.891 206.384 194.912 1.00 84.58  ? 2383 ARG A NH1   1 
ATOM   5966  N NH2   . ARG A 1 2383 ? 143.198 205.632 196.255 1.00 84.58  ? 2383 ARG A NH2   1 
ATOM   5967  N N     . SER A 1 2384 ? 143.861 209.147 187.866 1.00 84.79  ? 2384 SER A N     1 
ATOM   5968  C CA    . SER A 1 2384 ? 144.295 210.265 187.040 1.00 84.79  ? 2384 SER A CA    1 
ATOM   5969  C C     . SER A 1 2384 ? 143.778 210.200 185.613 1.00 84.79  ? 2384 SER A C     1 
ATOM   5970  O O     . SER A 1 2384 ? 143.182 211.165 185.128 1.00 84.79  ? 2384 SER A O     1 
ATOM   5971  C CB    . SER A 1 2384 ? 145.825 210.340 187.024 1.00 84.79  ? 2384 SER A CB    1 
ATOM   5972  O OG    . SER A 1 2384 ? 146.273 211.190 185.984 1.00 84.79  ? 2384 SER A OG    1 
ATOM   5973  N N     . ILE A 1 2385 ? 143.994 209.092 184.922 1.00 83.86  ? 2385 ILE A N     1 
ATOM   5974  C CA    . ILE A 1 2385 ? 143.656 209.012 183.500 1.00 83.86  ? 2385 ILE A CA    1 
ATOM   5975  C C     . ILE A 1 2385 ? 142.140 208.914 183.354 1.00 83.86  ? 2385 ILE A C     1 
ATOM   5976  O O     . ILE A 1 2385 ? 141.527 208.006 183.934 1.00 83.86  ? 2385 ILE A O     1 
ATOM   5977  C CB    . ILE A 1 2385 ? 144.348 207.820 182.852 1.00 83.86  ? 2385 ILE A CB    1 
ATOM   5978  C CG1   . ILE A 1 2385 ? 145.841 208.101 182.694 1.00 83.86  ? 2385 ILE A CG1   1 
ATOM   5979  C CG2   . ILE A 1 2385 ? 143.729 207.518 181.502 1.00 83.86  ? 2385 ILE A CG2   1 
ATOM   5980  C CD1   . ILE A 1 2385 ? 146.144 209.451 182.089 1.00 83.86  ? 2385 ILE A CD1   1 
ATOM   5981  N N     . PRO A 1 2386 ? 141.508 209.813 182.601 1.00 89.18  ? 2386 PRO A N     1 
ATOM   5982  C CA    . PRO A 1 2386 ? 140.070 209.680 182.344 1.00 89.18  ? 2386 PRO A CA    1 
ATOM   5983  C C     . PRO A 1 2386 ? 139.794 208.480 181.452 1.00 89.18  ? 2386 PRO A C     1 
ATOM   5984  O O     . PRO A 1 2386 ? 140.433 208.303 180.413 1.00 89.18  ? 2386 PRO A O     1 
ATOM   5985  C CB    . PRO A 1 2386 ? 139.705 210.994 181.640 1.00 89.18  ? 2386 PRO A CB    1 
ATOM   5986  C CG    . PRO A 1 2386 ? 140.886 211.895 181.823 1.00 89.18  ? 2386 PRO A CG    1 
ATOM   5987  C CD    . PRO A 1 2386 ? 142.074 211.012 181.967 1.00 89.18  ? 2386 PRO A CD    1 
ATOM   5988  N N     . LEU A 1 2387 ? 138.901 207.601 181.913 1.00 91.54  ? 2387 LEU A N     1 
ATOM   5989  C CA    . LEU A 1 2387 ? 138.601 206.368 181.140 1.00 91.54  ? 2387 LEU A CA    1 
ATOM   5990  C C     . LEU A 1 2387 ? 137.847 206.761 179.863 1.00 91.54  ? 2387 LEU A C     1 
ATOM   5991  O O     . LEU A 1 2387 ? 137.138 205.898 179.305 1.00 91.54  ? 2387 LEU A O     1 
ATOM   5992  C CB    . LEU A 1 2387 ? 137.796 205.391 181.993 1.00 91.54  ? 2387 LEU A CB    1 
ATOM   5993  C CG    . LEU A 1 2387 ? 138.521 204.100 182.380 1.00 91.54  ? 2387 LEU A CG    1 
ATOM   5994  C CD1   . LEU A 1 2387 ? 139.377 203.634 181.217 1.00 91.54  ? 2387 LEU A CD1   1 
ATOM   5995  C CD2   . LEU A 1 2387 ? 139.379 204.324 183.610 1.00 91.54  ? 2387 LEU A CD2   1 
ATOM   5996  N N     . ASP A 1 2388 ? 137.997 208.015 179.431 1.00 99.99  ? 2388 ASP A N     1 
ATOM   5997  C CA    . ASP A 1 2388 ? 137.292 208.506 178.216 1.00 99.99  ? 2388 ASP A CA    1 
ATOM   5998  C C     . ASP A 1 2388 ? 138.165 209.556 177.524 1.00 99.99  ? 2388 ASP A C     1 
ATOM   5999  O O     . ASP A 1 2388 ? 138.851 210.298 178.261 1.00 99.99  ? 2388 ASP A O     1 
ATOM   6000  C CB    . ASP A 1 2388 ? 135.917 209.047 178.569 1.00 30.00  ? 2388 ASP A CB    1 
ATOM   6001  C CG    . ASP A 1 2388 ? 135.656 209.202 180.059 1.00 30.00  ? 2388 ASP A CG    1 
ATOM   6002  O OD1   . ASP A 1 2388 ? 134.691 208.581 180.551 1.00 30.00  ? 2388 ASP A OD1   1 
ATOM   6003  O OD2   . ASP A 1 2388 ? 136.433 209.926 180.715 1.00 30.00  ? 2388 ASP A OD2   1 
ATOM   6004  N N     . SER A 1 2410 ? 135.698 215.332 183.786 1.00 100.90 ? 2410 SER A N     1 
ATOM   6005  C CA    . SER A 1 2410 ? 135.742 215.552 185.229 1.00 100.90 ? 2410 SER A CA    1 
ATOM   6006  C C     . SER A 1 2410 ? 134.719 214.712 186.011 1.00 100.90 ? 2410 SER A C     1 
ATOM   6007  O O     . SER A 1 2410 ? 135.066 214.157 187.053 1.00 100.90 ? 2410 SER A O     1 
ATOM   6008  C CB    . SER A 1 2410 ? 135.550 217.038 185.549 1.00 100.90 ? 2410 SER A CB    1 
ATOM   6009  O OG    . SER A 1 2410 ? 135.184 217.218 186.905 1.00 100.90 ? 2410 SER A OG    1 
ATOM   6010  N N     . PRO A 1 2411 ? 133.462 214.626 185.548 1.00 98.22  ? 2411 PRO A N     1 
ATOM   6011  C CA    . PRO A 1 2411 ? 132.538 213.694 186.216 1.00 98.22  ? 2411 PRO A CA    1 
ATOM   6012  C C     . PRO A 1 2411 ? 133.031 212.261 186.188 1.00 98.22  ? 2411 PRO A C     1 
ATOM   6013  O O     . PRO A 1 2411 ? 132.950 211.558 187.205 1.00 98.22  ? 2411 PRO A O     1 
ATOM   6014  C CB    . PRO A 1 2411 ? 131.233 213.867 185.425 1.00 98.22  ? 2411 PRO A CB    1 
ATOM   6015  C CG    . PRO A 1 2411 ? 131.649 214.446 184.122 1.00 98.22  ? 2411 PRO A CG    1 
ATOM   6016  C CD    . PRO A 1 2411 ? 132.781 215.352 184.462 1.00 98.22  ? 2411 PRO A CD    1 
ATOM   6017  N N     . MET A 1 2412 ? 133.571 211.817 185.051 1.00 93.65  ? 2412 MET A N     1 
ATOM   6018  C CA    . MET A 1 2412 ? 134.171 210.490 184.997 1.00 93.65  ? 2412 MET A CA    1 
ATOM   6019  C C     . MET A 1 2412 ? 135.353 210.399 185.948 1.00 93.65  ? 2412 MET A C     1 
ATOM   6020  O O     . MET A 1 2412 ? 135.590 209.352 186.556 1.00 93.65  ? 2412 MET A O     1 
ATOM   6021  C CB    . MET A 1 2412 ? 134.597 210.157 183.569 1.00 93.65  ? 2412 MET A CB    1 
ATOM   6022  N N     . LEU A 1 2413 ? 136.100 211.495 186.097 1.00 98.68  ? 2413 LEU A N     1 
ATOM   6023  C CA    . LEU A 1 2413 ? 137.176 211.524 187.081 1.00 98.68  ? 2413 LEU A CA    1 
ATOM   6024  C C     . LEU A 1 2413 ? 136.639 211.349 188.492 1.00 98.68  ? 2413 LEU A C     1 
ATOM   6025  O O     . LEU A 1 2413 ? 137.223 210.616 189.296 1.00 98.68  ? 2413 LEU A O     1 
ATOM   6026  C CB    . LEU A 1 2413 ? 137.961 212.829 186.973 1.00 98.68  ? 2413 LEU A CB    1 
ATOM   6027  C CG    . LEU A 1 2413 ? 139.282 212.765 186.214 1.00 98.68  ? 2413 LEU A CG    1 
ATOM   6028  C CD1   . LEU A 1 2413 ? 140.355 212.147 187.090 1.00 98.68  ? 2413 LEU A CD1   1 
ATOM   6029  C CD2   . LEU A 1 2413 ? 139.106 211.958 184.957 1.00 98.68  ? 2413 LEU A CD2   1 
ATOM   6030  N N     . GLN A 1 2414 ? 135.537 212.024 188.819 1.00 97.82  ? 2414 GLN A N     1 
ATOM   6031  C CA    . GLN A 1 2414 ? 134.967 211.878 190.152 1.00 97.82  ? 2414 GLN A CA    1 
ATOM   6032  C C     . GLN A 1 2414 ? 134.517 210.446 190.397 1.00 97.82  ? 2414 GLN A C     1 
ATOM   6033  O O     . GLN A 1 2414 ? 134.760 209.884 191.473 1.00 97.82  ? 2414 GLN A O     1 
ATOM   6034  C CB    . GLN A 1 2414 ? 133.801 212.846 190.335 1.00 97.82  ? 2414 GLN A CB    1 
ATOM   6035  C CG    . GLN A 1 2414 ? 133.448 213.122 191.785 1.00 97.82  ? 2414 GLN A CG    1 
ATOM   6036  C CD    . GLN A 1 2414 ? 134.671 213.285 192.664 1.00 97.82  ? 2414 GLN A CD    1 
ATOM   6037  O OE1   . GLN A 1 2414 ? 134.963 212.436 193.506 1.00 97.82  ? 2414 GLN A OE1   1 
ATOM   6038  N NE2   . GLN A 1 2414 ? 135.392 214.382 192.474 1.00 97.82  ? 2414 GLN A NE2   1 
ATOM   6039  N N     . ILE A 1 2415 ? 133.867 209.837 189.404 1.00 96.91  ? 2415 ILE A N     1 
ATOM   6040  C CA    . ILE A 1 2415 ? 133.425 208.454 189.554 1.00 96.91  ? 2415 ILE A CA    1 
ATOM   6041  C C     . ILE A 1 2415 ? 134.619 207.527 189.730 1.00 96.91  ? 2415 ILE A C     1 
ATOM   6042  O O     . ILE A 1 2415 ? 134.614 206.641 190.594 1.00 96.91  ? 2415 ILE A O     1 
ATOM   6043  C CB    . ILE A 1 2415 ? 132.556 208.036 188.356 1.00 96.91  ? 2415 ILE A CB    1 
ATOM   6044  C CG1   . ILE A 1 2415 ? 131.409 209.026 188.163 1.00 96.91  ? 2415 ILE A CG1   1 
ATOM   6045  C CG2   . ILE A 1 2415 ? 132.023 206.634 188.557 1.00 96.91  ? 2415 ILE A CG2   1 
ATOM   6046  C CD1   . ILE A 1 2415 ? 130.529 209.183 189.380 1.00 96.91  ? 2415 ILE A CD1   1 
ATOM   6047  N N     . GLN A 1 2416 ? 135.661 207.716 188.918 1.00 91.53  ? 2416 GLN A N     1 
ATOM   6048  C CA    . GLN A 1 2416 ? 136.841 206.871 189.030 1.00 91.53  ? 2416 GLN A CA    1 
ATOM   6049  C C     . GLN A 1 2416 ? 137.498 207.028 190.392 1.00 91.53  ? 2416 GLN A C     1 
ATOM   6050  O O     . GLN A 1 2416 ? 137.924 206.041 191.000 1.00 91.53  ? 2416 GLN A O     1 
ATOM   6051  C CB    . GLN A 1 2416 ? 137.835 207.201 187.918 1.00 91.53  ? 2416 GLN A CB    1 
ATOM   6052  C CG    . GLN A 1 2416 ? 137.441 206.676 186.553 1.00 91.53  ? 2416 GLN A CG    1 
ATOM   6053  C CD    . GLN A 1 2416 ? 138.326 207.213 185.450 1.00 91.53  ? 2416 GLN A CD    1 
ATOM   6054  O OE1   . GLN A 1 2416 ? 137.853 207.571 184.374 1.00 91.53  ? 2416 GLN A OE1   1 
ATOM   6055  N NE2   . GLN A 1 2416 ? 139.625 207.258 185.709 1.00 91.53  ? 2416 GLN A NE2   1 
ATOM   6056  N N     . ARG A 1 2417 ? 137.593 208.262 190.886 1.00 94.69  ? 2417 ARG A N     1 
ATOM   6057  C CA    . ARG A 1 2417 ? 138.219 208.491 192.181 1.00 94.69  ? 2417 ARG A CA    1 
ATOM   6058  C C     . ARG A 1 2417 ? 137.418 207.851 193.305 1.00 94.69  ? 2417 ARG A C     1 
ATOM   6059  O O     . ARG A 1 2417 ? 137.995 207.243 194.214 1.00 94.69  ? 2417 ARG A O     1 
ATOM   6060  C CB    . ARG A 1 2417 ? 138.389 209.988 192.424 1.00 94.69  ? 2417 ARG A CB    1 
ATOM   6061  C CG    . ARG A 1 2417 ? 139.657 210.564 191.825 1.00 94.69  ? 2417 ARG A CG    1 
ATOM   6062  C CD    . ARG A 1 2417 ? 139.447 211.993 191.371 1.00 94.69  ? 2417 ARG A CD    1 
ATOM   6063  N NE    . ARG A 1 2417 ? 140.484 212.430 190.446 1.00 94.69  ? 2417 ARG A NE    1 
ATOM   6064  C CZ    . ARG A 1 2417 ? 141.110 213.595 190.521 1.00 94.69  ? 2417 ARG A CZ    1 
ATOM   6065  N NH1   . ARG A 1 2417 ? 140.831 214.468 191.475 1.00 94.69  ? 2417 ARG A NH1   1 
ATOM   6066  N NH2   . ARG A 1 2417 ? 142.038 213.893 189.618 1.00 94.69  ? 2417 ARG A NH2   1 
ATOM   6067  N N     . ASP A 1 2418 ? 136.089 207.975 193.267 1.00 97.02  ? 2418 ASP A N     1 
ATOM   6068  C CA    . ASP A 1 2418 ? 135.272 207.327 194.287 1.00 97.02  ? 2418 ASP A CA    1 
ATOM   6069  C C     . ASP A 1 2418 ? 135.436 205.816 194.237 1.00 97.02  ? 2418 ASP A C     1 
ATOM   6070  O O     . ASP A 1 2418 ? 135.593 205.161 195.277 1.00 97.02  ? 2418 ASP A O     1 
ATOM   6071  C CB    . ASP A 1 2418 ? 133.804 207.711 194.117 1.00 97.02  ? 2418 ASP A CB    1 
ATOM   6072  C CG    . ASP A 1 2418 ? 133.564 209.194 194.299 1.00 97.02  ? 2418 ASP A CG    1 
ATOM   6073  O OD1   . ASP A 1 2418 ? 134.479 209.888 194.789 1.00 97.02  ? 2418 ASP A OD1   1 
ATOM   6074  O OD2   . ASP A 1 2418 ? 132.459 209.665 193.960 1.00 97.02  ? 2418 ASP A OD2   1 
ATOM   6075  N N     . ALA A 1 2419 ? 135.420 205.244 193.032 1.00 91.57  ? 2419 ALA A N     1 
ATOM   6076  C CA    . ALA A 1 2419 ? 135.594 203.804 192.906 1.00 91.57  ? 2419 ALA A CA    1 
ATOM   6077  C C     . ALA A 1 2419 ? 136.939 203.367 193.460 1.00 91.57  ? 2419 ALA A C     1 
ATOM   6078  O O     . ALA A 1 2419 ? 137.016 202.392 194.213 1.00 91.57  ? 2419 ALA A O     1 
ATOM   6079  C CB    . ALA A 1 2419 ? 135.453 203.383 191.445 1.00 91.57  ? 2419 ALA A CB    1 
ATOM   6080  N N     . ALA A 1 2420 ? 138.006 204.091 193.112 1.00 91.77  ? 2420 ALA A N     1 
ATOM   6081  C CA    . ALA A 1 2420 ? 139.340 203.735 193.582 1.00 91.77  ? 2420 ALA A CA    1 
ATOM   6082  C C     . ALA A 1 2420 ? 139.437 203.839 195.096 1.00 91.77  ? 2420 ALA A C     1 
ATOM   6083  O O     . ALA A 1 2420 ? 140.040 202.979 195.749 1.00 91.77  ? 2420 ALA A O     1 
ATOM   6084  C CB    . ALA A 1 2420 ? 140.387 204.628 192.919 1.00 91.77  ? 2420 ALA A CB    1 
ATOM   6085  N N     . THR A 1 2421 ? 138.862 204.895 195.671 1.00 90.39  ? 2421 THR A N     1 
ATOM   6086  C CA    . THR A 1 2421 ? 138.839 205.015 197.122 1.00 90.39  ? 2421 THR A CA    1 
ATOM   6087  C C     . THR A 1 2421 ? 138.126 203.827 197.746 1.00 90.39  ? 2421 THR A C     1 
ATOM   6088  O O     . THR A 1 2421 ? 138.542 203.321 198.794 1.00 90.39  ? 2421 THR A O     1 
ATOM   6089  C CB    . THR A 1 2421 ? 138.157 206.320 197.527 1.00 90.39  ? 2421 THR A CB    1 
ATOM   6090  O OG1   . THR A 1 2421 ? 138.874 207.427 196.969 1.00 90.39  ? 2421 THR A OG1   1 
ATOM   6091  C CG2   . THR A 1 2421 ? 138.130 206.457 199.037 1.00 90.39  ? 2421 THR A CG2   1 
ATOM   6092  N N     . ILE A 1 2422 ? 137.057 203.357 197.103 1.00 91.22  ? 2422 ILE A N     1 
ATOM   6093  C CA    . ILE A 1 2422 ? 136.331 202.206 197.628 1.00 91.22  ? 2422 ILE A CA    1 
ATOM   6094  C C     . ILE A 1 2422 ? 137.199 200.954 197.573 1.00 91.22  ? 2422 ILE A C     1 
ATOM   6095  O O     . ILE A 1 2422 ? 137.279 200.192 198.543 1.00 91.22  ? 2422 ILE A O     1 
ATOM   6096  C CB    . ILE A 1 2422 ? 135.012 202.008 196.863 1.00 91.22  ? 2422 ILE A CB    1 
ATOM   6097  C CG1   . ILE A 1 2422 ? 133.985 203.041 197.314 1.00 91.22  ? 2422 ILE A CG1   1 
ATOM   6098  C CG2   . ILE A 1 2422 ? 134.470 200.615 197.101 1.00 91.22  ? 2422 ILE A CG2   1 
ATOM   6099  C CD1   . ILE A 1 2422 ? 133.465 202.803 198.706 1.00 91.22  ? 2422 ILE A CD1   1 
ATOM   6100  N N     . MET A 1 2423 ? 137.869 200.725 196.442 1.00 90.75  ? 2423 MET A N     1 
ATOM   6101  C CA    . MET A 1 2423 ? 138.544 199.445 196.249 1.00 90.75  ? 2423 MET A CA    1 
ATOM   6102  C C     . MET A 1 2423 ? 139.955 199.426 196.814 1.00 90.75  ? 2423 MET A C     1 
ATOM   6103  O O     . MET A 1 2423 ? 140.595 198.370 196.789 1.00 90.75  ? 2423 MET A O     1 
ATOM   6104  C CB    . MET A 1 2423 ? 138.616 199.073 194.767 1.00 90.75  ? 2423 MET A CB    1 
ATOM   6105  C CG    . MET A 1 2423 ? 138.894 200.229 193.854 1.00 90.75  ? 2423 MET A CG    1 
ATOM   6106  S SD    . MET A 1 2423 ? 138.837 199.783 192.119 1.00 90.75  ? 2423 MET A SD    1 
ATOM   6107  C CE    . MET A 1 2423 ? 137.295 198.879 192.103 1.00 90.75  ? 2423 MET A CE    1 
ATOM   6108  N N     . GLN A 1 2424 ? 140.455 200.559 197.303 1.00 86.74  ? 2424 GLN A N     1 
ATOM   6109  C CA    . GLN A 1 2424 ? 141.812 200.616 197.843 1.00 86.74  ? 2424 GLN A CA    1 
ATOM   6110  C C     . GLN A 1 2424 ? 142.109 199.554 198.895 1.00 86.74  ? 2424 GLN A C     1 
ATOM   6111  O O     . GLN A 1 2424 ? 143.201 198.966 198.845 1.00 86.74  ? 2424 GLN A O     1 
ATOM   6112  C CB    . GLN A 1 2424 ? 142.069 202.025 198.395 1.00 86.74  ? 2424 GLN A CB    1 
ATOM   6113  C CG    . GLN A 1 2424 ? 143.311 202.132 199.253 1.00 86.74  ? 2424 GLN A CG    1 
ATOM   6114  C CD    . GLN A 1 2424 ? 144.556 202.396 198.434 1.00 86.74  ? 2424 GLN A CD    1 
ATOM   6115  O OE1   . GLN A 1 2424 ? 144.579 203.291 197.589 1.00 86.74  ? 2424 GLN A OE1   1 
ATOM   6116  N NE2   . GLN A 1 2424 ? 145.599 201.613 198.674 1.00 86.74  ? 2424 GLN A NE2   1 
ATOM   6117  N N     . PRO A 1 2425 ? 141.230 199.264 199.862 1.00 86.73  ? 2425 PRO A N     1 
ATOM   6118  C CA    . PRO A 1 2425 ? 141.579 198.243 200.864 1.00 86.73  ? 2425 PRO A CA    1 
ATOM   6119  C C     . PRO A 1 2425 ? 141.880 196.876 200.280 1.00 86.73  ? 2425 PRO A C     1 
ATOM   6120  O O     . PRO A 1 2425 ? 142.743 196.167 200.812 1.00 86.73  ? 2425 PRO A O     1 
ATOM   6121  C CB    . PRO A 1 2425 ? 140.338 198.201 201.764 1.00 86.73  ? 2425 PRO A CB    1 
ATOM   6122  C CG    . PRO A 1 2425 ? 139.733 199.532 201.620 1.00 86.73  ? 2425 PRO A CG    1 
ATOM   6123  C CD    . PRO A 1 2425 ? 139.953 199.919 200.195 1.00 86.73  ? 2425 PRO A CD    1 
ATOM   6124  N N     . TYR A 1 2426 ? 141.201 196.479 199.204 1.00 87.84  ? 2426 TYR A N     1 
ATOM   6125  C CA    . TYR A 1 2426 ? 141.390 195.130 198.682 1.00 87.84  ? 2426 TYR A CA    1 
ATOM   6126  C C     . TYR A 1 2426 ? 142.731 194.966 197.983 1.00 87.84  ? 2426 TYR A C     1 
ATOM   6127  O O     . TYR A 1 2426 ? 143.240 193.845 197.882 1.00 87.84  ? 2426 TYR A O     1 
ATOM   6128  C CB    . TYR A 1 2426 ? 140.248 194.769 197.739 1.00 87.84  ? 2426 TYR A CB    1 
ATOM   6129  C CG    . TYR A 1 2426 ? 138.919 194.682 198.442 1.00 87.84  ? 2426 TYR A CG    1 
ATOM   6130  C CD1   . TYR A 1 2426 ? 138.597 193.570 199.205 1.00 87.84  ? 2426 TYR A CD1   1 
ATOM   6131  C CD2   . TYR A 1 2426 ? 137.995 195.712 198.360 1.00 87.84  ? 2426 TYR A CD2   1 
ATOM   6132  C CE1   . TYR A 1 2426 ? 137.390 193.479 199.858 1.00 87.84  ? 2426 TYR A CE1   1 
ATOM   6133  C CE2   . TYR A 1 2426 ? 136.781 195.631 199.011 1.00 87.84  ? 2426 TYR A CE2   1 
ATOM   6134  C CZ    . TYR A 1 2426 ? 136.486 194.511 199.759 1.00 87.84  ? 2426 TYR A CZ    1 
ATOM   6135  O OH    . TYR A 1 2426 ? 135.283 194.416 200.414 1.00 87.84  ? 2426 TYR A OH    1 
ATOM   6136  N N     . PHE A 1 2427 ? 143.316 196.055 197.495 1.00 83.84  ? 2427 PHE A N     1 
ATOM   6137  C CA    . PHE A 1 2427 ? 144.601 195.987 196.802 1.00 83.84  ? 2427 PHE A CA    1 
ATOM   6138  C C     . PHE A 1 2427 ? 145.750 196.260 197.775 1.00 83.84  ? 2427 PHE A C     1 
ATOM   6139  O O     . PHE A 1 2427 ? 146.596 197.127 197.568 1.00 83.84  ? 2427 PHE A O     1 
ATOM   6140  C CB    . PHE A 1 2427 ? 144.618 196.961 195.630 1.00 83.84  ? 2427 PHE A CB    1 
ATOM   6141  C CG    . PHE A 1 2427 ? 143.800 196.508 194.458 1.00 83.84  ? 2427 PHE A CG    1 
ATOM   6142  C CD1   . PHE A 1 2427 ? 142.421 196.561 194.500 1.00 83.84  ? 2427 PHE A CD1   1 
ATOM   6143  C CD2   . PHE A 1 2427 ? 144.409 196.022 193.319 1.00 83.84  ? 2427 PHE A CD2   1 
ATOM   6144  C CE1   . PHE A 1 2427 ? 141.668 196.145 193.427 1.00 83.84  ? 2427 PHE A CE1   1 
ATOM   6145  C CE2   . PHE A 1 2427 ? 143.658 195.603 192.243 1.00 83.84  ? 2427 PHE A CE2   1 
ATOM   6146  C CZ    . PHE A 1 2427 ? 142.287 195.665 192.298 1.00 83.84  ? 2427 PHE A CZ    1 
ATOM   6147  N N     . THR A 1 2428 ? 145.765 195.489 198.858 1.00 93.61  ? 2428 THR A N     1 
ATOM   6148  C CA    . THR A 1 2428 ? 146.788 195.609 199.882 1.00 93.61  ? 2428 THR A CA    1 
ATOM   6149  C C     . THR A 1 2428 ? 147.783 194.459 199.767 1.00 93.61  ? 2428 THR A C     1 
ATOM   6150  O O     . THR A 1 2428 ? 147.691 193.606 198.882 1.00 93.61  ? 2428 THR A O     1 
ATOM   6151  C CB    . THR A 1 2428 ? 146.157 195.650 201.274 1.00 93.61  ? 2428 THR A CB    1 
ATOM   6152  O OG1   . THR A 1 2428 ? 145.012 194.790 201.307 1.00 93.61  ? 2428 THR A OG1   1 
ATOM   6153  C CG2   . THR A 1 2428 ? 145.737 197.067 201.628 1.00 93.61  ? 2428 THR A CG2   1 
ATOM   6154  N N     . SER A 1 2429 ? 148.755 194.444 200.681 1.00 98.75  ? 2429 SER A N     1 
ATOM   6155  C CA    . SER A 1 2429 ? 149.792 193.418 200.644 1.00 98.75  ? 2429 SER A CA    1 
ATOM   6156  C C     . SER A 1 2429 ? 149.207 192.029 200.860 1.00 98.75  ? 2429 SER A C     1 
ATOM   6157  O O     . SER A 1 2429 ? 149.577 191.076 200.164 1.00 98.75  ? 2429 SER A O     1 
ATOM   6158  C CB    . SER A 1 2429 ? 150.861 193.716 201.694 1.00 98.75  ? 2429 SER A CB    1 
ATOM   6159  O OG    . SER A 1 2429 ? 150.307 193.708 202.997 1.00 98.75  ? 2429 SER A OG    1 
ATOM   6160  N N     . ASN A 1 2430 ? 148.294 191.892 201.817 1.00 102.95 ? 2430 ASN A N     1 
ATOM   6161  C CA    . ASN A 1 2430 ? 147.664 190.614 202.119 1.00 102.95 ? 2430 ASN A CA    1 
ATOM   6162  C C     . ASN A 1 2430 ? 146.150 190.698 201.968 1.00 102.95 ? 2430 ASN A C     1 
ATOM   6163  O O     . ASN A 1 2430 ? 145.408 190.021 202.681 1.00 102.95 ? 2430 ASN A O     1 
ATOM   6164  C CB    . ASN A 1 2430 ? 148.040 190.143 203.523 1.00 102.95 ? 2430 ASN A CB    1 
ATOM   6165  C CG    . ASN A 1 2430 ? 147.579 191.103 204.603 1.00 102.95 ? 2430 ASN A CG    1 
ATOM   6166  O OD1   . ASN A 1 2430 ? 146.481 190.969 205.141 1.00 102.95 ? 2430 ASN A OD1   1 
ATOM   6167  N ND2   . ASN A 1 2430 ? 148.419 192.080 204.924 1.00 102.95 ? 2430 ASN A ND2   1 
ATOM   6168  N N     . GLY A 1 2431 ? 145.680 191.519 201.038 1.00 93.16  ? 2431 GLY A N     1 
ATOM   6169  C CA    . GLY A 1 2431 ? 144.263 191.724 200.852 1.00 93.16  ? 2431 GLY A CA    1 
ATOM   6170  C C     . GLY A 1 2431 ? 143.607 190.584 200.099 1.00 93.16  ? 2431 GLY A C     1 
ATOM   6171  O O     . GLY A 1 2431 ? 144.150 189.488 199.951 1.00 93.16  ? 2431 GLY A O     1 
ATOM   6172  N N     . LEU A 1 2432 ? 142.392 190.862 199.625 1.00 87.35  ? 2432 LEU A N     1 
ATOM   6173  C CA    . LEU A 1 2432 ? 141.643 189.866 198.868 1.00 87.35  ? 2432 LEU A CA    1 
ATOM   6174  C C     . LEU A 1 2432 ? 142.352 189.507 197.568 1.00 87.35  ? 2432 LEU A C     1 
ATOM   6175  O O     . LEU A 1 2432 ? 142.474 188.326 197.226 1.00 87.35  ? 2432 LEU A O     1 
ATOM   6176  C CB    . LEU A 1 2432 ? 140.237 190.391 198.582 1.00 87.35  ? 2432 LEU A CB    1 
ATOM   6177  C CG    . LEU A 1 2432 ? 139.068 189.420 198.417 1.00 87.35  ? 2432 LEU A CG    1 
ATOM   6178  C CD1   . LEU A 1 2432 ? 137.785 190.211 198.272 1.00 87.35  ? 2432 LEU A CD1   1 
ATOM   6179  C CD2   . LEU A 1 2432 ? 139.248 188.497 197.225 1.00 87.35  ? 2432 LEU A CD2   1 
ATOM   6180  N N     . VAL A 1 2433 ? 142.827 190.512 196.830 1.00 85.07  ? 2433 VAL A N     1 
ATOM   6181  C CA    . VAL A 1 2433 ? 143.335 190.265 195.486 1.00 85.07  ? 2433 VAL A CA    1 
ATOM   6182  C C     . VAL A 1 2433 ? 144.631 189.469 195.532 1.00 85.07  ? 2433 VAL A C     1 
ATOM   6183  O O     . VAL A 1 2433 ? 144.831 188.547 194.735 1.00 85.07  ? 2433 VAL A O     1 
ATOM   6184  C CB    . VAL A 1 2433 ? 143.514 191.590 194.729 1.00 85.07  ? 2433 VAL A CB    1 
ATOM   6185  C CG1   . VAL A 1 2433 ? 143.803 191.319 193.268 1.00 85.07  ? 2433 VAL A CG1   1 
ATOM   6186  C CG2   . VAL A 1 2433 ? 142.275 192.448 194.877 1.00 85.07  ? 2433 VAL A CG2   1 
ATOM   6187  N N     . THR A 1 2434 ? 145.537 189.814 196.446 1.00 88.91  ? 2434 THR A N     1 
ATOM   6188  C CA    . THR A 1 2434 ? 146.807 189.099 196.522 1.00 88.91  ? 2434 THR A CA    1 
ATOM   6189  C C     . THR A 1 2434 ? 146.595 187.642 196.914 1.00 88.91  ? 2434 THR A C     1 
ATOM   6190  O O     . THR A 1 2434 ? 147.190 186.734 196.320 1.00 88.91  ? 2434 THR A O     1 
ATOM   6191  C CB    . THR A 1 2434 ? 147.742 189.790 197.510 1.00 88.91  ? 2434 THR A CB    1 
ATOM   6192  O OG1   . THR A 1 2434 ? 147.796 191.191 197.215 1.00 88.91  ? 2434 THR A OG1   1 
ATOM   6193  C CG2   . THR A 1 2434 ? 149.140 189.205 197.413 1.00 88.91  ? 2434 THR A CG2   1 
ATOM   6194  N N     . LYS A 1 2435 ? 145.746 187.397 197.912 1.00 92.24  ? 2435 LYS A N     1 
ATOM   6195  C CA    . LYS A 1 2435 ? 145.470 186.024 198.316 1.00 92.24  ? 2435 LYS A CA    1 
ATOM   6196  C C     . LYS A 1 2435 ? 144.782 185.254 197.199 1.00 92.24  ? 2435 LYS A C     1 
ATOM   6197  O O     . LYS A 1 2435 ? 145.070 184.072 196.978 1.00 92.24  ? 2435 LYS A O     1 
ATOM   6198  C CB    . LYS A 1 2435 ? 144.622 186.009 199.586 1.00 92.24  ? 2435 LYS A CB    1 
ATOM   6199  C CG    . LYS A 1 2435 ? 145.391 186.359 200.848 1.00 92.24  ? 2435 LYS A CG    1 
ATOM   6200  C CD    . LYS A 1 2435 ? 144.449 186.717 201.986 1.00 92.24  ? 2435 LYS A CD    1 
ATOM   6201  C CE    . LYS A 1 2435 ? 145.202 186.879 203.295 1.00 92.24  ? 2435 LYS A CE    1 
ATOM   6202  N NZ    . LYS A 1 2435 ? 144.545 187.867 204.195 1.00 92.24  ? 2435 LYS A NZ    1 
ATOM   6203  N N     . ALA A 1 2436 ? 143.863 185.908 196.485 1.00 84.84  ? 2436 ALA A N     1 
ATOM   6204  C CA    . ALA A 1 2436 ? 143.200 185.251 195.367 1.00 84.84  ? 2436 ALA A CA    1 
ATOM   6205  C C     . ALA A 1 2436 ? 144.197 184.884 194.279 1.00 84.84  ? 2436 ALA A C     1 
ATOM   6206  O O     . ALA A 1 2436 ? 144.129 183.790 193.711 1.00 84.84  ? 2436 ALA A O     1 
ATOM   6207  C CB    . ALA A 1 2436 ? 142.098 186.148 194.810 1.00 84.84  ? 2436 ALA A CB    1 
ATOM   6208  N N     . LEU A 1 2437 ? 145.127 185.790 193.970 1.00 85.01  ? 2437 LEU A N     1 
ATOM   6209  C CA    . LEU A 1 2437 ? 146.174 185.472 193.007 1.00 85.01  ? 2437 LEU A CA    1 
ATOM   6210  C C     . LEU A 1 2437 ? 146.994 184.282 193.472 1.00 85.01  ? 2437 LEU A C     1 
ATOM   6211  O O     . LEU A 1 2437 ? 147.293 183.374 192.687 1.00 85.01  ? 2437 LEU A O     1 
ATOM   6212  C CB    . LEU A 1 2437 ? 147.088 186.678 192.793 1.00 85.01  ? 2437 LEU A CB    1 
ATOM   6213  C CG    . LEU A 1 2437 ? 146.835 187.621 191.619 1.00 85.01  ? 2437 LEU A CG    1 
ATOM   6214  C CD1   . LEU A 1 2437 ? 147.270 186.958 190.325 1.00 85.01  ? 2437 LEU A CD1   1 
ATOM   6215  C CD2   . LEU A 1 2437 ? 145.389 188.060 191.547 1.00 85.01  ? 2437 LEU A CD2   1 
ATOM   6216  N N     . GLU A 1 2438 ? 147.367 184.272 194.752 1.00 92.47  ? 2438 GLU A N     1 
ATOM   6217  C CA    . GLU A 1 2438 ? 148.184 183.183 195.266 1.00 92.47  ? 2438 GLU A CA    1 
ATOM   6218  C C     . GLU A 1 2438 ? 147.456 181.854 195.139 1.00 92.47  ? 2438 GLU A C     1 
ATOM   6219  O O     . GLU A 1 2438 ? 148.053 180.843 194.752 1.00 92.47  ? 2438 GLU A O     1 
ATOM   6220  C CB    . GLU A 1 2438 ? 148.560 183.454 196.721 1.00 92.47  ? 2438 GLU A CB    1 
ATOM   6221  C CG    . GLU A 1 2438 ? 149.512 182.434 197.310 1.00 92.47  ? 2438 GLU A CG    1 
ATOM   6222  C CD    . GLU A 1 2438 ? 150.802 182.329 196.521 1.00 92.47  ? 2438 GLU A CD    1 
ATOM   6223  O OE1   . GLU A 1 2438 ? 150.865 181.517 195.573 1.00 92.47  ? 2438 GLU A OE1   1 
ATOM   6224  O OE2   . GLU A 1 2438 ? 151.754 183.067 196.848 1.00 92.47  ? 2438 GLU A OE2   1 
ATOM   6225  N N     . HIS A 1 2439 ? 146.161 181.838 195.455 1.00 89.35  ? 2439 HIS A N     1 
ATOM   6226  C CA    . HIS A 1 2439 ? 145.393 180.603 195.350 1.00 89.35  ? 2439 HIS A CA    1 
ATOM   6227  C C     . HIS A 1 2439 ? 145.222 180.171 193.899 1.00 89.35  ? 2439 HIS A C     1 
ATOM   6228  O O     . HIS A 1 2439 ? 145.361 178.985 193.580 1.00 89.35  ? 2439 HIS A O     1 
ATOM   6229  C CB    . HIS A 1 2439 ? 144.032 180.772 196.018 1.00 89.35  ? 2439 HIS A CB    1 
ATOM   6230  C CG    . HIS A 1 2439 ? 143.269 179.494 196.157 1.00 89.35  ? 2439 HIS A CG    1 
ATOM   6231  N ND1   . HIS A 1 2439 ? 142.106 179.243 195.463 1.00 89.35  ? 2439 HIS A ND1   1 
ATOM   6232  C CD2   . HIS A 1 2439 ? 143.507 178.390 196.903 1.00 89.35  ? 2439 HIS A CD2   1 
ATOM   6233  C CE1   . HIS A 1 2439 ? 141.657 178.042 195.780 1.00 89.35  ? 2439 HIS A CE1   1 
ATOM   6234  N NE2   . HIS A 1 2439 ? 142.489 177.504 196.653 1.00 89.35  ? 2439 HIS A NE2   1 
ATOM   6235  N N     . ALA A 1 2440 ? 144.921 181.115 193.007 1.00 85.43  ? 2440 ALA A N     1 
ATOM   6236  C CA    . ALA A 1 2440 ? 144.690 180.758 191.613 1.00 85.43  ? 2440 ALA A CA    1 
ATOM   6237  C C     . ALA A 1 2440 ? 145.965 180.282 190.939 1.00 85.43  ? 2440 ALA A C     1 
ATOM   6238  O O     . ALA A 1 2440 ? 145.902 179.504 189.981 1.00 85.43  ? 2440 ALA A O     1 
ATOM   6239  C CB    . ALA A 1 2440 ? 144.106 181.944 190.852 1.00 85.43  ? 2440 ALA A CB    1 
ATOM   6240  N N     . PHE A 1 2441 ? 147.123 180.739 191.412 1.00 87.78  ? 2441 PHE A N     1 
ATOM   6241  C CA    . PHE A 1 2441 ? 148.372 180.229 190.863 1.00 87.78  ? 2441 PHE A CA    1 
ATOM   6242  C C     . PHE A 1 2441 ? 148.513 178.736 191.112 1.00 87.78  ? 2441 PHE A C     1 
ATOM   6243  O O     . PHE A 1 2441 ? 149.003 178.005 190.245 1.00 87.78  ? 2441 PHE A O     1 
ATOM   6244  C CB    . PHE A 1 2441 ? 149.553 180.991 191.456 1.00 87.78  ? 2441 PHE A CB    1 
ATOM   6245  C CG    . PHE A 1 2441 ? 150.068 182.081 190.568 1.00 87.78  ? 2441 PHE A CG    1 
ATOM   6246  C CD1   . PHE A 1 2441 ? 150.640 181.780 189.347 1.00 87.78  ? 2441 PHE A CD1   1 
ATOM   6247  C CD2   . PHE A 1 2441 ? 149.968 183.406 190.948 1.00 87.78  ? 2441 PHE A CD2   1 
ATOM   6248  C CE1   . PHE A 1 2441 ? 151.113 182.779 188.526 1.00 87.78  ? 2441 PHE A CE1   1 
ATOM   6249  C CE2   . PHE A 1 2441 ? 150.438 184.410 190.132 1.00 87.78  ? 2441 PHE A CE2   1 
ATOM   6250  C CZ    . PHE A 1 2441 ? 151.011 184.097 188.919 1.00 87.78  ? 2441 PHE A CZ    1 
ATOM   6251  N N     . GLN A 1 2442 ? 148.085 178.265 192.284 1.00 88.69  ? 2442 GLN A N     1 
ATOM   6252  C CA    . GLN A 1 2442 ? 148.062 176.831 192.540 1.00 88.69  ? 2442 GLN A CA    1 
ATOM   6253  C C     . GLN A 1 2442 ? 147.053 176.124 191.644 1.00 88.69  ? 2442 GLN A C     1 
ATOM   6254  O O     . GLN A 1 2442 ? 147.261 174.965 191.267 1.00 88.69  ? 2442 GLN A O     1 
ATOM   6255  C CB    . GLN A 1 2442 ? 147.760 176.580 194.020 1.00 88.69  ? 2442 GLN A CB    1 
ATOM   6256  C CG    . GLN A 1 2442 ? 147.178 175.216 194.348 1.00 88.69  ? 2442 GLN A CG    1 
ATOM   6257  C CD    . GLN A 1 2442 ? 145.666 175.201 194.282 1.00 88.69  ? 2442 GLN A CD    1 
ATOM   6258  O OE1   . GLN A 1 2442 ? 145.030 176.249 194.177 1.00 88.69  ? 2442 GLN A OE1   1 
ATOM   6259  N NE2   . GLN A 1 2442 ? 145.081 174.011 194.336 1.00 88.69  ? 2442 GLN A NE2   1 
ATOM   6260  N N     . LEU A 1 2443 ? 145.977 176.810 191.272 1.00 88.90  ? 2443 LEU A N     1 
ATOM   6261  C CA    . LEU A 1 2443 ? 144.910 176.210 190.489 1.00 88.90  ? 2443 LEU A CA    1 
ATOM   6262  C C     . LEU A 1 2443 ? 145.412 175.864 189.085 1.00 88.90  ? 2443 LEU A C     1 
ATOM   6263  O O     . LEU A 1 2443 ? 146.484 176.295 188.653 1.00 88.90  ? 2443 LEU A O     1 
ATOM   6264  C CB    . LEU A 1 2443 ? 143.718 177.164 190.426 1.00 88.90  ? 2443 LEU A CB    1 
ATOM   6265  C CG    . LEU A 1 2443 ? 142.372 176.677 189.897 1.00 88.90  ? 2443 LEU A CG    1 
ATOM   6266  C CD1   . LEU A 1 2443 ? 142.068 175.311 190.460 1.00 88.90  ? 2443 LEU A CD1   1 
ATOM   6267  C CD2   . LEU A 1 2443 ? 141.277 177.658 190.262 1.00 88.90  ? 2443 LEU A CD2   1 
ATOM   6268  N N     . GLU A 1 2444 ? 144.622 175.067 188.372 1.00 90.32  ? 2444 GLU A N     1 
ATOM   6269  C CA    . GLU A 1 2444 ? 144.966 174.599 187.035 1.00 90.32  ? 2444 GLU A CA    1 
ATOM   6270  C C     . GLU A 1 2444 ? 144.251 175.442 185.988 1.00 90.32  ? 2444 GLU A C     1 
ATOM   6271  O O     . GLU A 1 2444 ? 143.068 175.760 186.143 1.00 90.32  ? 2444 GLU A O     1 
ATOM   6272  C CB    . GLU A 1 2444 ? 144.598 173.124 186.872 1.00 90.32  ? 2444 GLU A CB    1 
ATOM   6273  C CG    . GLU A 1 2444 ? 144.745 172.588 185.459 1.00 90.32  ? 2444 GLU A CG    1 
ATOM   6274  C CD    . GLU A 1 2444 ? 143.480 172.753 184.642 1.00 90.32  ? 2444 GLU A CD    1 
ATOM   6275  O OE1   . GLU A 1 2444 ? 142.414 172.287 185.093 1.00 90.32  ? 2444 GLU A OE1   1 
ATOM   6276  O OE2   . GLU A 1 2444 ? 143.551 173.359 183.553 1.00 90.32  ? 2444 GLU A OE2   1 
ATOM   6277  N N     . HIS A 1 2445 ? 144.966 175.789 184.919 1.00 81.78  ? 2445 HIS A N     1 
ATOM   6278  C CA    . HIS A 1 2445 ? 144.433 176.620 183.851 1.00 81.78  ? 2445 HIS A CA    1 
ATOM   6279  C C     . HIS A 1 2445 ? 144.734 175.988 182.502 1.00 81.78  ? 2445 HIS A C     1 
ATOM   6280  O O     . HIS A 1 2445 ? 145.718 175.260 182.346 1.00 81.78  ? 2445 HIS A O     1 
ATOM   6281  C CB    . HIS A 1 2445 ? 145.017 178.029 183.900 1.00 81.78  ? 2445 HIS A CB    1 
ATOM   6282  C CG    . HIS A 1 2445 ? 144.751 178.742 185.185 1.00 81.78  ? 2445 HIS A CG    1 
ATOM   6283  N ND1   . HIS A 1 2445 ? 143.892 179.814 185.276 1.00 81.78  ? 2445 HIS A ND1   1 
ATOM   6284  C CD2   . HIS A 1 2445 ? 145.219 178.527 186.437 1.00 81.78  ? 2445 HIS A CD2   1 
ATOM   6285  C CE1   . HIS A 1 2445 ? 143.849 180.235 186.527 1.00 81.78  ? 2445 HIS A CE1   1 
ATOM   6286  N NE2   . HIS A 1 2445 ? 144.643 179.469 187.252 1.00 81.78  ? 2445 HIS A NE2   1 
ATOM   6287  N N     . ILE A 1 2446 ? 143.872 176.275 181.524 1.00 74.38  ? 2446 ILE A N     1 
ATOM   6288  C CA    . ILE A 1 2446 ? 144.041 175.698 180.195 1.00 74.38  ? 2446 ILE A CA    1 
ATOM   6289  C C     . ILE A 1 2446 ? 145.311 176.223 179.540 1.00 74.38  ? 2446 ILE A C     1 
ATOM   6290  O O     . ILE A 1 2446 ? 145.994 175.496 178.809 1.00 74.38  ? 2446 ILE A O     1 
ATOM   6291  C CB    . ILE A 1 2446 ? 142.796 175.965 179.330 1.00 74.38  ? 2446 ILE A CB    1 
ATOM   6292  C CG1   . ILE A 1 2446 ? 142.875 175.161 178.036 1.00 74.38  ? 2446 ILE A CG1   1 
ATOM   6293  C CG2   . ILE A 1 2446 ? 142.650 177.438 179.022 1.00 74.38  ? 2446 ILE A CG2   1 
ATOM   6294  C CD1   . ILE A 1 2446 ? 143.013 173.680 178.261 1.00 74.38  ? 2446 ILE A CD1   1 
ATOM   6295  N N     . MET A 1 2447 ? 145.650 177.482 179.788 1.00 79.67  ? 2447 MET A N     1 
ATOM   6296  C CA    . MET A 1 2447 ? 146.894 178.069 179.328 1.00 79.67  ? 2447 MET A CA    1 
ATOM   6297  C C     . MET A 1 2447 ? 147.734 178.450 180.537 1.00 79.67  ? 2447 MET A C     1 
ATOM   6298  O O     . MET A 1 2447 ? 147.230 178.556 181.656 1.00 79.67  ? 2447 MET A O     1 
ATOM   6299  C CB    . MET A 1 2447 ? 146.642 179.294 178.444 1.00 79.67  ? 2447 MET A CB    1 
ATOM   6300  C CG    . MET A 1 2447 ? 145.519 179.112 177.440 1.00 79.67  ? 2447 MET A CG    1 
ATOM   6301  S SD    . MET A 1 2447 ? 145.885 179.845 175.833 1.00 79.67  ? 2447 MET A SD    1 
ATOM   6302  C CE    . MET A 1 2447 ? 147.198 178.773 175.256 1.00 79.67  ? 2447 MET A CE    1 
ATOM   6303  N N     . ASP A 1 2448 ? 149.028 178.637 180.304 1.00 88.61  ? 2448 ASP A N     1 
ATOM   6304  C CA    . ASP A 1 2448 ? 149.936 178.981 181.389 1.00 88.61  ? 2448 ASP A CA    1 
ATOM   6305  C C     . ASP A 1 2448 ? 149.491 180.278 182.049 1.00 88.61  ? 2448 ASP A C     1 
ATOM   6306  O O     . ASP A 1 2448 ? 149.280 181.288 181.372 1.00 88.61  ? 2448 ASP A O     1 
ATOM   6307  C CB    . ASP A 1 2448 ? 151.357 179.111 180.851 1.00 88.61  ? 2448 ASP A CB    1 
ATOM   6308  C CG    . ASP A 1 2448 ? 151.693 178.037 179.839 1.00 88.61  ? 2448 ASP A CG    1 
ATOM   6309  O OD1   . ASP A 1 2448 ? 151.151 176.919 179.963 1.00 88.61  ? 2448 ASP A OD1   1 
ATOM   6310  O OD2   . ASP A 1 2448 ? 152.491 178.310 178.918 1.00 88.61  ? 2448 ASP A OD2   1 
ATOM   6311  N N     . LEU A 1 2449 ? 149.335 180.248 183.368 1.00 80.49  ? 2449 LEU A N     1 
ATOM   6312  C CA    . LEU A 1 2449 ? 148.866 181.426 184.084 1.00 80.49  ? 2449 LEU A CA    1 
ATOM   6313  C C     . LEU A 1 2449 ? 150.025 182.389 184.295 1.00 80.49  ? 2449 LEU A C     1 
ATOM   6314  O O     . LEU A 1 2449 ? 151.025 182.040 184.930 1.00 80.49  ? 2449 LEU A O     1 
ATOM   6315  C CB    . LEU A 1 2449 ? 148.255 181.026 185.423 1.00 80.49  ? 2449 LEU A CB    1 
ATOM   6316  C CG    . LEU A 1 2449 ? 147.892 182.160 186.387 1.00 80.49  ? 2449 LEU A CG    1 
ATOM   6317  C CD1   . LEU A 1 2449 ? 147.205 183.320 185.672 1.00 80.49  ? 2449 LEU A CD1   1 
ATOM   6318  C CD2   . LEU A 1 2449 ? 147.032 181.647 187.527 1.00 80.49  ? 2449 LEU A CD2   1 
ATOM   6319  N N     . THR A 1 2450 ? 149.886 183.600 183.773 1.00 81.33  ? 2450 THR A N     1 
ATOM   6320  C CA    . THR A 1 2450 ? 150.866 184.657 183.954 1.00 81.33  ? 2450 THR A CA    1 
ATOM   6321  C C     . THR A 1 2450 ? 150.234 185.776 184.767 1.00 81.33  ? 2450 THR A C     1 
ATOM   6322  O O     . THR A 1 2450 ? 149.104 186.190 184.492 1.00 81.33  ? 2450 THR A O     1 
ATOM   6323  C CB    . THR A 1 2450 ? 151.358 185.188 182.606 1.00 81.33  ? 2450 THR A CB    1 
ATOM   6324  O OG1   . THR A 1 2450 ? 152.213 184.215 181.995 1.00 81.33  ? 2450 THR A OG1   1 
ATOM   6325  C CG2   . THR A 1 2450 ? 152.129 186.483 182.785 1.00 81.33  ? 2450 THR A CG2   1 
ATOM   6326  N N     . ARG A 1 2451 ? 150.970 186.264 185.767 1.00 75.66  ? 2451 ARG A N     1 
ATOM   6327  C CA    . ARG A 1 2451 ? 150.410 187.252 186.682 1.00 75.66  ? 2451 ARG A CA    1 
ATOM   6328  C C     . ARG A 1 2451 ? 149.949 188.497 185.940 1.00 75.66  ? 2451 ARG A C     1 
ATOM   6329  O O     . ARG A 1 2451 ? 148.870 189.036 186.221 1.00 75.66  ? 2451 ARG A O     1 
ATOM   6330  C CB    . ARG A 1 2451 ? 151.443 187.618 187.742 1.00 75.66  ? 2451 ARG A CB    1 
ATOM   6331  C CG    . ARG A 1 2451 ? 151.025 188.763 188.627 1.00 75.66  ? 2451 ARG A CG    1 
ATOM   6332  C CD    . ARG A 1 2451 ? 152.156 189.178 189.538 1.00 75.66  ? 2451 ARG A CD    1 
ATOM   6333  N NE    . ARG A 1 2451 ? 153.333 189.572 188.777 1.00 75.66  ? 2451 ARG A NE    1 
ATOM   6334  C CZ    . ARG A 1 2451 ? 154.363 190.234 189.283 1.00 75.66  ? 2451 ARG A CZ    1 
ATOM   6335  N NH1   . ARG A 1 2451 ? 154.392 190.599 190.553 1.00 75.66  ? 2451 ARG A NH1   1 
ATOM   6336  N NH2   . ARG A 1 2451 ? 155.387 190.540 188.494 1.00 75.66  ? 2451 ARG A NH2   1 
ATOM   6337  N N     . LEU A 1 2452 ? 150.749 188.965 184.983 1.00 72.85  ? 2452 LEU A N     1 
ATOM   6338  C CA    . LEU A 1 2452 ? 150.410 190.198 184.284 1.00 72.85  ? 2452 LEU A CA    1 
ATOM   6339  C C     . LEU A 1 2452 ? 149.131 190.052 183.473 1.00 72.85  ? 2452 LEU A C     1 
ATOM   6340  O O     . LEU A 1 2452 ? 148.324 190.983 183.421 1.00 72.85  ? 2452 LEU A O     1 
ATOM   6341  C CB    . LEU A 1 2452 ? 151.565 190.635 183.390 1.00 72.85  ? 2452 LEU A CB    1 
ATOM   6342  C CG    . LEU A 1 2452 ? 152.337 191.829 183.943 1.00 72.85  ? 2452 LEU A CG    1 
ATOM   6343  C CD1   . LEU A 1 2452 ? 151.416 193.024 184.048 1.00 72.85  ? 2452 LEU A CD1   1 
ATOM   6344  C CD2   . LEU A 1 2452 ? 152.933 191.499 185.291 1.00 72.85  ? 2452 LEU A CD2   1 
ATOM   6345  N N     . ARG A 1 2453 ? 148.927 188.901 182.828 1.00 75.22  ? 2453 ARG A N     1 
ATOM   6346  C CA    . ARG A 1 2453 ? 147.705 188.701 182.054 1.00 75.22  ? 2453 ARG A CA    1 
ATOM   6347  C C     . ARG A 1 2453 ? 146.470 188.814 182.936 1.00 75.22  ? 2453 ARG A C     1 
ATOM   6348  O O     . ARG A 1 2453 ? 145.522 189.546 182.617 1.00 75.22  ? 2453 ARG A O     1 
ATOM   6349  C CB    . ARG A 1 2453 ? 147.733 187.342 181.358 1.00 75.22  ? 2453 ARG A CB    1 
ATOM   6350  C CG    . ARG A 1 2453 ? 146.352 186.838 180.980 1.00 75.22  ? 2453 ARG A CG    1 
ATOM   6351  C CD    . ARG A 1 2453 ? 146.416 185.665 180.021 1.00 75.22  ? 2453 ARG A CD    1 
ATOM   6352  N NE    . ARG A 1 2453 ? 146.832 184.424 180.660 1.00 75.22  ? 2453 ARG A NE    1 
ATOM   6353  C CZ    . ARG A 1 2453 ? 146.045 183.665 181.409 1.00 75.22  ? 2453 ARG A CZ    1 
ATOM   6354  N NH1   . ARG A 1 2453 ? 144.790 184.001 181.653 1.00 75.22  ? 2453 ARG A NH1   1 
ATOM   6355  N NH2   . ARG A 1 2453 ? 146.529 182.540 181.924 1.00 75.22  ? 2453 ARG A NH2   1 
ATOM   6356  N N     . CYS A 1 2454 ? 146.467 188.087 184.052 1.00 73.74  ? 2454 CYS A N     1 
ATOM   6357  C CA    . CYS A 1 2454 ? 145.311 188.099 184.936 1.00 73.74  ? 2454 CYS A CA    1 
ATOM   6358  C C     . CYS A 1 2454 ? 145.082 189.487 185.516 1.00 73.74  ? 2454 CYS A C     1 
ATOM   6359  O O     . CYS A 1 2454 ? 143.943 189.969 185.563 1.00 73.74  ? 2454 CYS A O     1 
ATOM   6360  C CB    . CYS A 1 2454 ? 145.503 187.071 186.046 1.00 73.74  ? 2454 CYS A CB    1 
ATOM   6361  S SG    . CYS A 1 2454 ? 143.965 186.380 186.649 1.00 73.74  ? 2454 CYS A SG    1 
ATOM   6362  N N     . LEU A 1 2455 ? 146.154 190.154 185.945 1.00 71.99  ? 2455 LEU A N     1 
ATOM   6363  C CA    . LEU A 1 2455 ? 145.996 191.488 186.510 1.00 71.99  ? 2455 LEU A CA    1 
ATOM   6364  C C     . LEU A 1 2455 ? 145.479 192.474 185.470 1.00 71.99  ? 2455 LEU A C     1 
ATOM   6365  O O     . LEU A 1 2455 ? 144.629 193.316 185.779 1.00 71.99  ? 2455 LEU A O     1 
ATOM   6366  C CB    . LEU A 1 2455 ? 147.316 191.964 187.107 1.00 71.99  ? 2455 LEU A CB    1 
ATOM   6367  C CG    . LEU A 1 2455 ? 147.715 191.184 188.357 1.00 71.99  ? 2455 LEU A CG    1 
ATOM   6368  C CD1   . LEU A 1 2455 ? 148.906 191.820 189.033 1.00 71.99  ? 2455 LEU A CD1   1 
ATOM   6369  C CD2   . LEU A 1 2455 ? 146.547 191.086 189.317 1.00 71.99  ? 2455 LEU A CD2   1 
ATOM   6370  N N     . GLY A 1 2456 ? 145.969 192.384 184.233 1.00 73.65  ? 2456 GLY A N     1 
ATOM   6371  C CA    . GLY A 1 2456 ? 145.498 193.286 183.198 1.00 73.65  ? 2456 GLY A CA    1 
ATOM   6372  C C     . GLY A 1 2456 ? 144.035 193.076 182.868 1.00 73.65  ? 2456 GLY A C     1 
ATOM   6373  O O     . GLY A 1 2456 ? 143.279 194.039 182.709 1.00 73.65  ? 2456 GLY A O     1 
ATOM   6374  N N     . SER A 1 2457 ? 143.611 191.815 182.769 1.00 70.49  ? 2457 SER A N     1 
ATOM   6375  C CA    . SER A 1 2457 ? 142.199 191.551 182.522 1.00 70.49  ? 2457 SER A CA    1 
ATOM   6376  C C     . SER A 1 2457 ? 141.340 192.066 183.669 1.00 70.49  ? 2457 SER A C     1 
ATOM   6377  O O     . SER A 1 2457 ? 140.268 192.647 183.446 1.00 70.49  ? 2457 SER A O     1 
ATOM   6378  C CB    . SER A 1 2457 ? 141.974 190.059 182.312 1.00 70.49  ? 2457 SER A CB    1 
ATOM   6379  O OG    . SER A 1 2457 ? 141.564 189.446 183.517 1.00 70.49  ? 2457 SER A OG    1 
ATOM   6380  N N     . LEU A 1 2458 ? 141.800 191.869 184.906 1.00 71.33  ? 2458 LEU A N     1 
ATOM   6381  C CA    . LEU A 1 2458 ? 141.058 192.367 186.058 1.00 71.33  ? 2458 LEU A CA    1 
ATOM   6382  C C     . LEU A 1 2458 ? 140.922 193.883 186.008 1.00 71.33  ? 2458 LEU A C     1 
ATOM   6383  O O     . LEU A 1 2458 ? 139.836 194.428 186.245 1.00 71.33  ? 2458 LEU A O     1 
ATOM   6384  C CB    . LEU A 1 2458 ? 141.756 191.929 187.342 1.00 71.33  ? 2458 LEU A CB    1 
ATOM   6385  C CG    . LEU A 1 2458 ? 141.243 192.503 188.655 1.00 71.33  ? 2458 LEU A CG    1 
ATOM   6386  C CD1   . LEU A 1 2458 ? 139.881 191.931 188.947 1.00 71.33  ? 2458 LEU A CD1   1 
ATOM   6387  C CD2   . LEU A 1 2458 ? 142.204 192.181 189.775 1.00 71.33  ? 2458 LEU A CD2   1 
ATOM   6388  N N     . PHE A 1 2459 ? 142.011 194.580 185.688 1.00 73.84  ? 2459 PHE A N     1 
ATOM   6389  C CA    . PHE A 1 2459 ? 141.954 196.035 185.603 1.00 73.84  ? 2459 PHE A CA    1 
ATOM   6390  C C     . PHE A 1 2459 ? 141.001 196.479 184.505 1.00 73.84  ? 2459 PHE A C     1 
ATOM   6391  O O     . PHE A 1 2459 ? 140.259 197.454 184.672 1.00 73.84  ? 2459 PHE A O     1 
ATOM   6392  C CB    . PHE A 1 2459 ? 143.350 196.604 185.366 1.00 73.84  ? 2459 PHE A CB    1 
ATOM   6393  C CG    . PHE A 1 2459 ? 144.344 196.222 186.419 1.00 73.84  ? 2459 PHE A CG    1 
ATOM   6394  C CD1   . PHE A 1 2459 ? 143.933 195.948 187.709 1.00 73.84  ? 2459 PHE A CD1   1 
ATOM   6395  C CD2   . PHE A 1 2459 ? 145.687 196.124 186.116 1.00 73.84  ? 2459 PHE A CD2   1 
ATOM   6396  C CE1   . PHE A 1 2459 ? 144.843 195.590 188.676 1.00 73.84  ? 2459 PHE A CE1   1 
ATOM   6397  C CE2   . PHE A 1 2459 ? 146.599 195.763 187.080 1.00 73.84  ? 2459 PHE A CE2   1 
ATOM   6398  C CZ    . PHE A 1 2459 ? 146.177 195.497 188.361 1.00 73.84  ? 2459 PHE A CZ    1 
ATOM   6399  N N     . SER A 1 2460 ? 141.011 195.778 183.371 1.00 76.32  ? 2460 SER A N     1 
ATOM   6400  C CA    . SER A 1 2460 ? 140.091 196.123 182.295 1.00 76.32  ? 2460 SER A CA    1 
ATOM   6401  C C     . SER A 1 2460 ? 138.645 195.983 182.746 1.00 76.32  ? 2460 SER A C     1 
ATOM   6402  O O     . SER A 1 2460 ? 137.805 196.846 182.459 1.00 76.32  ? 2460 SER A O     1 
ATOM   6403  C CB    . SER A 1 2460 ? 140.357 195.244 181.078 1.00 76.32  ? 2460 SER A CB    1 
ATOM   6404  O OG    . SER A 1 2460 ? 139.779 195.802 179.914 1.00 76.32  ? 2460 SER A OG    1 
ATOM   6405  N N     . MET A 1 2461 ? 138.336 194.907 183.464 1.00 77.78  ? 2461 MET A N     1 
ATOM   6406  C CA    . MET A 1 2461 ? 136.952 194.716 183.880 1.00 77.78  ? 2461 MET A CA    1 
ATOM   6407  C C     . MET A 1 2461 ? 136.542 195.729 184.943 1.00 77.78  ? 2461 MET A C     1 
ATOM   6408  O O     . MET A 1 2461 ? 135.387 196.172 184.963 1.00 77.78  ? 2461 MET A O     1 
ATOM   6409  C CB    . MET A 1 2461 ? 136.748 193.274 184.340 1.00 77.78  ? 2461 MET A CB    1 
ATOM   6410  C CG    . MET A 1 2461 ? 136.452 192.378 183.148 1.00 77.78  ? 2461 MET A CG    1 
ATOM   6411  S SD    . MET A 1 2461 ? 136.444 190.596 183.356 1.00 77.78  ? 2461 MET A SD    1 
ATOM   6412  C CE    . MET A 1 2461 ? 136.437 190.482 185.120 1.00 77.78  ? 2461 MET A CE    1 
ATOM   6413  N N     . LEU A 1 2462 ? 137.471 196.140 185.805 1.00 76.61  ? 2462 LEU A N     1 
ATOM   6414  C CA    . LEU A 1 2462 ? 137.171 197.223 186.741 1.00 76.61  ? 2462 LEU A CA    1 
ATOM   6415  C C     . LEU A 1 2462 ? 136.926 198.544 186.016 1.00 76.61  ? 2462 LEU A C     1 
ATOM   6416  O O     . LEU A 1 2462 ? 136.032 199.316 186.396 1.00 76.61  ? 2462 LEU A O     1 
ATOM   6417  C CB    . LEU A 1 2462 ? 138.302 197.350 187.756 1.00 76.61  ? 2462 LEU A CB    1 
ATOM   6418  C CG    . LEU A 1 2462 ? 138.134 196.539 189.038 1.00 76.61  ? 2462 LEU A CG    1 
ATOM   6419  C CD1   . LEU A 1 2462 ? 138.271 195.067 188.795 1.00 76.61  ? 2462 LEU A CD1   1 
ATOM   6420  C CD2   . LEU A 1 2462 ? 139.217 196.969 189.994 1.00 76.61  ? 2462 LEU A CD2   1 
ATOM   6421  N N     . HIS A 1 2463 ? 137.704 198.823 184.972 1.00 80.09  ? 2463 HIS A N     1 
ATOM   6422  C CA    . HIS A 1 2463 ? 137.436 200.009 184.168 1.00 80.09  ? 2463 HIS A CA    1 
ATOM   6423  C C     . HIS A 1 2463 ? 136.045 199.943 183.558 1.00 80.09  ? 2463 HIS A C     1 
ATOM   6424  O O     . HIS A 1 2463 ? 135.328 200.951 183.505 1.00 80.09  ? 2463 HIS A O     1 
ATOM   6425  C CB    . HIS A 1 2463 ? 138.485 200.153 183.069 1.00 80.09  ? 2463 HIS A CB    1 
ATOM   6426  C CG    . HIS A 1 2463 ? 139.822 200.603 183.562 1.00 80.09  ? 2463 HIS A CG    1 
ATOM   6427  N ND1   . HIS A 1 2463 ? 140.893 200.805 182.719 1.00 80.09  ? 2463 HIS A ND1   1 
ATOM   6428  C CD2   . HIS A 1 2463 ? 140.264 200.887 184.809 1.00 80.09  ? 2463 HIS A CD2   1 
ATOM   6429  C CE1   . HIS A 1 2463 ? 141.937 201.198 183.426 1.00 80.09  ? 2463 HIS A CE1   1 
ATOM   6430  N NE2   . HIS A 1 2463 ? 141.583 201.255 184.696 1.00 80.09  ? 2463 HIS A NE2   1 
ATOM   6431  N N     . GLN A 1 2464 ? 135.649 198.763 183.082 1.00 81.97  ? 2464 GLN A N     1 
ATOM   6432  C CA    . GLN A 1 2464 ? 134.303 198.616 182.540 1.00 81.97  ? 2464 GLN A CA    1 
ATOM   6433  C C     . GLN A 1 2464 ? 133.249 198.842 183.612 1.00 81.97  ? 2464 GLN A C     1 
ATOM   6434  O O     . GLN A 1 2464 ? 132.172 199.373 183.328 1.00 81.97  ? 2464 GLN A O     1 
ATOM   6435  C CB    . GLN A 1 2464 ? 134.129 197.241 181.907 1.00 81.97  ? 2464 GLN A CB    1 
ATOM   6436  C CG    . GLN A 1 2464 ? 132.708 196.955 181.453 1.00 81.97  ? 2464 GLN A CG    1 
ATOM   6437  C CD    . GLN A 1 2464 ? 132.173 198.009 180.506 1.00 81.97  ? 2464 GLN A CD    1 
ATOM   6438  O OE1   . GLN A 1 2464 ? 132.895 198.513 179.649 1.00 81.97  ? 2464 GLN A OE1   1 
ATOM   6439  N NE2   . GLN A 1 2464 ? 130.898 198.343 180.653 1.00 81.97  ? 2464 GLN A NE2   1 
ATOM   6440  N N     . ALA A 1 2465 ? 133.528 198.426 184.847 1.00 82.75  ? 2465 ALA A N     1 
ATOM   6441  C CA    . ALA A 1 2465 ? 132.599 198.712 185.937 1.00 82.75  ? 2465 ALA A CA    1 
ATOM   6442  C C     . ALA A 1 2465 ? 132.435 200.214 186.136 1.00 82.75  ? 2465 ALA A C     1 
ATOM   6443  O O     . ALA A 1 2465 ? 131.314 200.713 186.317 1.00 82.75  ? 2465 ALA A O     1 
ATOM   6444  C CB    . ALA A 1 2465 ? 133.078 198.055 187.229 1.00 82.75  ? 2465 ALA A CB    1 
ATOM   6445  N N     . CYS A 1 2466 ? 133.545 200.951 186.105 1.00 84.84  ? 2466 CYS A N     1 
ATOM   6446  C CA    . CYS A 1 2466 ? 133.454 202.404 186.220 1.00 84.84  ? 2466 CYS A CA    1 
ATOM   6447  C C     . CYS A 1 2466 ? 132.648 202.994 185.068 1.00 84.84  ? 2466 CYS A C     1 
ATOM   6448  O O     . CYS A 1 2466 ? 131.826 203.899 185.269 1.00 84.84  ? 2466 CYS A O     1 
ATOM   6449  C CB    . CYS A 1 2466 ? 134.849 203.022 186.270 1.00 84.84  ? 2466 CYS A CB    1 
ATOM   6450  S SG    . CYS A 1 2466 ? 135.858 202.468 187.657 1.00 84.84  ? 2466 CYS A SG    1 
ATOM   6451  N N     . ARG A 1 2467 ? 132.866 202.488 183.854 1.00 85.14  ? 2467 ARG A N     1 
ATOM   6452  C CA    . ARG A 1 2467 ? 132.096 202.968 182.711 1.00 85.14  ? 2467 ARG A CA    1 
ATOM   6453  C C     . ARG A 1 2467 ? 130.614 202.656 182.876 1.00 85.14  ? 2467 ARG A C     1 
ATOM   6454  O O     . ARG A 1 2467 ? 129.757 203.451 182.477 1.00 85.14  ? 2467 ARG A O     1 
ATOM   6455  C CB    . ARG A 1 2467 ? 132.629 202.361 181.415 1.00 85.14  ? 2467 ARG A CB    1 
ATOM   6456  C CG    . ARG A 1 2467 ? 132.801 203.374 180.296 1.00 85.14  ? 2467 ARG A CG    1 
ATOM   6457  C CD    . ARG A 1 2467 ? 133.609 202.815 179.137 1.00 85.14  ? 2467 ARG A CD    1 
ATOM   6458  N NE    . ARG A 1 2467 ? 134.956 202.417 179.526 1.00 85.14  ? 2467 ARG A NE    1 
ATOM   6459  C CZ    . ARG A 1 2467 ? 135.339 201.162 179.712 1.00 85.14  ? 2467 ARG A CZ    1 
ATOM   6460  N NH1   . ARG A 1 2467 ? 134.494 200.156 179.580 1.00 85.14  ? 2467 ARG A NH1   1 
ATOM   6461  N NH2   . ARG A 1 2467 ? 136.602 200.912 180.042 1.00 85.14  ? 2467 ARG A NH2   1 
ATOM   6462  N N     . ASN A 1 2468 ? 130.292 201.496 183.448 1.00 87.67  ? 2468 ASN A N     1 
ATOM   6463  C CA    . ASN A 1 2468 ? 128.897 201.163 183.705 1.00 87.67  ? 2468 ASN A CA    1 
ATOM   6464  C C     . ASN A 1 2468 ? 128.277 202.144 184.684 1.00 87.67  ? 2468 ASN A C     1 
ATOM   6465  O O     . ASN A 1 2468 ? 127.128 202.563 184.510 1.00 87.67  ? 2468 ASN A O     1 
ATOM   6466  C CB    . ASN A 1 2468 ? 128.778 199.737 184.240 1.00 87.67  ? 2468 ASN A CB    1 
ATOM   6467  C CG    . ASN A 1 2468 ? 128.999 198.696 183.170 1.00 87.67  ? 2468 ASN A CG    1 
ATOM   6468  O OD1   . ASN A 1 2468 ? 129.200 199.026 182.003 1.00 87.67  ? 2468 ASN A OD1   1 
ATOM   6469  N ND2   . ASN A 1 2468 ? 128.957 197.429 183.560 1.00 87.67  ? 2468 ASN A ND2   1 
ATOM   6470  N N     . VAL A 1 2469 ? 129.021 202.516 185.726 1.00 89.59  ? 2469 VAL A N     1 
ATOM   6471  C CA    . VAL A 1 2469 ? 128.501 203.499 186.674 1.00 89.59  ? 2469 VAL A CA    1 
ATOM   6472  C C     . VAL A 1 2469 ? 128.262 204.831 185.978 1.00 89.59  ? 2469 VAL A C     1 
ATOM   6473  O O     . VAL A 1 2469 ? 127.244 205.499 186.205 1.00 89.59  ? 2469 VAL A O     1 
ATOM   6474  C CB    . VAL A 1 2469 ? 129.450 203.651 187.874 1.00 89.59  ? 2469 VAL A CB    1 
ATOM   6475  C CG1   . VAL A 1 2469 ? 128.932 204.718 188.816 1.00 89.59  ? 2469 VAL A CG1   1 
ATOM   6476  C CG2   . VAL A 1 2469 ? 129.582 202.334 188.603 1.00 89.59  ? 2469 VAL A CG2   1 
ATOM   6477  N N     . ALA A 1 2470 ? 129.198 205.240 185.122 1.00 96.23  ? 2470 ALA A N     1 
ATOM   6478  C CA    . ALA A 1 2470 ? 129.020 206.488 184.385 1.00 96.23  ? 2470 ALA A CA    1 
ATOM   6479  C C     . ALA A 1 2470 ? 127.786 206.429 183.493 1.00 96.23  ? 2470 ALA A C     1 
ATOM   6480  O O     . ALA A 1 2470 ? 127.011 207.391 183.424 1.00 96.23  ? 2470 ALA A O     1 
ATOM   6481  C CB    . ALA A 1 2470 ? 130.265 206.794 183.555 1.00 96.23  ? 2470 ALA A CB    1 
ATOM   6482  N N     . GLN A 1 2471 ? 127.584 205.305 182.807 1.00 101.24 ? 2471 GLN A N     1 
ATOM   6483  C CA    . GLN A 1 2471 ? 126.416 205.159 181.947 1.00 101.24 ? 2471 GLN A CA    1 
ATOM   6484  C C     . GLN A 1 2471 ? 125.128 205.193 182.758 1.00 101.24 ? 2471 GLN A C     1 
ATOM   6485  O O     . GLN A 1 2471 ? 124.131 205.784 182.329 1.00 101.24 ? 2471 GLN A O     1 
ATOM   6486  C CB    . GLN A 1 2471 ? 126.513 203.860 181.149 1.00 101.24 ? 2471 GLN A CB    1 
ATOM   6487  C CG    . GLN A 1 2471 ? 125.260 203.478 180.368 1.00 101.24 ? 2471 GLN A CG    1 
ATOM   6488  C CD    . GLN A 1 2471 ? 124.914 204.450 179.252 1.00 101.24 ? 2471 GLN A CD    1 
ATOM   6489  O OE1   . GLN A 1 2471 ? 124.743 205.649 179.474 1.00 101.24 ? 2471 GLN A OE1   1 
ATOM   6490  N NE2   . GLN A 1 2471 ? 124.808 203.929 178.037 1.00 101.24 ? 2471 GLN A NE2   1 
ATOM   6491  N N     . TYR A 1 2472 ? 125.128 204.556 183.929 1.00 101.90 ? 2472 TYR A N     1 
ATOM   6492  C CA    . TYR A 1 2472 ? 123.945 204.572 184.781 1.00 101.90 ? 2472 TYR A CA    1 
ATOM   6493  C C     . TYR A 1 2472 ? 123.623 205.982 185.251 1.00 101.90 ? 2472 TYR A C     1 
ATOM   6494  O O     . TYR A 1 2472 ? 122.451 206.372 185.306 1.00 101.90 ? 2472 TYR A O     1 
ATOM   6495  C CB    . TYR A 1 2472 ? 124.145 203.645 185.975 1.00 101.90 ? 2472 TYR A CB    1 
ATOM   6496  C CG    . TYR A 1 2472 ? 123.080 203.782 187.033 1.00 101.90 ? 2472 TYR A CG    1 
ATOM   6497  C CD1   . TYR A 1 2472 ? 121.812 203.255 186.840 1.00 101.90 ? 2472 TYR A CD1   1 
ATOM   6498  C CD2   . TYR A 1 2472 ? 123.343 204.431 188.229 1.00 101.90 ? 2472 TYR A CD2   1 
ATOM   6499  C CE1   . TYR A 1 2472 ? 120.835 203.374 187.806 1.00 101.90 ? 2472 TYR A CE1   1 
ATOM   6500  C CE2   . TYR A 1 2472 ? 122.374 204.554 189.201 1.00 101.90 ? 2472 TYR A CE2   1 
ATOM   6501  C CZ    . TYR A 1 2472 ? 121.121 204.024 188.985 1.00 101.90 ? 2472 TYR A CZ    1 
ATOM   6502  O OH    . TYR A 1 2472 ? 120.150 204.145 189.952 1.00 101.90 ? 2472 TYR A OH    1 
ATOM   6503  N N     . ASN A 1 2473 ? 124.648 206.757 185.610 1.00 104.26 ? 2473 ASN A N     1 
ATOM   6504  C CA    . ASN A 1 2473 ? 124.409 208.151 185.975 1.00 104.26 ? 2473 ASN A CA    1 
ATOM   6505  C C     . ASN A 1 2473 ? 123.908 208.952 184.780 1.00 104.26 ? 2473 ASN A C     1 
ATOM   6506  O O     . ASN A 1 2473 ? 123.107 209.880 184.938 1.00 104.26 ? 2473 ASN A O     1 
ATOM   6507  C CB    . ASN A 1 2473 ? 125.674 208.779 186.556 1.00 104.26 ? 2473 ASN A CB    1 
ATOM   6508  C CG    . ASN A 1 2473 ? 125.674 208.786 188.071 1.00 104.26 ? 2473 ASN A CG    1 
ATOM   6509  O OD1   . ASN A 1 2473 ? 124.713 208.351 188.701 1.00 104.26 ? 2473 ASN A OD1   1 
ATOM   6510  N ND2   . ASN A 1 2473 ? 126.751 209.285 188.663 1.00 104.26 ? 2473 ASN A ND2   1 
ATOM   6511  N N     . ALA A 1 2474 ? 124.378 208.616 183.578 1.00 106.22 ? 2474 ALA A N     1 
ATOM   6512  C CA    . ALA A 1 2474 ? 123.877 209.285 182.381 1.00 106.22 ? 2474 ALA A CA    1 
ATOM   6513  C C     . ALA A 1 2474 ? 122.399 208.988 182.159 1.00 106.22 ? 2474 ALA A C     1 
ATOM   6514  O O     . ALA A 1 2474 ? 121.625 209.883 181.801 1.00 106.22 ? 2474 ALA A O     1 
ATOM   6515  C CB    . ALA A 1 2474 ? 124.697 208.865 181.162 1.00 106.22 ? 2474 ALA A CB    1 
ATOM   6516  N N     . ASN A 1 2475 ? 121.989 207.735 182.365 1.00 107.57 ? 2475 ASN A N     1 
ATOM   6517  C CA    . ASN A 1 2475 ? 120.591 207.363 182.178 1.00 107.57 ? 2475 ASN A CA    1 
ATOM   6518  C C     . ASN A 1 2475 ? 119.673 208.017 183.198 1.00 107.57 ? 2475 ASN A C     1 
ATOM   6519  O O     . ASN A 1 2475 ? 118.466 208.104 182.957 1.00 107.57 ? 2475 ASN A O     1 
ATOM   6520  C CB    . ASN A 1 2475 ? 120.425 205.845 182.252 1.00 107.57 ? 2475 ASN A CB    1 
ATOM   6521  C CG    . ASN A 1 2475 ? 120.542 205.180 180.897 1.00 107.57 ? 2475 ASN A CG    1 
ATOM   6522  O OD1   . ASN A 1 2475 ? 120.627 205.850 179.869 1.00 107.57 ? 2475 ASN A OD1   1 
ATOM   6523  N ND2   . ASN A 1 2475 ? 120.541 203.853 180.889 1.00 107.57 ? 2475 ASN A ND2   1 
ATOM   6524  N N     . HIS A 1 2476 ? 120.212 208.469 184.327 1.00 108.97 ? 2476 HIS A N     1 
ATOM   6525  C CA    . HIS A 1 2476 ? 119.427 209.080 185.397 1.00 108.97 ? 2476 HIS A CA    1 
ATOM   6526  C C     . HIS A 1 2476 ? 120.051 210.425 185.735 1.00 108.97 ? 2476 HIS A C     1 
ATOM   6527  O O     . HIS A 1 2476 ? 120.759 210.557 186.743 1.00 108.97 ? 2476 HIS A O     1 
ATOM   6528  C CB    . HIS A 1 2476 ? 119.368 208.176 186.629 1.00 108.97 ? 2476 HIS A CB    1 
ATOM   6529  C CG    . HIS A 1 2476 ? 118.837 206.806 186.349 1.00 108.97 ? 2476 HIS A CG    1 
ATOM   6530  N ND1   . HIS A 1 2476 ? 119.487 205.909 185.530 1.00 108.97 ? 2476 HIS A ND1   1 
ATOM   6531  C CD2   . HIS A 1 2476 ? 117.716 206.180 186.777 1.00 108.97 ? 2476 HIS A CD2   1 
ATOM   6532  C CE1   . HIS A 1 2476 ? 118.790 204.789 185.466 1.00 108.97 ? 2476 HIS A CE1   1 
ATOM   6533  N NE2   . HIS A 1 2476 ? 117.711 204.927 186.214 1.00 108.97 ? 2476 HIS A NE2   1 
ATOM   6534  N N     . PRO A 1 2477 ? 119.815 211.449 184.909 1.00 113.97 ? 2477 PRO A N     1 
ATOM   6535  C CA    . PRO A 1 2477 ? 120.390 212.770 185.214 1.00 113.97 ? 2477 PRO A CA    1 
ATOM   6536  C C     . PRO A 1 2477 ? 119.982 213.283 186.580 1.00 113.97 ? 2477 PRO A C     1 
ATOM   6537  O O     . PRO A 1 2477 ? 120.784 213.926 187.267 1.00 113.97 ? 2477 PRO A O     1 
ATOM   6538  C CB    . PRO A 1 2477 ? 119.853 213.656 184.081 1.00 113.97 ? 2477 PRO A CB    1 
ATOM   6539  C CG    . PRO A 1 2477 ? 119.500 212.706 182.984 1.00 113.97 ? 2477 PRO A CG    1 
ATOM   6540  C CD    . PRO A 1 2477 ? 119.029 211.460 183.664 1.00 113.97 ? 2477 PRO A CD    1 
ATOM   6541  N N     . ASP A 1 2478 ? 118.753 213.007 186.995 1.00 124.75 ? 2478 ASP A N     1 
ATOM   6542  C CA    . ASP A 1 2478 ? 118.317 213.291 188.350 1.00 124.75 ? 2478 ASP A CA    1 
ATOM   6543  C C     . ASP A 1 2478 ? 118.577 212.081 189.237 1.00 124.75 ? 2478 ASP A C     1 
ATOM   6544  O O     . ASP A 1 2478 ? 118.523 210.934 188.784 1.00 124.75 ? 2478 ASP A O     1 
ATOM   6545  C CB    . ASP A 1 2478 ? 116.834 213.659 188.377 1.00 124.75 ? 2478 ASP A CB    1 
ATOM   6546  C CG    . ASP A 1 2478 ? 116.507 214.804 187.445 1.00 124.75 ? 2478 ASP A CG    1 
ATOM   6547  O OD1   . ASP A 1 2478 ? 117.452 215.433 186.925 1.00 124.75 ? 2478 ASP A OD1   1 
ATOM   6548  O OD2   . ASP A 1 2478 ? 115.307 215.077 187.232 1.00 124.75 ? 2478 ASP A OD2   1 
ATOM   6549  N N     . PHE A 1 2479 ? 118.859 212.353 190.511 1.00 127.48 ? 2479 PHE A N     1 
ATOM   6550  C CA    . PHE A 1 2479 ? 119.220 211.333 191.488 1.00 127.48 ? 2479 PHE A CA    1 
ATOM   6551  C C     . PHE A 1 2479 ? 120.363 210.475 190.963 1.00 127.48 ? 2479 PHE A C     1 
ATOM   6552  O O     . PHE A 1 2479 ? 120.152 209.308 190.612 1.00 127.48 ? 2479 PHE A O     1 
ATOM   6553  C CB    . PHE A 1 2479 ? 118.016 210.458 191.840 1.00 127.48 ? 2479 PHE A CB    1 
ATOM   6554  C CG    . PHE A 1 2479 ? 116.700 211.168 191.735 1.00 127.48 ? 2479 PHE A CG    1 
ATOM   6555  C CD1   . PHE A 1 2479 ? 116.401 212.224 192.577 1.00 127.48 ? 2479 PHE A CD1   1 
ATOM   6556  C CD2   . PHE A 1 2479 ? 115.761 210.777 190.797 1.00 127.48 ? 2479 PHE A CD2   1 
ATOM   6557  C CE1   . PHE A 1 2479 ? 115.191 212.881 192.484 1.00 127.48 ? 2479 PHE A CE1   1 
ATOM   6558  C CE2   . PHE A 1 2479 ? 114.549 211.428 190.700 1.00 127.48 ? 2479 PHE A CE2   1 
ATOM   6559  C CZ    . PHE A 1 2479 ? 114.263 212.482 191.544 1.00 127.48 ? 2479 PHE A CZ    1 
ATOM   6560  N N     . PRO A 1 2480 ? 121.579 211.012 190.889 1.00 123.91 ? 2480 PRO A N     1 
ATOM   6561  C CA    . PRO A 1 2480 ? 122.706 210.213 190.396 1.00 123.91 ? 2480 PRO A CA    1 
ATOM   6562  C C     . PRO A 1 2480 ? 123.116 209.121 191.371 1.00 123.91 ? 2480 PRO A C     1 
ATOM   6563  O O     . PRO A 1 2480 ? 122.478 208.927 192.409 1.00 123.91 ? 2480 PRO A O     1 
ATOM   6564  C CB    . PRO A 1 2480 ? 123.818 211.251 190.213 1.00 123.91 ? 2480 PRO A CB    1 
ATOM   6565  C CG    . PRO A 1 2480 ? 123.495 212.311 191.203 1.00 123.91 ? 2480 PRO A CG    1 
ATOM   6566  C CD    . PRO A 1 2480 ? 121.994 212.368 191.289 1.00 123.91 ? 2480 PRO A CD    1 
ATOM   6567  N N     . MET A 1 2481 ? 124.184 208.403 191.036 1.00 112.36 ? 2481 MET A N     1 
ATOM   6568  C CA    . MET A 1 2481 ? 124.604 207.258 191.830 1.00 112.36 ? 2481 MET A CA    1 
ATOM   6569  C C     . MET A 1 2481 ? 125.081 207.730 193.200 1.00 112.36 ? 2481 MET A C     1 
ATOM   6570  O O     . MET A 1 2481 ? 125.894 208.653 193.302 1.00 112.36 ? 2481 MET A O     1 
ATOM   6571  C CB    . MET A 1 2481 ? 125.724 206.522 191.099 1.00 112.36 ? 2481 MET A CB    1 
ATOM   6572  C CG    . MET A 1 2481 ? 126.552 205.584 191.945 1.00 112.36 ? 2481 MET A CG    1 
ATOM   6573  S SD    . MET A 1 2481 ? 125.538 204.534 192.997 1.00 112.36 ? 2481 MET A SD    1 
ATOM   6574  C CE    . MET A 1 2481 ? 125.500 203.057 191.987 1.00 112.36 ? 2481 MET A CE    1 
ATOM   6575  N N     . GLN A 1 2482 ? 124.582 207.092 194.253 1.00 110.98 ? 2482 GLN A N     1 
ATOM   6576  C CA    . GLN A 1 2482 ? 124.915 207.482 195.614 1.00 110.98 ? 2482 GLN A CA    1 
ATOM   6577  C C     . GLN A 1 2482 ? 126.180 206.777 196.092 1.00 110.98 ? 2482 GLN A C     1 
ATOM   6578  O O     . GLN A 1 2482 ? 126.728 205.902 195.425 1.00 110.98 ? 2482 GLN A O     1 
ATOM   6579  C CB    . GLN A 1 2482 ? 123.753 207.182 196.561 1.00 110.98 ? 2482 GLN A CB    1 
ATOM   6580  C CG    . GLN A 1 2482 ? 122.562 208.102 196.383 1.00 110.98 ? 2482 GLN A CG    1 
ATOM   6581  C CD    . GLN A 1 2482 ? 122.952 209.564 196.437 1.00 110.98 ? 2482 GLN A CD    1 
ATOM   6582  O OE1   . GLN A 1 2482 ? 123.412 210.058 197.466 1.00 110.98 ? 2482 GLN A OE1   1 
ATOM   6583  N NE2   . GLN A 1 2482 ? 122.774 210.266 195.324 1.00 110.98 ? 2482 GLN A NE2   1 
ATOM   6584  N N     . ILE A 1 2483 ? 126.646 207.179 197.275 1.00 104.80 ? 2483 ILE A N     1 
ATOM   6585  C CA    . ILE A 1 2483 ? 127.895 206.638 197.802 1.00 104.80 ? 2483 ILE A CA    1 
ATOM   6586  C C     . ILE A 1 2483 ? 127.727 205.175 198.197 1.00 104.80 ? 2483 ILE A C     1 
ATOM   6587  O O     . ILE A 1 2483 ? 128.555 204.325 197.853 1.00 104.80 ? 2483 ILE A O     1 
ATOM   6588  C CB    . ILE A 1 2483 ? 128.391 207.491 198.982 1.00 104.80 ? 2483 ILE A CB    1 
ATOM   6589  C CG1   . ILE A 1 2483 ? 129.242 208.652 198.469 1.00 104.80 ? 2483 ILE A CG1   1 
ATOM   6590  C CG2   . ILE A 1 2483 ? 129.196 206.647 199.956 1.00 104.80 ? 2483 ILE A CG2   1 
ATOM   6591  C CD1   . ILE A 1 2483 ? 130.528 208.211 197.810 1.00 104.80 ? 2483 ILE A CD1   1 
ATOM   6592  N N     . GLU A 1 2484 ? 126.653 204.856 198.922 1.00 107.27 ? 2484 GLU A N     1 
ATOM   6593  C CA    . GLU A 1 2484 ? 126.507 203.498 199.434 1.00 107.27 ? 2484 GLU A CA    1 
ATOM   6594  C C     . GLU A 1 2484 ? 126.190 202.514 198.315 1.00 107.27 ? 2484 GLU A C     1 
ATOM   6595  O O     . GLU A 1 2484 ? 126.721 201.397 198.294 1.00 107.27 ? 2484 GLU A O     1 
ATOM   6596  C CB    . GLU A 1 2484 ? 125.437 203.458 200.529 1.00 107.27 ? 2484 GLU A CB    1 
ATOM   6597  C CG    . GLU A 1 2484 ? 123.994 203.601 200.058 1.00 107.27 ? 2484 GLU A CG    1 
ATOM   6598  C CD    . GLU A 1 2484 ? 123.610 205.030 199.724 1.00 107.27 ? 2484 GLU A CD    1 
ATOM   6599  O OE1   . GLU A 1 2484 ? 124.512 205.886 199.606 1.00 107.27 ? 2484 GLU A OE1   1 
ATOM   6600  O OE2   . GLU A 1 2484 ? 122.399 205.299 199.580 1.00 107.27 ? 2484 GLU A OE2   1 
ATOM   6601  N N     . GLN A 1 2485 ? 125.339 202.911 197.368 1.00 99.84  ? 2485 GLN A N     1 
ATOM   6602  C CA    . GLN A 1 2485 ? 125.028 202.024 196.254 1.00 99.84  ? 2485 GLN A CA    1 
ATOM   6603  C C     . GLN A 1 2485 ? 126.247 201.821 195.365 1.00 99.84  ? 2485 GLN A C     1 
ATOM   6604  O O     . GLN A 1 2485 ? 126.494 200.709 194.884 1.00 99.84  ? 2485 GLN A O     1 
ATOM   6605  C CB    . GLN A 1 2485 ? 123.854 202.581 195.454 1.00 99.84  ? 2485 GLN A CB    1 
ATOM   6606  C CG    . GLN A 1 2485 ? 123.322 201.632 194.401 1.00 99.84  ? 2485 GLN A CG    1 
ATOM   6607  C CD    . GLN A 1 2485 ? 121.916 201.982 193.967 1.00 99.84  ? 2485 GLN A CD    1 
ATOM   6608  O OE1   . GLN A 1 2485 ? 121.276 202.858 194.547 1.00 99.84  ? 2485 GLN A OE1   1 
ATOM   6609  N NE2   . GLN A 1 2485 ? 121.428 201.298 192.941 1.00 99.84  ? 2485 GLN A NE2   1 
ATOM   6610  N N     . LEU A 1 2486 ? 127.021 202.885 195.139 1.00 98.97  ? 2486 LEU A N     1 
ATOM   6611  C CA    . LEU A 1 2486 ? 128.267 202.746 194.395 1.00 98.97  ? 2486 LEU A CA    1 
ATOM   6612  C C     . LEU A 1 2486 ? 129.220 201.803 195.107 1.00 98.97  ? 2486 LEU A C     1 
ATOM   6613  O O     . LEU A 1 2486 ? 129.863 200.965 194.469 1.00 98.97  ? 2486 LEU A O     1 
ATOM   6614  C CB    . LEU A 1 2486 ? 128.925 204.110 194.201 1.00 98.97  ? 2486 LEU A CB    1 
ATOM   6615  C CG    . LEU A 1 2486 ? 130.223 204.136 193.396 1.00 98.97  ? 2486 LEU A CG    1 
ATOM   6616  C CD1   . LEU A 1 2486 ? 130.074 203.339 192.116 1.00 98.97  ? 2486 LEU A CD1   1 
ATOM   6617  C CD2   . LEU A 1 2486 ? 130.629 205.567 193.094 1.00 98.97  ? 2486 LEU A CD2   1 
ATOM   6618  N N     . GLU A 1 2487 ? 129.328 201.927 196.430 1.00 100.31 ? 2487 GLU A N     1 
ATOM   6619  C CA    . GLU A 1 2487 ? 130.179 201.018 197.185 1.00 100.31 ? 2487 GLU A CA    1 
ATOM   6620  C C     . GLU A 1 2487 ? 129.732 199.576 197.006 1.00 100.31 ? 2487 GLU A C     1 
ATOM   6621  O O     . GLU A 1 2487 ? 130.553 198.693 196.733 1.00 100.31 ? 2487 GLU A O     1 
ATOM   6622  C CB    . GLU A 1 2487 ? 130.167 201.401 198.664 1.00 100.31 ? 2487 GLU A CB    1 
ATOM   6623  C CG    . GLU A 1 2487 ? 130.634 200.293 199.591 1.00 100.31 ? 2487 GLU A CG    1 
ATOM   6624  C CD    . GLU A 1 2487 ? 129.481 199.538 200.225 1.00 100.31 ? 2487 GLU A CD    1 
ATOM   6625  O OE1   . GLU A 1 2487 ? 128.354 200.075 200.242 1.00 100.31 ? 2487 GLU A OE1   1 
ATOM   6626  O OE2   . GLU A 1 2487 ? 129.700 198.407 200.707 1.00 100.31 ? 2487 GLU A OE2   1 
ATOM   6627  N N     . ARG A 1 2488 ? 128.431 199.321 197.154 1.00 97.15  ? 2488 ARG A N     1 
ATOM   6628  C CA    . ARG A 1 2488 ? 127.924 197.960 197.011 1.00 97.15  ? 2488 ARG A CA    1 
ATOM   6629  C C     . ARG A 1 2488 ? 128.229 197.410 195.624 1.00 97.15  ? 2488 ARG A C     1 
ATOM   6630  O O     . ARG A 1 2488 ? 128.758 196.297 195.480 1.00 97.15  ? 2488 ARG A O     1 
ATOM   6631  C CB    . ARG A 1 2488 ? 126.419 197.931 197.277 1.00 97.15  ? 2488 ARG A CB    1 
ATOM   6632  C CG    . ARG A 1 2488 ? 126.022 198.305 198.693 1.00 97.15  ? 2488 ARG A CG    1 
ATOM   6633  C CD    . ARG A 1 2488 ? 124.612 197.838 199.011 1.00 97.15  ? 2488 ARG A CD    1 
ATOM   6634  N NE    . ARG A 1 2488 ? 123.630 198.903 198.844 1.00 97.15  ? 2488 ARG A NE    1 
ATOM   6635  C CZ    . ARG A 1 2488 ? 122.973 199.144 197.719 1.00 97.15  ? 2488 ARG A CZ    1 
ATOM   6636  N NH1   . ARG A 1 2488 ? 123.170 198.415 196.634 1.00 97.15  ? 2488 ARG A NH1   1 
ATOM   6637  N NH2   . ARG A 1 2488 ? 122.094 200.141 197.682 1.00 97.15  ? 2488 ARG A NH2   1 
ATOM   6638  N N     . TYR A 1 2489 ? 127.912 198.190 194.590 1.00 89.07  ? 2489 TYR A N     1 
ATOM   6639  C CA    . TYR A 1 2489 ? 128.136 197.738 193.225 1.00 89.07  ? 2489 TYR A CA    1 
ATOM   6640  C C     . TYR A 1 2489 ? 129.609 197.469 192.979 1.00 89.07  ? 2489 TYR A C     1 
ATOM   6641  O O     . TYR A 1 2489 ? 129.969 196.467 192.361 1.00 89.07  ? 2489 TYR A O     1 
ATOM   6642  C CB    . TYR A 1 2489 ? 127.615 198.774 192.235 1.00 89.07  ? 2489 TYR A CB    1 
ATOM   6643  C CG    . TYR A 1 2489 ? 127.931 198.443 190.797 1.00 89.07  ? 2489 TYR A CG    1 
ATOM   6644  C CD1   . TYR A 1 2489 ? 127.317 197.379 190.159 1.00 89.07  ? 2489 TYR A CD1   1 
ATOM   6645  C CD2   . TYR A 1 2489 ? 128.848 199.193 190.079 1.00 89.07  ? 2489 TYR A CD2   1 
ATOM   6646  C CE1   . TYR A 1 2489 ? 127.604 197.074 188.843 1.00 89.07  ? 2489 TYR A CE1   1 
ATOM   6647  C CE2   . TYR A 1 2489 ? 129.141 198.895 188.765 1.00 89.07  ? 2489 TYR A CE2   1 
ATOM   6648  C CZ    . TYR A 1 2489 ? 128.516 197.836 188.152 1.00 89.07  ? 2489 TYR A CZ    1 
ATOM   6649  O OH    . TYR A 1 2489 ? 128.806 197.537 186.843 1.00 89.07  ? 2489 TYR A OH    1 
ATOM   6650  N N     . ILE A 1 2490 ? 130.478 198.352 193.466 1.00 83.49  ? 2490 ILE A N     1 
ATOM   6651  C CA    . ILE A 1 2490 ? 131.900 198.216 193.187 1.00 83.49  ? 2490 ILE A CA    1 
ATOM   6652  C C     . ILE A 1 2490 ? 132.471 196.993 193.885 1.00 83.49  ? 2490 ILE A C     1 
ATOM   6653  O O     . ILE A 1 2490 ? 133.251 196.242 193.295 1.00 83.49  ? 2490 ILE A O     1 
ATOM   6654  C CB    . ILE A 1 2490 ? 132.647 199.500 193.581 1.00 83.49  ? 2490 ILE A CB    1 
ATOM   6655  C CG1   . ILE A 1 2490 ? 132.484 200.556 192.489 1.00 83.49  ? 2490 ILE A CG1   1 
ATOM   6656  C CG2   . ILE A 1 2490 ? 134.112 199.211 193.805 1.00 83.49  ? 2490 ILE A CG2   1 
ATOM   6657  C CD1   . ILE A 1 2490 ? 132.954 200.099 191.132 1.00 83.49  ? 2490 ILE A CD1   1 
ATOM   6658  N N     . GLN A 1 2491 ? 132.099 196.763 195.145 1.00 90.28  ? 2491 GLN A N     1 
ATOM   6659  C CA    . GLN A 1 2491 ? 132.610 195.584 195.838 1.00 90.28  ? 2491 GLN A CA    1 
ATOM   6660  C C     . GLN A 1 2491 ? 132.127 194.299 195.175 1.00 90.28  ? 2491 GLN A C     1 
ATOM   6661  O O     . GLN A 1 2491 ? 132.916 193.367 194.948 1.00 90.28  ? 2491 GLN A O     1 
ATOM   6662  C CB    . GLN A 1 2491 ? 132.202 195.617 197.309 1.00 90.28  ? 2491 GLN A CB    1 
ATOM   6663  C CG    . GLN A 1 2491 ? 132.577 196.897 198.026 1.00 90.28  ? 2491 GLN A CG    1 
ATOM   6664  C CD    . GLN A 1 2491 ? 133.499 196.660 199.196 1.00 90.28  ? 2491 GLN A CD    1 
ATOM   6665  O OE1   . GLN A 1 2491 ? 133.638 195.534 199.667 1.00 90.28  ? 2491 GLN A OE1   1 
ATOM   6666  N NE2   . GLN A 1 2491 ? 134.139 197.720 199.673 1.00 90.28  ? 2491 GLN A NE2   1 
ATOM   6667  N N     . ARG A 1 2492 ? 130.833 194.228 194.852 1.00 94.82  ? 2492 ARG A N     1 
ATOM   6668  C CA    . ARG A 1 2492 ? 130.323 193.018 194.219 1.00 94.82  ? 2492 ARG A CA    1 
ATOM   6669  C C     . ARG A 1 2492 ? 130.958 192.811 192.850 1.00 94.82  ? 2492 ARG A C     1 
ATOM   6670  O O     . ARG A 1 2492 ? 131.297 191.680 192.481 1.00 94.82  ? 2492 ARG A O     1 
ATOM   6671  C CB    . ARG A 1 2492 ? 128.803 193.080 194.114 1.00 94.82  ? 2492 ARG A CB    1 
ATOM   6672  C CG    . ARG A 1 2492 ? 128.090 192.529 195.332 1.00 94.82  ? 2492 ARG A CG    1 
ATOM   6673  C CD    . ARG A 1 2492 ? 126.696 193.108 195.447 1.00 94.82  ? 2492 ARG A CD    1 
ATOM   6674  N NE    . ARG A 1 2492 ? 126.195 193.067 196.814 1.00 94.82  ? 2492 ARG A NE    1 
ATOM   6675  C CZ    . ARG A 1 2492 ? 126.601 193.874 197.785 1.00 94.82  ? 2492 ARG A CZ    1 
ATOM   6676  N NH1   . ARG A 1 2492 ? 127.529 194.792 197.578 1.00 94.82  ? 2492 ARG A NH1   1 
ATOM   6677  N NH2   . ARG A 1 2492 ? 126.062 193.757 198.994 1.00 94.82  ? 2492 ARG A NH2   1 
ATOM   6678  N N     . TYR A 1 2493 ? 131.137 193.890 192.088 1.00 82.08  ? 2493 TYR A N     1 
ATOM   6679  C CA    . TYR A 1 2493 ? 131.808 193.779 190.804 1.00 82.08  ? 2493 TYR A CA    1 
ATOM   6680  C C     . TYR A 1 2493 ? 133.252 193.360 190.974 1.00 82.08  ? 2493 TYR A C     1 
ATOM   6681  O O     . TYR A 1 2493 ? 133.784 192.648 190.128 1.00 82.08  ? 2493 TYR A O     1 
ATOM   6682  C CB    . TYR A 1 2493 ? 131.736 195.100 190.045 1.00 82.08  ? 2493 TYR A CB    1 
ATOM   6683  C CG    . TYR A 1 2493 ? 131.906 194.945 188.554 1.00 82.08  ? 2493 TYR A CG    1 
ATOM   6684  C CD1   . TYR A 1 2493 ? 133.148 194.693 188.000 1.00 82.08  ? 2493 TYR A CD1   1 
ATOM   6685  C CD2   . TYR A 1 2493 ? 130.822 195.052 187.702 1.00 82.08  ? 2493 TYR A CD2   1 
ATOM   6686  C CE1   . TYR A 1 2493 ? 133.305 194.549 186.643 1.00 82.08  ? 2493 TYR A CE1   1 
ATOM   6687  C CE2   . TYR A 1 2493 ? 130.969 194.911 186.342 1.00 82.08  ? 2493 TYR A CE2   1 
ATOM   6688  C CZ    . TYR A 1 2493 ? 132.213 194.660 185.817 1.00 82.08  ? 2493 TYR A CZ    1 
ATOM   6689  O OH    . TYR A 1 2493 ? 132.363 194.519 184.459 1.00 82.08  ? 2493 TYR A OH    1 
ATOM   6690  N N     . LEU A 1 2494 ? 133.908 193.796 192.047 1.00 80.97  ? 2494 LEU A N     1 
ATOM   6691  C CA    . LEU A 1 2494 ? 135.280 193.369 192.288 1.00 80.97  ? 2494 LEU A CA    1 
ATOM   6692  C C     . LEU A 1 2494 ? 135.345 191.867 192.506 1.00 80.97  ? 2494 LEU A C     1 
ATOM   6693  O O     . LEU A 1 2494 ? 136.219 191.184 191.959 1.00 80.97  ? 2494 LEU A O     1 
ATOM   6694  C CB    . LEU A 1 2494 ? 135.860 194.110 193.490 1.00 80.97  ? 2494 LEU A CB    1 
ATOM   6695  C CG    . LEU A 1 2494 ? 137.276 193.689 193.880 1.00 80.97  ? 2494 LEU A CG    1 
ATOM   6696  C CD1   . LEU A 1 2494 ? 138.208 193.814 192.697 1.00 80.97  ? 2494 LEU A CD1   1 
ATOM   6697  C CD2   . LEU A 1 2494 ? 137.778 194.521 195.041 1.00 80.97  ? 2494 LEU A CD2   1 
ATOM   6698  N N     . VAL A 1 2495 ? 134.425 191.332 193.305 1.00 76.86  ? 2495 VAL A N     1 
ATOM   6699  C CA    . VAL A 1 2495 ? 134.428 189.888 193.529 1.00 76.86  ? 2495 VAL A CA    1 
ATOM   6700  C C     . VAL A 1 2495 ? 134.119 189.144 192.237 1.00 76.86  ? 2495 VAL A C     1 
ATOM   6701  O O     . VAL A 1 2495 ? 134.790 188.164 191.889 1.00 76.86  ? 2495 VAL A O     1 
ATOM   6702  C CB    . VAL A 1 2495 ? 133.447 189.514 194.647 1.00 76.86  ? 2495 VAL A CB    1 
ATOM   6703  C CG1   . VAL A 1 2495 ? 133.244 188.012 194.681 1.00 76.86  ? 2495 VAL A CG1   1 
ATOM   6704  C CG2   . VAL A 1 2495 ? 133.984 190.002 195.967 1.00 76.86  ? 2495 VAL A CG2   1 
ATOM   6705  N N     . TYR A 1 2496 ? 133.106 189.603 191.502 1.00 74.94  ? 2496 TYR A N     1 
ATOM   6706  C CA    . TYR A 1 2496 ? 132.760 188.990 190.224 1.00 74.94  ? 2496 TYR A CA    1 
ATOM   6707  C C     . TYR A 1 2496 ? 133.915 189.090 189.236 1.00 74.94  ? 2496 TYR A C     1 
ATOM   6708  O O     . TYR A 1 2496 ? 134.140 188.179 188.429 1.00 74.94  ? 2496 TYR A O     1 
ATOM   6709  C CB    . TYR A 1 2496 ? 131.493 189.660 189.694 1.00 74.94  ? 2496 TYR A CB    1 
ATOM   6710  C CG    . TYR A 1 2496 ? 131.339 189.754 188.199 1.00 74.94  ? 2496 TYR A CG    1 
ATOM   6711  C CD1   . TYR A 1 2496 ? 130.762 188.729 187.475 1.00 74.94  ? 2496 TYR A CD1   1 
ATOM   6712  C CD2   . TYR A 1 2496 ? 131.722 190.898 187.519 1.00 74.94  ? 2496 TYR A CD2   1 
ATOM   6713  C CE1   . TYR A 1 2496 ? 130.596 188.830 186.111 1.00 74.94  ? 2496 TYR A CE1   1 
ATOM   6714  C CE2   . TYR A 1 2496 ? 131.564 191.005 186.156 1.00 74.94  ? 2496 TYR A CE2   1 
ATOM   6715  C CZ    . TYR A 1 2496 ? 131.003 189.967 185.458 1.00 74.94  ? 2496 TYR A CZ    1 
ATOM   6716  O OH    . TYR A 1 2496 ? 130.843 190.069 184.098 1.00 74.94  ? 2496 TYR A OH    1 
ATOM   6717  N N     . ALA A 1 2497 ? 134.690 190.168 189.322 1.00 74.56  ? 2497 ALA A N     1 
ATOM   6718  C CA    . ALA A 1 2497 ? 135.804 190.371 188.411 1.00 74.56  ? 2497 ALA A CA    1 
ATOM   6719  C C     . ALA A 1 2497 ? 136.957 189.440 188.734 1.00 74.56  ? 2497 ALA A C     1 
ATOM   6720  O O     . ALA A 1 2497 ? 137.565 188.861 187.829 1.00 74.56  ? 2497 ALA A O     1 
ATOM   6721  C CB    . ALA A 1 2497 ? 136.261 191.826 188.465 1.00 74.56  ? 2497 ALA A CB    1 
ATOM   6722  N N     . ILE A 1 2498 ? 137.275 189.289 190.018 1.00 75.22  ? 2498 ILE A N     1 
ATOM   6723  C CA    . ILE A 1 2498 ? 138.279 188.308 190.411 1.00 75.22  ? 2498 ILE A CA    1 
ATOM   6724  C C     . ILE A 1 2498 ? 137.841 186.915 189.990 1.00 75.22  ? 2498 ILE A C     1 
ATOM   6725  O O     . ILE A 1 2498 ? 138.653 186.103 189.534 1.00 75.22  ? 2498 ILE A O     1 
ATOM   6726  C CB    . ILE A 1 2498 ? 138.545 188.386 191.923 1.00 75.22  ? 2498 ILE A CB    1 
ATOM   6727  C CG1   . ILE A 1 2498 ? 138.989 189.794 192.309 1.00 75.22  ? 2498 ILE A CG1   1 
ATOM   6728  C CG2   . ILE A 1 2498 ? 139.585 187.369 192.329 1.00 75.22  ? 2498 ILE A CG2   1 
ATOM   6729  C CD1   . ILE A 1 2498 ? 138.982 190.049 193.799 1.00 75.22  ? 2498 ILE A CD1   1 
ATOM   6730  N N     . LEU A 1 2499 ? 136.546 186.622 190.122 1.00 77.10  ? 2499 LEU A N     1 
ATOM   6731  C CA    . LEU A 1 2499 ? 136.048 185.306 189.741 1.00 77.10  ? 2499 LEU A CA    1 
ATOM   6732  C C     . LEU A 1 2499 ? 136.198 185.055 188.246 1.00 77.10  ? 2499 LEU A C     1 
ATOM   6733  O O     . LEU A 1 2499 ? 136.586 183.956 187.836 1.00 77.10  ? 2499 LEU A O     1 
ATOM   6734  C CB    . LEU A 1 2499 ? 134.588 185.162 190.154 1.00 77.10  ? 2499 LEU A CB    1 
ATOM   6735  C CG    . LEU A 1 2499 ? 134.015 183.765 189.940 1.00 77.10  ? 2499 LEU A CG    1 
ATOM   6736  C CD1   . LEU A 1 2499 ? 134.988 182.717 190.448 1.00 77.10  ? 2499 LEU A CD1   1 
ATOM   6737  C CD2   . LEU A 1 2499 ? 132.662 183.629 190.613 1.00 77.10  ? 2499 LEU A CD2   1 
ATOM   6738  N N     . TRP A 1 2500 ? 135.883 186.047 187.412 1.00 77.96  ? 2500 TRP A N     1 
ATOM   6739  C CA    . TRP A 1 2500 ? 135.918 185.818 185.972 1.00 77.96  ? 2500 TRP A CA    1 
ATOM   6740  C C     . TRP A 1 2500 ? 137.303 185.991 185.365 1.00 77.96  ? 2500 TRP A C     1 
ATOM   6741  O O     . TRP A 1 2500 ? 137.550 185.471 184.272 1.00 77.96  ? 2500 TRP A O     1 
ATOM   6742  C CB    . TRP A 1 2500 ? 134.938 186.743 185.252 1.00 77.96  ? 2500 TRP A CB    1 
ATOM   6743  C CG    . TRP A 1 2500 ? 133.680 186.061 184.804 1.00 77.96  ? 2500 TRP A CG    1 
ATOM   6744  C CD1   . TRP A 1 2500 ? 132.408 186.471 185.040 1.00 77.96  ? 2500 TRP A CD1   1 
ATOM   6745  C CD2   . TRP A 1 2500 ? 133.575 184.857 184.035 1.00 77.96  ? 2500 TRP A CD2   1 
ATOM   6746  N NE1   . TRP A 1 2500 ? 131.514 185.601 184.475 1.00 77.96  ? 2500 TRP A NE1   1 
ATOM   6747  C CE2   . TRP A 1 2500 ? 132.206 184.602 183.848 1.00 77.96  ? 2500 TRP A CE2   1 
ATOM   6748  C CE3   . TRP A 1 2500 ? 134.504 183.973 183.484 1.00 77.96  ? 2500 TRP A CE3   1 
ATOM   6749  C CZ2   . TRP A 1 2500 ? 131.743 183.499 183.143 1.00 77.96  ? 2500 TRP A CZ2   1 
ATOM   6750  C CZ3   . TRP A 1 2500 ? 134.041 182.878 182.785 1.00 77.96  ? 2500 TRP A CZ3   1 
ATOM   6751  C CH2   . TRP A 1 2500 ? 132.675 182.651 182.619 1.00 77.96  ? 2500 TRP A CH2   1 
ATOM   6752  N N     . SER A 1 2501 ? 138.208 186.705 186.031 1.00 75.95  ? 2501 SER A N     1 
ATOM   6753  C CA    . SER A 1 2501 ? 139.572 186.868 185.543 1.00 75.95  ? 2501 SER A CA    1 
ATOM   6754  C C     . SER A 1 2501 ? 140.469 185.737 186.027 1.00 75.95  ? 2501 SER A C     1 
ATOM   6755  O O     . SER A 1 2501 ? 141.044 185.001 185.222 1.00 75.95  ? 2501 SER A O     1 
ATOM   6756  C CB    . SER A 1 2501 ? 140.138 188.219 185.991 1.00 75.95  ? 2501 SER A CB    1 
ATOM   6757  O OG    . SER A 1 2501 ? 139.330 189.285 185.534 1.00 75.95  ? 2501 SER A OG    1 
ATOM   6758  N N     . LEU A 1 2502 ? 140.600 185.593 187.338 1.00 73.70  ? 2502 LEU A N     1 
ATOM   6759  C CA    . LEU A 1 2502 ? 141.275 184.435 187.898 1.00 73.70  ? 2502 LEU A CA    1 
ATOM   6760  C C     . LEU A 1 2502 ? 140.393 183.212 187.711 1.00 73.70  ? 2502 LEU A C     1 
ATOM   6761  O O     . LEU A 1 2502 ? 139.189 183.260 187.974 1.00 73.70  ? 2502 LEU A O     1 
ATOM   6762  C CB    . LEU A 1 2502 ? 141.564 184.657 189.377 1.00 73.70  ? 2502 LEU A CB    1 
ATOM   6763  C CG    . LEU A 1 2502 ? 142.624 185.686 189.751 1.00 73.70  ? 2502 LEU A CG    1 
ATOM   6764  C CD1   . LEU A 1 2502 ? 142.077 187.095 189.668 1.00 73.70  ? 2502 LEU A CD1   1 
ATOM   6765  C CD2   . LEU A 1 2502 ? 143.104 185.404 191.142 1.00 73.70  ? 2502 LEU A CD2   1 
ATOM   6766  N N     . SER A 1 2503 ? 140.983 182.125 187.232 1.00 82.90  ? 2503 SER A N     1 
ATOM   6767  C CA    . SER A 1 2503 ? 140.279 180.880 186.948 1.00 82.90  ? 2503 SER A CA    1 
ATOM   6768  C C     . SER A 1 2503 ? 139.201 181.038 185.886 1.00 82.90  ? 2503 SER A C     1 
ATOM   6769  O O     . SER A 1 2503 ? 138.444 180.094 185.638 1.00 82.90  ? 2503 SER A O     1 
ATOM   6770  C CB    . SER A 1 2503 ? 139.658 180.280 188.211 1.00 82.90  ? 2503 SER A CB    1 
ATOM   6771  O OG    . SER A 1 2503 ? 138.288 180.629 188.292 1.00 82.90  ? 2503 SER A OG    1 
ATOM   6772  N N     . GLY A 1 2504 ? 139.107 182.202 185.247 1.00 76.20  ? 2504 GLY A N     1 
ATOM   6773  C CA    . GLY A 1 2504 ? 138.189 182.349 184.135 1.00 76.20  ? 2504 GLY A CA    1 
ATOM   6774  C C     . GLY A 1 2504 ? 138.560 181.530 182.922 1.00 76.20  ? 2504 GLY A C     1 
ATOM   6775  O O     . GLY A 1 2504 ? 137.753 181.421 181.994 1.00 76.20  ? 2504 GLY A O     1 
ATOM   6776  N N     . ASP A 1 2505 ? 139.759 180.958 182.910 1.00 77.24  ? 2505 ASP A N     1 
ATOM   6777  C CA    . ASP A 1 2505 ? 140.225 180.108 181.828 1.00 77.24  ? 2505 ASP A CA    1 
ATOM   6778  C C     . ASP A 1 2505 ? 140.361 178.657 182.272 1.00 77.24  ? 2505 ASP A C     1 
ATOM   6779  O O     . ASP A 1 2505 ? 141.187 177.915 181.739 1.00 77.24  ? 2505 ASP A O     1 
ATOM   6780  C CB    . ASP A 1 2505 ? 141.555 180.626 181.294 1.00 77.24  ? 2505 ASP A CB    1 
ATOM   6781  C CG    . ASP A 1 2505 ? 142.463 181.127 182.398 1.00 77.24  ? 2505 ASP A CG    1 
ATOM   6782  O OD1   . ASP A 1 2505 ? 142.645 180.396 183.393 1.00 77.24  ? 2505 ASP A OD1   1 
ATOM   6783  O OD2   . ASP A 1 2505 ? 142.993 182.250 182.275 1.00 77.24  ? 2505 ASP A OD2   1 
ATOM   6784  N N     . SER A 1 2506 ? 139.566 178.240 183.250 1.00 81.67  ? 2506 SER A N     1 
ATOM   6785  C CA    . SER A 1 2506 ? 139.627 176.886 183.777 1.00 81.67  ? 2506 SER A CA    1 
ATOM   6786  C C     . SER A 1 2506 ? 138.258 176.226 183.690 1.00 81.67  ? 2506 SER A C     1 
ATOM   6787  O O     . SER A 1 2506 ? 137.257 176.851 183.331 1.00 81.67  ? 2506 SER A O     1 
ATOM   6788  C CB    . SER A 1 2506 ? 140.122 176.880 185.226 1.00 81.67  ? 2506 SER A CB    1 
ATOM   6789  O OG    . SER A 1 2506 ? 139.119 177.361 186.100 1.00 81.67  ? 2506 SER A OG    1 
ATOM   6790  N N     . ARG A 1 2507 ? 138.228 174.943 184.036 1.00 86.24  ? 2507 ARG A N     1 
ATOM   6791  C CA    . ARG A 1 2507 ? 137.005 174.164 183.975 1.00 86.24  ? 2507 ARG A CA    1 
ATOM   6792  C C     . ARG A 1 2507 ? 135.995 174.680 184.996 1.00 86.24  ? 2507 ARG A C     1 
ATOM   6793  O O     . ARG A 1 2507 ? 136.305 175.503 185.861 1.00 86.24  ? 2507 ARG A O     1 
ATOM   6794  C CB    . ARG A 1 2507 ? 137.306 172.688 184.224 1.00 86.24  ? 2507 ARG A CB    1 
ATOM   6795  C CG    . ARG A 1 2507 ? 136.329 171.721 183.583 1.00 86.24  ? 2507 ARG A CG    1 
ATOM   6796  C CD    . ARG A 1 2507 ? 136.991 170.384 183.289 1.00 86.24  ? 2507 ARG A CD    1 
ATOM   6797  N NE    . ARG A 1 2507 ? 138.125 170.524 182.383 1.00 86.24  ? 2507 ARG A NE    1 
ATOM   6798  C CZ    . ARG A 1 2507 ? 139.394 170.552 182.765 1.00 86.24  ? 2507 ARG A CZ    1 
ATOM   6799  N NH1   . ARG A 1 2507 ? 139.734 170.445 184.039 1.00 86.24  ? 2507 ARG A NH1   1 
ATOM   6800  N NH2   . ARG A 1 2507 ? 140.346 170.695 181.848 1.00 86.24  ? 2507 ARG A NH2   1 
ATOM   6801  N N     . LEU A 1 2508 ? 134.763 174.182 184.883 1.00 88.47  ? 2508 LEU A N     1 
ATOM   6802  C CA    . LEU A 1 2508 ? 133.703 174.630 185.779 1.00 88.47  ? 2508 LEU A CA    1 
ATOM   6803  C C     . LEU A 1 2508 ? 134.011 174.278 187.228 1.00 88.47  ? 2508 LEU A C     1 
ATOM   6804  O O     . LEU A 1 2508 ? 133.799 175.095 188.131 1.00 88.47  ? 2508 LEU A O     1 
ATOM   6805  C CB    . LEU A 1 2508 ? 132.368 174.023 185.358 1.00 88.47  ? 2508 LEU A CB    1 
ATOM   6806  C CG    . LEU A 1 2508 ? 131.220 174.285 186.331 1.00 88.47  ? 2508 LEU A CG    1 
ATOM   6807  C CD1   . LEU A 1 2508 ? 130.873 175.765 186.346 1.00 88.47  ? 2508 LEU A CD1   1 
ATOM   6808  C CD2   . LEU A 1 2508 ? 130.005 173.443 185.976 1.00 88.47  ? 2508 LEU A CD2   1 
ATOM   6809  N N     . LYS A 1 2509 ? 134.512 173.066 187.474 1.00 91.03  ? 2509 LYS A N     1 
ATOM   6810  C CA    . LYS A 1 2509 ? 134.786 172.660 188.849 1.00 91.03  ? 2509 LYS A CA    1 
ATOM   6811  C C     . LYS A 1 2509 ? 135.938 173.462 189.442 1.00 91.03  ? 2509 LYS A C     1 
ATOM   6812  O O     . LYS A 1 2509 ? 135.939 173.765 190.640 1.00 91.03  ? 2509 LYS A O     1 
ATOM   6813  C CB    . LYS A 1 2509 ? 135.064 171.156 188.910 1.00 91.03  ? 2509 LYS A CB    1 
ATOM   6814  C CG    . LYS A 1 2509 ? 136.520 170.755 188.784 1.00 91.03  ? 2509 LYS A CG    1 
ATOM   6815  C CD    . LYS A 1 2509 ? 136.664 169.460 188.008 1.00 91.03  ? 2509 LYS A CD    1 
ATOM   6816  C CE    . LYS A 1 2509 ? 138.121 169.053 187.881 1.00 91.03  ? 2509 LYS A CE    1 
ATOM   6817  N NZ    . LYS A 1 2509 ? 138.884 169.989 187.012 1.00 91.03  ? 2509 LYS A NZ    1 
ATOM   6818  N N     . MET A 1 2510 ? 136.918 173.836 188.617 1.00 90.81  ? 2510 MET A N     1 
ATOM   6819  C CA    . MET A 1 2510 ? 138.000 174.680 189.108 1.00 90.81  ? 2510 MET A CA    1 
ATOM   6820  C C     . MET A 1 2510 ? 137.477 176.062 189.477 1.00 90.81  ? 2510 MET A C     1 
ATOM   6821  O O     . MET A 1 2510 ? 137.877 176.639 190.496 1.00 90.81  ? 2510 MET A O     1 
ATOM   6822  C CB    . MET A 1 2510 ? 139.101 174.776 188.056 1.00 90.81  ? 2510 MET A CB    1 
ATOM   6823  C CG    . MET A 1 2510 ? 139.582 173.423 187.560 1.00 90.81  ? 2510 MET A CG    1 
ATOM   6824  S SD    . MET A 1 2510 ? 139.807 172.199 188.863 1.00 90.81  ? 2510 MET A SD    1 
ATOM   6825  C CE    . MET A 1 2510 ? 141.590 172.153 188.990 1.00 90.81  ? 2510 MET A CE    1 
ATOM   6826  N N     . ARG A 1 2511 ? 136.569 176.603 188.661 1.00 86.95  ? 2511 ARG A N     1 
ATOM   6827  C CA    . ARG A 1 2511 ? 135.938 177.872 188.997 1.00 86.95  ? 2511 ARG A CA    1 
ATOM   6828  C C     . ARG A 1 2511 ? 135.148 177.761 190.291 1.00 86.95  ? 2511 ARG A C     1 
ATOM   6829  O O     . ARG A 1 2511 ? 135.146 178.688 191.106 1.00 86.95  ? 2511 ARG A O     1 
ATOM   6830  C CB    . ARG A 1 2511 ? 135.026 178.328 187.862 1.00 86.95  ? 2511 ARG A CB    1 
ATOM   6831  C CG    . ARG A 1 2511 ? 135.751 178.719 186.599 1.00 86.95  ? 2511 ARG A CG    1 
ATOM   6832  C CD    . ARG A 1 2511 ? 134.784 179.276 185.576 1.00 86.95  ? 2511 ARG A CD    1 
ATOM   6833  N NE    . ARG A 1 2511 ? 135.331 179.219 184.228 1.00 86.95  ? 2511 ARG A NE    1 
ATOM   6834  C CZ    . ARG A 1 2511 ? 134.611 179.358 183.124 1.00 86.95  ? 2511 ARG A CZ    1 
ATOM   6835  N NH1   . ARG A 1 2511 ? 133.308 179.573 183.173 1.00 86.95  ? 2511 ARG A NH1   1 
ATOM   6836  N NH2   . ARG A 1 2511 ? 135.212 179.275 181.942 1.00 86.95  ? 2511 ARG A NH2   1 
ATOM   6837  N N     . ALA A 1 2512 ? 134.456 176.639 190.490 1.00 96.75  ? 2512 ALA A N     1 
ATOM   6838  C CA    . ALA A 1 2512 ? 133.713 176.448 191.730 1.00 96.75  ? 2512 ALA A CA    1 
ATOM   6839  C C     . ALA A 1 2512 ? 134.651 176.403 192.929 1.00 96.75  ? 2512 ALA A C     1 
ATOM   6840  O O     . ALA A 1 2512 ? 134.356 176.983 193.982 1.00 96.75  ? 2512 ALA A O     1 
ATOM   6841  C CB    . ALA A 1 2512 ? 132.878 175.171 191.650 1.00 96.75  ? 2512 ALA A CB    1 
ATOM   6842  N N     . GLU A 1 2513 ? 135.786 175.719 192.788 1.00 94.33  ? 2513 GLU A N     1 
ATOM   6843  C CA    . GLU A 1 2513 ? 136.770 175.684 193.865 1.00 94.33  ? 2513 GLU A CA    1 
ATOM   6844  C C     . GLU A 1 2513 ? 137.273 177.085 194.184 1.00 94.33  ? 2513 GLU A C     1 
ATOM   6845  O O     . GLU A 1 2513 ? 137.368 177.477 195.356 1.00 94.33  ? 2513 GLU A O     1 
ATOM   6846  C CB    . GLU A 1 2513 ? 137.931 174.770 193.480 1.00 94.33  ? 2513 GLU A CB    1 
ATOM   6847  C CG    . GLU A 1 2513 ? 139.037 174.705 194.514 1.00 94.33  ? 2513 GLU A CG    1 
ATOM   6848  C CD    . GLU A 1 2513 ? 140.153 173.764 194.112 1.00 94.33  ? 2513 GLU A CD    1 
ATOM   6849  O OE1   . GLU A 1 2513 ? 139.914 172.887 193.256 1.00 94.33  ? 2513 GLU A OE1   1 
ATOM   6850  O OE2   . GLU A 1 2513 ? 141.273 173.904 194.647 1.00 94.33  ? 2513 GLU A OE2   1 
ATOM   6851  N N     . LEU A 1 2514 ? 137.588 177.861 193.147 1.00 86.94  ? 2514 LEU A N     1 
ATOM   6852  C CA    . LEU A 1 2514 ? 138.051 179.224 193.378 1.00 86.94  ? 2514 LEU A CA    1 
ATOM   6853  C C     . LEU A 1 2514 ? 136.979 180.060 194.058 1.00 86.94  ? 2514 LEU A C     1 
ATOM   6854  O O     . LEU A 1 2514 ? 137.275 180.830 194.976 1.00 86.94  ? 2514 LEU A O     1 
ATOM   6855  C CB    . LEU A 1 2514 ? 138.473 179.878 192.068 1.00 86.94  ? 2514 LEU A CB    1 
ATOM   6856  C CG    . LEU A 1 2514 ? 139.099 181.252 192.298 1.00 86.94  ? 2514 LEU A CG    1 
ATOM   6857  C CD1   . LEU A 1 2514 ? 140.601 181.125 192.449 1.00 86.94  ? 2514 LEU A CD1   1 
ATOM   6858  C CD2   . LEU A 1 2514 ? 138.741 182.212 191.182 1.00 86.94  ? 2514 LEU A CD2   1 
ATOM   6859  N N     . GLY A 1 2515 ? 135.730 179.925 193.616 1.00 94.59  ? 2515 GLY A N     1 
ATOM   6860  C CA    . GLY A 1 2515 ? 134.654 180.677 194.235 1.00 94.59  ? 2515 GLY A CA    1 
ATOM   6861  C C     . GLY A 1 2515 ? 134.473 180.323 195.695 1.00 94.59  ? 2515 GLY A C     1 
ATOM   6862  O O     . GLY A 1 2515 ? 134.211 181.192 196.529 1.00 94.59  ? 2515 GLY A O     1 
ATOM   6863  N N     . GLU A 1 2516 ? 134.618 179.039 196.026 1.00 97.07  ? 2516 GLU A N     1 
ATOM   6864  C CA    . GLU A 1 2516 ? 134.557 178.632 197.425 1.00 97.07  ? 2516 GLU A CA    1 
ATOM   6865  C C     . GLU A 1 2516 ? 135.692 179.259 198.223 1.00 97.07  ? 2516 GLU A C     1 
ATOM   6866  O O     . GLU A 1 2516 ? 135.493 179.704 199.361 1.00 97.07  ? 2516 GLU A O     1 
ATOM   6867  C CB    . GLU A 1 2516 ? 134.597 177.110 197.530 1.00 97.07  ? 2516 GLU A CB    1 
ATOM   6868  C CG    . GLU A 1 2516 ? 133.875 176.571 198.745 1.00 97.07  ? 2516 GLU A CG    1 
ATOM   6869  C CD    . GLU A 1 2516 ? 132.588 177.318 199.023 1.00 97.07  ? 2516 GLU A CD    1 
ATOM   6870  O OE1   . GLU A 1 2516 ? 131.664 177.244 198.187 1.00 97.07  ? 2516 GLU A OE1   1 
ATOM   6871  O OE2   . GLU A 1 2516 ? 132.501 177.984 200.076 1.00 97.07  ? 2516 GLU A OE2   1 
ATOM   6872  N N     . TYR A 1 2517 ? 136.892 179.306 197.640 1.00 92.23  ? 2517 TYR A N     1 
ATOM   6873  C CA    . TYR A 1 2517 ? 138.013 179.946 198.324 1.00 92.23  ? 2517 TYR A CA    1 
ATOM   6874  C C     . TYR A 1 2517 ? 137.728 181.421 198.585 1.00 92.23  ? 2517 TYR A C     1 
ATOM   6875  O O     . TYR A 1 2517 ? 137.970 181.924 199.691 1.00 92.23  ? 2517 TYR A O     1 
ATOM   6876  C CB    . TYR A 1 2517 ? 139.287 179.783 197.498 1.00 92.23  ? 2517 TYR A CB    1 
ATOM   6877  C CG    . TYR A 1 2517 ? 140.508 180.471 198.070 1.00 92.23  ? 2517 TYR A CG    1 
ATOM   6878  C CD1   . TYR A 1 2517 ? 141.343 179.812 198.959 1.00 92.23  ? 2517 TYR A CD1   1 
ATOM   6879  C CD2   . TYR A 1 2517 ? 140.831 181.772 197.715 1.00 92.23  ? 2517 TYR A CD2   1 
ATOM   6880  C CE1   . TYR A 1 2517 ? 142.463 180.428 199.480 1.00 92.23  ? 2517 TYR A CE1   1 
ATOM   6881  C CE2   . TYR A 1 2517 ? 141.945 182.399 198.235 1.00 92.23  ? 2517 TYR A CE2   1 
ATOM   6882  C CZ    . TYR A 1 2517 ? 142.758 181.722 199.116 1.00 92.23  ? 2517 TYR A CZ    1 
ATOM   6883  O OH    . TYR A 1 2517 ? 143.872 182.340 199.634 1.00 92.23  ? 2517 TYR A OH    1 
ATOM   6884  N N     . ILE A 1 2518 ? 137.207 182.129 197.579 1.00 92.84  ? 2518 ILE A N     1 
ATOM   6885  C CA    . ILE A 1 2518 ? 136.880 183.543 197.763 1.00 92.84  ? 2518 ILE A CA    1 
ATOM   6886  C C     . ILE A 1 2518 ? 135.822 183.706 198.841 1.00 92.84  ? 2518 ILE A C     1 
ATOM   6887  O O     . ILE A 1 2518 ? 135.925 184.589 199.700 1.00 92.84  ? 2518 ILE A O     1 
ATOM   6888  C CB    . ILE A 1 2518 ? 136.436 184.201 196.441 1.00 92.84  ? 2518 ILE A CB    1 
ATOM   6889  C CG1   . ILE A 1 2518 ? 137.287 183.752 195.256 1.00 92.84  ? 2518 ILE A CG1   1 
ATOM   6890  C CG2   . ILE A 1 2518 ? 136.478 185.711 196.562 1.00 92.84  ? 2518 ILE A CG2   1 
ATOM   6891  C CD1   . ILE A 1 2518 ? 138.781 183.816 195.494 1.00 92.84  ? 2518 ILE A CD1   1 
ATOM   6892  N N     . ARG A 1 2519 ? 134.793 182.858 198.819 1.00 98.91  ? 2519 ARG A N     1 
ATOM   6893  C CA    . ARG A 1 2519 ? 133.756 182.933 199.841 1.00 98.91  ? 2519 ARG A CA    1 
ATOM   6894  C C     . ARG A 1 2519 ? 134.348 182.737 201.229 1.00 98.91  ? 2519 ARG A C     1 
ATOM   6895  O O     . ARG A 1 2519 ? 133.939 183.401 202.189 1.00 98.91  ? 2519 ARG A O     1 
ATOM   6896  C CB    . ARG A 1 2519 ? 132.672 181.894 199.561 1.00 98.91  ? 2519 ARG A CB    1 
ATOM   6897  C CG    . ARG A 1 2519 ? 131.717 181.659 200.716 1.00 98.91  ? 2519 ARG A CG    1 
ATOM   6898  C CD    . ARG A 1 2519 ? 130.622 180.681 200.331 1.00 98.91  ? 2519 ARG A CD    1 
ATOM   6899  N NE    . ARG A 1 2519 ? 129.953 181.075 199.097 1.00 98.91  ? 2519 ARG A NE    1 
ATOM   6900  C CZ    . ARG A 1 2519 ? 128.761 181.653 199.046 1.00 98.91  ? 2519 ARG A CZ    1 
ATOM   6901  N NH1   . ARG A 1 2519 ? 128.077 181.924 200.144 1.00 98.91  ? 2519 ARG A NH1   1 
ATOM   6902  N NH2   . ARG A 1 2519 ? 128.244 181.970 197.862 1.00 98.91  ? 2519 ARG A NH2   1 
ATOM   6903  N N     . ARG A 1 2520 ? 135.321 181.835 201.350 1.00 96.15  ? 2520 ARG A N     1 
ATOM   6904  C CA    . ARG A 1 2520 ? 135.986 181.636 202.632 1.00 96.15  ? 2520 ARG A CA    1 
ATOM   6905  C C     . ARG A 1 2520 ? 136.766 182.874 203.057 1.00 96.15  ? 2520 ARG A C     1 
ATOM   6906  O O     . ARG A 1 2520 ? 136.747 183.252 204.234 1.00 96.15  ? 2520 ARG A O     1 
ATOM   6907  C CB    . ARG A 1 2520 ? 136.912 180.424 202.558 1.00 96.15  ? 2520 ARG A CB    1 
ATOM   6908  C CG    . ARG A 1 2520 ? 136.188 179.093 202.541 1.00 96.15  ? 2520 ARG A CG    1 
ATOM   6909  C CD    . ARG A 1 2520 ? 137.092 177.975 203.027 1.00 96.15  ? 2520 ARG A CD    1 
ATOM   6910  N NE    . ARG A 1 2520 ? 138.248 177.788 202.159 1.00 96.15  ? 2520 ARG A NE    1 
ATOM   6911  C CZ    . ARG A 1 2520 ? 139.481 178.171 202.461 1.00 96.15  ? 2520 ARG A CZ    1 
ATOM   6912  N NH1   . ARG A 1 2520 ? 139.752 178.795 203.595 1.00 96.15  ? 2520 ARG A NH1   1 
ATOM   6913  N NH2   . ARG A 1 2520 ? 140.465 177.926 201.601 1.00 96.15  ? 2520 ARG A NH2   1 
ATOM   6914  N N     . ILE A 1 2521 ? 137.455 183.523 202.120 1.00 96.15  ? 2521 ILE A N     1 
ATOM   6915  C CA    . ILE A 1 2521 ? 138.399 184.568 202.509 1.00 96.15  ? 2521 ILE A CA    1 
ATOM   6916  C C     . ILE A 1 2521 ? 137.794 185.973 202.500 1.00 96.15  ? 2521 ILE A C     1 
ATOM   6917  O O     . ILE A 1 2521 ? 138.271 186.848 203.230 1.00 96.15  ? 2521 ILE A O     1 
ATOM   6918  C CB    . ILE A 1 2521 ? 139.652 184.514 201.619 1.00 96.15  ? 2521 ILE A CB    1 
ATOM   6919  C CG1   . ILE A 1 2521 ? 139.318 184.942 200.191 1.00 96.15  ? 2521 ILE A CG1   1 
ATOM   6920  C CG2   . ILE A 1 2521 ? 140.261 183.123 201.635 1.00 96.15  ? 2521 ILE A CG2   1 
ATOM   6921  C CD1   . ILE A 1 2521 ? 140.520 185.398 199.406 1.00 96.15  ? 2521 ILE A CD1   1 
ATOM   6922  N N     . THR A 1 2522 ? 136.766 186.224 201.696 1.00 98.76  ? 2522 THR A N     1 
ATOM   6923  C CA    . THR A 1 2522 ? 136.258 187.582 201.579 1.00 98.76  ? 2522 THR A CA    1 
ATOM   6924  C C     . THR A 1 2522 ? 135.317 187.920 202.730 1.00 98.76  ? 2522 THR A C     1 
ATOM   6925  O O     . THR A 1 2522 ? 134.899 187.060 203.510 1.00 98.76  ? 2522 THR A O     1 
ATOM   6926  C CB    . THR A 1 2522 ? 135.527 187.786 200.257 1.00 98.76  ? 2522 THR A CB    1 
ATOM   6927  O OG1   . THR A 1 2522 ? 135.354 189.188 200.027 1.00 98.76  ? 2522 THR A OG1   1 
ATOM   6928  C CG2   . THR A 1 2522 ? 134.159 187.136 200.309 1.00 98.76  ? 2522 THR A CG2   1 
ATOM   6929  N N     . THR A 1 2523 ? 134.984 189.208 202.826 1.00 103.66 ? 2523 THR A N     1 
ATOM   6930  C CA    . THR A 1 2523 ? 134.027 189.701 203.802 1.00 103.66 ? 2523 THR A CA    1 
ATOM   6931  C C     . THR A 1 2523 ? 132.767 190.277 203.175 1.00 103.66 ? 2523 THR A C     1 
ATOM   6932  O O     . THR A 1 2523 ? 131.785 190.495 203.892 1.00 103.66 ? 2523 THR A O     1 
ATOM   6933  C CB    . THR A 1 2523 ? 134.666 190.781 204.688 1.00 103.66 ? 2523 THR A CB    1 
ATOM   6934  O OG1   . THR A 1 2523 ? 134.515 192.060 204.063 1.00 103.66 ? 2523 THR A OG1   1 
ATOM   6935  C CG2   . THR A 1 2523 ? 136.145 190.499 204.891 1.00 103.66 ? 2523 THR A CG2   1 
ATOM   6936  N N     . VAL A 1 2524 ? 132.767 190.529 201.872 1.00 100.68 ? 2524 VAL A N     1 
ATOM   6937  C CA    . VAL A 1 2524 ? 131.642 191.150 201.178 1.00 100.68 ? 2524 VAL A CA    1 
ATOM   6938  C C     . VAL A 1 2524 ? 130.481 190.161 201.132 1.00 100.68 ? 2524 VAL A C     1 
ATOM   6939  O O     . VAL A 1 2524 ? 130.707 188.943 201.189 1.00 100.68 ? 2524 VAL A O     1 
ATOM   6940  C CB    . VAL A 1 2524 ? 132.066 191.597 199.768 1.00 100.68 ? 2524 VAL A CB    1 
ATOM   6941  C CG1   . VAL A 1 2524 ? 132.080 190.415 198.825 1.00 100.68 ? 2524 VAL A CG1   1 
ATOM   6942  C CG2   . VAL A 1 2524 ? 131.178 192.712 199.243 1.00 100.68 ? 2524 VAL A CG2   1 
ATOM   6943  N N     . PRO A 1 2525 ? 129.232 190.625 201.068 1.00 101.09 ? 2525 PRO A N     1 
ATOM   6944  C CA    . PRO A 1 2525 ? 128.116 189.698 200.855 1.00 101.09 ? 2525 PRO A CA    1 
ATOM   6945  C C     . PRO A 1 2525 ? 128.236 188.967 199.527 1.00 101.09 ? 2525 PRO A C     1 
ATOM   6946  O O     . PRO A 1 2525 ? 128.785 189.483 198.553 1.00 101.09 ? 2525 PRO A O     1 
ATOM   6947  C CB    . PRO A 1 2525 ? 126.888 190.611 200.877 1.00 101.09 ? 2525 PRO A CB    1 
ATOM   6948  C CG    . PRO A 1 2525 ? 127.292 191.739 201.746 1.00 101.09 ? 2525 PRO A CG    1 
ATOM   6949  C CD    . PRO A 1 2525 ? 128.763 191.949 201.513 1.00 101.09 ? 2525 PRO A CD    1 
ATOM   6950  N N     . LEU A 1 2526 ? 127.713 187.751 199.503 1.00 102.09 ? 2526 LEU A N     1 
ATOM   6951  C CA    . LEU A 1 2526 ? 127.765 186.855 198.360 1.00 102.09 ? 2526 LEU A CA    1 
ATOM   6952  C C     . LEU A 1 2526 ? 126.386 186.268 198.113 1.00 102.09 ? 2526 LEU A C     1 
ATOM   6953  O O     . LEU A 1 2526 ? 125.515 186.325 198.988 1.00 102.09 ? 2526 LEU A O     1 
ATOM   6954  C CB    . LEU A 1 2526 ? 128.781 185.729 198.595 1.00 102.09 ? 2526 LEU A CB    1 
ATOM   6955  C CG    . LEU A 1 2526 ? 130.227 186.110 198.297 1.00 102.09 ? 2526 LEU A CG    1 
ATOM   6956  C CD1   . LEU A 1 2526 ? 131.162 185.313 199.176 1.00 102.09 ? 2526 LEU A CD1   1 
ATOM   6957  C CD2   . LEU A 1 2526 ? 130.541 185.881 196.831 1.00 102.09 ? 2526 LEU A CD2   1 
ATOM   6958  N N     . PRO A 1 2527 ? 126.142 185.715 196.911 1.00 104.01 ? 2527 PRO A N     1 
ATOM   6959  C CA    . PRO A 1 2527 ? 124.850 185.066 196.649 1.00 104.01 ? 2527 PRO A CA    1 
ATOM   6960  C C     . PRO A 1 2527 ? 124.498 184.028 197.701 1.00 104.01 ? 2527 PRO A C     1 
ATOM   6961  O O     . PRO A 1 2527 ? 125.264 183.093 197.952 1.00 104.01 ? 2527 PRO A O     1 
ATOM   6962  C CB    . PRO A 1 2527 ? 125.054 184.425 195.272 1.00 104.01 ? 2527 PRO A CB    1 
ATOM   6963  C CG    . PRO A 1 2527 ? 126.065 185.283 194.616 1.00 104.01 ? 2527 PRO A CG    1 
ATOM   6964  C CD    . PRO A 1 2527 ? 126.986 185.762 195.704 1.00 104.01 ? 2527 PRO A CD    1 
ATOM   6965  N N     . THR A 1 2528 ? 123.331 184.196 198.323 1.00 114.85 ? 2528 THR A N     1 
ATOM   6966  C CA    . THR A 1 2528 ? 122.959 183.358 199.454 1.00 114.85 ? 2528 THR A CA    1 
ATOM   6967  C C     . THR A 1 2528 ? 122.526 181.960 199.036 1.00 114.85 ? 2528 THR A C     1 
ATOM   6968  O O     . THR A 1 2528 ? 122.500 181.059 199.880 1.00 114.85 ? 2528 THR A O     1 
ATOM   6969  C CB    . THR A 1 2528 ? 121.842 184.027 200.253 1.00 114.85 ? 2528 THR A CB    1 
ATOM   6970  O OG1   . THR A 1 2528 ? 120.947 184.692 199.353 1.00 114.85 ? 2528 THR A OG1   1 
ATOM   6971  C CG2   . THR A 1 2528 ? 122.422 185.044 201.223 1.00 114.85 ? 2528 THR A CG2   1 
ATOM   6972  N N     . ALA A 1 2529 ? 122.185 181.758 197.772 1.00 118.29 ? 2529 ALA A N     1 
ATOM   6973  C CA    . ALA A 1 2529 ? 121.784 180.434 197.315 1.00 118.29 ? 2529 ALA A CA    1 
ATOM   6974  C C     . ALA A 1 2529 ? 122.963 179.480 197.438 1.00 118.29 ? 2529 ALA A C     1 
ATOM   6975  O O     . ALA A 1 2529 ? 124.048 179.783 196.927 1.00 118.29 ? 2529 ALA A O     1 
ATOM   6976  C CB    . ALA A 1 2529 ? 121.288 180.492 195.876 1.00 118.29 ? 2529 ALA A CB    1 
ATOM   6977  N N     . PRO A 1 2530 ? 122.809 178.335 198.107 1.00 123.86 ? 2530 PRO A N     1 
ATOM   6978  C CA    . PRO A 1 2530 ? 123.954 177.450 198.349 1.00 123.86 ? 2530 PRO A CA    1 
ATOM   6979  C C     . PRO A 1 2530 ? 124.220 176.423 197.261 1.00 123.86 ? 2530 PRO A C     1 
ATOM   6980  O O     . PRO A 1 2530 ? 125.269 175.766 197.308 1.00 123.86 ? 2530 PRO A O     1 
ATOM   6981  C CB    . PRO A 1 2530 ? 123.557 176.754 199.656 1.00 123.86 ? 2530 PRO A CB    1 
ATOM   6982  C CG    . PRO A 1 2530 ? 122.062 176.666 199.576 1.00 123.86 ? 2530 PRO A CG    1 
ATOM   6983  C CD    . PRO A 1 2530 ? 121.579 177.837 198.746 1.00 123.86 ? 2530 PRO A CD    1 
ATOM   6984  N N     . ASN A 1 2531 ? 123.319 176.264 196.295 1.00 114.75 ? 2531 ASN A N     1 
ATOM   6985  C CA    . ASN A 1 2531 ? 123.493 175.264 195.251 1.00 114.75 ? 2531 ASN A CA    1 
ATOM   6986  C C     . ASN A 1 2531 ? 124.150 175.848 194.007 1.00 114.75 ? 2531 ASN A C     1 
ATOM   6987  O O     . ASN A 1 2531 ? 125.089 175.261 193.460 1.00 114.75 ? 2531 ASN A O     1 
ATOM   6988  C CB    . ASN A 1 2531 ? 122.140 174.652 194.887 1.00 114.75 ? 2531 ASN A CB    1 
ATOM   6989  C CG    . ASN A 1 2531 ? 121.028 175.677 194.883 1.00 114.75 ? 2531 ASN A CG    1 
ATOM   6990  O OD1   . ASN A 1 2531 ? 121.270 176.868 195.075 1.00 114.75 ? 2531 ASN A OD1   1 
ATOM   6991  N ND2   . ASN A 1 2531 ? 119.800 175.221 194.664 1.00 114.75 ? 2531 ASN A ND2   1 
ATOM   6992  N N     . ILE A 1 2532 ? 123.670 176.997 193.556 1.00 109.50 ? 2532 ILE A N     1 
ATOM   6993  C CA    . ILE A 1 2532 ? 124.151 177.589 192.308 1.00 109.50 ? 2532 ILE A CA    1 
ATOM   6994  C C     . ILE A 1 2532 ? 125.521 178.215 192.551 1.00 109.50 ? 2532 ILE A C     1 
ATOM   6995  O O     . ILE A 1 2532 ? 125.680 178.982 193.512 1.00 109.50 ? 2532 ILE A O     1 
ATOM   6996  C CB    . ILE A 1 2532 ? 123.159 178.623 191.792 1.00 109.50 ? 2532 ILE A CB    1 
ATOM   6997  C CG1   . ILE A 1 2532 ? 121.902 177.931 191.263 1.00 109.50 ? 2532 ILE A CG1   1 
ATOM   6998  C CG2   . ILE A 1 2532 ? 123.786 179.448 190.691 1.00 109.50 ? 2532 ILE A CG2   1 
ATOM   6999  C CD1   . ILE A 1 2532 ? 122.190 176.785 190.318 1.00 109.50 ? 2532 ILE A CD1   1 
ATOM   7000  N N     . PRO A 1 2533 ? 126.520 177.912 191.727 1.00 104.69 ? 2533 PRO A N     1 
ATOM   7001  C CA    . PRO A 1 2533 ? 127.838 178.531 191.897 1.00 104.69 ? 2533 PRO A CA    1 
ATOM   7002  C C     . PRO A 1 2533 ? 127.798 180.025 191.618 1.00 104.69 ? 2533 PRO A C     1 
ATOM   7003  O O     . PRO A 1 2533 ? 126.933 180.535 190.903 1.00 104.69 ? 2533 PRO A O     1 
ATOM   7004  C CB    . PRO A 1 2533 ? 128.713 177.803 190.870 1.00 104.69 ? 2533 PRO A CB    1 
ATOM   7005  C CG    . PRO A 1 2533 ? 127.968 176.553 190.534 1.00 104.69 ? 2533 PRO A CG    1 
ATOM   7006  C CD    . PRO A 1 2533 ? 126.519 176.886 190.673 1.00 104.69 ? 2533 PRO A CD    1 
ATOM   7007  N N     . ILE A 1 2534 ? 128.772 180.729 192.202 1.00 97.22  ? 2534 ILE A N     1 
ATOM   7008  C CA    . ILE A 1 2534 ? 128.838 182.182 192.069 1.00 97.22  ? 2534 ILE A CA    1 
ATOM   7009  C C     . ILE A 1 2534 ? 129.028 182.591 190.616 1.00 97.22  ? 2534 ILE A C     1 
ATOM   7010  O O     . ILE A 1 2534 ? 128.613 183.684 190.210 1.00 97.22  ? 2534 ILE A O     1 
ATOM   7011  C CB    . ILE A 1 2534 ? 129.965 182.746 192.956 1.00 97.22  ? 2534 ILE A CB    1 
ATOM   7012  C CG1   . ILE A 1 2534 ? 129.918 182.115 194.346 1.00 97.22  ? 2534 ILE A CG1   1 
ATOM   7013  C CG2   . ILE A 1 2534 ? 129.863 184.257 193.054 1.00 97.22  ? 2534 ILE A CG2   1 
ATOM   7014  C CD1   . ILE A 1 2534 ? 131.030 181.123 194.599 1.00 97.22  ? 2534 ILE A CD1   1 
ATOM   7015  N N     . ILE A 1 2535 ? 129.652 181.730 189.811 1.00 92.04  ? 2535 ILE A N     1 
ATOM   7016  C CA    . ILE A 1 2535 ? 129.949 182.083 188.426 1.00 92.04  ? 2535 ILE A CA    1 
ATOM   7017  C C     . ILE A 1 2535 ? 128.670 182.293 187.627 1.00 92.04  ? 2535 ILE A C     1 
ATOM   7018  O O     . ILE A 1 2535 ? 128.670 183.007 186.618 1.00 92.04  ? 2535 ILE A O     1 
ATOM   7019  C CB    . ILE A 1 2535 ? 130.848 181.009 187.788 1.00 92.04  ? 2535 ILE A CB    1 
ATOM   7020  C CG1   . ILE A 1 2535 ? 131.479 181.545 186.508 1.00 92.04  ? 2535 ILE A CG1   1 
ATOM   7021  C CG2   . ILE A 1 2535 ? 130.060 179.745 187.505 1.00 92.04  ? 2535 ILE A CG2   1 
ATOM   7022  C CD1   . ILE A 1 2535 ? 132.209 182.844 186.707 1.00 92.04  ? 2535 ILE A CD1   1 
ATOM   7023  N N     . ASP A 1 2536 ? 127.564 181.689 188.060 1.00 97.12  ? 2536 ASP A N     1 
ATOM   7024  C CA    . ASP A 1 2536 ? 126.296 181.846 187.360 1.00 97.12  ? 2536 ASP A CA    1 
ATOM   7025  C C     . ASP A 1 2536 ? 125.592 183.150 187.693 1.00 97.12  ? 2536 ASP A C     1 
ATOM   7026  O O     . ASP A 1 2536 ? 124.574 183.460 187.068 1.00 97.12  ? 2536 ASP A O     1 
ATOM   7027  C CB    . ASP A 1 2536 ? 125.364 180.680 187.686 1.00 97.12  ? 2536 ASP A CB    1 
ATOM   7028  C CG    . ASP A 1 2536 ? 126.053 179.342 187.579 1.00 97.12  ? 2536 ASP A CG    1 
ATOM   7029  O OD1   . ASP A 1 2536 ? 126.896 179.040 188.448 1.00 97.12  ? 2536 ASP A OD1   1 
ATOM   7030  O OD2   . ASP A 1 2536 ? 125.749 178.590 186.630 1.00 97.12  ? 2536 ASP A OD2   1 
ATOM   7031  N N     . TYR A 1 2537 ? 126.095 183.910 188.656 1.00 97.51  ? 2537 TYR A N     1 
ATOM   7032  C CA    . TYR A 1 2537 ? 125.468 185.159 189.053 1.00 97.51  ? 2537 TYR A CA    1 
ATOM   7033  C C     . TYR A 1 2537 ? 126.145 186.337 188.366 1.00 97.51  ? 2537 TYR A C     1 
ATOM   7034  O O     . TYR A 1 2537 ? 127.154 186.198 187.673 1.00 97.51  ? 2537 TYR A O     1 
ATOM   7035  C CB    . TYR A 1 2537 ? 125.519 185.327 190.572 1.00 97.51  ? 2537 TYR A CB    1 
ATOM   7036  C CG    . TYR A 1 2537 ? 124.440 184.565 191.296 1.00 97.51  ? 2537 TYR A CG    1 
ATOM   7037  C CD1   . TYR A 1 2537 ? 124.620 183.236 191.643 1.00 97.51  ? 2537 TYR A CD1   1 
ATOM   7038  C CD2   . TYR A 1 2537 ? 123.233 185.168 191.614 1.00 97.51  ? 2537 TYR A CD2   1 
ATOM   7039  C CE1   . TYR A 1 2537 ? 123.636 182.533 192.301 1.00 97.51  ? 2537 TYR A CE1   1 
ATOM   7040  C CE2   . TYR A 1 2537 ? 122.241 184.471 192.270 1.00 97.51  ? 2537 TYR A CE2   1 
ATOM   7041  C CZ    . TYR A 1 2537 ? 122.449 183.153 192.610 1.00 97.51  ? 2537 TYR A CZ    1 
ATOM   7042  O OH    . TYR A 1 2537 ? 121.466 182.449 193.263 1.00 97.51  ? 2537 TYR A OH    1 
ATOM   7043  N N     . GLU A 1 2538 ? 125.565 187.515 188.568 1.00 91.41  ? 2538 GLU A N     1 
ATOM   7044  C CA    . GLU A 1 2538 ? 126.108 188.746 188.020 1.00 91.41  ? 2538 GLU A CA    1 
ATOM   7045  C C     . GLU A 1 2538 ? 125.751 189.893 188.949 1.00 91.41  ? 2538 GLU A C     1 
ATOM   7046  O O     . GLU A 1 2538 ? 124.840 189.791 189.773 1.00 91.41  ? 2538 GLU A O     1 
ATOM   7047  C CB    . GLU A 1 2538 ? 125.578 189.021 186.613 1.00 91.41  ? 2538 GLU A CB    1 
ATOM   7048  C CG    . GLU A 1 2538 ? 124.137 189.479 186.583 1.00 91.41  ? 2538 GLU A CG    1 
ATOM   7049  C CD    . GLU A 1 2538 ? 123.848 190.403 185.423 1.00 91.41  ? 2538 GLU A CD    1 
ATOM   7050  O OE1   . GLU A 1 2538 ? 124.811 190.848 184.768 1.00 91.41  ? 2538 GLU A OE1   1 
ATOM   7051  O OE2   . GLU A 1 2538 ? 122.659 190.682 185.164 1.00 91.41  ? 2538 GLU A OE2   1 
ATOM   7052  N N     . VAL A 1 2539 ? 126.482 190.989 188.807 1.00 86.74  ? 2539 VAL A N     1 
ATOM   7053  C CA    . VAL A 1 2539 ? 126.259 192.186 189.603 1.00 86.74  ? 2539 VAL A CA    1 
ATOM   7054  C C     . VAL A 1 2539 ? 125.402 193.134 188.781 1.00 86.74  ? 2539 VAL A C     1 
ATOM   7055  O O     . VAL A 1 2539 ? 125.863 193.697 187.783 1.00 86.74  ? 2539 VAL A O     1 
ATOM   7056  C CB    . VAL A 1 2539 ? 127.578 192.846 190.014 1.00 86.74  ? 2539 VAL A CB    1 
ATOM   7057  C CG1   . VAL A 1 2539 ? 127.310 193.972 190.983 1.00 86.74  ? 2539 VAL A CG1   1 
ATOM   7058  C CG2   . VAL A 1 2539 ? 128.500 191.822 190.632 1.00 86.74  ? 2539 VAL A CG2   1 
ATOM   7059  N N     . SER A 1 2540 ? 124.153 193.310 189.194 1.00 87.50  ? 2540 SER A N     1 
ATOM   7060  C CA    . SER A 1 2540 ? 123.293 194.274 188.534 1.00 87.50  ? 2540 SER A CA    1 
ATOM   7061  C C     . SER A 1 2540 ? 123.747 195.691 188.862 1.00 87.50  ? 2540 SER A C     1 
ATOM   7062  O O     . SER A 1 2540 ? 124.460 195.934 189.839 1.00 87.50  ? 2540 SER A O     1 
ATOM   7063  C CB    . SER A 1 2540 ? 121.840 194.077 188.956 1.00 87.50  ? 2540 SER A CB    1 
ATOM   7064  O OG    . SER A 1 2540 ? 121.044 195.175 188.549 1.00 87.50  ? 2540 SER A OG    1 
ATOM   7065  N N     . ILE A 1 2541 ? 123.319 196.637 188.025 1.00 87.48  ? 2541 ILE A N     1 
ATOM   7066  C CA    . ILE A 1 2541 ? 123.700 198.028 188.225 1.00 87.48  ? 2541 ILE A CA    1 
ATOM   7067  C C     . ILE A 1 2541 ? 123.180 198.562 189.549 1.00 87.48  ? 2541 ILE A C     1 
ATOM   7068  O O     . ILE A 1 2541 ? 123.713 199.545 190.071 1.00 87.48  ? 2541 ILE A O     1 
ATOM   7069  C CB    . ILE A 1 2541 ? 123.207 198.890 187.045 1.00 87.48  ? 2541 ILE A CB    1 
ATOM   7070  C CG1   . ILE A 1 2541 ? 124.087 200.127 186.887 1.00 87.48  ? 2541 ILE A CG1   1 
ATOM   7071  C CG2   . ILE A 1 2541 ? 121.757 199.294 187.237 1.00 87.48  ? 2541 ILE A CG2   1 
ATOM   7072  C CD1   . ILE A 1 2541 ? 125.522 199.807 186.563 1.00 87.48  ? 2541 ILE A CD1   1 
ATOM   7073  N N     . SER A 1 2542 ? 122.151 197.933 190.114 1.00 90.40  ? 2542 SER A N     1 
ATOM   7074  C CA    . SER A 1 2542 ? 121.601 198.373 191.387 1.00 90.40  ? 2542 SER A CA    1 
ATOM   7075  C C     . SER A 1 2542 ? 122.431 197.921 192.579 1.00 90.40  ? 2542 SER A C     1 
ATOM   7076  O O     . SER A 1 2542 ? 122.244 198.455 193.677 1.00 90.40  ? 2542 SER A O     1 
ATOM   7077  C CB    . SER A 1 2542 ? 120.165 197.871 191.535 1.00 90.40  ? 2542 SER A CB    1 
ATOM   7078  O OG    . SER A 1 2542 ? 120.112 196.460 191.440 1.00 90.40  ? 2542 SER A OG    1 
ATOM   7079  N N     . GLY A 1 2543 ? 123.332 196.966 192.397 1.00 92.53  ? 2543 GLY A N     1 
ATOM   7080  C CA    . GLY A 1 2543 ? 124.225 196.545 193.448 1.00 92.53  ? 2543 GLY A CA    1 
ATOM   7081  C C     . GLY A 1 2543 ? 123.862 195.264 194.164 1.00 92.53  ? 2543 GLY A C     1 
ATOM   7082  O O     . GLY A 1 2543 ? 124.219 195.113 195.336 1.00 92.53  ? 2543 GLY A O     1 
ATOM   7083  N N     . GLU A 1 2544 ? 123.165 194.342 193.505 1.00 97.79  ? 2544 GLU A N     1 
ATOM   7084  C CA    . GLU A 1 2544 ? 122.829 193.059 194.104 1.00 97.79  ? 2544 GLU A CA    1 
ATOM   7085  C C     . GLU A 1 2544 ? 123.096 191.953 193.096 1.00 97.79  ? 2544 GLU A C     1 
ATOM   7086  O O     . GLU A 1 2544 ? 123.022 192.157 191.882 1.00 97.79  ? 2544 GLU A O     1 
ATOM   7087  C CB    . GLU A 1 2544 ? 121.363 192.994 194.562 1.00 97.79  ? 2544 GLU A CB    1 
ATOM   7088  C CG    . GLU A 1 2544 ? 120.841 194.246 195.245 1.00 97.79  ? 2544 GLU A CG    1 
ATOM   7089  C CD    . GLU A 1 2544 ? 120.467 195.330 194.258 1.00 97.79  ? 2544 GLU A CD    1 
ATOM   7090  O OE1   . GLU A 1 2544 ? 120.619 195.097 193.042 1.00 97.79  ? 2544 GLU A OE1   1 
ATOM   7091  O OE2   . GLU A 1 2544 ? 120.024 196.412 194.694 1.00 97.79  ? 2544 GLU A OE2   1 
ATOM   7092  N N     . TRP A 1 2545 ? 123.401 190.771 193.618 1.00 97.92  ? 2545 TRP A N     1 
ATOM   7093  C CA    . TRP A 1 2545 ? 123.623 189.604 192.778 1.00 97.92  ? 2545 TRP A CA    1 
ATOM   7094  C C     . TRP A 1 2545 ? 122.303 189.172 192.158 1.00 97.92  ? 2545 TRP A C     1 
ATOM   7095  O O     . TRP A 1 2545 ? 121.282 189.098 192.849 1.00 97.92  ? 2545 TRP A O     1 
ATOM   7096  C CB    . TRP A 1 2545 ? 124.223 188.465 193.596 1.00 97.92  ? 2545 TRP A CB    1 
ATOM   7097  C CG    . TRP A 1 2545 ? 125.430 188.853 194.364 1.00 97.92  ? 2545 TRP A CG    1 
ATOM   7098  C CD1   . TRP A 1 2545 ? 125.464 189.459 195.582 1.00 97.92  ? 2545 TRP A CD1   1 
ATOM   7099  C CD2   . TRP A 1 2545 ? 126.791 188.654 193.976 1.00 97.92  ? 2545 TRP A CD2   1 
ATOM   7100  N NE1   . TRP A 1 2545 ? 126.762 189.655 195.976 1.00 97.92  ? 2545 TRP A NE1   1 
ATOM   7101  C CE2   . TRP A 1 2545 ? 127.597 189.167 195.007 1.00 97.92  ? 2545 TRP A CE2   1 
ATOM   7102  C CE3   . TRP A 1 2545 ? 127.406 188.089 192.859 1.00 97.92  ? 2545 TRP A CE3   1 
ATOM   7103  C CZ2   . TRP A 1 2545 ? 128.985 189.135 194.952 1.00 97.92  ? 2545 TRP A CZ2   1 
ATOM   7104  C CZ3   . TRP A 1 2545 ? 128.782 188.058 192.807 1.00 97.92  ? 2545 TRP A CZ3   1 
ATOM   7105  C CH2   . TRP A 1 2545 ? 129.557 188.577 193.846 1.00 97.92  ? 2545 TRP A CH2   1 
ATOM   7106  N N     . SER A 1 2546 ? 122.318 188.895 190.858 1.00 96.18  ? 2546 SER A N     1 
ATOM   7107  C CA    . SER A 1 2546 ? 121.158 188.317 190.215 1.00 96.18  ? 2546 SER A CA    1 
ATOM   7108  C C     . SER A 1 2546 ? 121.588 187.156 189.330 1.00 96.18  ? 2546 SER A C     1 
ATOM   7109  O O     . SER A 1 2546 ? 122.668 187.202 188.734 1.00 96.18  ? 2546 SER A O     1 
ATOM   7110  C CB    . SER A 1 2546 ? 120.411 189.354 189.369 1.00 96.18  ? 2546 SER A CB    1 
ATOM   7111  O OG    . SER A 1 2546 ? 120.793 189.260 188.010 1.00 96.18  ? 2546 SER A OG    1 
ATOM   7112  N N     . PRO A 1 2547 ? 120.784 186.102 189.235 1.00 92.28  ? 2547 PRO A N     1 
ATOM   7113  C CA    . PRO A 1 2547 ? 121.158 184.977 188.374 1.00 92.28  ? 2547 PRO A CA    1 
ATOM   7114  C C     . PRO A 1 2547 ? 121.189 185.398 186.915 1.00 92.28  ? 2547 PRO A C     1 
ATOM   7115  O O     . PRO A 1 2547 ? 120.364 186.192 186.460 1.00 92.28  ? 2547 PRO A O     1 
ATOM   7116  C CB    . PRO A 1 2547 ? 120.058 183.945 188.641 1.00 92.28  ? 2547 PRO A CB    1 
ATOM   7117  C CG    . PRO A 1 2547 ? 118.895 184.751 189.100 1.00 92.28  ? 2547 PRO A CG    1 
ATOM   7118  C CD    . PRO A 1 2547 ? 119.468 185.906 189.864 1.00 92.28  ? 2547 PRO A CD    1 
ATOM   7119  N N     . TRP A 1 2548 ? 122.157 184.852 186.179 1.00 90.88  ? 2548 TRP A N     1 
ATOM   7120  C CA    . TRP A 1 2548 ? 122.239 185.124 184.751 1.00 90.88  ? 2548 TRP A CA    1 
ATOM   7121  C C     . TRP A 1 2548 ? 121.056 184.544 183.994 1.00 90.88  ? 2548 TRP A C     1 
ATOM   7122  O O     . TRP A 1 2548 ? 120.748 185.015 182.894 1.00 90.88  ? 2548 TRP A O     1 
ATOM   7123  C CB    . TRP A 1 2548 ? 123.538 184.561 184.180 1.00 90.88  ? 2548 TRP A CB    1 
ATOM   7124  C CG    . TRP A 1 2548 ? 124.701 185.499 184.250 1.00 90.88  ? 2548 TRP A CG    1 
ATOM   7125  C CD1   . TRP A 1 2548 ? 125.799 185.379 185.048 1.00 90.88  ? 2548 TRP A CD1   1 
ATOM   7126  C CD2   . TRP A 1 2548 ? 124.894 186.690 183.480 1.00 90.88  ? 2548 TRP A CD2   1 
ATOM   7127  N NE1   . TRP A 1 2548 ? 126.661 186.424 184.827 1.00 90.88  ? 2548 TRP A NE1   1 
ATOM   7128  C CE2   . TRP A 1 2548 ? 126.128 187.242 183.866 1.00 90.88  ? 2548 TRP A CE2   1 
ATOM   7129  C CE3   . TRP A 1 2548 ? 124.141 187.346 182.504 1.00 90.88  ? 2548 TRP A CE3   1 
ATOM   7130  C CZ2   . TRP A 1 2548 ? 126.624 188.417 183.315 1.00 90.88  ? 2548 TRP A CZ2   1 
ATOM   7131  C CZ3   . TRP A 1 2548 ? 124.637 188.510 181.955 1.00 90.88  ? 2548 TRP A CZ3   1 
ATOM   7132  C CH2   . TRP A 1 2548 ? 125.865 189.035 182.362 1.00 90.88  ? 2548 TRP A CH2   1 
ATOM   7133  N N     . GLN A 1 2549 ? 120.383 183.541 184.563 1.00 91.73  ? 2549 GLN A N     1 
ATOM   7134  C CA    . GLN A 1 2549 ? 119.271 182.900 183.872 1.00 91.73  ? 2549 GLN A CA    1 
ATOM   7135  C C     . GLN A 1 2549 ? 118.120 183.865 183.637 1.00 91.73  ? 2549 GLN A C     1 
ATOM   7136  O O     . GLN A 1 2549 ? 117.323 183.665 182.714 1.00 91.73  ? 2549 GLN A O     1 
ATOM   7137  C CB    . GLN A 1 2549 ? 118.793 181.689 184.671 1.00 91.73  ? 2549 GLN A CB    1 
ATOM   7138  C CG    . GLN A 1 2549 ? 118.014 180.678 183.854 1.00 91.73  ? 2549 GLN A CG    1 
ATOM   7139  C CD    . GLN A 1 2549 ? 118.558 180.523 182.451 1.00 91.73  ? 2549 GLN A CD    1 
ATOM   7140  O OE1   . GLN A 1 2549 ? 119.643 179.977 182.249 1.00 91.73  ? 2549 GLN A OE1   1 
ATOM   7141  N NE2   . GLN A 1 2549 ? 117.806 181.003 181.470 1.00 91.73  ? 2549 GLN A NE2   1 
ATOM   7142  N N     . ALA A 1 2550 ? 118.015 184.913 184.453 1.00 89.51  ? 2550 ALA A N     1 
ATOM   7143  C CA    . ALA A 1 2550 ? 116.936 185.875 184.274 1.00 89.51  ? 2550 ALA A CA    1 
ATOM   7144  C C     . ALA A 1 2550 ? 117.086 186.660 182.979 1.00 89.51  ? 2550 ALA A C     1 
ATOM   7145  O O     . ALA A 1 2550 ? 116.082 187.036 182.365 1.00 89.51  ? 2550 ALA A O     1 
ATOM   7146  C CB    . ALA A 1 2550 ? 116.880 186.829 185.465 1.00 89.51  ? 2550 ALA A CB    1 
ATOM   7147  N N     . LYS A 1 2551 ? 118.317 186.910 182.545 1.00 87.95  ? 2551 LYS A N     1 
ATOM   7148  C CA    . LYS A 1 2551 ? 118.568 187.748 181.382 1.00 87.95  ? 2551 LYS A CA    1 
ATOM   7149  C C     . LYS A 1 2551 ? 118.568 186.974 180.073 1.00 87.95  ? 2551 LYS A C     1 
ATOM   7150  O O     . LYS A 1 2551 ? 118.777 187.578 179.017 1.00 87.95  ? 2551 LYS A O     1 
ATOM   7151  C CB    . LYS A 1 2551 ? 119.903 188.479 181.542 1.00 87.95  ? 2551 LYS A CB    1 
ATOM   7152  C CG    . LYS A 1 2551 ? 119.857 189.643 182.517 1.00 87.95  ? 2551 LYS A CG    1 
ATOM   7153  C CD    . LYS A 1 2551 ? 120.910 190.690 182.190 1.00 87.95  ? 2551 LYS A CD    1 
ATOM   7154  C CE    . LYS A 1 2551 ? 120.829 191.126 180.738 1.00 87.95  ? 2551 LYS A CE    1 
ATOM   7155  N NZ    . LYS A 1 2551 ? 121.737 192.269 180.458 1.00 87.95  ? 2551 LYS A NZ    1 
ATOM   7156  N N     . VAL A 1 2552 ? 118.342 185.666 180.109 1.00 85.30  ? 2552 VAL A N     1 
ATOM   7157  C CA    . VAL A 1 2552 ? 118.358 184.835 178.910 1.00 85.30  ? 2552 VAL A CA    1 
ATOM   7158  C C     . VAL A 1 2552 ? 116.963 184.866 178.293 1.00 85.30  ? 2552 VAL A C     1 
ATOM   7159  O O     . VAL A 1 2552 ? 116.007 184.411 178.939 1.00 85.30  ? 2552 VAL A O     1 
ATOM   7160  C CB    . VAL A 1 2552 ? 118.782 183.399 179.227 1.00 85.30  ? 2552 VAL A CB    1 
ATOM   7161  C CG1   . VAL A 1 2552 ? 118.936 182.610 177.946 1.00 85.30  ? 2552 VAL A CG1   1 
ATOM   7162  C CG2   . VAL A 1 2552 ? 120.075 183.399 180.014 1.00 85.30  ? 2552 VAL A CG2   1 
ATOM   7163  N N     . PRO A 1 2553 ? 116.804 185.371 177.075 1.00 91.41  ? 2553 PRO A N     1 
ATOM   7164  C CA    . PRO A 1 2553 ? 115.472 185.457 176.475 1.00 91.41  ? 2553 PRO A CA    1 
ATOM   7165  C C     . PRO A 1 2553 ? 115.061 184.151 175.813 1.00 91.41  ? 2553 PRO A C     1 
ATOM   7166  O O     . PRO A 1 2553 ? 115.883 183.291 175.495 1.00 91.41  ? 2553 PRO A O     1 
ATOM   7167  C CB    . PRO A 1 2553 ? 115.633 186.567 175.434 1.00 91.41  ? 2553 PRO A CB    1 
ATOM   7168  C CG    . PRO A 1 2553 ? 117.060 186.455 175.011 1.00 91.41  ? 2553 PRO A CG    1 
ATOM   7169  C CD    . PRO A 1 2553 ? 117.842 185.947 176.203 1.00 91.41  ? 2553 PRO A CD    1 
ATOM   7170  N N     . GLN A 1 2554 ? 113.754 184.017 175.609 1.00 98.43  ? 2554 GLN A N     1 
ATOM   7171  C CA    . GLN A 1 2554 ? 113.191 182.877 174.897 1.00 98.43  ? 2554 GLN A CA    1 
ATOM   7172  C C     . GLN A 1 2554 ? 112.939 183.300 173.456 1.00 98.43  ? 2554 GLN A C     1 
ATOM   7173  O O     . GLN A 1 2554 ? 112.028 184.086 173.183 1.00 98.43  ? 2554 GLN A O     1 
ATOM   7174  C CB    . GLN A 1 2554 ? 111.907 182.398 175.568 1.00 98.43  ? 2554 GLN A CB    1 
ATOM   7175  C CG    . GLN A 1 2554 ? 111.230 181.225 174.875 1.00 98.43  ? 2554 GLN A CG    1 
ATOM   7176  C CD    . GLN A 1 2554 ? 112.217 180.263 174.248 1.00 98.43  ? 2554 GLN A CD    1 
ATOM   7177  O OE1   . GLN A 1 2554 ? 112.486 180.324 173.050 1.00 98.43  ? 2554 GLN A OE1   1 
ATOM   7178  N NE2   . GLN A 1 2554 ? 112.766 179.367 175.058 1.00 98.43  ? 2554 GLN A NE2   1 
ATOM   7179  N N     . ILE A 1 2555 ? 113.740 182.778 172.537 1.00 99.43  ? 2555 ILE A N     1 
ATOM   7180  C CA    . ILE A 1 2555 ? 113.692 183.164 171.133 1.00 99.43  ? 2555 ILE A CA    1 
ATOM   7181  C C     . ILE A 1 2555 ? 113.042 182.049 170.332 1.00 99.43  ? 2555 ILE A C     1 
ATOM   7182  O O     . ILE A 1 2555 ? 113.390 180.872 170.483 1.00 99.43  ? 2555 ILE A O     1 
ATOM   7183  C CB    . ILE A 1 2555 ? 115.104 183.478 170.602 1.00 99.43  ? 2555 ILE A CB    1 
ATOM   7184  C CG1   . ILE A 1 2555 ? 115.072 183.746 169.099 1.00 99.43  ? 2555 ILE A CG1   1 
ATOM   7185  C CG2   . ILE A 1 2555 ? 116.058 182.345 170.917 1.00 99.43  ? 2555 ILE A CG2   1 
ATOM   7186  C CD1   . ILE A 1 2555 ? 116.436 184.032 168.511 1.00 99.43  ? 2555 ILE A CD1   1 
ATOM   7187  N N     . GLU A 1 2556 ? 112.086 182.412 169.484 1.00 103.85 ? 2556 GLU A N     1 
ATOM   7188  C CA    . GLU A 1 2556 ? 111.424 181.464 168.598 1.00 103.85 ? 2556 GLU A CA    1 
ATOM   7189  C C     . GLU A 1 2556 ? 111.926 181.700 167.183 1.00 103.85 ? 2556 GLU A C     1 
ATOM   7190  O O     . GLU A 1 2556 ? 111.778 182.801 166.644 1.00 103.85 ? 2556 GLU A O     1 
ATOM   7191  C CB    . GLU A 1 2556 ? 109.905 181.610 168.671 1.00 103.85 ? 2556 GLU A CB    1 
ATOM   7192  C CG    . GLU A 1 2556 ? 109.318 181.249 170.026 1.00 103.85 ? 2556 GLU A CG    1 
ATOM   7193  C CD    . GLU A 1 2556 ? 109.365 179.760 170.306 1.00 103.85 ? 2556 GLU A CD    1 
ATOM   7194  O OE1   . GLU A 1 2556 ? 109.481 178.972 169.345 1.00 103.85 ? 2556 GLU A OE1   1 
ATOM   7195  O OE2   . GLU A 1 2556 ? 109.293 179.377 171.492 1.00 103.85 ? 2556 GLU A OE2   1 
ATOM   7196  N N     . VAL A 1 2557 ? 112.511 180.671 166.585 1.00 104.22 ? 2557 VAL A N     1 
ATOM   7197  C CA    . VAL A 1 2557 ? 113.131 180.790 165.277 1.00 104.22 ? 2557 VAL A CA    1 
ATOM   7198  C C     . VAL A 1 2557 ? 112.209 180.168 164.236 1.00 104.22 ? 2557 VAL A C     1 
ATOM   7199  O O     . VAL A 1 2557 ? 111.353 179.333 164.537 1.00 104.22 ? 2557 VAL A O     1 
ATOM   7200  C CB    . VAL A 1 2557 ? 114.531 180.142 165.250 1.00 104.22 ? 2557 VAL A CB    1 
ATOM   7201  C CG1   . VAL A 1 2557 ? 114.423 178.634 165.208 1.00 104.22 ? 2557 VAL A CG1   1 
ATOM   7202  C CG2   . VAL A 1 2557 ? 115.355 180.667 164.080 1.00 104.22 ? 2557 VAL A CG2   1 
ATOM   7203  N N     . GLU A 1 2558 ? 112.384 180.605 162.992 1.00 107.37 ? 2558 GLU A N     1 
ATOM   7204  C CA    . GLU A 1 2558 ? 111.552 180.142 161.896 1.00 107.37 ? 2558 GLU A CA    1 
ATOM   7205  C C     . GLU A 1 2558 ? 111.874 178.691 161.549 1.00 107.37 ? 2558 GLU A C     1 
ATOM   7206  O O     . GLU A 1 2558 ? 112.947 178.170 161.861 1.00 107.37 ? 2558 GLU A O     1 
ATOM   7207  C CB    . GLU A 1 2558 ? 111.745 181.036 160.674 1.00 107.37 ? 2558 GLU A CB    1 
ATOM   7208  C CG    . GLU A 1 2558 ? 112.192 182.440 161.032 1.00 107.37 ? 2558 GLU A CG    1 
ATOM   7209  C CD    . GLU A 1 2558 ? 112.597 183.248 159.823 1.00 107.37 ? 2558 GLU A CD    1 
ATOM   7210  O OE1   . GLU A 1 2558 ? 112.086 182.963 158.720 1.00 107.37 ? 2558 GLU A OE1   1 
ATOM   7211  O OE2   . GLU A 1 2558 ? 113.426 184.169 159.975 1.00 107.37 ? 2558 GLU A OE2   1 
ATOM   7212  N N     . THR A 1 2559 ? 110.913 178.038 160.891 1.00 104.12 ? 2559 THR A N     1 
ATOM   7213  C CA    . THR A 1 2559 ? 111.046 176.616 160.593 1.00 104.12 ? 2559 THR A CA    1 
ATOM   7214  C C     . THR A 1 2559 ? 112.222 176.347 159.663 1.00 104.12 ? 2559 THR A C     1 
ATOM   7215  O O     . THR A 1 2559 ? 113.014 175.427 159.897 1.00 104.12 ? 2559 THR A O     1 
ATOM   7216  C CB    . THR A 1 2559 ? 109.746 176.089 159.985 1.00 104.12 ? 2559 THR A CB    1 
ATOM   7217  O OG1   . THR A 1 2559 ? 108.784 175.882 161.025 1.00 104.12 ? 2559 THR A OG1   1 
ATOM   7218  C CG2   . THR A 1 2559 ? 109.987 174.777 159.263 1.00 104.12 ? 2559 THR A CG2   1 
ATOM   7219  N N     . HIS A 1 2560 ? 112.363 177.145 158.604 1.00 101.90 ? 2560 HIS A N     1 
ATOM   7220  C CA    . HIS A 1 2560 ? 113.446 176.908 157.658 1.00 101.90 ? 2560 HIS A CA    1 
ATOM   7221  C C     . HIS A 1 2560 ? 114.807 177.296 158.216 1.00 101.90 ? 2560 HIS A C     1 
ATOM   7222  O O     . HIS A 1 2560 ? 115.826 176.983 157.593 1.00 101.90 ? 2560 HIS A O     1 
ATOM   7223  C CB    . HIS A 1 2560 ? 113.184 177.661 156.354 1.00 101.90 ? 2560 HIS A CB    1 
ATOM   7224  C CG    . HIS A 1 2560 ? 113.661 179.079 156.364 1.00 101.90 ? 2560 HIS A CG    1 
ATOM   7225  N ND1   . HIS A 1 2560 ? 112.825 180.142 156.629 1.00 101.90 ? 2560 HIS A ND1   1 
ATOM   7226  C CD2   . HIS A 1 2560 ? 114.881 179.613 156.118 1.00 101.90 ? 2560 HIS A CD2   1 
ATOM   7227  C CE1   . HIS A 1 2560 ? 113.513 181.268 156.560 1.00 101.90 ? 2560 HIS A CE1   1 
ATOM   7228  N NE2   . HIS A 1 2560 ? 114.763 180.974 156.252 1.00 101.90 ? 2560 HIS A NE2   1 
ATOM   7229  N N     . LYS A 1 2561 ? 114.847 177.968 159.362 1.00 106.71 ? 2561 LYS A N     1 
ATOM   7230  C CA    . LYS A 1 2561 ? 116.091 178.388 159.987 1.00 106.71 ? 2561 LYS A CA    1 
ATOM   7231  C C     . LYS A 1 2561 ? 116.589 177.403 161.035 1.00 106.71 ? 2561 LYS A C     1 
ATOM   7232  O O     . LYS A 1 2561 ? 117.572 177.698 161.722 1.00 106.71 ? 2561 LYS A O     1 
ATOM   7233  C CB    . LYS A 1 2561 ? 115.920 179.769 160.623 1.00 106.71 ? 2561 LYS A CB    1 
ATOM   7234  C CG    . LYS A 1 2561 ? 115.998 180.918 159.638 1.00 106.71 ? 2561 LYS A CG    1 
ATOM   7235  C CD    . LYS A 1 2561 ? 117.409 181.076 159.101 1.00 106.71 ? 2561 LYS A CD    1 
ATOM   7236  C CE    . LYS A 1 2561 ? 117.621 182.457 158.510 1.00 106.71 ? 2561 LYS A CE    1 
ATOM   7237  N NZ    . LYS A 1 2561 ? 116.357 183.035 157.974 1.00 106.71 ? 2561 LYS A NZ    1 
ATOM   7238  N N     . VAL A 1 2562 ? 115.936 176.250 161.180 1.00 103.09 ? 2562 VAL A N     1 
ATOM   7239  C CA    . VAL A 1 2562 ? 116.301 175.318 162.240 1.00 103.09 ? 2562 VAL A CA    1 
ATOM   7240  C C     . VAL A 1 2562 ? 117.693 174.766 161.975 1.00 103.09 ? 2562 VAL A C     1 
ATOM   7241  O O     . VAL A 1 2562 ? 117.978 174.243 160.890 1.00 103.09 ? 2562 VAL A O     1 
ATOM   7242  C CB    . VAL A 1 2562 ? 115.267 174.189 162.351 1.00 103.09 ? 2562 VAL A CB    1 
ATOM   7243  C CG1   . VAL A 1 2562 ? 115.796 173.084 163.241 1.00 103.09 ? 2562 VAL A CG1   1 
ATOM   7244  C CG2   . VAL A 1 2562 ? 113.958 174.724 162.896 1.00 103.09 ? 2562 VAL A CG2   1 
ATOM   7245  N N     . ALA A 1 2563 ? 118.567 174.890 162.973 1.00 96.31  ? 2563 ALA A N     1 
ATOM   7246  C CA    . ALA A 1 2563 ? 119.952 174.435 162.898 1.00 96.31  ? 2563 ALA A CA    1 
ATOM   7247  C C     . ALA A 1 2563 ? 120.677 175.038 161.702 1.00 96.31  ? 2563 ALA A C     1 
ATOM   7248  O O     . ALA A 1 2563 ? 121.560 174.410 161.114 1.00 96.31  ? 2563 ALA A O     1 
ATOM   7249  C CB    . ALA A 1 2563 ? 120.040 172.908 162.869 1.00 96.31  ? 2563 ALA A CB    1 
ATOM   7250  N N     . ALA A 1 2564 ? 120.307 176.262 161.339 1.00 103.35 ? 2564 ALA A N     1 
ATOM   7251  C CA    . ALA A 1 2564 ? 121.008 176.970 160.288 1.00 103.35 ? 2564 ALA A CA    1 
ATOM   7252  C C     . ALA A 1 2564 ? 122.436 177.263 160.740 1.00 103.35 ? 2564 ALA A C     1 
ATOM   7253  O O     . ALA A 1 2564 ? 122.715 177.308 161.941 1.00 103.35 ? 2564 ALA A O     1 
ATOM   7254  C CB    . ALA A 1 2564 ? 120.283 178.270 159.946 1.00 103.35 ? 2564 ALA A CB    1 
ATOM   7255  N N     . PRO A 1 2565 ? 123.364 177.445 159.800 1.00 107.91 ? 2565 PRO A N     1 
ATOM   7256  C CA    . PRO A 1 2565 ? 124.764 177.642 160.203 1.00 107.91 ? 2565 PRO A CA    1 
ATOM   7257  C C     . PRO A 1 2565 ? 124.978 178.815 161.145 1.00 107.91 ? 2565 PRO A C     1 
ATOM   7258  O O     . PRO A 1 2565 ? 125.862 178.737 162.003 1.00 107.91 ? 2565 PRO A O     1 
ATOM   7259  C CB    . PRO A 1 2565 ? 125.487 177.856 158.866 1.00 107.91 ? 2565 PRO A CB    1 
ATOM   7260  C CG    . PRO A 1 2565 ? 124.617 177.205 157.856 1.00 107.91 ? 2565 PRO A CG    1 
ATOM   7261  C CD    . PRO A 1 2565 ? 123.214 177.385 158.336 1.00 107.91 ? 2565 PRO A CD    1 
ATOM   7262  N N     . ASP A 1 2566 ? 124.184 179.883 161.041 1.00 104.49 ? 2566 ASP A N     1 
ATOM   7263  C CA    . ASP A 1 2566 ? 124.477 181.120 161.752 1.00 104.49 ? 2566 ASP A CA    1 
ATOM   7264  C C     . ASP A 1 2566 ? 123.545 181.425 162.917 1.00 104.49 ? 2566 ASP A C     1 
ATOM   7265  O O     . ASP A 1 2566 ? 123.857 182.320 163.710 1.00 104.49 ? 2566 ASP A O     1 
ATOM   7266  C CB    . ASP A 1 2566 ? 124.455 182.307 160.779 1.00 104.49 ? 2566 ASP A CB    1 
ATOM   7267  C CG    . ASP A 1 2566 ? 125.497 182.183 159.691 1.00 104.49 ? 2566 ASP A CG    1 
ATOM   7268  O OD1   . ASP A 1 2566 ? 126.285 183.134 159.514 1.00 104.49 ? 2566 ASP A OD1   1 
ATOM   7269  O OD2   . ASP A 1 2566 ? 125.532 181.133 159.018 1.00 104.49 ? 2566 ASP A OD2   1 
ATOM   7270  N N     . VAL A 1 2567 ? 122.420 180.726 163.050 1.00 93.95  ? 2567 VAL A N     1 
ATOM   7271  C CA    . VAL A 1 2567 ? 121.486 181.039 164.124 1.00 93.95  ? 2567 VAL A CA    1 
ATOM   7272  C C     . VAL A 1 2567 ? 122.098 180.654 165.464 1.00 93.95  ? 2567 VAL A C     1 
ATOM   7273  O O     . VAL A 1 2567 ? 122.691 179.578 165.614 1.00 93.95  ? 2567 VAL A O     1 
ATOM   7274  C CB    . VAL A 1 2567 ? 120.145 180.323 163.898 1.00 93.95  ? 2567 VAL A CB    1 
ATOM   7275  C CG1   . VAL A 1 2567 ? 120.378 178.871 163.532 1.00 93.95  ? 2567 VAL A CG1   1 
ATOM   7276  C CG2   . VAL A 1 2567 ? 119.264 180.436 165.131 1.00 93.95  ? 2567 VAL A CG2   1 
ATOM   7277  N N     . VAL A 1 2568 ? 121.968 181.542 166.446 1.00 81.94  ? 2568 VAL A N     1 
ATOM   7278  C CA    . VAL A 1 2568 ? 122.458 181.299 167.796 1.00 81.94  ? 2568 VAL A CA    1 
ATOM   7279  C C     . VAL A 1 2568 ? 121.308 181.489 168.772 1.00 81.94  ? 2568 VAL A C     1 
ATOM   7280  O O     . VAL A 1 2568 ? 120.607 182.505 168.725 1.00 81.94  ? 2568 VAL A O     1 
ATOM   7281  C CB    . VAL A 1 2568 ? 123.635 182.224 168.154 1.00 81.94  ? 2568 VAL A CB    1 
ATOM   7282  C CG1   . VAL A 1 2568 ? 123.290 183.664 167.842 1.00 81.94  ? 2568 VAL A CG1   1 
ATOM   7283  C CG2   . VAL A 1 2568 ? 123.993 182.072 169.618 1.00 81.94  ? 2568 VAL A CG2   1 
ATOM   7284  N N     . VAL A 1 2569 ? 121.107 180.512 169.644 1.00 82.75  ? 2569 VAL A N     1 
ATOM   7285  C CA    . VAL A 1 2569 ? 120.071 180.569 170.670 1.00 82.75  ? 2569 VAL A CA    1 
ATOM   7286  C C     . VAL A 1 2569 ? 120.721 181.050 171.962 1.00 82.75  ? 2569 VAL A C     1 
ATOM   7287  O O     . VAL A 1 2569 ? 121.636 180.381 172.463 1.00 82.75  ? 2569 VAL A O     1 
ATOM   7288  C CB    . VAL A 1 2569 ? 119.396 179.207 170.869 1.00 82.75  ? 2569 VAL A CB    1 
ATOM   7289  C CG1   . VAL A 1 2569 ? 118.512 179.232 172.103 1.00 82.75  ? 2569 VAL A CG1   1 
ATOM   7290  C CG2   . VAL A 1 2569 ? 118.595 178.832 169.638 1.00 82.75  ? 2569 VAL A CG2   1 
ATOM   7291  N N     . PRO A 1 2570 ? 120.304 182.185 172.515 1.00 78.85  ? 2570 PRO A N     1 
ATOM   7292  C CA    . PRO A 1 2570 ? 120.929 182.675 173.746 1.00 78.85  ? 2570 PRO A CA    1 
ATOM   7293  C C     . PRO A 1 2570 ? 120.792 181.676 174.882 1.00 78.85  ? 2570 PRO A C     1 
ATOM   7294  O O     . PRO A 1 2570 ? 119.769 181.006 175.029 1.00 78.85  ? 2570 PRO A O     1 
ATOM   7295  C CB    . PRO A 1 2570 ? 120.162 183.966 174.040 1.00 78.85  ? 2570 PRO A CB    1 
ATOM   7296  C CG    . PRO A 1 2570 ? 119.663 184.408 172.718 1.00 78.85  ? 2570 PRO A CG    1 
ATOM   7297  C CD    . PRO A 1 2570 ? 119.360 183.159 171.950 1.00 78.85  ? 2570 PRO A CD    1 
ATOM   7298  N N     . THR A 1 2571 ? 121.845 181.584 175.685 1.00 83.22  ? 2571 THR A N     1 
ATOM   7299  C CA    . THR A 1 2571 ? 121.854 180.733 176.862 1.00 83.22  ? 2571 THR A CA    1 
ATOM   7300  C C     . THR A 1 2571 ? 122.756 181.375 177.902 1.00 83.22  ? 2571 THR A C     1 
ATOM   7301  O O     . THR A 1 2571 ? 123.394 182.400 177.650 1.00 83.22  ? 2571 THR A O     1 
ATOM   7302  C CB    . THR A 1 2571 ? 122.324 179.318 176.531 1.00 83.22  ? 2571 THR A CB    1 
ATOM   7303  O OG1   . THR A 1 2571 ? 122.259 178.507 177.710 1.00 83.22  ? 2571 THR A OG1   1 
ATOM   7304  C CG2   . THR A 1 2571 ? 123.749 179.347 176.019 1.00 83.22  ? 2571 THR A CG2   1 
ATOM   7305  N N     . LEU A 1 2572 ? 122.811 180.754 179.080 1.00 83.29  ? 2572 LEU A N     1 
ATOM   7306  C CA    . LEU A 1 2572 ? 123.569 181.345 180.178 1.00 83.29  ? 2572 LEU A CA    1 
ATOM   7307  C C     . LEU A 1 2572 ? 125.048 181.455 179.828 1.00 83.29  ? 2572 LEU A C     1 
ATOM   7308  O O     . LEU A 1 2572 ? 125.689 182.470 180.126 1.00 83.29  ? 2572 LEU A O     1 
ATOM   7309  C CB    . LEU A 1 2572 ? 123.339 180.543 181.459 1.00 83.29  ? 2572 LEU A CB    1 
ATOM   7310  C CG    . LEU A 1 2572 ? 123.725 179.068 181.555 1.00 83.29  ? 2572 LEU A CG    1 
ATOM   7311  C CD1   . LEU A 1 2572 ? 125.167 178.895 181.994 1.00 83.29  ? 2572 LEU A CD1   1 
ATOM   7312  C CD2   . LEU A 1 2572 ? 122.783 178.339 182.495 1.00 83.29  ? 2572 LEU A CD2   1 
ATOM   7313  N N     . ASP A 1 2573 ? 125.600 180.435 179.168 1.00 87.09  ? 2573 ASP A N     1 
ATOM   7314  C CA    . ASP A 1 2573 ? 126.961 180.545 178.655 1.00 87.09  ? 2573 ASP A CA    1 
ATOM   7315  C C     . ASP A 1 2573 ? 127.080 181.705 177.678 1.00 87.09  ? 2573 ASP A C     1 
ATOM   7316  O O     . ASP A 1 2573 ? 127.995 182.530 177.782 1.00 87.09  ? 2573 ASP A O     1 
ATOM   7317  C CB    . ASP A 1 2573 ? 127.378 179.238 177.984 1.00 87.09  ? 2573 ASP A CB    1 
ATOM   7318  C CG    . ASP A 1 2573 ? 127.726 178.158 178.980 1.00 87.09  ? 2573 ASP A CG    1 
ATOM   7319  O OD1   . ASP A 1 2573 ? 127.742 178.452 180.191 1.00 87.09  ? 2573 ASP A OD1   1 
ATOM   7320  O OD2   . ASP A 1 2573 ? 127.986 177.016 178.552 1.00 87.09  ? 2573 ASP A OD2   1 
ATOM   7321  N N     . THR A 1 2574 ? 126.155 181.787 176.723 1.00 84.78  ? 2574 THR A N     1 
ATOM   7322  C CA    . THR A 1 2574 ? 126.195 182.875 175.756 1.00 84.78  ? 2574 THR A CA    1 
ATOM   7323  C C     . THR A 1 2574 ? 125.952 184.221 176.424 1.00 84.78  ? 2574 THR A C     1 
ATOM   7324  O O     . THR A 1 2574 ? 126.620 185.209 176.101 1.00 84.78  ? 2574 THR A O     1 
ATOM   7325  C CB    . THR A 1 2574 ? 125.169 182.633 174.654 1.00 84.78  ? 2574 THR A CB    1 
ATOM   7326  O OG1   . THR A 1 2574 ? 125.474 181.403 173.988 1.00 84.78  ? 2574 THR A OG1   1 
ATOM   7327  C CG2   . THR A 1 2574 ? 125.199 183.769 173.646 1.00 84.78  ? 2574 THR A CG2   1 
ATOM   7328  N N     . VAL A 1 2575 ? 124.995 184.285 177.353 1.00 84.95  ? 2575 VAL A N     1 
ATOM   7329  C CA    . VAL A 1 2575 ? 124.674 185.557 177.985 1.00 84.95  ? 2575 VAL A CA    1 
ATOM   7330  C C     . VAL A 1 2575 ? 125.792 186.029 178.902 1.00 84.95  ? 2575 VAL A C     1 
ATOM   7331  O O     . VAL A 1 2575 ? 125.871 187.223 179.211 1.00 84.95  ? 2575 VAL A O     1 
ATOM   7332  C CB    . VAL A 1 2575 ? 123.337 185.461 178.740 1.00 84.95  ? 2575 VAL A CB    1 
ATOM   7333  C CG1   . VAL A 1 2575 ? 123.550 184.926 180.134 1.00 84.95  ? 2575 VAL A CG1   1 
ATOM   7334  C CG2   . VAL A 1 2575 ? 122.661 186.816 178.785 1.00 84.95  ? 2575 VAL A CG2   1 
ATOM   7335  N N     . ARG A 1 2576 ? 126.665 185.127 179.352 1.00 82.76  ? 2576 ARG A N     1 
ATOM   7336  C CA    . ARG A 1 2576 ? 127.835 185.561 180.105 1.00 82.76  ? 2576 ARG A CA    1 
ATOM   7337  C C     . ARG A 1 2576 ? 128.976 185.951 179.176 1.00 82.76  ? 2576 ARG A C     1 
ATOM   7338  O O     . ARG A 1 2576 ? 129.674 186.948 179.415 1.00 82.76  ? 2576 ARG A O     1 
ATOM   7339  C CB    . ARG A 1 2576 ? 128.285 184.452 181.051 1.00 82.76  ? 2576 ARG A CB    1 
ATOM   7340  C CG    . ARG A 1 2576 ? 127.478 184.362 182.317 1.00 82.76  ? 2576 ARG A CG    1 
ATOM   7341  C CD    . ARG A 1 2576 ? 127.986 183.238 183.189 1.00 82.76  ? 2576 ARG A CD    1 
ATOM   7342  N NE    . ARG A 1 2576 ? 128.341 182.070 182.395 1.00 82.76  ? 2576 ARG A NE    1 
ATOM   7343  C CZ    . ARG A 1 2576 ? 128.516 180.854 182.892 1.00 82.76  ? 2576 ARG A CZ    1 
ATOM   7344  N NH1   . ARG A 1 2576 ? 128.367 180.606 184.183 1.00 82.76  ? 2576 ARG A NH1   1 
ATOM   7345  N NH2   . ARG A 1 2576 ? 128.846 179.860 182.073 1.00 82.76  ? 2576 ARG A NH2   1 
ATOM   7346  N N     . HIS A 1 2577 ? 129.179 185.169 178.117 1.00 81.00  ? 2577 HIS A N     1 
ATOM   7347  C CA    . HIS A 1 2577 ? 130.290 185.429 177.216 1.00 81.00  ? 2577 HIS A CA    1 
ATOM   7348  C C     . HIS A 1 2577 ? 130.090 186.728 176.453 1.00 81.00  ? 2577 HIS A C     1 
ATOM   7349  O O     . HIS A 1 2577 ? 131.059 187.439 176.181 1.00 81.00  ? 2577 HIS A O     1 
ATOM   7350  C CB    . HIS A 1 2577 ? 130.475 184.254 176.263 1.00 81.00  ? 2577 HIS A CB    1 
ATOM   7351  C CG    . HIS A 1 2577 ? 130.921 182.999 176.943 1.00 81.00  ? 2577 HIS A CG    1 
ATOM   7352  N ND1   . HIS A 1 2577 ? 131.173 182.938 178.296 1.00 81.00  ? 2577 HIS A ND1   1 
ATOM   7353  C CD2   . HIS A 1 2577 ? 131.161 181.758 176.459 1.00 81.00  ? 2577 HIS A CD2   1 
ATOM   7354  C CE1   . HIS A 1 2577 ? 131.548 181.713 178.616 1.00 81.00  ? 2577 HIS A CE1   1 
ATOM   7355  N NE2   . HIS A 1 2577 ? 131.550 180.977 177.520 1.00 81.00  ? 2577 HIS A NE2   1 
ATOM   7356  N N     . GLU A 1 2578 ? 128.847 187.068 176.107 1.00 85.50  ? 2578 GLU A N     1 
ATOM   7357  C CA    . GLU A 1 2578 ? 128.614 188.350 175.449 1.00 85.50  ? 2578 GLU A CA    1 
ATOM   7358  C C     . GLU A 1 2578 ? 128.940 189.511 176.379 1.00 85.50  ? 2578 GLU A C     1 
ATOM   7359  O O     . GLU A 1 2578 ? 129.506 190.521 175.945 1.00 85.50  ? 2578 GLU A O     1 
ATOM   7360  C CB    . GLU A 1 2578 ? 127.172 188.450 174.953 1.00 85.50  ? 2578 GLU A CB    1 
ATOM   7361  C CG    . GLU A 1 2578 ? 126.112 188.279 176.023 1.00 85.50  ? 2578 GLU A CG    1 
ATOM   7362  C CD    . GLU A 1 2578 ? 124.725 188.100 175.441 1.00 85.50  ? 2578 GLU A CD    1 
ATOM   7363  O OE1   . GLU A 1 2578 ? 124.035 189.119 175.229 1.00 85.50  ? 2578 GLU A OE1   1 
ATOM   7364  O OE2   . GLU A 1 2578 ? 124.329 186.945 175.182 1.00 85.50  ? 2578 GLU A OE2   1 
ATOM   7365  N N     . ALA A 1 2579 ? 128.593 189.388 177.661 1.00 82.92  ? 2579 ALA A N     1 
ATOM   7366  C CA    . ALA A 1 2579 ? 128.901 190.448 178.613 1.00 82.92  ? 2579 ALA A CA    1 
ATOM   7367  C C     . ALA A 1 2579 ? 130.405 190.628 178.758 1.00 82.92  ? 2579 ALA A C     1 
ATOM   7368  O O     . ALA A 1 2579 ? 130.920 191.751 178.687 1.00 82.92  ? 2579 ALA A O     1 
ATOM   7369  C CB    . ALA A 1 2579 ? 128.261 190.141 179.965 1.00 82.92  ? 2579 ALA A CB    1 
ATOM   7370  N N     . LEU A 1 2580 ? 131.130 189.523 178.947 1.00 78.00  ? 2580 LEU A N     1 
ATOM   7371  C CA    . LEU A 1 2580 ? 132.582 189.622 179.064 1.00 78.00  ? 2580 LEU A CA    1 
ATOM   7372  C C     . LEU A 1 2580 ? 133.201 190.155 177.778 1.00 78.00  ? 2580 LEU A C     1 
ATOM   7373  O O     . LEU A 1 2580 ? 134.151 190.947 177.815 1.00 78.00  ? 2580 LEU A O     1 
ATOM   7374  C CB    . LEU A 1 2580 ? 133.181 188.267 179.425 1.00 78.00  ? 2580 LEU A CB    1 
ATOM   7375  C CG    . LEU A 1 2580 ? 132.669 187.653 180.725 1.00 78.00  ? 2580 LEU A CG    1 
ATOM   7376  C CD1   . LEU A 1 2580 ? 133.291 186.288 180.944 1.00 78.00  ? 2580 LEU A CD1   1 
ATOM   7377  C CD2   . LEU A 1 2580 ? 132.962 188.572 181.893 1.00 78.00  ? 2580 LEU A CD2   1 
ATOM   7378  N N     . LEU A 1 2581 ? 132.674 189.731 176.631 1.00 78.89  ? 2581 LEU A N     1 
ATOM   7379  C CA    . LEU A 1 2581 ? 133.176 190.203 175.350 1.00 78.89  ? 2581 LEU A CA    1 
ATOM   7380  C C     . LEU A 1 2581 ? 133.014 191.707 175.218 1.00 78.89  ? 2581 LEU A C     1 
ATOM   7381  O O     . LEU A 1 2581 ? 133.953 192.411 174.838 1.00 78.89  ? 2581 LEU A O     1 
ATOM   7382  C CB    . LEU A 1 2581 ? 132.437 189.492 174.224 1.00 78.89  ? 2581 LEU A CB    1 
ATOM   7383  C CG    . LEU A 1 2581 ? 133.043 189.552 172.829 1.00 78.89  ? 2581 LEU A CG    1 
ATOM   7384  C CD1   . LEU A 1 2581 ? 134.551 189.532 172.894 1.00 78.89  ? 2581 LEU A CD1   1 
ATOM   7385  C CD2   . LEU A 1 2581 ? 132.519 188.400 172.022 1.00 78.89  ? 2581 LEU A CD2   1 
ATOM   7386  N N     . TYR A 1 2582 ? 131.819 192.217 175.512 1.00 84.28  ? 2582 TYR A N     1 
ATOM   7387  C CA    . TYR A 1 2582 ? 131.594 193.655 175.426 1.00 84.28  ? 2582 TYR A CA    1 
ATOM   7388  C C     . TYR A 1 2582 ? 132.504 194.398 176.389 1.00 84.28  ? 2582 TYR A C     1 
ATOM   7389  O O     . TYR A 1 2582 ? 133.083 195.437 176.040 1.00 84.28  ? 2582 TYR A O     1 
ATOM   7390  C CB    . TYR A 1 2582 ? 130.127 193.967 175.709 1.00 84.28  ? 2582 TYR A CB    1 
ATOM   7391  C CG    . TYR A 1 2582 ? 129.181 193.410 174.670 1.00 84.28  ? 2582 TYR A CG    1 
ATOM   7392  C CD1   . TYR A 1 2582 ? 129.628 193.103 173.394 1.00 84.28  ? 2582 TYR A CD1   1 
ATOM   7393  C CD2   . TYR A 1 2582 ? 127.847 193.179 174.969 1.00 84.28  ? 2582 TYR A CD2   1 
ATOM   7394  C CE1   . TYR A 1 2582 ? 128.773 192.593 172.441 1.00 84.28  ? 2582 TYR A CE1   1 
ATOM   7395  C CE2   . TYR A 1 2582 ? 126.984 192.667 174.021 1.00 84.28  ? 2582 TYR A CE2   1 
ATOM   7396  C CZ    . TYR A 1 2582 ? 127.453 192.376 172.759 1.00 84.28  ? 2582 TYR A CZ    1 
ATOM   7397  O OH    . TYR A 1 2582 ? 126.602 191.866 171.808 1.00 84.28  ? 2582 TYR A OH    1 
ATOM   7398  N N     . THR A 1 2583 ? 132.666 193.858 177.597 1.00 77.72  ? 2583 THR A N     1 
ATOM   7399  C CA    . THR A 1 2583 ? 133.554 194.471 178.574 1.00 77.72  ? 2583 THR A CA    1 
ATOM   7400  C C     . THR A 1 2583 ? 134.965 194.613 178.023 1.00 77.72  ? 2583 THR A C     1 
ATOM   7401  O O     . THR A 1 2583 ? 135.556 195.697 178.064 1.00 77.72  ? 2583 THR A O     1 
ATOM   7402  C CB    . THR A 1 2583 ? 133.572 193.635 179.848 1.00 77.72  ? 2583 THR A CB    1 
ATOM   7403  O OG1   . THR A 1 2583 ? 132.371 193.863 180.594 1.00 77.72  ? 2583 THR A OG1   1 
ATOM   7404  C CG2   . THR A 1 2583 ? 134.760 194.010 180.682 1.00 77.72  ? 2583 THR A CG2   1 
ATOM   7405  N N     . TRP A 1 2584 ? 135.519 193.526 177.493 1.00 69.77  ? 2584 TRP A N     1 
ATOM   7406  C CA    . TRP A 1 2584 ? 136.910 193.552 177.067 1.00 69.77  ? 2584 TRP A CA    1 
ATOM   7407  C C     . TRP A 1 2584 ? 137.107 194.228 175.721 1.00 69.77  ? 2584 TRP A C     1 
ATOM   7408  O O     . TRP A 1 2584 ? 138.231 194.632 175.409 1.00 69.77  ? 2584 TRP A O     1 
ATOM   7409  C CB    . TRP A 1 2584 ? 137.472 192.135 177.025 1.00 69.77  ? 2584 TRP A CB    1 
ATOM   7410  C CG    . TRP A 1 2584 ? 137.828 191.642 178.376 1.00 69.77  ? 2584 TRP A CG    1 
ATOM   7411  C CD1   . TRP A 1 2584 ? 138.040 192.395 179.486 1.00 69.77  ? 2584 TRP A CD1   1 
ATOM   7412  C CD2   . TRP A 1 2584 ? 137.986 190.282 178.775 1.00 69.77  ? 2584 TRP A CD2   1 
ATOM   7413  N NE1   . TRP A 1 2584 ? 138.336 191.589 180.554 1.00 69.77  ? 2584 TRP A NE1   1 
ATOM   7414  C CE2   . TRP A 1 2584 ? 138.305 190.285 180.142 1.00 69.77  ? 2584 TRP A CE2   1 
ATOM   7415  C CE3   . TRP A 1 2584 ? 137.893 189.062 178.107 1.00 69.77  ? 2584 TRP A CE3   1 
ATOM   7416  C CZ2   . TRP A 1 2584 ? 138.533 189.118 180.852 1.00 69.77  ? 2584 TRP A CZ2   1 
ATOM   7417  C CZ3   . TRP A 1 2584 ? 138.118 187.906 178.813 1.00 69.77  ? 2584 TRP A CZ3   1 
ATOM   7418  C CH2   . TRP A 1 2584 ? 138.434 187.940 180.172 1.00 69.77  ? 2584 TRP A CH2   1 
ATOM   7419  N N     . LEU A 1 2585 ? 136.058 194.363 174.917 1.00 77.16  ? 2585 LEU A N     1 
ATOM   7420  C CA    . LEU A 1 2585 ? 136.175 195.142 173.696 1.00 77.16  ? 2585 LEU A CA    1 
ATOM   7421  C C     . LEU A 1 2585 ? 135.969 196.626 173.934 1.00 77.16  ? 2585 LEU A C     1 
ATOM   7422  O O     . LEU A 1 2585 ? 136.318 197.432 173.065 1.00 77.16  ? 2585 LEU A O     1 
ATOM   7423  C CB    . LEU A 1 2585 ? 135.175 194.662 172.644 1.00 77.16  ? 2585 LEU A CB    1 
ATOM   7424  C CG    . LEU A 1 2585 ? 135.255 193.200 172.218 1.00 77.16  ? 2585 LEU A CG    1 
ATOM   7425  C CD1   . LEU A 1 2585 ? 133.960 192.800 171.538 1.00 77.16  ? 2585 LEU A CD1   1 
ATOM   7426  C CD2   . LEU A 1 2585 ? 136.451 192.945 171.322 1.00 77.16  ? 2585 LEU A CD2   1 
ATOM   7427  N N     . ALA A 1 2586 ? 135.410 197.007 175.083 1.00 79.13  ? 2586 ALA A N     1 
ATOM   7428  C CA    . ALA A 1 2586 ? 135.329 198.427 175.400 1.00 79.13  ? 2586 ALA A CA    1 
ATOM   7429  C C     . ALA A 1 2586 ? 136.713 199.048 175.529 1.00 79.13  ? 2586 ALA A C     1 
ATOM   7430  O O     . ALA A 1 2586 ? 136.887 200.237 175.245 1.00 79.13  ? 2586 ALA A O     1 
ATOM   7431  C CB    . ALA A 1 2586 ? 134.529 198.634 176.683 1.00 79.13  ? 2586 ALA A CB    1 
ATOM   7432  N N     . GLU A 1 2587 ? 137.705 198.264 175.946 1.00 78.44  ? 2587 GLU A N     1 
ATOM   7433  C CA    . GLU A 1 2587 ? 139.073 198.740 176.097 1.00 78.44  ? 2587 GLU A CA    1 
ATOM   7434  C C     . GLU A 1 2587 ? 139.968 198.345 174.931 1.00 78.44  ? 2587 GLU A C     1 
ATOM   7435  O O     . GLU A 1 2587 ? 141.182 198.557 174.998 1.00 78.44  ? 2587 GLU A O     1 
ATOM   7436  C CB    . GLU A 1 2587 ? 139.671 198.218 177.403 1.00 78.44  ? 2587 GLU A CB    1 
ATOM   7437  C CG    . GLU A 1 2587 ? 138.862 198.565 178.634 1.00 78.44  ? 2587 GLU A CG    1 
ATOM   7438  C CD    . GLU A 1 2587 ? 139.560 199.575 179.519 1.00 78.44  ? 2587 GLU A CD    1 
ATOM   7439  O OE1   . GLU A 1 2587 ? 140.763 199.396 179.795 1.00 78.44  ? 2587 GLU A OE1   1 
ATOM   7440  O OE2   . GLU A 1 2587 ? 138.906 200.551 179.938 1.00 78.44  ? 2587 GLU A OE2   1 
ATOM   7441  N N     . HIS A 1 2588 ? 139.400 197.768 173.872 1.00 76.89  ? 2588 HIS A N     1 
ATOM   7442  C CA    . HIS A 1 2588 ? 140.146 197.317 172.699 1.00 76.89  ? 2588 HIS A CA    1 
ATOM   7443  C C     . HIS A 1 2588 ? 141.209 196.288 173.055 1.00 76.89  ? 2588 HIS A C     1 
ATOM   7444  O O     . HIS A 1 2588 ? 142.208 196.149 172.345 1.00 76.89  ? 2588 HIS A O     1 
ATOM   7445  C CB    . HIS A 1 2588 ? 140.777 198.497 171.958 1.00 76.89  ? 2588 HIS A CB    1 
ATOM   7446  C CG    . HIS A 1 2588 ? 139.951 199.742 172.007 1.00 76.89  ? 2588 HIS A CG    1 
ATOM   7447  N ND1   . HIS A 1 2588 ? 140.460 200.958 172.405 1.00 76.89  ? 2588 HIS A ND1   1 
ATOM   7448  C CD2   . HIS A 1 2588 ? 138.645 199.956 171.722 1.00 76.89  ? 2588 HIS A CD2   1 
ATOM   7449  C CE1   . HIS A 1 2588 ? 139.505 201.870 172.356 1.00 76.89  ? 2588 HIS A CE1   1 
ATOM   7450  N NE2   . HIS A 1 2588 ? 138.394 201.287 171.945 1.00 76.89  ? 2588 HIS A NE2   1 
ATOM   7451  N N     . LYS A 1 2589 ? 141.008 195.570 174.150 1.00 71.97  ? 2589 LYS A N     1 
ATOM   7452  C CA    . LYS A 1 2589 ? 141.938 194.530 174.559 1.00 71.97  ? 2589 LYS A CA    1 
ATOM   7453  C C     . LYS A 1 2589 ? 141.649 193.251 173.787 1.00 71.97  ? 2589 LYS A C     1 
ATOM   7454  O O     . LYS A 1 2589 ? 140.511 192.772 173.810 1.00 71.97  ? 2589 LYS A O     1 
ATOM   7455  C CB    . LYS A 1 2589 ? 141.823 194.274 176.054 1.00 71.97  ? 2589 LYS A CB    1 
ATOM   7456  C CG    . LYS A 1 2589 ? 142.936 193.427 176.625 1.00 71.97  ? 2589 LYS A CG    1 
ATOM   7457  C CD    . LYS A 1 2589 ? 142.911 193.457 178.137 1.00 71.97  ? 2589 LYS A CD    1 
ATOM   7458  C CE    . LYS A 1 2589 ? 142.925 194.881 178.651 1.00 71.97  ? 2589 LYS A CE    1 
ATOM   7459  N NZ    . LYS A 1 2589 ? 144.201 195.566 178.328 1.00 71.97  ? 2589 LYS A NZ    1 
ATOM   7460  N N     . PRO A 1 2590 ? 142.625 192.678 173.094 1.00 65.57  ? 2590 PRO A N     1 
ATOM   7461  C CA    . PRO A 1 2590 ? 142.384 191.411 172.403 1.00 65.57  ? 2590 PRO A CA    1 
ATOM   7462  C C     . PRO A 1 2590 ? 142.130 190.292 173.394 1.00 65.57  ? 2590 PRO A C     1 
ATOM   7463  O O     . PRO A 1 2590 ? 142.685 190.269 174.493 1.00 65.57  ? 2590 PRO A O     1 
ATOM   7464  C CB    . PRO A 1 2590 ? 143.681 191.172 171.623 1.00 65.57  ? 2590 PRO A CB    1 
ATOM   7465  C CG    . PRO A 1 2590 ? 144.468 192.427 171.752 1.00 65.57  ? 2590 PRO A CG    1 
ATOM   7466  C CD    . PRO A 1 2590 ? 144.023 193.106 172.988 1.00 65.57  ? 2590 PRO A CD    1 
ATOM   7467  N N     . LEU A 1 2591 ? 141.281 189.353 172.992 1.00 60.89  ? 2591 LEU A N     1 
ATOM   7468  C CA    . LEU A 1 2591 ? 140.940 188.227 173.845 1.00 60.89  ? 2591 LEU A CA    1 
ATOM   7469  C C     . LEU A 1 2591 ? 140.881 186.962 173.008 1.00 60.89  ? 2591 LEU A C     1 
ATOM   7470  O O     . LEU A 1 2591 ? 140.676 187.001 171.794 1.00 60.89  ? 2591 LEU A O     1 
ATOM   7471  C CB    . LEU A 1 2591 ? 139.609 188.438 174.568 1.00 60.89  ? 2591 LEU A CB    1 
ATOM   7472  C CG    . LEU A 1 2591 ? 138.367 187.962 173.825 1.00 60.89  ? 2591 LEU A CG    1 
ATOM   7473  C CD1   . LEU A 1 2591 ? 137.193 187.898 174.774 1.00 60.89  ? 2591 LEU A CD1   1 
ATOM   7474  C CD2   . LEU A 1 2591 ? 138.069 188.891 172.674 1.00 60.89  ? 2591 LEU A CD2   1 
ATOM   7475  N N     . VAL A 1 2592 ? 141.064 185.832 173.680 1.00 61.56  ? 2592 VAL A N     1 
ATOM   7476  C CA    . VAL A 1 2592 ? 141.066 184.526 173.041 1.00 61.56  ? 2592 VAL A CA    1 
ATOM   7477  C C     . VAL A 1 2592 ? 140.062 183.644 173.762 1.00 61.56  ? 2592 VAL A C     1 
ATOM   7478  O O     . VAL A 1 2592 ? 140.101 183.530 174.991 1.00 61.56  ? 2592 VAL A O     1 
ATOM   7479  C CB    . VAL A 1 2592 ? 142.464 183.883 173.063 1.00 61.56  ? 2592 VAL A CB    1 
ATOM   7480  C CG1   . VAL A 1 2592 ? 142.399 182.457 172.564 1.00 61.56  ? 2592 VAL A CG1   1 
ATOM   7481  C CG2   . VAL A 1 2592 ? 143.427 184.694 172.227 1.00 61.56  ? 2592 VAL A CG2   1 
ATOM   7482  N N     . LEU A 1 2593 ? 139.164 183.028 173.005 1.00 62.70  ? 2593 LEU A N     1 
ATOM   7483  C CA    . LEU A 1 2593 ? 138.217 182.064 173.544 1.00 62.70  ? 2593 LEU A CA    1 
ATOM   7484  C C     . LEU A 1 2593 ? 138.788 180.674 173.306 1.00 62.70  ? 2593 LEU A C     1 
ATOM   7485  O O     . LEU A 1 2593 ? 138.933 180.245 172.158 1.00 62.70  ? 2593 LEU A O     1 
ATOM   7486  C CB    . LEU A 1 2593 ? 136.849 182.218 172.888 1.00 62.70  ? 2593 LEU A CB    1 
ATOM   7487  C CG    . LEU A 1 2593 ? 136.128 183.531 173.174 1.00 62.70  ? 2593 LEU A CG    1 
ATOM   7488  C CD1   . LEU A 1 2593 ? 134.729 183.504 172.602 1.00 62.70  ? 2593 LEU A CD1   1 
ATOM   7489  C CD2   . LEU A 1 2593 ? 136.088 183.793 174.663 1.00 62.70  ? 2593 LEU A CD2   1 
ATOM   7490  N N     . CYS A 1 2594 ? 139.123 179.976 174.384 1.00 65.32  ? 2594 CYS A N     1 
ATOM   7491  C CA    . CYS A 1 2594 ? 139.704 178.644 174.301 1.00 65.32  ? 2594 CYS A CA    1 
ATOM   7492  C C     . CYS A 1 2594 ? 138.702 177.622 174.813 1.00 65.32  ? 2594 CYS A C     1 
ATOM   7493  O O     . CYS A 1 2594 ? 138.082 177.827 175.861 1.00 65.32  ? 2594 CYS A O     1 
ATOM   7494  C CB    . CYS A 1 2594 ? 141.004 178.562 175.099 1.00 65.32  ? 2594 CYS A CB    1 
ATOM   7495  S SG    . CYS A 1 2594 ? 142.000 177.114 174.716 1.00 65.32  ? 2594 CYS A SG    1 
ATOM   7496  N N     . GLY A 1 2595 ? 138.539 176.530 174.072 1.00 74.13  ? 2595 GLY A N     1 
ATOM   7497  C CA    . GLY A 1 2595 ? 137.625 175.483 174.456 1.00 74.13  ? 2595 GLY A CA    1 
ATOM   7498  C C     . GLY A 1 2595 ? 137.717 174.267 173.559 1.00 74.13  ? 2595 GLY A C     1 
ATOM   7499  O O     . GLY A 1 2595 ? 138.321 174.303 172.484 1.00 74.13  ? 2595 GLY A O     1 
ATOM   7500  N N     . PRO A 1 2596 ? 137.108 173.164 173.987 1.00 73.78  ? 2596 PRO A N     1 
ATOM   7501  C CA    . PRO A 1 2596 ? 137.152 171.951 173.182 1.00 73.78  ? 2596 PRO A CA    1 
ATOM   7502  C C     . PRO A 1 2596 ? 136.415 172.158 171.876 1.00 73.78  ? 2596 PRO A C     1 
ATOM   7503  O O     . PRO A 1 2596 ? 135.532 173.030 171.773 1.00 73.78  ? 2596 PRO A O     1 
ATOM   7504  C CB    . PRO A 1 2596 ? 136.448 170.913 174.067 1.00 73.78  ? 2596 PRO A CB    1 
ATOM   7505  C CG    . PRO A 1 2596 ? 136.461 171.494 175.437 1.00 73.78  ? 2596 PRO A CG    1 
ATOM   7506  C CD    . PRO A 1 2596 ? 136.372 172.966 175.243 1.00 73.78  ? 2596 PRO A CD    1 
ATOM   7507  N N     . PRO A 1 2597 ? 136.756 171.393 170.841 1.00 75.85  ? 2597 PRO A N     1 
ATOM   7508  C CA    . PRO A 1 2597 ? 136.115 171.594 169.538 1.00 75.85  ? 2597 PRO A CA    1 
ATOM   7509  C C     . PRO A 1 2597 ? 134.611 171.405 169.629 1.00 75.85  ? 2597 PRO A C     1 
ATOM   7510  O O     . PRO A 1 2597 ? 134.115 170.552 170.367 1.00 75.85  ? 2597 PRO A O     1 
ATOM   7511  C CB    . PRO A 1 2597 ? 136.764 170.526 168.652 1.00 75.85  ? 2597 PRO A CB    1 
ATOM   7512  C CG    . PRO A 1 2597 ? 138.031 170.175 169.340 1.00 75.85  ? 2597 PRO A CG    1 
ATOM   7513  C CD    . PRO A 1 2597 ? 137.755 170.315 170.801 1.00 75.85  ? 2597 PRO A CD    1 
ATOM   7514  N N     . GLY A 1 2598 ? 133.885 172.226 168.878 1.00 80.38  ? 2598 GLY A N     1 
ATOM   7515  C CA    . GLY A 1 2598 ? 132.443 172.143 168.867 1.00 80.38  ? 2598 GLY A CA    1 
ATOM   7516  C C     . GLY A 1 2598 ? 131.758 172.753 170.063 1.00 80.38  ? 2598 GLY A C     1 
ATOM   7517  O O     . GLY A 1 2598 ? 130.546 172.578 170.216 1.00 80.38  ? 2598 GLY A O     1 
ATOM   7518  N N     . SER A 1 2599 ? 132.488 173.466 170.919 1.00 75.98  ? 2599 SER A N     1 
ATOM   7519  C CA    . SER A 1 2599 ? 131.871 174.078 172.087 1.00 75.98  ? 2599 SER A CA    1 
ATOM   7520  C C     . SER A 1 2599 ? 131.042 175.304 171.742 1.00 75.98  ? 2599 SER A C     1 
ATOM   7521  O O     . SER A 1 2599 ? 130.346 175.824 172.618 1.00 75.98  ? 2599 SER A O     1 
ATOM   7522  C CB    . SER A 1 2599 ? 132.939 174.457 173.107 1.00 75.98  ? 2599 SER A CB    1 
ATOM   7523  O OG    . SER A 1 2599 ? 132.400 174.477 174.415 1.00 75.98  ? 2599 SER A OG    1 
ATOM   7524  N N     . GLY A 1 2600 ? 131.099 175.780 170.504 1.00 75.85  ? 2600 GLY A N     1 
ATOM   7525  C CA    . GLY A 1 2600 ? 130.341 176.948 170.116 1.00 75.85  ? 2600 GLY A CA    1 
ATOM   7526  C C     . GLY A 1 2600 ? 131.089 178.253 170.207 1.00 75.85  ? 2600 GLY A C     1 
ATOM   7527  O O     . GLY A 1 2600 ? 130.454 179.312 170.234 1.00 75.85  ? 2600 GLY A O     1 
ATOM   7528  N N     . LYS A 1 2601 ? 132.420 178.214 170.264 1.00 72.54  ? 2601 LYS A N     1 
ATOM   7529  C CA    . LYS A 1 2601 ? 133.188 179.447 170.372 1.00 72.54  ? 2601 LYS A CA    1 
ATOM   7530  C C     . LYS A 1 2601 ? 133.006 180.323 169.143 1.00 72.54  ? 2601 LYS A C     1 
ATOM   7531  O O     . LYS A 1 2601 ? 132.746 181.526 169.261 1.00 72.54  ? 2601 LYS A O     1 
ATOM   7532  C CB    . LYS A 1 2601 ? 134.665 179.119 170.568 1.00 72.54  ? 2601 LYS A CB    1 
ATOM   7533  C CG    . LYS A 1 2601 ? 134.930 178.135 171.684 1.00 72.54  ? 2601 LYS A CG    1 
ATOM   7534  C CD    . LYS A 1 2601 ? 136.388 177.728 171.720 1.00 72.54  ? 2601 LYS A CD    1 
ATOM   7535  C CE    . LYS A 1 2601 ? 136.722 176.799 170.579 1.00 72.54  ? 2601 LYS A CE    1 
ATOM   7536  N NZ    . LYS A 1 2601 ? 136.080 175.477 170.773 1.00 72.54  ? 2601 LYS A NZ    1 
ATOM   7537  N N     . THR A 1 2602 ? 133.117 179.730 167.954 1.00 76.94  ? 2602 THR A N     1 
ATOM   7538  C CA    . THR A 1 2602 ? 133.133 180.518 166.728 1.00 76.94  ? 2602 THR A CA    1 
ATOM   7539  C C     . THR A 1 2602 ? 131.835 181.294 166.555 1.00 76.94  ? 2602 THR A C     1 
ATOM   7540  O O     . THR A 1 2602 ? 131.854 182.494 166.266 1.00 76.94  ? 2602 THR A O     1 
ATOM   7541  C CB    . THR A 1 2602 ? 133.378 179.610 165.525 1.00 76.94  ? 2602 THR A CB    1 
ATOM   7542  O OG1   . THR A 1 2602 ? 134.497 178.755 165.787 1.00 76.94  ? 2602 THR A OG1   1 
ATOM   7543  C CG2   . THR A 1 2602 ? 133.676 180.443 164.296 1.00 76.94  ? 2602 THR A CG2   1 
ATOM   7544  N N     . MET A 1 2603 ? 130.694 180.632 166.743 1.00 85.24  ? 2603 MET A N     1 
ATOM   7545  C CA    . MET A 1 2603 ? 129.430 181.311 166.498 1.00 85.24  ? 2603 MET A CA    1 
ATOM   7546  C C     . MET A 1 2603 ? 129.053 182.268 167.617 1.00 85.24  ? 2603 MET A C     1 
ATOM   7547  O O     . MET A 1 2603 ? 128.477 183.325 167.342 1.00 85.24  ? 2603 MET A O     1 
ATOM   7548  C CB    . MET A 1 2603 ? 128.313 180.306 166.254 1.00 85.24  ? 2603 MET A CB    1 
ATOM   7549  C CG    . MET A 1 2603 ? 128.745 179.122 165.436 1.00 85.24  ? 2603 MET A CG    1 
ATOM   7550  S SD    . MET A 1 2603 ? 128.921 179.667 163.729 1.00 85.24  ? 2603 MET A SD    1 
ATOM   7551  C CE    . MET A 1 2603 ? 127.479 180.710 163.572 1.00 85.24  ? 2603 MET A CE    1 
ATOM   7552  N N     . THR A 1 2604 ? 129.349 181.934 168.872 1.00 75.27  ? 2604 THR A N     1 
ATOM   7553  C CA    . THR A 1 2604 ? 129.148 182.916 169.931 1.00 75.27  ? 2604 THR A CA    1 
ATOM   7554  C C     . THR A 1 2604 ? 129.940 184.178 169.634 1.00 75.27  ? 2604 THR A C     1 
ATOM   7555  O O     . THR A 1 2604 ? 129.413 185.295 169.709 1.00 75.27  ? 2604 THR A O     1 
ATOM   7556  C CB    . THR A 1 2604 ? 129.554 182.338 171.284 1.00 75.27  ? 2604 THR A CB    1 
ATOM   7557  O OG1   . THR A 1 2604 ? 128.690 181.246 171.617 1.00 75.27  ? 2604 THR A OG1   1 
ATOM   7558  C CG2   . THR A 1 2604 ? 129.463 183.403 172.360 1.00 75.27  ? 2604 THR A CG2   1 
ATOM   7559  N N     . LEU A 1 2605 ? 131.203 184.008 169.248 1.00 71.23  ? 2605 LEU A N     1 
ATOM   7560  C CA    . LEU A 1 2605 ? 132.048 185.150 168.932 1.00 71.23  ? 2605 LEU A CA    1 
ATOM   7561  C C     . LEU A 1 2605 ? 131.483 185.943 167.761 1.00 71.23  ? 2605 LEU A C     1 
ATOM   7562  O O     . LEU A 1 2605 ? 131.358 187.171 167.831 1.00 71.23  ? 2605 LEU A O     1 
ATOM   7563  C CB    . LEU A 1 2605 ? 133.461 184.656 168.633 1.00 71.23  ? 2605 LEU A CB    1 
ATOM   7564  C CG    . LEU A 1 2605 ? 134.648 185.597 168.777 1.00 71.23  ? 2605 LEU A CG    1 
ATOM   7565  C CD1   . LEU A 1 2605 ? 134.483 186.444 169.995 1.00 71.23  ? 2605 LEU A CD1   1 
ATOM   7566  C CD2   . LEU A 1 2605 ? 135.886 184.760 168.929 1.00 71.23  ? 2605 LEU A CD2   1 
ATOM   7567  N N     . PHE A 1 2606 ? 131.111 185.253 166.680 1.00 74.81  ? 2606 PHE A N     1 
ATOM   7568  C CA    . PHE A 1 2606 ? 130.627 185.942 165.489 1.00 74.81  ? 2606 PHE A CA    1 
ATOM   7569  C C     . PHE A 1 2606 ? 129.337 186.697 165.771 1.00 74.81  ? 2606 PHE A C     1 
ATOM   7570  O O     . PHE A 1 2606 ? 129.182 187.858 165.372 1.00 74.81  ? 2606 PHE A O     1 
ATOM   7571  C CB    . PHE A 1 2606 ? 130.422 184.944 164.352 1.00 74.81  ? 2606 PHE A CB    1 
ATOM   7572  C CG    . PHE A 1 2606 ? 131.490 184.992 163.304 1.00 74.81  ? 2606 PHE A CG    1 
ATOM   7573  C CD1   . PHE A 1 2606 ? 131.843 186.189 162.716 1.00 74.81  ? 2606 PHE A CD1   1 
ATOM   7574  C CD2   . PHE A 1 2606 ? 132.128 183.837 162.892 1.00 74.81  ? 2606 PHE A CD2   1 
ATOM   7575  C CE1   . PHE A 1 2606 ? 132.820 186.235 161.746 1.00 74.81  ? 2606 PHE A CE1   1 
ATOM   7576  C CE2   . PHE A 1 2606 ? 133.106 183.879 161.920 1.00 74.81  ? 2606 PHE A CE2   1 
ATOM   7577  C CZ    . PHE A 1 2606 ? 133.453 185.079 161.348 1.00 74.81  ? 2606 PHE A CZ    1 
ATOM   7578  N N     . SER A 1 2607 ? 128.393 186.054 166.457 1.00 74.59  ? 2607 SER A N     1 
ATOM   7579  C CA    . SER A 1 2607 ? 127.120 186.705 166.728 1.00 74.59  ? 2607 SER A CA    1 
ATOM   7580  C C     . SER A 1 2607 ? 127.297 187.888 167.665 1.00 74.59  ? 2607 SER A C     1 
ATOM   7581  O O     . SER A 1 2607 ? 126.697 188.947 167.450 1.00 74.59  ? 2607 SER A O     1 
ATOM   7582  C CB    . SER A 1 2607 ? 126.134 185.704 167.318 1.00 74.59  ? 2607 SER A CB    1 
ATOM   7583  O OG    . SER A 1 2607 ? 126.077 185.830 168.726 1.00 74.59  ? 2607 SER A OG    1 
ATOM   7584  N N     . ALA A 1 2608 ? 128.119 187.737 168.705 1.00 75.72  ? 2608 ALA A N     1 
ATOM   7585  C CA    . ALA A 1 2608 ? 128.332 188.851 169.618 1.00 75.72  ? 2608 ALA A CA    1 
ATOM   7586  C C     . ALA A 1 2608 ? 129.017 190.012 168.914 1.00 75.72  ? 2608 ALA A C     1 
ATOM   7587  O O     . ALA A 1 2608 ? 128.702 191.177 169.176 1.00 75.72  ? 2608 ALA A O     1 
ATOM   7588  C CB    . ALA A 1 2608 ? 129.146 188.393 170.825 1.00 75.72  ? 2608 ALA A CB    1 
ATOM   7589  N N     . LEU A 1 2609 ? 129.957 189.716 168.014 1.00 75.19  ? 2609 LEU A N     1 
ATOM   7590  C CA    . LEU A 1 2609 ? 130.634 190.783 167.288 1.00 75.19  ? 2609 LEU A CA    1 
ATOM   7591  C C     . LEU A 1 2609 ? 129.686 191.496 166.335 1.00 75.19  ? 2609 LEU A C     1 
ATOM   7592  O O     . LEU A 1 2609 ? 129.721 192.726 166.222 1.00 75.19  ? 2609 LEU A O     1 
ATOM   7593  C CB    . LEU A 1 2609 ? 131.833 190.220 166.532 1.00 75.19  ? 2609 LEU A CB    1 
ATOM   7594  C CG    . LEU A 1 2609 ? 133.176 190.424 167.223 1.00 75.19  ? 2609 LEU A CG    1 
ATOM   7595  C CD1   . LEU A 1 2609 ? 134.299 189.955 166.331 1.00 75.19  ? 2609 LEU A CD1   1 
ATOM   7596  C CD2   . LEU A 1 2609 ? 133.355 191.883 167.577 1.00 75.19  ? 2609 LEU A CD2   1 
ATOM   7597  N N     . ARG A 1 2610 ? 128.827 190.747 165.643 1.00 82.86  ? 2610 ARG A N     1 
ATOM   7598  C CA    . ARG A 1 2610 ? 127.907 191.380 164.707 1.00 82.86  ? 2610 ARG A CA    1 
ATOM   7599  C C     . ARG A 1 2610 ? 126.743 192.060 165.408 1.00 82.86  ? 2610 ARG A C     1 
ATOM   7600  O O     . ARG A 1 2610 ? 126.066 192.888 164.790 1.00 82.86  ? 2610 ARG A O     1 
ATOM   7601  C CB    . ARG A 1 2610 ? 127.385 190.355 163.706 1.00 82.86  ? 2610 ARG A CB    1 
ATOM   7602  C CG    . ARG A 1 2610 ? 128.447 189.863 162.752 1.00 82.86  ? 2610 ARG A CG    1 
ATOM   7603  C CD    . ARG A 1 2610 ? 127.861 189.007 161.657 1.00 82.86  ? 2610 ARG A CD    1 
ATOM   7604  N NE    . ARG A 1 2610 ? 128.884 188.603 160.703 1.00 82.86  ? 2610 ARG A NE    1 
ATOM   7605  C CZ    . ARG A 1 2610 ? 129.242 187.347 160.482 1.00 82.86  ? 2610 ARG A CZ    1 
ATOM   7606  N NH1   . ARG A 1 2610 ? 128.679 186.343 161.134 1.00 82.86  ? 2610 ARG A NH1   1 
ATOM   7607  N NH2   . ARG A 1 2610 ? 130.190 187.091 159.585 1.00 82.86  ? 2610 ARG A NH2   1 
ATOM   7608  N N     . ALA A 1 2611 ? 126.492 191.731 166.677 1.00 87.87  ? 2611 ALA A N     1 
ATOM   7609  C CA    . ALA A 1 2611 ? 125.416 192.391 167.408 1.00 87.87  ? 2611 ALA A CA    1 
ATOM   7610  C C     . ALA A 1 2611 ? 125.684 193.882 167.552 1.00 87.87  ? 2611 ALA A C     1 
ATOM   7611  O O     . ALA A 1 2611 ? 124.773 194.703 167.392 1.00 87.87  ? 2611 ALA A O     1 
ATOM   7612  C CB    . ALA A 1 2611 ? 125.238 191.742 168.779 1.00 87.87  ? 2611 ALA A CB    1 
ATOM   7613  N N     . LEU A 1 2612 ? 126.922 194.252 167.860 1.00 93.31  ? 2612 LEU A N     1 
ATOM   7614  C CA    . LEU A 1 2612 ? 127.273 195.661 167.923 1.00 93.31  ? 2612 LEU A CA    1 
ATOM   7615  C C     . LEU A 1 2612 ? 127.245 196.263 166.520 1.00 93.31  ? 2612 LEU A C     1 
ATOM   7616  O O     . LEU A 1 2612 ? 127.689 195.627 165.560 1.00 93.31  ? 2612 LEU A O     1 
ATOM   7617  C CB    . LEU A 1 2612 ? 128.652 195.843 168.548 1.00 93.31  ? 2612 LEU A CB    1 
ATOM   7618  C CG    . LEU A 1 2612 ? 128.905 195.095 169.856 1.00 93.31  ? 2612 LEU A CG    1 
ATOM   7619  C CD1   . LEU A 1 2612 ? 130.382 194.780 170.018 1.00 93.31  ? 2612 LEU A CD1   1 
ATOM   7620  C CD2   . LEU A 1 2612 ? 128.392 195.898 171.039 1.00 93.31  ? 2612 LEU A CD2   1 
ATOM   7621  N N     . PRO A 1 2613 ? 126.730 197.479 166.369 1.00 100.55 ? 2613 PRO A N     1 
ATOM   7622  C CA    . PRO A 1 2613 ? 126.534 198.032 165.023 1.00 100.55 ? 2613 PRO A CA    1 
ATOM   7623  C C     . PRO A 1 2613 ? 127.780 198.690 164.453 1.00 100.55 ? 2613 PRO A C     1 
ATOM   7624  O O     . PRO A 1 2613 ? 127.948 198.765 163.233 1.00 100.55 ? 2613 PRO A O     1 
ATOM   7625  C CB    . PRO A 1 2613 ? 125.417 199.057 165.238 1.00 100.55 ? 2613 PRO A CB    1 
ATOM   7626  C CG    . PRO A 1 2613 ? 125.626 199.526 166.645 1.00 100.55 ? 2613 PRO A CG    1 
ATOM   7627  C CD    . PRO A 1 2613 ? 126.219 198.376 167.420 1.00 100.55 ? 2613 PRO A CD    1 
ATOM   7628  N N     . ASP A 1 2614 ? 128.661 199.163 165.329 1.00 104.39 ? 2614 ASP A N     1 
ATOM   7629  C CA    . ASP A 1 2614 ? 129.798 199.982 164.936 1.00 104.39 ? 2614 ASP A CA    1 
ATOM   7630  C C     . ASP A 1 2614 ? 131.060 199.173 164.671 1.00 104.39 ? 2614 ASP A C     1 
ATOM   7631  O O     . ASP A 1 2614 ? 132.098 199.758 164.346 1.00 104.39 ? 2614 ASP A O     1 
ATOM   7632  C CB    . ASP A 1 2614 ? 130.065 201.035 166.008 1.00 104.39 ? 2614 ASP A CB    1 
ATOM   7633  C CG    . ASP A 1 2614 ? 129.803 200.514 167.404 1.00 104.39 ? 2614 ASP A CG    1 
ATOM   7634  O OD1   . ASP A 1 2614 ? 129.349 199.358 167.527 1.00 104.39 ? 2614 ASP A OD1   1 
ATOM   7635  O OD2   . ASP A 1 2614 ? 130.044 201.258 168.377 1.00 104.39 ? 2614 ASP A OD2   1 
ATOM   7636  N N     . MET A 1 2615 ? 131.003 197.853 164.800 1.00 101.23 ? 2615 MET A N     1 
ATOM   7637  C CA    . MET A 1 2615 ? 132.157 197.001 164.553 1.00 101.23 ? 2615 MET A CA    1 
ATOM   7638  C C     . MET A 1 2615 ? 131.976 196.242 163.248 1.00 101.23 ? 2615 MET A C     1 
ATOM   7639  O O     . MET A 1 2615 ? 130.881 195.764 162.941 1.00 101.23 ? 2615 MET A O     1 
ATOM   7640  C CB    . MET A 1 2615 ? 132.370 196.009 165.697 1.00 101.23 ? 2615 MET A CB    1 
ATOM   7641  C CG    . MET A 1 2615 ? 131.728 196.413 167.005 1.00 101.23 ? 2615 MET A CG    1 
ATOM   7642  S SD    . MET A 1 2615 ? 132.310 197.998 167.634 1.00 101.23 ? 2615 MET A SD    1 
ATOM   7643  C CE    . MET A 1 2615 ? 133.696 197.471 168.638 1.00 101.23 ? 2615 MET A CE    1 
ATOM   7644  N N     . GLU A 1 2616 ? 133.054 196.140 162.482 1.00 94.78  ? 2616 GLU A N     1 
ATOM   7645  C CA    . GLU A 1 2616 ? 133.083 195.362 161.253 1.00 94.78  ? 2616 GLU A CA    1 
ATOM   7646  C C     . GLU A 1 2616 ? 133.851 194.077 161.525 1.00 94.78  ? 2616 GLU A C     1 
ATOM   7647  O O     . GLU A 1 2616 ? 135.033 194.121 161.878 1.00 94.78  ? 2616 GLU A O     1 
ATOM   7648  C CB    . GLU A 1 2616 ? 133.726 196.157 160.118 1.00 94.78  ? 2616 GLU A CB    1 
ATOM   7649  C CG    . GLU A 1 2616 ? 133.946 195.364 158.844 1.00 94.78  ? 2616 GLU A CG    1 
ATOM   7650  C CD    . GLU A 1 2616 ? 134.143 196.255 157.633 1.00 94.78  ? 2616 GLU A CD    1 
ATOM   7651  O OE1   . GLU A 1 2616 ? 134.952 197.201 157.715 1.00 94.78  ? 2616 GLU A OE1   1 
ATOM   7652  O OE2   . GLU A 1 2616 ? 133.492 196.005 156.597 1.00 94.78  ? 2616 GLU A OE2   1 
ATOM   7653  N N     . VAL A 1 2617 ? 133.184 192.944 161.363 1.00 84.43  ? 2617 VAL A N     1 
ATOM   7654  C CA    . VAL A 1 2617 ? 133.754 191.651 161.718 1.00 84.43  ? 2617 VAL A CA    1 
ATOM   7655  C C     . VAL A 1 2617 ? 134.489 191.083 160.517 1.00 84.43  ? 2617 VAL A C     1 
ATOM   7656  O O     . VAL A 1 2617 ? 134.004 191.163 159.384 1.00 84.43  ? 2617 VAL A O     1 
ATOM   7657  C CB    . VAL A 1 2617 ? 132.663 190.685 162.198 1.00 84.43  ? 2617 VAL A CB    1 
ATOM   7658  C CG1   . VAL A 1 2617 ? 133.289 189.507 162.907 1.00 84.43  ? 2617 VAL A CG1   1 
ATOM   7659  C CG2   . VAL A 1 2617 ? 131.694 191.405 163.109 1.00 84.43  ? 2617 VAL A CG2   1 
ATOM   7660  N N     . VAL A 1 2618 ? 135.669 190.521 160.761 1.00 81.40  ? 2618 VAL A N     1 
ATOM   7661  C CA    . VAL A 1 2618 ? 136.471 189.886 159.723 1.00 81.40  ? 2618 VAL A CA    1 
ATOM   7662  C C     . VAL A 1 2618 ? 136.855 188.499 160.211 1.00 81.40  ? 2618 VAL A C     1 
ATOM   7663  O O     . VAL A 1 2618 ? 137.445 188.360 161.288 1.00 81.40  ? 2618 VAL A O     1 
ATOM   7664  C CB    . VAL A 1 2618 ? 137.729 190.700 159.392 1.00 81.40  ? 2618 VAL A CB    1 
ATOM   7665  C CG1   . VAL A 1 2618 ? 138.390 190.160 158.140 1.00 81.40  ? 2618 VAL A CG1   1 
ATOM   7666  C CG2   . VAL A 1 2618 ? 137.386 192.167 159.257 1.00 81.40  ? 2618 VAL A CG2   1 
ATOM   7667  N N     . GLY A 1 2619 ? 136.536 187.476 159.420 1.00 81.80  ? 2619 GLY A N     1 
ATOM   7668  C CA    . GLY A 1 2619 ? 136.869 186.113 159.756 1.00 81.80  ? 2619 GLY A CA    1 
ATOM   7669  C C     . GLY A 1 2619 ? 138.161 185.698 159.085 1.00 81.80  ? 2619 GLY A C     1 
ATOM   7670  O O     . GLY A 1 2619 ? 138.220 185.559 157.863 1.00 81.80  ? 2619 GLY A O     1 
ATOM   7671  N N     . LEU A 1 2620 ? 139.199 185.507 159.893 1.00 83.43  ? 2620 LEU A N     1 
ATOM   7672  C CA    . LEU A 1 2620 ? 140.522 185.146 159.400 1.00 83.43  ? 2620 LEU A CA    1 
ATOM   7673  C C     . LEU A 1 2620 ? 140.906 183.788 159.963 1.00 83.43  ? 2620 LEU A C     1 
ATOM   7674  O O     . LEU A 1 2620 ? 140.933 183.608 161.184 1.00 83.43  ? 2620 LEU A O     1 
ATOM   7675  C CB    . LEU A 1 2620 ? 141.557 186.199 159.794 1.00 83.43  ? 2620 LEU A CB    1 
ATOM   7676  C CG    . LEU A 1 2620 ? 142.098 187.053 158.653 1.00 83.43  ? 2620 LEU A CG    1 
ATOM   7677  C CD1   . LEU A 1 2620 ? 143.449 187.624 159.028 1.00 83.43  ? 2620 LEU A CD1   1 
ATOM   7678  C CD2   . LEU A 1 2620 ? 142.191 186.234 157.380 1.00 83.43  ? 2620 LEU A CD2   1 
ATOM   7679  N N     . ASN A 1 2621 ? 141.216 182.843 159.078 1.00 90.90  ? 2621 ASN A N     1 
ATOM   7680  C CA    . ASN A 1 2621 ? 141.599 181.493 159.478 1.00 90.90  ? 2621 ASN A CA    1 
ATOM   7681  C C     . ASN A 1 2621 ? 143.118 181.384 159.456 1.00 90.90  ? 2621 ASN A C     1 
ATOM   7682  O O     . ASN A 1 2621 ? 143.748 181.603 158.418 1.00 90.90  ? 2621 ASN A O     1 
ATOM   7683  C CB    . ASN A 1 2621 ? 140.965 180.456 158.560 1.00 90.90  ? 2621 ASN A CB    1 
ATOM   7684  C CG    . ASN A 1 2621 ? 139.584 180.857 158.102 1.00 90.90  ? 2621 ASN A CG    1 
ATOM   7685  O OD1   . ASN A 1 2621 ? 139.290 180.856 156.909 1.00 90.90  ? 2621 ASN A OD1   1 
ATOM   7686  N ND2   . ASN A 1 2621 ? 138.723 181.200 159.052 1.00 90.90  ? 2621 ASN A ND2   1 
ATOM   7687  N N     . PHE A 1 2622 ? 143.702 181.037 160.598 1.00 87.73  ? 2622 PHE A N     1 
ATOM   7688  C CA    . PHE A 1 2622 ? 145.149 180.922 160.729 1.00 87.73  ? 2622 PHE A CA    1 
ATOM   7689  C C     . PHE A 1 2622 ? 145.550 179.474 160.486 1.00 87.73  ? 2622 PHE A C     1 
ATOM   7690  O O     . PHE A 1 2622 ? 145.318 178.606 161.333 1.00 87.73  ? 2622 PHE A O     1 
ATOM   7691  C CB    . PHE A 1 2622 ? 145.606 181.389 162.107 1.00 87.73  ? 2622 PHE A CB    1 
ATOM   7692  C CG    . PHE A 1 2622 ? 145.788 182.871 162.214 1.00 87.73  ? 2622 PHE A CG    1 
ATOM   7693  C CD1   . PHE A 1 2622 ? 145.195 183.723 161.302 1.00 87.73  ? 2622 PHE A CD1   1 
ATOM   7694  C CD2   . PHE A 1 2622 ? 146.556 183.414 163.223 1.00 87.73  ? 2622 PHE A CD2   1 
ATOM   7695  C CE1   . PHE A 1 2622 ? 145.360 185.086 161.400 1.00 87.73  ? 2622 PHE A CE1   1 
ATOM   7696  C CE2   . PHE A 1 2622 ? 146.725 184.776 163.322 1.00 87.73  ? 2622 PHE A CE2   1 
ATOM   7697  C CZ    . PHE A 1 2622 ? 146.127 185.612 162.411 1.00 87.73  ? 2622 PHE A CZ    1 
ATOM   7698  N N     . SER A 1 2623 ? 146.154 179.213 159.333 1.00 100.84 ? 2623 SER A N     1 
ATOM   7699  C CA    . SER A 1 2623 ? 146.665 177.886 159.039 1.00 100.84 ? 2623 SER A CA    1 
ATOM   7700  C C     . SER A 1 2623 ? 148.017 177.693 159.718 1.00 100.84 ? 2623 SER A C     1 
ATOM   7701  O O     . SER A 1 2623 ? 148.561 178.601 160.351 1.00 100.84 ? 2623 SER A O     1 
ATOM   7702  C CB    . SER A 1 2623 ? 146.775 177.679 157.532 1.00 100.84 ? 2623 SER A CB    1 
ATOM   7703  O OG    . SER A 1 2623 ? 148.013 178.168 157.044 1.00 100.84 ? 2623 SER A OG    1 
ATOM   7704  N N     . SER A 1 2624 ? 148.573 176.491 159.586 1.00 102.79 ? 2624 SER A N     1 
ATOM   7705  C CA    . SER A 1 2624 ? 149.897 176.239 160.135 1.00 102.79 ? 2624 SER A CA    1 
ATOM   7706  C C     . SER A 1 2624 ? 150.980 177.051 159.443 1.00 102.79 ? 2624 SER A C     1 
ATOM   7707  O O     . SER A 1 2624 ? 152.002 177.346 160.070 1.00 102.79 ? 2624 SER A O     1 
ATOM   7708  C CB    . SER A 1 2624 ? 150.235 174.753 160.040 1.00 102.79 ? 2624 SER A CB    1 
ATOM   7709  O OG    . SER A 1 2624 ? 151.624 174.540 160.216 1.00 102.79 ? 2624 SER A OG    1 
ATOM   7710  N N     . ALA A 1 2625 ? 150.781 177.425 158.180 1.00 100.91 ? 2625 ALA A N     1 
ATOM   7711  C CA    . ALA A 1 2625 ? 151.754 178.202 157.424 1.00 100.91 ? 2625 ALA A CA    1 
ATOM   7712  C C     . ALA A 1 2625 ? 151.410 179.685 157.397 1.00 100.91 ? 2625 ALA A C     1 
ATOM   7713  O O     . ALA A 1 2625 ? 151.836 180.402 156.487 1.00 100.91 ? 2625 ALA A O     1 
ATOM   7714  C CB    . ALA A 1 2625 ? 151.876 177.661 156.000 1.00 100.91 ? 2625 ALA A CB    1 
ATOM   7715  N N     . THR A 1 2626 ? 150.642 180.158 158.372 1.00 98.30  ? 2626 THR A N     1 
ATOM   7716  C CA    . THR A 1 2626 ? 150.261 181.561 158.409 1.00 98.30  ? 2626 THR A CA    1 
ATOM   7717  C C     . THR A 1 2626 ? 151.450 182.431 158.790 1.00 98.30  ? 2626 THR A C     1 
ATOM   7718  O O     . THR A 1 2626 ? 152.149 182.159 159.770 1.00 98.30  ? 2626 THR A O     1 
ATOM   7719  C CB    . THR A 1 2626 ? 149.117 181.771 159.394 1.00 98.30  ? 2626 THR A CB    1 
ATOM   7720  O OG1   . THR A 1 2626 ? 148.020 180.920 159.038 1.00 98.30  ? 2626 THR A OG1   1 
ATOM   7721  C CG2   . THR A 1 2626 ? 148.666 183.213 159.372 1.00 98.30  ? 2626 THR A CG2   1 
ATOM   7722  N N     . THR A 1 2627 ? 151.675 183.475 158.009 1.00 103.10 ? 2627 THR A N     1 
ATOM   7723  C CA    . THR A 1 2627 ? 152.748 184.438 158.185 1.00 103.10 ? 2627 THR A CA    1 
ATOM   7724  C C     . THR A 1 2627 ? 152.143 185.831 158.142 1.00 103.10 ? 2627 THR A C     1 
ATOM   7725  O O     . THR A 1 2627 ? 150.998 186.000 157.710 1.00 103.10 ? 2627 THR A O     1 
ATOM   7726  C CB    . THR A 1 2627 ? 153.821 184.282 157.094 1.00 103.10 ? 2627 THR A CB    1 
ATOM   7727  O OG1   . THR A 1 2627 ? 153.333 184.813 155.860 1.00 103.10 ? 2627 THR A OG1   1 
ATOM   7728  C CG2   . THR A 1 2627 ? 154.192 182.821 156.902 1.00 103.10 ? 2627 THR A CG2   1 
ATOM   7729  N N     . PRO A 1 2628 ? 152.873 186.852 158.602 1.00 94.99  ? 2628 PRO A N     1 
ATOM   7730  C CA    . PRO A 1 2628 ? 152.285 188.200 158.663 1.00 94.99  ? 2628 PRO A CA    1 
ATOM   7731  C C     . PRO A 1 2628 ? 151.723 188.697 157.345 1.00 94.99  ? 2628 PRO A C     1 
ATOM   7732  O O     . PRO A 1 2628 ? 150.761 189.480 157.360 1.00 94.99  ? 2628 PRO A O     1 
ATOM   7733  C CB    . PRO A 1 2628 ? 153.461 189.068 159.120 1.00 94.99  ? 2628 PRO A CB    1 
ATOM   7734  C CG    . PRO A 1 2628 ? 154.296 188.155 159.916 1.00 94.99  ? 2628 PRO A CG    1 
ATOM   7735  C CD    . PRO A 1 2628 ? 154.188 186.808 159.268 1.00 94.99  ? 2628 PRO A CD    1 
ATOM   7736  N N     . GLU A 1 2629 ? 152.267 188.250 156.210 1.00 103.30 ? 2629 GLU A N     1 
ATOM   7737  C CA    . GLU A 1 2629 ? 151.836 188.786 154.924 1.00 103.30 ? 2629 GLU A CA    1 
ATOM   7738  C C     . GLU A 1 2629 ? 150.331 188.658 154.741 1.00 103.30 ? 2629 GLU A C     1 
ATOM   7739  O O     . GLU A 1 2629 ? 149.717 189.495 154.074 1.00 103.30 ? 2629 GLU A O     1 
ATOM   7740  C CB    . GLU A 1 2629 ? 152.575 188.082 153.784 1.00 103.30 ? 2629 GLU A CB    1 
ATOM   7741  C CG    . GLU A 1 2629 ? 152.231 186.612 153.636 1.00 103.30 ? 2629 GLU A CG    1 
ATOM   7742  C CD    . GLU A 1 2629 ? 153.168 185.879 152.696 1.00 103.30 ? 2629 GLU A CD    1 
ATOM   7743  O OE1   . GLU A 1 2629 ? 153.649 186.500 151.726 1.00 103.30 ? 2629 GLU A OE1   1 
ATOM   7744  O OE2   . GLU A 1 2629 ? 153.425 184.679 152.931 1.00 103.30 ? 2629 GLU A OE2   1 
ATOM   7745  N N     . LEU A 1 2630 ? 149.715 187.641 155.348 1.00 98.46  ? 2630 LEU A N     1 
ATOM   7746  C CA    . LEU A 1 2630 ? 148.260 187.554 155.331 1.00 98.46  ? 2630 LEU A CA    1 
ATOM   7747  C C     . LEU A 1 2630 ? 147.636 188.746 156.046 1.00 98.46  ? 2630 LEU A C     1 
ATOM   7748  O O     . LEU A 1 2630 ? 146.666 189.338 155.557 1.00 98.46  ? 2630 LEU A O     1 
ATOM   7749  C CB    . LEU A 1 2630 ? 147.808 186.244 155.973 1.00 98.46  ? 2630 LEU A CB    1 
ATOM   7750  C CG    . LEU A 1 2630 ? 146.426 186.250 156.625 1.00 98.46  ? 2630 LEU A CG    1 
ATOM   7751  C CD1   . LEU A 1 2630 ? 145.345 186.253 155.559 1.00 98.46  ? 2630 LEU A CD1   1 
ATOM   7752  C CD2   . LEU A 1 2630 ? 146.259 185.063 157.543 1.00 98.46  ? 2630 LEU A CD2   1 
ATOM   7753  N N     . LEU A 1 2631 ? 148.187 189.121 157.200 1.00 96.27  ? 2631 LEU A N     1 
ATOM   7754  C CA    . LEU A 1 2631 ? 147.667 190.281 157.914 1.00 96.27  ? 2631 LEU A CA    1 
ATOM   7755  C C     . LEU A 1 2631 ? 147.863 191.559 157.111 1.00 96.27  ? 2631 LEU A C     1 
ATOM   7756  O O     . LEU A 1 2631 ? 146.959 192.402 157.047 1.00 96.27  ? 2631 LEU A O     1 
ATOM   7757  C CB    . LEU A 1 2631 ? 148.334 190.398 159.282 1.00 96.27  ? 2631 LEU A CB    1 
ATOM   7758  C CG    . LEU A 1 2631 ? 147.864 189.374 160.308 1.00 96.27  ? 2631 LEU A CG    1 
ATOM   7759  C CD1   . LEU A 1 2631 ? 148.690 189.473 161.567 1.00 96.27  ? 2631 LEU A CD1   1 
ATOM   7760  C CD2   . LEU A 1 2631 ? 146.402 189.599 160.614 1.00 96.27  ? 2631 LEU A CD2   1 
ATOM   7761  N N     . LEU A 1 2632 ? 149.038 191.731 156.498 1.00 99.97  ? 2632 LEU A N     1 
ATOM   7762  C CA    . LEU A 1 2632 ? 149.245 192.928 155.686 1.00 99.97  ? 2632 LEU A CA    1 
ATOM   7763  C C     . LEU A 1 2632 ? 148.291 192.970 154.499 1.00 99.97  ? 2632 LEU A C     1 
ATOM   7764  O O     . LEU A 1 2632 ? 147.786 194.039 154.144 1.00 99.97  ? 2632 LEU A O     1 
ATOM   7765  C CB    . LEU A 1 2632 ? 150.695 193.052 155.218 1.00 99.97  ? 2632 LEU A CB    1 
ATOM   7766  C CG    . LEU A 1 2632 ? 151.809 193.239 156.255 1.00 99.97  ? 2632 LEU A CG    1 
ATOM   7767  C CD1   . LEU A 1 2632 ? 151.360 194.211 157.340 1.00 99.97  ? 2632 LEU A CD1   1 
ATOM   7768  C CD2   . LEU A 1 2632 ? 152.340 191.958 156.845 1.00 99.97  ? 2632 LEU A CD2   1 
ATOM   7769  N N     . LYS A 1 2633 ? 148.025 191.821 153.874 1.00 103.27 ? 2633 LYS A N     1 
ATOM   7770  C CA    . LYS A 1 2633 ? 147.025 191.788 152.813 1.00 103.27 ? 2633 LYS A CA    1 
ATOM   7771  C C     . LYS A 1 2633 ? 145.652 192.166 153.349 1.00 103.27 ? 2633 LYS A C     1 
ATOM   7772  O O     . LYS A 1 2633 ? 144.877 192.850 152.671 1.00 103.27 ? 2633 LYS A O     1 
ATOM   7773  C CB    . LYS A 1 2633 ? 146.980 190.407 152.161 1.00 103.27 ? 2633 LYS A CB    1 
ATOM   7774  C CG    . LYS A 1 2633 ? 148.111 190.136 151.186 1.00 103.27 ? 2633 LYS A CG    1 
ATOM   7775  C CD    . LYS A 1 2633 ? 148.025 188.721 150.639 1.00 103.27 ? 2633 LYS A CD    1 
ATOM   7776  C CE    . LYS A 1 2633 ? 149.400 188.150 150.349 1.00 103.27 ? 2633 LYS A CE    1 
ATOM   7777  N NZ    . LYS A 1 2633 ? 149.889 187.295 151.462 1.00 103.27 ? 2633 LYS A NZ    1 
ATOM   7778  N N     . THR A 1 2634 ? 145.331 191.723 154.566 1.00 97.26  ? 2634 THR A N     1 
ATOM   7779  C CA    . THR A 1 2634 ? 144.047 192.072 155.162 1.00 97.26  ? 2634 THR A CA    1 
ATOM   7780  C C     . THR A 1 2634 ? 143.923 193.579 155.350 1.00 97.26  ? 2634 THR A C     1 
ATOM   7781  O O     . THR A 1 2634 ? 142.895 194.177 155.006 1.00 97.26  ? 2634 THR A O     1 
ATOM   7782  C CB    . THR A 1 2634 ? 143.877 191.349 156.494 1.00 97.26  ? 2634 THR A CB    1 
ATOM   7783  O OG1   . THR A 1 2634 ? 144.207 189.967 156.328 1.00 97.26  ? 2634 THR A OG1   1 
ATOM   7784  C CG2   . THR A 1 2634 ? 142.442 191.461 156.968 1.00 97.26  ? 2634 THR A CG2   1 
ATOM   7785  N N     . PHE A 1 2635 ? 144.968 194.213 155.886 1.00 99.85  ? 2635 PHE A N     1 
ATOM   7786  C CA    . PHE A 1 2635 ? 144.926 195.667 156.022 1.00 99.85  ? 2635 PHE A CA    1 
ATOM   7787  C C     . PHE A 1 2635 ? 144.819 196.338 154.660 1.00 99.85  ? 2635 PHE A C     1 
ATOM   7788  O O     . PHE A 1 2635 ? 144.021 197.262 154.477 1.00 99.85  ? 2635 PHE A O     1 
ATOM   7789  C CB    . PHE A 1 2635 ? 146.151 196.209 156.763 1.00 99.85  ? 2635 PHE A CB    1 
ATOM   7790  C CG    . PHE A 1 2635 ? 146.501 195.465 158.010 1.00 99.85  ? 2635 PHE A CG    1 
ATOM   7791  C CD1   . PHE A 1 2635 ? 145.599 195.361 159.049 1.00 99.85  ? 2635 PHE A CD1   1 
ATOM   7792  C CD2   . PHE A 1 2635 ? 147.769 194.943 158.178 1.00 99.85  ? 2635 PHE A CD2   1 
ATOM   7793  C CE1   . PHE A 1 2635 ? 145.934 194.692 160.206 1.00 99.85  ? 2635 PHE A CE1   1 
ATOM   7794  C CE2   . PHE A 1 2635 ? 148.110 194.273 159.330 1.00 99.85  ? 2635 PHE A CE2   1 
ATOM   7795  C CZ    . PHE A 1 2635 ? 147.193 194.150 160.348 1.00 99.85  ? 2635 PHE A CZ    1 
ATOM   7796  N N     . ASP A 1 2636 ? 145.602 195.874 153.684 1.00 109.54 ? 2636 ASP A N     1 
ATOM   7797  C CA    . ASP A 1 2636 ? 145.566 196.484 152.360 1.00 109.54 ? 2636 ASP A CA    1 
ATOM   7798  C C     . ASP A 1 2636 ? 144.170 196.409 151.759 1.00 109.54 ? 2636 ASP A C     1 
ATOM   7799  O O     . ASP A 1 2636 ? 143.718 197.350 151.098 1.00 109.54 ? 2636 ASP A O     1 
ATOM   7800  C CB    . ASP A 1 2636 ? 146.580 195.805 151.439 1.00 109.54 ? 2636 ASP A CB    1 
ATOM   7801  C CG    . ASP A 1 2636 ? 148.014 196.121 151.814 1.00 109.54 ? 2636 ASP A CG    1 
ATOM   7802  O OD1   . ASP A 1 2636 ? 148.260 196.491 152.981 1.00 109.54 ? 2636 ASP A OD1   1 
ATOM   7803  O OD2   . ASP A 1 2636 ? 148.897 195.995 150.940 1.00 109.54 ? 2636 ASP A OD2   1 
ATOM   7804  N N     . HIS A 1 2637 ? 143.468 195.298 151.984 1.00 105.38 ? 2637 HIS A N     1 
ATOM   7805  C CA    . HIS A 1 2637 ? 142.161 195.129 151.362 1.00 105.38 ? 2637 HIS A CA    1 
ATOM   7806  C C     . HIS A 1 2637 ? 141.114 195.951 152.110 1.00 105.38 ? 2637 HIS A C     1 
ATOM   7807  O O     . HIS A 1 2637 ? 140.264 196.596 151.484 1.00 105.38 ? 2637 HIS A O     1 
ATOM   7808  C CB    . HIS A 1 2637 ? 141.825 193.630 151.314 1.00 105.38 ? 2637 HIS A CB    1 
ATOM   7809  C CG    . HIS A 1 2637 ? 140.390 193.291 151.023 1.00 105.38 ? 2637 HIS A CG    1 
ATOM   7810  N ND1   . HIS A 1 2637 ? 140.000 192.004 150.721 1.00 105.38 ? 2637 HIS A ND1   1 
ATOM   7811  C CD2   . HIS A 1 2637 ? 139.282 194.056 150.868 1.00 105.38 ? 2637 HIS A CD2   1 
ATOM   7812  C CE1   . HIS A 1 2637 ? 138.704 191.981 150.469 1.00 105.38 ? 2637 HIS A CE1   1 
ATOM   7813  N NE2   . HIS A 1 2637 ? 138.243 193.214 150.555 1.00 105.38 ? 2637 HIS A NE2   1 
ATOM   7814  N N     . TYR A 1 2638 ? 141.189 195.993 153.445 1.00 103.31 ? 2638 TYR A N     1 
ATOM   7815  C CA    . TYR A 1 2638 ? 140.183 196.701 154.231 1.00 103.31 ? 2638 TYR A CA    1 
ATOM   7816  C C     . TYR A 1 2638 ? 140.600 198.087 154.702 1.00 103.31 ? 2638 TYR A C     1 
ATOM   7817  O O     . TYR A 1 2638 ? 139.731 198.952 154.845 1.00 103.31 ? 2638 TYR A O     1 
ATOM   7818  C CB    . TYR A 1 2638 ? 139.783 195.890 155.475 1.00 103.31 ? 2638 TYR A CB    1 
ATOM   7819  C CG    . TYR A 1 2638 ? 138.945 194.661 155.205 1.00 103.31 ? 2638 TYR A CG    1 
ATOM   7820  C CD1   . TYR A 1 2638 ? 138.732 194.209 153.918 1.00 103.31 ? 2638 TYR A CD1   1 
ATOM   7821  C CD2   . TYR A 1 2638 ? 138.357 193.959 156.244 1.00 103.31 ? 2638 TYR A CD2   1 
ATOM   7822  C CE1   . TYR A 1 2638 ? 137.968 193.087 153.669 1.00 103.31 ? 2638 TYR A CE1   1 
ATOM   7823  C CE2   . TYR A 1 2638 ? 137.588 192.839 156.001 1.00 103.31 ? 2638 TYR A CE2   1 
ATOM   7824  C CZ    . TYR A 1 2638 ? 137.399 192.407 154.714 1.00 103.31 ? 2638 TYR A CZ    1 
ATOM   7825  O OH    . TYR A 1 2638 ? 136.636 191.290 154.467 1.00 103.31 ? 2638 TYR A OH    1 
ATOM   7826  N N     . CYS A 1 2639 ? 141.882 198.323 154.950 1.00 110.68 ? 2639 CYS A N     1 
ATOM   7827  C CA    . CYS A 1 2639 ? 142.335 199.552 155.585 1.00 110.68 ? 2639 CYS A CA    1 
ATOM   7828  C C     . CYS A 1 2639 ? 143.094 200.415 154.584 1.00 110.68 ? 2639 CYS A C     1 
ATOM   7829  O O     . CYS A 1 2639 ? 143.402 199.993 153.466 1.00 110.68 ? 2639 CYS A O     1 
ATOM   7830  C CB    . CYS A 1 2639 ? 143.223 199.244 156.797 1.00 110.68 ? 2639 CYS A CB    1 
ATOM   7831  S SG    . CYS A 1 2639 ? 142.347 199.101 158.367 1.00 110.68 ? 2639 CYS A SG    1 
ATOM   7832  N N     . GLU A 1 2640 ? 143.403 201.639 155.007 1.00 113.06 ? 2640 GLU A N     1 
ATOM   7833  C CA    . GLU A 1 2640 ? 144.081 202.608 154.161 1.00 113.06 ? 2640 GLU A CA    1 
ATOM   7834  C C     . GLU A 1 2640 ? 145.147 203.330 154.970 1.00 113.06 ? 2640 GLU A C     1 
ATOM   7835  O O     . GLU A 1 2640 ? 145.099 203.373 156.201 1.00 113.06 ? 2640 GLU A O     1 
ATOM   7836  C CB    . GLU A 1 2640 ? 143.098 203.623 153.572 1.00 113.06 ? 2640 GLU A CB    1 
ATOM   7837  C CG    . GLU A 1 2640 ? 142.331 204.400 154.624 1.00 113.06 ? 2640 GLU A CG    1 
ATOM   7838  C CD    . GLU A 1 2640 ? 141.564 205.566 154.040 1.00 113.06 ? 2640 GLU A CD    1 
ATOM   7839  O OE1   . GLU A 1 2640 ? 142.201 206.463 153.449 1.00 113.06 ? 2640 GLU A OE1   1 
ATOM   7840  O OE2   . GLU A 1 2640 ? 140.323 205.584 154.172 1.00 113.06 ? 2640 GLU A OE2   1 
ATOM   7841  N N     . TYR A 1 2641 ? 146.111 203.906 154.259 1.00 108.81 ? 2641 TYR A N     1 
ATOM   7842  C CA    . TYR A 1 2641 ? 147.202 204.648 154.874 1.00 108.81 ? 2641 TYR A CA    1 
ATOM   7843  C C     . TYR A 1 2641 ? 146.958 206.143 154.722 1.00 108.81 ? 2641 TYR A C     1 
ATOM   7844  O O     . TYR A 1 2641 ? 146.621 206.616 153.632 1.00 108.81 ? 2641 TYR A O     1 
ATOM   7845  C CB    . TYR A 1 2641 ? 148.545 204.263 154.253 1.00 108.81 ? 2641 TYR A CB    1 
ATOM   7846  C CG    . TYR A 1 2641 ? 148.956 202.834 154.522 1.00 108.81 ? 2641 TYR A CG    1 
ATOM   7847  C CD1   . TYR A 1 2641 ? 148.464 201.792 153.752 1.00 108.81 ? 2641 TYR A CD1   1 
ATOM   7848  C CD2   . TYR A 1 2641 ? 149.833 202.527 155.552 1.00 108.81 ? 2641 TYR A CD2   1 
ATOM   7849  C CE1   . TYR A 1 2641 ? 148.837 200.487 153.996 1.00 108.81 ? 2641 TYR A CE1   1 
ATOM   7850  C CE2   . TYR A 1 2641 ? 150.209 201.225 155.804 1.00 108.81 ? 2641 TYR A CE2   1 
ATOM   7851  C CZ    . TYR A 1 2641 ? 149.709 200.210 155.023 1.00 108.81 ? 2641 TYR A CZ    1 
ATOM   7852  O OH    . TYR A 1 2641 ? 150.081 198.910 155.267 1.00 108.81 ? 2641 TYR A OH    1 
ATOM   7853  N N     . ARG A 1 2642 ? 147.126 206.880 155.817 1.00 119.71 ? 2642 ARG A N     1 
ATOM   7854  C CA    . ARG A 1 2642 ? 146.906 208.320 155.844 1.00 119.71 ? 2642 ARG A CA    1 
ATOM   7855  C C     . ARG A 1 2642 ? 148.141 208.999 156.414 1.00 119.71 ? 2642 ARG A C     1 
ATOM   7856  O O     . ARG A 1 2642 ? 148.601 208.641 157.503 1.00 119.71 ? 2642 ARG A O     1 
ATOM   7857  C CB    . ARG A 1 2642 ? 145.667 208.666 156.674 1.00 119.71 ? 2642 ARG A CB    1 
ATOM   7858  C CG    . ARG A 1 2642 ? 145.175 210.083 156.494 1.00 119.71 ? 2642 ARG A CG    1 
ATOM   7859  C CD    . ARG A 1 2642 ? 143.857 210.294 157.208 1.00 119.71 ? 2642 ARG A CD    1 
ATOM   7860  N NE    . ARG A 1 2642 ? 143.969 210.037 158.638 1.00 119.71 ? 2642 ARG A NE    1 
ATOM   7861  C CZ    . ARG A 1 2642 ? 143.365 209.038 159.266 1.00 119.71 ? 2642 ARG A CZ    1 
ATOM   7862  N NH1   . ARG A 1 2642 ? 142.599 208.177 158.617 1.00 119.71 ? 2642 ARG A NH1   1 
ATOM   7863  N NH2   . ARG A 1 2642 ? 143.535 208.899 160.578 1.00 119.71 ? 2642 ARG A NH2   1 
ATOM   7864  N N     . ARG A 1 2643 ? 148.675 209.973 155.680 1.00 124.88 ? 2643 ARG A N     1 
ATOM   7865  C CA    . ARG A 1 2643 ? 149.864 210.705 156.092 1.00 124.88 ? 2643 ARG A CA    1 
ATOM   7866  C C     . ARG A 1 2643 ? 149.546 212.081 156.664 1.00 124.88 ? 2643 ARG A C     1 
ATOM   7867  O O     . ARG A 1 2643 ? 150.471 212.845 156.958 1.00 124.88 ? 2643 ARG A O     1 
ATOM   7868  C CB    . ARG A 1 2643 ? 150.828 210.845 154.908 1.00 124.88 ? 2643 ARG A CB    1 
ATOM   7869  C CG    . ARG A 1 2643 ? 152.281 211.035 155.306 1.00 124.88 ? 2643 ARG A CG    1 
ATOM   7870  C CD    . ARG A 1 2643 ? 153.191 210.975 154.097 1.00 124.88 ? 2643 ARG A CD    1 
ATOM   7871  N NE    . ARG A 1 2643 ? 154.025 209.780 154.100 1.00 124.88 ? 2643 ARG A NE    1 
ATOM   7872  C CZ    . ARG A 1 2643 ? 155.096 209.617 154.864 1.00 124.88 ? 2643 ARG A CZ    1 
ATOM   7873  N NH1   . ARG A 1 2643 ? 155.495 210.556 155.706 1.00 124.88 ? 2643 ARG A NH1   1 
ATOM   7874  N NH2   . ARG A 1 2643 ? 155.785 208.483 154.781 1.00 124.88 ? 2643 ARG A NH2   1 
ATOM   7875  N N     . THR A 1 2644 ? 148.266 212.410 156.833 1.00 131.47 ? 2644 THR A N     1 
ATOM   7876  C CA    . THR A 1 2644 ? 147.899 213.713 157.384 1.00 131.47 ? 2644 THR A CA    1 
ATOM   7877  C C     . THR A 1 2644 ? 148.470 213.993 158.772 1.00 131.47 ? 2644 THR A C     1 
ATOM   7878  O O     . THR A 1 2644 ? 149.000 215.100 158.972 1.00 131.47 ? 2644 THR A O     1 
ATOM   7879  C CB    . THR A 1 2644 ? 146.371 213.857 157.395 1.00 131.47 ? 2644 THR A CB    1 
ATOM   7880  O OG1   . THR A 1 2644 ? 145.804 212.957 158.356 1.00 131.47 ? 2644 THR A OG1   1 
ATOM   7881  C CG2   . THR A 1 2644 ? 145.797 213.568 156.017 1.00 131.47 ? 2644 THR A CG2   1 
ATOM   7882  N N     . PRO A 1 2645 ? 148.410 213.084 159.756 1.00 125.77 ? 2645 PRO A N     1 
ATOM   7883  C CA    . PRO A 1 2645 ? 148.897 213.448 161.086 1.00 125.77 ? 2645 PRO A CA    1 
ATOM   7884  C C     . PRO A 1 2645 ? 150.405 213.317 161.211 1.00 125.77 ? 2645 PRO A C     1 
ATOM   7885  O O     . PRO A 1 2645 ? 151.109 213.178 160.206 1.00 125.77 ? 2645 PRO A O     1 
ATOM   7886  C CB    . PRO A 1 2645 ? 148.141 212.467 161.991 1.00 125.77 ? 2645 PRO A CB    1 
ATOM   7887  C CG    . PRO A 1 2645 ? 147.756 211.287 161.044 1.00 125.77 ? 2645 PRO A CG    1 
ATOM   7888  C CD    . PRO A 1 2645 ? 148.351 211.617 159.701 1.00 125.77 ? 2645 PRO A CD    1 
ATOM   7889  N N     . ASN A 1 2646 ? 150.903 213.393 162.449 1.00 116.79 ? 2646 ASN A N     1 
ATOM   7890  C CA    . ASN A 1 2646 ? 152.343 213.423 162.692 1.00 116.79 ? 2646 ASN A CA    1 
ATOM   7891  C C     . ASN A 1 2646 ? 153.057 212.254 162.024 1.00 116.79 ? 2646 ASN A C     1 
ATOM   7892  O O     . ASN A 1 2646 ? 154.185 212.400 161.542 1.00 116.79 ? 2646 ASN A O     1 
ATOM   7893  C CB    . ASN A 1 2646 ? 152.606 213.418 164.197 1.00 116.79 ? 2646 ASN A CB    1 
ATOM   7894  C CG    . ASN A 1 2646 ? 152.102 214.673 164.879 1.00 116.79 ? 2646 ASN A CG    1 
ATOM   7895  O OD1   . ASN A 1 2646 ? 151.274 215.400 164.330 1.00 116.79 ? 2646 ASN A OD1   1 
ATOM   7896  N ND2   . ASN A 1 2646 ? 152.595 214.932 166.083 1.00 116.79 ? 2646 ASN A ND2   1 
ATOM   7897  N N     . GLY A 1 2647 ? 152.419 211.084 161.991 1.00 114.38 ? 2647 GLY A N     1 
ATOM   7898  C CA    . GLY A 1 2647 ? 152.967 209.929 161.313 1.00 114.38 ? 2647 GLY A CA    1 
ATOM   7899  C C     . GLY A 1 2647 ? 151.922 209.263 160.436 1.00 114.38 ? 2647 GLY A C     1 
ATOM   7900  O O     . GLY A 1 2647 ? 150.763 209.676 160.392 1.00 114.38 ? 2647 GLY A O     1 
ATOM   7901  N N     . VAL A 1 2648 ? 152.368 208.223 159.731 1.00 108.39 ? 2648 VAL A N     1 
ATOM   7902  C CA    . VAL A 1 2648 ? 151.452 207.423 158.929 1.00 108.39 ? 2648 VAL A CA    1 
ATOM   7903  C C     . VAL A 1 2648 ? 150.478 206.701 159.847 1.00 108.39 ? 2648 VAL A C     1 
ATOM   7904  O O     . VAL A 1 2648 ? 150.866 206.155 160.888 1.00 108.39 ? 2648 VAL A O     1 
ATOM   7905  C CB    . VAL A 1 2648 ? 152.231 206.427 158.054 1.00 108.39 ? 2648 VAL A CB    1 
ATOM   7906  C CG1   . VAL A 1 2648 ? 151.341 205.882 156.953 1.00 108.39 ? 2648 VAL A CG1   1 
ATOM   7907  C CG2   . VAL A 1 2648 ? 153.466 207.088 157.471 1.00 108.39 ? 2648 VAL A CG2   1 
ATOM   7908  N N     . VAL A 1 2649 ? 149.202 206.703 159.477 1.00 105.96 ? 2649 VAL A N     1 
ATOM   7909  C CA    . VAL A 1 2649 ? 148.159 206.073 160.275 1.00 105.96 ? 2649 VAL A CA    1 
ATOM   7910  C C     . VAL A 1 2649 ? 147.369 205.129 159.382 1.00 105.96 ? 2649 VAL A C     1 
ATOM   7911  O O     . VAL A 1 2649 ? 146.931 205.515 158.293 1.00 105.96 ? 2649 VAL A O     1 
ATOM   7912  C CB    . VAL A 1 2649 ? 147.232 207.114 160.931 1.00 105.96 ? 2649 VAL A CB    1 
ATOM   7913  C CG1   . VAL A 1 2649 ? 145.895 206.493 161.293 1.00 105.96 ? 2649 VAL A CG1   1 
ATOM   7914  C CG2   . VAL A 1 2649 ? 147.894 207.699 162.164 1.00 105.96 ? 2649 VAL A CG2   1 
ATOM   7915  N N     . LEU A 1 2650 ? 147.195 203.892 159.841 1.00 101.50 ? 2650 LEU A N     1 
ATOM   7916  C CA    . LEU A 1 2650 ? 146.431 202.878 159.129 1.00 101.50 ? 2650 LEU A CA    1 
ATOM   7917  C C     . LEU A 1 2650 ? 145.053 202.764 159.767 1.00 101.50 ? 2650 LEU A C     1 
ATOM   7918  O O     . LEU A 1 2650 ? 144.940 202.441 160.953 1.00 101.50 ? 2650 LEU A O     1 
ATOM   7919  C CB    . LEU A 1 2650 ? 147.155 201.535 159.166 1.00 101.50 ? 2650 LEU A CB    1 
ATOM   7920  C CG    . LEU A 1 2650 ? 146.527 200.393 158.377 1.00 101.50 ? 2650 LEU A CG    1 
ATOM   7921  C CD1   . LEU A 1 2650 ? 146.768 200.591 156.895 1.00 101.50 ? 2650 LEU A CD1   1 
ATOM   7922  C CD2   . LEU A 1 2650 ? 147.104 199.071 158.839 1.00 101.50 ? 2650 LEU A CD2   1 
ATOM   7923  N N     . ALA A 1 2651 ? 144.013 203.031 158.985 1.00 105.77 ? 2651 ALA A N     1 
ATOM   7924  C CA    . ALA A 1 2651 ? 142.649 203.042 159.485 1.00 105.77 ? 2651 ALA A CA    1 
ATOM   7925  C C     . ALA A 1 2651 ? 141.728 202.373 158.477 1.00 105.77 ? 2651 ALA A C     1 
ATOM   7926  O O     . ALA A 1 2651 ? 142.043 202.322 157.282 1.00 105.77 ? 2651 ALA A O     1 
ATOM   7927  C CB    . ALA A 1 2651 ? 142.164 204.474 159.760 1.00 105.77 ? 2651 ALA A CB    1 
ATOM   7928  N N     . PRO A 1 2652 ? 140.595 201.837 158.931 1.00 104.69 ? 2652 PRO A N     1 
ATOM   7929  C CA    . PRO A 1 2652 ? 139.628 201.262 157.992 1.00 104.69 ? 2652 PRO A CA    1 
ATOM   7930  C C     . PRO A 1 2652 ? 139.062 202.322 157.064 1.00 104.69 ? 2652 PRO A C     1 
ATOM   7931  O O     . PRO A 1 2652 ? 138.953 203.497 157.419 1.00 104.69 ? 2652 PRO A O     1 
ATOM   7932  C CB    . PRO A 1 2652 ? 138.541 200.687 158.905 1.00 104.69 ? 2652 PRO A CB    1 
ATOM   7933  C CG    . PRO A 1 2652 ? 139.193 200.522 160.223 1.00 104.69 ? 2652 PRO A CG    1 
ATOM   7934  C CD    . PRO A 1 2652 ? 140.204 201.613 160.330 1.00 104.69 ? 2652 PRO A CD    1 
ATOM   7935  N N     . VAL A 1 2653 ? 138.698 201.887 155.856 1.00 107.36 ? 2653 VAL A N     1 
ATOM   7936  C CA    . VAL A 1 2653 ? 138.100 202.802 154.889 1.00 107.36 ? 2653 VAL A CA    1 
ATOM   7937  C C     . VAL A 1 2653 ? 136.797 203.370 155.434 1.00 107.36 ? 2653 VAL A C     1 
ATOM   7938  O O     . VAL A 1 2653 ? 136.541 204.576 155.339 1.00 107.36 ? 2653 VAL A O     1 
ATOM   7939  C CB    . VAL A 1 2653 ? 137.892 202.089 153.540 1.00 107.36 ? 2653 VAL A CB    1 
ATOM   7940  C CG1   . VAL A 1 2653 ? 137.148 202.991 152.570 1.00 107.36 ? 2653 VAL A CG1   1 
ATOM   7941  C CG2   . VAL A 1 2653 ? 139.228 201.661 152.958 1.00 107.36 ? 2653 VAL A CG2   1 
ATOM   7942  N N     . GLN A 1 2654 ? 135.960 202.517 156.018 1.00 107.52 ? 2654 GLN A N     1 
ATOM   7943  C CA    . GLN A 1 2654 ? 134.730 202.988 156.636 1.00 107.52 ? 2654 GLN A CA    1 
ATOM   7944  C C     . GLN A 1 2654 ? 135.046 203.896 157.814 1.00 107.52 ? 2654 GLN A C     1 
ATOM   7945  O O     . GLN A 1 2654 ? 135.922 203.599 158.631 1.00 107.52 ? 2654 GLN A O     1 
ATOM   7946  C CB    . GLN A 1 2654 ? 133.880 201.809 157.100 1.00 107.52 ? 2654 GLN A CB    1 
ATOM   7947  C CG    . GLN A 1 2654 ? 133.800 200.672 156.105 1.00 107.52 ? 2654 GLN A CG    1 
ATOM   7948  C CD    . GLN A 1 2654 ? 132.660 199.724 156.406 1.00 107.52 ? 2654 GLN A CD    1 
ATOM   7949  O OE1   . GLN A 1 2654 ? 131.808 200.009 157.246 1.00 107.52 ? 2654 GLN A OE1   1 
ATOM   7950  N NE2   . GLN A 1 2654 ? 132.638 198.589 155.721 1.00 107.52 ? 2654 GLN A NE2   1 
ATOM   7951  N N     . LEU A 1 2655 ? 134.331 205.012 157.898 1.00 104.78 ? 2655 LEU A N     1 
ATOM   7952  C CA    . LEU A 1 2655 ? 134.542 205.980 158.963 1.00 104.78 ? 2655 LEU A CA    1 
ATOM   7953  C C     . LEU A 1 2655 ? 133.702 205.622 160.180 1.00 104.78 ? 2655 LEU A C     1 
ATOM   7954  O O     . LEU A 1 2655 ? 132.539 205.232 160.055 1.00 104.78 ? 2655 LEU A O     1 
ATOM   7955  C CB    . LEU A 1 2655 ? 134.201 207.393 158.489 1.00 104.78 ? 2655 LEU A CB    1 
ATOM   7956  C CG    . LEU A 1 2655 ? 135.356 208.240 157.946 1.00 104.78 ? 2655 LEU A CG    1 
ATOM   7957  C CD1   . LEU A 1 2655 ? 136.187 208.792 159.092 1.00 104.78 ? 2655 LEU A CD1   1 
ATOM   7958  C CD2   . LEU A 1 2655 ? 136.233 207.444 156.991 1.00 104.78 ? 2655 LEU A CD2   1 
ATOM   7959  N N     . GLY A 1 2656 ? 134.306 205.753 161.358 1.00 100.98 ? 2656 GLY A N     1 
ATOM   7960  C CA    . GLY A 1 2656 ? 133.604 205.452 162.588 1.00 100.98 ? 2656 GLY A CA    1 
ATOM   7961  C C     . GLY A 1 2656 ? 133.312 203.988 162.802 1.00 100.98 ? 2656 GLY A C     1 
ATOM   7962  O O     . GLY A 1 2656 ? 132.458 203.651 163.624 1.00 100.98 ? 2656 GLY A O     1 
ATOM   7963  N N     . LYS A 1 2657 ? 133.997 203.104 162.083 1.00 102.92 ? 2657 LYS A N     1 
ATOM   7964  C CA    . LYS A 1 2657 ? 133.793 201.668 162.193 1.00 102.92 ? 2657 LYS A CA    1 
ATOM   7965  C C     . LYS A 1 2657 ? 135.040 201.028 162.784 1.00 102.92 ? 2657 LYS A C     1 
ATOM   7966  O O     . LYS A 1 2657 ? 136.147 201.230 162.275 1.00 102.92 ? 2657 LYS A O     1 
ATOM   7967  C CB    . LYS A 1 2657 ? 133.478 201.055 160.828 1.00 102.92 ? 2657 LYS A CB    1 
ATOM   7968  C CG    . LYS A 1 2657 ? 132.065 201.324 160.346 1.00 102.92 ? 2657 LYS A CG    1 
ATOM   7969  C CD    . LYS A 1 2657 ? 131.036 200.701 161.273 1.00 102.92 ? 2657 LYS A CD    1 
ATOM   7970  C CE    . LYS A 1 2657 ? 129.673 200.641 160.608 1.00 102.92 ? 2657 LYS A CE    1 
ATOM   7971  N NZ    . LYS A 1 2657 ? 129.711 199.864 159.340 1.00 102.92 ? 2657 LYS A NZ    1 
ATOM   7972  N N     . TRP A 1 2658 ? 134.859 200.257 163.851 1.00 94.34  ? 2658 TRP A N     1 
ATOM   7973  C CA    . TRP A 1 2658 ? 135.967 199.597 164.530 1.00 94.34  ? 2658 TRP A CA    1 
ATOM   7974  C C     . TRP A 1 2658 ? 136.190 198.234 163.888 1.00 94.34  ? 2658 TRP A C     1 
ATOM   7975  O O     . TRP A 1 2658 ? 135.480 197.273 164.195 1.00 94.34  ? 2658 TRP A O     1 
ATOM   7976  C CB    . TRP A 1 2658 ? 135.675 199.459 166.020 1.00 94.34  ? 2658 TRP A CB    1 
ATOM   7977  C CG    . TRP A 1 2658 ? 136.132 200.626 166.816 1.00 94.34  ? 2658 TRP A CG    1 
ATOM   7978  C CD1   . TRP A 1 2658 ? 135.455 201.787 167.028 1.00 94.34  ? 2658 TRP A CD1   1 
ATOM   7979  C CD2   . TRP A 1 2658 ? 137.382 200.759 167.496 1.00 94.34  ? 2658 TRP A CD2   1 
ATOM   7980  N NE1   . TRP A 1 2658 ? 136.202 202.634 167.808 1.00 94.34  ? 2658 TRP A NE1   1 
ATOM   7981  C CE2   . TRP A 1 2658 ? 137.391 202.025 168.108 1.00 94.34  ? 2658 TRP A CE2   1 
ATOM   7982  C CE3   . TRP A 1 2658 ? 138.493 199.928 167.651 1.00 94.34  ? 2658 TRP A CE3   1 
ATOM   7983  C CZ2   . TRP A 1 2658 ? 138.466 202.479 168.861 1.00 94.34  ? 2658 TRP A CZ2   1 
ATOM   7984  C CZ3   . TRP A 1 2658 ? 139.559 200.381 168.398 1.00 94.34  ? 2658 TRP A CZ3   1 
ATOM   7985  C CH2   . TRP A 1 2658 ? 139.540 201.645 168.992 1.00 94.34  ? 2658 TRP A CH2   1 
ATOM   7986  N N     . LEU A 1 2659 ? 137.177 198.148 163.002 1.00 85.52  ? 2659 LEU A N     1 
ATOM   7987  C CA    . LEU A 1 2659 ? 137.467 196.887 162.333 1.00 85.52  ? 2659 LEU A CA    1 
ATOM   7988  C C     . LEU A 1 2659 ? 138.038 195.899 163.337 1.00 85.52  ? 2659 LEU A C     1 
ATOM   7989  O O     . LEU A 1 2659 ? 138.996 196.213 164.049 1.00 85.52  ? 2659 LEU A O     1 
ATOM   7990  C CB    . LEU A 1 2659 ? 138.445 197.102 161.184 1.00 85.52  ? 2659 LEU A CB    1 
ATOM   7991  C CG    . LEU A 1 2659 ? 138.695 195.882 160.300 1.00 85.52  ? 2659 LEU A CG    1 
ATOM   7992  C CD1   . LEU A 1 2659 ? 137.756 195.896 159.112 1.00 85.52  ? 2659 LEU A CD1   1 
ATOM   7993  C CD2   . LEU A 1 2659 ? 140.136 195.842 159.838 1.00 85.52  ? 2659 LEU A CD2   1 
ATOM   7994  N N     . VAL A 1 2660 ? 137.451 194.711 163.399 1.00 79.30  ? 2660 VAL A N     1 
ATOM   7995  C CA    . VAL A 1 2660 ? 137.872 193.670 164.326 1.00 79.30  ? 2660 VAL A CA    1 
ATOM   7996  C C     . VAL A 1 2660 ? 138.366 192.489 163.508 1.00 79.30  ? 2660 VAL A C     1 
ATOM   7997  O O     . VAL A 1 2660 ? 137.633 191.959 162.666 1.00 79.30  ? 2660 VAL A O     1 
ATOM   7998  C CB    . VAL A 1 2660 ? 136.732 193.250 165.263 1.00 79.30  ? 2660 VAL A CB    1 
ATOM   7999  C CG1   . VAL A 1 2660 ? 137.163 192.078 166.114 1.00 79.30  ? 2660 VAL A CG1   1 
ATOM   8000  C CG2   . VAL A 1 2660 ? 136.310 194.415 166.133 1.00 79.30  ? 2660 VAL A CG2   1 
ATOM   8001  N N     . LEU A 1 2661 ? 139.606 192.077 163.751 1.00 75.41  ? 2661 LEU A N     1 
ATOM   8002  C CA    . LEU A 1 2661 ? 140.188 190.938 163.047 1.00 75.41  ? 2661 LEU A CA    1 
ATOM   8003  C C     . LEU A 1 2661 ? 140.017 189.700 163.913 1.00 75.41  ? 2661 LEU A C     1 
ATOM   8004  O O     . LEU A 1 2661 ? 140.904 189.320 164.676 1.00 75.41  ? 2661 LEU A O     1 
ATOM   8005  C CB    . LEU A 1 2661 ? 141.651 191.195 162.717 1.00 75.41  ? 2661 LEU A CB    1 
ATOM   8006  C CG    . LEU A 1 2661 ? 141.922 192.258 161.656 1.00 75.41  ? 2661 LEU A CG    1 
ATOM   8007  C CD1   . LEU A 1 2661 ? 143.308 192.081 161.072 1.00 75.41  ? 2661 LEU A CD1   1 
ATOM   8008  C CD2   . LEU A 1 2661 ? 140.877 192.194 160.567 1.00 75.41  ? 2661 LEU A CD2   1 
ATOM   8009  N N     . PHE A 1 2662 ? 138.861 189.059 163.791 1.00 71.85  ? 2662 PHE A N     1 
ATOM   8010  C CA    . PHE A 1 2662 ? 138.614 187.785 164.458 1.00 71.85  ? 2662 PHE A CA    1 
ATOM   8011  C C     . PHE A 1 2662 ? 139.475 186.723 163.791 1.00 71.85  ? 2662 PHE A C     1 
ATOM   8012  O O     . PHE A 1 2662 ? 139.168 186.251 162.695 1.00 71.85  ? 2662 PHE A O     1 
ATOM   8013  C CB    . PHE A 1 2662 ? 137.132 187.434 164.394 1.00 71.85  ? 2662 PHE A CB    1 
ATOM   8014  C CG    . PHE A 1 2662 ? 136.819 186.006 164.744 1.00 71.85  ? 2662 PHE A CG    1 
ATOM   8015  C CD1   . PHE A 1 2662 ? 137.564 185.314 165.680 1.00 71.85  ? 2662 PHE A CD1   1 
ATOM   8016  C CD2   . PHE A 1 2662 ? 135.762 185.359 164.137 1.00 71.85  ? 2662 PHE A CD2   1 
ATOM   8017  C CE1   . PHE A 1 2662 ? 137.274 184.004 165.982 1.00 71.85  ? 2662 PHE A CE1   1 
ATOM   8018  C CE2   . PHE A 1 2662 ? 135.463 184.053 164.447 1.00 71.85  ? 2662 PHE A CE2   1 
ATOM   8019  C CZ    . PHE A 1 2662 ? 136.218 183.377 165.373 1.00 71.85  ? 2662 PHE A CZ    1 
ATOM   8020  N N     . CYS A 1 2663 ? 140.557 186.338 164.458 1.00 77.02  ? 2663 CYS A N     1 
ATOM   8021  C CA    . CYS A 1 2663 ? 141.474 185.320 163.956 1.00 77.02  ? 2663 CYS A CA    1 
ATOM   8022  C C     . CYS A 1 2663 ? 141.232 184.042 164.748 1.00 77.02  ? 2663 CYS A C     1 
ATOM   8023  O O     . CYS A 1 2663 ? 141.753 183.879 165.853 1.00 77.02  ? 2663 CYS A O     1 
ATOM   8024  C CB    . CYS A 1 2663 ? 142.920 185.784 164.086 1.00 77.02  ? 2663 CYS A CB    1 
ATOM   8025  S SG    . CYS A 1 2663 ? 143.218 187.467 163.520 1.00 77.02  ? 2663 CYS A SG    1 
ATOM   8026  N N     . ASP A 1 2664 ? 140.437 183.134 164.189 1.00 83.49  ? 2664 ASP A N     1 
ATOM   8027  C CA    . ASP A 1 2664 ? 140.197 181.877 164.878 1.00 83.49  ? 2664 ASP A CA    1 
ATOM   8028  C C     . ASP A 1 2664 ? 141.408 180.959 164.738 1.00 83.49  ? 2664 ASP A C     1 
ATOM   8029  O O     . ASP A 1 2664 ? 142.229 181.100 163.829 1.00 83.49  ? 2664 ASP A O     1 
ATOM   8030  C CB    . ASP A 1 2664 ? 138.934 181.194 164.352 1.00 83.49  ? 2664 ASP A CB    1 
ATOM   8031  C CG    . ASP A 1 2664 ? 138.939 181.026 162.849 1.00 83.49  ? 2664 ASP A CG    1 
ATOM   8032  O OD1   . ASP A 1 2664 ? 139.951 181.371 162.211 1.00 83.49  ? 2664 ASP A OD1   1 
ATOM   8033  O OD2   . ASP A 1 2664 ? 137.927 180.543 162.301 1.00 83.49  ? 2664 ASP A OD2   1 
ATOM   8034  N N     . GLU A 1 2665 ? 141.507 180.006 165.657 1.00 85.74  ? 2665 GLU A N     1 
ATOM   8035  C CA    . GLU A 1 2665 ? 142.641 179.090 165.735 1.00 85.74  ? 2665 GLU A CA    1 
ATOM   8036  C C     . GLU A 1 2665 ? 143.946 179.875 165.824 1.00 85.74  ? 2665 GLU A C     1 
ATOM   8037  O O     . GLU A 1 2665 ? 144.860 179.731 165.012 1.00 85.74  ? 2665 GLU A O     1 
ATOM   8038  C CB    . GLU A 1 2665 ? 142.649 178.126 164.551 1.00 85.74  ? 2665 GLU A CB    1 
ATOM   8039  C CG    . GLU A 1 2665 ? 141.402 177.236 164.374 1.00 85.74  ? 2665 GLU A CG    1 
ATOM   8040  C CD    . GLU A 1 2665 ? 141.005 176.385 165.589 1.00 85.74  ? 2665 GLU A CD    1 
ATOM   8041  O OE1   . GLU A 1 2665 ? 141.407 176.667 166.735 1.00 85.74  ? 2665 GLU A OE1   1 
ATOM   8042  O OE2   . GLU A 1 2665 ? 140.257 175.404 165.380 1.00 85.74  ? 2665 GLU A OE2   1 
ATOM   8043  N N     . ILE A 1 2666 ? 144.009 180.729 166.846 1.00 80.98  ? 2666 ILE A N     1 
ATOM   8044  C CA    . ILE A 1 2666 ? 145.122 181.660 166.978 1.00 80.98  ? 2666 ILE A CA    1 
ATOM   8045  C C     . ILE A 1 2666 ? 146.431 180.927 167.240 1.00 80.98  ? 2666 ILE A C     1 
ATOM   8046  O O     . ILE A 1 2666 ? 147.504 181.412 166.863 1.00 80.98  ? 2666 ILE A O     1 
ATOM   8047  C CB    . ILE A 1 2666 ? 144.807 182.689 168.079 1.00 80.98  ? 2666 ILE A CB    1 
ATOM   8048  C CG1   . ILE A 1 2666 ? 145.812 183.837 168.047 1.00 80.98  ? 2666 ILE A CG1   1 
ATOM   8049  C CG2   . ILE A 1 2666 ? 144.772 182.031 169.442 1.00 80.98  ? 2666 ILE A CG2   1 
ATOM   8050  C CD1   . ILE A 1 2666 ? 146.014 184.410 166.682 1.00 80.98  ? 2666 ILE A CD1   1 
ATOM   8051  N N     . ASN A 1 2667 ? 146.379 179.760 167.877 1.00 82.40  ? 2667 ASN A N     1 
ATOM   8052  C CA    . ASN A 1 2667 ? 147.591 179.042 168.243 1.00 82.40  ? 2667 ASN A CA    1 
ATOM   8053  C C     . ASN A 1 2667 ? 148.054 178.059 167.180 1.00 82.40  ? 2667 ASN A C     1 
ATOM   8054  O O     . ASN A 1 2667 ? 149.136 177.481 167.323 1.00 82.40  ? 2667 ASN A O     1 
ATOM   8055  C CB    . ASN A 1 2667 ? 147.379 178.297 169.562 1.00 82.40  ? 2667 ASN A CB    1 
ATOM   8056  C CG    . ASN A 1 2667 ? 146.183 177.384 169.521 1.00 82.40  ? 2667 ASN A CG    1 
ATOM   8057  O OD1   . ASN A 1 2667 ? 145.528 177.248 168.491 1.00 82.40  ? 2667 ASN A OD1   1 
ATOM   8058  N ND2   . ASN A 1 2667 ? 145.883 176.754 170.647 1.00 82.40  ? 2667 ASN A ND2   1 
ATOM   8059  N N     . LEU A 1 2668 ? 147.277 177.859 166.128 1.00 89.62  ? 2668 LEU A N     1 
ATOM   8060  C CA    . LEU A 1 2668 ? 147.622 176.903 165.084 1.00 89.62  ? 2668 LEU A CA    1 
ATOM   8061  C C     . LEU A 1 2668 ? 148.893 177.231 164.300 1.00 89.62  ? 2668 LEU A C     1 
ATOM   8062  O O     . LEU A 1 2668 ? 149.559 176.295 163.844 1.00 89.62  ? 2668 LEU A O     1 
ATOM   8063  C CB    . LEU A 1 2668 ? 146.459 176.749 164.105 1.00 89.62  ? 2668 LEU A CB    1 
ATOM   8064  C CG    . LEU A 1 2668 ? 145.644 175.472 164.309 1.00 89.62  ? 2668 LEU A CG    1 
ATOM   8065  C CD1   . LEU A 1 2668 ? 144.517 175.392 163.302 1.00 89.62  ? 2668 LEU A CD1   1 
ATOM   8066  C CD2   . LEU A 1 2668 ? 146.535 174.250 164.216 1.00 89.62  ? 2668 LEU A CD2   1 
ATOM   8067  N N     . PRO A 1 2669 ? 149.259 178.502 164.084 1.00 94.61  ? 2669 PRO A N     1 
ATOM   8068  C CA    . PRO A 1 2669 ? 150.485 178.779 163.326 1.00 94.61  ? 2669 PRO A CA    1 
ATOM   8069  C C     . PRO A 1 2669 ? 151.689 178.046 163.895 1.00 94.61  ? 2669 PRO A C     1 
ATOM   8070  O O     . PRO A 1 2669 ? 151.884 177.974 165.109 1.00 94.61  ? 2669 PRO A O     1 
ATOM   8071  C CB    . PRO A 1 2669 ? 150.641 180.295 163.454 1.00 94.61  ? 2669 PRO A CB    1 
ATOM   8072  C CG    . PRO A 1 2669 ? 149.265 180.781 163.526 1.00 94.61  ? 2669 PRO A CG    1 
ATOM   8073  C CD    . PRO A 1 2669 ? 148.464 179.735 164.252 1.00 94.61  ? 2669 PRO A CD    1 
ATOM   8074  N N     . ASP A 1 2670 ? 152.491 177.490 162.992 1.00 102.64 ? 2670 ASP A N     1 
ATOM   8075  C CA    . ASP A 1 2670 ? 153.587 176.618 163.384 1.00 102.64 ? 2670 ASP A CA    1 
ATOM   8076  C C     . ASP A 1 2670 ? 154.681 177.385 164.117 1.00 102.64 ? 2670 ASP A C     1 
ATOM   8077  O O     . ASP A 1 2670 ? 154.867 178.590 163.932 1.00 102.64 ? 2670 ASP A O     1 
ATOM   8078  C CB    . ASP A 1 2670 ? 154.166 175.907 162.159 1.00 102.64 ? 2670 ASP A CB    1 
ATOM   8079  C CG    . ASP A 1 2670 ? 154.765 176.868 161.141 1.00 102.64 ? 2670 ASP A CG    1 
ATOM   8080  O OD1   . ASP A 1 2670 ? 155.303 176.384 160.124 1.00 102.64 ? 2670 ASP A OD1   1 
ATOM   8081  O OD2   . ASP A 1 2670 ? 154.663 178.099 161.323 1.00 102.64 ? 2670 ASP A OD2   1 
ATOM   8082  N N     . MET A 1 2671 ? 155.399 176.668 164.972 1.00 98.64  ? 2671 MET A N     1 
ATOM   8083  C CA    . MET A 1 2671 ? 156.536 177.239 165.671 1.00 98.64  ? 2671 MET A CA    1 
ATOM   8084  C C     . MET A 1 2671 ? 157.785 177.067 164.821 1.00 98.64  ? 2671 MET A C     1 
ATOM   8085  O O     . MET A 1 2671 ? 158.041 175.985 164.286 1.00 98.64  ? 2671 MET A O     1 
ATOM   8086  C CB    . MET A 1 2671 ? 156.717 176.558 167.026 1.00 98.64  ? 2671 MET A CB    1 
ATOM   8087  C CG    . MET A 1 2671 ? 157.819 177.140 167.879 1.00 98.64  ? 2671 MET A CG    1 
ATOM   8088  S SD    . MET A 1 2671 ? 157.161 178.320 169.069 1.00 98.64  ? 2671 MET A SD    1 
ATOM   8089  C CE    . MET A 1 2671 ? 156.222 177.224 170.127 1.00 98.64  ? 2671 MET A CE    1 
ATOM   8090  N N     . ASP A 1 2672 ? 158.565 178.135 164.691 1.00 102.27 ? 2672 ASP A N     1 
ATOM   8091  C CA    . ASP A 1 2672 ? 159.760 178.083 163.860 1.00 102.27 ? 2672 ASP A CA    1 
ATOM   8092  C C     . ASP A 1 2672 ? 160.830 177.251 164.563 1.00 102.27 ? 2672 ASP A C     1 
ATOM   8093  O O     . ASP A 1 2672 ? 160.593 176.637 165.607 1.00 102.27 ? 2672 ASP A O     1 
ATOM   8094  C CB    . ASP A 1 2672 ? 160.250 179.489 163.528 1.00 102.27 ? 2672 ASP A CB    1 
ATOM   8095  C CG    . ASP A 1 2672 ? 160.854 180.200 164.721 1.00 102.27 ? 2672 ASP A CG    1 
ATOM   8096  O OD1   . ASP A 1 2672 ? 160.595 179.793 165.873 1.00 102.27 ? 2672 ASP A OD1   1 
ATOM   8097  O OD2   . ASP A 1 2672 ? 161.600 181.177 164.504 1.00 102.27 ? 2672 ASP A OD2   1 
ATOM   8098  N N     . LYS A 1 2673 ? 162.031 177.217 163.987 1.00 103.00 ? 2673 LYS A N     1 
ATOM   8099  C CA    . LYS A 1 2673 ? 163.104 176.434 164.585 1.00 103.00 ? 2673 LYS A CA    1 
ATOM   8100  C C     . LYS A 1 2673 ? 163.502 176.978 165.949 1.00 103.00 ? 2673 LYS A C     1 
ATOM   8101  O O     . LYS A 1 2673 ? 163.813 176.204 166.861 1.00 103.00 ? 2673 LYS A O     1 
ATOM   8102  C CB    . LYS A 1 2673 ? 164.310 176.399 163.646 1.00 103.00 ? 2673 LYS A CB    1 
ATOM   8103  C CG    . LYS A 1 2673 ? 165.646 176.240 164.345 1.00 103.00 ? 2673 LYS A CG    1 
ATOM   8104  C CD    . LYS A 1 2673 ? 166.692 175.682 163.402 1.00 103.00 ? 2673 LYS A CD    1 
ATOM   8105  C CE    . LYS A 1 2673 ? 166.414 174.227 163.082 1.00 103.00 ? 2673 LYS A CE    1 
ATOM   8106  N NZ    . LYS A 1 2673 ? 166.377 173.399 164.316 1.00 103.00 ? 2673 LYS A NZ    1 
ATOM   8107  N N     . TYR A 1 2674 ? 163.475 178.296 166.118 1.00 103.32 ? 2674 TYR A N     1 
ATOM   8108  C CA    . TYR A 1 2674 ? 163.978 178.949 167.321 1.00 103.32 ? 2674 TYR A CA    1 
ATOM   8109  C C     . TYR A 1 2674 ? 162.847 179.403 168.238 1.00 103.32 ? 2674 TYR A C     1 
ATOM   8110  O O     . TYR A 1 2674 ? 162.931 180.445 168.888 1.00 103.32 ? 2674 TYR A O     1 
ATOM   8111  C CB    . TYR A 1 2674 ? 164.877 180.120 166.945 1.00 103.32 ? 2674 TYR A CB    1 
ATOM   8112  C CG    . TYR A 1 2674 ? 165.942 179.744 165.941 1.00 103.32 ? 2674 TYR A CG    1 
ATOM   8113  C CD1   . TYR A 1 2674 ? 167.162 179.230 166.353 1.00 103.32 ? 2674 TYR A CD1   1 
ATOM   8114  C CD2   . TYR A 1 2674 ? 165.720 179.890 164.579 1.00 103.32 ? 2674 TYR A CD2   1 
ATOM   8115  C CE1   . TYR A 1 2674 ? 168.134 178.880 165.437 1.00 103.32 ? 2674 TYR A CE1   1 
ATOM   8116  C CE2   . TYR A 1 2674 ? 166.683 179.544 163.658 1.00 103.32 ? 2674 TYR A CE2   1 
ATOM   8117  C CZ    . TYR A 1 2674 ? 167.888 179.039 164.091 1.00 103.32 ? 2674 TYR A CZ    1 
ATOM   8118  O OH    . TYR A 1 2674 ? 168.851 178.693 163.173 1.00 103.32 ? 2674 TYR A OH    1 
ATOM   8119  N N     . GLY A 1 2675 ? 161.772 178.622 168.286 1.00 101.35 ? 2675 GLY A N     1 
ATOM   8120  C CA    . GLY A 1 2675 ? 160.730 178.808 169.285 1.00 101.35 ? 2675 GLY A CA    1 
ATOM   8121  C C     . GLY A 1 2675 ? 159.988 180.125 169.230 1.00 101.35 ? 2675 GLY A C     1 
ATOM   8122  O O     . GLY A 1 2675 ? 159.727 180.727 170.278 1.00 101.35 ? 2675 GLY A O     1 
ATOM   8123  N N     . THR A 1 2676 ? 159.630 180.585 168.034 1.00 102.18 ? 2676 THR A N     1 
ATOM   8124  C CA    . THR A 1 2676 ? 158.854 181.810 167.900 1.00 102.18 ? 2676 THR A CA    1 
ATOM   8125  C C     . THR A 1 2676 ? 157.789 181.620 166.832 1.00 102.18 ? 2676 THR A C     1 
ATOM   8126  O O     . THR A 1 2676 ? 157.974 180.861 165.878 1.00 102.18 ? 2676 THR A O     1 
ATOM   8127  C CB    . THR A 1 2676 ? 159.736 183.011 167.540 1.00 102.18 ? 2676 THR A CB    1 
ATOM   8128  O OG1   . THR A 1 2676 ? 160.588 182.669 166.441 1.00 102.18 ? 2676 THR A OG1   1 
ATOM   8129  C CG2   . THR A 1 2676 ? 160.588 183.428 168.724 1.00 102.18 ? 2676 THR A CG2   1 
ATOM   8130  N N     . GLN A 1 2677 ? 156.672 182.321 167.002 1.00 90.91  ? 2677 GLN A N     1 
ATOM   8131  C CA    . GLN A 1 2677 ? 155.614 182.377 166.002 1.00 90.91  ? 2677 GLN A CA    1 
ATOM   8132  C C     . GLN A 1 2677 ? 155.562 183.793 165.452 1.00 90.91  ? 2677 GLN A C     1 
ATOM   8133  O O     . GLN A 1 2677 ? 155.208 184.730 166.176 1.00 90.91  ? 2677 GLN A O     1 
ATOM   8134  C CB    . GLN A 1 2677 ? 154.266 181.974 166.596 1.00 90.91  ? 2677 GLN A CB    1 
ATOM   8135  C CG    . GLN A 1 2677 ? 154.361 180.942 167.700 1.00 90.91  ? 2677 GLN A CG    1 
ATOM   8136  C CD    . GLN A 1 2677 ? 153.007 180.401 168.103 1.00 90.91  ? 2677 GLN A CD    1 
ATOM   8137  O OE1   . GLN A 1 2677 ? 152.382 180.894 169.040 1.00 90.91  ? 2677 GLN A OE1   1 
ATOM   8138  N NE2   . GLN A 1 2677 ? 152.544 179.381 167.393 1.00 90.91  ? 2677 GLN A NE2   1 
ATOM   8139  N N     . ARG A 1 2678 ? 155.907 183.943 164.173 1.00 87.53  ? 2678 ARG A N     1 
ATOM   8140  C CA    . ARG A 1 2678 ? 156.094 185.273 163.606 1.00 87.53  ? 2678 ARG A CA    1 
ATOM   8141  C C     . ARG A 1 2678 ? 154.804 186.082 163.636 1.00 87.53  ? 2678 ARG A C     1 
ATOM   8142  O O     . ARG A 1 2678 ? 154.813 187.266 163.992 1.00 87.53  ? 2678 ARG A O     1 
ATOM   8143  C CB    . ARG A 1 2678 ? 156.625 185.152 162.181 1.00 87.53  ? 2678 ARG A CB    1 
ATOM   8144  C CG    . ARG A 1 2678 ? 157.902 184.336 162.079 1.00 87.53  ? 2678 ARG A CG    1 
ATOM   8145  C CD    . ARG A 1 2678 ? 158.893 184.979 161.132 1.00 87.53  ? 2678 ARG A CD    1 
ATOM   8146  N NE    . ARG A 1 2678 ? 158.241 185.439 159.913 1.00 87.53  ? 2678 ARG A NE    1 
ATOM   8147  C CZ    . ARG A 1 2678 ? 158.883 185.863 158.834 1.00 87.53  ? 2678 ARG A CZ    1 
ATOM   8148  N NH1   . ARG A 1 2678 ? 160.204 185.901 158.787 1.00 87.53  ? 2678 ARG A NH1   1 
ATOM   8149  N NH2   . ARG A 1 2678 ? 158.181 186.261 157.777 1.00 87.53  ? 2678 ARG A NH2   1 
ATOM   8150  N N     . VAL A 1 2679 ? 153.681 185.459 163.278 1.00 83.96  ? 2679 VAL A N     1 
ATOM   8151  C CA    . VAL A 1 2679 ? 152.417 186.185 163.259 1.00 83.96  ? 2679 VAL A CA    1 
ATOM   8152  C C     . VAL A 1 2679 ? 152.003 186.581 164.671 1.00 83.96  ? 2679 VAL A C     1 
ATOM   8153  O O     . VAL A 1 2679 ? 151.456 187.668 164.891 1.00 83.96  ? 2679 VAL A O     1 
ATOM   8154  C CB    . VAL A 1 2679 ? 151.335 185.349 162.553 1.00 83.96  ? 2679 VAL A CB    1 
ATOM   8155  C CG1   . VAL A 1 2679 ? 151.233 183.973 163.181 1.00 83.96  ? 2679 VAL A CG1   1 
ATOM   8156  C CG2   . VAL A 1 2679 ? 149.998 186.063 162.598 1.00 83.96  ? 2679 VAL A CG2   1 
ATOM   8157  N N     . ILE A 1 2680 ? 152.259 185.714 165.651 1.00 83.55  ? 2680 ILE A N     1 
ATOM   8158  C CA    . ILE A 1 2680 ? 151.926 186.048 167.031 1.00 83.55  ? 2680 ILE A CA    1 
ATOM   8159  C C     . ILE A 1 2680 ? 152.766 187.219 167.514 1.00 83.55  ? 2680 ILE A C     1 
ATOM   8160  O O     . ILE A 1 2680 ? 152.259 188.133 168.176 1.00 83.55  ? 2680 ILE A O     1 
ATOM   8161  C CB    . ILE A 1 2680 ? 152.093 184.817 167.935 1.00 83.55  ? 2680 ILE A CB    1 
ATOM   8162  C CG1   . ILE A 1 2680 ? 150.949 183.837 167.694 1.00 83.55  ? 2680 ILE A CG1   1 
ATOM   8163  C CG2   . ILE A 1 2680 ? 152.128 185.233 169.389 1.00 83.55  ? 2680 ILE A CG2   1 
ATOM   8164  C CD1   . ILE A 1 2680 ? 149.593 184.487 167.695 1.00 83.55  ? 2680 ILE A CD1   1 
ATOM   8165  N N     . SER A 1 2681 ? 154.061 187.216 167.198 1.00 86.12  ? 2681 SER A N     1 
ATOM   8166  C CA    . SER A 1 2681 ? 154.897 188.353 167.562 1.00 86.12  ? 2681 SER A CA    1 
ATOM   8167  C C     . SER A 1 2681 ? 154.409 189.621 166.881 1.00 86.12  ? 2681 SER A C     1 
ATOM   8168  O O     . SER A 1 2681 ? 154.457 190.706 167.466 1.00 86.12  ? 2681 SER A O     1 
ATOM   8169  C CB    . SER A 1 2681 ? 156.354 188.077 167.202 1.00 86.12  ? 2681 SER A CB    1 
ATOM   8170  O OG    . SER A 1 2681 ? 156.914 187.108 168.067 1.00 86.12  ? 2681 SER A OG    1 
ATOM   8171  N N     . PHE A 1 2682 ? 153.939 189.504 165.641 1.00 84.71  ? 2682 PHE A N     1 
ATOM   8172  C CA    . PHE A 1 2682 ? 153.421 190.666 164.929 1.00 84.71  ? 2682 PHE A CA    1 
ATOM   8173  C C     . PHE A 1 2682 ? 152.184 191.221 165.625 1.00 84.71  ? 2682 PHE A C     1 
ATOM   8174  O O     . PHE A 1 2682 ? 152.040 192.439 165.805 1.00 84.71  ? 2682 PHE A O     1 
ATOM   8175  C CB    . PHE A 1 2682 ? 153.118 190.269 163.486 1.00 84.71  ? 2682 PHE A CB    1 
ATOM   8176  C CG    . PHE A 1 2682 ? 153.068 191.417 162.535 1.00 84.71  ? 2682 PHE A CG    1 
ATOM   8177  C CD1   . PHE A 1 2682 ? 153.860 192.528 162.734 1.00 84.71  ? 2682 PHE A CD1   1 
ATOM   8178  C CD2   . PHE A 1 2682 ? 152.282 191.352 161.402 1.00 84.71  ? 2682 PHE A CD2   1 
ATOM   8179  C CE1   . PHE A 1 2682 ? 153.829 193.578 161.848 1.00 84.71  ? 2682 PHE A CE1   1 
ATOM   8180  C CE2   . PHE A 1 2682 ? 152.254 192.395 160.505 1.00 84.71  ? 2682 PHE A CE2   1 
ATOM   8181  C CZ    . PHE A 1 2682 ? 153.026 193.511 160.730 1.00 84.71  ? 2682 PHE A CZ    1 
ATOM   8182  N N     . ILE A 1 2683 ? 151.287 190.329 166.042 1.00 79.89  ? 2683 ILE A N     1 
ATOM   8183  C CA    . ILE A 1 2683 ? 150.096 190.754 166.768 1.00 79.89  ? 2683 ILE A CA    1 
ATOM   8184  C C     . ILE A 1 2683 ? 150.490 191.429 168.073 1.00 79.89  ? 2683 ILE A C     1 
ATOM   8185  O O     . ILE A 1 2683 ? 149.922 192.460 168.455 1.00 79.89  ? 2683 ILE A O     1 
ATOM   8186  C CB    . ILE A 1 2683 ? 149.164 189.555 167.011 1.00 79.89  ? 2683 ILE A CB    1 
ATOM   8187  C CG1   . ILE A 1 2683 ? 148.588 189.053 165.690 1.00 79.89  ? 2683 ILE A CG1   1 
ATOM   8188  C CG2   . ILE A 1 2683 ? 148.046 189.938 167.956 1.00 79.89  ? 2683 ILE A CG2   1 
ATOM   8189  C CD1   . ILE A 1 2683 ? 147.602 189.998 165.066 1.00 79.89  ? 2683 ILE A CD1   1 
ATOM   8190  N N     . ARG A 1 2684 ? 151.469 190.860 168.777 1.00 83.30  ? 2684 ARG A N     1 
ATOM   8191  C CA    . ARG A 1 2684 ? 151.921 191.461 170.026 1.00 83.30  ? 2684 ARG A CA    1 
ATOM   8192  C C     . ARG A 1 2684 ? 152.512 192.841 169.785 1.00 83.30  ? 2684 ARG A C     1 
ATOM   8193  O O     . ARG A 1 2684 ? 152.285 193.769 170.569 1.00 83.30  ? 2684 ARG A O     1 
ATOM   8194  C CB    . ARG A 1 2684 ? 152.949 190.566 170.710 1.00 83.30  ? 2684 ARG A CB    1 
ATOM   8195  C CG    . ARG A 1 2684 ? 153.448 191.139 172.018 1.00 83.30  ? 2684 ARG A CG    1 
ATOM   8196  C CD    . ARG A 1 2684 ? 154.722 190.472 172.486 1.00 83.30  ? 2684 ARG A CD    1 
ATOM   8197  N NE    . ARG A 1 2684 ? 155.294 191.175 173.627 1.00 83.30  ? 2684 ARG A NE    1 
ATOM   8198  C CZ    . ARG A 1 2684 ? 156.511 191.699 173.652 1.00 83.30  ? 2684 ARG A CZ    1 
ATOM   8199  N NH1   . ARG A 1 2684 ? 157.321 191.617 172.611 1.00 83.30  ? 2684 ARG A NH1   1 
ATOM   8200  N NH2   . ARG A 1 2684 ? 156.926 192.320 174.752 1.00 83.30  ? 2684 ARG A NH2   1 
ATOM   8201  N N     . GLN A 1 2685 ? 153.283 192.992 168.709 1.00 83.47  ? 2685 GLN A N     1 
ATOM   8202  C CA    . GLN A 1 2685 ? 153.864 194.290 168.398 1.00 83.47  ? 2685 GLN A CA    1 
ATOM   8203  C C     . GLN A 1 2685 ? 152.777 195.319 168.144 1.00 83.47  ? 2685 GLN A C     1 
ATOM   8204  O O     . GLN A 1 2685 ? 152.871 196.459 168.614 1.00 83.47  ? 2685 GLN A O     1 
ATOM   8205  C CB    . GLN A 1 2685 ? 154.794 194.180 167.193 1.00 83.47  ? 2685 GLN A CB    1 
ATOM   8206  C CG    . GLN A 1 2685 ? 155.258 195.520 166.659 1.00 83.47  ? 2685 GLN A CG    1 
ATOM   8207  C CD    . GLN A 1 2685 ? 156.000 195.397 165.348 1.00 83.47  ? 2685 GLN A CD    1 
ATOM   8208  O OE1   . GLN A 1 2685 ? 155.459 194.906 164.359 1.00 83.47  ? 2685 GLN A OE1   1 
ATOM   8209  N NE2   . GLN A 1 2685 ? 157.248 195.844 165.332 1.00 83.47  ? 2685 GLN A NE2   1 
ATOM   8210  N N     . MET A 1 2686 ? 151.729 194.938 167.413 1.00 84.93  ? 2686 MET A N     1 
ATOM   8211  C CA    . MET A 1 2686 ? 150.610 195.863 167.268 1.00 84.93  ? 2686 MET A CA    1 
ATOM   8212  C C     . MET A 1 2686 ? 149.946 196.185 168.595 1.00 84.93  ? 2686 MET A C     1 
ATOM   8213  O O     . MET A 1 2686 ? 149.605 197.346 168.836 1.00 84.93  ? 2686 MET A O     1 
ATOM   8214  C CB    . MET A 1 2686 ? 149.543 195.323 166.324 1.00 84.93  ? 2686 MET A CB    1 
ATOM   8215  C CG    . MET A 1 2686 ? 149.860 195.471 164.866 1.00 84.93  ? 2686 MET A CG    1 
ATOM   8216  S SD    . MET A 1 2686 ? 148.975 194.248 163.905 1.00 84.93  ? 2686 MET A SD    1 
ATOM   8217  C CE    . MET A 1 2686 ? 150.301 193.649 162.894 1.00 84.93  ? 2686 MET A CE    1 
ATOM   8218  N N     . VAL A 1 2687 ? 149.752 195.191 169.455 1.00 85.56  ? 2687 VAL A N     1 
ATOM   8219  C CA    . VAL A 1 2687 ? 148.939 195.396 170.647 1.00 85.56  ? 2687 VAL A CA    1 
ATOM   8220  C C     . VAL A 1 2687 ? 149.672 196.249 171.673 1.00 85.56  ? 2687 VAL A C     1 
ATOM   8221  O O     . VAL A 1 2687 ? 149.122 197.222 172.199 1.00 85.56  ? 2687 VAL A O     1 
ATOM   8222  C CB    . VAL A 1 2687 ? 148.527 194.039 171.238 1.00 85.56  ? 2687 VAL A CB    1 
ATOM   8223  C CG1   . VAL A 1 2687 ? 147.977 194.222 172.638 1.00 85.56  ? 2687 VAL A CG1   1 
ATOM   8224  C CG2   . VAL A 1 2687 ? 147.517 193.369 170.336 1.00 85.56  ? 2687 VAL A CG2   1 
ATOM   8225  N N     . GLU A 1 2688 ? 150.919 195.893 171.981 1.00 90.83  ? 2688 GLU A N     1 
ATOM   8226  C CA    . GLU A 1 2688 ? 151.638 196.580 173.049 1.00 90.83  ? 2688 GLU A CA    1 
ATOM   8227  C C     . GLU A 1 2688 ? 152.079 197.975 172.628 1.00 90.83  ? 2688 GLU A C     1 
ATOM   8228  O O     . GLU A 1 2688 ? 151.889 198.942 173.374 1.00 90.83  ? 2688 GLU A O     1 
ATOM   8229  C CB    . GLU A 1 2688 ? 152.843 195.750 173.486 1.00 90.83  ? 2688 GLU A CB    1 
ATOM   8230  C CG    . GLU A 1 2688 ? 153.201 195.906 174.951 1.00 90.83  ? 2688 GLU A CG    1 
ATOM   8231  C CD    . GLU A 1 2688 ? 153.984 197.169 175.228 1.00 90.83  ? 2688 GLU A CD    1 
ATOM   8232  O OE1   . GLU A 1 2688 ? 154.618 197.688 174.287 1.00 90.83  ? 2688 GLU A OE1   1 
ATOM   8233  O OE2   . GLU A 1 2688 ? 153.972 197.641 176.384 1.00 90.83  ? 2688 GLU A OE2   1 
ATOM   8234  N N     . HIS A 1 2689 ? 152.672 198.104 171.442 1.00 85.39  ? 2689 HIS A N     1 
ATOM   8235  C CA    . HIS A 1 2689 ? 153.209 199.385 171.006 1.00 85.39  ? 2689 HIS A CA    1 
ATOM   8236  C C     . HIS A 1 2689 ? 152.207 200.233 170.240 1.00 85.39  ? 2689 HIS A C     1 
ATOM   8237  O O     . HIS A 1 2689 ? 152.448 201.429 170.054 1.00 85.39  ? 2689 HIS A O     1 
ATOM   8238  C CB    . HIS A 1 2689 ? 154.451 199.172 170.140 1.00 85.39  ? 2689 HIS A CB    1 
ATOM   8239  C CG    . HIS A 1 2689 ? 155.480 198.290 170.771 1.00 85.39  ? 2689 HIS A CG    1 
ATOM   8240  N ND1   . HIS A 1 2689 ? 155.857 197.080 170.230 1.00 85.39  ? 2689 HIS A ND1   1 
ATOM   8241  C CD2   . HIS A 1 2689 ? 156.217 198.445 171.895 1.00 85.39  ? 2689 HIS A CD2   1 
ATOM   8242  C CE1   . HIS A 1 2689 ? 156.779 196.526 170.996 1.00 85.39  ? 2689 HIS A CE1   1 
ATOM   8243  N NE2   . HIS A 1 2689 ? 157.015 197.333 172.014 1.00 85.39  ? 2689 HIS A NE2   1 
ATOM   8244  N N     . GLY A 1 2690 ? 151.098 199.654 169.795 1.00 90.29  ? 2690 GLY A N     1 
ATOM   8245  C CA    . GLY A 1 2690 ? 150.099 200.424 169.087 1.00 90.29  ? 2690 GLY A CA    1 
ATOM   8246  C C     . GLY A 1 2690 ? 150.371 200.635 167.618 1.00 90.29  ? 2690 GLY A C     1 
ATOM   8247  O O     . GLY A 1 2690 ? 149.659 201.418 166.980 1.00 90.29  ? 2690 GLY A O     1 
ATOM   8248  N N     . GLY A 1 2691 ? 151.372 199.972 167.058 1.00 91.07  ? 2691 GLY A N     1 
ATOM   8249  C CA    . GLY A 1 2691 ? 151.655 200.147 165.651 1.00 91.07  ? 2691 GLY A CA    1 
ATOM   8250  C C     . GLY A 1 2691 ? 152.714 199.179 165.183 1.00 91.07  ? 2691 GLY A C     1 
ATOM   8251  O O     . GLY A 1 2691 ? 153.176 198.320 165.935 1.00 91.07  ? 2691 GLY A O     1 
ATOM   8252  N N     . PHE A 1 2692 ? 153.096 199.334 163.922 1.00 93.66  ? 2692 PHE A N     1 
ATOM   8253  C CA    . PHE A 1 2692 ? 154.114 198.485 163.324 1.00 93.66  ? 2692 PHE A CA    1 
ATOM   8254  C C     . PHE A 1 2692 ? 154.811 199.276 162.232 1.00 93.66  ? 2692 PHE A C     1 
ATOM   8255  O O     . PHE A 1 2692 ? 154.373 200.364 161.853 1.00 93.66  ? 2692 PHE A O     1 
ATOM   8256  C CB    . PHE A 1 2692 ? 153.512 197.193 162.772 1.00 93.66  ? 2692 PHE A CB    1 
ATOM   8257  C CG    . PHE A 1 2692 ? 152.991 197.318 161.376 1.00 93.66  ? 2692 PHE A CG    1 
ATOM   8258  C CD1   . PHE A 1 2692 ? 151.743 197.860 161.140 1.00 93.66  ? 2692 PHE A CD1   1 
ATOM   8259  C CD2   . PHE A 1 2692 ? 153.738 196.877 160.301 1.00 93.66  ? 2692 PHE A CD2   1 
ATOM   8260  C CE1   . PHE A 1 2692 ? 151.254 197.972 159.857 1.00 93.66  ? 2692 PHE A CE1   1 
ATOM   8261  C CE2   . PHE A 1 2692 ? 153.253 196.987 159.017 1.00 93.66  ? 2692 PHE A CE2   1 
ATOM   8262  C CZ    . PHE A 1 2692 ? 152.010 197.535 158.795 1.00 93.66  ? 2692 PHE A CZ    1 
ATOM   8263  N N     . TYR A 1 2693 ? 155.910 198.722 161.737 1.00 97.60  ? 2693 TYR A N     1 
ATOM   8264  C CA    . TYR A 1 2693 ? 156.732 199.388 160.738 1.00 97.60  ? 2693 TYR A CA    1 
ATOM   8265  C C     . TYR A 1 2693 ? 156.317 198.932 159.348 1.00 97.60  ? 2693 TYR A C     1 
ATOM   8266  O O     . TYR A 1 2693 ? 156.449 197.750 159.015 1.00 97.60  ? 2693 TYR A O     1 
ATOM   8267  C CB    . TYR A 1 2693 ? 158.212 199.098 160.974 1.00 97.60  ? 2693 TYR A CB    1 
ATOM   8268  C CG    . TYR A 1 2693 ? 158.872 200.080 161.903 1.00 97.60  ? 2693 TYR A CG    1 
ATOM   8269  C CD1   . TYR A 1 2693 ? 159.112 201.384 161.504 1.00 97.60  ? 2693 TYR A CD1   1 
ATOM   8270  C CD2   . TYR A 1 2693 ? 159.248 199.708 163.183 1.00 97.60  ? 2693 TYR A CD2   1 
ATOM   8271  C CE1   . TYR A 1 2693 ? 159.712 202.289 162.349 1.00 97.60  ? 2693 TYR A CE1   1 
ATOM   8272  C CE2   . TYR A 1 2693 ? 159.848 200.606 164.037 1.00 97.60  ? 2693 TYR A CE2   1 
ATOM   8273  C CZ    . TYR A 1 2693 ? 160.077 201.896 163.615 1.00 97.60  ? 2693 TYR A CZ    1 
ATOM   8274  O OH    . TYR A 1 2693 ? 160.676 202.800 164.462 1.00 97.60  ? 2693 TYR A OH    1 
ATOM   8275  N N     . ARG A 1 2694 ? 155.823 199.867 158.538 1.00 107.57 ? 2694 ARG A N     1 
ATOM   8276  C CA    . ARG A 1 2694 ? 155.542 199.570 157.141 1.00 107.57 ? 2694 ARG A CA    1 
ATOM   8277  C C     . ARG A 1 2694 ? 156.863 199.366 156.418 1.00 107.57 ? 2694 ARG A C     1 
ATOM   8278  O O     . ARG A 1 2694 ? 157.643 200.310 156.256 1.00 107.57 ? 2694 ARG A O     1 
ATOM   8279  C CB    . ARG A 1 2694 ? 154.736 200.685 156.482 1.00 107.57 ? 2694 ARG A CB    1 
ATOM   8280  C CG    . ARG A 1 2694 ? 154.136 200.259 155.153 1.00 107.57 ? 2694 ARG A CG    1 
ATOM   8281  C CD    . ARG A 1 2694 ? 153.389 201.380 154.457 1.00 107.57 ? 2694 ARG A CD    1 
ATOM   8282  N NE    . ARG A 1 2694 ? 153.982 202.689 154.698 1.00 107.57 ? 2694 ARG A NE    1 
ATOM   8283  C CZ    . ARG A 1 2694 ? 153.570 203.809 154.122 1.00 107.57 ? 2694 ARG A CZ    1 
ATOM   8284  N NH1   . ARG A 1 2694 ? 152.578 203.812 153.247 1.00 107.57 ? 2694 ARG A NH1   1 
ATOM   8285  N NH2   . ARG A 1 2694 ? 154.169 204.956 154.430 1.00 107.57 ? 2694 ARG A NH2   1 
ATOM   8286  N N     . THR A 1 2695 ? 157.113 198.133 155.986 1.00 107.61 ? 2695 THR A N     1 
ATOM   8287  C CA    . THR A 1 2695 ? 158.430 197.773 155.485 1.00 107.61 ? 2695 THR A CA    1 
ATOM   8288  C C     . THR A 1 2695 ? 158.738 198.383 154.124 1.00 107.61 ? 2695 THR A C     1 
ATOM   8289  O O     . THR A 1 2695 ? 159.909 198.424 153.734 1.00 107.61 ? 2695 THR A O     1 
ATOM   8290  C CB    . THR A 1 2695 ? 158.551 196.257 155.409 1.00 107.61 ? 2695 THR A CB    1 
ATOM   8291  O OG1   . THR A 1 2695 ? 157.566 195.748 154.503 1.00 107.61 ? 2695 THR A OG1   1 
ATOM   8292  C CG2   . THR A 1 2695 ? 158.325 195.645 156.775 1.00 107.61 ? 2695 THR A CG2   1 
ATOM   8293  N N     . SER A 1 2696 ? 157.723 198.845 153.391 1.00 108.39 ? 2696 SER A N     1 
ATOM   8294  C CA    . SER A 1 2696 ? 157.975 199.419 152.073 1.00 108.39 ? 2696 SER A CA    1 
ATOM   8295  C C     . SER A 1 2696 ? 158.840 200.668 152.170 1.00 108.39 ? 2696 SER A C     1 
ATOM   8296  O O     . SER A 1 2696 ? 159.792 200.835 151.399 1.00 108.39 ? 2696 SER A O     1 
ATOM   8297  C CB    . SER A 1 2696 ? 156.654 199.738 151.375 1.00 108.39 ? 2696 SER A CB    1 
ATOM   8298  O OG    . SER A 1 2696 ? 156.224 201.052 151.684 1.00 108.39 ? 2696 SER A OG    1 
ATOM   8299  N N     . ASP A 1 2697 ? 158.533 201.554 153.118 1.00 107.96 ? 2697 ASP A N     1 
ATOM   8300  C CA    . ASP A 1 2697 ? 159.305 202.776 153.301 1.00 107.96 ? 2697 ASP A CA    1 
ATOM   8301  C C     . ASP A 1 2697 ? 159.890 202.894 154.701 1.00 107.96 ? 2697 ASP A C     1 
ATOM   8302  O O     . ASP A 1 2697 ? 160.337 203.984 155.079 1.00 107.96 ? 2697 ASP A O     1 
ATOM   8303  C CB    . ASP A 1 2697 ? 158.449 204.008 152.991 1.00 107.96 ? 2697 ASP A CB    1 
ATOM   8304  C CG    . ASP A 1 2697 ? 157.036 203.873 153.500 1.00 107.96 ? 2697 ASP A CG    1 
ATOM   8305  O OD1   . ASP A 1 2697 ? 156.500 202.746 153.473 1.00 107.96 ? 2697 ASP A OD1   1 
ATOM   8306  O OD2   . ASP A 1 2697 ? 156.461 204.895 153.927 1.00 107.96 ? 2697 ASP A OD2   1 
ATOM   8307  N N     . GLN A 1 2698 ? 159.897 201.808 155.475 1.00 106.96 ? 2698 GLN A N     1 
ATOM   8308  C CA    . GLN A 1 2698 ? 160.534 201.778 156.790 1.00 106.96 ? 2698 GLN A CA    1 
ATOM   8309  C C     . GLN A 1 2698 ? 160.009 202.889 157.694 1.00 106.96 ? 2698 GLN A C     1 
ATOM   8310  O O     . GLN A 1 2698 ? 160.767 203.562 158.394 1.00 106.96 ? 2698 GLN A O     1 
ATOM   8311  C CB    . GLN A 1 2698 ? 162.054 201.852 156.658 1.00 106.96 ? 2698 GLN A CB    1 
ATOM   8312  C CG    . GLN A 1 2698 ? 162.699 200.536 156.264 1.00 106.96 ? 2698 GLN A CG    1 
ATOM   8313  C CD    . GLN A 1 2698 ? 162.715 200.315 154.766 1.00 106.96 ? 2698 GLN A CD    1 
ATOM   8314  O OE1   . GLN A 1 2698 ? 162.299 201.177 153.994 1.00 106.96 ? 2698 GLN A OE1   1 
ATOM   8315  N NE2   . GLN A 1 2698 ? 163.200 199.153 154.347 1.00 106.96 ? 2698 GLN A NE2   1 
ATOM   8316  N N     . THR A 1 2699 ? 158.696 203.084 157.677 1.00 104.84 ? 2699 THR A N     1 
ATOM   8317  C CA    . THR A 1 2699 ? 158.040 204.079 158.508 1.00 104.84 ? 2699 THR A CA    1 
ATOM   8318  C C     . THR A 1 2699 ? 157.205 203.400 159.584 1.00 104.84 ? 2699 THR A C     1 
ATOM   8319  O O     . THR A 1 2699 ? 156.807 202.241 159.458 1.00 104.84 ? 2699 THR A O     1 
ATOM   8320  C CB    . THR A 1 2699 ? 157.153 205.005 157.669 1.00 104.84 ? 2699 THR A CB    1 
ATOM   8321  O OG1   . THR A 1 2699 ? 156.770 206.140 158.455 1.00 104.84 ? 2699 THR A OG1   1 
ATOM   8322  C CG2   . THR A 1 2699 ? 155.906 204.273 157.205 1.00 104.84 ? 2699 THR A CG2   1 
ATOM   8323  N N     . TRP A 1 2700 ? 156.947 204.143 160.654 1.00 97.06  ? 2700 TRP A N     1 
ATOM   8324  C CA    . TRP A 1 2700 ? 156.205 203.640 161.806 1.00 97.06  ? 2700 TRP A CA    1 
ATOM   8325  C C     . TRP A 1 2700 ? 154.748 204.058 161.665 1.00 97.06  ? 2700 TRP A C     1 
ATOM   8326  O O     . TRP A 1 2700 ? 154.380 205.183 162.007 1.00 97.06  ? 2700 TRP A O     1 
ATOM   8327  C CB    . TRP A 1 2700 ? 156.808 204.167 163.101 1.00 97.06  ? 2700 TRP A CB    1 
ATOM   8328  C CG    . TRP A 1 2700 ? 156.001 203.834 164.301 1.00 97.06  ? 2700 TRP A CG    1 
ATOM   8329  C CD1   . TRP A 1 2700 ? 155.179 204.669 164.992 1.00 97.06  ? 2700 TRP A CD1   1 
ATOM   8330  C CD2   . TRP A 1 2700 ? 155.926 202.566 164.952 1.00 97.06  ? 2700 TRP A CD2   1 
ATOM   8331  N NE1   . TRP A 1 2700 ? 154.601 204.001 166.041 1.00 97.06  ? 2700 TRP A NE1   1 
ATOM   8332  C CE2   . TRP A 1 2700 ? 155.044 202.705 166.036 1.00 97.06  ? 2700 TRP A CE2   1 
ATOM   8333  C CE3   . TRP A 1 2700 ? 156.523 201.324 164.724 1.00 97.06  ? 2700 TRP A CE3   1 
ATOM   8334  C CZ2   . TRP A 1 2700 ? 154.744 201.652 166.890 1.00 97.06  ? 2700 TRP A CZ2   1 
ATOM   8335  C CZ3   . TRP A 1 2700 ? 156.224 200.281 165.573 1.00 97.06  ? 2700 TRP A CZ3   1 
ATOM   8336  C CH2   . TRP A 1 2700 ? 155.345 200.450 166.642 1.00 97.06  ? 2700 TRP A CH2   1 
ATOM   8337  N N     . VAL A 1 2701 ? 153.915 203.145 161.173 1.00 98.66  ? 2701 VAL A N     1 
ATOM   8338  C CA    . VAL A 1 2701 ? 152.505 203.457 160.995 1.00 98.66  ? 2701 VAL A CA    1 
ATOM   8339  C C     . VAL A 1 2701 ? 151.717 203.024 162.226 1.00 98.66  ? 2701 VAL A C     1 
ATOM   8340  O O     . VAL A 1 2701 ? 151.836 201.901 162.720 1.00 98.66  ? 2701 VAL A O     1 
ATOM   8341  C CB    . VAL A 1 2701 ? 151.949 202.816 159.713 1.00 98.66  ? 2701 VAL A CB    1 
ATOM   8342  C CG1   . VAL A 1 2701 ? 152.264 201.336 159.670 1.00 98.66  ? 2701 VAL A CG1   1 
ATOM   8343  C CG2   . VAL A 1 2701 ? 150.455 203.050 159.616 1.00 98.66  ? 2701 VAL A CG2   1 
ATOM   8344  N N     . LYS A 1 2702 ? 150.898 203.942 162.729 1.00 98.90  ? 2702 LYS A N     1 
ATOM   8345  C CA    . LYS A 1 2702 ? 150.163 203.757 163.971 1.00 98.90  ? 2702 LYS A CA    1 
ATOM   8346  C C     . LYS A 1 2702 ? 148.778 203.210 163.665 1.00 98.90  ? 2702 LYS A C     1 
ATOM   8347  O O     . LYS A 1 2702 ? 148.046 203.786 162.854 1.00 98.90  ? 2702 LYS A O     1 
ATOM   8348  C CB    . LYS A 1 2702 ? 150.050 205.077 164.736 1.00 98.90  ? 2702 LYS A CB    1 
ATOM   8349  C CG    . LYS A 1 2702 ? 149.336 204.967 166.066 1.00 98.90  ? 2702 LYS A CG    1 
ATOM   8350  C CD    . LYS A 1 2702 ? 149.471 206.252 166.861 1.00 98.90  ? 2702 LYS A CD    1 
ATOM   8351  C CE    . LYS A 1 2702 ? 148.177 207.048 166.847 1.00 98.90  ? 2702 LYS A CE    1 
ATOM   8352  N NZ    . LYS A 1 2702 ? 147.121 206.404 167.675 1.00 98.90  ? 2702 LYS A NZ    1 
ATOM   8353  N N     . LEU A 1 2703 ? 148.422 202.105 164.312 1.00 91.68  ? 2703 LEU A N     1 
ATOM   8354  C CA    . LEU A 1 2703 ? 147.096 201.535 164.133 1.00 91.68  ? 2703 LEU A CA    1 
ATOM   8355  C C     . LEU A 1 2703 ? 146.038 202.447 164.735 1.00 91.68  ? 2703 LEU A C     1 
ATOM   8356  O O     . LEU A 1 2703 ? 146.292 203.163 165.707 1.00 91.68  ? 2703 LEU A O     1 
ATOM   8357  C CB    . LEU A 1 2703 ? 147.016 200.156 164.779 1.00 91.68  ? 2703 LEU A CB    1 
ATOM   8358  C CG    . LEU A 1 2703 ? 147.003 198.980 163.810 1.00 91.68  ? 2703 LEU A CG    1 
ATOM   8359  C CD1   . LEU A 1 2703 ? 148.237 199.015 162.936 1.00 91.68  ? 2703 LEU A CD1   1 
ATOM   8360  C CD2   . LEU A 1 2703 ? 146.916 197.673 164.569 1.00 91.68  ? 2703 LEU A CD2   1 
ATOM   8361  N N     . GLU A 1 2704 ? 144.846 202.425 164.148 1.00 100.64 ? 2704 GLU A N     1 
ATOM   8362  C CA    . GLU A 1 2704 ? 143.737 203.207 164.673 1.00 100.64 ? 2704 GLU A CA    1 
ATOM   8363  C C     . GLU A 1 2704 ? 142.432 202.488 164.373 1.00 100.64 ? 2704 GLU A C     1 
ATOM   8364  O O     . GLU A 1 2704 ? 142.218 202.035 163.245 1.00 100.64 ? 2704 GLU A O     1 
ATOM   8365  C CB    . GLU A 1 2704 ? 143.721 204.616 164.074 1.00 100.64 ? 2704 GLU A CB    1 
ATOM   8366  C CG    . GLU A 1 2704 ? 142.396 205.357 164.230 1.00 100.64 ? 2704 GLU A CG    1 
ATOM   8367  C CD    . GLU A 1 2704 ? 141.965 205.536 165.679 1.00 100.64 ? 2704 GLU A CD    1 
ATOM   8368  O OE1   . GLU A 1 2704 ? 142.811 205.404 166.589 1.00 100.64 ? 2704 GLU A OE1   1 
ATOM   8369  O OE2   . GLU A 1 2704 ? 140.770 205.816 165.908 1.00 100.64 ? 2704 GLU A OE2   1 
ATOM   8370  N N     . ARG A 1 2705 ? 141.569 202.393 165.386 1.00 92.80  ? 2705 ARG A N     1 
ATOM   8371  C CA    . ARG A 1 2705 ? 140.270 201.733 165.264 1.00 92.80  ? 2705 ARG A CA    1 
ATOM   8372  C C     . ARG A 1 2705 ? 140.419 200.299 164.766 1.00 92.80  ? 2705 ARG A C     1 
ATOM   8373  O O     . ARG A 1 2705 ? 139.610 199.809 163.977 1.00 92.80  ? 2705 ARG A O     1 
ATOM   8374  C CB    . ARG A 1 2705 ? 139.325 202.525 164.359 1.00 92.80  ? 2705 ARG A CB    1 
ATOM   8375  C CG    . ARG A 1 2705 ? 138.596 203.649 165.068 1.00 92.80  ? 2705 ARG A CG    1 
ATOM   8376  C CD    . ARG A 1 2705 ? 137.583 204.321 164.158 1.00 92.80  ? 2705 ARG A CD    1 
ATOM   8377  N NE    . ARG A 1 2705 ? 137.739 203.917 162.767 1.00 92.80  ? 2705 ARG A NE    1 
ATOM   8378  C CZ    . ARG A 1 2705 ? 138.159 204.720 161.801 1.00 92.80  ? 2705 ARG A CZ    1 
ATOM   8379  N NH1   . ARG A 1 2705 ? 138.478 205.981 162.041 1.00 92.80  ? 2705 ARG A NH1   1 
ATOM   8380  N NH2   . ARG A 1 2705 ? 138.262 204.247 160.562 1.00 92.80  ? 2705 ARG A NH2   1 
ATOM   8381  N N     . ILE A 1 2706 ? 141.458 199.618 165.236 1.00 84.45  ? 2706 ILE A N     1 
ATOM   8382  C CA    . ILE A 1 2706 ? 141.734 198.234 164.872 1.00 84.45  ? 2706 ILE A CA    1 
ATOM   8383  C C     . ILE A 1 2706 ? 141.736 197.402 166.143 1.00 84.45  ? 2706 ILE A C     1 
ATOM   8384  O O     . ILE A 1 2706 ? 142.327 197.800 167.152 1.00 84.45  ? 2706 ILE A O     1 
ATOM   8385  C CB    . ILE A 1 2706 ? 143.071 198.092 164.123 1.00 84.45  ? 2706 ILE A CB    1 
ATOM   8386  C CG1   . ILE A 1 2706 ? 143.059 198.922 162.844 1.00 84.45  ? 2706 ILE A CG1   1 
ATOM   8387  C CG2   . ILE A 1 2706 ? 143.335 196.640 163.778 1.00 84.45  ? 2706 ILE A CG2   1 
ATOM   8388  C CD1   . ILE A 1 2706 ? 141.905 198.606 161.935 1.00 84.45  ? 2706 ILE A CD1   1 
ATOM   8389  N N     . GLN A 1 2707 ? 141.070 196.255 166.094 1.00 78.23  ? 2707 GLN A N     1 
ATOM   8390  C CA    . GLN A 1 2707 ? 140.954 195.365 167.234 1.00 78.23  ? 2707 GLN A CA    1 
ATOM   8391  C C     . GLN A 1 2707 ? 141.293 193.953 166.787 1.00 78.23  ? 2707 GLN A C     1 
ATOM   8392  O O     . GLN A 1 2707 ? 141.195 193.625 165.604 1.00 78.23  ? 2707 GLN A O     1 
ATOM   8393  C CB    . GLN A 1 2707 ? 139.546 195.411 167.823 1.00 78.23  ? 2707 GLN A CB    1 
ATOM   8394  C CG    . GLN A 1 2707 ? 139.471 195.994 169.210 1.00 78.23  ? 2707 GLN A CG    1 
ATOM   8395  C CD    . GLN A 1 2707 ? 138.046 196.200 169.660 1.00 78.23  ? 2707 GLN A CD    1 
ATOM   8396  O OE1   . GLN A 1 2707 ? 137.184 195.358 169.423 1.00 78.23  ? 2707 GLN A OE1   1 
ATOM   8397  N NE2   . GLN A 1 2707 ? 137.786 197.328 170.306 1.00 78.23  ? 2707 GLN A NE2   1 
ATOM   8398  N N     . PHE A 1 2708 ? 141.701 193.122 167.737 1.00 73.83  ? 2708 PHE A N     1 
ATOM   8399  C CA    . PHE A 1 2708 ? 142.020 191.732 167.455 1.00 73.83  ? 2708 PHE A CA    1 
ATOM   8400  C C     . PHE A 1 2708 ? 141.260 190.830 168.410 1.00 73.83  ? 2708 PHE A C     1 
ATOM   8401  O O     . PHE A 1 2708 ? 141.157 191.125 169.602 1.00 73.83  ? 2708 PHE A O     1 
ATOM   8402  C CB    . PHE A 1 2708 ? 143.515 191.479 167.569 1.00 73.83  ? 2708 PHE A CB    1 
ATOM   8403  C CG    . PHE A 1 2708 ? 144.312 192.163 166.513 1.00 73.83  ? 2708 PHE A CG    1 
ATOM   8404  C CD1   . PHE A 1 2708 ? 144.334 191.671 165.223 1.00 73.83  ? 2708 PHE A CD1   1 
ATOM   8405  C CD2   . PHE A 1 2708 ? 145.024 193.309 166.799 1.00 73.83  ? 2708 PHE A CD2   1 
ATOM   8406  C CE1   . PHE A 1 2708 ? 145.060 192.302 164.242 1.00 73.83  ? 2708 PHE A CE1   1 
ATOM   8407  C CE2   . PHE A 1 2708 ? 145.754 193.943 165.820 1.00 73.83  ? 2708 PHE A CE2   1 
ATOM   8408  C CZ    . PHE A 1 2708 ? 145.769 193.439 164.540 1.00 73.83  ? 2708 PHE A CZ    1 
ATOM   8409  N N     . VAL A 1 2709 ? 140.710 189.744 167.881 1.00 67.46  ? 2709 VAL A N     1 
ATOM   8410  C CA    . VAL A 1 2709 ? 139.989 188.762 168.678 1.00 67.46  ? 2709 VAL A CA    1 
ATOM   8411  C C     . VAL A 1 2709 ? 140.370 187.377 168.179 1.00 67.46  ? 2709 VAL A C     1 
ATOM   8412  O O     . VAL A 1 2709 ? 140.437 187.141 166.969 1.00 67.46  ? 2709 VAL A O     1 
ATOM   8413  C CB    . VAL A 1 2709 ? 138.465 188.975 168.600 1.00 67.46  ? 2709 VAL A CB    1 
ATOM   8414  C CG1   . VAL A 1 2709 ? 137.742 187.809 169.219 1.00 67.46  ? 2709 VAL A CG1   1 
ATOM   8415  C CG2   . VAL A 1 2709 ? 138.073 190.264 169.289 1.00 67.46  ? 2709 VAL A CG2   1 
ATOM   8416  N N     . GLY A 1 2710 ? 140.623 186.456 169.112 1.00 67.64  ? 2710 GLY A N     1 
ATOM   8417  C CA    . GLY A 1 2710 ? 141.043 185.116 168.777 1.00 67.64  ? 2710 GLY A CA    1 
ATOM   8418  C C     . GLY A 1 2710 ? 140.139 184.062 169.400 1.00 67.64  ? 2710 GLY A C     1 
ATOM   8419  O O     . GLY A 1 2710 ? 139.357 184.334 170.315 1.00 67.64  ? 2710 GLY A O     1 
ATOM   8420  N N     . ALA A 1 2711 ? 140.258 182.845 168.876 1.00 66.88  ? 2711 ALA A N     1 
ATOM   8421  C CA    . ALA A 1 2711 ? 139.538 181.697 169.410 1.00 66.88  ? 2711 ALA A CA    1 
ATOM   8422  C C     . ALA A 1 2711 ? 140.211 180.416 168.947 1.00 66.88  ? 2711 ALA A C     1 
ATOM   8423  O O     . ALA A 1 2711 ? 140.315 180.172 167.742 1.00 66.88  ? 2711 ALA A O     1 
ATOM   8424  C CB    . ALA A 1 2711 ? 138.075 181.721 168.975 1.00 66.88  ? 2711 ALA A CB    1 
ATOM   8425  N N     . CYS A 1 2712 ? 140.665 179.586 169.882 1.00 70.70  ? 2712 CYS A N     1 
ATOM   8426  C CA    . CYS A 1 2712 ? 141.510 178.463 169.513 1.00 70.70  ? 2712 CYS A CA    1 
ATOM   8427  C C     . CYS A 1 2712 ? 141.258 177.285 170.439 1.00 70.70  ? 2712 CYS A C     1 
ATOM   8428  O O     . CYS A 1 2712 ? 140.751 177.437 171.552 1.00 70.70  ? 2712 CYS A O     1 
ATOM   8429  C CB    . CYS A 1 2712 ? 142.989 178.847 169.555 1.00 70.70  ? 2712 CYS A CB    1 
ATOM   8430  S SG    . CYS A 1 2712 ? 143.644 179.018 171.226 1.00 70.70  ? 2712 CYS A SG    1 
ATOM   8431  N N     . ASN A 1 2713 ? 141.640 176.108 169.961 1.00 74.75  ? 2713 ASN A N     1 
ATOM   8432  C CA    . ASN A 1 2713 ? 141.549 174.875 170.720 1.00 74.75  ? 2713 ASN A CA    1 
ATOM   8433  C C     . ASN A 1 2713 ? 142.596 174.852 171.828 1.00 74.75  ? 2713 ASN A C     1 
ATOM   8434  O O     . ASN A 1 2713 ? 143.559 175.621 171.799 1.00 74.75  ? 2713 ASN A O     1 
ATOM   8435  C CB    . ASN A 1 2713 ? 141.739 173.683 169.790 1.00 74.75  ? 2713 ASN A CB    1 
ATOM   8436  C CG    . ASN A 1 2713 ? 140.501 173.374 168.987 1.00 74.75  ? 2713 ASN A CG    1 
ATOM   8437  O OD1   . ASN A 1 2713 ? 139.436 173.120 169.544 1.00 74.75  ? 2713 ASN A OD1   1 
ATOM   8438  N ND2   . ASN A 1 2713 ? 140.632 173.395 167.668 1.00 74.75  ? 2713 ASN A ND2   1 
ATOM   8439  N N     . PRO A 1 2714 ? 142.425 173.991 172.828 1.00 73.90  ? 2714 PRO A N     1 
ATOM   8440  C CA    . PRO A 1 2714 ? 143.424 173.880 173.892 1.00 73.90  ? 2714 PRO A CA    1 
ATOM   8441  C C     . PRO A 1 2714 ? 144.776 173.485 173.330 1.00 73.90  ? 2714 PRO A C     1 
ATOM   8442  O O     . PRO A 1 2714 ? 144.853 172.758 172.329 1.00 73.90  ? 2714 PRO A O     1 
ATOM   8443  C CB    . PRO A 1 2714 ? 142.858 172.778 174.795 1.00 73.90  ? 2714 PRO A CB    1 
ATOM   8444  C CG    . PRO A 1 2714 ? 141.406 172.821 174.564 1.00 73.90  ? 2714 PRO A CG    1 
ATOM   8445  C CD    . PRO A 1 2714 ? 141.223 173.193 173.126 1.00 73.90  ? 2714 PRO A CD    1 
ATOM   8446  N N     . PRO A 1 2715 ? 145.866 173.954 173.939 1.00 76.50  ? 2715 PRO A N     1 
ATOM   8447  C CA    . PRO A 1 2715 ? 147.199 173.632 173.408 1.00 76.50  ? 2715 PRO A CA    1 
ATOM   8448  C C     . PRO A 1 2715 ? 147.532 172.153 173.438 1.00 76.50  ? 2715 PRO A C     1 
ATOM   8449  O O     . PRO A 1 2715 ? 148.413 171.721 172.686 1.00 76.50  ? 2715 PRO A O     1 
ATOM   8450  C CB    . PRO A 1 2715 ? 148.138 174.435 174.316 1.00 76.50  ? 2715 PRO A CB    1 
ATOM   8451  C CG    . PRO A 1 2715 ? 147.368 174.630 175.571 1.00 76.50  ? 2715 PRO A CG    1 
ATOM   8452  C CD    . PRO A 1 2715 ? 145.937 174.766 175.162 1.00 76.50  ? 2715 PRO A CD    1 
ATOM   8453  N N     . THR A 1 2716 ? 146.867 171.362 174.280 1.00 80.49  ? 2716 THR A N     1 
ATOM   8454  C CA    . THR A 1 2716 ? 147.163 169.937 174.342 1.00 80.49  ? 2716 THR A CA    1 
ATOM   8455  C C     . THR A 1 2716 ? 146.728 169.195 173.086 1.00 80.49  ? 2716 THR A C     1 
ATOM   8456  O O     . THR A 1 2716 ? 147.275 168.127 172.797 1.00 80.49  ? 2716 THR A O     1 
ATOM   8457  C CB    . THR A 1 2716 ? 146.491 169.308 175.562 1.00 80.49  ? 2716 THR A CB    1 
ATOM   8458  O OG1   . THR A 1 2716 ? 145.115 169.045 175.267 1.00 80.49  ? 2716 THR A OG1   1 
ATOM   8459  C CG2   . THR A 1 2716 ? 146.575 170.244 176.752 1.00 80.49  ? 2716 THR A CG2   1 
ATOM   8460  N N     . ASP A 1 2717 ? 145.763 169.725 172.344 1.00 87.92  ? 2717 ASP A N     1 
ATOM   8461  C CA    . ASP A 1 2717 ? 145.314 169.060 171.132 1.00 87.92  ? 2717 ASP A CA    1 
ATOM   8462  C C     . ASP A 1 2717 ? 146.446 169.028 170.109 1.00 87.92  ? 2717 ASP A C     1 
ATOM   8463  O O     . ASP A 1 2717 ? 147.141 170.033 169.921 1.00 87.92  ? 2717 ASP A O     1 
ATOM   8464  C CB    . ASP A 1 2717 ? 144.090 169.773 170.553 1.00 87.92  ? 2717 ASP A CB    1 
ATOM   8465  C CG    . ASP A 1 2717 ? 143.866 169.466 169.082 1.00 87.92  ? 2717 ASP A CG    1 
ATOM   8466  O OD1   . ASP A 1 2717 ? 143.874 168.280 168.704 1.00 87.92  ? 2717 ASP A OD1   1 
ATOM   8467  O OD2   . ASP A 1 2717 ? 143.651 170.412 168.299 1.00 87.92  ? 2717 ASP A OD2   1 
ATOM   8468  N N     . PRO A 1 2718 ? 146.673 167.892 169.451 1.00 85.32  ? 2718 PRO A N     1 
ATOM   8469  C CA    . PRO A 1 2718 ? 147.761 167.810 168.472 1.00 85.32  ? 2718 PRO A CA    1 
ATOM   8470  C C     . PRO A 1 2718 ? 147.623 168.857 167.378 1.00 85.32  ? 2718 PRO A C     1 
ATOM   8471  O O     . PRO A 1 2718 ? 146.524 169.151 166.904 1.00 85.32  ? 2718 PRO A O     1 
ATOM   8472  C CB    . PRO A 1 2718 ? 147.618 166.394 167.912 1.00 85.32  ? 2718 PRO A CB    1 
ATOM   8473  C CG    . PRO A 1 2718 ? 147.032 165.620 169.035 1.00 85.32  ? 2718 PRO A CG    1 
ATOM   8474  C CD    . PRO A 1 2718 ? 146.129 166.564 169.782 1.00 85.32  ? 2718 PRO A CD    1 
ATOM   8475  N N     . GLY A 1 2719 ? 148.762 169.415 166.977 1.00 87.59  ? 2719 GLY A N     1 
ATOM   8476  C CA    . GLY A 1 2719 ? 148.803 170.491 166.014 1.00 87.59  ? 2719 GLY A CA    1 
ATOM   8477  C C     . GLY A 1 2719 ? 148.770 171.883 166.604 1.00 87.59  ? 2719 GLY A C     1 
ATOM   8478  O O     . GLY A 1 2719 ? 148.962 172.853 165.862 1.00 87.59  ? 2719 GLY A O     1 
ATOM   8479  N N     . ARG A 1 2720 ? 148.548 172.016 167.908 1.00 85.57  ? 2720 ARG A N     1 
ATOM   8480  C CA    . ARG A 1 2720 ? 148.451 173.312 168.565 1.00 85.57  ? 2720 ARG A CA    1 
ATOM   8481  C C     . ARG A 1 2720 ? 149.691 173.556 169.412 1.00 85.57  ? 2720 ARG A C     1 
ATOM   8482  O O     . ARG A 1 2720 ? 150.116 172.676 170.167 1.00 85.57  ? 2720 ARG A O     1 
ATOM   8483  C CB    . ARG A 1 2720 ? 147.197 173.395 169.437 1.00 85.57  ? 2720 ARG A CB    1 
ATOM   8484  C CG    . ARG A 1 2720 ? 145.967 173.895 168.707 1.00 85.57  ? 2720 ARG A CG    1 
ATOM   8485  C CD    . ARG A 1 2720 ? 145.424 172.837 167.773 1.00 85.57  ? 2720 ARG A CD    1 
ATOM   8486  N NE    . ARG A 1 2720 ? 144.460 173.370 166.820 1.00 85.57  ? 2720 ARG A NE    1 
ATOM   8487  C CZ    . ARG A 1 2720 ? 143.746 172.625 165.987 1.00 85.57  ? 2720 ARG A CZ    1 
ATOM   8488  N NH1   . ARG A 1 2720 ? 143.849 171.307 165.979 1.00 85.57  ? 2720 ARG A NH1   1 
ATOM   8489  N NH2   . ARG A 1 2720 ? 142.902 173.216 165.148 1.00 85.57  ? 2720 ARG A NH2   1 
ATOM   8490  N N     . LYS A 1 2721 ? 150.260 174.752 169.289 1.00 82.95  ? 2721 LYS A N     1 
ATOM   8491  C CA    . LYS A 1 2721 ? 151.444 175.129 170.036 1.00 82.95  ? 2721 LYS A CA    1 
ATOM   8492  C C     . LYS A 1 2721 ? 151.113 176.232 171.030 1.00 82.95  ? 2721 LYS A C     1 
ATOM   8493  O O     . LYS A 1 2721 ? 150.378 177.164 170.693 1.00 82.95  ? 2721 LYS A O     1 
ATOM   8494  C CB    . LYS A 1 2721 ? 152.554 175.613 169.099 1.00 82.95  ? 2721 LYS A CB    1 
ATOM   8495  C CG    . LYS A 1 2721 ? 152.923 174.619 168.017 1.00 82.95  ? 2721 LYS A CG    1 
ATOM   8496  C CD    . LYS A 1 2721 ? 152.205 174.936 166.719 1.00 82.95  ? 2721 LYS A CD    1 
ATOM   8497  C CE    . LYS A 1 2721 ? 152.358 173.810 165.717 1.00 82.95  ? 2721 LYS A CE    1 
ATOM   8498  N NZ    . LYS A 1 2721 ? 151.488 174.019 164.530 1.00 82.95  ? 2721 LYS A NZ    1 
ATOM   8499  N N     . PRO A 1 2722 ? 151.628 176.152 172.254 1.00 79.18  ? 2722 PRO A N     1 
ATOM   8500  C CA    . PRO A 1 2722 ? 151.313 177.179 173.252 1.00 79.18  ? 2722 PRO A CA    1 
ATOM   8501  C C     . PRO A 1 2722 ? 151.820 178.546 172.822 1.00 79.18  ? 2722 PRO A C     1 
ATOM   8502  O O     . PRO A 1 2722 ? 152.886 178.673 172.218 1.00 79.18  ? 2722 PRO A O     1 
ATOM   8503  C CB    . PRO A 1 2722 ? 152.031 176.682 174.510 1.00 79.18  ? 2722 PRO A CB    1 
ATOM   8504  C CG    . PRO A 1 2722 ? 153.116 175.803 173.999 1.00 79.18  ? 2722 PRO A CG    1 
ATOM   8505  C CD    . PRO A 1 2722 ? 152.566 175.145 172.773 1.00 79.18  ? 2722 PRO A CD    1 
ATOM   8506  N N     . LEU A 1 2723 ? 151.040 179.573 173.143 1.00 81.62  ? 2723 LEU A N     1 
ATOM   8507  C CA    . LEU A 1 2723 ? 151.393 180.934 172.770 1.00 81.62  ? 2723 LEU A CA    1 
ATOM   8508  C C     . LEU A 1 2723 ? 152.517 181.462 173.650 1.00 81.62  ? 2723 LEU A C     1 
ATOM   8509  O O     . LEU A 1 2723 ? 152.713 181.017 174.783 1.00 81.62  ? 2723 LEU A O     1 
ATOM   8510  C CB    . LEU A 1 2723 ? 150.176 181.847 172.883 1.00 81.62  ? 2723 LEU A CB    1 
ATOM   8511  C CG    . LEU A 1 2723 ? 149.054 181.591 171.883 1.00 81.62  ? 2723 LEU A CG    1 
ATOM   8512  C CD1   . LEU A 1 2723 ? 147.924 182.569 172.109 1.00 81.62  ? 2723 LEU A CD1   1 
ATOM   8513  C CD2   . LEU A 1 2723 ? 149.581 181.697 170.468 1.00 81.62  ? 2723 LEU A CD2   1 
ATOM   8514  N N     . SER A 1 2724 ? 153.258 182.428 173.117 1.00 78.42  ? 2724 SER A N     1 
ATOM   8515  C CA    . SER A 1 2724 ? 154.332 183.049 173.876 1.00 78.42  ? 2724 SER A CA    1 
ATOM   8516  C C     . SER A 1 2724 ? 153.767 183.836 175.051 1.00 78.42  ? 2724 SER A C     1 
ATOM   8517  O O     . SER A 1 2724 ? 152.709 184.460 174.947 1.00 78.42  ? 2724 SER A O     1 
ATOM   8518  C CB    . SER A 1 2724 ? 155.152 183.967 172.976 1.00 78.42  ? 2724 SER A CB    1 
ATOM   8519  O OG    . SER A 1 2724 ? 154.308 184.838 172.246 1.00 78.42  ? 2724 SER A OG    1 
ATOM   8520  N N     . HIS A 1 2725 ? 154.485 183.804 176.175 1.00 78.44  ? 2725 HIS A N     1 
ATOM   8521  C CA    . HIS A 1 2725 ? 154.014 184.494 177.372 1.00 78.44  ? 2725 HIS A CA    1 
ATOM   8522  C C     . HIS A 1 2725 ? 153.920 185.995 177.147 1.00 78.44  ? 2725 HIS A C     1 
ATOM   8523  O O     . HIS A 1 2725 ? 153.005 186.650 177.660 1.00 78.44  ? 2725 HIS A O     1 
ATOM   8524  C CB    . HIS A 1 2725 ? 154.937 184.192 178.549 1.00 78.44  ? 2725 HIS A CB    1 
ATOM   8525  C CG    . HIS A 1 2725 ? 154.628 182.905 179.243 1.00 78.44  ? 2725 HIS A CG    1 
ATOM   8526  N ND1   . HIS A 1 2725 ? 154.609 181.693 178.589 1.00 78.44  ? 2725 HIS A ND1   1 
ATOM   8527  C CD2   . HIS A 1 2725 ? 154.330 182.640 180.536 1.00 78.44  ? 2725 HIS A CD2   1 
ATOM   8528  C CE1   . HIS A 1 2725 ? 154.310 180.737 179.449 1.00 78.44  ? 2725 HIS A CE1   1 
ATOM   8529  N NE2   . HIS A 1 2725 ? 154.135 181.285 180.638 1.00 78.44  ? 2725 HIS A NE2   1 
ATOM   8530  N N     . ARG A 1 2726 ? 154.860 186.560 176.388 1.00 79.65  ? 2726 ARG A N     1 
ATOM   8531  C CA    . ARG A 1 2726 ? 154.835 187.996 176.139 1.00 79.65  ? 2726 ARG A CA    1 
ATOM   8532  C C     . ARG A 1 2726 ? 153.553 188.408 175.435 1.00 79.65  ? 2726 ARG A C     1 
ATOM   8533  O O     . ARG A 1 2726 ? 152.938 189.419 175.790 1.00 79.65  ? 2726 ARG A O     1 
ATOM   8534  C CB    . ARG A 1 2726 ? 156.052 188.409 175.316 1.00 79.65  ? 2726 ARG A CB    1 
ATOM   8535  C CG    . ARG A 1 2726 ? 157.367 187.896 175.858 1.00 79.65  ? 2726 ARG A CG    1 
ATOM   8536  C CD    . ARG A 1 2726 ? 158.519 188.453 175.055 1.00 79.65  ? 2726 ARG A CD    1 
ATOM   8537  N NE    . ARG A 1 2726 ? 158.732 189.865 175.344 1.00 79.65  ? 2726 ARG A NE    1 
ATOM   8538  C CZ    . ARG A 1 2726 ? 159.684 190.603 174.794 1.00 79.65  ? 2726 ARG A CZ    1 
ATOM   8539  N NH1   . ARG A 1 2726 ? 160.528 190.096 173.912 1.00 79.65  ? 2726 ARG A NH1   1 
ATOM   8540  N NH2   . ARG A 1 2726 ? 159.794 191.882 175.138 1.00 79.65  ? 2726 ARG A NH2   1 
ATOM   8541  N N     . PHE A 1 2727 ? 153.132 187.641 174.430 1.00 74.63  ? 2727 PHE A N     1 
ATOM   8542  C CA    . PHE A 1 2727 ? 151.843 187.912 173.809 1.00 74.63  ? 2727 PHE A CA    1 
ATOM   8543  C C     . PHE A 1 2727 ? 150.700 187.551 174.743 1.00 74.63  ? 2727 PHE A C     1 
ATOM   8544  O O     . PHE A 1 2727 ? 149.692 188.263 174.804 1.00 74.63  ? 2727 PHE A O     1 
ATOM   8545  C CB    . PHE A 1 2727 ? 151.708 187.142 172.501 1.00 74.63  ? 2727 PHE A CB    1 
ATOM   8546  C CG    . PHE A 1 2727 ? 150.315 187.135 171.958 1.00 74.63  ? 2727 PHE A CG    1 
ATOM   8547  C CD1   . PHE A 1 2727 ? 149.701 188.314 171.591 1.00 74.63  ? 2727 PHE A CD1   1 
ATOM   8548  C CD2   . PHE A 1 2727 ? 149.609 185.956 171.842 1.00 74.63  ? 2727 PHE A CD2   1 
ATOM   8549  C CE1   . PHE A 1 2727 ? 148.418 188.315 171.098 1.00 74.63  ? 2727 PHE A CE1   1 
ATOM   8550  C CE2   . PHE A 1 2727 ? 148.325 185.954 171.352 1.00 74.63  ? 2727 PHE A CE2   1 
ATOM   8551  C CZ    . PHE A 1 2727 ? 147.729 187.134 170.979 1.00 74.63  ? 2727 PHE A CZ    1 
ATOM   8552  N N     . LEU A 1 2728 ? 150.841 186.449 175.482 1.00 78.26  ? 2728 LEU A N     1 
ATOM   8553  C CA    . LEU A 1 2728 ? 149.759 185.987 176.342 1.00 78.26  ? 2728 LEU A CA    1 
ATOM   8554  C C     . LEU A 1 2728 ? 149.417 187.001 177.420 1.00 78.26  ? 2728 LEU A C     1 
ATOM   8555  O O     . LEU A 1 2728 ? 148.298 186.995 177.941 1.00 78.26  ? 2728 LEU A O     1 
ATOM   8556  C CB    . LEU A 1 2728 ? 150.129 184.653 176.983 1.00 78.26  ? 2728 LEU A CB    1 
ATOM   8557  C CG    . LEU A 1 2728 ? 148.974 183.703 177.286 1.00 78.26  ? 2728 LEU A CG    1 
ATOM   8558  C CD1   . LEU A 1 2728 ? 147.834 183.916 176.315 1.00 78.26  ? 2728 LEU A CD1   1 
ATOM   8559  C CD2   . LEU A 1 2728 ? 149.460 182.270 177.231 1.00 78.26  ? 2728 LEU A CD2   1 
ATOM   8560  N N     . ARG A 1 2729 ? 150.362 187.872 177.772 1.00 74.80  ? 2729 ARG A N     1 
ATOM   8561  C CA    . ARG A 1 2729 ? 150.110 188.836 178.836 1.00 74.80  ? 2729 ARG A CA    1 
ATOM   8562  C C     . ARG A 1 2729 ? 148.986 189.800 178.476 1.00 74.80  ? 2729 ARG A C     1 
ATOM   8563  O O     . ARG A 1 2729 ? 148.197 190.182 179.346 1.00 74.80  ? 2729 ARG A O     1 
ATOM   8564  C CB    . ARG A 1 2729 ? 151.394 189.599 179.154 1.00 74.80  ? 2729 ARG A CB    1 
ATOM   8565  C CG    . ARG A 1 2729 ? 151.175 191.002 179.670 1.00 74.80  ? 2729 ARG A CG    1 
ATOM   8566  C CD    . ARG A 1 2729 ? 152.486 191.653 180.041 1.00 74.80  ? 2729 ARG A CD    1 
ATOM   8567  N NE    . ARG A 1 2729 ? 152.344 193.097 180.156 1.00 74.80  ? 2729 ARG A NE    1 
ATOM   8568  C CZ    . ARG A 1 2729 ? 153.068 193.970 179.473 1.00 74.80  ? 2729 ARG A CZ    1 
ATOM   8569  N NH1   . ARG A 1 2729 ? 153.996 193.577 178.618 1.00 74.80  ? 2729 ARG A NH1   1 
ATOM   8570  N NH2   . ARG A 1 2729 ? 152.855 195.270 179.652 1.00 74.80  ? 2729 ARG A NH2   1 
ATOM   8571  N N     . HIS A 1 2730 ? 148.885 190.197 177.212 1.00 76.68  ? 2730 HIS A N     1 
ATOM   8572  C CA    . HIS A 1 2730 ? 147.912 191.203 176.810 1.00 76.68  ? 2730 HIS A CA    1 
ATOM   8573  C C     . HIS A 1 2730 ? 146.568 190.627 176.386 1.00 76.68  ? 2730 HIS A C     1 
ATOM   8574  O O     . HIS A 1 2730 ? 145.644 191.402 176.128 1.00 76.68  ? 2730 HIS A O     1 
ATOM   8575  C CB    . HIS A 1 2730 ? 148.472 192.051 175.669 1.00 76.68  ? 2730 HIS A CB    1 
ATOM   8576  C CG    . HIS A 1 2730 ? 149.871 192.519 175.899 1.00 76.68  ? 2730 HIS A CG    1 
ATOM   8577  N ND1   . HIS A 1 2730 ? 150.909 192.208 175.048 1.00 76.68  ? 2730 HIS A ND1   1 
ATOM   8578  C CD2   . HIS A 1 2730 ? 150.406 193.278 176.883 1.00 76.68  ? 2730 HIS A CD2   1 
ATOM   8579  C CE1   . HIS A 1 2730 ? 152.023 192.753 175.500 1.00 76.68  ? 2730 HIS A CE1   1 
ATOM   8580  N NE2   . HIS A 1 2730 ? 151.746 193.409 176.612 1.00 76.68  ? 2730 HIS A NE2   1 
ATOM   8581  N N     . VAL A 1 2731 ? 146.424 189.311 176.307 1.00 70.74  ? 2731 VAL A N     1 
ATOM   8582  C CA    . VAL A 1 2731 ? 145.211 188.685 175.799 1.00 70.74  ? 2731 VAL A CA    1 
ATOM   8583  C C     . VAL A 1 2731 ? 144.604 187.819 176.896 1.00 70.74  ? 2731 VAL A C     1 
ATOM   8584  O O     . VAL A 1 2731 ? 145.085 186.721 177.176 1.00 70.74  ? 2731 VAL A O     1 
ATOM   8585  C CB    . VAL A 1 2731 ? 145.486 187.864 174.525 1.00 70.74  ? 2731 VAL A CB    1 
ATOM   8586  C CG1   . VAL A 1 2731 ? 145.623 188.787 173.336 1.00 70.74  ? 2731 VAL A CG1   1 
ATOM   8587  C CG2   . VAL A 1 2731 ? 146.746 187.041 174.672 1.00 70.74  ? 2731 VAL A CG2   1 
ATOM   8588  N N     . PRO A 1 2732 ? 143.542 188.285 177.545 1.00 67.47  ? 2732 PRO A N     1 
ATOM   8589  C CA    . PRO A 1 2732 ? 142.803 187.415 178.462 1.00 67.47  ? 2732 PRO A CA    1 
ATOM   8590  C C     . PRO A 1 2732 ? 142.159 186.260 177.713 1.00 67.47  ? 2732 PRO A C     1 
ATOM   8591  O O     . PRO A 1 2732 ? 141.787 186.382 176.546 1.00 67.47  ? 2732 PRO A O     1 
ATOM   8592  C CB    . PRO A 1 2732 ? 141.747 188.348 179.060 1.00 67.47  ? 2732 PRO A CB    1 
ATOM   8593  C CG    . PRO A 1 2732 ? 141.607 189.438 178.057 1.00 67.47  ? 2732 PRO A CG    1 
ATOM   8594  C CD    . PRO A 1 2732 ? 142.981 189.642 177.512 1.00 67.47  ? 2732 PRO A CD    1 
ATOM   8595  N N     . VAL A 1 2733 ? 142.026 185.129 178.401 1.00 67.85  ? 2733 VAL A N     1 
ATOM   8596  C CA    . VAL A 1 2733 ? 141.470 183.914 177.820 1.00 67.85  ? 2733 VAL A CA    1 
ATOM   8597  C C     . VAL A 1 2733 ? 140.306 183.447 178.677 1.00 67.85  ? 2733 VAL A C     1 
ATOM   8598  O O     . VAL A 1 2733 ? 140.388 183.452 179.910 1.00 67.85  ? 2733 VAL A O     1 
ATOM   8599  C CB    . VAL A 1 2733 ? 142.529 182.802 177.697 1.00 67.85  ? 2733 VAL A CB    1 
ATOM   8600  C CG1   . VAL A 1 2733 ? 143.396 183.034 176.482 1.00 67.85  ? 2733 VAL A CG1   1 
ATOM   8601  C CG2   . VAL A 1 2733 ? 143.376 182.750 178.944 1.00 67.85  ? 2733 VAL A CG2   1 
ATOM   8602  N N     . VAL A 1 2734 ? 139.222 183.043 178.023 1.00 65.27  ? 2734 VAL A N     1 
ATOM   8603  C CA    . VAL A 1 2734 ? 138.043 182.511 178.692 1.00 65.27  ? 2734 VAL A CA    1 
ATOM   8604  C C     . VAL A 1 2734 ? 137.821 181.092 178.196 1.00 65.27  ? 2734 VAL A C     1 
ATOM   8605  O O     . VAL A 1 2734 ? 137.769 180.855 176.985 1.00 65.27  ? 2734 VAL A O     1 
ATOM   8606  C CB    . VAL A 1 2734 ? 136.800 183.379 178.432 1.00 65.27  ? 2734 VAL A CB    1 
ATOM   8607  C CG1   . VAL A 1 2734 ? 135.543 182.594 178.730 1.00 65.27  ? 2734 VAL A CG1   1 
ATOM   8608  C CG2   . VAL A 1 2734 ? 136.852 184.631 179.275 1.00 65.27  ? 2734 VAL A CG2   1 
ATOM   8609  N N     . TYR A 1 2735 ? 137.690 180.154 179.128 1.00 72.32  ? 2735 TYR A N     1 
ATOM   8610  C CA    . TYR A 1 2735 ? 137.504 178.749 178.787 1.00 72.32  ? 2735 TYR A CA    1 
ATOM   8611  C C     . TYR A 1 2735 ? 136.029 178.520 178.488 1.00 72.32  ? 2735 TYR A C     1 
ATOM   8612  O O     . TYR A 1 2735 ? 135.185 178.621 179.383 1.00 72.32  ? 2735 TYR A O     1 
ATOM   8613  C CB    . TYR A 1 2735 ? 137.982 177.849 179.921 1.00 72.32  ? 2735 TYR A CB    1 
ATOM   8614  C CG    . TYR A 1 2735 ? 137.993 176.380 179.579 1.00 72.32  ? 2735 TYR A CG    1 
ATOM   8615  C CD1   . TYR A 1 2735 ? 138.602 175.923 178.423 1.00 72.32  ? 2735 TYR A CD1   1 
ATOM   8616  C CD2   . TYR A 1 2735 ? 137.400 175.449 180.416 1.00 72.32  ? 2735 TYR A CD2   1 
ATOM   8617  C CE1   . TYR A 1 2735 ? 138.619 174.583 178.111 1.00 72.32  ? 2735 TYR A CE1   1 
ATOM   8618  C CE2   . TYR A 1 2735 ? 137.411 174.108 180.110 1.00 72.32  ? 2735 TYR A CE2   1 
ATOM   8619  C CZ    . TYR A 1 2735 ? 138.021 173.680 178.958 1.00 72.32  ? 2735 TYR A CZ    1 
ATOM   8620  O OH    . TYR A 1 2735 ? 138.033 172.341 178.651 1.00 72.32  ? 2735 TYR A OH    1 
ATOM   8621  N N     . VAL A 1 2736 ? 135.719 178.216 177.234 1.00 69.56  ? 2736 VAL A N     1 
ATOM   8622  C CA    . VAL A 1 2736 ? 134.343 177.984 176.803 1.00 69.56  ? 2736 VAL A CA    1 
ATOM   8623  C C     . VAL A 1 2736 ? 134.135 176.474 176.824 1.00 69.56  ? 2736 VAL A C     1 
ATOM   8624  O O     . VAL A 1 2736 ? 134.369 175.776 175.839 1.00 69.56  ? 2736 VAL A O     1 
ATOM   8625  C CB    . VAL A 1 2736 ? 134.064 178.586 175.431 1.00 69.56  ? 2736 VAL A CB    1 
ATOM   8626  C CG1   . VAL A 1 2736 ? 132.589 178.492 175.114 1.00 69.56  ? 2736 VAL A CG1   1 
ATOM   8627  C CG2   . VAL A 1 2736 ? 134.518 180.027 175.389 1.00 69.56  ? 2736 VAL A CG2   1 
ATOM   8628  N N     . ASP A 1 2737 ? 133.679 175.965 177.964 1.00 79.32  ? 2737 ASP A N     1 
ATOM   8629  C CA    . ASP A 1 2737 ? 133.441 174.540 178.111 1.00 79.32  ? 2737 ASP A CA    1 
ATOM   8630  C C     . ASP A 1 2737 ? 132.199 174.122 177.332 1.00 79.32  ? 2737 ASP A C     1 
ATOM   8631  O O     . ASP A 1 2737 ? 131.478 174.946 176.766 1.00 79.32  ? 2737 ASP A O     1 
ATOM   8632  C CB    . ASP A 1 2737 ? 133.287 174.169 179.584 1.00 79.32  ? 2737 ASP A CB    1 
ATOM   8633  C CG    . ASP A 1 2737 ? 133.774 172.769 179.881 1.00 79.32  ? 2737 ASP A CG    1 
ATOM   8634  O OD1   . ASP A 1 2737 ? 134.351 172.135 178.975 1.00 79.32  ? 2737 ASP A OD1   1 
ATOM   8635  O OD2   . ASP A 1 2737 ? 133.577 172.297 181.018 1.00 79.32  ? 2737 ASP A OD2   1 
ATOM   8636  N N     . TYR A 1 2738 ? 131.963 172.816 177.296 1.00 81.78  ? 2738 TYR A N     1 
ATOM   8637  C CA    . TYR A 1 2738 ? 130.774 172.298 176.643 1.00 81.78  ? 2738 TYR A CA    1 
ATOM   8638  C C     . TYR A 1 2738 ? 129.534 172.771 177.398 1.00 81.78  ? 2738 TYR A C     1 
ATOM   8639  O O     . TYR A 1 2738 ? 129.574 172.915 178.625 1.00 81.78  ? 2738 TYR A O     1 
ATOM   8640  C CB    . TYR A 1 2738 ? 130.810 170.771 176.593 1.00 81.78  ? 2738 TYR A CB    1 
ATOM   8641  C CG    . TYR A 1 2738 ? 131.720 170.208 175.524 1.00 81.78  ? 2738 TYR A CG    1 
ATOM   8642  C CD1   . TYR A 1 2738 ? 131.713 170.719 174.239 1.00 81.78  ? 2738 TYR A CD1   1 
ATOM   8643  C CD2   . TYR A 1 2738 ? 132.588 169.165 175.807 1.00 81.78  ? 2738 TYR A CD2   1 
ATOM   8644  C CE1   . TYR A 1 2738 ? 132.543 170.206 173.265 1.00 81.78  ? 2738 TYR A CE1   1 
ATOM   8645  C CE2   . TYR A 1 2738 ? 133.419 168.647 174.842 1.00 81.78  ? 2738 TYR A CE2   1 
ATOM   8646  C CZ    . TYR A 1 2738 ? 133.394 169.170 173.572 1.00 81.78  ? 2738 TYR A CZ    1 
ATOM   8647  O OH    . TYR A 1 2738 ? 134.226 168.655 172.606 1.00 81.78  ? 2738 TYR A OH    1 
ATOM   8648  N N     . PRO A 1 2739 ? 128.433 173.042 176.703 1.00 80.53  ? 2739 PRO A N     1 
ATOM   8649  C CA    . PRO A 1 2739 ? 127.247 173.574 177.382 1.00 80.53  ? 2739 PRO A CA    1 
ATOM   8650  C C     . PRO A 1 2739 ? 126.714 172.595 178.414 1.00 80.53  ? 2739 PRO A C     1 
ATOM   8651  O O     . PRO A 1 2739 ? 126.787 171.378 178.240 1.00 80.53  ? 2739 PRO A O     1 
ATOM   8652  C CB    . PRO A 1 2739 ? 126.249 173.781 176.239 1.00 80.53  ? 2739 PRO A CB    1 
ATOM   8653  C CG    . PRO A 1 2739 ? 127.088 173.871 175.010 1.00 80.53  ? 2739 PRO A CG    1 
ATOM   8654  C CD    . PRO A 1 2739 ? 128.242 172.951 175.248 1.00 80.53  ? 2739 PRO A CD    1 
ATOM   8655  N N     . GLY A 1 2740 ? 126.191 173.139 179.507 1.00 89.48  ? 2740 GLY A N     1 
ATOM   8656  C CA    . GLY A 1 2740 ? 125.602 172.325 180.541 1.00 89.48  ? 2740 GLY A CA    1 
ATOM   8657  C C     . GLY A 1 2740 ? 124.277 171.739 180.102 1.00 89.48  ? 2740 GLY A C     1 
ATOM   8658  O O     . GLY A 1 2740 ? 123.603 172.278 179.222 1.00 89.48  ? 2740 GLY A O     1 
ATOM   8659  N N     . PRO A 1 2741 ? 123.864 170.636 180.735 1.00 87.80  ? 2741 PRO A N     1 
ATOM   8660  C CA    . PRO A 1 2741 ? 122.633 169.958 180.294 1.00 87.80  ? 2741 PRO A CA    1 
ATOM   8661  C C     . PRO A 1 2741 ? 121.411 170.857 180.260 1.00 87.80  ? 2741 PRO A C     1 
ATOM   8662  O O     . PRO A 1 2741 ? 120.594 170.733 179.341 1.00 87.80  ? 2741 PRO A O     1 
ATOM   8663  C CB    . PRO A 1 2741 ? 122.473 168.833 181.321 1.00 87.80  ? 2741 PRO A CB    1 
ATOM   8664  C CG    . PRO A 1 2741 ? 123.849 168.596 181.832 1.00 87.80  ? 2741 PRO A CG    1 
ATOM   8665  C CD    . PRO A 1 2741 ? 124.513 169.935 181.853 1.00 87.80  ? 2741 PRO A CD    1 
ATOM   8666  N N     . ALA A 1 2742 ? 121.259 171.766 181.225 1.00 87.91  ? 2742 ALA A N     1 
ATOM   8667  C CA    . ALA A 1 2742 ? 120.128 172.689 181.177 1.00 87.91  ? 2742 ALA A CA    1 
ATOM   8668  C C     . ALA A 1 2742 ? 120.200 173.566 179.935 1.00 87.91  ? 2742 ALA A C     1 
ATOM   8669  O O     . ALA A 1 2742 ? 119.176 173.855 179.299 1.00 87.91  ? 2742 ALA A O     1 
ATOM   8670  C CB    . ALA A 1 2742 ? 120.085 173.546 182.442 1.00 87.91  ? 2742 ALA A CB    1 
ATOM   8671  N N     . SER A 1 2743 ? 121.408 173.991 179.572 1.00 86.19  ? 2743 SER A N     1 
ATOM   8672  C CA    . SER A 1 2743 ? 121.572 174.803 178.375 1.00 86.19  ? 2743 SER A CA    1 
ATOM   8673  C C     . SER A 1 2743 ? 121.158 174.039 177.124 1.00 86.19  ? 2743 SER A C     1 
ATOM   8674  O O     . SER A 1 2743 ? 120.459 174.588 176.262 1.00 86.19  ? 2743 SER A O     1 
ATOM   8675  C CB    . SER A 1 2743 ? 123.017 175.274 178.265 1.00 86.19  ? 2743 SER A CB    1 
ATOM   8676  O OG    . SER A 1 2743 ? 123.472 175.758 179.514 1.00 86.19  ? 2743 SER A OG    1 
ATOM   8677  N N     . LEU A 1 2744 ? 121.587 172.778 176.998 1.00 85.75  ? 2744 LEU A N     1 
ATOM   8678  C CA    . LEU A 1 2744 ? 121.161 171.984 175.851 1.00 85.75  ? 2744 LEU A CA    1 
ATOM   8679  C C     . LEU A 1 2744 ? 119.654 171.800 175.841 1.00 85.75  ? 2744 LEU A C     1 
ATOM   8680  O O     . LEU A 1 2744 ? 119.022 171.884 174.782 1.00 85.75  ? 2744 LEU A O     1 
ATOM   8681  C CB    . LEU A 1 2744 ? 121.850 170.618 175.813 1.00 85.75  ? 2744 LEU A CB    1 
ATOM   8682  C CG    . LEU A 1 2744 ? 123.345 170.405 175.588 1.00 85.75  ? 2744 LEU A CG    1 
ATOM   8683  C CD1   . LEU A 1 2744 ? 123.740 171.094 174.299 1.00 85.75  ? 2744 LEU A CD1   1 
ATOM   8684  C CD2   . LEU A 1 2744 ? 124.175 170.888 176.722 1.00 85.75  ? 2744 LEU A CD2   1 
ATOM   8685  N N     . THR A 1 2745 ? 119.060 171.543 177.008 1.00 89.58  ? 2745 THR A N     1 
ATOM   8686  C CA    . THR A 1 2745 ? 117.615 171.362 177.052 1.00 89.58  ? 2745 THR A CA    1 
ATOM   8687  C C     . THR A 1 2745 ? 116.917 172.601 176.521 1.00 89.58  ? 2745 THR A C     1 
ATOM   8688  O O     . THR A 1 2745 ? 116.029 172.506 175.673 1.00 89.58  ? 2745 THR A O     1 
ATOM   8689  C CB    . THR A 1 2745 ? 117.139 171.056 178.471 1.00 89.58  ? 2745 THR A CB    1 
ATOM   8690  O OG1   . THR A 1 2745 ? 117.673 172.025 179.378 1.00 89.58  ? 2745 THR A OG1   1 
ATOM   8691  C CG2   . THR A 1 2745 ? 117.585 169.663 178.896 1.00 89.58  ? 2745 THR A CG2   1 
ATOM   8692  N N     . GLN A 1 2746 ? 117.352 173.780 176.966 1.00 90.97  ? 2746 GLN A N     1 
ATOM   8693  C CA    . GLN A 1 2746 ? 116.721 175.011 176.499 1.00 90.97  ? 2746 GLN A CA    1 
ATOM   8694  C C     . GLN A 1 2746 ? 116.901 175.194 174.996 1.00 90.97  ? 2746 GLN A C     1 
ATOM   8695  O O     . GLN A 1 2746 ? 115.924 175.396 174.261 1.00 90.97  ? 2746 GLN A O     1 
ATOM   8696  C CB    . GLN A 1 2746 ? 117.287 176.213 177.249 1.00 90.97  ? 2746 GLN A CB    1 
ATOM   8697  C CG    . GLN A 1 2746 ? 116.819 177.538 176.680 1.00 90.97  ? 2746 GLN A CG    1 
ATOM   8698  C CD    . GLN A 1 2746 ? 117.589 178.712 177.231 1.00 90.97  ? 2746 GLN A CD    1 
ATOM   8699  O OE1   . GLN A 1 2746 ? 118.479 178.549 178.063 1.00 90.97  ? 2746 GLN A OE1   1 
ATOM   8700  N NE2   . GLN A 1 2746 ? 117.260 179.908 176.760 1.00 90.97  ? 2746 GLN A NE2   1 
ATOM   8701  N N     . ILE A 1 2747 ? 118.146 175.122 174.518 1.00 87.73  ? 2747 ILE A N     1 
ATOM   8702  C CA    . ILE A 1 2747 ? 118.402 175.461 173.120 1.00 87.73  ? 2747 ILE A CA    1 
ATOM   8703  C C     . ILE A 1 2747 ? 117.706 174.471 172.195 1.00 87.73  ? 2747 ILE A C     1 
ATOM   8704  O O     . ILE A 1 2747 ? 117.075 174.859 171.202 1.00 87.73  ? 2747 ILE A O     1 
ATOM   8705  C CB    . ILE A 1 2747 ? 119.915 175.545 172.843 1.00 87.73  ? 2747 ILE A CB    1 
ATOM   8706  C CG1   . ILE A 1 2747 ? 120.168 175.855 171.372 1.00 87.73  ? 2747 ILE A CG1   1 
ATOM   8707  C CG2   . ILE A 1 2747 ? 120.611 174.257 173.196 1.00 87.73  ? 2747 ILE A CG2   1 
ATOM   8708  C CD1   . ILE A 1 2747 ? 121.631 175.922 171.015 1.00 87.73  ? 2747 ILE A CD1   1 
ATOM   8709  N N     . TYR A 1 2748 ? 117.770 173.182 172.515 1.00 91.98  ? 2748 TYR A N     1 
ATOM   8710  C CA    . TYR A 1 2748 ? 117.181 172.205 171.619 1.00 91.98  ? 2748 TYR A CA    1 
ATOM   8711  C C     . TYR A 1 2748 ? 115.685 172.041 171.835 1.00 91.98  ? 2748 TYR A C     1 
ATOM   8712  O O     . TYR A 1 2748 ? 114.999 171.568 170.928 1.00 91.98  ? 2748 TYR A O     1 
ATOM   8713  C CB    . TYR A 1 2748 ? 117.927 170.882 171.753 1.00 91.98  ? 2748 TYR A CB    1 
ATOM   8714  C CG    . TYR A 1 2748 ? 119.297 170.970 171.126 1.00 91.98  ? 2748 TYR A CG    1 
ATOM   8715  C CD1   . TYR A 1 2748 ? 119.444 171.327 169.794 1.00 91.98  ? 2748 TYR A CD1   1 
ATOM   8716  C CD2   . TYR A 1 2748 ? 120.442 170.738 171.870 1.00 91.98  ? 2748 TYR A CD2   1 
ATOM   8717  C CE1   . TYR A 1 2748 ? 120.688 171.425 169.215 1.00 91.98  ? 2748 TYR A CE1   1 
ATOM   8718  C CE2   . TYR A 1 2748 ? 121.693 170.835 171.298 1.00 91.98  ? 2748 TYR A CE2   1 
ATOM   8719  C CZ    . TYR A 1 2748 ? 121.808 171.179 169.970 1.00 91.98  ? 2748 TYR A CZ    1 
ATOM   8720  O OH    . TYR A 1 2748 ? 123.050 171.275 169.394 1.00 91.98  ? 2748 TYR A OH    1 
ATOM   8721  N N     . GLY A 1 2749 ? 115.146 172.478 172.974 1.00 99.92  ? 2749 GLY A N     1 
ATOM   8722  C CA    . GLY A 1 2749 ? 113.709 172.643 173.067 1.00 99.92  ? 2749 GLY A CA    1 
ATOM   8723  C C     . GLY A 1 2749 ? 113.225 173.751 172.158 1.00 99.92  ? 2749 GLY A C     1 
ATOM   8724  O O     . GLY A 1 2749 ? 112.183 173.625 171.511 1.00 99.92  ? 2749 GLY A O     1 
ATOM   8725  N N     . THR A 1 2750 ? 113.985 174.844 172.080 1.00 97.79  ? 2750 THR A N     1 
ATOM   8726  C CA    . THR A 1 2750 ? 113.674 175.877 171.098 1.00 97.79  ? 2750 THR A CA    1 
ATOM   8727  C C     . THR A 1 2750 ? 113.734 175.321 169.683 1.00 97.79  ? 2750 THR A C     1 
ATOM   8728  O O     . THR A 1 2750 ? 112.832 175.565 168.868 1.00 97.79  ? 2750 THR A O     1 
ATOM   8729  C CB    . THR A 1 2750 ? 114.636 177.052 171.249 1.00 97.79  ? 2750 THR A CB    1 
ATOM   8730  O OG1   . THR A 1 2750 ? 114.273 177.823 172.401 1.00 97.79  ? 2750 THR A OG1   1 
ATOM   8731  C CG2   . THR A 1 2750 ? 114.607 177.932 170.010 1.00 97.79  ? 2750 THR A CG2   1 
ATOM   8732  N N     . PHE A 1 2751 ? 114.782 174.555 169.378 1.00 93.53  ? 2751 PHE A N     1 
ATOM   8733  C CA    . PHE A 1 2751 ? 114.906 173.985 168.040 1.00 93.53  ? 2751 PHE A CA    1 
ATOM   8734  C C     . PHE A 1 2751 ? 113.747 173.047 167.725 1.00 93.53  ? 2751 PHE A C     1 
ATOM   8735  O O     . PHE A 1 2751 ? 113.189 173.089 166.624 1.00 93.53  ? 2751 PHE A O     1 
ATOM   8736  C CB    . PHE A 1 2751 ? 116.234 173.248 167.891 1.00 93.53  ? 2751 PHE A CB    1 
ATOM   8737  C CG    . PHE A 1 2751 ? 117.339 174.106 167.370 1.00 93.53  ? 2751 PHE A CG    1 
ATOM   8738  C CD1   . PHE A 1 2751 ? 117.136 174.915 166.270 1.00 93.53  ? 2751 PHE A CD1   1 
ATOM   8739  C CD2   . PHE A 1 2751 ? 118.589 174.079 167.955 1.00 93.53  ? 2751 PHE A CD2   1 
ATOM   8740  C CE1   . PHE A 1 2751 ? 118.148 175.707 165.790 1.00 93.53  ? 2751 PHE A CE1   1 
ATOM   8741  C CE2   . PHE A 1 2751 ? 119.609 174.864 167.467 1.00 93.53  ? 2751 PHE A CE2   1 
ATOM   8742  C CZ    . PHE A 1 2751 ? 119.388 175.676 166.380 1.00 93.53  ? 2751 PHE A CZ    1 
ATOM   8743  N N     . ASN A 1 2752 ? 113.363 172.201 168.681 1.00 98.99  ? 2752 ASN A N     1 
ATOM   8744  C CA    . ASN A 1 2752 ? 112.281 171.254 168.444 1.00 98.99  ? 2752 ASN A CA    1 
ATOM   8745  C C     . ASN A 1 2752 ? 110.939 171.959 168.320 1.00 98.99  ? 2752 ASN A C     1 
ATOM   8746  O O     . ASN A 1 2752 ? 110.084 171.539 167.534 1.00 98.99  ? 2752 ASN A O     1 
ATOM   8747  C CB    . ASN A 1 2752 ? 112.240 170.221 169.564 1.00 98.99  ? 2752 ASN A CB    1 
ATOM   8748  C CG    . ASN A 1 2752 ? 113.381 169.242 169.481 1.00 98.99  ? 2752 ASN A CG    1 
ATOM   8749  O OD1   . ASN A 1 2752 ? 113.734 168.595 170.465 1.00 98.99  ? 2752 ASN A OD1   1 
ATOM   8750  N ND2   . ASN A 1 2752 ? 113.975 169.132 168.301 1.00 98.99  ? 2752 ASN A ND2   1 
ATOM   8751  N N     . ARG A 1 2753 ? 110.720 173.013 169.106 1.00 99.80  ? 2753 ARG A N     1 
ATOM   8752  C CA    . ARG A 1 2753 ? 109.478 173.765 168.985 1.00 99.80  ? 2753 ARG A CA    1 
ATOM   8753  C C     . ARG A 1 2753 ? 109.383 174.442 167.627 1.00 99.80  ? 2753 ARG A C     1 
ATOM   8754  O O     . ARG A 1 2753 ? 108.308 174.473 167.018 1.00 99.80  ? 2753 ARG A O     1 
ATOM   8755  C CB    . ARG A 1 2753 ? 109.369 174.787 170.114 1.00 99.80  ? 2753 ARG A CB    1 
ATOM   8756  C CG    . ARG A 1 2753 ? 109.010 174.174 171.455 1.00 99.80  ? 2753 ARG A CG    1 
ATOM   8757  C CD    . ARG A 1 2753 ? 108.973 175.220 172.550 1.00 99.80  ? 2753 ARG A CD    1 
ATOM   8758  N NE    . ARG A 1 2753 ? 109.618 176.458 172.134 1.00 99.80  ? 2753 ARG A NE    1 
ATOM   8759  C CZ    . ARG A 1 2753 ? 110.749 176.919 172.648 1.00 99.80  ? 2753 ARG A CZ    1 
ATOM   8760  N NH1   . ARG A 1 2753 ? 111.392 176.266 173.602 1.00 99.80  ? 2753 ARG A NH1   1 
ATOM   8761  N NH2   . ARG A 1 2753 ? 111.248 178.065 172.193 1.00 99.80  ? 2753 ARG A NH2   1 
ATOM   8762  N N     . ALA A 1 2754 ? 110.493 174.990 167.135 1.00 103.12 ? 2754 ALA A N     1 
ATOM   8763  C CA    . ALA A 1 2754 ? 110.490 175.535 165.782 1.00 103.12 ? 2754 ALA A CA    1 
ATOM   8764  C C     . ALA A 1 2754 ? 110.280 174.435 164.750 1.00 103.12 ? 2754 ALA A C     1 
ATOM   8765  O O     . ALA A 1 2754 ? 109.636 174.654 163.717 1.00 103.12 ? 2754 ALA A O     1 
ATOM   8766  C CB    . ALA A 1 2754 ? 111.793 176.280 165.513 1.00 103.12 ? 2754 ALA A CB    1 
ATOM   8767  N N     . MET A 1 2755 ? 110.833 173.250 165.008 1.00 99.60  ? 2755 MET A N     1 
ATOM   8768  C CA    . MET A 1 2755 ? 110.673 172.120 164.100 1.00 99.60  ? 2755 MET A CA    1 
ATOM   8769  C C     . MET A 1 2755 ? 109.220 171.692 163.966 1.00 99.60  ? 2755 MET A C     1 
ATOM   8770  O O     . MET A 1 2755 ? 108.688 171.584 162.856 1.00 99.60  ? 2755 MET A O     1 
ATOM   8771  C CB    . MET A 1 2755 ? 111.506 170.947 164.603 1.00 99.60  ? 2755 MET A CB    1 
ATOM   8772  C CG    . MET A 1 2755 ? 111.412 169.737 163.726 1.00 99.60  ? 2755 MET A CG    1 
ATOM   8773  S SD    . MET A 1 2755 ? 112.896 168.755 163.596 1.00 99.60  ? 2755 MET A SD    1 
ATOM   8774  C CE    . MET A 1 2755 ? 112.139 167.339 162.826 1.00 99.60  ? 2755 MET A CE    1 
ATOM   8775  N N     . LEU A 1 2756 ? 108.564 171.441 165.090 1.00 102.39 ? 2756 LEU A N     1 
ATOM   8776  C CA    . LEU A 1 2756 ? 107.314 170.698 165.087 1.00 102.39 ? 2756 LEU A CA    1 
ATOM   8777  C C     . LEU A 1 2756 ? 106.117 171.543 164.684 1.00 102.39 ? 2756 LEU A C     1 
ATOM   8778  O O     . LEU A 1 2756 ? 104.991 171.037 164.700 1.00 102.39 ? 2756 LEU A O     1 
ATOM   8779  C CB    . LEU A 1 2756 ? 107.088 170.066 166.460 1.00 102.39 ? 2756 LEU A CB    1 
ATOM   8780  C CG    . LEU A 1 2756 ? 108.128 168.996 166.810 1.00 102.39 ? 2756 LEU A CG    1 
ATOM   8781  C CD1   . LEU A 1 2756 ? 107.605 168.033 167.855 1.00 102.39 ? 2756 LEU A CD1   1 
ATOM   8782  C CD2   . LEU A 1 2756 ? 108.575 168.240 165.569 1.00 102.39 ? 2756 LEU A CD2   1 
ATOM   8783  N N     . ARG A 1 2757 ? 106.325 172.813 164.332 1.00 107.50 ? 2757 ARG A N     1 
ATOM   8784  C CA    . ARG A 1 2757 ? 105.253 173.586 163.721 1.00 107.50 ? 2757 ARG A CA    1 
ATOM   8785  C C     . ARG A 1 2757 ? 104.852 173.016 162.369 1.00 107.50 ? 2757 ARG A C     1 
ATOM   8786  O O     . ARG A 1 2757 ? 103.722 173.240 161.923 1.00 107.50 ? 2757 ARG A O     1 
ATOM   8787  C CB    . ARG A 1 2757 ? 105.672 175.047 163.565 1.00 107.50 ? 2757 ARG A CB    1 
ATOM   8788  C CG    . ARG A 1 2757 ? 105.310 175.925 164.745 1.00 107.50 ? 2757 ARG A CG    1 
ATOM   8789  C CD    . ARG A 1 2757 ? 105.682 177.371 164.479 1.00 107.50 ? 2757 ARG A CD    1 
ATOM   8790  N NE    . ARG A 1 2757 ? 107.118 177.537 164.302 1.00 107.50 ? 2757 ARG A NE    1 
ATOM   8791  C CZ    . ARG A 1 2757 ? 107.766 178.682 164.471 1.00 107.50 ? 2757 ARG A CZ    1 
ATOM   8792  N NH1   . ARG A 1 2757 ? 107.134 179.785 164.835 1.00 107.50 ? 2757 ARG A NH1   1 
ATOM   8793  N NH2   . ARG A 1 2757 ? 109.080 178.720 164.269 1.00 107.50 ? 2757 ARG A NH2   1 
ATOM   8794  N N     . LEU A 1 2758 ? 105.756 172.288 161.709 1.00 107.36 ? 2758 LEU A N     1 
ATOM   8795  C CA    . LEU A 1 2758 ? 105.410 171.635 160.451 1.00 107.36 ? 2758 LEU A CA    1 
ATOM   8796  C C     . LEU A 1 2758 ? 104.311 170.602 160.653 1.00 107.36 ? 2758 LEU A C     1 
ATOM   8797  O O     . LEU A 1 2758 ? 103.380 170.507 159.845 1.00 107.36 ? 2758 LEU A O     1 
ATOM   8798  C CB    . LEU A 1 2758 ? 106.652 170.982 159.845 1.00 107.36 ? 2758 LEU A CB    1 
ATOM   8799  C CG    . LEU A 1 2758 ? 107.408 171.797 158.798 1.00 107.36 ? 2758 LEU A CG    1 
ATOM   8800  C CD1   . LEU A 1 2758 ? 108.547 170.985 158.208 1.00 107.36 ? 2758 LEU A CD1   1 
ATOM   8801  C CD2   . LEU A 1 2758 ? 106.459 172.260 157.710 1.00 107.36 ? 2758 LEU A CD2   1 
ATOM   8802  N N     . ILE A 1 2759 ? 104.398 169.824 161.726 1.00 108.41 ? 2759 ILE A N     1 
ATOM   8803  C CA    . ILE A 1 2759 ? 103.415 168.784 162.011 1.00 108.41 ? 2759 ILE A CA    1 
ATOM   8804  C C     . ILE A 1 2759 ? 102.672 169.160 163.286 1.00 108.41 ? 2759 ILE A C     1 
ATOM   8805  O O     . ILE A 1 2759 ? 103.179 168.925 164.392 1.00 108.41 ? 2759 ILE A O     1 
ATOM   8806  C CB    . ILE A 1 2759 ? 104.083 167.407 162.139 1.00 108.41 ? 2759 ILE A CB    1 
ATOM   8807  C CG1   . ILE A 1 2759 ? 104.955 167.122 160.915 1.00 108.41 ? 2759 ILE A CG1   1 
ATOM   8808  C CG2   . ILE A 1 2759 ? 103.032 166.326 162.320 1.00 108.41 ? 2759 ILE A CG2   1 
ATOM   8809  C CD1   . ILE A 1 2759 ? 104.237 167.286 159.594 1.00 108.41 ? 2759 ILE A CD1   1 
ATOM   8810  N N     . PRO A 1 2760 ? 101.474 169.736 163.181 1.00 108.83 ? 2760 PRO A N     1 
ATOM   8811  C CA    . PRO A 1 2760 ? 100.785 170.222 164.387 1.00 108.83 ? 2760 PRO A CA    1 
ATOM   8812  C C     . PRO A 1 2760 ? 100.450 169.133 165.387 1.00 108.83 ? 2760 PRO A C     1 
ATOM   8813  O O     . PRO A 1 2760 ? 100.372 169.416 166.588 1.00 108.83 ? 2760 PRO A O     1 
ATOM   8814  C CB    . PRO A 1 2760 ? 99.516  170.871 163.821 1.00 108.83 ? 2760 PRO A CB    1 
ATOM   8815  C CG    . PRO A 1 2760 ? 99.293  170.179 162.520 1.00 108.83 ? 2760 PRO A CG    1 
ATOM   8816  C CD    . PRO A 1 2760 ? 100.660 169.912 161.968 1.00 108.83 ? 2760 PRO A CD    1 
ATOM   8817  N N     . SER A 1 2761 ? 100.247 167.896 164.931 1.00 113.81 ? 2761 SER A N     1 
ATOM   8818  C CA    . SER A 1 2761 ? 99.787  166.844 165.832 1.00 113.81 ? 2761 SER A CA    1 
ATOM   8819  C C     . SER A 1 2761 ? 100.823 166.506 166.896 1.00 113.81 ? 2761 SER A C     1 
ATOM   8820  O O     . SER A 1 2761 ? 100.466 166.024 167.976 1.00 113.81 ? 2761 SER A O     1 
ATOM   8821  C CB    . SER A 1 2761 ? 99.426  165.591 165.036 1.00 113.81 ? 2761 SER A CB    1 
ATOM   8822  O OG    . SER A 1 2761 ? 99.098  164.518 165.902 1.00 113.81 ? 2761 SER A OG    1 
ATOM   8823  N N     . LEU A 1 2762 ? 102.101 166.745 166.615 1.00 110.42 ? 2762 LEU A N     1 
ATOM   8824  C CA    . LEU A 1 2762 ? 103.176 166.412 167.537 1.00 110.42 ? 2762 LEU A CA    1 
ATOM   8825  C C     . LEU A 1 2762 ? 103.672 167.616 168.322 1.00 110.42 ? 2762 LEU A C     1 
ATOM   8826  O O     . LEU A 1 2762 ? 104.685 167.509 169.019 1.00 110.42 ? 2762 LEU A O     1 
ATOM   8827  C CB    . LEU A 1 2762 ? 104.339 165.779 166.776 1.00 110.42 ? 2762 LEU A CB    1 
ATOM   8828  C CG    . LEU A 1 2762 ? 103.949 164.821 165.654 1.00 110.42 ? 2762 LEU A CG    1 
ATOM   8829  C CD1   . LEU A 1 2762 ? 105.167 164.440 164.834 1.00 110.42 ? 2762 LEU A CD1   1 
ATOM   8830  C CD2   . LEU A 1 2762 ? 103.278 163.587 166.229 1.00 110.42 ? 2762 LEU A CD2   1 
ATOM   8831  N N     . ARG A 1 2763 ? 102.975 168.752 168.234 1.00 115.95 ? 2763 ARG A N     1 
ATOM   8832  C CA    . ARG A 1 2763 ? 103.484 169.987 168.824 1.00 115.95 ? 2763 ARG A CA    1 
ATOM   8833  C C     . ARG A 1 2763 ? 103.753 169.828 170.312 1.00 115.95 ? 2763 ARG A C     1 
ATOM   8834  O O     . ARG A 1 2763 ? 104.825 170.204 170.800 1.00 115.95 ? 2763 ARG A O     1 
ATOM   8835  C CB    . ARG A 1 2763 ? 102.493 171.124 168.593 1.00 115.95 ? 2763 ARG A CB    1 
ATOM   8836  C CG    . ARG A 1 2763 ? 102.613 171.807 167.251 1.00 115.95 ? 2763 ARG A CG    1 
ATOM   8837  C CD    . ARG A 1 2763 ? 101.488 172.812 167.072 1.00 115.95 ? 2763 ARG A CD    1 
ATOM   8838  N NE    . ARG A 1 2763 ? 101.175 173.509 168.316 1.00 115.95 ? 2763 ARG A NE    1 
ATOM   8839  C CZ    . ARG A 1 2763 ? 101.927 174.456 168.862 1.00 115.95 ? 2763 ARG A CZ    1 
ATOM   8840  N NH1   . ARG A 1 2763 ? 103.055 174.856 168.298 1.00 115.95 ? 2763 ARG A NH1   1 
ATOM   8841  N NH2   . ARG A 1 2763 ? 101.536 175.015 170.003 1.00 115.95 ? 2763 ARG A NH2   1 
ATOM   8842  N N     . THR A 1 2764 ? 102.801 169.261 171.049 1.00 116.08 ? 2764 THR A N     1 
ATOM   8843  C CA    . THR A 1 2764 ? 102.960 169.127 172.489 1.00 116.08 ? 2764 THR A CA    1 
ATOM   8844  C C     . THR A 1 2764 ? 103.986 168.072 172.876 1.00 116.08 ? 2764 THR A C     1 
ATOM   8845  O O     . THR A 1 2764 ? 104.325 167.970 174.059 1.00 116.08 ? 2764 THR A O     1 
ATOM   8846  C CB    . THR A 1 2764 ? 101.614 168.808 173.136 1.00 116.08 ? 2764 THR A CB    1 
ATOM   8847  O OG1   . THR A 1 2764 ? 101.814 168.442 174.507 1.00 116.08 ? 2764 THR A OG1   1 
ATOM   8848  C CG2   . THR A 1 2764 ? 100.918 167.679 172.397 1.00 116.08 ? 2764 THR A CG2   1 
ATOM   8849  N N     . TYR A 1 2765 ? 104.485 167.292 171.921 1.00 116.79 ? 2765 TYR A N     1 
ATOM   8850  C CA    . TYR A 1 2765 ? 105.480 166.267 172.201 1.00 116.79 ? 2765 TYR A CA    1 
ATOM   8851  C C     . TYR A 1 2765 ? 106.908 166.767 172.039 1.00 116.79 ? 2765 TYR A C     1 
ATOM   8852  O O     . TYR A 1 2765 ? 107.844 165.980 172.209 1.00 116.79 ? 2765 TYR A O     1 
ATOM   8853  C CB    . TYR A 1 2765 ? 105.270 165.048 171.292 1.00 116.79 ? 2765 TYR A CB    1 
ATOM   8854  C CG    . TYR A 1 2765 ? 104.007 164.244 171.542 1.00 116.79 ? 2765 TYR A CG    1 
ATOM   8855  C CD1   . TYR A 1 2765 ? 103.986 162.875 171.314 1.00 116.79 ? 2765 TYR A CD1   1 
ATOM   8856  C CD2   . TYR A 1 2765 ? 102.843 164.845 171.995 1.00 116.79 ? 2765 TYR A CD2   1 
ATOM   8857  C CE1   . TYR A 1 2765 ? 102.846 162.133 171.534 1.00 116.79 ? 2765 TYR A CE1   1 
ATOM   8858  C CE2   . TYR A 1 2765 ? 101.698 164.111 172.216 1.00 116.79 ? 2765 TYR A CE2   1 
ATOM   8859  C CZ    . TYR A 1 2765 ? 101.705 162.756 171.983 1.00 116.79 ? 2765 TYR A CZ    1 
ATOM   8860  O OH    . TYR A 1 2765 ? 100.566 162.019 172.203 1.00 116.79 ? 2765 TYR A OH    1 
ATOM   8861  N N     . ALA A 1 2766 ? 107.099 168.047 171.713 1.00 111.74 ? 2766 ALA A N     1 
ATOM   8862  C CA    . ALA A 1 2766 ? 108.441 168.552 171.442 1.00 111.74 ? 2766 ALA A CA    1 
ATOM   8863  C C     . ALA A 1 2766 ? 109.325 168.483 172.680 1.00 111.74 ? 2766 ALA A C     1 
ATOM   8864  O O     . ALA A 1 2766 ? 110.488 168.069 172.602 1.00 111.74 ? 2766 ALA A O     1 
ATOM   8865  C CB    . ALA A 1 2766 ? 108.365 169.984 170.915 1.00 111.74 ? 2766 ALA A CB    1 
ATOM   8866  N N     . GLU A 1 2767 ? 108.794 168.887 173.831 1.00 113.29 ? 2767 GLU A N     1 
ATOM   8867  C CA    . GLU A 1 2767 ? 109.603 168.913 175.049 1.00 113.29 ? 2767 GLU A CA    1 
ATOM   8868  C C     . GLU A 1 2767 ? 110.098 167.534 175.466 1.00 113.29 ? 2767 GLU A C     1 
ATOM   8869  O O     . GLU A 1 2767 ? 111.295 167.404 175.778 1.00 113.29 ? 2767 GLU A O     1 
ATOM   8870  C CB    . GLU A 1 2767 ? 108.818 169.596 176.174 1.00 113.29 ? 2767 GLU A CB    1 
ATOM   8871  C CG    . GLU A 1 2767 ? 107.904 170.724 175.714 1.00 113.29 ? 2767 GLU A CG    1 
ATOM   8872  C CD    . GLU A 1 2767 ? 108.594 171.727 174.803 1.00 113.29 ? 2767 GLU A CD    1 
ATOM   8873  O OE1   . GLU A 1 2767 ? 107.928 172.244 173.882 1.00 113.29 ? 2767 GLU A OE1   1 
ATOM   8874  O OE2   . GLU A 1 2767 ? 109.792 172.013 175.013 1.00 113.29 ? 2767 GLU A OE2   1 
ATOM   8875  N N     . PRO A 1 2768 ? 109.268 166.484 175.519 1.00 109.18 ? 2768 PRO A N     1 
ATOM   8876  C CA    . PRO A 1 2768 ? 109.824 165.161 175.844 1.00 109.18 ? 2768 PRO A CA    1 
ATOM   8877  C C     . PRO A 1 2768 ? 110.876 164.704 174.856 1.00 109.18 ? 2768 PRO A C     1 
ATOM   8878  O O     . PRO A 1 2768 ? 111.842 164.041 175.250 1.00 109.18 ? 2768 PRO A O     1 
ATOM   8879  C CB    . PRO A 1 2768 ? 108.591 164.248 175.830 1.00 109.18 ? 2768 PRO A CB    1 
ATOM   8880  C CG    . PRO A 1 2768 ? 107.441 165.157 176.035 1.00 109.18 ? 2768 PRO A CG    1 
ATOM   8881  C CD    . PRO A 1 2768 ? 107.807 166.425 175.346 1.00 109.18 ? 2768 PRO A CD    1 
ATOM   8882  N N     . LEU A 1 2769 ? 110.717 165.049 173.577 1.00 104.34 ? 2769 LEU A N     1 
ATOM   8883  C CA    . LEU A 1 2769 ? 111.724 164.695 172.583 1.00 104.34 ? 2769 LEU A CA    1 
ATOM   8884  C C     . LEU A 1 2769 ? 113.060 165.348 172.906 1.00 104.34 ? 2769 LEU A C     1 
ATOM   8885  O O     . LEU A 1 2769 ? 114.108 164.692 172.882 1.00 104.34 ? 2769 LEU A O     1 
ATOM   8886  C CB    . LEU A 1 2769 ? 111.250 165.104 171.190 1.00 104.34 ? 2769 LEU A CB    1 
ATOM   8887  C CG    . LEU A 1 2769 ? 112.313 165.068 170.095 1.00 104.34 ? 2769 LEU A CG    1 
ATOM   8888  C CD1   . LEU A 1 2769 ? 112.504 163.651 169.610 1.00 104.34 ? 2769 LEU A CD1   1 
ATOM   8889  C CD2   . LEU A 1 2769 ? 111.923 165.976 168.948 1.00 104.34 ? 2769 LEU A CD2   1 
ATOM   8890  N N     . THR A 1 2770 ? 113.037 166.643 173.221 1.00 101.74 ? 2770 THR A N     1 
ATOM   8891  C CA    . THR A 1 2770 ? 114.268 167.340 173.572 1.00 101.74 ? 2770 THR A CA    1 
ATOM   8892  C C     . THR A 1 2770 ? 114.889 166.755 174.832 1.00 101.74 ? 2770 THR A C     1 
ATOM   8893  O O     . THR A 1 2770 ? 116.109 166.556 174.899 1.00 101.74 ? 2770 THR A O     1 
ATOM   8894  C CB    . THR A 1 2770 ? 113.983 168.831 173.750 1.00 101.74 ? 2770 THR A CB    1 
ATOM   8895  O OG1   . THR A 1 2770 ? 113.961 169.471 172.469 1.00 101.74 ? 2770 THR A OG1   1 
ATOM   8896  C CG2   . THR A 1 2770 ? 115.040 169.484 174.617 1.00 101.74 ? 2770 THR A CG2   1 
ATOM   8897  N N     . ALA A 1 2771 ? 114.064 166.466 175.840 1.00 106.87 ? 2771 ALA A N     1 
ATOM   8898  C CA    . ALA A 1 2771 ? 114.584 165.924 177.091 1.00 106.87 ? 2771 ALA A CA    1 
ATOM   8899  C C     . ALA A 1 2771 ? 115.240 164.567 176.872 1.00 106.87 ? 2771 ALA A C     1 
ATOM   8900  O O     . ALA A 1 2771 ? 116.336 164.304 177.382 1.00 106.87 ? 2771 ALA A O     1 
ATOM   8901  C CB    . ALA A 1 2771 ? 113.462 165.823 178.123 1.00 106.87 ? 2771 ALA A CB    1 
ATOM   8902  N N     . ALA A 1 2772 ? 114.587 163.691 176.105 1.00 103.01 ? 2772 ALA A N     1 
ATOM   8903  C CA    . ALA A 1 2772 ? 115.167 162.384 175.823 1.00 103.01 ? 2772 ALA A CA    1 
ATOM   8904  C C     . ALA A 1 2772 ? 116.444 162.513 175.006 1.00 103.01 ? 2772 ALA A C     1 
ATOM   8905  O O     . ALA A 1 2772 ? 117.419 161.792 175.249 1.00 103.01 ? 2772 ALA A O     1 
ATOM   8906  C CB    . ALA A 1 2772 ? 114.151 161.502 175.101 1.00 103.01 ? 2772 ALA A CB    1 
ATOM   8907  N N     . MET A 1 2773 ? 116.458 163.423 174.029 1.00 97.32  ? 2773 MET A N     1 
ATOM   8908  C CA    . MET A 1 2773 ? 117.655 163.629 173.221 1.00 97.32  ? 2773 MET A CA    1 
ATOM   8909  C C     . MET A 1 2773 ? 118.830 164.056 174.089 1.00 97.32  ? 2773 MET A C     1 
ATOM   8910  O O     . MET A 1 2773 ? 119.933 163.503 173.986 1.00 97.32  ? 2773 MET A O     1 
ATOM   8911  C CB    . MET A 1 2773 ? 117.372 164.674 172.142 1.00 97.32  ? 2773 MET A CB    1 
ATOM   8912  C CG    . MET A 1 2773 ? 118.328 164.636 170.973 1.00 97.32  ? 2773 MET A CG    1 
ATOM   8913  S SD    . MET A 1 2773 ? 117.530 165.006 169.401 1.00 97.32  ? 2773 MET A SD    1 
ATOM   8914  C CE    . MET A 1 2773 ? 116.564 166.446 169.841 1.00 97.32  ? 2773 MET A CE    1 
ATOM   8915  N N     . VAL A 1 2774 ? 118.599 165.027 174.972 1.00 95.56  ? 2774 VAL A N     1 
ATOM   8916  C CA    . VAL A 1 2774 ? 119.663 165.509 175.844 1.00 95.56  ? 2774 VAL A CA    1 
ATOM   8917  C C     . VAL A 1 2774 ? 120.114 164.409 176.795 1.00 95.56  ? 2774 VAL A C     1 
ATOM   8918  O O     . VAL A 1 2774 ? 121.313 164.246 177.054 1.00 95.56  ? 2774 VAL A O     1 
ATOM   8919  C CB    . VAL A 1 2774 ? 119.197 166.764 176.600 1.00 95.56  ? 2774 VAL A CB    1 
ATOM   8920  C CG1   . VAL A 1 2774 ? 119.910 166.887 177.937 1.00 95.56  ? 2774 VAL A CG1   1 
ATOM   8921  C CG2   . VAL A 1 2774 ? 119.425 167.996 175.751 1.00 95.56  ? 2774 VAL A CG2   1 
ATOM   8922  N N     . GLU A 1 2775 ? 119.167 163.638 177.332 1.00 100.90 ? 2775 GLU A N     1 
ATOM   8923  C CA    . GLU A 1 2775 ? 119.527 162.570 178.256 1.00 100.90 ? 2775 GLU A CA    1 
ATOM   8924  C C     . GLU A 1 2775 ? 120.400 161.531 177.569 1.00 100.90 ? 2775 GLU A C     1 
ATOM   8925  O O     . GLU A 1 2775 ? 121.420 161.097 178.118 1.00 100.90 ? 2775 GLU A O     1 
ATOM   8926  C CB    . GLU A 1 2775 ? 118.264 161.925 178.823 1.00 100.90 ? 2775 GLU A CB    1 
ATOM   8927  C CG    . GLU A 1 2775 ? 118.470 161.237 180.159 1.00 100.90 ? 2775 GLU A CG    1 
ATOM   8928  C CD    . GLU A 1 2775 ? 119.091 159.865 180.020 1.00 100.90 ? 2775 GLU A CD    1 
ATOM   8929  O OE1   . GLU A 1 2775 ? 118.931 159.245 178.949 1.00 100.90 ? 2775 GLU A OE1   1 
ATOM   8930  O OE2   . GLU A 1 2775 ? 119.742 159.407 180.981 1.00 100.90 ? 2775 GLU A OE2   1 
ATOM   8931  N N     . PHE A 1 2776 ? 120.018 161.125 176.357 1.00 100.52 ? 2776 PHE A N     1 
ATOM   8932  C CA    . PHE A 1 2776 ? 120.811 160.140 175.634 1.00 100.52 ? 2776 PHE A CA    1 
ATOM   8933  C C     . PHE A 1 2776 ? 122.187 160.690 175.300 1.00 100.52 ? 2776 PHE A C     1 
ATOM   8934  O O     . PHE A 1 2776 ? 123.185 159.963 175.362 1.00 100.52 ? 2776 PHE A O     1 
ATOM   8935  C CB    . PHE A 1 2776 ? 120.095 159.703 174.360 1.00 100.52 ? 2776 PHE A CB    1 
ATOM   8936  C CG    . PHE A 1 2776 ? 120.925 158.817 173.484 1.00 100.52 ? 2776 PHE A CG    1 
ATOM   8937  C CD1   . PHE A 1 2776 ? 121.454 157.638 173.976 1.00 100.52 ? 2776 PHE A CD1   1 
ATOM   8938  C CD2   . PHE A 1 2776 ? 121.186 159.164 172.173 1.00 100.52 ? 2776 PHE A CD2   1 
ATOM   8939  C CE1   . PHE A 1 2776 ? 122.223 156.819 173.174 1.00 100.52 ? 2776 PHE A CE1   1 
ATOM   8940  C CE2   . PHE A 1 2776 ? 121.955 158.349 171.366 1.00 100.52 ? 2776 PHE A CE2   1 
ATOM   8941  C CZ    . PHE A 1 2776 ? 122.474 157.176 171.867 1.00 100.52 ? 2776 PHE A CZ    1 
ATOM   8942  N N     . TYR A 1 2777 ? 122.262 161.971 174.938 1.00 98.10  ? 2777 TYR A N     1 
ATOM   8943  C CA    . TYR A 1 2777 ? 123.563 162.572 174.672 1.00 98.10  ? 2777 TYR A CA    1 
ATOM   8944  C C     . TYR A 1 2777 ? 124.437 162.552 175.916 1.00 98.10  ? 2777 TYR A C     1 
ATOM   8945  O O     . TYR A 1 2777 ? 125.637 162.273 175.836 1.00 98.10  ? 2777 TYR A O     1 
ATOM   8946  C CB    . TYR A 1 2777 ? 123.380 163.997 174.158 1.00 98.10  ? 2777 TYR A CB    1 
ATOM   8947  C CG    . TYR A 1 2777 ? 124.658 164.787 173.987 1.00 98.10  ? 2777 TYR A CG    1 
ATOM   8948  C CD1   . TYR A 1 2777 ? 125.269 164.884 172.748 1.00 98.10  ? 2777 TYR A CD1   1 
ATOM   8949  C CD2   . TYR A 1 2777 ? 125.228 165.470 175.052 1.00 98.10  ? 2777 TYR A CD2   1 
ATOM   8950  C CE1   . TYR A 1 2777 ? 126.424 165.612 172.578 1.00 98.10  ? 2777 TYR A CE1   1 
ATOM   8951  C CE2   . TYR A 1 2777 ? 126.385 166.199 174.891 1.00 98.10  ? 2777 TYR A CE2   1 
ATOM   8952  C CZ    . TYR A 1 2777 ? 126.978 166.267 173.651 1.00 98.10  ? 2777 TYR A CZ    1 
ATOM   8953  O OH    . TYR A 1 2777 ? 128.131 166.994 173.484 1.00 98.10  ? 2777 TYR A OH    1 
ATOM   8954  N N     . THR A 1 2778 ? 123.856 162.848 177.077 1.00 101.75 ? 2778 THR A N     1 
ATOM   8955  C CA    . THR A 1 2778 ? 124.633 162.818 178.311 1.00 101.75 ? 2778 THR A CA    1 
ATOM   8956  C C     . THR A 1 2778 ? 125.129 161.410 178.617 1.00 101.75 ? 2778 THR A C     1 
ATOM   8957  O O     . THR A 1 2778 ? 126.287 161.226 179.014 1.00 101.75 ? 2778 THR A O     1 
ATOM   8958  C CB    . THR A 1 2778 ? 123.803 163.358 179.471 1.00 101.75 ? 2778 THR A CB    1 
ATOM   8959  O OG1   . THR A 1 2778 ? 123.336 164.672 179.148 1.00 101.75 ? 2778 THR A OG1   1 
ATOM   8960  C CG2   . THR A 1 2778 ? 124.641 163.425 180.734 1.00 101.75 ? 2778 THR A CG2   1 
ATOM   8961  N N     . MET A 1 2779 ? 124.268 160.402 178.444 1.00 106.83 ? 2779 MET A N     1 
ATOM   8962  C CA    . MET A 1 2779 ? 124.720 159.030 178.661 1.00 106.83 ? 2779 MET A CA    1 
ATOM   8963  C C     . MET A 1 2779 ? 125.845 158.667 177.705 1.00 106.83 ? 2779 MET A C     1 
ATOM   8964  O O     . MET A 1 2779 ? 126.848 158.072 178.112 1.00 106.83 ? 2779 MET A O     1 
ATOM   8965  C CB    . MET A 1 2779 ? 123.569 158.033 178.514 1.00 106.83 ? 2779 MET A CB    1 
ATOM   8966  C CG    . MET A 1 2779 ? 122.273 158.432 179.176 1.00 106.83 ? 2779 MET A CG    1 
ATOM   8967  S SD    . MET A 1 2779 ? 121.266 156.995 179.579 1.00 106.83 ? 2779 MET A SD    1 
ATOM   8968  C CE    . MET A 1 2779 ? 122.274 156.230 180.845 1.00 106.83 ? 2779 MET A CE    1 
ATOM   8969  N N     . SER A 1 2780 ? 125.705 159.026 176.433 1.00 104.41 ? 2780 SER A N     1 
ATOM   8970  C CA    . SER A 1 2780 ? 126.762 158.735 175.479 1.00 104.41 ? 2780 SER A CA    1 
ATOM   8971  C C     . SER A 1 2780 ? 128.046 159.482 175.805 1.00 104.41 ? 2780 SER A C     1 
ATOM   8972  O O     . SER A 1 2780 ? 129.131 158.993 175.480 1.00 104.41 ? 2780 SER A O     1 
ATOM   8973  C CB    . SER A 1 2780 ? 126.299 159.077 174.067 1.00 104.41 ? 2780 SER A CB    1 
ATOM   8974  O OG    . SER A 1 2780 ? 127.377 159.544 173.279 1.00 104.41 ? 2780 SER A OG    1 
ATOM   8975  N N     . GLN A 1 2781 ? 127.947 160.654 176.432 1.00 104.18 ? 2781 GLN A N     1 
ATOM   8976  C CA    . GLN A 1 2781 ? 129.142 161.417 176.773 1.00 104.18 ? 2781 GLN A CA    1 
ATOM   8977  C C     . GLN A 1 2781 ? 129.851 160.853 177.997 1.00 104.18 ? 2781 GLN A C     1 
ATOM   8978  O O     . GLN A 1 2781 ? 131.085 160.826 178.039 1.00 104.18 ? 2781 GLN A O     1 
ATOM   8979  C CB    . GLN A 1 2781 ? 128.785 162.884 177.002 1.00 104.18 ? 2781 GLN A CB    1 
ATOM   8980  C CG    . GLN A 1 2781 ? 129.980 163.817 176.951 1.00 104.18 ? 2781 GLN A CG    1 
ATOM   8981  C CD    . GLN A 1 2781 ? 129.594 165.274 177.105 1.00 104.18 ? 2781 GLN A CD    1 
ATOM   8982  O OE1   . GLN A 1 2781 ? 128.424 165.603 177.296 1.00 104.18 ? 2781 GLN A OE1   1 
ATOM   8983  N NE2   . GLN A 1 2781 ? 130.581 166.157 177.033 1.00 104.18 ? 2781 GLN A NE2   1 
ATOM   8984  N N     . GLU A 1 2782 ? 129.097 160.408 179.005 1.00 114.91 ? 2782 GLU A N     1 
ATOM   8985  C CA    . GLU A 1 2782 ? 129.738 159.928 180.226 1.00 114.91 ? 2782 GLU A CA    1 
ATOM   8986  C C     . GLU A 1 2782 ? 130.463 158.611 179.983 1.00 114.91 ? 2782 GLU A C     1 
ATOM   8987  O O     . GLU A 1 2782 ? 131.434 158.290 180.679 1.00 114.91 ? 2782 GLU A O     1 
ATOM   8988  C CB    . GLU A 1 2782 ? 128.709 159.846 181.365 1.00 114.91 ? 2782 GLU A CB    1 
ATOM   8989  C CG    . GLU A 1 2782 ? 127.440 158.972 181.198 1.00 114.91 ? 2782 GLU A CG    1 
ATOM   8990  C CD    . GLU A 1 2782 ? 127.664 157.486 180.945 1.00 114.91 ? 2782 GLU A CD    1 
ATOM   8991  O OE1   . GLU A 1 2782 ? 126.688 156.806 180.565 1.00 114.91 ? 2782 GLU A OE1   1 
ATOM   8992  O OE2   . GLU A 1 2782 ? 128.756 156.963 181.235 1.00 114.91 ? 2782 GLU A OE2   1 
ATOM   8993  N N     . ARG A 1 2783 ? 130.001 157.831 179.010 1.00 110.96 ? 2783 ARG A N     1 
ATOM   8994  C CA    . ARG A 1 2783 ? 130.732 156.665 178.546 1.00 110.96 ? 2783 ARG A CA    1 
ATOM   8995  C C     . ARG A 1 2783 ? 131.422 157.000 177.227 1.00 110.96 ? 2783 ARG A C     1 
ATOM   8996  O O     . ARG A 1 2783 ? 131.353 158.127 176.734 1.00 110.96 ? 2783 ARG A O     1 
ATOM   8997  C CB    . ARG A 1 2783 ? 129.799 155.463 178.406 1.00 110.96 ? 2783 ARG A CB    1 
ATOM   8998  C CG    . ARG A 1 2783 ? 129.816 154.534 179.607 1.00 110.96 ? 2783 ARG A CG    1 
ATOM   8999  C CD    . ARG A 1 2783 ? 128.778 153.433 179.482 1.00 110.96 ? 2783 ARG A CD    1 
ATOM   9000  N NE    . ARG A 1 2783 ? 129.013 152.576 178.327 1.00 110.96 ? 2783 ARG A NE    1 
ATOM   9001  C CZ    . ARG A 1 2783 ? 129.957 151.647 178.262 1.00 110.96 ? 2783 ARG A CZ    1 
ATOM   9002  N NH1   . ARG A 1 2783 ? 130.769 151.414 179.280 1.00 110.96 ? 2783 ARG A NH1   1 
ATOM   9003  N NH2   . ARG A 1 2783 ? 130.086 150.931 177.149 1.00 110.96 ? 2783 ARG A NH2   1 
ATOM   9004  N N     . PHE A 1 2784 ? 132.104 156.011 176.651 1.00 107.67 ? 2784 PHE A N     1 
ATOM   9005  C CA    . PHE A 1 2784 ? 132.807 156.175 175.380 1.00 107.67 ? 2784 PHE A CA    1 
ATOM   9006  C C     . PHE A 1 2784 ? 133.736 157.385 175.419 1.00 107.67 ? 2784 PHE A C     1 
ATOM   9007  O O     . PHE A 1 2784 ? 133.704 158.259 174.551 1.00 107.67 ? 2784 PHE A O     1 
ATOM   9008  C CB    . PHE A 1 2784 ? 131.821 156.277 174.219 1.00 107.67 ? 2784 PHE A CB    1 
ATOM   9009  C CG    . PHE A 1 2784 ? 130.741 155.240 174.251 1.00 107.67 ? 2784 PHE A CG    1 
ATOM   9010  C CD1   . PHE A 1 2784 ? 131.055 153.904 174.409 1.00 107.67 ? 2784 PHE A CD1   1 
ATOM   9011  C CD2   . PHE A 1 2784 ? 129.412 155.600 174.124 1.00 107.67 ? 2784 PHE A CD2   1 
ATOM   9012  C CE1   . PHE A 1 2784 ? 130.065 152.946 174.437 1.00 107.67 ? 2784 PHE A CE1   1 
ATOM   9013  C CE2   . PHE A 1 2784 ? 128.418 154.646 174.151 1.00 107.67 ? 2784 PHE A CE2   1 
ATOM   9014  C CZ    . PHE A 1 2784 ? 128.745 153.319 174.308 1.00 107.67 ? 2784 PHE A CZ    1 
ATOM   9015  N N     . THR A 1 2785 ? 134.560 157.438 176.457 1.00 116.38 ? 2785 THR A N     1 
ATOM   9016  C CA    . THR A 1 2785 ? 135.526 158.511 176.611 1.00 116.38 ? 2785 THR A CA    1 
ATOM   9017  C C     . THR A 1 2785 ? 136.635 158.360 175.569 1.00 116.38 ? 2785 THR A C     1 
ATOM   9018  O O     . THR A 1 2785 ? 136.903 157.267 175.064 1.00 116.38 ? 2785 THR A O     1 
ATOM   9019  C CB    . THR A 1 2785 ? 136.085 158.498 178.038 1.00 116.38 ? 2785 THR A CB    1 
ATOM   9020  O OG1   . THR A 1 2785 ? 135.018 158.740 178.962 1.00 116.38 ? 2785 THR A OG1   1 
ATOM   9021  C CG2   . THR A 1 2785 ? 137.149 159.568 178.246 1.00 116.38 ? 2785 THR A CG2   1 
ATOM   9022  N N     . GLN A 1 2786 ? 137.276 159.485 175.236 1.00 111.42 ? 2786 GLN A N     1 
ATOM   9023  C CA    . GLN A 1 2786 ? 138.332 159.482 174.230 1.00 111.42 ? 2786 GLN A CA    1 
ATOM   9024  C C     . GLN A 1 2786 ? 139.483 158.555 174.594 1.00 111.42 ? 2786 GLN A C     1 
ATOM   9025  O O     . GLN A 1 2786 ? 140.242 158.151 173.707 1.00 111.42 ? 2786 GLN A O     1 
ATOM   9026  C CB    . GLN A 1 2786 ? 138.859 160.902 174.024 1.00 111.42 ? 2786 GLN A CB    1 
ATOM   9027  C CG    . GLN A 1 2786 ? 139.662 161.090 172.748 1.00 111.42 ? 2786 GLN A CG    1 
ATOM   9028  C CD    . GLN A 1 2786 ? 139.619 162.513 172.237 1.00 111.42 ? 2786 GLN A CD    1 
ATOM   9029  O OE1   . GLN A 1 2786 ? 138.894 163.353 172.767 1.00 111.42 ? 2786 GLN A OE1   1 
ATOM   9030  N NE2   . GLN A 1 2786 ? 140.397 162.793 171.199 1.00 111.42 ? 2786 GLN A NE2   1 
ATOM   9031  N N     . ASP A 1 2787 ? 139.639 158.214 175.875 1.00 124.29 ? 2787 ASP A N     1 
ATOM   9032  C CA    . ASP A 1 2787 ? 140.707 157.300 176.269 1.00 124.29 ? 2787 ASP A CA    1 
ATOM   9033  C C     . ASP A 1 2787 ? 140.534 155.934 175.617 1.00 124.29 ? 2787 ASP A C     1 
ATOM   9034  O O     . ASP A 1 2787 ? 141.509 155.330 175.154 1.00 124.29 ? 2787 ASP A O     1 
ATOM   9035  C CB    . ASP A 1 2787 ? 140.748 157.169 177.791 1.00 124.29 ? 2787 ASP A CB    1 
ATOM   9036  C CG    . ASP A 1 2787 ? 139.399 156.813 178.384 1.00 124.29 ? 2787 ASP A CG    1 
ATOM   9037  O OD1   . ASP A 1 2787 ? 138.469 156.507 177.610 1.00 124.29 ? 2787 ASP A OD1   1 
ATOM   9038  O OD2   . ASP A 1 2787 ? 139.266 156.841 179.625 1.00 124.29 ? 2787 ASP A OD2   1 
ATOM   9039  N N     . THR A 1 2788 ? 139.299 155.426 175.578 1.00 120.61 ? 2788 THR A N     1 
ATOM   9040  C CA    . THR A 1 2788 ? 139.052 154.124 174.969 1.00 120.61 ? 2788 THR A CA    1 
ATOM   9041  C C     . THR A 1 2788 ? 139.338 154.143 173.473 1.00 120.61 ? 2788 THR A C     1 
ATOM   9042  O O     . THR A 1 2788 ? 139.958 153.214 172.943 1.00 120.61 ? 2788 THR A O     1 
ATOM   9043  C CB    . THR A 1 2788 ? 137.613 153.685 175.231 1.00 120.61 ? 2788 THR A CB    1 
ATOM   9044  O OG1   . THR A 1 2788 ? 137.310 153.850 176.621 1.00 120.61 ? 2788 THR A OG1   1 
ATOM   9045  C CG2   . THR A 1 2788 ? 137.427 152.229 174.849 1.00 120.61 ? 2788 THR A CG2   1 
ATOM   9046  N N     . GLN A 1 2789 ? 138.898 155.189 172.773 1.00 114.18 ? 2789 GLN A N     1 
ATOM   9047  C CA    . GLN A 1 2789 ? 139.123 155.312 171.343 1.00 114.18 ? 2789 GLN A CA    1 
ATOM   9048  C C     . GLN A 1 2789 ? 139.374 156.771 170.990 1.00 114.18 ? 2789 GLN A C     1 
ATOM   9049  O O     . GLN A 1 2789 ? 138.694 157.662 171.517 1.00 114.18 ? 2789 GLN A O     1 
ATOM   9050  C CB    . GLN A 1 2789 ? 137.931 154.784 170.535 1.00 114.18 ? 2789 GLN A CB    1 
ATOM   9051  C CG    . GLN A 1 2789 ? 137.802 153.272 170.528 1.00 114.18 ? 2789 GLN A CG    1 
ATOM   9052  C CD    . GLN A 1 2789 ? 138.949 152.587 169.810 1.00 114.18 ? 2789 GLN A CD    1 
ATOM   9053  O OE1   . GLN A 1 2789 ? 139.686 153.214 169.050 1.00 114.18 ? 2789 GLN A OE1   1 
ATOM   9054  N NE2   . GLN A 1 2789 ? 139.105 151.291 170.051 1.00 114.18 ? 2789 GLN A NE2   1 
ATOM   9055  N N     . PRO A 1 2790 ? 140.329 157.042 170.097 1.00 106.03 ? 2790 PRO A N     1 
ATOM   9056  C CA    . PRO A 1 2790 ? 140.657 158.440 169.775 1.00 106.03 ? 2790 PRO A CA    1 
ATOM   9057  C C     . PRO A 1 2790 ? 139.512 159.215 169.155 1.00 106.03 ? 2790 PRO A C     1 
ATOM   9058  O O     . PRO A 1 2790 ? 139.491 160.446 169.268 1.00 106.03 ? 2790 PRO A O     1 
ATOM   9059  C CB    . PRO A 1 2790 ? 141.831 158.306 168.797 1.00 106.03 ? 2790 PRO A CB    1 
ATOM   9060  C CG    . PRO A 1 2790 ? 141.677 156.948 168.209 1.00 106.03 ? 2790 PRO A CG    1 
ATOM   9061  C CD    . PRO A 1 2790 ? 141.120 156.090 169.303 1.00 106.03 ? 2790 PRO A CD    1 
ATOM   9062  N N     . HIS A 1 2791 ? 138.561 158.548 168.507 1.00 101.45 ? 2791 HIS A N     1 
ATOM   9063  C CA    . HIS A 1 2791 ? 137.463 159.226 167.835 1.00 101.45 ? 2791 HIS A CA    1 
ATOM   9064  C C     . HIS A 1 2791 ? 136.182 159.232 168.656 1.00 101.45 ? 2791 HIS A C     1 
ATOM   9065  O O     . HIS A 1 2791 ? 135.124 159.583 168.131 1.00 101.45 ? 2791 HIS A O     1 
ATOM   9066  C CB    . HIS A 1 2791 ? 137.203 158.587 166.473 1.00 101.45 ? 2791 HIS A CB    1 
ATOM   9067  C CG    . HIS A 1 2791 ? 136.600 157.221 166.552 1.00 101.45 ? 2791 HIS A CG    1 
ATOM   9068  N ND1   . HIS A 1 2791 ? 137.313 156.115 166.959 1.00 101.45 ? 2791 HIS A ND1   1 
ATOM   9069  C CD2   . HIS A 1 2791 ? 135.350 156.782 166.275 1.00 101.45 ? 2791 HIS A CD2   1 
ATOM   9070  C CE1   . HIS A 1 2791 ? 136.528 155.053 166.930 1.00 101.45 ? 2791 HIS A CE1   1 
ATOM   9071  N NE2   . HIS A 1 2791 ? 135.331 155.431 166.519 1.00 101.45 ? 2791 HIS A NE2   1 
ATOM   9072  N N     . TYR A 1 2792 ? 136.251 158.853 169.929 1.00 104.52 ? 2792 TYR A N     1 
ATOM   9073  C CA    . TYR A 1 2792 ? 135.072 158.833 170.794 1.00 104.52 ? 2792 TYR A CA    1 
ATOM   9074  C C     . TYR A 1 2792 ? 134.867 160.217 171.411 1.00 104.52 ? 2792 TYR A C     1 
ATOM   9075  O O     . TYR A 1 2792 ? 134.997 160.428 172.618 1.00 104.52 ? 2792 TYR A O     1 
ATOM   9076  C CB    . TYR A 1 2792 ? 135.222 157.767 171.869 1.00 104.52 ? 2792 TYR A CB    1 
ATOM   9077  C CG    . TYR A 1 2792 ? 134.903 156.363 171.419 1.00 104.52 ? 2792 TYR A CG    1 
ATOM   9078  C CD1   . TYR A 1 2792 ? 134.730 156.060 170.078 1.00 104.52 ? 2792 TYR A CD1   1 
ATOM   9079  C CD2   . TYR A 1 2792 ? 134.774 155.338 172.343 1.00 104.52 ? 2792 TYR A CD2   1 
ATOM   9080  C CE1   . TYR A 1 2792 ? 134.440 154.775 169.672 1.00 104.52 ? 2792 TYR A CE1   1 
ATOM   9081  C CE2   . TYR A 1 2792 ? 134.485 154.055 171.947 1.00 104.52 ? 2792 TYR A CE2   1 
ATOM   9082  C CZ    . TYR A 1 2792 ? 134.318 153.777 170.613 1.00 104.52 ? 2792 TYR A CZ    1 
ATOM   9083  O OH    . TYR A 1 2792 ? 134.028 152.491 170.223 1.00 104.52 ? 2792 TYR A OH    1 
ATOM   9084  N N     . ILE A 1 2793 ? 134.530 161.174 170.550 1.00 94.58  ? 2793 ILE A N     1 
ATOM   9085  C CA    . ILE A 1 2793 ? 134.360 162.566 170.948 1.00 94.58  ? 2793 ILE A CA    1 
ATOM   9086  C C     . ILE A 1 2793 ? 132.925 162.985 170.661 1.00 94.58  ? 2793 ILE A C     1 
ATOM   9087  O O     . ILE A 1 2793 ? 132.403 162.731 169.570 1.00 94.58  ? 2793 ILE A O     1 
ATOM   9088  C CB    . ILE A 1 2793 ? 135.365 163.487 170.232 1.00 94.58  ? 2793 ILE A CB    1 
ATOM   9089  C CG1   . ILE A 1 2793 ? 135.123 164.945 170.616 1.00 94.58  ? 2793 ILE A CG1   1 
ATOM   9090  C CG2   . ILE A 1 2793 ? 135.297 163.302 168.733 1.00 94.58  ? 2793 ILE A CG2   1 
ATOM   9091  C CD1   . ILE A 1 2793 ? 135.364 165.235 172.076 1.00 94.58  ? 2793 ILE A CD1   1 
ATOM   9092  N N     . TYR A 1 2794 ? 132.287 163.611 171.646 1.00 96.70  ? 2794 TYR A N     1 
ATOM   9093  C CA    . TYR A 1 2794 ? 130.897 164.033 171.548 1.00 96.70  ? 2794 TYR A CA    1 
ATOM   9094  C C     . TYR A 1 2794 ? 130.799 165.522 171.836 1.00 96.70  ? 2794 TYR A C     1 
ATOM   9095  O O     . TYR A 1 2794 ? 131.265 165.989 172.879 1.00 96.70  ? 2794 TYR A O     1 
ATOM   9096  C CB    . TYR A 1 2794 ? 130.021 163.245 172.522 1.00 96.70  ? 2794 TYR A CB    1 
ATOM   9097  C CG    . TYR A 1 2794 ? 129.923 161.785 172.167 1.00 96.70  ? 2794 TYR A CG    1 
ATOM   9098  C CD1   . TYR A 1 2794 ? 130.561 160.822 172.929 1.00 96.70  ? 2794 TYR A CD1   1 
ATOM   9099  C CD2   . TYR A 1 2794 ? 129.196 161.372 171.065 1.00 96.70  ? 2794 TYR A CD2   1 
ATOM   9100  C CE1   . TYR A 1 2794 ? 130.478 159.490 172.601 1.00 96.70  ? 2794 TYR A CE1   1 
ATOM   9101  C CE2   . TYR A 1 2794 ? 129.102 160.044 170.733 1.00 96.70  ? 2794 TYR A CE2   1 
ATOM   9102  C CZ    . TYR A 1 2794 ? 129.749 159.107 171.499 1.00 96.70  ? 2794 TYR A CZ    1 
ATOM   9103  O OH    . TYR A 1 2794 ? 129.657 157.778 171.165 1.00 96.70  ? 2794 TYR A OH    1 
ATOM   9104  N N     . SER A 1 2795 ? 130.185 166.255 170.920 1.00 89.34  ? 2795 SER A N     1 
ATOM   9105  C CA    . SER A 1 2795 ? 130.028 167.696 171.022 1.00 89.34  ? 2795 SER A CA    1 
ATOM   9106  C C     . SER A 1 2795 ? 128.592 168.041 170.670 1.00 89.34  ? 2795 SER A C     1 
ATOM   9107  O O     . SER A 1 2795 ? 127.891 167.234 170.052 1.00 89.34  ? 2795 SER A O     1 
ATOM   9108  C CB    . SER A 1 2795 ? 130.992 168.435 170.086 1.00 89.34  ? 2795 SER A CB    1 
ATOM   9109  O OG    . SER A 1 2795 ? 130.495 168.449 168.762 1.00 89.34  ? 2795 SER A OG    1 
ATOM   9110  N N     . PRO A 1 2796 ? 128.119 169.227 171.059 1.00 89.08  ? 2796 PRO A N     1 
ATOM   9111  C CA    . PRO A 1 2796 ? 126.767 169.635 170.652 1.00 89.08  ? 2796 PRO A CA    1 
ATOM   9112  C C     . PRO A 1 2796 ? 126.589 169.715 169.149 1.00 89.08  ? 2796 PRO A C     1 
ATOM   9113  O O     . PRO A 1 2796 ? 125.444 169.742 168.674 1.00 89.08  ? 2796 PRO A O     1 
ATOM   9114  C CB    . PRO A 1 2796 ? 126.594 171.010 171.315 1.00 89.08  ? 2796 PRO A CB    1 
ATOM   9115  C CG    . PRO A 1 2796 ? 127.958 171.429 171.722 1.00 89.08  ? 2796 PRO A CG    1 
ATOM   9116  C CD    . PRO A 1 2796 ? 128.703 170.175 172.018 1.00 89.08  ? 2796 PRO A CD    1 
ATOM   9117  N N     . ARG A 1 2797 ? 127.678 169.757 168.381 1.00 88.96  ? 2797 ARG A N     1 
ATOM   9118  C CA    . ARG A 1 2797 ? 127.549 169.674 166.932 1.00 88.96  ? 2797 ARG A CA    1 
ATOM   9119  C C     . ARG A 1 2797 ? 126.863 168.378 166.524 1.00 88.96  ? 2797 ARG A C     1 
ATOM   9120  O O     . ARG A 1 2797 ? 126.121 168.342 165.536 1.00 88.96  ? 2797 ARG A O     1 
ATOM   9121  C CB    . ARG A 1 2797 ? 128.922 169.794 166.276 1.00 88.96  ? 2797 ARG A CB    1 
ATOM   9122  C CG    . ARG A 1 2797 ? 128.889 170.512 164.945 1.00 88.96  ? 2797 ARG A CG    1 
ATOM   9123  C CD    . ARG A 1 2797 ? 130.175 170.320 164.172 1.00 88.96  ? 2797 ARG A CD    1 
ATOM   9124  N NE    . ARG A 1 2797 ? 131.359 170.539 164.994 1.00 88.96  ? 2797 ARG A NE    1 
ATOM   9125  C CZ    . ARG A 1 2797 ? 132.371 171.322 164.648 1.00 88.96  ? 2797 ARG A CZ    1 
ATOM   9126  N NH1   . ARG A 1 2797 ? 132.369 171.992 163.508 1.00 88.96  ? 2797 ARG A NH1   1 
ATOM   9127  N NH2   . ARG A 1 2797 ? 133.412 171.436 165.468 1.00 88.96  ? 2797 ARG A NH2   1 
ATOM   9128  N N     . GLU A 1 2798 ? 127.082 167.305 167.285 1.00 93.62  ? 2798 GLU A N     1 
ATOM   9129  C CA    . GLU A 1 2798 ? 126.363 166.065 167.021 1.00 93.62  ? 2798 GLU A CA    1 
ATOM   9130  C C     . GLU A 1 2798 ? 124.863 166.257 167.192 1.00 93.62  ? 2798 GLU A C     1 
ATOM   9131  O O     . GLU A 1 2798 ? 124.075 165.775 166.374 1.00 93.62  ? 2798 GLU A O     1 
ATOM   9132  C CB    . GLU A 1 2798 ? 126.867 164.949 167.936 1.00 93.62  ? 2798 GLU A CB    1 
ATOM   9133  C CG    . GLU A 1 2798 ? 128.369 164.726 167.896 1.00 93.62  ? 2798 GLU A CG    1 
ATOM   9134  C CD    . GLU A 1 2798 ? 128.828 164.019 166.636 1.00 93.62  ? 2798 GLU A CD    1 
ATOM   9135  O OE1   . GLU A 1 2798 ? 127.972 163.649 165.809 1.00 93.62  ? 2798 GLU A OE1   1 
ATOM   9136  O OE2   . GLU A 1 2798 ? 130.050 163.830 166.470 1.00 93.62  ? 2798 GLU A OE2   1 
ATOM   9137  N N     . MET A 1 2799 ? 124.447 166.962 168.245 1.00 86.96  ? 2799 MET A N     1 
ATOM   9138  C CA    . MET A 1 2799 ? 123.024 167.226 168.431 1.00 86.96  ? 2799 MET A CA    1 
ATOM   9139  C C     . MET A 1 2799 ? 122.469 168.090 167.311 1.00 86.96  ? 2799 MET A C     1 
ATOM   9140  O O     . MET A 1 2799 ? 121.329 167.895 166.874 1.00 86.96  ? 2799 MET A O     1 
ATOM   9141  C CB    . MET A 1 2799 ? 122.778 167.890 169.780 1.00 86.96  ? 2799 MET A CB    1 
ATOM   9142  C CG    . MET A 1 2799 ? 123.444 167.197 170.929 1.00 86.96  ? 2799 MET A CG    1 
ATOM   9143  S SD    . MET A 1 2799 ? 122.269 166.069 171.678 1.00 86.96  ? 2799 MET A SD    1 
ATOM   9144  C CE    . MET A 1 2799 ? 121.016 167.220 172.227 1.00 86.96  ? 2799 MET A CE    1 
ATOM   9145  N N     . THR A 1 2800 ? 123.246 169.070 166.853 1.00 91.34  ? 2800 THR A N     1 
ATOM   9146  C CA    . THR A 1 2800 ? 122.783 169.900 165.748 1.00 91.34  ? 2800 THR A CA    1 
ATOM   9147  C C     . THR A 1 2800 ? 122.589 169.071 164.485 1.00 91.34  ? 2800 THR A C     1 
ATOM   9148  O O     . THR A 1 2800 ? 121.584 169.225 163.779 1.00 91.34  ? 2800 THR A O     1 
ATOM   9149  C CB    . THR A 1 2800 ? 123.763 171.043 165.504 1.00 91.34  ? 2800 THR A CB    1 
ATOM   9150  O OG1   . THR A 1 2800 ? 123.909 171.803 166.708 1.00 91.34  ? 2800 THR A OG1   1 
ATOM   9151  C CG2   . THR A 1 2800 ? 123.249 171.951 164.409 1.00 91.34  ? 2800 THR A CG2   1 
ATOM   9152  N N     . ARG A 1 2801 ? 123.531 168.171 164.192 1.00 93.85  ? 2801 ARG A N     1 
ATOM   9153  C CA    . ARG A 1 2801 ? 123.367 167.275 163.050 1.00 93.85  ? 2801 ARG A CA    1 
ATOM   9154  C C     . ARG A 1 2801 ? 122.162 166.366 163.237 1.00 93.85  ? 2801 ARG A C     1 
ATOM   9155  O O     . ARG A 1 2801 ? 121.436 166.078 162.281 1.00 93.85  ? 2801 ARG A O     1 
ATOM   9156  C CB    . ARG A 1 2801 ? 124.631 166.445 162.842 1.00 93.85  ? 2801 ARG A CB    1 
ATOM   9157  C CG    . ARG A 1 2801 ? 125.870 167.266 162.561 1.00 93.85  ? 2801 ARG A CG    1 
ATOM   9158  C CD    . ARG A 1 2801 ? 126.793 166.564 161.582 1.00 93.85  ? 2801 ARG A CD    1 
ATOM   9159  N NE    . ARG A 1 2801 ? 127.415 165.382 162.166 1.00 93.85  ? 2801 ARG A NE    1 
ATOM   9160  C CZ    . ARG A 1 2801 ? 128.340 165.404 163.117 1.00 93.85  ? 2801 ARG A CZ    1 
ATOM   9161  N NH1   . ARG A 1 2801 ? 128.779 166.540 163.631 1.00 93.85  ? 2801 ARG A NH1   1 
ATOM   9162  N NH2   . ARG A 1 2801 ? 128.840 164.255 163.560 1.00 93.85  ? 2801 ARG A NH2   1 
ATOM   9163  N N     . TRP A 1 2802 ? 121.942 165.898 164.465 1.00 90.54  ? 2802 TRP A N     1 
ATOM   9164  C CA    . TRP A 1 2802 ? 120.781 165.070 164.773 1.00 90.54  ? 2802 TRP A CA    1 
ATOM   9165  C C     . TRP A 1 2802 ? 119.485 165.797 164.444 1.00 90.54  ? 2802 TRP A C     1 
ATOM   9166  O O     . TRP A 1 2802 ? 118.605 165.256 163.761 1.00 90.54  ? 2802 TRP A O     1 
ATOM   9167  C CB    . TRP A 1 2802 ? 120.830 164.691 166.251 1.00 90.54  ? 2802 TRP A CB    1 
ATOM   9168  C CG    . TRP A 1 2802 ? 119.865 163.653 166.682 1.00 90.54  ? 2802 TRP A CG    1 
ATOM   9169  C CD1   . TRP A 1 2802 ? 118.790 163.194 165.994 1.00 90.54  ? 2802 TRP A CD1   1 
ATOM   9170  C CD2   . TRP A 1 2802 ? 119.887 162.938 167.919 1.00 90.54  ? 2802 TRP A CD2   1 
ATOM   9171  N NE1   . TRP A 1 2802 ? 118.136 162.235 166.723 1.00 90.54  ? 2802 TRP A NE1   1 
ATOM   9172  C CE2   . TRP A 1 2802 ? 118.793 162.060 167.911 1.00 90.54  ? 2802 TRP A CE2   1 
ATOM   9173  C CE3   . TRP A 1 2802 ? 120.729 162.955 169.031 1.00 90.54  ? 2802 TRP A CE3   1 
ATOM   9174  C CZ2   . TRP A 1 2802 ? 118.515 161.209 168.971 1.00 90.54  ? 2802 TRP A CZ2   1 
ATOM   9175  C CZ3   . TRP A 1 2802 ? 120.453 162.108 170.082 1.00 90.54  ? 2802 TRP A CZ3   1 
ATOM   9176  C CH2   . TRP A 1 2802 ? 119.354 161.248 170.047 1.00 90.54  ? 2802 TRP A CH2   1 
ATOM   9177  N N     . VAL A 1 2803 ? 119.351 167.027 164.933 1.00 89.50  ? 2803 VAL A N     1 
ATOM   9178  C CA    . VAL A 1 2803 ? 118.135 167.794 164.690 1.00 89.50  ? 2803 VAL A CA    1 
ATOM   9179  C C     . VAL A 1 2803 ? 117.975 168.077 163.205 1.00 89.50  ? 2803 VAL A C     1 
ATOM   9180  O O     . VAL A 1 2803 ? 116.869 167.988 162.658 1.00 89.50  ? 2803 VAL A O     1 
ATOM   9181  C CB    . VAL A 1 2803 ? 118.143 169.087 165.521 1.00 89.50  ? 2803 VAL A CB    1 
ATOM   9182  C CG1   . VAL A 1 2803 ? 117.207 170.107 164.913 1.00 89.50  ? 2803 VAL A CG1   1 
ATOM   9183  C CG2   . VAL A 1 2803 ? 117.736 168.781 166.944 1.00 89.50  ? 2803 VAL A CG2   1 
ATOM   9184  N N     . ARG A 1 2804 ? 119.072 168.415 162.525 1.00 93.94  ? 2804 ARG A N     1 
ATOM   9185  C CA    . ARG A 1 2804 ? 119.003 168.645 161.087 1.00 93.94  ? 2804 ARG A CA    1 
ATOM   9186  C C     . ARG A 1 2804 ? 118.539 167.397 160.353 1.00 93.94  ? 2804 ARG A C     1 
ATOM   9187  O O     . ARG A 1 2804 ? 117.769 167.482 159.390 1.00 93.94  ? 2804 ARG A O     1 
ATOM   9188  C CB    . ARG A 1 2804 ? 120.361 169.093 160.566 1.00 93.94  ? 2804 ARG A CB    1 
ATOM   9189  C CG    . ARG A 1 2804 ? 120.422 170.559 160.225 1.00 93.94  ? 2804 ARG A CG    1 
ATOM   9190  C CD    . ARG A 1 2804 ? 121.785 170.930 159.695 1.00 93.94  ? 2804 ARG A CD    1 
ATOM   9191  N NE    . ARG A 1 2804 ? 122.803 170.870 160.735 1.00 93.94  ? 2804 ARG A NE    1 
ATOM   9192  C CZ    . ARG A 1 2804 ? 124.035 171.336 160.595 1.00 93.94  ? 2804 ARG A CZ    1 
ATOM   9193  N NH1   . ARG A 1 2804 ? 124.426 171.925 159.478 1.00 93.94  ? 2804 ARG A NH1   1 
ATOM   9194  N NH2   . ARG A 1 2804 ? 124.896 171.209 161.601 1.00 93.94  ? 2804 ARG A NH2   1 
ATOM   9195  N N     . GLY A 1 2805 ? 118.999 166.227 160.792 1.00 95.57  ? 2805 GLY A N     1 
ATOM   9196  C CA    . GLY A 1 2805 ? 118.568 164.993 160.161 1.00 95.57  ? 2805 GLY A CA    1 
ATOM   9197  C C     . GLY A 1 2805 ? 117.095 164.712 160.371 1.00 95.57  ? 2805 GLY A C     1 
ATOM   9198  O O     . GLY A 1 2805 ? 116.389 164.322 159.435 1.00 95.57  ? 2805 GLY A O     1 
ATOM   9199  N N     . ILE A 1 2806 ? 116.606 164.905 161.597 1.00 89.70  ? 2806 ILE A N     1 
ATOM   9200  C CA    . ILE A 1 2806 ? 115.180 164.696 161.832 1.00 89.70  ? 2806 ILE A CA    1 
ATOM   9201  C C     . ILE A 1 2806 ? 114.364 165.681 161.007 1.00 89.70  ? 2806 ILE A C     1 
ATOM   9202  O O     . ILE A 1 2806 ? 113.303 165.337 160.471 1.00 89.70  ? 2806 ILE A O     1 
ATOM   9203  C CB    . ILE A 1 2806 ? 114.842 164.795 163.329 1.00 89.70  ? 2806 ILE A CB    1 
ATOM   9204  C CG1   . ILE A 1 2806 ? 115.832 163.992 164.163 1.00 89.70  ? 2806 ILE A CG1   1 
ATOM   9205  C CG2   . ILE A 1 2806 ? 113.465 164.235 163.587 1.00 89.70  ? 2806 ILE A CG2   1 
ATOM   9206  C CD1   . ILE A 1 2806 ? 115.427 163.870 165.617 1.00 89.70  ? 2806 ILE A CD1   1 
ATOM   9207  N N     . PHE A 1 2807 ? 114.848 166.919 160.883 1.00 94.56  ? 2807 PHE A N     1 
ATOM   9208  C CA    . PHE A 1 2807 ? 114.135 167.916 160.089 1.00 94.56  ? 2807 PHE A CA    1 
ATOM   9209  C C     . PHE A 1 2807 ? 114.109 167.535 158.617 1.00 94.56  ? 2807 PHE A C     1 
ATOM   9210  O O     . PHE A 1 2807 ? 113.084 167.695 157.944 1.00 94.56  ? 2807 PHE A O     1 
ATOM   9211  C CB    . PHE A 1 2807 ? 114.770 169.290 160.273 1.00 94.56  ? 2807 PHE A CB    1 
ATOM   9212  C CG    . PHE A 1 2807 ? 114.169 170.351 159.405 1.00 94.56  ? 2807 PHE A CG    1 
ATOM   9213  C CD1   . PHE A 1 2807 ? 112.972 170.944 159.755 1.00 94.56  ? 2807 PHE A CD1   1 
ATOM   9214  C CD2   . PHE A 1 2807 ? 114.794 170.753 158.241 1.00 94.56  ? 2807 PHE A CD2   1 
ATOM   9215  C CE1   . PHE A 1 2807 ? 112.412 171.919 158.964 1.00 94.56  ? 2807 PHE A CE1   1 
ATOM   9216  C CE2   . PHE A 1 2807 ? 114.237 171.729 157.445 1.00 94.56  ? 2807 PHE A CE2   1 
ATOM   9217  C CZ    . PHE A 1 2807 ? 113.044 172.312 157.808 1.00 94.56  ? 2807 PHE A CZ    1 
ATOM   9218  N N     . GLU A 1 2808 ? 115.230 167.038 158.094 1.00 101.58 ? 2808 GLU A N     1 
ATOM   9219  C CA    . GLU A 1 2808 ? 115.249 166.592 156.707 1.00 101.58 ? 2808 GLU A CA    1 
ATOM   9220  C C     . GLU A 1 2808 ? 114.286 165.434 156.500 1.00 101.58 ? 2808 GLU A C     1 
ATOM   9221  O O     . GLU A 1 2808 ? 113.600 165.361 155.475 1.00 101.58 ? 2808 GLU A O     1 
ATOM   9222  C CB    . GLU A 1 2808 ? 116.665 166.195 156.298 1.00 101.58 ? 2808 GLU A CB    1 
ATOM   9223  C CG    . GLU A 1 2808 ? 116.805 165.846 154.824 1.00 101.58 ? 2808 GLU A CG    1 
ATOM   9224  C CD    . GLU A 1 2808 ? 116.418 164.411 154.523 1.00 101.58 ? 2808 GLU A CD    1 
ATOM   9225  O OE1   . GLU A 1 2808 ? 116.567 163.553 155.419 1.00 101.58 ? 2808 GLU A OE1   1 
ATOM   9226  O OE2   . GLU A 1 2808 ? 115.953 164.144 153.396 1.00 101.58 ? 2808 GLU A OE2   1 
ATOM   9227  N N     . ALA A 1 2809 ? 114.229 164.513 157.462 1.00 98.56  ? 2809 ALA A N     1 
ATOM   9228  C CA    . ALA A 1 2809 ? 113.291 163.401 157.355 1.00 98.56  ? 2809 ALA A CA    1 
ATOM   9229  C C     . ALA A 1 2809 ? 111.852 163.895 157.347 1.00 98.56  ? 2809 ALA A C     1 
ATOM   9230  O O     . ALA A 1 2809 ? 111.021 163.398 156.579 1.00 98.56  ? 2809 ALA A O     1 
ATOM   9231  C CB    . ALA A 1 2809 ? 113.508 162.417 158.502 1.00 98.56  ? 2809 ALA A CB    1 
ATOM   9232  N N     . LEU A 1 2810 ? 111.537 164.871 158.194 1.00 93.42  ? 2810 LEU A N     1 
ATOM   9233  C CA    . LEU A 1 2810 ? 110.159 165.322 158.325 1.00 93.42  ? 2810 LEU A CA    1 
ATOM   9234  C C     . LEU A 1 2810 ? 109.717 166.258 157.208 1.00 93.42  ? 2810 LEU A C     1 
ATOM   9235  O O     . LEU A 1 2810 ? 108.512 166.369 156.962 1.00 93.42  ? 2810 LEU A O     1 
ATOM   9236  C CB    . LEU A 1 2810 ? 109.962 166.023 159.668 1.00 93.42  ? 2810 LEU A CB    1 
ATOM   9237  C CG    . LEU A 1 2810 ? 109.290 165.206 160.767 1.00 93.42  ? 2810 LEU A CG    1 
ATOM   9238  C CD1   . LEU A 1 2810 ? 110.293 164.282 161.419 1.00 93.42  ? 2810 LEU A CD1   1 
ATOM   9239  C CD2   . LEU A 1 2810 ? 108.666 166.123 161.795 1.00 93.42  ? 2810 LEU A CD2   1 
ATOM   9240  N N     . ARG A 1 2811 ? 110.647 166.933 156.534 1.00 103.85 ? 2811 ARG A N     1 
ATOM   9241  C CA    . ARG A 1 2811 ? 110.250 168.019 155.639 1.00 103.85 ? 2811 ARG A CA    1 
ATOM   9242  C C     . ARG A 1 2811 ? 109.351 167.565 154.490 1.00 103.85 ? 2811 ARG A C     1 
ATOM   9243  O O     . ARG A 1 2811 ? 108.283 168.173 154.308 1.00 103.85 ? 2811 ARG A O     1 
ATOM   9244  C CB    . ARG A 1 2811 ? 111.505 168.753 155.153 1.00 103.85 ? 2811 ARG A CB    1 
ATOM   9245  C CG    . ARG A 1 2811 ? 111.240 169.990 154.319 1.00 103.85 ? 2811 ARG A CG    1 
ATOM   9246  C CD    . ARG A 1 2811 ? 111.649 169.749 152.877 1.00 103.85 ? 2811 ARG A CD    1 
ATOM   9247  N NE    . ARG A 1 2811 ? 113.080 169.938 152.675 1.00 103.85 ? 2811 ARG A NE    1 
ATOM   9248  C CZ    . ARG A 1 2811 ? 113.696 169.823 151.506 1.00 103.85 ? 2811 ARG A CZ    1 
ATOM   9249  N NH1   . ARG A 1 2811 ? 113.033 169.517 150.402 1.00 103.85 ? 2811 ARG A NH1   1 
ATOM   9250  N NH2   . ARG A 1 2811 ? 115.010 170.015 151.443 1.00 103.85 ? 2811 ARG A NH2   1 
ATOM   9251  N N     . PRO A 1 2812 ? 109.698 166.542 153.674 1.00 106.31 ? 2812 PRO A N     1 
ATOM   9252  C CA    . PRO A 1 2812 ? 108.714 166.039 152.707 1.00 106.31 ? 2812 PRO A CA    1 
ATOM   9253  C C     . PRO A 1 2812 ? 107.424 165.559 153.350 1.00 106.31 ? 2812 PRO A C     1 
ATOM   9254  O O     . PRO A 1 2812 ? 106.330 165.773 152.820 1.00 106.31 ? 2812 PRO A O     1 
ATOM   9255  C CB    . PRO A 1 2812 ? 109.451 164.860 152.046 1.00 106.31 ? 2812 PRO A CB    1 
ATOM   9256  C CG    . PRO A 1 2812 ? 110.850 164.865 152.672 1.00 106.31 ? 2812 PRO A CG    1 
ATOM   9257  C CD    . PRO A 1 2812 ? 111.031 166.251 153.135 1.00 106.31 ? 2812 PRO A CD    1 
ATOM   9258  N N     . LEU A 1 2813 ? 107.550 164.913 154.504 1.00 108.43 ? 2813 LEU A N     1 
ATOM   9259  C CA    . LEU A 1 2813 ? 106.474 164.097 155.046 1.00 108.43 ? 2813 LEU A CA    1 
ATOM   9260  C C     . LEU A 1 2813 ? 105.388 164.960 155.679 1.00 108.43 ? 2813 LEU A C     1 
ATOM   9261  O O     . LEU A 1 2813 ? 105.641 166.071 156.151 1.00 108.43 ? 2813 LEU A O     1 
ATOM   9262  C CB    . LEU A 1 2813 ? 107.037 163.110 156.066 1.00 108.43 ? 2813 LEU A CB    1 
ATOM   9263  C CG    . LEU A 1 2813 ? 106.148 161.958 156.524 1.00 108.43 ? 2813 LEU A CG    1 
ATOM   9264  C CD1   . LEU A 1 2813 ? 107.003 160.731 156.768 1.00 108.43 ? 2813 LEU A CD1   1 
ATOM   9265  C CD2   . LEU A 1 2813 ? 105.387 162.325 157.776 1.00 108.43 ? 2813 LEU A CD2   1 
ATOM   9266  N N     . GLU A 1 2814 ? 104.167 164.431 155.682 1.00 117.69 ? 2814 GLU A N     1 
ATOM   9267  C CA    . GLU A 1 2814 ? 103.005 165.126 156.211 1.00 117.69 ? 2814 GLU A CA    1 
ATOM   9268  C C     . GLU A 1 2814 ? 102.182 164.181 157.077 1.00 117.69 ? 2814 GLU A C     1 
ATOM   9269  O O     . GLU A 1 2814 ? 102.051 162.993 156.772 1.00 117.69 ? 2814 GLU A O     1 
ATOM   9270  C CB    . GLU A 1 2814 ? 102.141 165.686 155.072 1.00 117.69 ? 2814 GLU A CB    1 
ATOM   9271  C CG    . GLU A 1 2814 ? 101.029 166.603 155.524 1.00 117.69 ? 2814 GLU A CG    1 
ATOM   9272  C CD    . GLU A 1 2814 ? 101.503 167.616 156.540 1.00 117.69 ? 2814 GLU A CD    1 
ATOM   9273  O OE1   . GLU A 1 2814 ? 102.307 168.497 156.168 1.00 117.69 ? 2814 GLU A OE1   1 
ATOM   9274  O OE2   . GLU A 1 2814 ? 101.078 167.528 157.711 1.00 117.69 ? 2814 GLU A OE2   1 
ATOM   9275  N N     . THR A 1 2815 ? 101.628 164.725 158.164 1.00 120.46 ? 2815 THR A N     1 
ATOM   9276  C CA    . THR A 1 2815 ? 100.708 164.011 159.055 1.00 120.46 ? 2815 THR A CA    1 
ATOM   9277  C C     . THR A 1 2815 ? 101.341 162.737 159.624 1.00 120.46 ? 2815 THR A C     1 
ATOM   9278  O O     . THR A 1 2815 ? 100.908 161.616 159.351 1.00 120.46 ? 2815 THR A O     1 
ATOM   9279  C CB    . THR A 1 2815 ? 99.386  163.692 158.348 1.00 120.46 ? 2815 THR A CB    1 
ATOM   9280  O OG1   . THR A 1 2815 ? 99.616  162.746 157.296 1.00 120.46 ? 2815 THR A OG1   1 
ATOM   9281  C CG2   . THR A 1 2815 ? 98.769  164.955 157.771 1.00 120.46 ? 2815 THR A CG2   1 
ATOM   9282  N N     . LEU A 1 2816 ? 102.375 162.929 160.426 1.00 109.37 ? 2816 LEU A N     1 
ATOM   9283  C CA    . LEU A 1 2816 ? 103.039 161.795 161.060 1.00 109.37 ? 2816 LEU A CA    1 
ATOM   9284  C C     . LEU A 1 2816 ? 102.481 161.573 162.457 1.00 109.37 ? 2816 LEU A C     1 
ATOM   9285  O O     . LEU A 1 2816 ? 102.304 162.540 163.205 1.00 109.37 ? 2816 LEU A O     1 
ATOM   9286  C CB    . LEU A 1 2816 ? 104.538 162.025 161.154 1.00 109.37 ? 2816 LEU A CB    1 
ATOM   9287  C CG    . LEU A 1 2816 ? 105.395 160.798 161.461 1.00 109.37 ? 2816 LEU A CG    1 
ATOM   9288  C CD1   . LEU A 1 2816 ? 105.180 159.721 160.419 1.00 109.37 ? 2816 LEU A CD1   1 
ATOM   9289  C CD2   . LEU A 1 2816 ? 106.856 161.185 161.531 1.00 109.37 ? 2816 LEU A CD2   1 
ATOM   9290  N N     . PRO A 1 2817 ? 102.188 160.336 162.842 1.00 109.12 ? 2817 PRO A N     1 
ATOM   9291  C CA    . PRO A 1 2817 ? 101.854 160.060 164.242 1.00 109.12 ? 2817 PRO A CA    1 
ATOM   9292  C C     . PRO A 1 2817 ? 103.101 160.099 165.112 1.00 109.12 ? 2817 PRO A C     1 
ATOM   9293  O O     . PRO A 1 2817 ? 104.229 160.237 164.635 1.00 109.12 ? 2817 PRO A O     1 
ATOM   9294  C CB    . PRO A 1 2817 ? 101.249 158.656 164.194 1.00 109.12 ? 2817 PRO A CB    1 
ATOM   9295  C CG    . PRO A 1 2817 ? 101.862 158.033 162.991 1.00 109.12 ? 2817 PRO A CG    1 
ATOM   9296  C CD    . PRO A 1 2817 ? 102.044 159.142 161.994 1.00 109.12 ? 2817 PRO A CD    1 
ATOM   9297  N N     . VAL A 1 2818 ? 102.877 159.971 166.422 1.00 112.30 ? 2818 VAL A N     1 
ATOM   9298  C CA    . VAL A 1 2818 ? 103.989 159.919 167.367 1.00 112.30 ? 2818 VAL A CA    1 
ATOM   9299  C C     . VAL A 1 2818 ? 104.893 158.734 167.062 1.00 112.30 ? 2818 VAL A C     1 
ATOM   9300  O O     . VAL A 1 2818 ? 106.113 158.795 167.275 1.00 112.30 ? 2818 VAL A O     1 
ATOM   9301  C CB    . VAL A 1 2818 ? 103.447 159.872 168.811 1.00 112.30 ? 2818 VAL A CB    1 
ATOM   9302  C CG1   . VAL A 1 2818 ? 102.397 158.786 168.946 1.00 112.30 ? 2818 VAL A CG1   1 
ATOM   9303  C CG2   . VAL A 1 2818 ? 104.572 159.649 169.809 1.00 112.30 ? 2818 VAL A CG2   1 
ATOM   9304  N N     . GLU A 1 2819 ? 104.318 157.647 166.543 1.00 115.94 ? 2819 GLU A N     1 
ATOM   9305  C CA    . GLU A 1 2819 ? 105.105 156.461 166.231 1.00 115.94 ? 2819 GLU A CA    1 
ATOM   9306  C C     . GLU A 1 2819 ? 106.209 156.781 165.235 1.00 115.94 ? 2819 GLU A C     1 
ATOM   9307  O O     . GLU A 1 2819 ? 107.375 156.428 165.447 1.00 115.94 ? 2819 GLU A O     1 
ATOM   9308  C CB    . GLU A 1 2819 ? 104.192 155.360 165.691 1.00 115.94 ? 2819 GLU A CB    1 
ATOM   9309  C CG    . GLU A 1 2819 ? 103.427 154.603 166.764 1.00 115.94 ? 2819 GLU A CG    1 
ATOM   9310  C CD    . GLU A 1 2819 ? 102.261 155.391 167.320 1.00 115.94 ? 2819 GLU A CD    1 
ATOM   9311  O OE1   . GLU A 1 2819 ? 101.909 156.435 166.733 1.00 115.94 ? 2819 GLU A OE1   1 
ATOM   9312  O OE2   . GLU A 1 2819 ? 101.698 154.966 168.349 1.00 115.94 ? 2819 GLU A OE2   1 
ATOM   9313  N N     . GLY A 1 2820 ? 105.860 157.462 164.143 1.00 109.80 ? 2820 GLY A N     1 
ATOM   9314  C CA    . GLY A 1 2820 ? 106.868 157.826 163.165 1.00 109.80 ? 2820 GLY A CA    1 
ATOM   9315  C C     . GLY A 1 2820 ? 107.924 158.746 163.742 1.00 109.80 ? 2820 GLY A C     1 
ATOM   9316  O O     . GLY A 1 2820 ? 109.109 158.620 163.427 1.00 109.80 ? 2820 GLY A O     1 
ATOM   9317  N N     . LEU A 1 2821 ? 107.509 159.680 164.598 1.00 107.42 ? 2821 LEU A N     1 
ATOM   9318  C CA    . LEU A 1 2821 ? 108.461 160.609 165.196 1.00 107.42 ? 2821 LEU A CA    1 
ATOM   9319  C C     . LEU A 1 2821 ? 109.488 159.872 166.042 1.00 107.42 ? 2821 LEU A C     1 
ATOM   9320  O O     . LEU A 1 2821 ? 110.698 160.088 165.902 1.00 107.42 ? 2821 LEU A O     1 
ATOM   9321  C CB    . LEU A 1 2821 ? 107.724 161.648 166.036 1.00 107.42 ? 2821 LEU A CB    1 
ATOM   9322  C CG    . LEU A 1 2821 ? 108.631 162.699 166.670 1.00 107.42 ? 2821 LEU A CG    1 
ATOM   9323  C CD1   . LEU A 1 2821 ? 109.451 163.394 165.598 1.00 107.42 ? 2821 LEU A CD1   1 
ATOM   9324  C CD2   . LEU A 1 2821 ? 107.813 163.702 167.465 1.00 107.42 ? 2821 LEU A CD2   1 
ATOM   9325  N N     . ILE A 1 2822 ? 109.022 158.987 166.925 1.00 104.47 ? 2822 ILE A N     1 
ATOM   9326  C CA    . ILE A 1 2822 ? 109.950 158.249 167.774 1.00 104.47 ? 2822 ILE A CA    1 
ATOM   9327  C C     . ILE A 1 2822 ? 110.811 157.315 166.937 1.00 104.47 ? 2822 ILE A C     1 
ATOM   9328  O O     . ILE A 1 2822 ? 111.997 157.119 167.225 1.00 104.47 ? 2822 ILE A O     1 
ATOM   9329  C CB    . ILE A 1 2822 ? 109.189 157.494 168.876 1.00 104.47 ? 2822 ILE A CB    1 
ATOM   9330  C CG1   . ILE A 1 2822 ? 108.463 158.486 169.779 1.00 104.47 ? 2822 ILE A CG1   1 
ATOM   9331  C CG2   . ILE A 1 2822 ? 110.140 156.651 169.701 1.00 104.47 ? 2822 ILE A CG2   1 
ATOM   9332  C CD1   . ILE A 1 2822 ? 109.381 159.519 170.389 1.00 104.47 ? 2822 ILE A CD1   1 
ATOM   9333  N N     . ARG A 1 2823 ? 110.238 156.730 165.884 1.00 108.05 ? 2823 ARG A N     1 
ATOM   9334  C CA    . ARG A 1 2823 ? 111.030 155.864 165.021 1.00 108.05 ? 2823 ARG A CA    1 
ATOM   9335  C C     . ARG A 1 2823 ? 112.154 156.639 164.347 1.00 108.05 ? 2823 ARG A C     1 
ATOM   9336  O O     . ARG A 1 2823 ? 113.290 156.160 164.283 1.00 108.05 ? 2823 ARG A O     1 
ATOM   9337  C CB    . ARG A 1 2823 ? 110.134 155.198 163.981 1.00 108.05 ? 2823 ARG A CB    1 
ATOM   9338  C CG    . ARG A 1 2823 ? 110.776 154.007 163.294 1.00 108.05 ? 2823 ARG A CG    1 
ATOM   9339  C CD    . ARG A 1 2823 ? 110.277 152.686 163.848 1.00 108.05 ? 2823 ARG A CD    1 
ATOM   9340  N NE    . ARG A 1 2823 ? 111.003 151.562 163.269 1.00 108.05 ? 2823 ARG A NE    1 
ATOM   9341  C CZ    . ARG A 1 2823 ? 110.823 151.111 162.035 1.00 108.05 ? 2823 ARG A CZ    1 
ATOM   9342  N NH1   . ARG A 1 2823 ? 109.940 151.661 161.218 1.00 108.05 ? 2823 ARG A NH1   1 
ATOM   9343  N NH2   . ARG A 1 2823 ? 111.550 150.082 161.608 1.00 108.05 ? 2823 ARG A NH2   1 
ATOM   9344  N N     . ILE A 1 2824 ? 111.863 157.842 163.851 1.00 98.08  ? 2824 ILE A N     1 
ATOM   9345  C CA    . ILE A 1 2824 ? 112.902 158.637 163.203 1.00 98.08  ? 2824 ILE A CA    1 
ATOM   9346  C C     . ILE A 1 2824 ? 113.946 159.078 164.218 1.00 98.08  ? 2824 ILE A C     1 
ATOM   9347  O O     . ILE A 1 2824 ? 115.148 159.101 163.923 1.00 98.08  ? 2824 ILE A O     1 
ATOM   9348  C CB    . ILE A 1 2824 ? 112.283 159.836 162.465 1.00 98.08  ? 2824 ILE A CB    1 
ATOM   9349  C CG1   . ILE A 1 2824 ? 111.329 159.350 161.378 1.00 98.08  ? 2824 ILE A CG1   1 
ATOM   9350  C CG2   . ILE A 1 2824 ? 113.365 160.691 161.840 1.00 98.08  ? 2824 ILE A CG2   1 
ATOM   9351  C CD1   . ILE A 1 2824 ? 110.394 160.415 160.871 1.00 98.08  ? 2824 ILE A CD1   1 
ATOM   9352  N N     . TRP A 1 2825 ? 113.510 159.435 165.426 1.00 100.24 ? 2825 TRP A N     1 
ATOM   9353  C CA    . TRP A 1 2825 ? 114.455 159.814 166.470 1.00 100.24 ? 2825 TRP A CA    1 
ATOM   9354  C C     . TRP A 1 2825 ? 115.405 158.667 166.787 1.00 100.24 ? 2825 TRP A C     1 
ATOM   9355  O O     . TRP A 1 2825 ? 116.624 158.859 166.879 1.00 100.24 ? 2825 TRP A O     1 
ATOM   9356  C CB    . TRP A 1 2825 ? 113.692 160.245 167.721 1.00 100.24 ? 2825 TRP A CB    1 
ATOM   9357  C CG    . TRP A 1 2825 ? 114.536 160.401 168.941 1.00 100.24 ? 2825 TRP A CG    1 
ATOM   9358  C CD1   . TRP A 1 2825 ? 115.151 161.536 169.367 1.00 100.24 ? 2825 TRP A CD1   1 
ATOM   9359  C CD2   . TRP A 1 2825 ? 114.846 159.391 169.906 1.00 100.24 ? 2825 TRP A CD2   1 
ATOM   9360  N NE1   . TRP A 1 2825 ? 115.828 161.299 170.535 1.00 100.24 ? 2825 TRP A NE1   1 
ATOM   9361  C CE2   . TRP A 1 2825 ? 115.659 159.987 170.886 1.00 100.24 ? 2825 TRP A CE2   1 
ATOM   9362  C CE3   . TRP A 1 2825 ? 114.517 158.040 170.034 1.00 100.24 ? 2825 TRP A CE3   1 
ATOM   9363  C CZ2   . TRP A 1 2825 ? 116.148 159.280 171.979 1.00 100.24 ? 2825 TRP A CZ2   1 
ATOM   9364  C CZ3   . TRP A 1 2825 ? 115.005 157.340 171.119 1.00 100.24 ? 2825 TRP A CZ3   1 
ATOM   9365  C CH2   . TRP A 1 2825 ? 115.810 157.960 172.077 1.00 100.24 ? 2825 TRP A CH2   1 
ATOM   9366  N N     . ALA A 1 2826 ? 114.860 157.460 166.943 1.00 100.21 ? 2826 ALA A N     1 
ATOM   9367  C CA    . ALA A 1 2826 ? 115.698 156.300 167.225 1.00 100.21 ? 2826 ALA A CA    1 
ATOM   9368  C C     . ALA A 1 2826 ? 116.615 155.989 166.053 1.00 100.21 ? 2826 ALA A C     1 
ATOM   9369  O O     . ALA A 1 2826 ? 117.775 155.609 166.248 1.00 100.21 ? 2826 ALA A O     1 
ATOM   9370  C CB    . ALA A 1 2826 ? 114.827 155.092 167.565 1.00 100.21 ? 2826 ALA A CB    1 
ATOM   9371  N N     . HIS A 1 2827 ? 116.111 156.139 164.828 1.00 100.47 ? 2827 HIS A N     1 
ATOM   9372  C CA    . HIS A 1 2827 ? 116.944 155.920 163.654 1.00 100.47 ? 2827 HIS A CA    1 
ATOM   9373  C C     . HIS A 1 2827 ? 118.145 156.849 163.668 1.00 100.47 ? 2827 HIS A C     1 
ATOM   9374  O O     . HIS A 1 2827 ? 119.288 156.408 163.512 1.00 100.47 ? 2827 HIS A O     1 
ATOM   9375  C CB    . HIS A 1 2827 ? 116.122 156.130 162.385 1.00 100.47 ? 2827 HIS A CB    1 
ATOM   9376  C CG    . HIS A 1 2827 ? 116.947 156.246 161.142 1.00 100.47 ? 2827 HIS A CG    1 
ATOM   9377  N ND1   . HIS A 1 2827 ? 117.004 157.400 160.391 1.00 100.47 ? 2827 HIS A ND1   1 
ATOM   9378  C CD2   . HIS A 1 2827 ? 117.748 155.352 160.517 1.00 100.47 ? 2827 HIS A CD2   1 
ATOM   9379  C CE1   . HIS A 1 2827 ? 117.811 157.215 159.363 1.00 100.47 ? 2827 HIS A CE1   1 
ATOM   9380  N NE2   . HIS A 1 2827 ? 118.272 155.980 159.413 1.00 100.47 ? 2827 HIS A NE2   1 
ATOM   9381  N N     . GLU A 1 2828 ? 117.904 158.142 163.877 1.00 97.82  ? 2828 GLU A N     1 
ATOM   9382  C CA    . GLU A 1 2828 ? 119.003 159.100 163.869 1.00 97.82  ? 2828 GLU A CA    1 
ATOM   9383  C C     . GLU A 1 2828 ? 119.975 158.833 165.008 1.00 97.82  ? 2828 GLU A C     1 
ATOM   9384  O O     . GLU A 1 2828 ? 121.197 158.906 164.822 1.00 97.82  ? 2828 GLU A O     1 
ATOM   9385  C CB    . GLU A 1 2828 ? 118.461 160.523 163.945 1.00 97.82  ? 2828 GLU A CB    1 
ATOM   9386  C CG    . GLU A 1 2828 ? 117.925 161.039 162.626 1.00 97.82  ? 2828 GLU A CG    1 
ATOM   9387  C CD    . GLU A 1 2828 ? 118.831 160.707 161.460 1.00 97.82  ? 2828 GLU A CD    1 
ATOM   9388  O OE1   . GLU A 1 2828 ? 120.046 160.982 161.541 1.00 97.82  ? 2828 GLU A OE1   1 
ATOM   9389  O OE2   . GLU A 1 2828 ? 118.328 160.163 160.456 1.00 97.82  ? 2828 GLU A OE2   1 
ATOM   9390  N N     . ALA A 1 2829 ? 119.455 158.514 166.195 1.00 98.07  ? 2829 ALA A N     1 
ATOM   9391  C CA    . ALA A 1 2829 ? 120.336 158.207 167.315 1.00 98.07  ? 2829 ALA A CA    1 
ATOM   9392  C C     . ALA A 1 2829 ? 121.224 157.017 166.997 1.00 98.07  ? 2829 ALA A C     1 
ATOM   9393  O O     . ALA A 1 2829 ? 122.429 157.040 167.270 1.00 98.07  ? 2829 ALA A O     1 
ATOM   9394  C CB    . ALA A 1 2829 ? 119.518 157.935 168.574 1.00 98.07  ? 2829 ALA A CB    1 
ATOM   9395  N N     . LEU A 1 2830 ? 120.647 155.967 166.411 1.00 100.44 ? 2830 LEU A N     1 
ATOM   9396  C CA    . LEU A 1 2830 ? 121.444 154.810 166.030 1.00 100.44 ? 2830 LEU A CA    1 
ATOM   9397  C C     . LEU A 1 2830 ? 122.506 155.191 165.012 1.00 100.44 ? 2830 LEU A C     1 
ATOM   9398  O O     . LEU A 1 2830 ? 123.660 154.760 165.116 1.00 100.44 ? 2830 LEU A O     1 
ATOM   9399  C CB    . LEU A 1 2830 ? 120.548 153.711 165.463 1.00 100.44 ? 2830 LEU A CB    1 
ATOM   9400  C CG    . LEU A 1 2830 ? 120.254 152.491 166.333 1.00 100.44 ? 2830 LEU A CG    1 
ATOM   9401  C CD1   . LEU A 1 2830 ? 119.278 152.837 167.436 1.00 100.44 ? 2830 LEU A CD1   1 
ATOM   9402  C CD2   . LEU A 1 2830 ? 119.728 151.349 165.482 1.00 100.44 ? 2830 LEU A CD2   1 
ATOM   9403  N N     . ARG A 1 2831 ? 122.141 156.004 164.020 1.00 98.18  ? 2831 ARG A N     1 
ATOM   9404  C CA    . ARG A 1 2831 ? 123.065 156.215 162.915 1.00 98.18  ? 2831 ARG A CA    1 
ATOM   9405  C C     . ARG A 1 2831 ? 124.179 157.162 163.331 1.00 98.18  ? 2831 ARG A C     1 
ATOM   9406  O O     . ARG A 1 2831 ? 125.251 157.161 162.720 1.00 98.18  ? 2831 ARG A O     1 
ATOM   9407  C CB    . ARG A 1 2831 ? 122.335 156.776 161.696 1.00 98.18  ? 2831 ARG A CB    1 
ATOM   9408  C CG    . ARG A 1 2831 ? 121.137 155.946 161.225 1.00 98.18  ? 2831 ARG A CG    1 
ATOM   9409  C CD    . ARG A 1 2831 ? 121.143 154.452 161.608 1.00 98.18  ? 2831 ARG A CD    1 
ATOM   9410  N NE    . ARG A 1 2831 ? 121.936 153.529 160.806 1.00 98.18  ? 2831 ARG A NE    1 
ATOM   9411  C CZ    . ARG A 1 2831 ? 121.751 153.321 159.508 1.00 98.18  ? 2831 ARG A CZ    1 
ATOM   9412  N NH1   . ARG A 1 2831 ? 120.871 154.019 158.812 1.00 98.18  ? 2831 ARG A NH1   1 
ATOM   9413  N NH2   . ARG A 1 2831 ? 122.414 152.340 158.908 1.00 98.18  ? 2831 ARG A NH2   1 
ATOM   9414  N N     . LEU A 1 2832 ? 123.940 157.977 164.364 1.00 90.50  ? 2832 LEU A N     1 
ATOM   9415  C CA    . LEU A 1 2832 ? 124.927 158.950 164.821 1.00 90.50  ? 2832 LEU A CA    1 
ATOM   9416  C C     . LEU A 1 2832 ? 125.754 158.472 166.008 1.00 90.50  ? 2832 LEU A C     1 
ATOM   9417  O O     . LEU A 1 2832 ? 126.862 158.976 166.217 1.00 90.50  ? 2832 LEU A O     1 
ATOM   9418  C CB    . LEU A 1 2832 ? 124.234 160.262 165.197 1.00 90.50  ? 2832 LEU A CB    1 
ATOM   9419  C CG    . LEU A 1 2832 ? 123.946 161.246 164.064 1.00 90.50  ? 2832 LEU A CG    1 
ATOM   9420  C CD1   . LEU A 1 2832 ? 123.608 162.610 164.628 1.00 90.50  ? 2832 LEU A CD1   1 
ATOM   9421  C CD2   . LEU A 1 2832 ? 125.125 161.345 163.118 1.00 90.50  ? 2832 LEU A CD2   1 
ATOM   9422  N N     . PHE A 1 2833 ? 125.252 157.522 166.791 1.00 96.80  ? 2833 PHE A N     1 
ATOM   9423  C CA    . PHE A 1 2833 ? 125.942 157.061 167.991 1.00 96.80  ? 2833 PHE A CA    1 
ATOM   9424  C C     . PHE A 1 2833 ? 126.342 155.598 167.937 1.00 96.80  ? 2833 PHE A C     1 
ATOM   9425  O O     . PHE A 1 2833 ? 127.456 155.253 168.332 1.00 96.80  ? 2833 PHE A O     1 
ATOM   9426  C CB    . PHE A 1 2833 ? 125.061 157.279 169.231 1.00 96.80  ? 2833 PHE A CB    1 
ATOM   9427  C CG    . PHE A 1 2833 ? 124.812 158.719 169.562 1.00 96.80  ? 2833 PHE A CG    1 
ATOM   9428  C CD1   . PHE A 1 2833 ? 123.937 159.479 168.809 1.00 96.80  ? 2833 PHE A CD1   1 
ATOM   9429  C CD2   . PHE A 1 2833 ? 125.431 159.303 170.649 1.00 96.80  ? 2833 PHE A CD2   1 
ATOM   9430  C CE1   . PHE A 1 2833 ? 123.705 160.800 169.121 1.00 96.80  ? 2833 PHE A CE1   1 
ATOM   9431  C CE2   . PHE A 1 2833 ? 125.200 160.621 170.966 1.00 96.80  ? 2833 PHE A CE2   1 
ATOM   9432  C CZ    . PHE A 1 2833 ? 124.335 161.371 170.200 1.00 96.80  ? 2833 PHE A CZ    1 
ATOM   9433  N N     . GLN A 1 2834 ? 125.456 154.722 167.467 1.00 107.49 ? 2834 GLN A N     1 
ATOM   9434  C CA    . GLN A 1 2834 ? 125.721 153.291 167.541 1.00 107.49 ? 2834 GLN A CA    1 
ATOM   9435  C C     . GLN A 1 2834 ? 126.760 152.849 166.521 1.00 107.49 ? 2834 GLN A C     1 
ATOM   9436  O O     . GLN A 1 2834 ? 127.556 151.946 166.796 1.00 107.49 ? 2834 GLN A O     1 
ATOM   9437  C CB    . GLN A 1 2834 ? 124.423 152.512 167.348 1.00 107.49 ? 2834 GLN A CB    1 
ATOM   9438  C CG    . GLN A 1 2834 ? 124.451 151.113 167.921 1.00 107.49 ? 2834 GLN A CG    1 
ATOM   9439  C CD    . GLN A 1 2834 ? 124.084 150.064 166.894 1.00 107.49 ? 2834 GLN A CD    1 
ATOM   9440  O OE1   . GLN A 1 2834 ? 124.175 150.302 165.691 1.00 107.49 ? 2834 GLN A OE1   1 
ATOM   9441  N NE2   . GLN A 1 2834 ? 123.651 148.900 167.364 1.00 107.49 ? 2834 GLN A NE2   1 
ATOM   9442  N N     . ASP A 1 2835 ? 126.773 153.468 165.346 1.00 100.01 ? 2835 ASP A N     1 
ATOM   9443  C CA    . ASP A 1 2835 ? 127.634 153.007 164.266 1.00 100.01 ? 2835 ASP A CA    1 
ATOM   9444  C C     . ASP A 1 2835 ? 129.057 153.548 164.338 1.00 100.01 ? 2835 ASP A C     1 
ATOM   9445  O O     . ASP A 1 2835 ? 129.871 153.215 163.470 1.00 100.01 ? 2835 ASP A O     1 
ATOM   9446  C CB    . ASP A 1 2835 ? 126.951 153.304 162.917 1.00 100.01 ? 2835 ASP A CB    1 
ATOM   9447  C CG    . ASP A 1 2835 ? 127.297 154.673 162.316 1.00 100.01 ? 2835 ASP A CG    1 
ATOM   9448  O OD1   . ASP A 1 2835 ? 128.128 155.441 162.836 1.00 100.01 ? 2835 ASP A OD1   1 
ATOM   9449  O OD2   . ASP A 1 2835 ? 126.704 154.985 161.263 1.00 100.01 ? 2835 ASP A OD2   1 
ATOM   9450  N N     . ARG A 1 2836 ? 129.377 154.379 165.326 1.00 96.66  ? 2836 ARG A N     1 
ATOM   9451  C CA    . ARG A 1 2836 ? 130.747 154.834 165.514 1.00 96.66  ? 2836 ARG A CA    1 
ATOM   9452  C C     . ARG A 1 2836 ? 131.527 153.972 166.497 1.00 96.66  ? 2836 ARG A C     1 
ATOM   9453  O O     . ARG A 1 2836 ? 132.720 154.216 166.698 1.00 96.66  ? 2836 ARG A O     1 
ATOM   9454  C CB    . ARG A 1 2836 ? 130.767 156.284 166.000 1.00 96.66  ? 2836 ARG A CB    1 
ATOM   9455  C CG    . ARG A 1 2836 ? 130.165 156.465 167.373 1.00 96.66  ? 2836 ARG A CG    1 
ATOM   9456  C CD    . ARG A 1 2836 ? 130.779 157.645 168.096 1.00 96.66  ? 2836 ARG A CD    1 
ATOM   9457  N NE    . ARG A 1 2836 ? 130.351 158.917 167.529 1.00 96.66  ? 2836 ARG A NE    1 
ATOM   9458  C CZ    . ARG A 1 2836 ? 130.753 160.101 167.969 1.00 96.66  ? 2836 ARG A CZ    1 
ATOM   9459  N NH1   . ARG A 1 2836 ? 131.649 160.211 168.935 1.00 96.66  ? 2836 ARG A NH1   1 
ATOM   9460  N NH2   . ARG A 1 2836 ? 130.234 161.203 167.435 1.00 96.66  ? 2836 ARG A NH2   1 
ATOM   9461  N N     . LEU A 1 2837 ? 130.886 152.985 167.113 1.00 106.24 ? 2837 LEU A N     1 
ATOM   9462  C CA    . LEU A 1 2837 ? 131.516 152.137 168.113 1.00 106.24 ? 2837 LEU A CA    1 
ATOM   9463  C C     . LEU A 1 2837 ? 132.209 150.947 167.458 1.00 106.24 ? 2837 LEU A C     1 
ATOM   9464  O O     . LEU A 1 2837 ? 132.025 150.663 166.274 1.00 106.24 ? 2837 LEU A O     1 
ATOM   9465  C CB    . LEU A 1 2837 ? 130.478 151.656 169.121 1.00 106.24 ? 2837 LEU A CB    1 
ATOM   9466  C CG    . LEU A 1 2837 ? 129.502 152.746 169.554 1.00 106.24 ? 2837 LEU A CG    1 
ATOM   9467  C CD1   . LEU A 1 2837 ? 128.247 152.144 170.152 1.00 106.24 ? 2837 LEU A CD1   1 
ATOM   9468  C CD2   . LEU A 1 2837 ? 130.169 153.678 170.545 1.00 106.24 ? 2837 LEU A CD2   1 
ATOM   9469  N N     . VAL A 1 2838 ? 133.014 150.242 168.253 1.00 109.54 ? 2838 VAL A N     1 
ATOM   9470  C CA    . VAL A 1 2838 ? 133.825 149.149 167.728 1.00 109.54 ? 2838 VAL A CA    1 
ATOM   9471  C C     . VAL A 1 2838 ? 133.262 147.798 168.149 1.00 109.54 ? 2838 VAL A C     1 
ATOM   9472  O O     . VAL A 1 2838 ? 132.867 146.991 167.301 1.00 109.54 ? 2838 VAL A O     1 
ATOM   9473  C CB    . VAL A 1 2838 ? 135.290 149.292 168.174 1.00 109.54 ? 2838 VAL A CB    1 
ATOM   9474  C CG1   . VAL A 1 2838 ? 136.059 148.022 167.865 1.00 109.54 ? 2838 VAL A CG1   1 
ATOM   9475  C CG2   . VAL A 1 2838 ? 135.928 150.482 167.486 1.00 109.54 ? 2838 VAL A CG2   1 
ATOM   9476  N N     . GLU A 1 2839 ? 133.222 147.536 169.452 1.00 120.23 ? 2839 GLU A N     1 
ATOM   9477  C CA    . GLU A 1 2839 ? 132.786 146.234 169.935 1.00 120.23 ? 2839 GLU A CA    1 
ATOM   9478  C C     . GLU A 1 2839 ? 131.267 146.133 169.946 1.00 120.23 ? 2839 GLU A C     1 
ATOM   9479  O O     . GLU A 1 2839 ? 130.554 147.131 170.083 1.00 120.23 ? 2839 GLU A O     1 
ATOM   9480  C CB    . GLU A 1 2839 ? 133.333 145.962 171.336 1.00 120.23 ? 2839 GLU A CB    1 
ATOM   9481  C CG    . GLU A 1 2839 ? 134.833 146.152 171.461 1.00 120.23 ? 2839 GLU A CG    1 
ATOM   9482  C CD    . GLU A 1 2839 ? 135.273 146.374 172.891 1.00 120.23 ? 2839 GLU A CD    1 
ATOM   9483  O OE1   . GLU A 1 2839 ? 134.898 145.560 173.759 1.00 120.23 ? 2839 GLU A OE1   1 
ATOM   9484  O OE2   . GLU A 1 2839 ? 135.997 147.358 173.148 1.00 120.23 ? 2839 GLU A OE2   1 
ATOM   9485  N N     . ASP A 1 2840 ? 130.777 144.900 169.803 1.00 126.44 ? 2840 ASP A N     1 
ATOM   9486  C CA    . ASP A 1 2840 ? 129.337 144.672 169.775 1.00 126.44 ? 2840 ASP A CA    1 
ATOM   9487  C C     . ASP A 1 2840 ? 128.681 145.047 171.096 1.00 126.44 ? 2840 ASP A C     1 
ATOM   9488  O O     . ASP A 1 2840 ? 127.498 145.410 171.122 1.00 126.44 ? 2840 ASP A O     1 
ATOM   9489  C CB    . ASP A 1 2840 ? 129.046 143.210 169.438 1.00 126.44 ? 2840 ASP A CB    1 
ATOM   9490  C CG    . ASP A 1 2840 ? 129.611 142.251 170.469 1.00 126.44 ? 2840 ASP A CG    1 
ATOM   9491  O OD1   . ASP A 1 2840 ? 130.482 142.670 171.260 1.00 126.44 ? 2840 ASP A OD1   1 
ATOM   9492  O OD2   . ASP A 1 2840 ? 129.183 141.077 170.489 1.00 126.44 ? 2840 ASP A OD2   1 
ATOM   9493  N N     . GLU A 1 2841 ? 129.426 144.960 172.199 1.00 123.83 ? 2841 GLU A N     1 
ATOM   9494  C CA    . GLU A 1 2841 ? 128.862 145.333 173.490 1.00 123.83 ? 2841 GLU A CA    1 
ATOM   9495  C C     . GLU A 1 2841 ? 128.479 146.806 173.511 1.00 123.83 ? 2841 GLU A C     1 
ATOM   9496  O O     . GLU A 1 2841 ? 127.433 147.175 174.055 1.00 123.83 ? 2841 GLU A O     1 
ATOM   9497  C CB    . GLU A 1 2841 ? 129.846 144.996 174.614 1.00 123.83 ? 2841 GLU A CB    1 
ATOM   9498  C CG    . GLU A 1 2841 ? 131.131 145.810 174.626 1.00 123.83 ? 2841 GLU A CG    1 
ATOM   9499  C CD    . GLU A 1 2841 ? 131.016 147.063 175.470 1.00 123.83 ? 2841 GLU A CD    1 
ATOM   9500  O OE1   . GLU A 1 2841 ? 131.959 147.881 175.460 1.00 123.83 ? 2841 GLU A OE1   1 
ATOM   9501  O OE2   . GLU A 1 2841 ? 129.977 147.233 176.140 1.00 123.83 ? 2841 GLU A OE2   1 
ATOM   9502  N N     . GLU A 1 2842 ? 129.303 147.661 172.902 1.00 117.38 ? 2842 GLU A N     1 
ATOM   9503  C CA    . GLU A 1 2842 ? 128.962 149.076 172.832 1.00 117.38 ? 2842 GLU A CA    1 
ATOM   9504  C C     . GLU A 1 2842 ? 127.676 149.288 172.047 1.00 117.38 ? 2842 GLU A C     1 
ATOM   9505  O O     . GLU A 1 2842 ? 126.807 150.063 172.461 1.00 117.38 ? 2842 GLU A O     1 
ATOM   9506  C CB    . GLU A 1 2842 ? 130.108 149.865 172.199 1.00 117.38 ? 2842 GLU A CB    1 
ATOM   9507  C CG    . GLU A 1 2842 ? 131.455 149.695 172.881 1.00 117.38 ? 2842 GLU A CG    1 
ATOM   9508  C CD    . GLU A 1 2842 ? 132.618 149.800 171.911 1.00 117.38 ? 2842 GLU A CD    1 
ATOM   9509  O OE1   . GLU A 1 2842 ? 132.471 149.363 170.751 1.00 117.38 ? 2842 GLU A OE1   1 
ATOM   9510  O OE2   . GLU A 1 2842 ? 133.680 150.322 172.309 1.00 117.38 ? 2842 GLU A OE2   1 
ATOM   9511  N N     . ARG A 1 2843 ? 127.532 148.597 170.916 1.00 112.12 ? 2843 ARG A N     1 
ATOM   9512  C CA    . ARG A 1 2843 ? 126.340 148.770 170.094 1.00 112.12 ? 2843 ARG A CA    1 
ATOM   9513  C C     . ARG A 1 2843 ? 125.090 148.296 170.822 1.00 112.12 ? 2843 ARG A C     1 
ATOM   9514  O O     . ARG A 1 2843 ? 124.051 148.970 170.791 1.00 112.12 ? 2843 ARG A O     1 
ATOM   9515  C CB    . ARG A 1 2843 ? 126.507 148.026 168.772 1.00 112.12 ? 2843 ARG A CB    1 
ATOM   9516  C CG    . ARG A 1 2843 ? 127.764 148.400 168.017 1.00 112.12 ? 2843 ARG A CG    1 
ATOM   9517  C CD    . ARG A 1 2843 ? 127.679 147.972 166.567 1.00 112.12 ? 2843 ARG A CD    1 
ATOM   9518  N NE    . ARG A 1 2843 ? 128.953 148.135 165.880 1.00 112.12 ? 2843 ARG A NE    1 
ATOM   9519  C CZ    . ARG A 1 2843 ? 129.995 147.331 166.036 1.00 112.12 ? 2843 ARG A CZ    1 
ATOM   9520  N NH1   . ARG A 1 2843 ? 129.947 146.285 166.845 1.00 112.12 ? 2843 ARG A NH1   1 
ATOM   9521  N NH2   . ARG A 1 2843 ? 131.113 147.581 165.362 1.00 112.12 ? 2843 ARG A NH2   1 
ATOM   9522  N N     . ARG A 1 2844 ? 125.163 147.135 171.477 1.00 117.25 ? 2844 ARG A N     1 
ATOM   9523  C CA    . ARG A 1 2844 ? 123.987 146.633 172.181 1.00 117.25 ? 2844 ARG A CA    1 
ATOM   9524  C C     . ARG A 1 2844 ? 123.640 147.517 173.372 1.00 117.25 ? 2844 ARG A C     1 
ATOM   9525  O O     . ARG A 1 2844 ? 122.458 147.748 173.655 1.00 117.25 ? 2844 ARG A O     1 
ATOM   9526  C CB    . ARG A 1 2844 ? 124.200 145.179 172.608 1.00 117.25 ? 2844 ARG A CB    1 
ATOM   9527  C CG    . ARG A 1 2844 ? 125.281 144.957 173.647 1.00 117.25 ? 2844 ARG A CG    1 
ATOM   9528  C CD    . ARG A 1 2844 ? 124.872 143.897 174.656 1.00 117.25 ? 2844 ARG A CD    1 
ATOM   9529  N NE    . ARG A 1 2844 ? 123.644 144.257 175.354 1.00 117.25 ? 2844 ARG A NE    1 
ATOM   9530  C CZ    . ARG A 1 2844 ? 123.587 145.082 176.390 1.00 117.25 ? 2844 ARG A CZ    1 
ATOM   9531  N NH1   . ARG A 1 2844 ? 124.676 145.639 176.892 1.00 117.25 ? 2844 ARG A NH1   1 
ATOM   9532  N NH2   . ARG A 1 2844 ? 122.406 145.353 176.939 1.00 117.25 ? 2844 ARG A NH2   1 
ATOM   9533  N N     . TRP A 1 2845 ? 124.654 148.036 174.070 1.00 116.05 ? 2845 TRP A N     1 
ATOM   9534  C CA    . TRP A 1 2845 ? 124.404 148.983 175.148 1.00 116.05 ? 2845 TRP A CA    1 
ATOM   9535  C C     . TRP A 1 2845 ? 123.719 150.233 174.619 1.00 116.05 ? 2845 TRP A C     1 
ATOM   9536  O O     . TRP A 1 2845 ? 122.772 150.741 175.231 1.00 116.05 ? 2845 TRP A O     1 
ATOM   9537  C CB    . TRP A 1 2845 ? 125.723 149.335 175.834 1.00 116.05 ? 2845 TRP A CB    1 
ATOM   9538  C CG    . TRP A 1 2845 ? 125.605 150.294 176.970 1.00 116.05 ? 2845 TRP A CG    1 
ATOM   9539  C CD1   . TRP A 1 2845 ? 125.525 149.983 178.293 1.00 116.05 ? 2845 TRP A CD1   1 
ATOM   9540  C CD2   . TRP A 1 2845 ? 125.583 151.723 176.893 1.00 116.05 ? 2845 TRP A CD2   1 
ATOM   9541  N NE1   . TRP A 1 2845 ? 125.442 151.127 179.045 1.00 116.05 ? 2845 TRP A NE1   1 
ATOM   9542  C CE2   . TRP A 1 2845 ? 125.480 152.210 178.208 1.00 116.05 ? 2845 TRP A CE2   1 
ATOM   9543  C CE3   . TRP A 1 2845 ? 125.637 152.636 175.839 1.00 116.05 ? 2845 TRP A CE3   1 
ATOM   9544  C CZ2   . TRP A 1 2845 ? 125.420 153.568 178.498 1.00 116.05 ? 2845 TRP A CZ2   1 
ATOM   9545  C CZ3   . TRP A 1 2845 ? 125.582 153.984 176.128 1.00 116.05 ? 2845 TRP A CZ3   1 
ATOM   9546  C CH2   . TRP A 1 2845 ? 125.476 154.437 177.446 1.00 116.05 ? 2845 TRP A CH2   1 
ATOM   9547  N N     . THR A 1 2846 ? 124.181 150.734 173.472 1.00 117.93 ? 2846 THR A N     1 
ATOM   9548  C CA    . THR A 1 2846 ? 123.573 151.914 172.873 1.00 117.93 ? 2846 THR A CA    1 
ATOM   9549  C C     . THR A 1 2846 ? 122.113 151.659 172.529 1.00 117.93 ? 2846 THR A C     1 
ATOM   9550  O O     . THR A 1 2846 ? 121.239 152.475 172.840 1.00 117.93 ? 2846 THR A O     1 
ATOM   9551  C CB    . THR A 1 2846 ? 124.357 152.324 171.626 1.00 117.93 ? 2846 THR A CB    1 
ATOM   9552  O OG1   . THR A 1 2846 ? 125.625 152.865 172.015 1.00 117.93 ? 2846 THR A OG1   1 
ATOM   9553  C CG2   . THR A 1 2846 ? 123.594 153.362 170.830 1.00 117.93 ? 2846 THR A CG2   1 
ATOM   9554  N N     . ASP A 1 2847 ? 121.829 150.517 171.902 1.00 118.42 ? 2847 ASP A N     1 
ATOM   9555  C CA    . ASP A 1 2847 ? 120.451 150.218 171.526 1.00 118.42 ? 2847 ASP A CA    1 
ATOM   9556  C C     . ASP A 1 2847 ? 119.557 150.094 172.753 1.00 118.42 ? 2847 ASP A C     1 
ATOM   9557  O O     . ASP A 1 2847 ? 118.454 150.661 172.793 1.00 118.42 ? 2847 ASP A O     1 
ATOM   9558  C CB    . ASP A 1 2847 ? 120.404 148.938 170.692 1.00 118.42 ? 2847 ASP A CB    1 
ATOM   9559  C CG    . ASP A 1 2847 ? 121.156 149.068 169.386 1.00 118.42 ? 2847 ASP A CG    1 
ATOM   9560  O OD1   . ASP A 1 2847 ? 121.786 150.122 169.172 1.00 118.42 ? 2847 ASP A OD1   1 
ATOM   9561  O OD2   . ASP A 1 2847 ? 121.123 148.119 168.575 1.00 118.42 ? 2847 ASP A OD2   1 
ATOM   9562  N N     . GLU A 1 2848 ? 120.022 149.358 173.769 1.00 120.10 ? 2848 GLU A N     1 
ATOM   9563  C CA    . GLU A 1 2848 ? 119.217 149.161 174.968 1.00 120.10 ? 2848 GLU A CA    1 
ATOM   9564  C C     . GLU A 1 2848 ? 118.943 150.483 175.665 1.00 120.10 ? 2848 GLU A C     1 
ATOM   9565  O O     . GLU A 1 2848 ? 117.812 150.750 176.083 1.00 120.10 ? 2848 GLU A O     1 
ATOM   9566  C CB    . GLU A 1 2848 ? 119.917 148.189 175.917 1.00 120.10 ? 2848 GLU A CB    1 
ATOM   9567  C CG    . GLU A 1 2848 ? 119.373 148.205 177.338 1.00 120.10 ? 2848 GLU A CG    1 
ATOM   9568  C CD    . GLU A 1 2848 ? 120.147 149.137 178.251 1.00 120.10 ? 2848 GLU A CD    1 
ATOM   9569  O OE1   . GLU A 1 2848 ? 121.344 149.374 177.986 1.00 120.10 ? 2848 GLU A OE1   1 
ATOM   9570  O OE2   . GLU A 1 2848 ? 119.557 149.639 179.230 1.00 120.10 ? 2848 GLU A OE2   1 
ATOM   9571  N N     . ASN A 1 2849 ? 119.961 151.335 175.786 1.00 119.62 ? 2849 ASN A N     1 
ATOM   9572  C CA    . ASN A 1 2849 ? 119.740 152.636 176.402 1.00 119.62 ? 2849 ASN A CA    1 
ATOM   9573  C C     . ASN A 1 2849 ? 118.815 153.504 175.562 1.00 119.62 ? 2849 ASN A C     1 
ATOM   9574  O O     . ASN A 1 2849 ? 118.027 154.278 176.116 1.00 119.62 ? 2849 ASN A O     1 
ATOM   9575  C CB    . ASN A 1 2849 ? 121.076 153.333 176.637 1.00 119.62 ? 2849 ASN A CB    1 
ATOM   9576  C CG    . ASN A 1 2849 ? 121.790 152.806 177.859 1.00 119.62 ? 2849 ASN A CG    1 
ATOM   9577  O OD1   . ASN A 1 2849 ? 122.672 151.958 177.757 1.00 119.62 ? 2849 ASN A OD1   1 
ATOM   9578  N ND2   . ASN A 1 2849 ? 121.413 153.311 179.027 1.00 119.62 ? 2849 ASN A ND2   1 
ATOM   9579  N N     . ILE A 1 2850 ? 118.883 153.385 174.235 1.00 113.92 ? 2850 ILE A N     1 
ATOM   9580  C CA    . ILE A 1 2850 ? 118.017 154.189 173.380 1.00 113.92 ? 2850 ILE A CA    1 
ATOM   9581  C C     . ILE A 1 2850 ? 116.558 153.823 173.607 1.00 113.92 ? 2850 ILE A C     1 
ATOM   9582  O O     . ILE A 1 2850 ? 115.713 154.695 173.849 1.00 113.92 ? 2850 ILE A O     1 
ATOM   9583  C CB    . ILE A 1 2850 ? 118.421 154.032 171.905 1.00 113.92 ? 2850 ILE A CB    1 
ATOM   9584  C CG1   . ILE A 1 2850 ? 119.584 154.970 171.587 1.00 113.92 ? 2850 ILE A CG1   1 
ATOM   9585  C CG2   . ILE A 1 2850 ? 117.243 154.324 170.991 1.00 113.92 ? 2850 ILE A CG2   1 
ATOM   9586  C CD1   . ILE A 1 2850 ? 120.202 154.744 170.237 1.00 113.92 ? 2850 ILE A CD1   1 
ATOM   9587  N N     . ASP A 1 2851 ? 116.236 152.528 173.555 1.00 120.98 ? 2851 ASP A N     1 
ATOM   9588  C CA    . ASP A 1 2851 ? 114.836 152.179 173.781 1.00 120.98 ? 2851 ASP A CA    1 
ATOM   9589  C C     . ASP A 1 2851 ? 114.437 152.435 175.229 1.00 120.98 ? 2851 ASP A C     1 
ATOM   9590  O O     . ASP A 1 2851 ? 113.277 152.768 175.500 1.00 120.98 ? 2851 ASP A O     1 
ATOM   9591  C CB    . ASP A 1 2851 ? 114.524 150.731 173.380 1.00 120.98 ? 2851 ASP A CB    1 
ATOM   9592  C CG    . ASP A 1 2851 ? 115.611 149.757 173.756 1.00 120.98 ? 2851 ASP A CG    1 
ATOM   9593  O OD1   . ASP A 1 2851 ? 115.773 149.486 174.962 1.00 120.98 ? 2851 ASP A OD1   1 
ATOM   9594  O OD2   . ASP A 1 2851 ? 116.270 149.224 172.842 1.00 120.98 ? 2851 ASP A OD2   1 
ATOM   9595  N N     . THR A 1 2852 ? 115.388 152.331 176.163 1.00 118.60 ? 2852 THR A N     1 
ATOM   9596  C CA    . THR A 1 2852 ? 115.094 152.615 177.561 1.00 118.60 ? 2852 THR A CA    1 
ATOM   9597  C C     . THR A 1 2852 ? 114.667 154.065 177.753 1.00 118.60 ? 2852 THR A C     1 
ATOM   9598  O O     . THR A 1 2852 ? 113.633 154.342 178.368 1.00 118.60 ? 2852 THR A O     1 
ATOM   9599  C CB    . THR A 1 2852 ? 116.318 152.300 178.418 1.00 118.60 ? 2852 THR A CB    1 
ATOM   9600  O OG1   . THR A 1 2852 ? 116.657 150.916 178.274 1.00 118.60 ? 2852 THR A OG1   1 
ATOM   9601  C CG2   . THR A 1 2852 ? 116.034 152.598 179.876 1.00 118.60 ? 2852 THR A CG2   1 
ATOM   9602  N N     . VAL A 1 2853 ? 115.445 155.007 177.218 1.00 115.51 ? 2853 VAL A N     1 
ATOM   9603  C CA    . VAL A 1 2853 ? 115.075 156.412 177.368 1.00 115.51 ? 2853 VAL A CA    1 
ATOM   9604  C C     . VAL A 1 2853 ? 113.813 156.721 176.574 1.00 115.51 ? 2853 VAL A C     1 
ATOM   9605  O O     . VAL A 1 2853 ? 112.975 157.522 177.015 1.00 115.51 ? 2853 VAL A O     1 
ATOM   9606  C CB    . VAL A 1 2853 ? 116.243 157.337 176.975 1.00 115.51 ? 2853 VAL A CB    1 
ATOM   9607  C CG1   . VAL A 1 2853 ? 116.685 157.088 175.549 1.00 115.51 ? 2853 VAL A CG1   1 
ATOM   9608  C CG2   . VAL A 1 2853 ? 115.858 158.797 177.170 1.00 115.51 ? 2853 VAL A CG2   1 
ATOM   9609  N N     . ALA A 1 2854 ? 113.641 156.090 175.407 1.00 118.27 ? 2854 ALA A N     1 
ATOM   9610  C CA    . ALA A 1 2854 ? 112.442 156.331 174.612 1.00 118.27 ? 2854 ALA A CA    1 
ATOM   9611  C C     . ALA A 1 2854 ? 111.186 155.927 175.370 1.00 118.27 ? 2854 ALA A C     1 
ATOM   9612  O O     . ALA A 1 2854 ? 110.189 156.658 175.369 1.00 118.27 ? 2854 ALA A O     1 
ATOM   9613  C CB    . ALA A 1 2854 ? 112.534 155.579 173.286 1.00 118.27 ? 2854 ALA A CB    1 
ATOM   9614  N N     . LEU A 1 2855 ? 111.214 154.768 176.032 1.00 121.67 ? 2855 LEU A N     1 
ATOM   9615  C CA    . LEU A 1 2855 ? 110.066 154.371 176.839 1.00 121.67 ? 2855 LEU A CA    1 
ATOM   9616  C C     . LEU A 1 2855 ? 109.985 155.178 178.127 1.00 121.67 ? 2855 LEU A C     1 
ATOM   9617  O O     . LEU A 1 2855 ? 108.901 155.309 178.706 1.00 121.67 ? 2855 LEU A O     1 
ATOM   9618  C CB    . LEU A 1 2855 ? 110.122 152.873 177.145 1.00 121.67 ? 2855 LEU A CB    1 
ATOM   9619  C CG    . LEU A 1 2855 ? 111.127 152.367 178.183 1.00 121.67 ? 2855 LEU A CG    1 
ATOM   9620  C CD1   . LEU A 1 2855 ? 110.490 152.223 179.560 1.00 121.67 ? 2855 LEU A CD1   1 
ATOM   9621  C CD2   . LEU A 1 2855 ? 111.728 151.045 177.734 1.00 121.67 ? 2855 LEU A CD2   1 
ATOM   9622  N N     . LYS A 1 2856 ? 111.114 155.717 178.594 1.00 118.67 ? 2856 LYS A N     1 
ATOM   9623  C CA    . LYS A 1 2856 ? 111.103 156.511 179.817 1.00 118.67 ? 2856 LYS A CA    1 
ATOM   9624  C C     . LYS A 1 2856 ? 110.370 157.829 179.616 1.00 118.67 ? 2856 LYS A C     1 
ATOM   9625  O O     . LYS A 1 2856 ? 109.513 158.204 180.424 1.00 118.67 ? 2856 LYS A O     1 
ATOM   9626  C CB    . LYS A 1 2856 ? 112.533 156.761 180.295 1.00 118.67 ? 2856 LYS A CB    1 
ATOM   9627  C CG    . LYS A 1 2856 ? 112.629 157.764 181.432 1.00 118.67 ? 2856 LYS A CG    1 
ATOM   9628  C CD    . LYS A 1 2856 ? 114.035 157.823 182.004 1.00 118.67 ? 2856 LYS A CD    1 
ATOM   9629  C CE    . LYS A 1 2856 ? 114.502 156.449 182.456 1.00 118.67 ? 2856 LYS A CE    1 
ATOM   9630  N NZ    . LYS A 1 2856 ? 115.904 156.473 182.955 1.00 118.67 ? 2856 LYS A NZ    1 
ATOM   9631  N N     . HIS A 1 2857 ? 110.692 158.549 178.547 1.00 113.03 ? 2857 HIS A N     1 
ATOM   9632  C CA    . HIS A 1 2857 ? 110.064 159.840 178.309 1.00 113.03 ? 2857 HIS A CA    1 
ATOM   9633  C C     . HIS A 1 2857 ? 108.792 159.744 177.480 1.00 113.03 ? 2857 HIS A C     1 
ATOM   9634  O O     . HIS A 1 2857 ? 108.120 160.762 177.286 1.00 113.03 ? 2857 HIS A O     1 
ATOM   9635  C CB    . HIS A 1 2857 ? 111.054 160.794 177.641 1.00 113.03 ? 2857 HIS A CB    1 
ATOM   9636  C CG    . HIS A 1 2857 ? 112.108 161.304 178.571 1.00 113.03 ? 2857 HIS A CG    1 
ATOM   9637  N ND1   . HIS A 1 2857 ? 112.954 162.341 178.245 1.00 113.03 ? 2857 HIS A ND1   1 
ATOM   9638  C CD2   . HIS A 1 2857 ? 112.451 160.918 179.823 1.00 113.03 ? 2857 HIS A CD2   1 
ATOM   9639  C CE1   . HIS A 1 2857 ? 113.774 162.572 179.255 1.00 113.03 ? 2857 HIS A CE1   1 
ATOM   9640  N NE2   . HIS A 1 2857 ? 113.490 161.722 180.225 1.00 113.03 ? 2857 HIS A NE2   1 
ATOM   9641  N N     . PHE A 1 2858 ? 108.445 158.558 176.986 1.00 116.55 ? 2858 PHE A N     1 
ATOM   9642  C CA    . PHE A 1 2858 ? 107.188 158.339 176.269 1.00 116.55 ? 2858 PHE A CA    1 
ATOM   9643  C C     . PHE A 1 2858 ? 106.548 157.051 176.767 1.00 116.55 ? 2858 PHE A C     1 
ATOM   9644  O O     . PHE A 1 2858 ? 106.487 156.047 176.049 1.00 116.55 ? 2858 PHE A O     1 
ATOM   9645  C CB    . PHE A 1 2858 ? 107.426 158.293 174.760 1.00 116.55 ? 2858 PHE A CB    1 
ATOM   9646  C CG    . PHE A 1 2858 ? 108.048 159.537 174.214 1.00 116.55 ? 2858 PHE A CG    1 
ATOM   9647  C CD1   . PHE A 1 2858 ? 109.422 159.668 174.151 1.00 116.55 ? 2858 PHE A CD1   1 
ATOM   9648  C CD2   . PHE A 1 2858 ? 107.259 160.580 173.769 1.00 116.55 ? 2858 PHE A CD2   1 
ATOM   9649  C CE1   . PHE A 1 2858 ? 109.997 160.814 173.653 1.00 116.55 ? 2858 PHE A CE1   1 
ATOM   9650  C CE2   . PHE A 1 2858 ? 107.829 161.728 173.268 1.00 116.55 ? 2858 PHE A CE2   1 
ATOM   9651  C CZ    . PHE A 1 2858 ? 109.200 161.846 173.209 1.00 116.55 ? 2858 PHE A CZ    1 
ATOM   9652  N N     . PRO A 1 2859 ? 106.054 157.046 178.004 1.00 122.61 ? 2859 PRO A N     1 
ATOM   9653  C CA    . PRO A 1 2859 ? 105.479 155.812 178.554 1.00 122.61 ? 2859 PRO A CA    1 
ATOM   9654  C C     . PRO A 1 2859 ? 104.131 155.477 177.937 1.00 122.61 ? 2859 PRO A C     1 
ATOM   9655  O O     . PRO A 1 2859 ? 103.749 154.304 177.866 1.00 122.61 ? 2859 PRO A O     1 
ATOM   9656  C CB    . PRO A 1 2859 ? 105.352 156.115 180.055 1.00 122.61 ? 2859 PRO A CB    1 
ATOM   9657  C CG    . PRO A 1 2859 ? 106.011 157.457 180.268 1.00 122.61 ? 2859 PRO A CG    1 
ATOM   9658  C CD    . PRO A 1 2859 ? 105.968 158.159 178.958 1.00 122.61 ? 2859 PRO A CD    1 
ATOM   9659  N N     . ASN A 1 2860 ? 103.398 156.501 177.493 1.00 127.96 ? 2860 ASN A N     1 
ATOM   9660  C CA    . ASN A 1 2860 ? 102.088 156.259 176.897 1.00 127.96 ? 2860 ASN A CA    1 
ATOM   9661  C C     . ASN A 1 2860 ? 102.198 155.561 175.550 1.00 127.96 ? 2860 ASN A C     1 
ATOM   9662  O O     . ASN A 1 2860 ? 101.343 154.735 175.212 1.00 127.96 ? 2860 ASN A O     1 
ATOM   9663  C CB    . ASN A 1 2860 ? 101.321 157.572 176.752 1.00 127.96 ? 2860 ASN A CB    1 
ATOM   9664  C CG    . ASN A 1 2860 ? 100.595 157.962 178.023 1.00 127.96 ? 2860 ASN A CG    1 
ATOM   9665  O OD1   . ASN A 1 2860 ? 100.891 157.452 179.103 1.00 127.96 ? 2860 ASN A OD1   1 
ATOM   9666  N ND2   . ASN A 1 2860 ? 99.633  158.867 177.899 1.00 127.96 ? 2860 ASN A ND2   1 
ATOM   9667  N N     . ILE A 1 2861 ? 103.233 155.874 174.769 1.00 125.96 ? 2861 ILE A N     1 
ATOM   9668  C CA    . ILE A 1 2861 ? 103.412 155.201 173.491 1.00 125.96 ? 2861 ILE A CA    1 
ATOM   9669  C C     . ILE A 1 2861 ? 103.746 153.729 173.715 1.00 125.96 ? 2861 ILE A C     1 
ATOM   9670  O O     . ILE A 1 2861 ? 104.216 153.315 174.782 1.00 125.96 ? 2861 ILE A O     1 
ATOM   9671  C CB    . ILE A 1 2861 ? 104.496 155.897 172.655 1.00 125.96 ? 2861 ILE A CB    1 
ATOM   9672  C CG1   . ILE A 1 2861 ? 105.873 155.328 173.000 1.00 125.96 ? 2861 ILE A CG1   1 
ATOM   9673  C CG2   . ILE A 1 2861 ? 104.447 157.400 172.867 1.00 125.96 ? 2861 ILE A CG2   1 
ATOM   9674  C CD1   . ILE A 1 2861 ? 106.939 155.625 171.984 1.00 125.96 ? 2861 ILE A CD1   1 
ATOM   9675  N N     . ASP A 1 2862 ? 103.486 152.927 172.688 1.00 129.72 ? 2862 ASP A N     1 
ATOM   9676  C CA    . ASP A 1 2862 ? 103.739 151.498 172.751 1.00 129.72 ? 2862 ASP A CA    1 
ATOM   9677  C C     . ASP A 1 2862 ? 105.191 151.208 172.381 1.00 129.72 ? 2862 ASP A C     1 
ATOM   9678  O O     . ASP A 1 2862 ? 106.017 152.111 172.229 1.00 129.72 ? 2862 ASP A O     1 
ATOM   9679  C CB    . ASP A 1 2862 ? 102.778 150.751 171.830 1.00 129.72 ? 2862 ASP A CB    1 
ATOM   9680  C CG    . ASP A 1 2862 ? 102.651 151.405 170.468 1.00 129.72 ? 2862 ASP A CG    1 
ATOM   9681  O OD1   . ASP A 1 2862 ? 103.443 152.324 170.170 1.00 129.72 ? 2862 ASP A OD1   1 
ATOM   9682  O OD2   . ASP A 1 2862 ? 101.755 151.002 169.696 1.00 129.72 ? 2862 ASP A OD2   1 
ATOM   9683  N N     . ARG A 1 2863 ? 105.508 149.925 172.234 1.00 124.98 ? 2863 ARG A N     1 
ATOM   9684  C CA    . ARG A 1 2863 ? 106.830 149.503 171.799 1.00 124.98 ? 2863 ARG A CA    1 
ATOM   9685  C C     . ARG A 1 2863 ? 106.877 149.161 170.319 1.00 124.98 ? 2863 ARG A C     1 
ATOM   9686  O O     . ARG A 1 2863 ? 107.869 148.588 169.865 1.00 124.98 ? 2863 ARG A O     1 
ATOM   9687  C CB    . ARG A 1 2863 ? 107.303 148.303 172.623 1.00 124.98 ? 2863 ARG A CB    1 
ATOM   9688  C CG    . ARG A 1 2863 ? 107.328 148.556 174.117 1.00 124.98 ? 2863 ARG A CG    1 
ATOM   9689  C CD    . ARG A 1 2863 ? 108.600 149.280 174.549 1.00 124.98 ? 2863 ARG A CD    1 
ATOM   9690  N NE    . ARG A 1 2863 ? 108.593 150.699 174.206 1.00 124.98 ? 2863 ARG A NE    1 
ATOM   9691  C CZ    . ARG A 1 2863 ? 107.760 151.599 174.712 1.00 124.98 ? 2863 ARG A CZ    1 
ATOM   9692  N NH1   . ARG A 1 2863 ? 106.847 151.271 175.611 1.00 124.98 ? 2863 ARG A NH1   1 
ATOM   9693  N NH2   . ARG A 1 2863 ? 107.847 152.862 174.307 1.00 124.98 ? 2863 ARG A NH2   1 
ATOM   9694  N N     . GLU A 1 2864 ? 105.848 149.538 169.554 1.00 125.01 ? 2864 GLU A N     1 
ATOM   9695  C CA    . GLU A 1 2864 ? 105.770 149.150 168.148 1.00 125.01 ? 2864 GLU A CA    1 
ATOM   9696  C C     . GLU A 1 2864 ? 107.023 149.545 167.379 1.00 125.01 ? 2864 GLU A C     1 
ATOM   9697  O O     . GLU A 1 2864 ? 107.406 148.867 166.418 1.00 125.01 ? 2864 GLU A O     1 
ATOM   9698  C CB    . GLU A 1 2864 ? 104.537 149.789 167.510 1.00 125.01 ? 2864 GLU A CB    1 
ATOM   9699  C CG    . GLU A 1 2864 ? 104.346 149.461 166.044 1.00 125.01 ? 2864 GLU A CG    1 
ATOM   9700  C CD    . GLU A 1 2864 ? 103.643 150.571 165.293 1.00 125.01 ? 2864 GLU A CD    1 
ATOM   9701  O OE1   . GLU A 1 2864 ? 102.517 150.935 165.688 1.00 125.01 ? 2864 GLU A OE1   1 
ATOM   9702  O OE2   . GLU A 1 2864 ? 104.219 151.082 164.309 1.00 125.01 ? 2864 GLU A OE2   1 
ATOM   9703  N N     . LYS A 1 2865 ? 107.676 150.628 167.789 1.00 119.94 ? 2865 LYS A N     1 
ATOM   9704  C CA    . LYS A 1 2865 ? 108.937 151.049 167.199 1.00 119.94 ? 2865 LYS A CA    1 
ATOM   9705  C C     . LYS A 1 2865 ? 110.140 150.388 167.856 1.00 119.94 ? 2865 LYS A C     1 
ATOM   9706  O O     . LYS A 1 2865 ? 111.264 150.569 167.378 1.00 119.94 ? 2865 LYS A O     1 
ATOM   9707  C CB    . LYS A 1 2865 ? 109.081 152.570 167.299 1.00 119.94 ? 2865 LYS A CB    1 
ATOM   9708  C CG    . LYS A 1 2865 ? 107.971 153.364 166.624 1.00 119.94 ? 2865 LYS A CG    1 
ATOM   9709  C CD    . LYS A 1 2865 ? 106.759 153.512 167.532 1.00 119.94 ? 2865 LYS A CD    1 
ATOM   9710  C CE    . LYS A 1 2865 ? 106.951 154.610 168.556 1.00 119.94 ? 2865 LYS A CE    1 
ATOM   9711  N NZ    . LYS A 1 2865 ? 105.646 155.074 169.103 1.00 119.94 ? 2865 LYS A NZ    1 
ATOM   9712  N N     . ALA A 1 2866 ? 109.932 149.628 168.931 1.00 133.60 ? 2866 ALA A N     1 
ATOM   9713  C CA    . ALA A 1 2866 ? 111.033 149.064 169.702 1.00 133.60 ? 2866 ALA A CA    1 
ATOM   9714  C C     . ALA A 1 2866 ? 111.494 147.715 169.158 1.00 133.60 ? 2866 ALA A C     1 
ATOM   9715  O O     . ALA A 1 2866 ? 112.677 147.552 168.847 1.00 133.60 ? 2866 ALA A O     1 
ATOM   9716  C CB    . ALA A 1 2866 ? 110.636 148.935 171.177 1.00 133.60 ? 2866 ALA A CB    1 
ATOM   9717  N N     . MET A 1 2867 ? 110.586 146.738 169.025 1.00 137.68 ? 2867 MET A N     1 
ATOM   9718  C CA    . MET A 1 2867 ? 111.031 145.429 168.554 1.00 137.68 ? 2867 MET A CA    1 
ATOM   9719  C C     . MET A 1 2867 ? 111.493 145.470 167.105 1.00 137.68 ? 2867 MET A C     1 
ATOM   9720  O O     . MET A 1 2867 ? 112.100 144.501 166.636 1.00 137.68 ? 2867 MET A O     1 
ATOM   9721  C CB    . MET A 1 2867 ? 109.949 144.348 168.683 1.00 137.68 ? 2867 MET A CB    1 
ATOM   9722  C CG    . MET A 1 2867 ? 108.773 144.448 167.713 1.00 137.68 ? 2867 MET A CG    1 
ATOM   9723  S SD    . MET A 1 2867 ? 107.868 145.996 167.700 1.00 137.68 ? 2867 MET A SD    1 
ATOM   9724  C CE    . MET A 1 2867 ? 107.012 145.814 169.262 1.00 137.68 ? 2867 MET A CE    1 
ATOM   9725  N N     . SER A 1 2868 ? 111.213 146.555 166.387 1.00 124.09 ? 2868 SER A N     1 
ATOM   9726  C CA    . SER A 1 2868 ? 111.768 146.717 165.053 1.00 124.09 ? 2868 SER A CA    1 
ATOM   9727  C C     . SER A 1 2868 ? 113.280 146.811 165.179 1.00 124.09 ? 2868 SER A C     1 
ATOM   9728  O O     . SER A 1 2868 ? 113.809 147.819 165.655 1.00 124.09 ? 2868 SER A O     1 
ATOM   9729  C CB    . SER A 1 2868 ? 111.192 147.958 164.373 1.00 124.09 ? 2868 SER A CB    1 
ATOM   9730  O OG    . SER A 1 2868 ? 109.797 148.059 164.601 1.00 124.09 ? 2868 SER A OG    1 
ATOM   9731  N N     . ARG A 1 2869 ? 113.976 145.753 164.795 1.00 129.32 ? 2869 ARG A N     1 
ATOM   9732  C CA    . ARG A 1 2869 ? 115.420 145.696 164.968 1.00 129.32 ? 2869 ARG A CA    1 
ATOM   9733  C C     . ARG A 1 2869 ? 116.166 146.443 163.866 1.00 129.32 ? 2869 ARG A C     1 
ATOM   9734  O O     . ARG A 1 2869 ? 117.075 147.223 164.175 1.00 129.32 ? 2869 ARG A O     1 
ATOM   9735  C CB    . ARG A 1 2869 ? 115.886 144.240 165.049 1.00 129.32 ? 2869 ARG A CB    1 
ATOM   9736  C CG    . ARG A 1 2869 ? 115.247 143.452 166.184 1.00 129.32 ? 2869 ARG A CG    1 
ATOM   9737  C CD    . ARG A 1 2869 ? 115.950 143.706 167.513 1.00 129.32 ? 2869 ARG A CD    1 
ATOM   9738  N NE    . ARG A 1 2869 ? 115.597 144.996 168.093 1.00 129.32 ? 2869 ARG A NE    1 
ATOM   9739  C CZ    . ARG A 1 2869 ? 114.876 145.149 169.194 1.00 129.32 ? 2869 ARG A CZ    1 
ATOM   9740  N NH1   . ARG A 1 2869 ? 114.407 144.108 169.863 1.00 129.32 ? 2869 ARG A NH1   1 
ATOM   9741  N NH2   . ARG A 1 2869 ? 114.619 146.377 169.636 1.00 129.32 ? 2869 ARG A NH2   1 
ATOM   9742  N N     . PRO A 1 2870 ? 115.842 146.238 162.576 1.00 117.59 ? 2870 PRO A N     1 
ATOM   9743  C CA    . PRO A 1 2870 ? 116.586 146.953 161.532 1.00 117.59 ? 2870 PRO A CA    1 
ATOM   9744  C C     . PRO A 1 2870 ? 116.404 148.463 161.596 1.00 117.59 ? 2870 PRO A C     1 
ATOM   9745  O O     . PRO A 1 2870 ? 117.391 149.202 161.680 1.00 117.59 ? 2870 PRO A O     1 
ATOM   9746  C CB    . PRO A 1 2870 ? 116.013 146.372 160.234 1.00 117.59 ? 2870 PRO A CB    1 
ATOM   9747  C CG    . PRO A 1 2870 ? 115.465 145.055 160.623 1.00 117.59 ? 2870 PRO A CG    1 
ATOM   9748  C CD    . PRO A 1 2870 ? 114.894 145.280 161.979 1.00 117.59 ? 2870 PRO A CD    1 
ATOM   9749  N N     . ILE A 1 2871 ? 115.152 148.924 161.573 1.00 110.24 ? 2871 ILE A N     1 
ATOM   9750  C CA    . ILE A 1 2871 ? 114.834 150.348 161.507 1.00 110.24 ? 2871 ILE A CA    1 
ATOM   9751  C C     . ILE A 1 2871 ? 115.589 150.965 160.341 1.00 110.24 ? 2871 ILE A C     1 
ATOM   9752  O O     . ILE A 1 2871 ? 116.560 151.703 160.537 1.00 110.24 ? 2871 ILE A O     1 
ATOM   9753  C CB    . ILE A 1 2871 ? 115.166 151.076 162.821 1.00 110.24 ? 2871 ILE A CB    1 
ATOM   9754  C CG1   . ILE A 1 2871 ? 114.704 150.254 164.020 1.00 110.24 ? 2871 ILE A CG1   1 
ATOM   9755  C CG2   . ILE A 1 2871 ? 114.507 152.440 162.847 1.00 110.24 ? 2871 ILE A CG2   1 
ATOM   9756  C CD1   . ILE A 1 2871 ? 115.064 150.865 165.354 1.00 110.24 ? 2871 ILE A CD1   1 
ATOM   9757  N N     . LEU A 1 2872 ? 115.164 150.654 159.124 1.00 106.72 ? 2872 LEU A N     1 
ATOM   9758  C CA    . LEU A 1 2872 ? 115.855 151.090 157.922 1.00 106.72 ? 2872 LEU A CA    1 
ATOM   9759  C C     . LEU A 1 2872 ? 115.006 152.105 157.172 1.00 106.72 ? 2872 LEU A C     1 
ATOM   9760  O O     . LEU A 1 2872 ? 113.822 151.873 156.917 1.00 106.72 ? 2872 LEU A O     1 
ATOM   9761  C CB    . LEU A 1 2872 ? 116.173 149.899 157.017 1.00 106.72 ? 2872 LEU A CB    1 
ATOM   9762  C CG    . LEU A 1 2872 ? 116.930 148.753 157.689 1.00 106.72 ? 2872 LEU A CG    1 
ATOM   9763  C CD1   . LEU A 1 2872 ? 117.361 147.714 156.668 1.00 106.72 ? 2872 LEU A CD1   1 
ATOM   9764  C CD2   . LEU A 1 2872 ? 118.126 149.269 158.473 1.00 106.72 ? 2872 LEU A CD2   1 
ATOM   9765  N N     . TYR A 1 2873 ? 115.621 153.227 156.818 1.00 102.66 ? 2873 TYR A N     1 
ATOM   9766  C CA    . TYR A 1 2873 ? 114.947 154.302 156.111 1.00 102.66 ? 2873 TYR A CA    1 
ATOM   9767  C C     . TYR A 1 2873 ? 115.571 154.476 154.737 1.00 102.66 ? 2873 TYR A C     1 
ATOM   9768  O O     . TYR A 1 2873 ? 116.795 154.424 154.590 1.00 102.66 ? 2873 TYR A O     1 
ATOM   9769  C CB    . TYR A 1 2873 ? 115.037 155.616 156.886 1.00 102.66 ? 2873 TYR A CB    1 
ATOM   9770  C CG    . TYR A 1 2873 ? 114.018 155.757 157.990 1.00 102.66 ? 2873 TYR A CG    1 
ATOM   9771  C CD1   . TYR A 1 2873 ? 114.083 154.969 159.127 1.00 102.66 ? 2873 TYR A CD1   1 
ATOM   9772  C CD2   . TYR A 1 2873 ? 112.989 156.680 157.892 1.00 102.66 ? 2873 TYR A CD2   1 
ATOM   9773  C CE1   . TYR A 1 2873 ? 113.155 155.100 160.136 1.00 102.66 ? 2873 TYR A CE1   1 
ATOM   9774  C CE2   . TYR A 1 2873 ? 112.059 156.815 158.894 1.00 102.66 ? 2873 TYR A CE2   1 
ATOM   9775  C CZ    . TYR A 1 2873 ? 112.145 156.024 160.013 1.00 102.66 ? 2873 TYR A CZ    1 
ATOM   9776  O OH    . TYR A 1 2873 ? 111.214 156.160 161.012 1.00 102.66 ? 2873 TYR A OH    1 
ATOM   9777  N N     . SER A 1 2874 ? 114.725 154.685 153.733 1.00 106.28 ? 2874 SER A N     1 
ATOM   9778  C CA    . SER A 1 2874 ? 115.204 154.926 152.382 1.00 106.28 ? 2874 SER A CA    1 
ATOM   9779  C C     . SER A 1 2874 ? 114.163 155.726 151.621 1.00 106.28 ? 2874 SER A C     1 
ATOM   9780  O O     . SER A 1 2874 ? 113.010 155.848 152.041 1.00 106.28 ? 2874 SER A O     1 
ATOM   9781  C CB    . SER A 1 2874 ? 115.509 153.626 151.635 1.00 106.28 ? 2874 SER A CB    1 
ATOM   9782  O OG    . SER A 1 2874 ? 115.512 153.849 150.235 1.00 106.28 ? 2874 SER A OG    1 
ATOM   9783  N N     . ASN A 1 2875 ? 114.595 156.282 150.490 1.00 113.11 ? 2875 ASN A N     1 
ATOM   9784  C CA    . ASN A 1 2875 ? 113.716 157.051 149.623 1.00 113.11 ? 2875 ASN A CA    1 
ATOM   9785  C C     . ASN A 1 2875 ? 113.749 156.558 148.183 1.00 113.11 ? 2875 ASN A C     1 
ATOM   9786  O O     . ASN A 1 2875 ? 113.199 157.226 147.303 1.00 113.11 ? 2875 ASN A O     1 
ATOM   9787  C CB    . ASN A 1 2875 ? 114.083 158.537 149.667 1.00 113.11 ? 2875 ASN A CB    1 
ATOM   9788  C CG    . ASN A 1 2875 ? 115.317 158.850 148.852 1.00 113.11 ? 2875 ASN A CG    1 
ATOM   9789  O OD1   . ASN A 1 2875 ? 116.394 158.310 149.101 1.00 113.11 ? 2875 ASN A OD1   1 
ATOM   9790  N ND2   . ASN A 1 2875 ? 115.167 159.725 147.865 1.00 113.11 ? 2875 ASN A ND2   1 
ATOM   9791  N N     . TRP A 1 2876 ? 114.397 155.426 147.913 1.00 106.16 ? 2876 TRP A N     1 
ATOM   9792  C CA    . TRP A 1 2876 ? 114.425 154.907 146.550 1.00 106.16 ? 2876 TRP A CA    1 
ATOM   9793  C C     . TRP A 1 2876 ? 113.109 154.245 146.167 1.00 106.16 ? 2876 TRP A C     1 
ATOM   9794  O O     . TRP A 1 2876 ? 112.661 154.367 145.023 1.00 106.16 ? 2876 TRP A O     1 
ATOM   9795  C CB    . TRP A 1 2876 ? 115.583 153.925 146.382 1.00 106.16 ? 2876 TRP A CB    1 
ATOM   9796  C CG    . TRP A 1 2876 ? 116.888 154.443 146.891 1.00 106.16 ? 2876 TRP A CG    1 
ATOM   9797  C CD1   . TRP A 1 2876 ? 117.459 155.645 146.594 1.00 106.16 ? 2876 TRP A CD1   1 
ATOM   9798  C CD2   . TRP A 1 2876 ? 117.793 153.777 147.777 1.00 106.16 ? 2876 TRP A CD2   1 
ATOM   9799  N NE1   . TRP A 1 2876 ? 118.664 155.768 147.240 1.00 106.16 ? 2876 TRP A NE1   1 
ATOM   9800  C CE2   . TRP A 1 2876 ? 118.890 154.635 147.974 1.00 106.16 ? 2876 TRP A CE2   1 
ATOM   9801  C CE3   . TRP A 1 2876 ? 117.781 152.539 148.423 1.00 106.16 ? 2876 TRP A CE3   1 
ATOM   9802  C CZ2   . TRP A 1 2876 ? 119.963 154.295 148.789 1.00 106.16 ? 2876 TRP A CZ2   1 
ATOM   9803  C CZ3   . TRP A 1 2876 ? 118.847 152.205 149.233 1.00 106.16 ? 2876 TRP A CZ3   1 
ATOM   9804  C CH2   . TRP A 1 2876 ? 119.923 153.079 149.408 1.00 106.16 ? 2876 TRP A CH2   1 
ATOM   9805  N N     . LEU A 1 2877 ? 112.475 153.547 147.106 1.00 110.18 ? 2877 LEU A N     1 
ATOM   9806  C CA    . LEU A 1 2877 ? 111.290 152.770 146.769 1.00 110.18 ? 2877 LEU A CA    1 
ATOM   9807  C C     . LEU A 1 2877 ? 110.065 153.648 146.529 1.00 110.18 ? 2877 LEU A C     1 
ATOM   9808  O O     . LEU A 1 2877 ? 109.208 153.292 145.711 1.00 110.18 ? 2877 LEU A O     1 
ATOM   9809  C CB    . LEU A 1 2877 ? 111.020 151.743 147.866 1.00 110.18 ? 2877 LEU A CB    1 
ATOM   9810  C CG    . LEU A 1 2877 ? 112.236 150.862 148.166 1.00 110.18 ? 2877 LEU A CG    1 
ATOM   9811  C CD1   . LEU A 1 2877 ? 111.907 149.810 149.198 1.00 110.18 ? 2877 LEU A CD1   1 
ATOM   9812  C CD2   . LEU A 1 2877 ? 112.750 150.213 146.893 1.00 110.18 ? 2877 LEU A CD2   1 
ATOM   9813  N N     . SER A 1 2878 ? 109.957 154.778 147.223 1.00 112.08 ? 2878 SER A N     1 
ATOM   9814  C CA    . SER A 1 2878 ? 108.879 155.737 147.018 1.00 112.08 ? 2878 SER A CA    1 
ATOM   9815  C C     . SER A 1 2878 ? 109.468 157.125 146.747 1.00 112.08 ? 2878 SER A C     1 
ATOM   9816  O O     . SER A 1 2878 ? 110.670 157.292 146.521 1.00 112.08 ? 2878 SER A O     1 
ATOM   9817  C CB    . SER A 1 2878 ? 107.935 155.771 148.221 1.00 112.08 ? 2878 SER A CB    1 
ATOM   9818  O OG    . SER A 1 2878 ? 108.295 156.827 149.093 1.00 112.08 ? 2878 SER A OG    1 
ATOM   9819  N N     . LYS A 1 2879 ? 108.600 158.132 146.782 1.00 112.22 ? 2879 LYS A N     1 
ATOM   9820  C CA    . LYS A 1 2879 ? 109.004 159.516 146.577 1.00 112.22 ? 2879 LYS A CA    1 
ATOM   9821  C C     . LYS A 1 2879 ? 109.705 160.115 147.792 1.00 112.22 ? 2879 LYS A C     1 
ATOM   9822  O O     . LYS A 1 2879 ? 110.532 161.017 147.625 1.00 112.22 ? 2879 LYS A O     1 
ATOM   9823  C CB    . LYS A 1 2879 ? 107.774 160.349 146.193 1.00 112.22 ? 2879 LYS A CB    1 
ATOM   9824  C CG    . LYS A 1 2879 ? 107.954 161.862 146.215 1.00 112.22 ? 2879 LYS A CG    1 
ATOM   9825  C CD    . LYS A 1 2879 ? 107.187 162.479 147.375 1.00 112.22 ? 2879 LYS A CD    1 
ATOM   9826  C CE    . LYS A 1 2879 ? 107.340 163.991 147.406 1.00 112.22 ? 2879 LYS A CE    1 
ATOM   9827  N NZ    . LYS A 1 2879 ? 106.265 164.621 148.214 1.00 112.22 ? 2879 LYS A NZ    1 
ATOM   9828  N N     . ASP A 1 2880 ? 109.444 159.611 148.997 1.00 115.07 ? 2880 ASP A N     1 
ATOM   9829  C CA    . ASP A 1 2880 ? 109.966 160.245 150.200 1.00 115.07 ? 2880 ASP A CA    1 
ATOM   9830  C C     . ASP A 1 2880 ? 110.761 159.237 151.018 1.00 115.07 ? 2880 ASP A C     1 
ATOM   9831  O O     . ASP A 1 2880 ? 110.854 158.057 150.675 1.00 115.07 ? 2880 ASP A O     1 
ATOM   9832  C CB    . ASP A 1 2880 ? 108.841 160.849 151.044 1.00 115.07 ? 2880 ASP A CB    1 
ATOM   9833  C CG    . ASP A 1 2880 ? 107.676 159.904 151.215 1.00 115.07 ? 2880 ASP A CG    1 
ATOM   9834  O OD1   . ASP A 1 2880 ? 107.748 158.778 150.685 1.00 115.07 ? 2880 ASP A OD1   1 
ATOM   9835  O OD2   . ASP A 1 2880 ? 106.685 160.293 151.867 1.00 115.07 ? 2880 ASP A OD2   1 
ATOM   9836  N N     . TYR A 1 2881 ? 111.330 159.731 152.120 1.00 108.69 ? 2881 TYR A N     1 
ATOM   9837  C CA    . TYR A 1 2881 ? 112.191 158.953 153.012 1.00 108.69 ? 2881 TYR A CA    1 
ATOM   9838  C C     . TYR A 1 2881 ? 111.364 158.130 154.005 1.00 108.69 ? 2881 TYR A C     1 
ATOM   9839  O O     . TYR A 1 2881 ? 111.368 158.364 155.212 1.00 108.69 ? 2881 TYR A O     1 
ATOM   9840  C CB    . TYR A 1 2881 ? 113.146 159.893 153.739 1.00 108.69 ? 2881 TYR A CB    1 
ATOM   9841  C CG    . TYR A 1 2881 ? 114.452 159.276 154.187 1.00 108.69 ? 2881 TYR A CG    1 
ATOM   9842  C CD1   . TYR A 1 2881 ? 115.159 158.409 153.369 1.00 108.69 ? 2881 TYR A CD1   1 
ATOM   9843  C CD2   . TYR A 1 2881 ? 114.977 159.569 155.437 1.00 108.69 ? 2881 TYR A CD2   1 
ATOM   9844  C CE1   . TYR A 1 2881 ? 116.354 157.851 153.793 1.00 108.69 ? 2881 TYR A CE1   1 
ATOM   9845  C CE2   . TYR A 1 2881 ? 116.164 159.020 155.865 1.00 108.69 ? 2881 TYR A CE2   1 
ATOM   9846  C CZ    . TYR A 1 2881 ? 116.850 158.160 155.043 1.00 108.69 ? 2881 TYR A CZ    1 
ATOM   9847  O OH    . TYR A 1 2881 ? 118.037 157.608 155.469 1.00 108.69 ? 2881 TYR A OH    1 
ATOM   9848  N N     . ILE A 1 2882 ? 110.644 157.145 153.478 1.00 108.30 ? 2882 ILE A N     1 
ATOM   9849  C CA    . ILE A 1 2882 ? 109.822 156.285 154.327 1.00 108.30 ? 2882 ILE A CA    1 
ATOM   9850  C C     . ILE A 1 2882 ? 110.674 155.183 154.939 1.00 108.30 ? 2882 ILE A C     1 
ATOM   9851  O O     . ILE A 1 2882 ? 111.665 154.752 154.333 1.00 108.30 ? 2882 ILE A O     1 
ATOM   9852  C CB    . ILE A 1 2882 ? 108.659 155.652 153.555 1.00 108.30 ? 2882 ILE A CB    1 
ATOM   9853  C CG1   . ILE A 1 2882 ? 109.073 155.331 152.119 1.00 108.30 ? 2882 ILE A CG1   1 
ATOM   9854  C CG2   . ILE A 1 2882 ? 107.436 156.563 153.595 1.00 108.30 ? 2882 ILE A CG2   1 
ATOM   9855  C CD1   . ILE A 1 2882 ? 108.067 154.477 151.404 1.00 108.30 ? 2882 ILE A CD1   1 
ATOM   9856  N N     . PRO A 1 2883 ? 110.328 154.704 156.124 1.00 107.93 ? 2883 PRO A N     1 
ATOM   9857  C CA    . PRO A 1 2883 ? 111.025 153.542 156.687 1.00 107.93 ? 2883 PRO A CA    1 
ATOM   9858  C C     . PRO A 1 2883 ? 110.623 152.244 156.010 1.00 107.93 ? 2883 PRO A C     1 
ATOM   9859  O O     . PRO A 1 2883 ? 109.799 151.496 156.543 1.00 107.93 ? 2883 PRO A O     1 
ATOM   9860  C CB    . PRO A 1 2883 ? 110.584 153.547 158.155 1.00 107.93 ? 2883 PRO A CB    1 
ATOM   9861  C CG    . PRO A 1 2883 ? 109.303 154.300 158.154 1.00 107.93 ? 2883 PRO A CG    1 
ATOM   9862  C CD    . PRO A 1 2883 ? 109.445 155.348 157.108 1.00 107.93 ? 2883 PRO A CD    1 
ATOM   9863  N N     . VAL A 1 2884 ? 111.200 151.957 154.846 1.00 110.34 ? 2884 VAL A N     1 
ATOM   9864  C CA    . VAL A 1 2884 ? 110.833 150.773 154.077 1.00 110.34 ? 2884 VAL A CA    1 
ATOM   9865  C C     . VAL A 1 2884 ? 111.346 149.516 154.766 1.00 110.34 ? 2884 VAL A C     1 
ATOM   9866  O O     . VAL A 1 2884 ? 112.158 149.589 155.694 1.00 110.34 ? 2884 VAL A O     1 
ATOM   9867  C CB    . VAL A 1 2884 ? 111.365 150.868 152.640 1.00 110.34 ? 2884 VAL A CB    1 
ATOM   9868  C CG1   . VAL A 1 2884 ? 110.600 151.926 151.872 1.00 110.34 ? 2884 VAL A CG1   1 
ATOM   9869  C CG2   . VAL A 1 2884 ? 112.840 151.190 152.660 1.00 110.34 ? 2884 VAL A CG2   1 
ATOM   9870  N N     . ASP A 1 2885 ? 110.872 148.358 154.317 1.00 119.88 ? 2885 ASP A N     1 
ATOM   9871  C CA    . ASP A 1 2885 ? 111.196 147.078 154.928 1.00 119.88 ? 2885 ASP A CA    1 
ATOM   9872  C C     . ASP A 1 2885 ? 112.480 146.508 154.328 1.00 119.88 ? 2885 ASP A C     1 
ATOM   9873  O O     . ASP A 1 2885 ? 112.825 146.762 153.172 1.00 119.88 ? 2885 ASP A O     1 
ATOM   9874  C CB    . ASP A 1 2885 ? 110.020 146.109 154.762 1.00 119.88 ? 2885 ASP A CB    1 
ATOM   9875  C CG    . ASP A 1 2885 ? 110.390 144.665 155.041 1.00 119.88 ? 2885 ASP A CG    1 
ATOM   9876  O OD1   . ASP A 1 2885 ? 109.922 144.128 156.066 1.00 119.88 ? 2885 ASP A OD1   1 
ATOM   9877  O OD2   . ASP A 1 2885 ? 111.104 144.051 154.221 1.00 119.88 ? 2885 ASP A OD2   1 
ATOM   9878  N N     . GLN A 1 2886 ? 113.181 145.713 155.141 1.00 115.95 ? 2886 GLN A N     1 
ATOM   9879  C CA    . GLN A 1 2886 ? 114.544 145.306 154.811 1.00 115.95 ? 2886 GLN A CA    1 
ATOM   9880  C C     . GLN A 1 2886 ? 114.603 144.448 153.552 1.00 115.95 ? 2886 GLN A C     1 
ATOM   9881  O O     . GLN A 1 2886 ? 115.517 144.607 152.738 1.00 115.95 ? 2886 GLN A O     1 
ATOM   9882  C CB    . GLN A 1 2886 ? 115.161 144.558 155.991 1.00 115.95 ? 2886 GLN A CB    1 
ATOM   9883  C CG    . GLN A 1 2886 ? 116.540 143.984 155.713 1.00 115.95 ? 2886 GLN A CG    1 
ATOM   9884  C CD    . GLN A 1 2886 ? 117.141 143.309 156.929 1.00 115.95 ? 2886 GLN A CD    1 
ATOM   9885  O OE1   . GLN A 1 2886 ? 116.524 143.261 157.992 1.00 115.95 ? 2886 GLN A OE1   1 
ATOM   9886  N NE2   . GLN A 1 2886 ? 118.350 142.781 156.777 1.00 115.95 ? 2886 GLN A NE2   1 
ATOM   9887  N N     . GLU A 1 2887 ? 113.653 143.529 153.379 1.00 122.18 ? 2887 GLU A N     1 
ATOM   9888  C CA    . GLU A 1 2887 ? 113.786 142.512 152.335 1.00 122.18 ? 2887 GLU A CA    1 
ATOM   9889  C C     . GLU A 1 2887 ? 113.719 143.113 150.934 1.00 122.18 ? 2887 GLU A C     1 
ATOM   9890  O O     . GLU A 1 2887 ? 114.578 142.833 150.087 1.00 122.18 ? 2887 GLU A O     1 
ATOM   9891  C CB    . GLU A 1 2887 ? 112.712 141.438 152.515 1.00 122.18 ? 2887 GLU A CB    1 
ATOM   9892  C CG    . GLU A 1 2887 ? 112.904 140.516 153.726 1.00 122.18 ? 2887 GLU A CG    1 
ATOM   9893  C CD    . GLU A 1 2887 ? 112.550 141.153 155.060 1.00 122.18 ? 2887 GLU A CD    1 
ATOM   9894  O OE1   . GLU A 1 2887 ? 112.885 142.334 155.284 1.00 122.18 ? 2887 GLU A OE1   1 
ATOM   9895  O OE2   . GLU A 1 2887 ? 111.931 140.460 155.894 1.00 122.18 ? 2887 GLU A OE2   1 
ATOM   9896  N N     . GLU A 1 2888 ? 112.701 143.931 150.659 1.00 120.11 ? 2888 GLU A N     1 
ATOM   9897  C CA    . GLU A 1 2888 ? 112.550 144.439 149.300 1.00 120.11 ? 2888 GLU A CA    1 
ATOM   9898  C C     . GLU A 1 2888 ? 113.612 145.479 148.968 1.00 120.11 ? 2888 GLU A C     1 
ATOM   9899  O O     . GLU A 1 2888 ? 114.090 145.528 147.830 1.00 120.11 ? 2888 GLU A O     1 
ATOM   9900  C CB    . GLU A 1 2888 ? 111.142 145.001 149.086 1.00 120.11 ? 2888 GLU A CB    1 
ATOM   9901  C CG    . GLU A 1 2888 ? 110.866 146.341 149.734 1.00 120.11 ? 2888 GLU A CG    1 
ATOM   9902  C CD    . GLU A 1 2888 ? 110.548 146.222 151.207 1.00 120.11 ? 2888 GLU A CD    1 
ATOM   9903  O OE1   . GLU A 1 2888 ? 110.534 145.086 151.724 1.00 120.11 ? 2888 GLU A OE1   1 
ATOM   9904  O OE2   . GLU A 1 2888 ? 110.306 147.266 151.845 1.00 120.11 ? 2888 GLU A OE2   1 
ATOM   9905  N N     . LEU A 1 2889 ? 114.011 146.303 149.941 1.00 114.11 ? 2889 LEU A N     1 
ATOM   9906  C CA    . LEU A 1 2889 ? 115.119 147.218 149.696 1.00 114.11 ? 2889 LEU A CA    1 
ATOM   9907  C C     . LEU A 1 2889 ? 116.409 146.443 149.480 1.00 114.11 ? 2889 LEU A C     1 
ATOM   9908  O O     . LEU A 1 2889 ? 117.263 146.848 148.687 1.00 114.11 ? 2889 LEU A O     1 
ATOM   9909  C CB    . LEU A 1 2889 ? 115.258 148.218 150.849 1.00 114.11 ? 2889 LEU A CB    1 
ATOM   9910  C CG    . LEU A 1 2889 ? 115.853 147.824 152.205 1.00 114.11 ? 2889 LEU A CG    1 
ATOM   9911  C CD1   . LEU A 1 2889 ? 117.369 147.917 152.197 1.00 114.11 ? 2889 LEU A CD1   1 
ATOM   9912  C CD2   . LEU A 1 2889 ? 115.294 148.702 153.303 1.00 114.11 ? 2889 LEU A CD2   1 
ATOM   9913  N N     . ARG A 1 2890 ? 116.563 145.320 150.183 1.00 110.00 ? 2890 ARG A N     1 
ATOM   9914  C CA    . ARG A 1 2890 ? 117.716 144.455 149.974 1.00 110.00 ? 2890 ARG A CA    1 
ATOM   9915  C C     . ARG A 1 2890 ? 117.743 143.928 148.549 1.00 110.00 ? 2890 ARG A C     1 
ATOM   9916  O O     . ARG A 1 2890 ? 118.787 143.950 147.888 1.00 110.00 ? 2890 ARG A O     1 
ATOM   9917  C CB    . ARG A 1 2890 ? 117.674 143.303 150.979 1.00 110.00 ? 2890 ARG A CB    1 
ATOM   9918  C CG    . ARG A 1 2890 ? 118.588 142.138 150.660 1.00 110.00 ? 2890 ARG A CG    1 
ATOM   9919  C CD    . ARG A 1 2890 ? 118.392 141.024 151.672 1.00 110.00 ? 2890 ARG A CD    1 
ATOM   9920  N NE    . ARG A 1 2890 ? 118.983 141.341 152.966 1.00 110.00 ? 2890 ARG A NE    1 
ATOM   9921  C CZ    . ARG A 1 2890 ? 120.265 141.181 153.261 1.00 110.00 ? 2890 ARG A CZ    1 
ATOM   9922  N NH1   . ARG A 1 2890 ? 121.120 140.692 152.379 1.00 110.00 ? 2890 ARG A NH1   1 
ATOM   9923  N NH2   . ARG A 1 2890 ? 120.699 141.511 154.473 1.00 110.00 ? 2890 ARG A NH2   1 
ATOM   9924  N N     . ASP A 1 2891 ? 116.596 143.468 148.053 1.00 112.57 ? 2891 ASP A N     1 
ATOM   9925  C CA    . ASP A 1 2891 ? 116.529 142.998 146.674 1.00 112.57 ? 2891 ASP A CA    1 
ATOM   9926  C C     . ASP A 1 2891 ? 116.834 144.125 145.694 1.00 112.57 ? 2891 ASP A C     1 
ATOM   9927  O O     . ASP A 1 2891 ? 117.573 143.934 144.716 1.00 112.57 ? 2891 ASP A O     1 
ATOM   9928  C CB    . ASP A 1 2891 ? 115.152 142.401 146.393 1.00 112.57 ? 2891 ASP A CB    1 
ATOM   9929  C CG    . ASP A 1 2891 ? 115.229 141.116 145.600 1.00 112.57 ? 2891 ASP A CG    1 
ATOM   9930  O OD1   . ASP A 1 2891 ? 114.206 140.727 145.000 1.00 112.57 ? 2891 ASP A OD1   1 
ATOM   9931  O OD2   . ASP A 1 2891 ? 116.312 140.496 145.574 1.00 112.57 ? 2891 ASP A OD2   1 
ATOM   9932  N N     . TYR A 1 2892 ? 116.272 145.310 145.942 1.00 108.90 ? 2892 TYR A N     1 
ATOM   9933  C CA    . TYR A 1 2892 ? 116.482 146.430 145.033 1.00 108.90 ? 2892 TYR A CA    1 
ATOM   9934  C C     . TYR A 1 2892 ? 117.948 146.832 144.985 1.00 108.90 ? 2892 TYR A C     1 
ATOM   9935  O O     . TYR A 1 2892 ? 118.503 147.047 143.904 1.00 108.90 ? 2892 TYR A O     1 
ATOM   9936  C CB    . TYR A 1 2892 ? 115.619 147.619 145.450 1.00 108.90 ? 2892 TYR A CB    1 
ATOM   9937  C CG    . TYR A 1 2892 ? 116.019 148.906 144.774 1.00 108.90 ? 2892 TYR A CG    1 
ATOM   9938  C CD1   . TYR A 1 2892 ? 115.719 149.131 143.439 1.00 108.90 ? 2892 TYR A CD1   1 
ATOM   9939  C CD2   . TYR A 1 2892 ? 116.699 149.896 145.466 1.00 108.90 ? 2892 TYR A CD2   1 
ATOM   9940  C CE1   . TYR A 1 2892 ? 116.083 150.302 142.813 1.00 108.90 ? 2892 TYR A CE1   1 
ATOM   9941  C CE2   . TYR A 1 2892 ? 117.068 151.072 144.848 1.00 108.90 ? 2892 TYR A CE2   1 
ATOM   9942  C CZ    . TYR A 1 2892 ? 116.757 151.271 143.521 1.00 108.90 ? 2892 TYR A CZ    1 
ATOM   9943  O OH    . TYR A 1 2892 ? 117.122 152.440 142.897 1.00 108.90 ? 2892 TYR A OH    1 
ATOM   9944  N N     . VAL A 1 2893 ? 118.596 146.930 146.146 1.00 109.95 ? 2893 VAL A N     1 
ATOM   9945  C CA    . VAL A 1 2893 ? 120.001 147.313 146.159 1.00 109.95 ? 2893 VAL A CA    1 
ATOM   9946  C C     . VAL A 1 2893 ? 120.862 146.200 145.584 1.00 109.95 ? 2893 VAL A C     1 
ATOM   9947  O O     . VAL A 1 2893 ? 121.905 146.471 144.980 1.00 109.95 ? 2893 VAL A O     1 
ATOM   9948  C CB    . VAL A 1 2893 ? 120.448 147.714 147.579 1.00 109.95 ? 2893 VAL A CB    1 
ATOM   9949  C CG1   . VAL A 1 2893 ? 120.437 146.526 148.510 1.00 109.95 ? 2893 VAL A CG1   1 
ATOM   9950  C CG2   . VAL A 1 2893 ? 121.830 148.346 147.540 1.00 109.95 ? 2893 VAL A CG2   1 
ATOM   9951  N N     . LYS A 1 2894 ? 120.451 144.940 145.744 1.00 110.72 ? 2894 LYS A N     1 
ATOM   9952  C CA    . LYS A 1 2894 ? 121.183 143.849 145.111 1.00 110.72 ? 2894 LYS A CA    1 
ATOM   9953  C C     . LYS A 1 2894 ? 121.170 144.006 143.599 1.00 110.72 ? 2894 LYS A C     1 
ATOM   9954  O O     . LYS A 1 2894 ? 122.218 143.935 142.946 1.00 110.72 ? 2894 LYS A O     1 
ATOM   9955  C CB    . LYS A 1 2894 ? 120.581 142.506 145.524 1.00 110.72 ? 2894 LYS A CB    1 
ATOM   9956  C CG    . LYS A 1 2894 ? 121.050 141.322 144.688 1.00 110.72 ? 2894 LYS A CG    1 
ATOM   9957  C CD    . LYS A 1 2894 ? 122.566 141.181 144.710 1.00 110.72 ? 2894 LYS A CD    1 
ATOM   9958  C CE    . LYS A 1 2894 ? 122.990 139.723 144.727 1.00 110.72 ? 2894 LYS A CE    1 
ATOM   9959  N NZ    . LYS A 1 2894 ? 124.435 139.578 145.050 1.00 110.72 ? 2894 LYS A NZ    1 
ATOM   9960  N N     . ALA A 1 2895 ? 119.991 144.252 143.029 1.00 112.11 ? 2895 ALA A N     1 
ATOM   9961  C CA    . ALA A 1 2895 ? 119.912 144.477 141.589 1.00 112.11 ? 2895 ALA A CA    1 
ATOM   9962  C C     . ALA A 1 2895 ? 120.703 145.716 141.188 1.00 112.11 ? 2895 ALA A C     1 
ATOM   9963  O O     . ALA A 1 2895 ? 121.375 145.731 140.145 1.00 112.11 ? 2895 ALA A O     1 
ATOM   9964  C CB    . ALA A 1 2895 ? 118.453 144.604 141.156 1.00 112.11 ? 2895 ALA A CB    1 
ATOM   9965  N N     . ARG A 1 2896 ? 120.641 146.762 142.013 1.00 112.54 ? 2896 ARG A N     1 
ATOM   9966  C CA    . ARG A 1 2896 ? 121.344 147.998 141.699 1.00 112.54 ? 2896 ARG A CA    1 
ATOM   9967  C C     . ARG A 1 2896 ? 122.848 147.778 141.633 1.00 112.54 ? 2896 ARG A C     1 
ATOM   9968  O O     . ARG A 1 2896 ? 123.500 148.199 140.673 1.00 112.54 ? 2896 ARG A O     1 
ATOM   9969  C CB    . ARG A 1 2896 ? 120.999 149.070 142.732 1.00 112.54 ? 2896 ARG A CB    1 
ATOM   9970  C CG    . ARG A 1 2896 ? 119.625 149.694 142.551 1.00 112.54 ? 2896 ARG A CG    1 
ATOM   9971  C CD    . ARG A 1 2896 ? 119.306 149.900 141.083 1.00 112.54 ? 2896 ARG A CD    1 
ATOM   9972  N NE    . ARG A 1 2896 ? 120.211 150.857 140.459 1.00 112.54 ? 2896 ARG A NE    1 
ATOM   9973  C CZ    . ARG A 1 2896 ? 119.879 151.652 139.452 1.00 112.54 ? 2896 ARG A CZ    1 
ATOM   9974  N NH1   . ARG A 1 2896 ? 118.667 151.632 138.926 1.00 112.54 ? 2896 ARG A NH1   1 
ATOM   9975  N NH2   . ARG A 1 2896 ? 120.789 152.486 138.957 1.00 112.54 ? 2896 ARG A NH2   1 
ATOM   9976  N N     . LEU A 1 2897 ? 123.418 147.107 142.635 1.00 113.16 ? 2897 LEU A N     1 
ATOM   9977  C CA    . LEU A 1 2897 ? 124.857 146.874 142.612 1.00 113.16 ? 2897 LEU A CA    1 
ATOM   9978  C C     . LEU A 1 2897 ? 125.232 145.857 141.548 1.00 113.16 ? 2897 LEU A C     1 
ATOM   9979  O O     . LEU A 1 2897 ? 126.352 145.898 141.026 1.00 113.16 ? 2897 LEU A O     1 
ATOM   9980  C CB    . LEU A 1 2897 ? 125.368 146.435 143.986 1.00 113.16 ? 2897 LEU A CB    1 
ATOM   9981  C CG    . LEU A 1 2897 ? 124.816 145.234 144.757 1.00 113.16 ? 2897 LEU A CG    1 
ATOM   9982  C CD1   . LEU A 1 2897 ? 125.264 143.907 144.175 1.00 113.16 ? 2897 LEU A CD1   1 
ATOM   9983  C CD2   . LEU A 1 2897 ? 125.268 145.341 146.200 1.00 113.16 ? 2897 LEU A CD2   1 
ATOM   9984  N N     . LYS A 1 2898 ? 124.318 144.946 141.208 1.00 121.15 ? 2898 LYS A N     1 
ATOM   9985  C CA    . LYS A 1 2898 ? 124.565 144.062 140.078 1.00 121.15 ? 2898 LYS A CA    1 
ATOM   9986  C C     . LYS A 1 2898 ? 124.777 144.875 138.810 1.00 121.15 ? 2898 LYS A C     1 
ATOM   9987  O O     . LYS A 1 2898 ? 125.768 144.691 138.095 1.00 121.15 ? 2898 LYS A O     1 
ATOM   9988  C CB    . LYS A 1 2898 ? 123.404 143.083 139.908 1.00 121.15 ? 2898 LYS A CB    1 
ATOM   9989  C CG    . LYS A 1 2898 ? 123.738 141.892 139.026 1.00 121.15 ? 2898 LYS A CG    1 
ATOM   9990  C CD    . LYS A 1 2898 ? 123.175 142.060 137.624 1.00 121.15 ? 2898 LYS A CD    1 
ATOM   9991  C CE    . LYS A 1 2898 ? 123.142 140.738 136.879 1.00 121.15 ? 2898 LYS A CE    1 
ATOM   9992  N NZ    . LYS A 1 2898 ? 122.256 140.802 135.686 1.00 121.15 ? 2898 LYS A NZ    1 
ATOM   9993  N N     . VAL A 1 2899 ? 123.871 145.817 138.544 1.00 119.01 ? 2899 VAL A N     1 
ATOM   9994  C CA    . VAL A 1 2899 ? 124.038 146.697 137.390 1.00 119.01 ? 2899 VAL A CA    1 
ATOM   9995  C C     . VAL A 1 2899 ? 125.319 147.510 137.526 1.00 119.01 ? 2899 VAL A C     1 
ATOM   9996  O O     . VAL A 1 2899 ? 126.069 147.691 136.557 1.00 119.01 ? 2899 VAL A O     1 
ATOM   9997  C CB    . VAL A 1 2899 ? 122.807 147.606 137.229 1.00 119.01 ? 2899 VAL A CB    1 
ATOM   9998  C CG1   . VAL A 1 2899 ? 122.980 148.522 136.030 1.00 119.01 ? 2899 VAL A CG1   1 
ATOM   9999  C CG2   . VAL A 1 2899 ? 121.550 146.769 137.087 1.00 119.01 ? 2899 VAL A CG2   1 
ATOM   10000 N N     . PHE A 1 2900 ? 125.590 148.002 138.736 1.00 113.62 ? 2900 PHE A N     1 
ATOM   10001 C CA    . PHE A 1 2900 ? 126.742 148.866 138.968 1.00 113.62 ? 2900 PHE A CA    1 
ATOM   10002 C C     . PHE A 1 2900 ? 128.042 148.167 138.596 1.00 113.62 ? 2900 PHE A C     1 
ATOM   10003 O O     . PHE A 1 2900 ? 128.846 148.697 137.821 1.00 113.62 ? 2900 PHE A O     1 
ATOM   10004 C CB    . PHE A 1 2900 ? 126.759 149.304 140.434 1.00 113.62 ? 2900 PHE A CB    1 
ATOM   10005 C CG    . PHE A 1 2900 ? 127.971 150.100 140.819 1.00 113.62 ? 2900 PHE A CG    1 
ATOM   10006 C CD1   . PHE A 1 2900 ? 128.175 151.367 140.306 1.00 113.62 ? 2900 PHE A CD1   1 
ATOM   10007 C CD2   . PHE A 1 2900 ? 128.903 149.582 141.701 1.00 113.62 ? 2900 PHE A CD2   1 
ATOM   10008 C CE1   . PHE A 1 2900 ? 129.285 152.100 140.665 1.00 113.62 ? 2900 PHE A CE1   1 
ATOM   10009 C CE2   . PHE A 1 2900 ? 130.017 150.310 142.057 1.00 113.62 ? 2900 PHE A CE2   1 
ATOM   10010 C CZ    . PHE A 1 2900 ? 130.208 151.569 141.539 1.00 113.62 ? 2900 PHE A CZ    1 
ATOM   10011 N N     . TYR A 1 2901 ? 128.262 146.967 139.129 1.00 121.61 ? 2901 TYR A N     1 
ATOM   10012 C CA    . TYR A 1 2901 ? 129.479 146.240 138.800 1.00 121.61 ? 2901 TYR A CA    1 
ATOM   10013 C C     . TYR A 1 2901 ? 129.428 145.633 137.408 1.00 121.61 ? 2901 TYR A C     1 
ATOM   10014 O O     . TYR A 1 2901 ? 130.478 145.267 136.870 1.00 121.61 ? 2901 TYR A O     1 
ATOM   10015 C CB    . TYR A 1 2901 ? 129.765 145.162 139.853 1.00 121.61 ? 2901 TYR A CB    1 
ATOM   10016 C CG    . TYR A 1 2901 ? 129.204 143.783 139.569 1.00 121.61 ? 2901 TYR A CG    1 
ATOM   10017 C CD1   . TYR A 1 2901 ? 129.883 142.881 138.757 1.00 121.61 ? 2901 TYR A CD1   1 
ATOM   10018 C CD2   . TYR A 1 2901 ? 128.015 143.369 140.148 1.00 121.61 ? 2901 TYR A CD2   1 
ATOM   10019 C CE1   . TYR A 1 2901 ? 129.377 141.623 138.509 1.00 121.61 ? 2901 TYR A CE1   1 
ATOM   10020 C CE2   . TYR A 1 2901 ? 127.503 142.110 139.908 1.00 121.61 ? 2901 TYR A CE2   1 
ATOM   10021 C CZ    . TYR A 1 2901 ? 128.187 141.242 139.088 1.00 121.61 ? 2901 TYR A CZ    1 
ATOM   10022 O OH    . TYR A 1 2901 ? 127.678 139.987 138.846 1.00 121.61 ? 2901 TYR A OH    1 
ATOM   10023 N N     . GLU A 1 2902 ? 128.240 145.516 136.811 1.00 127.85 ? 2902 GLU A N     1 
ATOM   10024 C CA    . GLU A 1 2902 ? 128.171 145.082 135.423 1.00 127.85 ? 2902 GLU A CA    1 
ATOM   10025 C C     . GLU A 1 2902 ? 128.717 146.151 134.486 1.00 127.85 ? 2902 GLU A C     1 
ATOM   10026 O O     . GLU A 1 2902 ? 129.489 145.844 133.570 1.00 127.85 ? 2902 GLU A O     1 
ATOM   10027 C CB    . GLU A 1 2902 ? 126.730 144.731 135.056 1.00 127.85 ? 2902 GLU A CB    1 
ATOM   10028 C CG    . GLU A 1 2902 ? 126.471 144.653 133.562 1.00 127.85 ? 2902 GLU A CG    1 
ATOM   10029 C CD    . GLU A 1 2902 ? 125.867 145.929 133.012 1.00 127.85 ? 2902 GLU A CD    1 
ATOM   10030 O OE1   . GLU A 1 2902 ? 125.636 146.866 133.804 1.00 127.85 ? 2902 GLU A OE1   1 
ATOM   10031 O OE2   . GLU A 1 2902 ? 125.625 145.996 131.789 1.00 127.85 ? 2902 GLU A OE2   1 
ATOM   10032 N N     . GLU A 1 2903 ? 128.341 147.411 134.701 1.00 126.17 ? 2903 GLU A N     1 
ATOM   10033 C CA    . GLU A 1 2903 ? 128.748 148.473 133.788 1.00 126.17 ? 2903 GLU A CA    1 
ATOM   10034 C C     . GLU A 1 2903 ? 129.915 149.301 134.314 1.00 126.17 ? 2903 GLU A C     1 
ATOM   10035 O O     . GLU A 1 2903 ? 130.867 149.561 133.573 1.00 126.17 ? 2903 GLU A O     1 
ATOM   10036 C CB    . GLU A 1 2903 ? 127.558 149.386 133.466 1.00 126.17 ? 2903 GLU A CB    1 
ATOM   10037 C CG    . GLU A 1 2903 ? 126.896 150.027 134.667 1.00 126.17 ? 2903 GLU A CG    1 
ATOM   10038 C CD    . GLU A 1 2903 ? 125.448 150.368 134.406 1.00 126.17 ? 2903 GLU A CD    1 
ATOM   10039 O OE1   . GLU A 1 2903 ? 124.901 149.891 133.391 1.00 126.17 ? 2903 GLU A OE1   1 
ATOM   10040 O OE2   . GLU A 1 2903 ? 124.856 151.115 135.210 1.00 126.17 ? 2903 GLU A OE2   1 
ATOM   10041 N N     . GLU A 1 2904 ? 129.869 149.722 135.578 1.00 131.50 ? 2904 GLU A N     1 
ATOM   10042 C CA    . GLU A 1 2904 ? 130.890 150.634 136.084 1.00 131.50 ? 2904 GLU A CA    1 
ATOM   10043 C C     . GLU A 1 2904 ? 132.151 149.888 136.504 1.00 131.50 ? 2904 GLU A C     1 
ATOM   10044 O O     . GLU A 1 2904 ? 133.237 150.125 135.964 1.00 131.50 ? 2904 GLU A O     1 
ATOM   10045 C CB    . GLU A 1 2904 ? 130.338 151.448 137.254 1.00 131.50 ? 2904 GLU A CB    1 
ATOM   10046 C CG    . GLU A 1 2904 ? 131.386 152.305 137.931 1.00 131.50 ? 2904 GLU A CG    1 
ATOM   10047 C CD    . GLU A 1 2904 ? 132.150 153.163 136.947 1.00 131.50 ? 2904 GLU A CD    1 
ATOM   10048 O OE1   . GLU A 1 2904 ? 131.511 153.973 136.241 1.00 131.50 ? 2904 GLU A OE1   1 
ATOM   10049 O OE2   . GLU A 1 2904 ? 133.388 153.023 136.874 1.00 131.50 ? 2904 GLU A OE2   1 
ATOM   10050 N N     . LEU A 1 2905 ? 132.026 148.987 137.470 1.00 133.62 ? 2905 LEU A N     1 
ATOM   10051 C CA    . LEU A 1 2905 ? 133.186 148.293 137.996 1.00 133.62 ? 2905 LEU A CA    1 
ATOM   10052 C C     . LEU A 1 2905 ? 133.603 147.162 137.057 1.00 133.62 ? 2905 LEU A C     1 
ATOM   10053 O O     . LEU A 1 2905 ? 132.947 146.873 136.053 1.00 133.62 ? 2905 LEU A O     1 
ATOM   10054 C CB    . LEU A 1 2905 ? 132.891 147.755 139.395 1.00 133.62 ? 2905 LEU A CB    1 
ATOM   10055 C CG    . LEU A 1 2905 ? 134.055 147.776 140.386 1.00 133.62 ? 2905 LEU A CG    1 
ATOM   10056 C CD1   . LEU A 1 2905 ? 134.661 149.166 140.447 1.00 133.62 ? 2905 LEU A CD1   1 
ATOM   10057 C CD2   . LEU A 1 2905 ? 133.594 147.334 141.760 1.00 133.62 ? 2905 LEU A CD2   1 
ATOM   10058 N N     . ASP A 1 2906 ? 134.722 146.524 137.394 1.00 148.40 ? 2906 ASP A N     1 
ATOM   10059 C CA    . ASP A 1 2906 ? 135.247 145.404 136.623 1.00 148.40 ? 2906 ASP A CA    1 
ATOM   10060 C C     . ASP A 1 2906 ? 135.430 144.151 137.469 1.00 148.40 ? 2906 ASP A C     1 
ATOM   10061 O O     . ASP A 1 2906 ? 136.026 143.176 136.997 1.00 148.40 ? 2906 ASP A O     1 
ATOM   10062 C CB    . ASP A 1 2906 ? 136.575 145.792 135.971 1.00 148.40 ? 2906 ASP A CB    1 
ATOM   10063 C CG    . ASP A 1 2906 ? 137.480 146.552 136.916 1.00 148.40 ? 2906 ASP A CG    1 
ATOM   10064 O OD1   . ASP A 1 2906 ? 137.817 146.004 137.986 1.00 148.40 ? 2906 ASP A OD1   1 
ATOM   10065 O OD2   . ASP A 1 2906 ? 137.849 147.701 136.593 1.00 148.40 ? 2906 ASP A OD2   1 
ATOM   10066 N N     . VAL A 1 2907 ? 134.945 144.155 138.704 1.00 126.24 ? 2907 VAL A N     1 
ATOM   10067 C CA    . VAL A 1 2907 ? 135.064 143.008 139.598 1.00 126.24 ? 2907 VAL A CA    1 
ATOM   10068 C C     . VAL A 1 2907 ? 133.716 142.794 140.273 1.00 126.24 ? 2907 VAL A C     1 
ATOM   10069 O O     . VAL A 1 2907 ? 133.066 143.770 140.673 1.00 126.24 ? 2907 VAL A O     1 
ATOM   10070 C CB    . VAL A 1 2907 ? 136.190 143.223 140.622 1.00 126.24 ? 2907 VAL A CB    1 
ATOM   10071 C CG1   . VAL A 1 2907 ? 136.040 144.577 141.295 1.00 126.24 ? 2907 VAL A CG1   1 
ATOM   10072 C CG2   . VAL A 1 2907 ? 136.198 142.111 141.662 1.00 126.24 ? 2907 VAL A CG2   1 
ATOM   10073 N N     . PRO A 1 2908 ? 133.243 141.556 140.399 1.00 111.66 ? 2908 PRO A N     1 
ATOM   10074 C CA    . PRO A 1 2908 ? 131.958 141.332 141.065 1.00 111.66 ? 2908 PRO A CA    1 
ATOM   10075 C C     . PRO A 1 2908 ? 131.986 141.829 142.500 1.00 111.66 ? 2908 PRO A C     1 
ATOM   10076 O O     . PRO A 1 2908 ? 133.005 141.745 143.188 1.00 111.66 ? 2908 PRO A O     1 
ATOM   10077 C CB    . PRO A 1 2908 ? 131.785 139.811 140.998 1.00 111.66 ? 2908 PRO A CB    1 
ATOM   10078 C CG    . PRO A 1 2908 ? 132.607 139.392 139.840 1.00 111.66 ? 2908 PRO A CG    1 
ATOM   10079 C CD    . PRO A 1 2908 ? 133.785 140.318 139.816 1.00 111.66 ? 2908 PRO A CD    1 
ATOM   10080 N N     . LEU A 1 2909 ? 130.855 142.370 142.941 1.00 102.49 ? 2909 LEU A N     1 
ATOM   10081 C CA    . LEU A 1 2909 ? 130.670 142.795 144.320 1.00 102.49 ? 2909 LEU A CA    1 
ATOM   10082 C C     . LEU A 1 2909 ? 129.573 141.950 144.943 1.00 102.49 ? 2909 LEU A C     1 
ATOM   10083 O O     . LEU A 1 2909 ? 128.467 141.865 144.401 1.00 102.49 ? 2909 LEU A O     1 
ATOM   10084 C CB    . LEU A 1 2909 ? 130.310 144.276 144.408 1.00 102.49 ? 2909 LEU A CB    1 
ATOM   10085 C CG    . LEU A 1 2909 ? 131.365 145.248 143.903 1.00 102.49 ? 2909 LEU A CG    1 
ATOM   10086 C CD1   . LEU A 1 2909 ? 130.948 146.665 144.230 1.00 102.49 ? 2909 LEU A CD1   1 
ATOM   10087 C CD2   . LEU A 1 2909 ? 132.707 144.918 144.521 1.00 102.49 ? 2909 LEU A CD2   1 
ATOM   10088 N N     . VAL A 1 2910 ? 129.881 141.325 146.072 1.00 91.95  ? 2910 VAL A N     1 
ATOM   10089 C CA    . VAL A 1 2910 ? 128.876 140.597 146.830 1.00 91.95  ? 2910 VAL A CA    1 
ATOM   10090 C C     . VAL A 1 2910 ? 128.114 141.598 147.681 1.00 91.95  ? 2910 VAL A C     1 
ATOM   10091 O O     . VAL A 1 2910 ? 128.545 142.744 147.845 1.00 91.95  ? 2910 VAL A O     1 
ATOM   10092 C CB    . VAL A 1 2910 ? 129.518 139.506 147.700 1.00 91.95  ? 2910 VAL A CB    1 
ATOM   10093 C CG1   . VAL A 1 2910 ? 130.071 140.125 148.955 1.00 91.95  ? 2910 VAL A CG1   1 
ATOM   10094 C CG2   . VAL A 1 2910 ? 128.508 138.422 148.036 1.00 91.95  ? 2910 VAL A CG2   1 
ATOM   10095 N N     . LEU A 1 2911 ? 126.977 141.179 148.225 1.00 97.67  ? 2911 LEU A N     1 
ATOM   10096 C CA    . LEU A 1 2911 ? 126.195 141.996 149.148 1.00 97.67  ? 2911 LEU A CA    1 
ATOM   10097 C C     . LEU A 1 2911 ? 125.936 141.155 150.392 1.00 97.67  ? 2911 LEU A C     1 
ATOM   10098 O O     . LEU A 1 2911 ? 125.312 140.094 150.310 1.00 97.67  ? 2911 LEU A O     1 
ATOM   10099 C CB    . LEU A 1 2911 ? 124.898 142.474 148.497 1.00 97.67  ? 2911 LEU A CB    1 
ATOM   10100 C CG    . LEU A 1 2911 ? 123.769 143.127 149.306 1.00 97.67  ? 2911 LEU A CG    1 
ATOM   10101 C CD1   . LEU A 1 2911 ? 122.869 143.887 148.365 1.00 97.67  ? 2911 LEU A CD1   1 
ATOM   10102 C CD2   . LEU A 1 2911 ? 122.921 142.121 150.062 1.00 97.67  ? 2911 LEU A CD2   1 
ATOM   10103 N N     . PHE A 1 2912 ? 126.429 141.614 151.533 1.00 94.04  ? 2912 PHE A N     1 
ATOM   10104 C CA    . PHE A 1 2912 ? 126.065 141.045 152.818 1.00 94.04  ? 2912 PHE A CA    1 
ATOM   10105 C C     . PHE A 1 2912 ? 125.418 142.116 153.686 1.00 94.04  ? 2912 PHE A C     1 
ATOM   10106 O O     . PHE A 1 2912 ? 125.310 143.282 153.302 1.00 94.04  ? 2912 PHE A O     1 
ATOM   10107 C CB    . PHE A 1 2912 ? 127.279 140.430 153.522 1.00 94.04  ? 2912 PHE A CB    1 
ATOM   10108 C CG    . PHE A 1 2912 ? 128.550 141.205 153.346 1.00 94.04  ? 2912 PHE A CG    1 
ATOM   10109 C CD1   . PHE A 1 2912 ? 129.328 141.043 152.216 1.00 94.04  ? 2912 PHE A CD1   1 
ATOM   10110 C CD2   . PHE A 1 2912 ? 128.978 142.081 154.322 1.00 94.04  ? 2912 PHE A CD2   1 
ATOM   10111 C CE1   . PHE A 1 2912 ? 130.498 141.750 152.058 1.00 94.04  ? 2912 PHE A CE1   1 
ATOM   10112 C CE2   . PHE A 1 2912 ? 130.151 142.789 154.168 1.00 94.04  ? 2912 PHE A CE2   1 
ATOM   10113 C CZ    . PHE A 1 2912 ? 130.911 142.622 153.035 1.00 94.04  ? 2912 PHE A CZ    1 
ATOM   10114 N N     . ASN A 1 2913 ? 124.983 141.703 154.877 1.00 98.85  ? 2913 ASN A N     1 
ATOM   10115 C CA    . ASN A 1 2913 ? 124.230 142.607 155.739 1.00 98.85  ? 2913 ASN A CA    1 
ATOM   10116 C C     . ASN A 1 2913 ? 125.047 143.839 156.103 1.00 98.85  ? 2913 ASN A C     1 
ATOM   10117 O O     . ASN A 1 2913 ? 124.512 144.954 156.165 1.00 98.85  ? 2913 ASN A O     1 
ATOM   10118 C CB    . ASN A 1 2913 ? 123.780 141.869 156.997 1.00 98.85  ? 2913 ASN A CB    1 
ATOM   10119 C CG    . ASN A 1 2913 ? 123.355 140.448 156.711 1.00 98.85  ? 2913 ASN A CG    1 
ATOM   10120 O OD1   . ASN A 1 2913 ? 122.503 140.205 155.858 1.00 98.85  ? 2913 ASN A OD1   1 
ATOM   10121 N ND2   . ASN A 1 2913 ? 123.945 139.499 157.426 1.00 98.85  ? 2913 ASN A ND2   1 
ATOM   10122 N N     . GLU A 1 2914 ? 126.345 143.659 156.348 1.00 100.40 ? 2914 GLU A N     1 
ATOM   10123 C CA    . GLU A 1 2914 ? 127.191 144.802 156.665 1.00 100.40 ? 2914 GLU A CA    1 
ATOM   10124 C C     . GLU A 1 2914 ? 127.241 145.785 155.504 1.00 100.40 ? 2914 GLU A C     1 
ATOM   10125 O O     . GLU A 1 2914 ? 127.134 146.999 155.706 1.00 100.40 ? 2914 GLU A O     1 
ATOM   10126 C CB    . GLU A 1 2914 ? 128.594 144.329 157.043 1.00 100.40 ? 2914 GLU A CB    1 
ATOM   10127 C CG    . GLU A 1 2914 ? 128.613 143.124 157.969 1.00 100.40 ? 2914 GLU A CG    1 
ATOM   10128 C CD    . GLU A 1 2914 ? 127.636 143.259 159.121 1.00 100.40 ? 2914 GLU A CD    1 
ATOM   10129 O OE1   . GLU A 1 2914 ? 127.634 144.320 159.779 1.00 100.40 ? 2914 GLU A OE1   1 
ATOM   10130 O OE2   . GLU A 1 2914 ? 126.870 142.305 159.369 1.00 100.40 ? 2914 GLU A OE2   1 
ATOM   10131 N N     . VAL A 1 2915 ? 127.385 145.283 154.278 1.00 94.55  ? 2915 VAL A N     1 
ATOM   10132 C CA    . VAL A 1 2915 ? 127.364 146.174 153.123 1.00 94.55  ? 2915 VAL A CA    1 
ATOM   10133 C C     . VAL A 1 2915 ? 126.022 146.883 153.032 1.00 94.55  ? 2915 VAL A C     1 
ATOM   10134 O O     . VAL A 1 2915 ? 125.955 148.072 152.707 1.00 94.55  ? 2915 VAL A O     1 
ATOM   10135 C CB    . VAL A 1 2915 ? 127.695 145.399 151.835 1.00 94.55  ? 2915 VAL A CB    1 
ATOM   10136 C CG1   . VAL A 1 2915 ? 127.039 146.051 150.635 1.00 94.55  ? 2915 VAL A CG1   1 
ATOM   10137 C CG2   . VAL A 1 2915 ? 129.197 145.343 151.634 1.00 94.55  ? 2915 VAL A CG2   1 
ATOM   10138 N N     . LEU A 1 2916 ? 124.936 146.178 153.351 1.00 95.42  ? 2916 LEU A N     1 
ATOM   10139 C CA    . LEU A 1 2916 ? 123.611 146.785 153.271 1.00 95.42  ? 2916 LEU A CA    1 
ATOM   10140 C C     . LEU A 1 2916 ? 123.472 147.950 154.246 1.00 95.42  ? 2916 LEU A C     1 
ATOM   10141 O O     . LEU A 1 2916 ? 123.088 149.063 153.856 1.00 95.42  ? 2916 LEU A O     1 
ATOM   10142 C CB    . LEU A 1 2916 ? 122.541 145.729 153.537 1.00 95.42  ? 2916 LEU A CB    1 
ATOM   10143 C CG    . LEU A 1 2916 ? 121.109 146.245 153.461 1.00 95.42  ? 2916 LEU A CG    1 
ATOM   10144 C CD1   . LEU A 1 2916 ? 120.873 146.864 152.104 1.00 95.42  ? 2916 LEU A CD1   1 
ATOM   10145 C CD2   . LEU A 1 2916 ? 120.123 145.120 153.714 1.00 95.42  ? 2916 LEU A CD2   1 
ATOM   10146 N N     . ASP A 1 2917 ? 123.789 147.722 155.522 1.00 97.83  ? 2917 ASP A N     1 
ATOM   10147 C CA    . ASP A 1 2917 ? 123.612 148.795 156.494 1.00 97.83  ? 2917 ASP A CA    1 
ATOM   10148 C C     . ASP A 1 2917 ? 124.609 149.927 156.261 1.00 97.83  ? 2917 ASP A C     1 
ATOM   10149 O O     . ASP A 1 2917 ? 124.281 151.099 156.495 1.00 97.83  ? 2917 ASP A O     1 
ATOM   10150 C CB    . ASP A 1 2917 ? 123.699 148.242 157.919 1.00 97.83  ? 2917 ASP A CB    1 
ATOM   10151 C CG    . ASP A 1 2917 ? 124.963 147.452 158.173 1.00 97.83  ? 2917 ASP A CG    1 
ATOM   10152 O OD1   . ASP A 1 2917 ? 126.055 147.953 157.848 1.00 97.83  ? 2917 ASP A OD1   1 
ATOM   10153 O OD2   . ASP A 1 2917 ? 124.864 146.322 158.694 1.00 97.83  ? 2917 ASP A OD2   1 
ATOM   10154 N N     . HIS A 1 2918 ? 125.813 149.608 155.775 1.00 94.36  ? 2918 HIS A N     1 
ATOM   10155 C CA    . HIS A 1 2918 ? 126.755 150.657 155.400 1.00 94.36  ? 2918 HIS A CA    1 
ATOM   10156 C C     . HIS A 1 2918 ? 126.214 151.509 154.262 1.00 94.36  ? 2918 HIS A C     1 
ATOM   10157 O O     . HIS A 1 2918 ? 126.344 152.736 154.289 1.00 94.36  ? 2918 HIS A O     1 
ATOM   10158 C CB    . HIS A 1 2918 ? 128.094 150.048 155.000 1.00 94.36  ? 2918 HIS A CB    1 
ATOM   10159 C CG    . HIS A 1 2918 ? 129.004 149.778 156.152 1.00 94.36  ? 2918 HIS A CG    1 
ATOM   10160 N ND1   . HIS A 1 2918 ? 129.422 150.766 157.016 1.00 94.36  ? 2918 HIS A ND1   1 
ATOM   10161 C CD2   . HIS A 1 2918 ? 129.586 148.634 156.578 1.00 94.36  ? 2918 HIS A CD2   1 
ATOM   10162 C CE1   . HIS A 1 2918 ? 130.220 150.240 157.928 1.00 94.36  ? 2918 HIS A CE1   1 
ATOM   10163 N NE2   . HIS A 1 2918 ? 130.336 148.948 157.685 1.00 94.36  ? 2918 HIS A NE2   1 
ATOM   10164 N N     . VAL A 1 2919 ? 125.630 150.879 153.242 1.00 94.04  ? 2919 VAL A N     1 
ATOM   10165 C CA    . VAL A 1 2919 ? 125.043 151.641 152.147 1.00 94.04  ? 2919 VAL A CA    1 
ATOM   10166 C C     . VAL A 1 2919 ? 123.930 152.529 152.669 1.00 94.04  ? 2919 VAL A C     1 
ATOM   10167 O O     . VAL A 1 2919 ? 123.758 153.668 152.218 1.00 94.04  ? 2919 VAL A O     1 
ATOM   10168 C CB    . VAL A 1 2919 ? 124.541 150.700 151.038 1.00 94.04  ? 2919 VAL A CB    1 
ATOM   10169 C CG1   . VAL A 1 2919 ? 123.754 151.477 150.013 1.00 94.04  ? 2919 VAL A CG1   1 
ATOM   10170 C CG2   . VAL A 1 2919 ? 125.704 150.038 150.356 1.00 94.04  ? 2919 VAL A CG2   1 
ATOM   10171 N N     . LEU A 1 2920 ? 123.159 152.027 153.631 1.00 96.93  ? 2920 LEU A N     1 
ATOM   10172 C CA    . LEU A 1 2920 ? 122.105 152.847 154.216 1.00 96.93  ? 2920 LEU A CA    1 
ATOM   10173 C C     . LEU A 1 2920 ? 122.681 154.085 154.898 1.00 96.93  ? 2920 LEU A C     1 
ATOM   10174 O O     . LEU A 1 2920 ? 122.221 155.206 154.654 1.00 96.93  ? 2920 LEU A O     1 
ATOM   10175 C CB    . LEU A 1 2920 ? 121.279 152.008 155.188 1.00 96.93  ? 2920 LEU A CB    1 
ATOM   10176 C CG    . LEU A 1 2920 ? 120.352 151.050 154.441 1.00 96.93  ? 2920 LEU A CG    1 
ATOM   10177 C CD1   . LEU A 1 2920 ? 119.221 150.602 155.346 1.00 96.93  ? 2920 LEU A CD1   1 
ATOM   10178 C CD2   . LEU A 1 2920 ? 119.813 151.704 153.164 1.00 96.93  ? 2920 LEU A CD2   1 
ATOM   10179 N N     . ARG A 1 2921 ? 123.711 153.905 155.732 1.00 94.53  ? 2921 ARG A N     1 
ATOM   10180 C CA    . ARG A 1 2921 ? 124.349 155.060 156.368 1.00 94.53  ? 2921 ARG A CA    1 
ATOM   10181 C C     . ARG A 1 2921 ? 124.899 156.034 155.333 1.00 94.53  ? 2921 ARG A C     1 
ATOM   10182 O O     . ARG A 1 2921 ? 124.778 157.255 155.485 1.00 94.53  ? 2921 ARG A O     1 
ATOM   10183 C CB    . ARG A 1 2921 ? 125.473 154.618 157.303 1.00 94.53  ? 2921 ARG A CB    1 
ATOM   10184 C CG    . ARG A 1 2921 ? 125.076 153.623 158.361 1.00 94.53  ? 2921 ARG A CG    1 
ATOM   10185 C CD    . ARG A 1 2921 ? 126.252 152.757 158.777 1.00 94.53  ? 2921 ARG A CD    1 
ATOM   10186 N NE    . ARG A 1 2921 ? 125.880 151.725 159.742 1.00 94.53  ? 2921 ARG A NE    1 
ATOM   10187 C CZ    . ARG A 1 2921 ? 126.757 150.956 160.375 1.00 94.53  ? 2921 ARG A CZ    1 
ATOM   10188 N NH1   . ARG A 1 2921 ? 128.050 151.043 160.127 1.00 94.53  ? 2921 ARG A NH1   1 
ATOM   10189 N NH2   . ARG A 1 2921 ? 126.325 150.068 161.268 1.00 94.53  ? 2921 ARG A NH2   1 
ATOM   10190 N N     . ILE A 1 2922 ? 125.522 155.513 154.282 1.00 93.04  ? 2922 ILE A N     1 
ATOM   10191 C CA    . ILE A 1 2922 ? 126.184 156.371 153.307 1.00 93.04  ? 2922 ILE A CA    1 
ATOM   10192 C C     . ILE A 1 2922 ? 125.157 157.167 152.498 1.00 93.04  ? 2922 ILE A C     1 
ATOM   10193 O O     . ILE A 1 2922 ? 125.289 158.389 152.316 1.00 93.04  ? 2922 ILE A O     1 
ATOM   10194 C CB    . ILE A 1 2922 ? 127.088 155.492 152.428 1.00 93.04  ? 2922 ILE A CB    1 
ATOM   10195 C CG1   . ILE A 1 2922 ? 128.226 154.881 153.246 1.00 93.04  ? 2922 ILE A CG1   1 
ATOM   10196 C CG2   . ILE A 1 2922 ? 127.713 156.281 151.362 1.00 93.04  ? 2922 ILE A CG2   1 
ATOM   10197 C CD1   . ILE A 1 2922 ? 128.836 153.654 152.568 1.00 93.04  ? 2922 ILE A CD1   1 
ATOM   10198 N N     . ASP A 1 2923 ? 124.101 156.503 152.027 1.00 99.77  ? 2923 ASP A N     1 
ATOM   10199 C CA    . ASP A 1 2923 ? 123.036 157.230 151.350 1.00 99.77  ? 2923 ASP A CA    1 
ATOM   10200 C C     . ASP A 1 2923 ? 122.423 158.270 152.273 1.00 99.77  ? 2923 ASP A C     1 
ATOM   10201 O O     . ASP A 1 2923 ? 122.148 159.405 151.856 1.00 99.77  ? 2923 ASP A O     1 
ATOM   10202 C CB    . ASP A 1 2923 ? 121.957 156.273 150.853 1.00 99.77  ? 2923 ASP A CB    1 
ATOM   10203 C CG    . ASP A 1 2923 ? 120.652 156.985 150.576 1.00 99.77  ? 2923 ASP A CG    1 
ATOM   10204 O OD1   . ASP A 1 2923 ? 120.647 157.955 149.786 1.00 99.77  ? 2923 ASP A OD1   1 
ATOM   10205 O OD2   . ASP A 1 2923 ? 119.636 156.592 151.177 1.00 99.77  ? 2923 ASP A OD2   1 
ATOM   10206 N N     . ARG A 1 2924 ? 122.224 157.907 153.542 1.00 94.43  ? 2924 ARG A N     1 
ATOM   10207 C CA    . ARG A 1 2924 ? 121.727 158.863 154.516 1.00 94.43  ? 2924 ARG A CA    1 
ATOM   10208 C C     . ARG A 1 2924 ? 122.615 160.096 154.556 1.00 94.43  ? 2924 ARG A C     1 
ATOM   10209 O O     . ARG A 1 2924 ? 122.122 161.227 154.567 1.00 94.43  ? 2924 ARG A O     1 
ATOM   10210 C CB    . ARG A 1 2924 ? 121.671 158.214 155.897 1.00 94.43  ? 2924 ARG A CB    1 
ATOM   10211 C CG    . ARG A 1 2924 ? 120.646 158.842 156.823 1.00 94.43  ? 2924 ARG A CG    1 
ATOM   10212 C CD    . ARG A 1 2924 ? 121.124 160.168 157.386 1.00 94.43  ? 2924 ARG A CD    1 
ATOM   10213 N NE    . ARG A 1 2924 ? 122.230 160.064 158.327 1.00 94.43  ? 2924 ARG A NE    1 
ATOM   10214 C CZ    . ARG A 1 2924 ? 122.129 159.565 159.550 1.00 94.43  ? 2924 ARG A CZ    1 
ATOM   10215 N NH1   . ARG A 1 2924 ? 120.973 159.136 160.027 1.00 94.43  ? 2924 ARG A NH1   1 
ATOM   10216 N NH2   . ARG A 1 2924 ? 123.210 159.519 160.322 1.00 94.43  ? 2924 ARG A NH2   1 
ATOM   10217 N N     . ILE A 1 2925 ? 123.934 159.899 154.592 1.00 97.17  ? 2925 ILE A N     1 
ATOM   10218 C CA    . ILE A 1 2925 ? 124.796 161.044 154.860 1.00 97.17  ? 2925 ILE A CA    1 
ATOM   10219 C C     . ILE A 1 2925 ? 124.832 161.979 153.648 1.00 97.17  ? 2925 ILE A C     1 
ATOM   10220 O O     . ILE A 1 2925 ? 124.794 163.203 153.811 1.00 97.17  ? 2925 ILE A O     1 
ATOM   10221 C CB    . ILE A 1 2925 ? 126.206 160.604 155.300 1.00 97.17  ? 2925 ILE A CB    1 
ATOM   10222 C CG1   . ILE A 1 2925 ? 127.097 161.816 155.555 1.00 97.17  ? 2925 ILE A CG1   1 
ATOM   10223 C CG2   . ILE A 1 2925 ? 126.884 159.798 154.254 1.00 97.17  ? 2925 ILE A CG2   1 
ATOM   10224 C CD1   . ILE A 1 2925 ? 126.430 162.877 156.393 1.00 97.17  ? 2925 ILE A CD1   1 
ATOM   10225 N N     . PHE A 1 2926 ? 124.880 161.448 152.410 1.00 98.40  ? 2926 PHE A N     1 
ATOM   10226 C CA    . PHE A 1 2926 ? 124.690 162.416 151.315 1.00 98.40  ? 2926 PHE A CA    1 
ATOM   10227 C C     . PHE A 1 2926 ? 123.284 162.998 151.268 1.00 98.40  ? 2926 PHE A C     1 
ATOM   10228 O O     . PHE A 1 2926 ? 123.090 164.060 150.667 1.00 98.40  ? 2926 PHE A O     1 
ATOM   10229 C CB    . PHE A 1 2926 ? 125.047 161.930 149.898 1.00 98.40  ? 2926 PHE A CB    1 
ATOM   10230 C CG    . PHE A 1 2926 ? 126.288 161.116 149.787 1.00 98.40  ? 2926 PHE A CG    1 
ATOM   10231 C CD1   . PHE A 1 2926 ? 126.323 159.784 150.128 1.00 98.40  ? 2926 PHE A CD1   1 
ATOM   10232 C CD2   . PHE A 1 2926 ? 127.446 161.718 149.305 1.00 98.40  ? 2926 PHE A CD2   1 
ATOM   10233 C CE1   . PHE A 1 2926 ? 127.477 159.071 149.991 1.00 98.40  ? 2926 PHE A CE1   1 
ATOM   10234 C CE2   . PHE A 1 2926 ? 128.606 161.000 149.180 1.00 98.40  ? 2926 PHE A CE2   1 
ATOM   10235 C CZ    . PHE A 1 2926 ? 128.623 159.678 149.523 1.00 98.40  ? 2926 PHE A CZ    1 
ATOM   10236 N N     . ARG A 1 2927 ? 122.294 162.349 151.878 1.00 107.07 ? 2927 ARG A N     1 
ATOM   10237 C CA    . ARG A 1 2927 ? 120.964 162.942 151.812 1.00 107.07 ? 2927 ARG A CA    1 
ATOM   10238 C C     . ARG A 1 2927 ? 120.888 164.254 152.587 1.00 107.07 ? 2927 ARG A C     1 
ATOM   10239 O O     . ARG A 1 2927 ? 120.213 165.190 152.149 1.00 107.07 ? 2927 ARG A O     1 
ATOM   10240 C CB    . ARG A 1 2927 ? 119.913 161.958 152.317 1.00 107.07 ? 2927 ARG A CB    1 
ATOM   10241 C CG    . ARG A 1 2927 ? 118.492 162.465 152.142 1.00 107.07 ? 2927 ARG A CG    1 
ATOM   10242 C CD    . ARG A 1 2927 ? 117.535 161.347 151.769 1.00 107.07 ? 2927 ARG A CD    1 
ATOM   10243 N NE    . ARG A 1 2927 ? 118.170 160.385 150.878 1.00 107.07 ? 2927 ARG A NE    1 
ATOM   10244 C CZ    . ARG A 1 2927 ? 118.392 160.590 149.587 1.00 107.07 ? 2927 ARG A CZ    1 
ATOM   10245 N NH1   . ARG A 1 2927 ? 118.032 161.717 148.993 1.00 107.07 ? 2927 ARG A NH1   1 
ATOM   10246 N NH2   . ARG A 1 2927 ? 118.994 159.643 148.874 1.00 107.07 ? 2927 ARG A NH2   1 
ATOM   10247 N N     . GLN A 1 2928 ? 121.569 164.346 153.732 1.00 103.99 ? 2928 GLN A N     1 
ATOM   10248 C CA    . GLN A 1 2928 ? 121.457 165.515 154.594 1.00 103.99 ? 2928 GLN A CA    1 
ATOM   10249 C C     . GLN A 1 2928 ? 122.342 166.666 154.111 1.00 103.99 ? 2928 GLN A C     1 
ATOM   10250 O O     . GLN A 1 2928 ? 123.386 166.441 153.493 1.00 103.99 ? 2928 GLN A O     1 
ATOM   10251 C CB    . GLN A 1 2928 ? 121.838 165.150 156.021 1.00 103.99 ? 2928 GLN A CB    1 
ATOM   10252 C CG    . GLN A 1 2928 ? 120.852 164.220 156.689 1.00 103.99 ? 2928 GLN A CG    1 
ATOM   10253 C CD    . GLN A 1 2928 ? 121.183 163.993 158.141 1.00 103.99 ? 2928 GLN A CD    1 
ATOM   10254 O OE1   . GLN A 1 2928 ? 121.980 164.723 158.727 1.00 103.99 ? 2928 GLN A OE1   1 
ATOM   10255 N NE2   . GLN A 1 2928 ? 120.576 162.976 158.733 1.00 103.99 ? 2928 GLN A NE2   1 
ATOM   10256 N N     . PRO A 1 2929 ? 121.942 167.910 154.382 1.00 112.35 ? 2929 PRO A N     1 
ATOM   10257 C CA    . PRO A 1 2929 ? 122.796 169.052 154.037 1.00 112.35 ? 2929 PRO A CA    1 
ATOM   10258 C C     . PRO A 1 2929 ? 124.010 169.143 154.946 1.00 112.35 ? 2929 PRO A C     1 
ATOM   10259 O O     . PRO A 1 2929 ? 123.971 168.755 156.116 1.00 112.35 ? 2929 PRO A O     1 
ATOM   10260 C CB    . PRO A 1 2929 ? 121.874 170.263 154.229 1.00 112.35 ? 2929 PRO A CB    1 
ATOM   10261 C CG    . PRO A 1 2929 ? 120.490 169.703 154.327 1.00 112.35 ? 2929 PRO A CG    1 
ATOM   10262 C CD    . PRO A 1 2929 ? 120.640 168.341 154.911 1.00 112.35 ? 2929 PRO A CD    1 
ATOM   10263 N N     . GLN A 1 2930 ? 125.094 169.688 154.389 1.00 119.35 ? 2930 GLN A N     1 
ATOM   10264 C CA    . GLN A 1 2930 ? 126.377 169.802 155.087 1.00 119.35 ? 2930 GLN A CA    1 
ATOM   10265 C C     . GLN A 1 2930 ? 126.797 168.459 155.675 1.00 119.35 ? 2930 GLN A C     1 
ATOM   10266 O O     . GLN A 1 2930 ? 127.261 168.367 156.813 1.00 119.35 ? 2930 GLN A O     1 
ATOM   10267 C CB    . GLN A 1 2930 ? 126.339 170.884 156.168 1.00 119.35 ? 2930 GLN A CB    1 
ATOM   10268 C CG    . GLN A 1 2930 ? 127.705 171.511 156.441 1.00 119.35 ? 2930 GLN A CG    1 
ATOM   10269 C CD    . GLN A 1 2930 ? 127.620 172.829 157.184 1.00 119.35 ? 2930 GLN A CD    1 
ATOM   10270 O OE1   . GLN A 1 2930 ? 126.972 172.925 158.225 1.00 119.35 ? 2930 GLN A OE1   1 
ATOM   10271 N NE2   . GLN A 1 2930 ? 128.266 173.854 156.648 1.00 119.35 ? 2930 GLN A NE2   1 
ATOM   10272 N N     . GLY A 1 2931 ? 126.622 167.404 154.889 1.00 111.99 ? 2931 GLY A N     1 
ATOM   10273 C CA    . GLY A 1 2931 ? 126.933 166.071 155.353 1.00 111.99 ? 2931 GLY A CA    1 
ATOM   10274 C C     . GLY A 1 2931 ? 128.326 165.603 154.990 1.00 111.99 ? 2931 GLY A C     1 
ATOM   10275 O O     . GLY A 1 2931 ? 128.767 165.771 153.850 1.00 111.99 ? 2931 GLY A O     1 
ATOM   10276 N N     . HIS A 1 2932 ? 129.033 165.018 155.954 1.00 102.72 ? 2932 HIS A N     1 
ATOM   10277 C CA    . HIS A 1 2932 ? 130.377 164.511 155.724 1.00 102.72 ? 2932 HIS A CA    1 
ATOM   10278 C C     . HIS A 1 2932 ? 130.600 163.271 156.572 1.00 102.72 ? 2932 HIS A C     1 
ATOM   10279 O O     . HIS A 1 2932 ? 130.376 163.300 157.785 1.00 102.72 ? 2932 HIS A O     1 
ATOM   10280 C CB    . HIS A 1 2932 ? 131.427 165.575 156.049 1.00 102.72 ? 2932 HIS A CB    1 
ATOM   10281 C CG    . HIS A 1 2932 ? 131.172 166.889 155.383 1.00 102.72 ? 2932 HIS A CG    1 
ATOM   10282 N ND1   . HIS A 1 2932 ? 131.221 167.051 154.016 1.00 102.72 ? 2932 HIS A ND1   1 
ATOM   10283 C CD2   . HIS A 1 2932 ? 130.846 168.100 155.894 1.00 102.72 ? 2932 HIS A CD2   1 
ATOM   10284 C CE1   . HIS A 1 2932 ? 130.947 168.307 153.713 1.00 102.72 ? 2932 HIS A CE1   1 
ATOM   10285 N NE2   . HIS A 1 2932 ? 130.715 168.964 154.835 1.00 102.72 ? 2932 HIS A NE2   1 
ATOM   10286 N N     . LEU A 1 2933 ? 131.047 162.191 155.939 1.00 99.65  ? 2933 LEU A N     1 
ATOM   10287 C CA    . LEU A 1 2933 ? 131.253 160.915 156.608 1.00 99.65  ? 2933 LEU A CA    1 
ATOM   10288 C C     . LEU A 1 2933 ? 132.693 160.753 157.062 1.00 99.65  ? 2933 LEU A C     1 
ATOM   10289 O O     . LEU A 1 2933 ? 133.627 161.089 156.327 1.00 99.65  ? 2933 LEU A O     1 
ATOM   10290 C CB    . LEU A 1 2933 ? 130.890 159.740 155.704 1.00 99.65  ? 2933 LEU A CB    1 
ATOM   10291 C CG    . LEU A 1 2933 ? 130.019 158.674 156.365 1.00 99.65  ? 2933 LEU A CG    1 
ATOM   10292 C CD1   . LEU A 1 2933 ? 128.956 159.289 157.251 1.00 99.65  ? 2933 LEU A CD1   1 
ATOM   10293 C CD2   . LEU A 1 2933 ? 129.422 157.728 155.341 1.00 99.65  ? 2933 LEU A CD2   1 
ATOM   10294 N N     . LEU A 1 2934 ? 132.859 160.226 158.267 1.00 102.14 ? 2934 LEU A N     1 
ATOM   10295 C CA    . LEU A 1 2934 ? 134.122 159.670 158.725 1.00 102.14 ? 2934 LEU A CA    1 
ATOM   10296 C C     . LEU A 1 2934 ? 134.008 158.155 158.638 1.00 102.14 ? 2934 LEU A C     1 
ATOM   10297 O O     . LEU A 1 2934 ? 133.123 157.559 159.260 1.00 102.14 ? 2934 LEU A O     1 
ATOM   10298 C CB    . LEU A 1 2934 ? 134.426 160.113 160.154 1.00 102.14 ? 2934 LEU A CB    1 
ATOM   10299 C CG    . LEU A 1 2934 ? 135.784 159.747 160.744 1.00 102.14 ? 2934 LEU A CG    1 
ATOM   10300 C CD1   . LEU A 1 2934 ? 136.857 159.748 159.684 1.00 102.14 ? 2934 LEU A CD1   1 
ATOM   10301 C CD2   . LEU A 1 2934 ? 136.129 160.716 161.845 1.00 102.14 ? 2934 LEU A CD2   1 
ATOM   10302 N N     . LEU A 1 2935 ? 134.897 157.537 157.869 1.00 102.29 ? 2935 LEU A N     1 
ATOM   10303 C CA    . LEU A 1 2935 ? 134.792 156.120 157.539 1.00 102.29 ? 2935 LEU A CA    1 
ATOM   10304 C C     . LEU A 1 2935 ? 136.037 155.414 158.056 1.00 102.29 ? 2935 LEU A C     1 
ATOM   10305 O O     . LEU A 1 2935 ? 137.086 155.432 157.404 1.00 102.29 ? 2935 LEU A O     1 
ATOM   10306 C CB    . LEU A 1 2935 ? 134.624 155.939 156.033 1.00 102.29 ? 2935 LEU A CB    1 
ATOM   10307 C CG    . LEU A 1 2935 ? 133.196 155.616 155.591 1.00 102.29 ? 2935 LEU A CG    1 
ATOM   10308 C CD1   . LEU A 1 2935 ? 133.182 154.863 154.279 1.00 102.29 ? 2935 LEU A CD1   1 
ATOM   10309 C CD2   . LEU A 1 2935 ? 132.482 154.823 156.662 1.00 102.29 ? 2935 LEU A CD2   1 
ATOM   10310 N N     . ILE A 1 2936 ? 135.914 154.784 159.220 1.00 103.89 ? 2936 ILE A N     1 
ATOM   10311 C CA    . ILE A 1 2936 ? 137.042 154.202 159.936 1.00 103.89 ? 2936 ILE A CA    1 
ATOM   10312 C C     . ILE A 1 2936 ? 136.994 152.696 159.737 1.00 103.89 ? 2936 ILE A C     1 
ATOM   10313 O O     . ILE A 1 2936 ? 136.013 152.046 160.117 1.00 103.89 ? 2936 ILE A O     1 
ATOM   10314 C CB    . ILE A 1 2936 ? 136.996 154.544 161.430 1.00 103.89 ? 2936 ILE A CB    1 
ATOM   10315 C CG1   . ILE A 1 2936 ? 137.330 156.015 161.660 1.00 103.89 ? 2936 ILE A CG1   1 
ATOM   10316 C CG2   . ILE A 1 2936 ? 137.988 153.689 162.181 1.00 103.89 ? 2936 ILE A CG2   1 
ATOM   10317 C CD1   . ILE A 1 2936 ? 138.641 156.428 161.089 1.00 103.89 ? 2936 ILE A CD1   1 
ATOM   10318 N N     . GLY A 1 2937 ? 138.052 152.136 159.166 1.00 105.71 ? 2937 GLY A N     1 
ATOM   10319 C CA    . GLY A 1 2937 ? 138.105 150.699 158.973 1.00 105.71 ? 2937 GLY A CA    1 
ATOM   10320 C C     . GLY A 1 2937 ? 139.438 150.279 158.399 1.00 105.71 ? 2937 GLY A C     1 
ATOM   10321 O O     . GLY A 1 2937 ? 140.262 151.107 157.998 1.00 105.71 ? 2937 GLY A O     1 
ATOM   10322 N N     . VAL A 1 2938 ? 139.637 148.961 158.366 1.00 99.98  ? 2938 VAL A N     1 
ATOM   10323 C CA    . VAL A 1 2938 ? 140.872 148.408 157.833 1.00 99.98  ? 2938 VAL A CA    1 
ATOM   10324 C C     . VAL A 1 2938 ? 140.936 148.652 156.331 1.00 99.98  ? 2938 VAL A C     1 
ATOM   10325 O O     . VAL A 1 2938 ? 139.909 148.777 155.650 1.00 99.98  ? 2938 VAL A O     1 
ATOM   10326 C CB    . VAL A 1 2938 ? 140.973 146.908 158.164 1.00 99.98  ? 2938 VAL A CB    1 
ATOM   10327 C CG1   . VAL A 1 2938 ? 140.001 146.112 157.316 1.00 99.98  ? 2938 VAL A CG1   1 
ATOM   10328 C CG2   . VAL A 1 2938 ? 142.394 146.410 157.971 1.00 99.98  ? 2938 VAL A CG2   1 
ATOM   10329 N N     . SER A 1 2939 ? 142.156 148.738 155.808 1.00 100.95 ? 2939 SER A N     1 
ATOM   10330 C CA    . SER A 1 2939 ? 142.345 148.957 154.383 1.00 100.95 ? 2939 SER A CA    1 
ATOM   10331 C C     . SER A 1 2939 ? 141.801 147.779 153.586 1.00 100.95 ? 2939 SER A C     1 
ATOM   10332 O O     . SER A 1 2939 ? 141.852 146.627 154.023 1.00 100.95 ? 2939 SER A O     1 
ATOM   10333 C CB    . SER A 1 2939 ? 143.824 149.161 154.062 1.00 100.95 ? 2939 SER A CB    1 
ATOM   10334 O OG    . SER A 1 2939 ? 144.347 150.277 154.757 1.00 100.95 ? 2939 SER A OG    1 
ATOM   10335 N N     . GLY A 1 2940 ? 141.259 148.082 152.411 1.00 100.21 ? 2940 GLY A N     1 
ATOM   10336 C CA    . GLY A 1 2940 ? 140.724 147.061 151.540 1.00 100.21 ? 2940 GLY A CA    1 
ATOM   10337 C C     . GLY A 1 2940 ? 139.351 146.548 151.910 1.00 100.21 ? 2940 GLY A C     1 
ATOM   10338 O O     . GLY A 1 2940 ? 138.849 145.639 151.237 1.00 100.21 ? 2940 GLY A O     1 
ATOM   10339 N N     . ALA A 1 2941 ? 138.721 147.098 152.948 1.00 94.87  ? 2941 ALA A N     1 
ATOM   10340 C CA    . ALA A 1 2941 ? 137.391 146.653 153.343 1.00 94.87  ? 2941 ALA A CA    1 
ATOM   10341 C C     . ALA A 1 2941 ? 136.313 147.065 152.351 1.00 94.87  ? 2941 ALA A C     1 
ATOM   10342 O O     . ALA A 1 2941 ? 135.172 146.613 152.484 1.00 94.87  ? 2941 ALA A O     1 
ATOM   10343 C CB    . ALA A 1 2941 ? 137.045 147.191 154.730 1.00 94.87  ? 2941 ALA A CB    1 
ATOM   10344 N N     . GLY A 1 2942 ? 136.638 147.911 151.380 1.00 98.68  ? 2942 GLY A N     1 
ATOM   10345 C CA    . GLY A 1 2942 ? 135.697 148.309 150.357 1.00 98.68  ? 2942 GLY A CA    1 
ATOM   10346 C C     . GLY A 1 2942 ? 134.948 149.592 150.620 1.00 98.68  ? 2942 GLY A C     1 
ATOM   10347 O O     . GLY A 1 2942 ? 133.987 149.883 149.898 1.00 98.68  ? 2942 GLY A O     1 
ATOM   10348 N N     . LYS A 1 2943 ? 135.357 150.371 151.622 1.00 96.20  ? 2943 LYS A N     1 
ATOM   10349 C CA    . LYS A 1 2943 ? 134.625 151.585 151.964 1.00 96.20  ? 2943 LYS A CA    1 
ATOM   10350 C C     . LYS A 1 2943 ? 134.634 152.580 150.809 1.00 96.20  ? 2943 LYS A C     1 
ATOM   10351 O O     . LYS A 1 2943 ? 133.609 153.199 150.501 1.00 96.20  ? 2943 LYS A O     1 
ATOM   10352 C CB    . LYS A 1 2943 ? 135.210 152.198 153.234 1.00 96.20  ? 2943 LYS A CB    1 
ATOM   10353 C CG    . LYS A 1 2943 ? 136.721 152.114 153.331 1.00 96.20  ? 2943 LYS A CG    1 
ATOM   10354 C CD    . LYS A 1 2943 ? 137.164 152.064 154.784 1.00 96.20  ? 2943 LYS A CD    1 
ATOM   10355 C CE    . LYS A 1 2943 ? 138.644 152.370 154.938 1.00 96.20  ? 2943 LYS A CE    1 
ATOM   10356 N NZ    . LYS A 1 2943 ? 139.485 151.652 153.949 1.00 96.20  ? 2943 LYS A NZ    1 
ATOM   10357 N N     . THR A 1 2944 ? 135.781 152.738 150.145 1.00 96.41  ? 2944 THR A N     1 
ATOM   10358 C CA    . THR A 1 2944 ? 135.832 153.598 148.966 1.00 96.41  ? 2944 THR A CA    1 
ATOM   10359 C C     . THR A 1 2944 ? 134.930 153.069 147.860 1.00 96.41  ? 2944 THR A C     1 
ATOM   10360 O O     . THR A 1 2944 ? 134.185 153.834 147.234 1.00 96.41  ? 2944 THR A O     1 
ATOM   10361 C CB    . THR A 1 2944 ? 137.268 153.720 148.462 1.00 96.41  ? 2944 THR A CB    1 
ATOM   10362 O OG1   . THR A 1 2944 ? 138.072 154.363 149.457 1.00 96.41  ? 2944 THR A OG1   1 
ATOM   10363 C CG2   . THR A 1 2944 ? 137.316 154.528 147.182 1.00 96.41  ? 2944 THR A CG2   1 
ATOM   10364 N N     . THR A 1 2945 ? 134.981 151.761 147.607 1.00 97.44  ? 2945 THR A N     1 
ATOM   10365 C CA    . THR A 1 2945 ? 134.147 151.170 146.566 1.00 97.44  ? 2945 THR A CA    1 
ATOM   10366 C C     . THR A 1 2945 ? 132.670 151.327 146.891 1.00 97.44  ? 2945 THR A C     1 
ATOM   10367 O O     . THR A 1 2945 ? 131.863 151.676 146.022 1.00 97.44  ? 2945 THR A O     1 
ATOM   10368 C CB    . THR A 1 2945 ? 134.502 149.697 146.394 1.00 97.44  ? 2945 THR A CB    1 
ATOM   10369 O OG1   . THR A 1 2945 ? 135.832 149.587 145.873 1.00 97.44  ? 2945 THR A OG1   1 
ATOM   10370 C CG2   . THR A 1 2945 ? 133.529 149.025 145.450 1.00 97.44  ? 2945 THR A CG2   1 
ATOM   10371 N N     . LEU A 1 2946 ? 132.299 151.077 148.144 1.00 94.02  ? 2946 LEU A N     1 
ATOM   10372 C CA    . LEU A 1 2946 ? 130.902 151.212 148.534 1.00 94.02  ? 2946 LEU A CA    1 
ATOM   10373 C C     . LEU A 1 2946 ? 130.430 152.654 148.407 1.00 94.02  ? 2946 LEU A C     1 
ATOM   10374 O O     . LEU A 1 2946 ? 129.317 152.912 147.931 1.00 94.02  ? 2946 LEU A O     1 
ATOM   10375 C CB    . LEU A 1 2946 ? 130.716 150.712 149.960 1.00 94.02  ? 2946 LEU A CB    1 
ATOM   10376 C CG    . LEU A 1 2946 ? 129.357 150.089 150.236 1.00 94.02  ? 2946 LEU A CG    1 
ATOM   10377 C CD1   . LEU A 1 2946 ? 129.215 148.801 149.455 1.00 94.02  ? 2946 LEU A CD1   1 
ATOM   10378 C CD2   . LEU A 1 2946 ? 129.214 149.834 151.711 1.00 94.02  ? 2946 LEU A CD2   1 
ATOM   10379 N N     . SER A 1 2947 ? 131.262 153.607 148.826 1.00 92.85  ? 2947 SER A N     1 
ATOM   10380 C CA    . SER A 1 2947 ? 130.884 155.008 148.705 1.00 92.85  ? 2947 SER A CA    1 
ATOM   10381 C C     . SER A 1 2947 ? 130.733 155.410 147.246 1.00 92.85  ? 2947 SER A C     1 
ATOM   10382 O O     . SER A 1 2947 ? 129.811 156.153 146.895 1.00 92.85  ? 2947 SER A O     1 
ATOM   10383 C CB    . SER A 1 2947 ? 131.910 155.890 149.408 1.00 92.85  ? 2947 SER A CB    1 
ATOM   10384 O OG    . SER A 1 2947 ? 131.637 155.958 150.797 1.00 92.85  ? 2947 SER A OG    1 
ATOM   10385 N N     . ARG A 1 2948 ? 131.629 154.932 146.380 1.00 102.05 ? 2948 ARG A N     1 
ATOM   10386 C CA    . ARG A 1 2948 ? 131.501 155.241 144.960 1.00 102.05 ? 2948 ARG A CA    1 
ATOM   10387 C C     . ARG A 1 2948 ? 130.228 154.642 144.382 1.00 102.05 ? 2948 ARG A C     1 
ATOM   10388 O O     . ARG A 1 2948 ? 129.556 155.271 143.557 1.00 102.05 ? 2948 ARG A O     1 
ATOM   10389 C CB    . ARG A 1 2948 ? 132.724 154.746 144.193 1.00 102.05 ? 2948 ARG A CB    1 
ATOM   10390 C CG    . ARG A 1 2948 ? 133.957 155.591 144.412 1.00 102.05 ? 2948 ARG A CG    1 
ATOM   10391 C CD    . ARG A 1 2948 ? 135.080 155.146 143.510 1.00 102.05 ? 2948 ARG A CD    1 
ATOM   10392 N NE    . ARG A 1 2948 ? 134.570 154.641 142.243 1.00 102.05 ? 2948 ARG A NE    1 
ATOM   10393 C CZ    . ARG A 1 2948 ? 135.292 153.952 141.371 1.00 102.05 ? 2948 ARG A CZ    1 
ATOM   10394 N NH1   . ARG A 1 2948 ? 136.568 153.682 141.593 1.00 102.05 ? 2948 ARG A NH1   1 
ATOM   10395 N NH2   . ARG A 1 2948 ? 134.721 153.528 140.248 1.00 102.05 ? 2948 ARG A NH2   1 
ATOM   10396 N N     . PHE A 1 2949 ? 129.881 153.425 144.802 1.00 102.01 ? 2949 PHE A N     1 
ATOM   10397 C CA    . PHE A 1 2949 ? 128.629 152.823 144.358 1.00 102.01 ? 2949 PHE A CA    1 
ATOM   10398 C C     . PHE A 1 2949 ? 127.435 153.663 144.786 1.00 102.01 ? 2949 PHE A C     1 
ATOM   10399 O O     . PHE A 1 2949 ? 126.515 153.900 143.993 1.00 102.01 ? 2949 PHE A O     1 
ATOM   10400 C CB    . PHE A 1 2949 ? 128.504 151.406 144.911 1.00 102.01 ? 2949 PHE A CB    1 
ATOM   10401 C CG    . PHE A 1 2949 ? 127.090 150.919 145.013 1.00 102.01 ? 2949 PHE A CG    1 
ATOM   10402 C CD1   . PHE A 1 2949 ? 126.344 150.672 143.877 1.00 102.01 ? 2949 PHE A CD1   1 
ATOM   10403 C CD2   . PHE A 1 2949 ? 126.502 150.721 146.249 1.00 102.01 ? 2949 PHE A CD2   1 
ATOM   10404 C CE1   . PHE A 1 2949 ? 125.043 150.229 143.973 1.00 102.01 ? 2949 PHE A CE1   1 
ATOM   10405 C CE2   . PHE A 1 2949 ? 125.202 150.279 146.350 1.00 102.01 ? 2949 PHE A CE2   1 
ATOM   10406 C CZ    . PHE A 1 2949 ? 124.472 150.032 145.211 1.00 102.01 ? 2949 PHE A CZ    1 
ATOM   10407 N N     . VAL A 1 2950 ? 127.431 154.119 146.038 1.00 96.76  ? 2950 VAL A N     1 
ATOM   10408 C CA    . VAL A 1 2950 ? 126.312 154.922 146.523 1.00 96.76  ? 2950 VAL A CA    1 
ATOM   10409 C C     . VAL A 1 2950 ? 126.234 156.239 145.767 1.00 96.76  ? 2950 VAL A C     1 
ATOM   10410 O O     . VAL A 1 2950 ? 125.145 156.707 145.414 1.00 96.76  ? 2950 VAL A O     1 
ATOM   10411 C CB    . VAL A 1 2950 ? 126.429 155.143 148.040 1.00 96.76  ? 2950 VAL A CB    1 
ATOM   10412 C CG1   . VAL A 1 2950 ? 125.345 156.088 148.517 1.00 96.76  ? 2950 VAL A CG1   1 
ATOM   10413 C CG2   . VAL A 1 2950 ? 126.325 153.815 148.763 1.00 96.76  ? 2950 VAL A CG2   1 
ATOM   10414 N N     . ALA A 1 2951 ? 127.386 156.857 145.502 1.00 100.74 ? 2951 ALA A N     1 
ATOM   10415 C CA    . ALA A 1 2951 ? 127.396 158.107 144.750 1.00 100.74 ? 2951 ALA A CA    1 
ATOM   10416 C C     . ALA A 1 2951 ? 126.865 157.904 143.339 1.00 100.74 ? 2951 ALA A C     1 
ATOM   10417 O O     . ALA A 1 2951 ? 126.106 158.734 142.827 1.00 100.74 ? 2951 ALA A O     1 
ATOM   10418 C CB    . ALA A 1 2951 ? 128.808 158.686 144.714 1.00 100.74 ? 2951 ALA A CB    1 
ATOM   10419 N N     . TRP A 1 2952 ? 127.255 156.806 142.693 1.00 103.02 ? 2952 TRP A N     1 
ATOM   10420 C CA    . TRP A 1 2952 ? 126.760 156.526 141.351 1.00 103.02 ? 2952 TRP A CA    1 
ATOM   10421 C C     . TRP A 1 2952 ? 125.255 156.299 141.365 1.00 103.02 ? 2952 TRP A C     1 
ATOM   10422 O O     . TRP A 1 2952 ? 124.538 156.765 140.473 1.00 103.02 ? 2952 TRP A O     1 
ATOM   10423 C CB    . TRP A 1 2952 ? 127.477 155.309 140.770 1.00 103.02 ? 2952 TRP A CB    1 
ATOM   10424 C CG    . TRP A 1 2952 ? 126.778 154.713 139.594 1.00 103.02 ? 2952 TRP A CG    1 
ATOM   10425 C CD1   . TRP A 1 2952 ? 126.947 155.053 138.288 1.00 103.02 ? 2952 TRP A CD1   1 
ATOM   10426 C CD2   . TRP A 1 2952 ? 125.789 153.679 139.614 1.00 103.02 ? 2952 TRP A CD2   1 
ATOM   10427 N NE1   . TRP A 1 2952 ? 126.131 154.292 137.491 1.00 103.02 ? 2952 TRP A NE1   1 
ATOM   10428 C CE2   . TRP A 1 2952 ? 125.408 153.440 138.283 1.00 103.02 ? 2952 TRP A CE2   1 
ATOM   10429 C CE3   . TRP A 1 2952 ? 125.190 152.931 140.629 1.00 103.02 ? 2952 TRP A CE3   1 
ATOM   10430 C CZ2   . TRP A 1 2952 ? 124.457 152.488 137.940 1.00 103.02 ? 2952 TRP A CZ2   1 
ATOM   10431 C CZ3   . TRP A 1 2952 ? 124.245 151.985 140.286 1.00 103.02 ? 2952 TRP A CZ3   1 
ATOM   10432 C CH2   . TRP A 1 2952 ? 123.890 151.770 138.954 1.00 103.02 ? 2952 TRP A CH2   1 
ATOM   10433 N N     . MET A 1 2953 ? 124.758 155.580 142.371 1.00 100.39 ? 2953 MET A N     1 
ATOM   10434 C CA    . MET A 1 2953 ? 123.339 155.259 142.415 1.00 100.39 ? 2953 MET A CA    1 
ATOM   10435 C C     . MET A 1 2953 ? 122.484 156.435 142.864 1.00 100.39 ? 2953 MET A C     1 
ATOM   10436 O O     . MET A 1 2953 ? 121.276 156.436 142.606 1.00 100.39 ? 2953 MET A O     1 
ATOM   10437 C CB    . MET A 1 2953 ? 123.104 154.052 143.326 1.00 100.39 ? 2953 MET A CB    1 
ATOM   10438 C CG    . MET A 1 2953 ? 123.047 154.368 144.806 1.00 100.39 ? 2953 MET A CG    1 
ATOM   10439 S SD    . MET A 1 2953 ? 121.366 154.603 145.413 1.00 100.39 ? 2953 MET A SD    1 
ATOM   10440 C CE    . MET A 1 2953 ? 120.909 152.910 145.770 1.00 100.39 ? 2953 MET A CE    1 
ATOM   10441 N N     . ASN A 1 2954 ? 123.070 157.426 143.529 1.00 99.69  ? 2954 ASN A N     1 
ATOM   10442 C CA    . ASN A 1 2954 ? 122.334 158.613 143.941 1.00 99.69  ? 2954 ASN A CA    1 
ATOM   10443 C C     . ASN A 1 2954 ? 122.609 159.823 143.059 1.00 99.69  ? 2954 ASN A C     1 
ATOM   10444 O O     . ASN A 1 2954 ? 122.130 160.918 143.370 1.00 99.69  ? 2954 ASN A O     1 
ATOM   10445 C CB    . ASN A 1 2954 ? 122.650 158.952 145.397 1.00 99.69  ? 2954 ASN A CB    1 
ATOM   10446 C CG    . ASN A 1 2954 ? 121.571 158.487 146.345 1.00 99.69  ? 2954 ASN A CG    1 
ATOM   10447 O OD1   . ASN A 1 2954 ? 120.402 158.402 145.975 1.00 99.69  ? 2954 ASN A OD1   1 
ATOM   10448 N ND2   . ASN A 1 2954 ? 121.956 158.182 147.576 1.00 99.69  ? 2954 ASN A ND2   1 
ATOM   10449 N N     . GLY A 1 2955 ? 123.377 159.661 141.984 1.00 104.89 ? 2955 GLY A N     1 
ATOM   10450 C CA    . GLY A 1 2955 ? 123.549 160.702 140.997 1.00 104.89 ? 2955 GLY A CA    1 
ATOM   10451 C C     . GLY A 1 2955 ? 124.730 161.623 141.212 1.00 104.89 ? 2955 GLY A C     1 
ATOM   10452 O O     . GLY A 1 2955 ? 125.152 162.290 140.259 1.00 104.89 ? 2955 GLY A O     1 
ATOM   10453 N N     . LEU A 1 2956 ? 125.279 161.684 142.421 1.00 104.69 ? 2956 LEU A N     1 
ATOM   10454 C CA    . LEU A 1 2956 ? 126.402 162.574 142.677 1.00 104.69 ? 2956 LEU A CA    1 
ATOM   10455 C C     . LEU A 1 2956 ? 127.647 162.089 141.951 1.00 104.69 ? 2956 LEU A C     1 
ATOM   10456 O O     . LEU A 1 2956 ? 127.963 160.897 141.954 1.00 104.69 ? 2956 LEU A O     1 
ATOM   10457 C CB    . LEU A 1 2956 ? 126.684 162.671 144.176 1.00 104.69 ? 2956 LEU A CB    1 
ATOM   10458 C CG    . LEU A 1 2956 ? 125.512 162.876 145.137 1.00 104.69 ? 2956 LEU A CG    1 
ATOM   10459 C CD1   . LEU A 1 2956 ? 124.983 161.550 145.630 1.00 104.69 ? 2956 LEU A CD1   1 
ATOM   10460 C CD2   . LEU A 1 2956 ? 125.938 163.740 146.311 1.00 104.69 ? 2956 LEU A CD2   1 
ATOM   10461 N N     . SER A 1 2957 ? 128.359 163.020 141.327 1.00 103.56 ? 2957 SER A N     1 
ATOM   10462 C CA    . SER A 1 2957 ? 129.640 162.682 140.737 1.00 103.56 ? 2957 SER A CA    1 
ATOM   10463 C C     . SER A 1 2957 ? 130.675 162.460 141.834 1.00 103.56 ? 2957 SER A C     1 
ATOM   10464 O O     . SER A 1 2957 ? 130.540 162.944 142.960 1.00 103.56 ? 2957 SER A O     1 
ATOM   10465 C CB    . SER A 1 2957 ? 130.106 163.783 139.788 1.00 103.56 ? 2957 SER A CB    1 
ATOM   10466 O OG    . SER A 1 2957 ? 129.011 164.329 139.076 1.00 103.56 ? 2957 SER A OG    1 
ATOM   10467 N N     . VAL A 1 2958 ? 131.719 161.711 141.495 1.00 110.04 ? 2958 VAL A N     1 
ATOM   10468 C CA    . VAL A 1 2958 ? 132.798 161.397 142.423 1.00 110.04 ? 2958 VAL A CA    1 
ATOM   10469 C C     . VAL A 1 2958 ? 134.029 162.194 142.017 1.00 110.04 ? 2958 VAL A C     1 
ATOM   10470 O O     . VAL A 1 2958 ? 134.325 162.333 140.823 1.00 110.04 ? 2958 VAL A O     1 
ATOM   10471 C CB    . VAL A 1 2958 ? 133.089 159.886 142.467 1.00 110.04 ? 2958 VAL A CB    1 
ATOM   10472 C CG1   . VAL A 1 2958 ? 131.799 159.114 142.655 1.00 110.04 ? 2958 VAL A CG1   1 
ATOM   10473 C CG2   . VAL A 1 2958 ? 133.797 159.417 141.204 1.00 110.04 ? 2958 VAL A CG2   1 
ATOM   10474 N N     . TYR A 1 2959 ? 134.714 162.761 143.004 1.00 114.35 ? 2959 TYR A N     1 
ATOM   10475 C CA    . TYR A 1 2959 ? 135.960 163.476 142.779 1.00 114.35 ? 2959 TYR A CA    1 
ATOM   10476 C C     . TYR A 1 2959 ? 137.025 162.924 143.711 1.00 114.35 ? 2959 TYR A C     1 
ATOM   10477 O O     . TYR A 1 2959 ? 136.820 162.859 144.928 1.00 114.35 ? 2959 TYR A O     1 
ATOM   10478 C CB    . TYR A 1 2959 ? 135.798 164.980 142.997 1.00 114.35 ? 2959 TYR A CB    1 
ATOM   10479 C CG    . TYR A 1 2959 ? 136.995 165.769 142.524 1.00 114.35 ? 2959 TYR A CG    1 
ATOM   10480 C CD1   . TYR A 1 2959 ? 137.393 165.726 141.198 1.00 114.35 ? 2959 TYR A CD1   1 
ATOM   10481 C CD2   . TYR A 1 2959 ? 137.733 166.544 143.404 1.00 114.35 ? 2959 TYR A CD2   1 
ATOM   10482 C CE1   . TYR A 1 2959 ? 138.487 166.438 140.760 1.00 114.35 ? 2959 TYR A CE1   1 
ATOM   10483 C CE2   . TYR A 1 2959 ? 138.829 167.261 142.974 1.00 114.35 ? 2959 TYR A CE2   1 
ATOM   10484 C CZ    . TYR A 1 2959 ? 139.202 167.204 141.651 1.00 114.35 ? 2959 TYR A CZ    1 
ATOM   10485 O OH    . TYR A 1 2959 ? 140.294 167.916 141.215 1.00 114.35 ? 2959 TYR A OH    1 
ATOM   10486 N N     . GLN A 1 2960 ? 138.158 162.534 143.139 1.00 116.00 ? 2960 GLN A N     1 
ATOM   10487 C CA    . GLN A 1 2960 ? 139.271 161.975 143.889 1.00 116.00 ? 2960 GLN A CA    1 
ATOM   10488 C C     . GLN A 1 2960 ? 140.499 162.842 143.672 1.00 116.00 ? 2960 GLN A C     1 
ATOM   10489 O O     . GLN A 1 2960 ? 140.813 163.210 142.536 1.00 116.00 ? 2960 GLN A O     1 
ATOM   10490 C CB    . GLN A 1 2960 ? 139.560 160.537 143.458 1.00 116.00 ? 2960 GLN A CB    1 
ATOM   10491 C CG    . GLN A 1 2960 ? 138.364 159.611 143.542 1.00 116.00 ? 2960 GLN A CG    1 
ATOM   10492 C CD    . GLN A 1 2960 ? 138.703 158.291 144.198 1.00 116.00 ? 2960 GLN A CD    1 
ATOM   10493 O OE1   . GLN A 1 2960 ? 139.695 158.180 144.916 1.00 116.00 ? 2960 GLN A OE1   1 
ATOM   10494 N NE2   . GLN A 1 2960 ? 137.883 157.279 143.948 1.00 116.00 ? 2960 GLN A NE2   1 
ATOM   10495 N N     . ILE A 1 2961 ? 141.185 163.170 144.760 1.00 127.12 ? 2961 ILE A N     1 
ATOM   10496 C CA    . ILE A 1 2961 ? 142.441 163.904 144.676 1.00 127.12 ? 2961 ILE A CA    1 
ATOM   10497 C C     . ILE A 1 2961 ? 143.538 162.912 144.316 1.00 127.12 ? 2961 ILE A C     1 
ATOM   10498 O O     . ILE A 1 2961 ? 143.795 161.959 145.059 1.00 127.12 ? 2961 ILE A O     1 
ATOM   10499 C CB    . ILE A 1 2961 ? 142.748 164.623 145.995 1.00 127.12 ? 2961 ILE A CB    1 
ATOM   10500 C CG1   . ILE A 1 2961 ? 142.021 165.965 146.051 1.00 127.12 ? 2961 ILE A CG1   1 
ATOM   10501 C CG2   . ILE A 1 2961 ? 144.237 164.834 146.159 1.00 127.12 ? 2961 ILE A CG2   1 
ATOM   10502 C CD1   . ILE A 1 2961 ? 142.031 166.598 147.420 1.00 127.12 ? 2961 ILE A CD1   1 
ATOM   10503 N N     . LYS A 1 2962 ? 144.176 163.121 143.171 1.00 132.68 ? 2962 LYS A N     1 
ATOM   10504 C CA    . LYS A 1 2962 ? 145.224 162.226 142.689 1.00 132.68 ? 2962 LYS A CA    1 
ATOM   10505 C C     . LYS A 1 2962 ? 146.543 162.714 143.269 1.00 132.68 ? 2962 LYS A C     1 
ATOM   10506 O O     . LYS A 1 2962 ? 147.084 163.736 142.840 1.00 132.68 ? 2962 LYS A O     1 
ATOM   10507 C CB    . LYS A 1 2962 ? 145.250 162.181 141.166 1.00 132.68 ? 2962 LYS A CB    1 
ATOM   10508 C CG    . LYS A 1 2962 ? 143.876 162.043 140.524 1.00 132.68 ? 2962 LYS A CG    1 
ATOM   10509 C CD    . LYS A 1 2962 ? 143.075 160.892 141.123 1.00 132.68 ? 2962 LYS A CD    1 
ATOM   10510 C CE    . LYS A 1 2962 ? 143.759 159.550 140.918 1.00 132.68 ? 2962 LYS A CE    1 
ATOM   10511 N NZ    . LYS A 1 2962 ? 142.991 158.444 141.554 1.00 132.68 ? 2962 LYS A NZ    1 
ATOM   10512 N N     . VAL A 1 2963 ? 147.060 161.978 144.243 1.00 135.19 ? 2963 VAL A N     1 
ATOM   10513 C CA    . VAL A 1 2963 ? 148.231 162.390 145.006 1.00 135.19 ? 2963 VAL A CA    1 
ATOM   10514 C C     . VAL A 1 2963 ? 149.476 161.743 144.417 1.00 135.19 ? 2963 VAL A C     1 
ATOM   10515 O O     . VAL A 1 2963 ? 149.448 160.584 143.983 1.00 135.19 ? 2963 VAL A O     1 
ATOM   10516 C CB    . VAL A 1 2963 ? 148.066 162.038 146.498 1.00 135.19 ? 2963 VAL A CB    1 
ATOM   10517 C CG1   . VAL A 1 2963 ? 147.960 160.534 146.694 1.00 135.19 ? 2963 VAL A CG1   1 
ATOM   10518 C CG2   . VAL A 1 2963 ? 149.213 162.605 147.308 1.00 135.19 ? 2963 VAL A CG2   1 
ATOM   10519 N N     . HIS A 1 2964 ? 150.566 162.506 144.374 1.00 144.97 ? 2964 HIS A N     1 
ATOM   10520 C CA    . HIS A 1 2964 ? 151.871 161.994 143.990 1.00 144.97 ? 2964 HIS A CA    1 
ATOM   10521 C C     . HIS A 1 2964 ? 152.902 162.564 144.954 1.00 144.97 ? 2964 HIS A C     1 
ATOM   10522 O O     . HIS A 1 2964 ? 152.577 163.354 145.844 1.00 144.97 ? 2964 HIS A O     1 
ATOM   10523 C CB    . HIS A 1 2964 ? 152.207 162.341 142.534 1.00 144.97 ? 2964 HIS A CB    1 
ATOM   10524 C CG    . HIS A 1 2964 ? 151.895 163.756 142.158 1.00 144.97 ? 2964 HIS A CG    1 
ATOM   10525 N ND1   . HIS A 1 2964 ? 152.700 164.816 142.514 1.00 144.97 ? 2964 HIS A ND1   1 
ATOM   10526 C CD2   . HIS A 1 2964 ? 150.867 164.286 141.454 1.00 144.97 ? 2964 HIS A CD2   1 
ATOM   10527 C CE1   . HIS A 1 2964 ? 152.182 165.937 142.046 1.00 144.97 ? 2964 HIS A CE1   1 
ATOM   10528 N NE2   . HIS A 1 2964 ? 151.069 165.643 141.399 1.00 144.97 ? 2964 HIS A NE2   1 
ATOM   10529 N N     . ARG A 1 2965 ? 154.158 162.151 144.784 1.00 150.12 ? 2965 ARG A N     1 
ATOM   10530 C CA    . ARG A 1 2965 ? 155.211 162.653 145.660 1.00 150.12 ? 2965 ARG A CA    1 
ATOM   10531 C C     . ARG A 1 2965 ? 155.419 164.151 145.480 1.00 150.12 ? 2965 ARG A C     1 
ATOM   10532 O O     . ARG A 1 2965 ? 155.654 164.867 146.460 1.00 150.12 ? 2965 ARG A O     1 
ATOM   10533 C CB    . ARG A 1 2965 ? 156.514 161.898 145.405 1.00 150.12 ? 2965 ARG A CB    1 
ATOM   10534 C CG    . ARG A 1 2965 ? 157.667 162.347 146.284 1.00 150.12 ? 2965 ARG A CG    1 
ATOM   10535 C CD    . ARG A 1 2965 ? 157.295 162.261 147.756 1.00 150.12 ? 2965 ARG A CD    1 
ATOM   10536 N NE    . ARG A 1 2965 ? 156.811 160.936 148.124 1.00 150.12 ? 2965 ARG A NE    1 
ATOM   10537 C CZ    . ARG A 1 2965 ? 157.591 159.886 148.339 1.00 150.12 ? 2965 ARG A CZ    1 
ATOM   10538 N NH1   . ARG A 1 2965 ? 158.907 159.969 148.236 1.00 150.12 ? 2965 ARG A NH1   1 
ATOM   10539 N NH2   . ARG A 1 2965 ? 157.037 158.722 148.666 1.00 150.12 ? 2965 ARG A NH2   1 
ATOM   10540 N N     . LYS A 1 2966 ? 155.326 164.643 144.247 1.00 144.18 ? 2966 LYS A N     1 
ATOM   10541 C CA    . LYS A 1 2966 ? 155.517 166.057 143.951 1.00 144.18 ? 2966 LYS A CA    1 
ATOM   10542 C C     . LYS A 1 2966 ? 154.320 166.912 144.345 1.00 144.18 ? 2966 LYS A C     1 
ATOM   10543 O O     . LYS A 1 2966 ? 154.313 168.114 144.056 1.00 144.18 ? 2966 LYS A O     1 
ATOM   10544 C CB    . LYS A 1 2966 ? 155.818 166.248 142.461 1.00 144.18 ? 2966 LYS A CB    1 
ATOM   10545 C CG    . LYS A 1 2966 ? 156.920 165.352 141.911 1.00 144.18 ? 2966 LYS A CG    1 
ATOM   10546 C CD    . LYS A 1 2966 ? 158.121 165.288 142.844 1.00 144.18 ? 2966 LYS A CD    1 
ATOM   10547 C CE    . LYS A 1 2966 ? 159.057 164.155 142.455 1.00 144.18 ? 2966 LYS A CE    1 
ATOM   10548 N NZ    . LYS A 1 2966 ? 158.650 162.859 143.064 1.00 144.18 ? 2966 LYS A NZ    1 
ATOM   10549 N N     . TYR A 1 2967 ? 153.312 166.323 144.982 1.00 145.91 ? 2967 TYR A N     1 
ATOM   10550 C CA    . TYR A 1 2967 ? 152.127 167.071 145.376 1.00 145.91 ? 2967 TYR A CA    1 
ATOM   10551 C C     . TYR A 1 2967 ? 152.467 168.055 146.488 1.00 145.91 ? 2967 TYR A C     1 
ATOM   10552 O O     . TYR A 1 2967 ? 153.084 167.690 147.492 1.00 145.91 ? 2967 TYR A O     1 
ATOM   10553 C CB    . TYR A 1 2967 ? 151.036 166.099 145.827 1.00 145.91 ? 2967 TYR A CB    1 
ATOM   10554 C CG    . TYR A 1 2967 ? 149.620 166.615 145.707 1.00 145.91 ? 2967 TYR A CG    1 
ATOM   10555 C CD1   . TYR A 1 2967 ? 148.564 165.741 145.521 1.00 145.91 ? 2967 TYR A CD1   1 
ATOM   10556 C CD2   . TYR A 1 2967 ? 149.335 167.966 145.807 1.00 145.91 ? 2967 TYR A CD2   1 
ATOM   10557 C CE1   . TYR A 1 2967 ? 147.271 166.198 145.416 1.00 145.91 ? 2967 TYR A CE1   1 
ATOM   10558 C CE2   . TYR A 1 2967 ? 148.045 168.430 145.714 1.00 145.91 ? 2967 TYR A CE2   1 
ATOM   10559 C CZ    . TYR A 1 2967 ? 147.016 167.545 145.513 1.00 145.91 ? 2967 TYR A CZ    1 
ATOM   10560 O OH    . TYR A 1 2967 ? 145.727 168.013 145.414 1.00 145.91 ? 2967 TYR A OH    1 
ATOM   10561 N N     . THR A 1 2968 ? 152.057 169.308 146.302 1.00 147.12 ? 2968 THR A N     1 
ATOM   10562 C CA    . THR A 1 2968 ? 152.314 170.384 147.246 1.00 147.12 ? 2968 THR A CA    1 
ATOM   10563 C C     . THR A 1 2968 ? 150.996 171.048 147.629 1.00 147.12 ? 2968 THR A C     1 
ATOM   10564 O O     . THR A 1 2968 ? 149.912 170.608 147.235 1.00 147.12 ? 2968 THR A O     1 
ATOM   10565 C CB    . THR A 1 2968 ? 153.294 171.409 146.661 1.00 147.12 ? 2968 THR A CB    1 
ATOM   10566 O OG1   . THR A 1 2968 ? 153.661 172.356 147.671 1.00 147.12 ? 2968 THR A OG1   1 
ATOM   10567 C CG2   . THR A 1 2968 ? 152.665 172.140 145.486 1.00 147.12 ? 2968 THR A CG2   1 
ATOM   10568 N N     . GLY A 1 2969 ? 151.097 172.122 148.413 1.00 145.99 ? 2969 GLY A N     1 
ATOM   10569 C CA    . GLY A 1 2969 ? 149.899 172.800 148.882 1.00 145.99 ? 2969 GLY A CA    1 
ATOM   10570 C C     . GLY A 1 2969 ? 149.127 173.491 147.773 1.00 145.99 ? 2969 GLY A C     1 
ATOM   10571 O O     . GLY A 1 2969 ? 147.894 173.532 147.798 1.00 145.99 ? 2969 GLY A O     1 
ATOM   10572 N N     . GLU A 1 2970 ? 149.837 174.061 146.797 1.00 148.25 ? 2970 GLU A N     1 
ATOM   10573 C CA    . GLU A 1 2970 ? 149.165 174.851 145.770 1.00 148.25 ? 2970 GLU A CA    1 
ATOM   10574 C C     . GLU A 1 2970 ? 148.328 173.973 144.847 1.00 148.25 ? 2970 GLU A C     1 
ATOM   10575 O O     . GLU A 1 2970 ? 147.239 174.370 144.419 1.00 148.25 ? 2970 GLU A O     1 
ATOM   10576 C CB    . GLU A 1 2970 ? 150.189 175.672 144.981 1.00 148.25 ? 2970 GLU A CB    1 
ATOM   10577 C CG    . GLU A 1 2970 ? 150.939 174.920 143.898 1.00 148.25 ? 2970 GLU A CG    1 
ATOM   10578 C CD    . GLU A 1 2970 ? 151.676 175.850 142.957 1.00 148.25 ? 2970 GLU A CD    1 
ATOM   10579 O OE1   . GLU A 1 2970 ? 151.008 176.580 142.195 1.00 148.25 ? 2970 GLU A OE1   1 
ATOM   10580 O OE2   . GLU A 1 2970 ? 152.925 175.854 142.983 1.00 148.25 ? 2970 GLU A OE2   1 
ATOM   10581 N N     . ASP A 1 2971 ? 148.796 172.767 144.542 1.00 141.60 ? 2971 ASP A N     1 
ATOM   10582 C CA    . ASP A 1 2971 ? 147.954 171.864 143.768 1.00 141.60 ? 2971 ASP A CA    1 
ATOM   10583 C C     . ASP A 1 2971 ? 146.714 171.479 144.567 1.00 141.60 ? 2971 ASP A C     1 
ATOM   10584 O O     . ASP A 1 2971 ? 145.616 171.355 144.010 1.00 141.60 ? 2971 ASP A O     1 
ATOM   10585 C CB    . ASP A 1 2971 ? 148.757 170.635 143.351 1.00 141.60 ? 2971 ASP A CB    1 
ATOM   10586 C CG    . ASP A 1 2971 ? 150.092 170.999 142.735 1.00 141.60 ? 2971 ASP A CG    1 
ATOM   10587 O OD1   . ASP A 1 2971 ? 150.232 172.143 142.260 1.00 141.60 ? 2971 ASP A OD1   1 
ATOM   10588 O OD2   . ASP A 1 2971 ? 151.001 170.144 142.730 1.00 141.60 ? 2971 ASP A OD2   1 
ATOM   10589 N N     . PHE A 1 2972 ? 146.864 171.335 145.886 1.00 136.80 ? 2972 PHE A N     1 
ATOM   10590 C CA    . PHE A 1 2972 ? 145.723 171.010 146.735 1.00 136.80 ? 2972 PHE A CA    1 
ATOM   10591 C C     . PHE A 1 2972 ? 144.696 172.134 146.753 1.00 136.80 ? 2972 PHE A C     1 
ATOM   10592 O O     . PHE A 1 2972 ? 143.489 171.878 146.668 1.00 136.80 ? 2972 PHE A O     1 
ATOM   10593 C CB    . PHE A 1 2972 ? 146.188 170.703 148.155 1.00 136.80 ? 2972 PHE A CB    1 
ATOM   10594 C CG    . PHE A 1 2972 ? 145.081 170.269 149.069 1.00 136.80 ? 2972 PHE A CG    1 
ATOM   10595 C CD1   . PHE A 1 2972 ? 144.662 168.952 149.095 1.00 136.80 ? 2972 PHE A CD1   1 
ATOM   10596 C CD2   . PHE A 1 2972 ? 144.455 171.181 149.899 1.00 136.80 ? 2972 PHE A CD2   1 
ATOM   10597 C CE1   . PHE A 1 2972 ? 143.642 168.553 149.935 1.00 136.80 ? 2972 PHE A CE1   1 
ATOM   10598 C CE2   . PHE A 1 2972 ? 143.434 170.787 150.741 1.00 136.80 ? 2972 PHE A CE2   1 
ATOM   10599 C CZ    . PHE A 1 2972 ? 143.027 169.472 150.759 1.00 136.80 ? 2972 PHE A CZ    1 
ATOM   10600 N N     . ASP A 1 2973 ? 145.141 173.385 146.888 1.00 141.39 ? 2973 ASP A N     1 
ATOM   10601 C CA    . ASP A 1 2973 ? 144.159 174.461 146.953 1.00 141.39 ? 2973 ASP A CA    1 
ATOM   10602 C C     . ASP A 1 2973 ? 143.559 174.712 145.577 1.00 141.39 ? 2973 ASP A C     1 
ATOM   10603 O O     . ASP A 1 2973 ? 142.408 175.143 145.466 1.00 141.39 ? 2973 ASP A O     1 
ATOM   10604 C CB    . ASP A 1 2973 ? 144.761 175.738 147.556 1.00 141.39 ? 2973 ASP A CB    1 
ATOM   10605 C CG    . ASP A 1 2973 ? 145.989 176.233 146.826 1.00 141.39 ? 2973 ASP A CG    1 
ATOM   10606 O OD1   . ASP A 1 2973 ? 146.869 176.828 147.481 1.00 141.39 ? 2973 ASP A OD1   1 
ATOM   10607 O OD2   . ASP A 1 2973 ? 146.026 176.146 145.589 1.00 141.39 ? 2973 ASP A OD2   1 
ATOM   10608 N N     . GLU A 1 2974 ? 144.308 174.407 144.512 1.00 136.93 ? 2974 GLU A N     1 
ATOM   10609 C CA    . GLU A 1 2974 ? 143.711 174.412 143.181 1.00 136.93 ? 2974 GLU A CA    1 
ATOM   10610 C C     . GLU A 1 2974 ? 142.599 173.376 143.075 1.00 136.93 ? 2974 GLU A C     1 
ATOM   10611 O O     . GLU A 1 2974 ? 141.530 173.655 142.520 1.00 136.93 ? 2974 GLU A O     1 
ATOM   10612 C CB    . GLU A 1 2974 ? 144.783 174.155 142.123 1.00 136.93 ? 2974 GLU A CB    1 
ATOM   10613 C CG    . GLU A 1 2974 ? 144.259 174.166 140.698 1.00 136.93 ? 2974 GLU A CG    1 
ATOM   10614 C CD    . GLU A 1 2974 ? 143.311 175.317 140.433 1.00 136.93 ? 2974 GLU A CD    1 
ATOM   10615 O OE1   . GLU A 1 2974 ? 143.685 176.475 140.714 1.00 136.93 ? 2974 GLU A OE1   1 
ATOM   10616 O OE2   . GLU A 1 2974 ? 142.190 175.064 139.946 1.00 136.93 ? 2974 GLU A OE2   1 
ATOM   10617 N N     . ASP A 1 2975 ? 142.830 172.174 143.607 1.00 135.01 ? 2975 ASP A N     1 
ATOM   10618 C CA    . ASP A 1 2975 ? 141.792 171.147 143.584 1.00 135.01 ? 2975 ASP A CA    1 
ATOM   10619 C C     . ASP A 1 2975 ? 140.577 171.570 144.402 1.00 135.01 ? 2975 ASP A C     1 
ATOM   10620 O O     . ASP A 1 2975 ? 139.430 171.341 143.994 1.00 135.01 ? 2975 ASP A O     1 
ATOM   10621 C CB    . ASP A 1 2975 ? 142.355 169.827 144.106 1.00 135.01 ? 2975 ASP A CB    1 
ATOM   10622 C CG    . ASP A 1 2975 ? 143.475 169.294 143.242 1.00 135.01 ? 2975 ASP A CG    1 
ATOM   10623 O OD1   . ASP A 1 2975 ? 143.870 169.993 142.287 1.00 135.01 ? 2975 ASP A OD1   1 
ATOM   10624 O OD2   . ASP A 1 2975 ? 143.966 168.180 143.518 1.00 135.01 ? 2975 ASP A OD2   1 
ATOM   10625 N N     . LEU A 1 2976 ? 140.814 172.171 145.570 1.00 131.64 ? 2976 LEU A N     1 
ATOM   10626 C CA    . LEU A 1 2976 ? 139.710 172.647 146.398 1.00 131.64 ? 2976 LEU A CA    1 
ATOM   10627 C C     . LEU A 1 2976 ? 138.919 173.734 145.683 1.00 131.64 ? 2976 LEU A C     1 
ATOM   10628 O O     . LEU A 1 2976 ? 137.682 173.740 145.716 1.00 131.64 ? 2976 LEU A O     1 
ATOM   10629 C CB    . LEU A 1 2976 ? 140.241 173.156 147.736 1.00 131.64 ? 2976 LEU A CB    1 
ATOM   10630 C CG    . LEU A 1 2976 ? 140.324 172.132 148.869 1.00 131.64 ? 2976 LEU A CG    1 
ATOM   10631 C CD1   . LEU A 1 2976 ? 140.479 172.831 150.204 1.00 131.64 ? 2976 LEU A CD1   1 
ATOM   10632 C CD2   . LEU A 1 2976 ? 139.094 171.248 148.878 1.00 131.64 ? 2976 LEU A CD2   1 
ATOM   10633 N N     . ARG A 1 2977 ? 139.621 174.661 145.029 1.00 132.43 ? 2977 ARG A N     1 
ATOM   10634 C CA    . ARG A 1 2977 ? 138.959 175.661 144.202 1.00 132.43 ? 2977 ARG A CA    1 
ATOM   10635 C C     . ARG A 1 2977 ? 138.104 174.997 143.135 1.00 132.43 ? 2977 ARG A C     1 
ATOM   10636 O O     . ARG A 1 2977 ? 136.958 175.399 142.906 1.00 132.43 ? 2977 ARG A O     1 
ATOM   10637 C CB    . ARG A 1 2977 ? 140.008 176.567 143.555 1.00 132.43 ? 2977 ARG A CB    1 
ATOM   10638 C CG    . ARG A 1 2977 ? 139.605 178.020 143.425 1.00 132.43 ? 2977 ARG A CG    1 
ATOM   10639 C CD    . ARG A 1 2977 ? 140.710 178.857 142.788 1.00 132.43 ? 2977 ARG A CD    1 
ATOM   10640 N NE    . ARG A 1 2977 ? 141.829 179.103 143.691 1.00 132.43 ? 2977 ARG A NE    1 
ATOM   10641 C CZ    . ARG A 1 2977 ? 143.048 178.607 143.528 1.00 132.43 ? 2977 ARG A CZ    1 
ATOM   10642 N NH1   . ARG A 1 2977 ? 143.343 177.817 142.510 1.00 132.43 ? 2977 ARG A NH1   1 
ATOM   10643 N NH2   . ARG A 1 2977 ? 143.996 178.913 144.409 1.00 132.43 ? 2977 ARG A NH2   1 
ATOM   10644 N N     . THR A 1 2978 ? 138.646 173.969 142.482 1.00 125.57 ? 2978 THR A N     1 
ATOM   10645 C CA    . THR A 1 2978 ? 137.923 173.297 141.411 1.00 125.57 ? 2978 THR A CA    1 
ATOM   10646 C C     . THR A 1 2978 ? 136.628 172.681 141.922 1.00 125.57 ? 2978 THR A C     1 
ATOM   10647 O O     . THR A 1 2978 ? 135.556 172.886 141.340 1.00 125.57 ? 2978 THR A O     1 
ATOM   10648 C CB    . THR A 1 2978 ? 138.813 172.226 140.784 1.00 125.57 ? 2978 THR A CB    1 
ATOM   10649 O OG1   . THR A 1 2978 ? 140.129 172.757 140.585 1.00 125.57 ? 2978 THR A OG1   1 
ATOM   10650 C CG2   . THR A 1 2978 ? 138.252 171.788 139.452 1.00 125.57 ? 2978 THR A CG2   1 
ATOM   10651 N N     . VAL A 1 2979 ? 136.707 171.928 143.020 1.00 128.51 ? 2979 VAL A N     1 
ATOM   10652 C CA    . VAL A 1 2979 ? 135.514 171.239 143.507 1.00 128.51 ? 2979 VAL A CA    1 
ATOM   10653 C C     . VAL A 1 2979 ? 134.495 172.243 144.033 1.00 128.51 ? 2979 VAL A C     1 
ATOM   10654 O O     . VAL A 1 2979 ? 133.290 172.102 143.793 1.00 128.51 ? 2979 VAL A O     1 
ATOM   10655 C CB    . VAL A 1 2979 ? 135.872 170.181 144.569 1.00 128.51 ? 2979 VAL A CB    1 
ATOM   10656 C CG1   . VAL A 1 2979 ? 136.818 170.741 145.597 1.00 128.51 ? 2979 VAL A CG1   1 
ATOM   10657 C CG2   . VAL A 1 2979 ? 134.614 169.654 145.242 1.00 128.51 ? 2979 VAL A CG2   1 
ATOM   10658 N N     . LEU A 1 2980 ? 134.954 173.278 144.742 1.00 129.37 ? 2980 LEU A N     1 
ATOM   10659 C CA    . LEU A 1 2980 ? 134.025 174.284 145.243 1.00 129.37 ? 2980 LEU A CA    1 
ATOM   10660 C C     . LEU A 1 2980 ? 133.332 175.010 144.099 1.00 129.37 ? 2980 LEU A C     1 
ATOM   10661 O O     . LEU A 1 2980 ? 132.126 175.275 144.163 1.00 129.37 ? 2980 LEU A O     1 
ATOM   10662 C CB    . LEU A 1 2980 ? 134.761 175.274 146.142 1.00 129.37 ? 2980 LEU A CB    1 
ATOM   10663 C CG    . LEU A 1 2980 ? 135.096 174.747 147.534 1.00 129.37 ? 2980 LEU A CG    1 
ATOM   10664 C CD1   . LEU A 1 2980 ? 136.217 175.556 148.155 1.00 129.37 ? 2980 LEU A CD1   1 
ATOM   10665 C CD2   . LEU A 1 2980 ? 133.860 174.781 148.406 1.00 129.37 ? 2980 LEU A CD2   1 
ATOM   10666 N N     . ARG A 1 2981 ? 134.076 175.338 143.040 1.00 130.03 ? 2981 ARG A N     1 
ATOM   10667 C CA    . ARG A 1 2981 ? 133.468 175.985 141.886 1.00 130.03 ? 2981 ARG A CA    1 
ATOM   10668 C C     . ARG A 1 2981 ? 132.446 175.071 141.227 1.00 130.03 ? 2981 ARG A C     1 
ATOM   10669 O O     . ARG A 1 2981 ? 131.349 175.513 140.865 1.00 130.03 ? 2981 ARG A O     1 
ATOM   10670 C CB    . ARG A 1 2981 ? 134.548 176.387 140.884 1.00 130.03 ? 2981 ARG A CB    1 
ATOM   10671 C CG    . ARG A 1 2981 ? 134.008 176.931 139.575 1.00 130.03 ? 2981 ARG A CG    1 
ATOM   10672 C CD    . ARG A 1 2981 ? 135.088 177.648 138.784 1.00 130.03 ? 2981 ARG A CD    1 
ATOM   10673 N NE    . ARG A 1 2981 ? 135.738 178.700 139.555 1.00 130.03 ? 2981 ARG A NE    1 
ATOM   10674 C CZ    . ARG A 1 2981 ? 137.043 178.760 139.782 1.00 130.03 ? 2981 ARG A CZ    1 
ATOM   10675 N NH1   . ARG A 1 2981 ? 137.871 177.846 139.303 1.00 130.03 ? 2981 ARG A NH1   1 
ATOM   10676 N NH2   . ARG A 1 2981 ? 137.530 179.764 140.505 1.00 130.03 ? 2981 ARG A NH2   1 
ATOM   10677 N N     . ARG A 1 2982 ? 132.780 173.789 141.074 1.00 126.90 ? 2982 ARG A N     1 
ATOM   10678 C CA    . ARG A 1 2982 ? 131.867 172.880 140.395 1.00 126.90 ? 2982 ARG A CA    1 
ATOM   10679 C C     . ARG A 1 2982 ? 130.662 172.527 141.256 1.00 126.90 ? 2982 ARG A C     1 
ATOM   10680 O O     . ARG A 1 2982 ? 129.647 172.067 140.722 1.00 126.90 ? 2982 ARG A O     1 
ATOM   10681 C CB    . ARG A 1 2982 ? 132.608 171.612 139.967 1.00 126.90 ? 2982 ARG A CB    1 
ATOM   10682 C CG    . ARG A 1 2982 ? 131.852 170.771 138.945 1.00 126.90 ? 2982 ARG A CG    1 
ATOM   10683 C CD    . ARG A 1 2982 ? 132.474 169.388 138.722 1.00 126.90 ? 2982 ARG A CD    1 
ATOM   10684 N NE    . ARG A 1 2982 ? 133.934 169.342 138.671 1.00 126.90 ? 2982 ARG A NE    1 
ATOM   10685 C CZ    . ARG A 1 2982 ? 134.708 170.103 137.907 1.00 126.90 ? 2982 ARG A CZ    1 
ATOM   10686 N NH1   . ARG A 1 2982 ? 134.203 170.990 137.065 1.00 126.90 ? 2982 ARG A NH1   1 
ATOM   10687 N NH2   . ARG A 1 2982 ? 136.027 169.952 137.972 1.00 126.90 ? 2982 ARG A NH2   1 
ATOM   10688 N N     . SER A 1 2983 ? 130.740 172.745 142.568 1.00 125.58 ? 2983 SER A N     1 
ATOM   10689 C CA    . SER A 1 2983 ? 129.630 172.443 143.463 1.00 125.58 ? 2983 SER A CA    1 
ATOM   10690 C C     . SER A 1 2983 ? 128.868 173.673 143.927 1.00 125.58 ? 2983 SER A C     1 
ATOM   10691 O O     . SER A 1 2983 ? 127.698 173.554 144.302 1.00 125.58 ? 2983 SER A O     1 
ATOM   10692 C CB    . SER A 1 2983 ? 130.126 171.684 144.695 1.00 125.58 ? 2983 SER A CB    1 
ATOM   10693 O OG    . SER A 1 2983 ? 129.045 171.385 145.558 1.00 125.58 ? 2983 SER A OG    1 
ATOM   10694 N N     . GLY A 1 2984 ? 129.502 174.842 143.932 1.00 130.52 ? 2984 GLY A N     1 
ATOM   10695 C CA    . GLY A 1 2984 ? 128.832 176.055 144.356 1.00 130.52 ? 2984 GLY A CA    1 
ATOM   10696 C C     . GLY A 1 2984 ? 128.203 176.821 143.212 1.00 130.52 ? 2984 GLY A C     1 
ATOM   10697 O O     . GLY A 1 2984 ? 127.012 177.144 143.253 1.00 130.52 ? 2984 GLY A O     1 
ATOM   10698 N N     . CYS A 1 2985 ? 128.999 177.122 142.185 1.00 134.37 ? 2985 CYS A N     1 
ATOM   10699 C CA    . CYS A 1 2985 ? 128.467 177.834 141.029 1.00 134.37 ? 2985 CYS A CA    1 
ATOM   10700 C C     . CYS A 1 2985 ? 127.403 177.010 140.319 1.00 134.37 ? 2985 CYS A C     1 
ATOM   10701 O O     . CYS A 1 2985 ? 126.345 177.532 139.948 1.00 134.37 ? 2985 CYS A O     1 
ATOM   10702 C CB    . CYS A 1 2985 ? 129.600 178.190 140.067 1.00 134.37 ? 2985 CYS A CB    1 
ATOM   10703 S SG    . CYS A 1 2985 ? 131.136 178.680 140.879 1.00 134.37 ? 2985 CYS A SG    1 
ATOM   10704 N N     . LYS A 1 2986 ? 127.658 175.723 140.131 1.00 119.06 ? 2986 LYS A N     1 
ATOM   10705 C CA    . LYS A 1 2986 ? 126.715 174.822 139.491 1.00 119.06 ? 2986 LYS A CA    1 
ATOM   10706 C C     . LYS A 1 2986 ? 126.002 173.993 140.547 1.00 119.06 ? 2986 LYS A C     1 
ATOM   10707 O O     . LYS A 1 2986 ? 126.573 173.654 141.586 1.00 119.06 ? 2986 LYS A O     1 
ATOM   10708 C CB    . LYS A 1 2986 ? 127.426 173.902 138.499 1.00 119.06 ? 2986 LYS A CB    1 
ATOM   10709 C CG    . LYS A 1 2986 ? 127.574 174.489 137.110 1.00 119.06 ? 2986 LYS A CG    1 
ATOM   10710 C CD    . LYS A 1 2986 ? 128.794 175.389 137.019 1.00 119.06 ? 2986 LYS A CD    1 
ATOM   10711 C CE    . LYS A 1 2986 ? 130.080 174.585 137.072 1.00 119.06 ? 2986 LYS A CE    1 
ATOM   10712 N NZ    . LYS A 1 2986 ? 131.271 175.439 136.813 1.00 119.06 ? 2986 LYS A NZ    1 
ATOM   10713 N N     . ASN A 1 2987 ? 124.742 173.664 140.273 1.00 122.44 ? 2987 ASN A N     1 
ATOM   10714 C CA    . ASN A 1 2987 ? 123.970 172.858 141.210 1.00 122.44 ? 2987 ASN A CA    1 
ATOM   10715 C C     . ASN A 1 2987 ? 124.430 171.410 141.273 1.00 122.44 ? 2987 ASN A C     1 
ATOM   10716 O O     . ASN A 1 2987 ? 123.805 170.619 141.988 1.00 122.44 ? 2987 ASN A O     1 
ATOM   10717 C CB    . ASN A 1 2987 ? 122.487 172.908 140.846 1.00 122.44 ? 2987 ASN A CB    1 
ATOM   10718 C CG    . ASN A 1 2987 ? 121.670 173.683 141.853 1.00 122.44 ? 2987 ASN A CG    1 
ATOM   10719 O OD1   . ASN A 1 2987 ? 122.206 174.484 142.615 1.00 122.44 ? 2987 ASN A OD1   1 
ATOM   10720 N ND2   . ASN A 1 2987 ? 120.364 173.450 141.860 1.00 122.44 ? 2987 ASN A ND2   1 
ATOM   10721 N N     . GLU A 1 2988 ? 125.490 171.045 140.556 1.00 118.44 ? 2988 GLU A N     1 
ATOM   10722 C CA    . GLU A 1 2988 ? 125.960 169.667 140.556 1.00 118.44 ? 2988 GLU A CA    1 
ATOM   10723 C C     . GLU A 1 2988 ? 126.454 169.266 141.940 1.00 118.44 ? 2988 GLU A C     1 
ATOM   10724 O O     . GLU A 1 2988 ? 127.110 170.049 142.632 1.00 118.44 ? 2988 GLU A O     1 
ATOM   10725 C CB    . GLU A 1 2988 ? 127.075 169.494 139.530 1.00 118.44 ? 2988 GLU A CB    1 
ATOM   10726 C CG    . GLU A 1 2988 ? 127.496 168.059 139.324 1.00 118.44 ? 2988 GLU A CG    1 
ATOM   10727 C CD    . GLU A 1 2988 ? 128.821 167.760 139.975 1.00 118.44 ? 2988 GLU A CD    1 
ATOM   10728 O OE1   . GLU A 1 2988 ? 129.711 168.629 139.918 1.00 118.44 ? 2988 GLU A OE1   1 
ATOM   10729 O OE2   . GLU A 1 2988 ? 128.976 166.659 140.538 1.00 118.44 ? 2988 GLU A OE2   1 
ATOM   10730 N N     . LYS A 1 2989 ? 126.138 168.039 142.337 1.00 109.67 ? 2989 LYS A N     1 
ATOM   10731 C CA    . LYS A 1 2989 ? 126.475 167.524 143.655 1.00 109.67 ? 2989 LYS A CA    1 
ATOM   10732 C C     . LYS A 1 2989 ? 127.678 166.599 143.543 1.00 109.67 ? 2989 LYS A C     1 
ATOM   10733 O O     . LYS A 1 2989 ? 127.656 165.638 142.768 1.00 109.67 ? 2989 LYS A O     1 
ATOM   10734 C CB    . LYS A 1 2989 ? 125.282 166.781 144.254 1.00 109.67 ? 2989 LYS A CB    1 
ATOM   10735 C CG    . LYS A 1 2989 ? 123.947 167.296 143.751 1.00 109.67 ? 2989 LYS A CG    1 
ATOM   10736 C CD    . LYS A 1 2989 ? 122.807 166.402 144.190 1.00 109.67 ? 2989 LYS A CD    1 
ATOM   10737 C CE    . LYS A 1 2989 ? 122.539 166.548 145.674 1.00 109.67 ? 2989 LYS A CE    1 
ATOM   10738 N NZ    . LYS A 1 2989 ? 121.910 167.858 145.984 1.00 109.67 ? 2989 LYS A NZ    1 
ATOM   10739 N N     . ILE A 1 2990 ? 128.716 166.881 144.324 1.00 110.71 ? 2990 ILE A N     1 
ATOM   10740 C CA    . ILE A 1 2990 ? 129.989 166.179 144.234 1.00 110.71 ? 2990 ILE A CA    1 
ATOM   10741 C C     . ILE A 1 2990 ? 130.194 165.365 145.502 1.00 110.71 ? 2990 ILE A C     1 
ATOM   10742 O O     . ILE A 1 2990 ? 130.002 165.874 146.611 1.00 110.71 ? 2990 ILE A O     1 
ATOM   10743 C CB    . ILE A 1 2990 ? 131.161 167.154 144.021 1.00 110.71 ? 2990 ILE A CB    1 
ATOM   10744 C CG1   . ILE A 1 2990 ? 131.091 167.767 142.626 1.00 110.71 ? 2990 ILE A CG1   1 
ATOM   10745 C CG2   . ILE A 1 2990 ? 132.490 166.446 144.216 1.00 110.71 ? 2990 ILE A CG2   1 
ATOM   10746 C CD1   . ILE A 1 2990 ? 132.330 168.530 142.235 1.00 110.71 ? 2990 ILE A CD1   1 
ATOM   10747 N N     . ALA A 1 2991 ? 130.571 164.101 145.336 1.00 102.85 ? 2991 ALA A N     1 
ATOM   10748 C CA    . ALA A 1 2991 ? 131.010 163.270 146.448 1.00 102.85 ? 2991 ALA A CA    1 
ATOM   10749 C C     . ALA A 1 2991 ? 132.529 163.336 146.526 1.00 102.85 ? 2991 ALA A C     1 
ATOM   10750 O O     . ALA A 1 2991 ? 133.220 162.991 145.562 1.00 102.85 ? 2991 ALA A O     1 
ATOM   10751 C CB    . ALA A 1 2991 ? 130.538 161.829 146.274 1.00 102.85 ? 2991 ALA A CB    1 
ATOM   10752 N N     . PHE A 1 2992 ? 133.044 163.787 147.665 1.00 101.92 ? 2992 PHE A N     1 
ATOM   10753 C CA    . PHE A 1 2992 ? 134.476 163.997 147.840 1.00 101.92 ? 2992 PHE A CA    1 
ATOM   10754 C C     . PHE A 1 2992 ? 135.090 162.757 148.479 1.00 101.92 ? 2992 PHE A C     1 
ATOM   10755 O O     . PHE A 1 2992 ? 134.790 162.427 149.630 1.00 101.92 ? 2992 PHE A O     1 
ATOM   10756 C CB    . PHE A 1 2992 ? 134.733 165.236 148.690 1.00 101.92 ? 2992 PHE A CB    1 
ATOM   10757 C CG    . PHE A 1 2992 ? 136.090 165.835 148.494 1.00 101.92 ? 2992 PHE A CG    1 
ATOM   10758 C CD1   . PHE A 1 2992 ? 137.034 165.206 147.704 1.00 101.92 ? 2992 PHE A CD1   1 
ATOM   10759 C CD2   . PHE A 1 2992 ? 136.427 167.023 149.107 1.00 101.92 ? 2992 PHE A CD2   1 
ATOM   10760 C CE1   . PHE A 1 2992 ? 138.281 165.755 147.529 1.00 101.92 ? 2992 PHE A CE1   1 
ATOM   10761 C CE2   . PHE A 1 2992 ? 137.672 167.575 148.934 1.00 101.92 ? 2992 PHE A CE2   1 
ATOM   10762 C CZ    . PHE A 1 2992 ? 138.600 166.940 148.144 1.00 101.92 ? 2992 PHE A CZ    1 
ATOM   10763 N N     . ILE A 1 2993 ? 135.956 162.079 147.735 1.00 106.25 ? 2993 ILE A N     1 
ATOM   10764 C CA    . ILE A 1 2993 ? 136.675 160.914 148.234 1.00 106.25 ? 2993 ILE A CA    1 
ATOM   10765 C C     . ILE A 1 2993 ? 137.963 161.395 148.886 1.00 106.25 ? 2993 ILE A C     1 
ATOM   10766 O O     . ILE A 1 2993 ? 138.829 161.969 148.217 1.00 106.25 ? 2993 ILE A O     1 
ATOM   10767 C CB    . ILE A 1 2993 ? 136.972 159.921 147.102 1.00 106.25 ? 2993 ILE A CB    1 
ATOM   10768 C CG1   . ILE A 1 2993 ? 135.672 159.372 146.519 1.00 106.25 ? 2993 ILE A CG1   1 
ATOM   10769 C CG2   . ILE A 1 2993 ? 137.858 158.798 147.602 1.00 106.25 ? 2993 ILE A CG2   1 
ATOM   10770 C CD1   . ILE A 1 2993 ? 134.733 158.809 147.550 1.00 106.25 ? 2993 ILE A CD1   1 
ATOM   10771 N N     . MET A 1 2994 ? 138.099 161.157 150.189 1.00 113.58 ? 2994 MET A N     1 
ATOM   10772 C CA    . MET A 1 2994 ? 139.282 161.579 150.930 1.00 113.58 ? 2994 MET A CA    1 
ATOM   10773 C C     . MET A 1 2994 ? 139.880 160.364 151.618 1.00 113.58 ? 2994 MET A C     1 
ATOM   10774 O O     . MET A 1 2994 ? 139.177 159.652 152.341 1.00 113.58 ? 2994 MET A O     1 
ATOM   10775 C CB    . MET A 1 2994 ? 138.939 162.662 151.954 1.00 113.58 ? 2994 MET A CB    1 
ATOM   10776 C CG    . MET A 1 2994 ? 140.073 163.620 152.245 1.00 113.58 ? 2994 MET A CG    1 
ATOM   10777 S SD    . MET A 1 2994 ? 141.096 163.904 150.792 1.00 113.58 ? 2994 MET A SD    1 
ATOM   10778 C CE    . MET A 1 2994 ? 142.671 164.263 151.558 1.00 113.58 ? 2994 MET A CE    1 
ATOM   10779 N N     . ASP A 1 2995 ? 141.169 160.131 151.399 1.00 119.01 ? 2995 ASP A N     1 
ATOM   10780 C CA    . ASP A 1 2995 ? 141.866 158.997 151.981 1.00 119.01 ? 2995 ASP A CA    1 
ATOM   10781 C C     . ASP A 1 2995 ? 143.038 159.482 152.821 1.00 119.01 ? 2995 ASP A C     1 
ATOM   10782 O O     . ASP A 1 2995 ? 143.567 160.577 152.609 1.00 119.01 ? 2995 ASP A O     1 
ATOM   10783 C CB    . ASP A 1 2995 ? 142.370 158.034 150.902 1.00 119.01 ? 2995 ASP A CB    1 
ATOM   10784 C CG    . ASP A 1 2995 ? 141.372 156.941 150.589 1.00 119.01 ? 2995 ASP A CG    1 
ATOM   10785 O OD1   . ASP A 1 2995 ? 140.252 156.987 151.135 1.00 119.01 ? 2995 ASP A OD1   1 
ATOM   10786 O OD2   . ASP A 1 2995 ? 141.708 156.030 149.804 1.00 119.01 ? 2995 ASP A OD2   1 
ATOM   10787 N N     . GLU A 1 2996 ? 143.434 158.649 153.784 1.00 120.60 ? 2996 GLU A N     1 
ATOM   10788 C CA    . GLU A 1 2996 ? 144.573 158.980 154.632 1.00 120.60 ? 2996 GLU A CA    1 
ATOM   10789 C C     . GLU A 1 2996 ? 145.850 159.138 153.823 1.00 120.60 ? 2996 GLU A C     1 
ATOM   10790 O O     . GLU A 1 2996 ? 146.711 159.950 154.177 1.00 120.60 ? 2996 GLU A O     1 
ATOM   10791 C CB    . GLU A 1 2996 ? 144.751 157.904 155.700 1.00 120.60 ? 2996 GLU A CB    1 
ATOM   10792 C CG    . GLU A 1 2996 ? 144.957 156.502 155.153 1.00 120.60 ? 2996 GLU A CG    1 
ATOM   10793 C CD    . GLU A 1 2996 ? 143.650 155.760 154.949 1.00 120.60 ? 2996 GLU A CD    1 
ATOM   10794 O OE1   . GLU A 1 2996 ? 142.739 156.324 154.309 1.00 120.60 ? 2996 GLU A OE1   1 
ATOM   10795 O OE2   . GLU A 1 2996 ? 143.531 154.615 155.429 1.00 120.60 ? 2996 GLU A OE2   1 
ATOM   10796 N N     . SER A 1 2997 ? 145.994 158.373 152.740 1.00 120.54 ? 2997 SER A N     1 
ATOM   10797 C CA    . SER A 1 2997 ? 147.184 158.494 151.909 1.00 120.54 ? 2997 SER A CA    1 
ATOM   10798 C C     . SER A 1 2997 ? 147.257 159.856 151.235 1.00 120.54 ? 2997 SER A C     1 
ATOM   10799 O O     . SER A 1 2997 ? 148.352 160.399 151.054 1.00 120.54 ? 2997 SER A O     1 
ATOM   10800 C CB    . SER A 1 2997 ? 147.207 157.384 150.860 1.00 120.54 ? 2997 SER A CB    1 
ATOM   10801 O OG    . SER A 1 2997 ? 146.901 156.128 151.440 1.00 120.54 ? 2997 SER A OG    1 
ATOM   10802 N N     . ASN A 1 2998 ? 146.107 160.425 150.866 1.00 123.70 ? 2998 ASN A N     1 
ATOM   10803 C CA    . ASN A 1 2998 ? 146.098 161.715 150.191 1.00 123.70 ? 2998 ASN A CA    1 
ATOM   10804 C C     . ASN A 1 2998 ? 146.549 162.850 151.099 1.00 123.70 ? 2998 ASN A C     1 
ATOM   10805 O O     . ASN A 1 2998 ? 146.964 163.899 150.596 1.00 123.70 ? 2998 ASN A O     1 
ATOM   10806 C CB    . ASN A 1 2998 ? 144.702 162.016 149.642 1.00 123.70 ? 2998 ASN A CB    1 
ATOM   10807 C CG    . ASN A 1 2998 ? 144.085 160.831 148.924 1.00 123.70 ? 2998 ASN A CG    1 
ATOM   10808 O OD1   . ASN A 1 2998 ? 142.875 160.619 148.980 1.00 123.70 ? 2998 ASN A OD1   1 
ATOM   10809 N ND2   . ASN A 1 2998 ? 144.915 160.056 148.238 1.00 123.70 ? 2998 ASN A ND2   1 
ATOM   10810 N N     . VAL A 1 2999 ? 146.487 162.667 152.414 1.00 123.95 ? 2999 VAL A N     1 
ATOM   10811 C CA    . VAL A 1 2999 ? 146.927 163.685 153.361 1.00 123.95 ? 2999 VAL A CA    1 
ATOM   10812 C C     . VAL A 1 2999 ? 148.414 163.488 153.621 1.00 123.95 ? 2999 VAL A C     1 
ATOM   10813 O O     . VAL A 1 2999 ? 148.840 162.419 154.072 1.00 123.95 ? 2999 VAL A O     1 
ATOM   10814 C CB    . VAL A 1 2999 ? 146.126 163.615 154.669 1.00 123.95 ? 2999 VAL A CB    1 
ATOM   10815 C CG1   . VAL A 1 2999 ? 146.890 164.292 155.794 1.00 123.95 ? 2999 VAL A CG1   1 
ATOM   10816 C CG2   . VAL A 1 2999 ? 144.767 164.259 154.490 1.00 123.95 ? 2999 VAL A CG2   1 
ATOM   10817 N N     . LEU A 1 3000 ? 149.204 164.517 153.329 1.00 131.86 ? 3000 LEU A N     1 
ATOM   10818 C CA    . LEU A 1 3000 ? 150.644 164.493 153.550 1.00 131.86 ? 3000 LEU A CA    1 
ATOM   10819 C C     . LEU A 1 3000 ? 151.072 165.437 154.661 1.00 131.86 ? 3000 LEU A C     1 
ATOM   10820 O O     . LEU A 1 3000 ? 151.797 165.035 155.576 1.00 131.86 ? 3000 LEU A O     1 
ATOM   10821 C CB    . LEU A 1 3000 ? 151.391 164.848 152.254 1.00 131.86 ? 3000 LEU A CB    1 
ATOM   10822 C CG    . LEU A 1 3000 ? 151.608 163.777 151.177 1.00 131.86 ? 3000 LEU A CG    1 
ATOM   10823 C CD1   . LEU A 1 3000 ? 152.537 162.686 151.686 1.00 131.86 ? 3000 LEU A CD1   1 
ATOM   10824 C CD2   . LEU A 1 3000 ? 150.301 163.181 150.677 1.00 131.86 ? 3000 LEU A CD2   1 
ATOM   10825 N N     . ASP A 1 3001 ? 150.638 166.689 154.598 1.00 133.80 ? 3001 ASP A N     1 
ATOM   10826 C CA    . ASP A 1 3001 ? 150.948 167.697 155.596 1.00 133.80 ? 3001 ASP A CA    1 
ATOM   10827 C C     . ASP A 1 3001 ? 149.668 168.163 156.277 1.00 133.80 ? 3001 ASP A C     1 
ATOM   10828 O O     . ASP A 1 3001 ? 148.558 167.962 155.779 1.00 133.80 ? 3001 ASP A O     1 
ATOM   10829 C CB    . ASP A 1 3001 ? 151.686 168.877 154.955 1.00 133.80 ? 3001 ASP A CB    1 
ATOM   10830 C CG    . ASP A 1 3001 ? 151.021 169.355 153.680 1.00 133.80 ? 3001 ASP A CG    1 
ATOM   10831 O OD1   . ASP A 1 3001 ? 150.348 168.536 153.018 1.00 133.80 ? 3001 ASP A OD1   1 
ATOM   10832 O OD2   . ASP A 1 3001 ? 151.173 170.546 153.337 1.00 133.80 ? 3001 ASP A OD2   1 
ATOM   10833 N N     . SER A 1 3002 ? 149.836 168.798 157.437 1.00 127.91 ? 3002 SER A N     1 
ATOM   10834 C CA    . SER A 1 3002 ? 148.683 169.234 158.212 1.00 127.91 ? 3002 SER A CA    1 
ATOM   10835 C C     . SER A 1 3002 ? 147.932 170.380 157.548 1.00 127.91 ? 3002 SER A C     1 
ATOM   10836 O O     . SER A 1 3002 ? 146.766 170.611 157.884 1.00 127.91 ? 3002 SER A O     1 
ATOM   10837 C CB    . SER A 1 3002 ? 149.119 169.641 159.618 1.00 127.91 ? 3002 SER A CB    1 
ATOM   10838 O OG    . SER A 1 3002 ? 149.862 168.605 160.235 1.00 127.91 ? 3002 SER A OG    1 
ATOM   10839 N N     . GLY A 1 3003 ? 148.570 171.104 156.626 1.00 128.37 ? 3003 GLY A N     1 
ATOM   10840 C CA    . GLY A 1 3003 ? 147.871 172.176 155.937 1.00 128.37 ? 3003 GLY A CA    1 
ATOM   10841 C C     . GLY A 1 3003 ? 146.647 171.675 155.197 1.00 128.37 ? 3003 GLY A C     1 
ATOM   10842 O O     . GLY A 1 3003 ? 145.593 172.317 155.200 1.00 128.37 ? 3003 GLY A O     1 
ATOM   10843 N N     . PHE A 1 3004 ? 146.773 170.510 154.557 1.00 128.69 ? 3004 PHE A N     1 
ATOM   10844 C CA    . PHE A 1 3004 ? 145.625 169.882 153.916 1.00 128.69 ? 3004 PHE A CA    1 
ATOM   10845 C C     . PHE A 1 3004 ? 144.524 169.635 154.933 1.00 128.69 ? 3004 PHE A C     1 
ATOM   10846 O O     . PHE A 1 3004 ? 143.345 169.916 154.677 1.00 128.69 ? 3004 PHE A O     1 
ATOM   10847 C CB    . PHE A 1 3004 ? 146.038 168.554 153.273 1.00 128.69 ? 3004 PHE A CB    1 
ATOM   10848 C CG    . PHE A 1 3004 ? 146.982 168.686 152.105 1.00 128.69 ? 3004 PHE A CG    1 
ATOM   10849 C CD1   . PHE A 1 3004 ? 147.616 169.882 151.817 1.00 128.69 ? 3004 PHE A CD1   1 
ATOM   10850 C CD2   . PHE A 1 3004 ? 147.250 167.588 151.308 1.00 128.69 ? 3004 PHE A CD2   1 
ATOM   10851 C CE1   . PHE A 1 3004 ? 148.486 169.982 150.752 1.00 128.69 ? 3004 PHE A CE1   1 
ATOM   10852 C CE2   . PHE A 1 3004 ? 148.117 167.682 150.242 1.00 128.69 ? 3004 PHE A CE2   1 
ATOM   10853 C CZ    . PHE A 1 3004 ? 148.736 168.881 149.963 1.00 128.69 ? 3004 PHE A CZ    1 
ATOM   10854 N N     . LEU A 1 3005 ? 144.902 169.115 156.102 1.00 120.91 ? 3005 LEU A N     1 
ATOM   10855 C CA    . LEU A 1 3005 ? 143.928 168.779 157.131 1.00 120.91 ? 3005 LEU A CA    1 
ATOM   10856 C C     . LEU A 1 3005 ? 143.179 170.013 157.608 1.00 120.91 ? 3005 LEU A C     1 
ATOM   10857 O O     . LEU A 1 3005 ? 141.953 169.986 157.738 1.00 120.91 ? 3005 LEU A O     1 
ATOM   10858 C CB    . LEU A 1 3005 ? 144.629 168.095 158.302 1.00 120.91 ? 3005 LEU A CB    1 
ATOM   10859 C CG    . LEU A 1 3005 ? 143.876 166.960 158.989 1.00 120.91 ? 3005 LEU A CG    1 
ATOM   10860 C CD1   . LEU A 1 3005 ? 143.051 166.183 157.977 1.00 120.91 ? 3005 LEU A CD1   1 
ATOM   10861 C CD2   . LEU A 1 3005 ? 144.848 166.044 159.714 1.00 120.91 ? 3005 LEU A CD2   1 
ATOM   10862 N N     . GLU A 1 3006 ? 143.892 171.111 157.859 1.00 121.04 ? 3006 GLU A N     1 
ATOM   10863 C CA    . GLU A 1 3006 ? 143.215 172.314 158.327 1.00 121.04 ? 3006 GLU A CA    1 
ATOM   10864 C C     . GLU A 1 3006 ? 142.377 172.968 157.237 1.00 121.04 ? 3006 GLU A C     1 
ATOM   10865 O O     . GLU A 1 3006 ? 141.288 173.476 157.528 1.00 121.04 ? 3006 GLU A O     1 
ATOM   10866 C CB    . GLU A 1 3006 ? 144.224 173.309 158.900 1.00 121.04 ? 3006 GLU A CB    1 
ATOM   10867 C CG    . GLU A 1 3006 ? 145.333 172.655 159.700 1.00 121.04 ? 3006 GLU A CG    1 
ATOM   10868 C CD    . GLU A 1 3006 ? 146.496 173.585 159.968 1.00 121.04 ? 3006 GLU A CD    1 
ATOM   10869 O OE1   . GLU A 1 3006 ? 147.540 173.103 160.455 1.00 121.04 ? 3006 GLU A OE1   1 
ATOM   10870 O OE2   . GLU A 1 3006 ? 146.368 174.796 159.697 1.00 121.04 ? 3006 GLU A OE2   1 
ATOM   10871 N N     . ARG A 1 3007 ? 142.850 172.970 155.988 1.00 120.95 ? 3007 ARG A N     1 
ATOM   10872 C CA    . ARG A 1 3007 ? 142.016 173.463 154.898 1.00 120.95 ? 3007 ARG A CA    1 
ATOM   10873 C C     . ARG A 1 3007 ? 140.701 172.699 154.847 1.00 120.95 ? 3007 ARG A C     1 
ATOM   10874 O O     . ARG A 1 3007 ? 139.615 173.296 154.811 1.00 120.95 ? 3007 ARG A O     1 
ATOM   10875 C CB    . ARG A 1 3007 ? 142.763 173.339 153.570 1.00 120.95 ? 3007 ARG A CB    1 
ATOM   10876 C CG    . ARG A 1 3007 ? 143.768 174.443 153.312 1.00 120.95 ? 3007 ARG A CG    1 
ATOM   10877 C CD    . ARG A 1 3007 ? 143.191 175.498 152.386 1.00 120.95 ? 3007 ARG A CD    1 
ATOM   10878 N NE    . ARG A 1 3007 ? 144.197 176.464 151.962 1.00 120.95 ? 3007 ARG A NE    1 
ATOM   10879 C CZ    . ARG A 1 3007 ? 144.203 177.741 152.316 1.00 120.95 ? 3007 ARG A CZ    1 
ATOM   10880 N NH1   . ARG A 1 3007 ? 143.264 178.245 153.099 1.00 120.95 ? 3007 ARG A NH1   1 
ATOM   10881 N NH2   . ARG A 1 3007 ? 145.174 178.533 151.872 1.00 120.95 ? 3007 ARG A NH2   1 
ATOM   10882 N N     . MET A 1 3008 ? 140.782 171.368 154.889 1.00 121.30 ? 3008 MET A N     1 
ATOM   10883 C CA    . MET A 1 3008 ? 139.573 170.558 154.866 1.00 121.30 ? 3008 MET A CA    1 
ATOM   10884 C C     . MET A 1 3008 ? 138.713 170.829 156.093 1.00 121.30 ? 3008 MET A C     1 
ATOM   10885 O O     . MET A 1 3008 ? 137.481 170.842 156.006 1.00 121.30 ? 3008 MET A O     1 
ATOM   10886 C CB    . MET A 1 3008 ? 139.944 169.077 154.779 1.00 121.30 ? 3008 MET A CB    1 
ATOM   10887 C CG    . MET A 1 3008 ? 140.294 168.586 153.375 1.00 121.30 ? 3008 MET A CG    1 
ATOM   10888 S SD    . MET A 1 3008 ? 139.099 168.878 152.052 1.00 121.30 ? 3008 MET A SD    1 
ATOM   10889 C CE    . MET A 1 3008 ? 137.536 168.622 152.886 1.00 121.30 ? 3008 MET A CE    1 
ATOM   10890 N N     . ASN A 1 3009 ? 139.349 171.050 157.245 1.00 113.61 ? 3009 ASN A N     1 
ATOM   10891 C CA    . ASN A 1 3009 ? 138.618 171.309 158.481 1.00 113.61 ? 3009 ASN A CA    1 
ATOM   10892 C C     . ASN A 1 3009 ? 137.766 172.564 158.369 1.00 113.61 ? 3009 ASN A C     1 
ATOM   10893 O O     . ASN A 1 3009 ? 136.582 172.562 158.734 1.00 113.61 ? 3009 ASN A O     1 
ATOM   10894 C CB    . ASN A 1 3009 ? 139.605 171.433 159.640 1.00 113.61 ? 3009 ASN A CB    1 
ATOM   10895 C CG    . ASN A 1 3009 ? 139.115 170.760 160.900 1.00 113.61 ? 3009 ASN A CG    1 
ATOM   10896 O OD1   . ASN A 1 3009 ? 138.561 169.663 160.860 1.00 113.61 ? 3009 ASN A OD1   1 
ATOM   10897 N ND2   . ASN A 1 3009 ? 139.326 171.415 162.034 1.00 113.61 ? 3009 ASN A ND2   1 
ATOM   10898 N N     . THR A 1 3010 ? 138.358 173.657 157.883 1.00 118.91 ? 3010 THR A N     1 
ATOM   10899 C CA    . THR A 1 3010 ? 137.568 174.868 157.679 1.00 118.91 ? 3010 THR A CA    1 
ATOM   10900 C C     . THR A 1 3010 ? 136.502 174.651 156.617 1.00 118.91 ? 3010 THR A C     1 
ATOM   10901 O O     . THR A 1 3010 ? 135.401 175.206 156.715 1.00 118.91 ? 3010 THR A O     1 
ATOM   10902 C CB    . THR A 1 3010 ? 138.454 176.058 157.310 1.00 118.91 ? 3010 THR A CB    1 
ATOM   10903 O OG1   . THR A 1 3010 ? 138.632 176.108 155.890 1.00 118.91 ? 3010 THR A OG1   1 
ATOM   10904 C CG2   . THR A 1 3010 ? 139.791 176.004 158.017 1.00 118.91 ? 3010 THR A CG2   1 
ATOM   10905 N N     . LEU A 1 3011 ? 136.797 173.830 155.606 1.00 112.60 ? 3011 LEU A N     1 
ATOM   10906 C CA    . LEU A 1 3011 ? 135.789 173.538 154.591 1.00 112.60 ? 3011 LEU A CA    1 
ATOM   10907 C C     . LEU A 1 3011 ? 134.557 172.886 155.208 1.00 112.60 ? 3011 LEU A C     1 
ATOM   10908 O O     . LEU A 1 3011 ? 133.422 173.271 154.909 1.00 112.60 ? 3011 LEU A O     1 
ATOM   10909 C CB    . LEU A 1 3011 ? 136.380 172.644 153.504 1.00 112.60 ? 3011 LEU A CB    1 
ATOM   10910 C CG    . LEU A 1 3011 ? 135.439 172.271 152.358 1.00 112.60 ? 3011 LEU A CG    1 
ATOM   10911 C CD1   . LEU A 1 3011 ? 134.659 173.480 151.874 1.00 112.60 ? 3011 LEU A CD1   1 
ATOM   10912 C CD2   . LEU A 1 3011 ? 136.226 171.659 151.216 1.00 112.60 ? 3011 LEU A CD2   1 
ATOM   10913 N N     . LEU A 1 3012 ? 134.762 171.893 156.074 1.00 109.64 ? 3012 LEU A N     1 
ATOM   10914 C CA    . LEU A 1 3012 ? 133.619 171.216 156.686 1.00 109.64 ? 3012 LEU A CA    1 
ATOM   10915 C C     . LEU A 1 3012 ? 132.900 172.121 157.676 1.00 109.64 ? 3012 LEU A C     1 
ATOM   10916 O O     . LEU A 1 3012 ? 131.668 172.219 157.656 1.00 109.64 ? 3012 LEU A O     1 
ATOM   10917 C CB    . LEU A 1 3012 ? 134.044 169.916 157.370 1.00 109.64 ? 3012 LEU A CB    1 
ATOM   10918 C CG    . LEU A 1 3012 ? 135.234 169.130 156.834 1.00 109.64 ? 3012 LEU A CG    1 
ATOM   10919 C CD1   . LEU A 1 3012 ? 135.511 167.909 157.679 1.00 109.64 ? 3012 LEU A CD1   1 
ATOM   10920 C CD2   . LEU A 1 3012 ? 134.972 168.720 155.398 1.00 109.64 ? 3012 LEU A CD2   1 
ATOM   10921 N N     . ALA A 1 3013 ? 133.645 172.791 158.556 1.00 113.84 ? 3013 ALA A N     1 
ATOM   10922 C CA    . ALA A 1 3013 ? 132.993 173.566 159.607 1.00 113.84 ? 3013 ALA A CA    1 
ATOM   10923 C C     . ALA A 1 3013 ? 132.310 174.803 159.038 1.00 113.84 ? 3013 ALA A C     1 
ATOM   10924 O O     . ALA A 1 3013 ? 131.089 174.958 159.154 1.00 113.84 ? 3013 ALA A O     1 
ATOM   10925 C CB    . ALA A 1 3013 ? 134.004 173.958 160.681 1.00 113.84 ? 3013 ALA A CB    1 
ATOM   10926 N N     . ASN A 1 3014 ? 133.085 175.696 158.421 1.00 124.45 ? 3014 ASN A N     1 
ATOM   10927 C CA    . ASN A 1 3014 ? 132.528 176.938 157.900 1.00 124.45 ? 3014 ASN A CA    1 
ATOM   10928 C C     . ASN A 1 3014 ? 131.539 176.669 156.773 1.00 124.45 ? 3014 ASN A C     1 
ATOM   10929 O O     . ASN A 1 3014 ? 130.470 177.286 156.718 1.00 124.45 ? 3014 ASN A O     1 
ATOM   10930 C CB    . ASN A 1 3014 ? 133.666 177.844 157.418 1.00 124.45 ? 3014 ASN A CB    1 
ATOM   10931 C CG    . ASN A 1 3014 ? 133.190 179.219 156.982 1.00 124.45 ? 3014 ASN A CG    1 
ATOM   10932 O OD1   . ASN A 1 3014 ? 132.003 179.532 157.032 1.00 124.45 ? 3014 ASN A OD1   1 
ATOM   10933 N ND2   . ASN A 1 3014 ? 134.129 180.052 156.548 1.00 124.45 ? 3014 ASN A ND2   1 
ATOM   10934 N N     . GLY A 1 3015 ? 131.865 175.732 155.890 1.00 121.60 ? 3015 GLY A N     1 
ATOM   10935 C CA    . GLY A 1 3015 ? 131.149 175.535 154.652 1.00 121.60 ? 3015 GLY A CA    1 
ATOM   10936 C C     . GLY A 1 3015 ? 131.864 176.110 153.452 1.00 121.60 ? 3015 GLY A C     1 
ATOM   10937 O O     . GLY A 1 3015 ? 131.500 175.790 152.315 1.00 121.60 ? 3015 GLY A O     1 
ATOM   10938 N N     . GLU A 1 3016 ? 132.866 176.953 153.679 1.00 130.58 ? 3016 GLU A N     1 
ATOM   10939 C CA    . GLU A 1 3016 ? 133.701 177.493 152.619 1.00 130.58 ? 3016 GLU A CA    1 
ATOM   10940 C C     . GLU A 1 3016 ? 135.013 177.938 153.241 1.00 130.58 ? 3016 GLU A C     1 
ATOM   10941 O O     . GLU A 1 3016 ? 135.096 178.175 154.449 1.00 130.58 ? 3016 GLU A O     1 
ATOM   10942 C CB    . GLU A 1 3016 ? 133.014 178.656 151.898 1.00 130.58 ? 3016 GLU A CB    1 
ATOM   10943 C CG    . GLU A 1 3016 ? 133.423 180.026 152.411 1.00 130.58 ? 3016 GLU A CG    1 
ATOM   10944 C CD    . GLU A 1 3016 ? 132.762 180.374 153.734 1.00 130.58 ? 3016 GLU A CD    1 
ATOM   10945 O OE1   . GLU A 1 3016 ? 131.944 179.567 154.223 1.00 130.58 ? 3016 GLU A OE1   1 
ATOM   10946 O OE2   . GLU A 1 3016 ? 133.061 181.453 154.286 1.00 130.58 ? 3016 GLU A OE2   1 
ATOM   10947 N N     . VAL A 1 3017 ? 136.038 178.045 152.409 1.00 131.08 ? 3017 VAL A N     1 
ATOM   10948 C CA    . VAL A 1 3017 ? 137.360 178.469 152.853 1.00 131.08 ? 3017 VAL A CA    1 
ATOM   10949 C C     . VAL A 1 3017 ? 137.637 179.841 152.250 1.00 131.08 ? 3017 VAL A C     1 
ATOM   10950 O O     . VAL A 1 3017 ? 137.863 179.942 151.037 1.00 131.08 ? 3017 VAL A O     1 
ATOM   10951 C CB    . VAL A 1 3017 ? 138.446 177.461 152.452 1.00 131.08 ? 3017 VAL A CB    1 
ATOM   10952 C CG1   . VAL A 1 3017 ? 139.769 177.831 153.104 1.00 131.08 ? 3017 VAL A CG1   1 
ATOM   10953 C CG2   . VAL A 1 3017 ? 138.022 176.052 152.816 1.00 131.08 ? 3017 VAL A CG2   1 
ATOM   10954 N N     . PRO A 1 3018 ? 137.626 180.913 153.044 1.00 128.24 ? 3018 PRO A N     1 
ATOM   10955 C CA    . PRO A 1 3018 ? 137.812 182.257 152.472 1.00 128.24 ? 3018 PRO A CA    1 
ATOM   10956 C C     . PRO A 1 3018 ? 139.162 182.471 151.811 1.00 128.24 ? 3018 PRO A C     1 
ATOM   10957 O O     . PRO A 1 3018 ? 139.280 183.359 150.959 1.00 128.24 ? 3018 PRO A O     1 
ATOM   10958 C CB    . PRO A 1 3018 ? 137.634 183.183 153.684 1.00 128.24 ? 3018 PRO A CB    1 
ATOM   10959 C CG    . PRO A 1 3018 ? 136.908 182.362 154.703 1.00 128.24 ? 3018 PRO A CG    1 
ATOM   10960 C CD    . PRO A 1 3018 ? 137.354 180.954 154.488 1.00 128.24 ? 3018 PRO A CD    1 
ATOM   10961 N N     . GLY A 1 3019 ? 140.179 181.689 152.162 1.00 135.94 ? 3019 GLY A N     1 
ATOM   10962 C CA    . GLY A 1 3019 ? 141.507 181.927 151.631 1.00 135.94 ? 3019 GLY A CA    1 
ATOM   10963 C C     . GLY A 1 3019 ? 141.742 181.443 150.218 1.00 135.94 ? 3019 GLY A C     1 
ATOM   10964 O O     . GLY A 1 3019 ? 142.827 181.670 149.675 1.00 135.94 ? 3019 GLY A O     1 
ATOM   10965 N N     . LEU A 1 3020 ? 140.762 180.773 149.610 1.00 140.26 ? 3020 LEU A N     1 
ATOM   10966 C CA    . LEU A 1 3020 ? 140.952 180.245 148.263 1.00 140.26 ? 3020 LEU A CA    1 
ATOM   10967 C C     . LEU A 1 3020 ? 140.884 181.325 147.191 1.00 140.26 ? 3020 LEU A C     1 
ATOM   10968 O O     . LEU A 1 3020 ? 141.682 181.312 146.248 1.00 140.26 ? 3020 LEU A O     1 
ATOM   10969 C CB    . LEU A 1 3020 ? 139.920 179.157 147.974 1.00 140.26 ? 3020 LEU A CB    1 
ATOM   10970 C CG    . LEU A 1 3020 ? 140.395 177.733 148.236 1.00 140.26 ? 3020 LEU A CG    1 
ATOM   10971 C CD1   . LEU A 1 3020 ? 141.655 177.487 147.440 1.00 140.26 ? 3020 LEU A CD1   1 
ATOM   10972 C CD2   . LEU A 1 3020 ? 140.661 177.511 149.700 1.00 140.26 ? 3020 LEU A CD2   1 
ATOM   10973 N N     . PHE A 1 3021 ? 139.948 182.260 147.306 1.00 146.48 ? 3021 PHE A N     1 
ATOM   10974 C CA    . PHE A 1 3021 ? 139.605 183.150 146.199 1.00 146.48 ? 3021 PHE A CA    1 
ATOM   10975 C C     . PHE A 1 3021 ? 140.142 184.549 146.477 1.00 146.48 ? 3021 PHE A C     1 
ATOM   10976 O O     . PHE A 1 3021 ? 139.637 185.261 147.347 1.00 146.48 ? 3021 PHE A O     1 
ATOM   10977 C CB    . PHE A 1 3021 ? 138.097 183.158 145.981 1.00 146.48 ? 3021 PHE A CB    1 
ATOM   10978 C CG    . PHE A 1 3021 ? 137.536 181.808 145.641 1.00 146.48 ? 3021 PHE A CG    1 
ATOM   10979 C CD1   . PHE A 1 3021 ? 137.512 181.366 144.330 1.00 146.48 ? 3021 PHE A CD1   1 
ATOM   10980 C CD2   . PHE A 1 3021 ? 137.045 180.978 146.633 1.00 146.48 ? 3021 PHE A CD2   1 
ATOM   10981 C CE1   . PHE A 1 3021 ? 137.002 180.125 144.016 1.00 146.48 ? 3021 PHE A CE1   1 
ATOM   10982 C CE2   . PHE A 1 3021 ? 136.533 179.734 146.323 1.00 146.48 ? 3021 PHE A CE2   1 
ATOM   10983 C CZ    . PHE A 1 3021 ? 136.514 179.306 145.014 1.00 146.48 ? 3021 PHE A CZ    1 
ATOM   10984 N N     . GLU A 1 3022 ? 141.172 184.939 145.727 1.00 151.95 ? 3022 GLU A N     1 
ATOM   10985 C CA    . GLU A 1 3022 ? 141.713 186.287 145.768 1.00 151.95 ? 3022 GLU A CA    1 
ATOM   10986 C C     . GLU A 1 3022 ? 141.956 186.774 144.347 1.00 151.95 ? 3022 GLU A C     1 
ATOM   10987 O O     . GLU A 1 3022 ? 142.294 185.990 143.456 1.00 151.95 ? 3022 GLU A O     1 
ATOM   10988 C CB    . GLU A 1 3022 ? 143.028 186.360 146.555 1.00 151.95 ? 3022 GLU A CB    1 
ATOM   10989 C CG    . GLU A 1 3022 ? 143.948 185.171 146.346 1.00 151.95 ? 3022 GLU A CG    1 
ATOM   10990 C CD    . GLU A 1 3022 ? 143.833 184.143 147.448 1.00 151.95 ? 3022 GLU A CD    1 
ATOM   10991 O OE1   . GLU A 1 3022 ? 142.707 183.675 147.710 1.00 151.95 ? 3022 GLU A OE1   1 
ATOM   10992 O OE2   . GLU A 1 3022 ? 144.871 183.799 148.052 1.00 151.95 ? 3022 GLU A OE2   1 
ATOM   10993 N N     . GLY A 1 3023 ? 141.787 188.077 144.149 1.00 159.43 ? 3023 GLY A N     1 
ATOM   10994 C CA    . GLY A 1 3023 ? 142.121 188.675 142.866 1.00 159.43 ? 3023 GLY A CA    1 
ATOM   10995 C C     . GLY A 1 3023 ? 141.252 188.151 141.740 1.00 159.43 ? 3023 GLY A C     1 
ATOM   10996 O O     . GLY A 1 3023 ? 140.019 188.127 141.831 1.00 159.43 ? 3023 GLY A O     1 
ATOM   10997 N N     . ASP A 1 3024 ? 141.907 187.720 140.659 1.00 163.33 ? 3024 ASP A N     1 
ATOM   10998 C CA    . ASP A 1 3024 ? 141.180 187.305 139.463 1.00 163.33 ? 3024 ASP A CA    1 
ATOM   10999 C C     . ASP A 1 3024 ? 140.280 186.110 139.745 1.00 163.33 ? 3024 ASP A C     1 
ATOM   11000 O O     . ASP A 1 3024 ? 139.166 186.026 139.217 1.00 163.33 ? 3024 ASP A O     1 
ATOM   11001 C CB    . ASP A 1 3024 ? 142.160 186.978 138.338 1.00 163.33 ? 3024 ASP A CB    1 
ATOM   11002 C CG    . ASP A 1 3024 ? 143.396 186.261 138.836 1.00 163.33 ? 3024 ASP A CG    1 
ATOM   11003 O OD1   . ASP A 1 3024 ? 143.326 185.634 139.914 1.00 163.33 ? 3024 ASP A OD1   1 
ATOM   11004 O OD2   . ASP A 1 3024 ? 144.435 186.315 138.146 1.00 163.33 ? 3024 ASP A OD2   1 
ATOM   11005 N N     . GLU A 1 3025 ? 140.752 185.167 140.562 1.00 161.32 ? 3025 GLU A N     1 
ATOM   11006 C CA    . GLU A 1 3025 ? 139.928 184.012 140.900 1.00 161.32 ? 3025 GLU A CA    1 
ATOM   11007 C C     . GLU A 1 3025 ? 138.655 184.445 141.612 1.00 161.32 ? 3025 GLU A C     1 
ATOM   11008 O O     . GLU A 1 3025 ? 137.568 183.915 141.345 1.00 161.32 ? 3025 GLU A O     1 
ATOM   11009 C CB    . GLU A 1 3025 ? 140.725 183.035 141.765 1.00 161.32 ? 3025 GLU A CB    1 
ATOM   11010 C CG    . GLU A 1 3025 ? 142.181 182.861 141.346 1.00 161.32 ? 3025 GLU A CG    1 
ATOM   11011 C CD    . GLU A 1 3025 ? 142.340 182.413 139.902 1.00 161.32 ? 3025 GLU A CD    1 
ATOM   11012 O OE1   . GLU A 1 3025 ? 141.435 181.727 139.380 1.00 161.32 ? 3025 GLU A OE1   1 
ATOM   11013 O OE2   . GLU A 1 3025 ? 143.376 182.746 139.289 1.00 161.32 ? 3025 GLU A OE2   1 
ATOM   11014 N N     . TYR A 1 3026 ? 138.769 185.414 142.520 1.00 156.06 ? 3026 TYR A N     1 
ATOM   11015 C CA    . TYR A 1 3026 ? 137.594 185.907 143.225 1.00 156.06 ? 3026 TYR A CA    1 
ATOM   11016 C C     . TYR A 1 3026 ? 136.614 186.576 142.267 1.00 156.06 ? 3026 TYR A C     1 
ATOM   11017 O O     . TYR A 1 3026 ? 135.400 186.379 142.381 1.00 156.06 ? 3026 TYR A O     1 
ATOM   11018 C CB    . TYR A 1 3026 ? 138.026 186.859 144.339 1.00 156.06 ? 3026 TYR A CB    1 
ATOM   11019 C CG    . TYR A 1 3026 ? 136.922 187.233 145.295 1.00 156.06 ? 3026 TYR A CG    1 
ATOM   11020 C CD1   . TYR A 1 3026 ? 136.430 186.315 146.209 1.00 156.06 ? 3026 TYR A CD1   1 
ATOM   11021 C CD2   . TYR A 1 3026 ? 136.398 188.516 145.310 1.00 156.06 ? 3026 TYR A CD2   1 
ATOM   11022 C CE1   . TYR A 1 3026 ? 135.425 186.655 147.092 1.00 156.06 ? 3026 TYR A CE1   1 
ATOM   11023 C CE2   . TYR A 1 3026 ? 135.400 188.869 146.194 1.00 156.06 ? 3026 TYR A CE2   1 
ATOM   11024 C CZ    . TYR A 1 3026 ? 134.914 187.934 147.080 1.00 156.06 ? 3026 TYR A CZ    1 
ATOM   11025 O OH    . TYR A 1 3026 ? 133.917 188.281 147.960 1.00 156.06 ? 3026 TYR A OH    1 
ATOM   11026 N N     . ALA A 1 3027 ? 137.119 187.354 141.306 1.00 159.78 ? 3027 ALA A N     1 
ATOM   11027 C CA    . ALA A 1 3027 ? 136.238 187.969 140.316 1.00 159.78 ? 3027 ALA A CA    1 
ATOM   11028 C C     . ALA A 1 3027 ? 135.558 186.918 139.446 1.00 159.78 ? 3027 ALA A C     1 
ATOM   11029 O O     . ALA A 1 3027 ? 134.382 187.059 139.082 1.00 159.78 ? 3027 ALA A O     1 
ATOM   11030 C CB    . ALA A 1 3027 ? 137.025 188.953 139.452 1.00 159.78 ? 3027 ALA A CB    1 
ATOM   11031 N N     . THR A 1 3028 ? 136.287 185.861 139.087 1.00 158.37 ? 3028 THR A N     1 
ATOM   11032 C CA    . THR A 1 3028 ? 135.675 184.786 138.317 1.00 158.37 ? 3028 THR A CA    1 
ATOM   11033 C C     . THR A 1 3028 ? 134.576 184.101 139.116 1.00 158.37 ? 3028 THR A C     1 
ATOM   11034 O O     . THR A 1 3028 ? 133.535 183.734 138.561 1.00 158.37 ? 3028 THR A O     1 
ATOM   11035 C CB    . THR A 1 3028 ? 136.732 183.775 137.877 1.00 158.37 ? 3028 THR A CB    1 
ATOM   11036 O OG1   . THR A 1 3028 ? 137.487 183.344 139.015 1.00 158.37 ? 3028 THR A OG1   1 
ATOM   11037 C CG2   . THR A 1 3028 ? 137.667 184.395 136.849 1.00 158.37 ? 3028 THR A CG2   1 
ATOM   11038 N N     . LEU A 1 3029 ? 134.790 183.909 140.421 1.00 157.52 ? 3029 LEU A N     1 
ATOM   11039 C CA    . LEU A 1 3029 ? 133.719 183.379 141.263 1.00 157.52 ? 3029 LEU A CA    1 
ATOM   11040 C C     . LEU A 1 3029 ? 132.530 184.329 141.283 1.00 157.52 ? 3029 LEU A C     1 
ATOM   11041 O O     . LEU A 1 3029 ? 131.376 183.894 141.234 1.00 157.52 ? 3029 LEU A O     1 
ATOM   11042 C CB    . LEU A 1 3029 ? 134.219 183.106 142.685 1.00 157.52 ? 3029 LEU A CB    1 
ATOM   11043 C CG    . LEU A 1 3029 ? 133.211 182.406 143.614 1.00 157.52 ? 3029 LEU A CG    1 
ATOM   11044 C CD1   . LEU A 1 3029 ? 133.926 181.558 144.640 1.00 157.52 ? 3029 LEU A CD1   1 
ATOM   11045 C CD2   . LEU A 1 3029 ? 132.301 183.393 144.340 1.00 157.52 ? 3029 LEU A CD2   1 
ATOM   11046 N N     . MET A 1 3030 ? 132.799 185.634 141.371 1.00 161.20 ? 3030 MET A N     1 
ATOM   11047 C CA    . MET A 1 3030 ? 131.731 186.626 141.291 1.00 161.20 ? 3030 MET A CA    1 
ATOM   11048 C C     . MET A 1 3030 ? 130.882 186.393 140.048 1.00 161.20 ? 3030 MET A C     1 
ATOM   11049 O O     . MET A 1 3030 ? 129.653 186.259 140.132 1.00 161.20 ? 3030 MET A O     1 
ATOM   11050 C CB    . MET A 1 3030 ? 132.332 188.032 141.221 1.00 161.20 ? 3030 MET A CB    1 
ATOM   11051 C CG    . MET A 1 3030 ? 133.176 188.548 142.399 1.00 161.20 ? 3030 MET A CG    1 
ATOM   11052 S SD    . MET A 1 3030 ? 133.210 187.729 144.006 1.00 161.20 ? 3030 MET A SD    1 
ATOM   11053 C CE    . MET A 1 3030 ? 131.507 187.850 144.512 1.00 161.20 ? 3030 MET A CE    1 
ATOM   11054 N N     . THR A 1 3031 ? 131.542 186.290 138.893 1.00 160.75 ? 3031 THR A N     1 
ATOM   11055 C CA    . THR A 1 3031 ? 130.835 186.182 137.620 1.00 160.75 ? 3031 THR A CA    1 
ATOM   11056 C C     . THR A 1 3031 ? 130.069 184.869 137.519 1.00 160.75 ? 3031 THR A C     1 
ATOM   11057 O O     . THR A 1 3031 ? 128.884 184.852 137.160 1.00 160.75 ? 3031 THR A O     1 
ATOM   11058 C CB    . THR A 1 3031 ? 131.826 186.310 136.464 1.00 160.75 ? 3031 THR A CB    1 
ATOM   11059 O OG1   . THR A 1 3031 ? 132.764 187.354 136.751 1.00 160.75 ? 3031 THR A OG1   1 
ATOM   11060 C CG2   . THR A 1 3031 ? 131.095 186.629 135.172 1.00 160.75 ? 3031 THR A CG2   1 
ATOM   11061 N N     . GLN A 1 3032 ? 130.734 183.754 137.825 1.00 162.51 ? 3032 GLN A N     1 
ATOM   11062 C CA    . GLN A 1 3032 ? 130.087 182.454 137.694 1.00 162.51 ? 3032 GLN A CA    1 
ATOM   11063 C C     . GLN A 1 3032 ? 128.933 182.300 138.672 1.00 162.51 ? 3032 GLN A C     1 
ATOM   11064 O O     . GLN A 1 3032 ? 127.902 181.714 138.324 1.00 162.51 ? 3032 GLN A O     1 
ATOM   11065 C CB    . GLN A 1 3032 ? 131.103 181.329 137.890 1.00 162.51 ? 3032 GLN A CB    1 
ATOM   11066 C CG    . GLN A 1 3032 ? 132.318 181.399 136.971 1.00 162.51 ? 3032 GLN A CG    1 
ATOM   11067 C CD    . GLN A 1 3032 ? 132.030 182.098 135.656 1.00 162.51 ? 3032 GLN A CD    1 
ATOM   11068 O OE1   . GLN A 1 3032 ? 132.470 183.226 135.432 1.00 162.51 ? 3032 GLN A OE1   1 
ATOM   11069 N NE2   . GLN A 1 3032 ? 131.295 181.428 134.775 1.00 162.51 ? 3032 GLN A NE2   1 
ATOM   11070 N N     . CYS A 1 3033 ? 129.070 182.826 139.890 1.00 160.72 ? 3033 CYS A N     1 
ATOM   11071 C CA    . CYS A 1 3033 ? 127.986 182.718 140.852 1.00 160.72 ? 3033 CYS A CA    1 
ATOM   11072 C C     . CYS A 1 3033 ? 126.828 183.634 140.479 1.00 160.72 ? 3033 CYS A C     1 
ATOM   11073 O O     . CYS A 1 3033 ? 125.667 183.303 140.737 1.00 160.72 ? 3033 CYS A O     1 
ATOM   11074 C CB    . CYS A 1 3033 ? 128.505 183.030 142.251 1.00 160.72 ? 3033 CYS A CB    1 
ATOM   11075 S SG    . CYS A 1 3033 ? 129.321 181.644 143.065 1.00 160.72 ? 3033 CYS A SG    1 
ATOM   11076 N N     . LYS A 1 3034 ? 127.113 184.781 139.856 1.00 161.93 ? 3034 LYS A N     1 
ATOM   11077 C CA    . LYS A 1 3034 ? 126.025 185.602 139.334 1.00 161.93 ? 3034 LYS A CA    1 
ATOM   11078 C C     . LYS A 1 3034 ? 125.294 184.879 138.208 1.00 161.93 ? 3034 LYS A C     1 
ATOM   11079 O O     . LYS A 1 3034 ? 124.059 184.930 138.119 1.00 161.93 ? 3034 LYS A O     1 
ATOM   11080 C CB    . LYS A 1 3034 ? 126.563 186.956 138.868 1.00 161.93 ? 3034 LYS A CB    1 
ATOM   11081 C CG    . LYS A 1 3034 ? 125.821 187.564 137.690 1.00 161.93 ? 3034 LYS A CG    1 
ATOM   11082 C CD    . LYS A 1 3034 ? 126.460 188.873 137.249 1.00 161.93 ? 3034 LYS A CD    1 
ATOM   11083 C CE    . LYS A 1 3034 ? 127.958 188.731 137.057 1.00 161.93 ? 3034 LYS A CE    1 
ATOM   11084 N NZ    . LYS A 1 3034 ? 128.585 190.029 136.688 1.00 161.93 ? 3034 LYS A NZ    1 
ATOM   11085 N N     . GLU A 1 3035 ? 126.044 184.187 137.348 1.00 162.79 ? 3035 GLU A N     1 
ATOM   11086 C CA    . GLU A 1 3035 ? 125.423 183.382 136.300 1.00 162.79 ? 3035 GLU A CA    1 
ATOM   11087 C C     . GLU A 1 3035 ? 124.544 182.292 136.901 1.00 162.79 ? 3035 GLU A C     1 
ATOM   11088 O O     . GLU A 1 3035 ? 123.426 182.049 136.436 1.00 162.79 ? 3035 GLU A O     1 
ATOM   11089 C CB    . GLU A 1 3035 ? 126.500 182.772 135.405 1.00 162.79 ? 3035 GLU A CB    1 
ATOM   11090 C CG    . GLU A 1 3035 ? 127.289 183.787 134.601 1.00 162.79 ? 3035 GLU A CG    1 
ATOM   11091 C CD    . GLU A 1 3035 ? 128.168 183.138 133.552 1.00 162.79 ? 3035 GLU A CD    1 
ATOM   11092 O OE1   . GLU A 1 3035 ? 127.982 181.933 133.283 1.00 162.79 ? 3035 GLU A OE1   1 
ATOM   11093 O OE2   . GLU A 1 3035 ? 129.050 183.830 133.002 1.00 162.79 ? 3035 GLU A OE2   1 
ATOM   11094 N N     . GLY A 1 3036 ? 125.037 181.627 137.945 1.00 165.29 ? 3036 GLY A N     1 
ATOM   11095 C CA    . GLY A 1 3036 ? 124.241 180.602 138.601 1.00 165.29 ? 3036 GLY A CA    1 
ATOM   11096 C C     . GLY A 1 3036 ? 122.999 181.163 139.268 1.00 165.29 ? 3036 GLY A C     1 
ATOM   11097 O O     . GLY A 1 3036 ? 121.941 180.529 139.265 1.00 165.29 ? 3036 GLY A O     1 
ATOM   11098 N N     . ALA A 1 3037 ? 123.112 182.356 139.854 1.00 166.47 ? 3037 ALA A N     1 
ATOM   11099 C CA    . ALA A 1 3037 ? 121.955 182.993 140.472 1.00 166.47 ? 3037 ALA A CA    1 
ATOM   11100 C C     . ALA A 1 3037 ? 120.900 183.343 139.435 1.00 166.47 ? 3037 ALA A C     1 
ATOM   11101 O O     . ALA A 1 3037 ? 119.701 183.144 139.667 1.00 166.47 ? 3037 ALA A O     1 
ATOM   11102 C CB    . ALA A 1 3037 ? 122.390 184.241 141.237 1.00 166.47 ? 3037 ALA A CB    1 
ATOM   11103 N N     . GLN A 1 3038 ? 121.322 183.865 138.279 1.00 168.14 ? 3038 GLN A N     1 
ATOM   11104 C CA    . GLN A 1 3038 ? 120.339 184.198 137.253 1.00 168.14 ? 3038 GLN A CA    1 
ATOM   11105 C C     . GLN A 1 3038 ? 119.762 182.945 136.605 1.00 168.14 ? 3038 GLN A C     1 
ATOM   11106 O O     . GLN A 1 3038 ? 118.611 182.960 136.155 1.00 168.14 ? 3038 GLN A O     1 
ATOM   11107 C CB    . GLN A 1 3038 ? 120.943 185.126 136.196 1.00 168.14 ? 3038 GLN A CB    1 
ATOM   11108 C CG    . GLN A 1 3038 ? 121.955 184.491 135.267 1.00 168.14 ? 3038 GLN A CG    1 
ATOM   11109 C CD    . GLN A 1 3038 ? 122.677 185.517 134.415 1.00 168.14 ? 3038 GLN A CD    1 
ATOM   11110 O OE1   . GLN A 1 3038 ? 123.904 185.616 134.441 1.00 168.14 ? 3038 GLN A OE1   1 
ATOM   11111 N NE2   . GLN A 1 3038 ? 121.913 186.293 133.656 1.00 168.14 ? 3038 GLN A NE2   1 
ATOM   11112 N N     . LYS A 1 3039 ? 120.536 181.856 136.548 1.00 168.12 ? 3039 LYS A N     1 
ATOM   11113 C CA    . LYS A 1 3039 ? 119.978 180.584 136.097 1.00 168.12 ? 3039 LYS A CA    1 
ATOM   11114 C C     . LYS A 1 3039 ? 118.928 180.069 137.072 1.00 168.12 ? 3039 LYS A C     1 
ATOM   11115 O O     . LYS A 1 3039 ? 117.866 179.590 136.657 1.00 168.12 ? 3039 LYS A O     1 
ATOM   11116 C CB    . LYS A 1 3039 ? 121.085 179.541 135.925 1.00 168.12 ? 3039 LYS A CB    1 
ATOM   11117 C CG    . LYS A 1 3039 ? 122.059 179.781 134.779 1.00 168.12 ? 3039 LYS A CG    1 
ATOM   11118 C CD    . LYS A 1 3039 ? 121.494 180.687 133.704 1.00 168.12 ? 3039 LYS A CD    1 
ATOM   11119 C CE    . LYS A 1 3039 ? 122.543 180.974 132.646 1.00 168.12 ? 3039 LYS A CE    1 
ATOM   11120 N NZ    . LYS A 1 3039 ? 123.771 181.565 133.245 1.00 168.12 ? 3039 LYS A NZ    1 
ATOM   11121 N N     . GLU A 1 3040 ? 119.209 180.158 138.374 1.00 173.69 ? 3040 GLU A N     1 
ATOM   11122 C CA    . GLU A 1 3040 ? 118.286 179.633 139.372 1.00 173.69 ? 3040 GLU A CA    1 
ATOM   11123 C C     . GLU A 1 3040 ? 117.068 180.528 139.540 1.00 173.69 ? 3040 GLU A C     1 
ATOM   11124 O O     . GLU A 1 3040 ? 115.999 180.049 139.935 1.00 173.69 ? 3040 GLU A O     1 
ATOM   11125 C CB    . GLU A 1 3040 ? 119.005 179.466 140.709 1.00 173.69 ? 3040 GLU A CB    1 
ATOM   11126 C CG    . GLU A 1 3040 ? 118.433 178.371 141.594 1.00 173.69 ? 3040 GLU A CG    1 
ATOM   11127 C CD    . GLU A 1 3040 ? 117.297 178.861 142.468 1.00 173.69 ? 3040 GLU A CD    1 
ATOM   11128 O OE1   . GLU A 1 3040 ? 117.143 180.092 142.609 1.00 173.69 ? 3040 GLU A OE1   1 
ATOM   11129 O OE2   . GLU A 1 3040 ? 116.562 178.014 143.016 1.00 173.69 ? 3040 GLU A OE2   1 
ATOM   11130 N N     . GLY A 1 3041 ? 117.204 181.817 139.252 1.00 178.96 ? 3041 GLY A N     1 
ATOM   11131 C CA    . GLY A 1 3041 ? 116.103 182.741 139.426 1.00 178.96 ? 3041 GLY A CA    1 
ATOM   11132 C C     . GLY A 1 3041 ? 116.278 183.621 140.644 1.00 178.96 ? 3041 GLY A C     1 
ATOM   11133 O O     . GLY A 1 3041 ? 115.315 183.899 141.365 1.00 178.96 ? 3041 GLY A O     1 
ATOM   11134 N N     . LEU A 1 3042 ? 117.508 184.062 140.884 1.00 180.03 ? 3042 LEU A N     1 
ATOM   11135 C CA    . LEU A 1 3042 ? 117.831 184.903 142.023 1.00 180.03 ? 3042 LEU A CA    1 
ATOM   11136 C C     . LEU A 1 3042 ? 118.588 186.141 141.562 1.00 180.03 ? 3042 LEU A C     1 
ATOM   11137 O O     . LEU A 1 3042 ? 119.315 186.112 140.564 1.00 180.03 ? 3042 LEU A O     1 
ATOM   11138 C CB    . LEU A 1 3042 ? 118.665 184.139 143.058 1.00 180.03 ? 3042 LEU A CB    1 
ATOM   11139 C CG    . LEU A 1 3042 ? 117.922 183.106 143.906 1.00 180.03 ? 3042 LEU A CG    1 
ATOM   11140 C CD1   . LEU A 1 3042 ? 118.804 182.627 145.045 1.00 180.03 ? 3042 LEU A CD1   1 
ATOM   11141 C CD2   . LEU A 1 3042 ? 116.624 183.684 144.441 1.00 180.03 ? 3042 LEU A CD2   1 
ATOM   11142 N N     . MET A 1 3043 ? 118.404 187.230 142.301 1.00 184.72 ? 3043 MET A N     1 
ATOM   11143 C CA    . MET A 1 3043 ? 119.112 188.471 142.030 1.00 184.72 ? 3043 MET A CA    1 
ATOM   11144 C C     . MET A 1 3043 ? 120.498 188.438 142.662 1.00 184.72 ? 3043 MET A C     1 
ATOM   11145 O O     . MET A 1 3043 ? 120.720 187.776 143.679 1.00 184.72 ? 3043 MET A O     1 
ATOM   11146 C CB    . MET A 1 3043 ? 118.315 189.670 142.549 1.00 184.72 ? 3043 MET A CB    1 
ATOM   11147 C CG    . MET A 1 3043 ? 117.833 189.557 143.992 1.00 184.72 ? 3043 MET A CG    1 
ATOM   11148 S SD    . MET A 1 3043 ? 116.989 188.019 144.422 1.00 184.72 ? 3043 MET A SD    1 
ATOM   11149 C CE    . MET A 1 3043 ? 115.590 188.056 143.297 1.00 184.72 ? 3043 MET A CE    1 
ATOM   11150 N N     . LEU A 1 3044 ? 121.438 189.162 142.047 1.00 180.10 ? 3044 LEU A N     1 
ATOM   11151 C CA    . LEU A 1 3044 ? 122.837 189.054 142.452 1.00 180.10 ? 3044 LEU A CA    1 
ATOM   11152 C C     . LEU A 1 3044 ? 123.184 190.013 143.585 1.00 180.10 ? 3044 LEU A C     1 
ATOM   11153 O O     . LEU A 1 3044 ? 124.032 189.689 144.424 1.00 180.10 ? 3044 LEU A O     1 
ATOM   11154 C CB    . LEU A 1 3044 ? 123.743 189.278 141.237 1.00 180.10 ? 3044 LEU A CB    1 
ATOM   11155 C CG    . LEU A 1 3044 ? 123.959 190.689 140.682 1.00 180.10 ? 3044 LEU A CG    1 
ATOM   11156 C CD1   . LEU A 1 3044 ? 125.244 191.300 141.221 1.00 180.10 ? 3044 LEU A CD1   1 
ATOM   11157 C CD2   . LEU A 1 3044 ? 123.958 190.678 139.161 1.00 180.10 ? 3044 LEU A CD2   1 
ATOM   11158 N N     . ASP A 1 3045 ? 122.548 191.186 143.629 1.00 180.34 ? 3045 ASP A N     1 
ATOM   11159 C CA    . ASP A 1 3045 ? 122.744 192.185 144.687 1.00 180.34 ? 3045 ASP A CA    1 
ATOM   11160 C C     . ASP A 1 3045 ? 124.217 192.571 144.721 1.00 180.34 ? 3045 ASP A C     1 
ATOM   11161 O O     . ASP A 1 3045 ? 124.714 193.124 143.724 1.00 180.34 ? 3045 ASP A O     1 
ATOM   11162 C CB    . ASP A 1 3045 ? 122.178 191.645 146.001 1.00 180.34 ? 3045 ASP A CB    1 
ATOM   11163 C CG    . ASP A 1 3045 ? 120.767 191.133 145.855 1.00 180.34 ? 3045 ASP A CG    1 
ATOM   11164 O OD1   . ASP A 1 3045 ? 120.598 190.046 145.270 1.00 180.34 ? 3045 ASP A OD1   1 
ATOM   11165 O OD2   . ASP A 1 3045 ? 119.831 191.815 146.321 1.00 180.34 ? 3045 ASP A OD2   1 
ATOM   11166 N N     . SER A 1 3046 ? 124.938 192.332 145.809 1.00 166.88 ? 3046 SER A N     1 
ATOM   11167 C CA    . SER A 1 3046 ? 126.340 192.693 145.937 1.00 166.88 ? 3046 SER A CA    1 
ATOM   11168 C C     . SER A 1 3046 ? 127.190 191.437 146.084 1.00 166.88 ? 3046 SER A C     1 
ATOM   11169 O O     . SER A 1 3046 ? 126.701 190.307 145.996 1.00 166.88 ? 3046 SER A O     1 
ATOM   11170 C CB    . SER A 1 3046 ? 126.544 193.634 147.124 1.00 166.88 ? 3046 SER A CB    1 
ATOM   11171 O OG    . SER A 1 3046 ? 126.463 192.924 148.347 1.00 166.88 ? 3046 SER A OG    1 
ATOM   11172 N N     . HIS A 1 3047 ? 128.486 191.649 146.314 1.00 160.10 ? 3047 HIS A N     1 
ATOM   11173 C CA    . HIS A 1 3047 ? 129.410 190.527 146.439 1.00 160.10 ? 3047 HIS A CA    1 
ATOM   11174 C C     . HIS A 1 3047 ? 129.094 189.672 147.659 1.00 160.10 ? 3047 HIS A C     1 
ATOM   11175 O O     . HIS A 1 3047 ? 129.165 188.441 147.592 1.00 160.10 ? 3047 HIS A O     1 
ATOM   11176 C CB    . HIS A 1 3047 ? 130.848 191.038 146.498 1.00 160.10 ? 3047 HIS A CB    1 
ATOM   11177 C CG    . HIS A 1 3047 ? 131.403 191.427 145.164 1.00 160.10 ? 3047 HIS A CG    1 
ATOM   11178 N ND1   . HIS A 1 3047 ? 130.603 191.777 144.098 1.00 160.10 ? 3047 HIS A ND1   1 
ATOM   11179 C CD2   . HIS A 1 3047 ? 132.679 191.512 144.719 1.00 160.10 ? 3047 HIS A CD2   1 
ATOM   11180 C CE1   . HIS A 1 3047 ? 131.361 192.065 143.056 1.00 160.10 ? 3047 HIS A CE1   1 
ATOM   11181 N NE2   . HIS A 1 3047 ? 132.626 191.911 143.406 1.00 160.10 ? 3047 HIS A NE2   1 
ATOM   11182 N N     . GLU A 1 3048 ? 128.744 190.304 148.781 1.00 163.67 ? 3048 GLU A N     1 
ATOM   11183 C CA    . GLU A 1 3048 ? 128.558 189.556 150.022 1.00 163.67 ? 3048 GLU A CA    1 
ATOM   11184 C C     . GLU A 1 3048 ? 127.325 188.660 149.966 1.00 163.67 ? 3048 GLU A C     1 
ATOM   11185 O O     . GLU A 1 3048 ? 127.365 187.514 150.428 1.00 163.67 ? 3048 GLU A O     1 
ATOM   11186 C CB    . GLU A 1 3048 ? 128.520 190.528 151.210 1.00 163.67 ? 3048 GLU A CB    1 
ATOM   11187 C CG    . GLU A 1 3048 ? 127.402 191.580 151.225 1.00 163.67 ? 3048 GLU A CG    1 
ATOM   11188 C CD    . GLU A 1 3048 ? 126.033 191.051 151.618 1.00 163.67 ? 3048 GLU A CD    1 
ATOM   11189 O OE1   . GLU A 1 3048 ? 125.933 189.894 152.073 1.00 163.67 ? 3048 GLU A OE1   1 
ATOM   11190 O OE2   . GLU A 1 3048 ? 125.049 191.804 151.464 1.00 163.67 ? 3048 GLU A OE2   1 
ATOM   11191 N N     . GLU A 1 3049 ? 126.224 189.152 149.397 1.00 161.01 ? 3049 GLU A N     1 
ATOM   11192 C CA    . GLU A 1 3049 ? 125.022 188.329 149.303 1.00 161.01 ? 3049 GLU A CA    1 
ATOM   11193 C C     . GLU A 1 3049 ? 125.233 187.156 148.357 1.00 161.01 ? 3049 GLU A C     1 
ATOM   11194 O O     . GLU A 1 3049 ? 124.791 186.033 148.634 1.00 161.01 ? 3049 GLU A O     1 
ATOM   11195 C CB    . GLU A 1 3049 ? 123.839 189.179 148.849 1.00 161.01 ? 3049 GLU A CB    1 
ATOM   11196 C CG    . GLU A 1 3049 ? 122.987 189.714 149.984 1.00 161.01 ? 3049 GLU A CG    1 
ATOM   11197 C CD    . GLU A 1 3049 ? 122.503 188.620 150.913 1.00 161.01 ? 3049 GLU A CD    1 
ATOM   11198 O OE1   . GLU A 1 3049 ? 123.245 188.252 151.849 1.00 161.01 ? 3049 GLU A OE1   1 
ATOM   11199 O OE2   . GLU A 1 3049 ? 121.379 188.120 150.703 1.00 161.01 ? 3049 GLU A OE2   1 
ATOM   11200 N N     . LEU A 1 3050 ? 125.911 187.398 147.237 1.00 156.71 ? 3050 LEU A N     1 
ATOM   11201 C CA    . LEU A 1 3050 ? 126.174 186.319 146.296 1.00 156.71 ? 3050 LEU A CA    1 
ATOM   11202 C C     . LEU A 1 3050 ? 127.119 185.294 146.910 1.00 156.71 ? 3050 LEU A C     1 
ATOM   11203 O O     . LEU A 1 3050 ? 126.981 184.090 146.672 1.00 156.71 ? 3050 LEU A O     1 
ATOM   11204 C CB    . LEU A 1 3050 ? 126.744 186.894 145.000 1.00 156.71 ? 3050 LEU A CB    1 
ATOM   11205 C CG    . LEU A 1 3050 ? 127.444 185.961 144.012 1.00 156.71 ? 3050 LEU A CG    1 
ATOM   11206 C CD1   . LEU A 1 3050 ? 127.242 186.493 142.601 1.00 156.71 ? 3050 LEU A CD1   1 
ATOM   11207 C CD2   . LEU A 1 3050 ? 128.917 185.763 144.305 1.00 156.71 ? 3050 LEU A CD2   1 
ATOM   11208 N N     . TYR A 1 3051 ? 128.092 185.754 147.700 1.00 148.95 ? 3051 TYR A N     1 
ATOM   11209 C CA    . TYR A 1 3051 ? 128.978 184.832 148.404 1.00 148.95 ? 3051 TYR A CA    1 
ATOM   11210 C C     . TYR A 1 3051 ? 128.214 184.013 149.438 1.00 148.95 ? 3051 TYR A C     1 
ATOM   11211 O O     . TYR A 1 3051 ? 128.498 182.825 149.630 1.00 148.95 ? 3051 TYR A O     1 
ATOM   11212 C CB    . TYR A 1 3051 ? 130.117 185.603 149.067 1.00 148.95 ? 3051 TYR A CB    1 
ATOM   11213 C CG    . TYR A 1 3051 ? 131.374 184.789 149.264 1.00 148.95 ? 3051 TYR A CG    1 
ATOM   11214 C CD1   . TYR A 1 3051 ? 132.222 184.520 148.199 1.00 148.95 ? 3051 TYR A CD1   1 
ATOM   11215 C CD2   . TYR A 1 3051 ? 131.714 184.292 150.515 1.00 148.95 ? 3051 TYR A CD2   1 
ATOM   11216 C CE1   . TYR A 1 3051 ? 133.374 183.778 148.373 1.00 148.95 ? 3051 TYR A CE1   1 
ATOM   11217 C CE2   . TYR A 1 3051 ? 132.865 183.548 150.698 1.00 148.95 ? 3051 TYR A CE2   1 
ATOM   11218 C CZ    . TYR A 1 3051 ? 133.691 183.294 149.623 1.00 148.95 ? 3051 TYR A CZ    1 
ATOM   11219 O OH    . TYR A 1 3051 ? 134.838 182.554 149.797 1.00 148.95 ? 3051 TYR A OH    1 
ATOM   11220 N N     . LYS A 1 3052 ? 127.251 184.632 150.122 1.00 147.63 ? 3052 LYS A N     1 
ATOM   11221 C CA    . LYS A 1 3052 ? 126.411 183.884 151.052 1.00 147.63 ? 3052 LYS A CA    1 
ATOM   11222 C C     . LYS A 1 3052 ? 125.613 182.807 150.325 1.00 147.63 ? 3052 LYS A C     1 
ATOM   11223 O O     . LYS A 1 3052 ? 125.513 181.666 150.797 1.00 147.63 ? 3052 LYS A O     1 
ATOM   11224 C CB    . LYS A 1 3052 ? 125.478 184.841 151.792 1.00 147.63 ? 3052 LYS A CB    1 
ATOM   11225 C CG    . LYS A 1 3052 ? 124.628 184.183 152.861 1.00 147.63 ? 3052 LYS A CG    1 
ATOM   11226 C CD    . LYS A 1 3052 ? 124.491 185.081 154.080 1.00 147.63 ? 3052 LYS A CD    1 
ATOM   11227 C CE    . LYS A 1 3052 ? 125.847 185.398 154.688 1.00 147.63 ? 3052 LYS A CE    1 
ATOM   11228 N NZ    . LYS A 1 3052 ? 125.751 186.412 155.774 1.00 147.63 ? 3052 LYS A NZ    1 
ATOM   11229 N N     . TRP A 1 3053 ? 125.046 183.152 149.167 1.00 144.23 ? 3053 TRP A N     1 
ATOM   11230 C CA    . TRP A 1 3053 ? 124.334 182.160 148.364 1.00 144.23 ? 3053 TRP A CA    1 
ATOM   11231 C C     . TRP A 1 3053 ? 125.268 181.044 147.909 1.00 144.23 ? 3053 TRP A C     1 
ATOM   11232 O O     . TRP A 1 3053 ? 124.884 179.870 147.890 1.00 144.23 ? 3053 TRP A O     1 
ATOM   11233 C CB    . TRP A 1 3053 ? 123.679 182.836 147.162 1.00 144.23 ? 3053 TRP A CB    1 
ATOM   11234 C CG    . TRP A 1 3053 ? 123.230 181.887 146.094 1.00 144.23 ? 3053 TRP A CG    1 
ATOM   11235 C CD1   . TRP A 1 3053 ? 122.044 181.219 146.035 1.00 144.23 ? 3053 TRP A CD1   1 
ATOM   11236 C CD2   . TRP A 1 3053 ? 123.962 181.510 144.922 1.00 144.23 ? 3053 TRP A CD2   1 
ATOM   11237 N NE1   . TRP A 1 3053 ? 121.993 180.445 144.901 1.00 144.23 ? 3053 TRP A NE1   1 
ATOM   11238 C CE2   . TRP A 1 3053 ? 123.160 180.607 144.201 1.00 144.23 ? 3053 TRP A CE2   1 
ATOM   11239 C CE3   . TRP A 1 3053 ? 125.220 181.847 144.416 1.00 144.23 ? 3053 TRP A CE3   1 
ATOM   11240 C CZ2   . TRP A 1 3053 ? 123.574 180.037 143.002 1.00 144.23 ? 3053 TRP A CZ2   1 
ATOM   11241 C CZ3   . TRP A 1 3053 ? 125.628 181.281 143.227 1.00 144.23 ? 3053 TRP A CZ3   1 
ATOM   11242 C CH2   . TRP A 1 3053 ? 124.808 180.386 142.532 1.00 144.23 ? 3053 TRP A CH2   1 
ATOM   11243 N N     . PHE A 1 3054 ? 126.497 181.398 147.528 1.00 137.57 ? 3054 PHE A N     1 
ATOM   11244 C CA    . PHE A 1 3054 ? 127.482 180.399 147.127 1.00 137.57 ? 3054 PHE A CA    1 
ATOM   11245 C C     . PHE A 1 3054 ? 127.799 179.445 148.270 1.00 137.57 ? 3054 PHE A C     1 
ATOM   11246 O O     . PHE A 1 3054 ? 127.906 178.229 148.068 1.00 137.57 ? 3054 PHE A O     1 
ATOM   11247 C CB    . PHE A 1 3054 ? 128.747 181.103 146.643 1.00 137.57 ? 3054 PHE A CB    1 
ATOM   11248 C CG    . PHE A 1 3054 ? 129.959 180.223 146.602 1.00 137.57 ? 3054 PHE A CG    1 
ATOM   11249 C CD1   . PHE A 1 3054 ? 130.152 179.336 145.562 1.00 137.57 ? 3054 PHE A CD1   1 
ATOM   11250 C CD2   . PHE A 1 3054 ? 130.912 180.292 147.602 1.00 137.57 ? 3054 PHE A CD2   1 
ATOM   11251 C CE1   . PHE A 1 3054 ? 131.271 178.533 145.519 1.00 137.57 ? 3054 PHE A CE1   1 
ATOM   11252 C CE2   . PHE A 1 3054 ? 132.029 179.492 147.565 1.00 137.57 ? 3054 PHE A CE2   1 
ATOM   11253 C CZ    . PHE A 1 3054 ? 132.210 178.611 146.523 1.00 137.57 ? 3054 PHE A CZ    1 
ATOM   11254 N N     . THR A 1 3055 ? 127.960 179.982 149.480 1.00 140.11 ? 3055 THR A N     1 
ATOM   11255 C CA    . THR A 1 3055 ? 128.210 179.130 150.636 1.00 140.11 ? 3055 THR A CA    1 
ATOM   11256 C C     . THR A 1 3055 ? 127.031 178.208 150.897 1.00 140.11 ? 3055 THR A C     1 
ATOM   11257 O O     . THR A 1 3055 ? 127.214 177.029 151.223 1.00 140.11 ? 3055 THR A O     1 
ATOM   11258 C CB    . THR A 1 3055 ? 128.493 179.977 151.873 1.00 140.11 ? 3055 THR A CB    1 
ATOM   11259 O OG1   . THR A 1 3055 ? 127.563 181.063 151.929 1.00 140.11 ? 3055 THR A OG1   1 
ATOM   11260 C CG2   . THR A 1 3055 ? 129.895 180.539 151.812 1.00 140.11 ? 3055 THR A CG2   1 
ATOM   11261 N N     . SER A 1 3056 ? 125.809 178.731 150.772 1.00 135.19 ? 3056 SER A N     1 
ATOM   11262 C CA    . SER A 1 3056 ? 124.634 177.884 150.951 1.00 135.19 ? 3056 SER A CA    1 
ATOM   11263 C C     . SER A 1 3056 ? 124.609 176.762 149.921 1.00 135.19 ? 3056 SER A C     1 
ATOM   11264 O O     . SER A 1 3056 ? 124.318 175.606 150.254 1.00 135.19 ? 3056 SER A O     1 
ATOM   11265 C CB    . SER A 1 3056 ? 123.363 178.723 150.860 1.00 135.19 ? 3056 SER A CB    1 
ATOM   11266 O OG    . SER A 1 3056 ? 122.833 178.688 149.547 1.00 135.19 ? 3056 SER A OG    1 
ATOM   11267 N N     . GLN A 1 3057 ? 124.926 177.083 148.665 1.00 127.22 ? 3057 GLN A N     1 
ATOM   11268 C CA    . GLN A 1 3057 ? 124.965 176.059 147.627 1.00 127.22 ? 3057 GLN A CA    1 
ATOM   11269 C C     . GLN A 1 3057 ? 126.006 174.996 147.939 1.00 127.22 ? 3057 GLN A C     1 
ATOM   11270 O O     . GLN A 1 3057 ? 125.753 173.799 147.762 1.00 127.22 ? 3057 GLN A O     1 
ATOM   11271 C CB    . GLN A 1 3057 ? 125.248 176.692 146.267 1.00 127.22 ? 3057 GLN A CB    1 
ATOM   11272 C CG    . GLN A 1 3057 ? 124.060 177.407 145.674 1.00 127.22 ? 3057 GLN A CG    1 
ATOM   11273 C CD    . GLN A 1 3057 ? 122.964 176.446 145.282 1.00 127.22 ? 3057 GLN A CD    1 
ATOM   11274 O OE1   . GLN A 1 3057 ? 121.858 176.497 145.817 1.00 127.22 ? 3057 GLN A OE1   1 
ATOM   11275 N NE2   . GLN A 1 3057 ? 123.267 175.554 144.349 1.00 127.22 ? 3057 GLN A NE2   1 
ATOM   11276 N N     . VAL A 1 3058 ? 127.184 175.411 148.405 1.00 121.85 ? 3058 VAL A N     1 
ATOM   11277 C CA    . VAL A 1 3058 ? 128.231 174.441 148.708 1.00 121.85 ? 3058 VAL A CA    1 
ATOM   11278 C C     . VAL A 1 3058 ? 127.805 173.541 149.862 1.00 121.85 ? 3058 VAL A C     1 
ATOM   11279 O O     . VAL A 1 3058 ? 127.928 172.314 149.789 1.00 121.85 ? 3058 VAL A O     1 
ATOM   11280 C CB    . VAL A 1 3058 ? 129.562 175.151 149.003 1.00 121.85 ? 3058 VAL A CB    1 
ATOM   11281 C CG1   . VAL A 1 3058 ? 130.500 174.214 149.732 1.00 121.85 ? 3058 VAL A CG1   1 
ATOM   11282 C CG2   . VAL A 1 3058 ? 130.195 175.625 147.712 1.00 121.85 ? 3058 VAL A CG2   1 
ATOM   11283 N N     . ILE A 1 3059 ? 127.277 174.129 150.939 1.00 119.46 ? 3059 ILE A N     1 
ATOM   11284 C CA    . ILE A 1 3059 ? 126.887 173.300 152.076 1.00 119.46 ? 3059 ILE A CA    1 
ATOM   11285 C C     . ILE A 1 3059 ? 125.680 172.432 151.757 1.00 119.46 ? 3059 ILE A C     1 
ATOM   11286 O O     . ILE A 1 3059 ? 125.431 171.448 152.461 1.00 119.46 ? 3059 ILE A O     1 
ATOM   11287 C CB    . ILE A 1 3059 ? 126.601 174.137 153.337 1.00 119.46 ? 3059 ILE A CB    1 
ATOM   11288 C CG1   . ILE A 1 3059 ? 125.260 174.857 153.215 1.00 119.46 ? 3059 ILE A CG1   1 
ATOM   11289 C CG2   . ILE A 1 3059 ? 127.734 175.104 153.609 1.00 119.46 ? 3059 ILE A CG2   1 
ATOM   11290 C CD1   . ILE A 1 3059 ? 124.623 175.168 154.544 1.00 119.46 ? 3059 ILE A CD1   1 
ATOM   11291 N N     . ARG A 1 3060 ? 124.913 172.766 150.721 1.00 121.53 ? 3060 ARG A N     1 
ATOM   11292 C CA    . ARG A 1 3060 ? 123.798 171.910 150.341 1.00 121.53 ? 3060 ARG A CA    1 
ATOM   11293 C C     . ARG A 1 3060 ? 124.158 170.931 149.232 1.00 121.53 ? 3060 ARG A C     1 
ATOM   11294 O O     . ARG A 1 3060 ? 123.596 169.832 149.184 1.00 121.53 ? 3060 ARG A O     1 
ATOM   11295 C CB    . ARG A 1 3060 ? 122.598 172.758 149.908 1.00 121.53 ? 3060 ARG A CB    1 
ATOM   11296 C CG    . ARG A 1 3060 ? 121.292 171.980 149.806 1.00 121.53 ? 3060 ARG A CG    1 
ATOM   11297 C CD    . ARG A 1 3060 ? 120.127 172.883 149.425 1.00 121.53 ? 3060 ARG A CD    1 
ATOM   11298 N NE    . ARG A 1 3060 ? 120.433 173.723 148.273 1.00 121.53 ? 3060 ARG A NE    1 
ATOM   11299 C CZ    . ARG A 1 3060 ? 119.950 173.530 147.054 1.00 121.53 ? 3060 ARG A CZ    1 
ATOM   11300 N NH1   . ARG A 1 3060 ? 119.124 172.532 146.788 1.00 121.53 ? 3060 ARG A NH1   1 
ATOM   11301 N NH2   . ARG A 1 3060 ? 120.306 174.358 146.076 1.00 121.53 ? 3060 ARG A NH2   1 
ATOM   11302 N N     . ASN A 1 3061 ? 125.083 171.294 148.349 1.00 123.14 ? 3061 ASN A N     1 
ATOM   11303 C CA    . ASN A 1 3061 ? 125.422 170.483 147.186 1.00 123.14 ? 3061 ASN A CA    1 
ATOM   11304 C C     . ASN A 1 3061 ? 126.865 169.994 147.237 1.00 123.14 ? 3061 ASN A C     1 
ATOM   11305 O O     . ASN A 1 3061 ? 127.563 169.972 146.222 1.00 123.14 ? 3061 ASN A O     1 
ATOM   11306 C CB    . ASN A 1 3061 ? 125.178 171.258 145.892 1.00 123.14 ? 3061 ASN A CB    1 
ATOM   11307 C CG    . ASN A 1 3061 ? 123.734 171.681 145.725 1.00 123.14 ? 3061 ASN A CG    1 
ATOM   11308 O OD1   . ASN A 1 3061 ? 122.896 171.426 146.588 1.00 123.14 ? 3061 ASN A OD1   1 
ATOM   11309 N ND2   . ASN A 1 3061 ? 123.434 172.329 144.605 1.00 123.14 ? 3061 ASN A ND2   1 
ATOM   11310 N N     . LEU A 1 3062 ? 127.338 169.595 148.417 1.00 114.90 ? 3062 LEU A N     1 
ATOM   11311 C CA    . LEU A 1 3062 ? 128.670 169.012 148.535 1.00 114.90 ? 3062 LEU A CA    1 
ATOM   11312 C C     . LEU A 1 3062 ? 128.713 168.104 149.751 1.00 114.90 ? 3062 LEU A C     1 
ATOM   11313 O O     . LEU A 1 3062 ? 128.198 168.461 150.814 1.00 114.90 ? 3062 LEU A O     1 
ATOM   11314 C CB    . LEU A 1 3062 ? 129.754 170.090 148.650 1.00 114.90 ? 3062 LEU A CB    1 
ATOM   11315 C CG    . LEU A 1 3062 ? 131.208 169.612 148.616 1.00 114.90 ? 3062 LEU A CG    1 
ATOM   11316 C CD1   . LEU A 1 3062 ? 131.404 168.548 147.559 1.00 114.90 ? 3062 LEU A CD1   1 
ATOM   11317 C CD2   . LEU A 1 3062 ? 132.156 170.769 148.381 1.00 114.90 ? 3062 LEU A CD2   1 
ATOM   11318 N N     . HIS A 1 3063 ? 129.325 166.935 149.589 1.00 107.06 ? 3063 HIS A N     1 
ATOM   11319 C CA    . HIS A 1 3063 ? 129.481 165.983 150.677 1.00 107.06 ? 3063 HIS A CA    1 
ATOM   11320 C C     . HIS A 1 3063 ? 130.862 165.356 150.591 1.00 107.06 ? 3063 HIS A C     1 
ATOM   11321 O O     . HIS A 1 3063 ? 131.275 164.904 149.519 1.00 107.06 ? 3063 HIS A O     1 
ATOM   11322 C CB    . HIS A 1 3063 ? 128.395 164.910 150.621 1.00 107.06 ? 3063 HIS A CB    1 
ATOM   11323 C CG    . HIS A 1 3063 ? 127.012 165.468 150.512 1.00 107.06 ? 3063 HIS A CG    1 
ATOM   11324 N ND1   . HIS A 1 3063 ? 126.342 165.566 149.312 1.00 107.06 ? 3063 HIS A ND1   1 
ATOM   11325 C CD2   . HIS A 1 3063 ? 126.177 165.970 151.452 1.00 107.06 ? 3063 HIS A CD2   1 
ATOM   11326 C CE1   . HIS A 1 3063 ? 125.151 166.098 149.519 1.00 107.06 ? 3063 HIS A CE1   1 
ATOM   11327 N NE2   . HIS A 1 3063 ? 125.026 166.352 150.808 1.00 107.06 ? 3063 HIS A NE2   1 
ATOM   11328 N N     . VAL A 1 3064 ? 131.568 165.329 151.717 1.00 102.27 ? 3064 VAL A N     1 
ATOM   11329 C CA    . VAL A 1 3064 ? 132.950 164.872 151.781 1.00 102.27 ? 3064 VAL A CA    1 
ATOM   11330 C C     . VAL A 1 3064 ? 133.003 163.616 152.636 1.00 102.27 ? 3064 VAL A C     1 
ATOM   11331 O O     . VAL A 1 3064 ? 132.651 163.648 153.820 1.00 102.27 ? 3064 VAL A O     1 
ATOM   11332 C CB    . VAL A 1 3064 ? 133.877 165.954 152.352 1.00 102.27 ? 3064 VAL A CB    1 
ATOM   11333 C CG1   . VAL A 1 3064 ? 135.318 165.494 152.300 1.00 102.27 ? 3064 VAL A CG1   1 
ATOM   11334 C CG2   . VAL A 1 3064 ? 133.698 167.256 151.601 1.00 102.27 ? 3064 VAL A CG2   1 
ATOM   11335 N N     . VAL A 1 3065 ? 133.451 162.519 152.048 1.00 102.04 ? 3065 VAL A N     1 
ATOM   11336 C CA    . VAL A 1 3065 ? 133.686 161.281 152.777 1.00 102.04 ? 3065 VAL A CA    1 
ATOM   11337 C C     . VAL A 1 3065 ? 135.164 161.219 153.126 1.00 102.04 ? 3065 VAL A C     1 
ATOM   11338 O O     . VAL A 1 3065 ? 136.009 161.723 152.377 1.00 102.04 ? 3065 VAL A O     1 
ATOM   11339 C CB    . VAL A 1 3065 ? 133.244 160.053 151.958 1.00 102.04 ? 3065 VAL A CB    1 
ATOM   11340 C CG1   . VAL A 1 3065 ? 134.351 159.585 151.028 1.00 102.04 ? 3065 VAL A CG1   1 
ATOM   11341 C CG2   . VAL A 1 3065 ? 132.816 158.932 152.878 1.00 102.04 ? 3065 VAL A CG2   1 
ATOM   11342 N N     . PHE A 1 3066 ? 135.480 160.641 154.278 1.00 106.85 ? 3066 PHE A N     1 
ATOM   11343 C CA    . PHE A 1 3066 ? 136.866 160.561 154.709 1.00 106.85 ? 3066 PHE A CA    1 
ATOM   11344 C C     . PHE A 1 3066 ? 137.108 159.167 155.260 1.00 106.85 ? 3066 PHE A C     1 
ATOM   11345 O O     . PHE A 1 3066 ? 136.310 158.656 156.049 1.00 106.85 ? 3066 PHE A O     1 
ATOM   11346 C CB    . PHE A 1 3066 ? 137.179 161.653 155.750 1.00 106.85 ? 3066 PHE A CB    1 
ATOM   11347 C CG    . PHE A 1 3066 ? 138.578 161.597 156.317 1.00 106.85 ? 3066 PHE A CG    1 
ATOM   11348 C CD1   . PHE A 1 3066 ? 138.976 160.593 157.184 1.00 106.85 ? 3066 PHE A CD1   1 
ATOM   11349 C CD2   . PHE A 1 3066 ? 139.501 162.568 155.970 1.00 106.85 ? 3066 PHE A CD2   1 
ATOM   11350 C CE1   . PHE A 1 3066 ? 140.259 160.560 157.690 1.00 106.85 ? 3066 PHE A CE1   1 
ATOM   11351 C CE2   . PHE A 1 3066 ? 140.786 162.539 156.474 1.00 106.85 ? 3066 PHE A CE2   1 
ATOM   11352 C CZ    . PHE A 1 3066 ? 141.165 161.532 157.335 1.00 106.85 ? 3066 PHE A CZ    1 
ATOM   11353 N N     . THR A 1 3067 ? 138.217 158.562 154.846 1.00 111.93 ? 3067 THR A N     1 
ATOM   11354 C CA    . THR A 1 3067 ? 138.572 157.204 155.228 1.00 111.93 ? 3067 THR A CA    1 
ATOM   11355 C C     . THR A 1 3067 ? 139.895 157.206 155.978 1.00 111.93 ? 3067 THR A C     1 
ATOM   11356 O O     . THR A 1 3067 ? 140.837 157.906 155.593 1.00 111.93 ? 3067 THR A O     1 
ATOM   11357 C CB    . THR A 1 3067 ? 138.678 156.304 154.003 1.00 111.93 ? 3067 THR A CB    1 
ATOM   11358 O OG1   . THR A 1 3067 ? 139.806 156.709 153.220 1.00 111.93 ? 3067 THR A OG1   1 
ATOM   11359 C CG2   . THR A 1 3067 ? 137.423 156.413 153.159 1.00 111.93 ? 3067 THR A CG2   1 
ATOM   11360 N N     . MET A 1 3068 ? 139.962 156.419 157.048 1.00 114.46 ? 3068 MET A N     1 
ATOM   11361 C CA    . MET A 1 3068 ? 141.138 156.352 157.901 1.00 114.46 ? 3068 MET A CA    1 
ATOM   11362 C C     . MET A 1 3068 ? 141.211 154.984 158.560 1.00 114.46 ? 3068 MET A C     1 
ATOM   11363 O O     . MET A 1 3068 ? 140.207 154.460 159.047 1.00 114.46 ? 3068 MET A O     1 
ATOM   11364 C CB    . MET A 1 3068 ? 141.110 157.447 158.978 1.00 114.46 ? 3068 MET A CB    1 
ATOM   11365 C CG    . MET A 1 3068 ? 142.402 157.638 159.758 1.00 114.46 ? 3068 MET A CG    1 
ATOM   11366 S SD    . MET A 1 3068 ? 143.712 158.493 158.872 1.00 114.46 ? 3068 MET A SD    1 
ATOM   11367 C CE    . MET A 1 3068 ? 145.138 158.042 159.859 1.00 114.46 ? 3068 MET A CE    1 
ATOM   11368 N N     . ASN A 1 3069 ? 142.421 154.402 158.567 1.00 109.48 ? 3069 ASN A N     1 
ATOM   11369 C CA    . ASN A 1 3069 ? 142.555 153.166 159.321 1.00 109.48 ? 3069 ASN A CA    1 
ATOM   11370 C C     . ASN A 1 3069 ? 142.647 153.467 160.812 1.00 109.48 ? 3069 ASN A C     1 
ATOM   11371 O O     . ASN A 1 3069 ? 143.213 154.488 161.211 1.00 109.48 ? 3069 ASN A O     1 
ATOM   11372 C CB    . ASN A 1 3069 ? 143.797 152.403 158.882 1.00 109.48 ? 3069 ASN A CB    1 
ATOM   11373 C CG    . ASN A 1 3069 ? 143.962 152.381 157.384 1.00 109.48 ? 3069 ASN A CG    1 
ATOM   11374 O OD1   . ASN A 1 3069 ? 143.412 151.521 156.700 1.00 109.48 ? 3069 ASN A OD1   1 
ATOM   11375 N ND2   . ASN A 1 3069 ? 144.727 153.331 156.863 1.00 109.48 ? 3069 ASN A ND2   1 
ATOM   11376 N N     . PRO A 1 3070 ? 142.103 152.594 161.665 1.00 102.89 ? 3070 PRO A N     1 
ATOM   11377 C CA    . PRO A 1 3070 ? 142.145 152.837 163.108 1.00 102.89 ? 3070 PRO A CA    1 
ATOM   11378 C C     . PRO A 1 3070 ? 143.542 152.643 163.689 1.00 102.89 ? 3070 PRO A C     1 
ATOM   11379 O O     . PRO A 1 3070 ? 144.344 153.576 163.641 1.00 102.89 ? 3070 PRO A O     1 
ATOM   11380 C CB    . PRO A 1 3070 ? 141.171 151.797 163.664 1.00 102.89 ? 3070 PRO A CB    1 
ATOM   11381 C CG    . PRO A 1 3070 ? 141.186 150.703 162.659 1.00 102.89 ? 3070 PRO A CG    1 
ATOM   11382 C CD    . PRO A 1 3070 ? 141.359 151.369 161.329 1.00 102.89 ? 3070 PRO A CD    1 
ATOM   11383 N N     . SER A 1 3082 ? 143.229 163.714 165.018 1.00 88.51  ? 3082 SER A N     1 
ATOM   11384 C CA    . SER A 1 3082 ? 142.842 165.045 165.466 1.00 88.51  ? 3082 SER A CA    1 
ATOM   11385 C C     . SER A 1 3082 ? 141.371 165.093 165.845 1.00 88.51  ? 3082 SER A C     1 
ATOM   11386 O O     . SER A 1 3082 ? 140.513 164.738 165.041 1.00 88.51  ? 3082 SER A O     1 
ATOM   11387 C CB    . SER A 1 3082 ? 143.128 166.080 164.382 1.00 88.51  ? 3082 SER A CB    1 
ATOM   11388 O OG    . SER A 1 3082 ? 142.245 167.181 164.496 1.00 88.51  ? 3082 SER A OG    1 
ATOM   11389 N N     . PRO A 1 3083 ? 141.080 165.532 167.071 1.00 93.36  ? 3083 PRO A N     1 
ATOM   11390 C CA    . PRO A 1 3083 ? 139.675 165.631 167.496 1.00 93.36  ? 3083 PRO A CA    1 
ATOM   11391 C C     . PRO A 1 3083 ? 138.848 166.556 166.629 1.00 93.36  ? 3083 PRO A C     1 
ATOM   11392 O O     . PRO A 1 3083 ? 137.626 166.386 166.549 1.00 93.36  ? 3083 PRO A O     1 
ATOM   11393 C CB    . PRO A 1 3083 ? 139.782 166.151 168.935 1.00 93.36  ? 3083 PRO A CB    1 
ATOM   11394 C CG    . PRO A 1 3083 ? 141.131 165.730 169.384 1.00 93.36  ? 3083 PRO A CG    1 
ATOM   11395 C CD    . PRO A 1 3083 ? 142.011 165.812 168.174 1.00 93.36  ? 3083 PRO A CD    1 
ATOM   11396 N N     . ALA A 1 3084 ? 139.473 167.542 165.985 1.00 95.50  ? 3084 ALA A N     1 
ATOM   11397 C CA    . ALA A 1 3084 ? 138.730 168.414 165.082 1.00 95.50  ? 3084 ALA A CA    1 
ATOM   11398 C C     . ALA A 1 3084 ? 138.167 167.636 163.900 1.00 95.50  ? 3084 ALA A C     1 
ATOM   11399 O O     . ALA A 1 3084 ? 137.009 167.830 163.515 1.00 95.50  ? 3084 ALA A O     1 
ATOM   11400 C CB    . ALA A 1 3084 ? 139.628 169.551 164.602 1.00 95.50  ? 3084 ALA A CB    1 
ATOM   11401 N N     . LEU A 1 3085 ? 138.972 166.750 163.309 1.00 93.23  ? 3085 LEU A N     1 
ATOM   11402 C CA    . LEU A 1 3085 ? 138.485 165.944 162.194 1.00 93.23  ? 3085 LEU A CA    1 
ATOM   11403 C C     . LEU A 1 3085 ? 137.387 164.989 162.635 1.00 93.23  ? 3085 LEU A C     1 
ATOM   11404 O O     . LEU A 1 3085 ? 136.423 164.762 161.897 1.00 93.23  ? 3085 LEU A O     1 
ATOM   11405 C CB    . LEU A 1 3085 ? 139.630 165.165 161.554 1.00 93.23  ? 3085 LEU A CB    1 
ATOM   11406 C CG    . LEU A 1 3085 ? 140.271 165.800 160.325 1.00 93.23  ? 3085 LEU A CG    1 
ATOM   11407 C CD1   . LEU A 1 3085 ? 139.356 165.617 159.132 1.00 93.23  ? 3085 LEU A CD1   1 
ATOM   11408 C CD2   . LEU A 1 3085 ? 140.570 167.266 160.552 1.00 93.23  ? 3085 LEU A CD2   1 
ATOM   11409 N N     . PHE A 1 3086 ? 137.527 164.400 163.823 1.00 95.26  ? 3086 PHE A N     1 
ATOM   11410 C CA    . PHE A 1 3086 ? 136.499 163.485 164.304 1.00 95.26  ? 3086 PHE A CA    1 
ATOM   11411 C C     . PHE A 1 3086 ? 135.172 164.204 164.488 1.00 95.26  ? 3086 PHE A C     1 
ATOM   11412 O O     . PHE A 1 3086 ? 134.115 163.662 164.151 1.00 95.26  ? 3086 PHE A O     1 
ATOM   11413 C CB    . PHE A 1 3086 ? 136.948 162.823 165.604 1.00 95.26  ? 3086 PHE A CB    1 
ATOM   11414 C CG    . PHE A 1 3086 ? 138.170 161.972 165.452 1.00 95.26  ? 3086 PHE A CG    1 
ATOM   11415 C CD1   . PHE A 1 3086 ? 138.378 161.246 164.297 1.00 95.26  ? 3086 PHE A CD1   1 
ATOM   11416 C CD2   . PHE A 1 3086 ? 139.109 161.897 166.459 1.00 95.26  ? 3086 PHE A CD2   1 
ATOM   11417 C CE1   . PHE A 1 3086 ? 139.496 160.461 164.146 1.00 95.26  ? 3086 PHE A CE1   1 
ATOM   11418 C CE2   . PHE A 1 3086 ? 140.230 161.110 166.316 1.00 95.26  ? 3086 PHE A CE2   1 
ATOM   11419 C CZ    . PHE A 1 3086 ? 140.424 160.392 165.155 1.00 95.26  ? 3086 PHE A CZ    1 
ATOM   11420 N N     . ASN A 1 3087 ? 135.204 165.424 165.011 1.00 91.79  ? 3087 ASN A N     1 
ATOM   11421 C CA    . ASN A 1 3087 ? 134.010 166.249 165.023 1.00 91.79  ? 3087 ASN A CA    1 
ATOM   11422 C C     . ASN A 1 3087 ? 133.790 166.825 163.627 1.00 91.79  ? 3087 ASN A C     1 
ATOM   11423 O O     . ASN A 1 3087 ? 134.568 166.585 162.702 1.00 91.79  ? 3087 ASN A O     1 
ATOM   11424 C CB    . ASN A 1 3087 ? 134.128 167.344 166.078 1.00 91.79  ? 3087 ASN A CB    1 
ATOM   11425 C CG    . ASN A 1 3087 ? 132.791 167.727 166.663 1.00 91.79  ? 3087 ASN A CG    1 
ATOM   11426 O OD1   . ASN A 1 3087 ? 132.301 168.836 166.455 1.00 91.79  ? 3087 ASN A OD1   1 
ATOM   11427 N ND2   . ASN A 1 3087 ? 132.190 166.809 167.405 1.00 91.79  ? 3087 ASN A ND2   1 
ATOM   11428 N N     . ARG A 1 3088 ? 132.698 167.574 163.465 1.00 98.46  ? 3088 ARG A N     1 
ATOM   11429 C CA    . ARG A 1 3088 ? 132.268 168.149 162.187 1.00 98.46  ? 3088 ARG A CA    1 
ATOM   11430 C C     . ARG A 1 3088 ? 132.144 167.100 161.082 1.00 98.46  ? 3088 ARG A C     1 
ATOM   11431 O O     . ARG A 1 3088 ? 132.068 167.439 159.897 1.00 98.46  ? 3088 ARG A O     1 
ATOM   11432 C CB    . ARG A 1 3088 ? 133.175 169.313 161.756 1.00 98.46  ? 3088 ARG A CB    1 
ATOM   11433 C CG    . ARG A 1 3088 ? 134.423 168.972 160.967 1.00 98.46  ? 3088 ARG A CG    1 
ATOM   11434 C CD    . ARG A 1 3088 ? 135.376 170.149 160.975 1.00 98.46  ? 3088 ARG A CD    1 
ATOM   11435 N NE    . ARG A 1 3088 ? 135.447 170.773 162.290 1.00 98.46  ? 3088 ARG A NE    1 
ATOM   11436 C CZ    . ARG A 1 3088 ? 136.090 171.903 162.549 1.00 98.46  ? 3088 ARG A CZ    1 
ATOM   11437 N NH1   . ARG A 1 3088 ? 136.724 172.571 161.600 1.00 98.46  ? 3088 ARG A NH1   1 
ATOM   11438 N NH2   . ARG A 1 3088 ? 136.091 172.378 163.790 1.00 98.46  ? 3088 ARG A NH2   1 
ATOM   11439 N N     . CYS A 1 3089 ? 132.079 165.826 161.462 1.00 101.69 ? 3089 CYS A N     1 
ATOM   11440 C CA    . CYS A 1 3089 ? 131.832 164.734 160.535 1.00 101.69 ? 3089 CYS A CA    1 
ATOM   11441 C C     . CYS A 1 3089 ? 131.008 163.677 161.250 1.00 101.69 ? 3089 CYS A C     1 
ATOM   11442 O O     . CYS A 1 3089 ? 130.934 163.649 162.481 1.00 101.69 ? 3089 CYS A O     1 
ATOM   11443 C CB    . CYS A 1 3089 ? 133.132 164.118 160.010 1.00 101.69 ? 3089 CYS A CB    1 
ATOM   11444 S SG    . CYS A 1 3089 ? 133.897 165.006 158.648 1.00 101.69 ? 3089 CYS A SG    1 
ATOM   11445 N N     . VAL A 1 3090 ? 130.382 162.813 160.467 1.00 94.99  ? 3090 VAL A N     1 
ATOM   11446 C CA    . VAL A 1 3090 ? 129.666 161.668 161.009 1.00 94.99  ? 3090 VAL A CA    1 
ATOM   11447 C C     . VAL A 1 3090 ? 130.601 160.471 160.984 1.00 94.99  ? 3090 VAL A C     1 
ATOM   11448 O O     . VAL A 1 3090 ? 131.064 160.053 159.917 1.00 94.99  ? 3090 VAL A O     1 
ATOM   11449 C CB    . VAL A 1 3090 ? 128.384 161.388 160.212 1.00 94.99  ? 3090 VAL A CB    1 
ATOM   11450 C CG1   . VAL A 1 3090 ? 127.694 160.154 160.756 1.00 94.99  ? 3090 VAL A CG1   1 
ATOM   11451 C CG2   . VAL A 1 3090 ? 127.458 162.585 160.273 1.00 94.99  ? 3090 VAL A CG2   1 
ATOM   11452 N N     . LEU A 1 3091 ? 130.881 159.921 162.160 1.00 95.57  ? 3091 LEU A N     1 
ATOM   11453 C CA    . LEU A 1 3091 ? 131.852 158.849 162.315 1.00 95.57  ? 3091 LEU A CA    1 
ATOM   11454 C C     . LEU A 1 3091 ? 131.166 157.508 162.119 1.00 95.57  ? 3091 LEU A C     1 
ATOM   11455 O O     . LEU A 1 3091 ? 130.229 157.174 162.851 1.00 95.57  ? 3091 LEU A O     1 
ATOM   11456 C CB    . LEU A 1 3091 ? 132.513 158.903 163.692 1.00 95.57  ? 3091 LEU A CB    1 
ATOM   11457 C CG    . LEU A 1 3091 ? 133.087 160.244 164.145 1.00 95.57  ? 3091 LEU A CG    1 
ATOM   11458 C CD1   . LEU A 1 3091 ? 132.047 161.074 164.860 1.00 95.57  ? 3091 LEU A CD1   1 
ATOM   11459 C CD2   . LEU A 1 3091 ? 134.276 160.017 165.045 1.00 95.57  ? 3091 LEU A CD2   1 
ATOM   11460 N N     . ASN A 1 3092 ? 131.635 156.742 161.140 1.00 100.03 ? 3092 ASN A N     1 
ATOM   11461 C CA    . ASN A 1 3092 ? 131.095 155.420 160.859 1.00 100.03 ? 3092 ASN A CA    1 
ATOM   11462 C C     . ASN A 1 3092 ? 132.223 154.407 160.956 1.00 100.03 ? 3092 ASN A C     1 
ATOM   11463 O O     . ASN A 1 3092 ? 133.243 154.543 160.273 1.00 100.03 ? 3092 ASN A O     1 
ATOM   11464 C CB    . ASN A 1 3092 ? 130.438 155.376 159.479 1.00 100.03 ? 3092 ASN A CB    1 
ATOM   11465 C CG    . ASN A 1 3092 ? 129.712 154.076 159.226 1.00 100.03 ? 3092 ASN A CG    1 
ATOM   11466 O OD1   . ASN A 1 3092 ? 128.961 153.602 160.073 1.00 100.03 ? 3092 ASN A OD1   1 
ATOM   11467 N ND2   . ASN A 1 3092 ? 129.924 153.497 158.053 1.00 100.03 ? 3092 ASN A ND2   1 
ATOM   11468 N N     . TRP A 1 3093 ? 132.040 153.397 161.802 1.00 98.76  ? 3093 TRP A N     1 
ATOM   11469 C CA    . TRP A 1 3093 ? 133.060 152.379 162.036 1.00 98.76  ? 3093 TRP A CA    1 
ATOM   11470 C C     . TRP A 1 3093 ? 132.892 151.270 161.010 1.00 98.76  ? 3093 TRP A C     1 
ATOM   11471 O O     . TRP A 1 3093 ? 132.041 150.392 161.157 1.00 98.76  ? 3093 TRP A O     1 
ATOM   11472 C CB    . TRP A 1 3093 ? 132.957 151.842 163.457 1.00 98.76  ? 3093 TRP A CB    1 
ATOM   11473 C CG    . TRP A 1 3093 ? 133.735 150.588 163.686 1.00 98.76  ? 3093 TRP A CG    1 
ATOM   11474 C CD1   . TRP A 1 3093 ? 133.245 149.318 163.717 1.00 98.76  ? 3093 TRP A CD1   1 
ATOM   11475 C CD2   . TRP A 1 3093 ? 135.143 150.479 163.917 1.00 98.76  ? 3093 TRP A CD2   1 
ATOM   11476 N NE1   . TRP A 1 3093 ? 134.258 148.425 163.956 1.00 98.76  ? 3093 TRP A NE1   1 
ATOM   11477 C CE2   . TRP A 1 3093 ? 135.434 149.113 164.081 1.00 98.76  ? 3093 TRP A CE2   1 
ATOM   11478 C CE3   . TRP A 1 3093 ? 136.185 151.404 164.003 1.00 98.76  ? 3093 TRP A CE3   1 
ATOM   11479 C CZ2   . TRP A 1 3093 ? 136.722 148.651 164.323 1.00 98.76  ? 3093 TRP A CZ2   1 
ATOM   11480 C CZ3   . TRP A 1 3093 ? 137.462 150.942 164.242 1.00 98.76  ? 3093 TRP A CZ3   1 
ATOM   11481 C CH2   . TRP A 1 3093 ? 137.720 149.580 164.399 1.00 98.76  ? 3093 TRP A CH2   1 
ATOM   11482 N N     . PHE A 1 3094 ? 133.709 151.310 159.959 1.00 94.01  ? 3094 PHE A N     1 
ATOM   11483 C CA    . PHE A 1 3094 ? 133.682 150.290 158.912 1.00 94.01  ? 3094 PHE A CA    1 
ATOM   11484 C C     . PHE A 1 3094 ? 134.555 149.113 159.343 1.00 94.01  ? 3094 PHE A C     1 
ATOM   11485 O O     . PHE A 1 3094 ? 135.629 148.850 158.799 1.00 94.01  ? 3094 PHE A O     1 
ATOM   11486 C CB    . PHE A 1 3094 ? 134.146 150.872 157.587 1.00 94.01  ? 3094 PHE A CB    1 
ATOM   11487 C CG    . PHE A 1 3094 ? 133.434 150.307 156.403 1.00 94.01  ? 3094 PHE A CG    1 
ATOM   11488 C CD1   . PHE A 1 3094 ? 133.647 149.000 156.015 1.00 94.01  ? 3094 PHE A CD1   1 
ATOM   11489 C CD2   . PHE A 1 3094 ? 132.546 151.079 155.683 1.00 94.01  ? 3094 PHE A CD2   1 
ATOM   11490 C CE1   . PHE A 1 3094 ? 132.989 148.474 154.926 1.00 94.01  ? 3094 PHE A CE1   1 
ATOM   11491 C CE2   . PHE A 1 3094 ? 131.886 150.560 154.595 1.00 94.01  ? 3094 PHE A CE2   1 
ATOM   11492 C CZ    . PHE A 1 3094 ? 132.107 149.256 154.215 1.00 94.01  ? 3094 PHE A CZ    1 
ATOM   11493 N N     . GLY A 1 3095 ? 134.058 148.387 160.335 1.00 93.76  ? 3095 GLY A N     1 
ATOM   11494 C CA    . GLY A 1 3095 ? 134.828 147.319 160.939 1.00 93.76  ? 3095 GLY A CA    1 
ATOM   11495 C C     . GLY A 1 3095 ? 135.152 146.210 159.958 1.00 93.76  ? 3095 GLY A C     1 
ATOM   11496 O O     . GLY A 1 3095 ? 134.627 146.126 158.848 1.00 93.76  ? 3095 GLY A O     1 
ATOM   11497 N N     . ASP A 1 3096 ? 136.055 145.338 160.394 1.00 100.36 ? 3096 ASP A N     1 
ATOM   11498 C CA    . ASP A 1 3096 ? 136.489 144.226 159.564 1.00 100.36 ? 3096 ASP A CA    1 
ATOM   11499 C C     . ASP A 1 3096 ? 135.314 143.302 159.271 1.00 100.36 ? 3096 ASP A C     1 
ATOM   11500 O O     . ASP A 1 3096 ? 134.331 143.253 160.015 1.00 100.36 ? 3096 ASP A O     1 
ATOM   11501 C CB    . ASP A 1 3096 ? 137.610 143.456 160.262 1.00 100.36 ? 3096 ASP A CB    1 
ATOM   11502 C CG    . ASP A 1 3096 ? 138.239 142.398 159.377 1.00 100.36 ? 3096 ASP A CG    1 
ATOM   11503 O OD1   . ASP A 1 3096 ? 137.708 142.124 158.281 1.00 100.36 ? 3096 ASP A OD1   1 
ATOM   11504 O OD2   . ASP A 1 3096 ? 139.273 141.831 159.785 1.00 100.36 ? 3096 ASP A OD2   1 
ATOM   11505 N N     . TRP A 1 3097 ? 135.415 142.579 158.158 1.00 90.78  ? 3097 TRP A N     1 
ATOM   11506 C CA    . TRP A 1 3097 ? 134.362 141.652 157.770 1.00 90.78  ? 3097 TRP A CA    1 
ATOM   11507 C C     . TRP A 1 3097 ? 134.125 140.625 158.866 1.00 90.78  ? 3097 TRP A C     1 
ATOM   11508 O O     . TRP A 1 3097 ? 135.066 140.019 159.383 1.00 90.78  ? 3097 TRP A O     1 
ATOM   11509 C CB    . TRP A 1 3097 ? 134.730 140.951 156.466 1.00 90.78  ? 3097 TRP A CB    1 
ATOM   11510 C CG    . TRP A 1 3097 ? 134.779 141.861 155.292 1.00 90.78  ? 3097 TRP A CG    1 
ATOM   11511 C CD1   . TRP A 1 3097 ? 134.575 143.205 155.293 1.00 90.78  ? 3097 TRP A CD1   1 
ATOM   11512 C CD2   . TRP A 1 3097 ? 135.036 141.494 153.934 1.00 90.78  ? 3097 TRP A CD2   1 
ATOM   11513 N NE1   . TRP A 1 3097 ? 134.695 143.701 154.020 1.00 90.78  ? 3097 TRP A NE1   1 
ATOM   11514 C CE2   . TRP A 1 3097 ? 134.978 142.668 153.167 1.00 90.78  ? 3097 TRP A CE2   1 
ATOM   11515 C CE3   . TRP A 1 3097 ? 135.312 140.286 153.294 1.00 90.78  ? 3097 TRP A CE3   1 
ATOM   11516 C CZ2   . TRP A 1 3097 ? 135.185 142.672 151.795 1.00 90.78  ? 3097 TRP A CZ2   1 
ATOM   11517 C CZ3   . TRP A 1 3097 ? 135.518 140.291 151.933 1.00 90.78  ? 3097 TRP A CZ3   1 
ATOM   11518 C CH2   . TRP A 1 3097 ? 135.454 141.475 151.197 1.00 90.78  ? 3097 TRP A CH2   1 
ATOM   11519 N N     . SER A 1 3098 ? 132.859 140.433 159.220 1.00 100.06 ? 3098 SER A N     1 
ATOM   11520 C CA    . SER A 1 3098 ? 132.510 139.462 160.240 1.00 100.06 ? 3098 SER A CA    1 
ATOM   11521 C C     . SER A 1 3098 ? 132.604 138.047 159.679 1.00 100.06 ? 3098 SER A C     1 
ATOM   11522 O O     . SER A 1 3098 ? 132.815 137.832 158.483 1.00 100.06 ? 3098 SER A O     1 
ATOM   11523 C CB    . SER A 1 3098 ? 131.103 139.725 160.770 1.00 100.06 ? 3098 SER A CB    1 
ATOM   11524 O OG    . SER A 1 3098 ? 130.681 138.674 161.621 1.00 100.06 ? 3098 SER A OG    1 
ATOM   11525 N N     . THR A 1 3099 ? 132.442 137.070 160.572 1.00 100.66 ? 3099 THR A N     1 
ATOM   11526 C CA    . THR A 1 3099 ? 132.453 135.677 160.142 1.00 100.66 ? 3099 THR A CA    1 
ATOM   11527 C C     . THR A 1 3099 ? 131.326 135.402 159.158 1.00 100.66 ? 3099 THR A C     1 
ATOM   11528 O O     . THR A 1 3099 ? 131.524 134.711 158.153 1.00 100.66 ? 3099 THR A O     1 
ATOM   11529 C CB    . THR A 1 3099 ? 132.341 134.753 161.351 1.00 100.66 ? 3099 THR A CB    1 
ATOM   11530 O OG1   . THR A 1 3099 ? 131.019 134.840 161.893 1.00 100.66 ? 3099 THR A OG1   1 
ATOM   11531 C CG2   . THR A 1 3099 ? 133.342 135.157 162.415 1.00 100.66 ? 3099 THR A CG2   1 
ATOM   11532 N N     . GLU A 1 3100 ? 130.135 135.938 159.428 1.00 106.38 ? 3100 GLU A N     1 
ATOM   11533 C CA    . GLU A 1 3100 ? 129.027 135.779 158.493 1.00 106.38 ? 3100 GLU A CA    1 
ATOM   11534 C C     . GLU A 1 3100 ? 129.331 136.452 157.163 1.00 106.38 ? 3100 GLU A C     1 
ATOM   11535 O O     . GLU A 1 3100 ? 128.982 135.928 156.099 1.00 106.38 ? 3100 GLU A O     1 
ATOM   11536 C CB    . GLU A 1 3100 ? 127.745 136.344 159.100 1.00 106.38 ? 3100 GLU A CB    1 
ATOM   11537 C CG    . GLU A 1 3100 ? 126.479 135.993 158.337 1.00 106.38 ? 3100 GLU A CG    1 
ATOM   11538 C CD    . GLU A 1 3100 ? 126.411 134.532 157.939 1.00 106.38 ? 3100 GLU A CD    1 
ATOM   11539 O OE1   . GLU A 1 3100 ? 126.607 133.659 158.812 1.00 106.38 ? 3100 GLU A OE1   1 
ATOM   11540 O OE2   . GLU A 1 3100 ? 126.146 134.255 156.752 1.00 106.38 ? 3100 GLU A OE2   1 
ATOM   11541 N N     . ALA A 1 3101 ? 129.975 137.619 157.202 1.00 99.01  ? 3101 ALA A N     1 
ATOM   11542 C CA    . ALA A 1 3101 ? 130.331 138.305 155.966 1.00 99.01  ? 3101 ALA A CA    1 
ATOM   11543 C C     . ALA A 1 3101 ? 131.306 137.475 155.144 1.00 99.01  ? 3101 ALA A C     1 
ATOM   11544 O O     . ALA A 1 3101 ? 131.142 137.328 153.928 1.00 99.01  ? 3101 ALA A O     1 
ATOM   11545 C CB    . ALA A 1 3101 ? 130.924 139.678 156.279 1.00 99.01  ? 3101 ALA A CB    1 
ATOM   11546 N N     . LEU A 1 3102 ? 132.329 136.921 155.794 1.00 91.84  ? 3102 LEU A N     1 
ATOM   11547 C CA    . LEU A 1 3102 ? 133.284 136.086 155.077 1.00 91.84  ? 3102 LEU A CA    1 
ATOM   11548 C C     . LEU A 1 3102 ? 132.602 134.844 154.523 1.00 91.84  ? 3102 LEU A C     1 
ATOM   11549 O O     . LEU A 1 3102 ? 132.883 134.417 153.396 1.00 91.84  ? 3102 LEU A O     1 
ATOM   11550 C CB    . LEU A 1 3102 ? 134.437 135.703 156.000 1.00 91.84  ? 3102 LEU A CB    1 
ATOM   11551 C CG    . LEU A 1 3102 ? 135.294 136.873 156.483 1.00 91.84  ? 3102 LEU A CG    1 
ATOM   11552 C CD1   . LEU A 1 3102 ? 136.192 136.450 157.631 1.00 91.84  ? 3102 LEU A CD1   1 
ATOM   11553 C CD2   . LEU A 1 3102 ? 136.102 137.462 155.353 1.00 91.84  ? 3102 LEU A CD2   1 
ATOM   11554 N N     . TYR A 1 3103 ? 131.696 134.258 155.306 1.00 103.67 ? 3103 TYR A N     1 
ATOM   11555 C CA    . TYR A 1 3103 ? 130.945 133.094 154.852 1.00 103.67 ? 3103 TYR A CA    1 
ATOM   11556 C C     . TYR A 1 3103 ? 130.155 133.411 153.592 1.00 103.67 ? 3103 TYR A C     1 
ATOM   11557 O O     . TYR A 1 3103 ? 130.190 132.654 152.617 1.00 103.67 ? 3103 TYR A O     1 
ATOM   11558 C CB    . TYR A 1 3103 ? 130.015 132.624 155.969 1.00 103.67 ? 3103 TYR A CB    1 
ATOM   11559 C CG    . TYR A 1 3103 ? 129.059 131.524 155.579 1.00 103.67 ? 3103 TYR A CG    1 
ATOM   11560 C CD1   . TYR A 1 3103 ? 129.419 130.193 155.695 1.00 103.67 ? 3103 TYR A CD1   1 
ATOM   11561 C CD2   . TYR A 1 3103 ? 127.791 131.820 155.101 1.00 103.67 ? 3103 TYR A CD2   1 
ATOM   11562 C CE1   . TYR A 1 3103 ? 128.543 129.188 155.346 1.00 103.67 ? 3103 TYR A CE1   1 
ATOM   11563 C CE2   . TYR A 1 3103 ? 126.912 130.823 154.746 1.00 103.67 ? 3103 TYR A CE2   1 
ATOM   11564 C CZ    . TYR A 1 3103 ? 127.292 129.508 154.869 1.00 103.67 ? 3103 TYR A CZ    1 
ATOM   11565 O OH    . TYR A 1 3103 ? 126.416 128.509 154.517 1.00 103.67 ? 3103 TYR A OH    1 
ATOM   11566 N N     . GLN A 1 3104 ? 129.434 134.532 153.594 1.00 97.66  ? 3104 GLN A N     1 
ATOM   11567 C CA    . GLN A 1 3104 ? 128.622 134.886 152.436 1.00 97.66  ? 3104 GLN A CA    1 
ATOM   11568 C C     . GLN A 1 3104 ? 129.491 135.206 151.227 1.00 97.66  ? 3104 GLN A C     1 
ATOM   11569 O O     . GLN A 1 3104 ? 129.157 134.823 150.099 1.00 97.66  ? 3104 GLN A O     1 
ATOM   11570 C CB    . GLN A 1 3104 ? 127.714 136.065 152.772 1.00 97.66  ? 3104 GLN A CB    1 
ATOM   11571 C CG    . GLN A 1 3104 ? 126.482 135.681 153.565 1.00 97.66  ? 3104 GLN A CG    1 
ATOM   11572 C CD    . GLN A 1 3104 ? 125.836 136.871 154.240 1.00 97.66  ? 3104 GLN A CD    1 
ATOM   11573 O OE1   . GLN A 1 3104 ? 126.114 137.167 155.401 1.00 97.66  ? 3104 GLN A OE1   1 
ATOM   11574 N NE2   . GLN A 1 3104 ? 124.966 137.562 153.515 1.00 97.66  ? 3104 GLN A NE2   1 
ATOM   11575 N N     . VAL A 1 3105 ? 130.605 135.909 151.440 1.00 91.15  ? 3105 VAL A N     1 
ATOM   11576 C CA    . VAL A 1 3105 ? 131.506 136.215 150.334 1.00 91.15  ? 3105 VAL A CA    1 
ATOM   11577 C C     . VAL A 1 3105 ? 132.008 134.927 149.701 1.00 91.15  ? 3105 VAL A C     1 
ATOM   11578 O O     . VAL A 1 3105 ? 131.973 134.759 148.475 1.00 91.15  ? 3105 VAL A O     1 
ATOM   11579 C CB    . VAL A 1 3105 ? 132.678 137.087 150.815 1.00 91.15  ? 3105 VAL A CB    1 
ATOM   11580 C CG1   . VAL A 1 3105 ? 133.745 137.164 149.744 1.00 91.15  ? 3105 VAL A CG1   1 
ATOM   11581 C CG2   . VAL A 1 3105 ? 132.197 138.465 151.182 1.00 91.15  ? 3105 VAL A CG2   1 
ATOM   11582 N N     . GLY A 1 3106 ? 132.469 133.992 150.530 1.00 94.55  ? 3106 GLY A N     1 
ATOM   11583 C CA    . GLY A 1 3106 ? 132.954 132.732 149.998 1.00 94.55  ? 3106 GLY A CA    1 
ATOM   11584 C C     . GLY A 1 3106 ? 131.869 131.953 149.283 1.00 94.55  ? 3106 GLY A C     1 
ATOM   11585 O O     . GLY A 1 3106 ? 132.091 131.404 148.202 1.00 94.55  ? 3106 GLY A O     1 
ATOM   11586 N N     . LYS A 1 3107 ? 130.674 131.906 149.872 1.00 98.76  ? 3107 LYS A N     1 
ATOM   11587 C CA    . LYS A 1 3107 ? 129.590 131.141 149.271 1.00 98.76  ? 3107 LYS A CA    1 
ATOM   11588 C C     . LYS A 1 3107 ? 129.219 131.695 147.906 1.00 98.76  ? 3107 LYS A C     1 
ATOM   11589 O O     . LYS A 1 3107 ? 129.022 130.934 146.952 1.00 98.76  ? 3107 LYS A O     1 
ATOM   11590 C CB    . LYS A 1 3107 ? 128.374 131.141 150.194 1.00 98.76  ? 3107 LYS A CB    1 
ATOM   11591 C CG    . LYS A 1 3107 ? 127.128 130.542 149.571 1.00 98.76  ? 3107 LYS A CG    1 
ATOM   11592 C CD    . LYS A 1 3107 ? 127.175 129.028 149.607 1.00 98.76  ? 3107 LYS A CD    1 
ATOM   11593 C CE    . LYS A 1 3107 ? 127.713 128.531 150.939 1.00 98.76  ? 3107 LYS A CE    1 
ATOM   11594 N NZ    . LYS A 1 3107 ? 127.867 127.054 150.955 1.00 98.76  ? 3107 LYS A NZ    1 
ATOM   11595 N N     . GLU A 1 3108 ? 129.124 133.019 147.789 1.00 98.80  ? 3108 GLU A N     1 
ATOM   11596 C CA    . GLU A 1 3108 ? 128.784 133.607 146.500 1.00 98.80  ? 3108 GLU A CA    1 
ATOM   11597 C C     . GLU A 1 3108 ? 129.910 133.420 145.494 1.00 98.80  ? 3108 GLU A C     1 
ATOM   11598 O O     . GLU A 1 3108 ? 129.656 133.150 144.315 1.00 98.80  ? 3108 GLU A O     1 
ATOM   11599 C CB    . GLU A 1 3108 ? 128.455 135.088 146.666 1.00 98.80  ? 3108 GLU A CB    1 
ATOM   11600 C CG    . GLU A 1 3108 ? 127.636 135.671 145.527 1.00 98.80  ? 3108 GLU A CG    1 
ATOM   11601 C CD    . GLU A 1 3108 ? 128.484 136.043 144.325 1.00 98.80  ? 3108 GLU A CD    1 
ATOM   11602 O OE1   . GLU A 1 3108 ? 129.694 136.295 144.504 1.00 98.80  ? 3108 GLU A OE1   1 
ATOM   11603 O OE2   . GLU A 1 3108 ? 127.941 136.087 143.201 1.00 98.80  ? 3108 GLU A OE2   1 
ATOM   11604 N N     . PHE A 1 3109 ? 131.158 133.556 145.935 1.00 94.62  ? 3109 PHE A N     1 
ATOM   11605 C CA    . PHE A 1 3109 ? 132.281 133.490 145.013 1.00 94.62  ? 3109 PHE A CA    1 
ATOM   11606 C C     . PHE A 1 3109 ? 132.664 132.067 144.637 1.00 94.62  ? 3109 PHE A C     1 
ATOM   11607 O O     . PHE A 1 3109 ? 133.401 131.881 143.664 1.00 94.62  ? 3109 PHE A O     1 
ATOM   11608 C CB    . PHE A 1 3109 ? 133.489 134.196 145.621 1.00 94.62  ? 3109 PHE A CB    1 
ATOM   11609 C CG    . PHE A 1 3109 ? 133.675 135.597 145.136 1.00 94.62  ? 3109 PHE A CG    1 
ATOM   11610 C CD1   . PHE A 1 3109 ? 132.695 136.546 145.346 1.00 94.62  ? 3109 PHE A CD1   1 
ATOM   11611 C CD2   . PHE A 1 3109 ? 134.830 135.970 144.479 1.00 94.62  ? 3109 PHE A CD2   1 
ATOM   11612 C CE1   . PHE A 1 3109 ? 132.861 137.838 144.906 1.00 94.62  ? 3109 PHE A CE1   1 
ATOM   11613 C CE2   . PHE A 1 3109 ? 135.002 137.261 144.037 1.00 94.62  ? 3109 PHE A CE2   1 
ATOM   11614 C CZ    . PHE A 1 3109 ? 134.016 138.197 144.251 1.00 94.62  ? 3109 PHE A CZ    1 
ATOM   11615 N N     . THR A 1 3110 ? 132.194 131.065 145.380 1.00 106.10 ? 3110 THR A N     1 
ATOM   11616 C CA    . THR A 1 3110 ? 132.505 129.669 145.104 1.00 106.10 ? 3110 THR A CA    1 
ATOM   11617 C C     . THR A 1 3110 ? 131.328 128.929 144.481 1.00 106.10 ? 3110 THR A C     1 
ATOM   11618 O O     . THR A 1 3110 ? 131.379 127.705 144.328 1.00 106.10 ? 3110 THR A O     1 
ATOM   11619 C CB    . THR A 1 3110 ? 132.947 128.959 146.382 1.00 106.10 ? 3110 THR A CB    1 
ATOM   11620 O OG1   . THR A 1 3110 ? 131.982 129.191 147.413 1.00 106.10 ? 3110 THR A OG1   1 
ATOM   11621 C CG2   . THR A 1 3110 ? 134.286 129.493 146.845 1.00 106.10 ? 3110 THR A CG2   1 
ATOM   11622 N N     . SER A 1 3111 ? 130.266 129.647 144.118 1.00 108.03 ? 3111 SER A N     1 
ATOM   11623 C CA    . SER A 1 3111 ? 129.093 128.987 143.560 1.00 108.03 ? 3111 SER A CA    1 
ATOM   11624 C C     . SER A 1 3111 ? 129.380 128.387 142.192 1.00 108.03 ? 3111 SER A C     1 
ATOM   11625 O O     . SER A 1 3111 ? 128.804 127.352 141.840 1.00 108.03 ? 3111 SER A O     1 
ATOM   11626 C CB    . SER A 1 3111 ? 127.931 129.973 143.470 1.00 108.03 ? 3111 SER A CB    1 
ATOM   11627 O OG    . SER A 1 3111 ? 128.279 131.094 142.679 1.00 108.03 ? 3111 SER A OG    1 
ATOM   11628 N N     . LYS A 1 3112 ? 130.262 129.014 141.414 1.00 113.15 ? 3112 LYS A N     1 
ATOM   11629 C CA    . LYS A 1 3112 ? 130.533 128.544 140.058 1.00 113.15 ? 3112 LYS A CA    1 
ATOM   11630 C C     . LYS A 1 3112 ? 131.151 127.153 140.070 1.00 113.15 ? 3112 LYS A C     1 
ATOM   11631 O O     . LYS A 1 3112 ? 130.847 126.317 139.210 1.00 113.15 ? 3112 LYS A O     1 
ATOM   11632 C CB    . LYS A 1 3112 ? 131.454 129.531 139.343 1.00 113.15 ? 3112 LYS A CB    1 
ATOM   11633 C CG    . LYS A 1 3112 ? 132.181 128.947 138.147 1.00 113.15 ? 3112 LYS A CG    1 
ATOM   11634 C CD    . LYS A 1 3112 ? 133.650 128.727 138.459 1.00 113.15 ? 3112 LYS A CD    1 
ATOM   11635 C CE    . LYS A 1 3112 ? 134.257 127.675 137.541 1.00 113.15 ? 3112 LYS A CE    1 
ATOM   11636 N NZ    . LYS A 1 3112 ? 135.612 127.235 137.978 1.00 113.15 ? 3112 LYS A NZ    1 
ATOM   11637 N N     . MET A 1 3113 ? 132.019 126.892 141.041 1.00 116.46 ? 3113 MET A N     1 
ATOM   11638 C CA    . MET A 1 3113 ? 132.817 125.680 141.053 1.00 116.46 ? 3113 MET A CA    1 
ATOM   11639 C C     . MET A 1 3113 ? 131.951 124.445 141.263 1.00 116.46 ? 3113 MET A C     1 
ATOM   11640 O O     . MET A 1 3113 ? 130.907 124.480 141.922 1.00 116.46 ? 3113 MET A O     1 
ATOM   11641 C CB    . MET A 1 3113 ? 133.874 125.748 142.150 1.00 116.46 ? 3113 MET A CB    1 
ATOM   11642 C CG    . MET A 1 3113 ? 134.238 127.158 142.533 1.00 116.46 ? 3113 MET A CG    1 
ATOM   11643 S SD    . MET A 1 3113 ? 135.492 127.241 143.818 1.00 116.46 ? 3113 MET A SD    1 
ATOM   11644 C CE    . MET A 1 3113 ? 135.895 128.980 143.711 1.00 116.46 ? 3113 MET A CE    1 
ATOM   11645 N N     . ASP A 1 3114 ? 132.410 123.338 140.687 1.00 124.84 ? 3114 ASP A N     1 
ATOM   11646 C CA    . ASP A 1 3114 ? 131.802 122.029 140.909 1.00 124.84 ? 3114 ASP A CA    1 
ATOM   11647 C C     . ASP A 1 3114 ? 132.291 121.513 142.255 1.00 124.84 ? 3114 ASP A C     1 
ATOM   11648 O O     . ASP A 1 3114 ? 133.278 120.783 142.350 1.00 124.84 ? 3114 ASP A O     1 
ATOM   11649 C CB    . ASP A 1 3114 ? 132.151 121.069 139.778 1.00 124.84 ? 3114 ASP A CB    1 
ATOM   11650 C CG    . ASP A 1 3114 ? 131.696 119.644 140.056 1.00 124.84 ? 3114 ASP A CG    1 
ATOM   11651 O OD1   . ASP A 1 3114 ? 130.741 119.459 140.840 1.00 124.84 ? 3114 ASP A OD1   1 
ATOM   11652 O OD2   . ASP A 1 3114 ? 132.295 118.707 139.484 1.00 124.84 ? 3114 ASP A OD2   1 
ATOM   11653 N N     . LEU A 1 3115 ? 131.574 121.883 143.313 1.00 121.75 ? 3115 LEU A N     1 
ATOM   11654 C CA    . LEU A 1 3115 ? 131.943 121.531 144.677 1.00 121.75 ? 3115 LEU A CA    1 
ATOM   11655 C C     . LEU A 1 3115 ? 130.864 120.685 145.342 1.00 121.75 ? 3115 LEU A C     1 
ATOM   11656 O O     . LEU A 1 3115 ? 130.691 120.729 146.561 1.00 121.75 ? 3115 LEU A O     1 
ATOM   11657 C CB    . LEU A 1 3115 ? 132.223 122.791 145.496 1.00 121.75 ? 3115 LEU A CB    1 
ATOM   11658 C CG    . LEU A 1 3115 ? 133.689 123.147 145.749 1.00 121.75 ? 3115 LEU A CG    1 
ATOM   11659 C CD1   . LEU A 1 3115 ? 134.485 123.088 144.465 1.00 121.75 ? 3115 LEU A CD1   1 
ATOM   11660 C CD2   . LEU A 1 3115 ? 133.801 124.528 146.362 1.00 121.75 ? 3115 LEU A CD2   1 
ATOM   11661 N N     . GLU A 1 3116 ? 130.129 119.912 144.549 1.00 131.86 ? 3116 GLU A N     1 
ATOM   11662 C CA    . GLU A 1 3116 ? 129.023 119.103 145.045 1.00 131.86 ? 3116 GLU A CA    1 
ATOM   11663 C C     . GLU A 1 3116 ? 129.456 117.642 145.089 1.00 131.86 ? 3116 GLU A C     1 
ATOM   11664 O O     . GLU A 1 3116 ? 129.724 117.032 144.049 1.00 131.86 ? 3116 GLU A O     1 
ATOM   11665 C CB    . GLU A 1 3116 ? 127.783 119.289 144.172 1.00 131.86 ? 3116 GLU A CB    1 
ATOM   11666 C CG    . GLU A 1 3116 ? 128.060 119.353 142.677 1.00 131.86 ? 3116 GLU A CG    1 
ATOM   11667 C CD    . GLU A 1 3116 ? 128.327 120.766 142.189 1.00 131.86 ? 3116 GLU A CD    1 
ATOM   11668 O OE1   . GLU A 1 3116 ? 128.842 121.584 142.979 1.00 131.86 ? 3116 GLU A OE1   1 
ATOM   11669 O OE2   . GLU A 1 3116 ? 128.020 121.057 141.014 1.00 131.86 ? 3116 GLU A OE2   1 
ATOM   11670 N N     . LYS A 1 3117 ? 129.527 117.086 146.295 1.00 138.42 ? 3117 LYS A N     1 
ATOM   11671 C CA    . LYS A 1 3117 ? 129.855 115.675 146.497 1.00 138.42 ? 3117 LYS A CA    1 
ATOM   11672 C C     . LYS A 1 3117 ? 128.699 115.004 147.221 1.00 138.42 ? 3117 LYS A C     1 
ATOM   11673 O O     . LYS A 1 3117 ? 128.550 115.170 148.445 1.00 138.42 ? 3117 LYS A O     1 
ATOM   11674 C CB    . LYS A 1 3117 ? 131.150 115.516 147.291 1.00 138.42 ? 3117 LYS A CB    1 
ATOM   11675 C CG    . LYS A 1 3117 ? 131.508 114.071 147.585 1.00 138.42 ? 3117 LYS A CG    1 
ATOM   11676 C CD    . LYS A 1 3117 ? 132.883 113.956 148.209 1.00 138.42 ? 3117 LYS A CD    1 
ATOM   11677 C CE    . LYS A 1 3117 ? 132.934 114.652 149.550 1.00 138.42 ? 3117 LYS A CE    1 
ATOM   11678 N NZ    . LYS A 1 3117 ? 134.008 114.077 150.399 1.00 138.42 ? 3117 LYS A NZ    1 
ATOM   11679 N N     . PRO A 1 3118 ? 127.851 114.253 146.518 1.00 144.55 ? 3118 PRO A N     1 
ATOM   11680 C CA    . PRO A 1 3118 ? 126.717 113.605 147.195 1.00 144.55 ? 3118 PRO A CA    1 
ATOM   11681 C C     . PRO A 1 3118 ? 127.138 112.609 148.261 1.00 144.55 ? 3118 PRO A C     1 
ATOM   11682 O O     . PRO A 1 3118 ? 126.391 112.392 149.223 1.00 144.55 ? 3118 PRO A O     1 
ATOM   11683 C CB    . PRO A 1 3118 ? 125.969 112.921 146.043 1.00 144.55 ? 3118 PRO A CB    1 
ATOM   11684 C CG    . PRO A 1 3118 ? 127.006 112.724 144.984 1.00 144.55 ? 3118 PRO A CG    1 
ATOM   11685 C CD    . PRO A 1 3118 ? 127.926 113.903 145.089 1.00 144.55 ? 3118 PRO A CD    1 
ATOM   11686 N N     . ASN A 1 3119 ? 128.316 112.002 148.125 1.00 145.38 ? 3119 ASN A N     1 
ATOM   11687 C CA    . ASN A 1 3119 ? 128.801 111.010 149.072 1.00 145.38 ? 3119 ASN A CA    1 
ATOM   11688 C C     . ASN A 1 3119 ? 129.528 111.633 150.258 1.00 145.38 ? 3119 ASN A C     1 
ATOM   11689 O O     . ASN A 1 3119 ? 130.302 110.942 150.930 1.00 145.38 ? 3119 ASN A O     1 
ATOM   11690 C CB    . ASN A 1 3119 ? 129.715 110.008 148.364 1.00 145.38 ? 3119 ASN A CB    1 
ATOM   11691 C CG    . ASN A 1 3119 ? 130.686 110.678 147.411 1.00 145.38 ? 3119 ASN A CG    1 
ATOM   11692 O OD1   . ASN A 1 3119 ? 130.294 111.179 146.357 1.00 145.38 ? 3119 ASN A OD1   1 
ATOM   11693 N ND2   . ASN A 1 3119 ? 131.962 110.688 147.778 1.00 145.38 ? 3119 ASN A ND2   1 
ATOM   11694 N N     . TYR A 1 3120 ? 129.302 112.915 150.527 1.00 140.09 ? 3120 TYR A N     1 
ATOM   11695 C CA    . TYR A 1 3120 ? 129.944 113.564 151.660 1.00 140.09 ? 3120 TYR A CA    1 
ATOM   11696 C C     . TYR A 1 3120 ? 129.461 112.949 152.966 1.00 140.09 ? 3120 TYR A C     1 
ATOM   11697 O O     . TYR A 1 3120 ? 128.288 112.596 153.111 1.00 140.09 ? 3120 TYR A O     1 
ATOM   11698 C CB    . TYR A 1 3120 ? 129.664 115.069 151.639 1.00 140.09 ? 3120 TYR A CB    1 
ATOM   11699 C CG    . TYR A 1 3120 ? 130.175 115.825 152.849 1.00 140.09 ? 3120 TYR A CG    1 
ATOM   11700 C CD1   . TYR A 1 3120 ? 131.388 116.500 152.809 1.00 140.09 ? 3120 TYR A CD1   1 
ATOM   11701 C CD2   . TYR A 1 3120 ? 129.424 115.899 154.018 1.00 140.09 ? 3120 TYR A CD2   1 
ATOM   11702 C CE1   . TYR A 1 3120 ? 131.853 117.195 153.908 1.00 140.09 ? 3120 TYR A CE1   1 
ATOM   11703 C CE2   . TYR A 1 3120 ? 129.879 116.592 155.117 1.00 140.09 ? 3120 TYR A CE2   1 
ATOM   11704 C CZ    . TYR A 1 3120 ? 131.092 117.238 155.059 1.00 140.09 ? 3120 TYR A CZ    1 
ATOM   11705 O OH    . TYR A 1 3120 ? 131.540 117.930 156.161 1.00 140.09 ? 3120 TYR A OH    1 
ATOM   11706 N N     . ILE A 1 3121 ? 130.378 112.820 153.920 1.00 139.93 ? 3121 ILE A N     1 
ATOM   11707 C CA    . ILE A 1 3121 ? 130.085 112.272 155.238 1.00 139.93 ? 3121 ILE A CA    1 
ATOM   11708 C C     . ILE A 1 3121 ? 130.190 113.400 156.253 1.00 139.93 ? 3121 ILE A C     1 
ATOM   11709 O O     . ILE A 1 3121 ? 131.189 114.129 156.276 1.00 139.93 ? 3121 ILE A O     1 
ATOM   11710 C CB    . ILE A 1 3121 ? 131.039 111.120 155.595 1.00 139.93 ? 3121 ILE A CB    1 
ATOM   11711 C CG1   . ILE A 1 3121 ? 131.220 110.187 154.396 1.00 139.93 ? 3121 ILE A CG1   1 
ATOM   11712 C CG2   . ILE A 1 3121 ? 130.517 110.354 156.802 1.00 139.93 ? 3121 ILE A CG2   1 
ATOM   11713 C CD1   . ILE A 1 3121 ? 129.933 109.565 153.898 1.00 139.93 ? 3121 ILE A CD1   1 
ATOM   11714 N N     . VAL A 1 3122 ? 129.168 113.540 157.091 1.00 141.85 ? 3122 VAL A N     1 
ATOM   11715 C CA    . VAL A 1 3122 ? 129.103 114.632 158.059 1.00 141.85 ? 3122 VAL A CA    1 
ATOM   11716 C C     . VAL A 1 3122 ? 129.808 114.230 159.350 1.00 141.85 ? 3122 VAL A C     1 
ATOM   11717 O O     . VAL A 1 3122 ? 129.331 113.339 160.067 1.00 141.85 ? 3122 VAL A O     1 
ATOM   11718 C CB    . VAL A 1 3122 ? 127.649 115.038 158.338 1.00 141.85 ? 3122 VAL A CB    1 
ATOM   11719 C CG1   . VAL A 1 3122 ? 127.587 116.051 159.471 1.00 141.85 ? 3122 VAL A CG1   1 
ATOM   11720 C CG2   . VAL A 1 3122 ? 127.007 115.595 157.080 1.00 141.85 ? 3122 VAL A CG2   1 
ATOM   11721 N N     . PRO A 1 3123 ? 130.930 114.860 159.688 1.00 146.11 ? 3123 PRO A N     1 
ATOM   11722 C CA    . PRO A 1 3123 ? 131.575 114.587 160.977 1.00 146.11 ? 3123 PRO A CA    1 
ATOM   11723 C C     . PRO A 1 3123 ? 131.028 115.479 162.079 1.00 146.11 ? 3123 PRO A C     1 
ATOM   11724 O O     . PRO A 1 3123 ? 130.068 116.224 161.861 1.00 146.11 ? 3123 PRO A O     1 
ATOM   11725 C CB    . PRO A 1 3123 ? 133.050 114.875 160.688 1.00 146.11 ? 3123 PRO A CB    1 
ATOM   11726 C CG    . PRO A 1 3123 ? 133.009 115.947 159.645 1.00 146.11 ? 3123 PRO A CG    1 
ATOM   11727 C CD    . PRO A 1 3123 ? 131.722 115.790 158.863 1.00 146.11 ? 3123 PRO A CD    1 
ATOM   11728 N N     . ASP A 1 3124 ? 131.619 115.405 163.265 1.00 166.35 ? 3124 ASP A N     1 
ATOM   11729 C CA    . ASP A 1 3124 ? 131.186 116.205 164.401 1.00 166.35 ? 3124 ASP A CA    1 
ATOM   11730 C C     . ASP A 1 3124 ? 132.075 117.434 164.575 1.00 166.35 ? 3124 ASP A C     1 
ATOM   11731 O O     . ASP A 1 3124 ? 133.233 117.455 164.153 1.00 166.35 ? 3124 ASP A O     1 
ATOM   11732 C CB    . ASP A 1 3124 ? 131.193 115.368 165.682 1.00 166.35 ? 3124 ASP A CB    1 
ATOM   11733 C CG    . ASP A 1 3124 ? 130.292 115.940 166.753 1.00 166.35 ? 3124 ASP A CG    1 
ATOM   11734 O OD1   . ASP A 1 3124 ? 129.097 116.165 166.468 1.00 166.35 ? 3124 ASP A OD1   1 
ATOM   11735 O OD2   . ASP A 1 3124 ? 130.775 116.168 167.880 1.00 166.35 ? 3124 ASP A OD2   1 
ATOM   11736 N N     . TYR A 1 3125 ? 131.507 118.453 165.231 1.00 174.06 ? 3125 TYR A N     1 
ATOM   11737 C CA    . TYR A 1 3125 ? 132.145 119.734 165.538 1.00 174.06 ? 3125 TYR A CA    1 
ATOM   11738 C C     . TYR A 1 3125 ? 132.333 120.632 164.318 1.00 174.06 ? 3125 TYR A C     1 
ATOM   11739 O O     . TYR A 1 3125 ? 131.377 120.910 163.586 1.00 174.06 ? 3125 TYR A O     1 
ATOM   11740 C CB    . TYR A 1 3125 ? 133.500 119.522 166.227 1.00 174.06 ? 3125 TYR A CB    1 
ATOM   11741 C CG    . TYR A 1 3125 ? 133.483 118.525 167.364 1.00 174.06 ? 3125 TYR A CG    1 
ATOM   11742 C CD1   . TYR A 1 3125 ? 132.712 118.746 168.498 1.00 174.06 ? 3125 TYR A CD1   1 
ATOM   11743 C CD2   . TYR A 1 3125 ? 134.242 117.364 167.305 1.00 174.06 ? 3125 TYR A CD2   1 
ATOM   11744 C CE1   . TYR A 1 3125 ? 132.699 117.840 169.542 1.00 174.06 ? 3125 TYR A CE1   1 
ATOM   11745 C CE2   . TYR A 1 3125 ? 134.234 116.450 168.341 1.00 174.06 ? 3125 TYR A CE2   1 
ATOM   11746 C CZ    . TYR A 1 3125 ? 133.460 116.693 169.456 1.00 174.06 ? 3125 TYR A CZ    1 
ATOM   11747 O OH    . TYR A 1 3125 ? 133.447 115.787 170.492 1.00 174.06 ? 3125 TYR A OH    1 
ATOM   11748 N N     . MET A 1 3126 ? 133.571 121.076 164.095 1.00 162.07 ? 3126 MET A N     1 
ATOM   11749 C CA    . MET A 1 3126 ? 133.887 122.210 163.233 1.00 162.07 ? 3126 MET A CA    1 
ATOM   11750 C C     . MET A 1 3126 ? 132.990 123.424 163.502 1.00 162.07 ? 3126 MET A C     1 
ATOM   11751 O O     . MET A 1 3126 ? 132.308 123.908 162.599 1.00 162.07 ? 3126 MET A O     1 
ATOM   11752 C CB    . MET A 1 3126 ? 133.825 121.843 161.755 1.00 162.07 ? 3126 MET A CB    1 
ATOM   11753 C CG    . MET A 1 3126 ? 134.905 120.898 161.283 1.00 162.07 ? 3126 MET A CG    1 
ATOM   11754 S SD    . MET A 1 3126 ? 134.713 119.294 162.055 1.00 162.07 ? 3126 MET A SD    1 
ATOM   11755 C CE    . MET A 1 3126 ? 133.050 118.933 161.500 1.00 162.07 ? 3126 MET A CE    1 
ATOM   11756 N N     . PRO A 1 3127 ? 132.978 123.946 164.735 1.00 167.21 ? 3127 PRO A N     1 
ATOM   11757 C CA    . PRO A 1 3127 ? 132.229 125.183 164.976 1.00 167.21 ? 3127 PRO A CA    1 
ATOM   11758 C C     . PRO A 1 3127 ? 133.031 126.408 164.570 1.00 167.21 ? 3127 PRO A C     1 
ATOM   11759 O O     . PRO A 1 3127 ? 133.984 126.786 165.259 1.00 167.21 ? 3127 PRO A O     1 
ATOM   11760 C CB    . PRO A 1 3127 ? 131.971 125.146 166.486 1.00 167.21 ? 3127 PRO A CB    1 
ATOM   11761 C CG    . PRO A 1 3127 ? 133.090 124.296 167.051 1.00 167.21 ? 3127 PRO A CG    1 
ATOM   11762 C CD    . PRO A 1 3127 ? 133.759 123.548 165.918 1.00 167.21 ? 3127 PRO A CD    1 
ATOM   11763 N N     . VAL A 1 3128 ? 132.659 127.040 163.460 1.00 140.64 ? 3128 VAL A N     1 
ATOM   11764 C CA    . VAL A 1 3128 ? 133.361 128.233 163.004 1.00 140.64 ? 3128 VAL A CA    1 
ATOM   11765 C C     . VAL A 1 3128 ? 132.346 129.327 162.700 1.00 140.64 ? 3128 VAL A C     1 
ATOM   11766 O O     . VAL A 1 3128 ? 132.429 130.434 163.243 1.00 140.64 ? 3128 VAL A O     1 
ATOM   11767 C CB    . VAL A 1 3128 ? 134.246 127.925 161.784 1.00 140.64 ? 3128 VAL A CB    1 
ATOM   11768 C CG1   . VAL A 1 3128 ? 134.416 129.156 160.923 1.00 140.64 ? 3128 VAL A CG1   1 
ATOM   11769 C CG2   . VAL A 1 3128 ? 135.595 127.404 162.239 1.00 140.64 ? 3128 VAL A CG2   1 
ATOM   11770 N N     . VAL A 1 3129 ? 131.382 129.025 161.836 1.00 135.54 ? 3129 VAL A N     1 
ATOM   11771 C CA    . VAL A 1 3129 ? 130.303 129.946 161.506 1.00 135.54 ? 3129 VAL A CA    1 
ATOM   11772 C C     . VAL A 1 3129 ? 129.083 129.536 162.312 1.00 135.54 ? 3129 VAL A C     1 
ATOM   11773 O O     . VAL A 1 3129 ? 128.553 128.434 162.131 1.00 135.54 ? 3129 VAL A O     1 
ATOM   11774 C CB    . VAL A 1 3129 ? 129.995 129.943 160.002 1.00 135.54 ? 3129 VAL A CB    1 
ATOM   11775 C CG1   . VAL A 1 3129 ? 128.670 130.639 159.733 1.00 135.54 ? 3129 VAL A CG1   1 
ATOM   11776 C CG2   . VAL A 1 3129 ? 131.119 130.608 159.232 1.00 135.54 ? 3129 VAL A CG2   1 
ATOM   11777 N N     . TYR A 1 3130 ? 128.638 130.418 163.208 1.00 153.14 ? 3130 TYR A N     1 
ATOM   11778 C CA    . TYR A 1 3130 ? 127.470 130.104 164.022 1.00 153.14 ? 3130 TYR A CA    1 
ATOM   11779 C C     . TYR A 1 3130 ? 126.231 129.930 163.156 1.00 153.14 ? 3130 TYR A C     1 
ATOM   11780 O O     . TYR A 1 3130 ? 125.422 129.023 163.388 1.00 153.14 ? 3130 TYR A O     1 
ATOM   11781 C CB    . TYR A 1 3130 ? 127.245 131.195 165.067 1.00 153.14 ? 3130 TYR A CB    1 
ATOM   11782 C CG    . TYR A 1 3130 ? 126.520 130.712 166.304 1.00 153.14 ? 3130 TYR A CG    1 
ATOM   11783 C CD1   . TYR A 1 3130 ? 126.275 129.360 166.504 1.00 153.14 ? 3130 TYR A CD1   1 
ATOM   11784 C CD2   . TYR A 1 3130 ? 126.085 131.607 167.271 1.00 153.14 ? 3130 TYR A CD2   1 
ATOM   11785 C CE1   . TYR A 1 3130 ? 125.617 128.913 167.630 1.00 153.14 ? 3130 TYR A CE1   1 
ATOM   11786 C CE2   . TYR A 1 3130 ? 125.426 131.168 168.402 1.00 153.14 ? 3130 TYR A CE2   1 
ATOM   11787 C CZ    . TYR A 1 3130 ? 125.195 129.821 168.576 1.00 153.14 ? 3130 TYR A CZ    1 
ATOM   11788 O OH    . TYR A 1 3130 ? 124.538 129.380 169.701 1.00 153.14 ? 3130 TYR A OH    1 
ATOM   11789 N N     . ASP A 1 3131 ? 126.065 130.788 162.153 1.00 145.07 ? 3131 ASP A N     1 
ATOM   11790 C CA    . ASP A 1 3131 ? 124.917 130.709 161.252 1.00 145.07 ? 3131 ASP A CA    1 
ATOM   11791 C C     . ASP A 1 3131 ? 125.279 129.928 159.988 1.00 145.07 ? 3131 ASP A C     1 
ATOM   11792 O O     . ASP A 1 3131 ? 125.205 130.423 158.864 1.00 145.07 ? 3131 ASP A O     1 
ATOM   11793 C CB    . ASP A 1 3131 ? 124.411 132.107 160.922 1.00 145.07 ? 3131 ASP A CB    1 
ATOM   11794 C CG    . ASP A 1 3131 ? 123.965 132.869 162.154 1.00 145.07 ? 3131 ASP A CG    1 
ATOM   11795 O OD1   . ASP A 1 3131 ? 123.868 132.246 163.232 1.00 145.07 ? 3131 ASP A OD1   1 
ATOM   11796 O OD2   . ASP A 1 3131 ? 123.713 134.087 162.046 1.00 145.07 ? 3131 ASP A OD2   1 
ATOM   11797 N N     . LYS A 1 3132 ? 125.695 128.681 160.198 1.00 139.75 ? 3132 LYS A N     1 
ATOM   11798 C CA    . LYS A 1 3132 ? 125.871 127.760 159.085 1.00 139.75 ? 3132 LYS A CA    1 
ATOM   11799 C C     . LYS A 1 3132 ? 124.510 127.448 158.476 1.00 139.75 ? 3132 LYS A C     1 
ATOM   11800 O O     . LYS A 1 3132 ? 123.547 127.177 159.200 1.00 139.75 ? 3132 LYS A O     1 
ATOM   11801 C CB    . LYS A 1 3132 ? 126.558 126.480 159.557 1.00 139.75 ? 3132 LYS A CB    1 
ATOM   11802 C CG    . LYS A 1 3132 ? 126.504 125.336 158.561 1.00 139.75 ? 3132 LYS A CG    1 
ATOM   11803 C CD    . LYS A 1 3132 ? 127.272 125.652 157.287 1.00 139.75 ? 3132 LYS A CD    1 
ATOM   11804 C CE    . LYS A 1 3132 ? 128.723 125.990 157.575 1.00 139.75 ? 3132 LYS A CE    1 
ATOM   11805 N NZ    . LYS A 1 3132 ? 129.508 126.121 156.318 1.00 139.75 ? 3132 LYS A NZ    1 
ATOM   11806 N N     . LEU A 1 3133 ? 124.428 127.493 157.145 1.00 151.90 ? 3133 LEU A N     1 
ATOM   11807 C CA    . LEU A 1 3133 ? 123.124 127.422 156.488 1.00 151.90 ? 3133 LEU A CA    1 
ATOM   11808 C C     . LEU A 1 3133 ? 122.379 126.126 156.789 1.00 151.90 ? 3133 LEU A C     1 
ATOM   11809 O O     . LEU A 1 3133 ? 121.218 126.200 157.229 1.00 151.90 ? 3133 LEU A O     1 
ATOM   11810 C CB    . LEU A 1 3133 ? 123.297 127.653 154.981 1.00 151.90 ? 3133 LEU A CB    1 
ATOM   11811 C CG    . LEU A 1 3133 ? 122.032 127.932 154.167 1.00 151.90 ? 3133 LEU A CG    1 
ATOM   11812 C CD1   . LEU A 1 3133 ? 121.609 129.388 154.309 1.00 151.90 ? 3133 LEU A CD1   1 
ATOM   11813 C CD2   . LEU A 1 3133 ? 122.242 127.568 152.703 1.00 151.90 ? 3133 LEU A CD2   1 
ATOM   11814 N N     . PRO A 1 3134 ? 122.952 124.925 156.592 1.00 153.88 ? 3134 PRO A N     1 
ATOM   11815 C CA    . PRO A 1 3134 ? 122.259 123.717 157.057 1.00 153.88 ? 3134 PRO A CA    1 
ATOM   11816 C C     . PRO A 1 3134 ? 122.751 123.260 158.421 1.00 153.88 ? 3134 PRO A C     1 
ATOM   11817 O O     . PRO A 1 3134 ? 123.885 123.565 158.803 1.00 153.88 ? 3134 PRO A O     1 
ATOM   11818 C CB    . PRO A 1 3134 ? 122.589 122.694 155.966 1.00 153.88 ? 3134 PRO A CB    1 
ATOM   11819 C CG    . PRO A 1 3134 ? 123.939 123.135 155.435 1.00 153.88 ? 3134 PRO A CG    1 
ATOM   11820 C CD    . PRO A 1 3134 ? 124.179 124.572 155.853 1.00 153.88 ? 3134 PRO A CD    1 
ATOM   11821 N N     . GLN A 1 3135 ? 121.921 122.542 159.176 1.00 155.03 ? 3135 GLN A N     1 
ATOM   11822 C CA    . GLN A 1 3135 ? 122.454 121.852 160.348 1.00 155.03 ? 3135 GLN A CA    1 
ATOM   11823 C C     . GLN A 1 3135 ? 123.452 120.773 159.949 1.00 155.03 ? 3135 GLN A C     1 
ATOM   11824 O O     . GLN A 1 3135 ? 124.571 120.773 160.492 1.00 155.03 ? 3135 GLN A O     1 
ATOM   11825 C CB    . GLN A 1 3135 ? 121.311 121.299 161.209 1.00 155.03 ? 3135 GLN A CB    1 
ATOM   11826 C CG    . GLN A 1 3135 ? 121.708 120.132 162.117 1.00 155.03 ? 3135 GLN A CG    1 
ATOM   11827 C CD    . GLN A 1 3135 ? 122.882 120.441 163.038 1.00 155.03 ? 3135 GLN A CD    1 
ATOM   11828 O OE1   . GLN A 1 3135 ? 123.182 121.600 163.324 1.00 155.03 ? 3135 GLN A OE1   1 
ATOM   11829 N NE2   . GLN A 1 3135 ? 123.558 119.395 163.498 1.00 155.03 ? 3135 GLN A NE2   1 
ATOM   11830 N N     . PRO A 1 3136 ? 123.148 119.848 159.037 1.00 146.95 ? 3136 PRO A N     1 
ATOM   11831 C CA    . PRO A 1 3136 ? 124.207 119.026 158.463 1.00 146.95 ? 3136 PRO A CA    1 
ATOM   11832 C C     . PRO A 1 3136 ? 124.832 119.732 157.275 1.00 146.95 ? 3136 PRO A C     1 
ATOM   11833 O O     . PRO A 1 3136 ? 124.190 119.891 156.226 1.00 146.95 ? 3136 PRO A O     1 
ATOM   11834 C CB    . PRO A 1 3136 ? 123.474 117.747 158.039 1.00 146.95 ? 3136 PRO A CB    1 
ATOM   11835 C CG    . PRO A 1 3136 ? 122.068 118.178 157.783 1.00 146.95 ? 3136 PRO A CG    1 
ATOM   11836 C CD    . PRO A 1 3136 ? 121.839 119.517 158.443 1.00 146.95 ? 3136 PRO A CD    1 
ATOM   11837 N N     . PRO A 1 3137 ? 126.080 120.171 157.395 1.00 134.15 ? 3137 PRO A N     1 
ATOM   11838 C CA    . PRO A 1 3137 ? 126.696 120.922 156.301 1.00 134.15 ? 3137 PRO A CA    1 
ATOM   11839 C C     . PRO A 1 3137 ? 126.900 120.054 155.074 1.00 134.15 ? 3137 PRO A C     1 
ATOM   11840 O O     . PRO A 1 3137 ? 127.117 118.844 155.165 1.00 134.15 ? 3137 PRO A O     1 
ATOM   11841 C CB    . PRO A 1 3137 ? 128.035 121.375 156.891 1.00 134.15 ? 3137 PRO A CB    1 
ATOM   11842 C CG    . PRO A 1 3137 ? 128.335 120.368 157.942 1.00 134.15 ? 3137 PRO A CG    1 
ATOM   11843 C CD    . PRO A 1 3137 ? 127.011 119.951 158.514 1.00 134.15 ? 3137 PRO A CD    1 
ATOM   11844 N N     . SER A 1 3138 ? 126.819 120.689 153.913 1.00 120.62 ? 3138 SER A N     1 
ATOM   11845 C CA    . SER A 1 3138 ? 127.105 120.032 152.653 1.00 120.62 ? 3138 SER A CA    1 
ATOM   11846 C C     . SER A 1 3138 ? 128.575 120.233 152.299 1.00 120.62 ? 3138 SER A C     1 
ATOM   11847 O O     . SER A 1 3138 ? 129.336 120.874 153.027 1.00 120.62 ? 3138 SER A O     1 
ATOM   11848 C CB    . SER A 1 3138 ? 126.189 120.561 151.551 1.00 120.62 ? 3138 SER A CB    1 
ATOM   11849 O OG    . SER A 1 3138 ? 126.630 120.125 150.278 1.00 120.62 ? 3138 SER A OG    1 
ATOM   11850 N N     . HIS A 1 3139 ? 128.977 119.672 151.159 1.00 121.44 ? 3139 HIS A N     1 
ATOM   11851 C CA    . HIS A 1 3139 ? 130.370 119.771 150.738 1.00 121.44 ? 3139 HIS A CA    1 
ATOM   11852 C C     . HIS A 1 3139 ? 130.772 121.223 150.509 1.00 121.44 ? 3139 HIS A C     1 
ATOM   11853 O O     . HIS A 1 3139 ? 131.814 121.676 150.995 1.00 121.44 ? 3139 HIS A O     1 
ATOM   11854 C CB    . HIS A 1 3139 ? 130.586 118.940 149.473 1.00 121.44 ? 3139 HIS A CB    1 
ATOM   11855 C CG    . HIS A 1 3139 ? 131.940 119.108 148.860 1.00 121.44 ? 3139 HIS A CG    1 
ATOM   11856 N ND1   . HIS A 1 3139 ? 132.266 120.179 148.058 1.00 121.44 ? 3139 HIS A ND1   1 
ATOM   11857 C CD2   . HIS A 1 3139 ? 133.050 118.335 148.925 1.00 121.44 ? 3139 HIS A CD2   1 
ATOM   11858 C CE1   . HIS A 1 3139 ? 133.519 120.062 147.657 1.00 121.44 ? 3139 HIS A CE1   1 
ATOM   11859 N NE2   . HIS A 1 3139 ? 134.017 118.951 148.170 1.00 121.44 ? 3139 HIS A NE2   1 
ATOM   11860 N N     . ARG A 1 3140 ? 129.948 121.972 149.776 1.00 116.77 ? 3140 ARG A N     1 
ATOM   11861 C CA    . ARG A 1 3140 ? 130.272 123.367 149.505 1.00 116.77 ? 3140 ARG A CA    1 
ATOM   11862 C C     . ARG A 1 3140 ? 130.259 124.194 150.784 1.00 116.77 ? 3140 ARG A C     1 
ATOM   11863 O O     . ARG A 1 3140 ? 131.125 125.055 150.984 1.00 116.77 ? 3140 ARG A O     1 
ATOM   11864 C CB    . ARG A 1 3140 ? 129.297 123.934 148.476 1.00 116.77 ? 3140 ARG A CB    1 
ATOM   11865 C CG    . ARG A 1 3140 ? 129.462 125.413 148.208 1.00 116.77 ? 3140 ARG A CG    1 
ATOM   11866 C CD    . ARG A 1 3140 ? 128.932 125.764 146.833 1.00 116.77 ? 3140 ARG A CD    1 
ATOM   11867 N NE    . ARG A 1 3140 ? 129.298 124.752 145.850 1.00 116.77 ? 3140 ARG A NE    1 
ATOM   11868 C CZ    . ARG A 1 3140 ? 128.960 124.794 144.569 1.00 116.77 ? 3140 ARG A CZ    1 
ATOM   11869 N NH1   . ARG A 1 3140 ? 128.244 125.791 144.076 1.00 116.77 ? 3140 ARG A NH1   1 
ATOM   11870 N NH2   . ARG A 1 3140 ? 129.350 123.813 143.762 1.00 116.77 ? 3140 ARG A NH2   1 
ATOM   11871 N N     . GLU A 1 3141 ? 129.283 123.947 151.659 1.00 119.26 ? 3141 GLU A N     1 
ATOM   11872 C CA    . GLU A 1 3141 ? 129.228 124.660 152.930 1.00 119.26 ? 3141 GLU A CA    1 
ATOM   11873 C C     . GLU A 1 3141 ? 130.439 124.337 153.791 1.00 119.26 ? 3141 GLU A C     1 
ATOM   11874 O O     . GLU A 1 3141 ? 131.012 125.226 154.430 1.00 119.26 ? 3141 GLU A O     1 
ATOM   11875 C CB    . GLU A 1 3141 ? 127.934 124.321 153.671 1.00 119.26 ? 3141 GLU A CB    1 
ATOM   11876 C CG    . GLU A 1 3141 ? 126.638 124.865 153.051 1.00 119.26 ? 3141 GLU A CG    1 
ATOM   11877 C CD    . GLU A 1 3141 ? 126.384 124.432 151.610 1.00 119.26 ? 3141 GLU A CD    1 
ATOM   11878 O OE1   . GLU A 1 3141 ? 127.124 123.577 151.079 1.00 119.26 ? 3141 GLU A OE1   1 
ATOM   11879 O OE2   . GLU A 1 3141 ? 125.430 124.960 151.002 1.00 119.26 ? 3141 GLU A OE2   1 
ATOM   11880 N N     . ALA A 1 3142 ? 130.850 123.069 153.815 1.00 115.17 ? 3142 ALA A N     1 
ATOM   11881 C CA    . ALA A 1 3142 ? 132.050 122.707 154.559 1.00 115.17 ? 3142 ALA A CA    1 
ATOM   11882 C C     . ALA A 1 3142 ? 133.279 123.400 153.985 1.00 115.17 ? 3142 ALA A C     1 
ATOM   11883 O O     . ALA A 1 3142 ? 134.148 123.859 154.734 1.00 115.17 ? 3142 ALA A O     1 
ATOM   11884 C CB    . ALA A 1 3142 ? 132.235 121.192 154.555 1.00 115.17 ? 3142 ALA A CB    1 
ATOM   11885 N N     . ILE A 1 3143 ? 133.364 123.494 152.658 1.00 105.60 ? 3143 ILE A N     1 
ATOM   11886 C CA    . ILE A 1 3143 ? 134.516 124.138 152.035 1.00 105.60 ? 3143 ILE A CA    1 
ATOM   11887 C C     . ILE A 1 3143 ? 134.560 125.621 152.382 1.00 105.60 ? 3143 ILE A C     1 
ATOM   11888 O O     . ILE A 1 3143 ? 135.618 126.164 152.723 1.00 105.60 ? 3143 ILE A O     1 
ATOM   11889 C CB    . ILE A 1 3143 ? 134.489 123.909 150.515 1.00 105.60 ? 3143 ILE A CB    1 
ATOM   11890 C CG1   . ILE A 1 3143 ? 134.880 122.467 150.201 1.00 105.60 ? 3143 ILE A CG1   1 
ATOM   11891 C CG2   . ILE A 1 3143 ? 135.410 124.885 149.810 1.00 105.60 ? 3143 ILE A CG2   1 
ATOM   11892 C CD1   . ILE A 1 3143 ? 136.371 122.243 150.128 1.00 105.60 ? 3143 ILE A CD1   1 
ATOM   11893 N N     . VAL A 1 3144 ? 133.417 126.302 152.301 1.00 102.79 ? 3144 VAL A N     1 
ATOM   11894 C CA    . VAL A 1 3144 ? 133.406 127.730 152.608 1.00 102.79 ? 3144 VAL A CA    1 
ATOM   11895 C C     . VAL A 1 3144 ? 133.693 127.960 154.087 1.00 102.79 ? 3144 VAL A C     1 
ATOM   11896 O O     . VAL A 1 3144 ? 134.366 128.933 154.463 1.00 102.79 ? 3144 VAL A O     1 
ATOM   11897 C CB    . VAL A 1 3144 ? 132.079 128.373 152.159 1.00 102.79 ? 3144 VAL A CB    1 
ATOM   11898 C CG1   . VAL A 1 3144 ? 130.953 128.047 153.107 1.00 102.79 ? 3144 VAL A CG1   1 
ATOM   11899 C CG2   . VAL A 1 3144 ? 132.241 129.871 152.051 1.00 102.79 ? 3144 VAL A CG2   1 
ATOM   11900 N N     . ASN A 1 3145 ? 133.211 127.062 154.950 1.00 109.20 ? 3145 ASN A N     1 
ATOM   11901 C CA    . ASN A 1 3145 ? 133.528 127.173 156.367 1.00 109.20 ? 3145 ASN A CA    1 
ATOM   11902 C C     . ASN A 1 3145 ? 135.016 126.977 156.605 1.00 109.20 ? 3145 ASN A C     1 
ATOM   11903 O O     . ASN A 1 3145 ? 135.613 127.656 157.445 1.00 109.20 ? 3145 ASN A O     1 
ATOM   11904 C CB    . ASN A 1 3145 ? 132.721 126.163 157.173 1.00 109.20 ? 3145 ASN A CB    1 
ATOM   11905 C CG    . ASN A 1 3145 ? 132.968 126.286 158.655 1.00 109.20 ? 3145 ASN A CG    1 
ATOM   11906 O OD1   . ASN A 1 3145 ? 132.319 127.077 159.338 1.00 109.20 ? 3145 ASN A OD1   1 
ATOM   11907 N ND2   . ASN A 1 3145 ? 133.918 125.513 159.163 1.00 109.20 ? 3145 ASN A ND2   1 
ATOM   11908 N N     . SER A 1 3146 ? 135.634 126.054 155.871 1.00 108.32 ? 3146 SER A N     1 
ATOM   11909 C CA    . SER A 1 3146 ? 137.077 125.882 155.977 1.00 108.32 ? 3146 SER A CA    1 
ATOM   11910 C C     . SER A 1 3146 ? 137.814 127.130 155.510 1.00 108.32 ? 3146 SER A C     1 
ATOM   11911 O O     . SER A 1 3146 ? 138.842 127.499 156.082 1.00 108.32 ? 3146 SER A O     1 
ATOM   11912 C CB    . SER A 1 3146 ? 137.524 124.667 155.171 1.00 108.32 ? 3146 SER A CB    1 
ATOM   11913 O OG    . SER A 1 3146 ? 138.056 125.068 153.922 1.00 108.32 ? 3146 SER A OG    1 
ATOM   11914 N N     . CYS A 1 3147 ? 137.312 127.789 154.465 1.00 98.31  ? 3147 CYS A N     1 
ATOM   11915 C CA    . CYS A 1 3147 ? 137.958 129.009 153.989 1.00 98.31  ? 3147 CYS A CA    1 
ATOM   11916 C C     . CYS A 1 3147 ? 137.911 130.107 155.047 1.00 98.31  ? 3147 CYS A C     1 
ATOM   11917 O O     . CYS A 1 3147 ? 138.925 130.764 155.338 1.00 98.31  ? 3147 CYS A O     1 
ATOM   11918 C CB    . CYS A 1 3147 ? 137.297 129.480 152.695 1.00 98.31  ? 3147 CYS A CB    1 
ATOM   11919 S SG    . CYS A 1 3147 ? 137.540 128.375 151.293 1.00 98.31  ? 3147 CYS A SG    1 
ATOM   11920 N N     . VAL A 1 3148 ? 136.736 130.323 155.640 1.00 99.18  ? 3148 VAL A N     1 
ATOM   11921 C CA    . VAL A 1 3148 ? 136.654 131.364 156.660 1.00 99.18  ? 3148 VAL A CA    1 
ATOM   11922 C C     . VAL A 1 3148 ? 137.443 130.961 157.900 1.00 99.18  ? 3148 VAL A C     1 
ATOM   11923 O O     . VAL A 1 3148 ? 137.995 131.820 158.598 1.00 99.18  ? 3148 VAL A O     1 
ATOM   11924 C CB    . VAL A 1 3148 ? 135.190 131.706 156.984 1.00 99.18  ? 3148 VAL A CB    1 
ATOM   11925 C CG1   . VAL A 1 3148 ? 134.445 132.048 155.708 1.00 99.18  ? 3148 VAL A CG1   1 
ATOM   11926 C CG2   . VAL A 1 3148 ? 134.514 130.568 157.697 1.00 99.18  ? 3148 VAL A CG2   1 
ATOM   11927 N N     . PHE A 1 3149 ? 137.546 129.660 158.179 1.00 102.03 ? 3149 PHE A N     1 
ATOM   11928 C CA    . PHE A 1 3149 ? 138.419 129.207 159.255 1.00 102.03 ? 3149 PHE A CA    1 
ATOM   11929 C C     . PHE A 1 3149 ? 139.876 129.511 158.940 1.00 102.03 ? 3149 PHE A C     1 
ATOM   11930 O O     . PHE A 1 3149 ? 140.658 129.836 159.838 1.00 102.03 ? 3149 PHE A O     1 
ATOM   11931 C CB    . PHE A 1 3149 ? 138.230 127.712 159.494 1.00 102.03 ? 3149 PHE A CB    1 
ATOM   11932 C CG    . PHE A 1 3149 ? 139.251 127.115 160.415 1.00 102.03 ? 3149 PHE A CG    1 
ATOM   11933 C CD1   . PHE A 1 3149 ? 139.072 127.160 161.784 1.00 102.03 ? 3149 PHE A CD1   1 
ATOM   11934 C CD2   . PHE A 1 3149 ? 140.391 126.512 159.914 1.00 102.03 ? 3149 PHE A CD2   1 
ATOM   11935 C CE1   . PHE A 1 3149 ? 140.007 126.614 162.636 1.00 102.03 ? 3149 PHE A CE1   1 
ATOM   11936 C CE2   . PHE A 1 3149 ? 141.331 125.972 160.761 1.00 102.03 ? 3149 PHE A CE2   1 
ATOM   11937 C CZ    . PHE A 1 3149 ? 141.136 126.015 162.123 1.00 102.03 ? 3149 PHE A CZ    1 
ATOM   11938 N N     . VAL A 1 3150 ? 140.264 129.380 157.672 1.00 94.70  ? 3150 VAL A N     1 
ATOM   11939 C CA    . VAL A 1 3150 ? 141.630 129.701 157.271 1.00 94.70  ? 3150 VAL A CA    1 
ATOM   11940 C C     . VAL A 1 3150 ? 141.920 131.172 157.527 1.00 94.70  ? 3150 VAL A C     1 
ATOM   11941 O O     . VAL A 1 3150 ? 142.976 131.533 158.063 1.00 94.70  ? 3150 VAL A O     1 
ATOM   11942 C CB    . VAL A 1 3150 ? 141.850 129.327 155.795 1.00 94.70  ? 3150 VAL A CB    1 
ATOM   11943 C CG1   . VAL A 1 3150 ? 143.044 130.065 155.233 1.00 94.70  ? 3150 VAL A CG1   1 
ATOM   11944 C CG2   . VAL A 1 3150 ? 142.034 127.833 155.657 1.00 94.70  ? 3150 VAL A CG2   1 
ATOM   11945 N N     . HIS A 1 3151 ? 140.983 132.043 157.155 1.00 89.92  ? 3151 HIS A N     1 
ATOM   11946 C CA    . HIS A 1 3151 ? 141.177 133.465 157.432 1.00 89.92  ? 3151 HIS A CA    1 
ATOM   11947 C C     . HIS A 1 3151 ? 141.250 133.733 158.933 1.00 89.92  ? 3151 HIS A C     1 
ATOM   11948 O O     . HIS A 1 3151 ? 142.081 134.529 159.395 1.00 89.92  ? 3151 HIS A O     1 
ATOM   11949 C CB    . HIS A 1 3151 ? 140.065 134.290 156.794 1.00 89.92  ? 3151 HIS A CB    1 
ATOM   11950 C CG    . HIS A 1 3151 ? 140.301 135.765 156.858 1.00 89.92  ? 3151 HIS A CG    1 
ATOM   11951 N ND1   . HIS A 1 3151 ? 140.715 136.500 155.770 1.00 89.92  ? 3151 HIS A ND1   1 
ATOM   11952 C CD2   . HIS A 1 3151 ? 140.181 136.643 157.881 1.00 89.92  ? 3151 HIS A CD2   1 
ATOM   11953 C CE1   . HIS A 1 3151 ? 140.842 137.767 156.119 1.00 89.92  ? 3151 HIS A CE1   1 
ATOM   11954 N NE2   . HIS A 1 3151 ? 140.523 137.881 157.395 1.00 89.92  ? 3151 HIS A NE2   1 
ATOM   11955 N N     . GLN A 1 3152 ? 140.389 133.076 159.711 1.00 99.03  ? 3152 GLN A N     1 
ATOM   11956 C CA    . GLN A 1 3152 ? 140.425 133.258 161.158 1.00 99.03  ? 3152 GLN A CA    1 
ATOM   11957 C C     . GLN A 1 3152 ? 141.762 132.812 161.734 1.00 99.03  ? 3152 GLN A C     1 
ATOM   11958 O O     . GLN A 1 3152 ? 142.299 133.449 162.648 1.00 99.03  ? 3152 GLN A O     1 
ATOM   11959 C CB    . GLN A 1 3152 ? 139.276 132.494 161.812 1.00 99.03  ? 3152 GLN A CB    1 
ATOM   11960 C CG    . GLN A 1 3152 ? 138.765 133.124 163.099 1.00 99.03  ? 3152 GLN A CG    1 
ATOM   11961 C CD    . GLN A 1 3152 ? 139.583 132.723 164.312 1.00 99.03  ? 3152 GLN A CD    1 
ATOM   11962 O OE1   . GLN A 1 3152 ? 140.390 131.796 164.253 1.00 99.03  ? 3152 GLN A OE1   1 
ATOM   11963 N NE2   . GLN A 1 3152 ? 139.380 133.424 165.420 1.00 99.03  ? 3152 GLN A NE2   1 
ATOM   11964 N N     . THR A 1 3153 ? 142.312 131.711 161.222 1.00 96.97  ? 3153 THR A N     1 
ATOM   11965 C CA    . THR A 1 3153 ? 143.609 131.249 161.700 1.00 96.97  ? 3153 THR A CA    1 
ATOM   11966 C C     . THR A 1 3153 ? 144.723 132.195 161.292 1.00 96.97  ? 3153 THR A C     1 
ATOM   11967 O O     . THR A 1 3153 ? 145.702 132.335 162.025 1.00 96.97  ? 3153 THR A O     1 
ATOM   11968 C CB    . THR A 1 3153 ? 143.909 129.847 161.187 1.00 96.97  ? 3153 THR A CB    1 
ATOM   11969 O OG1   . THR A 1 3153 ? 143.619 129.776 159.787 1.00 96.97  ? 3153 THR A OG1   1 
ATOM   11970 C CG2   . THR A 1 3153 ? 143.075 128.831 161.934 1.00 96.97  ? 3153 THR A CG2   1 
ATOM   11971 N N     . LEU A 1 3154 ? 144.608 132.841 160.130 1.00 90.57  ? 3154 LEU A N     1 
ATOM   11972 C CA    . LEU A 1 3154 ? 145.571 133.887 159.798 1.00 90.57  ? 3154 LEU A CA    1 
ATOM   11973 C C     . LEU A 1 3154 ? 145.518 135.017 160.815 1.00 90.57  ? 3154 LEU A C     1 
ATOM   11974 O O     . LEU A 1 3154 ? 146.560 135.511 161.265 1.00 90.57  ? 3154 LEU A O     1 
ATOM   11975 C CB    . LEU A 1 3154 ? 145.319 134.431 158.397 1.00 90.57  ? 3154 LEU A CB    1 
ATOM   11976 C CG    . LEU A 1 3154 ? 146.290 133.948 157.328 1.00 90.57  ? 3154 LEU A CG    1 
ATOM   11977 C CD1   . LEU A 1 3154 ? 147.609 134.674 157.472 1.00 90.57  ? 3154 LEU A CD1   1 
ATOM   11978 C CD2   . LEU A 1 3154 ? 146.489 132.457 157.427 1.00 90.57  ? 3154 LEU A CD2   1 
ATOM   11979 N N     . HIS A 1 3155 ? 144.309 135.437 161.192 1.00 97.44  ? 3155 HIS A N     1 
ATOM   11980 C CA    . HIS A 1 3155 ? 144.183 136.480 162.207 1.00 97.44  ? 3155 HIS A CA    1 
ATOM   11981 C C     . HIS A 1 3155 ? 144.810 136.038 163.523 1.00 97.44  ? 3155 HIS A C     1 
ATOM   11982 O O     . HIS A 1 3155 ? 145.555 136.793 164.160 1.00 97.44  ? 3155 HIS A O     1 
ATOM   11983 C CB    . HIS A 1 3155 ? 142.715 136.844 162.416 1.00 97.44  ? 3155 HIS A CB    1 
ATOM   11984 C CG    . HIS A 1 3155 ? 142.237 137.949 161.529 1.00 97.44  ? 3155 HIS A CG    1 
ATOM   11985 N ND1   . HIS A 1 3155 ? 140.902 138.250 161.371 1.00 97.44  ? 3155 HIS A ND1   1 
ATOM   11986 C CD2   . HIS A 1 3155 ? 142.915 138.824 160.752 1.00 97.44  ? 3155 HIS A CD2   1 
ATOM   11987 C CE1   . HIS A 1 3155 ? 140.778 139.263 160.532 1.00 97.44  ? 3155 HIS A CE1   1 
ATOM   11988 N NE2   . HIS A 1 3155 ? 141.985 139.630 160.142 1.00 97.44  ? 3155 HIS A NE2   1 
ATOM   11989 N N     . GLN A 1 3156 ? 144.521 134.807 163.941 1.00 104.61 ? 3156 GLN A N     1 
ATOM   11990 C CA    . GLN A 1 3156 ? 145.056 134.306 165.202 1.00 104.61 ? 3156 GLN A CA    1 
ATOM   11991 C C     . GLN A 1 3156 ? 146.574 134.188 165.151 1.00 104.61 ? 3156 GLN A C     1 
ATOM   11992 O O     . GLN A 1 3156 ? 147.258 134.483 166.137 1.00 104.61 ? 3156 GLN A O     1 
ATOM   11993 C CB    . GLN A 1 3156 ? 144.414 132.961 165.542 1.00 104.61 ? 3156 GLN A CB    1 
ATOM   11994 C CG    . GLN A 1 3156 ? 145.160 132.154 166.588 1.00 104.61 ? 3156 GLN A CG    1 
ATOM   11995 C CD    . GLN A 1 3156 ? 144.870 130.672 166.490 1.00 104.61 ? 3156 GLN A CD    1 
ATOM   11996 O OE1   . GLN A 1 3156 ? 145.785 129.851 166.459 1.00 104.61 ? 3156 GLN A OE1   1 
ATOM   11997 N NE2   . GLN A 1 3156 ? 143.591 130.320 166.446 1.00 104.61 ? 3156 GLN A NE2   1 
ATOM   11998 N N     . ALA A 1 3157 ? 147.119 133.755 164.013 1.00 102.53 ? 3157 ALA A N     1 
ATOM   11999 C CA    . ALA A 1 3157 ? 148.565 133.643 163.875 1.00 102.53 ? 3157 ALA A CA    1 
ATOM   12000 C C     . ALA A 1 3157 ? 149.231 135.008 163.931 1.00 102.53 ? 3157 ALA A C     1 
ATOM   12001 O O     . ALA A 1 3157 ? 150.285 135.166 164.556 1.00 102.53 ? 3157 ALA A O     1 
ATOM   12002 C CB    . ALA A 1 3157 ? 148.913 132.929 162.570 1.00 102.53 ? 3157 ALA A CB    1 
ATOM   12003 N N     . ASN A 1 3158 ? 148.636 136.009 163.281 1.00 107.50 ? 3158 ASN A N     1 
ATOM   12004 C CA    . ASN A 1 3158 ? 149.180 137.359 163.383 1.00 107.50 ? 3158 ASN A CA    1 
ATOM   12005 C C     . ASN A 1 3158 ? 149.136 137.860 164.819 1.00 107.50 ? 3158 ASN A C     1 
ATOM   12006 O O     . ASN A 1 3158 ? 150.094 138.477 165.299 1.00 107.50 ? 3158 ASN A O     1 
ATOM   12007 C CB    . ASN A 1 3158 ? 148.424 138.310 162.461 1.00 107.50 ? 3158 ASN A CB    1 
ATOM   12008 C CG    . ASN A 1 3158 ? 149.278 138.808 161.322 1.00 107.50 ? 3158 ASN A CG    1 
ATOM   12009 O OD1   . ASN A 1 3158 ? 150.358 138.280 161.068 1.00 107.50 ? 3158 ASN A OD1   1 
ATOM   12010 N ND2   . ASN A 1 3158 ? 148.803 139.835 160.633 1.00 107.50 ? 3158 ASN A ND2   1 
ATOM   12011 N N     . ALA A 1 3159 ? 148.032 137.601 165.523 1.00 107.34 ? 3159 ALA A N     1 
ATOM   12012 C CA    . ALA A 1 3159 ? 147.931 138.032 166.914 1.00 107.34 ? 3159 ALA A CA    1 
ATOM   12013 C C     . ALA A 1 3159 ? 148.983 137.353 167.782 1.00 107.34 ? 3159 ALA A C     1 
ATOM   12014 O O     . ALA A 1 3159 ? 149.610 137.999 168.630 1.00 107.34 ? 3159 ALA A O     1 
ATOM   12015 C CB    . ALA A 1 3159 ? 146.529 137.749 167.449 1.00 107.34 ? 3159 ALA A CB    1 
ATOM   12016 N N     . ARG A 1 3160 ? 149.191 136.050 167.585 1.00 111.60 ? 3160 ARG A N     1 
ATOM   12017 C CA    . ARG A 1 3160 ? 150.205 135.336 168.355 1.00 111.60 ? 3160 ARG A CA    1 
ATOM   12018 C C     . ARG A 1 3160 ? 151.604 135.853 168.044 1.00 111.60 ? 3160 ARG A C     1 
ATOM   12019 O O     . ARG A 1 3160 ? 152.420 136.036 168.955 1.00 111.60 ? 3160 ARG A O     1 
ATOM   12020 C CB    . ARG A 1 3160 ? 150.112 133.835 168.083 1.00 111.60 ? 3160 ARG A CB    1 
ATOM   12021 C CG    . ARG A 1 3160 ? 151.431 133.096 168.232 1.00 111.60 ? 3160 ARG A CG    1 
ATOM   12022 C CD    . ARG A 1 3160 ? 151.260 131.613 167.970 1.00 111.60 ? 3160 ARG A CD    1 
ATOM   12023 N NE    . ARG A 1 3160 ? 150.612 131.361 166.690 1.00 111.60 ? 3160 ARG A NE    1 
ATOM   12024 C CZ    . ARG A 1 3160 ? 149.436 130.765 166.552 1.00 111.60 ? 3160 ARG A CZ    1 
ATOM   12025 N NH1   . ARG A 1 3160 ? 148.753 130.334 167.600 1.00 111.60 ? 3160 ARG A NH1   1 
ATOM   12026 N NH2   . ARG A 1 3160 ? 148.932 130.597 165.333 1.00 111.60 ? 3160 ARG A NH2   1 
ATOM   12027 N N     . LEU A 1 3161 ? 151.900 136.098 166.766 1.00 114.42 ? 3161 LEU A N     1 
ATOM   12028 C CA    . LEU A 1 3161 ? 153.208 136.628 166.402 1.00 114.42 ? 3161 LEU A CA    1 
ATOM   12029 C C     . LEU A 1 3161 ? 153.431 138.001 167.020 1.00 114.42 ? 3161 LEU A C     1 
ATOM   12030 O O     . LEU A 1 3161 ? 154.541 138.321 167.458 1.00 114.42 ? 3161 LEU A O     1 
ATOM   12031 C CB    . LEU A 1 3161 ? 153.346 136.692 164.883 1.00 114.42 ? 3161 LEU A CB    1 
ATOM   12032 C CG    . LEU A 1 3161 ? 154.751 136.435 164.340 1.00 114.42 ? 3161 LEU A CG    1 
ATOM   12033 C CD1   . LEU A 1 3161 ? 155.182 135.014 164.650 1.00 114.42 ? 3161 LEU A CD1   1 
ATOM   12034 C CD2   . LEU A 1 3161 ? 154.816 136.705 162.846 1.00 114.42 ? 3161 LEU A CD2   1 
ATOM   12035 N N     . ALA A 1 3162 ? 152.386 138.830 167.055 1.00 116.87 ? 3162 ALA A N     1 
ATOM   12036 C CA    . ALA A 1 3162 ? 152.492 140.119 167.727 1.00 116.87 ? 3162 ALA A CA    1 
ATOM   12037 C C     . ALA A 1 3162 ? 152.734 139.941 169.220 1.00 116.87 ? 3162 ALA A C     1 
ATOM   12038 O O     . ALA A 1 3162 ? 153.504 140.696 169.826 1.00 116.87 ? 3162 ALA A O     1 
ATOM   12039 C CB    . ALA A 1 3162 ? 151.232 140.947 167.481 1.00 116.87 ? 3162 ALA A CB    1 
ATOM   12040 N N     . LYS A 1 3163 ? 152.079 138.953 169.831 1.00 117.06 ? 3163 LYS A N     1 
ATOM   12041 C CA    . LYS A 1 3163 ? 152.261 138.715 171.259 1.00 117.06 ? 3163 LYS A CA    1 
ATOM   12042 C C     . LYS A 1 3163 ? 153.702 138.332 171.575 1.00 117.06 ? 3163 LYS A C     1 
ATOM   12043 O O     . LYS A 1 3163 ? 154.320 138.892 172.488 1.00 117.06 ? 3163 LYS A O     1 
ATOM   12044 C CB    . LYS A 1 3163 ? 151.301 137.625 171.736 1.00 117.06 ? 3163 LYS A CB    1 
ATOM   12045 C CG    . LYS A 1 3163 ? 151.618 137.089 173.123 1.00 117.06 ? 3163 LYS A CG    1 
ATOM   12046 C CD    . LYS A 1 3163 ? 150.643 136.001 173.541 1.00 117.06 ? 3163 LYS A CD    1 
ATOM   12047 C CE    . LYS A 1 3163 ? 151.027 135.410 174.889 1.00 117.06 ? 3163 LYS A CE    1 
ATOM   12048 N NZ    . LYS A 1 3163 ? 150.139 134.281 175.281 1.00 117.06 ? 3163 LYS A NZ    1 
ATOM   12049 N N     . ARG A 1 3164 ? 154.256 137.384 170.825 1.00 122.54 ? 3164 ARG A N     1 
ATOM   12050 C CA    . ARG A 1 3164 ? 155.614 136.892 171.052 1.00 122.54 ? 3164 ARG A CA    1 
ATOM   12051 C C     . ARG A 1 3164 ? 156.536 137.594 170.061 1.00 122.54 ? 3164 ARG A C     1 
ATOM   12052 O O     . ARG A 1 3164 ? 156.797 137.098 168.965 1.00 122.54 ? 3164 ARG A O     1 
ATOM   12053 C CB    . ARG A 1 3164 ? 155.672 135.378 170.908 1.00 122.54 ? 3164 ARG A CB    1 
ATOM   12054 C CG    . ARG A 1 3164 ? 154.676 134.642 171.786 1.00 122.54 ? 3164 ARG A CG    1 
ATOM   12055 C CD    . ARG A 1 3164 ? 155.291 133.395 172.391 1.00 122.54 ? 3164 ARG A CD    1 
ATOM   12056 N NE    . ARG A 1 3164 ? 156.265 133.711 173.428 1.00 122.54 ? 3164 ARG A NE    1 
ATOM   12057 C CZ    . ARG A 1 3164 ? 156.080 133.478 174.720 1.00 122.54 ? 3164 ARG A CZ    1 
ATOM   12058 N NH1   . ARG A 1 3164 ? 154.962 132.934 175.171 1.00 122.54 ? 3164 ARG A NH1   1 
ATOM   12059 N NH2   . ARG A 1 3164 ? 157.041 133.798 175.581 1.00 122.54 ? 3164 ARG A NH2   1 
ATOM   12060 N N     . GLY A 1 3165 ? 157.035 138.758 170.459 1.00 119.76 ? 3165 GLY A N     1 
ATOM   12061 C CA    . GLY A 1 3165 ? 157.879 139.548 169.588 1.00 119.76 ? 3165 GLY A CA    1 
ATOM   12062 C C     . GLY A 1 3165 ? 157.076 140.532 168.766 1.00 119.76 ? 3165 GLY A C     1 
ATOM   12063 O O     . GLY A 1 3165 ? 156.630 141.561 169.280 1.00 119.76 ? 3165 GLY A O     1 
ATOM   12064 N N     . GLY A 1 3166 ? 156.877 140.222 167.489 1.00 120.19 ? 3166 GLY A N     1 
ATOM   12065 C CA    . GLY A 1 3166 ? 156.110 141.092 166.622 1.00 120.19 ? 3166 GLY A CA    1 
ATOM   12066 C C     . GLY A 1 3166 ? 156.402 140.876 165.153 1.00 120.19 ? 3166 GLY A C     1 
ATOM   12067 O O     . GLY A 1 3166 ? 156.447 139.735 164.685 1.00 120.19 ? 3166 GLY A O     1 
ATOM   12068 N N     . ARG A 1 3167 ? 156.603 141.972 164.421 1.00 126.61 ? 3167 ARG A N     1 
ATOM   12069 C CA    . ARG A 1 3167 ? 156.872 141.939 162.985 1.00 126.61 ? 3167 ARG A CA    1 
ATOM   12070 C C     . ARG A 1 3167 ? 155.748 141.216 162.241 1.00 126.61 ? 3167 ARG A C     1 
ATOM   12071 O O     . ARG A 1 3167 ? 155.943 140.174 161.612 1.00 126.61 ? 3167 ARG A O     1 
ATOM   12072 C CB    . ARG A 1 3167 ? 158.234 141.301 162.697 1.00 126.61 ? 3167 ARG A CB    1 
ATOM   12073 C CG    . ARG A 1 3167 ? 159.391 142.272 162.804 1.00 126.61 ? 3167 ARG A CG    1 
ATOM   12074 C CD    . ARG A 1 3167 ? 159.438 143.218 161.614 1.00 126.61 ? 3167 ARG A CD    1 
ATOM   12075 N NE    . ARG A 1 3167 ? 159.931 142.565 160.407 1.00 126.61 ? 3167 ARG A NE    1 
ATOM   12076 C CZ    . ARG A 1 3167 ? 161.186 142.180 160.220 1.00 126.61 ? 3167 ARG A CZ    1 
ATOM   12077 N NH1   . ARG A 1 3167 ? 162.112 142.363 161.147 1.00 126.61 ? 3167 ARG A NH1   1 
ATOM   12078 N NH2   . ARG A 1 3167 ? 161.520 141.597 159.073 1.00 126.61 ? 3167 ARG A NH2   1 
ATOM   12079 N N     . THR A 1 3168 ? 154.553 141.790 162.337 1.00 121.80 ? 3168 THR A N     1 
ATOM   12080 C CA    . THR A 1 3168 ? 153.357 141.227 161.736 1.00 121.80 ? 3168 THR A CA    1 
ATOM   12081 C C     . THR A 1 3168 ? 152.776 142.197 160.717 1.00 121.80 ? 3168 THR A C     1 
ATOM   12082 O O     . THR A 1 3168 ? 152.644 143.395 160.981 1.00 121.80 ? 3168 THR A O     1 
ATOM   12083 C CB    . THR A 1 3168 ? 152.302 140.914 162.798 1.00 121.80 ? 3168 THR A CB    1 
ATOM   12084 O OG1   . THR A 1 3168 ? 151.627 142.122 163.168 1.00 121.80 ? 3168 THR A OG1   1 
ATOM   12085 C CG2   . THR A 1 3168 ? 152.958 140.319 164.031 1.00 121.80 ? 3168 THR A CG2   1 
ATOM   12086 N N     . MET A 1 3169 ? 152.425 141.668 159.550 1.00 110.03 ? 3169 MET A N     1 
ATOM   12087 C CA    . MET A 1 3169 ? 151.769 142.439 158.504 1.00 110.03 ? 3169 MET A CA    1 
ATOM   12088 C C     . MET A 1 3169 ? 150.259 142.319 158.629 1.00 110.03 ? 3169 MET A C     1 
ATOM   12089 O O     . MET A 1 3169 ? 149.734 141.251 158.955 1.00 110.03 ? 3169 MET A O     1 
ATOM   12090 C CB    . MET A 1 3169 ? 152.219 141.982 157.117 1.00 110.03 ? 3169 MET A CB    1 
ATOM   12091 C CG    . MET A 1 3169 ? 153.618 141.423 157.075 1.00 110.03 ? 3169 MET A CG    1 
ATOM   12092 S SD    . MET A 1 3169 ? 154.769 142.452 158.003 1.00 110.03 ? 3169 MET A SD    1 
ATOM   12093 C CE    . MET A 1 3169 ? 154.672 143.985 157.080 1.00 110.03 ? 3169 MET A CE    1 
ATOM   12094 N N     . ALA A 1 3170 ? 149.568 143.425 158.370 1.00 95.95  ? 3170 ALA A N     1 
ATOM   12095 C CA    . ALA A 1 3170 ? 148.123 143.460 158.531 1.00 95.95  ? 3170 ALA A CA    1 
ATOM   12096 C C     . ALA A 1 3170 ? 147.449 142.495 157.568 1.00 95.95  ? 3170 ALA A C     1 
ATOM   12097 O O     . ALA A 1 3170 ? 147.886 142.318 156.429 1.00 95.95  ? 3170 ALA A O     1 
ATOM   12098 C CB    . ALA A 1 3170 ? 147.601 144.878 158.308 1.00 95.95  ? 3170 ALA A CB    1 
ATOM   12099 N N     . ILE A 1 3171 ? 146.377 141.866 158.038 1.00 98.69  ? 3171 ILE A N     1 
ATOM   12100 C CA    . ILE A 1 3171 ? 145.582 140.942 157.242 1.00 98.69  ? 3171 ILE A CA    1 
ATOM   12101 C C     . ILE A 1 3171 ? 144.251 141.611 156.939 1.00 98.69  ? 3171 ILE A C     1 
ATOM   12102 O O     . ILE A 1 3171 ? 143.522 142.006 157.858 1.00 98.69  ? 3171 ILE A O     1 
ATOM   12103 C CB    . ILE A 1 3171 ? 145.381 139.602 157.968 1.00 98.69  ? 3171 ILE A CB    1 
ATOM   12104 C CG1   . ILE A 1 3171 ? 146.602 138.714 157.754 1.00 98.69  ? 3171 ILE A CG1   1 
ATOM   12105 C CG2   . ILE A 1 3171 ? 144.129 138.907 157.472 1.00 98.69  ? 3171 ILE A CG2   1 
ATOM   12106 C CD1   . ILE A 1 3171 ? 146.933 138.493 156.301 1.00 98.69  ? 3171 ILE A CD1   1 
ATOM   12107 N N     . THR A 1 3172 ? 143.937 141.735 155.659 1.00 97.10  ? 3172 THR A N     1 
ATOM   12108 C CA    . THR A 1 3172 ? 142.798 142.493 155.176 1.00 97.10  ? 3172 THR A CA    1 
ATOM   12109 C C     . THR A 1 3172 ? 141.900 141.611 154.323 1.00 97.10  ? 3172 THR A C     1 
ATOM   12110 O O     . THR A 1 3172 ? 142.343 140.586 153.794 1.00 97.10  ? 3172 THR A O     1 
ATOM   12111 C CB    . THR A 1 3172 ? 143.263 143.696 154.343 1.00 97.10  ? 3172 THR A CB    1 
ATOM   12112 O OG1   . THR A 1 3172 ? 143.422 143.294 152.978 1.00 97.10  ? 3172 THR A OG1   1 
ATOM   12113 C CG2   . THR A 1 3172 ? 144.588 144.221 154.861 1.00 97.10  ? 3172 THR A CG2   1 
ATOM   12114 N N     . PRO A 1 3173 ? 140.628 141.979 154.167 1.00 91.69  ? 3173 PRO A N     1 
ATOM   12115 C CA    . PRO A 1 3173 ? 139.750 141.206 153.280 1.00 91.69  ? 3173 PRO A CA    1 
ATOM   12116 C C     . PRO A 1 3173 ? 140.239 141.130 151.847 1.00 91.69  ? 3173 PRO A C     1 
ATOM   12117 O O     . PRO A 1 3173 ? 139.813 140.227 151.116 1.00 91.69  ? 3173 PRO A O     1 
ATOM   12118 C CB    . PRO A 1 3173 ? 138.417 141.952 153.378 1.00 91.69  ? 3173 PRO A CB    1 
ATOM   12119 C CG    . PRO A 1 3173 ? 138.443 142.548 154.732 1.00 91.69  ? 3173 PRO A CG    1 
ATOM   12120 C CD    . PRO A 1 3173 ? 139.870 142.934 154.990 1.00 91.69  ? 3173 PRO A CD    1 
ATOM   12121 N N     . ARG A 1 3174 ? 141.108 142.045 151.412 1.00 102.50 ? 3174 ARG A N     1 
ATOM   12122 C CA    . ARG A 1 3174 ? 141.718 141.893 150.095 1.00 102.50 ? 3174 ARG A CA    1 
ATOM   12123 C C     . ARG A 1 3174 ? 142.506 140.595 150.008 1.00 102.50 ? 3174 ARG A C     1 
ATOM   12124 O O     . ARG A 1 3174 ? 142.531 139.944 148.958 1.00 102.50 ? 3174 ARG A O     1 
ATOM   12125 C CB    . ARG A 1 3174 ? 142.614 143.087 149.778 1.00 102.50 ? 3174 ARG A CB    1 
ATOM   12126 C CG    . ARG A 1 3174 ? 142.088 143.970 148.664 1.00 102.50 ? 3174 ARG A CG    1 
ATOM   12127 C CD    . ARG A 1 3174 ? 142.768 145.328 148.669 1.00 102.50 ? 3174 ARG A CD    1 
ATOM   12128 N NE    . ARG A 1 3174 ? 142.504 146.085 147.451 1.00 102.50 ? 3174 ARG A NE    1 
ATOM   12129 C CZ    . ARG A 1 3174 ? 143.089 145.856 146.283 1.00 102.50 ? 3174 ARG A CZ    1 
ATOM   12130 N NH1   . ARG A 1 3174 ? 143.983 144.893 146.134 1.00 102.50 ? 3174 ARG A NH1   1 
ATOM   12131 N NH2   . ARG A 1 3174 ? 142.771 146.616 145.239 1.00 102.50 ? 3174 ARG A NH2   1 
ATOM   12132 N N     . HIS A 1 3175 ? 143.147 140.194 151.109 1.00 97.51  ? 3175 HIS A N     1 
ATOM   12133 C CA    . HIS A 1 3175 ? 143.803 138.891 151.141 1.00 97.51  ? 3175 HIS A CA    1 
ATOM   12134 C C     . HIS A 1 3175 ? 142.801 137.768 150.929 1.00 97.51  ? 3175 HIS A C     1 
ATOM   12135 O O     . HIS A 1 3175 ? 143.075 136.816 150.193 1.00 97.51  ? 3175 HIS A O     1 
ATOM   12136 C CB    . HIS A 1 3175 ? 144.536 138.690 152.465 1.00 97.51  ? 3175 HIS A CB    1 
ATOM   12137 C CG    . HIS A 1 3175 ? 145.663 139.645 152.685 1.00 97.51  ? 3175 HIS A CG    1 
ATOM   12138 N ND1   . HIS A 1 3175 ? 145.797 140.383 153.840 1.00 97.51  ? 3175 HIS A ND1   1 
ATOM   12139 C CD2   . HIS A 1 3175 ? 146.719 139.971 151.904 1.00 97.51  ? 3175 HIS A CD2   1 
ATOM   12140 C CE1   . HIS A 1 3175 ? 146.882 141.130 153.758 1.00 97.51  ? 3175 HIS A CE1   1 
ATOM   12141 N NE2   . HIS A 1 3175 ? 147.460 140.899 152.593 1.00 97.51  ? 3175 HIS A NE2   1 
ATOM   12142 N N     . TYR A 1 3176 ? 141.640 137.853 151.577 1.00 90.66  ? 3176 TYR A N     1 
ATOM   12143 C CA    . TYR A 1 3176 ? 140.640 136.802 151.430 1.00 90.66  ? 3176 TYR A CA    1 
ATOM   12144 C C     . TYR A 1 3176 ? 140.137 136.736 149.996 1.00 90.66  ? 3176 TYR A C     1 
ATOM   12145 O O     . TYR A 1 3176 ? 139.951 135.646 149.444 1.00 90.66  ? 3176 TYR A O     1 
ATOM   12146 C CB    . TYR A 1 3176 ? 139.504 137.043 152.426 1.00 90.66  ? 3176 TYR A CB    1 
ATOM   12147 C CG    . TYR A 1 3176 ? 138.342 136.066 152.409 1.00 90.66  ? 3176 TYR A CG    1 
ATOM   12148 C CD1   . TYR A 1 3176 ? 138.016 135.352 153.548 1.00 90.66  ? 3176 TYR A CD1   1 
ATOM   12149 C CD2   . TYR A 1 3176 ? 137.524 135.921 151.298 1.00 90.66  ? 3176 TYR A CD2   1 
ATOM   12150 C CE1   . TYR A 1 3176 ? 136.952 134.482 153.566 1.00 90.66  ? 3176 TYR A CE1   1 
ATOM   12151 C CE2   . TYR A 1 3176 ? 136.458 135.051 151.308 1.00 90.66  ? 3176 TYR A CE2   1 
ATOM   12152 C CZ    . TYR A 1 3176 ? 136.175 134.336 152.445 1.00 90.66  ? 3176 TYR A CZ    1 
ATOM   12153 O OH    . TYR A 1 3176 ? 135.108 133.470 152.463 1.00 90.66  ? 3176 TYR A OH    1 
ATOM   12154 N N     . LEU A 1 3177 ? 139.913 137.892 149.373 1.00 92.95  ? 3177 LEU A N     1 
ATOM   12155 C CA    . LEU A 1 3177 ? 139.476 137.895 147.983 1.00 92.95  ? 3177 LEU A CA    1 
ATOM   12156 C C     . LEU A 1 3177 ? 140.546 137.321 147.063 1.00 92.95  ? 3177 LEU A C     1 
ATOM   12157 O O     . LEU A 1 3177 ? 140.234 136.564 146.136 1.00 92.95  ? 3177 LEU A O     1 
ATOM   12158 C CB    . LEU A 1 3177 ? 139.096 139.309 147.556 1.00 92.95  ? 3177 LEU A CB    1 
ATOM   12159 C CG    . LEU A 1 3177 ? 137.871 139.867 148.273 1.00 92.95  ? 3177 LEU A CG    1 
ATOM   12160 C CD1   . LEU A 1 3177 ? 137.402 141.141 147.608 1.00 92.95  ? 3177 LEU A CD1   1 
ATOM   12161 C CD2   . LEU A 1 3177 ? 136.765 138.835 148.281 1.00 92.95  ? 3177 LEU A CD2   1 
ATOM   12162 N N     . ASP A 1 3178 ? 141.813 137.668 147.297 1.00 101.21 ? 3178 ASP A N     1 
ATOM   12163 C CA    . ASP A 1 3178 ? 142.881 137.103 146.482 1.00 101.21 ? 3178 ASP A CA    1 
ATOM   12164 C C     . ASP A 1 3178 ? 142.971 135.596 146.675 1.00 101.21 ? 3178 ASP A C     1 
ATOM   12165 O O     . ASP A 1 3178 ? 143.207 134.851 145.718 1.00 101.21 ? 3178 ASP A O     1 
ATOM   12166 C CB    . ASP A 1 3178 ? 144.212 137.774 146.818 1.00 101.21 ? 3178 ASP A CB    1 
ATOM   12167 C CG    . ASP A 1 3178 ? 145.220 137.666 145.688 1.00 101.21 ? 3178 ASP A CG    1 
ATOM   12168 O OD1   . ASP A 1 3178 ? 144.938 136.953 144.705 1.00 101.21 ? 3178 ASP A OD1   1 
ATOM   12169 O OD2   . ASP A 1 3178 ? 146.294 138.297 145.781 1.00 101.21 ? 3178 ASP A OD2   1 
ATOM   12170 N N     . PHE A 1 3179 ? 142.782 135.129 147.909 1.00 90.94  ? 3179 PHE A N     1 
ATOM   12171 C CA    . PHE A 1 3179 ? 142.792 133.696 148.172 1.00 90.94  ? 3179 PHE A CA    1 
ATOM   12172 C C     . PHE A 1 3179 ? 141.649 132.998 147.453 1.00 90.94  ? 3179 PHE A C     1 
ATOM   12173 O O     . PHE A 1 3179 ? 141.826 131.906 146.908 1.00 90.94  ? 3179 PHE A O     1 
ATOM   12174 C CB    . PHE A 1 3179 ? 142.719 133.443 149.675 1.00 90.94  ? 3179 PHE A CB    1 
ATOM   12175 C CG    . PHE A 1 3179 ? 142.223 132.078 150.038 1.00 90.94  ? 3179 PHE A CG    1 
ATOM   12176 C CD1   . PHE A 1 3179 ? 142.910 130.948 149.641 1.00 90.94  ? 3179 PHE A CD1   1 
ATOM   12177 C CD2   . PHE A 1 3179 ? 141.080 131.927 150.794 1.00 90.94  ? 3179 PHE A CD2   1 
ATOM   12178 C CE1   . PHE A 1 3179 ? 142.456 129.696 149.979 1.00 90.94  ? 3179 PHE A CE1   1 
ATOM   12179 C CE2   . PHE A 1 3179 ? 140.624 130.676 151.139 1.00 90.94  ? 3179 PHE A CE2   1 
ATOM   12180 C CZ    . PHE A 1 3179 ? 141.313 129.560 150.731 1.00 90.94  ? 3179 PHE A CZ    1 
ATOM   12181 N N     . ILE A 1 3180 ? 140.466 133.610 147.446 1.00 91.77  ? 3180 ILE A N     1 
ATOM   12182 C CA    . ILE A 1 3180 ? 139.335 133.013 146.743 1.00 91.77  ? 3180 ILE A CA    1 
ATOM   12183 C C     . ILE A 1 3180 ? 139.605 132.956 145.247 1.00 91.77  ? 3180 ILE A C     1 
ATOM   12184 O O     . ILE A 1 3180 ? 139.311 131.953 144.586 1.00 91.77  ? 3180 ILE A O     1 
ATOM   12185 C CB    . ILE A 1 3180 ? 138.043 133.783 147.055 1.00 91.77  ? 3180 ILE A CB    1 
ATOM   12186 C CG1   . ILE A 1 3180 ? 137.568 133.458 148.468 1.00 91.77  ? 3180 ILE A CG1   1 
ATOM   12187 C CG2   . ILE A 1 3180 ? 136.975 133.440 146.042 1.00 91.77  ? 3180 ILE A CG2   1 
ATOM   12188 C CD1   . ILE A 1 3180 ? 137.082 132.046 148.628 1.00 91.77  ? 3180 ILE A CD1   1 
ATOM   12189 N N     . ASN A 1 3181 ? 140.161 134.031 144.686 1.00 99.17  ? 3181 ASN A N     1 
ATOM   12190 C CA    . ASN A 1 3181 ? 140.502 134.018 143.267 1.00 99.17  ? 3181 ASN A CA    1 
ATOM   12191 C C     . ASN A 1 3181 ? 141.521 132.931 142.954 1.00 99.17  ? 3181 ASN A C     1 
ATOM   12192 O O     . ASN A 1 3181 ? 141.399 132.224 141.946 1.00 99.17  ? 3181 ASN A O     1 
ATOM   12193 C CB    . ASN A 1 3181 ? 141.037 135.383 142.837 1.00 99.17  ? 3181 ASN A CB    1 
ATOM   12194 C CG    . ASN A 1 3181 ? 139.943 136.315 142.371 1.00 99.17  ? 3181 ASN A CG    1 
ATOM   12195 O OD1   . ASN A 1 3181 ? 138.825 135.887 142.094 1.00 99.17  ? 3181 ASN A OD1   1 
ATOM   12196 N ND2   . ASN A 1 3181 ? 140.263 137.599 142.276 1.00 99.17  ? 3181 ASN A ND2   1 
ATOM   12197 N N     . HIS A 1 3182 ? 142.541 132.792 143.801 1.00 103.42 ? 3182 HIS A N     1 
ATOM   12198 C CA    . HIS A 1 3182 ? 143.549 131.766 143.572 1.00 103.42 ? 3182 HIS A CA    1 
ATOM   12199 C C     . HIS A 1 3182 ? 142.943 130.376 143.679 1.00 103.42 ? 3182 HIS A C     1 
ATOM   12200 O O     . HIS A 1 3182 ? 143.282 129.484 142.897 1.00 103.42 ? 3182 HIS A O     1 
ATOM   12201 C CB    . HIS A 1 3182 ? 144.700 131.935 144.558 1.00 103.42 ? 3182 HIS A CB    1 
ATOM   12202 C CG    . HIS A 1 3182 ? 145.816 132.778 144.030 1.00 103.42 ? 3182 HIS A CG    1 
ATOM   12203 N ND1   . HIS A 1 3182 ? 146.440 133.745 144.787 1.00 103.42 ? 3182 HIS A ND1   1 
ATOM   12204 C CD2   . HIS A 1 3182 ? 146.410 132.809 142.815 1.00 103.42 ? 3182 HIS A CD2   1 
ATOM   12205 C CE1   . HIS A 1 3182 ? 147.378 134.329 144.064 1.00 103.42 ? 3182 HIS A CE1   1 
ATOM   12206 N NE2   . HIS A 1 3182 ? 147.379 133.782 142.862 1.00 103.42 ? 3182 HIS A NE2   1 
ATOM   12207 N N     . TYR A 1 3183 ? 142.039 130.180 144.638 1.00 102.63 ? 3183 TYR A N     1 
ATOM   12208 C CA    . TYR A 1 3183 ? 141.352 128.902 144.767 1.00 102.63 ? 3183 TYR A CA    1 
ATOM   12209 C C     . TYR A 1 3183 ? 140.554 128.593 143.512 1.00 102.63 ? 3183 TYR A C     1 
ATOM   12210 O O     . TYR A 1 3183 ? 140.591 127.471 143.001 1.00 102.63 ? 3183 TYR A O     1 
ATOM   12211 C CB    . TYR A 1 3183 ? 140.445 128.928 145.997 1.00 102.63 ? 3183 TYR A CB    1 
ATOM   12212 C CG    . TYR A 1 3183 ? 139.760 127.620 146.325 1.00 102.63 ? 3183 TYR A CG    1 
ATOM   12213 C CD1   . TYR A 1 3183 ? 140.326 126.404 145.979 1.00 102.63 ? 3183 TYR A CD1   1 
ATOM   12214 C CD2   . TYR A 1 3183 ? 138.550 127.607 147.000 1.00 102.63 ? 3183 TYR A CD2   1 
ATOM   12215 C CE1   . TYR A 1 3183 ? 139.697 125.212 146.287 1.00 102.63 ? 3183 TYR A CE1   1 
ATOM   12216 C CE2   . TYR A 1 3183 ? 137.917 126.425 147.312 1.00 102.63 ? 3183 TYR A CE2   1 
ATOM   12217 C CZ    . TYR A 1 3183 ? 138.492 125.231 146.955 1.00 102.63 ? 3183 TYR A CZ    1 
ATOM   12218 O OH    . TYR A 1 3183 ? 137.857 124.052 147.269 1.00 102.63 ? 3183 TYR A OH    1 
ATOM   12219 N N     . ALA A 1 3184 ? 139.832 129.585 142.993 1.00 105.01 ? 3184 ALA A N     1 
ATOM   12220 C CA    . ALA A 1 3184 ? 139.035 129.361 141.793 1.00 105.01 ? 3184 ALA A CA    1 
ATOM   12221 C C     . ALA A 1 3184 ? 139.919 128.994 140.612 1.00 105.01 ? 3184 ALA A C     1 
ATOM   12222 O O     . ALA A 1 3184 ? 139.655 128.012 139.908 1.00 105.01 ? 3184 ALA A O     1 
ATOM   12223 C CB    . ALA A 1 3184 ? 138.200 130.600 141.478 1.00 105.01 ? 3184 ALA A CB    1 
ATOM   12224 N N     . ASN A 1 3185 ? 140.979 129.772 140.381 1.00 108.59 ? 3185 ASN A N     1 
ATOM   12225 C CA    . ASN A 1 3185 ? 141.856 129.495 139.249 1.00 108.59 ? 3185 ASN A CA    1 
ATOM   12226 C C     . ASN A 1 3185 ? 142.509 128.127 139.380 1.00 108.59 ? 3185 ASN A C     1 
ATOM   12227 O O     . ASN A 1 3185 ? 142.540 127.350 138.420 1.00 108.59 ? 3185 ASN A O     1 
ATOM   12228 C CB    . ASN A 1 3185 ? 142.921 130.583 139.108 1.00 108.59 ? 3185 ASN A CB    1 
ATOM   12229 C CG    . ASN A 1 3185 ? 142.333 131.923 138.739 1.00 108.59 ? 3185 ASN A CG    1 
ATOM   12230 O OD1   . ASN A 1 3185 ? 141.335 131.994 138.026 1.00 108.59 ? 3185 ASN A OD1   1 
ATOM   12231 N ND2   . ASN A 1 3185 ? 142.966 132.996 139.195 1.00 108.59 ? 3185 ASN A ND2   1 
ATOM   12232 N N     . LEU A 1 3186 ? 143.023 127.805 140.570 1.00 107.89 ? 3186 LEU A N     1 
ATOM   12233 C CA    . LEU A 1 3186 ? 143.680 126.518 140.761 1.00 107.89 ? 3186 LEU A CA    1 
ATOM   12234 C C     . LEU A 1 3186 ? 142.703 125.370 140.574 1.00 107.89 ? 3186 LEU A C     1 
ATOM   12235 O O     . LEU A 1 3186 ? 143.014 124.388 139.892 1.00 107.89 ? 3186 LEU A O     1 
ATOM   12236 C CB    . LEU A 1 3186 ? 144.321 126.446 142.143 1.00 107.89 ? 3186 LEU A CB    1 
ATOM   12237 C CG    . LEU A 1 3186 ? 145.815 126.743 142.204 1.00 107.89 ? 3186 LEU A CG    1 
ATOM   12238 C CD1   . LEU A 1 3186 ? 146.556 125.678 141.435 1.00 107.89 ? 3186 LEU A CD1   1 
ATOM   12239 C CD2   . LEU A 1 3186 ? 146.128 128.114 141.649 1.00 107.89 ? 3186 LEU A CD2   1 
ATOM   12240 N N     . PHE A 1 3187 ? 141.515 125.475 141.169 1.00 114.28 ? 3187 PHE A N     1 
ATOM   12241 C CA    . PHE A 1 3187 ? 140.536 124.406 141.054 1.00 114.28 ? 3187 PHE A CA    1 
ATOM   12242 C C     . PHE A 1 3187 ? 140.139 124.193 139.603 1.00 114.28 ? 3187 PHE A C     1 
ATOM   12243 O O     . PHE A 1 3187 ? 140.141 123.061 139.108 1.00 114.28 ? 3187 PHE A O     1 
ATOM   12244 C CB    . PHE A 1 3187 ? 139.311 124.726 141.906 1.00 114.28 ? 3187 PHE A CB    1 
ATOM   12245 C CG    . PHE A 1 3187 ? 138.268 123.654 141.890 1.00 114.28 ? 3187 PHE A CG    1 
ATOM   12246 C CD1   . PHE A 1 3187 ? 138.311 122.620 142.803 1.00 114.28 ? 3187 PHE A CD1   1 
ATOM   12247 C CD2   . PHE A 1 3187 ? 137.244 123.680 140.964 1.00 114.28 ? 3187 PHE A CD2   1 
ATOM   12248 C CE1   . PHE A 1 3187 ? 137.354 121.633 142.791 1.00 114.28 ? 3187 PHE A CE1   1 
ATOM   12249 C CE2   . PHE A 1 3187 ? 136.285 122.694 140.947 1.00 114.28 ? 3187 PHE A CE2   1 
ATOM   12250 C CZ    . PHE A 1 3187 ? 136.340 121.669 141.861 1.00 114.28 ? 3187 PHE A CZ    1 
ATOM   12251 N N     . HIS A 1 3188 ? 139.805 125.277 138.901 1.00 122.34 ? 3188 HIS A N     1 
ATOM   12252 C CA    . HIS A 1 3188 ? 139.384 125.143 137.514 1.00 122.34 ? 3188 HIS A CA    1 
ATOM   12253 C C     . HIS A 1 3188 ? 140.501 124.573 136.654 1.00 122.34 ? 3188 HIS A C     1 
ATOM   12254 O O     . HIS A 1 3188 ? 140.264 123.682 135.833 1.00 122.34 ? 3188 HIS A O     1 
ATOM   12255 C CB    . HIS A 1 3188 ? 138.913 126.496 136.978 1.00 122.34 ? 3188 HIS A CB    1 
ATOM   12256 C CG    . HIS A 1 3188 ? 138.854 126.572 135.483 1.00 122.34 ? 3188 HIS A CG    1 
ATOM   12257 N ND1   . HIS A 1 3188 ? 139.982 126.658 134.694 1.00 122.34 ? 3188 HIS A ND1   1 
ATOM   12258 C CD2   . HIS A 1 3188 ? 137.801 126.569 134.633 1.00 122.34 ? 3188 HIS A CD2   1 
ATOM   12259 C CE1   . HIS A 1 3188 ? 139.625 126.708 133.423 1.00 122.34 ? 3188 HIS A CE1   1 
ATOM   12260 N NE2   . HIS A 1 3188 ? 138.307 126.656 133.359 1.00 122.34 ? 3188 HIS A NE2   1 
ATOM   12261 N N     . GLU A 1 3189 ? 141.730 125.059 136.839 1.00 130.13 ? 3189 GLU A N     1 
ATOM   12262 C CA    . GLU A 1 3189 ? 142.841 124.606 136.013 1.00 130.13 ? 3189 GLU A CA    1 
ATOM   12263 C C     . GLU A 1 3189 ? 143.143 123.131 136.253 1.00 130.13 ? 3189 GLU A C     1 
ATOM   12264 O O     . GLU A 1 3189 ? 143.332 122.360 135.302 1.00 130.13 ? 3189 GLU A O     1 
ATOM   12265 C CB    . GLU A 1 3189 ? 144.068 125.472 136.294 1.00 130.13 ? 3189 GLU A CB    1 
ATOM   12266 C CG    . GLU A 1 3189 ? 145.390 124.851 135.906 1.00 130.13 ? 3189 GLU A CG    1 
ATOM   12267 C CD    . GLU A 1 3189 ? 146.565 125.759 136.215 1.00 130.13 ? 3189 GLU A CD    1 
ATOM   12268 O OE1   . GLU A 1 3189 ? 146.350 126.978 136.378 1.00 130.13 ? 3189 GLU A OE1   1 
ATOM   12269 O OE2   . GLU A 1 3189 ? 147.703 125.253 136.301 1.00 130.13 ? 3189 GLU A OE2   1 
ATOM   12270 N N     . LYS A 1 3190 ? 143.175 122.712 137.519 1.00 129.62 ? 3190 LYS A N     1 
ATOM   12271 C CA    . LYS A 1 3190 ? 143.487 121.319 137.813 1.00 129.62 ? 3190 LYS A CA    1 
ATOM   12272 C C     . LYS A 1 3190 ? 142.366 120.393 137.360 1.00 129.62 ? 3190 LYS A C     1 
ATOM   12273 O O     . LYS A 1 3190 ? 142.630 119.304 136.833 1.00 129.62 ? 3190 LYS A O     1 
ATOM   12274 C CB    . LYS A 1 3190 ? 143.771 121.145 139.303 1.00 129.62 ? 3190 LYS A CB    1 
ATOM   12275 C CG    . LYS A 1 3190 ? 145.046 121.837 139.779 1.00 129.62 ? 3190 LYS A CG    1 
ATOM   12276 C CD    . LYS A 1 3190 ? 146.073 121.972 138.661 1.00 129.62 ? 3190 LYS A CD    1 
ATOM   12277 C CE    . LYS A 1 3190 ? 147.423 122.418 139.191 1.00 129.62 ? 3190 LYS A CE    1 
ATOM   12278 N NZ    . LYS A 1 3190 ? 148.033 121.401 140.085 1.00 129.62 ? 3190 LYS A NZ    1 
ATOM   12279 N N     . ARG A 1 3191 ? 141.110 120.804 137.543 1.00 135.78 ? 3191 ARG A N     1 
ATOM   12280 C CA    . ARG A 1 3191 ? 140.003 119.991 137.057 1.00 135.78 ? 3191 ARG A CA    1 
ATOM   12281 C C     . ARG A 1 3191 ? 140.031 119.886 135.540 1.00 135.78 ? 3191 ARG A C     1 
ATOM   12282 O O     . ARG A 1 3191 ? 139.734 118.825 134.981 1.00 135.78 ? 3191 ARG A O     1 
ATOM   12283 C CB    . ARG A 1 3191 ? 138.673 120.570 137.535 1.00 135.78 ? 3191 ARG A CB    1 
ATOM   12284 C CG    . ARG A 1 3191 ? 138.266 120.094 138.912 1.00 135.78 ? 3191 ARG A CG    1 
ATOM   12285 C CD    . ARG A 1 3191 ? 137.695 118.688 138.863 1.00 135.78 ? 3191 ARG A CD    1 
ATOM   12286 N NE    . ARG A 1 3191 ? 136.495 118.591 138.040 1.00 135.78 ? 3191 ARG A NE    1 
ATOM   12287 C CZ    . ARG A 1 3191 ? 135.352 119.215 138.291 1.00 135.78 ? 3191 ARG A CZ    1 
ATOM   12288 N NH1   . ARG A 1 3191 ? 135.199 119.980 139.358 1.00 135.78 ? 3191 ARG A NH1   1 
ATOM   12289 N NH2   . ARG A 1 3191 ? 134.330 119.055 137.456 1.00 135.78 ? 3191 ARG A NH2   1 
ATOM   12290 N N     . SER A 1 3192 ? 140.388 120.974 134.855 1.00 152.89 ? 3192 SER A N     1 
ATOM   12291 C CA    . SER A 1 3192 ? 140.506 120.924 133.404 1.00 152.89 ? 3192 SER A CA    1 
ATOM   12292 C C     . SER A 1 3192 ? 141.595 119.952 132.974 1.00 152.89 ? 3192 SER A C     1 
ATOM   12293 O O     . SER A 1 3192 ? 141.396 119.162 132.044 1.00 152.89 ? 3192 SER A O     1 
ATOM   12294 C CB    . SER A 1 3192 ? 140.787 122.319 132.850 1.00 152.89 ? 3192 SER A CB    1 
ATOM   12295 O OG    . SER A 1 3192 ? 141.521 122.247 131.641 1.00 152.89 ? 3192 SER A OG    1 
ATOM   12296 N N     . GLU A 1 3193 ? 142.753 119.991 133.640 1.00 161.77 ? 3193 GLU A N     1 
ATOM   12297 C CA    . GLU A 1 3193 ? 143.812 119.044 133.299 1.00 161.77 ? 3193 GLU A CA    1 
ATOM   12298 C C     . GLU A 1 3193 ? 143.356 117.609 133.521 1.00 161.77 ? 3193 GLU A C     1 
ATOM   12299 O O     . GLU A 1 3193 ? 143.560 116.744 132.660 1.00 161.77 ? 3193 GLU A O     1 
ATOM   12300 C CB    . GLU A 1 3193 ? 145.074 119.317 134.116 1.00 161.77 ? 3193 GLU A CB    1 
ATOM   12301 C CG    . GLU A 1 3193 ? 145.671 120.693 133.945 1.00 161.77 ? 3193 GLU A CG    1 
ATOM   12302 C CD    . GLU A 1 3193 ? 146.759 120.967 134.963 1.00 161.77 ? 3193 GLU A CD    1 
ATOM   12303 O OE1   . GLU A 1 3193 ? 147.576 120.057 135.218 1.00 161.77 ? 3193 GLU A OE1   1 
ATOM   12304 O OE2   . GLU A 1 3193 ? 146.799 122.088 135.507 1.00 161.77 ? 3193 GLU A OE2   1 
ATOM   12305 N N     . LEU A 1 3194 ? 142.726 117.342 134.666 1.00 172.39 ? 3194 LEU A N     1 
ATOM   12306 C CA    . LEU A 1 3194 ? 142.281 115.985 134.965 1.00 172.39 ? 3194 LEU A CA    1 
ATOM   12307 C C     . LEU A 1 3194 ? 141.251 115.505 133.951 1.00 172.39 ? 3194 LEU A C     1 
ATOM   12308 O O     . LEU A 1 3194 ? 141.315 114.362 133.481 1.00 172.39 ? 3194 LEU A O     1 
ATOM   12309 C CB    . LEU A 1 3194 ? 141.709 115.927 136.379 1.00 172.39 ? 3194 LEU A CB    1 
ATOM   12310 C CG    . LEU A 1 3194 ? 141.079 114.602 136.796 1.00 172.39 ? 3194 LEU A CG    1 
ATOM   12311 C CD1   . LEU A 1 3194 ? 142.124 113.683 137.393 1.00 172.39 ? 3194 LEU A CD1   1 
ATOM   12312 C CD2   . LEU A 1 3194 ? 139.955 114.847 137.777 1.00 172.39 ? 3194 LEU A CD2   1 
ATOM   12313 N N     . GLU A 1 3195 ? 140.298 116.366 133.593 1.00 181.94 ? 3195 GLU A N     1 
ATOM   12314 C CA    . GLU A 1 3195 ? 139.261 115.964 132.652 1.00 181.94 ? 3195 GLU A CA    1 
ATOM   12315 C C     . GLU A 1 3195 ? 139.829 115.751 131.255 1.00 181.94 ? 3195 GLU A C     1 
ATOM   12316 O O     . GLU A 1 3195 ? 139.415 114.823 130.551 1.00 181.94 ? 3195 GLU A O     1 
ATOM   12317 C CB    . GLU A 1 3195 ? 138.141 117.002 132.633 1.00 181.94 ? 3195 GLU A CB    1 
ATOM   12318 C CG    . GLU A 1 3195 ? 136.985 116.668 133.559 1.00 181.94 ? 3195 GLU A CG    1 
ATOM   12319 C CD    . GLU A 1 3195 ? 135.896 117.720 133.531 1.00 181.94 ? 3195 GLU A CD    1 
ATOM   12320 O OE1   . GLU A 1 3195 ? 135.075 117.704 132.590 1.00 181.94 ? 3195 GLU A OE1   1 
ATOM   12321 O OE2   . GLU A 1 3195 ? 135.860 118.564 134.450 1.00 181.94 ? 3195 GLU A OE2   1 
ATOM   12322 N N     . GLU A 1 3196 ? 140.775 116.594 130.829 1.00 188.09 ? 3196 GLU A N     1 
ATOM   12323 C CA    . GLU A 1 3196 ? 141.389 116.381 129.522 1.00 188.09 ? 3196 GLU A CA    1 
ATOM   12324 C C     . GLU A 1 3196 ? 142.199 115.090 129.507 1.00 188.09 ? 3196 GLU A C     1 
ATOM   12325 O O     . GLU A 1 3196 ? 142.204 114.366 128.504 1.00 188.09 ? 3196 GLU A O     1 
ATOM   12326 C CB    . GLU A 1 3196 ? 142.248 117.588 129.131 1.00 188.09 ? 3196 GLU A CB    1 
ATOM   12327 C CG    . GLU A 1 3196 ? 143.721 117.503 129.502 1.00 188.09 ? 3196 GLU A CG    1 
ATOM   12328 C CD    . GLU A 1 3196 ? 144.439 118.829 129.347 1.00 188.09 ? 3196 GLU A CD    1 
ATOM   12329 O OE1   . GLU A 1 3196 ? 144.161 119.546 128.364 1.00 188.09 ? 3196 GLU A OE1   1 
ATOM   12330 O OE2   . GLU A 1 3196 ? 145.282 119.155 130.210 1.00 188.09 ? 3196 GLU A OE2   1 
ATOM   12331 N N     . GLN A 1 3197 ? 142.864 114.767 130.620 1.00 200.06 ? 3197 GLN A N     1 
ATOM   12332 C CA    . GLN A 1 3197 ? 143.582 113.501 130.699 1.00 200.06 ? 3197 GLN A CA    1 
ATOM   12333 C C     . GLN A 1 3197 ? 142.622 112.321 130.626 1.00 200.06 ? 3197 GLN A C     1 
ATOM   12334 O O     . GLN A 1 3197 ? 142.900 111.326 129.949 1.00 200.06 ? 3197 GLN A O     1 
ATOM   12335 C CB    . GLN A 1 3197 ? 144.406 113.444 131.983 1.00 200.06 ? 3197 GLN A CB    1 
ATOM   12336 C CG    . GLN A 1 3197 ? 145.589 114.395 132.012 1.00 200.06 ? 3197 GLN A CG    1 
ATOM   12337 C CD    . GLN A 1 3197 ? 145.890 114.899 133.409 1.00 200.06 ? 3197 GLN A CD    1 
ATOM   12338 O OE1   . GLN A 1 3197 ? 146.149 116.086 133.611 1.00 200.06 ? 3197 GLN A OE1   1 
ATOM   12339 N NE2   . GLN A 1 3197 ? 145.854 113.998 134.385 1.00 200.06 ? 3197 GLN A NE2   1 
ATOM   12340 N N     . GLN A 1 3198 ? 141.484 112.416 131.315 1.00 212.91 ? 3198 GLN A N     1 
ATOM   12341 C CA    . GLN A 1 3198 ? 140.501 111.337 131.265 1.00 212.91 ? 3198 GLN A CA    1 
ATOM   12342 C C     . GLN A 1 3198 ? 139.928 111.176 129.862 1.00 212.91 ? 3198 GLN A C     1 
ATOM   12343 O O     . GLN A 1 3198 ? 139.715 110.050 129.392 1.00 212.91 ? 3198 GLN A O     1 
ATOM   12344 C CB    . GLN A 1 3198 ? 139.386 111.598 132.275 1.00 212.91 ? 3198 GLN A CB    1 
ATOM   12345 C CG    . GLN A 1 3198 ? 138.388 110.463 132.397 1.00 212.91 ? 3198 GLN A CG    1 
ATOM   12346 C CD    . GLN A 1 3198 ? 137.539 110.569 133.647 1.00 212.91 ? 3198 GLN A CD    1 
ATOM   12347 O OE1   . GLN A 1 3198 ? 138.059 110.707 134.755 1.00 212.91 ? 3198 GLN A OE1   1 
ATOM   12348 N NE2   . GLN A 1 3198 ? 136.224 110.503 133.476 1.00 212.91 ? 3198 GLN A NE2   1 
ATOM   12349 N N     . MET A 1 3199 ? 139.661 112.292 129.180 1.00 230.18 ? 3199 MET A N     1 
ATOM   12350 C CA    . MET A 1 3199 ? 139.155 112.218 127.813 1.00 230.18 ? 3199 MET A CA    1 
ATOM   12351 C C     . MET A 1 3199 ? 140.181 111.586 126.882 1.00 230.18 ? 3199 MET A C     1 
ATOM   12352 O O     . MET A 1 3199 ? 139.829 110.778 126.013 1.00 230.18 ? 3199 MET A O     1 
ATOM   12353 C CB    . MET A 1 3199 ? 138.767 113.611 127.317 1.00 230.18 ? 3199 MET A CB    1 
ATOM   12354 C CG    . MET A 1 3199 ? 137.520 113.634 126.448 1.00 230.18 ? 3199 MET A CG    1 
ATOM   12355 S SD    . MET A 1 3199 ? 136.673 115.224 126.477 1.00 230.18 ? 3199 MET A SD    1 
ATOM   12356 C CE    . MET A 1 3199 ? 135.303 114.896 125.372 1.00 230.18 ? 3199 MET A CE    1 
ATOM   12357 N N     . HIS A 1 3200 ? 141.456 111.947 127.043 1.00 247.21 ? 3200 HIS A N     1 
ATOM   12358 C CA    . HIS A 1 3200 ? 142.502 111.328 126.236 1.00 247.21 ? 3200 HIS A CA    1 
ATOM   12359 C C     . HIS A 1 3200 ? 142.597 109.835 126.526 1.00 247.21 ? 3200 HIS A C     1 
ATOM   12360 O O     . HIS A 1 3200 ? 142.784 109.026 125.610 1.00 247.21 ? 3200 HIS A O     1 
ATOM   12361 C CB    . HIS A 1 3200 ? 143.837 112.025 126.497 1.00 247.21 ? 3200 HIS A CB    1 
ATOM   12362 C CG    . HIS A 1 3200 ? 144.691 112.173 125.276 1.00 247.21 ? 3200 HIS A CG    1 
ATOM   12363 N ND1   . HIS A 1 3200 ? 145.857 112.907 125.270 1.00 247.21 ? 3200 HIS A ND1   1 
ATOM   12364 C CD2   . HIS A 1 3200 ? 144.549 111.682 124.022 1.00 247.21 ? 3200 HIS A CD2   1 
ATOM   12365 C CE1   . HIS A 1 3200 ? 146.396 112.863 124.065 1.00 247.21 ? 3200 HIS A CE1   1 
ATOM   12366 N NE2   . HIS A 1 3200 ? 145.623 112.125 123.289 1.00 247.21 ? 3200 HIS A NE2   1 
ATOM   12367 N N     . LEU A 1 3201 ? 142.455 109.455 127.798 1.00 259.23 ? 3201 LEU A N     1 
ATOM   12368 C CA    . LEU A 1 3201 ? 142.417 108.044 128.169 1.00 259.23 ? 3201 LEU A CA    1 
ATOM   12369 C C     . LEU A 1 3201 ? 141.289 107.309 127.454 1.00 259.23 ? 3201 LEU A C     1 
ATOM   12370 O O     . LEU A 1 3201 ? 141.499 106.225 126.898 1.00 259.23 ? 3201 LEU A O     1 
ATOM   12371 C CB    . LEU A 1 3201 ? 142.255 107.915 129.684 1.00 259.23 ? 3201 LEU A CB    1 
ATOM   12372 C CG    . LEU A 1 3201 ? 142.297 106.522 130.316 1.00 259.23 ? 3201 LEU A CG    1 
ATOM   12373 C CD1   . LEU A 1 3201 ? 143.308 106.453 131.447 1.00 259.23 ? 3201 LEU A CD1   1 
ATOM   12374 C CD2   . LEU A 1 3201 ? 140.912 106.137 130.816 1.00 259.23 ? 3201 LEU A CD2   1 
ATOM   12375 N N     . ASN A 1 3202 ? 140.084 107.881 127.463 1.00 263.68 ? 3202 ASN A N     1 
ATOM   12376 C CA    . ASN A 1 3202 ? 138.946 107.214 126.833 1.00 263.68 ? 3202 ASN A CA    1 
ATOM   12377 C C     . ASN A 1 3202 ? 139.119 107.119 125.321 1.00 263.68 ? 3202 ASN A C     1 
ATOM   12378 O O     . ASN A 1 3202 ? 138.792 106.088 124.714 1.00 263.68 ? 3202 ASN A O     1 
ATOM   12379 C CB    . ASN A 1 3202 ? 137.651 107.942 127.185 1.00 263.68 ? 3202 ASN A CB    1 
ATOM   12380 C CG    . ASN A 1 3202 ? 137.294 107.814 128.652 1.00 263.68 ? 3202 ASN A CG    1 
ATOM   12381 O OD1   . ASN A 1 3202 ? 137.358 106.727 129.225 1.00 263.68 ? 3202 ASN A OD1   1 
ATOM   12382 N ND2   . ASN A 1 3202 ? 136.916 108.928 129.268 1.00 263.68 ? 3202 ASN A ND2   1 
ATOM   12383 N N     . VAL A 1 3203 ? 139.627 108.184 124.695 1.00 280.12 ? 3203 VAL A N     1 
ATOM   12384 C CA    . VAL A 1 3203 ? 139.859 108.161 123.253 1.00 280.12 ? 3203 VAL A CA    1 
ATOM   12385 C C     . VAL A 1 3203 ? 140.887 107.095 122.900 1.00 280.12 ? 3203 VAL A C     1 
ATOM   12386 O O     . VAL A 1 3203 ? 140.716 106.333 121.937 1.00 280.12 ? 3203 VAL A O     1 
ATOM   12387 C CB    . VAL A 1 3203 ? 140.292 109.554 122.760 1.00 280.12 ? 3203 VAL A CB    1 
ATOM   12388 C CG1   . VAL A 1 3203 ? 140.914 109.463 121.376 1.00 280.12 ? 3203 VAL A CG1   1 
ATOM   12389 C CG2   . VAL A 1 3203 ? 139.106 110.504 122.755 1.00 280.12 ? 3203 VAL A CG2   1 
ATOM   12390 N N     . GLY A 1 3204 ? 141.965 107.016 123.680 1.00 291.48 ? 3204 GLY A N     1 
ATOM   12391 C CA    . GLY A 1 3204 ? 142.952 105.979 123.449 1.00 291.48 ? 3204 GLY A CA    1 
ATOM   12392 C C     . GLY A 1 3204 ? 142.394 104.585 123.652 1.00 291.48 ? 3204 GLY A C     1 
ATOM   12393 O O     . GLY A 1 3204 ? 142.751 103.658 122.927 1.00 291.48 ? 3204 GLY A O     1 
ATOM   12394 N N     . LEU A 1 3205 ? 141.517 104.416 124.645 1.00 296.40 ? 3205 LEU A N     1 
ATOM   12395 C CA    . LEU A 1 3205 ? 140.900 103.111 124.868 1.00 296.40 ? 3205 LEU A CA    1 
ATOM   12396 C C     . LEU A 1 3205 ? 140.044 102.694 123.679 1.00 296.40 ? 3205 LEU A C     1 
ATOM   12397 O O     . LEU A 1 3205 ? 140.087 101.534 123.247 1.00 296.40 ? 3205 LEU A O     1 
ATOM   12398 C CB    . LEU A 1 3205 ? 140.063 103.135 126.146 1.00 296.40 ? 3205 LEU A CB    1 
ATOM   12399 C CG    . LEU A 1 3205 ? 140.791 102.715 127.422 1.00 296.40 ? 3205 LEU A CG    1 
ATOM   12400 C CD1   . LEU A 1 3205 ? 139.799 102.379 128.530 1.00 296.40 ? 3205 LEU A CD1   1 
ATOM   12401 C CD2   . LEU A 1 3205 ? 141.715 101.542 127.147 1.00 296.40 ? 3205 LEU A CD2   1 
ATOM   12402 N N     . ARG A 1 3206 ? 139.260 103.627 123.134 1.00 301.86 ? 3206 ARG A N     1 
ATOM   12403 C CA    . ARG A 1 3206 ? 138.474 103.313 121.944 1.00 301.86 ? 3206 ARG A CA    1 
ATOM   12404 C C     . ARG A 1 3206 ? 139.376 102.972 120.762 1.00 301.86 ? 3206 ARG A C     1 
ATOM   12405 O O     . ARG A 1 3206 ? 139.104 102.022 120.013 1.00 301.86 ? 3206 ARG A O     1 
ATOM   12406 C CB    . ARG A 1 3206 ? 137.546 104.477 121.595 1.00 301.86 ? 3206 ARG A CB    1 
ATOM   12407 C CG    . ARG A 1 3206 ? 136.413 104.688 122.585 1.00 301.86 ? 3206 ARG A CG    1 
ATOM   12408 C CD    . ARG A 1 3206 ? 135.751 106.043 122.390 1.00 301.86 ? 3206 ARG A CD    1 
ATOM   12409 N NE    . ARG A 1 3206 ? 136.684 107.043 121.884 1.00 301.86 ? 3206 ARG A NE    1 
ATOM   12410 C CZ    . ARG A 1 3206 ? 136.460 107.812 120.827 1.00 301.86 ? 3206 ARG A CZ    1 
ATOM   12411 N NH1   . ARG A 1 3206 ? 135.342 107.715 120.126 1.00 301.86 ? 3206 ARG A NH1   1 
ATOM   12412 N NH2   . ARG A 1 3206 ? 137.381 108.699 120.463 1.00 301.86 ? 3206 ARG A NH2   1 
ATOM   12413 N N     . LYS A 1 3207 ? 140.460 103.731 120.582 1.00 313.60 ? 3207 LYS A N     1 
ATOM   12414 C CA    . LYS A 1 3207 ? 141.375 103.441 119.482 1.00 313.60 ? 3207 LYS A CA    1 
ATOM   12415 C C     . LYS A 1 3207 ? 142.026 102.074 119.654 1.00 313.60 ? 3207 LYS A C     1 
ATOM   12416 O O     . LYS A 1 3207 ? 142.234 101.349 118.675 1.00 313.60 ? 3207 LYS A O     1 
ATOM   12417 C CB    . LYS A 1 3207 ? 142.435 104.537 119.371 1.00 313.60 ? 3207 LYS A CB    1 
ATOM   12418 C CG    . LYS A 1 3207 ? 143.395 104.361 118.197 1.00 313.60 ? 3207 LYS A CG    1 
ATOM   12419 C CD    . LYS A 1 3207 ? 144.695 103.710 118.637 1.00 313.60 ? 3207 LYS A CD    1 
ATOM   12420 C CE    . LYS A 1 3207 ? 145.171 104.294 119.952 1.00 313.60 ? 3207 LYS A CE    1 
ATOM   12421 N NZ    . LYS A 1 3207 ? 146.091 103.368 120.652 1.00 313.60 ? 3207 LYS A NZ    1 
ATOM   12422 N N     . ILE A 1 3208 ? 142.367 101.706 120.890 1.00 320.06 ? 3208 ILE A N     1 
ATOM   12423 C CA    . ILE A 1 3208 ? 142.962 100.397 121.130 1.00 320.06 ? 3208 ILE A CA    1 
ATOM   12424 C C     . ILE A 1 3208 ? 141.945 99.289  120.891 1.00 320.06 ? 3208 ILE A C     1 
ATOM   12425 O O     . ILE A 1 3208 ? 142.302 98.207  120.417 1.00 320.06 ? 3208 ILE A O     1 
ATOM   12426 C CB    . ILE A 1 3208 ? 143.567 100.318 122.543 1.00 320.06 ? 3208 ILE A CB    1 
ATOM   12427 C CG1   . ILE A 1 3208 ? 144.717 101.309 122.686 1.00 320.06 ? 3208 ILE A CG1   1 
ATOM   12428 C CG2   . ILE A 1 3208 ? 144.111 98.940  122.806 1.00 320.06 ? 3208 ILE A CG2   1 
ATOM   12429 C CD1   . ILE A 1 3208 ? 145.321 101.332 124.067 1.00 320.06 ? 3208 ILE A CD1   1 
ATOM   12430 N N     . LYS A 1 3209 ? 140.671 99.524  121.212 1.00 322.75 ? 3209 LYS A N     1 
ATOM   12431 C CA    . LYS A 1 3209 ? 139.643 98.549  120.857 1.00 322.75 ? 3209 LYS A CA    1 
ATOM   12432 C C     . LYS A 1 3209 ? 139.558 98.371  119.343 1.00 322.75 ? 3209 LYS A C     1 
ATOM   12433 O O     . LYS A 1 3209 ? 139.408 97.247  118.843 1.00 322.75 ? 3209 LYS A O     1 
ATOM   12434 C CB    . LYS A 1 3209 ? 138.291 98.975  121.430 1.00 322.75 ? 3209 LYS A CB    1 
ATOM   12435 C CG    . LYS A 1 3209 ? 138.120 98.691  122.918 1.00 322.75 ? 3209 LYS A CG    1 
ATOM   12436 C CD    . LYS A 1 3209 ? 138.352 97.223  123.248 1.00 322.75 ? 3209 LYS A CD    1 
ATOM   12437 C CE    . LYS A 1 3209 ? 137.265 96.338  122.664 1.00 322.75 ? 3209 LYS A CE    1 
ATOM   12438 N NZ    . LYS A 1 3209 ? 136.063 96.285  123.539 1.00 322.75 ? 3209 LYS A NZ    1 
ATOM   12439 N N     . GLU A 1 3210 ? 139.655 99.475  118.598 1.00 335.56 ? 3210 GLU A N     1 
ATOM   12440 C CA    . GLU A 1 3210 ? 139.673 99.378  117.139 1.00 335.56 ? 3210 GLU A CA    1 
ATOM   12441 C C     . GLU A 1 3210 ? 140.892 98.602  116.649 1.00 335.56 ? 3210 GLU A C     1 
ATOM   12442 O O     . GLU A 1 3210 ? 140.794 97.793  115.717 1.00 335.56 ? 3210 GLU A O     1 
ATOM   12443 C CB    . GLU A 1 3210 ? 139.637 100.774 116.516 1.00 335.56 ? 3210 GLU A CB    1 
ATOM   12444 C CG    . GLU A 1 3210 ? 138.381 101.570 116.846 1.00 335.56 ? 3210 GLU A CG    1 
ATOM   12445 C CD    . GLU A 1 3210 ? 137.154 100.690 117.007 1.00 335.56 ? 3210 GLU A CD    1 
ATOM   12446 O OE1   . GLU A 1 3210 ? 136.619 100.218 115.982 1.00 335.56 ? 3210 GLU A OE1   1 
ATOM   12447 O OE2   . GLU A 1 3210 ? 136.722 100.472 118.159 1.00 335.56 ? 3210 GLU A OE2   1 
ATOM   12448 N N     . THR A 1 3211 ? 142.054 98.838  117.262 1.00 339.23 ? 3211 THR A N     1 
ATOM   12449 C CA    . THR A 1 3211 ? 143.242 98.069  116.902 1.00 339.23 ? 3211 THR A CA    1 
ATOM   12450 C C     . THR A 1 3211 ? 143.083 96.596  117.257 1.00 339.23 ? 3211 THR A C     1 
ATOM   12451 O O     . THR A 1 3211 ? 143.622 95.734  116.560 1.00 339.23 ? 3211 THR A O     1 
ATOM   12452 C CB    . THR A 1 3211 ? 144.487 98.641  117.582 1.00 339.23 ? 3211 THR A CB    1 
ATOM   12453 O OG1   . THR A 1 3211 ? 144.349 98.542  119.004 1.00 339.23 ? 3211 THR A OG1   1 
ATOM   12454 C CG2   . THR A 1 3211 ? 144.699 100.096 117.187 1.00 339.23 ? 3211 THR A CG2   1 
ATOM   12455 N N     . VAL A 1 3212 ? 142.353 96.289  118.331 1.00 344.63 ? 3212 VAL A N     1 
ATOM   12456 C CA    . VAL A 1 3212 ? 142.067 94.898  118.679 1.00 344.63 ? 3212 VAL A CA    1 
ATOM   12457 C C     . VAL A 1 3212 ? 141.206 94.249  117.603 1.00 344.63 ? 3212 VAL A C     1 
ATOM   12458 O O     . VAL A 1 3212 ? 141.426 93.094  117.215 1.00 344.63 ? 3212 VAL A O     1 
ATOM   12459 C CB    . VAL A 1 3212 ? 141.396 94.824  120.064 1.00 344.63 ? 3212 VAL A CB    1 
ATOM   12460 C CG1   . VAL A 1 3212 ? 140.680 93.495  120.246 1.00 344.63 ? 3212 VAL A CG1   1 
ATOM   12461 C CG2   . VAL A 1 3212 ? 142.423 95.029  121.161 1.00 344.63 ? 3212 VAL A CG2   1 
ATOM   12462 N N     . ASP A 1 3213 ? 140.202 94.980  117.115 1.00 349.67 ? 3213 ASP A N     1 
ATOM   12463 C CA    . ASP A 1 3213 ? 139.394 94.470  116.010 1.00 349.67 ? 3213 ASP A CA    1 
ATOM   12464 C C     . ASP A 1 3213 ? 140.248 94.242  114.766 1.00 349.67 ? 3213 ASP A C     1 
ATOM   12465 O O     . ASP A 1 3213 ? 140.076 93.243  114.056 1.00 349.67 ? 3213 ASP A O     1 
ATOM   12466 C CB    . ASP A 1 3213 ? 138.246 95.434  115.713 1.00 349.67 ? 3213 ASP A CB    1 
ATOM   12467 C CG    . ASP A 1 3213 ? 137.427 95.757  116.947 1.00 349.67 ? 3213 ASP A CG    1 
ATOM   12468 O OD1   . ASP A 1 3213 ? 137.371 94.909  117.861 1.00 349.67 ? 3213 ASP A OD1   1 
ATOM   12469 O OD2   . ASP A 1 3213 ? 136.840 96.858  117.005 1.00 349.67 ? 3213 ASP A OD2   1 
ATOM   12470 N N     . GLN A 1 3214 ? 141.177 95.161  114.490 1.00 353.37 ? 3214 GLN A N     1 
ATOM   12471 C CA    . GLN A 1 3214 ? 142.098 94.971  113.372 1.00 353.37 ? 3214 GLN A CA    1 
ATOM   12472 C C     . GLN A 1 3214 ? 142.977 93.743  113.584 1.00 353.37 ? 3214 GLN A C     1 
ATOM   12473 O O     . GLN A 1 3214 ? 143.292 93.022  112.632 1.00 353.37 ? 3214 GLN A O     1 
ATOM   12474 C CB    . GLN A 1 3214 ? 142.958 96.220  113.177 1.00 353.37 ? 3214 GLN A CB    1 
ATOM   12475 C CG    . GLN A 1 3214 ? 143.267 96.545  111.720 1.00 353.37 ? 3214 GLN A CG    1 
ATOM   12476 C CD    . GLN A 1 3214 ? 144.594 95.970  111.259 1.00 353.37 ? 3214 GLN A CD    1 
ATOM   12477 O OE1   . GLN A 1 3214 ? 145.398 95.509  112.067 1.00 353.37 ? 3214 GLN A OE1   1 
ATOM   12478 N NE2   . GLN A 1 3214 ? 144.827 95.993  109.952 1.00 353.37 ? 3214 GLN A NE2   1 
ATOM   12479 N N     . VAL A 1 3215 ? 143.391 93.500  114.828 1.00 355.84 ? 3215 VAL A N     1 
ATOM   12480 C CA    . VAL A 1 3215 ? 144.175 92.310  115.151 1.00 355.84 ? 3215 VAL A CA    1 
ATOM   12481 C C     . VAL A 1 3215 ? 143.374 91.055  114.837 1.00 355.84 ? 3215 VAL A C     1 
ATOM   12482 O O     . VAL A 1 3215 ? 143.881 90.101  114.233 1.00 355.84 ? 3215 VAL A O     1 
ATOM   12483 C CB    . VAL A 1 3215 ? 144.603 92.340  116.630 1.00 355.84 ? 3215 VAL A CB    1 
ATOM   12484 C CG1   . VAL A 1 3215 ? 145.065 90.962  117.089 1.00 355.84 ? 3215 VAL A CG1   1 
ATOM   12485 C CG2   . VAL A 1 3215 ? 145.679 93.379  116.851 1.00 355.84 ? 3215 VAL A CG2   1 
ATOM   12486 N N     . GLU A 1 3216 ? 142.106 91.042  115.249 1.00 357.09 ? 3216 GLU A N     1 
ATOM   12487 C CA    . GLU A 1 3216 ? 141.253 89.888  114.987 1.00 357.09 ? 3216 GLU A CA    1 
ATOM   12488 C C     . GLU A 1 3216 ? 141.062 89.673  113.491 1.00 357.09 ? 3216 GLU A C     1 
ATOM   12489 O O     . GLU A 1 3216 ? 141.042 88.530  113.019 1.00 357.09 ? 3216 GLU A O     1 
ATOM   12490 C CB    . GLU A 1 3216 ? 139.904 90.059  115.685 1.00 357.09 ? 3216 GLU A CB    1 
ATOM   12491 C CG    . GLU A 1 3216 ? 140.002 90.166  117.195 1.00 357.09 ? 3216 GLU A CG    1 
ATOM   12492 C CD    . GLU A 1 3216 ? 140.215 88.820  117.857 1.00 357.09 ? 3216 GLU A CD    1 
ATOM   12493 O OE1   . GLU A 1 3216 ? 139.794 87.798  117.276 1.00 357.09 ? 3216 GLU A OE1   1 
ATOM   12494 O OE2   . GLU A 1 3216 ? 140.805 88.783  118.957 1.00 357.09 ? 3216 GLU A OE2   1 
ATOM   12495 N N     . GLU A 1 3217 ? 140.912 90.759  112.730 1.00 362.17 ? 3217 GLU A N     1 
ATOM   12496 C CA    . GLU A 1 3217 ? 140.793 90.623  111.280 1.00 362.17 ? 3217 GLU A CA    1 
ATOM   12497 C C     . GLU A 1 3217 ? 142.075 90.075  110.661 1.00 362.17 ? 3217 GLU A C     1 
ATOM   12498 O O     . GLU A 1 3217 ? 142.027 89.194  109.795 1.00 362.17 ? 3217 GLU A O     1 
ATOM   12499 C CB    . GLU A 1 3217 ? 140.432 91.964  110.641 1.00 362.17 ? 3217 GLU A CB    1 
ATOM   12500 C CG    . GLU A 1 3217 ? 139.013 92.431  110.908 1.00 362.17 ? 3217 GLU A CG    1 
ATOM   12501 C CD    . GLU A 1 3217 ? 138.880 93.941  110.864 1.00 362.17 ? 3217 GLU A CD    1 
ATOM   12502 O OE1   . GLU A 1 3217 ? 139.711 94.595  110.197 1.00 362.17 ? 3217 GLU A OE1   1 
ATOM   12503 O OE2   . GLU A 1 3217 ? 137.940 94.474  111.492 1.00 362.17 ? 3217 GLU A OE2   1 
ATOM   12504 N N     . LEU A 1 3218 ? 143.232 90.581  111.093 1.00 355.39 ? 3218 LEU A N     1 
ATOM   12505 C CA    . LEU A 1 3218 ? 144.494 90.215  110.462 1.00 355.39 ? 3218 LEU A CA    1 
ATOM   12506 C C     . LEU A 1 3218 ? 145.012 88.852  110.900 1.00 355.39 ? 3218 LEU A C     1 
ATOM   12507 O O     . LEU A 1 3218 ? 145.867 88.284  110.212 1.00 355.39 ? 3218 LEU A O     1 
ATOM   12508 C CB    . LEU A 1 3218 ? 145.556 91.280  110.749 1.00 355.39 ? 3218 LEU A CB    1 
ATOM   12509 C CG    . LEU A 1 3218 ? 145.535 92.524  109.857 1.00 355.39 ? 3218 LEU A CG    1 
ATOM   12510 C CD1   . LEU A 1 3218 ? 146.891 93.215  109.859 1.00 355.39 ? 3218 LEU A CD1   1 
ATOM   12511 C CD2   . LEU A 1 3218 ? 145.113 92.168  108.438 1.00 355.39 ? 3218 LEU A CD2   1 
ATOM   12512 N N     . ARG A 1 3219 ? 144.527 88.319  112.025 1.00 355.93 ? 3219 ARG A N     1 
ATOM   12513 C CA    . ARG A 1 3219 ? 144.997 87.011  112.475 1.00 355.93 ? 3219 ARG A CA    1 
ATOM   12514 C C     . ARG A 1 3219 ? 144.625 85.916  111.483 1.00 355.93 ? 3219 ARG A C     1 
ATOM   12515 O O     . ARG A 1 3219 ? 145.429 85.019  111.206 1.00 355.93 ? 3219 ARG A O     1 
ATOM   12516 C CB    . ARG A 1 3219 ? 144.432 86.689  113.858 1.00 355.93 ? 3219 ARG A CB    1 
ATOM   12517 C CG    . ARG A 1 3219 ? 144.966 85.388  114.443 1.00 355.93 ? 3219 ARG A CG    1 
ATOM   12518 C CD    . ARG A 1 3219 ? 144.533 85.197  115.887 1.00 355.93 ? 3219 ARG A CD    1 
ATOM   12519 N NE    . ARG A 1 3219 ? 144.386 86.465  116.591 1.00 355.93 ? 3219 ARG A NE    1 
ATOM   12520 C CZ    . ARG A 1 3219 ? 143.261 86.881  117.157 1.00 355.93 ? 3219 ARG A CZ    1 
ATOM   12521 N NH1   . ARG A 1 3219 ? 142.161 86.146  117.130 1.00 355.93 ? 3219 ARG A NH1   1 
ATOM   12522 N NH2   . ARG A 1 3219 ? 143.241 88.063  117.767 1.00 355.93 ? 3219 ARG A NH2   1 
ATOM   12523 N N     . ARG A 1 3220 ? 143.412 85.970  110.942 1.00 347.19 ? 3220 ARG A N     1 
ATOM   12524 C CA    . ARG A 1 3220 ? 142.948 84.957  110.001 1.00 347.19 ? 3220 ARG A CA    1 
ATOM   12525 C C     . ARG A 1 3220 ? 142.611 85.568  108.646 1.00 347.19 ? 3220 ARG A C     1 
ATOM   12526 O O     . ARG A 1 3220 ? 142.221 84.863  107.715 0.00 347.19 ? 3220 ARG A O     1 
ATOM   12527 C CB    . ARG A 1 3220 ? 141.730 84.223  110.563 1.00 347.19 ? 3220 ARG A CB    1 
ATOM   12528 C CG    . ARG A 1 3220 ? 141.770 84.008  112.067 1.00 347.19 ? 3220 ARG A CG    1 
ATOM   12529 C CD    . ARG A 1 3220 ? 140.542 83.247  112.548 1.00 347.19 ? 3220 ARG A CD    1 
ATOM   12530 N NE    . ARG A 1 3220 ? 140.545 81.849  112.128 1.00 347.19 ? 3220 ARG A NE    1 
ATOM   12531 C CZ    . ARG A 1 3220 ? 141.442 80.943  112.499 1.00 347.19 ? 3220 ARG A CZ    1 
ATOM   12532 N NH1   . ARG A 1 3220 ? 142.419 81.236  113.341 1.00 347.19 ? 3220 ARG A NH1   1 
ATOM   12533 N NH2   . ARG A 1 3220 ? 141.348 79.706  112.020 1.00 347.19 ? 3220 ARG A NH2   1 
ATOM   12534 N N     . LYS A 1 3471 ? 151.938 85.572  112.058 1.00 348.51 ? 3471 LYS A N     1 
ATOM   12535 C CA    . LYS A 1 3471 ? 152.391 84.470  112.897 1.00 348.51 ? 3471 LYS A CA    1 
ATOM   12536 C C     . LYS A 1 3471 ? 151.447 84.285  114.084 1.00 348.51 ? 3471 LYS A C     1 
ATOM   12537 O O     . LYS A 1 3471 ? 150.955 85.259  114.653 1.00 348.51 ? 3471 LYS A O     1 
ATOM   12538 C CB    . LYS A 1 3471 ? 153.820 84.719  113.381 1.00 348.51 ? 3471 LYS A CB    1 
ATOM   12539 C CG    . LYS A 1 3471 ? 154.711 83.492  113.368 1.00 348.51 ? 3471 LYS A CG    1 
ATOM   12540 C CD    . LYS A 1 3471 ? 156.170 83.881  113.522 1.00 348.51 ? 3471 LYS A CD    1 
ATOM   12541 C CE    . LYS A 1 3471 ? 156.693 84.565  112.271 1.00 348.51 ? 3471 LYS A CE    1 
ATOM   12542 N NZ    . LYS A 1 3471 ? 158.023 85.197  112.500 1.00 348.51 ? 3471 LYS A NZ    1 
ATOM   12543 N N     . VAL A 1 3472 ? 151.193 83.026  114.449 1.00 354.05 ? 3472 VAL A N     1 
ATOM   12544 C CA    . VAL A 1 3472 ? 150.290 82.741  115.561 1.00 354.05 ? 3472 VAL A CA    1 
ATOM   12545 C C     . VAL A 1 3472 ? 150.909 83.182  116.884 1.00 354.05 ? 3472 VAL A C     1 
ATOM   12546 O O     . VAL A 1 3472 ? 150.210 83.684  117.775 1.00 354.05 ? 3472 VAL A O     1 
ATOM   12547 C CB    . VAL A 1 3472 ? 149.916 81.246  115.570 1.00 354.05 ? 3472 VAL A CB    1 
ATOM   12548 C CG1   . VAL A 1 3472 ? 151.166 80.377  115.517 1.00 354.05 ? 3472 VAL A CG1   1 
ATOM   12549 C CG2   . VAL A 1 3472 ? 149.070 80.908  116.791 1.00 354.05 ? 3472 VAL A CG2   1 
ATOM   12550 N N     . ASN A 1 3473 ? 152.224 83.006  117.034 1.00 358.56 ? 3473 ASN A N     1 
ATOM   12551 C CA    . ASN A 1 3473 ? 152.894 83.447  118.252 1.00 358.56 ? 3473 ASN A CA    1 
ATOM   12552 C C     . ASN A 1 3473 ? 152.766 84.953  118.429 1.00 358.56 ? 3473 ASN A C     1 
ATOM   12553 O O     . ASN A 1 3473 ? 152.570 85.442  119.550 1.00 358.56 ? 3473 ASN A O     1 
ATOM   12554 C CB    . ASN A 1 3473 ? 154.365 83.032  118.223 1.00 358.56 ? 3473 ASN A CB    1 
ATOM   12555 C CG    . ASN A 1 3473 ? 154.561 81.619  117.708 1.00 358.56 ? 3473 ASN A CG    1 
ATOM   12556 O OD1   . ASN A 1 3473 ? 153.646 80.797  117.751 1.00 358.56 ? 3473 ASN A OD1   1 
ATOM   12557 N ND2   . ASN A 1 3473 ? 155.761 81.329  117.218 1.00 358.56 ? 3473 ASN A ND2   1 
ATOM   12558 N N     . ARG A 1 3474 ? 152.873 85.705  117.331 1.00 353.78 ? 3474 ARG A N     1 
ATOM   12559 C CA    . ARG A 1 3474 ? 152.677 87.148  117.400 1.00 353.78 ? 3474 ARG A CA    1 
ATOM   12560 C C     . ARG A 1 3474 ? 151.269 87.486  117.870 1.00 353.78 ? 3474 ARG A C     1 
ATOM   12561 O O     . ARG A 1 3474 ? 151.083 88.378  118.704 1.00 353.78 ? 3474 ARG A O     1 
ATOM   12562 C CB    . ARG A 1 3474 ? 152.956 87.781  116.037 1.00 353.78 ? 3474 ARG A CB    1 
ATOM   12563 C CG    . ARG A 1 3474 ? 154.365 87.544  115.512 1.00 353.78 ? 3474 ARG A CG    1 
ATOM   12564 C CD    . ARG A 1 3474 ? 155.414 87.820  116.570 1.00 353.78 ? 3474 ARG A CD    1 
ATOM   12565 N NE    . ARG A 1 3474 ? 155.973 86.596  117.130 1.00 353.78 ? 3474 ARG A NE    1 
ATOM   12566 C CZ    . ARG A 1 3474 ? 156.979 85.919  116.596 1.00 353.78 ? 3474 ARG A CZ    1 
ATOM   12567 N NH1   . ARG A 1 3474 ? 157.563 86.317  115.477 1.00 353.78 ? 3474 ARG A NH1   1 
ATOM   12568 N NH2   . ARG A 1 3474 ? 157.413 84.817  117.200 1.00 353.78 ? 3474 ARG A NH2   1 
ATOM   12569 N N     . SER A 1 3475 ? 150.264 86.775  117.354 1.00 356.14 ? 3475 SER A N     1 
ATOM   12570 C CA    . SER A 1 3475 ? 148.888 87.034  117.770 1.00 356.14 ? 3475 SER A CA    1 
ATOM   12571 C C     . SER A 1 3475 ? 148.689 86.737  119.252 1.00 356.14 ? 3475 SER A C     1 
ATOM   12572 O O     . SER A 1 3475 ? 148.030 87.505  119.963 1.00 356.14 ? 3475 SER A O     1 
ATOM   12573 C CB    . SER A 1 3475 ? 147.920 86.209  116.922 1.00 356.14 ? 3475 SER A CB    1 
ATOM   12574 O OG    . SER A 1 3475 ? 148.051 84.826  117.199 1.00 356.14 ? 3475 SER A OG    1 
ATOM   12575 N N     . THR A 1 3476 ? 149.247 85.625  119.737 1.00 358.53 ? 3476 THR A N     1 
ATOM   12576 C CA    . THR A 1 3476 ? 149.105 85.289  121.152 1.00 358.53 ? 3476 THR A CA    1 
ATOM   12577 C C     . THR A 1 3476 ? 149.808 86.311  122.041 1.00 358.53 ? 3476 THR A C     1 
ATOM   12578 O O     . THR A 1 3476 ? 149.265 86.722  123.077 1.00 358.53 ? 3476 THR A O     1 
ATOM   12579 C CB    . THR A 1 3476 ? 149.645 83.884  121.417 1.00 358.53 ? 3476 THR A CB    1 
ATOM   12580 O OG1   . THR A 1 3476 ? 151.024 83.818  121.033 1.00 358.53 ? 3476 THR A OG1   1 
ATOM   12581 C CG2   . THR A 1 3476 ? 148.852 82.852  120.628 1.00 358.53 ? 3476 THR A CG2   1 
ATOM   12582 N N     . ALA A 1 3477 ? 151.018 86.731  121.656 1.00 355.98 ? 3477 ALA A N     1 
ATOM   12583 C CA    . ALA A 1 3477 ? 151.729 87.741  122.432 1.00 355.98 ? 3477 ALA A CA    1 
ATOM   12584 C C     . ALA A 1 3477 ? 150.964 89.057  122.446 1.00 355.98 ? 3477 ALA A C     1 
ATOM   12585 O O     . ALA A 1 3477 ? 150.887 89.733  123.480 1.00 355.98 ? 3477 ALA A O     1 
ATOM   12586 C CB    . ALA A 1 3477 ? 153.136 87.942  121.872 1.00 355.98 ? 3477 ALA A CB    1 
ATOM   12587 N N     . LEU A 1 3478 ? 150.390 89.436  121.302 1.00 349.09 ? 3478 LEU A N     1 
ATOM   12588 C CA    . LEU A 1 3478 ? 149.590 90.651  121.241 1.00 349.09 ? 3478 LEU A CA    1 
ATOM   12589 C C     . LEU A 1 3478 ? 148.359 90.548  122.130 1.00 349.09 ? 3478 LEU A C     1 
ATOM   12590 O O     . LEU A 1 3478 ? 148.004 91.510  122.814 1.00 349.09 ? 3478 LEU A O     1 
ATOM   12591 C CB    . LEU A 1 3478 ? 149.198 90.939  119.793 1.00 349.09 ? 3478 LEU A CB    1 
ATOM   12592 C CG    . LEU A 1 3478 ? 149.174 92.409  119.377 1.00 349.09 ? 3478 LEU A CG    1 
ATOM   12593 C CD1   . LEU A 1 3478 ? 150.492 93.079  119.693 1.00 349.09 ? 3478 LEU A CD1   1 
ATOM   12594 C CD2   . LEU A 1 3478 ? 148.902 92.501  117.892 1.00 349.09 ? 3478 LEU A CD2   1 
ATOM   12595 N N     . LEU A 1 3479 ? 147.700 89.386  122.145 1.00 340.99 ? 3479 LEU A N     1 
ATOM   12596 C CA    . LEU A 1 3479 ? 146.539 89.213  123.015 1.00 340.99 ? 3479 LEU A CA    1 
ATOM   12597 C C     . LEU A 1 3479 ? 146.927 89.341  124.484 1.00 340.99 ? 3479 LEU A C     1 
ATOM   12598 O O     . LEU A 1 3479 ? 146.226 89.998  125.265 1.00 340.99 ? 3479 LEU A O     1 
ATOM   12599 C CB    . LEU A 1 3479 ? 145.871 87.862  122.738 1.00 340.99 ? 3479 LEU A CB    1 
ATOM   12600 C CG    . LEU A 1 3479 ? 144.881 87.261  123.745 1.00 340.99 ? 3479 LEU A CG    1 
ATOM   12601 C CD1   . LEU A 1 3479 ? 143.852 86.419  123.012 1.00 340.99 ? 3479 LEU A CD1   1 
ATOM   12602 C CD2   . LEU A 1 3479 ? 145.579 86.400  124.793 1.00 340.99 ? 3479 LEU A CD2   1 
ATOM   12603 N N     . LYS A 1 3480 ? 148.039 88.716  124.878 1.00 340.57 ? 3480 LYS A N     1 
ATOM   12604 C CA    . LYS A 1 3480 ? 148.480 88.802  126.268 1.00 340.57 ? 3480 LYS A CA    1 
ATOM   12605 C C     . LYS A 1 3480 ? 148.806 90.242  126.652 1.00 340.57 ? 3480 LYS A C     1 
ATOM   12606 O O     . LYS A 1 3480 ? 148.356 90.743  127.695 1.00 340.57 ? 3480 LYS A O     1 
ATOM   12607 C CB    . LYS A 1 3480 ? 149.695 87.900  126.488 1.00 340.57 ? 3480 LYS A CB    1 
ATOM   12608 C CG    . LYS A 1 3480 ? 149.359 86.506  126.987 1.00 340.57 ? 3480 LYS A CG    1 
ATOM   12609 C CD    . LYS A 1 3480 ? 150.578 85.598  126.944 1.00 340.57 ? 3480 LYS A CD    1 
ATOM   12610 C CE    . LYS A 1 3480 ? 150.894 85.156  125.526 1.00 340.57 ? 3480 LYS A CE    1 
ATOM   12611 N NZ    . LYS A 1 3480 ? 149.725 84.509  124.872 1.00 340.57 ? 3480 LYS A NZ    1 
ATOM   12612 N N     . SER A 1 3481 ? 149.589 90.925  125.812 1.00 335.31 ? 3481 SER A N     1 
ATOM   12613 C CA    . SER A 1 3481 ? 149.946 92.310  126.095 1.00 335.31 ? 3481 SER A CA    1 
ATOM   12614 C C     . SER A 1 3481 ? 148.718 93.207  126.110 1.00 335.31 ? 3481 SER A C     1 
ATOM   12615 O O     . SER A 1 3481 ? 148.657 94.161  126.892 1.00 335.31 ? 3481 SER A O     1 
ATOM   12616 C CB    . SER A 1 3481 ? 150.963 92.807  125.067 1.00 335.31 ? 3481 SER A CB    1 
ATOM   12617 O OG    . SER A 1 3481 ? 150.427 92.767  123.756 1.00 335.31 ? 3481 SER A OG    1 
ATOM   12618 N N     . LEU A 1 3482 ? 147.722 92.905  125.276 1.00 328.26 ? 3482 LEU A N     1 
ATOM   12619 C CA    . LEU A 1 3482 ? 146.510 93.710  125.244 1.00 328.26 ? 3482 LEU A CA    1 
ATOM   12620 C C     . LEU A 1 3482 ? 145.678 93.514  126.502 1.00 328.26 ? 3482 LEU A C     1 
ATOM   12621 O O     . LEU A 1 3482 ? 145.108 94.475  127.027 1.00 328.26 ? 3482 LEU A O     1 
ATOM   12622 C CB    . LEU A 1 3482 ? 145.696 93.370  123.998 1.00 328.26 ? 3482 LEU A CB    1 
ATOM   12623 C CG    . LEU A 1 3482 ? 145.843 94.392  122.876 1.00 328.26 ? 3482 LEU A CG    1 
ATOM   12624 C CD1   . LEU A 1 3482 ? 145.219 95.684  123.326 1.00 328.26 ? 3482 LEU A CD1   1 
ATOM   12625 C CD2   . LEU A 1 3482 ? 147.302 94.611  122.511 1.00 328.26 ? 3482 LEU A CD2   1 
ATOM   12626 N N     . SER A 1 3483 ? 145.590 92.279  127.001 1.00 326.25 ? 3483 SER A N     1 
ATOM   12627 C CA    . SER A 1 3483 ? 144.900 92.059  128.270 1.00 326.25 ? 3483 SER A CA    1 
ATOM   12628 C C     . SER A 1 3483 ? 145.607 92.786  129.408 1.00 326.25 ? 3483 SER A C     1 
ATOM   12629 O O     . SER A 1 3483 ? 144.958 93.407  130.265 1.00 326.25 ? 3483 SER A O     1 
ATOM   12630 C CB    . SER A 1 3483 ? 144.800 90.563  128.566 1.00 326.25 ? 3483 SER A CB    1 
ATOM   12631 O OG    . SER A 1 3483 ? 144.438 89.835  127.406 1.00 326.25 ? 3483 SER A OG    1 
ATOM   12632 N N     . ALA A 1 3484 ? 146.943 92.725  129.429 1.00 321.48 ? 3484 ALA A N     1 
ATOM   12633 C CA    . ALA A 1 3484 ? 147.693 93.441  130.457 1.00 321.48 ? 3484 ALA A CA    1 
ATOM   12634 C C     . ALA A 1 3484 ? 147.457 94.945  130.367 1.00 321.48 ? 3484 ALA A C     1 
ATOM   12635 O O     . ALA A 1 3484 ? 147.254 95.616  131.389 1.00 321.48 ? 3484 ALA A O     1 
ATOM   12636 C CB    . ALA A 1 3484 ? 149.182 93.121  130.339 1.00 321.48 ? 3484 ALA A CB    1 
ATOM   12637 N N     . GLU A 1 3485 ? 147.472 95.491  129.149 1.00 315.28 ? 3485 GLU A N     1 
ATOM   12638 C CA    . GLU A 1 3485 ? 147.216 96.914  128.961 1.00 315.28 ? 3485 GLU A CA    1 
ATOM   12639 C C     . GLU A 1 3485 ? 145.803 97.284  129.394 1.00 315.28 ? 3485 GLU A C     1 
ATOM   12640 O O     . GLU A 1 3485 ? 145.584 98.352  129.974 1.00 315.28 ? 3485 GLU A O     1 
ATOM   12641 C CB    . GLU A 1 3485 ? 147.449 97.291  127.499 1.00 315.28 ? 3485 GLU A CB    1 
ATOM   12642 C CG    . GLU A 1 3485 ? 147.183 98.747  127.181 1.00 315.28 ? 3485 GLU A CG    1 
ATOM   12643 C CD    . GLU A 1 3485 ? 145.802 98.959  126.599 1.00 315.28 ? 3485 GLU A CD    1 
ATOM   12644 O OE1   . GLU A 1 3485 ? 145.362 98.119  125.786 1.00 315.28 ? 3485 GLU A OE1   1 
ATOM   12645 O OE2   . GLU A 1 3485 ? 145.151 99.960  126.962 1.00 315.28 ? 3485 GLU A OE2   1 
ATOM   12646 N N     . ARG A 1 3486 ? 144.829 96.417  129.110 1.00 315.54 ? 3486 ARG A N     1 
ATOM   12647 C CA    . ARG A 1 3486 ? 143.452 96.680  129.514 1.00 315.54 ? 3486 ARG A CA    1 
ATOM   12648 C C     . ARG A 1 3486 ? 143.335 96.757  131.030 1.00 315.54 ? 3486 ARG A C     1 
ATOM   12649 O O     . ARG A 1 3486 ? 142.688 97.663  131.571 1.00 315.54 ? 3486 ARG A O     1 
ATOM   12650 C CB    . ARG A 1 3486 ? 142.532 95.592  128.958 1.00 315.54 ? 3486 ARG A CB    1 
ATOM   12651 C CG    . ARG A 1 3486 ? 142.037 95.847  127.544 1.00 315.54 ? 3486 ARG A CG    1 
ATOM   12652 C CD    . ARG A 1 3486 ? 141.183 97.098  127.474 1.00 315.54 ? 3486 ARG A CD    1 
ATOM   12653 N NE    . ARG A 1 3486 ? 140.848 97.456  126.101 1.00 315.54 ? 3486 ARG A NE    1 
ATOM   12654 C CZ    . ARG A 1 3486 ? 141.605 98.216  125.321 1.00 315.54 ? 3486 ARG A CZ    1 
ATOM   12655 N NH1   . ARG A 1 3486 ? 142.760 98.703  125.744 1.00 315.54 ? 3486 ARG A NH1   1 
ATOM   12656 N NH2   . ARG A 1 3486 ? 141.192 98.496  124.089 1.00 315.54 ? 3486 ARG A NH2   1 
ATOM   12657 N N     . GLU A 1 3487 ? 143.961 95.811  131.736 1.00 303.29 ? 3487 GLU A N     1 
ATOM   12658 C CA    . GLU A 1 3487 ? 143.914 95.851  133.196 1.00 303.29 ? 3487 GLU A CA    1 
ATOM   12659 C C     . GLU A 1 3487 ? 144.631 97.087  133.738 1.00 303.29 ? 3487 GLU A C     1 
ATOM   12660 O O     . GLU A 1 3487 ? 144.143 97.738  134.676 1.00 303.29 ? 3487 GLU A O     1 
ATOM   12661 C CB    . GLU A 1 3487 ? 144.493 94.558  133.779 1.00 303.29 ? 3487 GLU A CB    1 
ATOM   12662 C CG    . GLU A 1 3487 ? 145.981 94.576  134.098 1.00 303.29 ? 3487 GLU A CG    1 
ATOM   12663 C CD    . GLU A 1 3487 ? 146.486 93.246  134.616 1.00 303.29 ? 3487 GLU A CD    1 
ATOM   12664 O OE1   . GLU A 1 3487 ? 145.832 92.215  134.349 1.00 303.29 ? 3487 GLU A OE1   1 
ATOM   12665 O OE2   . GLU A 1 3487 ? 147.539 93.231  135.288 1.00 303.29 ? 3487 GLU A OE2   1 
ATOM   12666 N N     . ARG A 1 3488 ? 145.769 97.449  133.134 1.00 298.27 ? 3488 ARG A N     1 
ATOM   12667 C CA    . ARG A 1 3488 ? 146.499 98.632  133.576 1.00 298.27 ? 3488 ARG A CA    1 
ATOM   12668 C C     . ARG A 1 3488 ? 145.670 99.893  133.382 1.00 298.27 ? 3488 ARG A C     1 
ATOM   12669 O O     . ARG A 1 3488 ? 145.646 100.771 134.251 1.00 298.27 ? 3488 ARG A O     1 
ATOM   12670 C CB    . ARG A 1 3488 ? 147.820 98.745  132.818 1.00 298.27 ? 3488 ARG A CB    1 
ATOM   12671 C CG    . ARG A 1 3488 ? 148.907 97.801  133.293 1.00 298.27 ? 3488 ARG A CG    1 
ATOM   12672 C CD    . ARG A 1 3488 ? 150.275 98.281  132.832 1.00 298.27 ? 3488 ARG A CD    1 
ATOM   12673 N NE    . ARG A 1 3488 ? 150.270 98.648  131.420 1.00 298.27 ? 3488 ARG A NE    1 
ATOM   12674 C CZ    . ARG A 1 3488 ? 150.458 99.879  130.964 1.00 298.27 ? 3488 ARG A CZ    1 
ATOM   12675 N NH1   . ARG A 1 3488 ? 150.695 100.891 131.783 1.00 298.27 ? 3488 ARG A NH1   1 
ATOM   12676 N NH2   . ARG A 1 3488 ? 150.400 100.101 129.655 1.00 298.27 ? 3488 ARG A NH2   1 
ATOM   12677 N N     . TRP A 1 3489 ? 144.974 99.996  132.250 1.00 287.89 ? 3489 TRP A N     1 
ATOM   12678 C CA    . TRP A 1 3489 ? 144.185 101.189 131.976 1.00 287.89 ? 3489 TRP A CA    1 
ATOM   12679 C C     . TRP A 1 3489 ? 142.927 101.243 132.830 1.00 287.89 ? 3489 TRP A C     1 
ATOM   12680 O O     . TRP A 1 3489 ? 142.478 102.334 133.194 1.00 287.89 ? 3489 TRP A O     1 
ATOM   12681 C CB    . TRP A 1 3489 ? 143.840 101.254 130.493 1.00 287.89 ? 3489 TRP A CB    1 
ATOM   12682 C CG    . TRP A 1 3489 ? 144.966 101.792 129.676 1.00 287.89 ? 3489 TRP A CG    1 
ATOM   12683 C CD1   . TRP A 1 3489 ? 146.221 101.271 129.568 1.00 287.89 ? 3489 TRP A CD1   1 
ATOM   12684 C CD2   . TRP A 1 3489 ? 144.947 102.965 128.860 1.00 287.89 ? 3489 TRP A CD2   1 
ATOM   12685 N NE1   . TRP A 1 3489 ? 146.984 102.044 128.729 1.00 287.89 ? 3489 TRP A NE1   1 
ATOM   12686 C CE2   . TRP A 1 3489 ? 146.224 103.092 128.281 1.00 287.89 ? 3489 TRP A CE2   1 
ATOM   12687 C CE3   . TRP A 1 3489 ? 143.973 103.920 128.559 1.00 287.89 ? 3489 TRP A CE3   1 
ATOM   12688 C CZ2   . TRP A 1 3489 ? 146.551 104.133 127.419 1.00 287.89 ? 3489 TRP A CZ2   1 
ATOM   12689 C CZ3   . TRP A 1 3489 ? 144.299 104.952 127.705 1.00 287.89 ? 3489 TRP A CZ3   1 
ATOM   12690 C CH2   . TRP A 1 3489 ? 145.578 105.053 127.147 1.00 287.89 ? 3489 TRP A CH2   1 
ATOM   12691 N N     . GLU A 1 3490 ? 142.345 100.090 133.166 1.00 278.06 ? 3490 GLU A N     1 
ATOM   12692 C CA    . GLU A 1 3490 ? 141.243 100.093 134.122 1.00 278.06 ? 3490 GLU A CA    1 
ATOM   12693 C C     . GLU A 1 3490 ? 141.705 100.597 135.484 1.00 278.06 ? 3490 GLU A C     1 
ATOM   12694 O O     . GLU A 1 3490 ? 141.024 101.414 136.122 1.00 278.06 ? 3490 GLU A O     1 
ATOM   12695 C CB    . GLU A 1 3490 ? 140.638 98.695  134.238 1.00 278.06 ? 3490 GLU A CB    1 
ATOM   12696 C CG    . GLU A 1 3490 ? 139.437 98.631  135.163 1.00 278.06 ? 3490 GLU A CG    1 
ATOM   12697 C CD    . GLU A 1 3490 ? 138.226 99.340  134.590 1.00 278.06 ? 3490 GLU A CD    1 
ATOM   12698 O OE1   . GLU A 1 3490 ? 138.067 99.342  133.352 1.00 278.06 ? 3490 GLU A OE1   1 
ATOM   12699 O OE2   . GLU A 1 3490 ? 137.437 99.903  135.377 1.00 278.06 ? 3490 GLU A OE2   1 
ATOM   12700 N N     . LYS A 1 3491 ? 142.875 100.137 135.938 1.00 270.39 ? 3491 LYS A N     1 
ATOM   12701 C CA    . LYS A 1 3491 ? 143.423 100.657 137.188 1.00 270.39 ? 3491 LYS A CA    1 
ATOM   12702 C C     . LYS A 1 3491 ? 143.713 102.151 137.083 1.00 270.39 ? 3491 LYS A C     1 
ATOM   12703 O O     . LYS A 1 3491 ? 143.522 102.901 138.050 1.00 270.39 ? 3491 LYS A O     1 
ATOM   12704 C CB    . LYS A 1 3491 ? 144.686 99.886  137.570 1.00 270.39 ? 3491 LYS A CB    1 
ATOM   12705 C CG    . LYS A 1 3491 ? 144.418 98.615  138.356 1.00 270.39 ? 3491 LYS A CG    1 
ATOM   12706 C CD    . LYS A 1 3491 ? 145.588 97.651  138.269 1.00 270.39 ? 3491 LYS A CD    1 
ATOM   12707 C CE    . LYS A 1 3491 ? 145.153 96.311  137.703 1.00 270.39 ? 3491 LYS A CE    1 
ATOM   12708 N NZ    . LYS A 1 3491 ? 146.291 95.358  137.612 1.00 270.39 ? 3491 LYS A NZ    1 
ATOM   12709 N N     . THR A 1 3492 ? 144.187 102.597 135.918 1.00 258.62 ? 3492 THR A N     1 
ATOM   12710 C CA    . THR A 1 3492 ? 144.456 104.017 135.712 1.00 258.62 ? 3492 THR A CA    1 
ATOM   12711 C C     . THR A 1 3492 ? 143.178 104.840 135.808 1.00 258.62 ? 3492 THR A C     1 
ATOM   12712 O O     . THR A 1 3492 ? 143.165 105.915 136.418 1.00 258.62 ? 3492 THR A O     1 
ATOM   12713 C CB    . THR A 1 3492 ? 145.129 104.231 134.357 1.00 258.62 ? 3492 THR A CB    1 
ATOM   12714 O OG1   . THR A 1 3492 ? 146.156 103.249 134.172 1.00 258.62 ? 3492 THR A OG1   1 
ATOM   12715 C CG2   . THR A 1 3492 ? 145.745 105.616 134.286 1.00 258.62 ? 3492 THR A CG2   1 
ATOM   12716 N N     . SER A 1 3493 ? 142.092 104.352 135.210 1.00 248.56 ? 3493 SER A N     1 
ATOM   12717 C CA    . SER A 1 3493 ? 140.814 105.045 135.323 1.00 248.56 ? 3493 SER A CA    1 
ATOM   12718 C C     . SER A 1 3493 ? 140.344 105.089 136.771 1.00 248.56 ? 3493 SER A C     1 
ATOM   12719 O O     . SER A 1 3493 ? 139.812 106.107 137.231 1.00 248.56 ? 3493 SER A O     1 
ATOM   12720 C CB    . SER A 1 3493 ? 139.769 104.369 134.438 1.00 248.56 ? 3493 SER A CB    1 
ATOM   12721 O OG    . SER A 1 3493 ? 138.989 103.452 135.186 1.00 248.56 ? 3493 SER A OG    1 
ATOM   12722 N N     . GLU A 1 3494 ? 140.529 103.990 137.507 1.00 230.81 ? 3494 GLU A N     1 
ATOM   12723 C CA    . GLU A 1 3494 ? 140.106 103.973 138.904 1.00 230.81 ? 3494 GLU A CA    1 
ATOM   12724 C C     . GLU A 1 3494 ? 140.889 104.983 139.740 1.00 230.81 ? 3494 GLU A C     1 
ATOM   12725 O O     . GLU A 1 3494 ? 140.306 105.724 140.544 1.00 230.81 ? 3494 GLU A O     1 
ATOM   12726 C CB    . GLU A 1 3494 ? 140.254 102.567 139.479 1.00 230.81 ? 3494 GLU A CB    1 
ATOM   12727 C CG    . GLU A 1 3494 ? 139.462 102.349 140.751 1.00 230.81 ? 3494 GLU A CG    1 
ATOM   12728 C CD    . GLU A 1 3494 ? 137.970 102.472 140.522 1.00 230.81 ? 3494 GLU A CD    1 
ATOM   12729 O OE1   . GLU A 1 3494 ? 137.340 101.462 140.145 1.00 230.81 ? 3494 GLU A OE1   1 
ATOM   12730 O OE2   . GLU A 1 3494 ? 137.425 103.579 140.718 1.00 230.81 ? 3494 GLU A OE2   1 
ATOM   12731 N N     . THR A 1 3495 ? 142.212 105.037 139.562 1.00 223.65 ? 3495 THR A N     1 
ATOM   12732 C CA    . THR A 1 3495 ? 142.987 105.993 140.347 1.00 223.65 ? 3495 THR A CA    1 
ATOM   12733 C C     . THR A 1 3495 ? 142.728 107.425 139.894 1.00 223.65 ? 3495 THR A C     1 
ATOM   12734 O O     . THR A 1 3495 ? 142.830 108.353 140.702 1.00 223.65 ? 3495 THR A O     1 
ATOM   12735 C CB    . THR A 1 3495 ? 144.483 105.672 140.294 1.00 223.65 ? 3495 THR A CB    1 
ATOM   12736 O OG1   . THR A 1 3495 ? 145.205 106.658 141.043 1.00 223.65 ? 3495 THR A OG1   1 
ATOM   12737 C CG2   . THR A 1 3495 ? 144.994 105.670 138.872 1.00 223.65 ? 3495 THR A CG2   1 
ATOM   12738 N N     . PHE A 1 3496 ? 142.369 107.626 138.623 1.00 208.26 ? 3496 PHE A N     1 
ATOM   12739 C CA    . PHE A 1 3496 ? 141.934 108.948 138.185 1.00 208.26 ? 3496 PHE A CA    1 
ATOM   12740 C C     . PHE A 1 3496 ? 140.641 109.351 138.879 1.00 208.26 ? 3496 PHE A C     1 
ATOM   12741 O O     . PHE A 1 3496 ? 140.471 110.512 139.275 1.00 208.26 ? 3496 PHE A O     1 
ATOM   12742 C CB    . PHE A 1 3496 ? 141.762 108.967 136.668 1.00 208.26 ? 3496 PHE A CB    1 
ATOM   12743 C CG    . PHE A 1 3496 ? 142.929 109.552 135.938 1.00 208.26 ? 3496 PHE A CG    1 
ATOM   12744 C CD1   . PHE A 1 3496 ? 144.217 109.362 136.404 1.00 208.26 ? 3496 PHE A CD1   1 
ATOM   12745 C CD2   . PHE A 1 3496 ? 142.741 110.293 134.787 1.00 208.26 ? 3496 PHE A CD2   1 
ATOM   12746 C CE1   . PHE A 1 3496 ? 145.294 109.900 135.735 1.00 208.26 ? 3496 PHE A CE1   1 
ATOM   12747 C CE2   . PHE A 1 3496 ? 143.813 110.832 134.115 1.00 208.26 ? 3496 PHE A CE2   1 
ATOM   12748 C CZ    . PHE A 1 3496 ? 145.092 110.637 134.589 1.00 208.26 ? 3496 PHE A CZ    1 
ATOM   12749 N N     . LYS A 1 3497 ? 139.714 108.404 139.034 1.00 194.93 ? 3497 LYS A N     1 
ATOM   12750 C CA    . LYS A 1 3497 ? 138.497 108.685 139.787 1.00 194.93 ? 3497 LYS A CA    1 
ATOM   12751 C C     . LYS A 1 3497 ? 138.826 109.051 141.228 1.00 194.93 ? 3497 LYS A C     1 
ATOM   12752 O O     . LYS A 1 3497 ? 138.226 109.969 141.797 1.00 194.93 ? 3497 LYS A O     1 
ATOM   12753 C CB    . LYS A 1 3497 ? 137.551 107.482 139.730 1.00 194.93 ? 3497 LYS A CB    1 
ATOM   12754 C CG    . LYS A 1 3497 ? 136.249 107.645 140.517 1.00 194.93 ? 3497 LYS A CG    1 
ATOM   12755 C CD    . LYS A 1 3497 ? 136.352 107.115 141.944 1.00 194.93 ? 3497 LYS A CD    1 
ATOM   12756 C CE    . LYS A 1 3497 ? 135.080 107.396 142.727 1.00 194.93 ? 3497 LYS A CE    1 
ATOM   12757 N NZ    . LYS A 1 3497 ? 135.339 107.492 144.190 1.00 194.93 ? 3497 LYS A NZ    1 
ATOM   12758 N N     . ASN A 1 3498 ? 139.774 108.338 141.837 1.00 185.84 ? 3498 ASN A N     1 
ATOM   12759 C CA    . ASN A 1 3498 ? 140.175 108.666 143.205 1.00 185.84 ? 3498 ASN A CA    1 
ATOM   12760 C C     . ASN A 1 3498 ? 140.768 110.071 143.282 1.00 185.84 ? 3498 ASN A C     1 
ATOM   12761 O O     . ASN A 1 3498 ? 140.456 110.847 144.197 1.00 185.84 ? 3498 ASN A O     1 
ATOM   12762 C CB    . ASN A 1 3498 ? 141.175 107.632 143.719 1.00 185.84 ? 3498 ASN A CB    1 
ATOM   12763 C CG    . ASN A 1 3498 ? 140.512 106.525 144.507 1.00 185.84 ? 3498 ASN A CG    1 
ATOM   12764 O OD1   . ASN A 1 3498 ? 139.346 106.203 144.285 1.00 185.84 ? 3498 ASN A OD1   1 
ATOM   12765 N ND2   . ASN A 1 3498 ? 141.254 105.933 145.435 1.00 185.84 ? 3498 ASN A ND2   1 
ATOM   12766 N N     . GLN A 1 3499 ? 141.623 110.415 142.318 1.00 178.03 ? 3499 GLN A N     1 
ATOM   12767 C CA    . GLN A 1 3499 ? 142.227 111.742 142.291 1.00 178.03 ? 3499 GLN A CA    1 
ATOM   12768 C C     . GLN A 1 3499 ? 141.164 112.823 142.146 1.00 178.03 ? 3499 GLN A C     1 
ATOM   12769 O O     . GLN A 1 3499 ? 141.251 113.882 142.778 1.00 178.03 ? 3499 GLN A O     1 
ATOM   12770 C CB    . GLN A 1 3499 ? 143.249 111.822 141.155 1.00 178.03 ? 3499 GLN A CB    1 
ATOM   12771 C CG    . GLN A 1 3499 ? 143.567 113.227 140.689 1.00 178.03 ? 3499 GLN A CG    1 
ATOM   12772 C CD    . GLN A 1 3499 ? 144.842 113.291 139.876 1.00 178.03 ? 3499 GLN A CD    1 
ATOM   12773 O OE1   . GLN A 1 3499 ? 145.584 112.314 139.790 1.00 178.03 ? 3499 GLN A OE1   1 
ATOM   12774 N NE2   . GLN A 1 3499 ? 145.106 114.446 139.278 1.00 178.03 ? 3499 GLN A NE2   1 
ATOM   12775 N N     . MET A 1 3500 ? 140.148 112.571 141.319 1.00 170.98 ? 3500 MET A N     1 
ATOM   12776 C CA    . MET A 1 3500 ? 139.012 113.485 141.248 1.00 170.98 ? 3500 MET A CA    1 
ATOM   12777 C C     . MET A 1 3500 ? 138.315 113.578 142.598 1.00 170.98 ? 3500 MET A C     1 
ATOM   12778 O O     . MET A 1 3500 ? 137.908 114.664 143.023 1.00 170.98 ? 3500 MET A O     1 
ATOM   12779 C CB    . MET A 1 3500 ? 138.043 113.025 140.155 1.00 170.98 ? 3500 MET A CB    1 
ATOM   12780 C CG    . MET A 1 3500 ? 136.835 113.930 139.871 1.00 170.98 ? 3500 MET A CG    1 
ATOM   12781 S SD    . MET A 1 3500 ? 135.545 114.036 141.130 1.00 170.98 ? 3500 MET A SD    1 
ATOM   12782 C CE    . MET A 1 3500 ? 134.425 112.752 140.578 1.00 170.98 ? 3500 MET A CE    1 
ATOM   12783 N N     . SER A 1 3501 ? 138.171 112.444 143.286 1.00 163.97 ? 3501 SER A N     1 
ATOM   12784 C CA    . SER A 1 3501 ? 137.516 112.442 144.590 1.00 163.97 ? 3501 SER A CA    1 
ATOM   12785 C C     . SER A 1 3501 ? 138.260 113.309 145.593 1.00 163.97 ? 3501 SER A C     1 
ATOM   12786 O O     . SER A 1 3501 ? 137.635 113.922 146.465 1.00 163.97 ? 3501 SER A O     1 
ATOM   12787 C CB    . SER A 1 3501 ? 137.391 111.014 145.119 1.00 163.97 ? 3501 SER A CB    1 
ATOM   12788 O OG    . SER A 1 3501 ? 138.616 110.571 145.675 1.00 163.97 ? 3501 SER A OG    1 
ATOM   12789 N N     . THR A 1 3502 ? 139.586 113.377 145.495 1.00 144.20 ? 3502 THR A N     1 
ATOM   12790 C CA    . THR A 1 3502 ? 140.372 114.239 146.380 1.00 144.20 ? 3502 THR A CA    1 
ATOM   12791 C C     . THR A 1 3502 ? 141.150 115.258 145.545 1.00 144.20 ? 3502 THR A C     1 
ATOM   12792 O O     . THR A 1 3502 ? 142.323 115.065 145.220 1.00 144.20 ? 3502 THR A O     1 
ATOM   12793 C CB    . THR A 1 3502 ? 141.305 113.393 147.288 1.00 144.20 ? 3502 THR A CB    1 
ATOM   12794 O OG1   . THR A 1 3502 ? 142.221 114.254 147.974 1.00 144.20 ? 3502 THR A OG1   1 
ATOM   12795 C CG2   . THR A 1 3502 ? 142.065 112.338 146.491 1.00 144.20 ? 3502 THR A CG2   1 
ATOM   12796 N N     . ILE A 1 3503 ? 140.486 116.362 145.205 1.00 126.34 ? 3503 ILE A N     1 
ATOM   12797 C CA    . ILE A 1 3503 ? 141.148 117.479 144.540 1.00 126.34 ? 3503 ILE A CA    1 
ATOM   12798 C C     . ILE A 1 3503 ? 140.855 118.782 145.275 1.00 126.34 ? 3503 ILE A C     1 
ATOM   12799 O O     . ILE A 1 3503 ? 141.756 119.601 145.487 1.00 126.34 ? 3503 ILE A O     1 
ATOM   12800 C CB    . ILE A 1 3503 ? 140.749 117.573 143.055 1.00 126.34 ? 3503 ILE A CB    1 
ATOM   12801 C CG1   . ILE A 1 3503 ? 141.353 118.829 142.422 1.00 126.34 ? 3503 ILE A CG1   1 
ATOM   12802 C CG2   . ILE A 1 3503 ? 139.241 117.548 142.890 1.00 126.34 ? 3503 ILE A CG2   1 
ATOM   12803 C CD1   . ILE A 1 3503 ? 141.591 118.713 140.939 1.00 126.34 ? 3503 ILE A CD1   1 
ATOM   12804 N N     . ALA A 1 3504 ? 139.594 118.982 145.668 1.00 110.69 ? 3504 ALA A N     1 
ATOM   12805 C CA    . ALA A 1 3504 ? 139.161 120.288 146.156 1.00 110.69 ? 3504 ALA A CA    1 
ATOM   12806 C C     . ALA A 1 3504 ? 139.944 120.719 147.388 1.00 110.69 ? 3504 ALA A C     1 
ATOM   12807 O O     . ALA A 1 3504 ? 140.395 121.867 147.474 1.00 110.69 ? 3504 ALA A O     1 
ATOM   12808 C CB    . ALA A 1 3504 ? 137.665 120.262 146.458 1.00 110.69 ? 3504 ALA A CB    1 
ATOM   12809 N N     . GLY A 1 3505 ? 140.120 119.814 148.349 1.00 113.86 ? 3505 GLY A N     1 
ATOM   12810 C CA    . GLY A 1 3505 ? 140.864 120.167 149.545 1.00 113.86 ? 3505 GLY A CA    1 
ATOM   12811 C C     . GLY A 1 3505 ? 142.307 120.520 149.246 1.00 113.86 ? 3505 GLY A C     1 
ATOM   12812 O O     . GLY A 1 3505 ? 142.868 121.445 149.839 1.00 113.86 ? 3505 GLY A O     1 
ATOM   12813 N N     . ASP A 1 3506 ? 142.928 119.787 148.321 1.00 118.82 ? 3506 ASP A N     1 
ATOM   12814 C CA    . ASP A 1 3506 ? 144.315 120.064 147.966 1.00 118.82 ? 3506 ASP A CA    1 
ATOM   12815 C C     . ASP A 1 3506 ? 144.452 121.421 147.289 1.00 118.82 ? 3506 ASP A C     1 
ATOM   12816 O O     . ASP A 1 3506 ? 145.384 122.181 147.583 1.00 118.82 ? 3506 ASP A O     1 
ATOM   12817 C CB    . ASP A 1 3506 ? 144.846 118.950 147.070 1.00 118.82 ? 3506 ASP A CB    1 
ATOM   12818 C CG    . ASP A 1 3506 ? 144.372 117.582 147.513 1.00 118.82 ? 3506 ASP A CG    1 
ATOM   12819 O OD1   . ASP A 1 3506 ? 144.904 117.068 148.517 1.00 118.82 ? 3506 ASP A OD1   1 
ATOM   12820 O OD2   . ASP A 1 3506 ? 143.463 117.025 146.863 1.00 118.82 ? 3506 ASP A OD2   1 
ATOM   12821 N N     . CYS A 1 3507 ? 143.531 121.745 146.382 1.00 113.68 ? 3507 CYS A N     1 
ATOM   12822 C CA    . CYS A 1 3507 ? 143.552 123.061 145.758 1.00 113.68 ? 3507 CYS A CA    1 
ATOM   12823 C C     . CYS A 1 3507 ? 143.345 124.154 146.795 1.00 113.68 ? 3507 CYS A C     1 
ATOM   12824 O O     . CYS A 1 3507 ? 143.995 125.203 146.739 1.00 113.68 ? 3507 CYS A O     1 
ATOM   12825 C CB    . CYS A 1 3507 ? 142.490 123.143 144.664 1.00 113.68 ? 3507 CYS A CB    1 
ATOM   12826 S SG    . CYS A 1 3507 ? 142.840 122.118 143.220 1.00 113.68 ? 3507 CYS A SG    1 
ATOM   12827 N N     . LEU A 1 3508 ? 142.446 123.923 147.753 1.00 103.18 ? 3508 LEU A N     1 
ATOM   12828 C CA    . LEU A 1 3508 ? 142.225 124.899 148.815 1.00 103.18 ? 3508 LEU A CA    1 
ATOM   12829 C C     . LEU A 1 3508 ? 143.492 125.125 149.625 1.00 103.18 ? 3508 LEU A C     1 
ATOM   12830 O O     . LEU A 1 3508 ? 143.851 126.266 149.933 1.00 103.18 ? 3508 LEU A O     1 
ATOM   12831 C CB    . LEU A 1 3508 ? 141.087 124.431 149.720 1.00 103.18 ? 3508 LEU A CB    1 
ATOM   12832 C CG    . LEU A 1 3508 ? 140.328 125.493 150.511 1.00 103.18 ? 3508 LEU A CG    1 
ATOM   12833 C CD1   . LEU A 1 3508 ? 138.949 124.977 150.846 1.00 103.18 ? 3508 LEU A CD1   1 
ATOM   12834 C CD2   . LEU A 1 3508 ? 141.071 125.855 151.779 1.00 103.18 ? 3508 LEU A CD2   1 
ATOM   12835 N N     . LEU A 1 3509 ? 144.178 124.042 149.993 1.00 99.88  ? 3509 LEU A N     1 
ATOM   12836 C CA    . LEU A 1 3509 ? 145.400 124.181 150.776 1.00 99.88  ? 3509 LEU A CA    1 
ATOM   12837 C C     . LEU A 1 3509 ? 146.472 124.921 149.991 1.00 99.88  ? 3509 LEU A C     1 
ATOM   12838 O O     . LEU A 1 3509 ? 147.148 125.807 150.530 1.00 99.88  ? 3509 LEU A O     1 
ATOM   12839 C CB    . LEU A 1 3509 ? 145.901 122.807 151.215 1.00 99.88  ? 3509 LEU A CB    1 
ATOM   12840 C CG    . LEU A 1 3509 ? 145.017 122.090 152.236 1.00 99.88  ? 3509 LEU A CG    1 
ATOM   12841 C CD1   . LEU A 1 3509 ? 145.775 120.966 152.912 1.00 99.88  ? 3509 LEU A CD1   1 
ATOM   12842 C CD2   . LEU A 1 3509 ? 144.493 123.070 153.264 1.00 99.88  ? 3509 LEU A CD2   1 
ATOM   12843 N N     . SER A 1 3510 ? 146.630 124.586 148.710 1.00 100.96 ? 3510 SER A N     1 
ATOM   12844 C CA    . SER A 1 3510 ? 147.631 125.268 147.897 1.00 100.96 ? 3510 SER A CA    1 
ATOM   12845 C C     . SER A 1 3510 ? 147.310 126.748 147.758 1.00 100.96 ? 3510 SER A C     1 
ATOM   12846 O O     . SER A 1 3510 ? 148.206 127.594 147.840 1.00 100.96 ? 3510 SER A O     1 
ATOM   12847 C CB    . SER A 1 3510 ? 147.731 124.615 146.523 1.00 100.96 ? 3510 SER A CB    1 
ATOM   12848 O OG    . SER A 1 3510 ? 146.453 124.213 146.072 1.00 100.96 ? 3510 SER A OG    1 
ATOM   12849 N N     . ALA A 1 3511 ? 146.036 127.085 147.546 1.00 95.49  ? 3511 ALA A N     1 
ATOM   12850 C CA    . ALA A 1 3511 ? 145.661 128.488 147.417 1.00 95.49  ? 3511 ALA A CA    1 
ATOM   12851 C C     . ALA A 1 3511 ? 145.886 129.243 148.718 1.00 95.49  ? 3511 ALA A C     1 
ATOM   12852 O O     . ALA A 1 3511 ? 146.391 130.372 148.711 1.00 95.49  ? 3511 ALA A O     1 
ATOM   12853 C CB    . ALA A 1 3511 ? 144.204 128.603 146.978 1.00 95.49  ? 3511 ALA A CB    1 
ATOM   12854 N N     . ALA A 1 3512 ? 145.519 128.637 149.847 1.00 94.41  ? 3512 ALA A N     1 
ATOM   12855 C CA    . ALA A 1 3512 ? 145.730 129.293 151.129 1.00 94.41  ? 3512 ALA A CA    1 
ATOM   12856 C C     . ALA A 1 3512 ? 147.209 129.532 151.376 1.00 94.41  ? 3512 ALA A C     1 
ATOM   12857 O O     . ALA A 1 3512 ? 147.597 130.577 151.909 1.00 94.41  ? 3512 ALA A O     1 
ATOM   12858 C CB    . ALA A 1 3512 ? 145.123 128.460 152.254 1.00 94.41  ? 3512 ALA A CB    1 
ATOM   12859 N N     . PHE A 1 3513 ? 148.052 128.575 150.994 1.00 96.38  ? 3513 PHE A N     1 
ATOM   12860 C CA    . PHE A 1 3513 ? 149.488 128.778 151.132 1.00 96.38  ? 3513 PHE A CA    1 
ATOM   12861 C C     . PHE A 1 3513 ? 149.981 129.881 150.204 1.00 96.38  ? 3513 PHE A C     1 
ATOM   12862 O O     . PHE A 1 3513 ? 150.819 130.699 150.597 1.00 96.38  ? 3513 PHE A O     1 
ATOM   12863 C CB    . PHE A 1 3513 ? 150.217 127.452 150.889 1.00 96.38  ? 3513 PHE A CB    1 
ATOM   12864 C CG    . PHE A 1 3513 ? 151.691 127.585 150.588 1.00 96.38  ? 3513 PHE A CG    1 
ATOM   12865 C CD1   . PHE A 1 3513 ? 152.145 128.064 149.367 1.00 96.38  ? 3513 PHE A CD1   1 
ATOM   12866 C CD2   . PHE A 1 3513 ? 152.623 127.237 151.544 1.00 96.38  ? 3513 PHE A CD2   1 
ATOM   12867 C CE1   . PHE A 1 3513 ? 153.488 128.180 149.110 1.00 96.38  ? 3513 PHE A CE1   1 
ATOM   12868 C CE2   . PHE A 1 3513 ? 153.970 127.352 151.288 1.00 96.38  ? 3513 PHE A CE2   1 
ATOM   12869 C CZ    . PHE A 1 3513 ? 154.401 127.826 150.069 1.00 96.38  ? 3513 PHE A CZ    1 
ATOM   12870 N N     . ILE A 1 3514 ? 149.484 129.918 148.967 1.00 92.96  ? 3514 ILE A N     1 
ATOM   12871 C CA    . ILE A 1 3514 ? 150.034 130.845 147.985 1.00 92.96  ? 3514 ILE A CA    1 
ATOM   12872 C C     . ILE A 1 3514 ? 149.535 132.268 148.187 1.00 92.96  ? 3514 ILE A C     1 
ATOM   12873 O O     . ILE A 1 3514 ? 150.162 133.210 147.690 1.00 92.96  ? 3514 ILE A O     1 
ATOM   12874 C CB    . ILE A 1 3514 ? 149.720 130.378 146.555 1.00 92.96  ? 3514 ILE A CB    1 
ATOM   12875 C CG1   . ILE A 1 3514 ? 150.726 130.963 145.569 1.00 92.96  ? 3514 ILE A CG1   1 
ATOM   12876 C CG2   . ILE A 1 3514 ? 148.322 130.787 146.149 1.00 92.96  ? 3514 ILE A CG2   1 
ATOM   12877 C CD1   . ILE A 1 3514 ? 150.628 130.367 144.191 1.00 92.96  ? 3514 ILE A CD1   1 
ATOM   12878 N N     . ALA A 1 3515 ? 148.428 132.458 148.899 1.00 85.53  ? 3515 ALA A N     1 
ATOM   12879 C CA    . ALA A 1 3515 ? 147.897 133.794 149.129 1.00 85.53  ? 3515 ALA A CA    1 
ATOM   12880 C C     . ALA A 1 3515 ? 148.164 134.297 150.539 1.00 85.53  ? 3515 ALA A C     1 
ATOM   12881 O O     . ALA A 1 3515 ? 148.698 135.394 150.717 1.00 85.53  ? 3515 ALA A O     1 
ATOM   12882 C CB    . ALA A 1 3515 ? 146.392 133.821 148.847 1.00 85.53  ? 3515 ALA A CB    1 
ATOM   12883 N N     . TYR A 1 3516 ? 147.809 133.509 151.551 1.00 86.53  ? 3516 TYR A N     1 
ATOM   12884 C CA    . TYR A 1 3516 ? 147.955 133.966 152.926 1.00 86.53  ? 3516 TYR A CA    1 
ATOM   12885 C C     . TYR A 1 3516 ? 149.385 133.806 153.423 1.00 86.53  ? 3516 TYR A C     1 
ATOM   12886 O O     . TYR A 1 3516 ? 149.965 134.744 153.979 1.00 86.53  ? 3516 TYR A O     1 
ATOM   12887 C CB    . TYR A 1 3516 ? 146.998 133.198 153.835 1.00 86.53  ? 3516 TYR A CB    1 
ATOM   12888 C CG    . TYR A 1 3516 ? 145.613 133.782 153.918 1.00 86.53  ? 3516 TYR A CG    1 
ATOM   12889 C CD1   . TYR A 1 3516 ? 145.423 135.134 154.132 1.00 86.53  ? 3516 TYR A CD1   1 
ATOM   12890 C CD2   . TYR A 1 3516 ? 144.496 132.974 153.805 1.00 86.53  ? 3516 TYR A CD2   1 
ATOM   12891 C CE1   . TYR A 1 3516 ? 144.157 135.669 154.218 1.00 86.53  ? 3516 TYR A CE1   1 
ATOM   12892 C CE2   . TYR A 1 3516 ? 143.227 133.497 153.890 1.00 86.53  ? 3516 TYR A CE2   1 
ATOM   12893 C CZ    . TYR A 1 3516 ? 143.062 134.846 154.097 1.00 86.53  ? 3516 TYR A CZ    1 
ATOM   12894 O OH    . TYR A 1 3516 ? 141.797 135.375 154.182 1.00 86.53  ? 3516 TYR A OH    1 
ATOM   12895 N N     . ALA A 1 3517 ? 149.975 132.629 153.222 1.00 87.93  ? 3517 ALA A N     1 
ATOM   12896 C CA    . ALA A 1 3517 ? 151.255 132.288 153.839 1.00 87.93  ? 3517 ALA A CA    1 
ATOM   12897 C C     . ALA A 1 3517 ? 152.410 132.992 153.127 1.00 87.93  ? 3517 ALA A C     1 
ATOM   12898 O O     . ALA A 1 3517 ? 153.316 132.376 152.571 1.00 87.93  ? 3517 ALA A O     1 
ATOM   12899 C CB    . ALA A 1 3517 ? 151.450 130.779 153.847 1.00 87.93  ? 3517 ALA A CB    1 
ATOM   12900 N N     . GLY A 1 3518 ? 152.359 134.317 153.158 1.00 100.06 ? 3518 GLY A N     1 
ATOM   12901 C CA    . GLY A 1 3518 ? 153.450 135.127 152.661 1.00 100.06 ? 3518 GLY A CA    1 
ATOM   12902 C C     . GLY A 1 3518 ? 154.172 135.808 153.803 1.00 100.06 ? 3518 GLY A C     1 
ATOM   12903 O O     . GLY A 1 3518 ? 153.607 135.955 154.890 1.00 100.06 ? 3518 GLY A O     1 
ATOM   12904 N N     . TYR A 1 3519 ? 155.439 136.164 153.589 1.00 109.73 ? 3519 TYR A N     1 
ATOM   12905 C CA    . TYR A 1 3519 ? 156.238 136.915 154.553 1.00 109.73 ? 3519 TYR A CA    1 
ATOM   12906 C C     . TYR A 1 3519 ? 156.598 136.057 155.761 1.00 109.73 ? 3519 TYR A C     1 
ATOM   12907 O O     . TYR A 1 3519 ? 157.448 136.441 156.570 1.00 109.73 ? 3519 TYR A O     1 
ATOM   12908 C CB    . TYR A 1 3519 ? 155.498 138.184 154.997 1.00 109.73 ? 3519 TYR A CB    1 
ATOM   12909 C CG    . TYR A 1 3519 ? 156.147 138.935 156.133 1.00 109.73 ? 3519 TYR A CG    1 
ATOM   12910 C CD1   . TYR A 1 3519 ? 157.210 139.793 155.903 1.00 109.73 ? 3519 TYR A CD1   1 
ATOM   12911 C CD2   . TYR A 1 3519 ? 155.703 138.779 157.438 1.00 109.73 ? 3519 TYR A CD2   1 
ATOM   12912 C CE1   . TYR A 1 3519 ? 157.809 140.480 156.937 1.00 109.73 ? 3519 TYR A CE1   1 
ATOM   12913 C CE2   . TYR A 1 3519 ? 156.297 139.459 158.480 1.00 109.73 ? 3519 TYR A CE2   1 
ATOM   12914 C CZ    . TYR A 1 3519 ? 157.350 140.309 158.223 1.00 109.73 ? 3519 TYR A CZ    1 
ATOM   12915 O OH    . TYR A 1 3519 ? 157.947 140.995 159.256 1.00 109.73 ? 3519 TYR A OH    1 
ATOM   12916 N N     . PHE A 1 3520 ? 156.009 134.875 155.867 1.00 100.67 ? 3520 PHE A N     1 
ATOM   12917 C CA    . PHE A 1 3520 ? 156.222 134.033 157.030 1.00 100.67 ? 3520 PHE A CA    1 
ATOM   12918 C C     . PHE A 1 3520 ? 157.427 133.127 156.827 1.00 100.67 ? 3520 PHE A C     1 
ATOM   12919 O O     . PHE A 1 3520 ? 157.737 132.710 155.709 1.00 100.67 ? 3520 PHE A O     1 
ATOM   12920 C CB    . PHE A 1 3520 ? 154.978 133.197 157.325 1.00 100.67 ? 3520 PHE A CB    1 
ATOM   12921 C CG    . PHE A 1 3520 ? 153.841 133.987 157.901 1.00 100.67 ? 3520 PHE A CG    1 
ATOM   12922 C CD1   . PHE A 1 3520 ? 153.966 134.604 159.131 1.00 100.67 ? 3520 PHE A CD1   1 
ATOM   12923 C CD2   . PHE A 1 3520 ? 152.648 134.109 157.217 1.00 100.67 ? 3520 PHE A CD2   1 
ATOM   12924 C CE1   . PHE A 1 3520 ? 152.922 135.329 159.665 1.00 100.67 ? 3520 PHE A CE1   1 
ATOM   12925 C CE2   . PHE A 1 3520 ? 151.601 134.834 157.749 1.00 100.67 ? 3520 PHE A CE2   1 
ATOM   12926 C CZ    . PHE A 1 3520 ? 151.739 135.444 158.973 1.00 100.67 ? 3520 PHE A CZ    1 
ATOM   12927 N N     . ASP A 1 3521 ? 158.107 132.829 157.930 1.00 109.64 ? 3521 ASP A N     1 
ATOM   12928 C CA    . ASP A 1 3521 ? 159.257 131.944 157.901 1.00 109.64 ? 3521 ASP A CA    1 
ATOM   12929 C C     . ASP A 1 3521 ? 158.828 130.520 157.550 1.00 109.64 ? 3521 ASP A C     1 
ATOM   12930 O O     . ASP A 1 3521 ? 157.640 130.198 157.468 1.00 109.64 ? 3521 ASP A O     1 
ATOM   12931 C CB    . ASP A 1 3521 ? 159.974 131.965 159.248 1.00 109.64 ? 3521 ASP A CB    1 
ATOM   12932 C CG    . ASP A 1 3521 ? 159.009 131.950 160.417 1.00 109.64 ? 3521 ASP A CG    1 
ATOM   12933 O OD1   . ASP A 1 3521 ? 158.155 132.858 160.492 1.00 109.64 ? 3521 ASP A OD1   1 
ATOM   12934 O OD2   . ASP A 1 3521 ? 159.097 131.029 161.255 1.00 109.64 ? 3521 ASP A OD2   1 
ATOM   12935 N N     . GLN A 1 3522 ? 159.824 129.657 157.343 1.00 107.16 ? 3522 GLN A N     1 
ATOM   12936 C CA    . GLN A 1 3522 ? 159.531 128.275 156.984 1.00 107.16 ? 3522 GLN A CA    1 
ATOM   12937 C C     . GLN A 1 3522 ? 158.761 127.566 158.091 1.00 107.16 ? 3522 GLN A C     1 
ATOM   12938 O O     . GLN A 1 3522 ? 157.792 126.845 157.820 1.00 107.16 ? 3522 GLN A O     1 
ATOM   12939 C CB    . GLN A 1 3522 ? 160.827 127.534 156.666 1.00 107.16 ? 3522 GLN A CB    1 
ATOM   12940 C CG    . GLN A 1 3522 ? 160.631 126.075 156.316 1.00 107.16 ? 3522 GLN A CG    1 
ATOM   12941 C CD    . GLN A 1 3522 ? 161.472 125.649 155.132 1.00 107.16 ? 3522 GLN A CD    1 
ATOM   12942 O OE1   . GLN A 1 3522 ? 161.732 126.438 154.226 1.00 107.16 ? 3522 GLN A OE1   1 
ATOM   12943 N NE2   . GLN A 1 3522 ? 161.906 124.395 155.137 1.00 107.16 ? 3522 GLN A NE2   1 
ATOM   12944 N N     . GLN A 1 3523 ? 159.168 127.765 159.346 1.00 106.75 ? 3523 GLN A N     1 
ATOM   12945 C CA    . GLN A 1 3523 ? 158.470 127.122 160.454 1.00 106.75 ? 3523 GLN A CA    1 
ATOM   12946 C C     . GLN A 1 3523 ? 157.038 127.622 160.568 1.00 106.75 ? 3523 GLN A C     1 
ATOM   12947 O O     . GLN A 1 3523 ? 156.118 126.838 160.826 1.00 106.75 ? 3523 GLN A O     1 
ATOM   12948 C CB    . GLN A 1 3523 ? 159.218 127.355 161.763 1.00 106.75 ? 3523 GLN A CB    1 
ATOM   12949 C CG    . GLN A 1 3523 ? 158.883 126.338 162.837 1.00 106.75 ? 3523 GLN A CG    1 
ATOM   12950 C CD    . GLN A 1 3523 ? 159.062 126.887 164.237 1.00 106.75 ? 3523 GLN A CD    1 
ATOM   12951 O OE1   . GLN A 1 3523 ? 158.210 127.615 164.744 1.00 106.75 ? 3523 GLN A OE1   1 
ATOM   12952 N NE2   . GLN A 1 3523 ? 160.175 126.537 164.872 1.00 106.75 ? 3523 GLN A NE2   1 
ATOM   12953 N N     . MET A 1 3524 ? 156.829 128.928 160.391 1.00 103.98 ? 3524 MET A N     1 
ATOM   12954 C CA    . MET A 1 3524 ? 155.475 129.466 160.445 1.00 103.98 ? 3524 MET A CA    1 
ATOM   12955 C C     . MET A 1 3524 ? 154.617 128.909 159.318 1.00 103.98 ? 3524 MET A C     1 
ATOM   12956 O O     . MET A 1 3524 ? 153.447 128.568 159.529 1.00 103.98 ? 3524 MET A O     1 
ATOM   12957 C CB    . MET A 1 3524 ? 155.512 130.990 160.391 1.00 103.98 ? 3524 MET A CB    1 
ATOM   12958 C CG    . MET A 1 3524 ? 154.436 131.659 161.223 1.00 103.98 ? 3524 MET A CG    1 
ATOM   12959 S SD    . MET A 1 3524 ? 154.504 131.194 162.961 1.00 103.98 ? 3524 MET A SD    1 
ATOM   12960 C CE    . MET A 1 3524 ? 153.086 130.108 163.081 1.00 103.98 ? 3524 MET A CE    1 
ATOM   12961 N N     . ARG A 1 3525 ? 155.183 128.806 158.113 1.00 100.83 ? 3525 ARG A N     1 
ATOM   12962 C CA    . ARG A 1 3525 ? 154.444 128.213 157.004 1.00 100.83 ? 3525 ARG A CA    1 
ATOM   12963 C C     . ARG A 1 3525 ? 154.053 126.779 157.319 1.00 100.83 ? 3525 ARG A C     1 
ATOM   12964 O O     . ARG A 1 3525 ? 152.915 126.368 157.068 1.00 100.83 ? 3525 ARG A O     1 
ATOM   12965 C CB    . ARG A 1 3525 ? 155.276 128.256 155.726 1.00 100.83 ? 3525 ARG A CB    1 
ATOM   12966 C CG    . ARG A 1 3525 ? 155.427 129.623 155.109 1.00 100.83 ? 3525 ARG A CG    1 
ATOM   12967 C CD    . ARG A 1 3525 ? 156.316 129.541 153.887 1.00 100.83 ? 3525 ARG A CD    1 
ATOM   12968 N NE    . ARG A 1 3525 ? 156.928 130.822 153.562 1.00 100.83 ? 3525 ARG A NE    1 
ATOM   12969 C CZ    . ARG A 1 3525 ? 157.672 131.038 152.487 1.00 100.83 ? 3525 ARG A CZ    1 
ATOM   12970 N NH1   . ARG A 1 3525 ? 157.920 130.076 151.614 1.00 100.83 ? 3525 ARG A NH1   1 
ATOM   12971 N NH2   . ARG A 1 3525 ? 158.182 132.249 152.283 1.00 100.83 ? 3525 ARG A NH2   1 
ATOM   12972 N N     . GLN A 1 3526 ? 154.986 126.001 157.869 1.00 102.28 ? 3526 GLN A N     1 
ATOM   12973 C CA    . GLN A 1 3526 ? 154.680 124.612 158.184 1.00 102.28 ? 3526 GLN A CA    1 
ATOM   12974 C C     . GLN A 1 3526 ? 153.610 124.517 159.261 1.00 102.28 ? 3526 GLN A C     1 
ATOM   12975 O O     . GLN A 1 3526 ? 152.719 123.665 159.184 1.00 102.28 ? 3526 GLN A O     1 
ATOM   12976 C CB    . GLN A 1 3526 ? 155.942 123.873 158.616 1.00 102.28 ? 3526 GLN A CB    1 
ATOM   12977 C CG    . GLN A 1 3526 ? 155.747 122.374 158.702 1.00 102.28 ? 3526 GLN A CG    1 
ATOM   12978 C CD    . GLN A 1 3526 ? 154.970 121.830 157.521 1.00 102.28 ? 3526 GLN A CD    1 
ATOM   12979 O OE1   . GLN A 1 3526 ? 155.362 122.012 156.369 1.00 102.28 ? 3526 GLN A OE1   1 
ATOM   12980 N NE2   . GLN A 1 3526 ? 153.860 121.160 157.801 1.00 102.28 ? 3526 GLN A NE2   1 
ATOM   12981 N N     . ASN A 1 3527 ? 153.681 125.381 160.274 1.00 98.51  ? 3527 ASN A N     1 
ATOM   12982 C CA    . ASN A 1 3527 ? 152.672 125.367 161.327 1.00 98.51  ? 3527 ASN A CA    1 
ATOM   12983 C C     . ASN A 1 3527 ? 151.295 125.698 160.765 1.00 98.51  ? 3527 ASN A C     1 
ATOM   12984 O O     . ASN A 1 3527 ? 150.301 125.040 161.099 1.00 98.51  ? 3527 ASN A O     1 
ATOM   12985 C CB    . ASN A 1 3527 ? 153.069 126.349 162.430 1.00 98.51  ? 3527 ASN A CB    1 
ATOM   12986 C CG    . ASN A 1 3527 ? 152.127 126.318 163.621 1.00 98.51  ? 3527 ASN A CG    1 
ATOM   12987 O OD1   . ASN A 1 3527 ? 150.912 126.449 163.482 1.00 98.51  ? 3527 ASN A OD1   1 
ATOM   12988 N ND2   . ASN A 1 3527 ? 152.693 126.142 164.808 1.00 98.51  ? 3527 ASN A ND2   1 
ATOM   12989 N N     . LEU A 1 3528 ? 151.218 126.709 159.900 1.00 102.77 ? 3528 LEU A N     1 
ATOM   12990 C CA    . LEU A 1 3528 ? 149.934 127.073 159.312 1.00 102.77 ? 3528 LEU A CA    1 
ATOM   12991 C C     . LEU A 1 3528 ? 149.394 125.954 158.432 1.00 102.77 ? 3528 LEU A C     1 
ATOM   12992 O O     . LEU A 1 3528 ? 148.190 125.664 158.452 1.00 102.77 ? 3528 LEU A O     1 
ATOM   12993 C CB    . LEU A 1 3528 ? 150.071 128.367 158.513 1.00 102.77 ? 3528 LEU A CB    1 
ATOM   12994 C CG    . LEU A 1 3528 ? 149.775 129.683 159.233 1.00 102.77 ? 3528 LEU A CG    1 
ATOM   12995 C CD1   . LEU A 1 3528 ? 148.290 129.952 159.196 1.00 102.77 ? 3528 LEU A CD1   1 
ATOM   12996 C CD2   . LEU A 1 3528 ? 150.275 129.671 160.664 1.00 102.77 ? 3528 LEU A CD2   1 
ATOM   12997 N N     . PHE A 1 3529 ? 150.266 125.324 157.641 1.00 102.38 ? 3529 PHE A N     1 
ATOM   12998 C CA    . PHE A 1 3529 ? 149.833 124.221 156.792 1.00 102.38 ? 3529 PHE A CA    1 
ATOM   12999 C C     . PHE A 1 3529 ? 149.333 123.056 157.631 1.00 102.38 ? 3529 PHE A C     1 
ATOM   13000 O O     . PHE A 1 3529 ? 148.344 122.404 157.277 1.00 102.38 ? 3529 PHE A O     1 
ATOM   13001 C CB    . PHE A 1 3529 ? 150.982 123.781 155.889 1.00 102.38 ? 3529 PHE A CB    1 
ATOM   13002 C CG    . PHE A 1 3529 ? 150.538 123.159 154.604 1.00 102.38 ? 3529 PHE A CG    1 
ATOM   13003 C CD1   . PHE A 1 3529 ? 150.099 121.849 154.571 1.00 102.38 ? 3529 PHE A CD1   1 
ATOM   13004 C CD2   . PHE A 1 3529 ? 150.569 123.880 153.426 1.00 102.38 ? 3529 PHE A CD2   1 
ATOM   13005 C CE1   . PHE A 1 3529 ? 149.695 121.272 153.387 1.00 102.38 ? 3529 PHE A CE1   1 
ATOM   13006 C CE2   . PHE A 1 3529 ? 150.164 123.309 152.240 1.00 102.38 ? 3529 PHE A CE2   1 
ATOM   13007 C CZ    . PHE A 1 3529 ? 149.728 122.003 152.220 1.00 102.38 ? 3529 PHE A CZ    1 
ATOM   13008 N N     . THR A 1 3530 ? 150.005 122.785 158.751 1.00 106.32 ? 3530 THR A N     1 
ATOM   13009 C CA    . THR A 1 3530 ? 149.538 121.756 159.671 1.00 106.32 ? 3530 THR A CA    1 
ATOM   13010 C C     . THR A 1 3530 ? 148.165 122.107 160.223 1.00 106.32 ? 3530 THR A C     1 
ATOM   13011 O O     . THR A 1 3530 ? 147.289 121.242 160.321 1.00 106.32 ? 3530 THR A O     1 
ATOM   13012 C CB    . THR A 1 3530 ? 150.547 121.574 160.806 1.00 106.32 ? 3530 THR A CB    1 
ATOM   13013 O OG1   . THR A 1 3530 ? 151.621 120.737 160.362 1.00 106.32 ? 3530 THR A OG1   1 
ATOM   13014 C CG2   . THR A 1 3530 ? 149.890 120.938 162.019 1.00 106.32 ? 3530 THR A CG2   1 
ATOM   13015 N N     . THR A 1 3531 ? 147.956 123.375 160.578 1.00 100.37 ? 3531 THR A N     1 
ATOM   13016 C CA    . THR A 1 3531 ? 146.656 123.796 161.090 1.00 100.37 ? 3531 THR A CA    1 
ATOM   13017 C C     . THR A 1 3531 ? 145.560 123.573 160.056 1.00 100.37 ? 3531 THR A C     1 
ATOM   13018 O O     . THR A 1 3531 ? 144.499 123.010 160.360 1.00 100.37 ? 3531 THR A O     1 
ATOM   13019 C CB    . THR A 1 3531 ? 146.711 125.266 161.492 1.00 100.37 ? 3531 THR A CB    1 
ATOM   13020 O OG1   . THR A 1 3531 ? 147.986 125.553 162.078 1.00 100.37 ? 3531 THR A OG1   1 
ATOM   13021 C CG2   . THR A 1 3531 ? 145.616 125.577 162.494 1.00 100.37 ? 3531 THR A CG2   1 
ATOM   13022 N N     . TRP A 1 3532 ? 145.806 124.009 158.819 1.00 99.02  ? 3532 TRP A N     1 
ATOM   13023 C CA    . TRP A 1 3532 ? 144.802 123.864 157.770 1.00 99.02  ? 3532 TRP A CA    1 
ATOM   13024 C C     . TRP A 1 3532 ? 144.512 122.398 157.480 1.00 99.02  ? 3532 TRP A C     1 
ATOM   13025 O O     . TRP A 1 3532 ? 143.350 122.006 157.329 1.00 99.02  ? 3532 TRP A O     1 
ATOM   13026 C CB    . TRP A 1 3532 ? 145.258 124.576 156.498 1.00 99.02  ? 3532 TRP A CB    1 
ATOM   13027 C CG    . TRP A 1 3532 ? 145.544 126.026 156.683 1.00 99.02  ? 3532 TRP A CG    1 
ATOM   13028 C CD1   . TRP A 1 3532 ? 145.047 126.842 157.652 1.00 99.02  ? 3532 TRP A CD1   1 
ATOM   13029 C CD2   . TRP A 1 3532 ? 146.391 126.840 155.867 1.00 99.02  ? 3532 TRP A CD2   1 
ATOM   13030 N NE1   . TRP A 1 3532 ? 145.537 128.115 157.494 1.00 99.02  ? 3532 TRP A NE1   1 
ATOM   13031 C CE2   . TRP A 1 3532 ? 146.364 128.139 156.403 1.00 99.02  ? 3532 TRP A CE2   1 
ATOM   13032 C CE3   . TRP A 1 3532 ? 147.173 126.595 154.735 1.00 99.02  ? 3532 TRP A CE3   1 
ATOM   13033 C CZ2   . TRP A 1 3532 ? 147.088 129.188 155.847 1.00 99.02  ? 3532 TRP A CZ2   1 
ATOM   13034 C CZ3   . TRP A 1 3532 ? 147.891 127.638 154.186 1.00 99.02  ? 3532 TRP A CZ3   1 
ATOM   13035 C CH2   . TRP A 1 3532 ? 147.843 128.917 154.740 1.00 99.02  ? 3532 TRP A CH2   1 
ATOM   13036 N N     . SER A 1 3533 ? 145.556 121.569 157.398 1.00 105.25 ? 3533 SER A N     1 
ATOM   13037 C CA    . SER A 1 3533 ? 145.351 120.152 157.126 1.00 105.25 ? 3533 SER A CA    1 
ATOM   13038 C C     . SER A 1 3533 ? 144.605 119.472 158.266 1.00 105.25 ? 3533 SER A C     1 
ATOM   13039 O O     . SER A 1 3533 ? 143.757 118.605 158.029 1.00 105.25 ? 3533 SER A O     1 
ATOM   13040 C CB    . SER A 1 3533 ? 146.692 119.467 156.883 1.00 105.25 ? 3533 SER A CB    1 
ATOM   13041 O OG    . SER A 1 3533 ? 147.621 119.815 157.892 1.00 105.25 ? 3533 SER A OG    1 
ATOM   13042 N N     . HIS A 1 3534 ? 144.920 119.839 159.509 1.00 112.22 ? 3534 HIS A N     1 
ATOM   13043 C CA    . HIS A 1 3534 ? 144.226 119.257 160.650 1.00 112.22 ? 3534 HIS A CA    1 
ATOM   13044 C C     . HIS A 1 3534 ? 142.751 119.627 160.640 1.00 112.22 ? 3534 HIS A C     1 
ATOM   13045 O O     . HIS A 1 3534 ? 141.891 118.785 160.924 1.00 112.22 ? 3534 HIS A O     1 
ATOM   13046 C CB    . HIS A 1 3534 ? 144.892 119.708 161.948 1.00 112.22 ? 3534 HIS A CB    1 
ATOM   13047 C CG    . HIS A 1 3534 ? 144.083 119.420 163.174 1.00 112.22 ? 3534 HIS A CG    1 
ATOM   13048 N ND1   . HIS A 1 3534 ? 143.151 120.303 163.674 1.00 112.22 ? 3534 HIS A ND1   1 
ATOM   13049 C CD2   . HIS A 1 3534 ? 144.063 118.346 163.997 1.00 112.22 ? 3534 HIS A CD2   1 
ATOM   13050 C CE1   . HIS A 1 3534 ? 142.595 119.787 164.755 1.00 112.22 ? 3534 HIS A CE1   1 
ATOM   13051 N NE2   . HIS A 1 3534 ? 143.130 118.599 164.972 1.00 112.22 ? 3534 HIS A NE2   1 
ATOM   13052 N N     . HIS A 1 3535 ? 142.435 120.880 160.314 1.00 108.08 ? 3535 HIS A N     1 
ATOM   13053 C CA    . HIS A 1 3535 ? 141.029 121.251 160.195 1.00 108.08 ? 3535 HIS A CA    1 
ATOM   13054 C C     . HIS A 1 3535 ? 140.354 120.494 159.060 1.00 108.08 ? 3535 HIS A C     1 
ATOM   13055 O O     . HIS A 1 3535 ? 139.217 120.031 159.206 1.00 108.08 ? 3535 HIS A O     1 
ATOM   13056 C CB    . HIS A 1 3535 ? 140.887 122.753 159.984 1.00 108.08 ? 3535 HIS A CB    1 
ATOM   13057 C CG    . HIS A 1 3535 ? 139.472 123.235 160.046 1.00 108.08 ? 3535 HIS A CG    1 
ATOM   13058 N ND1   . HIS A 1 3535 ? 138.893 123.695 161.208 1.00 108.08 ? 3535 HIS A ND1   1 
ATOM   13059 C CD2   . HIS A 1 3535 ? 138.517 123.321 159.091 1.00 108.08 ? 3535 HIS A CD2   1 
ATOM   13060 C CE1   . HIS A 1 3535 ? 137.643 124.048 160.965 1.00 108.08 ? 3535 HIS A CE1   1 
ATOM   13061 N NE2   . HIS A 1 3535 ? 137.391 123.831 159.688 1.00 108.08 ? 3535 HIS A NE2   1 
ATOM   13062 N N     . LEU A 1 3536 ? 141.037 120.357 157.920 1.00 112.11 ? 3536 LEU A N     1 
ATOM   13063 C CA    . LEU A 1 3536 ? 140.433 119.683 156.775 1.00 112.11 ? 3536 LEU A CA    1 
ATOM   13064 C C     . LEU A 1 3536 ? 140.133 118.222 157.082 1.00 112.11 ? 3536 LEU A C     1 
ATOM   13065 O O     . LEU A 1 3536 ? 139.040 117.730 156.778 1.00 112.11 ? 3536 LEU A O     1 
ATOM   13066 C CB    . LEU A 1 3536 ? 141.345 119.795 155.557 1.00 112.11 ? 3536 LEU A CB    1 
ATOM   13067 C CG    . LEU A 1 3536 ? 140.850 120.769 154.490 1.00 112.11 ? 3536 LEU A CG    1 
ATOM   13068 C CD1   . LEU A 1 3536 ? 140.904 122.187 155.021 1.00 112.11 ? 3536 LEU A CD1   1 
ATOM   13069 C CD2   . LEU A 1 3536 ? 141.661 120.638 153.210 1.00 112.11 ? 3536 LEU A CD2   1 
ATOM   13070 N N     . GLN A 1 3537 ? 141.087 117.510 157.688 1.00 118.64 ? 3537 GLN A N     1 
ATOM   13071 C CA    . GLN A 1 3537 ? 140.822 116.124 158.059 1.00 118.64 ? 3537 GLN A CA    1 
ATOM   13072 C C     . GLN A 1 3537 ? 139.753 116.050 159.140 1.00 118.64 ? 3537 GLN A C     1 
ATOM   13073 O O     . GLN A 1 3537 ? 138.929 115.128 159.143 1.00 118.64 ? 3537 GLN A O     1 
ATOM   13074 C CB    . GLN A 1 3537 ? 142.104 115.428 158.516 1.00 118.64 ? 3537 GLN A CB    1 
ATOM   13075 C CG    . GLN A 1 3537 ? 142.771 116.058 159.719 1.00 118.64 ? 3537 GLN A CG    1 
ATOM   13076 C CD    . GLN A 1 3537 ? 143.466 115.043 160.599 1.00 118.64 ? 3537 GLN A CD    1 
ATOM   13077 O OE1   . GLN A 1 3537 ? 143.484 113.851 160.296 1.00 118.64 ? 3537 GLN A OE1   1 
ATOM   13078 N NE2   . GLN A 1 3537 ? 144.039 115.511 161.703 1.00 118.64 ? 3537 GLN A NE2   1 
ATOM   13079 N N     . GLN A 1 3538 ? 139.745 117.013 160.065 1.00 123.01 ? 3538 GLN A N     1 
ATOM   13080 C CA    . GLN A 1 3538 ? 138.660 117.084 161.033 1.00 123.01 ? 3538 GLN A CA    1 
ATOM   13081 C C     . GLN A 1 3538 ? 137.334 117.378 160.350 1.00 123.01 ? 3538 GLN A C     1 
ATOM   13082 O O     . GLN A 1 3538 ? 136.286 116.898 160.794 1.00 123.01 ? 3538 GLN A O     1 
ATOM   13083 C CB    . GLN A 1 3538 ? 138.966 118.143 162.089 1.00 123.01 ? 3538 GLN A CB    1 
ATOM   13084 C CG    . GLN A 1 3538 ? 137.900 118.272 163.158 1.00 123.01 ? 3538 GLN A CG    1 
ATOM   13085 C CD    . GLN A 1 3538 ? 138.460 118.716 164.490 1.00 123.01 ? 3538 GLN A CD    1 
ATOM   13086 O OE1   . GLN A 1 3538 ? 139.652 118.995 164.612 1.00 123.01 ? 3538 GLN A OE1   1 
ATOM   13087 N NE2   . GLN A 1 3538 ? 137.599 118.801 165.495 1.00 123.01 ? 3538 GLN A NE2   1 
ATOM   13088 N N     . ALA A 1 3539 ? 137.361 118.146 159.266 1.00 123.26 ? 3539 ALA A N     1 
ATOM   13089 C CA    . ALA A 1 3539 ? 136.161 118.474 158.512 1.00 123.26 ? 3539 ALA A CA    1 
ATOM   13090 C C     . ALA A 1 3539 ? 135.750 117.370 157.550 1.00 123.26 ? 3539 ALA A C     1 
ATOM   13091 O O     . ALA A 1 3539 ? 134.770 117.542 156.820 1.00 123.26 ? 3539 ALA A O     1 
ATOM   13092 C CB    . ALA A 1 3539 ? 136.361 119.778 157.737 1.00 123.26 ? 3539 ALA A CB    1 
ATOM   13093 N N     . ASN A 1 3540 ? 136.479 116.254 157.528 1.00 122.98 ? 3540 ASN A N     1 
ATOM   13094 C CA    . ASN A 1 3540 ? 136.185 115.130 156.642 1.00 122.98 ? 3540 ASN A CA    1 
ATOM   13095 C C     . ASN A 1 3540 ? 136.198 115.548 155.178 1.00 122.98 ? 3540 ASN A C     1 
ATOM   13096 O O     . ASN A 1 3540 ? 135.402 115.060 154.373 1.00 122.98 ? 3540 ASN A O     1 
ATOM   13097 C CB    . ASN A 1 3540 ? 134.849 114.473 156.995 1.00 122.98 ? 3540 ASN A CB    1 
ATOM   13098 C CG    . ASN A 1 3540 ? 135.020 113.248 157.864 1.00 122.98 ? 3540 ASN A CG    1 
ATOM   13099 O OD1   . ASN A 1 3540 ? 136.101 112.998 158.396 1.00 122.98 ? 3540 ASN A OD1   1 
ATOM   13100 N ND2   . ASN A 1 3540 ? 133.950 112.479 158.021 1.00 122.98 ? 3540 ASN A ND2   1 
ATOM   13101 N N     . ILE A 1 3541 ? 137.095 116.460 154.826 1.00 118.69 ? 3541 ILE A N     1 
ATOM   13102 C CA    . ILE A 1 3541 ? 137.281 116.871 153.442 1.00 118.69 ? 3541 ILE A CA    1 
ATOM   13103 C C     . ILE A 1 3541 ? 138.424 116.054 152.859 1.00 118.69 ? 3541 ILE A C     1 
ATOM   13104 O O     . ILE A 1 3541 ? 139.543 116.072 153.381 1.00 118.69 ? 3541 ILE A O     1 
ATOM   13105 C CB    . ILE A 1 3541 ? 137.564 118.374 153.341 1.00 118.69 ? 3541 ILE A CB    1 
ATOM   13106 C CG1   . ILE A 1 3541 ? 136.521 119.148 154.142 1.00 118.69 ? 3541 ILE A CG1   1 
ATOM   13107 C CG2   . ILE A 1 3541 ? 137.560 118.815 151.890 1.00 118.69 ? 3541 ILE A CG2   1 
ATOM   13108 C CD1   . ILE A 1 3541 ? 135.105 118.874 153.704 1.00 118.69 ? 3541 ILE A CD1   1 
ATOM   13109 N N     . GLN A 1 3542 ? 138.145 115.339 151.776 1.00 122.70 ? 3542 GLN A N     1 
ATOM   13110 C CA    . GLN A 1 3542 ? 139.108 114.404 151.209 1.00 122.70 ? 3542 GLN A CA    1 
ATOM   13111 C C     . GLN A 1 3542 ? 140.205 115.190 150.507 1.00 122.70 ? 3542 GLN A C     1 
ATOM   13112 O O     . GLN A 1 3542 ? 140.049 115.617 149.362 1.00 122.70 ? 3542 GLN A O     1 
ATOM   13113 C CB    . GLN A 1 3542 ? 138.417 113.437 150.256 1.00 122.70 ? 3542 GLN A CB    1 
ATOM   13114 C CG    . GLN A 1 3542 ? 137.256 112.680 150.880 1.00 122.70 ? 3542 GLN A CG    1 
ATOM   13115 C CD    . GLN A 1 3542 ? 137.684 111.767 152.013 1.00 122.70 ? 3542 GLN A CD    1 
ATOM   13116 O OE1   . GLN A 1 3542 ? 138.864 111.451 152.166 1.00 122.70 ? 3542 GLN A OE1   1 
ATOM   13117 N NE2   . GLN A 1 3542 ? 136.720 111.337 152.816 1.00 122.70 ? 3542 GLN A NE2   1 
ATOM   13118 N N     . PHE A 1 3543 ? 141.318 115.389 151.203 1.00 121.47 ? 3543 PHE A N     1 
ATOM   13119 C CA    . PHE A 1 3543 ? 142.513 115.991 150.636 1.00 121.47 ? 3543 PHE A CA    1 
ATOM   13120 C C     . PHE A 1 3543 ? 143.632 114.961 150.641 1.00 121.47 ? 3543 PHE A C     1 
ATOM   13121 O O     . PHE A 1 3543 ? 143.706 114.120 151.542 1.00 121.47 ? 3543 PHE A O     1 
ATOM   13122 C CB    . PHE A 1 3543 ? 142.940 117.230 151.423 1.00 121.47 ? 3543 PHE A CB    1 
ATOM   13123 C CG    . PHE A 1 3543 ? 143.589 116.916 152.737 1.00 121.47 ? 3543 PHE A CG    1 
ATOM   13124 C CD1   . PHE A 1 3543 ? 142.831 116.489 153.813 1.00 121.47 ? 3543 PHE A CD1   1 
ATOM   13125 C CD2   . PHE A 1 3543 ? 144.956 117.046 152.897 1.00 121.47 ? 3543 PHE A CD2   1 
ATOM   13126 C CE1   . PHE A 1 3543 ? 143.425 116.199 155.021 1.00 121.47 ? 3543 PHE A CE1   1 
ATOM   13127 C CE2   . PHE A 1 3543 ? 145.555 116.756 154.103 1.00 121.47 ? 3543 PHE A CE2   1 
ATOM   13128 C CZ    . PHE A 1 3543 ? 144.789 116.332 155.167 1.00 121.47 ? 3543 PHE A CZ    1 
ATOM   13129 N N     . ARG A 1 3544 ? 144.492 115.018 149.628 1.00 134.21 ? 3544 ARG A N     1 
ATOM   13130 C CA    . ARG A 1 3544 ? 145.603 114.081 149.552 1.00 134.21 ? 3544 ARG A CA    1 
ATOM   13131 C C     . ARG A 1 3544 ? 146.508 114.253 150.763 1.00 134.21 ? 3544 ARG A C     1 
ATOM   13132 O O     . ARG A 1 3544 ? 146.939 115.365 151.077 1.00 134.21 ? 3544 ARG A O     1 
ATOM   13133 C CB    . ARG A 1 3544 ? 146.396 114.302 148.264 1.00 134.21 ? 3544 ARG A CB    1 
ATOM   13134 C CG    . ARG A 1 3544 ? 145.580 114.126 146.993 1.00 134.21 ? 3544 ARG A CG    1 
ATOM   13135 C CD    . ARG A 1 3544 ? 146.453 114.135 145.746 1.00 134.21 ? 3544 ARG A CD    1 
ATOM   13136 N NE    . ARG A 1 3544 ? 147.428 113.052 145.736 1.00 134.21 ? 3544 ARG A NE    1 
ATOM   13137 C CZ    . ARG A 1 3544 ? 148.703 113.187 146.074 1.00 134.21 ? 3544 ARG A CZ    1 
ATOM   13138 N NH1   . ARG A 1 3544 ? 149.192 114.348 146.474 1.00 134.21 ? 3544 ARG A NH1   1 
ATOM   13139 N NH2   . ARG A 1 3544 ? 149.507 112.129 146.007 1.00 134.21 ? 3544 ARG A NH2   1 
ATOM   13140 N N     . THR A 1 3545 ? 146.790 113.149 151.446 1.00 135.67 ? 3545 THR A N     1 
ATOM   13141 C CA    . THR A 1 3545 ? 147.673 113.204 152.598 1.00 135.67 ? 3545 THR A CA    1 
ATOM   13142 C C     . THR A 1 3545 ? 149.100 113.500 152.149 1.00 135.67 ? 3545 THR A C     1 
ATOM   13143 O O     . THR A 1 3545 ? 149.469 113.278 150.994 1.00 135.67 ? 3545 THR A O     1 
ATOM   13144 C CB    . THR A 1 3545 ? 147.621 111.893 153.380 1.00 135.67 ? 3545 THR A CB    1 
ATOM   13145 O OG1   . THR A 1 3545 ? 146.292 111.361 153.331 1.00 135.67 ? 3545 THR A OG1   1 
ATOM   13146 C CG2   . THR A 1 3545 ? 148.006 112.121 154.832 1.00 135.67 ? 3545 THR A CG2   1 
ATOM   13147 N N     . ASP A 1 3546 ? 149.882 114.059 153.076 1.00 144.32 ? 3546 ASP A N     1 
ATOM   13148 C CA    . ASP A 1 3546 ? 151.296 114.401 152.920 1.00 144.32 ? 3546 ASP A CA    1 
ATOM   13149 C C     . ASP A 1 3546 ? 151.650 114.911 151.526 1.00 144.32 ? 3546 ASP A C     1 
ATOM   13150 O O     . ASP A 1 3546 ? 152.671 114.524 150.949 1.00 144.32 ? 3546 ASP A O     1 
ATOM   13151 C CB    . ASP A 1 3546 ? 152.182 113.211 153.335 1.00 144.32 ? 3546 ASP A CB    1 
ATOM   13152 C CG    . ASP A 1 3546 ? 152.010 111.968 152.456 1.00 144.32 ? 3546 ASP A CG    1 
ATOM   13153 O OD1   . ASP A 1 3546 ? 151.673 112.064 151.261 1.00 144.32 ? 3546 ASP A OD1   1 
ATOM   13154 O OD2   . ASP A 1 3546 ? 152.214 110.859 152.992 1.00 144.32 ? 3546 ASP A OD2   1 
ATOM   13155 N N     . ILE A 1 3547 ? 150.828 115.807 150.997 1.00 135.60 ? 3547 ILE A N     1 
ATOM   13156 C CA    . ILE A 1 3547 ? 151.091 116.419 149.701 1.00 135.60 ? 3547 ILE A CA    1 
ATOM   13157 C C     . ILE A 1 3547 ? 152.128 117.519 149.872 1.00 135.60 ? 3547 ILE A C     1 
ATOM   13158 O O     . ILE A 1 3547 ? 151.987 118.396 150.731 1.00 135.60 ? 3547 ILE A O     1 
ATOM   13159 C CB    . ILE A 1 3547 ? 149.794 116.969 149.088 1.00 135.60 ? 3547 ILE A CB    1 
ATOM   13160 C CG1   . ILE A 1 3547 ? 150.105 117.891 147.906 1.00 135.60 ? 3547 ILE A CG1   1 
ATOM   13161 C CG2   . ILE A 1 3547 ? 148.966 117.694 150.141 1.00 135.60 ? 3547 ILE A CG2   1 
ATOM   13162 C CD1   . ILE A 1 3547 ? 150.776 117.204 146.740 1.00 135.60 ? 3547 ILE A CD1   1 
ATOM   13163 N N     . ALA A 1 3548 ? 153.178 117.473 149.060 1.00 120.88 ? 3548 ALA A N     1 
ATOM   13164 C CA    . ALA A 1 3548 ? 154.171 118.536 149.032 1.00 120.88 ? 3548 ALA A CA    1 
ATOM   13165 C C     . ALA A 1 3548 ? 153.692 119.618 148.074 1.00 120.88 ? 3548 ALA A C     1 
ATOM   13166 O O     . ALA A 1 3548 ? 153.311 119.324 146.937 1.00 120.88 ? 3548 ALA A O     1 
ATOM   13167 C CB    . ALA A 1 3548 ? 155.536 117.998 148.613 1.00 120.88 ? 3548 ALA A CB    1 
ATOM   13168 N N     . ARG A 1 3549 ? 153.693 120.866 148.538 1.00 111.96 ? 3549 ARG A N     1 
ATOM   13169 C CA    . ARG A 1 3549 ? 153.194 121.958 147.715 1.00 111.96 ? 3549 ARG A CA    1 
ATOM   13170 C C     . ARG A 1 3549 ? 154.174 122.378 146.632 1.00 111.96 ? 3549 ARG A C     1 
ATOM   13171 O O     . ARG A 1 3549 ? 153.793 123.145 145.743 1.00 111.96 ? 3549 ARG A O     1 
ATOM   13172 C CB    . ARG A 1 3549 ? 152.863 123.160 148.595 1.00 111.96 ? 3549 ARG A CB    1 
ATOM   13173 C CG    . ARG A 1 3549 ? 153.921 123.449 149.637 1.00 111.96 ? 3549 ARG A CG    1 
ATOM   13174 C CD    . ARG A 1 3549 ? 153.298 123.807 150.968 1.00 111.96 ? 3549 ARG A CD    1 
ATOM   13175 N NE    . ARG A 1 3549 ? 154.309 124.094 151.977 1.00 111.96 ? 3549 ARG A NE    1 
ATOM   13176 C CZ    . ARG A 1 3549 ? 154.981 123.167 152.644 1.00 111.96 ? 3549 ARG A CZ    1 
ATOM   13177 N NH1   . ARG A 1 3549 ? 154.773 121.879 152.435 1.00 111.96 ? 3549 ARG A NH1   1 
ATOM   13178 N NH2   . ARG A 1 3549 ? 155.886 123.544 153.542 1.00 111.96 ? 3549 ARG A NH2   1 
ATOM   13179 N N     . THR A 1 3550 ? 155.418 121.904 146.683 1.00 116.75 ? 3550 THR A N     1 
ATOM   13180 C CA    . THR A 1 3550 ? 156.421 122.366 145.732 1.00 116.75 ? 3550 THR A CA    1 
ATOM   13181 C C     . THR A 1 3550 ? 156.089 121.922 144.313 1.00 116.75 ? 3550 THR A C     1 
ATOM   13182 O O     . THR A 1 3550 ? 156.127 122.726 143.376 1.00 116.75 ? 3550 THR A O     1 
ATOM   13183 C CB    . THR A 1 3550 ? 157.801 121.862 146.144 1.00 116.75 ? 3550 THR A CB    1 
ATOM   13184 O OG1   . THR A 1 3550 ? 158.127 122.373 147.441 1.00 116.75 ? 3550 THR A OG1   1 
ATOM   13185 C CG2   . THR A 1 3550 ? 158.850 122.321 145.149 1.00 116.75 ? 3550 THR A CG2   1 
ATOM   13186 N N     . GLU A 1 3551 ? 155.761 120.646 144.132 1.00 126.81 ? 3551 GLU A N     1 
ATOM   13187 C CA    . GLU A 1 3551 ? 155.484 120.130 142.798 1.00 126.81 ? 3551 GLU A CA    1 
ATOM   13188 C C     . GLU A 1 3551 ? 154.014 120.213 142.417 1.00 126.81 ? 3551 GLU A C     1 
ATOM   13189 O O     . GLU A 1 3551 ? 153.679 119.978 141.252 1.00 126.81 ? 3551 GLU A O     1 
ATOM   13190 C CB    . GLU A 1 3551 ? 155.963 118.676 142.674 1.00 126.81 ? 3551 GLU A CB    1 
ATOM   13191 C CG    . GLU A 1 3551 ? 155.146 117.618 143.421 1.00 126.81 ? 3551 GLU A CG    1 
ATOM   13192 C CD    . GLU A 1 3551 ? 155.002 117.866 144.912 1.00 126.81 ? 3551 GLU A CD    1 
ATOM   13193 O OE1   . GLU A 1 3551 ? 154.185 117.163 145.542 1.00 126.81 ? 3551 GLU A OE1   1 
ATOM   13194 O OE2   . GLU A 1 3551 ? 155.710 118.733 145.465 1.00 126.81 ? 3551 GLU A OE2   1 
ATOM   13195 N N     . TYR A 1 3552 ? 153.132 120.541 143.362 1.00 115.66 ? 3552 TYR A N     1 
ATOM   13196 C CA    . TYR A 1 3552 ? 151.724 120.710 143.024 1.00 115.66 ? 3552 TYR A CA    1 
ATOM   13197 C C     . TYR A 1 3552 ? 151.534 121.870 142.059 1.00 115.66 ? 3552 TYR A C     1 
ATOM   13198 O O     . TYR A 1 3552 ? 150.762 121.770 141.099 1.00 115.66 ? 3552 TYR A O     1 
ATOM   13199 C CB    . TYR A 1 3552 ? 150.902 120.931 144.295 1.00 115.66 ? 3552 TYR A CB    1 
ATOM   13200 C CG    . TYR A 1 3552 ? 149.446 120.535 144.179 1.00 115.66 ? 3552 TYR A CG    1 
ATOM   13201 C CD1   . TYR A 1 3552 ? 148.621 121.107 143.223 1.00 115.66 ? 3552 TYR A CD1   1 
ATOM   13202 C CD2   . TYR A 1 3552 ? 148.895 119.595 145.036 1.00 115.66 ? 3552 TYR A CD2   1 
ATOM   13203 C CE1   . TYR A 1 3552 ? 147.295 120.747 143.118 1.00 115.66 ? 3552 TYR A CE1   1 
ATOM   13204 C CE2   . TYR A 1 3552 ? 147.572 119.230 144.938 1.00 115.66 ? 3552 TYR A CE2   1 
ATOM   13205 C CZ    . TYR A 1 3552 ? 146.777 119.810 143.978 1.00 115.66 ? 3552 TYR A CZ    1 
ATOM   13206 O OH    . TYR A 1 3552 ? 145.456 119.451 143.876 1.00 115.66 ? 3552 TYR A OH    1 
ATOM   13207 N N     . LEU A 1 3553 ? 152.234 122.975 142.293 1.00 111.43 ? 3553 LEU A N     1 
ATOM   13208 C CA    . LEU A 1 3553 ? 152.034 124.200 141.537 1.00 111.43 ? 3553 LEU A CA    1 
ATOM   13209 C C     . LEU A 1 3553 ? 153.143 124.474 140.531 1.00 111.43 ? 3553 LEU A C     1 
ATOM   13210 O O     . LEU A 1 3553 ? 153.137 125.533 139.897 1.00 111.43 ? 3553 LEU A O     1 
ATOM   13211 C CB    . LEU A 1 3553 ? 151.901 125.379 142.501 1.00 111.43 ? 3553 LEU A CB    1 
ATOM   13212 C CG    . LEU A 1 3553 ? 151.041 125.030 143.715 1.00 111.43 ? 3553 LEU A CG    1 
ATOM   13213 C CD1   . LEU A 1 3553 ? 151.257 126.011 144.846 1.00 111.43 ? 3553 LEU A CD1   1 
ATOM   13214 C CD2   . LEU A 1 3553 ? 149.579 124.968 143.331 1.00 111.43 ? 3553 LEU A CD2   1 
ATOM   13215 N N     . SER A 1 3554 ? 154.087 123.553 140.365 1.00 121.62 ? 3554 SER A N     1 
ATOM   13216 C CA    . SER A 1 3554 ? 155.177 123.746 139.413 1.00 121.62 ? 3554 SER A CA    1 
ATOM   13217 C C     . SER A 1 3554 ? 155.743 122.384 139.061 1.00 121.62 ? 3554 SER A C     1 
ATOM   13218 O O     . SER A 1 3554 ? 156.122 121.622 139.956 1.00 121.62 ? 3554 SER A O     1 
ATOM   13219 C CB    . SER A 1 3554 ? 156.260 124.647 139.996 1.00 121.62 ? 3554 SER A CB    1 
ATOM   13220 O OG    . SER A 1 3554 ? 157.060 123.939 140.926 1.00 121.62 ? 3554 SER A OG    1 
ATOM   13221 N N     . ASN A 1 3555 ? 155.806 122.078 137.770 1.00 131.77 ? 3555 ASN A N     1 
ATOM   13222 C CA    . ASN A 1 3555 ? 156.287 120.781 137.318 1.00 131.77 ? 3555 ASN A CA    1 
ATOM   13223 C C     . ASN A 1 3555 ? 157.813 120.802 137.240 1.00 131.77 ? 3555 ASN A C     1 
ATOM   13224 O O     . ASN A 1 3555 ? 158.469 121.780 137.609 1.00 131.77 ? 3555 ASN A O     1 
ATOM   13225 C CB    . ASN A 1 3555 ? 155.616 120.413 135.995 1.00 131.77 ? 3555 ASN A CB    1 
ATOM   13226 C CG    . ASN A 1 3555 ? 156.327 120.991 134.788 1.00 131.77 ? 3555 ASN A CG    1 
ATOM   13227 O OD1   . ASN A 1 3555 ? 157.448 120.604 134.459 1.00 131.77 ? 3555 ASN A OD1   1 
ATOM   13228 N ND2   . ASN A 1 3555 ? 155.674 121.935 134.122 1.00 131.77 ? 3555 ASN A ND2   1 
ATOM   13229 N N     . ALA A 1 3556 ? 158.394 119.706 136.747 1.00 134.08 ? 3556 ALA A N     1 
ATOM   13230 C CA    . ALA A 1 3556 ? 159.847 119.570 136.734 1.00 134.08 ? 3556 ALA A CA    1 
ATOM   13231 C C     . ALA A 1 3556 ? 160.498 120.603 135.825 1.00 134.08 ? 3556 ALA A C     1 
ATOM   13232 O O     . ALA A 1 3556 ? 161.573 121.124 136.141 1.00 134.08 ? 3556 ALA A O     1 
ATOM   13233 C CB    . ALA A 1 3556 ? 160.240 118.157 136.305 1.00 134.08 ? 3556 ALA A CB    1 
ATOM   13234 N N     . ASP A 1 3557 ? 159.875 120.897 134.683 1.00 137.93 ? 3557 ASP A N     1 
ATOM   13235 C CA    . ASP A 1 3557 ? 160.479 121.834 133.741 1.00 137.93 ? 3557 ASP A CA    1 
ATOM   13236 C C     . ASP A 1 3557 ? 160.570 123.247 134.320 1.00 137.93 ? 3557 ASP A C     1 
ATOM   13237 O O     . ASP A 1 3557 ? 161.590 123.923 134.148 1.00 137.93 ? 3557 ASP A O     1 
ATOM   13238 C CB    . ASP A 1 3557 ? 159.743 121.758 132.391 1.00 137.93 ? 3557 ASP A CB    1 
ATOM   13239 C CG    . ASP A 1 3557 ? 158.562 122.725 132.257 1.00 137.93 ? 3557 ASP A CG    1 
ATOM   13240 O OD1   . ASP A 1 3557 ? 158.170 123.413 133.219 1.00 137.93 ? 3557 ASP A OD1   1 
ATOM   13241 O OD2   . ASP A 1 3557 ? 158.009 122.793 131.140 1.00 137.93 ? 3557 ASP A OD2   1 
ATOM   13242 N N     . GLU A 1 3558 ? 159.534 123.699 135.032 1.00 134.92 ? 3558 GLU A N     1 
ATOM   13243 C CA    . GLU A 1 3558 ? 159.621 124.986 135.719 1.00 134.92 ? 3558 GLU A CA    1 
ATOM   13244 C C     . GLU A 1 3558 ? 160.722 124.984 136.771 1.00 134.92 ? 3558 GLU A C     1 
ATOM   13245 O O     . GLU A 1 3558 ? 161.465 125.965 136.906 1.00 134.92 ? 3558 GLU A O     1 
ATOM   13246 C CB    . GLU A 1 3558 ? 158.279 125.339 136.359 1.00 134.92 ? 3558 GLU A CB    1 
ATOM   13247 C CG    . GLU A 1 3558 ? 157.113 125.455 135.397 1.00 134.92 ? 3558 GLU A CG    1 
ATOM   13248 C CD    . GLU A 1 3558 ? 157.448 126.304 134.189 1.00 134.92 ? 3558 GLU A CD    1 
ATOM   13249 O OE1   . GLU A 1 3558 ? 158.006 127.405 134.378 1.00 134.92 ? 3558 GLU A OE1   1 
ATOM   13250 O OE2   . GLU A 1 3558 ? 157.144 125.885 133.055 1.00 134.92 ? 3558 GLU A OE2   1 
ATOM   13251 N N     . ARG A 1 3559 ? 160.837 123.897 137.534 1.00 125.95 ? 3559 ARG A N     1 
ATOM   13252 C CA    . ARG A 1 3559 ? 161.854 123.839 138.577 1.00 125.95 ? 3559 ARG A CA    1 
ATOM   13253 C C     . ARG A 1 3559 ? 163.255 123.897 137.985 1.00 125.95 ? 3559 ARG A C     1 
ATOM   13254 O O     . ARG A 1 3559 ? 164.117 124.628 138.485 1.00 125.95 ? 3559 ARG A O     1 
ATOM   13255 C CB    . ARG A 1 3559 ? 161.671 122.576 139.417 1.00 125.95 ? 3559 ARG A CB    1 
ATOM   13256 C CG    . ARG A 1 3559 ? 160.496 122.653 140.374 1.00 125.95 ? 3559 ARG A CG    1 
ATOM   13257 C CD    . ARG A 1 3559 ? 160.192 121.308 141.002 1.00 125.95 ? 3559 ARG A CD    1 
ATOM   13258 N NE    . ARG A 1 3559 ? 159.026 120.678 140.397 1.00 125.95 ? 3559 ARG A NE    1 
ATOM   13259 C CZ    . ARG A 1 3559 ? 158.726 119.392 140.515 1.00 125.95 ? 3559 ARG A CZ    1 
ATOM   13260 N NH1   . ARG A 1 3559 ? 159.479 118.570 141.226 1.00 125.95 ? 3559 ARG A NH1   1 
ATOM   13261 N NH2   . ARG A 1 3559 ? 157.641 118.920 139.908 1.00 125.95 ? 3559 ARG A NH2   1 
ATOM   13262 N N     . LEU A 1 3560 ? 163.499 123.143 136.912 1.00 135.78 ? 3560 LEU A N     1 
ATOM   13263 C CA    . LEU A 1 3560 ? 164.819 123.171 136.292 1.00 135.78 ? 3560 LEU A CA    1 
ATOM   13264 C C     . LEU A 1 3560 ? 165.088 124.509 135.619 1.00 135.78 ? 3560 LEU A C     1 
ATOM   13265 O O     . LEU A 1 3560 ? 166.236 124.962 135.590 1.00 135.78 ? 3560 LEU A O     1 
ATOM   13266 C CB    . LEU A 1 3560 ? 164.971 122.015 135.299 1.00 135.78 ? 3560 LEU A CB    1 
ATOM   13267 C CG    . LEU A 1 3560 ? 164.060 121.890 134.074 1.00 135.78 ? 3560 LEU A CG    1 
ATOM   13268 C CD1   . LEU A 1 3560 ? 164.531 122.741 132.900 1.00 135.78 ? 3560 LEU A CD1   1 
ATOM   13269 C CD2   . LEU A 1 3560 ? 163.929 120.433 133.661 1.00 135.78 ? 3560 LEU A CD2   1 
ATOM   13270 N N     . ARG A 1 3561 ? 164.053 125.153 135.073 1.00 137.42 ? 3561 ARG A N     1 
ATOM   13271 C CA    . ARG A 1 3561 ? 164.233 126.488 134.517 1.00 137.42 ? 3561 ARG A CA    1 
ATOM   13272 C C     . ARG A 1 3561 ? 164.632 127.480 135.600 1.00 137.42 ? 3561 ARG A C     1 
ATOM   13273 O O     . ARG A 1 3561 ? 165.514 128.321 135.391 1.00 137.42 ? 3561 ARG A O     1 
ATOM   13274 C CB    . ARG A 1 3561 ? 162.954 126.939 133.814 1.00 137.42 ? 3561 ARG A CB    1 
ATOM   13275 C CG    . ARG A 1 3561 ? 163.197 127.856 132.636 1.00 137.42 ? 3561 ARG A CG    1 
ATOM   13276 C CD    . ARG A 1 3561 ? 163.002 129.309 133.025 1.00 137.42 ? 3561 ARG A CD    1 
ATOM   13277 N NE    . ARG A 1 3561 ? 161.636 129.579 133.457 1.00 137.42 ? 3561 ARG A NE    1 
ATOM   13278 C CZ    . ARG A 1 3561 ? 160.612 129.750 132.632 1.00 137.42 ? 3561 ARG A CZ    1 
ATOM   13279 N NH1   . ARG A 1 3561 ? 160.765 129.690 131.320 1.00 137.42 ? 3561 ARG A NH1   1 
ATOM   13280 N NH2   . ARG A 1 3561 ? 159.405 129.988 133.137 1.00 137.42 ? 3561 ARG A NH2   1 
ATOM   13281 N N     . TRP A 1 3562 ? 163.991 127.394 136.768 1.00 133.28 ? 3562 TRP A N     1 
ATOM   13282 C CA    . TRP A 1 3562 ? 164.356 128.264 137.881 1.00 133.28 ? 3562 TRP A CA    1 
ATOM   13283 C C     . TRP A 1 3562 ? 165.770 127.977 138.365 1.00 133.28 ? 3562 TRP A C     1 
ATOM   13284 O O     . TRP A 1 3562 ? 166.524 128.903 138.685 1.00 133.28 ? 3562 TRP A O     1 
ATOM   13285 C CB    . TRP A 1 3562 ? 163.357 128.101 139.022 1.00 133.28 ? 3562 TRP A CB    1 
ATOM   13286 C CG    . TRP A 1 3562 ? 161.987 128.564 138.675 1.00 133.28 ? 3562 TRP A CG    1 
ATOM   13287 C CD1   . TRP A 1 3562 ? 161.644 129.422 137.675 1.00 133.28 ? 3562 TRP A CD1   1 
ATOM   13288 C CD2   . TRP A 1 3562 ? 160.770 128.200 139.329 1.00 133.28 ? 3562 TRP A CD2   1 
ATOM   13289 N NE1   . TRP A 1 3562 ? 160.285 129.614 137.664 1.00 133.28 ? 3562 TRP A NE1   1 
ATOM   13290 C CE2   . TRP A 1 3562 ? 159.725 128.874 138.671 1.00 133.28 ? 3562 TRP A CE2   1 
ATOM   13291 C CE3   . TRP A 1 3562 ? 160.462 127.369 140.409 1.00 133.28 ? 3562 TRP A CE3   1 
ATOM   13292 C CZ2   . TRP A 1 3562 ? 158.397 128.744 139.056 1.00 133.28 ? 3562 TRP A CZ2   1 
ATOM   13293 C CZ3   . TRP A 1 3562 ? 159.143 127.241 140.789 1.00 133.28 ? 3562 TRP A CZ3   1 
ATOM   13294 C CH2   . TRP A 1 3562 ? 158.126 127.925 140.115 1.00 133.28 ? 3562 TRP A CH2   1 
ATOM   13295 N N     . GLN A 1 3563 ? 166.143 126.697 138.435 1.00 134.71 ? 3563 GLN A N     1 
ATOM   13296 C CA    . GLN A 1 3563 ? 167.505 126.348 138.825 1.00 134.71 ? 3563 GLN A CA    1 
ATOM   13297 C C     . GLN A 1 3563 ? 168.517 126.923 137.843 1.00 134.71 ? 3563 GLN A C     1 
ATOM   13298 O O     . GLN A 1 3563 ? 169.553 127.461 138.249 1.00 134.71 ? 3563 GLN A O     1 
ATOM   13299 C CB    . GLN A 1 3563 ? 167.654 124.830 138.922 1.00 134.71 ? 3563 GLN A CB    1 
ATOM   13300 C CG    . GLN A 1 3563 ? 166.831 124.193 140.024 1.00 134.71 ? 3563 GLN A CG    1 
ATOM   13301 C CD    . GLN A 1 3563 ? 167.477 124.325 141.386 1.00 134.71 ? 3563 GLN A CD    1 
ATOM   13302 O OE1   . GLN A 1 3563 ? 166.850 124.059 142.411 1.00 134.71 ? 3563 GLN A OE1   1 
ATOM   13303 N NE2   . GLN A 1 3563 ? 168.742 124.730 141.405 1.00 134.71 ? 3563 GLN A NE2   1 
ATOM   13304 N N     . ALA A 1 3564 ? 168.230 126.823 136.544 1.00 136.56 ? 3564 ALA A N     1 
ATOM   13305 C CA    . ALA A 1 3564 ? 169.074 127.457 135.542 1.00 136.56 ? 3564 ALA A CA    1 
ATOM   13306 C C     . ALA A 1 3564 ? 168.968 128.974 135.584 1.00 136.56 ? 3564 ALA A C     1 
ATOM   13307 O O     . ALA A 1 3564 ? 169.846 129.659 135.051 1.00 136.56 ? 3564 ALA A O     1 
ATOM   13308 C CB    . ALA A 1 3564 ? 168.712 126.948 134.148 1.00 136.56 ? 3564 ALA A CB    1 
ATOM   13309 N N     . SER A 1 3565 ? 167.919 129.510 136.204 1.00 138.42 ? 3565 SER A N     1 
ATOM   13310 C CA    . SER A 1 3565 ? 167.743 130.946 136.355 1.00 138.42 ? 3565 SER A CA    1 
ATOM   13311 C C     . SER A 1 3565 ? 168.389 131.481 137.627 1.00 138.42 ? 3565 SER A C     1 
ATOM   13312 O O     . SER A 1 3565 ? 167.946 132.511 138.149 1.00 138.42 ? 3565 SER A O     1 
ATOM   13313 C CB    . SER A 1 3565 ? 166.255 131.299 136.329 1.00 138.42 ? 3565 SER A CB    1 
ATOM   13314 O OG    . SER A 1 3565 ? 166.058 132.663 135.999 1.00 138.42 ? 3565 SER A OG    1 
ATOM   13315 N N     . SER A 1 3566 ? 169.416 130.798 138.135 1.00 134.68 ? 3566 SER A N     1 
ATOM   13316 C CA    . SER A 1 3566 ? 170.154 131.220 139.324 1.00 134.68 ? 3566 SER A CA    1 
ATOM   13317 C C     . SER A 1 3566 ? 169.229 131.338 140.537 1.00 134.68 ? 3566 SER A C     1 
ATOM   13318 O O     . SER A 1 3566 ? 169.029 132.413 141.104 1.00 134.68 ? 3566 SER A O     1 
ATOM   13319 C CB    . SER A 1 3566 ? 170.899 132.534 139.068 1.00 134.68 ? 3566 SER A CB    1 
ATOM   13320 O OG    . SER A 1 3566 ? 170.010 133.636 139.116 1.00 134.68 ? 3566 SER A OG    1 
ATOM   13321 N N     . LEU A 1 3567 ? 168.657 130.200 140.921 1.00 130.24 ? 3567 LEU A N     1 
ATOM   13322 C CA    . LEU A 1 3567 ? 167.847 130.110 142.120 1.00 130.24 ? 3567 LEU A CA    1 
ATOM   13323 C C     . LEU A 1 3567 ? 168.384 129.022 143.040 1.00 130.24 ? 3567 LEU A C     1 
ATOM   13324 O O     . LEU A 1 3567 ? 168.742 127.936 142.571 1.00 130.24 ? 3567 LEU A O     1 
ATOM   13325 C CB    . LEU A 1 3567 ? 166.378 129.812 141.784 1.00 130.24 ? 3567 LEU A CB    1 
ATOM   13326 C CG    . LEU A 1 3567 ? 165.459 129.515 142.973 1.00 130.24 ? 3567 LEU A CG    1 
ATOM   13327 C CD1   . LEU A 1 3567 ? 164.848 130.783 143.534 1.00 130.24 ? 3567 LEU A CD1   1 
ATOM   13328 C CD2   . LEU A 1 3567 ? 164.372 128.532 142.574 1.00 130.24 ? 3567 LEU A CD2   1 
ATOM   13329 N N     . PRO A 1 3568 ? 168.465 129.283 144.342 1.00 129.74 ? 3568 PRO A N     1 
ATOM   13330 C CA    . PRO A 1 3568 ? 168.886 128.232 145.272 1.00 129.74 ? 3568 PRO A CA    1 
ATOM   13331 C C     . PRO A 1 3568 ? 167.902 127.075 145.259 1.00 129.74 ? 3568 PRO A C     1 
ATOM   13332 O O     . PRO A 1 3568 ? 166.702 127.253 145.045 1.00 129.74 ? 3568 PRO A O     1 
ATOM   13333 C CB    . PRO A 1 3568 ? 168.898 128.941 146.633 1.00 129.74 ? 3568 PRO A CB    1 
ATOM   13334 C CG    . PRO A 1 3568 ? 168.950 130.400 146.312 1.00 129.74 ? 3568 PRO A CG    1 
ATOM   13335 C CD    . PRO A 1 3568 ? 168.214 130.562 145.024 1.00 129.74 ? 3568 PRO A CD    1 
ATOM   13336 N N     . ALA A 1 3569 ? 168.426 125.876 145.484 1.00 131.43 ? 3569 ALA A N     1 
ATOM   13337 C CA    . ALA A 1 3569 ? 167.592 124.684 145.547 1.00 131.43 ? 3569 ALA A CA    1 
ATOM   13338 C C     . ALA A 1 3569 ? 166.874 124.541 146.879 1.00 131.43 ? 3569 ALA A C     1 
ATOM   13339 O O     . ALA A 1 3569 ? 166.267 123.495 147.131 1.00 131.43 ? 3569 ALA A O     1 
ATOM   13340 C CB    . ALA A 1 3569 ? 168.435 123.436 145.274 1.00 131.43 ? 3569 ALA A CB    1 
ATOM   13341 N N     . ASP A 1 3570 ? 166.931 125.560 147.730 1.00 126.96 ? 3570 ASP A N     1 
ATOM   13342 C CA    . ASP A 1 3570 ? 166.279 125.491 149.028 1.00 126.96 ? 3570 ASP A CA    1 
ATOM   13343 C C     . ASP A 1 3570 ? 164.766 125.425 148.859 1.00 126.96 ? 3570 ASP A C     1 
ATOM   13344 O O     . ASP A 1 3570 ? 164.200 126.021 147.939 1.00 126.96 ? 3570 ASP A O     1 
ATOM   13345 C CB    . ASP A 1 3570 ? 166.671 126.702 149.874 1.00 126.96 ? 3570 ASP A CB    1 
ATOM   13346 C CG    . ASP A 1 3570 ? 165.685 126.987 150.993 1.00 126.96 ? 3570 ASP A CG    1 
ATOM   13347 O OD1   . ASP A 1 3570 ? 165.177 126.029 151.615 1.00 126.96 ? 3570 ASP A OD1   1 
ATOM   13348 O OD2   . ASP A 1 3570 ? 165.419 128.178 151.252 1.00 126.96 ? 3570 ASP A OD2   1 
ATOM   13349 N N     . ASP A 1 3571 ? 164.115 124.691 149.764 1.00 124.53 ? 3571 ASP A N     1 
ATOM   13350 C CA    . ASP A 1 3571 ? 162.667 124.527 149.689 1.00 124.53 ? 3571 ASP A CA    1 
ATOM   13351 C C     . ASP A 1 3571 ? 161.949 125.864 149.825 1.00 124.53 ? 3571 ASP A C     1 
ATOM   13352 O O     . ASP A 1 3571 ? 160.971 126.128 149.115 1.00 124.53 ? 3571 ASP A O     1 
ATOM   13353 C CB    . ASP A 1 3571 ? 162.202 123.546 150.766 1.00 124.53 ? 3571 ASP A CB    1 
ATOM   13354 C CG    . ASP A 1 3571 ? 160.701 123.558 150.958 1.00 124.53 ? 3571 ASP A CG    1 
ATOM   13355 O OD1   . ASP A 1 3571 ? 160.201 124.414 151.717 1.00 124.53 ? 3571 ASP A OD1   1 
ATOM   13356 O OD2   . ASP A 1 3571 ? 160.019 122.708 150.348 1.00 124.53 ? 3571 ASP A OD2   1 
ATOM   13357 N N     . LEU A 1 3572 ? 162.420 126.721 150.734 1.00 118.29 ? 3572 LEU A N     1 
ATOM   13358 C CA    . LEU A 1 3572 ? 161.801 128.031 150.898 1.00 118.29 ? 3572 LEU A CA    1 
ATOM   13359 C C     . LEU A 1 3572 ? 161.921 128.853 149.623 1.00 118.29 ? 3572 LEU A C     1 
ATOM   13360 O O     . LEU A 1 3572 ? 160.973 129.542 149.228 1.00 118.29 ? 3572 LEU A O     1 
ATOM   13361 C CB    . LEU A 1 3572 ? 162.431 128.763 152.085 1.00 118.29 ? 3572 LEU A CB    1 
ATOM   13362 C CG    . LEU A 1 3572 ? 162.127 130.244 152.319 1.00 118.29 ? 3572 LEU A CG    1 
ATOM   13363 C CD1   . LEU A 1 3572 ? 162.151 130.535 153.805 1.00 118.29 ? 3572 LEU A CD1   1 
ATOM   13364 C CD2   . LEU A 1 3572 ? 163.131 131.134 151.612 1.00 118.29 ? 3572 LEU A CD2   1 
ATOM   13365 N N     . CYS A 1 3573 ? 163.079 128.795 148.965 1.00 123.59 ? 3573 CYS A N     1 
ATOM   13366 C CA    . CYS A 1 3573 ? 163.237 129.511 147.705 1.00 123.59 ? 3573 CYS A CA    1 
ATOM   13367 C C     . CYS A 1 3573 ? 162.300 128.962 146.638 1.00 123.59 ? 3573 CYS A C     1 
ATOM   13368 O O     . CYS A 1 3573 ? 161.738 129.726 145.847 1.00 123.59 ? 3573 CYS A O     1 
ATOM   13369 C CB    . CYS A 1 3573 ? 164.689 129.445 147.234 1.00 123.59 ? 3573 CYS A CB    1 
ATOM   13370 S SG    . CYS A 1 3573 ? 165.906 129.821 148.511 1.00 123.59 ? 3573 CYS A SG    1 
ATOM   13371 N N     . THR A 1 3574 ? 162.120 127.641 146.596 1.00 119.53 ? 3574 THR A N     1 
ATOM   13372 C CA    . THR A 1 3574 ? 161.195 127.067 145.624 1.00 119.53 ? 3574 THR A CA    1 
ATOM   13373 C C     . THR A 1 3574 ? 159.770 127.534 145.881 1.00 119.53 ? 3574 THR A C     1 
ATOM   13374 O O     . THR A 1 3574 ? 159.044 127.888 144.944 1.00 119.53 ? 3574 THR A O     1 
ATOM   13375 C CB    . THR A 1 3574 ? 161.267 125.542 145.660 1.00 119.53 ? 3574 THR A CB    1 
ATOM   13376 O OG1   . THR A 1 3574 ? 160.978 125.084 146.985 1.00 119.53 ? 3574 THR A OG1   1 
ATOM   13377 C CG2   . THR A 1 3574 ? 162.649 125.063 145.248 1.00 119.53 ? 3574 THR A CG2   1 
ATOM   13378 N N     . GLU A 1 3575 ? 159.351 127.548 147.146 1.00 113.79 ? 3575 GLU A N     1 
ATOM   13379 C CA    . GLU A 1 3575 ? 158.005 128.010 147.464 1.00 113.79 ? 3575 GLU A CA    1 
ATOM   13380 C C     . GLU A 1 3575 ? 157.833 129.481 147.112 1.00 113.79 ? 3575 GLU A C     1 
ATOM   13381 O O     . GLU A 1 3575 ? 156.788 129.890 146.590 1.00 113.79 ? 3575 GLU A O     1 
ATOM   13382 C CB    . GLU A 1 3575 ? 157.711 127.767 148.940 1.00 113.79 ? 3575 GLU A CB    1 
ATOM   13383 C CG    . GLU A 1 3575 ? 157.450 126.315 149.272 1.00 113.79 ? 3575 GLU A CG    1 
ATOM   13384 C CD    . GLU A 1 3575 ? 157.450 126.057 150.761 1.00 113.79 ? 3575 GLU A CD    1 
ATOM   13385 O OE1   . GLU A 1 3575 ? 157.848 126.965 151.520 1.00 113.79 ? 3575 GLU A OE1   1 
ATOM   13386 O OE2   . GLU A 1 3575 ? 157.050 124.949 151.176 1.00 113.79 ? 3575 GLU A OE2   1 
ATOM   13387 N N     . ASN A 1 3576 ? 158.852 130.293 147.387 1.00 110.38 ? 3576 ASN A N     1 
ATOM   13388 C CA    . ASN A 1 3576 ? 158.777 131.705 147.036 1.00 110.38 ? 3576 ASN A CA    1 
ATOM   13389 C C     . ASN A 1 3576 ? 158.697 131.892 145.527 1.00 110.38 ? 3576 ASN A C     1 
ATOM   13390 O O     . ASN A 1 3576 ? 157.966 132.761 145.041 1.00 110.38 ? 3576 ASN A O     1 
ATOM   13391 C CB    . ASN A 1 3576 ? 159.975 132.444 147.618 1.00 110.38 ? 3576 ASN A CB    1 
ATOM   13392 C CG    . ASN A 1 3576 ? 159.922 132.526 149.125 1.00 110.38 ? 3576 ASN A CG    1 
ATOM   13393 O OD1   . ASN A 1 3576 ? 158.982 132.039 149.750 1.00 110.38 ? 3576 ASN A OD1   1 
ATOM   13394 N ND2   . ASN A 1 3576 ? 160.934 133.140 149.720 1.00 110.38 ? 3576 ASN A ND2   1 
ATOM   13395 N N     . ALA A 1 3577 ? 159.438 131.085 144.768 1.00 115.56 ? 3577 ALA A N     1 
ATOM   13396 C CA    . ALA A 1 3577 ? 159.341 131.151 143.315 1.00 115.56 ? 3577 ALA A CA    1 
ATOM   13397 C C     . ALA A 1 3577 ? 157.952 130.747 142.845 1.00 115.56 ? 3577 ALA A C     1 
ATOM   13398 O O     . ALA A 1 3577 ? 157.421 131.316 141.884 1.00 115.56 ? 3577 ALA A O     1 
ATOM   13399 C CB    . ALA A 1 3577 ? 160.406 130.264 142.675 1.00 115.56 ? 3577 ALA A CB    1 
ATOM   13400 N N     . ILE A 1 3578 ? 157.352 129.758 143.508 1.00 110.56 ? 3578 ILE A N     1 
ATOM   13401 C CA    . ILE A 1 3578 ? 155.972 129.388 143.207 1.00 110.56 ? 3578 ILE A CA    1 
ATOM   13402 C C     . ILE A 1 3578 ? 155.058 130.585 143.410 1.00 110.56 ? 3578 ILE A C     1 
ATOM   13403 O O     . ILE A 1 3578 ? 154.196 130.886 142.575 1.00 110.56 ? 3578 ILE A O     1 
ATOM   13404 C CB    . ILE A 1 3578 ? 155.533 128.199 144.076 1.00 110.56 ? 3578 ILE A CB    1 
ATOM   13405 C CG1   . ILE A 1 3578 ? 156.012 126.884 143.471 1.00 110.56 ? 3578 ILE A CG1   1 
ATOM   13406 C CG2   . ILE A 1 3578 ? 154.028 128.186 144.242 1.00 110.56 ? 3578 ILE A CG2   1 
ATOM   13407 C CD1   . ILE A 1 3578 ? 155.728 125.696 144.347 1.00 110.56 ? 3578 ILE A CD1   1 
ATOM   13408 N N     . MET A 1 3579 ? 155.243 131.292 144.523 1.00 102.69 ? 3579 MET A N     1 
ATOM   13409 C CA    . MET A 1 3579 ? 154.435 132.478 144.784 1.00 102.69 ? 3579 MET A CA    1 
ATOM   13410 C C     . MET A 1 3579 ? 154.642 133.529 143.701 1.00 102.69 ? 3579 MET A C     1 
ATOM   13411 O O     . MET A 1 3579 ? 153.684 134.169 143.254 1.00 102.69 ? 3579 MET A O     1 
ATOM   13412 C CB    . MET A 1 3579 ? 154.771 133.048 146.160 1.00 102.69 ? 3579 MET A CB    1 
ATOM   13413 C CG    . MET A 1 3579 ? 154.124 132.298 147.305 1.00 102.69 ? 3579 MET A CG    1 
ATOM   13414 S SD    . MET A 1 3579 ? 154.849 132.697 148.902 1.00 102.69 ? 3579 MET A SD    1 
ATOM   13415 C CE    . MET A 1 3579 ? 154.596 134.465 148.948 1.00 102.69 ? 3579 MET A CE    1 
ATOM   13416 N N     . LEU A 1 3580 ? 155.887 133.716 143.265 1.00 111.61 ? 3580 LEU A N     1 
ATOM   13417 C CA    . LEU A 1 3580 ? 156.167 134.699 142.222 1.00 111.61 ? 3580 LEU A CA    1 
ATOM   13418 C C     . LEU A 1 3580 ? 155.498 134.328 140.906 1.00 111.61 ? 3580 LEU A C     1 
ATOM   13419 O O     . LEU A 1 3580 ? 154.997 135.201 140.190 1.00 111.61 ? 3580 LEU A O     1 
ATOM   13420 C CB    . LEU A 1 3580 ? 157.674 134.850 142.021 1.00 111.61 ? 3580 LEU A CB    1 
ATOM   13421 C CG    . LEU A 1 3580 ? 158.493 135.282 143.234 1.00 111.61 ? 3580 LEU A CG    1 
ATOM   13422 C CD1   . LEU A 1 3580 ? 159.888 135.694 142.805 1.00 111.61 ? 3580 LEU A CD1   1 
ATOM   13423 C CD2   . LEU A 1 3580 ? 157.798 136.417 143.960 1.00 111.61 ? 3580 LEU A CD2   1 
ATOM   13424 N N     . LYS A 1 3581 ? 155.496 133.041 140.557 1.00 116.95 ? 3581 LYS A N     1 
ATOM   13425 C CA    . LYS A 1 3581 ? 154.966 132.636 139.259 1.00 116.95 ? 3581 LYS A CA    1 
ATOM   13426 C C     . LYS A 1 3581 ? 153.457 132.838 139.184 1.00 116.95 ? 3581 LYS A C     1 
ATOM   13427 O O     . LYS A 1 3581 ? 152.946 133.408 138.214 1.00 116.95 ? 3581 LYS A O     1 
ATOM   13428 C CB    . LYS A 1 3581 ? 155.329 131.179 138.975 1.00 116.95 ? 3581 LYS A CB    1 
ATOM   13429 C CG    . LYS A 1 3581 ? 155.331 130.819 137.496 1.00 116.95 ? 3581 LYS A CG    1 
ATOM   13430 C CD    . LYS A 1 3581 ? 155.987 131.905 136.658 1.00 116.95 ? 3581 LYS A CD    1 
ATOM   13431 C CE    . LYS A 1 3581 ? 157.498 131.759 136.647 1.00 116.95 ? 3581 LYS A CE    1 
ATOM   13432 N NZ    . LYS A 1 3581 ? 158.123 132.565 135.564 1.00 116.95 ? 3581 LYS A NZ    1 
ATOM   13433 N N     . ARG A 1 3582 ? 152.728 132.382 140.199 1.00 108.05 ? 3582 ARG A N     1 
ATOM   13434 C CA    . ARG A 1 3582 ? 151.270 132.470 140.229 1.00 108.05 ? 3582 ARG A CA    1 
ATOM   13435 C C     . ARG A 1 3582 ? 150.884 133.526 141.255 1.00 108.05 ? 3582 ARG A C     1 
ATOM   13436 O O     . ARG A 1 3582 ? 151.107 133.348 142.455 1.00 108.05 ? 3582 ARG A O     1 
ATOM   13437 C CB    . ARG A 1 3582 ? 150.648 131.119 140.563 1.00 108.05 ? 3582 ARG A CB    1 
ATOM   13438 C CG    . ARG A 1 3582 ? 151.569 129.943 140.323 1.00 108.05 ? 3582 ARG A CG    1 
ATOM   13439 C CD    . ARG A 1 3582 ? 151.006 128.680 140.939 1.00 108.05 ? 3582 ARG A CD    1 
ATOM   13440 N NE    . ARG A 1 3582 ? 149.966 128.091 140.107 1.00 108.05 ? 3582 ARG A NE    1 
ATOM   13441 C CZ    . ARG A 1 3582 ? 150.190 127.195 139.157 1.00 108.05 ? 3582 ARG A CZ    1 
ATOM   13442 N NH1   . ARG A 1 3582 ? 151.409 126.756 138.896 1.00 108.05 ? 3582 ARG A NH1   1 
ATOM   13443 N NH2   . ARG A 1 3582 ? 149.164 126.727 138.451 1.00 108.05 ? 3582 ARG A NH2   1 
ATOM   13444 N N     . PHE A 1 3583 ? 150.302 134.623 140.782 1.00 112.68 ? 3583 PHE A N     1 
ATOM   13445 C CA    . PHE A 1 3583 ? 149.930 135.730 141.646 1.00 112.68 ? 3583 PHE A CA    1 
ATOM   13446 C C     . PHE A 1 3583 ? 148.881 136.586 140.957 1.00 112.68 ? 3583 PHE A C     1 
ATOM   13447 O O     . PHE A 1 3583 ? 148.849 136.687 139.728 1.00 112.68 ? 3583 PHE A O     1 
ATOM   13448 C CB    . PHE A 1 3583 ? 151.142 136.597 141.996 1.00 112.68 ? 3583 PHE A CB    1 
ATOM   13449 C CG    . PHE A 1 3583 ? 151.659 137.403 140.840 1.00 112.68 ? 3583 PHE A CG    1 
ATOM   13450 C CD1   . PHE A 1 3583 ? 152.444 136.816 139.866 1.00 112.68 ? 3583 PHE A CD1   1 
ATOM   13451 C CD2   . PHE A 1 3583 ? 151.357 138.747 140.725 1.00 112.68 ? 3583 PHE A CD2   1 
ATOM   13452 C CE1   . PHE A 1 3583 ? 152.921 137.554 138.801 1.00 112.68 ? 3583 PHE A CE1   1 
ATOM   13453 C CE2   . PHE A 1 3583 ? 151.829 139.489 139.663 1.00 112.68 ? 3583 PHE A CE2   1 
ATOM   13454 C CZ    . PHE A 1 3583 ? 152.612 138.892 138.701 1.00 112.68 ? 3583 PHE A CZ    1 
ATOM   13455 N N     . ASN A 1 3584 ? 148.025 137.208 141.762 1.00 115.56 ? 3584 ASN A N     1 
ATOM   13456 C CA    . ASN A 1 3584 ? 147.095 138.220 141.281 1.00 115.56 ? 3584 ASN A CA    1 
ATOM   13457 C C     . ASN A 1 3584 ? 147.497 139.618 141.723 1.00 115.56 ? 3584 ASN A C     1 
ATOM   13458 O O     . ASN A 1 3584 ? 147.601 140.524 140.892 1.00 115.56 ? 3584 ASN A O     1 
ATOM   13459 C CB    . ASN A 1 3584 ? 145.672 137.911 141.760 1.00 115.56 ? 3584 ASN A CB    1 
ATOM   13460 C CG    . ASN A 1 3584 ? 145.234 136.510 141.405 1.00 115.56 ? 3584 ASN A CG    1 
ATOM   13461 O OD1   . ASN A 1 3584 ? 145.526 135.558 142.124 1.00 115.56 ? 3584 ASN A OD1   1 
ATOM   13462 N ND2   . ASN A 1 3584 ? 144.533 136.375 140.287 1.00 115.56 ? 3584 ASN A ND2   1 
ATOM   13463 N N     . ARG A 1 3585 ? 147.724 139.815 143.017 1.00 112.74 ? 3585 ARG A N     1 
ATOM   13464 C CA    . ARG A 1 3585 ? 148.315 141.047 143.510 1.00 112.74 ? 3585 ARG A CA    1 
ATOM   13465 C C     . ARG A 1 3585 ? 149.813 141.014 143.265 1.00 112.74 ? 3585 ARG A C     1 
ATOM   13466 O O     . ARG A 1 3585 ? 150.461 139.980 143.447 1.00 112.74 ? 3585 ARG A O     1 
ATOM   13467 C CB    . ARG A 1 3585 ? 148.031 141.238 144.999 1.00 112.74 ? 3585 ARG A CB    1 
ATOM   13468 C CG    . ARG A 1 3585 ? 146.567 141.432 145.322 1.00 112.74 ? 3585 ARG A CG    1 
ATOM   13469 C CD    . ARG A 1 3585 ? 146.335 141.497 146.818 1.00 112.74 ? 3585 ARG A CD    1 
ATOM   13470 N NE    . ARG A 1 3585 ? 146.662 140.244 147.485 1.00 112.74 ? 3585 ARG A NE    1 
ATOM   13471 C CZ    . ARG A 1 3585 ? 147.347 140.157 148.616 1.00 112.74 ? 3585 ARG A CZ    1 
ATOM   13472 N NH1   . ARG A 1 3585 ? 147.806 141.234 149.231 1.00 112.74 ? 3585 ARG A NH1   1 
ATOM   13473 N NH2   . ARG A 1 3585 ? 147.574 138.959 149.146 1.00 112.74 ? 3585 ARG A NH2   1 
ATOM   13474 N N     . TYR A 1 3586 ? 150.354 142.144 142.843 1.00 125.70 ? 3586 TYR A N     1 
ATOM   13475 C CA    . TYR A 1 3586 ? 151.762 142.207 142.491 1.00 125.70 ? 3586 TYR A CA    1 
ATOM   13476 C C     . TYR A 1 3586 ? 152.614 141.942 143.727 1.00 125.70 ? 3586 TYR A C     1 
ATOM   13477 O O     . TYR A 1 3586 ? 152.272 142.413 144.816 1.00 125.70 ? 3586 TYR A O     1 
ATOM   13478 C CB    . TYR A 1 3586 ? 152.082 143.571 141.897 1.00 125.70 ? 3586 TYR A CB    1 
ATOM   13479 C CG    . TYR A 1 3586 ? 151.598 143.709 140.479 1.00 125.70 ? 3586 TYR A CG    1 
ATOM   13480 C CD1   . TYR A 1 3586 ? 152.101 142.897 139.476 1.00 125.70 ? 3586 TYR A CD1   1 
ATOM   13481 C CD2   . TYR A 1 3586 ? 150.624 144.637 140.145 1.00 125.70 ? 3586 TYR A CD2   1 
ATOM   13482 C CE1   . TYR A 1 3586 ? 151.660 143.013 138.179 1.00 125.70 ? 3586 TYR A CE1   1 
ATOM   13483 C CE2   . TYR A 1 3586 ? 150.179 144.764 138.849 1.00 125.70 ? 3586 TYR A CE2   1 
ATOM   13484 C CZ    . TYR A 1 3586 ? 150.699 143.947 137.869 1.00 125.70 ? 3586 TYR A CZ    1 
ATOM   13485 O OH    . TYR A 1 3586 ? 150.258 144.062 136.572 1.00 125.70 ? 3586 TYR A OH    1 
ATOM   13486 N N     . PRO A 1 3587 ? 153.694 141.177 143.613 1.00 118.94 ? 3587 PRO A N     1 
ATOM   13487 C CA    . PRO A 1 3587 ? 154.486 140.842 144.799 1.00 118.94 ? 3587 PRO A CA    1 
ATOM   13488 C C     . PRO A 1 3587 ? 155.460 141.946 145.172 1.00 118.94 ? 3587 PRO A C     1 
ATOM   13489 O O     . PRO A 1 3587 ? 155.800 142.811 144.362 1.00 118.94 ? 3587 PRO A O     1 
ATOM   13490 C CB    . PRO A 1 3587 ? 155.236 139.571 144.379 1.00 118.94 ? 3587 PRO A CB    1 
ATOM   13491 C CG    . PRO A 1 3587 ? 154.588 139.123 143.100 1.00 118.94 ? 3587 PRO A CG    1 
ATOM   13492 C CD    . PRO A 1 3587 ? 154.086 140.365 142.454 1.00 118.94 ? 3587 PRO A CD    1 
ATOM   13493 N N     . LEU A 1 3588 ? 155.913 141.903 146.425 1.00 123.15 ? 3588 LEU A N     1 
ATOM   13494 C CA    . LEU A 1 3588 ? 157.017 142.728 146.909 1.00 123.15 ? 3588 LEU A CA    1 
ATOM   13495 C C     . LEU A 1 3588 ? 158.089 141.783 147.434 1.00 123.15 ? 3588 LEU A C     1 
ATOM   13496 O O     . LEU A 1 3588 ? 157.808 140.920 148.271 1.00 123.15 ? 3588 LEU A O     1 
ATOM   13497 C CB    . LEU A 1 3588 ? 156.557 143.722 147.980 1.00 123.15 ? 3588 LEU A CB    1 
ATOM   13498 C CG    . LEU A 1 3588 ? 156.427 143.351 149.461 1.00 123.15 ? 3588 LEU A CG    1 
ATOM   13499 C CD1   . LEU A 1 3588 ? 157.726 143.607 150.202 1.00 123.15 ? 3588 LEU A CD1   1 
ATOM   13500 C CD2   . LEU A 1 3588 ? 155.298 144.117 150.113 1.00 123.15 ? 3588 LEU A CD2   1 
ATOM   13501 N N     . ILE A 1 3589 ? 159.307 141.933 146.934 1.00 125.17 ? 3589 ILE A N     1 
ATOM   13502 C CA    . ILE A 1 3589 ? 160.378 140.999 147.256 1.00 125.17 ? 3589 ILE A CA    1 
ATOM   13503 C C     . ILE A 1 3589 ? 161.150 141.502 148.465 1.00 125.17 ? 3589 ILE A C     1 
ATOM   13504 O O     . ILE A 1 3589 ? 161.675 142.620 148.460 1.00 125.17 ? 3589 ILE A O     1 
ATOM   13505 C CB    . ILE A 1 3589 ? 161.306 140.804 146.050 1.00 125.17 ? 3589 ILE A CB    1 
ATOM   13506 C CG1   . ILE A 1 3589 ? 160.543 140.160 144.894 1.00 125.17 ? 3589 ILE A CG1   1 
ATOM   13507 C CG2   . ILE A 1 3589 ? 162.508 139.979 146.447 1.00 125.17 ? 3589 ILE A CG2   1 
ATOM   13508 C CD1   . ILE A 1 3589 ? 161.432 139.625 143.798 1.00 125.17 ? 3589 ILE A CD1   1 
ATOM   13509 N N     . ILE A 1 3590 ? 161.231 140.671 149.500 1.00 123.59 ? 3590 ILE A N     1 
ATOM   13510 C CA    . ILE A 1 3590 ? 162.034 140.951 150.684 1.00 123.59 ? 3590 ILE A CA    1 
ATOM   13511 C C     . ILE A 1 3590 ? 163.189 139.962 150.695 1.00 123.59 ? 3590 ILE A C     1 
ATOM   13512 O O     . ILE A 1 3590 ? 162.970 138.746 150.761 1.00 123.59 ? 3590 ILE A O     1 
ATOM   13513 C CB    . ILE A 1 3590 ? 161.212 140.842 151.976 1.00 123.59 ? 3590 ILE A CB    1 
ATOM   13514 C CG1   . ILE A 1 3590 ? 160.372 142.097 152.185 1.00 123.59 ? 3590 ILE A CG1   1 
ATOM   13515 C CG2   . ILE A 1 3590 ? 162.123 140.644 153.169 1.00 123.59 ? 3590 ILE A CG2   1 
ATOM   13516 C CD1   . ILE A 1 3590 ? 159.431 142.000 153.361 1.00 123.59 ? 3590 ILE A CD1   1 
ATOM   13517 N N     . ASP A 1 3591 ? 164.411 140.477 150.627 1.00 138.75 ? 3591 ASP A N     1 
ATOM   13518 C CA    . ASP A 1 3591 ? 165.585 139.617 150.636 1.00 138.75 ? 3591 ASP A CA    1 
ATOM   13519 C C     . ASP A 1 3591 ? 166.786 140.412 151.127 1.00 138.75 ? 3591 ASP A C     1 
ATOM   13520 O O     . ASP A 1 3591 ? 167.123 141.451 150.545 1.00 138.75 ? 3591 ASP A O     1 
ATOM   13521 C CB    . ASP A 1 3591 ? 165.843 139.044 149.240 1.00 138.75 ? 3591 ASP A CB    1 
ATOM   13522 C CG    . ASP A 1 3591 ? 167.215 138.390 149.106 1.00 138.75 ? 3591 ASP A CG    1 
ATOM   13523 O OD1   . ASP A 1 3591 ? 167.783 137.935 150.122 1.00 138.75 ? 3591 ASP A OD1   1 
ATOM   13524 O OD2   . ASP A 1 3591 ? 167.725 138.321 147.968 1.00 138.75 ? 3591 ASP A OD2   1 
ATOM   13525 N N     . PRO A 1 3592 ? 167.447 139.968 152.198 1.00 138.60 ? 3592 PRO A N     1 
ATOM   13526 C CA    . PRO A 1 3592 ? 168.681 140.646 152.621 1.00 138.60 ? 3592 PRO A CA    1 
ATOM   13527 C C     . PRO A 1 3592 ? 169.749 140.655 151.546 1.00 138.60 ? 3592 PRO A C     1 
ATOM   13528 O O     . PRO A 1 3592 ? 170.476 141.647 151.409 1.00 138.60 ? 3592 PRO A O     1 
ATOM   13529 C CB    . PRO A 1 3592 ? 169.124 139.835 153.848 1.00 138.60 ? 3592 PRO A CB    1 
ATOM   13530 C CG    . PRO A 1 3592 ? 167.898 139.118 154.305 1.00 138.60 ? 3592 PRO A CG    1 
ATOM   13531 C CD    . PRO A 1 3592 ? 167.099 138.840 153.076 1.00 138.60 ? 3592 PRO A CD    1 
ATOM   13532 N N     . SER A 1 3593 ? 169.859 139.584 150.770 1.00 142.75 ? 3593 SER A N     1 
ATOM   13533 C CA    . SER A 1 3593 ? 170.822 139.502 149.690 1.00 142.75 ? 3593 SER A CA    1 
ATOM   13534 C C     . SER A 1 3593 ? 170.207 140.061 148.411 1.00 142.75 ? 3593 SER A C     1 
ATOM   13535 O O     . SER A 1 3593 ? 169.137 140.673 148.417 1.00 142.75 ? 3593 SER A O     1 
ATOM   13536 C CB    . SER A 1 3593 ? 171.284 138.057 149.498 1.00 142.75 ? 3593 SER A CB    1 
ATOM   13537 O OG    . SER A 1 3593 ? 170.175 137.181 149.401 1.00 142.75 ? 3593 SER A OG    1 
ATOM   13538 N N     . GLY A 1 3594 ? 170.909 139.861 147.300 1.00 144.19 ? 3594 GLY A N     1 
ATOM   13539 C CA    . GLY A 1 3594 ? 170.382 140.222 146.001 1.00 144.19 ? 3594 GLY A CA    1 
ATOM   13540 C C     . GLY A 1 3594 ? 169.947 139.007 145.209 1.00 144.19 ? 3594 GLY A C     1 
ATOM   13541 O O     . GLY A 1 3594 ? 169.688 139.100 144.006 1.00 144.19 ? 3594 GLY A O     1 
ATOM   13542 N N     . GLN A 1 3595 ? 169.859 137.860 145.886 1.00 144.18 ? 3595 GLN A N     1 
ATOM   13543 C CA    . GLN A 1 3595 ? 169.604 136.599 145.196 1.00 144.18 ? 3595 GLN A CA    1 
ATOM   13544 C C     . GLN A 1 3595 ? 168.263 136.622 144.474 1.00 144.18 ? 3595 GLN A C     1 
ATOM   13545 O O     . GLN A 1 3595 ? 168.164 136.221 143.309 1.00 144.18 ? 3595 GLN A O     1 
ATOM   13546 C CB    . GLN A 1 3595 ? 169.658 135.444 146.195 1.00 144.18 ? 3595 GLN A CB    1 
ATOM   13547 C CG    . GLN A 1 3595 ? 169.263 134.098 145.616 1.00 144.18 ? 3595 GLN A CG    1 
ATOM   13548 C CD    . GLN A 1 3595 ? 170.353 133.491 144.756 1.00 144.18 ? 3595 GLN A CD    1 
ATOM   13549 O OE1   . GLN A 1 3595 ? 170.081 132.903 143.710 1.00 144.18 ? 3595 GLN A OE1   1 
ATOM   13550 N NE2   . GLN A 1 3595 ? 171.599 133.630 145.194 1.00 144.18 ? 3595 GLN A NE2   1 
ATOM   13551 N N     . ALA A 1 3596 ? 167.216 137.096 145.150 1.00 142.40 ? 3596 ALA A N     1 
ATOM   13552 C CA    . ALA A 1 3596 ? 165.896 137.129 144.530 1.00 142.40 ? 3596 ALA A CA    1 
ATOM   13553 C C     . ALA A 1 3596 ? 165.844 138.134 143.389 1.00 142.40 ? 3596 ALA A C     1 
ATOM   13554 O O     . ALA A 1 3596 ? 165.188 137.891 142.369 1.00 142.40 ? 3596 ALA A O     1 
ATOM   13555 C CB    . ALA A 1 3596 ? 164.833 137.448 145.577 1.00 142.40 ? 3596 ALA A CB    1 
ATOM   13556 N N     . THR A 1 3597 ? 166.506 139.280 143.551 1.00 145.72 ? 3597 THR A N     1 
ATOM   13557 C CA    . THR A 1 3597 ? 166.554 140.252 142.466 1.00 145.72 ? 3597 THR A CA    1 
ATOM   13558 C C     . THR A 1 3597 ? 167.268 139.675 141.255 1.00 145.72 ? 3597 THR A C     1 
ATOM   13559 O O     . THR A 1 3597 ? 166.819 139.853 140.119 1.00 145.72 ? 3597 THR A O     1 
ATOM   13560 C CB    . THR A 1 3597 ? 167.242 141.533 142.932 1.00 145.72 ? 3597 THR A CB    1 
ATOM   13561 O OG1   . THR A 1 3597 ? 168.387 141.198 143.723 1.00 145.72 ? 3597 THR A OG1   1 
ATOM   13562 C CG2   . THR A 1 3597 ? 166.285 142.377 143.763 1.00 145.72 ? 3597 THR A CG2   1 
ATOM   13563 N N     . GLU A 1 3598 ? 168.375 138.965 141.481 1.00 144.92 ? 3598 GLU A N     1 
ATOM   13564 C CA    . GLU A 1 3598 ? 169.060 138.298 140.379 1.00 144.92 ? 3598 GLU A CA    1 
ATOM   13565 C C     . GLU A 1 3598 ? 168.158 137.263 139.721 1.00 144.92 ? 3598 GLU A C     1 
ATOM   13566 O O     . GLU A 1 3598 ? 168.135 137.140 138.491 1.00 144.92 ? 3598 GLU A O     1 
ATOM   13567 C CB    . GLU A 1 3598 ? 170.346 137.643 140.883 1.00 144.92 ? 3598 GLU A CB    1 
ATOM   13568 C CG    . GLU A 1 3598 ? 171.382 138.626 141.394 1.00 144.92 ? 3598 GLU A CG    1 
ATOM   13569 C CD    . GLU A 1 3598 ? 172.450 137.960 142.238 1.00 144.92 ? 3598 GLU A CD    1 
ATOM   13570 O OE1   . GLU A 1 3598 ? 172.857 136.829 141.900 1.00 144.92 ? 3598 GLU A OE1   1 
ATOM   13571 O OE2   . GLU A 1 3598 ? 172.881 138.567 143.240 1.00 144.92 ? 3598 GLU A OE2   1 
ATOM   13572 N N     . PHE A 1 3599 ? 167.412 136.508 140.530 1.00 142.22 ? 3599 PHE A N     1 
ATOM   13573 C CA    . PHE A 1 3599 ? 166.495 135.509 139.994 1.00 142.22 ? 3599 PHE A CA    1 
ATOM   13574 C C     . PHE A 1 3599 ? 165.465 136.161 139.080 1.00 142.22 ? 3599 PHE A C     1 
ATOM   13575 O O     . PHE A 1 3599 ? 165.292 135.743 137.929 1.00 142.22 ? 3599 PHE A O     1 
ATOM   13576 C CB    . PHE A 1 3599 ? 165.809 134.782 141.155 1.00 142.22 ? 3599 PHE A CB    1 
ATOM   13577 C CG    . PHE A 1 3599 ? 164.724 133.812 140.745 1.00 142.22 ? 3599 PHE A CG    1 
ATOM   13578 C CD1   . PHE A 1 3599 ? 164.662 133.280 139.466 1.00 142.22 ? 3599 PHE A CD1   1 
ATOM   13579 C CD2   . PHE A 1 3599 ? 163.736 133.463 141.650 1.00 142.22 ? 3599 PHE A CD2   1 
ATOM   13580 C CE1   . PHE A 1 3599 ? 163.659 132.402 139.112 1.00 142.22 ? 3599 PHE A CE1   1 
ATOM   13581 C CE2   . PHE A 1 3599 ? 162.729 132.591 141.300 1.00 142.22 ? 3599 PHE A CE2   1 
ATOM   13582 C CZ    . PHE A 1 3599 ? 162.690 132.059 140.030 1.00 142.22 ? 3599 PHE A CZ    1 
ATOM   13583 N N     . ILE A 1 3600 ? 164.781 137.195 139.572 1.00 143.02 ? 3600 ILE A N     1 
ATOM   13584 C CA    . ILE A 1 3600 ? 163.758 137.843 138.760 1.00 143.02 ? 3600 ILE A CA    1 
ATOM   13585 C C     . ILE A 1 3600 ? 164.388 138.532 137.559 1.00 143.02 ? 3600 ILE A C     1 
ATOM   13586 O O     . ILE A 1 3600 ? 163.732 138.719 136.527 1.00 143.02 ? 3600 ILE A O     1 
ATOM   13587 C CB    . ILE A 1 3600 ? 162.925 138.819 139.610 1.00 143.02 ? 3600 ILE A CB    1 
ATOM   13588 C CG1   . ILE A 1 3600 ? 161.467 138.808 139.148 1.00 143.02 ? 3600 ILE A CG1   1 
ATOM   13589 C CG2   . ILE A 1 3600 ? 163.486 140.221 139.524 1.00 143.02 ? 3600 ILE A CG2   1 
ATOM   13590 C CD1   . ILE A 1 3600 ? 160.796 137.463 139.304 1.00 143.02 ? 3600 ILE A CD1   1 
ATOM   13591 N N     . MET A 1 3601 ? 165.662 138.918 137.662 1.00 146.34 ? 3601 MET A N     1 
ATOM   13592 C CA    . MET A 1 3601 ? 166.367 139.438 136.499 1.00 146.34 ? 3601 MET A CA    1 
ATOM   13593 C C     . MET A 1 3601 ? 166.489 138.366 135.428 1.00 146.34 ? 3601 MET A C     1 
ATOM   13594 O O     . MET A 1 3601 ? 166.087 138.572 134.279 1.00 146.34 ? 3601 MET A O     1 
ATOM   13595 C CB    . MET A 1 3601 ? 167.750 139.948 136.912 1.00 146.34 ? 3601 MET A CB    1 
ATOM   13596 C CG    . MET A 1 3601 ? 168.505 140.767 135.857 1.00 146.34 ? 3601 MET A CG    1 
ATOM   13597 S SD    . MET A 1 3601 ? 167.584 141.877 134.761 1.00 146.34 ? 3601 MET A SD    1 
ATOM   13598 C CE    . MET A 1 3601 ? 166.538 142.779 135.907 1.00 146.34 ? 3601 MET A CE    1 
ATOM   13599 N N     . ASN A 1 3602 ? 167.010 137.196 135.804 1.00 146.37 ? 3602 ASN A N     1 
ATOM   13600 C CA    . ASN A 1 3602 ? 167.237 136.142 134.819 1.00 146.37 ? 3602 ASN A CA    1 
ATOM   13601 C C     . ASN A 1 3602 ? 165.931 135.586 134.273 1.00 146.37 ? 3602 ASN A C     1 
ATOM   13602 O O     . ASN A 1 3602 ? 165.888 135.124 133.128 1.00 146.37 ? 3602 ASN A O     1 
ATOM   13603 C CB    . ASN A 1 3602 ? 168.074 135.006 135.410 1.00 146.37 ? 3602 ASN A CB    1 
ATOM   13604 C CG    . ASN A 1 3602 ? 169.125 135.492 136.382 1.00 146.37 ? 3602 ASN A CG    1 
ATOM   13605 O OD1   . ASN A 1 3602 ? 169.301 134.917 137.455 1.00 146.37 ? 3602 ASN A OD1   1 
ATOM   13606 N ND2   . ASN A 1 3602 ? 169.833 136.553 136.012 1.00 146.37 ? 3602 ASN A ND2   1 
ATOM   13607 N N     . GLU A 1 3603 ? 164.862 135.619 135.066 1.00 147.55 ? 3603 GLU A N     1 
ATOM   13608 C CA    . GLU A 1 3603 ? 163.615 135.009 134.622 1.00 147.55 ? 3603 GLU A CA    1 
ATOM   13609 C C     . GLU A 1 3603 ? 162.926 135.841 133.548 1.00 147.55 ? 3603 GLU A C     1 
ATOM   13610 O O     . GLU A 1 3603 ? 162.169 135.294 132.738 1.00 147.55 ? 3603 GLU A O     1 
ATOM   13611 C CB    . GLU A 1 3603 ? 162.685 134.795 135.816 1.00 147.55 ? 3603 GLU A CB    1 
ATOM   13612 C CG    . GLU A 1 3603 ? 161.484 133.909 135.523 1.00 147.55 ? 3603 GLU A CG    1 
ATOM   13613 C CD    . GLU A 1 3603 ? 161.775 132.438 135.750 1.00 147.55 ? 3603 GLU A CD    1 
ATOM   13614 O OE1   . GLU A 1 3603 ? 162.931 132.102 136.082 1.00 147.55 ? 3603 GLU A OE1   1 
ATOM   13615 O OE2   . GLU A 1 3603 ? 160.848 131.617 135.595 1.00 147.55 ? 3603 GLU A OE2   1 
ATOM   13616 N N     . TYR A 1 3604 ? 163.173 137.152 133.511 1.00 152.60 ? 3604 TYR A N     1 
ATOM   13617 C CA    . TYR A 1 3604 ? 162.429 138.041 132.625 1.00 152.60 ? 3604 TYR A CA    1 
ATOM   13618 C C     . TYR A 1 3604 ? 163.325 138.807 131.654 1.00 152.60 ? 3604 TYR A C     1 
ATOM   13619 O O     . TYR A 1 3604 ? 162.917 139.858 131.150 1.00 152.60 ? 3604 TYR A O     1 
ATOM   13620 C CB    . TYR A 1 3604 ? 161.582 139.018 133.443 1.00 152.60 ? 3604 TYR A CB    1 
ATOM   13621 C CG    . TYR A 1 3604 ? 160.333 138.404 134.036 1.00 152.60 ? 3604 TYR A CG    1 
ATOM   13622 C CD1   . TYR A 1 3604 ? 160.413 137.399 134.990 1.00 152.60 ? 3604 TYR A CD1   1 
ATOM   13623 C CD2   . TYR A 1 3604 ? 159.073 138.828 133.640 1.00 152.60 ? 3604 TYR A CD2   1 
ATOM   13624 C CE1   . TYR A 1 3604 ? 159.275 136.835 135.533 1.00 152.60 ? 3604 TYR A CE1   1 
ATOM   13625 C CE2   . TYR A 1 3604 ? 157.929 138.269 134.179 1.00 152.60 ? 3604 TYR A CE2   1 
ATOM   13626 C CZ    . TYR A 1 3604 ? 158.037 137.275 135.124 1.00 152.60 ? 3604 TYR A CZ    1 
ATOM   13627 O OH    . TYR A 1 3604 ? 156.902 136.716 135.661 1.00 152.60 ? 3604 TYR A OH    1 
ATOM   13628 N N     . LYS A 1 3605 ? 164.532 138.307 131.371 1.00 154.08 ? 3605 LYS A N     1 
ATOM   13629 C CA    . LYS A 1 3605 ? 165.359 138.945 130.349 1.00 154.08 ? 3605 LYS A CA    1 
ATOM   13630 C C     . LYS A 1 3605 ? 164.657 138.941 128.999 1.00 154.08 ? 3605 LYS A C     1 
ATOM   13631 O O     . LYS A 1 3605 ? 164.732 139.920 128.248 1.00 154.08 ? 3605 LYS A O     1 
ATOM   13632 C CB    . LYS A 1 3605 ? 166.715 138.247 130.233 1.00 154.08 ? 3605 LYS A CB    1 
ATOM   13633 C CG    . LYS A 1 3605 ? 167.353 137.855 131.546 1.00 154.08 ? 3605 LYS A CG    1 
ATOM   13634 C CD    . LYS A 1 3605 ? 168.221 138.985 132.075 1.00 154.08 ? 3605 LYS A CD    1 
ATOM   13635 C CE    . LYS A 1 3605 ? 169.268 138.469 133.045 1.00 154.08 ? 3605 LYS A CE    1 
ATOM   13636 N NZ    . LYS A 1 3605 ? 170.221 137.536 132.388 1.00 154.08 ? 3605 LYS A NZ    1 
ATOM   13637 N N     . ASP A 1 3606 ? 163.969 137.843 128.676 1.00 160.95 ? 3606 ASP A N     1 
ATOM   13638 C CA    . ASP A 1 3606 ? 163.234 137.763 127.419 1.00 160.95 ? 3606 ASP A CA    1 
ATOM   13639 C C     . ASP A 1 3606 ? 162.185 138.860 127.311 1.00 160.95 ? 3606 ASP A C     1 
ATOM   13640 O O     . ASP A 1 3606 ? 161.907 139.348 126.209 1.00 160.95 ? 3606 ASP A O     1 
ATOM   13641 C CB    . ASP A 1 3606 ? 162.581 136.387 127.290 1.00 160.95 ? 3606 ASP A CB    1 
ATOM   13642 C CG    . ASP A 1 3606 ? 161.906 135.942 128.574 1.00 160.95 ? 3606 ASP A CG    1 
ATOM   13643 O OD1   . ASP A 1 3606 ? 162.592 135.879 129.616 1.00 160.95 ? 3606 ASP A OD1   1 
ATOM   13644 O OD2   . ASP A 1 3606 ? 160.691 135.656 128.542 1.00 160.95 ? 3606 ASP A OD2   1 
ATOM   13645 N N     . ARG A 1 3607 ? 161.602 139.265 128.434 1.00 161.00 ? 3607 ARG A N     1 
ATOM   13646 C CA    . ARG A 1 3607 ? 160.605 140.324 128.457 1.00 161.00 ? 3607 ARG A CA    1 
ATOM   13647 C C     . ARG A 1 3607 ? 161.218 141.708 128.629 1.00 161.00 ? 3607 ARG A C     1 
ATOM   13648 O O     . ARG A 1 3607 ? 160.475 142.692 128.702 1.00 161.00 ? 3607 ARG A O     1 
ATOM   13649 C CB    . ARG A 1 3607 ? 159.591 140.060 129.574 1.00 161.00 ? 3607 ARG A CB    1 
ATOM   13650 C CG    . ARG A 1 3607 ? 159.244 138.592 129.753 1.00 161.00 ? 3607 ARG A CG    1 
ATOM   13651 C CD    . ARG A 1 3607 ? 158.013 138.219 128.948 1.00 161.00 ? 3607 ARG A CD    1 
ATOM   13652 N NE    . ARG A 1 3607 ? 156.896 139.116 129.219 1.00 161.00 ? 3607 ARG A NE    1 
ATOM   13653 C CZ    . ARG A 1 3607 ? 156.094 139.018 130.270 1.00 161.00 ? 3607 ARG A CZ    1 
ATOM   13654 N NH1   . ARG A 1 3607 ? 156.245 138.058 131.169 1.00 161.00 ? 3607 ARG A NH1   1 
ATOM   13655 N NH2   . ARG A 1 3607 ? 155.112 139.902 130.422 1.00 161.00 ? 3607 ARG A NH2   1 
ATOM   13656 N N     . LYS A 1 3608 ? 162.549 141.802 128.690 1.00 160.80 ? 3608 LYS A N     1 
ATOM   13657 C CA    . LYS A 1 3608 ? 163.264 143.071 128.833 1.00 160.80 ? 3608 LYS A CA    1 
ATOM   13658 C C     . LYS A 1 3608 ? 162.879 143.776 130.136 1.00 160.80 ? 3608 LYS A C     1 
ATOM   13659 O O     . LYS A 1 3608 ? 162.346 144.888 130.148 1.00 160.80 ? 3608 LYS A O     1 
ATOM   13660 C CB    . LYS A 1 3608 ? 163.027 143.977 127.620 1.00 160.80 ? 3608 LYS A CB    1 
ATOM   13661 C CG    . LYS A 1 3608 ? 163.560 143.411 126.312 1.00 160.80 ? 3608 LYS A CG    1 
ATOM   13662 C CD    . LYS A 1 3608 ? 162.958 144.126 125.112 1.00 160.80 ? 3608 LYS A CD    1 
ATOM   13663 C CE    . LYS A 1 3608 ? 161.448 144.247 125.235 1.00 160.80 ? 3608 LYS A CE    1 
ATOM   13664 N NZ    . LYS A 1 3608 ? 160.927 145.443 124.516 1.00 160.80 ? 3608 LYS A NZ    1 
ATOM   13665 N N     . ILE A 1 3609 ? 163.164 143.096 131.246 1.00 157.82 ? 3609 ILE A N     1 
ATOM   13666 C CA    . ILE A 1 3609 ? 162.886 143.647 132.566 1.00 157.82 ? 3609 ILE A CA    1 
ATOM   13667 C C     . ILE A 1 3609 ? 163.853 144.788 132.848 1.00 157.82 ? 3609 ILE A C     1 
ATOM   13668 O O     . ILE A 1 3609 ? 165.070 144.654 132.663 1.00 157.82 ? 3609 ILE A O     1 
ATOM   13669 C CB    . ILE A 1 3609 ? 162.987 142.547 133.633 1.00 157.82 ? 3609 ILE A CB    1 
ATOM   13670 C CG1   . ILE A 1 3609 ? 163.029 143.154 135.035 1.00 157.82 ? 3609 ILE A CG1   1 
ATOM   13671 C CG2   . ILE A 1 3609 ? 164.213 141.681 133.392 1.00 157.82 ? 3609 ILE A CG2   1 
ATOM   13672 C CD1   . ILE A 1 3609 ? 161.733 143.784 135.456 1.00 157.82 ? 3609 ILE A CD1   1 
ATOM   13673 N N     . THR A 1 3610 ? 163.318 145.920 133.293 1.00 157.65 ? 3610 THR A N     1 
ATOM   13674 C CA    . THR A 1 3610 ? 164.110 147.114 133.550 1.00 157.65 ? 3610 THR A CA    1 
ATOM   13675 C C     . THR A 1 3610 ? 164.191 147.382 135.047 1.00 157.65 ? 3610 THR A C     1 
ATOM   13676 O O     . THR A 1 3610 ? 163.177 147.348 135.751 1.00 157.65 ? 3610 THR A O     1 
ATOM   13677 C CB    . THR A 1 3610 ? 163.517 148.330 132.837 1.00 157.65 ? 3610 THR A CB    1 
ATOM   13678 O OG1   . THR A 1 3610 ? 163.270 148.005 131.464 1.00 157.65 ? 3610 THR A OG1   1 
ATOM   13679 C CG2   . THR A 1 3610 ? 164.473 149.511 132.911 1.00 157.65 ? 3610 THR A CG2   1 
ATOM   13680 N N     . ARG A 1 3611 ? 165.402 147.651 135.524 1.00 153.62 ? 3611 ARG A N     1 
ATOM   13681 C CA    . ARG A 1 3611 ? 165.638 147.950 136.929 1.00 153.62 ? 3611 ARG A CA    1 
ATOM   13682 C C     . ARG A 1 3611 ? 165.302 149.408 137.209 1.00 153.62 ? 3611 ARG A C     1 
ATOM   13683 O O     . ARG A 1 3611 ? 165.588 150.287 136.390 1.00 153.62 ? 3611 ARG A O     1 
ATOM   13684 C CB    . ARG A 1 3611 ? 167.090 147.655 137.304 1.00 153.62 ? 3611 ARG A CB    1 
ATOM   13685 C CG    . ARG A 1 3611 ? 167.340 146.213 137.710 1.00 153.62 ? 3611 ARG A CG    1 
ATOM   13686 C CD    . ARG A 1 3611 ? 168.472 146.109 138.718 1.00 153.62 ? 3611 ARG A CD    1 
ATOM   13687 N NE    . ARG A 1 3611 ? 168.587 144.765 139.268 1.00 153.62 ? 3611 ARG A NE    1 
ATOM   13688 C CZ    . ARG A 1 3611 ? 169.487 144.400 140.171 1.00 153.62 ? 3611 ARG A CZ    1 
ATOM   13689 N NH1   . ARG A 1 3611 ? 170.373 145.257 140.648 1.00 153.62 ? 3611 ARG A NH1   1 
ATOM   13690 N NH2   . ARG A 1 3611 ? 169.499 143.143 140.604 1.00 153.62 ? 3611 ARG A NH2   1 
ATOM   13691 N N     . THR A 1 3612 ? 164.692 149.659 138.365 1.00 158.42 ? 3612 THR A N     1 
ATOM   13692 C CA    . THR A 1 3612 ? 164.233 150.992 138.726 1.00 158.42 ? 3612 THR A CA    1 
ATOM   13693 C C     . THR A 1 3612 ? 164.184 151.067 140.248 1.00 158.42 ? 3612 THR A C     1 
ATOM   13694 O O     . THR A 1 3612 ? 164.132 150.044 140.935 1.00 158.42 ? 3612 THR A O     1 
ATOM   13695 C CB    . THR A 1 3612 ? 162.871 151.282 138.065 1.00 158.42 ? 3612 THR A CB    1 
ATOM   13696 O OG1   . THR A 1 3612 ? 163.060 151.458 136.656 1.00 158.42 ? 3612 THR A OG1   1 
ATOM   13697 C CG2   . THR A 1 3612 ? 162.211 152.539 138.618 1.00 158.42 ? 3612 THR A CG2   1 
ATOM   13698 N N     . SER A 1 3613 ? 164.246 152.287 140.780 1.00 160.08 ? 3613 SER A N     1 
ATOM   13699 C CA    . SER A 1 3613 ? 164.103 152.500 142.212 1.00 160.08 ? 3613 SER A CA    1 
ATOM   13700 C C     . SER A 1 3613 ? 163.158 153.669 142.451 1.00 160.08 ? 3613 SER A C     1 
ATOM   13701 O O     . SER A 1 3613 ? 163.007 154.554 141.605 1.00 160.08 ? 3613 SER A O     1 
ATOM   13702 C CB    . SER A 1 3613 ? 165.455 152.759 142.881 1.00 160.08 ? 3613 SER A CB    1 
ATOM   13703 O OG    . SER A 1 3613 ? 165.799 154.129 142.799 1.00 160.08 ? 3613 SER A OG    1 
ATOM   13704 N N     . PHE A 1 3614 ? 162.516 153.657 143.623 1.00 158.96 ? 3614 PHE A N     1 
ATOM   13705 C CA    . PHE A 1 3614 ? 161.590 154.731 143.972 1.00 158.96 ? 3614 PHE A CA    1 
ATOM   13706 C C     . PHE A 1 3614 ? 162.293 156.075 144.098 1.00 158.96 ? 3614 PHE A C     1 
ATOM   13707 O O     . PHE A 1 3614 ? 161.745 157.098 143.675 1.00 158.96 ? 3614 PHE A O     1 
ATOM   13708 C CB    . PHE A 1 3614 ? 160.857 154.403 145.272 1.00 158.96 ? 3614 PHE A CB    1 
ATOM   13709 C CG    . PHE A 1 3614 ? 159.562 153.672 145.073 1.00 158.96 ? 3614 PHE A CG    1 
ATOM   13710 C CD1   . PHE A 1 3614 ? 158.640 154.111 144.139 1.00 158.96 ? 3614 PHE A CD1   1 
ATOM   13711 C CD2   . PHE A 1 3614 ? 159.257 152.556 145.831 1.00 158.96 ? 3614 PHE A CD2   1 
ATOM   13712 C CE1   . PHE A 1 3614 ? 157.445 153.444 143.959 1.00 158.96 ? 3614 PHE A CE1   1 
ATOM   13713 C CE2   . PHE A 1 3614 ? 158.063 151.887 145.654 1.00 158.96 ? 3614 PHE A CE2   1 
ATOM   13714 C CZ    . PHE A 1 3614 ? 157.157 152.331 144.717 1.00 158.96 ? 3614 PHE A CZ    1 
ATOM   13715 N N     . LEU A 1 3615 ? 163.493 156.100 144.680 1.00 168.61 ? 3615 LEU A N     1 
ATOM   13716 C CA    . LEU A 1 3615 ? 164.198 157.360 144.877 1.00 168.61 ? 3615 LEU A CA    1 
ATOM   13717 C C     . LEU A 1 3615 ? 164.635 158.004 143.568 1.00 168.61 ? 3615 LEU A C     1 
ATOM   13718 O O     . LEU A 1 3615 ? 164.908 159.209 143.548 1.00 168.61 ? 3615 LEU A O     1 
ATOM   13719 C CB    . LEU A 1 3615 ? 165.411 157.148 145.790 1.00 168.61 ? 3615 LEU A CB    1 
ATOM   13720 C CG    . LEU A 1 3615 ? 166.400 156.014 145.501 1.00 168.61 ? 3615 LEU A CG    1 
ATOM   13721 C CD1   . LEU A 1 3615 ? 167.400 156.386 144.411 1.00 168.61 ? 3615 LEU A CD1   1 
ATOM   13722 C CD2   . LEU A 1 3615 ? 167.124 155.604 146.775 1.00 168.61 ? 3615 LEU A CD2   1 
ATOM   13723 N N     . ASP A 1 3616 ? 164.706 157.237 142.483 1.00 176.00 ? 3616 ASP A N     1 
ATOM   13724 C CA    . ASP A 1 3616 ? 165.122 157.788 141.202 1.00 176.00 ? 3616 ASP A CA    1 
ATOM   13725 C C     . ASP A 1 3616 ? 164.077 158.762 140.671 1.00 176.00 ? 3616 ASP A C     1 
ATOM   13726 O O     . ASP A 1 3616 ? 162.871 158.519 140.764 1.00 176.00 ? 3616 ASP A O     1 
ATOM   13727 C CB    . ASP A 1 3616 ? 165.356 156.664 140.193 1.00 176.00 ? 3616 ASP A CB    1 
ATOM   13728 C CG    . ASP A 1 3616 ? 166.214 157.101 139.021 1.00 176.00 ? 3616 ASP A CG    1 
ATOM   13729 O OD1   . ASP A 1 3616 ? 165.780 157.993 138.263 1.00 176.00 ? 3616 ASP A OD1   1 
ATOM   13730 O OD2   . ASP A 1 3616 ? 167.324 156.553 138.858 1.00 176.00 ? 3616 ASP A OD2   1 
ATOM   13731 N N     . ASP A 1 3617 ? 164.551 159.877 140.113 1.00 186.53 ? 3617 ASP A N     1 
ATOM   13732 C CA    . ASP A 1 3617 ? 163.649 160.877 139.555 1.00 186.53 ? 3617 ASP A CA    1 
ATOM   13733 C C     . ASP A 1 3617 ? 163.028 160.419 138.242 1.00 186.53 ? 3617 ASP A C     1 
ATOM   13734 O O     . ASP A 1 3617 ? 161.888 160.788 137.938 1.00 186.53 ? 3617 ASP A O     1 
ATOM   13735 C CB    . ASP A 1 3617 ? 164.391 162.197 139.349 1.00 186.53 ? 3617 ASP A CB    1 
ATOM   13736 C CG    . ASP A 1 3617 ? 164.868 162.804 140.653 1.00 186.53 ? 3617 ASP A CG    1 
ATOM   13737 O OD1   . ASP A 1 3617 ? 164.014 163.184 141.481 1.00 186.53 ? 3617 ASP A OD1   1 
ATOM   13738 O OD2   . ASP A 1 3617 ? 166.098 162.900 140.850 1.00 186.53 ? 3617 ASP A OD2   1 
ATOM   13739 N N     . ALA A 1 3618 ? 163.751 159.622 137.461 1.00 178.30 ? 3618 ALA A N     1 
ATOM   13740 C CA    . ALA A 1 3618 ? 163.249 159.097 136.199 1.00 178.30 ? 3618 ALA A CA    1 
ATOM   13741 C C     . ALA A 1 3618 ? 162.322 157.905 136.386 1.00 178.30 ? 3618 ALA A C     1 
ATOM   13742 O O     . ALA A 1 3618 ? 161.924 157.285 135.395 1.00 178.30 ? 3618 ALA A O     1 
ATOM   13743 C CB    . ALA A 1 3618 ? 164.418 158.706 135.293 1.00 178.30 ? 3618 ALA A CB    1 
ATOM   13744 N N     . PHE A 1 3619 ? 161.984 157.575 137.633 1.00 173.03 ? 3619 PHE A N     1 
ATOM   13745 C CA    . PHE A 1 3619 ? 161.147 156.413 137.904 1.00 173.03 ? 3619 PHE A CA    1 
ATOM   13746 C C     . PHE A 1 3619 ? 159.760 156.576 137.296 1.00 173.03 ? 3619 PHE A C     1 
ATOM   13747 O O     . PHE A 1 3619 ? 159.182 155.610 136.781 1.00 173.03 ? 3619 PHE A O     1 
ATOM   13748 C CB    . PHE A 1 3619 ? 161.079 156.187 139.415 1.00 173.03 ? 3619 PHE A CB    1 
ATOM   13749 C CG    . PHE A 1 3619 ? 159.732 155.767 139.922 1.00 173.03 ? 3619 PHE A CG    1 
ATOM   13750 C CD1   . PHE A 1 3619 ? 159.326 154.447 139.839 1.00 173.03 ? 3619 PHE A CD1   1 
ATOM   13751 C CD2   . PHE A 1 3619 ? 158.883 156.689 140.510 1.00 173.03 ? 3619 PHE A CD2   1 
ATOM   13752 C CE1   . PHE A 1 3619 ? 158.091 154.059 140.320 1.00 173.03 ? 3619 PHE A CE1   1 
ATOM   13753 C CE2   . PHE A 1 3619 ? 157.646 156.307 140.991 1.00 173.03 ? 3619 PHE A CE2   1 
ATOM   13754 C CZ    . PHE A 1 3619 ? 157.251 154.991 140.899 1.00 173.03 ? 3619 PHE A CZ    1 
ATOM   13755 N N     . ARG A 1 3620 ? 159.215 157.794 137.331 1.00 176.42 ? 3620 ARG A N     1 
ATOM   13756 C CA    . ARG A 1 3620 ? 157.898 158.028 136.750 1.00 176.42 ? 3620 ARG A CA    1 
ATOM   13757 C C     . ARG A 1 3620 ? 157.901 157.773 135.247 1.00 176.42 ? 3620 ARG A C     1 
ATOM   13758 O O     . ARG A 1 3620 ? 157.042 157.046 134.729 1.00 176.42 ? 3620 ARG A O     1 
ATOM   13759 C CB    . ARG A 1 3620 ? 157.433 159.452 137.052 1.00 176.42 ? 3620 ARG A CB    1 
ATOM   13760 C CG    . ARG A 1 3620 ? 156.253 159.909 136.211 1.00 176.42 ? 3620 ARG A CG    1 
ATOM   13761 C CD    . ARG A 1 3620 ? 154.977 159.204 136.645 1.00 176.42 ? 3620 ARG A CD    1 
ATOM   13762 N NE    . ARG A 1 3620 ? 153.775 159.914 136.224 1.00 176.42 ? 3620 ARG A NE    1 
ATOM   13763 C CZ    . ARG A 1 3620 ? 153.235 160.929 136.884 1.00 176.42 ? 3620 ARG A CZ    1 
ATOM   13764 N NH1   . ARG A 1 3620 ? 153.769 161.388 138.004 1.00 176.42 ? 3620 ARG A NH1   1 
ATOM   13765 N NH2   . ARG A 1 3620 ? 152.130 161.497 136.409 1.00 176.42 ? 3620 ARG A NH2   1 
ATOM   13766 N N     . LYS A 1 3621 ? 158.866 158.350 134.530 1.00 178.25 ? 3621 LYS A N     1 
ATOM   13767 C CA    . LYS A 1 3621 ? 158.913 158.148 133.087 1.00 178.25 ? 3621 LYS A CA    1 
ATOM   13768 C C     . LYS A 1 3621 ? 159.230 156.697 132.748 1.00 178.25 ? 3621 LYS A C     1 
ATOM   13769 O O     . LYS A 1 3621 ? 158.726 156.162 131.753 1.00 178.25 ? 3621 LYS A O     1 
ATOM   13770 C CB    . LYS A 1 3621 ? 159.924 159.104 132.449 1.00 178.25 ? 3621 LYS A CB    1 
ATOM   13771 C CG    . LYS A 1 3621 ? 161.385 158.751 132.664 1.00 178.25 ? 3621 LYS A CG    1 
ATOM   13772 C CD    . LYS A 1 3621 ? 162.276 159.499 131.685 1.00 178.25 ? 3621 LYS A CD    1 
ATOM   13773 C CE    . LYS A 1 3621 ? 163.726 159.065 131.813 1.00 178.25 ? 3621 LYS A CE    1 
ATOM   13774 N NZ    . LYS A 1 3621 ? 164.664 160.060 131.223 1.00 178.25 ? 3621 LYS A NZ    1 
ATOM   13775 N N     . ASN A 1 3622 ? 160.041 156.032 133.577 1.00 174.30 ? 3622 ASN A N     1 
ATOM   13776 C CA    . ASN A 1 3622 ? 160.323 154.620 133.345 1.00 174.30 ? 3622 ASN A CA    1 
ATOM   13777 C C     . ASN A 1 3622 ? 159.061 153.778 133.468 1.00 174.30 ? 3622 ASN A C     1 
ATOM   13778 O O     . ASN A 1 3622 ? 158.796 152.918 132.617 1.00 174.30 ? 3622 ASN A O     1 
ATOM   13779 C CB    . ASN A 1 3622 ? 161.392 154.123 134.319 1.00 174.30 ? 3622 ASN A CB    1 
ATOM   13780 C CG    . ASN A 1 3622 ? 162.769 154.662 133.995 1.00 174.30 ? 3622 ASN A CG    1 
ATOM   13781 O OD1   . ASN A 1 3622 ? 163.508 155.087 134.883 1.00 174.30 ? 3622 ASN A OD1   1 
ATOM   13782 N ND2   . ASN A 1 3622 ? 163.123 154.644 132.715 1.00 174.30 ? 3622 ASN A ND2   1 
ATOM   13783 N N     . LEU A 1 3623 ? 158.263 154.013 134.513 1.00 174.85 ? 3623 LEU A N     1 
ATOM   13784 C CA    . LEU A 1 3623 ? 157.050 153.220 134.663 1.00 174.85 ? 3623 LEU A CA    1 
ATOM   13785 C C     . LEU A 1 3623 ? 156.063 153.531 133.549 1.00 174.85 ? 3623 LEU A C     1 
ATOM   13786 O O     . LEU A 1 3623 ? 155.378 152.630 133.058 1.00 174.85 ? 3623 LEU A O     1 
ATOM   13787 C CB    . LEU A 1 3623 ? 156.399 153.440 136.031 1.00 174.85 ? 3623 LEU A CB    1 
ATOM   13788 C CG    . LEU A 1 3623 ? 155.674 154.743 136.353 1.00 174.85 ? 3623 LEU A CG    1 
ATOM   13789 C CD1   . LEU A 1 3623 ? 154.180 154.515 136.277 1.00 174.85 ? 3623 LEU A CD1   1 
ATOM   13790 C CD2   . LEU A 1 3623 ? 156.043 155.221 137.728 1.00 174.85 ? 3623 LEU A CD2   1 
ATOM   13791 N N     . GLU A 1 3624 ? 155.980 154.797 133.129 1.00 181.56 ? 3624 GLU A N     1 
ATOM   13792 C CA    . GLU A 1 3624 ? 155.071 155.139 132.038 1.00 181.56 ? 3624 GLU A CA    1 
ATOM   13793 C C     . GLU A 1 3624 ? 155.480 154.449 130.741 1.00 181.56 ? 3624 GLU A C     1 
ATOM   13794 O O     . GLU A 1 3624 ? 154.635 153.882 130.035 1.00 181.56 ? 3624 GLU A O     1 
ATOM   13795 C CB    . GLU A 1 3624 ? 155.019 156.656 131.852 1.00 181.56 ? 3624 GLU A CB    1 
ATOM   13796 C CG    . GLU A 1 3624 ? 154.456 157.406 133.050 1.00 181.56 ? 3624 GLU A CG    1 
ATOM   13797 C CD    . GLU A 1 3624 ? 152.954 157.582 132.982 1.00 181.56 ? 3624 GLU A CD    1 
ATOM   13798 O OE1   . GLU A 1 3624 ? 152.246 156.570 132.803 1.00 181.56 ? 3624 GLU A OE1   1 
ATOM   13799 O OE2   . GLU A 1 3624 ? 152.481 158.730 133.115 1.00 181.56 ? 3624 GLU A OE2   1 
ATOM   13800 N N     . SER A 1 3625 ? 156.776 154.473 130.418 1.00 178.40 ? 3625 SER A N     1 
ATOM   13801 C CA    . SER A 1 3625 ? 157.244 153.807 129.208 1.00 178.40 ? 3625 SER A CA    1 
ATOM   13802 C C     . SER A 1 3625 ? 156.996 152.306 129.274 1.00 178.40 ? 3625 SER A C     1 
ATOM   13803 O O     . SER A 1 3625 ? 156.509 151.711 128.307 1.00 178.40 ? 3625 SER A O     1 
ATOM   13804 C CB    . SER A 1 3625 ? 158.728 154.097 128.988 1.00 178.40 ? 3625 SER A CB    1 
ATOM   13805 O OG    . SER A 1 3625 ? 158.951 155.480 128.777 1.00 178.40 ? 3625 SER A OG    1 
ATOM   13806 N N     . ALA A 1 3626 ? 157.304 151.680 130.413 1.00 175.72 ? 3626 ALA A N     1 
ATOM   13807 C CA    . ALA A 1 3626 ? 157.082 150.244 130.541 1.00 175.72 ? 3626 ALA A CA    1 
ATOM   13808 C C     . ALA A 1 3626 ? 155.603 149.902 130.431 1.00 175.72 ? 3626 ALA A C     1 
ATOM   13809 O O     . ALA A 1 3626 ? 155.236 148.898 129.812 1.00 175.72 ? 3626 ALA A O     1 
ATOM   13810 C CB    . ALA A 1 3626 ? 157.652 149.743 131.864 1.00 175.72 ? 3626 ALA A CB    1 
ATOM   13811 N N     . LEU A 1 3627 ? 154.741 150.726 131.029 1.00 177.19 ? 3627 LEU A N     1 
ATOM   13812 C CA    . LEU A 1 3627 ? 153.303 150.547 130.908 1.00 177.19 ? 3627 LEU A CA    1 
ATOM   13813 C C     . LEU A 1 3627 ? 152.829 150.687 129.471 1.00 177.19 ? 3627 LEU A C     1 
ATOM   13814 O O     . LEU A 1 3627 ? 151.861 150.025 129.081 1.00 177.19 ? 3627 LEU A O     1 
ATOM   13815 C CB    . LEU A 1 3627 ? 152.592 151.563 131.799 1.00 177.19 ? 3627 LEU A CB    1 
ATOM   13816 C CG    . LEU A 1 3627 ? 151.069 151.559 131.872 1.00 177.19 ? 3627 LEU A CG    1 
ATOM   13817 C CD1   . LEU A 1 3627 ? 150.539 150.163 132.137 1.00 177.19 ? 3627 LEU A CD1   1 
ATOM   13818 C CD2   . LEU A 1 3627 ? 150.628 152.523 132.954 1.00 177.19 ? 3627 LEU A CD2   1 
ATOM   13819 N N     . ARG A 1 3628 ? 153.483 151.534 128.678 1.00 175.44 ? 3628 ARG A N     1 
ATOM   13820 C CA    . ARG A 1 3628 ? 153.107 151.661 127.276 1.00 175.44 ? 3628 ARG A CA    1 
ATOM   13821 C C     . ARG A 1 3628 ? 153.362 150.383 126.486 1.00 175.44 ? 3628 ARG A C     1 
ATOM   13822 O O     . ARG A 1 3628 ? 152.495 149.949 125.721 1.00 175.44 ? 3628 ARG A O     1 
ATOM   13823 C CB    . ARG A 1 3628 ? 153.853 152.830 126.631 1.00 175.44 ? 3628 ARG A CB    1 
ATOM   13824 C CG    . ARG A 1 3628 ? 153.613 152.951 125.137 1.00 175.44 ? 3628 ARG A CG    1 
ATOM   13825 C CD    . ARG A 1 3628 ? 152.265 153.587 124.853 1.00 175.44 ? 3628 ARG A CD    1 
ATOM   13826 N NE    . ARG A 1 3628 ? 151.916 154.593 125.847 1.00 175.44 ? 3628 ARG A NE    1 
ATOM   13827 C CZ    . ARG A 1 3628 ? 150.678 154.985 126.111 1.00 175.44 ? 3628 ARG A CZ    1 
ATOM   13828 N NH1   . ARG A 1 3628 ? 149.639 154.467 125.476 1.00 175.44 ? 3628 ARG A NH1   1 
ATOM   13829 N NH2   . ARG A 1 3628 ? 150.476 155.920 127.034 1.00 175.44 ? 3628 ARG A NH2   1 
ATOM   13830 N N     . PHE A 1 3629 ? 154.527 149.761 126.662 1.00 173.58 ? 3629 PHE A N     1 
ATOM   13831 C CA    . PHE A 1 3629 ? 154.878 148.546 125.938 1.00 173.58 ? 3629 PHE A CA    1 
ATOM   13832 C C     . PHE A 1 3629 ? 154.603 147.283 126.743 1.00 173.58 ? 3629 PHE A C     1 
ATOM   13833 O O     . PHE A 1 3629 ? 154.931 146.185 126.284 1.00 173.58 ? 3629 PHE A O     1 
ATOM   13834 C CB    . PHE A 1 3629 ? 156.350 148.576 125.518 1.00 173.58 ? 3629 PHE A CB    1 
ATOM   13835 C CG    . PHE A 1 3629 ? 156.904 149.959 125.320 1.00 173.58 ? 3629 PHE A CG    1 
ATOM   13836 C CD1   . PHE A 1 3629 ? 158.006 150.384 126.042 1.00 173.58 ? 3629 PHE A CD1   1 
ATOM   13837 C CD2   . PHE A 1 3629 ? 156.339 150.826 124.398 1.00 173.58 ? 3629 PHE A CD2   1 
ATOM   13838 C CE1   . PHE A 1 3629 ? 158.524 151.652 125.864 1.00 173.58 ? 3629 PHE A CE1   1 
ATOM   13839 C CE2   . PHE A 1 3629 ? 156.853 152.095 124.215 1.00 173.58 ? 3629 PHE A CE2   1 
ATOM   13840 C CZ    . PHE A 1 3629 ? 157.947 152.508 124.949 1.00 173.58 ? 3629 PHE A CZ    1 
ATOM   13841 N N     . GLY A 1 3630 ? 154.009 147.412 127.926 1.00 169.93 ? 3630 GLY A N     1 
ATOM   13842 C CA    . GLY A 1 3630 ? 153.809 146.258 128.785 1.00 169.93 ? 3630 GLY A CA    1 
ATOM   13843 C C     . GLY A 1 3630 ? 155.100 145.643 129.269 1.00 169.93 ? 3630 GLY A C     1 
ATOM   13844 O O     . GLY A 1 3630 ? 155.171 144.423 129.452 1.00 169.93 ? 3630 GLY A O     1 
ATOM   13845 N N     . ASN A 1 3631 ? 156.122 146.454 129.483 1.00 166.44 ? 3631 ASN A N     1 
ATOM   13846 C CA    . ASN A 1 3631 ? 157.427 145.963 129.903 1.00 166.44 ? 3631 ASN A CA    1 
ATOM   13847 C C     . ASN A 1 3631 ? 157.410 145.634 131.390 1.00 166.44 ? 3631 ASN A C     1 
ATOM   13848 O O     . ASN A 1 3631 ? 156.889 146.424 132.185 1.00 166.44 ? 3631 ASN A O     1 
ATOM   13849 C CB    . ASN A 1 3631 ? 158.508 146.994 129.619 1.00 166.44 ? 3631 ASN A CB    1 
ATOM   13850 C CG    . ASN A 1 3631 ? 159.172 146.783 128.275 1.00 166.44 ? 3631 ASN A CG    1 
ATOM   13851 O OD1   . ASN A 1 3631 ? 158.575 146.219 127.358 1.00 166.44 ? 3631 ASN A OD1   1 
ATOM   13852 N ND2   . ASN A 1 3631 ? 160.414 147.236 128.150 1.00 166.44 ? 3631 ASN A ND2   1 
ATOM   13853 N N     . PRO A 1 3632 ? 157.944 144.483 131.795 1.00 159.36 ? 3632 PRO A N     1 
ATOM   13854 C CA    . PRO A 1 3632 ? 158.064 144.190 133.226 1.00 159.36 ? 3632 PRO A CA    1 
ATOM   13855 C C     . PRO A 1 3632 ? 158.974 145.191 133.916 1.00 159.36 ? 3632 PRO A C     1 
ATOM   13856 O O     . PRO A 1 3632 ? 159.966 145.655 133.351 1.00 159.36 ? 3632 PRO A O     1 
ATOM   13857 C CB    . PRO A 1 3632 ? 158.669 142.783 133.251 1.00 159.36 ? 3632 PRO A CB    1 
ATOM   13858 C CG    . PRO A 1 3632 ? 159.338 142.639 131.930 1.00 159.36 ? 3632 PRO A CG    1 
ATOM   13859 C CD    . PRO A 1 3632 ? 158.481 143.396 130.965 1.00 159.36 ? 3632 PRO A CD    1 
ATOM   13860 N N     . LEU A 1 3633 ? 158.636 145.512 135.160 1.00 154.21 ? 3633 LEU A N     1 
ATOM   13861 C CA    . LEU A 1 3633 ? 159.411 146.459 135.943 1.00 154.21 ? 3633 LEU A CA    1 
ATOM   13862 C C     . LEU A 1 3633 ? 159.679 145.910 137.334 1.00 154.21 ? 3633 LEU A C     1 
ATOM   13863 O O     . LEU A 1 3633 ? 158.892 145.133 137.881 1.00 154.21 ? 3633 LEU A O     1 
ATOM   13864 C CB    . LEU A 1 3633 ? 158.706 147.809 136.060 1.00 154.21 ? 3633 LEU A CB    1 
ATOM   13865 C CG    . LEU A 1 3633 ? 158.978 148.842 134.974 1.00 154.21 ? 3633 LEU A CG    1 
ATOM   13866 C CD1   . LEU A 1 3633 ? 158.773 150.233 135.533 1.00 154.21 ? 3633 LEU A CD1   1 
ATOM   13867 C CD2   . LEU A 1 3633 ? 160.383 148.688 134.438 1.00 154.21 ? 3633 LEU A CD2   1 
ATOM   13868 N N     . LEU A 1 3634 ? 160.811 146.321 137.893 1.00 151.78 ? 3634 LEU A N     1 
ATOM   13869 C CA    . LEU A 1 3634 ? 161.137 146.098 139.292 1.00 151.78 ? 3634 LEU A CA    1 
ATOM   13870 C C     . LEU A 1 3634 ? 161.596 147.413 139.897 1.00 151.78 ? 3634 LEU A C     1 
ATOM   13871 O O     . LEU A 1 3634 ? 162.453 148.100 139.334 1.00 151.78 ? 3634 LEU A O     1 
ATOM   13872 C CB    . LEU A 1 3634 ? 162.214 145.011 139.461 1.00 151.78 ? 3634 LEU A CB    1 
ATOM   13873 C CG    . LEU A 1 3634 ? 162.836 144.817 140.850 1.00 151.78 ? 3634 LEU A CG    1 
ATOM   13874 C CD1   . LEU A 1 3634 ? 163.268 143.388 141.040 1.00 151.78 ? 3634 LEU A CD1   1 
ATOM   13875 C CD2   . LEU A 1 3634 ? 164.056 145.708 141.026 1.00 151.78 ? 3634 LEU A CD2   1 
ATOM   13876 N N     . VAL A 1 3635 ? 161.026 147.759 141.046 1.00 150.72 ? 3635 VAL A N     1 
ATOM   13877 C CA    . VAL A 1 3635 ? 161.350 148.996 141.743 1.00 150.72 ? 3635 VAL A CA    1 
ATOM   13878 C C     . VAL A 1 3635 ? 161.975 148.641 143.084 1.00 150.72 ? 3635 VAL A C     1 
ATOM   13879 O O     . VAL A 1 3635 ? 161.397 147.873 143.864 1.00 150.72 ? 3635 VAL A O     1 
ATOM   13880 C CB    . VAL A 1 3635 ? 160.115 149.890 141.923 1.00 150.72 ? 3635 VAL A CB    1 
ATOM   13881 C CG1   . VAL A 1 3635 ? 159.783 150.591 140.618 1.00 150.72 ? 3635 VAL A CG1   1 
ATOM   13882 C CG2   . VAL A 1 3635 ? 158.938 149.061 142.374 1.00 150.72 ? 3635 VAL A CG2   1 
ATOM   13883 N N     . GLN A 1 3636 ? 163.160 149.180 143.340 1.00 152.14 ? 3636 GLN A N     1 
ATOM   13884 C CA    . GLN A 1 3636 ? 163.856 148.993 144.602 1.00 152.14 ? 3636 GLN A CA    1 
ATOM   13885 C C     . GLN A 1 3636 ? 163.551 150.155 145.539 1.00 152.14 ? 3636 GLN A C     1 
ATOM   13886 O O     . GLN A 1 3636 ? 162.934 151.151 145.153 1.00 152.14 ? 3636 GLN A O     1 
ATOM   13887 C CB    . GLN A 1 3636 ? 165.362 148.861 144.365 1.00 152.14 ? 3636 GLN A CB    1 
ATOM   13888 C CG    . GLN A 1 3636 ? 165.721 147.801 143.342 1.00 152.14 ? 3636 GLN A CG    1 
ATOM   13889 C CD    . GLN A 1 3636 ? 167.117 147.967 142.787 1.00 152.14 ? 3636 GLN A CD    1 
ATOM   13890 O OE1   . GLN A 1 3636 ? 167.298 148.187 141.590 1.00 152.14 ? 3636 GLN A OE1   1 
ATOM   13891 N NE2   . GLN A 1 3636 ? 168.116 147.860 143.653 1.00 152.14 ? 3636 GLN A NE2   1 
ATOM   13892 N N     . ASP A 1 3637 ? 163.992 150.012 146.790 1.00 159.73 ? 3637 ASP A N     1 
ATOM   13893 C CA    . ASP A 1 3637 ? 163.764 151.016 147.829 1.00 159.73 ? 3637 ASP A CA    1 
ATOM   13894 C C     . ASP A 1 3637 ? 162.264 151.254 148.017 1.00 159.73 ? 3637 ASP A C     1 
ATOM   13895 O O     . ASP A 1 3637 ? 161.746 152.358 147.839 1.00 159.73 ? 3637 ASP A O     1 
ATOM   13896 C CB    . ASP A 1 3637 ? 164.510 152.315 147.495 1.00 159.73 ? 3637 ASP A CB    1 
ATOM   13897 C CG    . ASP A 1 3637 ? 164.343 153.383 148.559 1.00 159.73 ? 3637 ASP A CG    1 
ATOM   13898 O OD1   . ASP A 1 3637 ? 164.119 153.027 149.732 1.00 159.73 ? 3637 ASP A OD1   1 
ATOM   13899 O OD2   . ASP A 1 3637 ? 164.430 154.581 148.217 1.00 159.73 ? 3637 ASP A OD2   1 
ATOM   13900 N N     . VAL A 1 3638 ? 161.563 150.176 148.371 1.00 148.72 ? 3638 VAL A N     1 
ATOM   13901 C CA    . VAL A 1 3638 ? 160.111 150.242 148.481 1.00 148.72 ? 3638 VAL A CA    1 
ATOM   13902 C C     . VAL A 1 3638 ? 159.663 150.951 149.752 1.00 148.72 ? 3638 VAL A C     1 
ATOM   13903 O O     . VAL A 1 3638 ? 158.512 151.396 149.832 1.00 148.72 ? 3638 VAL A O     1 
ATOM   13904 C CB    . VAL A 1 3638 ? 159.504 148.831 148.411 1.00 148.72 ? 3638 VAL A CB    1 
ATOM   13905 C CG1   . VAL A 1 3638 ? 159.774 148.072 149.694 1.00 148.72 ? 3638 VAL A CG1   1 
ATOM   13906 C CG2   . VAL A 1 3638 ? 158.012 148.892 148.112 1.00 148.72 ? 3638 VAL A CG2   1 
ATOM   13907 N N     . GLU A 1 3639 ? 160.545 151.083 150.745 1.00 154.83 ? 3639 GLU A N     1 
ATOM   13908 C CA    . GLU A 1 3639 ? 160.170 151.765 151.980 1.00 154.83 ? 3639 GLU A CA    1 
ATOM   13909 C C     . GLU A 1 3639 ? 159.774 153.211 151.718 1.00 154.83 ? 3639 GLU A C     1 
ATOM   13910 O O     . GLU A 1 3639 ? 158.927 153.761 152.431 1.00 154.83 ? 3639 GLU A O     1 
ATOM   13911 C CB    . GLU A 1 3639 ? 161.318 151.692 152.988 1.00 154.83 ? 3639 GLU A CB    1 
ATOM   13912 C CG    . GLU A 1 3639 ? 162.681 152.085 152.431 1.00 154.83 ? 3639 GLU A CG    1 
ATOM   13913 C CD    . GLU A 1 3639 ? 163.382 150.951 151.702 1.00 154.83 ? 3639 GLU A CD    1 
ATOM   13914 O OE1   . GLU A 1 3639 ? 162.689 150.111 151.089 1.00 154.83 ? 3639 GLU A OE1   1 
ATOM   13915 O OE2   . GLU A 1 3639 ? 164.629 150.903 151.736 1.00 154.83 ? 3639 GLU A OE2   1 
ATOM   13916 N N     . SER A 1 3640 ? 160.368 153.837 150.708 1.00 155.07 ? 3640 SER A N     1 
ATOM   13917 C CA    . SER A 1 3640 ? 159.932 155.152 150.240 1.00 155.07 ? 3640 SER A CA    1 
ATOM   13918 C C     . SER A 1 3640 ? 158.936 154.990 149.093 1.00 155.07 ? 3640 SER A C     1 
ATOM   13919 O O     . SER A 1 3640 ? 159.142 155.457 147.973 1.00 155.07 ? 3640 SER A O     1 
ATOM   13920 C CB    . SER A 1 3640 ? 161.134 155.989 149.818 1.00 155.07 ? 3640 SER A CB    1 
ATOM   13921 O OG    . SER A 1 3640 ? 161.960 155.273 148.919 1.00 155.07 ? 3640 SER A OG    1 
ATOM   13922 N N     . TYR A 1 3641 ? 157.843 154.298 149.398 1.00 152.21 ? 3641 TYR A N     1 
ATOM   13923 C CA    . TYR A 1 3641 ? 156.848 153.972 148.388 1.00 152.21 ? 3641 TYR A CA    1 
ATOM   13924 C C     . TYR A 1 3641 ? 156.187 155.233 147.850 1.00 152.21 ? 3641 TYR A C     1 
ATOM   13925 O O     . TYR A 1 3641 ? 155.954 156.196 148.586 1.00 152.21 ? 3641 TYR A O     1 
ATOM   13926 C CB    . TYR A 1 3641 ? 155.797 153.030 148.972 1.00 152.21 ? 3641 TYR A CB    1 
ATOM   13927 C CG    . TYR A 1 3641 ? 154.511 152.952 148.181 1.00 152.21 ? 3641 TYR A CG    1 
ATOM   13928 C CD1   . TYR A 1 3641 ? 154.415 152.148 147.056 1.00 152.21 ? 3641 TYR A CD1   1 
ATOM   13929 C CD2   . TYR A 1 3641 ? 153.385 153.662 148.576 1.00 152.21 ? 3641 TYR A CD2   1 
ATOM   13930 C CE1   . TYR A 1 3641 ? 153.242 152.068 146.335 1.00 152.21 ? 3641 TYR A CE1   1 
ATOM   13931 C CE2   . TYR A 1 3641 ? 152.208 153.586 147.861 1.00 152.21 ? 3641 TYR A CE2   1 
ATOM   13932 C CZ    . TYR A 1 3641 ? 152.142 152.788 146.742 1.00 152.21 ? 3641 TYR A CZ    1 
ATOM   13933 O OH    . TYR A 1 3641 ? 150.971 152.708 146.024 1.00 152.21 ? 3641 TYR A OH    1 
ATOM   13934 N N     . ASP A 1 3642 ? 155.889 155.223 146.552 1.00 153.07 ? 3642 ASP A N     1 
ATOM   13935 C CA    . ASP A 1 3642 ? 155.251 156.354 145.900 1.00 153.07 ? 3642 ASP A CA    1 
ATOM   13936 C C     . ASP A 1 3642 ? 153.762 156.089 145.773 1.00 153.07 ? 3642 ASP A C     1 
ATOM   13937 O O     . ASP A 1 3642 ? 153.373 155.125 145.096 1.00 153.07 ? 3642 ASP A O     1 
ATOM   13938 C CB    . ASP A 1 3642 ? 155.863 156.593 144.526 1.00 153.07 ? 3642 ASP A CB    1 
ATOM   13939 C CG    . ASP A 1 3642 ? 155.781 158.040 144.100 1.00 153.07 ? 3642 ASP A CG    1 
ATOM   13940 O OD1   . ASP A 1 3642 ? 154.668 158.605 144.137 1.00 153.07 ? 3642 ASP A OD1   1 
ATOM   13941 O OD2   . ASP A 1 3642 ? 156.827 158.613 143.730 1.00 153.07 ? 3642 ASP A OD2   1 
ATOM   13942 N N     . PRO A 1 3643 ? 152.901 156.892 146.398 1.00 146.21 ? 3643 PRO A N     1 
ATOM   13943 C CA    . PRO A 1 3643 ? 151.454 156.663 146.289 1.00 146.21 ? 3643 PRO A CA    1 
ATOM   13944 C C     . PRO A 1 3643 ? 150.945 156.684 144.856 1.00 146.21 ? 3643 PRO A C     1 
ATOM   13945 O O     . PRO A 1 3643 ? 149.837 156.212 144.584 1.00 146.21 ? 3643 PRO A O     1 
ATOM   13946 C CB    . PRO A 1 3643 ? 150.846 157.816 147.098 1.00 146.21 ? 3643 PRO A CB    1 
ATOM   13947 C CG    . PRO A 1 3643 ? 151.958 158.395 147.909 1.00 146.21 ? 3643 PRO A CG    1 
ATOM   13948 C CD    . PRO A 1 3643 ? 153.249 157.729 147.556 1.00 146.21 ? 3643 PRO A CD    1 
ATOM   13949 N N     . VAL A 1 3644 ? 151.742 157.227 143.932 1.00 146.20 ? 3644 VAL A N     1 
ATOM   13950 C CA    . VAL A 1 3644 ? 151.335 157.302 142.533 1.00 146.20 ? 3644 VAL A CA    1 
ATOM   13951 C C     . VAL A 1 3644 ? 151.071 155.924 141.945 1.00 146.20 ? 3644 VAL A C     1 
ATOM   13952 O O     . VAL A 1 3644 ? 150.384 155.808 140.925 1.00 146.20 ? 3644 VAL A O     1 
ATOM   13953 C CB    . VAL A 1 3644 ? 152.401 158.058 141.710 1.00 146.20 ? 3644 VAL A CB    1 
ATOM   13954 C CG1   . VAL A 1 3644 ? 153.538 157.126 141.313 1.00 146.20 ? 3644 VAL A CG1   1 
ATOM   13955 C CG2   . VAL A 1 3644 ? 151.772 158.693 140.483 1.00 146.20 ? 3644 VAL A CG2   1 
ATOM   13956 N N     . LEU A 1 3645 ? 151.592 154.871 142.567 1.00 142.73 ? 3645 LEU A N     1 
ATOM   13957 C CA    . LEU A 1 3645 ? 151.399 153.511 142.088 1.00 142.73 ? 3645 LEU A CA    1 
ATOM   13958 C C     . LEU A 1 3645 ? 150.126 152.870 142.621 1.00 142.73 ? 3645 LEU A C     1 
ATOM   13959 O O     . LEU A 1 3645 ? 149.828 151.728 142.255 1.00 142.73 ? 3645 LEU A O     1 
ATOM   13960 C CB    . LEU A 1 3645 ? 152.605 152.650 142.470 1.00 142.73 ? 3645 LEU A CB    1 
ATOM   13961 C CG    . LEU A 1 3645 ? 153.611 152.377 141.356 1.00 142.73 ? 3645 LEU A CG    1 
ATOM   13962 C CD1   . LEU A 1 3645 ? 154.705 151.452 141.852 1.00 142.73 ? 3645 LEU A CD1   1 
ATOM   13963 C CD2   . LEU A 1 3645 ? 152.913 151.788 140.148 1.00 142.73 ? 3645 LEU A CD2   1 
ATOM   13964 N N     . ASN A 1 3646 ? 149.373 153.569 143.472 1.00 142.59 ? 3646 ASN A N     1 
ATOM   13965 C CA    . ASN A 1 3646 ? 148.156 152.988 144.037 1.00 142.59 ? 3646 ASN A CA    1 
ATOM   13966 C C     . ASN A 1 3646 ? 147.140 152.579 142.980 1.00 142.59 ? 3646 ASN A C     1 
ATOM   13967 O O     . ASN A 1 3646 ? 146.598 151.465 143.083 1.00 142.59 ? 3646 ASN A O     1 
ATOM   13968 C CB    . ASN A 1 3646 ? 147.540 153.961 145.047 1.00 142.59 ? 3646 ASN A CB    1 
ATOM   13969 C CG    . ASN A 1 3646 ? 148.132 153.813 146.427 1.00 142.59 ? 3646 ASN A CG    1 
ATOM   13970 O OD1   . ASN A 1 3646 ? 148.223 152.709 146.959 1.00 142.59 ? 3646 ASN A OD1   1 
ATOM   13971 N ND2   . ASN A 1 3646 ? 148.540 154.929 147.018 1.00 142.59 ? 3646 ASN A ND2   1 
ATOM   13972 N N     . PRO A 1 3647 ? 146.808 153.402 141.976 1.00 150.65 ? 3647 PRO A N     1 
ATOM   13973 C CA    . PRO A 1 3647 ? 145.868 152.921 140.949 1.00 150.65 ? 3647 PRO A CA    1 
ATOM   13974 C C     . PRO A 1 3647 ? 146.373 151.705 140.193 1.00 150.65 ? 3647 PRO A C     1 
ATOM   13975 O O     . PRO A 1 3647 ? 145.575 150.833 139.830 1.00 150.65 ? 3647 PRO A O     1 
ATOM   13976 C CB    . PRO A 1 3647 ? 145.704 154.140 140.030 1.00 150.65 ? 3647 PRO A CB    1 
ATOM   13977 C CG    . PRO A 1 3647 ? 146.061 155.304 140.880 1.00 150.65 ? 3647 PRO A CG    1 
ATOM   13978 C CD    . PRO A 1 3647 ? 147.167 154.814 141.754 1.00 150.65 ? 3647 PRO A CD    1 
ATOM   13979 N N     . VAL A 1 3648 ? 147.681 151.620 139.944 1.00 142.33 ? 3648 VAL A N     1 
ATOM   13980 C CA    . VAL A 1 3648 ? 148.223 150.459 139.247 1.00 142.33 ? 3648 VAL A CA    1 
ATOM   13981 C C     . VAL A 1 3648 ? 148.166 149.227 140.139 1.00 142.33 ? 3648 VAL A C     1 
ATOM   13982 O O     . VAL A 1 3648 ? 147.810 148.132 139.687 1.00 142.33 ? 3648 VAL A O     1 
ATOM   13983 C CB    . VAL A 1 3648 ? 149.656 150.743 138.765 1.00 142.33 ? 3648 VAL A CB    1 
ATOM   13984 C CG1   . VAL A 1 3648 ? 150.167 149.589 137.921 1.00 142.33 ? 3648 VAL A CG1   1 
ATOM   13985 C CG2   . VAL A 1 3648 ? 149.702 152.043 137.981 1.00 142.33 ? 3648 VAL A CG2   1 
ATOM   13986 N N     . LEU A 1 3649 ? 148.519 149.383 141.416 1.00 135.36 ? 3649 LEU A N     1 
ATOM   13987 C CA    . LEU A 1 3649 ? 148.461 148.256 142.339 1.00 135.36 ? 3649 LEU A CA    1 
ATOM   13988 C C     . LEU A 1 3649 ? 147.036 147.750 142.497 1.00 135.36 ? 3649 LEU A C     1 
ATOM   13989 O O     . LEU A 1 3649 ? 146.801 146.537 142.539 1.00 135.36 ? 3649 LEU A O     1 
ATOM   13990 C CB    . LEU A 1 3649 ? 149.038 148.658 143.695 1.00 135.36 ? 3649 LEU A CB    1 
ATOM   13991 C CG    . LEU A 1 3649 ? 150.478 148.236 143.982 1.00 135.36 ? 3649 LEU A CG    1 
ATOM   13992 C CD1   . LEU A 1 3649 ? 150.542 146.740 144.223 1.00 135.36 ? 3649 LEU A CD1   1 
ATOM   13993 C CD2   . LEU A 1 3649 ? 151.402 148.640 142.845 1.00 135.36 ? 3649 LEU A CD2   1 
ATOM   13994 N N     . ASN A 1 3650 ? 146.069 148.665 142.575 1.00 138.18 ? 3650 ASN A N     1 
ATOM   13995 C CA    . ASN A 1 3650 ? 144.669 148.283 142.708 1.00 138.18 ? 3650 ASN A CA    1 
ATOM   13996 C C     . ASN A 1 3650 ? 144.142 147.553 141.483 1.00 138.18 ? 3650 ASN A C     1 
ATOM   13997 O O     . ASN A 1 3650 ? 143.061 146.958 141.559 1.00 138.18 ? 3650 ASN A O     1 
ATOM   13998 C CB    . ASN A 1 3650 ? 143.815 149.522 142.971 1.00 138.18 ? 3650 ASN A CB    1 
ATOM   13999 C CG    . ASN A 1 3650 ? 144.017 150.080 144.357 1.00 138.18 ? 3650 ASN A CG    1 
ATOM   14000 O OD1   . ASN A 1 3650 ? 144.663 149.459 145.198 1.00 138.18 ? 3650 ASN A OD1   1 
ATOM   14001 N ND2   . ASN A 1 3650 ? 143.473 151.264 144.604 1.00 138.18 ? 3650 ASN A ND2   1 
ATOM   14002 N N     . ARG A 1 3651 ? 144.872 147.591 140.367 1.00 149.14 ? 3651 ARG A N     1 
ATOM   14003 C CA    . ARG A 1 3651 ? 144.442 146.983 139.110 1.00 149.14 ? 3651 ARG A CA    1 
ATOM   14004 C C     . ARG A 1 3651 ? 143.086 147.516 138.663 1.00 149.14 ? 3651 ARG A C     1 
ATOM   14005 O O     . ARG A 1 3651 ? 142.286 146.790 138.071 1.00 149.14 ? 3651 ARG A O     1 
ATOM   14006 C CB    . ARG A 1 3651 ? 144.413 145.456 139.203 1.00 149.14 ? 3651 ARG A CB    1 
ATOM   14007 C CG    . ARG A 1 3651 ? 145.717 144.837 139.670 1.00 149.14 ? 3651 ARG A CG    1 
ATOM   14008 C CD    . ARG A 1 3651 ? 145.525 143.370 140.012 1.00 149.14 ? 3651 ARG A CD    1 
ATOM   14009 N NE    . ARG A 1 3651 ? 145.648 142.522 138.832 1.00 149.14 ? 3651 ARG A NE    1 
ATOM   14010 C CZ    . ARG A 1 3651 ? 146.795 142.207 138.247 1.00 149.14 ? 3651 ARG A CZ    1 
ATOM   14011 N NH1   . ARG A 1 3651 ? 147.952 142.634 138.720 1.00 149.14 ? 3651 ARG A NH1   1 
ATOM   14012 N NH2   . ARG A 1 3651 ? 146.780 141.440 137.160 1.00 149.14 ? 3651 ARG A NH2   1 
ATOM   14013 N N     . GLU A 1 3652 ? 142.821 148.787 138.954 1.00 181.80 ? 3652 GLU A N     1 
ATOM   14014 C CA    . GLU A 1 3652 ? 141.622 149.435 138.447 1.00 181.80 ? 3652 GLU A CA    1 
ATOM   14015 C C     . GLU A 1 3652 ? 141.667 149.498 136.924 1.00 181.80 ? 3652 GLU A C     1 
ATOM   14016 O O     . GLU A 1 3652 ? 142.734 149.606 136.316 1.00 181.80 ? 3652 GLU A O     1 
ATOM   14017 C CB    . GLU A 1 3652 ? 141.483 150.835 139.048 1.00 181.80 ? 3652 GLU A CB    1 
ATOM   14018 C CG    . GLU A 1 3652 ? 142.484 151.856 138.522 1.00 181.80 ? 3652 GLU A CG    1 
ATOM   14019 C CD    . GLU A 1 3652 ? 141.921 152.705 137.403 1.00 181.80 ? 3652 GLU A CD    1 
ATOM   14020 O OE1   . GLU A 1 3652 ? 140.734 152.525 137.060 1.00 181.80 ? 3652 GLU A OE1   1 
ATOM   14021 O OE2   . GLU A 1 3652 ? 142.663 153.556 136.871 1.00 181.80 ? 3652 GLU A OE2   1 
ATOM   14022 N N     . VAL A 1 3653 ? 140.494 149.391 136.303 1.00 188.23 ? 3653 VAL A N     1 
ATOM   14023 C CA    . VAL A 1 3653 ? 140.390 149.360 134.849 1.00 188.23 ? 3653 VAL A CA    1 
ATOM   14024 C C     . VAL A 1 3653 ? 139.263 150.289 134.421 1.00 188.23 ? 3653 VAL A C     1 
ATOM   14025 O O     . VAL A 1 3653 ? 138.115 150.111 134.842 1.00 188.23 ? 3653 VAL A O     1 
ATOM   14026 C CB    . VAL A 1 3653 ? 140.142 147.938 134.317 1.00 188.23 ? 3653 VAL A CB    1 
ATOM   14027 C CG1   . VAL A 1 3653 ? 139.661 147.989 132.880 1.00 188.23 ? 3653 VAL A CG1   1 
ATOM   14028 C CG2   . VAL A 1 3653 ? 141.404 147.101 134.434 1.00 188.23 ? 3653 VAL A CG2   1 
ATOM   14029 N N     . ARG A 1 3654 ? 139.587 151.278 133.595 1.00 190.97 ? 3654 ARG A N     1 
ATOM   14030 C CA    . ARG A 1 3654 ? 138.579 152.139 132.974 1.00 190.97 ? 3654 ARG A CA    1 
ATOM   14031 C C     . ARG A 1 3654 ? 138.300 151.683 131.542 1.00 190.97 ? 3654 ARG A C     1 
ATOM   14032 O O     . ARG A 1 3654 ? 138.534 152.400 130.571 1.00 190.97 ? 3654 ARG A O     1 
ATOM   14033 C CB    . ARG A 1 3654 ? 139.029 153.596 133.017 1.00 190.97 ? 3654 ARG A CB    1 
ATOM   14034 C CG    . ARG A 1 3654 ? 139.270 154.133 134.418 1.00 190.97 ? 3654 ARG A CG    1 
ATOM   14035 C CD    . ARG A 1 3654 ? 137.981 154.662 135.025 1.00 190.97 ? 3654 ARG A CD    1 
ATOM   14036 N NE    . ARG A 1 3654 ? 137.198 153.603 135.650 1.00 190.97 ? 3654 ARG A NE    1 
ATOM   14037 C CZ    . ARG A 1 3654 ? 137.383 153.165 136.889 1.00 190.97 ? 3654 ARG A CZ    1 
ATOM   14038 N NH1   . ARG A 1 3654 ? 138.309 153.688 137.676 1.00 190.97 ? 3654 ARG A NH1   1 
ATOM   14039 N NH2   . ARG A 1 3654 ? 136.619 152.180 137.350 1.00 190.97 ? 3654 ARG A NH2   1 
ATOM   14040 N N     . ARG A 1 3655 ? 137.779 150.464 131.424 1.00 190.97 ? 3655 ARG A N     1 
ATOM   14041 C CA    . ARG A 1 3655 ? 137.504 149.877 130.116 1.00 190.97 ? 3655 ARG A CA    1 
ATOM   14042 C C     . ARG A 1 3655 ? 136.397 150.667 129.427 1.00 190.97 ? 3655 ARG A C     1 
ATOM   14043 O O     . ARG A 1 3655 ? 135.225 150.575 129.806 1.00 190.97 ? 3655 ARG A O     1 
ATOM   14044 C CB    . ARG A 1 3655 ? 137.123 148.407 130.270 1.00 190.97 ? 3655 ARG A CB    1 
ATOM   14045 C CG    . ARG A 1 3655 ? 136.175 148.126 131.427 1.00 190.97 ? 3655 ARG A CG    1 
ATOM   14046 C CD    . ARG A 1 3655 ? 135.997 146.636 131.673 1.00 190.97 ? 3655 ARG A CD    1 
ATOM   14047 N NE    . ARG A 1 3655 ? 137.000 146.106 132.588 1.00 190.97 ? 3655 ARG A NE    1 
ATOM   14048 C CZ    . ARG A 1 3655 ? 137.779 145.067 132.326 1.00 190.97 ? 3655 ARG A CZ    1 
ATOM   14049 N NH1   . ARG A 1 3655 ? 137.692 144.408 131.183 1.00 190.97 ? 3655 ARG A NH1   1 
ATOM   14050 N NH2   . ARG A 1 3655 ? 138.668 144.677 133.236 1.00 190.97 ? 3655 ARG A NH2   1 
ATOM   14051 N N     . THR A 1 3656 ? 136.766 151.450 128.415 1.00 206.74 ? 3656 THR A N     1 
ATOM   14052 C CA    . THR A 1 3656 ? 135.806 152.262 127.682 1.00 206.74 ? 3656 THR A CA    1 
ATOM   14053 C C     . THR A 1 3656 ? 136.171 152.255 126.205 1.00 206.74 ? 3656 THR A C     1 
ATOM   14054 O O     . THR A 1 3656 ? 137.346 152.383 125.848 1.00 206.74 ? 3656 THR A O     1 
ATOM   14055 C CB    . THR A 1 3656 ? 135.768 153.703 128.205 1.00 206.74 ? 3656 THR A CB    1 
ATOM   14056 O OG1   . THR A 1 3656 ? 135.640 153.693 129.632 1.00 206.74 ? 3656 THR A OG1   1 
ATOM   14057 C CG2   . THR A 1 3656 ? 134.591 154.456 127.606 1.00 206.74 ? 3656 THR A CG2   1 
ATOM   14058 N N     . GLY A 1 3657 ? 135.159 152.105 125.357 1.00 211.86 ? 3657 GLY A N     1 
ATOM   14059 C CA    . GLY A 1 3657 ? 135.369 152.133 123.918 1.00 211.86 ? 3657 GLY A CA    1 
ATOM   14060 C C     . GLY A 1 3657 ? 136.265 151.027 123.409 1.00 211.86 ? 3657 GLY A C     1 
ATOM   14061 O O     . GLY A 1 3657 ? 137.046 151.243 122.474 1.00 211.86 ? 3657 GLY A O     1 
ATOM   14062 N N     . GLY A 1 3658 ? 136.171 149.840 124.004 1.00 208.81 ? 3658 GLY A N     1 
ATOM   14063 C CA    . GLY A 1 3658 ? 137.026 148.741 123.610 1.00 208.81 ? 3658 GLY A CA    1 
ATOM   14064 C C     . GLY A 1 3658 ? 138.487 148.923 123.939 1.00 208.81 ? 3658 GLY A C     1 
ATOM   14065 O O     . GLY A 1 3658 ? 139.320 148.169 123.428 1.00 208.81 ? 3658 GLY A O     1 
ATOM   14066 N N     . ARG A 1 3659 ? 138.829 149.900 124.775 1.00 206.48 ? 3659 ARG A N     1 
ATOM   14067 C CA    . ARG A 1 3659 ? 140.210 150.166 125.139 1.00 206.48 ? 3659 ARG A CA    1 
ATOM   14068 C C     . ARG A 1 3659 ? 140.322 150.263 126.653 1.00 206.48 ? 3659 ARG A C     1 
ATOM   14069 O O     . ARG A 1 3659 ? 139.563 150.987 127.302 1.00 206.48 ? 3659 ARG A O     1 
ATOM   14070 C CB    . ARG A 1 3659 ? 140.719 151.454 124.476 1.00 206.48 ? 3659 ARG A CB    1 
ATOM   14071 C CG    . ARG A 1 3659 ? 142.188 151.758 124.721 1.00 206.48 ? 3659 ARG A CG    1 
ATOM   14072 C CD    . ARG A 1 3659 ? 142.512 153.215 124.410 1.00 206.48 ? 3659 ARG A CD    1 
ATOM   14073 N NE    . ARG A 1 3659 ? 143.639 153.718 125.186 1.00 206.48 ? 3659 ARG A NE    1 
ATOM   14074 C CZ    . ARG A 1 3659 ? 144.006 154.992 125.236 1.00 206.48 ? 3659 ARG A CZ    1 
ATOM   14075 N NH1   . ARG A 1 3659 ? 143.349 155.927 124.570 1.00 206.48 ? 3659 ARG A NH1   1 
ATOM   14076 N NH2   . ARG A 1 3659 ? 145.061 155.335 125.970 1.00 206.48 ? 3659 ARG A NH2   1 
ATOM   14077 N N     . VAL A 1 3660 ? 141.285 149.532 127.208 1.00 203.85 ? 3660 VAL A N     1 
ATOM   14078 C CA    . VAL A 1 3660 ? 141.475 149.433 128.651 1.00 203.85 ? 3660 VAL A CA    1 
ATOM   14079 C C     . VAL A 1 3660 ? 142.279 150.642 129.111 1.00 203.85 ? 3660 VAL A C     1 
ATOM   14080 O O     . VAL A 1 3660 ? 143.281 151.008 128.485 1.00 203.85 ? 3660 VAL A O     1 
ATOM   14081 C CB    . VAL A 1 3660 ? 142.164 148.109 129.030 1.00 203.85 ? 3660 VAL A CB    1 
ATOM   14082 C CG1   . VAL A 1 3660 ? 143.473 147.934 128.267 1.00 203.85 ? 3660 VAL A CG1   1 
ATOM   14083 C CG2   . VAL A 1 3660 ? 142.381 148.025 130.526 1.00 203.85 ? 3660 VAL A CG2   1 
ATOM   14084 N N     . LEU A 1 3661 ? 141.825 151.282 130.187 1.00 200.33 ? 3661 LEU A N     1 
ATOM   14085 C CA    . LEU A 1 3661 ? 142.312 152.603 130.551 1.00 200.33 ? 3661 LEU A CA    1 
ATOM   14086 C C     . LEU A 1 3661 ? 142.567 152.690 132.051 1.00 200.33 ? 3661 LEU A C     1 
ATOM   14087 O O     . LEU A 1 3661 ? 141.866 152.068 132.853 1.00 200.33 ? 3661 LEU A O     1 
ATOM   14088 C CB    . LEU A 1 3661 ? 141.297 153.668 130.128 1.00 200.33 ? 3661 LEU A CB    1 
ATOM   14089 C CG    . LEU A 1 3661 ? 141.811 154.958 129.501 1.00 200.33 ? 3661 LEU A CG    1 
ATOM   14090 C CD1   . LEU A 1 3661 ? 142.927 154.658 128.516 1.00 200.33 ? 3661 LEU A CD1   1 
ATOM   14091 C CD2   . LEU A 1 3661 ? 140.673 155.710 128.826 1.00 200.33 ? 3661 LEU A CD2   1 
ATOM   14092 N N     . ILE A 1 3662 ? 143.590 153.466 132.422 1.00 202.10 ? 3662 ILE A N     1 
ATOM   14093 C CA    . ILE A 1 3662 ? 143.848 153.814 133.813 1.00 202.10 ? 3662 ILE A CA    1 
ATOM   14094 C C     . ILE A 1 3662 ? 144.142 155.303 133.903 1.00 202.10 ? 3662 ILE A C     1 
ATOM   14095 O O     . ILE A 1 3662 ? 144.588 155.935 132.943 1.00 202.10 ? 3662 ILE A O     1 
ATOM   14096 C CB    . ILE A 1 3662 ? 145.018 153.023 134.438 1.00 202.10 ? 3662 ILE A CB    1 
ATOM   14097 C CG1   . ILE A 1 3662 ? 146.192 152.927 133.466 1.00 202.10 ? 3662 ILE A CG1   1 
ATOM   14098 C CG2   . ILE A 1 3662 ? 144.559 151.656 134.902 1.00 202.10 ? 3662 ILE A CG2   1 
ATOM   14099 C CD1   . ILE A 1 3662 ? 147.281 152.010 133.947 1.00 202.10 ? 3662 ILE A CD1   1 
ATOM   14100 N N     . THR A 1 3663 ? 143.909 155.855 135.090 1.00 199.51 ? 3663 THR A N     1 
ATOM   14101 C CA    . THR A 1 3663 ? 144.186 157.256 135.375 1.00 199.51 ? 3663 THR A CA    1 
ATOM   14102 C C     . THR A 1 3663 ? 145.398 157.341 136.295 1.00 199.51 ? 3663 THR A C     1 
ATOM   14103 O O     . THR A 1 3663 ? 145.328 156.935 137.459 1.00 199.51 ? 3663 THR A O     1 
ATOM   14104 C CB    . THR A 1 3663 ? 142.977 157.932 136.020 1.00 199.51 ? 3663 THR A CB    1 
ATOM   14105 O OG1   . THR A 1 3663 ? 142.956 157.635 137.421 1.00 199.51 ? 3663 THR A OG1   1 
ATOM   14106 C CG2   . THR A 1 3663 ? 141.690 157.430 135.384 1.00 199.51 ? 3663 THR A CG2   1 
ATOM   14107 N N     . LEU A 1 3664 ? 146.501 157.870 135.773 1.00 200.64 ? 3664 LEU A N     1 
ATOM   14108 C CA    . LEU A 1 3664 ? 147.738 158.049 136.528 1.00 200.64 ? 3664 LEU A CA    1 
ATOM   14109 C C     . LEU A 1 3664 ? 147.908 159.544 136.777 1.00 200.64 ? 3664 LEU A C     1 
ATOM   14110 O O     . LEU A 1 3664 ? 148.528 160.249 135.977 1.00 200.64 ? 3664 LEU A O     1 
ATOM   14111 C CB    . LEU A 1 3664 ? 148.926 157.469 135.778 1.00 200.64 ? 3664 LEU A CB    1 
ATOM   14112 C CG    . LEU A 1 3664 ? 150.030 156.863 136.642 1.00 200.64 ? 3664 LEU A CG    1 
ATOM   14113 C CD1   . LEU A 1 3664 ? 149.438 156.080 137.804 1.00 200.64 ? 3664 LEU A CD1   1 
ATOM   14114 C CD2   . LEU A 1 3664 ? 150.934 155.983 135.799 1.00 200.64 ? 3664 LEU A CD2   1 
ATOM   14115 N N     . GLY A 1 3665 ? 147.370 160.018 137.897 1.00 203.87 ? 3665 GLY A N     1 
ATOM   14116 C CA    . GLY A 1 3665 ? 147.388 161.446 138.164 1.00 203.87 ? 3665 GLY A CA    1 
ATOM   14117 C C     . GLY A 1 3665 ? 146.612 162.189 137.096 1.00 203.87 ? 3665 GLY A C     1 
ATOM   14118 O O     . GLY A 1 3665 ? 145.456 161.869 136.799 1.00 203.87 ? 3665 GLY A O     1 
ATOM   14119 N N     . ASP A 1 3666 ? 147.250 163.199 136.503 1.00 210.61 ? 3666 ASP A N     1 
ATOM   14120 C CA    . ASP A 1 3666 ? 146.630 163.919 135.400 1.00 210.61 ? 3666 ASP A CA    1 
ATOM   14121 C C     . ASP A 1 3666 ? 146.804 163.211 134.064 1.00 210.61 ? 3666 ASP A C     1 
ATOM   14122 O O     . ASP A 1 3666 ? 146.106 163.553 133.104 1.00 210.61 ? 3666 ASP A O     1 
ATOM   14123 C CB    . ASP A 1 3666 ? 147.198 165.337 135.306 1.00 210.61 ? 3666 ASP A CB    1 
ATOM   14124 C CG    . ASP A 1 3666 ? 146.776 166.212 136.469 1.00 210.61 ? 3666 ASP A CG    1 
ATOM   14125 O OD1   . ASP A 1 3666 ? 145.977 165.745 137.309 1.00 210.61 ? 3666 ASP A OD1   1 
ATOM   14126 O OD2   . ASP A 1 3666 ? 147.240 167.370 136.542 1.00 210.61 ? 3666 ASP A OD2   1 
ATOM   14127 N N     . GLN A 1 3667 ? 147.700 162.234 133.982 1.00 212.51 ? 3667 GLN A N     1 
ATOM   14128 C CA    . GLN A 1 3667 ? 147.966 161.535 132.735 1.00 212.51 ? 3667 GLN A CA    1 
ATOM   14129 C C     . GLN A 1 3667 ? 147.141 160.258 132.653 1.00 212.51 ? 3667 GLN A C     1 
ATOM   14130 O O     . GLN A 1 3667 ? 146.945 159.553 133.646 1.00 212.51 ? 3667 GLN A O     1 
ATOM   14131 C CB    . GLN A 1 3667 ? 149.454 161.205 132.604 1.00 212.51 ? 3667 GLN A CB    1 
ATOM   14132 C CG    . GLN A 1 3667 ? 149.922 160.931 131.176 1.00 212.51 ? 3667 GLN A CG    1 
ATOM   14133 C CD    . GLN A 1 3667 ? 149.620 162.072 130.222 1.00 212.51 ? 3667 GLN A CD    1 
ATOM   14134 O OE1   . GLN A 1 3667 ? 148.987 161.879 129.184 1.00 212.51 ? 3667 GLN A OE1   1 
ATOM   14135 N NE2   . GLN A 1 3667 ? 150.082 163.268 130.567 1.00 212.51 ? 3667 GLN A NE2   1 
ATOM   14136 N N     . ASP A 1 3668 ? 146.659 159.967 131.449 1.00 211.15 ? 3668 ASP A N     1 
ATOM   14137 C CA    . ASP A 1 3668 ? 145.823 158.806 131.188 1.00 211.15 ? 3668 ASP A CA    1 
ATOM   14138 C C     . ASP A 1 3668 ? 146.574 157.856 130.266 1.00 211.15 ? 3668 ASP A C     1 
ATOM   14139 O O     . ASP A 1 3668 ? 147.069 158.273 129.214 1.00 211.15 ? 3668 ASP A O     1 
ATOM   14140 C CB    . ASP A 1 3668 ? 144.492 159.232 130.567 1.00 211.15 ? 3668 ASP A CB    1 
ATOM   14141 C CG    . ASP A 1 3668 ? 143.730 158.072 129.989 1.00 211.15 ? 3668 ASP A CG    1 
ATOM   14142 O OD1   . ASP A 1 3668 ? 143.682 157.025 130.659 1.00 211.15 ? 3668 ASP A OD1   1 
ATOM   14143 O OD2   . ASP A 1 3668 ? 143.179 158.204 128.877 1.00 211.15 ? 3668 ASP A OD2   1 
ATOM   14144 N N     . ILE A 1 3669 ? 146.667 156.586 130.663 1.00 202.82 ? 3669 ILE A N     1 
ATOM   14145 C CA    . ILE A 1 3669 ? 147.492 155.598 129.977 1.00 202.82 ? 3669 ILE A CA    1 
ATOM   14146 C C     . ILE A 1 3669 ? 146.671 154.345 129.703 1.00 202.82 ? 3669 ILE A C     1 
ATOM   14147 O O     . ILE A 1 3669 ? 145.805 153.970 130.501 1.00 202.82 ? 3669 ILE A O     1 
ATOM   14148 C CB    . ILE A 1 3669 ? 148.750 155.241 130.797 1.00 202.82 ? 3669 ILE A CB    1 
ATOM   14149 C CG1   . ILE A 1 3669 ? 149.402 156.500 131.368 1.00 202.82 ? 3669 ILE A CG1   1 
ATOM   14150 C CG2   . ILE A 1 3669 ? 149.751 154.482 129.941 1.00 202.82 ? 3669 ILE A CG2   1 
ATOM   14151 C CD1   . ILE A 1 3669 ? 150.053 157.375 130.322 1.00 202.82 ? 3669 ILE A CD1   1 
ATOM   14152 N N     . ASP A 1 3670 ? 146.942 153.705 128.567 1.00 201.97 ? 3670 ASP A N     1 
ATOM   14153 C CA    . ASP A 1 3670 ? 146.370 152.403 128.253 1.00 201.97 ? 3670 ASP A CA    1 
ATOM   14154 C C     . ASP A 1 3670 ? 147.233 151.288 128.832 1.00 201.97 ? 3670 ASP A C     1 
ATOM   14155 O O     . ASP A 1 3670 ? 148.459 151.401 128.917 1.00 201.97 ? 3670 ASP A O     1 
ATOM   14156 C CB    . ASP A 1 3670 ? 146.236 152.229 126.739 1.00 201.97 ? 3670 ASP A CB    1 
ATOM   14157 C CG    . ASP A 1 3670 ? 145.969 150.789 126.334 1.00 201.97 ? 3670 ASP A CG    1 
ATOM   14158 O OD1   . ASP A 1 3670 ? 146.943 150.036 126.122 1.00 201.97 ? 3670 ASP A OD1   1 
ATOM   14159 O OD2   . ASP A 1 3670 ? 144.785 150.410 126.226 1.00 201.97 ? 3670 ASP A OD2   1 
ATOM   14160 N N     . LEU A 1 3671 ? 146.578 150.196 129.226 1.00 196.13 ? 3671 LEU A N     1 
ATOM   14161 C CA    . LEU A 1 3671 ? 147.250 149.071 129.875 1.00 196.13 ? 3671 LEU A CA    1 
ATOM   14162 C C     . LEU A 1 3671 ? 147.658 148.064 128.811 1.00 196.13 ? 3671 LEU A C     1 
ATOM   14163 O O     . LEU A 1 3671 ? 146.839 147.266 128.347 1.00 196.13 ? 3671 LEU A O     1 
ATOM   14164 C CB    . LEU A 1 3671 ? 146.352 148.413 130.918 1.00 196.13 ? 3671 LEU A CB    1 
ATOM   14165 C CG    . LEU A 1 3671 ? 145.883 149.212 132.134 1.00 196.13 ? 3671 LEU A CG    1 
ATOM   14166 C CD1   . LEU A 1 3671 ? 144.827 150.222 131.739 1.00 196.13 ? 3671 LEU A CD1   1 
ATOM   14167 C CD2   . LEU A 1 3671 ? 145.365 148.291 133.228 1.00 196.13 ? 3671 LEU A CD2   1 
ATOM   14168 N N     . SER A 1 3672 ? 148.924 148.088 128.431 1.00 178.89 ? 3672 SER A N     1 
ATOM   14169 C CA    . SER A 1 3672 ? 149.442 147.044 127.564 1.00 178.89 ? 3672 SER A CA    1 
ATOM   14170 C C     . SER A 1 3672 ? 149.467 145.732 128.337 1.00 178.89 ? 3672 SER A C     1 
ATOM   14171 O O     . SER A 1 3672 ? 150.052 145.672 129.425 1.00 178.89 ? 3672 SER A O     1 
ATOM   14172 C CB    . SER A 1 3672 ? 150.838 147.403 127.066 1.00 178.89 ? 3672 SER A CB    1 
ATOM   14173 O OG    . SER A 1 3672 ? 151.425 146.320 126.366 1.00 178.89 ? 3672 SER A OG    1 
ATOM   14174 N N     . PRO A 1 3673 ? 148.839 144.673 127.830 1.00 170.84 ? 3673 PRO A N     1 
ATOM   14175 C CA    . PRO A 1 3673 ? 148.814 143.403 128.564 1.00 170.84 ? 3673 PRO A CA    1 
ATOM   14176 C C     . PRO A 1 3673 ? 150.213 142.832 128.738 1.00 170.84 ? 3673 PRO A C     1 
ATOM   14177 O O     . PRO A 1 3673 ? 151.199 143.327 128.188 1.00 170.84 ? 3673 PRO A O     1 
ATOM   14178 C CB    . PRO A 1 3673 ? 147.938 142.496 127.693 1.00 170.84 ? 3673 PRO A CB    1 
ATOM   14179 C CG    . PRO A 1 3673 ? 147.930 143.137 126.347 1.00 170.84 ? 3673 PRO A CG    1 
ATOM   14180 C CD    . PRO A 1 3673 ? 148.071 144.607 126.577 1.00 170.84 ? 3673 PRO A CD    1 
ATOM   14181 N N     . SER A 1 3674 ? 150.283 141.758 129.526 1.00 167.77 ? 3674 SER A N     1 
ATOM   14182 C CA    . SER A 1 3674 ? 151.553 141.142 129.911 1.00 167.77 ? 3674 SER A CA    1 
ATOM   14183 C C     . SER A 1 3674 ? 152.465 142.152 130.604 1.00 167.77 ? 3674 SER A C     1 
ATOM   14184 O O     . SER A 1 3674 ? 153.672 142.197 130.362 1.00 167.77 ? 3674 SER A O     1 
ATOM   14185 C CB    . SER A 1 3674 ? 152.254 140.509 128.707 1.00 167.77 ? 3674 SER A CB    1 
ATOM   14186 O OG    . SER A 1 3674 ? 153.249 141.375 128.191 1.00 167.77 ? 3674 SER A OG    1 
ATOM   14187 N N     . PHE A 1 3675 ? 151.877 142.972 131.472 1.00 157.52 ? 3675 PHE A N     1 
ATOM   14188 C CA    . PHE A 1 3675 ? 152.604 143.960 132.260 1.00 157.52 ? 3675 PHE A CA    1 
ATOM   14189 C C     . PHE A 1 3675 ? 152.674 143.483 133.704 1.00 157.52 ? 3675 PHE A C     1 
ATOM   14190 O O     . PHE A 1 3675 ? 151.639 143.209 134.320 1.00 157.52 ? 3675 PHE A O     1 
ATOM   14191 C CB    . PHE A 1 3675 ? 151.925 145.326 132.191 1.00 157.52 ? 3675 PHE A CB    1 
ATOM   14192 C CG    . PHE A 1 3675 ? 152.196 146.192 133.386 1.00 157.52 ? 3675 PHE A CG    1 
ATOM   14193 C CD1   . PHE A 1 3675 ? 153.451 146.735 133.594 1.00 157.52 ? 3675 PHE A CD1   1 
ATOM   14194 C CD2   . PHE A 1 3675 ? 151.201 146.447 134.313 1.00 157.52 ? 3675 PHE A CD2   1 
ATOM   14195 C CE1   . PHE A 1 3675 ? 153.704 147.528 134.694 1.00 157.52 ? 3675 PHE A CE1   1 
ATOM   14196 C CE2   . PHE A 1 3675 ? 151.449 147.237 135.415 1.00 157.52 ? 3675 PHE A CE2   1 
ATOM   14197 C CZ    . PHE A 1 3675 ? 152.702 147.778 135.606 1.00 157.52 ? 3675 PHE A CZ    1 
ATOM   14198 N N     . VAL A 1 3676 ? 153.886 143.392 134.243 1.00 146.70 ? 3676 VAL A N     1 
ATOM   14199 C CA    . VAL A 1 3676 ? 154.089 142.956 135.616 1.00 146.70 ? 3676 VAL A CA    1 
ATOM   14200 C C     . VAL A 1 3676 ? 155.051 143.911 136.309 1.00 146.70 ? 3676 VAL A C     1 
ATOM   14201 O O     . VAL A 1 3676 ? 155.992 144.430 135.701 1.00 146.70 ? 3676 VAL A O     1 
ATOM   14202 C CB    . VAL A 1 3676 ? 154.607 141.501 135.690 1.00 146.70 ? 3676 VAL A CB    1 
ATOM   14203 C CG1   . VAL A 1 3676 ? 153.596 140.545 135.077 1.00 146.70 ? 3676 VAL A CG1   1 
ATOM   14204 C CG2   . VAL A 1 3676 ? 155.941 141.368 134.992 1.00 146.70 ? 3676 VAL A CG2   1 
ATOM   14205 N N     . ILE A 1 3677 ? 154.795 144.154 137.592 1.00 140.44 ? 3677 ILE A N     1 
ATOM   14206 C CA    . ILE A 1 3677 ? 155.647 144.981 138.438 1.00 140.44 ? 3677 ILE A CA    1 
ATOM   14207 C C     . ILE A 1 3677 ? 155.995 144.190 139.689 1.00 140.44 ? 3677 ILE A C     1 
ATOM   14208 O O     . ILE A 1 3677 ? 155.120 143.567 140.299 1.00 140.44 ? 3677 ILE A O     1 
ATOM   14209 C CB    . ILE A 1 3677 ? 154.979 146.324 138.801 1.00 140.44 ? 3677 ILE A CB    1 
ATOM   14210 C CG1   . ILE A 1 3677 ? 155.866 147.143 139.742 1.00 140.44 ? 3677 ILE A CG1   1 
ATOM   14211 C CG2   . ILE A 1 3677 ? 153.620 146.114 139.412 1.00 140.44 ? 3677 ILE A CG2   1 
ATOM   14212 C CD1   . ILE A 1 3677 ? 157.166 147.577 139.152 1.00 140.44 ? 3677 ILE A CD1   1 
ATOM   14213 N N     . PHE A 1 3678 ? 157.274 144.189 140.050 1.00 136.43 ? 3678 PHE A N     1 
ATOM   14214 C CA    . PHE A 1 3678 ? 157.766 143.472 141.224 1.00 136.43 ? 3678 PHE A CA    1 
ATOM   14215 C C     . PHE A 1 3678 ? 158.420 144.475 142.166 1.00 136.43 ? 3678 PHE A C     1 
ATOM   14216 O O     . PHE A 1 3678 ? 159.534 144.943 141.914 1.00 136.43 ? 3678 PHE A O     1 
ATOM   14217 C CB    . PHE A 1 3678 ? 158.742 142.371 140.822 1.00 136.43 ? 3678 PHE A CB    1 
ATOM   14218 C CG    . PHE A 1 3678 ? 158.165 141.367 139.867 1.00 136.43 ? 3678 PHE A CG    1 
ATOM   14219 C CD1   . PHE A 1 3678 ? 157.083 140.587 140.233 1.00 136.43 ? 3678 PHE A CD1   1 
ATOM   14220 C CD2   . PHE A 1 3678 ? 158.706 141.204 138.604 1.00 136.43 ? 3678 PHE A CD2   1 
ATOM   14221 C CE1   . PHE A 1 3678 ? 156.554 139.660 139.357 1.00 136.43 ? 3678 PHE A CE1   1 
ATOM   14222 C CE2   . PHE A 1 3678 ? 158.180 140.280 137.724 1.00 136.43 ? 3678 PHE A CE2   1 
ATOM   14223 C CZ    . PHE A 1 3678 ? 157.103 139.508 138.100 1.00 136.43 ? 3678 PHE A CZ    1 
ATOM   14224 N N     . LEU A 1 3679 ? 157.726 144.803 143.250 1.00 129.97 ? 3679 LEU A N     1 
ATOM   14225 C CA    . LEU A 1 3679 ? 158.298 145.659 144.280 1.00 129.97 ? 3679 LEU A CA    1 
ATOM   14226 C C     . LEU A 1 3679 ? 159.457 144.930 144.949 1.00 129.97 ? 3679 LEU A C     1 
ATOM   14227 O O     . LEU A 1 3679 ? 159.420 143.707 145.107 1.00 129.97 ? 3679 LEU A O     1 
ATOM   14228 C CB    . LEU A 1 3679 ? 157.232 146.030 145.308 1.00 129.97 ? 3679 LEU A CB    1 
ATOM   14229 C CG    . LEU A 1 3679 ? 155.915 146.678 144.860 1.00 129.97 ? 3679 LEU A CG    1 
ATOM   14230 C CD1   . LEU A 1 3679 ? 155.403 147.619 145.931 1.00 129.97 ? 3679 LEU A CD1   1 
ATOM   14231 C CD2   . LEU A 1 3679 ? 156.060 147.435 143.555 1.00 129.97 ? 3679 LEU A CD2   1 
ATOM   14232 N N     . SER A 1 3680 ? 160.494 145.671 145.335 1.00 138.94 ? 3680 SER A N     1 
ATOM   14233 C CA    . SER A 1 3680 ? 161.685 145.063 145.908 1.00 138.94 ? 3680 SER A CA    1 
ATOM   14234 C C     . SER A 1 3680 ? 162.241 145.913 147.041 1.00 138.94 ? 3680 SER A C     1 
ATOM   14235 O O     . SER A 1 3680 ? 162.012 147.121 147.120 1.00 138.94 ? 3680 SER A O     1 
ATOM   14236 C CB    . SER A 1 3680 ? 162.771 144.849 144.844 1.00 138.94 ? 3680 SER A CB    1 
ATOM   14237 O OG    . SER A 1 3680 ? 162.772 145.903 143.902 1.00 138.94 ? 3680 SER A OG    1 
ATOM   14238 N N     . THR A 1 3681 ? 162.989 145.249 147.919 1.00 138.01 ? 3681 THR A N     1 
ATOM   14239 C CA    . THR A 1 3681 ? 163.699 145.898 149.014 1.00 138.01 ? 3681 THR A CA    1 
ATOM   14240 C C     . THR A 1 3681 ? 164.852 145.002 149.436 1.00 138.01 ? 3681 THR A C     1 
ATOM   14241 O O     . THR A 1 3681 ? 164.954 143.848 149.013 1.00 138.01 ? 3681 THR A O     1 
ATOM   14242 C CB    . THR A 1 3681 ? 162.780 146.184 150.204 1.00 138.01 ? 3681 THR A CB    1 
ATOM   14243 O OG1   . THR A 1 3681 ? 163.577 146.513 151.350 1.00 138.01 ? 3681 THR A OG1   1 
ATOM   14244 C CG2   . THR A 1 3681 ? 161.939 144.973 150.525 1.00 138.01 ? 3681 THR A CG2   1 
ATOM   14245 N N     . ARG A 1 3682 ? 165.722 145.556 150.279 1.00 138.55 ? 3682 ARG A N     1 
ATOM   14246 C CA    . ARG A 1 3682 ? 166.868 144.832 150.809 1.00 138.55 ? 3682 ARG A CA    1 
ATOM   14247 C C     . ARG A 1 3682 ? 166.869 144.692 152.324 1.00 138.55 ? 3682 ARG A C     1 
ATOM   14248 O O     . ARG A 1 3682 ? 167.718 143.966 152.853 1.00 138.55 ? 3682 ARG A O     1 
ATOM   14249 C CB    . ARG A 1 3682 ? 168.177 145.519 150.393 1.00 138.55 ? 3682 ARG A CB    1 
ATOM   14250 C CG    . ARG A 1 3682 ? 168.261 145.887 148.925 1.00 138.55 ? 3682 ARG A CG    1 
ATOM   14251 C CD    . ARG A 1 3682 ? 168.159 144.646 148.058 1.00 138.55 ? 3682 ARG A CD    1 
ATOM   14252 N NE    . ARG A 1 3682 ? 169.246 143.714 148.332 1.00 138.55 ? 3682 ARG A NE    1 
ATOM   14253 C CZ    . ARG A 1 3682 ? 170.514 143.914 147.997 1.00 138.55 ? 3682 ARG A CZ    1 
ATOM   14254 N NH1   . ARG A 1 3682 ? 170.896 144.998 147.341 1.00 138.55 ? 3682 ARG A NH1   1 
ATOM   14255 N NH2   . ARG A 1 3682 ? 171.422 143.000 148.324 1.00 138.55 ? 3682 ARG A NH2   1 
ATOM   14256 N N     . ASP A 1 3683 ? 165.954 145.353 153.032 1.00 136.37 ? 3683 ASP A N     1 
ATOM   14257 C CA    . ASP A 1 3683 ? 166.026 145.428 154.481 1.00 136.37 ? 3683 ASP A CA    1 
ATOM   14258 C C     . ASP A 1 3683 ? 164.945 144.532 155.066 1.00 136.37 ? 3683 ASP A C     1 
ATOM   14259 O O     . ASP A 1 3683 ? 163.755 144.791 154.838 1.00 136.37 ? 3683 ASP A O     1 
ATOM   14260 C CB    . ASP A 1 3683 ? 165.859 146.876 154.933 1.00 136.37 ? 3683 ASP A CB    1 
ATOM   14261 C CG    . ASP A 1 3683 ? 165.535 147.047 156.428 1.00 136.37 ? 3683 ASP A CG    1 
ATOM   14262 O OD1   . ASP A 1 3683 ? 164.981 146.150 157.094 1.00 136.37 ? 3683 ASP A OD1   1 
ATOM   14263 O OD2   . ASP A 1 3683 ? 165.838 148.139 156.951 1.00 136.37 ? 3683 ASP A OD2   1 
ATOM   14264 N N     . PRO A 1 3684 ? 165.304 143.466 155.787 1.00 130.31 ? 3684 PRO A N     1 
ATOM   14265 C CA    . PRO A 1 3684 ? 164.280 142.631 156.420 1.00 130.31 ? 3684 PRO A CA    1 
ATOM   14266 C C     . PRO A 1 3684 ? 163.268 143.385 157.264 1.00 130.31 ? 3684 PRO A C     1 
ATOM   14267 O O     . PRO A 1 3684 ? 162.069 143.069 157.202 1.00 130.31 ? 3684 PRO A O     1 
ATOM   14268 C CB    . PRO A 1 3684 ? 165.136 141.719 157.301 1.00 130.31 ? 3684 PRO A CB    1 
ATOM   14269 C CG    . PRO A 1 3684 ? 166.406 141.498 156.448 1.00 130.31 ? 3684 PRO A CG    1 
ATOM   14270 C CD    . PRO A 1 3684 ? 166.375 142.561 155.324 1.00 130.31 ? 3684 PRO A CD    1 
ATOM   14271 N N     . THR A 1 3685 ? 163.699 144.363 158.055 1.00 130.27 ? 3685 THR A N     1 
ATOM   14272 C CA    . THR A 1 3685 ? 162.824 145.001 159.041 1.00 130.27 ? 3685 THR A CA    1 
ATOM   14273 C C     . THR A 1 3685 ? 162.316 146.333 158.490 1.00 130.27 ? 3685 THR A C     1 
ATOM   14274 O O     . THR A 1 3685 ? 162.842 147.409 158.781 1.00 130.27 ? 3685 THR A O     1 
ATOM   14275 C CB    . THR A 1 3685 ? 163.552 145.172 160.375 1.00 130.27 ? 3685 THR A CB    1 
ATOM   14276 O OG1   . THR A 1 3685 ? 162.822 146.080 161.212 1.00 130.27 ? 3685 THR A OG1   1 
ATOM   14277 C CG2   . THR A 1 3685 ? 164.974 145.681 160.170 1.00 130.27 ? 3685 THR A CG2   1 
ATOM   14278 N N     . VAL A 1 3686 ? 161.273 146.247 157.669 1.00 130.20 ? 3686 VAL A N     1 
ATOM   14279 C CA    . VAL A 1 3686 ? 160.572 147.420 157.169 1.00 130.20 ? 3686 VAL A CA    1 
ATOM   14280 C C     . VAL A 1 3686 ? 159.097 147.258 157.517 1.00 130.20 ? 3686 VAL A C     1 
ATOM   14281 O O     . VAL A 1 3686 ? 158.472 146.257 157.140 1.00 130.20 ? 3686 VAL A O     1 
ATOM   14282 C CB    . VAL A 1 3686 ? 160.744 147.607 155.651 1.00 130.20 ? 3686 VAL A CB    1 
ATOM   14283 C CG1   . VAL A 1 3686 ? 160.153 148.932 155.214 1.00 130.20 ? 3686 VAL A CG1   1 
ATOM   14284 C CG2   . VAL A 1 3686 ? 162.209 147.537 155.275 1.00 130.20 ? 3686 VAL A CG2   1 
ATOM   14285 N N     . GLU A 1 3687 ? 158.540 148.234 158.227 1.00 131.86 ? 3687 GLU A N     1 
ATOM   14286 C CA    . GLU A 1 3687 ? 157.136 148.223 158.620 1.00 131.86 ? 3687 GLU A CA    1 
ATOM   14287 C C     . GLU A 1 3687 ? 156.360 149.043 157.598 1.00 131.86 ? 3687 GLU A C     1 
ATOM   14288 O O     . GLU A 1 3687 ? 156.450 150.272 157.569 1.00 131.86 ? 3687 GLU A O     1 
ATOM   14289 C CB    . GLU A 1 3687 ? 156.963 148.774 160.030 1.00 131.86 ? 3687 GLU A CB    1 
ATOM   14290 C CG    . GLU A 1 3687 ? 157.516 147.875 161.121 1.00 131.86 ? 3687 GLU A CG    1 
ATOM   14291 C CD    . GLU A 1 3687 ? 156.538 146.797 161.543 1.00 131.86 ? 3687 GLU A CD    1 
ATOM   14292 O OE1   . GLU A 1 3687 ? 156.979 145.780 162.117 1.00 131.86 ? 3687 GLU A OE1   1 
ATOM   14293 O OE2   . GLU A 1 3687 ? 155.324 146.969 161.300 1.00 131.86 ? 3687 GLU A OE2   1 
ATOM   14294 N N     . PHE A 1 3688 ? 155.605 148.358 156.749 1.00 124.15 ? 3688 PHE A N     1 
ATOM   14295 C CA    . PHE A 1 3688 ? 154.847 149.028 155.708 1.00 124.15 ? 3688 PHE A CA    1 
ATOM   14296 C C     . PHE A 1 3688 ? 153.472 149.448 156.222 1.00 124.15 ? 3688 PHE A C     1 
ATOM   14297 O O     . PHE A 1 3688 ? 152.908 148.804 157.111 1.00 124.15 ? 3688 PHE A O     1 
ATOM   14298 C CB    . PHE A 1 3688 ? 154.688 148.111 154.505 1.00 124.15 ? 3688 PHE A CB    1 
ATOM   14299 C CG    . PHE A 1 3688 ? 155.982 147.554 154.004 1.00 124.15 ? 3688 PHE A CG    1 
ATOM   14300 C CD1   . PHE A 1 3688 ? 156.773 148.284 153.139 1.00 124.15 ? 3688 PHE A CD1   1 
ATOM   14301 C CD2   . PHE A 1 3688 ? 156.415 146.305 154.411 1.00 124.15 ? 3688 PHE A CD2   1 
ATOM   14302 C CE1   . PHE A 1 3688 ? 157.967 147.774 152.679 1.00 124.15 ? 3688 PHE A CE1   1 
ATOM   14303 C CE2   . PHE A 1 3688 ? 157.609 145.791 153.955 1.00 124.15 ? 3688 PHE A CE2   1 
ATOM   14304 C CZ    . PHE A 1 3688 ? 158.387 146.527 153.087 1.00 124.15 ? 3688 PHE A CZ    1 
ATOM   14305 N N     . PRO A 1 3689 ? 152.912 150.530 155.680 1.00 117.09 ? 3689 PRO A N     1 
ATOM   14306 C CA    . PRO A 1 3689 ? 151.558 150.916 156.065 1.00 117.09 ? 3689 PRO A CA    1 
ATOM   14307 C C     . PRO A 1 3689 ? 150.550 149.894 155.575 1.00 117.09 ? 3689 PRO A C     1 
ATOM   14308 O O     . PRO A 1 3689 ? 150.782 149.208 154.564 1.00 117.09 ? 3689 PRO A O     1 
ATOM   14309 C CB    . PRO A 1 3689 ? 151.365 152.275 155.368 1.00 117.09 ? 3689 PRO A CB    1 
ATOM   14310 C CG    . PRO A 1 3689 ? 152.335 152.258 154.239 1.00 117.09 ? 3689 PRO A CG    1 
ATOM   14311 C CD    . PRO A 1 3689 ? 153.513 151.477 154.726 1.00 117.09 ? 3689 PRO A CD    1 
ATOM   14312 N N     . PRO A 1 3690 ? 149.415 149.749 156.264 1.00 113.46 ? 3690 PRO A N     1 
ATOM   14313 C CA    . PRO A 1 3690 ? 148.432 148.731 155.855 1.00 113.46 ? 3690 PRO A CA    1 
ATOM   14314 C C     . PRO A 1 3690 ? 147.897 148.910 154.444 1.00 113.46 ? 3690 PRO A C     1 
ATOM   14315 O O     . PRO A 1 3690 ? 147.528 147.916 153.807 1.00 113.46 ? 3690 PRO A O     1 
ATOM   14316 C CB    . PRO A 1 3690 ? 147.320 148.883 156.902 1.00 113.46 ? 3690 PRO A CB    1 
ATOM   14317 C CG    . PRO A 1 3690 ? 147.995 149.488 158.083 1.00 113.46 ? 3690 PRO A CG    1 
ATOM   14318 C CD    . PRO A 1 3690 ? 149.041 150.404 157.527 1.00 113.46 ? 3690 PRO A CD    1 
ATOM   14319 N N     . ASP A 1 3691 ? 147.825 150.143 153.936 1.00 114.08 ? 3691 ASP A N     1 
ATOM   14320 C CA    . ASP A 1 3691 ? 147.361 150.335 152.565 1.00 114.08 ? 3691 ASP A CA    1 
ATOM   14321 C C     . ASP A 1 3691 ? 148.306 149.671 151.572 1.00 114.08 ? 3691 ASP A C     1 
ATOM   14322 O O     . ASP A 1 3691 ? 147.865 149.061 150.592 1.00 114.08 ? 3691 ASP A O     1 
ATOM   14323 C CB    . ASP A 1 3691 ? 147.204 151.826 152.260 1.00 114.08 ? 3691 ASP A CB    1 
ATOM   14324 C CG    . ASP A 1 3691 ? 148.532 152.551 152.160 1.00 114.08 ? 3691 ASP A CG    1 
ATOM   14325 O OD1   . ASP A 1 3691 ? 149.525 152.066 152.741 1.00 114.08 ? 3691 ASP A OD1   1 
ATOM   14326 O OD2   . ASP A 1 3691 ? 148.584 153.606 151.493 1.00 114.08 ? 3691 ASP A OD2   1 
ATOM   14327 N N     . LEU A 1 3692 ? 149.613 149.781 151.811 1.00 113.26 ? 3692 LEU A N     1 
ATOM   14328 C CA    . LEU A 1 3692 ? 150.580 149.048 151.006 1.00 113.26 ? 3692 LEU A CA    1 
ATOM   14329 C C     . LEU A 1 3692 ? 150.501 147.557 151.303 1.00 113.26 ? 3692 LEU A C     1 
ATOM   14330 O O     . LEU A 1 3692 ? 150.782 146.731 150.429 1.00 113.26 ? 3692 LEU A O     1 
ATOM   14331 C CB    . LEU A 1 3692 ? 151.984 149.583 151.289 1.00 113.26 ? 3692 LEU A CB    1 
ATOM   14332 C CG    . LEU A 1 3692 ? 153.241 149.015 150.628 1.00 113.26 ? 3692 LEU A CG    1 
ATOM   14333 C CD1   . LEU A 1 3692 ? 152.972 148.519 149.226 1.00 113.26 ? 3692 LEU A CD1   1 
ATOM   14334 C CD2   . LEU A 1 3692 ? 154.342 150.059 150.619 1.00 113.26 ? 3692 LEU A CD2   1 
ATOM   14335 N N     . CYS A 1 3693 ? 150.109 147.200 152.527 1.00 115.74 ? 3693 CYS A N     1 
ATOM   14336 C CA    . CYS A 1 3693 ? 150.032 145.796 152.917 1.00 115.74 ? 3693 CYS A CA    1 
ATOM   14337 C C     . CYS A 1 3693 ? 148.955 145.053 152.137 1.00 115.74 ? 3693 CYS A C     1 
ATOM   14338 O O     . CYS A 1 3693 ? 149.174 143.926 151.681 1.00 115.74 ? 3693 CYS A O     1 
ATOM   14339 C CB    . CYS A 1 3693 ? 149.763 145.694 154.416 1.00 115.74 ? 3693 CYS A CB    1 
ATOM   14340 S SG    . CYS A 1 3693 ? 150.554 144.309 155.234 1.00 115.74 ? 3693 CYS A SG    1 
ATOM   14341 N N     . SER A 1 3694 ? 147.784 145.666 151.980 1.00 111.16 ? 3694 SER A N     1 
ATOM   14342 C CA    . SER A 1 3694 ? 146.648 144.971 151.390 1.00 111.16 ? 3694 SER A CA    1 
ATOM   14343 C C     . SER A 1 3694 ? 146.793 144.748 149.892 1.00 111.16 ? 3694 SER A C     1 
ATOM   14344 O O     . SER A 1 3694 ? 146.287 143.744 149.379 1.00 111.16 ? 3694 SER A O     1 
ATOM   14345 C CB    . SER A 1 3694 ? 145.360 145.745 151.661 1.00 111.16 ? 3694 SER A CB    1 
ATOM   14346 O OG    . SER A 1 3694 ? 145.061 146.613 150.585 1.00 111.16 ? 3694 SER A OG    1 
ATOM   14347 N N     . ARG A 1 3695 ? 147.466 145.647 149.180 1.00 118.44 ? 3695 ARG A N     1 
ATOM   14348 C CA    . ARG A 1 3695 ? 147.537 145.589 147.728 1.00 118.44 ? 3695 ARG A CA    1 
ATOM   14349 C C     . ARG A 1 3695 ? 148.631 144.669 147.211 1.00 118.44 ? 3695 ARG A C     1 
ATOM   14350 O O     . ARG A 1 3695 ? 148.713 144.454 145.998 1.00 118.44 ? 3695 ARG A O     1 
ATOM   14351 C CB    . ARG A 1 3695 ? 147.764 146.991 147.156 1.00 118.44 ? 3695 ARG A CB    1 
ATOM   14352 C CG    . ARG A 1 3695 ? 146.603 147.933 147.367 1.00 118.44 ? 3695 ARG A CG    1 
ATOM   14353 C CD    . ARG A 1 3695 ? 147.054 149.378 147.305 1.00 118.44 ? 3695 ARG A CD    1 
ATOM   14354 N NE    . ARG A 1 3695 ? 145.916 150.287 147.328 1.00 118.44 ? 3695 ARG A NE    1 
ATOM   14355 C CZ    . ARG A 1 3695 ? 145.274 150.648 148.430 1.00 118.44 ? 3695 ARG A CZ    1 
ATOM   14356 N NH1   . ARG A 1 3695 ? 145.651 150.216 149.622 1.00 118.44 ? 3695 ARG A NH1   1 
ATOM   14357 N NH2   . ARG A 1 3695 ? 144.226 151.461 148.334 1.00 118.44 ? 3695 ARG A NH2   1 
ATOM   14358 N N     . VAL A 1 3696 ? 149.473 144.128 148.089 1.00 116.02 ? 3696 VAL A N     1 
ATOM   14359 C CA    . VAL A 1 3696 ? 150.688 143.440 147.682 1.00 116.02 ? 3696 VAL A CA    1 
ATOM   14360 C C     . VAL A 1 3696 ? 150.761 142.077 148.355 1.00 116.02 ? 3696 VAL A C     1 
ATOM   14361 O O     . VAL A 1 3696 ? 150.267 141.876 149.467 1.00 116.02 ? 3696 VAL A O     1 
ATOM   14362 C CB    . VAL A 1 3696 ? 151.941 144.279 148.013 1.00 116.02 ? 3696 VAL A CB    1 
ATOM   14363 C CG1   . VAL A 1 3696 ? 153.152 143.729 147.321 1.00 116.02 ? 3696 VAL A CG1   1 
ATOM   14364 C CG2   . VAL A 1 3696 ? 151.730 145.708 147.579 1.00 116.02 ? 3696 VAL A CG2   1 
ATOM   14365 N N     . THR A 1 3697 ? 151.382 141.130 147.656 1.00 116.96 ? 3697 THR A N     1 
ATOM   14366 C CA    . THR A 1 3697 ? 151.653 139.800 148.189 1.00 116.96 ? 3697 THR A CA    1 
ATOM   14367 C C     . THR A 1 3697 ? 153.094 139.778 148.680 1.00 116.96 ? 3697 THR A C     1 
ATOM   14368 O O     . THR A 1 3697 ? 154.030 139.912 147.885 1.00 116.96 ? 3697 THR A O     1 
ATOM   14369 C CB    . THR A 1 3697 ? 151.427 138.723 147.131 1.00 116.96 ? 3697 THR A CB    1 
ATOM   14370 O OG1   . THR A 1 3697 ? 152.017 139.139 145.894 1.00 116.96 ? 3697 THR A OG1   1 
ATOM   14371 C CG2   . THR A 1 3697 ? 149.945 138.489 146.916 1.00 116.96 ? 3697 THR A CG2   1 
ATOM   14372 N N     . PHE A 1 3698 ? 153.273 139.608 149.985 1.00 118.54 ? 3698 PHE A N     1 
ATOM   14373 C CA    . PHE A 1 3698 ? 154.606 139.598 150.574 1.00 118.54 ? 3698 PHE A CA    1 
ATOM   14374 C C     . PHE A 1 3698 ? 155.288 138.273 150.263 1.00 118.54 ? 3698 PHE A C     1 
ATOM   14375 O O     . PHE A 1 3698 ? 154.774 137.206 150.612 1.00 118.54 ? 3698 PHE A O     1 
ATOM   14376 C CB    . PHE A 1 3698 ? 154.522 139.803 152.082 1.00 118.54 ? 3698 PHE A CB    1 
ATOM   14377 C CG    . PHE A 1 3698 ? 154.108 141.182 152.497 1.00 118.54 ? 3698 PHE A CG    1 
ATOM   14378 C CD1   . PHE A 1 3698 ? 152.797 141.597 152.362 1.00 118.54 ? 3698 PHE A CD1   1 
ATOM   14379 C CD2   . PHE A 1 3698 ? 155.027 142.053 153.051 1.00 118.54 ? 3698 PHE A CD2   1 
ATOM   14380 C CE1   . PHE A 1 3698 ? 152.414 142.860 152.756 1.00 118.54 ? 3698 PHE A CE1   1 
ATOM   14381 C CE2   . PHE A 1 3698 ? 154.649 143.317 153.449 1.00 118.54 ? 3698 PHE A CE2   1 
ATOM   14382 C CZ    . PHE A 1 3698 ? 153.343 143.721 153.300 1.00 118.54 ? 3698 PHE A CZ    1 
ATOM   14383 N N     . VAL A 1 3699 ? 156.448 138.330 149.619 1.00 115.29 ? 3699 VAL A N     1 
ATOM   14384 C CA    . VAL A 1 3699 ? 157.302 137.163 149.437 1.00 115.29 ? 3699 VAL A CA    1 
ATOM   14385 C C     . VAL A 1 3699 ? 158.619 137.440 150.151 1.00 115.29 ? 3699 VAL A C     1 
ATOM   14386 O O     . VAL A 1 3699 ? 159.265 138.466 149.908 1.00 115.29 ? 3699 VAL A O     1 
ATOM   14387 C CB    . VAL A 1 3699 ? 157.508 136.830 147.952 1.00 115.29 ? 3699 VAL A CB    1 
ATOM   14388 C CG1   . VAL A 1 3699 ? 157.988 138.039 147.182 1.00 115.29 ? 3699 VAL A CG1   1 
ATOM   14389 C CG2   . VAL A 1 3699 ? 158.489 135.691 147.804 1.00 115.29 ? 3699 VAL A CG2   1 
ATOM   14390 N N     . ASN A 1 3700 ? 159.005 136.539 151.049 1.00 115.50 ? 3700 ASN A N     1 
ATOM   14391 C CA    . ASN A 1 3700 ? 160.112 136.768 151.967 1.00 115.50 ? 3700 ASN A CA    1 
ATOM   14392 C C     . ASN A 1 3700 ? 161.227 135.767 151.710 1.00 115.50 ? 3700 ASN A C     1 
ATOM   14393 O O     . ASN A 1 3700 ? 160.968 134.568 151.562 1.00 115.50 ? 3700 ASN A O     1 
ATOM   14394 C CB    . ASN A 1 3700 ? 159.639 136.664 153.415 1.00 115.50 ? 3700 ASN A CB    1 
ATOM   14395 C CG    . ASN A 1 3700 ? 160.688 137.117 154.401 1.00 115.50 ? 3700 ASN A CG    1 
ATOM   14396 O OD1   . ASN A 1 3700 ? 161.777 137.536 154.015 1.00 115.50 ? 3700 ASN A OD1   1 
ATOM   14397 N ND2   . ASN A 1 3700 ? 160.366 137.038 155.686 1.00 115.50 ? 3700 ASN A ND2   1 
ATOM   14398 N N     . PHE A 1 3701 ? 162.466 136.261 151.669 1.00 119.07 ? 3701 PHE A N     1 
ATOM   14399 C CA    . PHE A 1 3701 ? 163.643 135.430 151.457 1.00 119.07 ? 3701 PHE A CA    1 
ATOM   14400 C C     . PHE A 1 3701 ? 164.578 135.420 152.660 1.00 119.07 ? 3701 PHE A C     1 
ATOM   14401 O O     . PHE A 1 3701 ? 165.701 134.918 152.560 1.00 119.07 ? 3701 PHE A O     1 
ATOM   14402 C CB    . PHE A 1 3701 ? 164.415 135.890 150.220 1.00 119.07 ? 3701 PHE A CB    1 
ATOM   14403 C CG    . PHE A 1 3701 ? 163.817 135.441 148.925 1.00 119.07 ? 3701 PHE A CG    1 
ATOM   14404 C CD1   . PHE A 1 3701 ? 162.500 135.717 148.619 1.00 119.07 ? 3701 PHE A CD1   1 
ATOM   14405 C CD2   . PHE A 1 3701 ? 164.572 134.725 148.017 1.00 119.07 ? 3701 PHE A CD2   1 
ATOM   14406 C CE1   . PHE A 1 3701 ? 161.955 135.301 147.430 1.00 119.07 ? 3701 PHE A CE1   1 
ATOM   14407 C CE2   . PHE A 1 3701 ? 164.028 134.302 146.828 1.00 119.07 ? 3701 PHE A CE2   1 
ATOM   14408 C CZ    . PHE A 1 3701 ? 162.718 134.592 146.533 1.00 119.07 ? 3701 PHE A CZ    1 
ATOM   14409 N N     . THR A 1 3702 ? 164.147 135.969 153.792 1.00 116.63 ? 3702 THR A N     1 
ATOM   14410 C CA    . THR A 1 3702 ? 165.033 136.072 154.943 1.00 116.63 ? 3702 THR A CA    1 
ATOM   14411 C C     . THR A 1 3702 ? 165.364 134.690 155.486 1.00 116.63 ? 3702 THR A C     1 
ATOM   14412 O O     . THR A 1 3702 ? 164.473 133.864 155.704 1.00 116.63 ? 3702 THR A O     1 
ATOM   14413 C CB    . THR A 1 3702 ? 164.391 136.921 156.037 1.00 116.63 ? 3702 THR A CB    1 
ATOM   14414 O OG1   . THR A 1 3702 ? 163.017 136.545 156.190 1.00 116.63 ? 3702 THR A OG1   1 
ATOM   14415 C CG2   . THR A 1 3702 ? 164.471 138.394 155.679 1.00 116.63 ? 3702 THR A CG2   1 
ATOM   14416 N N     . VAL A 1 3703 ? 166.649 134.442 155.707 1.00 102.11 ? 3703 VAL A N     1 
ATOM   14417 C CA    . VAL A 1 3703 ? 167.098 133.169 156.254 1.00 102.11 ? 3703 VAL A CA    1 
ATOM   14418 C C     . VAL A 1 3703 ? 166.862 133.165 157.758 1.00 102.11 ? 3703 VAL A C     1 
ATOM   14419 O O     . VAL A 1 3703 ? 167.199 134.126 158.458 1.00 102.11 ? 3703 VAL A O     1 
ATOM   14420 C CB    . VAL A 1 3703 ? 168.574 132.919 155.910 1.00 102.11 ? 3703 VAL A CB    1 
ATOM   14421 C CG1   . VAL A 1 3703 ? 168.725 132.687 154.421 1.00 102.11 ? 3703 VAL A CG1   1 
ATOM   14422 C CG2   . VAL A 1 3703 ? 169.427 134.100 156.334 1.00 102.11 ? 3703 VAL A CG2   1 
ATOM   14423 N N     . THR A 1 3704 ? 166.259 132.095 158.255 1.00 100.57 ? 3704 THR A N     1 
ATOM   14424 C CA    . THR A 1 3704 ? 165.894 131.968 159.656 1.00 100.57 ? 3704 THR A CA    1 
ATOM   14425 C C     . THR A 1 3704 ? 166.536 130.718 160.244 1.00 100.57 ? 3704 THR A C     1 
ATOM   14426 O O     . THR A 1 3704 ? 167.341 130.043 159.600 1.00 100.57 ? 3704 THR A O     1 
ATOM   14427 C CB    . THR A 1 3704 ? 164.375 131.912 159.820 1.00 100.57 ? 3704 THR A CB    1 
ATOM   14428 O OG1   . THR A 1 3704 ? 163.900 130.639 159.367 1.00 100.57 ? 3704 THR A OG1   1 
ATOM   14429 C CG2   . THR A 1 3704 ? 163.714 133.008 159.005 1.00 100.57 ? 3704 THR A CG2   1 
ATOM   14430 N N     . ARG A 1 3705 ? 166.171 130.416 161.491 1.00 99.46  ? 3705 ARG A N     1 
ATOM   14431 C CA    . ARG A 1 3705 ? 166.635 129.182 162.115 1.00 99.46  ? 3705 ARG A CA    1 
ATOM   14432 C C     . ARG A 1 3705 ? 166.158 127.969 161.331 1.00 99.46  ? 3705 ARG A C     1 
ATOM   14433 O O     . ARG A 1 3705 ? 166.956 127.110 160.941 1.00 99.46  ? 3705 ARG A O     1 
ATOM   14434 C CB    . ARG A 1 3705 ? 166.144 129.108 163.561 1.00 99.46  ? 3705 ARG A CB    1 
ATOM   14435 C CG    . ARG A 1 3705 ? 166.780 130.116 164.495 1.00 99.46  ? 3705 ARG A CG    1 
ATOM   14436 C CD    . ARG A 1 3705 ? 167.979 129.520 165.205 1.00 99.46  ? 3705 ARG A CD    1 
ATOM   14437 N NE    . ARG A 1 3705 ? 168.702 130.524 165.974 1.00 99.46  ? 3705 ARG A NE    1 
ATOM   14438 C CZ    . ARG A 1 3705 ? 169.849 130.303 166.601 1.00 99.46  ? 3705 ARG A CZ    1 
ATOM   14439 N NH1   . ARG A 1 3705 ? 170.438 129.119 166.567 1.00 99.46  ? 3705 ARG A NH1   1 
ATOM   14440 N NH2   . ARG A 1 3705 ? 170.421 131.296 167.275 1.00 99.46  ? 3705 ARG A NH2   1 
ATOM   14441 N N     . SER A 1 3706 ? 164.853 127.897 161.072 1.00 106.51 ? 3706 SER A N     1 
ATOM   14442 C CA    . SER A 1 3706 ? 164.302 126.736 160.389 1.00 106.51 ? 3706 SER A CA    1 
ATOM   14443 C C     . SER A 1 3706 ? 164.755 126.680 158.937 1.00 106.51 ? 3706 SER A C     1 
ATOM   14444 O O     . SER A 1 3706 ? 165.009 125.594 158.405 1.00 106.51 ? 3706 SER A O     1 
ATOM   14445 C CB    . SER A 1 3706 ? 162.780 126.755 160.483 1.00 106.51 ? 3706 SER A CB    1 
ATOM   14446 O OG    . SER A 1 3706 ? 162.368 126.808 161.836 1.00 106.51 ? 3706 SER A OG    1 
ATOM   14447 N N     . SER A 1 3707 ? 164.867 127.835 158.280 1.00 108.76 ? 3707 SER A N     1 
ATOM   14448 C CA    . SER A 1 3707 ? 165.262 127.844 156.875 1.00 108.76 ? 3707 SER A CA    1 
ATOM   14449 C C     . SER A 1 3707 ? 166.664 127.276 156.694 1.00 108.76 ? 3707 SER A C     1 
ATOM   14450 O O     . SER A 1 3707 ? 166.875 126.347 155.905 1.00 108.76 ? 3707 SER A O     1 
ATOM   14451 C CB    . SER A 1 3707 ? 165.184 129.265 156.320 1.00 108.76 ? 3707 SER A CB    1 
ATOM   14452 O OG    . SER A 1 3707 ? 165.751 129.332 155.023 1.00 108.76 ? 3707 SER A OG    1 
ATOM   14453 N N     . LEU A 1 3708 ? 167.635 127.809 157.436 1.00 103.87 ? 3708 LEU A N     1 
ATOM   14454 C CA    . LEU A 1 3708 ? 168.995 127.299 157.322 1.00 103.87 ? 3708 LEU A CA    1 
ATOM   14455 C C     . LEU A 1 3708 ? 169.104 125.888 157.871 1.00 103.87 ? 3708 LEU A C     1 
ATOM   14456 O O     . LEU A 1 3708 ? 169.907 125.093 157.374 1.00 103.87 ? 3708 LEU A O     1 
ATOM   14457 C CB    . LEU A 1 3708 ? 169.972 128.224 158.041 1.00 103.87 ? 3708 LEU A CB    1 
ATOM   14458 C CG    . LEU A 1 3708 ? 171.422 128.142 157.564 1.00 103.87 ? 3708 LEU A CG    1 
ATOM   14459 C CD1   . LEU A 1 3708 ? 171.489 127.770 156.095 1.00 103.87 ? 3708 LEU A CD1   1 
ATOM   14460 C CD2   . LEU A 1 3708 ? 172.126 129.460 157.800 1.00 103.87 ? 3708 LEU A CD2   1 
ATOM   14461 N N     . GLN A 1 3709 ? 168.305 125.559 158.886 1.00 104.02 ? 3709 GLN A N     1 
ATOM   14462 C CA    . GLN A 1 3709 ? 168.295 124.204 159.419 1.00 104.02 ? 3709 GLN A CA    1 
ATOM   14463 C C     . GLN A 1 3709 ? 167.905 123.203 158.337 1.00 104.02 ? 3709 GLN A C     1 
ATOM   14464 O O     . GLN A 1 3709 ? 168.598 122.201 158.113 1.00 104.02 ? 3709 GLN A O     1 
ATOM   14465 C CB    . GLN A 1 3709 ? 167.332 124.144 160.605 1.00 104.02 ? 3709 GLN A CB    1 
ATOM   14466 C CG    . GLN A 1 3709 ? 167.487 122.946 161.501 1.00 104.02 ? 3709 GLN A CG    1 
ATOM   14467 C CD    . GLN A 1 3709 ? 166.875 121.704 160.907 1.00 104.02 ? 3709 GLN A CD    1 
ATOM   14468 O OE1   . GLN A 1 3709 ? 167.547 120.690 160.744 1.00 104.02 ? 3709 GLN A OE1   1 
ATOM   14469 N NE2   . GLN A 1 3709 ? 165.596 121.779 160.564 1.00 104.02 ? 3709 GLN A NE2   1 
ATOM   14470 N N     . SER A 1 3710 ? 166.808 123.481 157.632 1.00 110.69 ? 3710 SER A N     1 
ATOM   14471 C CA    . SER A 1 3710 ? 166.360 122.598 156.563 1.00 110.69 ? 3710 SER A CA    1 
ATOM   14472 C C     . SER A 1 3710 ? 167.339 122.597 155.397 1.00 110.69 ? 3710 SER A C     1 
ATOM   14473 O O     . SER A 1 3710 ? 167.545 121.560 154.758 1.00 110.69 ? 3710 SER A O     1 
ATOM   14474 C CB    . SER A 1 3710 ? 164.966 123.011 156.096 1.00 110.69 ? 3710 SER A CB    1 
ATOM   14475 O OG    . SER A 1 3710 ? 164.871 124.417 155.962 1.00 110.69 ? 3710 SER A OG    1 
ATOM   14476 N N     . GLN A 1 3711 ? 167.947 123.746 155.095 1.00 111.00 ? 3711 GLN A N     1 
ATOM   14477 C CA    . GLN A 1 3711 ? 168.934 123.782 154.022 1.00 111.00 ? 3711 GLN A CA    1 
ATOM   14478 C C     . GLN A 1 3711 ? 170.123 122.889 154.340 1.00 111.00 ? 3711 GLN A C     1 
ATOM   14479 O O     . GLN A 1 3711 ? 170.581 122.117 153.487 1.00 111.00 ? 3711 GLN A O     1 
ATOM   14480 C CB    . GLN A 1 3711 ? 169.400 125.214 153.785 1.00 111.00 ? 3711 GLN A CB    1 
ATOM   14481 C CG    . GLN A 1 3711 ? 168.568 125.973 152.785 1.00 111.00 ? 3711 GLN A CG    1 
ATOM   14482 C CD    . GLN A 1 3711 ? 169.235 127.252 152.339 1.00 111.00 ? 3711 GLN A CD    1 
ATOM   14483 O OE1   . GLN A 1 3711 ? 170.397 127.250 151.934 1.00 111.00 ? 3711 GLN A OE1   1 
ATOM   14484 N NE2   . GLN A 1 3711 ? 168.505 128.357 152.417 1.00 111.00 ? 3711 GLN A NE2   1 
ATOM   14485 N N     . CYS A 1 3712 ? 170.635 122.976 155.567 1.00 108.51 ? 3712 CYS A N     1 
ATOM   14486 C CA    . CYS A 1 3712 ? 171.761 122.140 155.955 1.00 108.51 ? 3712 CYS A CA    1 
ATOM   14487 C C     . CYS A 1 3712 ? 171.373 120.671 155.950 1.00 108.51 ? 3712 CYS A C     1 
ATOM   14488 O O     . CYS A 1 3712 ? 172.166 119.815 155.543 1.00 108.51 ? 3712 CYS A O     1 
ATOM   14489 C CB    . CYS A 1 3712 ? 172.276 122.559 157.329 1.00 108.51 ? 3712 CYS A CB    1 
ATOM   14490 S SG    . CYS A 1 3712 ? 173.427 123.945 157.281 1.00 108.51 ? 3712 CYS A SG    1 
ATOM   14491 N N     . LEU A 1 3713 ? 170.156 120.355 156.399 1.00 108.98 ? 3713 LEU A N     1 
ATOM   14492 C CA    . LEU A 1 3713 ? 169.702 118.971 156.332 1.00 108.98 ? 3713 LEU A CA    1 
ATOM   14493 C C     . LEU A 1 3713 ? 169.674 118.471 154.895 1.00 108.98 ? 3713 LEU A C     1 
ATOM   14494 O O     . LEU A 1 3713 ? 170.163 117.375 154.601 1.00 108.98 ? 3713 LEU A O     1 
ATOM   14495 C CB    . LEU A 1 3713 ? 168.321 118.828 156.964 1.00 108.98 ? 3713 LEU A CB    1 
ATOM   14496 C CG    . LEU A 1 3713 ? 168.288 118.284 158.390 1.00 108.98 ? 3713 LEU A CG    1 
ATOM   14497 C CD1   . LEU A 1 3713 ? 166.866 118.277 158.919 1.00 108.98 ? 3713 LEU A CD1   1 
ATOM   14498 C CD2   . LEU A 1 3713 ? 168.893 116.894 158.441 1.00 108.98 ? 3713 LEU A CD2   1 
ATOM   14499 N N     . ASN A 1 3714 ? 169.108 119.259 153.983 1.00 119.88 ? 3714 ASN A N     1 
ATOM   14500 C CA    . ASN A 1 3714 ? 169.040 118.824 152.594 1.00 119.88 ? 3714 ASN A CA    1 
ATOM   14501 C C     . ASN A 1 3714 ? 170.437 118.615 152.032 1.00 119.88 ? 3714 ASN A C     1 
ATOM   14502 O O     . ASN A 1 3714 ? 170.697 117.620 151.347 1.00 119.88 ? 3714 ASN A O     1 
ATOM   14503 C CB    . ASN A 1 3714 ? 168.246 119.836 151.763 1.00 119.88 ? 3714 ASN A CB    1 
ATOM   14504 C CG    . ASN A 1 3714 ? 168.597 119.803 150.279 1.00 119.88 ? 3714 ASN A CG    1 
ATOM   14505 O OD1   . ASN A 1 3714 ? 169.689 120.197 149.865 1.00 119.88 ? 3714 ASN A OD1   1 
ATOM   14506 N ND2   . ASN A 1 3714 ? 167.660 119.323 149.470 1.00 119.88 ? 3714 ASN A ND2   1 
ATOM   14507 N N     . GLU A 1 3715 ? 171.359 119.529 152.340 1.00 118.05 ? 3715 GLU A N     1 
ATOM   14508 C CA    . GLU A 1 3715 ? 172.725 119.384 151.852 1.00 118.05 ? 3715 GLU A CA    1 
ATOM   14509 C C     . GLU A 1 3715 ? 173.382 118.127 152.408 1.00 118.05 ? 3715 GLU A C     1 
ATOM   14510 O O     . GLU A 1 3715 ? 174.092 117.419 151.684 1.00 118.05 ? 3715 GLU A O     1 
ATOM   14511 C CB    . GLU A 1 3715 ? 173.544 120.622 152.211 1.00 118.05 ? 3715 GLU A CB    1 
ATOM   14512 C CG    . GLU A 1 3715 ? 173.976 121.459 151.016 1.00 118.05 ? 3715 GLU A CG    1 
ATOM   14513 C CD    . GLU A 1 3715 ? 174.915 120.716 150.086 1.00 118.05 ? 3715 GLU A CD    1 
ATOM   14514 O OE1   . GLU A 1 3715 ? 175.766 119.951 150.582 1.00 118.05 ? 3715 GLU A OE1   1 
ATOM   14515 O OE2   . GLU A 1 3715 ? 174.809 120.906 148.857 1.00 118.05 ? 3715 GLU A OE2   1 
ATOM   14516 N N     . VAL A 1 3716 ? 173.161 117.829 153.691 1.00 117.45 ? 3716 VAL A N     1 
ATOM   14517 C CA    . VAL A 1 3716 ? 173.860 116.701 154.298 1.00 117.45 ? 3716 VAL A CA    1 
ATOM   14518 C C     . VAL A 1 3716 ? 173.291 115.377 153.800 1.00 117.45 ? 3716 VAL A C     1 
ATOM   14519 O O     . VAL A 1 3716 ? 174.036 114.413 153.598 1.00 117.45 ? 3716 VAL A O     1 
ATOM   14520 C CB    . VAL A 1 3716 ? 173.846 116.801 155.836 1.00 117.45 ? 3716 VAL A CB    1 
ATOM   14521 C CG1   . VAL A 1 3716 ? 172.485 116.481 156.414 1.00 117.45 ? 3716 VAL A CG1   1 
ATOM   14522 C CG2   . VAL A 1 3716 ? 174.904 115.889 156.423 1.00 117.45 ? 3716 VAL A CG2   1 
ATOM   14523 N N     . LEU A 1 3717 ? 171.973 115.295 153.590 1.00 127.32 ? 3717 LEU A N     1 
ATOM   14524 C CA    . LEU A 1 3717 ? 171.441 114.086 152.964 1.00 127.32 ? 3717 LEU A CA    1 
ATOM   14525 C C     . LEU A 1 3717 ? 171.883 113.961 151.513 1.00 127.32 ? 3717 LEU A C     1 
ATOM   14526 O O     . LEU A 1 3717 ? 172.121 112.848 151.033 1.00 127.32 ? 3717 LEU A O     1 
ATOM   14527 C CB    . LEU A 1 3717 ? 169.916 114.010 153.072 1.00 127.32 ? 3717 LEU A CB    1 
ATOM   14528 C CG    . LEU A 1 3717 ? 169.263 113.652 154.417 1.00 127.32 ? 3717 LEU A CG    1 
ATOM   14529 C CD1   . LEU A 1 3717 ? 170.038 112.518 155.067 1.00 127.32 ? 3717 LEU A CD1   1 
ATOM   14530 C CD2   . LEU A 1 3717 ? 169.071 114.790 155.394 1.00 127.32 ? 3717 LEU A CD2   1 
ATOM   14531 N N     . LYS A 1 3718 ? 172.003 115.080 150.796 1.00 133.45 ? 3718 LYS A N     1 
ATOM   14532 C CA    . LYS A 1 3718 ? 172.455 115.009 149.410 1.00 133.45 ? 3718 LYS A CA    1 
ATOM   14533 C C     . LYS A 1 3718 ? 173.897 114.526 149.319 1.00 133.45 ? 3718 LYS A C     1 
ATOM   14534 O O     . LYS A 1 3718 ? 174.242 113.735 148.433 1.00 133.45 ? 3718 LYS A O     1 
ATOM   14535 C CB    . LYS A 1 3718 ? 172.302 116.371 148.736 1.00 133.45 ? 3718 LYS A CB    1 
ATOM   14536 C CG    . LYS A 1 3718 ? 173.120 116.529 147.468 1.00 133.45 ? 3718 LYS A CG    1 
ATOM   14537 C CD    . LYS A 1 3718 ? 172.271 116.271 146.238 1.00 133.45 ? 3718 LYS A CD    1 
ATOM   14538 C CE    . LYS A 1 3718 ? 170.927 116.973 146.334 1.00 133.45 ? 3718 LYS A CE    1 
ATOM   14539 N NZ    . LYS A 1 3718 ? 170.046 116.634 145.184 1.00 133.45 ? 3718 LYS A NZ    1 
ATOM   14540 N N     . ALA A 1 3719 ? 174.754 114.990 150.225 1.00 131.21 ? 3719 ALA A N     1 
ATOM   14541 C CA    . ALA A 1 3719 ? 176.171 114.655 150.139 1.00 131.21 ? 3719 ALA A CA    1 
ATOM   14542 C C     . ALA A 1 3719 ? 176.474 113.307 150.782 1.00 131.21 ? 3719 ALA A C     1 
ATOM   14543 O O     . ALA A 1 3719 ? 177.046 112.417 150.144 1.00 131.21 ? 3719 ALA A O     1 
ATOM   14544 C CB    . ALA A 1 3719 ? 177.008 115.758 150.788 1.00 131.21 ? 3719 ALA A CB    1 
ATOM   14545 N N     . GLU A 1 3720 ? 176.106 113.142 152.053 1.00 135.78 ? 3720 GLU A N     1 
ATOM   14546 C CA    . GLU A 1 3720 ? 176.574 111.989 152.813 1.00 135.78 ? 3720 GLU A CA    1 
ATOM   14547 C C     . GLU A 1 3720 ? 175.878 110.701 152.389 1.00 135.78 ? 3720 GLU A C     1 
ATOM   14548 O O     . GLU A 1 3720 ? 176.532 109.666 152.219 1.00 135.78 ? 3720 GLU A O     1 
ATOM   14549 C CB    . GLU A 1 3720 ? 176.379 112.233 154.307 1.00 135.78 ? 3720 GLU A CB    1 
ATOM   14550 C CG    . GLU A 1 3720 ? 177.246 111.340 155.158 1.00 135.78 ? 3720 GLU A CG    1 
ATOM   14551 C CD    . GLU A 1 3720 ? 178.639 111.194 154.582 1.00 135.78 ? 3720 GLU A CD    1 
ATOM   14552 O OE1   . GLU A 1 3720 ? 179.325 112.223 154.409 1.00 135.78 ? 3720 GLU A OE1   1 
ATOM   14553 O OE2   . GLU A 1 3720 ? 179.045 110.051 154.285 1.00 135.78 ? 3720 GLU A OE2   1 
ATOM   14554 N N     . ARG A 1 3721 ? 174.560 110.737 152.214 1.00 138.33 ? 3721 ARG A N     1 
ATOM   14555 C CA    . ARG A 1 3721 ? 173.770 109.542 151.919 1.00 138.33 ? 3721 ARG A CA    1 
ATOM   14556 C C     . ARG A 1 3721 ? 172.967 109.791 150.652 1.00 138.33 ? 3721 ARG A C     1 
ATOM   14557 O O     . ARG A 1 3721 ? 171.755 110.042 150.709 1.00 138.33 ? 3721 ARG A O     1 
ATOM   14558 C CB    . ARG A 1 3721 ? 172.854 109.182 153.089 1.00 138.33 ? 3721 ARG A CB    1 
ATOM   14559 C CG    . ARG A 1 3721 ? 173.397 108.097 154.001 1.00 138.33 ? 3721 ARG A CG    1 
ATOM   14560 C CD    . ARG A 1 3721 ? 172.268 107.256 154.573 1.00 138.33 ? 3721 ARG A CD    1 
ATOM   14561 N NE    . ARG A 1 3721 ? 172.686 106.436 155.705 1.00 138.33 ? 3721 ARG A NE    1 
ATOM   14562 C CZ    . ARG A 1 3721 ? 171.902 105.563 156.324 1.00 138.33 ? 3721 ARG A CZ    1 
ATOM   14563 N NH1   . ARG A 1 3721 ? 170.662 105.341 155.921 1.00 138.33 ? 3721 ARG A NH1   1 
ATOM   14564 N NH2   . ARG A 1 3721 ? 172.373 104.897 157.373 1.00 138.33 ? 3721 ARG A NH2   1 
ATOM   14565 N N     . PRO A 1 3722 ? 173.610 109.723 149.484 1.00 147.23 ? 3722 PRO A N     1 
ATOM   14566 C CA    . PRO A 1 3722 ? 172.880 109.991 148.235 1.00 147.23 ? 3722 PRO A CA    1 
ATOM   14567 C C     . PRO A 1 3722 ? 171.749 109.016 147.974 1.00 147.23 ? 3722 PRO A C     1 
ATOM   14568 O O     . PRO A 1 3722 ? 170.799 109.368 147.267 1.00 147.23 ? 3722 PRO A O     1 
ATOM   14569 C CB    . PRO A 1 3722 ? 173.974 109.891 147.162 1.00 147.23 ? 3722 PRO A CB    1 
ATOM   14570 C CG    . PRO A 1 3722 ? 175.026 109.039 147.774 1.00 147.23 ? 3722 PRO A CG    1 
ATOM   14571 C CD    . PRO A 1 3722 ? 175.016 109.363 149.236 1.00 147.23 ? 3722 PRO A CD    1 
ATOM   14572 N N     . ASP A 1 3723 ? 171.817 107.801 148.519 1.00 157.94 ? 3723 ASP A N     1 
ATOM   14573 C CA    . ASP A 1 3723 ? 170.747 106.836 148.289 1.00 157.94 ? 3723 ASP A CA    1 
ATOM   14574 C C     . ASP A 1 3723 ? 169.447 107.273 148.958 1.00 157.94 ? 3723 ASP A C     1 
ATOM   14575 O O     . ASP A 1 3723 ? 168.374 107.208 148.345 1.00 157.94 ? 3723 ASP A O     1 
ATOM   14576 C CB    . ASP A 1 3723 ? 171.179 105.450 148.771 1.00 157.94 ? 3723 ASP A CB    1 
ATOM   14577 C CG    . ASP A 1 3723 ? 171.456 105.407 150.257 1.00 157.94 ? 3723 ASP A CG    1 
ATOM   14578 O OD1   . ASP A 1 3723 ? 172.599 105.707 150.661 1.00 157.94 ? 3723 ASP A OD1   1 
ATOM   14579 O OD2   . ASP A 1 3723 ? 170.531 105.065 151.021 1.00 157.94 ? 3723 ASP A OD2   1 
ATOM   14580 N N     . VAL A 1 3724 ? 169.520 107.734 150.208 1.00 163.46 ? 3724 VAL A N     1 
ATOM   14581 C CA    . VAL A 1 3724 ? 168.318 108.227 150.873 1.00 163.46 ? 3724 VAL A CA    1 
ATOM   14582 C C     . VAL A 1 3724 ? 167.820 109.492 150.192 1.00 163.46 ? 3724 VAL A C     1 
ATOM   14583 O O     . VAL A 1 3724 ? 166.612 109.735 150.115 1.00 163.46 ? 3724 VAL A O     1 
ATOM   14584 C CB    . VAL A 1 3724 ? 168.576 108.449 152.373 1.00 163.46 ? 3724 VAL A CB    1 
ATOM   14585 C CG1   . VAL A 1 3724 ? 167.299 108.890 153.067 1.00 163.46 ? 3724 VAL A CG1   1 
ATOM   14586 C CG2   . VAL A 1 3724 ? 169.091 107.176 153.002 1.00 163.46 ? 3724 VAL A CG2   1 
ATOM   14587 N N     . ASP A 1 3725 ? 168.738 110.319 149.688 1.00 168.85 ? 3725 ASP A N     1 
ATOM   14588 C CA    . ASP A 1 3725 ? 168.325 111.502 148.940 1.00 168.85 ? 3725 ASP A CA    1 
ATOM   14589 C C     . ASP A 1 3725 ? 167.553 111.117 147.684 1.00 168.85 ? 3725 ASP A C     1 
ATOM   14590 O O     . ASP A 1 3725 ? 166.527 111.730 147.361 1.00 168.85 ? 3725 ASP A O     1 
ATOM   14591 C CB    . ASP A 1 3725 ? 169.545 112.344 148.578 1.00 168.85 ? 3725 ASP A CB    1 
ATOM   14592 C CG    . ASP A 1 3725 ? 169.183 113.573 147.777 1.00 168.85 ? 3725 ASP A CG    1 
ATOM   14593 O OD1   . ASP A 1 3725 ? 169.992 113.983 146.919 1.00 168.85 ? 3725 ASP A OD1   1 
ATOM   14594 O OD2   . ASP A 1 3725 ? 168.090 114.132 148.008 1.00 168.85 ? 3725 ASP A OD2   1 
ATOM   14595 N N     . GLU A 1 3726 ? 168.032 110.103 146.961 1.00 177.53 ? 3726 GLU A N     1 
ATOM   14596 C CA    . GLU A 1 3726 ? 167.326 109.644 145.771 1.00 177.53 ? 3726 GLU A CA    1 
ATOM   14597 C C     . GLU A 1 3726 ? 165.970 109.056 146.131 1.00 177.53 ? 3726 GLU A C     1 
ATOM   14598 O O     . GLU A 1 3726 ? 164.990 109.251 145.405 1.00 177.53 ? 3726 GLU A O     1 
ATOM   14599 C CB    . GLU A 1 3726 ? 168.173 108.621 145.016 1.00 177.53 ? 3726 GLU A CB    1 
ATOM   14600 C CG    . GLU A 1 3726 ? 169.423 109.198 144.370 1.00 177.53 ? 3726 GLU A CG    1 
ATOM   14601 C CD    . GLU A 1 3726 ? 169.149 109.850 143.028 1.00 177.53 ? 3726 GLU A CD    1 
ATOM   14602 O OE1   . GLU A 1 3726 ? 168.158 110.600 142.911 1.00 177.53 ? 3726 GLU A OE1   1 
ATOM   14603 O OE2   . GLU A 1 3726 ? 169.931 109.608 142.085 1.00 177.53 ? 3726 GLU A OE2   1 
ATOM   14604 N N     . LYS A 1 3727 ? 165.893 108.326 147.244 1.00 178.81 ? 3727 LYS A N     1 
ATOM   14605 C CA    . LYS A 1 3727 ? 164.601 107.799 147.674 1.00 178.81 ? 3727 LYS A CA    1 
ATOM   14606 C C     . LYS A 1 3727 ? 163.641 108.927 148.033 1.00 178.81 ? 3727 LYS A C     1 
ATOM   14607 O O     . LYS A 1 3727 ? 162.443 108.852 147.736 1.00 178.81 ? 3727 LYS A O     1 
ATOM   14608 C CB    . LYS A 1 3727 ? 164.786 106.841 148.848 1.00 178.81 ? 3727 LYS A CB    1 
ATOM   14609 C CG    . LYS A 1 3727 ? 165.242 105.455 148.424 1.00 178.81 ? 3727 LYS A CG    1 
ATOM   14610 C CD    . LYS A 1 3727 ? 165.940 104.725 149.555 1.00 178.81 ? 3727 LYS A CD    1 
ATOM   14611 C CE    . LYS A 1 3727 ? 164.948 103.915 150.368 1.00 178.81 ? 3727 LYS A CE    1 
ATOM   14612 N NZ    . LYS A 1 3727 ? 165.447 102.537 150.628 1.00 178.81 ? 3727 LYS A NZ    1 
ATOM   14613 N N     . ARG A 1 3728 ? 164.149 109.985 148.672 1.00 185.34 ? 3728 ARG A N     1 
ATOM   14614 C CA    . ARG A 1 3728 ? 163.319 111.153 148.957 1.00 185.34 ? 3728 ARG A CA    1 
ATOM   14615 C C     . ARG A 1 3728 ? 162.820 111.798 147.673 1.00 185.34 ? 3728 ARG A C     1 
ATOM   14616 O O     . ARG A 1 3728 ? 161.648 112.179 147.571 1.00 185.34 ? 3728 ARG A O     1 
ATOM   14617 C CB    . ARG A 1 3728 ? 164.105 112.175 149.777 1.00 185.34 ? 3728 ARG A CB    1 
ATOM   14618 C CG    . ARG A 1 3728 ? 164.441 111.757 151.192 1.00 185.34 ? 3728 ARG A CG    1 
ATOM   14619 C CD    . ARG A 1 3728 ? 165.363 112.781 151.834 1.00 185.34 ? 3728 ARG A CD    1 
ATOM   14620 N NE    . ARG A 1 3728 ? 165.232 114.095 151.213 1.00 185.34 ? 3728 ARG A NE    1 
ATOM   14621 C CZ    . ARG A 1 3728 ? 166.230 114.766 150.652 1.00 185.34 ? 3728 ARG A CZ    1 
ATOM   14622 N NH1   . ARG A 1 3728 ? 167.458 114.277 150.617 1.00 185.34 ? 3728 ARG A NH1   1 
ATOM   14623 N NH2   . ARG A 1 3728 ? 165.988 115.957 150.112 1.00 185.34 ? 3728 ARG A NH2   1 
ATOM   14624 N N     . SER A 1 3729 ? 163.703 111.942 146.685 1.00 193.52 ? 3729 SER A N     1 
ATOM   14625 C CA    . SER A 1 3729 ? 163.292 112.514 145.408 1.00 193.52 ? 3729 SER A CA    1 
ATOM   14626 C C     . SER A 1 3729 ? 162.236 111.644 144.739 1.00 193.52 ? 3729 SER A C     1 
ATOM   14627 O O     . SER A 1 3729 ? 161.300 112.155 144.115 1.00 193.52 ? 3729 SER A O     1 
ATOM   14628 C CB    . SER A 1 3729 ? 164.505 112.693 144.496 1.00 193.52 ? 3729 SER A CB    1 
ATOM   14629 O OG    . SER A 1 3729 ? 164.123 113.179 143.221 1.00 193.52 ? 3729 SER A OG    1 
ATOM   14630 N N     . ASP A 1 3730 ? 162.381 110.323 144.850 1.00 204.83 ? 3730 ASP A N     1 
ATOM   14631 C CA    . ASP A 1 3730 ? 161.383 109.418 144.291 1.00 204.83 ? 3730 ASP A CA    1 
ATOM   14632 C C     . ASP A 1 3730 ? 160.042 109.573 144.995 1.00 204.83 ? 3730 ASP A C     1 
ATOM   14633 O O     . ASP A 1 3730 ? 158.990 109.564 144.348 1.00 204.83 ? 3730 ASP A O     1 
ATOM   14634 C CB    . ASP A 1 3730 ? 161.875 107.975 144.379 1.00 204.83 ? 3730 ASP A CB    1 
ATOM   14635 C CG    . ASP A 1 3730 ? 163.089 107.722 143.511 1.00 204.83 ? 3730 ASP A CG    1 
ATOM   14636 O OD1   . ASP A 1 3730 ? 163.420 108.599 142.686 1.00 204.83 ? 3730 ASP A OD1   1 
ATOM   14637 O OD2   . ASP A 1 3730 ? 163.711 106.648 143.651 1.00 204.83 ? 3730 ASP A OD2   1 
ATOM   14638 N N     . LEU A 1 3731 ? 160.058 109.709 146.322 1.00 198.91 ? 3731 LEU A N     1 
ATOM   14639 C CA    . LEU A 1 3731 ? 158.813 109.951 147.046 1.00 198.91 ? 3731 LEU A CA    1 
ATOM   14640 C C     . LEU A 1 3731 ? 158.176 111.264 146.609 1.00 198.91 ? 3731 LEU A C     1 
ATOM   14641 O O     . LEU A 1 3731 ? 156.949 111.359 146.489 1.00 198.91 ? 3731 LEU A O     1 
ATOM   14642 C CB    . LEU A 1 3731 ? 159.060 109.956 148.553 1.00 198.91 ? 3731 LEU A CB    1 
ATOM   14643 C CG    . LEU A 1 3731 ? 159.638 108.691 149.187 1.00 198.91 ? 3731 LEU A CG    1 
ATOM   14644 C CD1   . LEU A 1 3731 ? 159.537 108.770 150.703 1.00 198.91 ? 3731 LEU A CD1   1 
ATOM   14645 C CD2   . LEU A 1 3731 ? 158.932 107.455 148.657 1.00 198.91 ? 3731 LEU A CD2   1 
ATOM   14646 N N     . LEU A 1 3732 ? 158.997 112.291 146.380 1.00 203.49 ? 3732 LEU A N     1 
ATOM   14647 C CA    . LEU A 1 3732 ? 158.473 113.570 145.910 1.00 203.49 ? 3732 LEU A CA    1 
ATOM   14648 C C     . LEU A 1 3732 ? 157.838 113.439 144.532 1.00 203.49 ? 3732 LEU A C     1 
ATOM   14649 O O     . LEU A 1 3732 ? 156.749 113.973 144.288 1.00 203.49 ? 3732 LEU A O     1 
ATOM   14650 C CB    . LEU A 1 3732 ? 159.586 114.618 145.881 1.00 203.49 ? 3732 LEU A CB    1 
ATOM   14651 C CG    . LEU A 1 3732 ? 160.107 115.112 147.229 1.00 203.49 ? 3732 LEU A CG    1 
ATOM   14652 C CD1   . LEU A 1 3732 ? 161.066 116.273 147.039 1.00 203.49 ? 3732 LEU A CD1   1 
ATOM   14653 C CD2   . LEU A 1 3732 ? 158.948 115.514 148.126 1.00 203.49 ? 3732 LEU A CD2   1 
ATOM   14654 N N     . LYS A 1 3733 ? 158.502 112.731 143.615 1.00 207.53 ? 3733 LYS A N     1 
ATOM   14655 C CA    . LYS A 1 3733 ? 157.996 112.646 142.249 1.00 207.53 ? 3733 LYS A CA    1 
ATOM   14656 C C     . LYS A 1 3733 ? 156.803 111.705 142.134 1.00 207.53 ? 3733 LYS A C     1 
ATOM   14657 O O     . LYS A 1 3733 ? 155.967 111.889 141.245 1.00 207.53 ? 3733 LYS A O     1 
ATOM   14658 C CB    . LYS A 1 3733 ? 159.102 112.206 141.289 1.00 207.53 ? 3733 LYS A CB    1 
ATOM   14659 C CG    . LYS A 1 3733 ? 160.236 113.203 141.134 1.00 207.53 ? 3733 LYS A CG    1 
ATOM   14660 C CD    . LYS A 1 3733 ? 161.144 112.812 139.979 1.00 207.53 ? 3733 LYS A CD    1 
ATOM   14661 C CE    . LYS A 1 3733 ? 162.115 111.716 140.369 1.00 207.53 ? 3733 LYS A CE    1 
ATOM   14662 N NZ    . LYS A 1 3733 ? 162.584 111.868 141.767 1.00 207.53 ? 3733 LYS A NZ    1 
ATOM   14663 N N     . LEU A 1 3734 ? 156.694 110.715 143.023 1.00 213.14 ? 3734 LEU A N     1 
ATOM   14664 C CA    . LEU A 1 3734 ? 155.644 109.708 142.897 1.00 213.14 ? 3734 LEU A CA    1 
ATOM   14665 C C     . LEU A 1 3734 ? 154.250 110.322 142.891 1.00 213.14 ? 3734 LEU A C     1 
ATOM   14666 O O     . LEU A 1 3734 ? 153.319 109.737 142.324 1.00 213.14 ? 3734 LEU A O     1 
ATOM   14667 C CB    . LEU A 1 3734 ? 155.770 108.691 144.031 1.00 213.14 ? 3734 LEU A CB    1 
ATOM   14668 C CG    . LEU A 1 3734 ? 154.802 107.508 144.029 1.00 213.14 ? 3734 LEU A CG    1 
ATOM   14669 C CD1   . LEU A 1 3734 ? 155.273 106.422 143.075 1.00 213.14 ? 3734 LEU A CD1   1 
ATOM   14670 C CD2   . LEU A 1 3734 ? 154.642 106.961 145.438 1.00 213.14 ? 3734 LEU A CD2   1 
ATOM   14671 N N     . GLN A 1 3735 ? 154.083 111.496 143.500 1.00 184.42 ? 3735 GLN A N     1 
ATOM   14672 C CA    . GLN A 1 3735 ? 152.756 112.096 143.599 1.00 184.42 ? 3735 GLN A CA    1 
ATOM   14673 C C     . GLN A 1 3735 ? 152.257 112.564 142.234 1.00 184.42 ? 3735 GLN A C     1 
ATOM   14674 O O     . GLN A 1 3735 ? 151.183 112.152 141.781 1.00 184.42 ? 3735 GLN A O     1 
ATOM   14675 C CB    . GLN A 1 3735 ? 152.779 113.244 144.611 1.00 184.42 ? 3735 GLN A CB    1 
ATOM   14676 C CG    . GLN A 1 3735 ? 153.263 112.808 145.994 1.00 184.42 ? 3735 GLN A CG    1 
ATOM   14677 C CD    . GLN A 1 3735 ? 152.700 113.653 147.124 1.00 184.42 ? 3735 GLN A CD    1 
ATOM   14678 O OE1   . GLN A 1 3735 ? 152.852 114.873 147.137 1.00 184.42 ? 3735 GLN A OE1   1 
ATOM   14679 N NE2   . GLN A 1 3735 ? 152.054 113.003 148.083 1.00 184.42 ? 3735 GLN A NE2   1 
ATOM   14680 N N     . GLY A 1 3736 ? 153.017 113.428 141.562 1.00 217.68 ? 3736 GLY A N     1 
ATOM   14681 C CA    . GLY A 1 3736 ? 152.581 113.901 140.260 1.00 217.68 ? 3736 GLY A CA    1 
ATOM   14682 C C     . GLY A 1 3736 ? 153.480 113.604 139.073 1.00 217.68 ? 3736 GLY A C     1 
ATOM   14683 O O     . GLY A 1 3736 ? 152.985 113.338 137.972 1.00 217.68 ? 3736 GLY A O     1 
ATOM   14684 N N     . GLU A 1 3737 ? 154.798 113.611 139.281 1.00 226.08 ? 3737 GLU A N     1 
ATOM   14685 C CA    . GLU A 1 3737 ? 155.718 113.521 138.151 1.00 226.08 ? 3737 GLU A CA    1 
ATOM   14686 C C     . GLU A 1 3737 ? 155.730 112.120 137.553 1.00 226.08 ? 3737 GLU A C     1 
ATOM   14687 O O     . GLU A 1 3737 ? 155.703 111.962 136.327 1.00 226.08 ? 3737 GLU A O     1 
ATOM   14688 C CB    . GLU A 1 3737 ? 157.122 113.930 138.593 1.00 226.08 ? 3737 GLU A CB    1 
ATOM   14689 C CG    . GLU A 1 3737 ? 158.230 113.546 137.626 1.00 226.08 ? 3737 GLU A CG    1 
ATOM   14690 C CD    . GLU A 1 3737 ? 158.089 114.217 136.275 1.00 226.08 ? 3737 GLU A CD    1 
ATOM   14691 O OE1   . GLU A 1 3737 ? 158.371 115.429 136.182 1.00 226.08 ? 3737 GLU A OE1   1 
ATOM   14692 O OE2   . GLU A 1 3737 ? 157.710 113.533 135.302 1.00 226.08 ? 3737 GLU A OE2   1 
ATOM   14693 N N     . PHE A 1 3738 ? 155.776 111.089 138.400 1.00 237.17 ? 3738 PHE A N     1 
ATOM   14694 C CA    . PHE A 1 3738 ? 155.753 109.721 137.893 1.00 237.17 ? 3738 PHE A CA    1 
ATOM   14695 C C     . PHE A 1 3738 ? 154.440 109.421 137.181 1.00 237.17 ? 3738 PHE A C     1 
ATOM   14696 O O     . PHE A 1 3738 ? 154.427 108.760 136.136 1.00 237.17 ? 3738 PHE A O     1 
ATOM   14697 C CB    . PHE A 1 3738 ? 155.987 108.729 139.033 1.00 237.17 ? 3738 PHE A CB    1 
ATOM   14698 C CG    . PHE A 1 3738 ? 157.436 108.549 139.395 1.00 237.17 ? 3738 PHE A CG    1 
ATOM   14699 C CD1   . PHE A 1 3738 ? 158.437 108.987 138.545 1.00 237.17 ? 3738 PHE A CD1   1 
ATOM   14700 C CD2   . PHE A 1 3738 ? 157.795 107.927 140.578 1.00 237.17 ? 3738 PHE A CD2   1 
ATOM   14701 C CE1   . PHE A 1 3738 ? 159.768 108.820 138.874 1.00 237.17 ? 3738 PHE A CE1   1 
ATOM   14702 C CE2   . PHE A 1 3738 ? 159.123 107.755 140.911 1.00 237.17 ? 3738 PHE A CE2   1 
ATOM   14703 C CZ    . PHE A 1 3738 ? 160.111 108.202 140.057 1.00 237.17 ? 3738 PHE A CZ    1 
ATOM   14704 N N     . GLN A 1 3739 ? 153.323 109.897 137.736 1.00 247.61 ? 3739 GLN A N     1 
ATOM   14705 C CA    . GLN A 1 3739 ? 152.035 109.704 137.080 1.00 247.61 ? 3739 GLN A CA    1 
ATOM   14706 C C     . GLN A 1 3739 ? 151.993 110.408 135.730 1.00 247.61 ? 3739 GLN A C     1 
ATOM   14707 O O     . GLN A 1 3739 ? 151.464 109.861 134.756 1.00 247.61 ? 3739 GLN A O     1 
ATOM   14708 C CB    . GLN A 1 3739 ? 150.903 110.198 137.983 1.00 247.61 ? 3739 GLN A CB    1 
ATOM   14709 C CG    . GLN A 1 3739 ? 149.480 110.002 137.435 1.00 247.61 ? 3739 GLN A CG    1 
ATOM   14710 C CD    . GLN A 1 3739 ? 149.053 108.544 137.278 1.00 247.61 ? 3739 GLN A CD    1 
ATOM   14711 O OE1   . GLN A 1 3739 ? 149.869 107.651 137.049 1.00 247.61 ? 3739 GLN A OE1   1 
ATOM   14712 N NE2   . GLN A 1 3739 ? 147.752 108.305 137.396 1.00 247.61 ? 3739 GLN A NE2   1 
ATOM   14713 N N     . LEU A 1 3740 ? 152.548 111.621 135.648 1.00 257.47 ? 3740 LEU A N     1 
ATOM   14714 C CA    . LEU A 1 3740 ? 152.594 112.321 134.367 1.00 257.47 ? 3740 LEU A CA    1 
ATOM   14715 C C     . LEU A 1 3740 ? 153.460 111.574 133.360 1.00 257.47 ? 3740 LEU A C     1 
ATOM   14716 O O     . LEU A 1 3740 ? 153.113 111.484 132.176 1.00 257.47 ? 3740 LEU A O     1 
ATOM   14717 C CB    . LEU A 1 3740 ? 153.110 113.746 134.561 1.00 257.47 ? 3740 LEU A CB    1 
ATOM   14718 C CG    . LEU A 1 3740 ? 153.261 114.570 133.280 1.00 257.47 ? 3740 LEU A CG    1 
ATOM   14719 C CD1   . LEU A 1 3740 ? 151.935 114.666 132.542 1.00 257.47 ? 3740 LEU A CD1   1 
ATOM   14720 C CD2   . LEU A 1 3740 ? 153.816 115.954 133.579 1.00 257.47 ? 3740 LEU A CD2   1 
ATOM   14721 N N     . ARG A 1 3741 ? 154.599 111.042 133.809 1.00 265.22 ? 3741 ARG A N     1 
ATOM   14722 C CA    . ARG A 1 3741 ? 155.458 110.275 132.913 1.00 265.22 ? 3741 ARG A CA    1 
ATOM   14723 C C     . ARG A 1 3741 ? 154.742 109.032 132.399 1.00 265.22 ? 3741 ARG A C     1 
ATOM   14724 O O     . ARG A 1 3741 ? 154.820 108.705 131.208 1.00 265.22 ? 3741 ARG A O     1 
ATOM   14725 C CB    . ARG A 1 3741 ? 156.752 109.892 133.631 1.00 265.22 ? 3741 ARG A CB    1 
ATOM   14726 C CG    . ARG A 1 3741 ? 157.695 109.042 132.795 1.00 265.22 ? 3741 ARG A CG    1 
ATOM   14727 C CD    . ARG A 1 3741 ? 158.139 107.793 133.542 1.00 265.22 ? 3741 ARG A CD    1 
ATOM   14728 N NE    . ARG A 1 3741 ? 157.017 106.931 133.893 1.00 265.22 ? 3741 ARG A NE    1 
ATOM   14729 C CZ    . ARG A 1 3741 ? 156.838 106.386 135.088 1.00 265.22 ? 3741 ARG A CZ    1 
ATOM   14730 N NH1   . ARG A 1 3741 ? 157.698 106.583 136.073 1.00 265.22 ? 3741 ARG A NH1   1 
ATOM   14731 N NH2   . ARG A 1 3741 ? 155.770 105.621 135.299 1.00 265.22 ? 3741 ARG A NH2   1 
ATOM   14732 N N     . LEU A 1 3742 ? 154.030 108.333 133.286 1.00 272.06 ? 3742 LEU A N     1 
ATOM   14733 C CA    . LEU A 1 3742 ? 153.265 107.164 132.869 1.00 272.06 ? 3742 LEU A CA    1 
ATOM   14734 C C     . LEU A 1 3742 ? 152.175 107.546 131.876 1.00 272.06 ? 3742 LEU A C     1 
ATOM   14735 O O     . LEU A 1 3742 ? 151.948 106.839 130.887 1.00 272.06 ? 3742 LEU A O     1 
ATOM   14736 C CB    . LEU A 1 3742 ? 152.661 106.474 134.091 1.00 272.06 ? 3742 LEU A CB    1 
ATOM   14737 C CG    . LEU A 1 3742 ? 152.164 105.042 133.899 1.00 272.06 ? 3742 LEU A CG    1 
ATOM   14738 C CD1   . LEU A 1 3742 ? 153.259 104.172 133.303 1.00 272.06 ? 3742 LEU A CD1   1 
ATOM   14739 C CD2   . LEU A 1 3742 ? 151.673 104.471 135.220 1.00 272.06 ? 3742 LEU A CD2   1 
ATOM   14740 N N     . ARG A 1 3743 ? 151.491 108.666 132.122 1.00 271.94 ? 3743 ARG A N     1 
ATOM   14741 C CA    . ARG A 1 3743 ? 150.453 109.118 131.203 1.00 271.94 ? 3743 ARG A CA    1 
ATOM   14742 C C     . ARG A 1 3743 ? 151.032 109.431 129.830 1.00 271.94 ? 3743 ARG A C     1 
ATOM   14743 O O     . ARG A 1 3743 ? 150.445 109.075 128.803 1.00 271.94 ? 3743 ARG A O     1 
ATOM   14744 C CB    . ARG A 1 3743 ? 149.745 110.346 131.775 1.00 271.94 ? 3743 ARG A CB    1 
ATOM   14745 C CG    . ARG A 1 3743 ? 148.807 110.053 132.935 1.00 271.94 ? 3743 ARG A CG    1 
ATOM   14746 C CD    . ARG A 1 3743 ? 148.097 108.729 132.750 1.00 271.94 ? 3743 ARG A CD    1 
ATOM   14747 N NE    . ARG A 1 3743 ? 147.127 108.794 131.667 1.00 271.94 ? 3743 ARG A NE    1 
ATOM   14748 C CZ    . ARG A 1 3743 ? 146.621 107.735 131.052 1.00 271.94 ? 3743 ARG A CZ    1 
ATOM   14749 N NH1   . ARG A 1 3743 ? 146.953 106.505 131.409 1.00 271.94 ? 3743 ARG A NH1   1 
ATOM   14750 N NH2   . ARG A 1 3743 ? 145.766 107.915 130.051 1.00 271.94 ? 3743 ARG A NH2   1 
ATOM   14751 N N     . GLN A 1 3744 ? 152.187 110.099 129.793 1.00 282.87 ? 3744 GLN A N     1 
ATOM   14752 C CA    . GLN A 1 3744 ? 152.798 110.430 128.509 1.00 282.87 ? 3744 GLN A CA    1 
ATOM   14753 C C     . GLN A 1 3744 ? 153.270 109.178 127.781 1.00 282.87 ? 3744 GLN A C     1 
ATOM   14754 O O     . GLN A 1 3744 ? 153.185 109.102 126.550 1.00 282.87 ? 3744 GLN A O     1 
ATOM   14755 C CB    . GLN A 1 3744 ? 153.951 111.410 128.708 1.00 282.87 ? 3744 GLN A CB    1 
ATOM   14756 C CG    . GLN A 1 3744 ? 153.514 112.771 129.229 1.00 282.87 ? 3744 GLN A CG    1 
ATOM   14757 C CD    . GLN A 1 3744 ? 152.457 113.426 128.359 1.00 282.87 ? 3744 GLN A CD    1 
ATOM   14758 O OE1   . GLN A 1 3744 ? 152.424 113.231 127.145 1.00 282.87 ? 3744 GLN A OE1   1 
ATOM   14759 N NE2   . GLN A 1 3744 ? 151.584 114.211 128.980 1.00 282.87 ? 3744 GLN A NE2   1 
ATOM   14760 N N     . LEU A 1 3745 ? 153.770 108.184 128.518 1.00 290.26 ? 3745 LEU A N     1 
ATOM   14761 C CA    . LEU A 1 3745 ? 154.135 106.922 127.882 1.00 290.26 ? 3745 LEU A CA    1 
ATOM   14762 C C     . LEU A 1 3745 ? 152.908 106.218 127.312 1.00 290.26 ? 3745 LEU A C     1 
ATOM   14763 O O     . LEU A 1 3745 ? 152.966 105.634 126.222 1.00 290.26 ? 3745 LEU A O     1 
ATOM   14764 C CB    . LEU A 1 3745 ? 154.862 106.019 128.876 1.00 290.26 ? 3745 LEU A CB    1 
ATOM   14765 C CG    . LEU A 1 3745 ? 156.378 105.954 128.694 1.00 290.26 ? 3745 LEU A CG    1 
ATOM   14766 C CD1   . LEU A 1 3745 ? 156.726 105.177 127.434 1.00 290.26 ? 3745 LEU A CD1   1 
ATOM   14767 C CD2   . LEU A 1 3745 ? 156.977 107.351 128.651 1.00 290.26 ? 3745 LEU A CD2   1 
ATOM   14768 N N     . GLU A 1 3746 ? 151.786 106.266 128.033 1.00 293.13 ? 3746 GLU A N     1 
ATOM   14769 C CA    . GLU A 1 3746 ? 150.549 105.703 127.499 1.00 293.13 ? 3746 GLU A CA    1 
ATOM   14770 C C     . GLU A 1 3746 ? 150.114 106.433 126.234 1.00 293.13 ? 3746 GLU A C     1 
ATOM   14771 O O     . GLU A 1 3746 ? 149.659 105.805 125.274 1.00 293.13 ? 3746 GLU A O     1 
ATOM   14772 C CB    . GLU A 1 3746 ? 149.440 105.752 128.550 1.00 293.13 ? 3746 GLU A CB    1 
ATOM   14773 C CG    . GLU A 1 3746 ? 149.727 104.969 129.822 1.00 293.13 ? 3746 GLU A CG    1 
ATOM   14774 C CD    . GLU A 1 3746 ? 149.573 103.468 129.650 1.00 293.13 ? 3746 GLU A CD    1 
ATOM   14775 O OE1   . GLU A 1 3746 ? 149.241 103.016 128.534 1.00 293.13 ? 3746 GLU A OE1   1 
ATOM   14776 O OE2   . GLU A 1 3746 ? 149.775 102.739 130.644 1.00 293.13 ? 3746 GLU A OE2   1 
ATOM   14777 N N     . LYS A 1 3747 ? 150.245 107.761 126.217 1.00 291.67 ? 3747 LYS A N     1 
ATOM   14778 C CA    . LYS A 1 3747 ? 149.897 108.524 125.019 1.00 291.67 ? 3747 LYS A CA    1 
ATOM   14779 C C     . LYS A 1 3747 ? 150.815 108.178 123.851 1.00 291.67 ? 3747 LYS A C     1 
ATOM   14780 O O     . LYS A 1 3747 ? 150.373 108.136 122.696 1.00 291.67 ? 3747 LYS A O     1 
ATOM   14781 C CB    . LYS A 1 3747 ? 149.945 110.023 125.311 1.00 291.67 ? 3747 LYS A CB    1 
ATOM   14782 C CG    . LYS A 1 3747 ? 148.987 110.487 126.396 1.00 291.67 ? 3747 LYS A CG    1 
ATOM   14783 C CD    . LYS A 1 3747 ? 147.541 110.168 126.046 1.00 291.67 ? 3747 LYS A CD    1 
ATOM   14784 C CE    . LYS A 1 3747 ? 146.695 109.985 127.297 1.00 291.67 ? 3747 LYS A CE    1 
ATOM   14785 N NZ    . LYS A 1 3747 ? 145.790 108.808 127.207 1.00 291.67 ? 3747 LYS A NZ    1 
ATOM   14786 N N     . SER A 1 3748 ? 152.102 107.954 124.127 1.00 305.92 ? 3748 SER A N     1 
ATOM   14787 C CA    . SER A 1 3748 ? 153.010 107.507 123.074 1.00 305.92 ? 3748 SER A CA    1 
ATOM   14788 C C     . SER A 1 3748 ? 152.591 106.144 122.539 1.00 305.92 ? 3748 SER A C     1 
ATOM   14789 O O     . SER A 1 3748 ? 152.637 105.900 121.327 1.00 305.92 ? 3748 SER A O     1 
ATOM   14790 C CB    . SER A 1 3748 ? 154.448 107.467 123.592 1.00 305.92 ? 3748 SER A CB    1 
ATOM   14791 O OG    . SER A 1 3748 ? 154.766 108.646 124.311 1.00 305.92 ? 3748 SER A OG    1 
ATOM   14792 N N     . LEU A 1 3749 ? 152.174 105.244 123.432 1.00 309.56 ? 3749 LEU A N     1 
ATOM   14793 C CA    . LEU A 1 3749 ? 151.626 103.967 122.987 1.00 309.56 ? 3749 LEU A CA    1 
ATOM   14794 C C     . LEU A 1 3749 ? 150.403 104.176 122.104 1.00 309.56 ? 3749 LEU A C     1 
ATOM   14795 O O     . LEU A 1 3749 ? 150.235 103.492 121.088 1.00 309.56 ? 3749 LEU A O     1 
ATOM   14796 C CB    . LEU A 1 3749 ? 151.270 103.098 124.193 1.00 309.56 ? 3749 LEU A CB    1 
ATOM   14797 C CG    . LEU A 1 3749 ? 150.202 102.028 123.949 1.00 309.56 ? 3749 LEU A CG    1 
ATOM   14798 C CD1   . LEU A 1 3749 ? 150.762 100.880 123.119 1.00 309.56 ? 3749 LEU A CD1   1 
ATOM   14799 C CD2   . LEU A 1 3749 ? 149.617 101.525 125.264 1.00 309.56 ? 3749 LEU A CD2   1 
ATOM   14800 N N     . LEU A 1 3750 ? 149.537 105.118 122.480 1.00 309.96 ? 3750 LEU A N     1 
ATOM   14801 C CA    . LEU A 1 3750 ? 148.336 105.394 121.697 1.00 309.96 ? 3750 LEU A CA    1 
ATOM   14802 C C     . LEU A 1 3750 ? 148.686 105.871 120.295 1.00 309.96 ? 3750 LEU A C     1 
ATOM   14803 O O     . LEU A 1 3750 ? 148.118 105.396 119.302 1.00 309.96 ? 3750 LEU A O     1 
ATOM   14804 C CB    . LEU A 1 3750 ? 147.475 106.438 122.406 1.00 309.96 ? 3750 LEU A CB    1 
ATOM   14805 C CG    . LEU A 1 3750 ? 146.985 106.082 123.805 1.00 309.96 ? 3750 LEU A CG    1 
ATOM   14806 C CD1   . LEU A 1 3750 ? 146.098 107.183 124.352 1.00 309.96 ? 3750 LEU A CD1   1 
ATOM   14807 C CD2   . LEU A 1 3750 ? 146.259 104.755 123.773 1.00 309.96 ? 3750 LEU A CD2   1 
ATOM   14808 N N     . GLN A 1 3751 ? 149.606 106.832 120.196 1.00 314.45 ? 3751 GLN A N     1 
ATOM   14809 C CA    . GLN A 1 3751 ? 149.958 107.357 118.881 1.00 314.45 ? 3751 GLN A CA    1 
ATOM   14810 C C     . GLN A 1 3751 ? 150.655 106.295 118.040 1.00 314.45 ? 3751 GLN A C     1 
ATOM   14811 O O     . GLN A 1 3751 ? 150.397 106.185 116.836 1.00 314.45 ? 3751 GLN A O     1 
ATOM   14812 C CB    . GLN A 1 3751 ? 150.811 108.622 119.005 1.00 314.45 ? 3751 GLN A CB    1 
ATOM   14813 C CG    . GLN A 1 3751 ? 152.131 108.466 119.728 1.00 314.45 ? 3751 GLN A CG    1 
ATOM   14814 C CD    . GLN A 1 3751 ? 152.523 109.717 120.492 1.00 314.45 ? 3751 GLN A CD    1 
ATOM   14815 O OE1   . GLN A 1 3751 ? 151.686 110.576 120.770 1.00 314.45 ? 3751 GLN A OE1   1 
ATOM   14816 N NE2   . GLN A 1 3751 ? 153.802 109.828 120.832 1.00 314.45 ? 3751 GLN A NE2   1 
ATOM   14817 N N     . ALA A 1 3752 ? 151.509 105.475 118.659 1.00 324.04 ? 3752 ALA A N     1 
ATOM   14818 C CA    . ALA A 1 3752 ? 152.135 104.383 117.922 1.00 324.04 ? 3752 ALA A CA    1 
ATOM   14819 C C     . ALA A 1 3752 ? 151.093 103.393 117.412 1.00 324.04 ? 3752 ALA A C     1 
ATOM   14820 O O     . ALA A 1 3752 ? 151.165 102.941 116.263 1.00 324.04 ? 3752 ALA A O     1 
ATOM   14821 C CB    . ALA A 1 3752 ? 153.163 103.676 118.803 1.00 324.04 ? 3752 ALA A CB    1 
ATOM   14822 N N     . LEU A 1 3753 ? 150.110 103.053 118.250 1.00 327.64 ? 3753 LEU A N     1 
ATOM   14823 C CA    . LEU A 1 3753 ? 149.102 102.076 117.856 1.00 327.64 ? 3753 LEU A CA    1 
ATOM   14824 C C     . LEU A 1 3753 ? 148.218 102.602 116.733 1.00 327.64 ? 3753 LEU A C     1 
ATOM   14825 O O     . LEU A 1 3753 ? 147.902 101.865 115.792 1.00 327.64 ? 3753 LEU A O     1 
ATOM   14826 C CB    . LEU A 1 3753 ? 148.257 101.678 119.063 1.00 327.64 ? 3753 LEU A CB    1 
ATOM   14827 C CG    . LEU A 1 3753 ? 148.456 100.257 119.594 1.00 327.64 ? 3753 LEU A CG    1 
ATOM   14828 C CD1   . LEU A 1 3753 ? 147.496 99.973  120.737 1.00 327.64 ? 3753 LEU A CD1   1 
ATOM   14829 C CD2   . LEU A 1 3753 ? 148.282 99.240  118.476 1.00 327.64 ? 3753 LEU A CD2   1 
ATOM   14830 N N     . ASN A 1 3754 ? 147.799 103.869 116.808 1.00 324.89 ? 3754 ASN A N     1 
ATOM   14831 C CA    . ASN A 1 3754 ? 146.981 104.400 115.722 1.00 324.89 ? 3754 ASN A CA    1 
ATOM   14832 C C     . ASN A 1 3754 ? 147.799 104.661 114.465 1.00 324.89 ? 3754 ASN A C     1 
ATOM   14833 O O     . ASN A 1 3754 ? 147.227 104.703 113.371 1.00 324.89 ? 3754 ASN A O     1 
ATOM   14834 C CB    . ASN A 1 3754 ? 146.237 105.671 116.149 1.00 324.89 ? 3754 ASN A CB    1 
ATOM   14835 C CG    . ASN A 1 3754 ? 147.157 106.763 116.646 1.00 324.89 ? 3754 ASN A CG    1 
ATOM   14836 O OD1   . ASN A 1 3754 ? 148.052 107.216 115.933 1.00 324.89 ? 3754 ASN A OD1   1 
ATOM   14837 N ND2   . ASN A 1 3754 ? 146.920 107.216 117.872 1.00 324.89 ? 3754 ASN A ND2   1 
ATOM   14838 N N     . GLU A 1 3755 ? 149.117 104.835 114.589 1.00 330.90 ? 3755 GLU A N     1 
ATOM   14839 C CA    . GLU A 1 3755 ? 149.956 104.895 113.398 1.00 330.90 ? 3755 GLU A CA    1 
ATOM   14840 C C     . GLU A 1 3755 ? 150.077 103.525 112.742 1.00 330.90 ? 3755 GLU A C     1 
ATOM   14841 O O     . GLU A 1 3755 ? 150.046 103.415 111.511 1.00 330.90 ? 3755 GLU A O     1 
ATOM   14842 C CB    . GLU A 1 3755 ? 151.337 105.445 113.753 1.00 330.90 ? 3755 GLU A CB    1 
ATOM   14843 C CG    . GLU A 1 3755 ? 152.338 105.395 112.607 0.00 330.90 ? 3755 GLU A CG    1 
ATOM   14844 C CD    . GLU A 1 3755 ? 153.290 104.220 112.713 0.00 330.90 ? 3755 GLU A CD    1 
ATOM   14845 O OE1   . GLU A 1 3755 ? 154.046 104.152 113.705 0.00 330.90 ? 3755 GLU A OE1   1 
ATOM   14846 O OE2   . GLU A 1 3755 ? 153.279 103.363 111.805 0.00 330.90 ? 3755 GLU A OE2   1 
ATOM   14847 N N     . VAL A 1 3756 ? 150.214 102.467 113.547 1.00 339.18 ? 3756 VAL A N     1 
ATOM   14848 C CA    . VAL A 1 3756 ? 150.380 101.120 113.004 1.00 339.18 ? 3756 VAL A CA    1 
ATOM   14849 C C     . VAL A 1 3756 ? 149.060 100.392 112.794 1.00 339.18 ? 3756 VAL A C     1 
ATOM   14850 O O     . VAL A 1 3756 ? 149.057 99.304  112.197 1.00 339.18 ? 3756 VAL A O     1 
ATOM   14851 C CB    . VAL A 1 3756 ? 151.283 100.261 113.912 1.00 339.18 ? 3756 VAL A CB    1 
ATOM   14852 C CG1   . VAL A 1 3756 ? 152.589 100.987 114.199 1.00 339.18 ? 3756 VAL A CG1   1 
ATOM   14853 C CG2   . VAL A 1 3756 ? 150.560 99.909  115.204 1.00 339.18 ? 3756 VAL A CG2   1 
ATOM   14854 N N     . LYS A 1 3757 ? 147.945 100.946 113.271 1.00 342.38 ? 3757 LYS A N     1 
ATOM   14855 C CA    . LYS A 1 3757 ? 146.610 100.368 113.111 1.00 342.38 ? 3757 LYS A CA    1 
ATOM   14856 C C     . LYS A 1 3757 ? 146.496 98.973  113.719 1.00 342.38 ? 3757 LYS A C     1 
ATOM   14857 O O     . LYS A 1 3757 ? 145.629 98.189  113.317 1.00 342.38 ? 3757 LYS A O     1 
ATOM   14858 C CB    . LYS A 1 3757 ? 146.189 100.330 111.636 1.00 342.38 ? 3757 LYS A CB    1 
ATOM   14859 C CG    . LYS A 1 3757 ? 146.464 101.615 110.872 0.00 342.38 ? 3757 LYS A CG    1 
ATOM   14860 C CD    . LYS A 1 3757 ? 146.509 101.362 109.371 0.00 342.38 ? 3757 LYS A CD    1 
ATOM   14861 C CE    . LYS A 1 3757 ? 147.486 100.251 109.022 0.00 342.38 ? 3757 LYS A CE    1 
ATOM   14862 N NZ    . LYS A 1 3757 ? 148.860 100.544 109.511 0.00 342.38 ? 3757 LYS A NZ    1 
ATOM   14863 N N     . GLY A 1 3758 ? 147.351 98.646  114.685 1.00 347.16 ? 3758 GLY A N     1 
ATOM   14864 C CA    . GLY A 1 3758 ? 147.292 97.360  115.354 1.00 347.16 ? 3758 GLY A CA    1 
ATOM   14865 C C     . GLY A 1 3758 ? 147.540 96.173  114.445 1.00 347.16 ? 3758 GLY A C     1 
ATOM   14866 O O     . GLY A 1 3758 ? 146.805 95.183  114.494 1.00 347.16 ? 3758 GLY A O     1 
ATOM   14867 N N     . ARG A 1 3759 ? 148.568 96.260  113.607 1.00 348.34 ? 3759 ARG A N     1 
ATOM   14868 C CA    . ARG A 1 3759 ? 148.903 95.166  112.707 1.00 348.34 ? 3759 ARG A CA    1 
ATOM   14869 C C     . ARG A 1 3759 ? 149.562 94.026  113.473 1.00 348.34 ? 3759 ARG A C     1 
ATOM   14870 O O     . ARG A 1 3759 ? 150.334 94.251  114.410 1.00 348.34 ? 3759 ARG A O     1 
ATOM   14871 C CB    . ARG A 1 3759 ? 149.829 95.660  111.596 1.00 348.34 ? 3759 ARG A CB    1 
ATOM   14872 C CG    . ARG A 1 3759 ? 149.126 96.509  110.548 0.00 348.34 ? 3759 ARG A CG    1 
ATOM   14873 C CD    . ARG A 1 3759 ? 150.116 97.178  109.607 0.00 348.34 ? 3759 ARG A CD    1 
ATOM   14874 N NE    . ARG A 1 3759 ? 150.895 96.216  108.839 0.00 348.34 ? 3759 ARG A NE    1 
ATOM   14875 C CZ    . ARG A 1 3759 ? 150.921 96.166  107.514 0.00 348.34 ? 3759 ARG A CZ    1 
ATOM   14876 N NH1   . ARG A 1 3759 ? 150.218 97.010  106.776 0.00 348.34 ? 3759 ARG A NH1   1 
ATOM   14877 N NH2   . ARG A 1 3759 ? 151.672 95.246  106.914 0.00 348.34 ? 3759 ARG A NH2   1 
ATOM   14878 N N     . ILE A 1 3760 ? 149.244 92.792  113.072 1.00 351.21 ? 3760 ILE A N     1 
ATOM   14879 C CA    . ILE A 1 3760 ? 149.887 91.624  113.669 1.00 351.21 ? 3760 ILE A CA    1 
ATOM   14880 C C     . ILE A 1 3760 ? 151.376 91.603  113.342 1.00 351.21 ? 3760 ILE A C     1 
ATOM   14881 O O     . ILE A 1 3760 ? 152.173 90.997  114.069 1.00 351.21 ? 3760 ILE A O     1 
ATOM   14882 C CB    . ILE A 1 3760 ? 149.181 90.331  113.209 1.00 351.21 ? 3760 ILE A CB    1 
ATOM   14883 C CG1   . ILE A 1 3760 ? 149.666 89.129  114.023 0.00 351.21 ? 3760 ILE A CG1   1 
ATOM   14884 C CG2   . ILE A 1 3760 ? 149.393 90.097  111.718 0.00 351.21 ? 3760 ILE A CG2   1 
ATOM   14885 C CD1   . ILE A 1 3760 ? 148.961 87.834  113.681 0.00 351.21 ? 3760 ILE A CD1   1 
ATOM   14886 N N     . LEU A 1 3761 ? 151.777 92.256  112.248 1.00 352.53 ? 3761 LEU A N     1 
ATOM   14887 C CA    . LEU A 1 3761 ? 153.195 92.350  111.919 1.00 352.53 ? 3761 LEU A CA    1 
ATOM   14888 C C     . LEU A 1 3761 ? 153.933 93.274  112.880 1.00 352.53 ? 3761 LEU A C     1 
ATOM   14889 O O     . LEU A 1 3761 ? 155.107 93.039  113.186 1.00 352.53 ? 3761 LEU A O     1 
ATOM   14890 C CB    . LEU A 1 3761 ? 153.370 92.832  110.479 1.00 352.53 ? 3761 LEU A CB    1 
ATOM   14891 C CG    . LEU A 1 3761 ? 154.798 92.828  109.932 0.00 352.53 ? 3761 LEU A CG    1 
ATOM   14892 C CD1   . LEU A 1 3761 ? 155.228 91.415  109.572 0.00 352.53 ? 3761 LEU A CD1   1 
ATOM   14893 C CD2   . LEU A 1 3761 ? 154.915 93.750  108.732 0.00 352.53 ? 3761 LEU A CD2   1 
ATOM   14894 N N     . ASP A 1 3762 ? 153.264 94.321  113.363 1.00 354.97 ? 3762 ASP A N     1 
ATOM   14895 C CA    . ASP A 1 3762 ? 153.823 95.246  114.342 1.00 354.97 ? 3762 ASP A CA    1 
ATOM   14896 C C     . ASP A 1 3762 ? 153.775 94.697  115.764 1.00 354.97 ? 3762 ASP A C     1 
ATOM   14897 O O     . ASP A 1 3762 ? 154.008 95.455  116.717 1.00 354.97 ? 3762 ASP A O     1 
ATOM   14898 C CB    . ASP A 1 3762 ? 153.081 96.584  114.274 1.00 354.97 ? 3762 ASP A CB    1 
ATOM   14899 C CG    . ASP A 1 3762 ? 153.935 97.749  114.729 0.00 354.97 ? 3762 ASP A CG    1 
ATOM   14900 O OD1   . ASP A 1 3762 ? 154.746 98.243  113.917 0.00 354.97 ? 3762 ASP A OD1   1 
ATOM   14901 O OD2   . ASP A 1 3762 ? 153.796 98.174  115.896 0.00 354.97 ? 3762 ASP A OD2   1 
ATOM   14902 N N     . ASP A 1 3763 ? 153.483 93.400  115.909 1.00 355.19 ? 3763 ASP A N     1 
ATOM   14903 C CA    . ASP A 1 3763 ? 153.315 92.806  117.230 1.00 355.19 ? 3763 ASP A CA    1 
ATOM   14904 C C     . ASP A 1 3763 ? 154.576 92.936  118.069 1.00 355.19 ? 3763 ASP A C     1 
ATOM   14905 O O     . ASP A 1 3763 ? 154.494 93.165  119.276 1.00 355.19 ? 3763 ASP A O     1 
ATOM   14906 C CB    . ASP A 1 3763 ? 152.933 91.333  117.107 1.00 355.19 ? 3763 ASP A CB    1 
ATOM   14907 C CG    . ASP A 1 3763 ? 153.190 90.565  118.387 0.00 355.19 ? 3763 ASP A CG    1 
ATOM   14908 O OD1   . ASP A 1 3763 ? 152.385 90.684  119.330 0.00 355.19 ? 3763 ASP A OD1   1 
ATOM   14909 O OD2   . ASP A 1 3763 ? 154.217 89.864  118.468 0.00 355.19 ? 3763 ASP A OD2   1 
ATOM   14910 N N     . ASP A 1 3764 ? 155.748 92.762  117.456 1.00 355.91 ? 3764 ASP A N     1 
ATOM   14911 C CA    . ASP A 1 3764 ? 156.992 92.806  118.220 1.00 355.91 ? 3764 ASP A CA    1 
ATOM   14912 C C     . ASP A 1 3764 ? 157.175 94.161  118.892 1.00 355.91 ? 3764 ASP A C     1 
ATOM   14913 O O     . ASP A 1 3764 ? 157.411 94.242  120.104 1.00 355.91 ? 3764 ASP A O     1 
ATOM   14914 C CB    . ASP A 1 3764 ? 158.177 92.488  117.307 1.00 355.91 ? 3764 ASP A CB    1 
ATOM   14915 C CG    . ASP A 1 3764 ? 159.502 92.515  118.041 0.00 355.91 ? 3764 ASP A CG    1 
ATOM   14916 O OD1   . ASP A 1 3764 ? 159.648 91.772  119.035 0.00 355.91 ? 3764 ASP A OD1   1 
ATOM   14917 O OD2   . ASP A 1 3764 ? 160.398 93.277  117.624 0.00 355.91 ? 3764 ASP A OD2   1 
ATOM   14918 N N     . THR A 1 3765 ? 157.046 95.243  118.120 1.00 352.35 ? 3765 THR A N     1 
ATOM   14919 C CA    . THR A 1 3765 ? 157.165 96.576  118.698 1.00 352.35 ? 3765 THR A CA    1 
ATOM   14920 C C     . THR A 1 3765 ? 156.052 96.857  119.699 1.00 352.35 ? 3765 THR A C     1 
ATOM   14921 O O     . THR A 1 3765 ? 156.307 97.451  120.756 1.00 352.35 ? 3765 THR A O     1 
ATOM   14922 C CB    . THR A 1 3765 ? 157.159 97.632  117.594 1.00 352.35 ? 3765 THR A CB    1 
ATOM   14923 O OG1   . THR A 1 3765 ? 155.811 97.886  117.181 1.00 352.35 ? 3765 THR A OG1   1 
ATOM   14924 C CG2   . THR A 1 3765 ? 157.970 97.153  116.401 1.00 352.35 ? 3765 THR A CG2   1 
ATOM   14925 N N     . ILE A 1 3766 ? 154.819 96.440  119.394 1.00 349.38 ? 3766 ILE A N     1 
ATOM   14926 C CA    . ILE A 1 3766 ? 153.710 96.716  120.302 1.00 349.38 ? 3766 ILE A CA    1 
ATOM   14927 C C     . ILE A 1 3766 ? 153.929 96.023  121.641 1.00 349.38 ? 3766 ILE A C     1 
ATOM   14928 O O     . ILE A 1 3766 ? 153.738 96.624  122.703 1.00 349.38 ? 3766 ILE A O     1 
ATOM   14929 C CB    . ILE A 1 3766 ? 152.369 96.307  119.667 1.00 349.38 ? 3766 ILE A CB    1 
ATOM   14930 C CG1   . ILE A 1 3766 ? 152.059 97.193  118.462 1.00 349.38 ? 3766 ILE A CG1   1 
ATOM   14931 C CG2   . ILE A 1 3766 ? 151.248 96.425  120.683 1.00 349.38 ? 3766 ILE A CG2   1 
ATOM   14932 C CD1   . ILE A 1 3766 ? 152.101 98.670  118.768 1.00 349.38 ? 3766 ILE A CD1   1 
ATOM   14933 N N     . ILE A 1 3767 ? 154.341 94.752  121.615 1.00 349.12 ? 3767 ILE A N     1 
ATOM   14934 C CA    . ILE A 1 3767 ? 154.531 94.021  122.863 1.00 349.12 ? 3767 ILE A CA    1 
ATOM   14935 C C     . ILE A 1 3767 ? 155.765 94.518  123.598 1.00 349.12 ? 3767 ILE A C     1 
ATOM   14936 O O     . ILE A 1 3767 ? 155.790 94.513  124.829 1.00 349.12 ? 3767 ILE A O     1 
ATOM   14937 C CB    . ILE A 1 3767 ? 154.596 92.498  122.633 1.00 349.12 ? 3767 ILE A CB    1 
ATOM   14938 C CG1   . ILE A 1 3767 ? 155.805 92.111  121.779 1.00 349.12 ? 3767 ILE A CG1   1 
ATOM   14939 C CG2   . ILE A 1 3767 ? 153.296 91.998  122.026 1.00 349.12 ? 3767 ILE A CG2   1 
ATOM   14940 C CD1   . ILE A 1 3767 ? 155.849 90.646  121.412 1.00 349.12 ? 3767 ILE A CD1   1 
ATOM   14941 N N     . THR A 1 3768 ? 156.805 94.951  122.880 1.00 347.89 ? 3768 THR A N     1 
ATOM   14942 C CA    . THR A 1 3768 ? 157.952 95.545  123.561 1.00 347.89 ? 3768 THR A CA    1 
ATOM   14943 C C     . THR A 1 3768 ? 157.539 96.805  124.312 1.00 347.89 ? 3768 THR A C     1 
ATOM   14944 O O     . THR A 1 3768 ? 157.873 96.983  125.493 1.00 347.89 ? 3768 THR A O     1 
ATOM   14945 C CB    . THR A 1 3768 ? 159.060 95.853  122.553 1.00 347.89 ? 3768 THR A CB    1 
ATOM   14946 O OG1   . THR A 1 3768 ? 159.193 94.760  121.635 1.00 347.89 ? 3768 THR A OG1   1 
ATOM   14947 C CG2   . THR A 1 3768 ? 160.384 96.070  123.270 1.00 347.89 ? 3768 THR A CG2   1 
ATOM   14948 N N     . THR A 1 3769 ? 156.783 97.681  123.645 1.00 342.25 ? 3769 THR A N     1 
ATOM   14949 C CA    . THR A 1 3769 ? 156.316 98.901  124.293 1.00 342.25 ? 3769 THR A CA    1 
ATOM   14950 C C     . THR A 1 3769 ? 155.392 98.585  125.463 1.00 342.25 ? 3769 THR A C     1 
ATOM   14951 O O     . THR A 1 3769 ? 155.495 99.201  126.531 1.00 342.25 ? 3769 THR A O     1 
ATOM   14952 C CB    . THR A 1 3769 ? 155.610 99.796  123.273 1.00 342.25 ? 3769 THR A CB    1 
ATOM   14953 O OG1   . THR A 1 3769 ? 156.331 99.771  122.035 1.00 342.25 ? 3769 THR A OG1   1 
ATOM   14954 C CG2   . THR A 1 3769 ? 155.539 101.229 123.777 1.00 342.25 ? 3769 THR A CG2   1 
ATOM   14955 N N     . LEU A 1 3770 ? 154.492 97.615  125.288 1.00 334.31 ? 3770 LEU A N     1 
ATOM   14956 C CA    . LEU A 1 3770 ? 153.546 97.280  126.347 1.00 334.31 ? 3770 LEU A CA    1 
ATOM   14957 C C     . LEU A 1 3770 ? 154.243 96.617  127.527 1.00 334.31 ? 3770 LEU A C     1 
ATOM   14958 O O     . LEU A 1 3770 ? 153.850 96.825  128.678 1.00 334.31 ? 3770 LEU A O     1 
ATOM   14959 C CB    . LEU A 1 3770 ? 152.435 96.386  125.798 1.00 334.31 ? 3770 LEU A CB    1 
ATOM   14960 C CG    . LEU A 1 3770 ? 151.243 97.163  125.234 1.00 334.31 ? 3770 LEU A CG    1 
ATOM   14961 C CD1   . LEU A 1 3770 ? 150.134 96.231  124.782 1.00 334.31 ? 3770 LEU A CD1   1 
ATOM   14962 C CD2   . LEU A 1 3770 ? 150.727 98.155  126.263 1.00 334.31 ? 3770 LEU A CD2   1 
ATOM   14963 N N     . GLU A 1 3771 ? 155.284 95.824  127.270 1.00 329.12 ? 3771 GLU A N     1 
ATOM   14964 C CA    . GLU A 1 3771 ? 156.028 95.215  128.363 1.00 329.12 ? 3771 GLU A CA    1 
ATOM   14965 C C     . GLU A 1 3771 ? 156.837 96.258  129.118 1.00 329.12 ? 3771 GLU A C     1 
ATOM   14966 O O     . GLU A 1 3771 ? 156.935 96.189  130.347 1.00 329.12 ? 3771 GLU A O     1 
ATOM   14967 C CB    . GLU A 1 3771 ? 156.928 94.099  127.822 1.00 329.12 ? 3771 GLU A CB    1 
ATOM   14968 C CG    . GLU A 1 3771 ? 157.373 93.050  128.849 1.00 329.12 ? 3771 GLU A CG    1 
ATOM   14969 C CD    . GLU A 1 3771 ? 158.353 93.568  129.885 1.00 329.12 ? 3771 GLU A CD    1 
ATOM   14970 O OE1   . GLU A 1 3771 ? 158.390 93.002  130.998 1.00 329.12 ? 3771 GLU A OE1   1 
ATOM   14971 O OE2   . GLU A 1 3771 ? 159.110 94.513  129.584 1.00 329.12 ? 3771 GLU A OE2   1 
ATOM   14972 N N     . ASN A 1 3772 ? 157.416 97.235  128.412 1.00 324.37 ? 3772 ASN A N     1 
ATOM   14973 C CA    . ASN A 1 3772 ? 158.085 98.327  129.113 1.00 324.37 ? 3772 ASN A CA    1 
ATOM   14974 C C     . ASN A 1 3772 ? 157.094 99.135  129.943 1.00 324.37 ? 3772 ASN A C     1 
ATOM   14975 O O     . ASN A 1 3772 ? 157.402 99.541  131.071 1.00 324.37 ? 3772 ASN A O     1 
ATOM   14976 C CB    . ASN A 1 3772 ? 158.820 99.228  128.124 1.00 324.37 ? 3772 ASN A CB    1 
ATOM   14977 C CG    . ASN A 1 3772 ? 159.996 99.942  128.758 1.00 324.37 ? 3772 ASN A CG    1 
ATOM   14978 O OD1   . ASN A 1 3772 ? 159.821 100.834 129.587 1.00 324.37 ? 3772 ASN A OD1   1 
ATOM   14979 N ND2   . ASN A 1 3772 ? 161.204 99.544  128.379 1.00 324.37 ? 3772 ASN A ND2   1 
ATOM   14980 N N     . LEU A 1 3773 ? 155.897 99.375  129.401 1.00 316.80 ? 3773 LEU A N     1 
ATOM   14981 C CA    . LEU A 1 3773 ? 154.861 100.062 130.165 1.00 316.80 ? 3773 LEU A CA    1 
ATOM   14982 C C     . LEU A 1 3773 ? 154.455 99.259  131.395 1.00 316.80 ? 3773 LEU A C     1 
ATOM   14983 O O     . LEU A 1 3773 ? 154.243 99.824  132.473 1.00 316.80 ? 3773 LEU A O     1 
ATOM   14984 C CB    . LEU A 1 3773 ? 153.648 100.328 129.274 1.00 316.80 ? 3773 LEU A CB    1 
ATOM   14985 C CG    . LEU A 1 3773 ? 153.640 101.636 128.484 1.00 316.80 ? 3773 LEU A CG    1 
ATOM   14986 C CD1   . LEU A 1 3773 ? 152.711 101.525 127.290 1.00 316.80 ? 3773 LEU A CD1   1 
ATOM   14987 C CD2   . LEU A 1 3773 ? 153.226 102.792 129.377 1.00 316.80 ? 3773 LEU A CD2   1 
ATOM   14988 N N     . LYS A 1 3774 ? 154.335 97.937  131.250 1.00 313.65 ? 3774 LYS A N     1 
ATOM   14989 C CA    . LYS A 1 3774 ? 153.989 97.088  132.384 1.00 313.65 ? 3774 LYS A CA    1 
ATOM   14990 C C     . LYS A 1 3774 ? 155.089 97.099  133.437 1.00 313.65 ? 3774 LYS A C     1 
ATOM   14991 O O     . LYS A 1 3774 ? 154.807 97.101  134.639 1.00 313.65 ? 3774 LYS A O     1 
ATOM   14992 C CB    . LYS A 1 3774 ? 153.709 95.663  131.907 1.00 313.65 ? 3774 LYS A CB    1 
ATOM   14993 C CG    . LYS A 1 3774 ? 153.220 94.726  133.002 1.00 313.65 ? 3774 LYS A CG    1 
ATOM   14994 C CD    . LYS A 1 3774 ? 152.706 93.411  132.432 1.00 313.65 ? 3774 LYS A CD    1 
ATOM   14995 C CE    . LYS A 1 3774 ? 153.627 92.866  131.352 1.00 313.65 ? 3774 LYS A CE    1 
ATOM   14996 N NZ    . LYS A 1 3774 ? 153.544 91.382  131.251 1.00 313.65 ? 3774 LYS A NZ    1 
ATOM   14997 N N     . ARG A 1 3775 ? 156.351 97.100  133.005 1.00 310.41 ? 3775 ARG A N     1 
ATOM   14998 C CA    . ARG A 1 3775 ? 157.460 97.192  133.949 1.00 310.41 ? 3775 ARG A CA    1 
ATOM   14999 C C     . ARG A 1 3775 ? 157.437 98.518  134.699 1.00 310.41 ? 3775 ARG A C     1 
ATOM   15000 O O     . ARG A 1 3775 ? 157.658 98.557  135.916 1.00 310.41 ? 3775 ARG A O     1 
ATOM   15001 C CB    . ARG A 1 3775 ? 158.787 97.010  133.214 1.00 310.41 ? 3775 ARG A CB    1 
ATOM   15002 C CG    . ARG A 1 3775 ? 159.990 96.867  134.128 0.00 310.41 ? 3775 ARG A CG    1 
ATOM   15003 C CD    . ARG A 1 3775 ? 161.201 96.344  133.370 0.00 310.41 ? 3775 ARG A CD    1 
ATOM   15004 N NE    . ARG A 1 3775 ? 160.875 95.205  132.519 0.00 310.41 ? 3775 ARG A NE    1 
ATOM   15005 C CZ    . ARG A 1 3775 ? 160.768 93.955  132.949 0.00 310.41 ? 3775 ARG A CZ    1 
ATOM   15006 N NH1   . ARG A 1 3775 ? 160.942 93.645  134.224 0.00 310.41 ? 3775 ARG A NH1   1 
ATOM   15007 N NH2   . ARG A 1 3775 ? 160.480 92.991  132.079 0.00 310.41 ? 3775 ARG A NH2   1 
ATOM   15008 N N     . GLU A 1 3776 ? 157.172 99.617  133.988 1.00 297.13 ? 3776 GLU A N     1 
ATOM   15009 C CA    . GLU A 1 3776 ? 157.071 100.915 134.649 1.00 297.13 ? 3776 GLU A CA    1 
ATOM   15010 C C     . GLU A 1 3776 ? 155.917 100.939 135.644 1.00 297.13 ? 3776 GLU A C     1 
ATOM   15011 O O     . GLU A 1 3776 ? 156.054 101.462 136.759 1.00 297.13 ? 3776 GLU A O     1 
ATOM   15012 C CB    . GLU A 1 3776 ? 156.907 102.021 133.607 1.00 297.13 ? 3776 GLU A CB    1 
ATOM   15013 C CG    . GLU A 1 3776 ? 158.151 102.275 132.779 1.00 297.13 ? 3776 GLU A CG    1 
ATOM   15014 C CD    . GLU A 1 3776 ? 159.353 102.615 133.635 1.00 297.13 ? 3776 GLU A CD    1 
ATOM   15015 O OE1   . GLU A 1 3776 ? 159.274 103.586 134.417 1.00 297.13 ? 3776 GLU A OE1   1 
ATOM   15016 O OE2   . GLU A 1 3776 ? 160.378 101.909 133.531 1.00 297.13 ? 3776 GLU A OE2   1 
ATOM   15017 N N     . ALA A 1 3777 ? 154.769 100.378 135.259 1.00 295.50 ? 3777 ALA A N     1 
ATOM   15018 C CA    . ALA A 1 3777 ? 153.626 100.326 136.163 1.00 295.50 ? 3777 ALA A CA    1 
ATOM   15019 C C     . ALA A 1 3777 ? 153.932 99.477  137.389 1.00 295.50 ? 3777 ALA A C     1 
ATOM   15020 O O     . ALA A 1 3777 ? 153.527 99.818  138.505 1.00 295.50 ? 3777 ALA A O     1 
ATOM   15021 C CB    . ALA A 1 3777 ? 152.399 99.788  135.428 1.00 295.50 ? 3777 ALA A CB    1 
ATOM   15022 N N     . ALA A 1 3778 ? 154.639 98.362  137.199 1.00 292.77 ? 3778 ALA A N     1 
ATOM   15023 C CA    . ALA A 1 3778 ? 155.020 97.521  138.329 1.00 292.77 ? 3778 ALA A CA    1 
ATOM   15024 C C     . ALA A 1 3778 ? 155.979 98.251  139.259 1.00 292.77 ? 3778 ALA A C     1 
ATOM   15025 O O     . ALA A 1 3778 ? 155.874 98.130  140.485 1.00 292.77 ? 3778 ALA A O     1 
ATOM   15026 C CB    . ALA A 1 3778 ? 155.642 96.218  137.828 1.00 292.77 ? 3778 ALA A CB    1 
ATOM   15027 N N     . GLU A 1 3779 ? 156.924 99.008  138.697 1.00 280.34 ? 3779 GLU A N     1 
ATOM   15028 C CA    . GLU A 1 3779 ? 157.820 99.803  139.531 1.00 280.34 ? 3779 GLU A CA    1 
ATOM   15029 C C     . GLU A 1 3779 ? 157.046 100.847 140.327 1.00 280.34 ? 3779 GLU A C     1 
ATOM   15030 O O     . GLU A 1 3779 ? 157.302 101.046 141.521 1.00 280.34 ? 3779 GLU A O     1 
ATOM   15031 C CB    . GLU A 1 3779 ? 158.890 100.468 138.668 1.00 280.34 ? 3779 GLU A CB    1 
ATOM   15032 C CG    . GLU A 1 3779 ? 160.205 100.701 139.390 1.00 280.34 ? 3779 GLU A CG    1 
ATOM   15033 C CD    . GLU A 1 3779 ? 160.530 99.599  140.379 1.00 280.34 ? 3779 GLU A CD    1 
ATOM   15034 O OE1   . GLU A 1 3779 ? 160.780 98.458  139.940 1.00 280.34 ? 3779 GLU A OE1   1 
ATOM   15035 O OE2   . GLU A 1 3779 ? 160.536 99.876  141.596 1.00 280.34 ? 3779 GLU A OE2   1 
ATOM   15036 N N     . VAL A 1 3780 ? 156.086 101.513 139.683 1.00 272.94 ? 3780 VAL A N     1 
ATOM   15037 C CA    . VAL A 1 3780 ? 155.276 102.509 140.379 1.00 272.94 ? 3780 VAL A CA    1 
ATOM   15038 C C     . VAL A 1 3780 ? 154.465 101.855 141.492 1.00 272.94 ? 3780 VAL A C     1 
ATOM   15039 O O     . VAL A 1 3780 ? 154.346 102.397 142.598 1.00 272.94 ? 3780 VAL A O     1 
ATOM   15040 C CB    . VAL A 1 3780 ? 154.372 103.254 139.378 1.00 272.94 ? 3780 VAL A CB    1 
ATOM   15041 C CG1   . VAL A 1 3780 ? 153.316 104.065 140.111 1.00 272.94 ? 3780 VAL A CG1   1 
ATOM   15042 C CG2   . VAL A 1 3780 ? 155.208 104.147 138.472 1.00 272.94 ? 3780 VAL A CG2   1 
ATOM   15043 N N     . THR A 1 3781 ? 153.889 100.683 141.214 1.00 273.45 ? 3781 THR A N     1 
ATOM   15044 C CA    . THR A 1 3781 ? 153.102 99.979  142.220 1.00 273.45 ? 3781 THR A CA    1 
ATOM   15045 C C     . THR A 1 3781 ? 153.968 99.539  143.393 1.00 273.45 ? 3781 THR A C     1 
ATOM   15046 O O     . THR A 1 3781 ? 153.538 99.605  144.550 1.00 273.45 ? 3781 THR A O     1 
ATOM   15047 C CB    . THR A 1 3781 ? 152.401 98.776  141.590 1.00 273.45 ? 3781 THR A CB    1 
ATOM   15048 O OG1   . THR A 1 3781 ? 151.933 99.127  140.282 1.00 273.45 ? 3781 THR A OG1   1 
ATOM   15049 C CG2   . THR A 1 3781 ? 151.221 98.340  142.447 1.00 273.45 ? 3781 THR A CG2   1 
ATOM   15050 N N     . ARG A 1 3782 ? 155.189 99.079  143.117 1.00 268.94 ? 3782 ARG A N     1 
ATOM   15051 C CA    . ARG A 1 3782 ? 156.107 98.742  144.199 1.00 268.94 ? 3782 ARG A CA    1 
ATOM   15052 C C     . ARG A 1 3782 ? 156.449 99.976  145.021 1.00 268.94 ? 3782 ARG A C     1 
ATOM   15053 O O     . ARG A 1 3782 ? 156.549 99.906  146.252 1.00 268.94 ? 3782 ARG A O     1 
ATOM   15054 C CB    . ARG A 1 3782 ? 157.375 98.098  143.636 1.00 268.94 ? 3782 ARG A CB    1 
ATOM   15055 C CG    . ARG A 1 3782 ? 158.554 98.104  144.599 1.00 268.94 ? 3782 ARG A CG    1 
ATOM   15056 C CD    . ARG A 1 3782 ? 159.837 97.636  143.930 1.00 268.94 ? 3782 ARG A CD    1 
ATOM   15057 N NE    . ARG A 1 3782 ? 161.003 97.862  144.777 1.00 268.94 ? 3782 ARG A NE    1 
ATOM   15058 C CZ    . ARG A 1 3782 ? 161.847 98.875  144.635 1.00 268.94 ? 3782 ARG A CZ    1 
ATOM   15059 N NH1   . ARG A 1 3782 ? 161.689 99.779  143.682 1.00 268.94 ? 3782 ARG A NH1   1 
ATOM   15060 N NH2   . ARG A 1 3782 ? 162.875 98.984  145.472 1.00 268.94 ? 3782 ARG A NH2   1 
ATOM   15061 N N     . LYS A 1 3783 ? 156.629 101.120 144.355 1.00 254.75 ? 3783 LYS A N     1 
ATOM   15062 C CA    . LYS A 1 3783 ? 156.921 102.355 145.075 1.00 254.75 ? 3783 LYS A CA    1 
ATOM   15063 C C     . LYS A 1 3783 ? 155.768 102.750 145.990 1.00 254.75 ? 3783 LYS A C     1 
ATOM   15064 O O     . LYS A 1 3783 ? 155.986 103.131 147.147 1.00 254.75 ? 3783 LYS A O     1 
ATOM   15065 C CB    . LYS A 1 3783 ? 157.232 103.477 144.086 1.00 254.75 ? 3783 LYS A CB    1 
ATOM   15066 C CG    . LYS A 1 3783 ? 158.611 103.380 143.465 1.00 254.75 ? 3783 LYS A CG    1 
ATOM   15067 C CD    . LYS A 1 3783 ? 158.966 104.647 142.711 1.00 254.75 ? 3783 LYS A CD    1 
ATOM   15068 C CE    . LYS A 1 3783 ? 160.398 104.599 142.207 1.00 254.75 ? 3783 LYS A CE    1 
ATOM   15069 N NZ    . LYS A 1 3783 ? 161.287 103.850 143.137 1.00 254.75 ? 3783 LYS A NZ    1 
ATOM   15070 N N     . VAL A 1 3784 ? 154.531 102.661 145.495 1.00 253.39 ? 3784 VAL A N     1 
ATOM   15071 C CA    . VAL A 1 3784 ? 153.387 103.025 146.329 1.00 253.39 ? 3784 VAL A CA    1 
ATOM   15072 C C     . VAL A 1 3784 ? 153.092 101.968 147.384 1.00 253.39 ? 3784 VAL A C     1 
ATOM   15073 O O     . VAL A 1 3784 ? 152.414 102.266 148.375 1.00 253.39 ? 3784 VAL A O     1 
ATOM   15074 C CB    . VAL A 1 3784 ? 152.121 103.287 145.495 1.00 253.39 ? 3784 VAL A CB    1 
ATOM   15075 C CG1   . VAL A 1 3784 ? 152.430 104.209 144.328 1.00 253.39 ? 3784 VAL A CG1   1 
ATOM   15076 C CG2   . VAL A 1 3784 ? 151.503 101.982 145.017 1.00 253.39 ? 3784 VAL A CG2   1 
ATOM   15077 N N     . GLU A 1 3785 ? 153.576 100.742 147.201 1.00 256.91 ? 3785 GLU A N     1 
ATOM   15078 C CA    . GLU A 1 3785 ? 153.447 99.706  148.214 1.00 256.91 ? 3785 GLU A CA    1 
ATOM   15079 C C     . GLU A 1 3785 ? 154.545 99.772  149.264 1.00 256.91 ? 3785 GLU A C     1 
ATOM   15080 O O     . GLU A 1 3785 ? 154.422 99.126  150.311 1.00 256.91 ? 3785 GLU A O     1 
ATOM   15081 C CB    . GLU A 1 3785 ? 153.456 98.322  147.556 1.00 256.91 ? 3785 GLU A CB    1 
ATOM   15082 C CG    . GLU A 1 3785 ? 152.141 97.935  146.903 1.00 256.91 ? 3785 GLU A CG    1 
ATOM   15083 C CD    . GLU A 1 3785 ? 152.333 96.993  145.731 1.00 256.91 ? 3785 GLU A CD    1 
ATOM   15084 O OE1   . GLU A 1 3785 ? 153.491 96.808  145.302 1.00 256.91 ? 3785 GLU A OE1   1 
ATOM   15085 O OE2   . GLU A 1 3785 ? 151.329 96.441  145.235 1.00 256.91 ? 3785 GLU A OE2   1 
ATOM   15086 N N     . GLU A 1 3786 ? 155.609 100.539 149.014 1.00 248.07 ? 3786 GLU A N     1 
ATOM   15087 C CA    . GLU A 1 3786 ? 156.738 100.651 149.930 1.00 248.07 ? 3786 GLU A CA    1 
ATOM   15088 C C     . GLU A 1 3786 ? 156.897 102.066 150.473 1.00 248.07 ? 3786 GLU A C     1 
ATOM   15089 O O     . GLU A 1 3786 ? 157.924 102.376 151.086 1.00 248.07 ? 3786 GLU A O     1 
ATOM   15090 C CB    . GLU A 1 3786 ? 158.031 100.209 149.240 1.00 248.07 ? 3786 GLU A CB    1 
ATOM   15091 C CG    . GLU A 1 3786 ? 158.129 98.719  148.974 1.00 248.07 ? 3786 GLU A CG    1 
ATOM   15092 C CD    . GLU A 1 3786 ? 159.527 98.299  148.563 1.00 248.07 ? 3786 GLU A CD    1 
ATOM   15093 O OE1   . GLU A 1 3786 ? 160.494 98.704  149.243 1.00 248.07 ? 3786 GLU A OE1   1 
ATOM   15094 O OE2   . GLU A 1 3786 ? 159.660 97.568  147.560 1.00 248.07 ? 3786 GLU A OE2   1 
ATOM   15095 N N     . THR A 1 3787 ? 155.901 102.931 150.264 1.00 227.02 ? 3787 THR A N     1 
ATOM   15096 C CA    . THR A 1 3787 ? 156.046 104.326 150.664 1.00 227.02 ? 3787 THR A CA    1 
ATOM   15097 C C     . THR A 1 3787 ? 156.182 104.460 152.177 1.00 227.02 ? 3787 THR A C     1 
ATOM   15098 O O     . THR A 1 3787 ? 156.882 105.354 152.664 1.00 227.02 ? 3787 THR A O     1 
ATOM   15099 C CB    . THR A 1 3787 ? 154.870 105.156 150.137 1.00 227.02 ? 3787 THR A CB    1 
ATOM   15100 O OG1   . THR A 1 3787 ? 155.172 106.551 150.261 1.00 227.02 ? 3787 THR A OG1   1 
ATOM   15101 C CG2   . THR A 1 3787 ? 153.582 104.847 150.890 1.00 227.02 ? 3787 THR A CG2   1 
ATOM   15102 N N     . ASP A 1 3788 ? 155.540 103.571 152.939 1.00 219.15 ? 3788 ASP A N     1 
ATOM   15103 C CA    . ASP A 1 3788 ? 155.675 103.622 154.391 1.00 219.15 ? 3788 ASP A CA    1 
ATOM   15104 C C     . ASP A 1 3788 ? 157.087 103.255 154.829 1.00 219.15 ? 3788 ASP A C     1 
ATOM   15105 O O     . ASP A 1 3788 ? 157.660 103.913 155.705 1.00 219.15 ? 3788 ASP A O     1 
ATOM   15106 C CB    . ASP A 1 3788 ? 154.650 102.700 155.048 1.00 219.15 ? 3788 ASP A CB    1 
ATOM   15107 C CG    . ASP A 1 3788 ? 153.234 103.219 154.914 1.00 219.15 ? 3788 ASP A CG    1 
ATOM   15108 O OD1   . ASP A 1 3788 ? 153.017 104.151 154.113 1.00 219.15 ? 3788 ASP A OD1   1 
ATOM   15109 O OD2   . ASP A 1 3788 ? 152.339 102.699 155.612 1.00 219.15 ? 3788 ASP A OD2   1 
ATOM   15110 N N     . ILE A 1 3789 ? 157.666 102.214 154.228 1.00 213.74 ? 3789 ILE A N     1 
ATOM   15111 C CA    . ILE A 1 3789 ? 159.011 101.787 154.606 1.00 213.74 ? 3789 ILE A CA    1 
ATOM   15112 C C     . ILE A 1 3789 ? 160.031 102.860 154.244 1.00 213.74 ? 3789 ILE A C     1 
ATOM   15113 O O     . ILE A 1 3789 ? 160.915 103.200 155.041 1.00 213.74 ? 3789 ILE A O     1 
ATOM   15114 C CB    . ILE A 1 3789 ? 159.350 100.438 153.948 1.00 213.74 ? 3789 ILE A CB    1 
ATOM   15115 C CG1   . ILE A 1 3789 ? 158.420 99.343  154.473 1.00 213.74 ? 3789 ILE A CG1   1 
ATOM   15116 C CG2   . ILE A 1 3789 ? 160.801 100.068 154.205 1.00 213.74 ? 3789 ILE A CG2   1 
ATOM   15117 C CD1   . ILE A 1 3789 ? 158.323 99.291  155.982 1.00 213.74 ? 3789 ILE A CD1   1 
ATOM   15118 N N     . VAL A 1 3790 ? 159.922 103.411 153.033 1.00 201.66 ? 3790 VAL A N     1 
ATOM   15119 C CA    . VAL A 1 3790 ? 160.848 104.456 152.609 1.00 201.66 ? 3790 VAL A CA    1 
ATOM   15120 C C     . VAL A 1 3790 ? 160.679 105.699 153.474 1.00 201.66 ? 3790 VAL A C     1 
ATOM   15121 O O     . VAL A 1 3790 ? 161.662 106.351 153.843 1.00 201.66 ? 3790 VAL A O     1 
ATOM   15122 C CB    . VAL A 1 3790 ? 160.657 104.769 151.114 1.00 201.66 ? 3790 VAL A CB    1 
ATOM   15123 C CG1   . VAL A 1 3790 ? 161.650 105.828 150.661 1.00 201.66 ? 3790 VAL A CG1   1 
ATOM   15124 C CG2   . VAL A 1 3790 ? 160.819 103.505 150.289 1.00 201.66 ? 3790 VAL A CG2   1 
ATOM   15125 N N     . MET A 1 3791 ? 159.435 106.046 153.813 1.00 197.15 ? 3791 MET A N     1 
ATOM   15126 C CA    . MET A 1 3791 ? 159.195 107.198 154.674 1.00 197.15 ? 3791 MET A CA    1 
ATOM   15127 C C     . MET A 1 3791 ? 159.801 106.994 156.056 1.00 197.15 ? 3791 MET A C     1 
ATOM   15128 O O     . MET A 1 3791 ? 160.406 107.914 156.616 1.00 197.15 ? 3791 MET A O     1 
ATOM   15129 C CB    . MET A 1 3791 ? 157.696 107.471 154.782 1.00 197.15 ? 3791 MET A CB    1 
ATOM   15130 C CG    . MET A 1 3791 ? 157.163 108.398 153.706 1.00 197.15 ? 3791 MET A CG    1 
ATOM   15131 S SD    . MET A 1 3791 ? 155.525 109.042 154.087 1.00 197.15 ? 3791 MET A SD    1 
ATOM   15132 C CE    . MET A 1 3791 ? 154.783 109.025 152.459 1.00 197.15 ? 3791 MET A CE    1 
ATOM   15133 N N     . GLN A 1 3792 ? 159.650 105.797 156.626 1.00 188.36 ? 3792 GLN A N     1 
ATOM   15134 C CA    . GLN A 1 3792 ? 160.233 105.540 157.938 1.00 188.36 ? 3792 GLN A CA    1 
ATOM   15135 C C     . GLN A 1 3792 ? 161.755 105.568 157.881 1.00 188.36 ? 3792 GLN A C     1 
ATOM   15136 O O     . GLN A 1 3792 ? 162.405 106.077 158.801 1.00 188.36 ? 3792 GLN A O     1 
ATOM   15137 C CB    . GLN A 1 3792 ? 159.735 104.206 158.490 1.00 188.36 ? 3792 GLN A CB    1 
ATOM   15138 C CG    . GLN A 1 3792 ? 160.045 104.006 159.968 1.00 188.36 ? 3792 GLN A CG    1 
ATOM   15139 C CD    . GLN A 1 3792 ? 158.894 103.379 160.729 1.00 188.36 ? 3792 GLN A CD    1 
ATOM   15140 O OE1   . GLN A 1 3792 ? 157.732 103.723 160.514 1.00 188.36 ? 3792 GLN A OE1   1 
ATOM   15141 N NE2   . GLN A 1 3792 ? 159.212 102.455 161.629 1.00 188.36 ? 3792 GLN A NE2   1 
ATOM   15142 N N     . GLU A 1 3793 ? 162.344 105.028 156.811 1.00 184.38 ? 3793 GLU A N     1 
ATOM   15143 C CA    . GLU A 1 3793 ? 163.796 105.091 156.677 1.00 184.38 ? 3793 GLU A CA    1 
ATOM   15144 C C     . GLU A 1 3793 ? 164.272 106.534 156.564 1.00 184.38 ? 3793 GLU A C     1 
ATOM   15145 O O     . GLU A 1 3793 ? 165.264 106.924 157.196 1.00 184.38 ? 3793 GLU A O     1 
ATOM   15146 C CB    . GLU A 1 3793 ? 164.257 104.278 155.467 1.00 184.38 ? 3793 GLU A CB    1 
ATOM   15147 C CG    . GLU A 1 3793 ? 165.492 104.847 154.783 1.00 184.38 ? 3793 GLU A CG    1 
ATOM   15148 C CD    . GLU A 1 3793 ? 165.995 103.975 153.653 1.00 184.38 ? 3793 GLU A CD    1 
ATOM   15149 O OE1   . GLU A 1 3793 ? 166.797 104.470 152.833 1.00 184.38 ? 3793 GLU A OE1   1 
ATOM   15150 O OE2   . GLU A 1 3793 ? 165.589 102.796 153.584 1.00 184.38 ? 3793 GLU A OE2   1 
ATOM   15151 N N     . VAL A 1 3794 ? 163.568 107.345 155.771 1.00 175.90 ? 3794 VAL A N     1 
ATOM   15152 C CA    . VAL A 1 3794 ? 163.928 108.751 155.630 1.00 175.90 ? 3794 VAL A CA    1 
ATOM   15153 C C     . VAL A 1 3794 ? 163.806 109.464 156.968 1.00 175.90 ? 3794 VAL A C     1 
ATOM   15154 O O     . VAL A 1 3794 ? 164.656 110.284 157.329 1.00 175.90 ? 3794 VAL A O     1 
ATOM   15155 C CB    . VAL A 1 3794 ? 163.059 109.416 154.548 1.00 175.90 ? 3794 VAL A CB    1 
ATOM   15156 C CG1   . VAL A 1 3794 ? 163.172 110.927 154.627 1.00 175.90 ? 3794 VAL A CG1   1 
ATOM   15157 C CG2   . VAL A 1 3794 ? 163.468 108.920 153.173 1.00 175.90 ? 3794 VAL A CG2   1 
ATOM   15158 N N     . GLU A 1 3795 ? 162.753 109.156 157.728 1.00 175.21 ? 3795 GLU A N     1 
ATOM   15159 C CA    . GLU A 1 3795 ? 162.589 109.756 159.047 1.00 175.21 ? 3795 GLU A CA    1 
ATOM   15160 C C     . GLU A 1 3795 ? 163.739 109.377 159.970 1.00 175.21 ? 3795 GLU A C     1 
ATOM   15161 O O     . GLU A 1 3795 ? 164.258 110.224 160.704 1.00 175.21 ? 3795 GLU A O     1 
ATOM   15162 C CB    . GLU A 1 3795 ? 161.252 109.330 159.656 1.00 175.21 ? 3795 GLU A CB    1 
ATOM   15163 C CG    . GLU A 1 3795 ? 161.170 109.490 161.169 1.00 175.21 ? 3795 GLU A CG    1 
ATOM   15164 C CD    . GLU A 1 3795 ? 161.590 108.236 161.918 1.00 175.21 ? 3795 GLU A CD    1 
ATOM   15165 O OE1   . GLU A 1 3795 ? 161.495 107.136 161.337 1.00 175.21 ? 3795 GLU A OE1   1 
ATOM   15166 O OE2   . GLU A 1 3795 ? 162.024 108.354 163.083 1.00 175.21 ? 3795 GLU A OE2   1 
ATOM   15167 N N     . THR A 1 3796 ? 164.143 108.105 159.955 1.00 166.08 ? 3796 THR A N     1 
ATOM   15168 C CA    . THR A 1 3796 ? 165.240 107.672 160.815 1.00 166.08 ? 3796 THR A CA    1 
ATOM   15169 C C     . THR A 1 3796 ? 166.537 108.380 160.446 1.00 166.08 ? 3796 THR A C     1 
ATOM   15170 O O     . THR A 1 3796 ? 167.272 108.853 161.321 1.00 166.08 ? 3796 THR A O     1 
ATOM   15171 C CB    . THR A 1 3796 ? 165.415 106.156 160.728 1.00 166.08 ? 3796 THR A CB    1 
ATOM   15172 O OG1   . THR A 1 3796 ? 165.523 105.766 159.355 1.00 166.08 ? 3796 THR A OG1   1 
ATOM   15173 C CG2   . THR A 1 3796 ? 164.237 105.444 161.369 1.00 166.08 ? 3796 THR A CG2   1 
ATOM   15174 N N     . VAL A 1 3797 ? 166.830 108.474 159.150 1.00 152.62 ? 3797 VAL A N     1 
ATOM   15175 C CA    . VAL A 1 3797 ? 168.066 109.130 158.734 1.00 152.62 ? 3797 VAL A CA    1 
ATOM   15176 C C     . VAL A 1 3797 ? 168.023 110.617 159.067 1.00 152.62 ? 3797 VAL A C     1 
ATOM   15177 O O     . VAL A 1 3797 ? 169.029 111.204 159.490 1.00 152.62 ? 3797 VAL A O     1 
ATOM   15178 C CB    . VAL A 1 3797 ? 168.327 108.882 157.239 1.00 152.62 ? 3797 VAL A CB    1 
ATOM   15179 C CG1   . VAL A 1 3797 ? 169.666 109.463 156.839 1.00 152.62 ? 3797 VAL A CG1   1 
ATOM   15180 C CG2   . VAL A 1 3797 ? 168.308 107.397 156.952 1.00 152.62 ? 3797 VAL A CG2   1 
ATOM   15181 N N     . SER A 1 3798 ? 166.863 111.251 158.890 1.00 152.61 ? 3798 SER A N     1 
ATOM   15182 C CA    . SER A 1 3798 ? 166.736 112.664 159.226 1.00 152.61 ? 3798 SER A CA    1 
ATOM   15183 C C     . SER A 1 3798 ? 166.895 112.895 160.722 1.00 152.61 ? 3798 SER A C     1 
ATOM   15184 O O     . SER A 1 3798 ? 167.510 113.881 161.137 1.00 152.61 ? 3798 SER A O     1 
ATOM   15185 C CB    . SER A 1 3798 ? 165.391 113.200 158.737 1.00 152.61 ? 3798 SER A CB    1 
ATOM   15186 O OG    . SER A 1 3798 ? 165.273 113.057 157.332 1.00 152.61 ? 3798 SER A OG    1 
ATOM   15187 N N     . GLN A 1 3799 ? 166.341 112.008 161.548 1.00 141.26 ? 3799 GLN A N     1 
ATOM   15188 C CA    . GLN A 1 3799 ? 166.542 112.128 162.986 1.00 141.26 ? 3799 GLN A CA    1 
ATOM   15189 C C     . GLN A 1 3799 ? 168.001 111.911 163.359 1.00 141.26 ? 3799 GLN A C     1 
ATOM   15190 O O     . GLN A 1 3799 ? 168.498 112.534 164.304 1.00 141.26 ? 3799 GLN A O     1 
ATOM   15191 C CB    . GLN A 1 3799 ? 165.647 111.141 163.732 1.00 141.26 ? 3799 GLN A CB    1 
ATOM   15192 C CG    . GLN A 1 3799 ? 164.189 111.566 163.814 1.00 141.26 ? 3799 GLN A CG    1 
ATOM   15193 C CD    . GLN A 1 3799 ? 163.968 112.747 164.743 1.00 141.26 ? 3799 GLN A CD    1 
ATOM   15194 O OE1   . GLN A 1 3799 ? 164.862 113.141 165.492 1.00 141.26 ? 3799 GLN A OE1   1 
ATOM   15195 N NE2   . GLN A 1 3799 ? 162.770 113.318 164.697 1.00 141.26 ? 3799 GLN A NE2   1 
ATOM   15196 N N     . GLN A 1 3800 ? 168.695 111.030 162.638 1.00 133.51 ? 3800 GLN A N     1 
ATOM   15197 C CA    . GLN A 1 3800 ? 170.124 110.850 162.868 1.00 133.51 ? 3800 GLN A CA    1 
ATOM   15198 C C     . GLN A 1 3800 ? 170.902 112.118 162.538 1.00 133.51 ? 3800 GLN A C     1 
ATOM   15199 O O     . GLN A 1 3800 ? 171.805 112.514 163.283 1.00 133.51 ? 3800 GLN A O     1 
ATOM   15200 C CB    . GLN A 1 3800 ? 170.642 109.677 162.038 1.00 133.51 ? 3800 GLN A CB    1 
ATOM   15201 C CG    . GLN A 1 3800 ? 172.154 109.603 161.952 1.00 133.51 ? 3800 GLN A CG    1 
ATOM   15202 C CD    . GLN A 1 3800 ? 172.637 108.367 161.224 1.00 133.51 ? 3800 GLN A CD    1 
ATOM   15203 O OE1   . GLN A 1 3800 ? 172.166 108.053 160.132 1.00 133.51 ? 3800 GLN A OE1   1 
ATOM   15204 N NE2   . GLN A 1 3800 ? 173.584 107.659 161.824 1.00 133.51 ? 3800 GLN A NE2   1 
ATOM   15205 N N     . TYR A 1 3801 ? 170.563 112.771 161.432 1.00 120.14 ? 3801 TYR A N     1 
ATOM   15206 C CA    . TYR A 1 3801 ? 171.342 113.901 160.945 1.00 120.14 ? 3801 TYR A CA    1 
ATOM   15207 C C     . TYR A 1 3801 ? 170.847 115.252 161.450 1.00 120.14 ? 3801 TYR A C     1 
ATOM   15208 O O     . TYR A 1 3801 ? 171.463 116.274 161.135 1.00 120.14 ? 3801 TYR A O     1 
ATOM   15209 C CB    . TYR A 1 3801 ? 171.359 113.900 159.417 1.00 120.14 ? 3801 TYR A CB    1 
ATOM   15210 C CG    . TYR A 1 3801 ? 172.310 112.890 158.822 1.00 120.14 ? 3801 TYR A CG    1 
ATOM   15211 C CD1   . TYR A 1 3801 ? 172.160 111.534 159.069 1.00 120.14 ? 3801 TYR A CD1   1 
ATOM   15212 C CD2   . TYR A 1 3801 ? 173.357 113.293 158.011 1.00 120.14 ? 3801 TYR A CD2   1 
ATOM   15213 C CE1   . TYR A 1 3801 ? 173.027 110.612 158.528 1.00 120.14 ? 3801 TYR A CE1   1 
ATOM   15214 C CE2   . TYR A 1 3801 ? 174.228 112.378 157.463 1.00 120.14 ? 3801 TYR A CE2   1 
ATOM   15215 C CZ    . TYR A 1 3801 ? 174.059 111.039 157.726 1.00 120.14 ? 3801 TYR A CZ    1 
ATOM   15216 O OH    . TYR A 1 3801 ? 174.926 110.122 157.183 1.00 120.14 ? 3801 TYR A OH    1 
ATOM   15217 N N     . LEU A 1 3802 ? 169.756 115.284 162.210 1.00 111.27 ? 3802 LEU A N     1 
ATOM   15218 C CA    . LEU A 1 3802 ? 169.245 116.553 162.729 1.00 111.27 ? 3802 LEU A CA    1 
ATOM   15219 C C     . LEU A 1 3802 ? 170.230 117.296 163.623 1.00 111.27 ? 3802 LEU A C     1 
ATOM   15220 O O     . LEU A 1 3802 ? 170.364 118.523 163.462 1.00 111.27 ? 3802 LEU A O     1 
ATOM   15221 C CB    . LEU A 1 3802 ? 167.925 116.302 163.464 1.00 111.27 ? 3802 LEU A CB    1 
ATOM   15222 C CG    . LEU A 1 3802 ? 167.415 117.446 164.338 1.00 111.27 ? 3802 LEU A CG    1 
ATOM   15223 C CD1   . LEU A 1 3802 ? 166.925 118.590 163.469 1.00 111.27 ? 3802 LEU A CD1   1 
ATOM   15224 C CD2   . LEU A 1 3802 ? 166.317 116.964 165.272 1.00 111.27 ? 3802 LEU A CD2   1 
ATOM   15225 N N     . PRO A 1 3803 ? 170.915 116.659 164.581 1.00 102.59 ? 3803 PRO A N     1 
ATOM   15226 C CA    . PRO A 1 3803 ? 171.807 117.433 165.458 1.00 102.59 ? 3803 PRO A CA    1 
ATOM   15227 C C     . PRO A 1 3803 ? 172.864 118.217 164.710 1.00 102.59 ? 3803 PRO A C     1 
ATOM   15228 O O     . PRO A 1 3803 ? 173.183 119.343 165.112 1.00 102.59 ? 3803 PRO A O     1 
ATOM   15229 C CB    . PRO A 1 3803 ? 172.429 116.357 166.357 1.00 102.59 ? 3803 PRO A CB    1 
ATOM   15230 C CG    . PRO A 1 3803 ? 171.422 115.279 166.383 1.00 102.59 ? 3803 PRO A CG    1 
ATOM   15231 C CD    . PRO A 1 3803 ? 170.845 115.249 165.006 1.00 102.59 ? 3803 PRO A CD    1 
ATOM   15232 N N     . LEU A 1 3804 ? 173.406 117.667 163.623 1.00 97.47  ? 3804 LEU A N     1 
ATOM   15233 C CA    . LEU A 1 3804 ? 174.398 118.404 162.850 1.00 97.47  ? 3804 LEU A CA    1 
ATOM   15234 C C     . LEU A 1 3804 ? 173.809 119.685 162.281 1.00 97.47  ? 3804 LEU A C     1 
ATOM   15235 O O     . LEU A 1 3804 ? 174.448 120.742 162.318 1.00 97.47  ? 3804 LEU A O     1 
ATOM   15236 C CB    . LEU A 1 3804 ? 174.954 117.521 161.734 1.00 97.47  ? 3804 LEU A CB    1 
ATOM   15237 C CG    . LEU A 1 3804 ? 175.862 118.142 160.669 1.00 97.47  ? 3804 LEU A CG    1 
ATOM   15238 C CD1   . LEU A 1 3804 ? 176.774 117.077 160.134 1.00 97.47  ? 3804 LEU A CD1   1 
ATOM   15239 C CD2   . LEU A 1 3804 ? 175.073 118.729 159.513 1.00 97.47  ? 3804 LEU A CD2   1 
ATOM   15240 N N     . SER A 1 3805 ? 172.594 119.613 161.741 1.00 100.36 ? 3805 SER A N     1 
ATOM   15241 C CA    . SER A 1 3805 ? 171.998 120.799 161.140 1.00 100.36 ? 3805 SER A CA    1 
ATOM   15242 C C     . SER A 1 3805 ? 171.619 121.826 162.200 1.00 100.36 ? 3805 SER A C     1 
ATOM   15243 O O     . SER A 1 3805 ? 171.744 123.035 161.972 1.00 100.36 ? 3805 SER A O     1 
ATOM   15244 C CB    . SER A 1 3805 ? 170.784 120.409 160.303 1.00 100.36 ? 3805 SER A CB    1 
ATOM   15245 O OG    . SER A 1 3805 ? 169.875 121.486 160.208 1.00 100.36 ? 3805 SER A OG    1 
ATOM   15246 N N     . THR A 1 3806 ? 171.149 121.369 163.365 1.00 97.00  ? 3806 THR A N     1 
ATOM   15247 C CA    . THR A 1 3806 ? 170.886 122.308 164.453 1.00 97.00  ? 3806 THR A CA    1 
ATOM   15248 C C     . THR A 1 3806 ? 172.167 123.008 164.884 1.00 97.00  ? 3806 THR A C     1 
ATOM   15249 O O     . THR A 1 3806 ? 172.178 124.227 165.109 1.00 97.00  ? 3806 THR A O     1 
ATOM   15250 C CB    . THR A 1 3806 ? 170.248 121.590 165.641 1.00 97.00  ? 3806 THR A CB    1 
ATOM   15251 O OG1   . THR A 1 3806 ? 171.102 120.525 166.074 1.00 97.00  ? 3806 THR A OG1   1 
ATOM   15252 C CG2   . THR A 1 3806 ? 168.892 121.030 165.265 1.00 97.00  ? 3806 THR A CG2   1 
ATOM   15253 N N     . ALA A 1 3807 ? 173.260 122.252 164.992 1.00 92.01  ? 3807 ALA A N     1 
ATOM   15254 C CA    . ALA A 1 3807 ? 174.542 122.852 165.329 1.00 92.01  ? 3807 ALA A CA    1 
ATOM   15255 C C     . ALA A 1 3807 ? 174.980 123.842 164.263 1.00 92.01  ? 3807 ALA A C     1 
ATOM   15256 O O     . ALA A 1 3807 ? 175.546 124.890 164.580 1.00 92.01  ? 3807 ALA A O     1 
ATOM   15257 C CB    . ALA A 1 3807 ? 175.597 121.765 165.518 1.00 92.01  ? 3807 ALA A CB    1 
ATOM   15258 N N     . CYS A 1 3808 ? 174.737 123.525 162.991 1.00 91.61  ? 3808 CYS A N     1 
ATOM   15259 C CA    . CYS A 1 3808 ? 175.105 124.447 161.921 1.00 91.61  ? 3808 CYS A CA    1 
ATOM   15260 C C     . CYS A 1 3808 ? 174.317 125.745 162.008 1.00 91.61  ? 3808 CYS A C     1 
ATOM   15261 O O     . CYS A 1 3808 ? 174.877 126.834 161.834 1.00 91.61  ? 3808 CYS A O     1 
ATOM   15262 C CB    . CYS A 1 3808 ? 174.893 123.792 160.562 1.00 91.61  ? 3808 CYS A CB    1 
ATOM   15263 S SG    . CYS A 1 3808 ? 176.369 123.004 159.947 1.00 91.61  ? 3808 CYS A SG    1 
ATOM   15264 N N     . SER A 1 3809 ? 173.014 125.651 162.262 1.00 92.94  ? 3809 SER A N     1 
ATOM   15265 C CA    . SER A 1 3809 ? 172.215 126.861 162.409 1.00 92.94  ? 3809 SER A CA    1 
ATOM   15266 C C     . SER A 1 3809 ? 172.705 127.693 163.585 1.00 92.94  ? 3809 SER A C     1 
ATOM   15267 O O     . SER A 1 3809 ? 172.835 128.921 163.478 1.00 92.94  ? 3809 SER A O     1 
ATOM   15268 C CB    . SER A 1 3809 ? 170.742 126.499 162.582 1.00 92.94  ? 3809 SER A CB    1 
ATOM   15269 O OG    . SER A 1 3809 ? 170.602 125.312 163.341 1.00 92.94  ? 3809 SER A OG    1 
ATOM   15270 N N     . SER A 1 3810 ? 172.997 127.039 164.712 1.00 87.86  ? 3810 SER A N     1 
ATOM   15271 C CA    . SER A 1 3810 ? 173.505 127.765 165.870 1.00 87.86  ? 3810 SER A CA    1 
ATOM   15272 C C     . SER A 1 3810 ? 174.846 128.421 165.564 1.00 87.86  ? 3810 SER A C     1 
ATOM   15273 O O     . SER A 1 3810 ? 175.091 129.566 165.961 1.00 87.86  ? 3810 SER A O     1 
ATOM   15274 C CB    . SER A 1 3810 ? 173.625 126.821 167.064 1.00 87.86  ? 3810 SER A CB    1 
ATOM   15275 O OG    . SER A 1 3810 ? 172.418 126.111 167.270 1.00 87.86  ? 3810 SER A OG    1 
ATOM   15276 N N     . ILE A 1 3811 ? 175.723 127.711 164.852 1.00 87.07  ? 3811 ILE A N     1 
ATOM   15277 C CA    . ILE A 1 3811 ? 177.020 128.265 164.477 1.00 87.07  ? 3811 ILE A CA    1 
ATOM   15278 C C     . ILE A 1 3811 ? 176.836 129.505 163.617 1.00 87.07  ? 3811 ILE A C     1 
ATOM   15279 O O     . ILE A 1 3811 ? 177.469 130.542 163.848 1.00 87.07  ? 3811 ILE A O     1 
ATOM   15280 C CB    . ILE A 1 3811 ? 177.863 127.207 163.744 1.00 87.07  ? 3811 ILE A CB    1 
ATOM   15281 C CG1   . ILE A 1 3811 ? 178.436 126.182 164.721 1.00 87.07  ? 3811 ILE A CG1   1 
ATOM   15282 C CG2   . ILE A 1 3811 ? 178.980 127.868 162.956 1.00 87.07  ? 3811 ILE A CG2   1 
ATOM   15283 C CD1   . ILE A 1 3811 ? 178.944 126.776 165.995 1.00 87.07  ? 3811 ILE A CD1   1 
ATOM   15284 N N     . TYR A 1 3812 ? 175.972 129.416 162.604 1.00 89.32  ? 3812 TYR A N     1 
ATOM   15285 C CA    . TYR A 1 3812 ? 175.794 130.555 161.713 1.00 89.32  ? 3812 TYR A CA    1 
ATOM   15286 C C     . TYR A 1 3812 ? 175.218 131.748 162.454 1.00 89.32  ? 3812 TYR A C     1 
ATOM   15287 O O     . TYR A 1 3812 ? 175.644 132.885 162.233 1.00 89.32  ? 3812 TYR A O     1 
ATOM   15288 C CB    . TYR A 1 3812 ? 174.893 130.206 160.536 1.00 89.32  ? 3812 TYR A CB    1 
ATOM   15289 C CG    . TYR A 1 3812 ? 174.490 131.444 159.770 1.00 89.32  ? 3812 TYR A CG    1 
ATOM   15290 C CD1   . TYR A 1 3812 ? 175.381 132.067 158.913 1.00 89.32  ? 3812 TYR A CD1   1 
ATOM   15291 C CD2   . TYR A 1 3812 ? 173.233 132.008 159.929 1.00 89.32  ? 3812 TYR A CD2   1 
ATOM   15292 C CE1   . TYR A 1 3812 ? 175.028 133.202 158.222 1.00 89.32  ? 3812 TYR A CE1   1 
ATOM   15293 C CE2   . TYR A 1 3812 ? 172.871 133.143 159.242 1.00 89.32  ? 3812 TYR A CE2   1 
ATOM   15294 C CZ    . TYR A 1 3812 ? 173.773 133.735 158.390 1.00 89.32  ? 3812 TYR A CZ    1 
ATOM   15295 O OH    . TYR A 1 3812 ? 173.417 134.870 157.701 1.00 89.32  ? 3812 TYR A OH    1 
ATOM   15296 N N     . PHE A 1 3813 ? 174.233 131.520 163.321 1.00 93.99  ? 3813 PHE A N     1 
ATOM   15297 C CA    . PHE A 1 3813 ? 173.624 132.655 164.000 1.00 93.99  ? 3813 PHE A CA    1 
ATOM   15298 C C     . PHE A 1 3813 ? 174.565 133.260 165.032 1.00 93.99  ? 3813 PHE A C     1 
ATOM   15299 O O     . PHE A 1 3813 ? 174.567 134.482 165.223 1.00 93.99  ? 3813 PHE A O     1 
ATOM   15300 C CB    . PHE A 1 3813 ? 172.297 132.243 164.627 1.00 93.99  ? 3813 PHE A CB    1 
ATOM   15301 C CG    . PHE A 1 3813 ? 171.158 132.267 163.657 1.00 93.99  ? 3813 PHE A CG    1 
ATOM   15302 C CD1   . PHE A 1 3813 ? 170.775 133.451 163.052 1.00 93.99  ? 3813 PHE A CD1   1 
ATOM   15303 C CD2   . PHE A 1 3813 ? 170.490 131.108 163.324 1.00 93.99  ? 3813 PHE A CD2   1 
ATOM   15304 C CE1   . PHE A 1 3813 ? 169.737 133.478 162.149 1.00 93.99  ? 3813 PHE A CE1   1 
ATOM   15305 C CE2   . PHE A 1 3813 ? 169.451 131.129 162.420 1.00 93.99  ? 3813 PHE A CE2   1 
ATOM   15306 C CZ    . PHE A 1 3813 ? 169.073 132.315 161.833 1.00 93.99  ? 3813 PHE A CZ    1 
ATOM   15307 N N     . THR A 1 3814 ? 175.389 132.438 165.682 1.00 89.31  ? 3814 THR A N     1 
ATOM   15308 C CA    . THR A 1 3814 ? 176.426 132.982 166.546 1.00 89.31  ? 3814 THR A CA    1 
ATOM   15309 C C     . THR A 1 3814 ? 177.412 133.825 165.748 1.00 89.31  ? 3814 THR A C     1 
ATOM   15310 O O     . THR A 1 3814 ? 177.763 134.938 166.155 1.00 89.31  ? 3814 THR A O     1 
ATOM   15311 C CB    . THR A 1 3814 ? 177.150 131.847 167.264 1.00 89.31  ? 3814 THR A CB    1 
ATOM   15312 O OG1   . THR A 1 3814 ? 176.251 131.214 168.180 1.00 89.31  ? 3814 THR A OG1   1 
ATOM   15313 C CG2   . THR A 1 3814 ? 178.347 132.376 168.026 1.00 89.31  ? 3814 THR A CG2   1 
ATOM   15314 N N     . MET A 1 3815 ? 177.849 133.322 164.594 1.00 92.63  ? 3815 MET A N     1 
ATOM   15315 C CA    . MET A 1 3815 ? 178.812 134.064 163.788 1.00 92.63  ? 3815 MET A CA    1 
ATOM   15316 C C     . MET A 1 3815 ? 178.203 135.357 163.258 1.00 92.63  ? 3815 MET A C     1 
ATOM   15317 O O     . MET A 1 3815 ? 178.901 136.365 163.103 1.00 92.63  ? 3815 MET A O     1 
ATOM   15318 C CB    . MET A 1 3815 ? 179.325 133.177 162.656 1.00 92.63  ? 3815 MET A CB    1 
ATOM   15319 C CG    . MET A 1 3815 ? 179.727 133.907 161.396 1.00 92.63  ? 3815 MET A CG    1 
ATOM   15320 S SD    . MET A 1 3815 ? 180.583 132.830 160.234 1.00 92.63  ? 3815 MET A SD    1 
ATOM   15321 C CE    . MET A 1 3815 ? 179.887 131.241 160.668 1.00 92.63  ? 3815 MET A CE    1 
ATOM   15322 N N     . GLU A 1 3816 ? 176.897 135.352 162.986 1.00 97.55  ? 3816 GLU A N     1 
ATOM   15323 C CA    . GLU A 1 3816 ? 176.227 136.571 162.544 1.00 97.55  ? 3816 GLU A CA    1 
ATOM   15324 C C     . GLU A 1 3816 ? 176.123 137.586 163.673 1.00 97.55  ? 3816 GLU A C     1 
ATOM   15325 O O     . GLU A 1 3816 ? 176.444 138.765 163.486 1.00 97.55  ? 3816 GLU A O     1 
ATOM   15326 C CB    . GLU A 1 3816 ? 174.840 136.233 161.998 1.00 97.55  ? 3816 GLU A CB    1 
ATOM   15327 C CG    . GLU A 1 3816 ? 174.076 137.413 161.429 1.00 97.55  ? 3816 GLU A CG    1 
ATOM   15328 C CD    . GLU A 1 3816 ? 174.358 137.633 159.959 1.00 97.55  ? 3816 GLU A CD    1 
ATOM   15329 O OE1   . GLU A 1 3816 ? 174.109 136.706 159.160 1.00 97.55  ? 3816 GLU A OE1   1 
ATOM   15330 O OE2   . GLU A 1 3816 ? 174.816 138.736 159.601 1.00 97.55  ? 3816 GLU A OE2   1 
ATOM   15331 N N     . SER A 1 3817 ? 175.686 137.146 164.854 1.00 95.69  ? 3817 SER A N     1 
ATOM   15332 C CA    . SER A 1 3817 ? 175.558 138.049 165.988 1.00 95.69  ? 3817 SER A CA    1 
ATOM   15333 C C     . SER A 1 3817 ? 176.904 138.480 166.552 1.00 95.69  ? 3817 SER A C     1 
ATOM   15334 O O     . SER A 1 3817 ? 176.940 139.390 167.384 1.00 95.69  ? 3817 SER A O     1 
ATOM   15335 C CB    . SER A 1 3817 ? 174.719 137.396 167.083 1.00 95.69  ? 3817 SER A CB    1 
ATOM   15336 O OG    . SER A 1 3817 ? 174.525 138.287 168.166 1.00 95.69  ? 3817 SER A OG    1 
ATOM   15337 N N     . LEU A 1 3818 ? 178.001 137.846 166.127 1.00 94.38  ? 3818 LEU A N     1 
ATOM   15338 C CA    . LEU A 1 3818 ? 179.337 138.297 166.508 1.00 94.38  ? 3818 LEU A CA    1 
ATOM   15339 C C     . LEU A 1 3818 ? 179.570 139.783 166.249 1.00 94.38  ? 3818 LEU A C     1 
ATOM   15340 O O     . LEU A 1 3818 ? 180.492 140.360 166.833 1.00 94.38  ? 3818 LEU A O     1 
ATOM   15341 C CB    . LEU A 1 3818 ? 180.396 137.483 165.761 1.00 94.38  ? 3818 LEU A CB    1 
ATOM   15342 C CG    . LEU A 1 3818 ? 181.642 136.974 166.495 1.00 94.38  ? 3818 LEU A CG    1 
ATOM   15343 C CD1   . LEU A 1 3818 ? 181.345 136.439 167.873 1.00 94.38  ? 3818 LEU A CD1   1 
ATOM   15344 C CD2   . LEU A 1 3818 ? 182.337 135.909 165.665 1.00 94.38  ? 3818 LEU A CD2   1 
ATOM   15345 N N     . LYS A 1 3819 ? 178.766 140.418 165.394 1.00 95.62  ? 3819 LYS A N     1 
ATOM   15346 C CA    . LYS A 1 3819 ? 178.982 141.825 165.083 1.00 95.62  ? 3819 LYS A CA    1 
ATOM   15347 C C     . LYS A 1 3819 ? 178.817 142.726 166.296 1.00 95.62  ? 3819 LYS A C     1 
ATOM   15348 O O     . LYS A 1 3819 ? 179.323 143.852 166.287 1.00 95.62  ? 3819 LYS A O     1 
ATOM   15349 C CB    . LYS A 1 3819 ? 178.023 142.270 163.983 1.00 95.62  ? 3819 LYS A CB    1 
ATOM   15350 C CG    . LYS A 1 3819 ? 176.556 142.167 164.356 1.00 95.62  ? 3819 LYS A CG    1 
ATOM   15351 C CD    . LYS A 1 3819 ? 175.674 142.579 163.190 1.00 95.62  ? 3819 LYS A CD    1 
ATOM   15352 C CE    . LYS A 1 3819 ? 175.995 141.767 161.945 1.00 95.62  ? 3819 LYS A CE    1 
ATOM   15353 N NZ    . LYS A 1 3819 ? 175.131 142.139 160.789 1.00 95.62  ? 3819 LYS A NZ    1 
ATOM   15354 N N     . GLN A 1 3820 ? 178.124 142.263 167.336 1.00 97.57  ? 3820 GLN A N     1 
ATOM   15355 C CA    . GLN A 1 3820 ? 177.866 143.125 168.484 1.00 97.57  ? 3820 GLN A CA    1 
ATOM   15356 C C     . GLN A 1 3820 ? 179.135 143.392 169.281 1.00 97.57  ? 3820 GLN A C     1 
ATOM   15357 O O     . GLN A 1 3820 ? 179.309 144.487 169.827 1.00 97.57  ? 3820 GLN A O     1 
ATOM   15358 C CB    . GLN A 1 3820 ? 176.789 142.508 169.372 1.00 97.57  ? 3820 GLN A CB    1 
ATOM   15359 C CG    . GLN A 1 3820 ? 175.562 142.054 168.610 1.00 97.57  ? 3820 GLN A CG    1 
ATOM   15360 C CD    . GLN A 1 3820 ? 174.835 143.205 167.951 1.00 97.57  ? 3820 GLN A CD    1 
ATOM   15361 O OE1   . GLN A 1 3820 ? 174.847 144.330 168.448 1.00 97.57  ? 3820 GLN A OE1   1 
ATOM   15362 N NE2   . GLN A 1 3820 ? 174.208 142.931 166.814 1.00 97.57  ? 3820 GLN A NE2   1 
ATOM   15363 N N     . ILE A 1 3821 ? 180.028 142.407 169.368 1.00 95.43  ? 3821 ILE A N     1 
ATOM   15364 C CA    . ILE A 1 3821 ? 181.267 142.597 170.117 1.00 95.43  ? 3821 ILE A CA    1 
ATOM   15365 C C     . ILE A 1 3821 ? 182.158 143.631 169.438 1.00 95.43  ? 3821 ILE A C     1 
ATOM   15366 O O     . ILE A 1 3821 ? 182.656 144.561 170.082 1.00 95.43  ? 3821 ILE A O     1 
ATOM   15367 C CB    . ILE A 1 3821 ? 182.005 141.258 170.308 1.00 95.43  ? 3821 ILE A CB    1 
ATOM   15368 C CG1   . ILE A 1 3821 ? 181.076 140.169 170.855 1.00 95.43  ? 3821 ILE A CG1   1 
ATOM   15369 C CG2   . ILE A 1 3821 ? 183.210 141.444 171.200 1.00 95.43  ? 3821 ILE A CG2   1 
ATOM   15370 C CD1   . ILE A 1 3821 ? 180.342 139.367 169.815 1.00 95.43  ? 3821 ILE A CD1   1 
ATOM   15371 N N     . HIS A 1 3822 ? 182.373 143.489 168.135 1.00 97.84  ? 3822 HIS A N     1 
ATOM   15372 C CA    . HIS A 1 3822 ? 183.248 144.394 167.407 1.00 97.84  ? 3822 HIS A CA    1 
ATOM   15373 C C     . HIS A 1 3822 ? 182.653 144.675 166.040 1.00 97.84  ? 3822 HIS A C     1 
ATOM   15374 O O     . HIS A 1 3822 ? 182.046 143.794 165.427 1.00 97.84  ? 3822 HIS A O     1 
ATOM   15375 C CB    . HIS A 1 3822 ? 184.654 143.806 167.257 1.00 97.84  ? 3822 HIS A CB    1 
ATOM   15376 C CG    . HIS A 1 3822 ? 185.727 144.837 167.107 1.00 97.84  ? 3822 HIS A CG    1 
ATOM   15377 N ND1   . HIS A 1 3822 ? 186.686 144.773 166.120 1.00 97.84  ? 3822 HIS A ND1   1 
ATOM   15378 C CD2   . HIS A 1 3822 ? 185.994 145.957 167.818 1.00 97.84  ? 3822 HIS A CD2   1 
ATOM   15379 C CE1   . HIS A 1 3822 ? 187.498 145.809 166.230 1.00 97.84  ? 3822 HIS A CE1   1 
ATOM   15380 N NE2   . HIS A 1 3822 ? 187.100 146.543 167.252 1.00 97.84  ? 3822 HIS A NE2   1 
ATOM   15381 N N     . PHE A 1 3823 ? 182.834 145.906 165.561 1.00 100.36 ? 3823 PHE A N     1 
ATOM   15382 C CA    . PHE A 1 3823 ? 182.328 146.255 164.241 1.00 100.36 ? 3823 PHE A CA    1 
ATOM   15383 C C     . PHE A 1 3823 ? 183.045 145.491 163.141 1.00 100.36 ? 3823 PHE A C     1 
ATOM   15384 O O     . PHE A 1 3823 ? 182.574 145.477 162.000 1.00 100.36 ? 3823 PHE A O     1 
ATOM   15385 C CB    . PHE A 1 3823 ? 182.458 147.758 164.003 1.00 100.36 ? 3823 PHE A CB    1 
ATOM   15386 C CG    . PHE A 1 3823 ? 183.862 148.274 164.120 1.00 100.36 ? 3823 PHE A CG    1 
ATOM   15387 C CD1   . PHE A 1 3823 ? 184.705 148.287 163.021 1.00 100.36 ? 3823 PHE A CD1   1 
ATOM   15388 C CD2   . PHE A 1 3823 ? 184.338 148.756 165.326 1.00 100.36 ? 3823 PHE A CD2   1 
ATOM   15389 C CE1   . PHE A 1 3823 ? 185.996 148.764 163.125 1.00 100.36 ? 3823 PHE A CE1   1 
ATOM   15390 C CE2   . PHE A 1 3823 ? 185.629 149.233 165.435 1.00 100.36 ? 3823 PHE A CE2   1 
ATOM   15391 C CZ    . PHE A 1 3823 ? 186.458 149.238 164.332 1.00 100.36 ? 3823 PHE A CZ    1 
ATOM   15392 N N     . LEU A 1 3824 ? 184.169 144.859 163.457 1.00 96.73  ? 3824 LEU A N     1 
ATOM   15393 C CA    . LEU A 1 3824 ? 184.970 144.139 162.481 1.00 96.73  ? 3824 LEU A CA    1 
ATOM   15394 C C     . LEU A 1 3824 ? 184.447 142.735 162.211 1.00 96.73  ? 3824 LEU A C     1 
ATOM   15395 O O     . LEU A 1 3824 ? 184.932 142.071 161.293 1.00 96.73  ? 3824 LEU A O     1 
ATOM   15396 C CB    . LEU A 1 3824 ? 186.424 144.074 162.961 1.00 96.73  ? 3824 LEU A CB    1 
ATOM   15397 C CG    . LEU A 1 3824 ? 187.516 143.538 162.040 1.00 96.73  ? 3824 LEU A CG    1 
ATOM   15398 C CD1   . LEU A 1 3824 ? 187.356 144.117 160.658 1.00 96.73  ? 3824 LEU A CD1   1 
ATOM   15399 C CD2   . LEU A 1 3824 ? 188.883 143.864 162.592 1.00 96.73  ? 3824 LEU A CD2   1 
ATOM   15400 N N     . TYR A 1 3825 ? 183.447 142.279 162.959 1.00 94.52  ? 3825 TYR A N     1 
ATOM   15401 C CA    . TYR A 1 3825 ? 183.036 140.877 162.947 1.00 94.52  ? 3825 TYR A CA    1 
ATOM   15402 C C     . TYR A 1 3825 ? 181.824 140.633 162.060 1.00 94.52  ? 3825 TYR A C     1 
ATOM   15403 O O     . TYR A 1 3825 ? 180.936 139.856 162.415 1.00 94.52  ? 3825 TYR A O     1 
ATOM   15404 C CB    . TYR A 1 3825 ? 182.764 140.398 164.368 1.00 94.52  ? 3825 TYR A CB    1 
ATOM   15405 C CG    . TYR A 1 3825 ? 183.985 140.393 165.261 1.00 94.52  ? 3825 TYR A CG    1 
ATOM   15406 C CD1   . TYR A 1 3825 ? 185.255 140.578 164.737 1.00 94.52  ? 3825 TYR A CD1   1 
ATOM   15407 C CD2   . TYR A 1 3825 ? 183.867 140.194 166.627 1.00 94.52  ? 3825 TYR A CD2   1 
ATOM   15408 C CE1   . TYR A 1 3825 ? 186.366 140.574 165.548 1.00 94.52  ? 3825 TYR A CE1   1 
ATOM   15409 C CE2   . TYR A 1 3825 ? 184.973 140.185 167.443 1.00 94.52  ? 3825 TYR A CE2   1 
ATOM   15410 C CZ    . TYR A 1 3825 ? 186.220 140.374 166.899 1.00 94.52  ? 3825 TYR A CZ    1 
ATOM   15411 O OH    . TYR A 1 3825 ? 187.327 140.365 167.710 1.00 94.52  ? 3825 TYR A OH    1 
ATOM   15412 N N     . GLN A 1 3826 ? 181.746 141.297 160.911 1.00 97.09  ? 3826 GLN A N     1 
ATOM   15413 C CA    . GLN A 1 3826 ? 180.644 141.077 159.985 1.00 97.09  ? 3826 GLN A CA    1 
ATOM   15414 C C     . GLN A 1 3826 ? 180.906 139.846 159.126 1.00 97.09  ? 3826 GLN A C     1 
ATOM   15415 O O     . GLN A 1 3826 ? 181.982 139.706 158.538 1.00 97.09  ? 3826 GLN A O     1 
ATOM   15416 C CB    . GLN A 1 3826 ? 180.444 142.304 159.100 1.00 97.09  ? 3826 GLN A CB    1 
ATOM   15417 C CG    . GLN A 1 3826 ? 180.713 143.620 159.799 1.00 97.09  ? 3826 GLN A CG    1 
ATOM   15418 C CD    . GLN A 1 3826 ? 179.523 144.112 160.597 1.00 97.09  ? 3826 GLN A CD    1 
ATOM   15419 O OE1   . GLN A 1 3826 ? 178.710 143.322 161.074 1.00 97.09  ? 3826 GLN A OE1   1 
ATOM   15420 N NE2   . GLN A 1 3826 ? 179.416 145.426 160.747 1.00 97.09  ? 3826 GLN A NE2   1 
ATOM   15421 N N     . TYR A 1 3827 ? 179.919 138.955 159.053 1.00 91.21  ? 3827 TYR A N     1 
ATOM   15422 C CA    . TYR A 1 3827 ? 179.996 137.764 158.220 1.00 91.21  ? 3827 TYR A CA    1 
ATOM   15423 C C     . TYR A 1 3827 ? 178.682 137.572 157.480 1.00 91.21  ? 3827 TYR A C     1 
ATOM   15424 O O     . TYR A 1 3827 ? 177.632 138.055 157.909 1.00 91.21  ? 3827 TYR A O     1 
ATOM   15425 C CB    . TYR A 1 3827 ? 180.307 136.512 159.039 1.00 91.21  ? 3827 TYR A CB    1 
ATOM   15426 C CG    . TYR A 1 3827 ? 181.568 136.609 159.859 1.00 91.21  ? 3827 TYR A CG    1 
ATOM   15427 C CD1   . TYR A 1 3827 ? 181.560 137.199 161.112 1.00 91.21  ? 3827 TYR A CD1   1 
ATOM   15428 C CD2   . TYR A 1 3827 ? 182.768 136.116 159.377 1.00 91.21  ? 3827 TYR A CD2   1 
ATOM   15429 C CE1   . TYR A 1 3827 ? 182.709 137.291 161.863 1.00 91.21  ? 3827 TYR A CE1   1 
ATOM   15430 C CE2   . TYR A 1 3827 ? 183.922 136.203 160.122 1.00 91.21  ? 3827 TYR A CE2   1 
ATOM   15431 C CZ    . TYR A 1 3827 ? 183.886 136.791 161.363 1.00 91.21  ? 3827 TYR A CZ    1 
ATOM   15432 O OH    . TYR A 1 3827 ? 185.035 136.880 162.107 1.00 91.21  ? 3827 TYR A OH    1 
ATOM   15433 N N     . SER A 1 3828 ? 178.750 136.860 156.362 1.00 93.40  ? 3828 SER A N     1 
ATOM   15434 C CA    . SER A 1 3828 ? 177.595 136.632 155.508 1.00 93.40  ? 3828 SER A CA    1 
ATOM   15435 C C     . SER A 1 3828 ? 177.196 135.161 155.513 1.00 93.40  ? 3828 SER A C     1 
ATOM   15436 O O     . SER A 1 3828 ? 177.916 134.291 156.005 1.00 93.40  ? 3828 SER A O     1 
ATOM   15437 C CB    . SER A 1 3828 ? 177.887 137.090 154.078 1.00 93.40  ? 3828 SER A CB    1 
ATOM   15438 O OG    . SER A 1 3828 ? 178.988 136.381 153.537 1.00 93.40  ? 3828 SER A OG    1 
ATOM   15439 N N     . LEU A 1 3829 ? 176.019 134.892 154.945 1.00 94.62  ? 3829 LEU A N     1 
ATOM   15440 C CA    . LEU A 1 3829 ? 175.580 133.512 154.776 1.00 94.62  ? 3829 LEU A CA    1 
ATOM   15441 C C     . LEU A 1 3829 ? 176.436 132.783 153.752 1.00 94.62  ? 3829 LEU A C     1 
ATOM   15442 O O     . LEU A 1 3829 ? 176.630 131.567 153.861 1.00 94.62  ? 3829 LEU A O     1 
ATOM   15443 C CB    . LEU A 1 3829 ? 174.102 133.479 154.380 1.00 94.62  ? 3829 LEU A CB    1 
ATOM   15444 C CG    . LEU A 1 3829 ? 173.683 133.631 152.912 1.00 94.62  ? 3829 LEU A CG    1 
ATOM   15445 C CD1   . LEU A 1 3829 ? 173.658 132.298 152.167 1.00 94.62  ? 3829 LEU A CD1   1 
ATOM   15446 C CD2   . LEU A 1 3829 ? 172.336 134.332 152.805 1.00 94.62  ? 3829 LEU A CD2   1 
ATOM   15447 N N     . GLN A 1 3830 ? 176.946 133.503 152.751 1.00 96.78  ? 3830 GLN A N     1 
ATOM   15448 C CA    . GLN A 1 3830 ? 177.835 132.884 151.777 1.00 96.78  ? 3830 GLN A CA    1 
ATOM   15449 C C     . GLN A 1 3830 ? 179.079 132.336 152.453 1.00 96.78  ? 3830 GLN A C     1 
ATOM   15450 O O     . GLN A 1 3830 ? 179.555 131.247 152.112 1.00 96.78  ? 3830 GLN A O     1 
ATOM   15451 C CB    . GLN A 1 3830 ? 178.215 133.893 150.696 1.00 96.78  ? 3830 GLN A CB    1 
ATOM   15452 C CG    . GLN A 1 3830 ? 178.851 133.268 149.473 1.00 96.78  ? 3830 GLN A CG    1 
ATOM   15453 C CD    . GLN A 1 3830 ? 178.131 132.017 149.022 1.00 96.78  ? 3830 GLN A CD    1 
ATOM   15454 O OE1   . GLN A 1 3830 ? 176.930 132.038 148.760 1.00 96.78  ? 3830 GLN A OE1   1 
ATOM   15455 N NE2   . GLN A 1 3830 ? 178.866 130.917 148.927 1.00 96.78  ? 3830 GLN A NE2   1 
ATOM   15456 N N     . PHE A 1 3831 ? 179.614 133.072 153.425 1.00 96.11  ? 3831 PHE A N     1 
ATOM   15457 C CA    . PHE A 1 3831 ? 180.778 132.598 154.160 1.00 96.11  ? 3831 PHE A CA    1 
ATOM   15458 C C     . PHE A 1 3831 ? 180.482 131.271 154.848 1.00 96.11  ? 3831 PHE A C     1 
ATOM   15459 O O     . PHE A 1 3831 ? 181.205 130.285 154.655 1.00 96.11  ? 3831 PHE A O     1 
ATOM   15460 C CB    . PHE A 1 3831 ? 181.206 133.659 155.171 1.00 96.11  ? 3831 PHE A CB    1 
ATOM   15461 C CG    . PHE A 1 3831 ? 182.430 133.299 155.954 1.00 96.11  ? 3831 PHE A CG    1 
ATOM   15462 C CD1   . PHE A 1 3831 ? 183.595 132.934 155.312 1.00 96.11  ? 3831 PHE A CD1   1 
ATOM   15463 C CD2   . PHE A 1 3831 ? 182.417 133.343 157.335 1.00 96.11  ? 3831 PHE A CD2   1 
ATOM   15464 C CE1   . PHE A 1 3831 ? 184.719 132.608 156.033 1.00 96.11  ? 3831 PHE A CE1   1 
ATOM   15465 C CE2   . PHE A 1 3831 ? 183.538 133.020 158.061 1.00 96.11  ? 3831 PHE A CE2   1 
ATOM   15466 C CZ    . PHE A 1 3831 ? 184.692 132.654 157.410 1.00 96.11  ? 3831 PHE A CZ    1 
ATOM   15467 N N     . PHE A 1 3832 ? 179.397 131.219 155.625 1.00 90.09  ? 3832 PHE A N     1 
ATOM   15468 C CA    . PHE A 1 3832 ? 179.073 129.996 156.350 1.00 90.09  ? 3832 PHE A CA    1 
ATOM   15469 C C     . PHE A 1 3832 ? 178.817 128.843 155.395 1.00 90.09  ? 3832 PHE A C     1 
ATOM   15470 O O     . PHE A 1 3832 ? 179.213 127.703 155.668 1.00 90.09  ? 3832 PHE A O     1 
ATOM   15471 C CB    . PHE A 1 3832 ? 177.870 130.205 157.261 1.00 90.09  ? 3832 PHE A CB    1 
ATOM   15472 C CG    . PHE A 1 3832 ? 177.430 128.954 157.951 1.00 90.09  ? 3832 PHE A CG    1 
ATOM   15473 C CD1   . PHE A 1 3832 ? 178.138 128.463 159.028 1.00 90.09  ? 3832 PHE A CD1   1 
ATOM   15474 C CD2   . PHE A 1 3832 ? 176.326 128.255 157.509 1.00 90.09  ? 3832 PHE A CD2   1 
ATOM   15475 C CE1   . PHE A 1 3832 ? 177.746 127.306 159.662 1.00 90.09  ? 3832 PHE A CE1   1 
ATOM   15476 C CE2   . PHE A 1 3832 ? 175.929 127.097 158.140 1.00 90.09  ? 3832 PHE A CE2   1 
ATOM   15477 C CZ    . PHE A 1 3832 ? 176.640 126.622 159.217 1.00 90.09  ? 3832 PHE A CZ    1 
ATOM   15478 N N     . LEU A 1 3833 ? 178.151 129.118 154.273 1.00 97.04  ? 3833 LEU A N     1 
ATOM   15479 C CA    . LEU A 1 3833 ? 177.995 128.093 153.250 1.00 97.04  ? 3833 LEU A CA    1 
ATOM   15480 C C     . LEU A 1 3833 ? 179.349 127.632 152.736 1.00 97.04  ? 3833 LEU A C     1 
ATOM   15481 O O     . LEU A 1 3833 ? 179.518 126.463 152.373 1.00 97.04  ? 3833 LEU A O     1 
ATOM   15482 C CB    . LEU A 1 3833 ? 177.132 128.616 152.104 1.00 97.04  ? 3833 LEU A CB    1 
ATOM   15483 C CG    . LEU A 1 3833 ? 175.662 128.195 152.126 1.00 97.04  ? 3833 LEU A CG    1 
ATOM   15484 C CD1   . LEU A 1 3833 ? 175.536 126.741 151.717 1.00 97.04  ? 3833 LEU A CD1   1 
ATOM   15485 C CD2   . LEU A 1 3833 ? 175.044 128.416 153.495 1.00 97.04  ? 3833 LEU A CD2   1 
ATOM   15486 N N     . ASP A 1 3834 ? 180.332 128.532 152.706 1.00 102.54 ? 3834 ASP A N     1 
ATOM   15487 C CA    . ASP A 1 3834 ? 181.659 128.136 152.252 1.00 102.54 ? 3834 ASP A CA    1 
ATOM   15488 C C     . ASP A 1 3834 ? 182.315 127.179 153.239 1.00 102.54 ? 3834 ASP A C     1 
ATOM   15489 O O     . ASP A 1 3834 ? 182.902 126.172 152.828 1.00 102.54 ? 3834 ASP A O     1 
ATOM   15490 C CB    . ASP A 1 3834 ? 182.537 129.365 152.020 1.00 102.54 ? 3834 ASP A CB    1 
ATOM   15491 C CG    . ASP A 1 3834 ? 183.832 129.030 151.299 1.00 102.54 ? 3834 ASP A CG    1 
ATOM   15492 O OD1   . ASP A 1 3834 ? 184.661 128.282 151.860 1.00 102.54 ? 3834 ASP A OD1   1 
ATOM   15493 O OD2   . ASP A 1 3834 ? 184.018 129.514 150.163 1.00 102.54 ? 3834 ASP A OD2   1 
ATOM   15494 N N     . ILE A 1 3835 ? 182.238 127.470 154.543 1.00 95.61  ? 3835 ILE A N     1 
ATOM   15495 C CA    . ILE A 1 3835 ? 182.781 126.496 155.498 1.00 95.61  ? 3835 ILE A CA    1 
ATOM   15496 C C     . ILE A 1 3835 ? 182.027 125.176 155.422 1.00 95.61  ? 3835 ILE A C     1 
ATOM   15497 O O     . ILE A 1 3835 ? 182.631 124.101 155.510 1.00 95.61  ? 3835 ILE A O     1 
ATOM   15498 C CB    . ILE A 1 3835 ? 182.858 126.999 156.958 1.00 95.61  ? 3835 ILE A CB    1 
ATOM   15499 C CG1   . ILE A 1 3835 ? 183.306 128.452 157.131 1.00 95.61  ? 3835 ILE A CG1   1 
ATOM   15500 C CG2   . ILE A 1 3835 ? 183.699 126.072 157.792 1.00 95.61  ? 3835 ILE A CG2   1 
ATOM   15501 C CD1   . ILE A 1 3835 ? 182.261 129.437 157.168 1.00 95.61  ? 3835 ILE A CD1   1 
ATOM   15502 N N     . TYR A 1 3836 ? 180.705 125.225 155.268 1.00 101.82 ? 3836 TYR A N     1 
ATOM   15503 C CA    . TYR A 1 3836 ? 179.955 123.977 155.184 1.00 101.82 ? 3836 TYR A CA    1 
ATOM   15504 C C     . TYR A 1 3836 ? 180.357 123.155 153.966 1.00 101.82 ? 3836 TYR A C     1 
ATOM   15505 O O     . TYR A 1 3836 ? 180.541 121.937 154.065 1.00 101.82 ? 3836 TYR A O     1 
ATOM   15506 C CB    . TYR A 1 3836 ? 178.459 124.257 155.175 1.00 101.82 ? 3836 TYR A CB    1 
ATOM   15507 C CG    . TYR A 1 3836 ? 177.658 123.036 155.525 1.00 101.82 ? 3836 TYR A CG    1 
ATOM   15508 C CD1   . TYR A 1 3836 ? 177.611 122.561 156.823 1.00 101.82 ? 3836 TYR A CD1   1 
ATOM   15509 C CD2   . TYR A 1 3836 ? 176.947 122.354 154.553 1.00 101.82 ? 3836 TYR A CD2   1 
ATOM   15510 C CE1   . TYR A 1 3836 ? 176.885 121.436 157.141 1.00 101.82 ? 3836 TYR A CE1   1 
ATOM   15511 C CE2   . TYR A 1 3836 ? 176.211 121.236 154.865 1.00 101.82 ? 3836 TYR A CE2   1 
ATOM   15512 C CZ    . TYR A 1 3836 ? 176.184 120.783 156.161 1.00 101.82 ? 3836 TYR A CZ    1 
ATOM   15513 O OH    . TYR A 1 3836 ? 175.455 119.664 156.477 1.00 101.82 ? 3836 TYR A OH    1 
ATOM   15514 N N     . HIS A 1 3837 ? 180.505 123.796 152.807 1.00 103.29 ? 3837 HIS A N     1 
ATOM   15515 C CA    . HIS A 1 3837 ? 180.922 123.057 151.621 1.00 103.29 ? 3837 HIS A CA    1 
ATOM   15516 C C     . HIS A 1 3837 ? 182.343 122.532 151.766 1.00 103.29 ? 3837 HIS A C     1 
ATOM   15517 O O     . HIS A 1 3837 ? 182.624 121.388 151.390 1.00 103.29 ? 3837 HIS A O     1 
ATOM   15518 C CB    . HIS A 1 3837 ? 180.793 123.932 150.378 1.00 103.29 ? 3837 HIS A CB    1 
ATOM   15519 C CG    . HIS A 1 3837 ? 179.390 124.056 149.876 1.00 103.29 ? 3837 HIS A CG    1 
ATOM   15520 N ND1   . HIS A 1 3837 ? 178.966 125.111 149.098 1.00 103.29 ? 3837 HIS A ND1   1 
ATOM   15521 C CD2   . HIS A 1 3837 ? 178.312 123.253 150.039 1.00 103.29 ? 3837 HIS A CD2   1 
ATOM   15522 C CE1   . HIS A 1 3837 ? 177.688 124.954 148.804 1.00 103.29 ? 3837 HIS A CE1   1 
ATOM   15523 N NE2   . HIS A 1 3837 ? 177.267 123.834 149.364 1.00 103.29 ? 3837 HIS A NE2   1 
ATOM   15524 N N     . ASN A 1 3838 ? 183.251 123.342 152.314 1.00 103.47 ? 3838 ASN A N     1 
ATOM   15525 C CA    . ASN A 1 3838 ? 184.631 122.898 152.466 1.00 103.47 ? 3838 ASN A CA    1 
ATOM   15526 C C     . ASN A 1 3838 ? 184.727 121.698 153.395 1.00 103.47 ? 3838 ASN A C     1 
ATOM   15527 O O     . ASN A 1 3838 ? 185.458 120.743 153.110 1.00 103.47 ? 3838 ASN A O     1 
ATOM   15528 C CB    . ASN A 1 3838 ? 185.503 124.034 152.991 1.00 103.47 ? 3838 ASN A CB    1 
ATOM   15529 C CG    . ASN A 1 3838 ? 186.828 123.540 153.527 1.00 103.47 ? 3838 ASN A CG    1 
ATOM   15530 O OD1   . ASN A 1 3838 ? 186.980 123.315 154.725 1.00 103.47 ? 3838 ASN A OD1   1 
ATOM   15531 N ND2   . ASN A 1 3838 ? 187.793 123.359 152.638 1.00 103.47 ? 3838 ASN A ND2   1 
ATOM   15532 N N     . VAL A 1 3839 ? 184.003 121.729 154.515 1.00 101.39 ? 3839 VAL A N     1 
ATOM   15533 C CA    . VAL A 1 3839 ? 184.054 120.600 155.434 1.00 101.39 ? 3839 VAL A CA    1 
ATOM   15534 C C     . VAL A 1 3839 ? 183.352 119.388 154.835 1.00 101.39 ? 3839 VAL A C     1 
ATOM   15535 O O     . VAL A 1 3839 ? 183.782 118.250 155.052 1.00 101.39 ? 3839 VAL A O     1 
ATOM   15536 C CB    . VAL A 1 3839 ? 183.470 120.989 156.807 1.00 101.39 ? 3839 VAL A CB    1 
ATOM   15537 C CG1   . VAL A 1 3839 ? 181.979 121.229 156.727 1.00 101.39 ? 3839 VAL A CG1   1 
ATOM   15538 C CG2   . VAL A 1 3839 ? 183.774 119.923 157.831 1.00 101.39 ? 3839 VAL A CG2   1 
ATOM   15539 N N     . LEU A 1 3840 ? 182.291 119.601 154.050 1.00 100.16 ? 3840 LEU A N     1 
ATOM   15540 C CA    . LEU A 1 3840 ? 181.527 118.474 153.526 1.00 100.16 ? 3840 LEU A CA    1 
ATOM   15541 C C     . LEU A 1 3840 ? 182.299 117.703 152.463 1.00 100.16 ? 3840 LEU A C     1 
ATOM   15542 O O     . LEU A 1 3840 ? 182.351 116.470 152.505 1.00 100.16 ? 3840 LEU A O     1 
ATOM   15543 C CB    . LEU A 1 3840 ? 180.194 118.957 152.963 1.00 100.16 ? 3840 LEU A CB    1 
ATOM   15544 C CG    . LEU A 1 3840 ? 178.976 118.550 153.786 1.00 100.16 ? 3840 LEU A CG    1 
ATOM   15545 C CD1   . LEU A 1 3840 ? 177.707 118.739 152.983 1.00 100.16 ? 3840 LEU A CD1   1 
ATOM   15546 C CD2   . LEU A 1 3840 ? 179.111 117.113 154.240 1.00 100.16 ? 3840 LEU A CD2   1 
ATOM   15547 N N     . TYR A 1 3841 ? 182.902 118.401 151.502 1.00 106.46 ? 3841 TYR A N     1 
ATOM   15548 C CA    . TYR A 1 3841 ? 183.534 117.742 150.365 1.00 106.46 ? 3841 TYR A CA    1 
ATOM   15549 C C     . TYR A 1 3841 ? 185.053 117.710 150.476 1.00 106.46 ? 3841 TYR A C     1 
ATOM   15550 O O     . TYR A 1 3841 ? 185.648 116.632 150.434 1.00 106.46 ? 3841 TYR A O     1 
ATOM   15551 C CB    . TYR A 1 3841 ? 183.109 118.418 149.054 1.00 106.46 ? 3841 TYR A CB    1 
ATOM   15552 C CG    . TYR A 1 3841 ? 181.613 118.495 148.870 1.00 106.46 ? 3841 TYR A CG    1 
ATOM   15553 C CD1   . TYR A 1 3841 ? 180.817 117.371 149.037 1.00 106.46 ? 3841 TYR A CD1   1 
ATOM   15554 C CD2   . TYR A 1 3841 ? 180.996 119.688 148.527 1.00 106.46 ? 3841 TYR A CD2   1 
ATOM   15555 C CE1   . TYR A 1 3841 ? 179.449 117.434 148.871 1.00 106.46 ? 3841 TYR A CE1   1 
ATOM   15556 C CE2   . TYR A 1 3841 ? 179.627 119.761 148.361 1.00 106.46 ? 3841 TYR A CE2   1 
ATOM   15557 C CZ    . TYR A 1 3841 ? 178.860 118.630 148.535 1.00 106.46 ? 3841 TYR A CZ    1 
ATOM   15558 O OH    . TYR A 1 3841 ? 177.497 118.697 148.369 1.00 106.46 ? 3841 TYR A OH    1 
ATOM   15559 N N     . GLU A 1 3842 ? 185.703 118.861 150.621 1.00 111.21 ? 3842 GLU A N     1 
ATOM   15560 C CA    . GLU A 1 3842 ? 187.164 118.909 150.668 1.00 111.21 ? 3842 GLU A CA    1 
ATOM   15561 C C     . GLU A 1 3842 ? 187.666 118.633 152.086 1.00 111.21 ? 3842 GLU A C     1 
ATOM   15562 O O     . GLU A 1 3842 ? 188.300 119.464 152.732 1.00 111.21 ? 3842 GLU A O     1 
ATOM   15563 C CB    . GLU A 1 3842 ? 187.665 120.254 150.156 1.00 111.21 ? 3842 GLU A CB    1 
ATOM   15564 C CG    . GLU A 1 3842 ? 187.458 120.476 148.667 1.00 111.21 ? 3842 GLU A CG    1 
ATOM   15565 C CD    . GLU A 1 3842 ? 186.105 121.079 148.350 1.00 111.21 ? 3842 GLU A CD    1 
ATOM   15566 O OE1   . GLU A 1 3842 ? 185.994 121.797 147.335 1.00 111.21 ? 3842 GLU A OE1   1 
ATOM   15567 O OE2   . GLU A 1 3842 ? 185.151 120.832 149.114 1.00 111.21 ? 3842 GLU A OE2   1 
ATOM   15568 N N     . ASN A 1 3843 ? 187.371 117.426 152.561 1.00 108.77 ? 3843 ASN A N     1 
ATOM   15569 C CA    . ASN A 1 3843 ? 187.715 117.029 153.921 1.00 108.77 ? 3843 ASN A CA    1 
ATOM   15570 C C     . ASN A 1 3843 ? 188.761 115.925 153.905 1.00 108.77 ? 3843 ASN A C     1 
ATOM   15571 O O     . ASN A 1 3843 ? 188.453 114.796 153.491 1.00 108.77 ? 3843 ASN A O     1 
ATOM   15572 C CB    . ASN A 1 3843 ? 186.467 116.566 154.669 1.00 108.77 ? 3843 ASN A CB    1 
ATOM   15573 C CG    . ASN A 1 3843 ? 186.482 116.973 156.122 1.00 108.77 ? 3843 ASN A CG    1 
ATOM   15574 O OD1   . ASN A 1 3843 ? 187.524 116.952 156.773 1.00 108.77 ? 3843 ASN A OD1   1 
ATOM   15575 N ND2   . ASN A 1 3843 ? 185.323 117.349 156.639 1.00 108.77 ? 3843 ASN A ND2   1 
ATOM   15576 N N     . PRO A 1 3844 ? 189.996 116.191 154.334 1.00 105.32 ? 3844 PRO A N     1 
ATOM   15577 C CA    . PRO A 1 3844 ? 190.995 115.114 154.394 1.00 105.32 ? 3844 PRO A CA    1 
ATOM   15578 C C     . PRO A 1 3844 ? 190.613 113.985 155.331 1.00 105.32 ? 3844 PRO A C     1 
ATOM   15579 O O     . PRO A 1 3844 ? 190.947 112.826 155.055 1.00 105.32 ? 3844 PRO A O     1 
ATOM   15580 C CB    . PRO A 1 3844 ? 192.258 115.839 154.875 1.00 105.32 ? 3844 PRO A CB    1 
ATOM   15581 C CG    . PRO A 1 3844 ? 191.750 117.034 155.597 1.00 105.32 ? 3844 PRO A CG    1 
ATOM   15582 C CD    . PRO A 1 3844 ? 190.518 117.460 154.861 1.00 105.32 ? 3844 PRO A CD    1 
ATOM   15583 N N     . ASN A 1 3845 ? 189.922 114.284 156.432 1.00 109.61 ? 3845 ASN A N     1 
ATOM   15584 C CA    . ASN A 1 3845 ? 189.561 113.259 157.405 1.00 109.61 ? 3845 ASN A CA    1 
ATOM   15585 C C     . ASN A 1 3845 ? 188.600 112.222 156.849 1.00 109.61 ? 3845 ASN A C     1 
ATOM   15586 O O     . ASN A 1 3845 ? 188.554 111.105 157.373 1.00 109.61 ? 3845 ASN A O     1 
ATOM   15587 C CB    . ASN A 1 3845 ? 188.932 113.898 158.643 1.00 109.61 ? 3845 ASN A CB    1 
ATOM   15588 C CG    . ASN A 1 3845 ? 189.923 114.692 159.457 1.00 109.61 ? 3845 ASN A CG    1 
ATOM   15589 O OD1   . ASN A 1 3845 ? 190.890 114.146 159.983 1.00 109.61 ? 3845 ASN A OD1   1 
ATOM   15590 N ND2   . ASN A 1 3845 ? 189.686 115.992 159.570 1.00 109.61 ? 3845 ASN A ND2   1 
ATOM   15591 N N     . LEU A 1 3846 ? 187.841 112.553 155.807 1.00 116.91 ? 3846 LEU A N     1 
ATOM   15592 C CA    . LEU A 1 3846 ? 186.804 111.673 155.289 1.00 116.91 ? 3846 LEU A CA    1 
ATOM   15593 C C     . LEU A 1 3846 ? 187.251 110.927 154.037 1.00 116.91 ? 3846 LEU A C     1 
ATOM   15594 O O     . LEU A 1 3846 ? 186.410 110.464 153.261 1.00 116.91 ? 3846 LEU A O     1 
ATOM   15595 C CB    . LEU A 1 3846 ? 185.532 112.473 155.010 1.00 116.91 ? 3846 LEU A CB    1 
ATOM   15596 C CG    . LEU A 1 3846 ? 184.472 112.466 156.116 1.00 116.91 ? 3846 LEU A CG    1 
ATOM   15597 C CD1   . LEU A 1 3846 ? 183.097 112.758 155.544 1.00 116.91 ? 3846 LEU A CD1   1 
ATOM   15598 C CD2   . LEU A 1 3846 ? 184.466 111.143 156.862 1.00 116.91 ? 3846 LEU A CD2   1 
ATOM   15599 N N     . LYS A 1 3847 ? 188.561 110.808 153.821 1.00 119.63 ? 3847 LYS A N     1 
ATOM   15600 C CA    . LYS A 1 3847 ? 189.055 110.101 152.644 1.00 119.63 ? 3847 LYS A CA    1 
ATOM   15601 C C     . LYS A 1 3847 ? 188.877 108.594 152.785 1.00 119.63 ? 3847 LYS A C     1 
ATOM   15602 O O     . LYS A 1 3847 ? 188.454 107.918 151.841 1.00 119.63 ? 3847 LYS A O     1 
ATOM   15603 C CB    . LYS A 1 3847 ? 190.523 110.450 152.402 1.00 119.63 ? 3847 LYS A CB    1 
ATOM   15604 C CG    . LYS A 1 3847 ? 190.874 110.660 150.942 1.00 119.63 ? 3847 LYS A CG    1 
ATOM   15605 C CD    . LYS A 1 3847 ? 192.372 110.788 150.757 1.00 119.63 ? 3847 LYS A CD    1 
ATOM   15606 C CE    . LYS A 1 3847 ? 193.015 109.424 150.613 1.00 119.63 ? 3847 LYS A CE    1 
ATOM   15607 N NZ    . LYS A 1 3847 ? 192.183 108.516 149.779 1.00 119.63 ? 3847 LYS A NZ    1 
ATOM   15608 N N     . GLY A 1 3848 ? 189.197 108.048 153.956 1.00 119.01 ? 3848 GLY A N     1 
ATOM   15609 C CA    . GLY A 1 3848 ? 189.152 106.612 154.143 1.00 119.01 ? 3848 GLY A CA    1 
ATOM   15610 C C     . GLY A 1 3848 ? 187.997 106.122 154.991 1.00 119.01 ? 3848 GLY A C     1 
ATOM   15611 O O     . GLY A 1 3848 ? 187.759 104.915 155.086 1.00 119.01 ? 3848 GLY A O     1 
ATOM   15612 N N     . VAL A 1 3849 ? 187.273 107.042 155.609 1.00 119.79 ? 3849 VAL A N     1 
ATOM   15613 C CA    . VAL A 1 3849 ? 186.172 106.673 156.491 1.00 119.79 ? 3849 VAL A CA    1 
ATOM   15614 C C     . VAL A 1 3849 ? 184.940 106.355 155.657 1.00 119.79 ? 3849 VAL A C     1 
ATOM   15615 O O     . VAL A 1 3849 ? 184.613 107.069 154.702 1.00 119.79 ? 3849 VAL A O     1 
ATOM   15616 C CB    . VAL A 1 3849 ? 185.893 107.797 157.502 1.00 119.79 ? 3849 VAL A CB    1 
ATOM   15617 C CG1   . VAL A 1 3849 ? 184.962 107.304 158.592 1.00 119.79 ? 3849 VAL A CG1   1 
ATOM   15618 C CG2   . VAL A 1 3849 ? 187.192 108.293 158.101 1.00 119.79 ? 3849 VAL A CG2   1 
ATOM   15619 N N     . THR A 1 3850 ? 184.256 105.269 156.013 1.00 123.49 ? 3850 THR A N     1 
ATOM   15620 C CA    . THR A 1 3850 ? 183.061 104.833 155.304 1.00 123.49 ? 3850 THR A CA    1 
ATOM   15621 C C     . THR A 1 3850 ? 181.845 104.644 156.196 1.00 123.49 ? 3850 THR A C     1 
ATOM   15622 O O     . THR A 1 3850 ? 180.722 104.826 155.721 1.00 123.49 ? 3850 THR A O     1 
ATOM   15623 C CB    . THR A 1 3850 ? 183.328 103.514 154.563 1.00 123.49 ? 3850 THR A CB    1 
ATOM   15624 O OG1   . THR A 1 3850 ? 183.767 102.520 155.497 1.00 123.49 ? 3850 THR A OG1   1 
ATOM   15625 C CG2   . THR A 1 3850 ? 184.392 103.709 153.491 1.00 123.49 ? 3850 THR A CG2   1 
ATOM   15626 N N     . ASP A 1 3851 ? 182.030 104.278 157.462 1.00 121.36 ? 3851 ASP A N     1 
ATOM   15627 C CA    . ASP A 1 3851 ? 180.897 104.052 158.349 1.00 121.36 ? 3851 ASP A CA    1 
ATOM   15628 C C     . ASP A 1 3851 ? 180.099 105.337 158.532 1.00 121.36 ? 3851 ASP A C     1 
ATOM   15629 O O     . ASP A 1 3851 ? 180.666 106.400 158.802 1.00 121.36 ? 3851 ASP A O     1 
ATOM   15630 C CB    . ASP A 1 3851 ? 181.391 103.537 159.698 1.00 121.36 ? 3851 ASP A CB    1 
ATOM   15631 C CG    . ASP A 1 3851 ? 182.504 102.518 159.558 1.00 121.36 ? 3851 ASP A CG    1 
ATOM   15632 O OD1   . ASP A 1 3851 ? 182.198 101.324 159.368 1.00 121.36 ? 3851 ASP A OD1   1 
ATOM   15633 O OD2   . ASP A 1 3851 ? 183.685 102.914 159.635 1.00 121.36 ? 3851 ASP A OD2   1 
ATOM   15634 N N     . HIS A 1 3852 ? 178.774 105.230 158.400 1.00 126.97 ? 3852 HIS A N     1 
ATOM   15635 C CA    . HIS A 1 3852 ? 177.926 106.420 158.390 1.00 126.97 ? 3852 HIS A CA    1 
ATOM   15636 C C     . HIS A 1 3852 ? 178.054 107.206 159.686 1.00 126.97 ? 3852 HIS A C     1 
ATOM   15637 O O     . HIS A 1 3852 ? 178.236 108.428 159.666 1.00 126.97 ? 3852 HIS A O     1 
ATOM   15638 C CB    . HIS A 1 3852 ? 176.471 106.025 158.149 1.00 126.97 ? 3852 HIS A CB    1 
ATOM   15639 C CG    . HIS A 1 3852 ? 176.227 105.410 156.808 1.00 126.97 ? 3852 HIS A CG    1 
ATOM   15640 N ND1   . HIS A 1 3852 ? 175.110 104.654 156.529 1.00 126.97 ? 3852 HIS A ND1   1 
ATOM   15641 C CD2   . HIS A 1 3852 ? 176.953 105.445 155.666 1.00 126.97 ? 3852 HIS A CD2   1 
ATOM   15642 C CE1   . HIS A 1 3852 ? 175.159 104.247 155.274 1.00 126.97 ? 3852 HIS A CE1   1 
ATOM   15643 N NE2   . HIS A 1 3852 ? 176.268 104.713 154.728 1.00 126.97 ? 3852 HIS A NE2   1 
ATOM   15644 N N     . THR A 1 3853 ? 177.963 106.521 160.827 1.00 122.38 ? 3853 THR A N     1 
ATOM   15645 C CA    . THR A 1 3853 ? 178.086 107.215 162.105 1.00 122.38 ? 3853 THR A CA    1 
ATOM   15646 C C     . THR A 1 3853 ? 179.484 107.797 162.281 1.00 122.38 ? 3853 THR A C     1 
ATOM   15647 O O     . THR A 1 3853 ? 179.643 108.901 162.819 1.00 122.38 ? 3853 THR A O     1 
ATOM   15648 C CB    . THR A 1 3853 ? 177.737 106.270 163.256 1.00 122.38 ? 3853 THR A CB    1 
ATOM   15649 O OG1   . THR A 1 3853 ? 178.088 106.881 164.503 1.00 122.38 ? 3853 THR A OG1   1 
ATOM   15650 C CG2   . THR A 1 3853 ? 178.468 104.942 163.112 1.00 122.38 ? 3853 THR A CG2   1 
ATOM   15651 N N     . GLN A 1 3854 ? 180.510 107.071 161.829 1.00 120.66 ? 3854 GLN A N     1 
ATOM   15652 C CA    . GLN A 1 3854 ? 181.869 107.594 161.901 1.00 120.66 ? 3854 GLN A CA    1 
ATOM   15653 C C     . GLN A 1 3854 ? 182.024 108.839 161.042 1.00 120.66 ? 3854 GLN A C     1 
ATOM   15654 O O     . GLN A 1 3854 ? 182.625 109.829 161.476 1.00 120.66 ? 3854 GLN A O     1 
ATOM   15655 C CB    . GLN A 1 3854 ? 182.871 106.523 161.474 1.00 120.66 ? 3854 GLN A CB    1 
ATOM   15656 C CG    . GLN A 1 3854 ? 182.976 105.357 162.435 1.00 120.66 ? 3854 GLN A CG    1 
ATOM   15657 C CD    . GLN A 1 3854 ? 183.211 105.797 163.865 1.00 120.66 ? 3854 GLN A CD    1 
ATOM   15658 O OE1   . GLN A 1 3854 ? 183.974 106.729 164.123 1.00 120.66 ? 3854 GLN A OE1   1 
ATOM   15659 N NE2   . GLN A 1 3854 ? 182.553 105.129 164.804 1.00 120.66 ? 3854 GLN A NE2   1 
ATOM   15660 N N     . ARG A 1 3855 ? 181.485 108.814 159.822 1.00 116.53 ? 3855 ARG A N     1 
ATOM   15661 C CA    . ARG A 1 3855 ? 181.580 109.989 158.965 1.00 116.53 ? 3855 ARG A CA    1 
ATOM   15662 C C     . ARG A 1 3855 ? 180.800 111.158 159.549 1.00 116.53 ? 3855 ARG A C     1 
ATOM   15663 O O     . ARG A 1 3855 ? 181.220 112.311 159.427 1.00 116.53 ? 3855 ARG A O     1 
ATOM   15664 C CB    . ARG A 1 3855 ? 181.100 109.661 157.552 1.00 116.53 ? 3855 ARG A CB    1 
ATOM   15665 C CG    . ARG A 1 3855 ? 181.870 108.528 156.891 1.00 116.53 ? 3855 ARG A CG    1 
ATOM   15666 C CD    . ARG A 1 3855 ? 181.616 108.452 155.392 1.00 116.53 ? 3855 ARG A CD    1 
ATOM   15667 N NE    . ARG A 1 3855 ? 182.654 109.121 154.619 1.00 116.53 ? 3855 ARG A NE    1 
ATOM   15668 C CZ    . ARG A 1 3855 ? 182.422 109.922 153.588 1.00 116.53 ? 3855 ARG A CZ    1 
ATOM   15669 N NH1   . ARG A 1 3855 ? 181.192 110.181 153.178 1.00 116.53 ? 3855 ARG A NH1   1 
ATOM   15670 N NH2   . ARG A 1 3855 ? 183.450 110.474 152.951 1.00 116.53 ? 3855 ARG A NH2   1 
ATOM   15671 N N     . LEU A 1 3856 ? 179.669 110.883 160.200 1.00 113.91 ? 3856 LEU A N     1 
ATOM   15672 C CA    . LEU A 1 3856 ? 178.912 111.962 160.826 1.00 113.91 ? 3856 LEU A CA    1 
ATOM   15673 C C     . LEU A 1 3856 ? 179.682 112.581 161.987 1.00 113.91 ? 3856 LEU A C     1 
ATOM   15674 O O     . LEU A 1 3856 ? 179.733 113.809 162.124 1.00 113.91 ? 3856 LEU A O     1 
ATOM   15675 C CB    . LEU A 1 3856 ? 177.552 111.447 161.292 1.00 113.91 ? 3856 LEU A CB    1 
ATOM   15676 C CG    . LEU A 1 3856 ? 176.686 112.427 162.084 1.00 113.91 ? 3856 LEU A CG    1 
ATOM   15677 C CD1   . LEU A 1 3856 ? 175.267 112.417 161.552 1.00 113.91 ? 3856 LEU A CD1   1 
ATOM   15678 C CD2   . LEU A 1 3856 ? 176.697 112.081 163.563 1.00 113.91 ? 3856 LEU A CD2   1 
ATOM   15679 N N     . SER A 1 3857 ? 180.291 111.751 162.835 1.00 109.96 ? 3857 SER A N     1 
ATOM   15680 C CA    . SER A 1 3857 ? 181.091 112.295 163.928 1.00 109.96 ? 3857 SER A CA    1 
ATOM   15681 C C     . SER A 1 3857 ? 182.268 113.101 163.391 1.00 109.96 ? 3857 SER A C     1 
ATOM   15682 O O     . SER A 1 3857 ? 182.573 114.191 163.897 1.00 109.96 ? 3857 SER A O     1 
ATOM   15683 C CB    . SER A 1 3857 ? 181.579 111.167 164.833 1.00 109.96 ? 3857 SER A CB    1 
ATOM   15684 O OG    . SER A 1 3857 ? 182.357 110.236 164.105 1.00 109.96 ? 3857 SER A OG    1 
ATOM   15685 N N     . ILE A 1 3858 ? 182.928 112.584 162.353 1.00 105.38 ? 3858 ILE A N     1 
ATOM   15686 C CA    . ILE A 1 3858 ? 184.061 113.283 161.760 1.00 105.38 ? 3858 ILE A CA    1 
ATOM   15687 C C     . ILE A 1 3858 ? 183.624 114.619 161.181 1.00 105.38 ? 3858 ILE A C     1 
ATOM   15688 O O     . ILE A 1 3858 ? 184.293 115.640 161.371 1.00 105.38 ? 3858 ILE A O     1 
ATOM   15689 C CB    . ILE A 1 3858 ? 184.730 112.399 160.694 1.00 105.38 ? 3858 ILE A CB    1 
ATOM   15690 C CG1   . ILE A 1 3858 ? 185.558 111.301 161.359 1.00 105.38 ? 3858 ILE A CG1   1 
ATOM   15691 C CG2   . ILE A 1 3858 ? 185.585 113.237 159.765 1.00 105.38 ? 3858 ILE A CG2   1 
ATOM   15692 C CD1   . ILE A 1 3858 ? 186.910 111.767 161.838 1.00 105.38 ? 3858 ILE A CD1   1 
ATOM   15693 N N     . ILE A 1 3859 ? 182.500 114.636 160.463 1.00 104.43 ? 3859 ILE A N     1 
ATOM   15694 C CA    . ILE A 1 3859 ? 182.057 115.872 159.831 1.00 104.43 ? 3859 ILE A CA    1 
ATOM   15695 C C     . ILE A 1 3859 ? 181.648 116.891 160.884 1.00 104.43 ? 3859 ILE A C     1 
ATOM   15696 O O     . ILE A 1 3859 ? 181.915 118.085 160.735 1.00 104.43 ? 3859 ILE A O     1 
ATOM   15697 C CB    . ILE A 1 3859 ? 180.934 115.596 158.810 1.00 104.43 ? 3859 ILE A CB    1 
ATOM   15698 C CG1   . ILE A 1 3859 ? 180.661 116.836 157.964 1.00 104.43 ? 3859 ILE A CG1   1 
ATOM   15699 C CG2   . ILE A 1 3859 ? 179.663 115.164 159.470 1.00 104.43 ? 3859 ILE A CG2   1 
ATOM   15700 C CD1   . ILE A 1 3859 ? 181.673 117.059 156.898 1.00 104.43 ? 3859 ILE A CD1   1 
ATOM   15701 N N     . THR A 1 3860 ? 181.039 116.443 161.984 1.00 99.14  ? 3860 THR A N     1 
ATOM   15702 C CA    . THR A 1 3860 ? 180.697 117.379 163.051 1.00 99.14  ? 3860 THR A CA    1 
ATOM   15703 C C     . THR A 1 3860 ? 181.948 117.987 163.676 1.00 99.14  ? 3860 THR A C     1 
ATOM   15704 O O     . THR A 1 3860 ? 182.048 119.215 163.836 1.00 99.14  ? 3860 THR A O     1 
ATOM   15705 C CB    . THR A 1 3860 ? 179.857 116.678 164.115 1.00 99.14  ? 3860 THR A CB    1 
ATOM   15706 O OG1   . THR A 1 3860 ? 178.663 116.164 163.516 1.00 99.14  ? 3860 THR A OG1   1 
ATOM   15707 C CG2   . THR A 1 3860 ? 179.487 117.647 165.222 1.00 99.14  ? 3860 THR A CG2   1 
ATOM   15708 N N     . LYS A 1 3861 ? 182.915 117.141 164.038 1.00 97.37  ? 3861 LYS A N     1 
ATOM   15709 C CA    . LYS A 1 3861 ? 184.131 117.643 164.669 1.00 97.37  ? 3861 LYS A CA    1 
ATOM   15710 C C     . LYS A 1 3861 ? 184.875 118.592 163.741 1.00 97.37  ? 3861 LYS A C     1 
ATOM   15711 O O     . LYS A 1 3861 ? 185.317 119.671 164.156 1.00 97.37  ? 3861 LYS A O     1 
ATOM   15712 C CB    . LYS A 1 3861 ? 185.030 116.478 165.077 1.00 97.37  ? 3861 LYS A CB    1 
ATOM   15713 C CG    . LYS A 1 3861 ? 186.391 116.903 165.600 1.00 97.37  ? 3861 LYS A CG    1 
ATOM   15714 C CD    . LYS A 1 3861 ? 187.357 115.731 165.657 1.00 97.37  ? 3861 LYS A CD    1 
ATOM   15715 C CE    . LYS A 1 3861 ? 186.716 114.511 166.299 1.00 97.37  ? 3861 LYS A CE    1 
ATOM   15716 N NZ    . LYS A 1 3861 ? 186.180 114.800 167.657 1.00 97.37  ? 3861 LYS A NZ    1 
ATOM   15717 N N     . ASP A 1 3862 ? 185.010 118.210 162.471 1.00 102.12 ? 3862 ASP A N     1 
ATOM   15718 C CA    . ASP A 1 3862 ? 185.715 119.057 161.523 1.00 102.12 ? 3862 ASP A CA    1 
ATOM   15719 C C     . ASP A 1 3862 ? 184.951 120.338 161.239 1.00 102.12 ? 3862 ASP A C     1 
ATOM   15720 O O     . ASP A 1 3862 ? 185.570 121.379 161.016 1.00 102.12 ? 3862 ASP A O     1 
ATOM   15721 C CB    . ASP A 1 3862 ? 185.982 118.290 160.231 1.00 102.12 ? 3862 ASP A CB    1 
ATOM   15722 C CG    . ASP A 1 3862 ? 186.857 117.079 160.453 1.00 102.12 ? 3862 ASP A CG    1 
ATOM   15723 O OD1   . ASP A 1 3862 ? 187.279 116.862 161.608 1.00 102.12 ? 3862 ASP A OD1   1 
ATOM   15724 O OD2   . ASP A 1 3862 ? 187.125 116.347 159.477 1.00 102.12 ? 3862 ASP A OD2   1 
ATOM   15725 N N     . LEU A 1 3863 ? 183.617 120.294 161.253 1.00 95.97  ? 3863 LEU A N     1 
ATOM   15726 C CA    . LEU A 1 3863 ? 182.844 121.519 161.113 1.00 95.97  ? 3863 LEU A CA    1 
ATOM   15727 C C     . LEU A 1 3863 ? 183.168 122.485 162.236 1.00 95.97  ? 3863 LEU A C     1 
ATOM   15728 O O     . LEU A 1 3863 ? 183.486 123.655 161.992 1.00 95.97  ? 3863 LEU A O     1 
ATOM   15729 C CB    . LEU A 1 3863 ? 181.351 121.204 161.108 1.00 95.97  ? 3863 LEU A CB    1 
ATOM   15730 C CG    . LEU A 1 3863 ? 180.484 122.396 161.509 1.00 95.97  ? 3863 LEU A CG    1 
ATOM   15731 C CD1   . LEU A 1 3863 ? 180.375 123.389 160.369 1.00 95.97  ? 3863 LEU A CD1   1 
ATOM   15732 C CD2   . LEU A 1 3863 ? 179.118 121.945 161.978 1.00 95.97  ? 3863 LEU A CD2   1 
ATOM   15733 N N     . PHE A 1 3864 ? 183.113 122.006 163.479 1.00 85.91  ? 3864 PHE A N     1 
ATOM   15734 C CA    . PHE A 1 3864 ? 183.422 122.882 164.604 1.00 85.91  ? 3864 PHE A CA    1 
ATOM   15735 C C     . PHE A 1 3864 ? 184.831 123.448 164.479 1.00 85.91  ? 3864 PHE A C     1 
ATOM   15736 O O     . PHE A 1 3864 ? 185.039 124.665 164.585 1.00 85.91  ? 3864 PHE A O     1 
ATOM   15737 C CB    . PHE A 1 3864 ? 183.263 122.128 165.921 1.00 85.91  ? 3864 PHE A CB    1 
ATOM   15738 C CG    . PHE A 1 3864 ? 181.899 122.251 166.530 1.00 85.91  ? 3864 PHE A CG    1 
ATOM   15739 C CD1   . PHE A 1 3864 ? 181.394 123.487 166.883 1.00 85.91  ? 3864 PHE A CD1   1 
ATOM   15740 C CD2   . PHE A 1 3864 ? 181.137 121.128 166.785 1.00 85.91  ? 3864 PHE A CD2   1 
ATOM   15741 C CE1   . PHE A 1 3864 ? 180.148 123.600 167.453 1.00 85.91  ? 3864 PHE A CE1   1 
ATOM   15742 C CE2   . PHE A 1 3864 ? 179.891 121.237 167.358 1.00 85.91  ? 3864 PHE A CE2   1 
ATOM   15743 C CZ    . PHE A 1 3864 ? 179.396 122.475 167.692 1.00 85.91  ? 3864 PHE A CZ    1 
ATOM   15744 N N     . GLN A 1 3865 ? 185.808 122.578 164.219 1.00 86.84  ? 3865 GLN A N     1 
ATOM   15745 C CA    . GLN A 1 3865 ? 187.201 123.012 164.173 1.00 86.84  ? 3865 GLN A CA    1 
ATOM   15746 C C     . GLN A 1 3865 ? 187.433 124.025 163.062 1.00 86.84  ? 3865 GLN A C     1 
ATOM   15747 O O     . GLN A 1 3865 ? 188.062 125.067 163.277 1.00 86.84  ? 3865 GLN A O     1 
ATOM   15748 C CB    . GLN A 1 3865 ? 188.116 121.804 163.989 1.00 86.84  ? 3865 GLN A CB    1 
ATOM   15749 C CG    . GLN A 1 3865 ? 189.583 122.157 163.911 1.00 86.84  ? 3865 GLN A CG    1 
ATOM   15750 C CD    . GLN A 1 3865 ? 190.123 122.655 165.228 1.00 86.84  ? 3865 GLN A CD    1 
ATOM   15751 O OE1   . GLN A 1 3865 ? 190.259 121.893 166.183 1.00 86.84  ? 3865 GLN A OE1   1 
ATOM   15752 N NE2   . GLN A 1 3865 ? 190.438 123.941 165.288 1.00 86.84  ? 3865 GLN A NE2   1 
ATOM   15753 N N     . VAL A 1 3866 ? 186.938 123.734 161.860 1.00 86.39  ? 3866 VAL A N     1 
ATOM   15754 C CA    . VAL A 1 3866 ? 187.216 124.598 160.724 1.00 86.39  ? 3866 VAL A CA    1 
ATOM   15755 C C     . VAL A 1 3866 ? 186.483 125.921 160.876 1.00 86.39  ? 3866 VAL A C     1 
ATOM   15756 O O     . VAL A 1 3866 ? 187.013 126.981 160.522 1.00 86.39  ? 3866 VAL A O     1 
ATOM   15757 C CB    . VAL A 1 3866 ? 186.856 123.882 159.411 1.00 86.39  ? 3866 VAL A CB    1 
ATOM   15758 C CG1   . VAL A 1 3866 ? 186.871 124.855 158.258 1.00 86.39  ? 3866 VAL A CG1   1 
ATOM   15759 C CG2   . VAL A 1 3866 ? 187.818 122.738 159.155 1.00 86.39  ? 3866 VAL A CG2   1 
ATOM   15760 N N     . ALA A 1 3867 ? 185.260 125.891 161.413 1.00 85.87  ? 3867 ALA A N     1 
ATOM   15761 C CA    . ALA A 1 3867 ? 184.544 127.134 161.661 1.00 85.87  ? 3867 ALA A CA    1 
ATOM   15762 C C     . ALA A 1 3867 ? 185.306 128.008 162.644 1.00 85.87  ? 3867 ALA A C     1 
ATOM   15763 O O     . ALA A 1 3867 ? 185.467 129.214 162.424 1.00 85.87  ? 3867 ALA A O     1 
ATOM   15764 C CB    . ALA A 1 3867 ? 183.139 126.839 162.180 1.00 85.87  ? 3867 ALA A CB    1 
ATOM   15765 N N     . PHE A 1 3868 ? 185.805 127.412 163.731 1.00 86.87  ? 3868 PHE A N     1 
ATOM   15766 C CA    . PHE A 1 3868 ? 186.559 128.205 164.695 1.00 86.87  ? 3868 PHE A CA    1 
ATOM   15767 C C     . PHE A 1 3868 ? 187.825 128.771 164.072 1.00 86.87  ? 3868 PHE A C     1 
ATOM   15768 O O     . PHE A 1 3868 ? 188.156 129.942 164.283 1.00 86.87  ? 3868 PHE A O     1 
ATOM   15769 C CB    . PHE A 1 3868 ? 186.917 127.374 165.920 1.00 86.87  ? 3868 PHE A CB    1 
ATOM   15770 C CG    . PHE A 1 3868 ? 187.790 128.100 166.898 1.00 86.87  ? 3868 PHE A CG    1 
ATOM   15771 C CD1   . PHE A 1 3868 ? 187.248 129.031 167.764 1.00 86.87  ? 3868 PHE A CD1   1 
ATOM   15772 C CD2   . PHE A 1 3868 ? 189.150 127.868 166.942 1.00 86.87  ? 3868 PHE A CD2   1 
ATOM   15773 C CE1   . PHE A 1 3868 ? 188.042 129.704 168.665 1.00 86.87  ? 3868 PHE A CE1   1 
ATOM   15774 C CE2   . PHE A 1 3868 ? 189.950 128.541 167.840 1.00 86.87  ? 3868 PHE A CE2   1 
ATOM   15775 C CZ    . PHE A 1 3868 ? 189.394 129.459 168.703 1.00 86.87  ? 3868 PHE A CZ    1 
ATOM   15776 N N     . ASN A 1 3869 ? 188.553 127.950 163.311 1.00 89.54  ? 3869 ASN A N     1 
ATOM   15777 C CA    . ASN A 1 3869 ? 189.794 128.421 162.706 1.00 89.54  ? 3869 ASN A CA    1 
ATOM   15778 C C     . ASN A 1 3869 ? 189.529 129.574 161.752 1.00 89.54  ? 3869 ASN A C     1 
ATOM   15779 O O     . ASN A 1 3869 ? 190.207 130.607 161.800 1.00 89.54  ? 3869 ASN A O     1 
ATOM   15780 C CB    . ASN A 1 3869 ? 190.495 127.279 161.974 1.00 89.54  ? 3869 ASN A CB    1 
ATOM   15781 C CG    . ASN A 1 3869 ? 190.839 126.129 162.888 1.00 89.54  ? 3869 ASN A CG    1 
ATOM   15782 O OD1   . ASN A 1 3869 ? 190.655 126.211 164.100 1.00 89.54  ? 3869 ASN A OD1   1 
ATOM   15783 N ND2   . ASN A 1 3869 ? 191.345 125.046 162.312 1.00 89.54  ? 3869 ASN A ND2   1 
ATOM   15784 N N     . ARG A 1 3870 ? 188.526 129.426 160.888 1.00 92.76  ? 3870 ARG A N     1 
ATOM   15785 C CA    . ARG A 1 3870 ? 188.265 130.452 159.890 1.00 92.76  ? 3870 ARG A CA    1 
ATOM   15786 C C     . ARG A 1 3870 ? 187.708 131.721 160.514 1.00 92.76  ? 3870 ARG A C     1 
ATOM   15787 O O     . ARG A 1 3870 ? 187.957 132.816 159.999 1.00 92.76  ? 3870 ARG A O     1 
ATOM   15788 C CB    . ARG A 1 3870 ? 187.317 129.915 158.824 1.00 92.76  ? 3870 ARG A CB    1 
ATOM   15789 C CG    . ARG A 1 3870 ? 187.956 128.880 157.922 1.00 92.76  ? 3870 ARG A CG    1 
ATOM   15790 C CD    . ARG A 1 3870 ? 186.949 128.297 156.960 1.00 92.76  ? 3870 ARG A CD    1 
ATOM   15791 N NE    . ARG A 1 3870 ? 186.952 129.017 155.694 1.00 92.76  ? 3870 ARG A NE    1 
ATOM   15792 C CZ    . ARG A 1 3870 ? 187.242 128.469 154.523 1.00 92.76  ? 3870 ARG A CZ    1 
ATOM   15793 N NH1   . ARG A 1 3870 ? 187.563 127.191 154.419 1.00 92.76  ? 3870 ARG A NH1   1 
ATOM   15794 N NH2   . ARG A 1 3870 ? 187.211 129.224 153.429 1.00 92.76  ? 3870 ARG A NH2   1 
ATOM   15795 N N     . VAL A 1 3871 ? 186.954 131.610 161.607 1.00 87.16  ? 3871 VAL A N     1 
ATOM   15796 C CA    . VAL A 1 3871 ? 186.487 132.814 162.282 1.00 87.16  ? 3871 VAL A CA    1 
ATOM   15797 C C     . VAL A 1 3871 ? 187.647 133.520 162.971 1.00 87.16  ? 3871 VAL A C     1 
ATOM   15798 O O     . VAL A 1 3871 ? 187.837 134.731 162.819 1.00 87.16  ? 3871 VAL A O     1 
ATOM   15799 C CB    . VAL A 1 3871 ? 185.368 132.475 163.280 1.00 87.16  ? 3871 VAL A CB    1 
ATOM   15800 C CG1   . VAL A 1 3871 ? 185.231 133.580 164.309 1.00 87.16  ? 3871 VAL A CG1   1 
ATOM   15801 C CG2   . VAL A 1 3871 ? 184.063 132.269 162.548 1.00 87.16  ? 3871 VAL A CG2   1 
ATOM   15802 N N     . ALA A 1 3872 ? 188.456 132.772 163.719 1.00 92.52  ? 3872 ALA A N     1 
ATOM   15803 C CA    . ALA A 1 3872 ? 189.474 133.393 164.550 1.00 92.52  ? 3872 ALA A CA    1 
ATOM   15804 C C     . ALA A 1 3872 ? 190.694 133.846 163.764 1.00 92.52  ? 3872 ALA A C     1 
ATOM   15805 O O     . ALA A 1 3872 ? 191.477 134.646 164.283 1.00 92.52  ? 3872 ALA A O     1 
ATOM   15806 C CB    . ALA A 1 3872 ? 189.900 132.433 165.659 1.00 92.52  ? 3872 ALA A CB    1 
ATOM   15807 N N     . ARG A 1 3873 ? 190.883 133.358 162.536 1.00 98.67  ? 3873 ARG A N     1 
ATOM   15808 C CA    . ARG A 1 3873 ? 192.010 133.830 161.740 1.00 98.67  ? 3873 ARG A CA    1 
ATOM   15809 C C     . ARG A 1 3873 ? 191.934 135.330 161.506 1.00 98.67  ? 3873 ARG A C     1 
ATOM   15810 O O     . ARG A 1 3873 ? 192.968 136.001 161.431 1.00 98.67  ? 3873 ARG A O     1 
ATOM   15811 C CB    . ARG A 1 3873 ? 192.059 133.091 160.403 1.00 98.67  ? 3873 ARG A CB    1 
ATOM   15812 C CG    . ARG A 1 3873 ? 192.854 131.798 160.425 1.00 98.67  ? 3873 ARG A CG    1 
ATOM   15813 C CD    . ARG A 1 3873 ? 194.205 131.984 161.086 1.00 98.67  ? 3873 ARG A CD    1 
ATOM   15814 N NE    . ARG A 1 3873 ? 195.044 130.802 160.933 1.00 98.67  ? 3873 ARG A NE    1 
ATOM   15815 C CZ    . ARG A 1 3873 ? 196.234 130.648 161.498 1.00 98.67  ? 3873 ARG A CZ    1 
ATOM   15816 N NH1   . ARG A 1 3873 ? 196.767 131.593 162.254 1.00 98.67  ? 3873 ARG A NH1   1 
ATOM   15817 N NH2   . ARG A 1 3873 ? 196.908 129.520 161.295 1.00 98.67  ? 3873 ARG A NH2   1 
ATOM   15818 N N     . GLY A 1 3874 ? 190.726 135.870 161.395 1.00 94.35  ? 3874 GLY A N     1 
ATOM   15819 C CA    . GLY A 1 3874 ? 190.540 137.292 161.204 1.00 94.35  ? 3874 GLY A CA    1 
ATOM   15820 C C     . GLY A 1 3874 ? 189.806 137.918 162.367 1.00 94.35  ? 3874 GLY A C     1 
ATOM   15821 O O     . GLY A 1 3874 ? 188.891 138.721 162.180 1.00 94.35  ? 3874 GLY A O     1 
ATOM   15822 N N     . MET A 1 3875 ? 190.191 137.545 163.579 1.00 95.22  ? 3875 MET A N     1 
ATOM   15823 C CA    . MET A 1 3875 ? 189.475 137.952 164.773 1.00 95.22  ? 3875 MET A CA    1 
ATOM   15824 C C     . MET A 1 3875 ? 190.478 138.270 165.873 1.00 95.22  ? 3875 MET A C     1 
ATOM   15825 O O     . MET A 1 3875 ? 191.579 137.715 165.905 1.00 95.22  ? 3875 MET A O     1 
ATOM   15826 C CB    . MET A 1 3875 ? 188.496 136.844 165.170 1.00 95.22  ? 3875 MET A CB    1 
ATOM   15827 C CG    . MET A 1 3875 ? 187.231 137.306 165.840 1.00 95.22  ? 3875 MET A CG    1 
ATOM   15828 S SD    . MET A 1 3875 ? 186.540 136.003 166.861 1.00 95.22  ? 3875 MET A SD    1 
ATOM   15829 C CE    . MET A 1 3875 ? 187.412 136.312 168.372 1.00 95.22  ? 3875 MET A CE    1 
ATOM   15830 N N     . LEU A 1 3876 ? 190.100 139.184 166.763 1.00 92.24  ? 3876 LEU A N     1 
ATOM   15831 C CA    . LEU A 1 3876 ? 191.041 139.691 167.755 1.00 92.24  ? 3876 LEU A CA    1 
ATOM   15832 C C     . LEU A 1 3876 ? 191.517 138.579 168.680 1.00 92.24  ? 3876 LEU A C     1 
ATOM   15833 O O     . LEU A 1 3876 ? 190.777 137.640 168.986 1.00 92.24  ? 3876 LEU A O     1 
ATOM   15834 C CB    . LEU A 1 3876 ? 190.398 140.808 168.575 1.00 92.24  ? 3876 LEU A CB    1 
ATOM   15835 C CG    . LEU A 1 3876 ? 190.836 142.235 168.251 1.00 92.24  ? 3876 LEU A CG    1 
ATOM   15836 C CD1   . LEU A 1 3876 ? 192.237 142.483 168.774 1.00 92.24  ? 3876 LEU A CD1   1 
ATOM   15837 C CD2   . LEU A 1 3876 ? 190.770 142.493 166.761 1.00 92.24  ? 3876 LEU A CD2   1 
ATOM   15838 N N     . HIS A 1 3877 ? 192.772 138.685 169.122 1.00 95.04  ? 3877 HIS A N     1 
ATOM   15839 C CA    . HIS A 1 3877 ? 193.319 137.669 170.014 1.00 95.04  ? 3877 HIS A CA    1 
ATOM   15840 C C     . HIS A 1 3877 ? 192.647 137.689 171.379 1.00 95.04  ? 3877 HIS A C     1 
ATOM   15841 O O     . HIS A 1 3877 ? 192.483 136.635 172.001 1.00 95.04  ? 3877 HIS A O     1 
ATOM   15842 C CB    . HIS A 1 3877 ? 194.825 137.852 170.180 1.00 95.04  ? 3877 HIS A CB    1 
ATOM   15843 C CG    . HIS A 1 3877 ? 195.490 136.718 170.894 1.00 95.04  ? 3877 HIS A CG    1 
ATOM   15844 N ND1   . HIS A 1 3877 ? 195.578 136.653 172.268 1.00 95.04  ? 3877 HIS A ND1   1 
ATOM   15845 C CD2   . HIS A 1 3877 ? 196.095 135.600 170.426 1.00 95.04  ? 3877 HIS A CD2   1 
ATOM   15846 C CE1   . HIS A 1 3877 ? 196.210 135.546 172.615 1.00 95.04  ? 3877 HIS A CE1   1 
ATOM   15847 N NE2   . HIS A 1 3877 ? 196.534 134.889 171.515 1.00 95.04  ? 3877 HIS A NE2   1 
ATOM   15848 N N     . GLN A 1 3878 ? 192.260 138.867 171.867 1.00 88.12  ? 3878 GLN A N     1 
ATOM   15849 C CA    . GLN A 1 3878 ? 191.645 138.947 173.185 1.00 88.12  ? 3878 GLN A CA    1 
ATOM   15850 C C     . GLN A 1 3878 ? 190.255 138.332 173.227 1.00 88.12  ? 3878 GLN A C     1 
ATOM   15851 O O     . GLN A 1 3878 ? 189.713 138.154 174.322 1.00 88.12  ? 3878 GLN A O     1 
ATOM   15852 C CB    . GLN A 1 3878 ? 191.569 140.401 173.650 1.00 88.12  ? 3878 GLN A CB    1 
ATOM   15853 C CG    . GLN A 1 3878 ? 190.664 141.278 172.806 1.00 88.12  ? 3878 GLN A CG    1 
ATOM   15854 C CD    . GLN A 1 3878 ? 190.579 142.699 173.328 1.00 88.12  ? 3878 GLN A CD    1 
ATOM   15855 O OE1   . GLN A 1 3878 ? 191.331 143.091 174.218 1.00 88.12  ? 3878 GLN A OE1   1 
ATOM   15856 N NE2   . GLN A 1 3878 ? 189.660 143.479 172.773 1.00 88.12  ? 3878 GLN A NE2   1 
ATOM   15857 N N     . ASP A 1 3879 ? 189.666 138.008 172.079 1.00 93.37  ? 3879 ASP A N     1 
ATOM   15858 C CA    . ASP A 1 3879 ? 188.312 137.482 172.027 1.00 93.37  ? 3879 ASP A CA    1 
ATOM   15859 C C     . ASP A 1 3879 ? 188.235 136.050 171.517 1.00 93.37  ? 3879 ASP A C     1 
ATOM   15860 O O     . ASP A 1 3879 ? 187.129 135.510 171.418 1.00 93.37  ? 3879 ASP A O     1 
ATOM   15861 C CB    . ASP A 1 3879 ? 187.431 138.381 171.155 1.00 93.37  ? 3879 ASP A CB    1 
ATOM   15862 C CG    . ASP A 1 3879 ? 187.384 139.806 171.651 1.00 93.37  ? 3879 ASP A CG    1 
ATOM   15863 O OD1   . ASP A 1 3879 ? 187.634 140.021 172.855 1.00 93.37  ? 3879 ASP A OD1   1 
ATOM   15864 O OD2   . ASP A 1 3879 ? 187.102 140.711 170.839 1.00 93.37  ? 3879 ASP A OD2   1 
ATOM   15865 N N     . HIS A 1 3880 ? 189.367 135.426 171.178 1.00 89.16  ? 3880 HIS A N     1 
ATOM   15866 C CA    . HIS A 1 3880 ? 189.345 134.035 170.730 1.00 89.16  ? 3880 HIS A CA    1 
ATOM   15867 C C     . HIS A 1 3880 ? 188.630 133.144 171.731 1.00 89.16  ? 3880 HIS A C     1 
ATOM   15868 O O     . HIS A 1 3880 ? 187.854 132.256 171.351 1.00 89.16  ? 3880 HIS A O     1 
ATOM   15869 C CB    . HIS A 1 3880 ? 190.768 133.525 170.515 1.00 89.16  ? 3880 HIS A CB    1 
ATOM   15870 C CG    . HIS A 1 3880 ? 191.407 134.018 169.260 1.00 89.16  ? 3880 HIS A CG    1 
ATOM   15871 N ND1   . HIS A 1 3880 ? 190.758 134.844 168.370 1.00 89.16  ? 3880 HIS A ND1   1 
ATOM   15872 C CD2   . HIS A 1 3880 ? 192.637 133.796 168.740 1.00 89.16  ? 3880 HIS A CD2   1 
ATOM   15873 C CE1   . HIS A 1 3880 ? 191.562 135.112 167.357 1.00 89.16  ? 3880 HIS A CE1   1 
ATOM   15874 N NE2   . HIS A 1 3880 ? 192.708 134.488 167.558 1.00 89.16  ? 3880 HIS A NE2   1 
ATOM   15875 N N     . ILE A 1 3881 ? 188.878 133.371 173.020 1.00 83.32  ? 3881 ILE A N     1 
ATOM   15876 C CA    . ILE A 1 3881 ? 188.274 132.539 174.048 1.00 83.32  ? 3881 ILE A CA    1 
ATOM   15877 C C     . ILE A 1 3881 ? 186.762 132.698 174.051 1.00 83.32  ? 3881 ILE A C     1 
ATOM   15878 O O     . ILE A 1 3881 ? 186.037 131.756 174.379 1.00 83.32  ? 3881 ILE A O     1 
ATOM   15879 C CB    . ILE A 1 3881 ? 188.885 132.869 175.419 1.00 83.32  ? 3881 ILE A CB    1 
ATOM   15880 C CG1   . ILE A 1 3881 ? 188.450 131.833 176.449 1.00 83.32  ? 3881 ILE A CG1   1 
ATOM   15881 C CG2   . ILE A 1 3881 ? 188.480 134.259 175.853 1.00 83.32  ? 3881 ILE A CG2   1 
ATOM   15882 C CD1   . ILE A 1 3881 ? 188.858 130.425 176.092 1.00 83.32  ? 3881 ILE A CD1   1 
ATOM   15883 N N     . THR A 1 3882 ? 186.257 133.872 173.670 1.00 88.67  ? 3882 THR A N     1 
ATOM   15884 C CA    . THR A 1 3882 ? 184.812 134.073 173.638 1.00 88.67  ? 3882 THR A CA    1 
ATOM   15885 C C     . THR A 1 3882 ? 184.154 133.166 172.607 1.00 88.67  ? 3882 THR A C     1 
ATOM   15886 O O     . THR A 1 3882 ? 183.184 132.458 172.911 1.00 88.67  ? 3882 THR A O     1 
ATOM   15887 C CB    . THR A 1 3882 ? 184.496 135.536 173.343 1.00 88.67  ? 3882 THR A CB    1 
ATOM   15888 O OG1   . THR A 1 3882 ? 184.701 136.313 174.528 1.00 88.67  ? 3882 THR A OG1   1 
ATOM   15889 C CG2   . THR A 1 3882 ? 183.060 135.690 172.882 1.00 88.67  ? 3882 THR A CG2   1 
ATOM   15890 N N     . PHE A 1 3883 ? 184.673 133.164 171.381 1.00 83.77  ? 3883 PHE A N     1 
ATOM   15891 C CA    . PHE A 1 3883 ? 184.101 132.298 170.361 1.00 83.77  ? 3883 PHE A CA    1 
ATOM   15892 C C     . PHE A 1 3883 ? 184.341 130.832 170.680 1.00 83.77  ? 3883 PHE A C     1 
ATOM   15893 O O     . PHE A 1 3883 ? 183.493 129.987 170.370 1.00 83.77  ? 3883 PHE A O     1 
ATOM   15894 C CB    . PHE A 1 3883 ? 184.671 132.642 168.992 1.00 83.77  ? 3883 PHE A CB    1 
ATOM   15895 C CG    . PHE A 1 3883 ? 183.851 132.119 167.859 1.00 83.77  ? 3883 PHE A CG    1 
ATOM   15896 C CD1   . PHE A 1 3883 ? 182.514 132.446 167.754 1.00 83.77  ? 3883 PHE A CD1   1 
ATOM   15897 C CD2   . PHE A 1 3883 ? 184.412 131.298 166.901 1.00 83.77  ? 3883 PHE A CD2   1 
ATOM   15898 C CE1   . PHE A 1 3883 ? 181.753 131.966 166.712 1.00 83.77  ? 3883 PHE A CE1   1 
ATOM   15899 C CE2   . PHE A 1 3883 ? 183.655 130.815 165.857 1.00 83.77  ? 3883 PHE A CE2   1 
ATOM   15900 C CZ    . PHE A 1 3883 ? 182.325 131.152 165.761 1.00 83.77  ? 3883 PHE A CZ    1 
ATOM   15901 N N     . ALA A 1 3884 ? 185.477 130.508 171.298 1.00 86.98  ? 3884 ALA A N     1 
ATOM   15902 C CA    . ALA A 1 3884 ? 185.696 129.131 171.723 1.00 86.98  ? 3884 ALA A CA    1 
ATOM   15903 C C     . ALA A 1 3884 ? 184.649 128.701 172.742 1.00 86.98  ? 3884 ALA A C     1 
ATOM   15904 O O     . ALA A 1 3884 ? 184.128 127.584 172.672 1.00 86.98  ? 3884 ALA A O     1 
ATOM   15905 C CB    . ALA A 1 3884 ? 187.103 128.971 172.293 1.00 86.98  ? 3884 ALA A CB    1 
ATOM   15906 N N     . MET A 1 3885 ? 184.321 129.576 173.692 1.00 86.74  ? 3885 MET A N     1 
ATOM   15907 C CA    . MET A 1 3885 ? 183.288 129.260 174.671 1.00 86.74  ? 3885 MET A CA    1 
ATOM   15908 C C     . MET A 1 3885 ? 181.928 129.102 174.004 1.00 86.74  ? 3885 MET A C     1 
ATOM   15909 O O     . MET A 1 3885 ? 181.141 128.222 174.372 1.00 86.74  ? 3885 MET A O     1 
ATOM   15910 C CB    . MET A 1 3885 ? 183.240 130.344 175.745 1.00 86.74  ? 3885 MET A CB    1 
ATOM   15911 C CG    . MET A 1 3885 ? 184.456 130.368 176.645 1.00 86.74  ? 3885 MET A CG    1 
ATOM   15912 S SD    . MET A 1 3885 ? 184.631 128.887 177.649 1.00 86.74  ? 3885 MET A SD    1 
ATOM   15913 C CE    . MET A 1 3885 ? 182.938 128.631 178.167 1.00 86.74  ? 3885 MET A CE    1 
ATOM   15914 N N     . LEU A 1 3886 ? 181.622 129.963 173.033 1.00 81.29  ? 3886 LEU A N     1 
ATOM   15915 C CA    . LEU A 1 3886 ? 180.349 129.831 172.330 1.00 81.29  ? 3886 LEU A CA    1 
ATOM   15916 C C     . LEU A 1 3886 ? 180.259 128.498 171.602 1.00 81.29  ? 3886 LEU A C     1 
ATOM   15917 O O     . LEU A 1 3886 ? 179.223 127.823 171.648 1.00 81.29  ? 3886 LEU A O     1 
ATOM   15918 C CB    . LEU A 1 3886 ? 180.152 130.985 171.352 1.00 81.29  ? 3886 LEU A CB    1 
ATOM   15919 C CG    . LEU A 1 3886 ? 179.310 132.152 171.861 1.00 81.29  ? 3886 LEU A CG    1 
ATOM   15920 C CD1   . LEU A 1 3886 ? 177.839 131.813 171.740 1.00 81.29  ? 3886 LEU A CD1   1 
ATOM   15921 C CD2   . LEU A 1 3886 ? 179.655 132.480 173.289 1.00 81.29  ? 3886 LEU A CD2   1 
ATOM   15922 N N     . LEU A 1 3887 ? 181.335 128.100 170.927 1.00 83.20  ? 3887 LEU A N     1 
ATOM   15923 C CA    . LEU A 1 3887 ? 181.333 126.806 170.258 1.00 83.20  ? 3887 LEU A CA    1 
ATOM   15924 C C     . LEU A 1 3887 ? 181.237 125.669 171.264 1.00 83.20  ? 3887 LEU A C     1 
ATOM   15925 O O     . LEU A 1 3887 ? 180.609 124.641 170.991 1.00 83.20  ? 3887 LEU A O     1 
ATOM   15926 C CB    . LEU A 1 3887 ? 182.576 126.653 169.389 1.00 83.20  ? 3887 LEU A CB    1 
ATOM   15927 C CG    . LEU A 1 3887 ? 182.331 126.892 167.903 1.00 83.20  ? 3887 LEU A CG    1 
ATOM   15928 C CD1   . LEU A 1 3887 ? 181.877 128.309 167.669 1.00 83.20  ? 3887 LEU A CD1   1 
ATOM   15929 C CD2   . LEU A 1 3887 ? 183.586 126.605 167.120 1.00 83.20  ? 3887 LEU A CD2   1 
ATOM   15930 N N     . ALA A 1 3888 ? 181.859 125.828 172.432 1.00 88.44  ? 3888 ALA A N     1 
ATOM   15931 C CA    . ALA A 1 3888 ? 181.741 124.805 173.461 1.00 88.44  ? 3888 ALA A CA    1 
ATOM   15932 C C     . ALA A 1 3888 ? 180.299 124.645 173.907 1.00 88.44  ? 3888 ALA A C     1 
ATOM   15933 O O     . ALA A 1 3888 ? 179.799 123.522 174.030 1.00 88.44  ? 3888 ALA A O     1 
ATOM   15934 C CB    . ALA A 1 3888 ? 182.635 125.145 174.650 1.00 88.44  ? 3888 ALA A CB    1 
ATOM   15935 N N     . ARG A 1 3889 ? 179.610 125.760 174.134 1.00 89.92  ? 3889 ARG A N     1 
ATOM   15936 C CA    . ARG A 1 3889 ? 178.215 125.686 174.546 1.00 89.92  ? 3889 ARG A CA    1 
ATOM   15937 C C     . ARG A 1 3889 ? 177.356 125.078 173.446 1.00 89.92  ? 3889 ARG A C     1 
ATOM   15938 O O     . ARG A 1 3889 ? 176.436 124.301 173.723 1.00 89.92  ? 3889 ARG A O     1 
ATOM   15939 C CB    . ARG A 1 3889 ? 177.707 127.074 174.929 1.00 89.92  ? 3889 ARG A CB    1 
ATOM   15940 C CG    . ARG A 1 3889 ? 178.215 127.549 176.276 1.00 89.92  ? 3889 ARG A CG    1 
ATOM   15941 C CD    . ARG A 1 3889 ? 177.619 128.885 176.646 1.00 89.92  ? 3889 ARG A CD    1 
ATOM   15942 N NE    . ARG A 1 3889 ? 176.197 128.935 176.339 1.00 89.92  ? 3889 ARG A NE    1 
ATOM   15943 C CZ    . ARG A 1 3889 ? 175.244 129.052 177.252 1.00 89.92  ? 3889 ARG A CZ    1 
ATOM   15944 N NH1   . ARG A 1 3889 ? 175.531 129.150 178.539 1.00 89.92  ? 3889 ARG A NH1   1 
ATOM   15945 N NH2   . ARG A 1 3889 ? 173.973 129.071 176.865 1.00 89.92  ? 3889 ARG A NH2   1 
ATOM   15946 N N     . ILE A 1 3890 ? 177.647 125.414 172.188 1.00 87.74  ? 3890 ILE A N     1 
ATOM   15947 C CA    . ILE A 1 3890 ? 176.867 124.867 171.083 1.00 87.74  ? 3890 ILE A CA    1 
ATOM   15948 C C     . ILE A 1 3890 ? 177.072 123.361 170.964 1.00 87.74  ? 3890 ILE A C     1 
ATOM   15949 O O     . ILE A 1 3890 ? 176.112 122.605 170.776 1.00 87.74  ? 3890 ILE A O     1 
ATOM   15950 C CB    . ILE A 1 3890 ? 177.210 125.603 169.779 1.00 87.74  ? 3890 ILE A CB    1 
ATOM   15951 C CG1   . ILE A 1 3890 ? 176.613 127.010 169.820 1.00 87.74  ? 3890 ILE A CG1   1 
ATOM   15952 C CG2   . ILE A 1 3890 ? 176.703 124.826 168.581 1.00 87.74  ? 3890 ILE A CG2   1 
ATOM   15953 C CD1   . ILE A 1 3890 ? 176.793 127.802 168.557 1.00 87.74  ? 3890 ILE A CD1   1 
ATOM   15954 N N     . LYS A 1 3891 ? 178.318 122.897 171.077 1.00 92.03  ? 3891 LYS A N     1 
ATOM   15955 C CA    . LYS A 1 3891 ? 178.571 121.460 171.042 1.00 92.03  ? 3891 LYS A CA    1 
ATOM   15956 C C     . LYS A 1 3891 ? 177.914 120.760 172.223 1.00 92.03  ? 3891 LYS A C     1 
ATOM   15957 O O     . LYS A 1 3891 ? 177.374 119.657 172.079 1.00 92.03  ? 3891 LYS A O     1 
ATOM   15958 C CB    . LYS A 1 3891 ? 180.073 121.186 171.027 1.00 92.03  ? 3891 LYS A CB    1 
ATOM   15959 C CG    . LYS A 1 3891 ? 180.433 119.734 171.300 1.00 92.03  ? 3891 LYS A CG    1 
ATOM   15960 C CD    . LYS A 1 3891 ? 180.539 118.932 170.015 1.00 92.03  ? 3891 LYS A CD    1 
ATOM   15961 C CE    . LYS A 1 3891 ? 181.368 117.672 170.214 1.00 92.03  ? 3891 LYS A CE    1 
ATOM   15962 N NZ    . LYS A 1 3891 ? 182.827 117.935 170.127 1.00 92.03  ? 3891 LYS A NZ    1 
ATOM   15963 N N     . LEU A 1 3892 ? 177.950 121.386 173.400 1.00 98.80  ? 3892 LEU A N     1 
ATOM   15964 C CA    . LEU A 1 3892 ? 177.288 120.812 174.564 1.00 98.80  ? 3892 LEU A CA    1 
ATOM   15965 C C     . LEU A 1 3892 ? 175.791 120.670 174.331 1.00 98.80  ? 3892 LEU A C     1 
ATOM   15966 O O     . LEU A 1 3892 ? 175.193 119.645 174.679 1.00 98.80  ? 3892 LEU A O     1 
ATOM   15967 C CB    . LEU A 1 3892 ? 177.558 121.677 175.793 1.00 98.80  ? 3892 LEU A CB    1 
ATOM   15968 C CG    . LEU A 1 3892 ? 177.355 120.993 177.139 1.00 98.80  ? 3892 LEU A CG    1 
ATOM   15969 C CD1   . LEU A 1 3892 ? 178.141 119.702 177.183 1.00 98.80  ? 3892 LEU A CD1   1 
ATOM   15970 C CD2   . LEU A 1 3892 ? 177.777 121.917 178.263 1.00 98.80  ? 3892 LEU A CD2   1 
ATOM   15971 N N     . LYS A 1 3893 ? 175.168 121.691 173.743 1.00 100.76 ? 3893 LYS A N     1 
ATOM   15972 C CA    . LYS A 1 3893 ? 173.751 121.593 173.414 1.00 100.76 ? 3893 LYS A CA    1 
ATOM   15973 C C     . LYS A 1 3893 ? 173.500 120.517 172.369 1.00 100.76 ? 3893 LYS A C     1 
ATOM   15974 O O     . LYS A 1 3893 ? 172.455 119.858 172.394 1.00 100.76 ? 3893 LYS A O     1 
ATOM   15975 C CB    . LYS A 1 3893 ? 173.231 122.943 172.925 1.00 100.76 ? 3893 LYS A CB    1 
ATOM   15976 C CG    . LYS A 1 3893 ? 171.725 123.091 173.008 1.00 100.76 ? 3893 LYS A CG    1 
ATOM   15977 C CD    . LYS A 1 3893 ? 171.257 123.110 174.453 1.00 100.76 ? 3893 LYS A CD    1 
ATOM   15978 C CE    . LYS A 1 3893 ? 169.741 123.118 174.544 1.00 100.76 ? 3893 LYS A CE    1 
ATOM   15979 N NZ    . LYS A 1 3893 ? 169.153 124.307 173.871 1.00 100.76 ? 3893 LYS A NZ    1 
ATOM   15980 N N     . GLY A 1 3894 ? 174.444 120.322 171.448 1.00 104.51 ? 3894 GLY A N     1 
ATOM   15981 C CA    . GLY A 1 3894 ? 174.257 119.328 170.407 1.00 104.51 ? 3894 GLY A CA    1 
ATOM   15982 C C     . GLY A 1 3894 ? 174.604 117.917 170.825 1.00 104.51 ? 3894 GLY A C     1 
ATOM   15983 O O     . GLY A 1 3894 ? 174.125 116.957 170.215 1.00 104.51 ? 3894 GLY A O     1 
ATOM   15984 N N     . THR A 1 3895 ? 175.431 117.762 171.854 1.00 115.23 ? 3895 THR A N     1 
ATOM   15985 C CA    . THR A 1 3895 ? 175.816 116.428 172.282 1.00 115.23 ? 3895 THR A CA    1 
ATOM   15986 C C     . THR A 1 3895 ? 174.694 115.778 173.087 1.00 115.23 ? 3895 THR A C     1 
ATOM   15987 O O     . THR A 1 3895 ? 173.769 116.439 173.566 1.00 115.23 ? 3895 THR A O     1 
ATOM   15988 C CB    . THR A 1 3895 ? 177.103 116.468 173.106 1.00 115.23 ? 3895 THR A CB    1 
ATOM   15989 O OG1   . THR A 1 3895 ? 177.762 115.197 173.024 1.00 115.23 ? 3895 THR A OG1   1 
ATOM   15990 C CG2   . THR A 1 3895 ? 176.799 116.777 174.564 1.00 115.23 ? 3895 THR A CG2   1 
ATOM   15991 N N     . VAL A 1 3896 ? 174.788 114.458 173.230 1.00 125.30 ? 3896 VAL A N     1 
ATOM   15992 C CA    . VAL A 1 3896 ? 173.764 113.664 173.892 1.00 125.30 ? 3896 VAL A CA    1 
ATOM   15993 C C     . VAL A 1 3896 ? 174.355 113.036 175.146 1.00 125.30 ? 3896 VAL A C     1 
ATOM   15994 O O     . VAL A 1 3896 ? 175.573 112.994 175.339 1.00 125.30 ? 3896 VAL A O     1 
ATOM   15995 C CB    . VAL A 1 3896 ? 173.187 112.577 172.966 1.00 125.30 ? 3896 VAL A CB    1 
ATOM   15996 C CG1   . VAL A 1 3896 ? 172.411 113.212 171.826 1.00 125.30 ? 3896 VAL A CG1   1 
ATOM   15997 C CG2   . VAL A 1 3896 ? 174.304 111.695 172.433 1.00 125.30 ? 3896 VAL A CG2   1 
ATOM   15998 N N     . GLY A 1 3897 ? 173.467 112.541 176.004 1.00 131.53 ? 3897 GLY A N     1 
ATOM   15999 C CA    . GLY A 1 3897 ? 173.898 111.906 177.232 1.00 131.53 ? 3897 GLY A CA    1 
ATOM   16000 C C     . GLY A 1 3897 ? 174.617 112.817 178.195 1.00 131.53 ? 3897 GLY A C     1 
ATOM   16001 O O     . GLY A 1 3897 ? 175.549 112.374 178.871 1.00 131.53 ? 3897 GLY A O     1 
ATOM   16002 N N     . GLU A 1 3898 ? 174.225 114.085 178.268 1.00 131.93 ? 3898 GLU A N     1 
ATOM   16003 C CA    . GLU A 1 3898 ? 174.835 115.045 179.171 1.00 131.93 ? 3898 GLU A CA    1 
ATOM   16004 C C     . GLU A 1 3898 ? 173.769 115.898 179.837 1.00 131.93 ? 3898 GLU A C     1 
ATOM   16005 O O     . GLU A 1 3898 ? 172.709 116.145 179.255 1.00 131.93 ? 3898 GLU A O     1 
ATOM   16006 C CB    . GLU A 1 3898 ? 175.826 115.952 178.428 1.00 131.93 ? 3898 GLU A CB    1 
ATOM   16007 C CG    . GLU A 1 3898 ? 177.026 115.208 177.878 1.00 131.93 ? 3898 GLU A CG    1 
ATOM   16008 C CD    . GLU A 1 3898 ? 178.151 115.121 178.884 1.00 131.93 ? 3898 GLU A CD    1 
ATOM   16009 O OE1   . GLU A 1 3898 ? 178.090 115.843 179.902 1.00 131.93 ? 3898 GLU A OE1   1 
ATOM   16010 O OE2   . GLU A 1 3898 ? 179.087 114.323 178.669 1.00 131.93 ? 3898 GLU A OE2   1 
ATOM   16011 N N     . PRO A 1 3899 ? 174.023 116.359 181.058 1.00 127.45 ? 3899 PRO A N     1 
ATOM   16012 C CA    . PRO A 1 3899 ? 173.074 117.264 181.712 1.00 127.45 ? 3899 PRO A CA    1 
ATOM   16013 C C     . PRO A 1 3899 ? 172.970 118.581 180.965 1.00 127.45 ? 3899 PRO A C     1 
ATOM   16014 O O     . PRO A 1 3899 ? 173.900 119.014 180.282 1.00 127.45 ? 3899 PRO A O     1 
ATOM   16015 C CB    . PRO A 1 3899 ? 173.671 117.461 183.110 1.00 127.45 ? 3899 PRO A CB    1 
ATOM   16016 C CG    . PRO A 1 3899 ? 174.595 116.304 183.303 1.00 127.45 ? 3899 PRO A CG    1 
ATOM   16017 C CD    . PRO A 1 3899 ? 175.134 115.985 181.946 1.00 127.45 ? 3899 PRO A CD    1 
ATOM   16018 N N     . THR A 1 3900 ? 171.806 119.217 181.099 1.00 127.57 ? 3900 THR A N     1 
ATOM   16019 C CA    . THR A 1 3900 ? 171.540 120.442 180.355 1.00 127.57 ? 3900 THR A CA    1 
ATOM   16020 C C     . THR A 1 3900 ? 172.419 121.598 180.819 1.00 127.57 ? 3900 THR A C     1 
ATOM   16021 O O     . THR A 1 3900 ? 172.823 122.431 180.000 1.00 127.57 ? 3900 THR A O     1 
ATOM   16022 C CB    . THR A 1 3900 ? 170.062 120.805 180.475 1.00 127.57 ? 3900 THR A CB    1 
ATOM   16023 O OG1   . THR A 1 3900 ? 169.829 121.443 181.736 1.00 127.57 ? 3900 THR A OG1   1 
ATOM   16024 C CG2   . THR A 1 3900 ? 169.201 119.559 180.374 1.00 127.57 ? 3900 THR A CG2   1 
ATOM   16025 N N     . TYR A 1 3901 ? 172.717 121.672 182.118 1.00 122.69 ? 3901 TYR A N     1 
ATOM   16026 C CA    . TYR A 1 3901 ? 173.634 122.673 182.673 1.00 122.69 ? 3901 TYR A CA    1 
ATOM   16027 C C     . TYR A 1 3901 ? 173.174 124.102 182.394 1.00 122.69 ? 3901 TYR A C     1 
ATOM   16028 O O     . TYR A 1 3901 ? 173.989 124.999 182.173 1.00 122.69 ? 3901 TYR A O     1 
ATOM   16029 C CB    . TYR A 1 3901 ? 175.060 122.469 182.158 1.00 122.69 ? 3901 TYR A CB    1 
ATOM   16030 C CG    . TYR A 1 3901 ? 175.708 121.186 182.612 1.00 122.69 ? 3901 TYR A CG    1 
ATOM   16031 C CD1   . TYR A 1 3901 ? 175.590 120.755 183.925 1.00 122.69 ? 3901 TYR A CD1   1 
ATOM   16032 C CD2   . TYR A 1 3901 ? 176.455 120.415 181.734 1.00 122.69 ? 3901 TYR A CD2   1 
ATOM   16033 C CE1   . TYR A 1 3901 ? 176.185 119.585 184.349 1.00 122.69 ? 3901 TYR A CE1   1 
ATOM   16034 C CE2   . TYR A 1 3901 ? 177.056 119.243 182.148 1.00 122.69 ? 3901 TYR A CE2   1 
ATOM   16035 C CZ    . TYR A 1 3901 ? 176.918 118.833 183.457 1.00 122.69 ? 3901 TYR A CZ    1 
ATOM   16036 O OH    . TYR A 1 3901 ? 177.510 117.665 183.880 1.00 122.69 ? 3901 TYR A OH    1 
ATOM   16037 N N     . ASP A 1 3902 ? 171.861 124.328 182.413 1.00 122.79 ? 3902 ASP A N     1 
ATOM   16038 C CA    . ASP A 1 3902 ? 171.365 125.691 182.255 1.00 122.79 ? 3902 ASP A CA    1 
ATOM   16039 C C     . ASP A 1 3902 ? 171.586 126.516 183.515 1.00 122.79 ? 3902 ASP A C     1 
ATOM   16040 O O     . ASP A 1 3902 ? 171.950 127.693 183.431 1.00 122.79 ? 3902 ASP A O     1 
ATOM   16041 C CB    . ASP A 1 3902 ? 169.886 125.681 181.877 1.00 122.79 ? 3902 ASP A CB    1 
ATOM   16042 C CG    . ASP A 1 3902 ? 169.599 124.780 180.703 1.00 122.79 ? 3902 ASP A CG    1 
ATOM   16043 O OD1   . ASP A 1 3902 ? 170.362 123.816 180.508 1.00 122.79 ? 3902 ASP A OD1   1 
ATOM   16044 O OD2   . ASP A 1 3902 ? 168.612 125.030 179.980 1.00 122.79 ? 3902 ASP A OD2   1 
ATOM   16045 N N     . ALA A 1 3903 ? 171.368 125.925 184.689 1.00 116.48 ? 3903 ALA A N     1 
ATOM   16046 C CA    . ALA A 1 3903 ? 171.474 126.689 185.928 1.00 116.48 ? 3903 ALA A CA    1 
ATOM   16047 C C     . ALA A 1 3903 ? 172.909 127.135 186.182 1.00 116.48 ? 3903 ALA A C     1 
ATOM   16048 O O     . ALA A 1 3903 ? 173.160 128.303 186.504 1.00 116.48 ? 3903 ALA A O     1 
ATOM   16049 C CB    . ALA A 1 3903 ? 170.951 125.861 187.099 1.00 116.48 ? 3903 ALA A CB    1 
ATOM   16050 N N     . GLU A 1 3904 ? 173.865 126.213 186.047 1.00 115.11 ? 3904 GLU A N     1 
ATOM   16051 C CA    . GLU A 1 3904 ? 175.261 126.561 186.285 1.00 115.11 ? 3904 GLU A CA    1 
ATOM   16052 C C     . GLU A 1 3904 ? 175.744 127.604 185.290 1.00 115.11 ? 3904 GLU A C     1 
ATOM   16053 O O     . GLU A 1 3904 ? 176.429 128.561 185.667 1.00 115.11 ? 3904 GLU A O     1 
ATOM   16054 C CB    . GLU A 1 3904 ? 176.137 125.310 186.215 1.00 115.11 ? 3904 GLU A CB    1 
ATOM   16055 C CG    . GLU A 1 3904 ? 175.678 124.161 187.097 1.00 115.11 ? 3904 GLU A CG    1 
ATOM   16056 C CD    . GLU A 1 3904 ? 174.635 123.288 186.431 1.00 115.11 ? 3904 GLU A CD    1 
ATOM   16057 O OE1   . GLU A 1 3904 ? 173.805 123.825 185.669 1.00 115.11 ? 3904 GLU A OE1   1 
ATOM   16058 O OE2   . GLU A 1 3904 ? 174.648 122.062 186.667 1.00 115.11 ? 3904 GLU A OE2   1 
ATOM   16059 N N     . PHE A 1 3905 ? 175.394 127.440 184.014 1.00 105.28 ? 3905 PHE A N     1 
ATOM   16060 C CA    . PHE A 1 3905 ? 175.809 128.409 183.007 1.00 105.28 ? 3905 PHE A CA    1 
ATOM   16061 C C     . PHE A 1 3905 ? 175.171 129.768 183.251 1.00 105.28 ? 3905 PHE A C     1 
ATOM   16062 O O     . PHE A 1 3905 ? 175.818 130.805 183.072 1.00 105.28 ? 3905 PHE A O     1 
ATOM   16063 C CB    . PHE A 1 3905 ? 175.460 127.895 181.615 1.00 105.28 ? 3905 PHE A CB    1 
ATOM   16064 C CG    . PHE A 1 3905 ? 176.629 127.337 180.871 1.00 105.28 ? 3905 PHE A CG    1 
ATOM   16065 C CD1   . PHE A 1 3905 ? 177.778 128.084 180.708 1.00 105.28 ? 3905 PHE A CD1   1 
ATOM   16066 C CD2   . PHE A 1 3905 ? 176.583 126.063 180.339 1.00 105.28 ? 3905 PHE A CD2   1 
ATOM   16067 C CE1   . PHE A 1 3905 ? 178.857 127.574 180.022 1.00 105.28 ? 3905 PHE A CE1   1 
ATOM   16068 C CE2   . PHE A 1 3905 ? 177.660 125.547 179.654 1.00 105.28 ? 3905 PHE A CE2   1 
ATOM   16069 C CZ    . PHE A 1 3905 ? 178.799 126.305 179.495 1.00 105.28 ? 3905 PHE A CZ    1 
ATOM   16070 N N     . GLN A 1 3906 ? 173.898 129.785 183.647 1.00 110.04 ? 3906 GLN A N     1 
ATOM   16071 C CA    . GLN A 1 3906 ? 173.231 131.049 183.935 1.00 110.04 ? 3906 GLN A CA    1 
ATOM   16072 C C     . GLN A 1 3906 ? 173.885 131.754 185.115 1.00 110.04 ? 3906 GLN A C     1 
ATOM   16073 O O     . GLN A 1 3906 ? 174.074 132.975 185.092 1.00 110.04 ? 3906 GLN A O     1 
ATOM   16074 C CB    . GLN A 1 3906 ? 171.748 130.807 184.207 1.00 110.04 ? 3906 GLN A CB    1 
ATOM   16075 C CG    . GLN A 1 3906 ? 171.003 132.029 184.701 1.00 110.04 ? 3906 GLN A CG    1 
ATOM   16076 C CD    . GLN A 1 3906 ? 171.141 133.206 183.758 1.00 110.04 ? 3906 GLN A CD    1 
ATOM   16077 O OE1   . GLN A 1 3906 ? 171.753 134.219 184.095 1.00 110.04 ? 3906 GLN A OE1   1 
ATOM   16078 N NE2   . GLN A 1 3906 ? 170.575 133.076 182.565 1.00 110.04 ? 3906 GLN A NE2   1 
ATOM   16079 N N     . HIS A 1 3907 ? 174.235 131.002 186.159 1.00 110.31 ? 3907 HIS A N     1 
ATOM   16080 C CA    . HIS A 1 3907 ? 174.941 131.605 187.283 1.00 110.31 ? 3907 HIS A CA    1 
ATOM   16081 C C     . HIS A 1 3907 ? 176.311 132.114 186.856 1.00 110.31 ? 3907 HIS A C     1 
ATOM   16082 O O     . HIS A 1 3907 ? 176.752 133.181 187.296 1.00 110.31 ? 3907 HIS A O     1 
ATOM   16083 C CB    . HIS A 1 3907 ? 175.073 130.600 188.423 1.00 110.31 ? 3907 HIS A CB    1 
ATOM   16084 C CG    . HIS A 1 3907 ? 175.650 131.183 189.674 1.00 110.31 ? 3907 HIS A CG    1 
ATOM   16085 N ND1   . HIS A 1 3907 ? 175.077 132.252 190.328 1.00 110.31 ? 3907 HIS A ND1   1 
ATOM   16086 C CD2   . HIS A 1 3907 ? 176.744 130.843 190.395 1.00 110.31 ? 3907 HIS A CD2   1 
ATOM   16087 C CE1   . HIS A 1 3907 ? 175.796 132.549 191.395 1.00 110.31 ? 3907 HIS A CE1   1 
ATOM   16088 N NE2   . HIS A 1 3907 ? 176.812 131.708 191.460 1.00 110.31 ? 3907 HIS A NE2   1 
ATOM   16089 N N     . PHE A 1 3908 ? 176.994 131.361 185.996 1.00 101.00 ? 3908 PHE A N     1 
ATOM   16090 C CA    . PHE A 1 3908 ? 178.308 131.767 185.518 1.00 101.00 ? 3908 PHE A CA    1 
ATOM   16091 C C     . PHE A 1 3908 ? 178.243 133.039 184.685 1.00 101.00 ? 3908 PHE A C     1 
ATOM   16092 O O     . PHE A 1 3908 ? 179.151 133.872 184.760 1.00 101.00 ? 3908 PHE A O     1 
ATOM   16093 C CB    . PHE A 1 3908 ? 178.923 130.630 184.708 1.00 101.00 ? 3908 PHE A CB    1 
ATOM   16094 C CG    . PHE A 1 3908 ? 180.221 130.979 184.055 1.00 101.00 ? 3908 PHE A CG    1 
ATOM   16095 C CD1   . PHE A 1 3908 ? 181.382 131.062 184.796 1.00 101.00 ? 3908 PHE A CD1   1 
ATOM   16096 C CD2   . PHE A 1 3908 ? 180.286 131.191 182.694 1.00 101.00 ? 3908 PHE A CD2   1 
ATOM   16097 C CE1   . PHE A 1 3908 ? 182.577 131.374 184.194 1.00 101.00 ? 3908 PHE A CE1   1 
ATOM   16098 C CE2   . PHE A 1 3908 ? 181.479 131.498 182.087 1.00 101.00 ? 3908 PHE A CE2   1 
ATOM   16099 C CZ    . PHE A 1 3908 ? 182.626 131.587 182.836 1.00 101.00 ? 3908 PHE A CZ    1 
ATOM   16100 N N     . LEU A 1 3909 ? 177.189 133.204 183.890 1.00 101.34 ? 3909 LEU A N     1 
ATOM   16101 C CA    . LEU A 1 3909 ? 177.091 134.357 183.003 1.00 101.34 ? 3909 LEU A CA    1 
ATOM   16102 C C     . LEU A 1 3909 ? 176.636 135.596 183.760 1.00 101.34 ? 3909 LEU A C     1 
ATOM   16103 O O     . LEU A 1 3909 ? 177.354 136.598 183.829 1.00 101.34 ? 3909 LEU A O     1 
ATOM   16104 C CB    . LEU A 1 3909 ? 176.116 134.062 181.861 1.00 101.34 ? 3909 LEU A CB    1 
ATOM   16105 C CG    . LEU A 1 3909 ? 176.650 133.500 180.546 1.00 101.34 ? 3909 LEU A CG    1 
ATOM   16106 C CD1   . LEU A 1 3909 ? 177.324 134.587 179.731 1.00 101.34 ? 3909 LEU A CD1   1 
ATOM   16107 C CD2   . LEU A 1 3909 ? 177.578 132.335 180.796 1.00 101.34 ? 3909 LEU A CD2   1 
ATOM   16108 N N     . ARG A 1 3910 ? 175.440 135.540 184.333 1.00 114.62 ? 3910 ARG A N     1 
ATOM   16109 C CA    . ARG A 1 3910 ? 174.807 136.687 184.963 1.00 114.62 ? 3910 ARG A CA    1 
ATOM   16110 C C     . ARG A 1 3910 ? 174.491 136.475 186.433 1.00 114.62 ? 3910 ARG A C     1 
ATOM   16111 O O     . ARG A 1 3910 ? 174.522 137.440 187.201 1.00 114.62 ? 3910 ARG A O     1 
ATOM   16112 C CB    . ARG A 1 3910 ? 173.514 137.048 184.208 1.00 114.62 ? 3910 ARG A CB    1 
ATOM   16113 C CG    . ARG A 1 3910 ? 172.430 137.713 185.035 1.00 114.62 ? 3910 ARG A CG    1 
ATOM   16114 C CD    . ARG A 1 3910 ? 171.054 137.434 184.459 1.00 114.62 ? 3910 ARG A CD    1 
ATOM   16115 N NE    . ARG A 1 3910 ? 171.087 137.284 183.009 1.00 114.62 ? 3910 ARG A NE    1 
ATOM   16116 C CZ    . ARG A 1 3910 ? 170.992 138.289 182.149 1.00 114.62 ? 3910 ARG A CZ    1 
ATOM   16117 N NH1   . ARG A 1 3910 ? 170.858 139.539 182.560 1.00 114.62 ? 3910 ARG A NH1   1 
ATOM   16118 N NH2   . ARG A 1 3910 ? 171.033 138.033 180.845 1.00 114.62 ? 3910 ARG A NH2   1 
ATOM   16119 N N     . GLY A 1 3911 ? 174.239 135.238 186.854 1.00 118.44 ? 3911 GLY A N     1 
ATOM   16120 C CA    . GLY A 1 3911 ? 173.847 134.952 188.220 1.00 118.44 ? 3911 GLY A CA    1 
ATOM   16121 C C     . GLY A 1 3911 ? 174.849 135.374 189.275 1.00 118.44 ? 3911 GLY A C     1 
ATOM   16122 O O     . GLY A 1 3911 ? 174.575 135.266 190.473 1.00 118.44 ? 3911 GLY A O     1 
ATOM   16123 N N     . ASN A 1 3912 ? 176.023 135.842 188.849 1.00 118.33 ? 3912 ASN A N     1 
ATOM   16124 C CA    . ASN A 1 3912 ? 176.966 136.407 189.804 1.00 118.33 ? 3912 ASN A CA    1 
ATOM   16125 C C     . ASN A 1 3912 ? 176.482 137.749 190.332 1.00 118.33 ? 3912 ASN A C     1 
ATOM   16126 O O     . ASN A 1 3912 ? 176.725 138.079 191.497 1.00 118.33 ? 3912 ASN A O     1 
ATOM   16127 C CB    . ASN A 1 3912 ? 178.344 136.555 189.162 1.00 118.33 ? 3912 ASN A CB    1 
ATOM   16128 C CG    . ASN A 1 3912 ? 179.239 137.519 189.918 1.00 118.33 ? 3912 ASN A CG    1 
ATOM   16129 O OD1   . ASN A 1 3912 ? 179.158 138.734 189.739 1.00 118.33 ? 3912 ASN A OD1   1 
ATOM   16130 N ND2   . ASN A 1 3912 ? 180.095 136.977 190.775 1.00 118.33 ? 3912 ASN A ND2   1 
ATOM   16131 N N     . GLU A 1 3913 ? 175.802 138.531 189.500 1.00 120.13 ? 3913 GLU A N     1 
ATOM   16132 C CA    . GLU A 1 3913 ? 175.347 139.861 189.894 1.00 120.13 ? 3913 GLU A CA    1 
ATOM   16133 C C     . GLU A 1 3913 ? 173.917 139.788 190.428 1.00 120.13 ? 3913 GLU A C     1 
ATOM   16134 O O     . GLU A 1 3913 ? 172.959 140.277 189.830 1.00 120.13 ? 3913 GLU A O     1 
ATOM   16135 C CB    . GLU A 1 3913 ? 175.471 140.832 188.724 1.00 120.13 ? 3913 GLU A CB    1 
ATOM   16136 C CG    . GLU A 1 3913 ? 176.900 141.028 188.240 1.00 120.13 ? 3913 GLU A CG    1 
ATOM   16137 C CD    . GLU A 1 3913 ? 177.236 140.175 187.038 1.00 120.13 ? 3913 GLU A CD    1 
ATOM   16138 O OE1   . GLU A 1 3913 ? 176.624 140.384 185.971 1.00 120.13 ? 3913 GLU A OE1   1 
ATOM   16139 O OE2   . GLU A 1 3913 ? 178.114 139.297 187.159 1.00 120.13 ? 3913 GLU A OE2   1 
ATOM   16140 N N     . ILE A 1 3914 ? 173.799 139.153 191.589 1.00 126.46 ? 3914 ILE A N     1 
ATOM   16141 C CA    . ILE A 1 3914 ? 172.563 139.110 192.358 1.00 126.46 ? 3914 ILE A CA    1 
ATOM   16142 C C     . ILE A 1 3914 ? 172.850 139.709 193.726 1.00 126.46 ? 3914 ILE A C     1 
ATOM   16143 O O     . ILE A 1 3914 ? 173.922 139.497 194.300 1.00 126.46 ? 3914 ILE A O     1 
ATOM   16144 C CB    . ILE A 1 3914 ? 172.007 137.676 192.496 1.00 126.46 ? 3914 ILE A CB    1 
ATOM   16145 C CG1   . ILE A 1 3914 ? 172.015 136.959 191.145 1.00 126.46 ? 3914 ILE A CG1   1 
ATOM   16146 C CG2   . ILE A 1 3914 ? 170.601 137.697 193.077 1.00 126.46 ? 3914 ILE A CG2   1 
ATOM   16147 C CD1   . ILE A 1 3914 ? 171.194 137.643 190.080 1.00 126.46 ? 3914 ILE A CD1   1 
ATOM   16148 N N     . VAL A 1 3915 ? 171.890 140.469 194.249 1.00 130.40 ? 3915 VAL A N     1 
ATOM   16149 C CA    . VAL A 1 3915 ? 172.087 141.137 195.532 1.00 130.40 ? 3915 VAL A CA    1 
ATOM   16150 C C     . VAL A 1 3915 ? 172.186 140.074 196.628 1.00 130.40 ? 3915 VAL A C     1 
ATOM   16151 O O     . VAL A 1 3915 ? 171.249 139.310 196.873 1.00 130.40 ? 3915 VAL A O     1 
ATOM   16152 C CB    . VAL A 1 3915 ? 170.989 142.176 195.810 1.00 130.40 ? 3915 VAL A CB    1 
ATOM   16153 C CG1   . VAL A 1 3915 ? 169.639 141.547 196.164 1.00 130.40 ? 3915 VAL A CG1   1 
ATOM   16154 C CG2   . VAL A 1 3915 ? 171.436 143.125 196.911 1.00 130.40 ? 3915 VAL A CG2   1 
ATOM   16155 N N     . LEU A 1 3916 ? 173.372 139.963 197.229 1.00 136.89 ? 3916 LEU A N     1 
ATOM   16156 C CA    . LEU A 1 3916 ? 173.610 138.986 198.283 1.00 136.89 ? 3916 LEU A CA    1 
ATOM   16157 C C     . LEU A 1 3916 ? 174.548 139.531 199.354 1.00 136.89 ? 3916 LEU A C     1 
ATOM   16158 O O     . LEU A 1 3916 ? 175.325 138.774 199.946 1.00 136.89 ? 3916 LEU A O     1 
ATOM   16159 C CB    . LEU A 1 3916 ? 174.162 137.684 197.702 1.00 136.89 ? 3916 LEU A CB    1 
ATOM   16160 C CG    . LEU A 1 3916 ? 173.086 136.683 197.274 1.00 136.89 ? 3916 LEU A CG    1 
ATOM   16161 C CD1   . LEU A 1 3916 ? 173.703 135.405 196.736 1.00 136.89 ? 3916 LEU A CD1   1 
ATOM   16162 C CD2   . LEU A 1 3916 ? 172.151 136.381 198.436 1.00 136.89 ? 3916 LEU A CD2   1 
ATOM   16163 N N     . SER A 1 3917 ? 174.498 140.841 199.611 1.00 143.24 ? 3917 SER A N     1 
ATOM   16164 C CA    . SER A 1 3917 ? 175.424 141.445 200.563 1.00 143.24 ? 3917 SER A CA    1 
ATOM   16165 C C     . SER A 1 3917 ? 175.153 140.995 201.992 1.00 143.24 ? 3917 SER A C     1 
ATOM   16166 O O     . SER A 1 3917 ? 176.072 140.982 202.818 1.00 143.24 ? 3917 SER A O     1 
ATOM   16167 C CB    . SER A 1 3917 ? 175.351 142.968 200.474 1.00 143.24 ? 3917 SER A CB    1 
ATOM   16168 O OG    . SER A 1 3917 ? 174.076 143.436 200.873 1.00 143.24 ? 3917 SER A OG    1 
ATOM   16169 N N     . ALA A 1 3918 ? 173.911 140.631 202.303 1.00 145.03 ? 3918 ALA A N     1 
ATOM   16170 C CA    . ALA A 1 3918 ? 173.559 140.250 203.664 1.00 145.03 ? 3918 ALA A CA    1 
ATOM   16171 C C     . ALA A 1 3918 ? 174.276 138.971 204.076 1.00 145.03 ? 3918 ALA A C     1 
ATOM   16172 O O     . ALA A 1 3918 ? 174.413 138.032 203.286 1.00 145.03 ? 3918 ALA A O     1 
ATOM   16173 C CB    . ALA A 1 3918 ? 172.047 140.067 203.788 1.00 145.03 ? 3918 ALA A CB    1 
ATOM   16174 N N     . GLY A 1 3919 ? 174.729 138.937 205.324 1.00 143.71 ? 3919 GLY A N     1 
ATOM   16175 C CA    . GLY A 1 3919 ? 175.415 137.768 205.848 1.00 143.71 ? 3919 GLY A CA    1 
ATOM   16176 C C     . GLY A 1 3919 ? 176.748 137.480 205.192 1.00 143.71 ? 3919 GLY A C     1 
ATOM   16177 O O     . GLY A 1 3919 ? 177.051 136.317 204.899 1.00 143.71 ? 3919 GLY A O     1 
ATOM   16178 N N     . SER A 1 3920 ? 177.556 138.513 204.954 1.00 144.32 ? 3920 SER A N     1 
ATOM   16179 C CA    . SER A 1 3920 ? 178.856 138.351 204.303 1.00 144.32 ? 3920 SER A CA    1 
ATOM   16180 C C     . SER A 1 3920 ? 179.934 138.238 205.377 1.00 144.32 ? 3920 SER A C     1 
ATOM   16181 O O     . SER A 1 3920 ? 180.693 139.170 205.650 1.00 144.32 ? 3920 SER A O     1 
ATOM   16182 C CB    . SER A 1 3920 ? 179.123 139.511 203.355 1.00 144.32 ? 3920 SER A CB    1 
ATOM   16183 O OG    . SER A 1 3920 ? 179.042 140.750 204.037 1.00 144.32 ? 3920 SER A OG    1 
ATOM   16184 N N     . THR A 1 3921 ? 179.997 137.063 205.996 1.00 148.44 ? 3921 THR A N     1 
ATOM   16185 C CA    . THR A 1 3921 ? 180.976 136.835 207.044 1.00 148.44 ? 3921 THR A CA    1 
ATOM   16186 C C     . THR A 1 3921 ? 182.366 136.634 206.441 1.00 148.44 ? 3921 THR A C     1 
ATOM   16187 O O     . THR A 1 3921 ? 182.500 136.124 205.326 1.00 148.44 ? 3921 THR A O     1 
ATOM   16188 C CB    . THR A 1 3921 ? 180.595 135.617 207.879 1.00 148.44 ? 3921 THR A CB    1 
ATOM   16189 O OG1   . THR A 1 3921 ? 181.142 134.438 207.280 1.00 148.44 ? 3921 THR A OG1   1 
ATOM   16190 C CG2   . THR A 1 3921 ? 179.083 135.481 207.960 1.00 148.44 ? 3921 THR A CG2   1 
ATOM   16191 N N     . PRO A 1 3922 ? 183.418 137.036 207.159 1.00 147.39 ? 3922 PRO A N     1 
ATOM   16192 C CA    . PRO A 1 3922 ? 184.781 136.834 206.638 1.00 147.39 ? 3922 PRO A CA    1 
ATOM   16193 C C     . PRO A 1 3922 ? 185.169 135.375 206.484 1.00 147.39 ? 3922 PRO A C     1 
ATOM   16194 O O     . PRO A 1 3922 ? 186.098 135.080 205.722 1.00 147.39 ? 3922 PRO A O     1 
ATOM   16195 C CB    . PRO A 1 3922 ? 185.664 137.540 207.678 1.00 147.39 ? 3922 PRO A CB    1 
ATOM   16196 C CG    . PRO A 1 3922 ? 184.831 137.592 208.917 1.00 147.39 ? 3922 PRO A CG    1 
ATOM   16197 C CD    . PRO A 1 3922 ? 183.416 137.741 208.452 1.00 147.39 ? 3922 PRO A CD    1 
ATOM   16198 N N     . ARG A 1 3923 ? 184.496 134.461 207.184 1.00 150.10 ? 3923 ARG A N     1 
ATOM   16199 C CA    . ARG A 1 3923 ? 184.793 133.033 207.122 1.00 150.10 ? 3923 ARG A CA    1 
ATOM   16200 C C     . ARG A 1 3923 ? 186.250 132.763 207.482 1.00 150.10 ? 3923 ARG A C     1 
ATOM   16201 O O     . ARG A 1 3923 ? 186.665 132.993 208.622 1.00 150.10 ? 3923 ARG A O     1 
ATOM   16202 C CB    . ARG A 1 3923 ? 184.471 132.470 205.736 1.00 150.10 ? 3923 ARG A CB    1 
ATOM   16203 C CG    . ARG A 1 3923 ? 183.156 132.962 205.146 1.00 150.10 ? 3923 ARG A CG    1 
ATOM   16204 C CD    . ARG A 1 3923 ? 181.997 132.030 205.468 1.00 150.10 ? 3923 ARG A CD    1 
ATOM   16205 N NE    . ARG A 1 3923 ? 180.744 132.756 205.653 1.00 150.10 ? 3923 ARG A NE    1 
ATOM   16206 C CZ    . ARG A 1 3923 ? 180.042 133.313 204.674 1.00 150.10 ? 3923 ARG A CZ    1 
ATOM   16207 N NH1   . ARG A 1 3923 ? 180.434 133.240 203.413 1.00 150.10 ? 3923 ARG A NH1   1 
ATOM   16208 N NH2   . ARG A 1 3923 ? 178.919 133.962 204.969 1.00 150.10 ? 3923 ARG A NH2   1 
ATOM   16209 N N     . ILE A 1 3924 ? 187.031 132.281 206.521 1.00 149.00 ? 3924 ILE A N     1 
ATOM   16210 C CA    . ILE A 1 3924 ? 188.423 131.938 206.758 1.00 149.00 ? 3924 ILE A CA    1 
ATOM   16211 C C     . ILE A 1 3924 ? 189.286 133.159 206.467 1.00 149.00 ? 3924 ILE A C     1 
ATOM   16212 O O     . ILE A 1 3924 ? 188.979 133.985 205.602 1.00 149.00 ? 3924 ILE A O     1 
ATOM   16213 C CB    . ILE A 1 3924 ? 188.864 130.715 205.916 1.00 149.00 ? 3924 ILE A CB    1 
ATOM   16214 C CG1   . ILE A 1 3924 ? 190.272 130.261 206.305 1.00 149.00 ? 3924 ILE A CG1   1 
ATOM   16215 C CG2   . ILE A 1 3924 ? 188.800 131.025 204.436 1.00 149.00 ? 3924 ILE A CG2   1 
ATOM   16216 C CD1   . ILE A 1 3924 ? 190.394 129.851 207.754 1.00 149.00 ? 3924 ILE A CD1   1 
ATOM   16217 N N     . GLN A 1 3925 ? 190.387 133.280 207.216 1.00 149.40 ? 3925 GLN A N     1 
ATOM   16218 C CA    . GLN A 1 3925 ? 191.254 134.448 207.099 1.00 149.40 ? 3925 GLN A CA    1 
ATOM   16219 C C     . GLN A 1 3925 ? 191.878 134.562 205.714 1.00 149.40 ? 3925 GLN A C     1 
ATOM   16220 O O     . GLN A 1 3925 ? 192.195 135.672 205.271 1.00 149.40 ? 3925 GLN A O     1 
ATOM   16221 C CB    . GLN A 1 3925 ? 192.344 134.398 208.169 1.00 149.40 ? 3925 GLN A CB    1 
ATOM   16222 C CG    . GLN A 1 3925 ? 193.299 133.225 208.019 1.00 149.40 ? 3925 GLN A CG    1 
ATOM   16223 C CD    . GLN A 1 3925 ? 192.869 132.017 208.828 1.00 149.40 ? 3925 GLN A CD    1 
ATOM   16224 O OE1   . GLN A 1 3925 ? 191.910 132.081 209.597 1.00 149.40 ? 3925 GLN A OE1   1 
ATOM   16225 N NE2   . GLN A 1 3925 ? 193.574 130.905 208.652 1.00 149.40 ? 3925 GLN A NE2   1 
ATOM   16226 N N     . GLY A 1 3926 ? 192.058 133.442 205.015 1.00 141.69 ? 3926 GLY A N     1 
ATOM   16227 C CA    . GLY A 1 3926 ? 192.617 133.489 203.675 1.00 141.69 ? 3926 GLY A CA    1 
ATOM   16228 C C     . GLY A 1 3926 ? 191.651 133.970 202.619 1.00 141.69 ? 3926 GLY A C     1 
ATOM   16229 O O     . GLY A 1 3926 ? 192.049 134.129 201.460 1.00 141.69 ? 3926 GLY A O     1 
ATOM   16230 N N     . LEU A 1 3927 ? 190.398 134.200 202.993 1.00 140.09 ? 3927 LEU A N     1 
ATOM   16231 C CA    . LEU A 1 3927 ? 189.354 134.579 202.056 1.00 140.09 ? 3927 LEU A CA    1 
ATOM   16232 C C     . LEU A 1 3927 ? 189.043 136.066 202.201 1.00 140.09 ? 3927 LEU A C     1 
ATOM   16233 O O     . LEU A 1 3927 ? 188.740 136.537 203.301 1.00 140.09 ? 3927 LEU A O     1 
ATOM   16234 C CB    . LEU A 1 3927 ? 188.110 133.734 202.320 1.00 140.09 ? 3927 LEU A CB    1 
ATOM   16235 C CG    . LEU A 1 3927 ? 186.735 134.292 201.995 1.00 140.09 ? 3927 LEU A CG    1 
ATOM   16236 C CD1   . LEU A 1 3927 ? 186.594 134.281 200.515 1.00 140.09 ? 3927 LEU A CD1   1 
ATOM   16237 C CD2   . LEU A 1 3927 ? 185.667 133.439 202.625 1.00 140.09 ? 3927 LEU A CD2   1 
ATOM   16238 N N     . THR A 1 3928 ? 189.115 136.797 201.091 1.00 137.77 ? 3928 THR A N     1 
ATOM   16239 C CA    . THR A 1 3928 ? 188.889 138.235 201.093 1.00 137.77 ? 3928 THR A CA    1 
ATOM   16240 C C     . THR A 1 3928 ? 187.397 138.551 201.020 1.00 137.77 ? 3928 THR A C     1 
ATOM   16241 O O     . THR A 1 3928 ? 186.552 137.667 200.877 1.00 137.77 ? 3928 THR A O     1 
ATOM   16242 C CB    . THR A 1 3928 ? 189.622 138.904 199.931 1.00 137.77 ? 3928 THR A CB    1 
ATOM   16243 O OG1   . THR A 1 3928 ? 189.508 138.088 198.760 1.00 137.77 ? 3928 THR A OG1   1 
ATOM   16244 C CG2   . THR A 1 3928 ? 191.090 139.095 200.265 1.00 137.77 ? 3928 THR A CG2   1 
ATOM   16245 N N     . VAL A 1 3929 ? 187.080 139.844 201.116 1.00 138.33 ? 3929 VAL A N     1 
ATOM   16246 C CA    . VAL A 1 3929 ? 185.682 140.264 201.172 1.00 138.33 ? 3929 VAL A CA    1 
ATOM   16247 C C     . VAL A 1 3929 ? 184.983 140.010 199.840 1.00 138.33 ? 3929 VAL A C     1 
ATOM   16248 O O     . VAL A 1 3929 ? 183.887 139.441 199.800 1.00 138.33 ? 3929 VAL A O     1 
ATOM   16249 C CB    . VAL A 1 3929 ? 185.578 141.739 201.605 1.00 138.33 ? 3929 VAL A CB    1 
ATOM   16250 C CG1   . VAL A 1 3929 ? 186.465 142.626 200.746 1.00 138.33 ? 3929 VAL A CG1   1 
ATOM   16251 C CG2   . VAL A 1 3929 ? 184.132 142.207 201.544 1.00 138.33 ? 3929 VAL A CG2   1 
ATOM   16252 N N     . GLU A 1 3930 ? 185.602 140.420 198.729 1.00 141.21 ? 3930 GLU A N     1 
ATOM   16253 C CA    . GLU A 1 3930 ? 184.974 140.209 197.427 1.00 141.21 ? 3930 GLU A CA    1 
ATOM   16254 C C     . GLU A 1 3930 ? 184.908 138.726 197.090 1.00 141.21 ? 3930 GLU A C     1 
ATOM   16255 O O     . GLU A 1 3930 ? 183.916 138.250 196.521 1.00 141.21 ? 3930 GLU A O     1 
ATOM   16256 C CB    . GLU A 1 3930 ? 185.721 140.992 196.342 1.00 141.21 ? 3930 GLU A CB    1 
ATOM   16257 C CG    . GLU A 1 3930 ? 187.084 140.436 195.946 1.00 141.21 ? 3930 GLU A CG    1 
ATOM   16258 C CD    . GLU A 1 3930 ? 188.155 140.677 196.993 1.00 141.21 ? 3930 GLU A CD    1 
ATOM   16259 O OE1   . GLU A 1 3930 ? 187.881 141.388 197.982 1.00 141.21 ? 3930 GLU A OE1   1 
ATOM   16260 O OE2   . GLU A 1 3930 ? 189.277 140.154 196.825 1.00 141.21 ? 3930 GLU A OE2   1 
ATOM   16261 N N     . GLN A 1 3931 ? 185.946 137.975 197.456 1.00 134.61 ? 3931 GLN A N     1 
ATOM   16262 C CA    . GLN A 1 3931 ? 185.893 136.529 197.302 1.00 134.61 ? 3931 GLN A CA    1 
ATOM   16263 C C     . GLN A 1 3931 ? 184.808 135.936 198.190 1.00 134.61 ? 3931 GLN A C     1 
ATOM   16264 O O     . GLN A 1 3931 ? 184.165 134.948 197.822 1.00 134.61 ? 3931 GLN A O     1 
ATOM   16265 C CB    . GLN A 1 3931 ? 187.257 135.922 197.625 1.00 134.61 ? 3931 GLN A CB    1 
ATOM   16266 C CG    . GLN A 1 3931 ? 188.183 135.749 196.434 1.00 134.61 ? 3931 GLN A CG    1 
ATOM   16267 C CD    . GLN A 1 3931 ? 189.648 135.813 196.827 1.00 134.61 ? 3931 GLN A CD    1 
ATOM   16268 O OE1   . GLN A 1 3931 ? 189.980 135.993 197.998 1.00 134.61 ? 3931 GLN A OE1   1 
ATOM   16269 N NE2   . GLN A 1 3931 ? 190.531 135.667 195.848 1.00 134.61 ? 3931 GLN A NE2   1 
ATOM   16270 N N     . ALA A 1 3932 ? 184.588 136.529 199.366 1.00 133.87 ? 3932 ALA A N     1 
ATOM   16271 C CA    . ALA A 1 3932 ? 183.505 136.071 200.229 1.00 133.87 ? 3932 ALA A CA    1 
ATOM   16272 C C     . ALA A 1 3932 ? 182.150 136.287 199.573 1.00 133.87 ? 3932 ALA A C     1 
ATOM   16273 O O     . ALA A 1 3932 ? 181.274 135.417 199.640 1.00 133.87 ? 3932 ALA A O     1 
ATOM   16274 C CB    . ALA A 1 3932 ? 183.568 136.783 201.579 1.00 133.87 ? 3932 ALA A CB    1 
ATOM   16275 N N     . GLU A 1 3933 ? 181.956 137.443 198.936 1.00 133.54 ? 3933 GLU A N     1 
ATOM   16276 C CA    . GLU A 1 3933 ? 180.709 137.671 198.212 1.00 133.54 ? 3933 GLU A CA    1 
ATOM   16277 C C     . GLU A 1 3933 ? 180.553 136.670 197.077 1.00 133.54 ? 3933 GLU A C     1 
ATOM   16278 O O     . GLU A 1 3933 ? 179.459 136.139 196.853 1.00 133.54 ? 3933 GLU A O     1 
ATOM   16279 C CB    . GLU A 1 3933 ? 180.651 139.100 197.672 1.00 133.54 ? 3933 GLU A CB    1 
ATOM   16280 C CG    . GLU A 1 3933 ? 181.150 140.171 198.627 1.00 133.54 ? 3933 GLU A CG    1 
ATOM   16281 C CD    . GLU A 1 3933 ? 180.494 140.114 199.991 1.00 133.54 ? 3933 GLU A CD    1 
ATOM   16282 O OE1   . GLU A 1 3933 ? 181.163 140.482 200.979 1.00 133.54 ? 3933 GLU A OE1   1 
ATOM   16283 O OE2   . GLU A 1 3933 ? 179.309 139.728 200.078 1.00 133.54 ? 3933 GLU A OE2   1 
ATOM   16284 N N     . ALA A 1 3934 ? 181.640 136.398 196.351 1.00 129.79 ? 3934 ALA A N     1 
ATOM   16285 C CA    . ALA A 1 3934 ? 181.579 135.415 195.274 1.00 129.79 ? 3934 ALA A CA    1 
ATOM   16286 C C     . ALA A 1 3934 ? 181.194 134.040 195.805 1.00 129.79 ? 3934 ALA A C     1 
ATOM   16287 O O     . ALA A 1 3934 ? 180.396 133.327 195.187 1.00 129.79 ? 3934 ALA A O     1 
ATOM   16288 C CB    . ALA A 1 3934 ? 182.919 135.350 194.545 1.00 129.79 ? 3934 ALA A CB    1 
ATOM   16289 N N     . VAL A 1 3935 ? 181.753 133.654 196.952 1.00 127.84 ? 3935 VAL A N     1 
ATOM   16290 C CA    . VAL A 1 3935 ? 181.418 132.369 197.559 1.00 127.84 ? 3935 VAL A CA    1 
ATOM   16291 C C     . VAL A 1 3935 ? 179.950 132.337 197.955 1.00 127.84 ? 3935 VAL A C     1 
ATOM   16292 O O     . VAL A 1 3935 ? 179.255 131.335 197.747 1.00 127.84 ? 3935 VAL A O     1 
ATOM   16293 C CB    . VAL A 1 3935 ? 182.327 132.102 198.769 1.00 127.84 ? 3935 VAL A CB    1 
ATOM   16294 C CG1   . VAL A 1 3935 ? 181.760 130.987 199.620 1.00 127.84 ? 3935 VAL A CG1   1 
ATOM   16295 C CG2   . VAL A 1 3935 ? 183.713 131.769 198.310 1.00 127.84 ? 3935 VAL A CG2   1 
ATOM   16296 N N     . VAL A 1 3936 ? 179.459 133.429 198.540 1.00 125.95 ? 3936 VAL A N     1 
ATOM   16297 C CA    . VAL A 1 3936 ? 178.057 133.492 198.935 1.00 125.95 ? 3936 VAL A CA    1 
ATOM   16298 C C     . VAL A 1 3936 ? 177.159 133.319 197.720 1.00 125.95 ? 3936 VAL A C     1 
ATOM   16299 O O     . VAL A 1 3936 ? 176.169 132.578 197.762 1.00 125.95 ? 3936 VAL A O     1 
ATOM   16300 C CB    . VAL A 1 3936 ? 177.768 134.813 199.669 1.00 125.95 ? 3936 VAL A CB    1 
ATOM   16301 C CG1   . VAL A 1 3936 ? 176.271 135.011 199.833 1.00 125.95 ? 3936 VAL A CG1   1 
ATOM   16302 C CG2   . VAL A 1 3936 ? 178.462 134.827 201.017 1.00 125.95 ? 3936 VAL A CG2   1 
ATOM   16303 N N     . ARG A 1 3937 ? 177.493 133.990 196.617 1.00 125.92 ? 3937 ARG A N     1 
ATOM   16304 C CA    . ARG A 1 3937 ? 176.693 133.848 195.404 1.00 125.92 ? 3937 ARG A CA    1 
ATOM   16305 C C     . ARG A 1 3937 ? 176.767 132.429 194.855 1.00 125.92 ? 3937 ARG A C     1 
ATOM   16306 O O     . ARG A 1 3937 ? 175.762 131.885 194.386 1.00 125.92 ? 3937 ARG A O     1 
ATOM   16307 C CB    . ARG A 1 3937 ? 177.141 134.855 194.348 1.00 125.92 ? 3937 ARG A CB    1 
ATOM   16308 C CG    . ARG A 1 3937 ? 177.244 136.276 194.857 1.00 125.92 ? 3937 ARG A CG    1 
ATOM   16309 C CD    . ARG A 1 3937 ? 176.049 137.119 194.465 1.00 125.92 ? 3937 ARG A CD    1 
ATOM   16310 N NE    . ARG A 1 3937 ? 176.148 138.468 195.011 1.00 125.92 ? 3937 ARG A NE    1 
ATOM   16311 C CZ    . ARG A 1 3937 ? 176.973 139.404 194.560 1.00 125.92 ? 3937 ARG A CZ    1 
ATOM   16312 N NH1   . ARG A 1 3937 ? 177.774 139.183 193.530 1.00 125.92 ? 3937 ARG A NH1   1 
ATOM   16313 N NH2   . ARG A 1 3937 ? 176.993 140.593 195.155 1.00 125.92 ? 3937 ARG A NH2   1 
ATOM   16314 N N     . LEU A 1 3938 ? 177.950 131.815 194.904 1.00 125.82 ? 3938 LEU A N     1 
ATOM   16315 C CA    . LEU A 1 3938 ? 178.094 130.453 194.399 1.00 125.82 ? 3938 LEU A CA    1 
ATOM   16316 C C     . LEU A 1 3938 ? 177.288 129.466 195.232 1.00 125.82 ? 3938 LEU A C     1 
ATOM   16317 O O     . LEU A 1 3938 ? 176.759 128.483 194.700 1.00 125.82 ? 3938 LEU A O     1 
ATOM   16318 C CB    . LEU A 1 3938 ? 179.567 130.051 194.377 1.00 125.82 ? 3938 LEU A CB    1 
ATOM   16319 C CG    . LEU A 1 3938 ? 180.262 130.089 193.015 1.00 125.82 ? 3938 LEU A CG    1 
ATOM   16320 C CD1   . LEU A 1 3938 ? 179.894 128.864 192.197 1.00 125.82 ? 3938 LEU A CD1   1 
ATOM   16321 C CD2   . LEU A 1 3938 ? 179.930 131.365 192.261 1.00 125.82 ? 3938 LEU A CD2   1 
ATOM   16322 N N     . SER A 1 3939 ? 177.183 129.709 196.540 1.00 127.74 ? 3939 SER A N     1 
ATOM   16323 C CA    . SER A 1 3939 ? 176.442 128.812 197.418 1.00 127.74 ? 3939 SER A CA    1 
ATOM   16324 C C     . SER A 1 3939 ? 174.958 128.763 197.094 1.00 127.74 ? 3939 SER A C     1 
ATOM   16325 O O     . SER A 1 3939 ? 174.272 127.849 197.562 1.00 127.74 ? 3939 SER A O     1 
ATOM   16326 C CB    . SER A 1 3939 ? 176.629 129.224 198.878 1.00 127.74 ? 3939 SER A CB    1 
ATOM   16327 O OG    . SER A 1 3939 ? 176.616 130.632 199.013 1.00 127.74 ? 3939 SER A OG    1 
ATOM   16328 N N     . CYS A 1 3940 ? 174.450 129.720 196.315 1.00 127.39 ? 3940 CYS A N     1 
ATOM   16329 C CA    . CYS A 1 3940 ? 173.051 129.681 195.908 1.00 127.39 ? 3940 CYS A CA    1 
ATOM   16330 C C     . CYS A 1 3940 ? 172.733 128.417 195.121 1.00 127.39 ? 3940 CYS A C     1 
ATOM   16331 O O     . CYS A 1 3940 ? 171.622 127.885 195.225 1.00 127.39 ? 3940 CYS A O     1 
ATOM   16332 C CB    . CYS A 1 3940 ? 172.716 130.924 195.085 1.00 127.39 ? 3940 CYS A CB    1 
ATOM   16333 S SG    . CYS A 1 3940 ? 171.236 130.781 194.063 1.00 127.39 ? 3940 CYS A SG    1 
ATOM   16334 N N     . LEU A 1 3941 ? 173.688 127.922 194.342 1.00 127.83 ? 3941 LEU A N     1 
ATOM   16335 C CA    . LEU A 1 3941 ? 173.469 126.698 193.587 1.00 127.83 ? 3941 LEU A CA    1 
ATOM   16336 C C     . LEU A 1 3941 ? 173.357 125.504 194.533 1.00 127.83 ? 3941 LEU A C     1 
ATOM   16337 O O     . LEU A 1 3941 ? 174.054 125.450 195.552 1.00 127.83 ? 3941 LEU A O     1 
ATOM   16338 C CB    . LEU A 1 3941 ? 174.605 126.470 192.592 1.00 127.83 ? 3941 LEU A CB    1 
ATOM   16339 C CG    . LEU A 1 3941 ? 174.279 126.827 191.143 1.00 127.83 ? 3941 LEU A CG    1 
ATOM   16340 C CD1   . LEU A 1 3941 ? 173.979 128.310 191.023 1.00 127.83 ? 3941 LEU A CD1   1 
ATOM   16341 C CD2   . LEU A 1 3941 ? 175.419 126.430 190.221 1.00 127.83 ? 3941 LEU A CD2   1 
ATOM   16342 N N     . PRO A 1 3942 ? 172.488 124.537 194.228 1.00 124.89 ? 3942 PRO A N     1 
ATOM   16343 C CA    . PRO A 1 3942 ? 172.354 123.370 195.114 1.00 124.89 ? 3942 PRO A CA    1 
ATOM   16344 C C     . PRO A 1 3942 ? 173.635 122.572 195.260 1.00 124.89 ? 3942 PRO A C     1 
ATOM   16345 O O     . PRO A 1 3942 ? 173.909 122.050 196.347 1.00 124.89 ? 3942 PRO A O     1 
ATOM   16346 C CB    . PRO A 1 3942 ? 171.251 122.545 194.437 1.00 124.89 ? 3942 PRO A CB    1 
ATOM   16347 C CG    . PRO A 1 3942 ? 171.294 122.964 193.004 1.00 124.89 ? 3942 PRO A CG    1 
ATOM   16348 C CD    . PRO A 1 3942 ? 171.647 124.420 193.025 1.00 124.89 ? 3942 PRO A CD    1 
ATOM   16349 N N     . ALA A 1 3943 ? 174.434 122.466 194.199 1.00 121.17 ? 3943 ALA A N     1 
ATOM   16350 C CA    . ALA A 1 3943 ? 175.672 121.702 194.275 1.00 121.17 ? 3943 ALA A CA    1 
ATOM   16351 C C     . ALA A 1 3943 ? 176.740 122.397 195.104 1.00 121.17 ? 3943 ALA A C     1 
ATOM   16352 O O     . ALA A 1 3943 ? 177.736 121.758 195.460 1.00 121.17 ? 3943 ALA A O     1 
ATOM   16353 C CB    . ALA A 1 3943 ? 176.205 121.428 192.868 1.00 121.17 ? 3943 ALA A CB    1 
ATOM   16354 N N     . PHE A 1 3944 ? 176.559 123.678 195.423 1.00 123.61 ? 3944 PHE A N     1 
ATOM   16355 C CA    . PHE A 1 3944 ? 177.533 124.433 196.200 1.00 123.61 ? 3944 PHE A CA    1 
ATOM   16356 C C     . PHE A 1 3944 ? 176.960 124.922 197.524 1.00 123.61 ? 3944 PHE A C     1 
ATOM   16357 O O     . PHE A 1 3944 ? 177.537 125.817 198.149 1.00 123.61 ? 3944 PHE A O     1 
ATOM   16358 C CB    . PHE A 1 3944 ? 178.065 125.618 195.392 1.00 123.61 ? 3944 PHE A CB    1 
ATOM   16359 C CG    . PHE A 1 3944 ? 178.926 125.226 194.226 1.00 123.61 ? 3944 PHE A CG    1 
ATOM   16360 C CD1   . PHE A 1 3944 ? 178.365 124.955 192.992 1.00 123.61 ? 3944 PHE A CD1   1 
ATOM   16361 C CD2   . PHE A 1 3944 ? 180.299 125.137 194.364 1.00 123.61 ? 3944 PHE A CD2   1 
ATOM   16362 C CE1   . PHE A 1 3944 ? 179.157 124.598 191.921 1.00 123.61 ? 3944 PHE A CE1   1 
ATOM   16363 C CE2   . PHE A 1 3944 ? 181.094 124.780 193.298 1.00 123.61 ? 3944 PHE A CE2   1 
ATOM   16364 C CZ    . PHE A 1 3944 ? 180.522 124.510 192.074 1.00 123.61 ? 3944 PHE A CZ    1 
ATOM   16365 N N     . LYS A 1 3945 ? 175.835 124.361 197.969 1.00 126.38 ? 3945 LYS A N     1 
ATOM   16366 C CA    . LYS A 1 3945 ? 175.271 124.796 199.241 1.00 126.38 ? 3945 LYS A CA    1 
ATOM   16367 C C     . LYS A 1 3945 ? 176.198 124.466 200.403 1.00 126.38 ? 3945 LYS A C     1 
ATOM   16368 O O     . LYS A 1 3945 ? 176.176 125.156 201.428 1.00 126.38 ? 3945 LYS A O     1 
ATOM   16369 C CB    . LYS A 1 3945 ? 173.894 124.167 199.454 1.00 126.38 ? 3945 LYS A CB    1 
ATOM   16370 C CG    . LYS A 1 3945 ? 173.915 122.668 199.692 1.00 126.38 ? 3945 LYS A CG    1 
ATOM   16371 C CD    . LYS A 1 3945 ? 172.772 122.239 200.596 1.00 126.38 ? 3945 LYS A CD    1 
ATOM   16372 C CE    . LYS A 1 3945 ? 172.732 120.729 200.751 1.00 126.38 ? 3945 LYS A CE    1 
ATOM   16373 N NZ    . LYS A 1 3945 ? 172.011 120.077 199.623 1.00 126.38 ? 3945 LYS A NZ    1 
ATOM   16374 N N     . ASP A 1 3946 ? 177.027 123.432 200.260 1.00 130.40 ? 3946 ASP A N     1 
ATOM   16375 C CA    . ASP A 1 3946 ? 177.976 123.035 201.292 1.00 130.40 ? 3946 ASP A CA    1 
ATOM   16376 C C     . ASP A 1 3946 ? 179.352 123.650 201.075 1.00 130.40 ? 3946 ASP A C     1 
ATOM   16377 O O     . ASP A 1 3946 ? 180.352 123.132 201.582 1.00 130.40 ? 3946 ASP A O     1 
ATOM   16378 C CB    . ASP A 1 3946 ? 178.082 121.512 201.358 1.00 130.40 ? 3946 ASP A CB    1 
ATOM   16379 C CG    . ASP A 1 3946 ? 176.736 120.828 201.238 1.00 130.40 ? 3946 ASP A CG    1 
ATOM   16380 O OD1   . ASP A 1 3946 ? 176.328 120.513 200.102 1.00 130.40 ? 3946 ASP A OD1   1 
ATOM   16381 O OD2   . ASP A 1 3946 ? 176.085 120.606 202.281 1.00 130.40 ? 3946 ASP A OD2   1 
ATOM   16382 N N     . LEU A 1 3947 ? 179.419 124.753 200.327 1.00 130.27 ? 3947 LEU A N     1 
ATOM   16383 C CA    . LEU A 1 3947 ? 180.709 125.364 200.025 1.00 130.27 ? 3947 LEU A CA    1 
ATOM   16384 C C     . LEU A 1 3947 ? 181.382 125.896 201.283 1.00 130.27 ? 3947 LEU A C     1 
ATOM   16385 O O     . LEU A 1 3947 ? 182.601 125.766 201.443 1.00 130.27 ? 3947 LEU A O     1 
ATOM   16386 C CB    . LEU A 1 3947 ? 180.530 126.483 199.000 1.00 130.27 ? 3947 LEU A CB    1 
ATOM   16387 C CG    . LEU A 1 3947 ? 181.794 126.938 198.273 1.00 130.27 ? 3947 LEU A CG    1 
ATOM   16388 C CD1   . LEU A 1 3947 ? 182.475 125.757 197.608 1.00 130.27 ? 3947 LEU A CD1   1 
ATOM   16389 C CD2   . LEU A 1 3947 ? 181.460 128.011 197.253 1.00 130.27 ? 3947 LEU A CD2   1 
ATOM   16390 N N     . ILE A 1 3948 ? 180.606 126.503 202.184 1.00 137.48 ? 3948 ILE A N     1 
ATOM   16391 C CA    . ILE A 1 3948 ? 181.182 127.094 203.390 1.00 137.48 ? 3948 ILE A CA    1 
ATOM   16392 C C     . ILE A 1 3948 ? 181.828 126.021 204.256 1.00 137.48 ? 3948 ILE A C     1 
ATOM   16393 O O     . ILE A 1 3948 ? 182.983 126.150 204.682 1.00 137.48 ? 3948 ILE A O     1 
ATOM   16394 C CB    . ILE A 1 3948 ? 180.108 127.868 204.172 1.00 137.48 ? 3948 ILE A CB    1 
ATOM   16395 C CG1   . ILE A 1 3948 ? 179.403 128.868 203.258 1.00 137.48 ? 3948 ILE A CG1   1 
ATOM   16396 C CG2   . ILE A 1 3948 ? 180.727 128.571 205.369 1.00 137.48 ? 3948 ILE A CG2   1 
ATOM   16397 C CD1   . ILE A 1 3948 ? 180.324 129.914 202.697 1.00 137.48 ? 3948 ILE A CD1   1 
ATOM   16398 N N     . ALA A 1 3949 ? 181.090 124.947 204.537 1.00 140.04 ? 3949 ALA A N     1 
ATOM   16399 C CA    . ALA A 1 3949 ? 181.647 123.882 205.360 1.00 140.04 ? 3949 ALA A CA    1 
ATOM   16400 C C     . ALA A 1 3949 ? 182.871 123.272 204.696 1.00 140.04 ? 3949 ALA A C     1 
ATOM   16401 O O     . ALA A 1 3949 ? 183.874 122.987 205.361 1.00 140.04 ? 3949 ALA A O     1 
ATOM   16402 C CB    . ALA A 1 3949 ? 180.586 122.815 205.626 1.00 140.04 ? 3949 ALA A CB    1 
ATOM   16403 N N     . LYS A 1 3950 ? 182.815 123.093 203.376 1.00 134.69 ? 3950 LYS A N     1 
ATOM   16404 C CA    . LYS A 1 3950 ? 183.940 122.512 202.658 1.00 134.69 ? 3950 LYS A CA    1 
ATOM   16405 C C     . LYS A 1 3950 ? 185.179 123.389 202.781 1.00 134.69 ? 3950 LYS A C     1 
ATOM   16406 O O     . LYS A 1 3950 ? 186.284 122.890 203.022 1.00 134.69 ? 3950 LYS A O     1 
ATOM   16407 C CB    . LYS A 1 3950 ? 183.566 122.308 201.192 1.00 134.69 ? 3950 LYS A CB    1 
ATOM   16408 C CG    . LYS A 1 3950 ? 182.788 121.032 200.915 1.00 134.69 ? 3950 LYS A CG    1 
ATOM   16409 C CD    . LYS A 1 3950 ? 183.689 119.921 200.407 1.00 134.69 ? 3950 LYS A CD    1 
ATOM   16410 C CE    . LYS A 1 3950 ? 182.870 118.765 199.858 1.00 134.69 ? 3950 LYS A CE    1 
ATOM   16411 N NZ    . LYS A 1 3950 ? 183.728 117.626 199.437 1.00 134.69 ? 3950 LYS A NZ    1 
ATOM   16412 N N     . VAL A 1 3951 ? 185.016 124.704 202.626 1.00 136.33 ? 3951 VAL A N     1 
ATOM   16413 C CA    . VAL A 1 3951 ? 186.184 125.579 202.615 1.00 136.33 ? 3951 VAL A CA    1 
ATOM   16414 C C     . VAL A 1 3951 ? 186.766 125.726 204.017 1.00 136.33 ? 3951 VAL A C     1 
ATOM   16415 O O     . VAL A 1 3951 ? 187.991 125.752 204.187 1.00 136.33 ? 3951 VAL A O     1 
ATOM   16416 C CB    . VAL A 1 3951 ? 185.853 126.943 201.978 1.00 136.33 ? 3951 VAL A CB    1 
ATOM   16417 C CG1   . VAL A 1 3951 ? 184.749 127.657 202.726 1.00 136.33 ? 3951 VAL A CG1   1 
ATOM   16418 C CG2   . VAL A 1 3951 ? 187.100 127.807 201.912 1.00 136.33 ? 3951 VAL A CG2   1 
ATOM   16419 N N     . GLN A 1 3952 ? 185.916 125.820 205.046 1.00 141.57 ? 3952 GLN A N     1 
ATOM   16420 C CA    . GLN A 1 3952 ? 186.464 125.889 206.400 1.00 141.57 ? 3952 GLN A CA    1 
ATOM   16421 C C     . GLN A 1 3952 ? 187.079 124.560 206.821 1.00 141.57 ? 3952 GLN A C     1 
ATOM   16422 O O     . GLN A 1 3952 ? 187.986 124.530 207.661 1.00 141.57 ? 3952 GLN A O     1 
ATOM   16423 C CB    . GLN A 1 3952 ? 185.407 126.333 207.413 1.00 141.57 ? 3952 GLN A CB    1 
ATOM   16424 C CG    . GLN A 1 3952 ? 184.417 127.358 206.910 1.00 141.57 ? 3952 GLN A CG    1 
ATOM   16425 C CD    . GLN A 1 3952 ? 185.001 128.754 206.843 1.00 141.57 ? 3952 GLN A CD    1 
ATOM   16426 O OE1   . GLN A 1 3952 ? 185.655 129.119 205.867 1.00 141.57 ? 3952 GLN A OE1   1 
ATOM   16427 N NE2   . GLN A 1 3952 ? 184.766 129.544 207.884 1.00 141.57 ? 3952 GLN A NE2   1 
ATOM   16428 N N     . ALA A 1 3953 ? 186.603 123.450 206.253 1.00 141.29 ? 3953 ALA A N     1 
ATOM   16429 C CA    . ALA A 1 3953 ? 187.184 122.154 206.587 1.00 141.29 ? 3953 ALA A CA    1 
ATOM   16430 C C     . ALA A 1 3953 ? 188.571 121.988 205.977 1.00 141.29 ? 3953 ALA A C     1 
ATOM   16431 O O     . ALA A 1 3953 ? 189.465 121.408 206.603 1.00 141.29 ? 3953 ALA A O     1 
ATOM   16432 C CB    . ALA A 1 3953 ? 186.258 121.031 206.125 1.00 141.29 ? 3953 ALA A CB    1 
ATOM   16433 N N     . ASP A 1 3954 ? 188.769 122.487 204.759 1.00 146.37 ? 3954 ASP A N     1 
ATOM   16434 C CA    . ASP A 1 3954 ? 190.020 122.264 204.047 1.00 146.37 ? 3954 ASP A CA    1 
ATOM   16435 C C     . ASP A 1 3954 ? 191.168 123.043 204.678 1.00 146.37 ? 3954 ASP A C     1 
ATOM   16436 O O     . ASP A 1 3954 ? 190.982 124.144 205.203 1.00 146.37 ? 3954 ASP A O     1 
ATOM   16437 C CB    . ASP A 1 3954 ? 189.873 122.656 202.579 1.00 146.37 ? 3954 ASP A CB    1 
ATOM   16438 C CG    . ASP A 1 3954 ? 191.037 122.183 201.731 1.00 146.37 ? 3954 ASP A CG    1 
ATOM   16439 O OD1   . ASP A 1 3954 ? 191.845 121.370 202.228 1.00 146.37 ? 3954 ASP A OD1   1 
ATOM   16440 O OD2   . ASP A 1 3954 ? 191.148 122.627 200.569 1.00 146.37 ? 3954 ASP A OD2   1 
ATOM   16441 N N     . GLU A 1 3955 ? 192.364 122.458 204.617 1.00 143.75 ? 3955 GLU A N     1 
ATOM   16442 C CA    . GLU A 1 3955 ? 193.582 123.089 205.109 1.00 143.75 ? 3955 GLU A CA    1 
ATOM   16443 C C     . GLU A 1 3955 ? 194.562 123.461 204.009 1.00 143.75 ? 3955 GLU A C     1 
ATOM   16444 O O     . GLU A 1 3955 ? 195.372 124.368 204.206 1.00 143.75 ? 3955 GLU A O     1 
ATOM   16445 C CB    . GLU A 1 3955 ? 194.291 122.171 206.113 1.00 143.75 ? 3955 GLU A CB    1 
ATOM   16446 C CG    . GLU A 1 3955 ? 194.841 120.887 205.512 1.00 143.75 ? 3955 GLU A CG    1 
ATOM   16447 C CD    . GLU A 1 3955 ? 193.772 119.835 205.295 1.00 143.75 ? 3955 GLU A CD    1 
ATOM   16448 O OE1   . GLU A 1 3955 ? 192.630 120.040 205.758 1.00 143.75 ? 3955 GLU A OE1   1 
ATOM   16449 O OE2   . GLU A 1 3955 ? 194.073 118.803 204.660 1.00 143.75 ? 3955 GLU A OE2   1 
ATOM   16450 N N     . GLN A 1 3956 ? 194.513 122.783 202.865 1.00 137.37 ? 3956 GLN A N     1 
ATOM   16451 C CA    . GLN A 1 3956 ? 195.327 123.132 201.708 1.00 137.37 ? 3956 GLN A CA    1 
ATOM   16452 C C     . GLN A 1 3956 ? 194.653 124.168 200.822 1.00 137.37 ? 3956 GLN A C     1 
ATOM   16453 O O     . GLN A 1 3956 ? 195.198 124.520 199.770 1.00 137.37 ? 3956 GLN A O     1 
ATOM   16454 C CB    . GLN A 1 3956 ? 195.644 121.879 200.888 1.00 137.37 ? 3956 GLN A CB    1 
ATOM   16455 C CG    . GLN A 1 3956 ? 196.453 120.844 201.643 1.00 137.37 ? 3956 GLN A CG    1 
ATOM   16456 C CD    . GLN A 1 3956 ? 197.555 121.468 202.474 1.00 137.37 ? 3956 GLN A CD    1 
ATOM   16457 O OE1   . GLN A 1 3956 ? 197.487 121.489 203.704 1.00 137.37 ? 3956 GLN A OE1   1 
ATOM   16458 N NE2   . GLN A 1 3956 ? 198.577 121.988 201.805 1.00 137.37 ? 3956 GLN A NE2   1 
ATOM   16459 N N     . PHE A 1 3957 ? 193.481 124.653 201.231 1.00 127.02 ? 3957 PHE A N     1 
ATOM   16460 C CA    . PHE A 1 3957 ? 192.736 125.611 200.425 1.00 127.02 ? 3957 PHE A CA    1 
ATOM   16461 C C     . PHE A 1 3957 ? 193.528 126.896 200.228 1.00 127.02 ? 3957 PHE A C     1 
ATOM   16462 O O     . PHE A 1 3957 ? 193.557 127.452 199.125 1.00 127.02 ? 3957 PHE A O     1 
ATOM   16463 C CB    . PHE A 1 3957 ? 191.389 125.889 201.092 1.00 127.02 ? 3957 PHE A CB    1 
ATOM   16464 C CG    . PHE A 1 3957 ? 190.544 126.894 200.372 1.00 127.02 ? 3957 PHE A CG    1 
ATOM   16465 C CD1   . PHE A 1 3957 ? 190.708 128.249 200.593 1.00 127.02 ? 3957 PHE A CD1   1 
ATOM   16466 C CD2   . PHE A 1 3957 ? 189.570 126.477 199.484 1.00 127.02 ? 3957 PHE A CD2   1 
ATOM   16467 C CE1   . PHE A 1 3957 ? 189.927 129.168 199.933 1.00 127.02 ? 3957 PHE A CE1   1 
ATOM   16468 C CE2   . PHE A 1 3957 ? 188.786 127.392 198.823 1.00 127.02 ? 3957 PHE A CE2   1 
ATOM   16469 C CZ    . PHE A 1 3957 ? 188.966 128.738 199.048 1.00 127.02 ? 3957 PHE A CZ    1 
ATOM   16470 N N     . GLY A 1 3958 ? 194.171 127.388 201.288 1.00 121.90 ? 3958 GLY A N     1 
ATOM   16471 C CA    . GLY A 1 3958 ? 194.980 128.589 201.155 1.00 121.90 ? 3958 GLY A CA    1 
ATOM   16472 C C     . GLY A 1 3958 ? 196.174 128.388 200.243 1.00 121.90 ? 3958 GLY A C     1 
ATOM   16473 O O     . GLY A 1 3958 ? 196.518 129.269 199.450 1.00 121.90 ? 3958 GLY A O     1 
ATOM   16474 N N     . ILE A 1 3959 ? 196.824 127.227 200.346 1.00 119.44 ? 3959 ILE A N     1 
ATOM   16475 C CA    . ILE A 1 3959 ? 197.946 126.921 199.465 1.00 119.44 ? 3959 ILE A CA    1 
ATOM   16476 C C     . ILE A 1 3959 ? 197.487 126.909 198.014 1.00 119.44 ? 3959 ILE A C     1 
ATOM   16477 O O     . ILE A 1 3959 ? 198.163 127.445 197.127 1.00 119.44 ? 3959 ILE A O     1 
ATOM   16478 C CB    . ILE A 1 3959 ? 198.591 125.583 199.868 1.00 119.44 ? 3959 ILE A CB    1 
ATOM   16479 C CG1   . ILE A 1 3959 ? 199.532 125.780 201.057 1.00 119.44 ? 3959 ILE A CG1   1 
ATOM   16480 C CG2   . ILE A 1 3959 ? 199.335 124.966 198.693 1.00 119.44 ? 3959 ILE A CG2   1 
ATOM   16481 C CD1   . ILE A 1 3959 ? 200.883 126.349 200.681 1.00 119.44 ? 3959 ILE A CD1   1 
ATOM   16482 N N     . TRP A 1 3960 ? 196.328 126.304 197.750 1.00 113.64 ? 3960 TRP A N     1 
ATOM   16483 C CA    . TRP A 1 3960 ? 195.788 126.318 196.395 1.00 113.64 ? 3960 TRP A CA    1 
ATOM   16484 C C     . TRP A 1 3960 ? 195.477 127.737 195.940 1.00 113.64 ? 3960 TRP A C     1 
ATOM   16485 O O     . TRP A 1 3960 ? 195.762 128.107 194.795 1.00 113.64 ? 3960 TRP A O     1 
ATOM   16486 C CB    . TRP A 1 3960 ? 194.535 125.452 196.317 1.00 113.64 ? 3960 TRP A CB    1 
ATOM   16487 C CG    . TRP A 1 3960 ? 193.786 125.640 195.044 1.00 113.64 ? 3960 TRP A CG    1 
ATOM   16488 C CD1   . TRP A 1 3960 ? 194.145 125.190 193.809 1.00 113.64 ? 3960 TRP A CD1   1 
ATOM   16489 C CD2   . TRP A 1 3960 ? 192.555 126.349 194.871 1.00 113.64 ? 3960 TRP A CD2   1 
ATOM   16490 N NE1   . TRP A 1 3960 ? 193.207 125.564 192.878 1.00 113.64 ? 3960 TRP A NE1   1 
ATOM   16491 C CE2   . TRP A 1 3960 ? 192.221 126.279 193.506 1.00 113.64 ? 3960 TRP A CE2   1 
ATOM   16492 C CE3   . TRP A 1 3960 ? 191.702 127.033 195.739 1.00 113.64 ? 3960 TRP A CE3   1 
ATOM   16493 C CZ2   . TRP A 1 3960 ? 191.072 126.865 192.991 1.00 113.64 ? 3960 TRP A CZ2   1 
ATOM   16494 C CZ3   . TRP A 1 3960 ? 190.564 127.613 195.224 1.00 113.64 ? 3960 TRP A CZ3   1 
ATOM   16495 C CH2   . TRP A 1 3960 ? 190.258 127.526 193.865 1.00 113.64 ? 3960 TRP A CH2   1 
ATOM   16496 N N     . LEU A 1 3961 ? 194.891 128.546 196.824 1.00 113.73 ? 3961 LEU A N     1 
ATOM   16497 C CA    . LEU A 1 3961 ? 194.530 129.910 196.461 1.00 113.73 ? 3961 LEU A CA    1 
ATOM   16498 C C     . LEU A 1 3961 ? 195.757 130.740 196.115 1.00 113.73 ? 3961 LEU A C     1 
ATOM   16499 O O     . LEU A 1 3961 ? 195.721 131.534 195.170 1.00 113.73 ? 3961 LEU A O     1 
ATOM   16500 C CB    . LEU A 1 3961 ? 193.747 130.565 197.598 1.00 113.73 ? 3961 LEU A CB    1 
ATOM   16501 C CG    . LEU A 1 3961 ? 193.070 131.899 197.286 1.00 113.73 ? 3961 LEU A CG    1 
ATOM   16502 C CD1   . LEU A 1 3961 ? 191.664 131.928 197.857 1.00 113.73 ? 3961 LEU A CD1   1 
ATOM   16503 C CD2   . LEU A 1 3961 ? 193.888 133.057 197.829 1.00 113.73 ? 3961 LEU A CD2   1 
ATOM   16504 N N     . ASP A 1 3962 ? 196.846 130.570 196.858 1.00 118.60 ? 3962 ASP A N     1 
ATOM   16505 C CA    . ASP A 1 3962 ? 198.079 131.297 196.590 1.00 118.60 ? 3962 ASP A CA    1 
ATOM   16506 C C     . ASP A 1 3962 ? 198.929 130.642 195.513 1.00 118.60 ? 3962 ASP A C     1 
ATOM   16507 O O     . ASP A 1 3962 ? 199.999 131.165 195.188 1.00 118.60 ? 3962 ASP A O     1 
ATOM   16508 C CB    . ASP A 1 3962 ? 198.903 131.437 197.873 1.00 118.60 ? 3962 ASP A CB    1 
ATOM   16509 C CG    . ASP A 1 3962 ? 198.215 132.291 198.913 1.00 118.60 ? 3962 ASP A CG    1 
ATOM   16510 O OD1   . ASP A 1 3962 ? 196.969 132.370 198.887 1.00 118.60 ? 3962 ASP A OD1   1 
ATOM   16511 O OD2   . ASP A 1 3962 ? 198.920 132.885 199.756 1.00 118.60 ? 3962 ASP A OD2   1 
ATOM   16512 N N     . SER A 1 3963 ? 198.488 129.518 194.958 1.00 111.12 ? 3963 SER A N     1 
ATOM   16513 C CA    . SER A 1 3963 ? 199.252 128.859 193.912 1.00 111.12 ? 3963 SER A CA    1 
ATOM   16514 C C     . SER A 1 3963 ? 199.295 129.720 192.657 1.00 111.12 ? 3963 SER A C     1 
ATOM   16515 O O     . SER A 1 3963 ? 198.391 130.516 192.388 1.00 111.12 ? 3963 SER A O     1 
ATOM   16516 C CB    . SER A 1 3963 ? 198.649 127.495 193.587 1.00 111.12 ? 3963 SER A CB    1 
ATOM   16517 O OG    . SER A 1 3963 ? 198.447 126.740 194.766 1.00 111.12 ? 3963 SER A OG    1 
ATOM   16518 N N     . SER A 1 3964 ? 200.373 129.560 191.889 1.00 105.65 ? 3964 SER A N     1 
ATOM   16519 C CA    . SER A 1 3964 ? 200.516 130.320 190.652 1.00 105.65 ? 3964 SER A CA    1 
ATOM   16520 C C     . SER A 1 3964 ? 199.437 129.944 189.646 1.00 105.65 ? 3964 SER A C     1 
ATOM   16521 O O     . SER A 1 3964 ? 198.898 130.811 188.950 1.00 105.65 ? 3964 SER A O     1 
ATOM   16522 C CB    . SER A 1 3964 ? 201.903 130.095 190.056 1.00 105.65 ? 3964 SER A CB    1 
ATOM   16523 O OG    . SER A 1 3964 ? 201.958 128.859 189.366 1.00 105.65 ? 3964 SER A OG    1 
ATOM   16524 N N     . SER A 1 3965 ? 199.103 128.657 189.557 1.00 104.70 ? 3965 SER A N     1 
ATOM   16525 C CA    . SER A 1 3965 ? 198.137 128.151 188.582 1.00 104.70 ? 3965 SER A CA    1 
ATOM   16526 C C     . SER A 1 3965 ? 197.070 127.350 189.314 1.00 104.70 ? 3965 SER A C     1 
ATOM   16527 O O     . SER A 1 3965 ? 197.115 126.114 189.343 1.00 104.70 ? 3965 SER A O     1 
ATOM   16528 C CB    . SER A 1 3965 ? 198.823 127.299 187.515 1.00 104.70 ? 3965 SER A CB    1 
ATOM   16529 O OG    . SER A 1 3965 ? 199.514 126.214 188.104 1.00 104.70 ? 3965 SER A OG    1 
ATOM   16530 N N     . PRO A 1 3966 ? 196.094 128.027 189.919 1.00 104.12 ? 3966 PRO A N     1 
ATOM   16531 C CA    . PRO A 1 3966 ? 195.037 127.302 190.642 1.00 104.12 ? 3966 PRO A CA    1 
ATOM   16532 C C     . PRO A 1 3966 ? 194.222 126.372 189.766 1.00 104.12 ? 3966 PRO A C     1 
ATOM   16533 O O     . PRO A 1 3966 ? 193.777 125.322 190.246 1.00 104.12 ? 3966 PRO A O     1 
ATOM   16534 C CB    . PRO A 1 3966 ? 194.166 128.429 191.212 1.00 104.12 ? 3966 PRO A CB    1 
ATOM   16535 C CG    . PRO A 1 3966 ? 195.028 129.641 191.184 1.00 104.12 ? 3966 PRO A CG    1 
ATOM   16536 C CD    . PRO A 1 3966 ? 195.927 129.484 190.006 1.00 104.12 ? 3966 PRO A CD    1 
ATOM   16537 N N     . GLU A 1 3967 ? 194.001 126.726 188.497 1.00 104.17 ? 3967 GLU A N     1 
ATOM   16538 C CA    . GLU A 1 3967 ? 193.149 125.915 187.636 1.00 104.17 ? 3967 GLU A CA    1 
ATOM   16539 C C     . GLU A 1 3967 ? 193.767 124.564 187.309 1.00 104.17 ? 3967 GLU A C     1 
ATOM   16540 O O     . GLU A 1 3967 ? 193.040 123.647 186.914 1.00 104.17 ? 3967 GLU A O     1 
ATOM   16541 C CB    . GLU A 1 3967 ? 192.832 126.656 186.334 1.00 104.17 ? 3967 GLU A CB    1 
ATOM   16542 C CG    . GLU A 1 3967 ? 193.988 126.803 185.341 1.00 104.17 ? 3967 GLU A CG    1 
ATOM   16543 C CD    . GLU A 1 3967 ? 195.148 127.658 185.833 1.00 104.17 ? 3967 GLU A CD    1 
ATOM   16544 O OE1   . GLU A 1 3967 ? 195.293 127.872 187.051 1.00 104.17 ? 3967 GLU A OE1   1 
ATOM   16545 O OE2   . GLU A 1 3967 ? 195.930 128.123 184.978 1.00 104.17 ? 3967 GLU A OE2   1 
ATOM   16546 N N     . GLN A 1 3968 ? 195.085 124.420 187.454 1.00 103.13 ? 3968 GLN A N     1 
ATOM   16547 C CA    . GLN A 1 3968 ? 195.717 123.133 187.187 1.00 103.13 ? 3968 GLN A CA    1 
ATOM   16548 C C     . GLN A 1 3968 ? 195.171 122.056 188.114 1.00 103.13 ? 3968 GLN A C     1 
ATOM   16549 O O     . GLN A 1 3968 ? 194.822 120.957 187.671 1.00 103.13 ? 3968 GLN A O     1 
ATOM   16550 C CB    . GLN A 1 3968 ? 197.232 123.251 187.337 1.00 103.13 ? 3968 GLN A CB    1 
ATOM   16551 C CG    . GLN A 1 3968 ? 197.933 123.915 186.166 1.00 103.13 ? 3968 GLN A CG    1 
ATOM   16552 C CD    . GLN A 1 3968 ? 197.413 123.440 184.825 1.00 103.13 ? 3968 GLN A CD    1 
ATOM   16553 O OE1   . GLN A 1 3968 ? 196.958 124.237 184.008 1.00 103.13 ? 3968 GLN A OE1   1 
ATOM   16554 N NE2   . GLN A 1 3968 ? 197.482 122.135 184.591 1.00 103.13 ? 3968 GLN A NE2   1 
ATOM   16555 N N     . THR A 1 3969 ? 195.086 122.357 189.410 1.00 111.56 ? 3969 THR A N     1 
ATOM   16556 C CA    . THR A 1 3969 ? 194.599 121.417 190.421 1.00 111.56 ? 3969 THR A CA    1 
ATOM   16557 C C     . THR A 1 3969 ? 193.503 122.111 191.224 1.00 111.56 ? 3969 THR A C     1 
ATOM   16558 O O     . THR A 1 3969 ? 193.771 122.693 192.277 1.00 111.56 ? 3969 THR A O     1 
ATOM   16559 C CB    . THR A 1 3969 ? 195.731 120.941 191.330 1.00 111.56 ? 3969 THR A CB    1 
ATOM   16560 O OG1   . THR A 1 3969 ? 195.931 121.894 192.381 1.00 111.56 ? 3969 THR A OG1   1 
ATOM   16561 C CG2   . THR A 1 3969 ? 197.025 120.781 190.549 1.00 111.56 ? 3969 THR A CG2   1 
ATOM   16562 N N     . VAL A 1 3970 ? 192.272 122.042 190.734 1.00 109.24 ? 3970 VAL A N     1 
ATOM   16563 C CA    . VAL A 1 3970 ? 191.121 122.610 191.427 1.00 109.24 ? 3970 VAL A CA    1 
ATOM   16564 C C     . VAL A 1 3970 ? 190.605 121.564 192.410 1.00 109.24 ? 3970 VAL A C     1 
ATOM   16565 O O     . VAL A 1 3970 ? 190.263 120.451 191.982 1.00 109.24 ? 3970 VAL A O     1 
ATOM   16566 C CB    . VAL A 1 3970 ? 190.020 123.027 190.448 1.00 109.24 ? 3970 VAL A CB    1 
ATOM   16567 C CG1   . VAL A 1 3970 ? 188.771 123.428 191.208 1.00 109.24 ? 3970 VAL A CG1   1 
ATOM   16568 C CG2   . VAL A 1 3970 ? 190.502 124.165 189.578 1.00 109.24 ? 3970 VAL A CG2   1 
ATOM   16569 N N     . PRO A 1 3971 ? 190.547 121.862 193.705 1.00 116.57 ? 3971 PRO A N     1 
ATOM   16570 C CA    . PRO A 1 3971 ? 190.036 120.876 194.662 1.00 116.57 ? 3971 PRO A CA    1 
ATOM   16571 C C     . PRO A 1 3971 ? 188.576 120.545 194.392 1.00 116.57 ? 3971 PRO A C     1 
ATOM   16572 O O     . PRO A 1 3971 ? 187.776 121.413 194.041 1.00 116.57 ? 3971 PRO A O     1 
ATOM   16573 C CB    . PRO A 1 3971 ? 190.216 121.571 196.016 1.00 116.57 ? 3971 PRO A CB    1 
ATOM   16574 C CG    . PRO A 1 3971 ? 190.234 123.026 195.691 1.00 116.57 ? 3971 PRO A CG    1 
ATOM   16575 C CD    . PRO A 1 3971 ? 190.895 123.137 194.351 1.00 116.57 ? 3971 PRO A CD    1 
ATOM   16576 N N     . TYR A 1 3972 ? 188.236 119.273 194.571 1.00 122.29 ? 3972 TYR A N     1 
ATOM   16577 C CA    . TYR A 1 3972 ? 186.866 118.799 194.393 1.00 122.29 ? 3972 TYR A CA    1 
ATOM   16578 C C     . TYR A 1 3972 ? 186.036 119.269 195.579 1.00 122.29 ? 3972 TYR A C     1 
ATOM   16579 O O     . TYR A 1 3972 ? 186.062 118.663 196.652 1.00 122.29 ? 3972 TYR A O     1 
ATOM   16580 C CB    . TYR A 1 3972 ? 186.853 117.281 194.262 1.00 122.29 ? 3972 TYR A CB    1 
ATOM   16581 C CG    . TYR A 1 3972 ? 185.477 116.660 194.269 1.00 122.29 ? 3972 TYR A CG    1 
ATOM   16582 C CD1   . TYR A 1 3972 ? 184.453 117.179 193.493 1.00 122.29 ? 3972 TYR A CD1   1 
ATOM   16583 C CD2   . TYR A 1 3972 ? 185.205 115.547 195.051 1.00 122.29 ? 3972 TYR A CD2   1 
ATOM   16584 C CE1   . TYR A 1 3972 ? 183.196 116.608 193.497 1.00 122.29 ? 3972 TYR A CE1   1 
ATOM   16585 C CE2   . TYR A 1 3972 ? 183.952 114.970 195.063 1.00 122.29 ? 3972 TYR A CE2   1 
ATOM   16586 C CZ    . TYR A 1 3972 ? 182.950 115.505 194.285 1.00 122.29 ? 3972 TYR A CZ    1 
ATOM   16587 O OH    . TYR A 1 3972 ? 181.700 114.931 194.295 1.00 122.29 ? 3972 TYR A OH    1 
ATOM   16588 N N     . LEU A 1 3973 ? 185.295 120.359 195.392 1.00 119.20 ? 3973 LEU A N     1 
ATOM   16589 C CA    . LEU A 1 3973 ? 184.543 120.977 196.475 1.00 119.20 ? 3973 LEU A CA    1 
ATOM   16590 C C     . LEU A 1 3973 ? 183.037 120.878 196.315 1.00 119.20 ? 3973 LEU A C     1 
ATOM   16591 O O     . LEU A 1 3973 ? 182.324 120.874 197.320 1.00 119.20 ? 3973 LEU A O     1 
ATOM   16592 C CB    . LEU A 1 3973 ? 184.928 122.454 196.611 1.00 119.20 ? 3973 LEU A CB    1 
ATOM   16593 C CG    . LEU A 1 3973 ? 186.408 122.730 196.878 1.00 119.20 ? 3973 LEU A CG    1 
ATOM   16594 C CD1   . LEU A 1 3973 ? 186.606 124.157 197.349 1.00 119.20 ? 3973 LEU A CD1   1 
ATOM   16595 C CD2   . LEU A 1 3973 ? 186.961 121.752 197.898 1.00 119.20 ? 3973 LEU A CD2   1 
ATOM   16596 N N     . TRP A 1 3974 ? 182.534 120.805 195.088 1.00 121.64 ? 3974 TRP A N     1 
ATOM   16597 C CA    . TRP A 1 3974 ? 181.098 120.709 194.878 1.00 121.64 ? 3974 TRP A CA    1 
ATOM   16598 C C     . TRP A 1 3974 ? 180.589 119.333 195.288 1.00 121.64 ? 3974 TRP A C     1 
ATOM   16599 O O     . TRP A 1 3974 ? 181.274 118.320 195.133 1.00 121.64 ? 3974 TRP A O     1 
ATOM   16600 C CB    . TRP A 1 3974 ? 180.752 120.981 193.417 1.00 121.64 ? 3974 TRP A CB    1 
ATOM   16601 C CG    . TRP A 1 3974 ? 181.294 119.966 192.457 1.00 121.64 ? 3974 TRP A CG    1 
ATOM   16602 C CD1   . TRP A 1 3974 ? 180.616 118.922 191.905 1.00 121.64 ? 3974 TRP A CD1   1 
ATOM   16603 C CD2   . TRP A 1 3974 ? 182.625 119.900 191.936 1.00 121.64 ? 3974 TRP A CD2   1 
ATOM   16604 N NE1   . TRP A 1 3974 ? 181.439 118.212 191.067 1.00 121.64 ? 3974 TRP A NE1   1 
ATOM   16605 C CE2   . TRP A 1 3974 ? 182.679 118.792 191.069 1.00 121.64 ? 3974 TRP A CE2   1 
ATOM   16606 C CE3   . TRP A 1 3974 ? 183.776 120.670 192.116 1.00 121.64 ? 3974 TRP A CE3   1 
ATOM   16607 C CZ2   . TRP A 1 3974 ? 183.837 118.434 190.387 1.00 121.64 ? 3974 TRP A CZ2   1 
ATOM   16608 C CZ3   . TRP A 1 3974 ? 184.924 120.313 191.437 1.00 121.64 ? 3974 TRP A CZ3   1 
ATOM   16609 C CH2   . TRP A 1 3974 ? 184.947 119.205 190.583 1.00 121.64 ? 3974 TRP A CH2   1 
ATOM   16610 N N     . SER A 1 3975 ? 179.368 119.303 195.811 1.00 126.20 ? 3975 SER A N     1 
ATOM   16611 C CA    . SER A 1 3975 ? 178.753 118.072 196.289 1.00 126.20 ? 3975 SER A CA    1 
ATOM   16612 C C     . SER A 1 3975 ? 177.784 117.554 195.236 1.00 126.20 ? 3975 SER A C     1 
ATOM   16613 O O     . SER A 1 3975 ? 176.815 118.238 194.889 1.00 126.20 ? 3975 SER A O     1 
ATOM   16614 C CB    . SER A 1 3975 ? 178.026 118.303 197.613 1.00 126.20 ? 3975 SER A CB    1 
ATOM   16615 O OG    . SER A 1 3975 ? 176.657 118.599 197.392 1.00 126.20 ? 3975 SER A OG    1 
ATOM   16616 N N     . GLU A 1 3976 ? 178.041 116.350 194.735 1.00 135.36 ? 3976 GLU A N     1 
ATOM   16617 C CA    . GLU A 1 3976 ? 177.166 115.709 193.765 1.00 135.36 ? 3976 GLU A CA    1 
ATOM   16618 C C     . GLU A 1 3976 ? 176.902 114.273 194.187 1.00 135.36 ? 3976 GLU A C     1 
ATOM   16619 O O     . GLU A 1 3976 ? 177.818 113.558 194.605 1.00 135.36 ? 3976 GLU A O     1 
ATOM   16620 C CB    . GLU A 1 3976 ? 177.766 115.742 192.358 1.00 135.36 ? 3976 GLU A CB    1 
ATOM   16621 C CG    . GLU A 1 3976 ? 179.222 115.329 192.284 1.00 135.36 ? 3976 GLU A CG    1 
ATOM   16622 C CD    . GLU A 1 3976 ? 179.737 115.299 190.859 1.00 135.36 ? 3976 GLU A CD    1 
ATOM   16623 O OE1   . GLU A 1 3976 ? 178.903 115.312 189.931 1.00 135.36 ? 3976 GLU A OE1   1 
ATOM   16624 O OE2   . GLU A 1 3976 ? 180.970 115.265 190.666 1.00 135.36 ? 3976 GLU A OE2   1 
ATOM   16625 N N     . GLU A 1 3977 ? 175.640 113.857 194.071 1.00 138.26 ? 3977 GLU A N     1 
ATOM   16626 C CA    . GLU A 1 3977 ? 175.263 112.512 194.488 1.00 138.26 ? 3977 GLU A CA    1 
ATOM   16627 C C     . GLU A 1 3977 ? 175.840 111.451 193.561 1.00 138.26 ? 3977 GLU A C     1 
ATOM   16628 O O     . GLU A 1 3977 ? 176.098 110.324 193.999 1.00 138.26 ? 3977 GLU A O     1 
ATOM   16629 C CB    . GLU A 1 3977 ? 173.738 112.397 194.554 1.00 138.26 ? 3977 GLU A CB    1 
ATOM   16630 C CG    . GLU A 1 3977 ? 173.045 112.248 193.200 1.00 138.26 ? 3977 GLU A CG    1 
ATOM   16631 C CD    . GLU A 1 3977 ? 173.046 113.527 192.375 1.00 138.26 ? 3977 GLU A CD    1 
ATOM   16632 O OE1   . GLU A 1 3977 ? 173.600 114.548 192.834 1.00 138.26 ? 3977 GLU A OE1   1 
ATOM   16633 O OE2   . GLU A 1 3977 ? 172.486 113.511 191.259 1.00 138.26 ? 3977 GLU A OE2   1 
ATOM   16634 N N     . THR A 1 3978 ? 176.060 111.787 192.296 1.00 139.29 ? 3978 THR A N     1 
ATOM   16635 C CA    . THR A 1 3978 ? 176.543 110.839 191.307 1.00 139.29 ? 3978 THR A CA    1 
ATOM   16636 C C     . THR A 1 3978 ? 177.753 111.413 190.589 1.00 139.29 ? 3978 THR A C     1 
ATOM   16637 O O     . THR A 1 3978 ? 177.860 112.632 190.422 1.00 139.29 ? 3978 THR A O     1 
ATOM   16638 C CB    . THR A 1 3978 ? 175.452 110.504 190.279 1.00 139.29 ? 3978 THR A CB    1 
ATOM   16639 O OG1   . THR A 1 3978 ? 176.026 109.787 189.180 1.00 139.29 ? 3978 THR A OG1   1 
ATOM   16640 C CG2   . THR A 1 3978 ? 174.801 111.775 189.759 1.00 139.29 ? 3978 THR A CG2   1 
ATOM   16641 N N     . PRO A 1 3979 ? 178.686 110.560 190.167 1.00 136.05 ? 3979 PRO A N     1 
ATOM   16642 C CA    . PRO A 1 3979 ? 179.819 111.051 189.376 1.00 136.05 ? 3979 PRO A CA    1 
ATOM   16643 C C     . PRO A 1 3979 ? 179.338 111.687 188.082 1.00 136.05 ? 3979 PRO A C     1 
ATOM   16644 O O     . PRO A 1 3979 ? 178.377 111.229 187.461 1.00 136.05 ? 3979 PRO A O     1 
ATOM   16645 C CB    . PRO A 1 3979 ? 180.644 109.787 189.113 1.00 136.05 ? 3979 PRO A CB    1 
ATOM   16646 C CG    . PRO A 1 3979 ? 180.270 108.858 190.214 1.00 136.05 ? 3979 PRO A CG    1 
ATOM   16647 C CD    . PRO A 1 3979 ? 178.829 109.137 190.515 1.00 136.05 ? 3979 PRO A CD    1 
ATOM   16648 N N     . ALA A 1 3980 ? 180.013 112.756 187.683 1.00 125.62 ? 3980 ALA A N     1 
ATOM   16649 C CA    . ALA A 1 3980 ? 179.631 113.524 186.510 1.00 125.62 ? 3980 ALA A CA    1 
ATOM   16650 C C     . ALA A 1 3980 ? 180.638 113.321 185.388 1.00 125.62 ? 3980 ALA A C     1 
ATOM   16651 O O     . ALA A 1 3980 ? 181.737 112.795 185.583 1.00 125.62 ? 3980 ALA A O     1 
ATOM   16652 C CB    . ALA A 1 3980 ? 179.508 115.013 186.849 1.00 125.62 ? 3980 ALA A CB    1 
ATOM   16653 N N     . THR A 1 3981 ? 180.240 113.756 184.198 1.00 118.22 ? 3981 THR A N     1 
ATOM   16654 C CA    . THR A 1 3981 ? 181.105 113.692 183.040 1.00 118.22 ? 3981 THR A CA    1 
ATOM   16655 C C     . THR A 1 3981 ? 182.251 114.686 183.194 1.00 118.22 ? 3981 THR A C     1 
ATOM   16656 O O     . THR A 1 3981 ? 182.177 115.608 184.009 1.00 118.22 ? 3981 THR A O     1 
ATOM   16657 C CB    . THR A 1 3981 ? 180.312 113.996 181.774 1.00 118.22 ? 3981 THR A CB    1 
ATOM   16658 O OG1   . THR A 1 3981 ? 180.319 115.408 181.537 1.00 118.22 ? 3981 THR A OG1   1 
ATOM   16659 C CG2   . THR A 1 3981 ? 178.878 113.524 181.928 1.00 118.22 ? 3981 THR A CG2   1 
ATOM   16660 N N     . PRO A 1 3982 ? 183.334 114.508 182.435 1.00 115.07 ? 3982 PRO A N     1 
ATOM   16661 C CA    . PRO A 1 3982 ? 184.427 115.490 182.495 1.00 115.07 ? 3982 PRO A CA    1 
ATOM   16662 C C     . PRO A 1 3982 ? 183.976 116.903 182.185 1.00 115.07 ? 3982 PRO A C     1 
ATOM   16663 O O     . PRO A 1 3982 ? 184.541 117.860 182.729 1.00 115.07 ? 3982 PRO A O     1 
ATOM   16664 C CB    . PRO A 1 3982 ? 185.418 114.972 181.446 1.00 115.07 ? 3982 PRO A CB    1 
ATOM   16665 C CG    . PRO A 1 3982 ? 185.155 113.516 181.374 1.00 115.07 ? 3982 PRO A CG    1 
ATOM   16666 C CD    . PRO A 1 3982 ? 183.685 113.342 181.606 1.00 115.07 ? 3982 PRO A CD    1 
ATOM   16667 N N     . ILE A 1 3983 ? 182.967 117.063 181.329 1.00 113.43 ? 3983 ILE A N     1 
ATOM   16668 C CA    . ILE A 1 3983 ? 182.449 118.393 181.025 1.00 113.43 ? 3983 ILE A CA    1 
ATOM   16669 C C     . ILE A 1 3983 ? 181.812 119.020 182.259 1.00 113.43 ? 3983 ILE A C     1 
ATOM   16670 O O     . ILE A 1 3983 ? 182.013 120.206 182.542 1.00 113.43 ? 3983 ILE A O     1 
ATOM   16671 C CB    . ILE A 1 3983 ? 181.462 118.318 179.849 1.00 113.43 ? 3983 ILE A CB    1 
ATOM   16672 C CG1   . ILE A 1 3983 ? 182.152 117.706 178.628 1.00 113.43 ? 3983 ILE A CG1   1 
ATOM   16673 C CG2   . ILE A 1 3983 ? 180.912 119.692 179.539 1.00 113.43 ? 3983 ILE A CG2   1 
ATOM   16674 C CD1   . ILE A 1 3983 ? 181.265 117.598 177.411 1.00 113.43 ? 3983 ILE A CD1   1 
ATOM   16675 N N     . GLY A 1 3984 ? 181.025 118.245 183.007 1.00 113.97 ? 3984 GLY A N     1 
ATOM   16676 C CA    . GLY A 1 3984 ? 180.443 118.772 184.231 1.00 113.97 ? 3984 GLY A CA    1 
ATOM   16677 C C     . GLY A 1 3984 ? 181.490 119.095 185.278 1.00 113.97 ? 3984 GLY A C     1 
ATOM   16678 O O     . GLY A 1 3984 ? 181.385 120.098 185.993 1.00 113.97 ? 3984 GLY A O     1 
ATOM   16679 N N     . GLN A 1 3985 ? 182.511 118.244 185.388 1.00 114.91 ? 3985 GLN A N     1 
ATOM   16680 C CA    . GLN A 1 3985 ? 183.640 118.538 186.260 1.00 114.91 ? 3985 GLN A CA    1 
ATOM   16681 C C     . GLN A 1 3985 ? 184.266 119.873 185.890 1.00 114.91 ? 3985 GLN A C     1 
ATOM   16682 O O     . GLN A 1 3985 ? 184.523 120.718 186.756 1.00 114.91 ? 3985 GLN A O     1 
ATOM   16683 C CB    . GLN A 1 3985 ? 184.675 117.418 186.157 1.00 114.91 ? 3985 GLN A CB    1 
ATOM   16684 C CG    . GLN A 1 3985 ? 185.684 117.371 187.286 1.00 114.91 ? 3985 GLN A CG    1 
ATOM   16685 C CD    . GLN A 1 3985 ? 186.046 115.952 187.671 1.00 114.91 ? 3985 GLN A CD    1 
ATOM   16686 O OE1   . GLN A 1 3985 ? 185.435 114.995 187.198 1.00 114.91 ? 3985 GLN A OE1   1 
ATOM   16687 N NE2   . GLN A 1 3985 ? 187.047 115.808 188.530 1.00 114.91 ? 3985 GLN A NE2   1 
ATOM   16688 N N     . ALA A 1 3986 ? 184.507 120.081 184.595 1.00 111.07 ? 3986 ALA A N     1 
ATOM   16689 C CA    . ALA A 1 3986 ? 185.105 121.329 184.141 1.00 111.07 ? 3986 ALA A CA    1 
ATOM   16690 C C     . ALA A 1 3986 ? 184.196 122.511 184.436 1.00 111.07 ? 3986 ALA A C     1 
ATOM   16691 O O     . ALA A 1 3986 ? 184.671 123.584 184.816 1.00 111.07 ? 3986 ALA A O     1 
ATOM   16692 C CB    . ALA A 1 3986 ? 185.419 121.249 182.648 1.00 111.07 ? 3986 ALA A CB    1 
ATOM   16693 N N     . ILE A 1 3987 ? 182.886 122.336 184.270 1.00 107.32 ? 3987 ILE A N     1 
ATOM   16694 C CA    . ILE A 1 3987 ? 181.952 123.428 184.534 1.00 107.32 ? 3987 ILE A CA    1 
ATOM   16695 C C     . ILE A 1 3987 ? 182.001 123.826 186.003 1.00 107.32 ? 3987 ILE A C     1 
ATOM   16696 O O     . ILE A 1 3987 ? 182.068 125.015 186.345 1.00 107.32 ? 3987 ILE A O     1 
ATOM   16697 C CB    . ILE A 1 3987 ? 180.530 123.032 184.104 1.00 107.32 ? 3987 ILE A CB    1 
ATOM   16698 C CG1   . ILE A 1 3987 ? 180.342 123.295 182.614 1.00 107.32 ? 3987 ILE A CG1   1 
ATOM   16699 C CG2   . ILE A 1 3987 ? 179.493 123.800 184.905 1.00 107.32 ? 3987 ILE A CG2   1 
ATOM   16700 C CD1   . ILE A 1 3987 ? 180.191 124.758 182.283 1.00 107.32 ? 3987 ILE A CD1   1 
ATOM   16701 N N     . HIS A 1 3988 ? 181.964 122.839 186.896 1.00 113.47 ? 3988 HIS A N     1 
ATOM   16702 C CA    . HIS A 1 3988 ? 181.972 123.161 188.318 1.00 113.47 ? 3988 HIS A CA    1 
ATOM   16703 C C     . HIS A 1 3988 ? 183.302 123.775 188.734 1.00 113.47 ? 3988 HIS A C     1 
ATOM   16704 O O     . HIS A 1 3988 ? 183.335 124.725 189.527 1.00 113.47 ? 3988 HIS A O     1 
ATOM   16705 C CB    . HIS A 1 3988 ? 181.652 121.916 189.139 1.00 113.47 ? 3988 HIS A CB    1 
ATOM   16706 C CG    . HIS A 1 3988 ? 180.213 121.517 189.073 1.00 113.47 ? 3988 HIS A CG    1 
ATOM   16707 N ND1   . HIS A 1 3988 ? 179.472 121.212 190.193 1.00 113.47 ? 3988 HIS A ND1   1 
ATOM   16708 C CD2   . HIS A 1 3988 ? 179.373 121.388 188.019 1.00 113.47 ? 3988 HIS A CD2   1 
ATOM   16709 C CE1   . HIS A 1 3988 ? 178.239 120.904 189.832 1.00 113.47 ? 3988 HIS A CE1   1 
ATOM   16710 N NE2   . HIS A 1 3988 ? 178.152 121.003 188.518 1.00 113.47 ? 3988 HIS A NE2   1 
ATOM   16711 N N     . ARG A 1 3989 ? 184.408 123.266 188.196 1.00 109.34 ? 3989 ARG A N     1 
ATOM   16712 C CA    . ARG A 1 3989 ? 185.695 123.872 188.506 1.00 109.34 ? 3989 ARG A CA    1 
ATOM   16713 C C     . ARG A 1 3989 ? 185.796 125.281 187.936 1.00 109.34 ? 3989 ARG A C     1 
ATOM   16714 O O     . ARG A 1 3989 ? 186.461 126.138 188.522 1.00 109.34 ? 3989 ARG A O     1 
ATOM   16715 C CB    . ARG A 1 3989 ? 186.823 122.987 187.987 1.00 109.34 ? 3989 ARG A CB    1 
ATOM   16716 C CG    . ARG A 1 3989 ? 186.857 121.609 188.613 1.00 109.34 ? 3989 ARG A CG    1 
ATOM   16717 C CD    . ARG A 1 3989 ? 187.932 120.751 187.983 1.00 109.34 ? 3989 ARG A CD    1 
ATOM   16718 N NE    . ARG A 1 3989 ? 188.258 119.594 188.806 1.00 109.34 ? 3989 ARG A NE    1 
ATOM   16719 C CZ    . ARG A 1 3989 ? 188.986 118.567 188.393 1.00 109.34 ? 3989 ARG A CZ    1 
ATOM   16720 N NH1   . ARG A 1 3989 ? 189.462 118.510 187.160 1.00 109.34 ? 3989 ARG A NH1   1 
ATOM   16721 N NH2   . ARG A 1 3989 ? 189.247 117.574 189.239 1.00 109.34 ? 3989 ARG A NH2   1 
ATOM   16722 N N     . LEU A 1 3990 ? 185.135 125.545 186.808 1.00 100.47 ? 3990 LEU A N     1 
ATOM   16723 C CA    . LEU A 1 3990 ? 185.125 126.892 186.251 1.00 100.47 ? 3990 LEU A CA    1 
ATOM   16724 C C     . LEU A 1 3990 ? 184.336 127.839 187.138 1.00 100.47 ? 3990 LEU A C     1 
ATOM   16725 O O     . LEU A 1 3990 ? 184.722 128.997 187.324 1.00 100.47 ? 3990 LEU A O     1 
ATOM   16726 C CB    . LEU A 1 3990 ? 184.541 126.868 184.843 1.00 100.47 ? 3990 LEU A CB    1 
ATOM   16727 C CG    . LEU A 1 3990 ? 184.206 128.221 184.224 1.00 100.47 ? 3990 LEU A CG    1 
ATOM   16728 C CD1   . LEU A 1 3990 ? 185.459 128.872 183.680 1.00 100.47 ? 3990 LEU A CD1   1 
ATOM   16729 C CD2   . LEU A 1 3990 ? 183.173 128.062 183.134 1.00 100.47 ? 3990 LEU A CD2   1 
ATOM   16730 N N     . LEU A 1 3991 ? 183.223 127.360 187.690 1.00 107.01 ? 3991 LEU A N     1 
ATOM   16731 C CA    . LEU A 1 3991 ? 182.494 128.153 188.673 1.00 107.01 ? 3991 LEU A CA    1 
ATOM   16732 C C     . LEU A 1 3991 ? 183.370 128.447 189.885 1.00 107.01 ? 3991 LEU A C     1 
ATOM   16733 O O     . LEU A 1 3991 ? 183.386 129.575 190.396 1.00 107.01 ? 3991 LEU A O     1 
ATOM   16734 C CB    . LEU A 1 3991 ? 181.221 127.422 189.090 1.00 107.01 ? 3991 LEU A CB    1 
ATOM   16735 C CG    . LEU A 1 3991 ? 180.041 127.528 188.129 1.00 107.01 ? 3991 LEU A CG    1 
ATOM   16736 C CD1   . LEU A 1 3991 ? 178.816 126.874 188.734 1.00 107.01 ? 3991 LEU A CD1   1 
ATOM   16737 C CD2   . LEU A 1 3991 ? 179.763 128.984 187.816 1.00 107.01 ? 3991 LEU A CD2   1 
ATOM   16738 N N     . LEU A 1 3992 ? 184.120 127.444 190.345 1.00 107.31 ? 3992 LEU A N     1 
ATOM   16739 C CA    . LEU A 1 3992 ? 185.039 127.663 191.457 1.00 107.31 ? 3992 LEU A CA    1 
ATOM   16740 C C     . LEU A 1 3992 ? 186.084 128.715 191.109 1.00 107.31 ? 3992 LEU A C     1 
ATOM   16741 O O     . LEU A 1 3992 ? 186.392 129.589 191.927 1.00 107.31 ? 3992 LEU A O     1 
ATOM   16742 C CB    . LEU A 1 3992 ? 185.713 126.351 191.849 1.00 107.31 ? 3992 LEU A CB    1 
ATOM   16743 C CG    . LEU A 1 3992 ? 185.010 125.539 192.936 1.00 107.31 ? 3992 LEU A CG    1 
ATOM   16744 C CD1   . LEU A 1 3992 ? 186.004 124.654 193.664 1.00 107.31 ? 3992 LEU A CD1   1 
ATOM   16745 C CD2   . LEU A 1 3992 ? 184.290 126.453 193.909 1.00 107.31 ? 3992 LEU A CD2   1 
ATOM   16746 N N     . ILE A 1 3993 ? 186.637 128.648 189.898 1.00 99.46  ? 3993 ILE A N     1 
ATOM   16747 C CA    . ILE A 1 3993 ? 187.642 129.620 189.477 1.00 99.46  ? 3993 ILE A CA    1 
ATOM   16748 C C     . ILE A 1 3993 ? 187.038 131.015 189.411 1.00 99.46  ? 3993 ILE A C     1 
ATOM   16749 O O     . ILE A 1 3993 ? 187.691 132.010 189.745 1.00 99.46  ? 3993 ILE A O     1 
ATOM   16750 C CB    . ILE A 1 3993 ? 188.258 129.198 188.132 1.00 99.46  ? 3993 ILE A CB    1 
ATOM   16751 C CG1   . ILE A 1 3993 ? 189.183 128.003 188.335 1.00 99.46  ? 3993 ILE A CG1   1 
ATOM   16752 C CG2   . ILE A 1 3993 ? 189.019 130.345 187.503 1.00 99.46  ? 3993 ILE A CG2   1 
ATOM   16753 C CD1   . ILE A 1 3993 ? 190.271 128.255 189.347 1.00 99.46  ? 3993 ILE A CD1   1 
ATOM   16754 N N     . GLN A 1 3994 ? 185.782 131.113 188.977 1.00 100.44 ? 3994 GLN A N     1 
ATOM   16755 C CA    . GLN A 1 3994 ? 185.098 132.399 189.027 1.00 100.44 ? 3994 GLN A CA    1 
ATOM   16756 C C     . GLN A 1 3994 ? 184.989 132.897 190.460 1.00 100.44 ? 3994 GLN A C     1 
ATOM   16757 O O     . GLN A 1 3994 ? 185.116 134.098 190.721 1.00 100.44 ? 3994 GLN A O     1 
ATOM   16758 C CB    . GLN A 1 3994 ? 183.714 132.293 188.394 1.00 100.44 ? 3994 GLN A CB    1 
ATOM   16759 C CG    . GLN A 1 3994 ? 182.965 133.609 188.359 1.00 100.44 ? 3994 GLN A CG    1 
ATOM   16760 C CD    . GLN A 1 3994 ? 181.573 133.471 187.789 1.00 100.44 ? 3994 GLN A CD    1 
ATOM   16761 O OE1   . GLN A 1 3994 ? 180.711 132.818 188.375 1.00 100.44 ? 3994 GLN A OE1   1 
ATOM   16762 N NE2   . GLN A 1 3994 ? 181.343 134.084 186.635 1.00 100.44 ? 3994 GLN A NE2   1 
ATOM   16763 N N     . ALA A 1 3995 ? 184.751 131.985 191.403 1.00 106.60 ? 3995 ALA A N     1 
ATOM   16764 C CA    . ALA A 1 3995 ? 184.687 132.373 192.809 1.00 106.60 ? 3995 ALA A CA    1 
ATOM   16765 C C     . ALA A 1 3995 ? 186.073 132.694 193.358 1.00 106.60 ? 3995 ALA A C     1 
ATOM   16766 O O     . ALA A 1 3995 ? 186.294 133.764 193.934 1.00 106.60 ? 3995 ALA A O     1 
ATOM   16767 C CB    . ALA A 1 3995 ? 184.026 131.264 193.628 1.00 106.60 ? 3995 ALA A CB    1 
ATOM   16768 N N     . PHE A 1 3996 ? 187.022 131.779 193.185 1.00 107.37 ? 3996 PHE A N     1 
ATOM   16769 C CA    . PHE A 1 3996 ? 188.364 131.923 193.733 1.00 107.37 ? 3996 PHE A CA    1 
ATOM   16770 C C     . PHE A 1 3996 ? 189.356 132.231 192.622 1.00 107.37 ? 3996 PHE A C     1 
ATOM   16771 O O     . PHE A 1 3996 ? 189.433 131.493 191.636 1.00 107.37 ? 3996 PHE A O     1 
ATOM   16772 C CB    . PHE A 1 3996 ? 188.800 130.650 194.454 1.00 107.37 ? 3996 PHE A CB    1 
ATOM   16773 C CG    . PHE A 1 3996 ? 187.818 130.161 195.462 1.00 107.37 ? 3996 PHE A CG    1 
ATOM   16774 C CD1   . PHE A 1 3996 ? 187.546 130.904 196.590 1.00 107.37 ? 3996 PHE A CD1   1 
ATOM   16775 C CD2   . PHE A 1 3996 ? 187.168 128.955 195.283 1.00 107.37 ? 3996 PHE A CD2   1 
ATOM   16776 C CE1   . PHE A 1 3996 ? 186.648 130.454 197.521 1.00 107.37 ? 3996 PHE A CE1   1 
ATOM   16777 C CE2   . PHE A 1 3996 ? 186.264 128.501 196.213 1.00 107.37 ? 3996 PHE A CE2   1 
ATOM   16778 C CZ    . PHE A 1 3996 ? 186.002 129.252 197.334 1.00 107.37 ? 3996 PHE A CZ    1 
ATOM   16779 N N     . ARG A 1 3997 ? 190.133 133.294 192.805 1.00 99.50  ? 3997 ARG A N     1 
ATOM   16780 C CA    . ARG A 1 3997 ? 191.163 133.683 191.852 1.00 99.50  ? 3997 ARG A CA    1 
ATOM   16781 C C     . ARG A 1 3997 ? 190.557 133.902 190.473 1.00 99.50  ? 3997 ARG A C     1 
ATOM   16782 O O     . ARG A 1 3997 ? 190.827 133.125 189.549 1.00 99.50  ? 3997 ARG A O     1 
ATOM   16783 C CB    . ARG A 1 3997 ? 192.264 132.623 191.782 1.00 99.50  ? 3997 ARG A CB    1 
ATOM   16784 C CG    . ARG A 1 3997 ? 193.156 132.565 193.003 1.00 99.50  ? 3997 ARG A CG    1 
ATOM   16785 C CD    . ARG A 1 3997 ? 194.143 133.712 193.009 1.00 99.50  ? 3997 ARG A CD    1 
ATOM   16786 N NE    . ARG A 1 3997 ? 195.140 133.566 191.957 1.00 99.50  ? 3997 ARG A NE    1 
ATOM   16787 C CZ    . ARG A 1 3997 ? 196.178 132.744 192.018 1.00 99.50  ? 3997 ARG A CZ    1 
ATOM   16788 N NH1   . ARG A 1 3997 ? 196.396 131.982 193.076 1.00 99.50  ? 3997 ARG A NH1   1 
ATOM   16789 N NH2   . ARG A 1 3997 ? 197.020 132.686 190.991 1.00 99.50  ? 3997 ARG A NH2   1 
ATOM   16790 N N     . PRO A 1 3998 ? 189.739 134.941 190.286 1.00 93.05  ? 3998 PRO A N     1 
ATOM   16791 C CA    . PRO A 1 3998 ? 189.159 135.187 188.959 1.00 93.05  ? 3998 PRO A CA    1 
ATOM   16792 C C     . PRO A 1 3998 ? 190.185 135.565 187.909 1.00 93.05  ? 3998 PRO A C     1 
ATOM   16793 O O     . PRO A 1 3998 ? 189.838 135.613 186.724 1.00 93.05  ? 3998 PRO A O     1 
ATOM   16794 C CB    . PRO A 1 3998 ? 188.179 136.336 189.213 1.00 93.05  ? 3998 PRO A CB    1 
ATOM   16795 C CG    . PRO A 1 3998 ? 188.731 137.036 190.396 1.00 93.05  ? 3998 PRO A CG    1 
ATOM   16796 C CD    . PRO A 1 3998 ? 189.350 135.976 191.258 1.00 93.05  ? 3998 PRO A CD    1 
ATOM   16797 N N     . ASP A 1 3999 ? 191.428 135.844 188.302 1.00 92.13  ? 3999 ASP A N     1 
ATOM   16798 C CA    . ASP A 1 3999 ? 192.444 136.208 187.323 1.00 92.13  ? 3999 ASP A CA    1 
ATOM   16799 C C     . ASP A 1 3999 ? 192.721 135.073 186.350 1.00 92.13  ? 3999 ASP A C     1 
ATOM   16800 O O     . ASP A 1 3999 ? 192.890 135.315 185.151 1.00 92.13  ? 3999 ASP A O     1 
ATOM   16801 C CB    . ASP A 1 3999 ? 193.729 136.623 188.035 1.00 92.13  ? 3999 ASP A CB    1 
ATOM   16802 C CG    . ASP A 1 3999 ? 194.169 135.613 189.069 1.00 92.13  ? 3999 ASP A CG    1 
ATOM   16803 O OD1   . ASP A 1 3999 ? 193.412 135.384 190.033 1.00 92.13  ? 3999 ASP A OD1   1 
ATOM   16804 O OD2   . ASP A 1 3999 ? 195.272 135.049 188.920 1.00 92.13  ? 3999 ASP A OD2   1 
ATOM   16805 N N     . ARG A 1 4000 ? 192.761 133.835 186.836 1.00 89.50  ? 4000 ARG A N     1 
ATOM   16806 C CA    . ARG A 1 4000 ? 193.034 132.682 185.991 1.00 89.50  ? 4000 ARG A CA    1 
ATOM   16807 C C     . ARG A 1 4000 ? 191.795 132.187 185.259 1.00 89.50  ? 4000 ARG A C     1 
ATOM   16808 O O     . ARG A 1 4000 ? 191.778 131.044 184.784 1.00 89.50  ? 4000 ARG A O     1 
ATOM   16809 C CB    . ARG A 1 4000 ? 193.638 131.554 186.825 1.00 89.50  ? 4000 ARG A CB    1 
ATOM   16810 C CG    . ARG A 1 4000 ? 194.696 132.022 187.799 1.00 89.50  ? 4000 ARG A CG    1 
ATOM   16811 C CD    . ARG A 1 4000 ? 195.951 132.484 187.081 1.00 89.50  ? 4000 ARG A CD    1 
ATOM   16812 N NE    . ARG A 1 4000 ? 196.582 131.401 186.338 1.00 89.50  ? 4000 ARG A NE    1 
ATOM   16813 C CZ    . ARG A 1 4000 ? 197.017 131.502 185.090 1.00 89.50  ? 4000 ARG A CZ    1 
ATOM   16814 N NH1   . ARG A 1 4000 ? 196.921 132.635 184.415 1.00 89.50  ? 4000 ARG A NH1   1 
ATOM   16815 N NH2   . ARG A 1 4000 ? 197.567 130.442 184.506 1.00 89.50  ? 4000 ARG A NH2   1 
ATOM   16816 N N     . LEU A 1 4001 ? 190.758 133.022 185.163 1.00 86.62  ? 4001 LEU A N     1 
ATOM   16817 C CA    . LEU A 1 4001 ? 189.551 132.625 184.451 1.00 86.62  ? 4001 LEU A CA    1 
ATOM   16818 C C     . LEU A 1 4001 ? 189.841 132.361 182.982 1.00 86.62  ? 4001 LEU A C     1 
ATOM   16819 O O     . LEU A 1 4001 ? 189.260 131.453 182.384 1.00 86.62  ? 4001 LEU A O     1 
ATOM   16820 C CB    . LEU A 1 4001 ? 188.476 133.698 184.595 1.00 86.62  ? 4001 LEU A CB    1 
ATOM   16821 C CG    . LEU A 1 4001 ? 187.080 133.268 184.159 1.00 86.62  ? 4001 LEU A CG    1 
ATOM   16822 C CD1   . LEU A 1 4001 ? 186.568 132.193 185.086 1.00 86.62  ? 4001 LEU A CD1   1 
ATOM   16823 C CD2   . LEU A 1 4001 ? 186.142 134.455 184.141 1.00 86.62  ? 4001 LEU A CD2   1 
ATOM   16824 N N     . LEU A 1 4002 ? 190.738 133.144 182.382 1.00 83.44  ? 4002 LEU A N     1 
ATOM   16825 C CA    . LEU A 1 4002 ? 191.110 132.914 180.991 1.00 83.44  ? 4002 LEU A CA    1 
ATOM   16826 C C     . LEU A 1 4002 ? 191.738 131.539 180.813 1.00 83.44  ? 4002 LEU A C     1 
ATOM   16827 O O     . LEU A 1 4002 ? 191.360 130.775 179.914 1.00 83.44  ? 4002 LEU A O     1 
ATOM   16828 C CB    . LEU A 1 4002 ? 192.072 134.005 180.532 1.00 83.44  ? 4002 LEU A CB    1 
ATOM   16829 C CG    . LEU A 1 4002 ? 191.456 135.105 179.679 1.00 83.44  ? 4002 LEU A CG    1 
ATOM   16830 C CD1   . LEU A 1 4002 ? 190.861 134.496 178.442 1.00 83.44  ? 4002 LEU A CD1   1 
ATOM   16831 C CD2   . LEU A 1 4002 ? 190.398 135.844 180.462 1.00 83.44  ? 4002 LEU A CD2   1 
ATOM   16832 N N     . ALA A 1 4003 ? 192.699 131.202 181.673 1.00 91.03  ? 4003 ALA A N     1 
ATOM   16833 C CA    . ALA A 1 4003 ? 193.353 129.904 181.571 1.00 91.03  ? 4003 ALA A CA    1 
ATOM   16834 C C     . ALA A 1 4003 ? 192.361 128.776 181.792 1.00 91.03  ? 4003 ALA A C     1 
ATOM   16835 O O     . ALA A 1 4003 ? 192.385 127.764 181.081 1.00 91.03  ? 4003 ALA A O     1 
ATOM   16836 C CB    . ALA A 1 4003 ? 194.498 129.811 182.577 1.00 91.03  ? 4003 ALA A CB    1 
ATOM   16837 N N     . MET A 1 4004 ? 191.466 128.932 182.766 1.00 97.31  ? 4004 MET A N     1 
ATOM   16838 C CA    . MET A 1 4004 ? 190.544 127.838 183.029 1.00 97.31  ? 4004 MET A CA    1 
ATOM   16839 C C     . MET A 1 4004 ? 189.496 127.720 181.929 1.00 97.31  ? 4004 MET A C     1 
ATOM   16840 O O     . MET A 1 4004 ? 189.032 126.616 181.632 1.00 97.31  ? 4004 MET A O     1 
ATOM   16841 C CB    . MET A 1 4004 ? 189.894 127.992 184.401 1.00 97.31  ? 4004 MET A CB    1 
ATOM   16842 C CG    . MET A 1 4004 ? 188.654 127.159 184.505 1.00 97.31  ? 4004 MET A CG    1 
ATOM   16843 S SD    . MET A 1 4004 ? 189.205 125.452 184.686 1.00 97.31  ? 4004 MET A SD    1 
ATOM   16844 C CE    . MET A 1 4004 ? 187.692 124.651 185.151 1.00 97.31  ? 4004 MET A CE    1 
ATOM   16845 N N     . ALA A 1 4005 ? 189.125 128.833 181.297 1.00 90.62  ? 4005 ALA A N     1 
ATOM   16846 C CA    . ALA A 1 4005 ? 188.253 128.755 180.133 1.00 90.62  ? 4005 ALA A CA    1 
ATOM   16847 C C     . ALA A 1 4005 ? 188.940 128.023 178.992 1.00 90.62  ? 4005 ALA A C     1 
ATOM   16848 O O     . ALA A 1 4005 ? 188.306 127.242 178.272 1.00 90.62  ? 4005 ALA A O     1 
ATOM   16849 C CB    . ALA A 1 4005 ? 187.829 130.156 179.699 1.00 90.62  ? 4005 ALA A CB    1 
ATOM   16850 N N     . HIS A 1 4006 ? 190.240 128.262 178.810 1.00 92.61  ? 4006 HIS A N     1 
ATOM   16851 C CA    . HIS A 1 4006 ? 190.989 127.476 177.835 1.00 92.61  ? 4006 HIS A CA    1 
ATOM   16852 C C     . HIS A 1 4006 ? 190.950 125.995 178.187 1.00 92.61  ? 4006 HIS A C     1 
ATOM   16853 O O     . HIS A 1 4006 ? 190.780 125.140 177.308 1.00 92.61  ? 4006 HIS A O     1 
ATOM   16854 C CB    . HIS A 1 4006 ? 192.432 127.967 177.756 1.00 92.61  ? 4006 HIS A CB    1 
ATOM   16855 C CG    . HIS A 1 4006 ? 192.584 129.280 177.060 1.00 92.61  ? 4006 HIS A CG    1 
ATOM   16856 N ND1   . HIS A 1 4006 ? 192.075 129.517 175.803 1.00 92.61  ? 4006 HIS A ND1   1 
ATOM   16857 C CD2   . HIS A 1 4006 ? 193.183 130.431 177.446 1.00 92.61  ? 4006 HIS A CD2   1 
ATOM   16858 C CE1   . HIS A 1 4006 ? 192.356 130.756 175.442 1.00 92.61  ? 4006 HIS A CE1   1 
ATOM   16859 N NE2   . HIS A 1 4006 ? 193.028 131.332 176.422 1.00 92.61  ? 4006 HIS A NE2   1 
ATOM   16860 N N     . MET A 1 4007 ? 191.101 125.677 179.473 1.00 96.06  ? 4007 MET A N     1 
ATOM   16861 C CA    . MET A 1 4007 ? 191.019 124.284 179.904 1.00 96.06  ? 4007 MET A CA    1 
ATOM   16862 C C     . MET A 1 4007 ? 189.653 123.688 179.585 1.00 96.06  ? 4007 MET A C     1 
ATOM   16863 O O     . MET A 1 4007 ? 189.556 122.550 179.111 1.00 96.06  ? 4007 MET A O     1 
ATOM   16864 C CB    . MET A 1 4007 ? 191.307 124.181 181.400 1.00 96.06  ? 4007 MET A CB    1 
ATOM   16865 C CG    . MET A 1 4007 ? 191.746 122.802 181.849 1.00 96.06  ? 4007 MET A CG    1 
ATOM   16866 S SD    . MET A 1 4007 ? 193.537 122.647 181.920 1.00 96.06  ? 4007 MET A SD    1 
ATOM   16867 C CE    . MET A 1 4007 ? 193.899 123.750 183.279 1.00 96.06  ? 4007 MET A CE    1 
ATOM   16868 N N     . PHE A 1 4008 ? 188.589 124.447 179.841 1.00 89.92  ? 4008 PHE A N     1 
ATOM   16869 C CA    . PHE A 1 4008 ? 187.236 123.971 179.574 1.00 89.92  ? 4008 PHE A CA    1 
ATOM   16870 C C     . PHE A 1 4008 ? 187.023 123.716 178.088 1.00 89.92  ? 4008 PHE A C     1 
ATOM   16871 O O     . PHE A 1 4008 ? 186.432 122.699 177.698 1.00 89.92  ? 4008 PHE A O     1 
ATOM   16872 C CB    . PHE A 1 4008 ? 186.225 124.990 180.098 1.00 89.92  ? 4008 PHE A CB    1 
ATOM   16873 C CG    . PHE A 1 4008 ? 184.808 124.695 179.718 1.00 89.92  ? 4008 PHE A CG    1 
ATOM   16874 C CD1   . PHE A 1 4008 ? 184.047 123.821 180.467 1.00 89.92  ? 4008 PHE A CD1   1 
ATOM   16875 C CD2   . PHE A 1 4008 ? 184.232 125.299 178.616 1.00 89.92  ? 4008 PHE A CD2   1 
ATOM   16876 C CE1   . PHE A 1 4008 ? 182.742 123.550 180.121 1.00 89.92  ? 4008 PHE A CE1   1 
ATOM   16877 C CE2   . PHE A 1 4008 ? 182.928 125.031 178.266 1.00 89.92  ? 4008 PHE A CE2   1 
ATOM   16878 C CZ    . PHE A 1 4008 ? 182.183 124.157 179.020 1.00 89.92  ? 4008 PHE A CZ    1 
ATOM   16879 N N     . VAL A 1 4009 ? 187.495 124.633 177.244 1.00 86.43  ? 4009 VAL A N     1 
ATOM   16880 C CA    . VAL A 1 4009 ? 187.363 124.450 175.804 1.00 86.43  ? 4009 VAL A CA    1 
ATOM   16881 C C     . VAL A 1 4009 ? 188.123 123.211 175.355 1.00 86.43  ? 4009 VAL A C     1 
ATOM   16882 O O     . VAL A 1 4009 ? 187.626 122.421 174.543 1.00 86.43  ? 4009 VAL A O     1 
ATOM   16883 C CB    . VAL A 1 4009 ? 187.840 125.708 175.058 1.00 86.43  ? 4009 VAL A CB    1 
ATOM   16884 C CG1   . VAL A 1 4009 ? 187.997 125.418 173.582 1.00 86.43  ? 4009 VAL A CG1   1 
ATOM   16885 C CG2   . VAL A 1 4009 ? 186.858 126.839 175.268 1.00 86.43  ? 4009 VAL A CG2   1 
ATOM   16886 N N     . SER A 1 4010 ? 189.335 123.016 175.878 1.00 92.88  ? 4010 SER A N     1 
ATOM   16887 C CA    . SER A 1 4010 ? 190.106 121.835 175.503 1.00 92.88  ? 4010 SER A CA    1 
ATOM   16888 C C     . SER A 1 4010 ? 189.402 120.556 175.936 1.00 92.88  ? 4010 SER A C     1 
ATOM   16889 O O     . SER A 1 4010 ? 189.401 119.562 175.203 1.00 92.88  ? 4010 SER A O     1 
ATOM   16890 C CB    . SER A 1 4010 ? 191.506 121.905 176.104 1.00 92.88  ? 4010 SER A CB    1 
ATOM   16891 O OG    . SER A 1 4010 ? 191.469 122.450 177.408 1.00 92.88  ? 4010 SER A OG    1 
ATOM   16892 N N     . THR A 1 4011 ? 188.804 120.555 177.129 1.00 91.99  ? 4011 THR A N     1 
ATOM   16893 C CA    . THR A 1 4011 ? 188.098 119.362 177.584 1.00 91.99  ? 4011 THR A CA    1 
ATOM   16894 C C     . THR A 1 4011 ? 186.878 119.064 176.727 1.00 91.99  ? 4011 THR A C     1 
ATOM   16895 O O     . THR A 1 4011 ? 186.609 117.897 176.424 1.00 91.99  ? 4011 THR A O     1 
ATOM   16896 C CB    . THR A 1 4011 ? 187.675 119.508 179.044 1.00 91.99  ? 4011 THR A CB    1 
ATOM   16897 O OG1   . THR A 1 4011 ? 186.928 120.720 179.206 1.00 91.99  ? 4011 THR A OG1   1 
ATOM   16898 C CG2   . THR A 1 4011 ? 188.891 119.529 179.954 1.00 91.99  ? 4011 THR A CG2   1 
ATOM   16899 N N     . ASN A 1 4012 ? 186.126 120.091 176.332 1.00 92.43  ? 4012 ASN A N     1 
ATOM   16900 C CA    . ASN A 1 4012 ? 184.897 119.844 175.584 1.00 92.43  ? 4012 ASN A CA    1 
ATOM   16901 C C     . ASN A 1 4012 ? 185.181 119.514 174.122 1.00 92.43  ? 4012 ASN A C     1 
ATOM   16902 O O     . ASN A 1 4012 ? 184.781 118.456 173.626 1.00 92.43  ? 4012 ASN A O     1 
ATOM   16903 C CB    . ASN A 1 4012 ? 183.968 121.052 175.688 1.00 92.43  ? 4012 ASN A CB    1 
ATOM   16904 C CG    . ASN A 1 4012 ? 183.352 121.188 177.057 1.00 92.43  ? 4012 ASN A CG    1 
ATOM   16905 O OD1   . ASN A 1 4012 ? 184.000 120.927 178.070 1.00 92.43  ? 4012 ASN A OD1   1 
ATOM   16906 N ND2   . ASN A 1 4012 ? 182.094 121.600 177.099 1.00 92.43  ? 4012 ASN A ND2   1 
ATOM   16907 N N     . LEU A 1 4013 ? 185.859 120.412 173.416 1.00 89.52  ? 4013 LEU A N     1 
ATOM   16908 C CA    . LEU A 1 4013 ? 186.104 120.268 171.987 1.00 89.52  ? 4013 LEU A CA    1 
ATOM   16909 C C     . LEU A 1 4013 ? 187.435 119.605 171.673 1.00 89.52  ? 4013 LEU A C     1 
ATOM   16910 O O     . LEU A 1 4013 ? 187.929 119.736 170.549 1.00 89.52  ? 4013 LEU A O     1 
ATOM   16911 C CB    . LEU A 1 4013 ? 186.020 121.628 171.283 1.00 89.52  ? 4013 LEU A CB    1 
ATOM   16912 C CG    . LEU A 1 4013 ? 184.679 122.366 171.159 1.00 89.52  ? 4013 LEU A CG    1 
ATOM   16913 C CD1   . LEU A 1 4013 ? 183.881 122.399 172.429 1.00 89.52  ? 4013 LEU A CD1   1 
ATOM   16914 C CD2   . LEU A 1 4013 ? 184.911 123.784 170.680 1.00 89.52  ? 4013 LEU A CD2   1 
ATOM   16915 N N     . GLY A 1 4014 ? 188.025 118.911 172.629 1.00 94.55  ? 4014 GLY A N     1 
ATOM   16916 C CA    . GLY A 1 4014 ? 189.280 118.247 172.332 1.00 94.55  ? 4014 GLY A CA    1 
ATOM   16917 C C     . GLY A 1 4014 ? 190.464 119.174 172.500 1.00 94.55  ? 4014 GLY A C     1 
ATOM   16918 O O     . GLY A 1 4014 ? 190.380 120.385 172.306 1.00 94.55  ? 4014 GLY A O     1 
ATOM   16919 N N     . GLU A 1 4015 ? 191.593 118.584 172.874 1.00 101.79 ? 4015 GLU A N     1 
ATOM   16920 C CA    . GLU A 1 4015 ? 192.802 119.359 173.086 1.00 101.79 ? 4015 GLU A CA    1 
ATOM   16921 C C     . GLU A 1 4015 ? 193.301 119.933 171.764 1.00 101.79 ? 4015 GLU A C     1 
ATOM   16922 O O     . GLU A 1 4015 ? 192.952 119.463 170.677 1.00 101.79 ? 4015 GLU A O     1 
ATOM   16923 C CB    . GLU A 1 4015 ? 193.884 118.496 173.734 1.00 101.79 ? 4015 GLU A CB    1 
ATOM   16924 C CG    . GLU A 1 4015 ? 194.748 119.228 174.748 1.00 101.79 ? 4015 GLU A CG    1 
ATOM   16925 C CD    . GLU A 1 4015 ? 195.843 120.049 174.100 1.00 101.79 ? 4015 GLU A CD    1 
ATOM   16926 O OE1   . GLU A 1 4015 ? 196.354 120.986 174.748 1.00 101.79 ? 4015 GLU A OE1   1 
ATOM   16927 O OE2   . GLU A 1 4015 ? 196.187 119.762 172.935 1.00 101.79 ? 4015 GLU A OE2   1 
ATOM   16928 N N     . SER A 1 4016 ? 194.107 120.986 171.873 1.00 96.23  ? 4016 SER A N     1 
ATOM   16929 C CA    . SER A 1 4016 ? 194.692 121.670 170.726 1.00 96.23  ? 4016 SER A CA    1 
ATOM   16930 C C     . SER A 1 4016 ? 193.635 122.277 169.817 1.00 96.23  ? 4016 SER A C     1 
ATOM   16931 O O     . SER A 1 4016 ? 193.856 122.411 168.611 1.00 96.23  ? 4016 SER A O     1 
ATOM   16932 C CB    . SER A 1 4016 ? 195.598 120.733 169.921 1.00 96.23  ? 4016 SER A CB    1 
ATOM   16933 O OG    . SER A 1 4016 ? 194.842 120.008 168.968 1.00 96.23  ? 4016 SER A OG    1 
ATOM   16934 N N     . PHE A 1 4017 ? 192.477 122.640 170.370 1.00 89.35  ? 4017 PHE A N     1 
ATOM   16935 C CA    . PHE A 1 4017 ? 191.451 123.276 169.554 1.00 89.35  ? 4017 PHE A CA    1 
ATOM   16936 C C     . PHE A 1 4017 ? 191.918 124.627 169.033 1.00 89.35  ? 4017 PHE A C     1 
ATOM   16937 O O     . PHE A 1 4017 ? 191.678 124.969 167.870 1.00 89.35  ? 4017 PHE A O     1 
ATOM   16938 C CB    . PHE A 1 4017 ? 190.159 123.433 170.347 1.00 89.35  ? 4017 PHE A CB    1 
ATOM   16939 C CG    . PHE A 1 4017 ? 188.975 123.757 169.494 1.00 89.35  ? 4017 PHE A CG    1 
ATOM   16940 C CD1   . PHE A 1 4017 ? 188.398 122.789 168.699 1.00 89.35  ? 4017 PHE A CD1   1 
ATOM   16941 C CD2   . PHE A 1 4017 ? 188.456 125.034 169.467 1.00 89.35  ? 4017 PHE A CD2   1 
ATOM   16942 C CE1   . PHE A 1 4017 ? 187.314 123.087 167.906 1.00 89.35  ? 4017 PHE A CE1   1 
ATOM   16943 C CE2   . PHE A 1 4017 ? 187.373 125.335 168.677 1.00 89.35  ? 4017 PHE A CE2   1 
ATOM   16944 C CZ    . PHE A 1 4017 ? 186.804 124.362 167.893 1.00 89.35  ? 4017 PHE A CZ    1 
ATOM   16945 N N     . MET A 1 4018 ? 192.584 125.410 169.876 1.00 97.78  ? 4018 MET A N     1 
ATOM   16946 C CA    . MET A 1 4018 ? 193.120 126.701 169.471 1.00 97.78  ? 4018 MET A CA    1 
ATOM   16947 C C     . MET A 1 4018 ? 194.598 126.638 169.115 1.00 97.78  ? 4018 MET A C     1 
ATOM   16948 O O     . MET A 1 4018 ? 195.208 127.685 168.878 1.00 97.78  ? 4018 MET A O     1 
ATOM   16949 C CB    . MET A 1 4018 ? 192.909 127.734 170.580 1.00 97.78  ? 4018 MET A CB    1 
ATOM   16950 C CG    . MET A 1 4018 ? 191.509 127.753 171.145 1.00 97.78  ? 4018 MET A CG    1 
ATOM   16951 S SD    . MET A 1 4018 ? 191.246 126.341 172.225 1.00 97.78  ? 4018 MET A SD    1 
ATOM   16952 C CE    . MET A 1 4018 ? 192.112 126.885 173.693 1.00 97.78  ? 4018 MET A CE    1 
ATOM   16953 N N     . SER A 1 4019 ? 195.185 125.440 169.075 1.00 104.15 ? 4019 SER A N     1 
ATOM   16954 C CA    . SER A 1 4019 ? 196.613 125.323 168.801 1.00 104.15 ? 4019 SER A CA    1 
ATOM   16955 C C     . SER A 1 4019 ? 196.967 125.841 167.416 1.00 104.15 ? 4019 SER A C     1 
ATOM   16956 O O     . SER A 1 4019 ? 198.091 126.309 167.198 1.00 104.15 ? 4019 SER A O     1 
ATOM   16957 C CB    . SER A 1 4019 ? 197.057 123.870 168.945 1.00 104.15 ? 4019 SER A CB    1 
ATOM   16958 O OG    . SER A 1 4019 ? 196.582 123.090 167.862 1.00 104.15 ? 4019 SER A OG    1 
ATOM   16959 N N     . ILE A 1 4020 ? 196.034 125.760 166.467 1.00 104.09 ? 4020 ILE A N     1 
ATOM   16960 C CA    . ILE A 1 4020 ? 196.291 126.296 165.135 1.00 104.09 ? 4020 ILE A CA    1 
ATOM   16961 C C     . ILE A 1 4020 ? 196.475 127.807 165.199 1.00 104.09 ? 4020 ILE A C     1 
ATOM   16962 O O     . ILE A 1 4020 ? 197.202 128.395 164.390 1.00 104.09 ? 4020 ILE A O     1 
ATOM   16963 C CB    . ILE A 1 4020 ? 195.159 125.894 164.171 1.00 104.09 ? 4020 ILE A CB    1 
ATOM   16964 C CG1   . ILE A 1 4020 ? 195.461 126.360 162.743 1.00 104.09 ? 4020 ILE A CG1   1 
ATOM   16965 C CG2   . ILE A 1 4020 ? 193.828 126.435 164.656 1.00 104.09 ? 4020 ILE A CG2   1 
ATOM   16966 C CD1   . ILE A 1 4020 ? 196.846 125.997 162.254 1.00 104.09 ? 4020 ILE A CD1   1 
ATOM   16967 N N     . MET A 1 4021 ? 195.828 128.458 166.165 1.00 101.58 ? 4021 MET A N     1 
ATOM   16968 C CA    . MET A 1 4021 ? 195.963 129.904 166.295 1.00 101.58 ? 4021 MET A CA    1 
ATOM   16969 C C     . MET A 1 4021 ? 197.355 130.296 166.771 1.00 101.58 ? 4021 MET A C     1 
ATOM   16970 O O     . MET A 1 4021 ? 197.897 131.324 166.347 1.00 101.58 ? 4021 MET A O     1 
ATOM   16971 C CB    . MET A 1 4021 ? 194.890 130.442 167.241 1.00 101.58 ? 4021 MET A CB    1 
ATOM   16972 C CG    . MET A 1 4021 ? 193.490 130.628 166.631 1.00 101.58 ? 4021 MET A CG    1 
ATOM   16973 S SD    . MET A 1 4021 ? 193.164 131.446 165.035 1.00 101.58 ? 4021 MET A SD    1 
ATOM   16974 C CE    . MET A 1 4021 ? 194.650 132.364 164.622 1.00 101.58 ? 4021 MET A CE    1 
ATOM   16975 N N     . GLU A 1 4022 ? 197.951 129.493 167.654 1.00 108.06 ? 4022 GLU A N     1 
ATOM   16976 C CA    . GLU A 1 4022 ? 199.275 129.822 168.173 1.00 108.06 ? 4022 GLU A CA    1 
ATOM   16977 C C     . GLU A 1 4022 ? 200.322 129.805 167.069 1.00 108.06 ? 4022 GLU A C     1 
ATOM   16978 O O     . GLU A 1 4022 ? 201.221 130.653 167.042 1.00 108.06 ? 4022 GLU A O     1 
ATOM   16979 C CB    . GLU A 1 4022 ? 199.654 128.852 169.290 1.00 108.06 ? 4022 GLU A CB    1 
ATOM   16980 C CG    . GLU A 1 4022 ? 198.513 128.562 170.240 1.00 108.06 ? 4022 GLU A CG    1 
ATOM   16981 C CD    . GLU A 1 4022 ? 197.849 129.828 170.732 1.00 108.06 ? 4022 GLU A CD    1 
ATOM   16982 O OE1   . GLU A 1 4022 ? 198.531 130.636 171.394 1.00 108.06 ? 4022 GLU A OE1   1 
ATOM   16983 O OE2   . GLU A 1 4022 ? 196.650 130.023 170.443 1.00 108.06 ? 4022 GLU A OE2   1 
ATOM   16984 N N     . GLN A 1 4023 ? 200.219 128.853 166.150 1.00 112.33 ? 4023 GLN A N     1 
ATOM   16985 C CA    . GLN A 1 4023 ? 201.159 128.777 165.048 1.00 112.33 ? 4023 GLN A CA    1 
ATOM   16986 C C     . GLN A 1 4023 ? 201.019 130.006 164.151 1.00 112.33 ? 4023 GLN A C     1 
ATOM   16987 O O     . GLN A 1 4023 ? 199.952 130.622 164.093 1.00 112.33 ? 4023 GLN A O     1 
ATOM   16988 C CB    . GLN A 1 4023 ? 200.916 127.509 164.239 1.00 112.33 ? 4023 GLN A CB    1 
ATOM   16989 C CG    . GLN A 1 4023 ? 200.918 126.250 165.083 1.00 112.33 ? 4023 GLN A CG    1 
ATOM   16990 C CD    . GLN A 1 4023 ? 200.153 125.116 164.438 1.00 112.33 ? 4023 GLN A CD    1 
ATOM   16991 O OE1   . GLN A 1 4023 ? 200.414 124.748 163.293 1.00 112.33 ? 4023 GLN A OE1   1 
ATOM   16992 N NE2   . GLN A 1 4023 ? 199.201 124.553 165.173 1.00 112.33 ? 4023 GLN A NE2   1 
ATOM   16993 N N     . PRO A 1 4024 ? 202.088 130.396 163.459 1.00 107.27 ? 4024 PRO A N     1 
ATOM   16994 C CA    . PRO A 1 4024 ? 201.986 131.532 162.537 1.00 107.27 ? 4024 PRO A CA    1 
ATOM   16995 C C     . PRO A 1 4024 ? 200.973 131.245 161.441 1.00 107.27 ? 4024 PRO A C     1 
ATOM   16996 O O     . PRO A 1 4024 ? 200.782 130.099 161.030 1.00 107.27 ? 4024 PRO A O     1 
ATOM   16997 C CB    . PRO A 1 4024 ? 203.405 131.667 161.975 1.00 107.27 ? 4024 PRO A CB    1 
ATOM   16998 C CG    . PRO A 1 4024 ? 204.031 130.331 162.193 1.00 107.27 ? 4024 PRO A CG    1 
ATOM   16999 C CD    . PRO A 1 4024 ? 203.440 129.816 163.469 1.00 107.27 ? 4024 PRO A CD    1 
ATOM   17000 N N     . LEU A 1 4025 ? 200.312 132.302 160.980 1.00 108.49 ? 4025 LEU A N     1 
ATOM   17001 C CA    . LEU A 1 4025 ? 199.233 132.154 160.014 1.00 108.49 ? 4025 LEU A CA    1 
ATOM   17002 C C     . LEU A 1 4025 ? 199.759 131.621 158.688 1.00 108.49 ? 4025 LEU A C     1 
ATOM   17003 O O     . LEU A 1 4025 ? 200.448 132.333 157.950 1.00 108.49 ? 4025 LEU A O     1 
ATOM   17004 C CB    . LEU A 1 4025 ? 198.512 133.490 159.823 1.00 108.49 ? 4025 LEU A CB    1 
ATOM   17005 C CG    . LEU A 1 4025 ? 197.671 133.695 158.564 1.00 108.49 ? 4025 LEU A CG    1 
ATOM   17006 C CD1   . LEU A 1 4025 ? 196.536 132.695 158.496 1.00 108.49 ? 4025 LEU A CD1   1 
ATOM   17007 C CD2   . LEU A 1 4025 ? 197.129 135.106 158.529 1.00 108.49 ? 4025 LEU A CD2   1 
ATOM   17008 N N     . ASP A 1 4026 ? 199.446 130.359 158.387 1.00 117.84 ? 4026 ASP A N     1 
ATOM   17009 C CA    . ASP A 1 4026 ? 199.775 129.758 157.095 1.00 117.84 ? 4026 ASP A CA    1 
ATOM   17010 C C     . ASP A 1 4026 ? 198.738 130.216 156.071 1.00 117.84 ? 4026 ASP A C     1 
ATOM   17011 O O     . ASP A 1 4026 ? 197.832 129.486 155.665 1.00 117.84 ? 4026 ASP A O     1 
ATOM   17012 C CB    . ASP A 1 4026 ? 199.827 128.241 157.198 1.00 117.84 ? 4026 ASP A CB    1 
ATOM   17013 C CG    . ASP A 1 4026 ? 200.076 127.574 155.856 1.00 117.84 ? 4026 ASP A CG    1 
ATOM   17014 O OD1   . ASP A 1 4026 ? 201.112 127.868 155.223 1.00 117.84 ? 4026 ASP A OD1   1 
ATOM   17015 O OD2   . ASP A 1 4026 ? 199.230 126.759 155.431 1.00 117.84 ? 4026 ASP A OD2   1 
ATOM   17016 N N     . LEU A 1 4027 ? 198.885 131.469 155.660 1.00 116.42 ? 4027 LEU A N     1 
ATOM   17017 C CA    . LEU A 1 4027 ? 197.905 132.085 154.782 1.00 116.42 ? 4027 LEU A CA    1 
ATOM   17018 C C     . LEU A 1 4027 ? 198.138 131.775 153.313 1.00 116.42 ? 4027 LEU A C     1 
ATOM   17019 O O     . LEU A 1 4027 ? 197.330 132.200 152.487 1.00 116.42 ? 4027 LEU A O     1 
ATOM   17020 C CB    . LEU A 1 4027 ? 197.881 133.599 154.996 1.00 116.42 ? 4027 LEU A CB    1 
ATOM   17021 C CG    . LEU A 1 4027 ? 198.876 134.466 154.231 1.00 116.42 ? 4027 LEU A CG    1 
ATOM   17022 C CD1   . LEU A 1 4027 ? 198.547 135.926 154.462 1.00 116.42 ? 4027 LEU A CD1   1 
ATOM   17023 C CD2   . LEU A 1 4027 ? 200.301 134.168 154.659 1.00 116.42 ? 4027 LEU A CD2   1 
ATOM   17024 N N     . THR A 1 4028 ? 199.207 131.056 152.967 1.00 119.14 ? 4028 THR A N     1 
ATOM   17025 C CA    . THR A 1 4028 ? 199.417 130.672 151.573 1.00 119.14 ? 4028 THR A CA    1 
ATOM   17026 C C     . THR A 1 4028 ? 198.270 129.804 151.072 1.00 119.14 ? 4028 THR A C     1 
ATOM   17027 O O     . THR A 1 4028 ? 197.705 130.051 149.998 1.00 119.14 ? 4028 THR A O     1 
ATOM   17028 C CB    . THR A 1 4028 ? 200.745 129.932 151.425 1.00 119.14 ? 4028 THR A CB    1 
ATOM   17029 O OG1   . THR A 1 4028 ? 200.658 128.662 152.084 1.00 119.14 ? 4028 THR A OG1   1 
ATOM   17030 C CG2   . THR A 1 4028 ? 201.875 130.740 152.040 1.00 119.14 ? 4028 THR A CG2   1 
ATOM   17031 N N     . HIS A 1 4029 ? 197.900 128.790 151.855 1.00 115.67 ? 4029 HIS A N     1 
ATOM   17032 C CA    . HIS A 1 4029 ? 196.754 127.966 151.499 1.00 115.67 ? 4029 HIS A CA    1 
ATOM   17033 C C     . HIS A 1 4029 ? 195.481 128.793 151.422 1.00 115.67 ? 4029 HIS A C     1 
ATOM   17034 O O     . HIS A 1 4029 ? 194.596 128.496 150.613 1.00 115.67 ? 4029 HIS A O     1 
ATOM   17035 C CB    . HIS A 1 4029 ? 196.588 126.837 152.512 1.00 115.67 ? 4029 HIS A CB    1 
ATOM   17036 C CG    . HIS A 1 4029 ? 195.695 125.734 152.042 1.00 115.67 ? 4029 HIS A CG    1 
ATOM   17037 N ND1   . HIS A 1 4029 ? 195.303 124.696 152.858 1.00 115.67 ? 4029 HIS A ND1   1 
ATOM   17038 C CD2   . HIS A 1 4029 ? 195.115 125.509 150.840 1.00 115.67 ? 4029 HIS A CD2   1 
ATOM   17039 C CE1   . HIS A 1 4029 ? 194.518 123.878 152.179 1.00 115.67 ? 4029 HIS A CE1   1 
ATOM   17040 N NE2   . HIS A 1 4029 ? 194.388 124.349 150.952 1.00 115.67 ? 4029 HIS A NE2   1 
ATOM   17041 N N     . ILE A 1 4030 ? 195.371 129.832 152.249 1.00 113.99 ? 4030 ILE A N     1 
ATOM   17042 C CA    . ILE A 1 4030 ? 194.167 130.651 152.236 1.00 113.99 ? 4030 ILE A CA    1 
ATOM   17043 C C     . ILE A 1 4030 ? 194.093 131.481 150.964 1.00 113.99 ? 4030 ILE A C     1 
ATOM   17044 O O     . ILE A 1 4030 ? 193.042 131.557 150.321 1.00 113.99 ? 4030 ILE A O     1 
ATOM   17045 C CB    . ILE A 1 4030 ? 194.110 131.536 153.488 1.00 113.99 ? 4030 ILE A CB    1 
ATOM   17046 C CG1   . ILE A 1 4030 ? 194.539 130.735 154.712 1.00 113.99 ? 4030 ILE A CG1   1 
ATOM   17047 C CG2   . ILE A 1 4030 ? 192.708 132.078 153.675 1.00 113.99 ? 4030 ILE A CG2   1 
ATOM   17048 C CD1   . ILE A 1 4030 ? 193.624 129.577 155.021 1.00 113.99 ? 4030 ILE A CD1   1 
ATOM   17049 N N     . VAL A 1 4031 ? 195.202 132.119 150.572 1.00 118.76 ? 4031 VAL A N     1 
ATOM   17050 C CA    . VAL A 1 4031 ? 195.188 132.918 149.349 1.00 118.76 ? 4031 VAL A CA    1 
ATOM   17051 C C     . VAL A 1 4031 ? 195.229 132.040 148.115 1.00 118.76 ? 4031 VAL A C     1 
ATOM   17052 O O     . VAL A 1 4031 ? 195.103 132.548 146.993 1.00 118.76 ? 4031 VAL A O     1 
ATOM   17053 C CB    . VAL A 1 4031 ? 196.349 133.929 149.282 1.00 118.76 ? 4031 VAL A CB    1 
ATOM   17054 C CG1   . VAL A 1 4031 ? 195.991 135.163 150.090 1.00 118.76 ? 4031 VAL A CG1   1 
ATOM   17055 C CG2   . VAL A 1 4031 ? 197.650 133.306 149.730 1.00 118.76 ? 4031 VAL A CG2   1 
ATOM   17056 N N     . GLY A 1 4032 ? 195.385 130.734 148.292 1.00 119.98 ? 4032 GLY A N     1 
ATOM   17057 C CA    . GLY A 1 4032 ? 195.169 129.808 147.205 1.00 119.98 ? 4032 GLY A CA    1 
ATOM   17058 C C     . GLY A 1 4032 ? 193.722 129.370 147.212 1.00 119.98 ? 4032 GLY A C     1 
ATOM   17059 O O     . GLY A 1 4032 ? 192.838 130.153 146.857 1.00 119.98 ? 4032 GLY A O     1 
ATOM   17060 N N     . THR A 1 4033 ? 193.459 128.132 147.611 1.00 119.30 ? 4033 THR A N     1 
ATOM   17061 C CA    . THR A 1 4033 ? 192.083 127.689 147.760 1.00 119.30 ? 4033 THR A CA    1 
ATOM   17062 C C     . THR A 1 4033 ? 191.462 128.294 149.026 1.00 119.30 ? 4033 THR A C     1 
ATOM   17063 O O     . THR A 1 4033 ? 192.061 129.128 149.710 1.00 119.30 ? 4033 THR A O     1 
ATOM   17064 C CB    . THR A 1 4033 ? 192.024 126.167 147.730 1.00 119.30 ? 4033 THR A CB    1 
ATOM   17065 O OG1   . THR A 1 4033 ? 192.522 125.641 148.961 1.00 119.30 ? 4033 THR A OG1   1 
ATOM   17066 C CG2   . THR A 1 4033 ? 192.867 125.616 146.573 1.00 119.30 ? 4033 THR A CG2   1 
ATOM   17067 N N     . GLU A 1 4034 ? 190.215 127.903 149.305 1.00 121.01 ? 4034 GLU A N     1 
ATOM   17068 C CA    . GLU A 1 4034 ? 189.354 128.516 150.320 1.00 121.01 ? 4034 GLU A CA    1 
ATOM   17069 C C     . GLU A 1 4034 ? 189.105 130.012 150.132 1.00 121.01 ? 4034 GLU A C     1 
ATOM   17070 O O     . GLU A 1 4034 ? 188.498 130.642 151.004 1.00 121.01 ? 4034 GLU A O     1 
ATOM   17071 C CB    . GLU A 1 4034 ? 189.847 128.279 151.764 1.00 121.01 ? 4034 GLU A CB    1 
ATOM   17072 C CG    . GLU A 1 4034 ? 190.211 126.844 152.238 1.00 121.01 ? 4034 GLU A CG    1 
ATOM   17073 C CD    . GLU A 1 4034 ? 191.231 126.080 151.434 1.00 121.01 ? 4034 GLU A CD    1 
ATOM   17074 O OE1   . GLU A 1 4034 ? 191.042 124.859 151.236 1.00 121.01 ? 4034 GLU A OE1   1 
ATOM   17075 O OE2   . GLU A 1 4034 ? 192.274 126.653 151.070 1.00 121.01 ? 4034 GLU A OE2   1 
ATOM   17076 N N     . VAL A 1 4035 ? 189.540 130.598 149.016 1.00 116.67 ? 4035 VAL A N     1 
ATOM   17077 C CA    . VAL A 1 4035 ? 189.257 132.003 148.732 1.00 116.67 ? 4035 VAL A CA    1 
ATOM   17078 C C     . VAL A 1 4035 ? 188.989 132.162 147.240 1.00 116.67 ? 4035 VAL A C     1 
ATOM   17079 O O     . VAL A 1 4035 ? 189.863 131.875 146.414 1.00 116.67 ? 4035 VAL A O     1 
ATOM   17080 C CB    . VAL A 1 4035 ? 190.401 132.931 149.173 1.00 116.67 ? 4035 VAL A CB    1 
ATOM   17081 C CG1   . VAL A 1 4035 ? 190.349 134.242 148.411 1.00 116.67 ? 4035 VAL A CG1   1 
ATOM   17082 C CG2   . VAL A 1 4035 ? 190.304 133.194 150.663 1.00 116.67 ? 4035 VAL A CG2   1 
ATOM   17083 N N     . LYS A 1 4036 ? 187.784 132.616 146.895 1.00 119.12 ? 4036 LYS A N     1 
ATOM   17084 C CA    . LYS A 1 4036 ? 187.438 132.903 145.514 1.00 119.12 ? 4036 LYS A CA    1 
ATOM   17085 C C     . LYS A 1 4036 ? 188.045 134.236 145.081 1.00 119.12 ? 4036 LYS A C     1 
ATOM   17086 O O     . LYS A 1 4036 ? 188.187 135.152 145.894 1.00 119.12 ? 4036 LYS A O     1 
ATOM   17087 C CB    . LYS A 1 4036 ? 185.925 132.953 145.345 1.00 119.12 ? 4036 LYS A CB    1 
ATOM   17088 C CG    . LYS A 1 4036 ? 185.197 131.815 146.037 1.00 119.12 ? 4036 LYS A CG    1 
ATOM   17089 C CD    . LYS A 1 4036 ? 185.016 130.634 145.098 1.00 119.12 ? 4036 LYS A CD    1 
ATOM   17090 C CE    . LYS A 1 4036 ? 184.662 129.367 145.858 1.00 119.12 ? 4036 LYS A CE    1 
ATOM   17091 N NZ    . LYS A 1 4036 ? 185.884 128.609 146.247 1.00 119.12 ? 4036 LYS A NZ    1 
ATOM   17092 N N     . PRO A 1 4037 ? 188.413 134.367 143.803 1.00 122.09 ? 4037 PRO A N     1 
ATOM   17093 C CA    . PRO A 1 4037 ? 188.935 135.660 143.328 1.00 122.09 ? 4037 PRO A CA    1 
ATOM   17094 C C     . PRO A 1 4037 ? 187.944 136.797 143.482 1.00 122.09 ? 4037 PRO A C     1 
ATOM   17095 O O     . PRO A 1 4037 ? 188.358 137.955 143.615 1.00 122.09 ? 4037 PRO A O     1 
ATOM   17096 C CB    . PRO A 1 4037 ? 189.265 135.389 141.852 1.00 122.09 ? 4037 PRO A CB    1 
ATOM   17097 C CG    . PRO A 1 4037 ? 188.534 134.136 141.502 1.00 122.09 ? 4037 PRO A CG    1 
ATOM   17098 C CD    . PRO A 1 4037 ? 188.454 133.334 142.757 1.00 122.09 ? 4037 PRO A CD    1 
ATOM   17099 N N     . ASN A 1 4038 ? 186.644 136.504 143.466 1.00 123.35 ? 4038 ASN A N     1 
ATOM   17100 C CA    . ASN A 1 4038 ? 185.643 137.538 143.686 1.00 123.35 ? 4038 ASN A CA    1 
ATOM   17101 C C     . ASN A 1 4038 ? 185.591 137.998 145.137 1.00 123.35 ? 4038 ASN A C     1 
ATOM   17102 O O     . ASN A 1 4038 ? 184.972 139.027 145.424 1.00 123.35 ? 4038 ASN A O     1 
ATOM   17103 C CB    . ASN A 1 4038 ? 184.270 137.035 143.250 1.00 123.35 ? 4038 ASN A CB    1 
ATOM   17104 C CG    . ASN A 1 4038 ? 183.475 138.085 142.509 1.00 123.35 ? 4038 ASN A CG    1 
ATOM   17105 O OD1   . ASN A 1 4038 ? 182.991 139.047 143.104 1.00 123.35 ? 4038 ASN A OD1   1 
ATOM   17106 N ND2   . ASN A 1 4038 ? 183.338 137.910 141.201 1.00 123.35 ? 4038 ASN A ND2   1 
ATOM   17107 N N     . THR A 1 4039 ? 186.213 137.261 146.054 1.00 111.69 ? 4039 THR A N     1 
ATOM   17108 C CA    . THR A 1 4039 ? 186.211 137.632 147.463 1.00 111.69 ? 4039 THR A CA    1 
ATOM   17109 C C     . THR A 1 4039 ? 187.505 138.354 147.805 1.00 111.69 ? 4039 THR A C     1 
ATOM   17110 O O     . THR A 1 4039 ? 188.578 137.744 147.721 1.00 111.69 ? 4039 THR A O     1 
ATOM   17111 C CB    . THR A 1 4039 ? 186.067 136.404 148.341 1.00 111.69 ? 4039 THR A CB    1 
ATOM   17112 O OG1   . THR A 1 4039 ? 187.156 135.509 148.085 1.00 111.69 ? 4039 THR A OG1   1 
ATOM   17113 C CG2   . THR A 1 4039 ? 184.759 135.694 148.050 1.00 111.69 ? 4039 THR A CG2   1 
ATOM   17114 N N     . PRO A 1 4040 ? 187.459 139.625 148.188 1.00 102.74 ? 4040 PRO A N     1 
ATOM   17115 C CA    . PRO A 1 4040 ? 188.691 140.329 148.556 1.00 102.74 ? 4040 PRO A CA    1 
ATOM   17116 C C     . PRO A 1 4040 ? 189.298 139.762 149.829 1.00 102.74 ? 4040 PRO A C     1 
ATOM   17117 O O     . PRO A 1 4040 ? 188.601 139.316 150.742 1.00 102.74 ? 4040 PRO A O     1 
ATOM   17118 C CB    . PRO A 1 4040 ? 188.227 141.772 148.763 1.00 102.74 ? 4040 PRO A CB    1 
ATOM   17119 C CG    . PRO A 1 4040 ? 186.795 141.649 149.131 1.00 102.74 ? 4040 PRO A CG    1 
ATOM   17120 C CD    . PRO A 1 4040 ? 186.263 140.459 148.385 1.00 102.74 ? 4040 PRO A CD    1 
ATOM   17121 N N     . VAL A 1 4041 ? 190.624 139.796 149.882 1.00 97.00  ? 4041 VAL A N     1 
ATOM   17122 C CA    . VAL A 1 4041 ? 191.378 139.386 151.059 1.00 97.00  ? 4041 VAL A CA    1 
ATOM   17123 C C     . VAL A 1 4041 ? 191.608 140.646 151.880 1.00 97.00  ? 4041 VAL A C     1 
ATOM   17124 O O     . VAL A 1 4041 ? 192.353 141.543 151.472 1.00 97.00  ? 4041 VAL A O     1 
ATOM   17125 C CB    . VAL A 1 4041 ? 192.697 138.701 150.694 1.00 97.00  ? 4041 VAL A CB    1 
ATOM   17126 C CG1   . VAL A 1 4041 ? 193.498 138.408 151.948 1.00 97.00  ? 4041 VAL A CG1   1 
ATOM   17127 C CG2   . VAL A 1 4041 ? 192.424 137.420 149.930 1.00 97.00  ? 4041 VAL A CG2   1 
ATOM   17128 N N     . LEU A 1 4042 ? 190.966 140.719 153.038 1.00 95.91  ? 4042 LEU A N     1 
ATOM   17129 C CA    . LEU A 1 4042 ? 190.886 141.955 153.797 1.00 95.91  ? 4042 LEU A CA    1 
ATOM   17130 C C     . LEU A 1 4042 ? 191.868 141.897 154.960 1.00 95.91  ? 4042 LEU A C     1 
ATOM   17131 O O     . LEU A 1 4042 ? 191.722 141.066 155.860 1.00 95.91  ? 4042 LEU A O     1 
ATOM   17132 C CB    . LEU A 1 4042 ? 189.455 142.151 154.290 1.00 95.91  ? 4042 LEU A CB    1 
ATOM   17133 C CG    . LEU A 1 4042 ? 188.754 143.412 153.791 1.00 95.91  ? 4042 LEU A CG    1 
ATOM   17134 C CD1   . LEU A 1 4042 ? 187.433 143.624 154.497 1.00 95.91  ? 4042 LEU A CD1   1 
ATOM   17135 C CD2   . LEU A 1 4042 ? 189.640 144.606 153.953 1.00 95.91  ? 4042 LEU A CD2   1 
ATOM   17136 N N     . MET A 1 4043 ? 192.856 142.786 154.947 1.00 99.49  ? 4043 MET A N     1 
ATOM   17137 C CA    . MET A 1 4043 ? 193.995 142.726 155.864 1.00 99.49  ? 4043 MET A CA    1 
ATOM   17138 C C     . MET A 1 4043 ? 193.864 143.854 156.885 1.00 99.49  ? 4043 MET A C     1 
ATOM   17139 O O     . MET A 1 4043 ? 194.278 144.986 156.637 1.00 99.49  ? 4043 MET A O     1 
ATOM   17140 C CB    . MET A 1 4043 ? 195.304 142.837 155.094 1.00 99.49  ? 4043 MET A CB    1 
ATOM   17141 C CG    . MET A 1 4043 ? 195.925 141.515 154.721 1.00 99.49  ? 4043 MET A CG    1 
ATOM   17142 S SD    . MET A 1 4043 ? 196.333 140.489 156.135 1.00 99.49  ? 4043 MET A SD    1 
ATOM   17143 C CE    . MET A 1 4043 ? 197.187 139.159 155.302 1.00 99.49  ? 4043 MET A CE    1 
ATOM   17144 N N     . CYS A 1 4044 ? 193.297 143.539 158.043 1.00 98.33  ? 4044 CYS A N     1 
ATOM   17145 C CA    . CYS A 1 4044 ? 193.140 144.520 159.107 1.00 98.33  ? 4044 CYS A CA    1 
ATOM   17146 C C     . CYS A 1 4044 ? 194.306 144.418 160.080 1.00 98.33  ? 4044 CYS A C     1 
ATOM   17147 O O     . CYS A 1 4044 ? 194.711 143.316 160.462 1.00 98.33  ? 4044 CYS A O     1 
ATOM   17148 C CB    . CYS A 1 4044 ? 191.817 144.317 159.840 1.00 98.33  ? 4044 CYS A CB    1 
ATOM   17149 S SG    . CYS A 1 4044 ? 190.372 144.765 158.861 1.00 98.33  ? 4044 CYS A SG    1 
ATOM   17150 N N     . SER A 1 4045 ? 194.844 145.568 160.473 1.00 104.87 ? 4045 SER A N     1 
ATOM   17151 C CA    . SER A 1 4045 ? 195.979 145.630 161.378 1.00 104.87 ? 4045 SER A CA    1 
ATOM   17152 C C     . SER A 1 4045 ? 195.716 146.659 162.465 1.00 104.87 ? 4045 SER A C     1 
ATOM   17153 O O     . SER A 1 4045 ? 195.042 147.667 162.240 1.00 104.87 ? 4045 SER A O     1 
ATOM   17154 C CB    . SER A 1 4045 ? 197.269 145.982 160.631 1.00 104.87 ? 4045 SER A CB    1 
ATOM   17155 O OG    . SER A 1 4045 ? 198.215 146.570 161.503 1.00 104.87 ? 4045 SER A OG    1 
ATOM   17156 N N     . VAL A 1 4046 ? 196.253 146.388 163.651 1.00 105.70 ? 4046 VAL A N     1 
ATOM   17157 C CA    . VAL A 1 4046 ? 196.124 147.335 164.762 1.00 105.70 ? 4046 VAL A CA    1 
ATOM   17158 C C     . VAL A 1 4046 ? 196.863 148.617 164.406 1.00 105.70 ? 4046 VAL A C     1 
ATOM   17159 O O     . VAL A 1 4046 ? 197.873 148.563 163.675 1.00 105.70 ? 4046 VAL A O     1 
ATOM   17160 C CB    . VAL A 1 4046 ? 196.676 146.715 166.056 1.00 105.70 ? 4046 VAL A CB    1 
ATOM   17161 C CG1   . VAL A 1 4046 ? 196.209 147.476 167.285 1.00 105.70 ? 4046 VAL A CG1   1 
ATOM   17162 C CG2   . VAL A 1 4046 ? 196.245 145.269 166.155 1.00 105.70 ? 4046 VAL A CG2   1 
ATOM   17163 N N     . PRO A 1 4047 ? 196.407 149.786 164.853 1.00 108.25 ? 4047 PRO A N     1 
ATOM   17164 C CA    . PRO A 1 4047 ? 197.135 151.026 164.560 1.00 108.25 ? 4047 PRO A CA    1 
ATOM   17165 C C     . PRO A 1 4047 ? 198.595 150.941 164.978 1.00 108.25 ? 4047 PRO A C     1 
ATOM   17166 O O     . PRO A 1 4047 ? 198.932 150.382 166.023 1.00 108.25 ? 4047 PRO A O     1 
ATOM   17167 C CB    . PRO A 1 4047 ? 196.377 152.070 165.382 1.00 108.25 ? 4047 PRO A CB    1 
ATOM   17168 C CG    . PRO A 1 4047 ? 194.988 151.563 165.409 1.00 108.25 ? 4047 PRO A CG    1 
ATOM   17169 C CD    . PRO A 1 4047 ? 195.073 150.060 165.415 1.00 108.25 ? 4047 PRO A CD    1 
ATOM   17170 N N     . GLY A 1 4048 ? 199.465 151.495 164.141 1.00 111.20 ? 4048 GLY A N     1 
ATOM   17171 C CA    . GLY A 1 4048 ? 200.890 151.441 164.371 1.00 111.20 ? 4048 GLY A CA    1 
ATOM   17172 C C     . GLY A 1 4048 ? 201.569 150.184 163.883 1.00 111.20 ? 4048 GLY A C     1 
ATOM   17173 O O     . GLY A 1 4048 ? 202.769 150.018 164.124 1.00 111.20 ? 4048 GLY A O     1 
ATOM   17174 N N     . TYR A 1 4049 ? 200.846 149.297 163.209 1.00 101.28 ? 4049 TYR A N     1 
ATOM   17175 C CA    . TYR A 1 4049 ? 201.393 148.047 162.712 1.00 101.28 ? 4049 TYR A CA    1 
ATOM   17176 C C     . TYR A 1 4049 ? 201.162 147.951 161.213 1.00 101.28 ? 4049 TYR A C     1 
ATOM   17177 O O     . TYR A 1 4049 ? 200.189 148.495 160.683 1.00 101.28 ? 4049 TYR A O     1 
ATOM   17178 C CB    . TYR A 1 4049 ? 200.757 146.845 163.413 1.00 101.28 ? 4049 TYR A CB    1 
ATOM   17179 C CG    . TYR A 1 4049 ? 201.520 145.556 163.234 1.00 101.28 ? 4049 TYR A CG    1 
ATOM   17180 C CD1   . TYR A 1 4049 ? 202.656 145.292 163.980 1.00 101.28 ? 4049 TYR A CD1   1 
ATOM   17181 C CD2   . TYR A 1 4049 ? 201.109 144.608 162.310 1.00 101.28 ? 4049 TYR A CD2   1 
ATOM   17182 C CE1   . TYR A 1 4049 ? 203.356 144.115 163.820 1.00 101.28 ? 4049 TYR A CE1   1 
ATOM   17183 C CE2   . TYR A 1 4049 ? 201.802 143.429 162.142 1.00 101.28 ? 4049 TYR A CE2   1 
ATOM   17184 C CZ    . TYR A 1 4049 ? 202.926 143.187 162.898 1.00 101.28 ? 4049 TYR A CZ    1 
ATOM   17185 O OH    . TYR A 1 4049 ? 203.623 142.013 162.733 1.00 101.28 ? 4049 TYR A OH    1 
ATOM   17186 N N     . ASP A 1 4050 ? 202.065 147.254 160.532 1.00 110.94 ? 4050 ASP A N     1 
ATOM   17187 C CA    . ASP A 1 4050 ? 201.997 147.081 159.090 1.00 110.94 ? 4050 ASP A CA    1 
ATOM   17188 C C     . ASP A 1 4050 ? 201.933 145.599 158.755 1.00 110.94 ? 4050 ASP A C     1 
ATOM   17189 O O     . ASP A 1 4050 ? 202.617 144.781 159.377 1.00 110.94 ? 4050 ASP A O     1 
ATOM   17190 C CB    . ASP A 1 4050 ? 203.200 147.722 158.396 1.00 110.94 ? 4050 ASP A CB    1 
ATOM   17191 C CG    . ASP A 1 4050 ? 202.933 148.026 156.934 1.00 110.94 ? 4050 ASP A CG    1 
ATOM   17192 O OD1   . ASP A 1 4050 ? 202.096 147.332 156.320 1.00 110.94 ? 4050 ASP A OD1   1 
ATOM   17193 O OD2   . ASP A 1 4050 ? 203.560 148.965 156.399 1.00 110.94 ? 4050 ASP A OD2   1 
ATOM   17194 N N     . ALA A 1 4051 ? 201.108 145.261 157.768 1.00 106.09 ? 4051 ALA A N     1 
ATOM   17195 C CA    . ALA A 1 4051 ? 200.905 143.879 157.368 1.00 106.09 ? 4051 ALA A CA    1 
ATOM   17196 C C     . ALA A 1 4051 ? 201.443 143.564 155.982 1.00 106.09 ? 4051 ALA A C     1 
ATOM   17197 O O     . ALA A 1 4051 ? 201.361 142.406 155.555 1.00 106.09 ? 4051 ALA A O     1 
ATOM   17198 C CB    . ALA A 1 4051 ? 199.414 143.529 157.421 1.00 106.09 ? 4051 ALA A CB    1 
ATOM   17199 N N     . SER A 1 4052 ? 201.998 144.547 155.272 1.00 112.69 ? 4052 SER A N     1 
ATOM   17200 C CA    . SER A 1 4052 ? 202.445 144.315 153.903 1.00 112.69 ? 4052 SER A CA    1 
ATOM   17201 C C     . SER A 1 4052 ? 203.574 143.298 153.827 1.00 112.69 ? 4052 SER A C     1 
ATOM   17202 O O     . SER A 1 4052 ? 203.786 142.703 152.765 1.00 112.69 ? 4052 SER A O     1 
ATOM   17203 C CB    . SER A 1 4052 ? 202.888 145.632 153.266 1.00 112.69 ? 4052 SER A CB    1 
ATOM   17204 O OG    . SER A 1 4052 ? 201.986 146.677 153.583 1.00 112.69 ? 4052 SER A OG    1 
ATOM   17205 N N     . GLY A 1 4053 ? 204.300 143.084 154.924 1.00 119.32 ? 4053 GLY A N     1 
ATOM   17206 C CA    . GLY A 1 4053 ? 205.390 142.125 154.894 1.00 119.32 ? 4053 GLY A CA    1 
ATOM   17207 C C     . GLY A 1 4053 ? 204.925 140.720 154.568 1.00 119.32 ? 4053 GLY A C     1 
ATOM   17208 O O     . GLY A 1 4053 ? 205.539 140.027 153.754 1.00 119.32 ? 4053 GLY A O     1 
ATOM   17209 N N     . HIS A 1 4054 ? 203.824 140.287 155.185 1.00 114.24 ? 4054 HIS A N     1 
ATOM   17210 C CA    . HIS A 1 4054 ? 203.336 138.930 154.960 1.00 114.24 ? 4054 HIS A CA    1 
ATOM   17211 C C     . HIS A 1 4054 ? 202.946 138.722 153.503 1.00 114.24 ? 4054 HIS A C     1 
ATOM   17212 O O     . HIS A 1 4054 ? 203.343 137.731 152.875 1.00 114.24 ? 4054 HIS A O     1 
ATOM   17213 C CB    . HIS A 1 4054 ? 202.149 138.643 155.878 1.00 114.24 ? 4054 HIS A CB    1 
ATOM   17214 C CG    . HIS A 1 4054 ? 202.415 138.928 157.323 1.00 114.24 ? 4054 HIS A CG    1 
ATOM   17215 N ND1   . HIS A 1 4054 ? 202.354 140.198 157.855 1.00 114.24 ? 4054 HIS A ND1   1 
ATOM   17216 C CD2   . HIS A 1 4054 ? 202.732 138.105 158.350 1.00 114.24 ? 4054 HIS A CD2   1 
ATOM   17217 C CE1   . HIS A 1 4054 ? 202.629 140.146 159.146 1.00 114.24 ? 4054 HIS A CE1   1 
ATOM   17218 N NE2   . HIS A 1 4054 ? 202.861 138.887 159.472 1.00 114.24 ? 4054 HIS A NE2   1 
ATOM   17219 N N     . VAL A 1 4055 ? 202.173 139.655 152.943 1.00 119.60 ? 4055 VAL A N     1 
ATOM   17220 C CA    . VAL A 1 4055 ? 201.713 139.496 151.569 1.00 119.60 ? 4055 VAL A CA    1 
ATOM   17221 C C     . VAL A 1 4055 ? 202.885 139.573 150.600 1.00 119.60 ? 4055 VAL A C     1 
ATOM   17222 O O     . VAL A 1 4055 ? 202.971 138.786 149.649 1.00 119.60 ? 4055 VAL A O     1 
ATOM   17223 C CB    . VAL A 1 4055 ? 200.615 140.527 151.238 1.00 119.60 ? 4055 VAL A CB    1 
ATOM   17224 C CG1   . VAL A 1 4055 ? 201.082 141.939 151.513 1.00 119.60 ? 4055 VAL A CG1   1 
ATOM   17225 C CG2   . VAL A 1 4055 ? 200.177 140.390 149.792 1.00 119.60 ? 4055 VAL A CG2   1 
ATOM   17226 N N     . GLU A 1 4056 ? 203.821 140.496 150.834 1.00 126.56 ? 4056 GLU A N     1 
ATOM   17227 C CA    . GLU A 1 4056 ? 204.972 140.599 149.946 1.00 126.56 ? 4056 GLU A CA    1 
ATOM   17228 C C     . GLU A 1 4056 ? 205.815 139.331 149.984 1.00 126.56 ? 4056 GLU A C     1 
ATOM   17229 O O     . GLU A 1 4056 ? 206.240 138.830 148.936 1.00 126.56 ? 4056 GLU A O     1 
ATOM   17230 C CB    . GLU A 1 4056 ? 205.816 141.818 150.315 1.00 126.56 ? 4056 GLU A CB    1 
ATOM   17231 C CG    . GLU A 1 4056 ? 205.161 143.146 149.977 1.00 126.56 ? 4056 GLU A CG    1 
ATOM   17232 C CD    . GLU A 1 4056 ? 205.308 143.523 148.518 1.00 126.56 ? 4056 GLU A CD    1 
ATOM   17233 O OE1   . GLU A 1 4056 ? 205.753 142.674 147.720 1.00 126.56 ? 4056 GLU A OE1   1 
ATOM   17234 O OE2   . GLU A 1 4056 ? 204.973 144.674 148.168 1.00 126.56 ? 4056 GLU A OE2   1 
ATOM   17235 N N     . ASP A 1 4057 ? 206.058 138.788 151.180 1.00 131.72 ? 4057 ASP A N     1 
ATOM   17236 C CA    . ASP A 1 4057 ? 206.869 137.581 151.287 1.00 131.72 ? 4057 ASP A CA    1 
ATOM   17237 C C     . ASP A 1 4057 ? 206.183 136.385 150.641 1.00 131.72 ? 4057 ASP A C     1 
ATOM   17238 O O     . ASP A 1 4057 ? 206.831 135.597 149.941 1.00 131.72 ? 4057 ASP A O     1 
ATOM   17239 C CB    . ASP A 1 4057 ? 207.191 137.295 152.752 1.00 131.72 ? 4057 ASP A CB    1 
ATOM   17240 C CG    . ASP A 1 4057 ? 208.228 138.244 153.311 1.00 131.72 ? 4057 ASP A CG    1 
ATOM   17241 O OD1   . ASP A 1 4057 ? 209.146 137.776 154.017 1.00 131.72 ? 4057 ASP A OD1   1 
ATOM   17242 O OD2   . ASP A 1 4057 ? 208.136 139.458 153.035 1.00 131.72 ? 4057 ASP A OD2   1 
ATOM   17243 N N     . LEU A 1 4058 ? 204.875 136.226 150.862 1.00 129.43 ? 4058 LEU A N     1 
ATOM   17244 C CA    . LEU A 1 4058 ? 204.179 135.103 150.244 1.00 129.43 ? 4058 LEU A CA    1 
ATOM   17245 C C     . LEU A 1 4058 ? 204.169 135.236 148.727 1.00 129.43 ? 4058 LEU A C     1 
ATOM   17246 O O     . LEU A 1 4058 ? 204.300 134.237 148.011 1.00 129.43 ? 4058 LEU A O     1 
ATOM   17247 C CB    . LEU A 1 4058 ? 202.760 134.981 150.803 1.00 129.43 ? 4058 LEU A CB    1 
ATOM   17248 C CG    . LEU A 1 4058 ? 201.663 135.991 150.453 1.00 129.43 ? 4058 LEU A CG    1 
ATOM   17249 C CD1   . LEU A 1 4058 ? 200.976 135.690 149.129 1.00 129.43 ? 4058 LEU A CD1   1 
ATOM   17250 C CD2   . LEU A 1 4058 ? 200.644 136.045 151.561 1.00 129.43 ? 4058 LEU A CD2   1 
ATOM   17251 N N     . ALA A 1 4059 ? 204.010 136.460 148.217 1.00 130.68 ? 4059 ALA A N     1 
ATOM   17252 C CA    . ALA A 1 4059 ? 204.049 136.659 146.775 1.00 130.68 ? 4059 ALA A CA    1 
ATOM   17253 C C     . ALA A 1 4059 ? 205.426 136.342 146.213 1.00 130.68 ? 4059 ALA A C     1 
ATOM   17254 O O     . ALA A 1 4059 ? 205.544 135.721 145.150 1.00 130.68 ? 4059 ALA A O     1 
ATOM   17255 C CB    . ALA A 1 4059 ? 203.650 138.090 146.436 1.00 130.68 ? 4059 ALA A CB    1 
ATOM   17256 N N     . ALA A 1 4060 ? 206.481 136.762 146.914 1.00 136.16 ? 4060 ALA A N     1 
ATOM   17257 C CA    . ALA A 1 4060 ? 207.833 136.457 146.463 1.00 136.16 ? 4060 ALA A CA    1 
ATOM   17258 C C     . ALA A 1 4060 ? 208.077 134.955 146.447 1.00 136.16 ? 4060 ALA A C     1 
ATOM   17259 O O     . ALA A 1 4060 ? 208.702 134.430 145.518 1.00 136.16 ? 4060 ALA A O     1 
ATOM   17260 C CB    . ALA A 1 4060 ? 208.857 137.160 147.353 1.00 136.16 ? 4060 ALA A CB    1 
ATOM   17261 N N     . GLU A 1 4061 ? 207.588 134.246 147.467 1.00 141.39 ? 4061 GLU A N     1 
ATOM   17262 C CA    . GLU A 1 4061 ? 207.723 132.794 147.479 1.00 141.39 ? 4061 GLU A CA    1 
ATOM   17263 C C     . GLU A 1 4061 ? 206.912 132.165 146.353 1.00 141.39 ? 4061 GLU A C     1 
ATOM   17264 O O     . GLU A 1 4061 ? 207.332 131.164 145.761 1.00 141.39 ? 4061 GLU A O     1 
ATOM   17265 C CB    . GLU A 1 4061 ? 207.308 132.241 148.846 1.00 141.39 ? 4061 GLU A CB    1 
ATOM   17266 C CG    . GLU A 1 4061 ? 207.383 130.721 148.986 1.00 141.39 ? 4061 GLU A CG    1 
ATOM   17267 C CD    . GLU A 1 4061 ? 206.150 130.000 148.470 1.00 141.39 ? 4061 GLU A CD    1 
ATOM   17268 O OE1   . GLU A 1 4061 ? 205.164 130.675 148.113 1.00 141.39 ? 4061 GLU A OE1   1 
ATOM   17269 O OE2   . GLU A 1 4061 ? 206.171 128.753 148.418 1.00 141.39 ? 4061 GLU A OE2   1 
ATOM   17270 N N     . GLN A 1 4062 ? 205.752 132.735 146.041 1.00 139.06 ? 4062 GLN A N     1 
ATOM   17271 C CA    . GLN A 1 4062 ? 204.933 132.264 144.935 1.00 139.06 ? 4062 GLN A CA    1 
ATOM   17272 C C     . GLN A 1 4062 ? 205.296 132.921 143.612 1.00 139.06 ? 4062 GLN A C     1 
ATOM   17273 O O     . GLN A 1 4062 ? 204.605 132.681 142.616 1.00 139.06 ? 4062 GLN A O     1 
ATOM   17274 C CB    . GLN A 1 4062 ? 203.449 132.501 145.226 1.00 139.06 ? 4062 GLN A CB    1 
ATOM   17275 C CG    . GLN A 1 4062 ? 202.826 131.482 146.156 1.00 139.06 ? 4062 GLN A CG    1 
ATOM   17276 C CD    . GLN A 1 4062 ? 201.894 132.116 147.164 1.00 139.06 ? 4062 GLN A CD    1 
ATOM   17277 O OE1   . GLN A 1 4062 ? 201.635 133.318 147.112 1.00 139.06 ? 4062 GLN A OE1   1 
ATOM   17278 N NE2   . GLN A 1 4062 ? 201.384 131.313 148.091 1.00 139.06 ? 4062 GLN A NE2   1 
ATOM   17279 N N     . ASN A 1 4063 ? 206.346 133.745 143.591 1.00 144.08 ? 4063 ASN A N     1 
ATOM   17280 C CA    . ASN A 1 4063 ? 206.837 134.433 142.391 1.00 144.08 ? 4063 ASN A CA    1 
ATOM   17281 C C     . ASN A 1 4063 ? 205.692 135.037 141.578 1.00 144.08 ? 4063 ASN A C     1 
ATOM   17282 O O     . ASN A 1 4063 ? 205.623 134.911 140.353 1.00 144.08 ? 4063 ASN A O     1 
ATOM   17283 C CB    . ASN A 1 4063 ? 207.707 133.506 141.532 1.00 144.08 ? 4063 ASN A CB    1 
ATOM   17284 C CG    . ASN A 1 4063 ? 206.948 132.313 140.985 1.00 144.08 ? 4063 ASN A CG    1 
ATOM   17285 O OD1   . ASN A 1 4063 ? 206.918 131.247 141.600 1.00 144.08 ? 4063 ASN A OD1   1 
ATOM   17286 N ND2   . ASN A 1 4063 ? 206.328 132.487 139.824 1.00 144.08 ? 4063 ASN A ND2   1 
ATOM   17287 N N     . THR A 1 4064 ? 204.784 135.710 142.280 1.00 134.28 ? 4064 THR A N     1 
ATOM   17288 C CA    . THR A 1 4064 ? 203.648 136.382 141.668 1.00 134.28 ? 4064 THR A CA    1 
ATOM   17289 C C     . THR A 1 4064 ? 203.764 137.877 141.918 1.00 134.28 ? 4064 THR A C     1 
ATOM   17290 O O     . THR A 1 4064 ? 203.996 138.304 143.054 1.00 134.28 ? 4064 THR A O     1 
ATOM   17291 C CB    . THR A 1 4064 ? 202.328 135.851 142.225 1.00 134.28 ? 4064 THR A CB    1 
ATOM   17292 O OG1   . THR A 1 4064 ? 202.426 134.433 142.408 1.00 134.28 ? 4064 THR A OG1   1 
ATOM   17293 C CG2   . THR A 1 4064 ? 201.190 136.156 141.269 1.00 134.28 ? 4064 THR A CG2   1 
ATOM   17294 N N     . GLN A 1 4065 ? 203.603 138.665 140.861 1.00 127.97 ? 4065 GLN A N     1 
ATOM   17295 C CA    . GLN A 1 4065 ? 203.790 140.105 140.963 1.00 127.97 ? 4065 GLN A CA    1 
ATOM   17296 C C     . GLN A 1 4065 ? 202.675 140.743 141.782 1.00 127.97 ? 4065 GLN A C     1 
ATOM   17297 O O     . GLN A 1 4065 ? 201.526 140.294 141.773 1.00 127.97 ? 4065 GLN A O     1 
ATOM   17298 C CB    . GLN A 1 4065 ? 203.876 140.723 139.560 1.00 127.97 ? 4065 GLN A CB    1 
ATOM   17299 C CG    . GLN A 1 4065 ? 202.558 141.078 138.849 1.00 127.97 ? 4065 GLN A CG    1 
ATOM   17300 C CD    . GLN A 1 4065 ? 201.828 142.280 139.431 1.00 127.97 ? 4065 GLN A CD    1 
ATOM   17301 O OE1   . GLN A 1 4065 ? 202.362 143.387 139.468 1.00 127.97 ? 4065 GLN A OE1   1 
ATOM   17302 N NE2   . GLN A 1 4065 ? 200.600 142.061 139.889 1.00 127.97 ? 4065 GLN A NE2   1 
ATOM   17303 N N     . ILE A 1 4066 ? 203.030 141.809 142.494 1.00 121.92 ? 4066 ILE A N     1 
ATOM   17304 C CA    . ILE A 1 4066 ? 202.081 142.629 143.235 1.00 121.92 ? 4066 ILE A CA    1 
ATOM   17305 C C     . ILE A 1 4066 ? 202.212 144.066 142.761 1.00 121.92 ? 4066 ILE A C     1 
ATOM   17306 O O     . ILE A 1 4066 ? 203.321 144.601 142.668 1.00 121.92 ? 4066 ILE A O     1 
ATOM   17307 C CB    . ILE A 1 4066 ? 202.308 142.553 144.757 1.00 121.92 ? 4066 ILE A CB    1 
ATOM   17308 C CG1   . ILE A 1 4066 ? 202.441 141.104 145.206 1.00 121.92 ? 4066 ILE A CG1   1 
ATOM   17309 C CG2   . ILE A 1 4066 ? 201.170 143.240 145.493 1.00 121.92 ? 4066 ILE A CG2   1 
ATOM   17310 C CD1   . ILE A 1 4066 ? 201.202 140.288 144.977 1.00 121.92 ? 4066 ILE A CD1   1 
ATOM   17311 N N     . THR A 1 4067 ? 201.078 144.689 142.465 1.00 115.73 ? 4067 THR A N     1 
ATOM   17312 C CA    . THR A 1 4067 ? 201.030 146.105 142.117 1.00 115.73 ? 4067 THR A CA    1 
ATOM   17313 C C     . THR A 1 4067 ? 200.755 146.873 143.404 1.00 115.73 ? 4067 THR A C     1 
ATOM   17314 O O     . THR A 1 4067 ? 199.606 147.087 143.785 1.00 115.73 ? 4067 THR A O     1 
ATOM   17315 C CB    . THR A 1 4067 ? 199.969 146.373 141.059 1.00 115.73 ? 4067 THR A CB    1 
ATOM   17316 O OG1   . THR A 1 4067 ? 200.007 145.336 140.072 1.00 115.73 ? 4067 THR A OG1   1 
ATOM   17317 C CG2   . THR A 1 4067 ? 200.222 147.709 140.387 1.00 115.73 ? 4067 THR A CG2   1 
ATOM   17318 N N     . SER A 1 4068 ? 201.822 147.270 144.091 1.00 114.35 ? 4068 SER A N     1 
ATOM   17319 C CA    . SER A 1 4068 ? 201.671 148.000 145.342 1.00 114.35 ? 4068 SER A CA    1 
ATOM   17320 C C     . SER A 1 4068 ? 201.189 149.418 145.070 1.00 114.35 ? 4068 SER A C     1 
ATOM   17321 O O     . SER A 1 4068 ? 201.794 150.152 144.284 1.00 114.35 ? 4068 SER A O     1 
ATOM   17322 C CB    . SER A 1 4068 ? 202.993 148.029 146.104 1.00 114.35 ? 4068 SER A CB    1 
ATOM   17323 O OG    . SER A 1 4068 ? 202.801 148.488 147.429 1.00 114.35 ? 4068 SER A OG    1 
ATOM   17324 N N     . ILE A 1 4069 ? 200.096 149.803 145.724 1.00 110.78 ? 4069 ILE A N     1 
ATOM   17325 C CA    . ILE A 1 4069 ? 199.462 151.098 145.507 1.00 110.78 ? 4069 ILE A CA    1 
ATOM   17326 C C     . ILE A 1 4069 ? 199.150 151.727 146.854 1.00 110.78 ? 4069 ILE A C     1 
ATOM   17327 O O     . ILE A 1 4069 ? 198.575 151.076 147.731 1.00 110.78 ? 4069 ILE A O     1 
ATOM   17328 C CB    . ILE A 1 4069 ? 198.171 150.969 144.677 1.00 110.78 ? 4069 ILE A CB    1 
ATOM   17329 C CG1   . ILE A 1 4069 ? 198.304 149.835 143.668 1.00 110.78 ? 4069 ILE A CG1   1 
ATOM   17330 C CG2   . ILE A 1 4069 ? 197.857 152.277 143.980 1.00 110.78 ? 4069 ILE A CG2   1 
ATOM   17331 C CD1   . ILE A 1 4069 ? 197.045 149.516 142.943 1.00 110.78 ? 4069 ILE A CD1   1 
ATOM   17332 N N     . ALA A 1 4070 ? 199.520 152.993 147.017 1.00 113.28 ? 4070 ALA A N     1 
ATOM   17333 C CA    . ALA A 1 4070 ? 199.129 153.766 148.184 1.00 113.28 ? 4070 ALA A CA    1 
ATOM   17334 C C     . ALA A 1 4070 ? 197.923 154.627 147.838 1.00 113.28 ? 4070 ALA A C     1 
ATOM   17335 O O     . ALA A 1 4070 ? 197.911 155.316 146.815 1.00 113.28 ? 4070 ALA A O     1 
ATOM   17336 C CB    . ALA A 1 4070 ? 200.283 154.639 148.674 1.00 113.28 ? 4070 ALA A CB    1 
ATOM   17337 N N     . ILE A 1 4071 ? 196.911 154.586 148.698 1.00 112.03 ? 4071 ILE A N     1 
ATOM   17338 C CA    . ILE A 1 4071 ? 195.625 155.205 148.411 1.00 112.03 ? 4071 ILE A CA    1 
ATOM   17339 C C     . ILE A 1 4071 ? 195.502 156.571 149.098 1.00 112.03 ? 4071 ILE A C     1 
ATOM   17340 O O     . ILE A 1 4071 ? 194.411 157.128 149.194 1.00 112.03 ? 4071 ILE A O     1 
ATOM   17341 C CB    . ILE A 1 4071 ? 194.471 154.260 148.790 1.00 112.03 ? 4071 ILE A CB    1 
ATOM   17342 C CG1   . ILE A 1 4071 ? 194.692 152.893 148.149 1.00 112.03 ? 4071 ILE A CG1   1 
ATOM   17343 C CG2   . ILE A 1 4071 ? 193.143 154.728 148.230 1.00 112.03 ? 4071 ILE A CG2   1 
ATOM   17344 C CD1   . ILE A 1 4071 ? 195.094 152.952 146.688 1.00 112.03 ? 4071 ILE A CD1   1 
ATOM   17345 N N     . GLY A 1 4072 ? 196.618 157.125 149.573 1.00 120.17 ? 4072 GLY A N     1 
ATOM   17346 C CA    . GLY A 1 4072 ? 196.572 158.450 150.171 1.00 120.17 ? 4072 GLY A CA    1 
ATOM   17347 C C     . GLY A 1 4072 ? 196.247 159.541 149.168 1.00 120.17 ? 4072 GLY A C     1 
ATOM   17348 O O     . GLY A 1 4072 ? 195.441 160.433 149.446 1.00 120.17 ? 4072 GLY A O     1 
ATOM   17349 N N     . SER A 1 4073 ? 196.863 159.486 147.991 1.00 132.53 ? 4073 SER A N     1 
ATOM   17350 C CA    . SER A 1 4073 ? 196.688 160.524 146.989 1.00 132.53 ? 4073 SER A CA    1 
ATOM   17351 C C     . SER A 1 4073 ? 195.414 160.295 146.183 1.00 132.53 ? 4073 SER A C     1 
ATOM   17352 O O     . SER A 1 4073 ? 194.853 159.196 146.151 1.00 132.53 ? 4073 SER A O     1 
ATOM   17353 C CB    . SER A 1 4073 ? 197.894 160.572 146.052 1.00 132.53 ? 4073 SER A CB    1 
ATOM   17354 O OG    . SER A 1 4073 ? 197.623 159.886 144.841 1.00 132.53 ? 4073 SER A OG    1 
ATOM   17355 N N     . ALA A 1 4074 ? 194.957 161.361 145.522 1.00 139.26 ? 4074 ALA A N     1 
ATOM   17356 C CA    . ALA A 1 4074 ? 193.780 161.249 144.666 1.00 139.26 ? 4074 ALA A CA    1 
ATOM   17357 C C     . ALA A 1 4074 ? 194.100 160.497 143.380 1.00 139.26 ? 4074 ALA A C     1 
ATOM   17358 O O     . ALA A 1 4074 ? 193.286 159.699 142.902 1.00 139.26 ? 4074 ALA A O     1 
ATOM   17359 C CB    . ALA A 1 4074 ? 193.223 162.637 144.354 1.00 139.26 ? 4074 ALA A CB    1 
ATOM   17360 N N     . GLU A 1 4075 ? 195.279 160.743 142.802 1.00 141.35 ? 4075 GLU A N     1 
ATOM   17361 C CA    . GLU A 1 4075 ? 195.706 160.001 141.621 1.00 141.35 ? 4075 GLU A CA    1 
ATOM   17362 C C     . GLU A 1 4075 ? 195.833 158.512 141.911 1.00 141.35 ? 4075 GLU A C     1 
ATOM   17363 O O     . GLU A 1 4075 ? 195.684 157.689 140.995 1.00 141.35 ? 4075 GLU A O     1 
ATOM   17364 C CB    . GLU A 1 4075 ? 197.033 160.574 141.112 1.00 141.35 ? 4075 GLU A CB    1 
ATOM   17365 C CG    . GLU A 1 4075 ? 197.695 159.797 139.984 1.00 141.35 ? 4075 GLU A CG    1 
ATOM   17366 C CD    . GLU A 1 4075 ? 198.724 158.804 140.488 1.00 141.35 ? 4075 GLU A CD    1 
ATOM   17367 O OE1   . GLU A 1 4075 ? 199.224 158.987 141.618 1.00 141.35 ? 4075 GLU A OE1   1 
ATOM   17368 O OE2   . GLU A 1 4075 ? 199.033 157.842 139.755 1.00 141.35 ? 4075 GLU A OE2   1 
ATOM   17369 N N     . GLY A 1 4076 ? 196.093 158.155 143.170 1.00 131.01 ? 4076 GLY A N     1 
ATOM   17370 C CA    . GLY A 1 4076 ? 196.127 156.756 143.544 1.00 131.01 ? 4076 GLY A CA    1 
ATOM   17371 C C     . GLY A 1 4076 ? 194.819 156.043 143.280 1.00 131.01 ? 4076 GLY A C     1 
ATOM   17372 O O     . GLY A 1 4076 ? 194.812 154.844 143.012 1.00 131.01 ? 4076 GLY A O     1 
ATOM   17373 N N     . PHE A 1 4077 ? 193.699 156.767 143.337 1.00 129.80 ? 4077 PHE A N     1 
ATOM   17374 C CA    . PHE A 1 4077 ? 192.411 156.162 143.010 1.00 129.80 ? 4077 PHE A CA    1 
ATOM   17375 C C     . PHE A 1 4077 ? 192.422 155.608 141.592 1.00 129.80 ? 4077 PHE A C     1 
ATOM   17376 O O     . PHE A 1 4077 ? 192.128 154.427 141.363 1.00 129.80 ? 4077 PHE A O     1 
ATOM   17377 C CB    . PHE A 1 4077 ? 191.298 157.201 143.151 1.00 129.80 ? 4077 PHE A CB    1 
ATOM   17378 C CG    . PHE A 1 4077 ? 190.915 157.512 144.569 1.00 129.80 ? 4077 PHE A CG    1 
ATOM   17379 C CD1   . PHE A 1 4077 ? 191.689 157.081 145.631 1.00 129.80 ? 4077 PHE A CD1   1 
ATOM   17380 C CD2   . PHE A 1 4077 ? 189.786 158.268 144.834 1.00 129.80 ? 4077 PHE A CD2   1 
ATOM   17381 C CE1   . PHE A 1 4077 ? 191.332 157.382 146.929 1.00 129.80 ? 4077 PHE A CE1   1 
ATOM   17382 C CE2   . PHE A 1 4077 ? 189.423 158.567 146.129 1.00 129.80 ? 4077 PHE A CE2   1 
ATOM   17383 C CZ    . PHE A 1 4077 ? 190.198 158.125 147.178 1.00 129.80 ? 4077 PHE A CZ    1 
ATOM   17384 N N     . ASN A 1 4078 ? 192.782 156.454 140.626 1.00 135.71 ? 4078 ASN A N     1 
ATOM   17385 C CA    . ASN A 1 4078 ? 192.816 156.030 139.234 1.00 135.71 ? 4078 ASN A CA    1 
ATOM   17386 C C     . ASN A 1 4078 ? 193.883 154.969 139.010 1.00 135.71 ? 4078 ASN A C     1 
ATOM   17387 O O     . ASN A 1 4078 ? 193.661 153.999 138.272 1.00 135.71 ? 4078 ASN A O     1 
ATOM   17388 C CB    . ASN A 1 4078 ? 193.062 157.238 138.333 1.00 135.71 ? 4078 ASN A CB    1 
ATOM   17389 C CG    . ASN A 1 4078 ? 191.993 158.297 138.483 1.00 135.71 ? 4078 ASN A CG    1 
ATOM   17390 O OD1   . ASN A 1 4078 ? 190.924 158.040 139.036 1.00 135.71 ? 4078 ASN A OD1   1 
ATOM   17391 N ND2   . ASN A 1 4078 ? 192.279 159.499 137.999 1.00 135.71 ? 4078 ASN A ND2   1 
ATOM   17392 N N     . GLN A 1 4079 ? 195.053 155.141 139.631 1.00 136.14 ? 4079 GLN A N     1 
ATOM   17393 C CA    . GLN A 1 4079 ? 196.115 154.156 139.462 1.00 136.14 ? 4079 GLN A CA    1 
ATOM   17394 C C     . GLN A 1 4079 ? 195.662 152.790 139.953 1.00 136.14 ? 4079 GLN A C     1 
ATOM   17395 O O     . GLN A 1 4079 ? 195.875 151.774 139.283 1.00 136.14 ? 4079 GLN A O     1 
ATOM   17396 C CB    . GLN A 1 4079 ? 197.377 154.600 140.200 1.00 136.14 ? 4079 GLN A CB    1 
ATOM   17397 C CG    . GLN A 1 4079 ? 198.386 153.478 140.384 1.00 136.14 ? 4079 GLN A CG    1 
ATOM   17398 C CD    . GLN A 1 4079 ? 199.817 153.934 140.192 1.00 136.14 ? 4079 GLN A CD    1 
ATOM   17399 O OE1   . GLN A 1 4079 ? 200.109 155.129 140.211 1.00 136.14 ? 4079 GLN A OE1   1 
ATOM   17400 N NE2   . GLN A 1 4079 ? 200.721 152.979 140.001 1.00 136.14 ? 4079 GLN A NE2   1 
ATOM   17401 N N     . ALA A 1 4080 ? 195.006 152.753 141.113 1.00 132.92 ? 4080 ALA A N     1 
ATOM   17402 C CA    . ALA A 1 4080 ? 194.506 151.498 141.650 1.00 132.92 ? 4080 ALA A CA    1 
ATOM   17403 C C     . ALA A 1 4080 ? 193.434 150.904 140.754 1.00 132.92 ? 4080 ALA A C     1 
ATOM   17404 O O     . ALA A 1 4080 ? 193.409 149.690 140.539 1.00 132.92 ? 4080 ALA A O     1 
ATOM   17405 C CB    . ALA A 1 4080 ? 193.968 151.711 143.063 1.00 132.92 ? 4080 ALA A CB    1 
ATOM   17406 N N     . ASP A 1 4081 ? 192.532 151.735 140.232 1.00 133.40 ? 4081 ASP A N     1 
ATOM   17407 C CA    . ASP A 1 4081 ? 191.483 151.202 139.372 1.00 133.40 ? 4081 ASP A CA    1 
ATOM   17408 C C     . ASP A 1 4081 ? 192.077 150.543 138.133 1.00 133.40 ? 4081 ASP A C     1 
ATOM   17409 O O     . ASP A 1 4081 ? 191.738 149.400 137.797 1.00 133.40 ? 4081 ASP A O     1 
ATOM   17410 C CB    . ASP A 1 4081 ? 190.505 152.310 138.989 1.00 133.40 ? 4081 ASP A CB    1 
ATOM   17411 C CG    . ASP A 1 4081 ? 189.061 151.869 139.102 1.00 133.40 ? 4081 ASP A CG    1 
ATOM   17412 O OD1   . ASP A 1 4081 ? 188.774 150.694 138.791 1.00 133.40 ? 4081 ASP A OD1   1 
ATOM   17413 O OD2   . ASP A 1 4081 ? 188.215 152.691 139.512 1.00 133.40 ? 4081 ASP A OD2   1 
ATOM   17414 N N     . LYS A 1 4082 ? 192.996 151.237 137.456 1.00 133.88 ? 4082 LYS A N     1 
ATOM   17415 C CA    . LYS A 1 4082 ? 193.611 150.650 136.267 1.00 133.88 ? 4082 LYS A CA    1 
ATOM   17416 C C     . LYS A 1 4082 ? 194.419 149.408 136.621 1.00 133.88 ? 4082 LYS A C     1 
ATOM   17417 O O     . LYS A 1 4082 ? 194.387 148.409 135.890 1.00 133.88 ? 4082 LYS A O     1 
ATOM   17418 C CB    . LYS A 1 4082 ? 194.490 151.674 135.543 1.00 133.88 ? 4082 LYS A CB    1 
ATOM   17419 C CG    . LYS A 1 4082 ? 193.885 153.066 135.350 1.00 133.88 ? 4082 LYS A CG    1 
ATOM   17420 C CD    . LYS A 1 4082 ? 192.404 153.031 134.977 1.00 133.88 ? 4082 LYS A CD    1 
ATOM   17421 C CE    . LYS A 1 4082 ? 192.180 152.437 133.595 1.00 133.88 ? 4082 LYS A CE    1 
ATOM   17422 N NZ    . LYS A 1 4082 ? 190.734 152.221 133.317 1.00 133.88 ? 4082 LYS A NZ    1 
ATOM   17423 N N     . ALA A 1 4083 ? 195.147 149.449 137.739 1.00 131.79 ? 4083 ALA A N     1 
ATOM   17424 C CA    . ALA A 1 4083 ? 195.962 148.306 138.128 1.00 131.79 ? 4083 ALA A CA    1 
ATOM   17425 C C     . ALA A 1 4083 ? 195.103 147.085 138.414 1.00 131.79 ? 4083 ALA A C     1 
ATOM   17426 O O     . ALA A 1 4083 ? 195.423 145.979 137.966 1.00 131.79 ? 4083 ALA A O     1 
ATOM   17427 C CB    . ALA A 1 4083 ? 196.814 148.661 139.345 1.00 131.79 ? 4083 ALA A CB    1 
ATOM   17428 N N     . ILE A 1 4084 ? 194.003 147.261 139.150 1.00 130.82 ? 4084 ILE A N     1 
ATOM   17429 C CA    . ILE A 1 4084 ? 193.153 146.118 139.463 1.00 130.82 ? 4084 ILE A CA    1 
ATOM   17430 C C     . ILE A 1 4084 ? 192.468 145.606 138.205 1.00 130.82 ? 4084 ILE A C     1 
ATOM   17431 O O     . ILE A 1 4084 ? 192.272 144.398 138.051 1.00 130.82 ? 4084 ILE A O     1 
ATOM   17432 C CB    . ILE A 1 4084 ? 192.137 146.451 140.573 1.00 130.82 ? 4084 ILE A CB    1 
ATOM   17433 C CG1   . ILE A 1 4084 ? 191.118 147.489 140.113 1.00 130.82 ? 4084 ILE A CG1   1 
ATOM   17434 C CG2   . ILE A 1 4084 ? 192.846 146.904 141.834 1.00 130.82 ? 4084 ILE A CG2   1 
ATOM   17435 C CD1   . ILE A 1 4084 ? 189.713 147.188 140.566 1.00 130.82 ? 4084 ILE A CD1   1 
ATOM   17436 N N     . ASN A 1 4085 ? 192.100 146.502 137.283 1.00 130.48 ? 4085 ASN A N     1 
ATOM   17437 C CA    . ASN A 1 4085 ? 191.517 146.047 136.024 1.00 130.48 ? 4085 ASN A CA    1 
ATOM   17438 C C     . ASN A 1 4085 ? 192.501 145.180 135.247 1.00 130.48 ? 4085 ASN A C     1 
ATOM   17439 O O     . ASN A 1 4085 ? 192.161 144.077 134.797 1.00 130.48 ? 4085 ASN A O     1 
ATOM   17440 C CB    . ASN A 1 4085 ? 191.073 147.245 135.187 1.00 130.48 ? 4085 ASN A CB    1 
ATOM   17441 C CG    . ASN A 1 4085 ? 189.963 148.033 135.848 1.00 130.48 ? 4085 ASN A CG    1 
ATOM   17442 O OD1   . ASN A 1 4085 ? 189.069 147.463 136.471 1.00 130.48 ? 4085 ASN A OD1   1 
ATOM   17443 N ND2   . ASN A 1 4085 ? 190.017 149.353 135.720 1.00 130.48 ? 4085 ASN A ND2   1 
ATOM   17444 N N     . THR A 1 4086 ? 193.736 145.659 135.090 1.00 132.52 ? 4086 THR A N     1 
ATOM   17445 C CA    . THR A 1 4086 ? 194.740 144.873 134.381 1.00 132.52 ? 4086 THR A CA    1 
ATOM   17446 C C     . THR A 1 4086 ? 195.010 143.556 135.095 1.00 132.52 ? 4086 THR A C     1 
ATOM   17447 O O     . THR A 1 4086 ? 195.202 142.519 134.450 1.00 132.52 ? 4086 THR A O     1 
ATOM   17448 C CB    . THR A 1 4086 ? 196.032 145.672 134.233 1.00 132.52 ? 4086 THR A CB    1 
ATOM   17449 O OG1   . THR A 1 4086 ? 196.551 145.989 135.531 1.00 132.52 ? 4086 THR A OG1   1 
ATOM   17450 C CG2   . THR A 1 4086 ? 195.781 146.954 133.455 1.00 132.52 ? 4086 THR A CG2   1 
ATOM   17451 N N     . ALA A 1 4087 ? 195.026 143.578 136.429 1.00 131.64 ? 4087 ALA A N     1 
ATOM   17452 C CA    . ALA A 1 4087 ? 195.295 142.362 137.186 1.00 131.64 ? 4087 ALA A CA    1 
ATOM   17453 C C     . ALA A 1 4087 ? 194.186 141.335 137.003 1.00 131.64 ? 4087 ALA A C     1 
ATOM   17454 O O     . ALA A 1 4087 ? 194.466 140.152 136.780 1.00 131.64 ? 4087 ALA A O     1 
ATOM   17455 C CB    . ALA A 1 4087 ? 195.480 142.694 138.665 1.00 131.64 ? 4087 ALA A CB    1 
ATOM   17456 N N     . VAL A 1 4088 ? 192.922 141.760 137.089 1.00 131.87 ? 4088 VAL A N     1 
ATOM   17457 C CA    . VAL A 1 4088 ? 191.835 140.800 136.958 1.00 131.87 ? 4088 VAL A CA    1 
ATOM   17458 C C     . VAL A 1 4088 ? 191.758 140.289 135.529 1.00 131.87 ? 4088 VAL A C     1 
ATOM   17459 O O     . VAL A 1 4088 ? 191.392 139.129 135.307 1.00 131.87 ? 4088 VAL A O     1 
ATOM   17460 C CB    . VAL A 1 4088 ? 190.479 141.395 137.398 1.00 131.87 ? 4088 VAL A CB    1 
ATOM   17461 C CG1   . VAL A 1 4088 ? 190.209 142.728 136.738 1.00 131.87 ? 4088 VAL A CG1   1 
ATOM   17462 C CG2   . VAL A 1 4088 ? 189.345 140.424 137.155 1.00 131.87 ? 4088 VAL A CG2   1 
ATOM   17463 N N     . LYS A 1 4089 ? 192.121 141.114 134.545 1.00 132.75 ? 4089 LYS A N     1 
ATOM   17464 C CA    . LYS A 1 4089 ? 192.189 140.615 133.176 1.00 132.75 ? 4089 LYS A CA    1 
ATOM   17465 C C     . LYS A 1 4089 ? 193.274 139.553 133.042 1.00 132.75 ? 4089 LYS A C     1 
ATOM   17466 O O     . LYS A 1 4089 ? 193.000 138.409 132.661 1.00 132.75 ? 4089 LYS A O     1 
ATOM   17467 C CB    . LYS A 1 4089 ? 192.444 141.768 132.204 1.00 132.75 ? 4089 LYS A CB    1 
ATOM   17468 C CG    . LYS A 1 4089 ? 191.302 142.765 132.076 1.00 132.75 ? 4089 LYS A CG    1 
ATOM   17469 C CD    . LYS A 1 4089 ? 189.947 142.129 132.332 1.00 132.75 ? 4089 LYS A CD    1 
ATOM   17470 C CE    . LYS A 1 4089 ? 188.862 143.189 132.417 1.00 132.75 ? 4089 LYS A CE    1 
ATOM   17471 N NZ    . LYS A 1 4089 ? 189.196 144.241 133.418 1.00 132.75 ? 4089 LYS A NZ    1 
ATOM   17472 N N     . SER A 1 4090 ? 194.516 139.912 133.370 1.00 134.56 ? 4090 SER A N     1 
ATOM   17473 C CA    . SER A 1 4090 ? 195.635 139.002 133.149 1.00 134.56 ? 4090 SER A CA    1 
ATOM   17474 C C     . SER A 1 4090 ? 195.671 137.889 134.188 1.00 134.56 ? 4090 SER A C     1 
ATOM   17475 O O     . SER A 1 4090 ? 196.166 136.791 133.909 1.00 134.56 ? 4090 SER A O     1 
ATOM   17476 C CB    . SER A 1 4090 ? 196.949 139.781 133.159 1.00 134.56 ? 4090 SER A CB    1 
ATOM   17477 O OG    . SER A 1 4090 ? 196.934 140.782 134.161 1.00 134.56 ? 4090 SER A OG    1 
ATOM   17478 N N     . GLY A 1 4091 ? 195.168 138.149 135.383 1.00 132.08 ? 4091 GLY A N     1 
ATOM   17479 C CA    . GLY A 1 4091 ? 195.234 137.203 136.470 1.00 132.08 ? 4091 GLY A CA    1 
ATOM   17480 C C     . GLY A 1 4091 ? 196.302 137.475 137.512 1.00 132.08 ? 4091 GLY A C     1 
ATOM   17481 O O     . GLY A 1 4091 ? 196.508 136.627 138.390 1.00 132.08 ? 4091 GLY A O     1 
ATOM   17482 N N     . ARG A 1 4092 ? 196.979 138.618 137.448 1.00 129.64 ? 4092 ARG A N     1 
ATOM   17483 C CA    . ARG A 1 4092 ? 198.008 138.955 138.415 1.00 129.64 ? 4092 ARG A CA    1 
ATOM   17484 C C     . ARG A 1 4092 ? 197.356 139.501 139.685 1.00 129.64 ? 4092 ARG A C     1 
ATOM   17485 O O     . ARG A 1 4092 ? 196.144 139.719 139.745 1.00 129.64 ? 4092 ARG A O     1 
ATOM   17486 C CB    . ARG A 1 4092 ? 198.994 139.951 137.808 1.00 129.64 ? 4092 ARG A CB    1 
ATOM   17487 C CG    . ARG A 1 4092 ? 200.026 139.309 136.887 1.00 129.64 ? 4092 ARG A CG    1 
ATOM   17488 C CD    . ARG A 1 4092 ? 200.664 140.336 135.961 1.00 129.64 ? 4092 ARG A CD    1 
ATOM   17489 N NE    . ARG A 1 4092 ? 199.712 140.879 134.999 1.00 129.64 ? 4092 ARG A NE    1 
ATOM   17490 C CZ    . ARG A 1 4092 ? 199.568 142.171 134.742 1.00 129.64 ? 4092 ARG A CZ    1 
ATOM   17491 N NH1   . ARG A 1 4092 ? 200.304 143.084 135.353 1.00 129.64 ? 4092 ARG A NH1   1 
ATOM   17492 N NH2   . ARG A 1 4092 ? 198.659 142.558 133.851 1.00 129.64 ? 4092 ARG A NH2   1 
ATOM   17493 N N     . TRP A 1 4093 ? 198.166 139.726 140.716 1.00 122.25 ? 4093 TRP A N     1 
ATOM   17494 C CA    . TRP A 1 4093 ? 197.677 140.117 142.031 1.00 122.25 ? 4093 TRP A CA    1 
ATOM   17495 C C     . TRP A 1 4093 ? 197.928 141.597 142.274 1.00 122.25 ? 4093 TRP A C     1 
ATOM   17496 O O     . TRP A 1 4093 ? 198.920 142.158 141.796 1.00 122.25 ? 4093 TRP A O     1 
ATOM   17497 C CB    . TRP A 1 4093 ? 198.350 139.307 143.138 1.00 122.25 ? 4093 TRP A CB    1 
ATOM   17498 C CG    . TRP A 1 4093 ? 198.003 137.863 143.147 1.00 122.25 ? 4093 TRP A CG    1 
ATOM   17499 C CD1   . TRP A 1 4093 ? 197.241 137.198 142.237 1.00 122.25 ? 4093 TRP A CD1   1 
ATOM   17500 C CD2   . TRP A 1 4093 ? 198.405 136.895 144.121 1.00 122.25 ? 4093 TRP A CD2   1 
ATOM   17501 N NE1   . TRP A 1 4093 ? 197.145 135.872 142.581 1.00 122.25 ? 4093 TRP A NE1   1 
ATOM   17502 C CE2   . TRP A 1 4093 ? 197.852 135.661 143.735 1.00 122.25 ? 4093 TRP A CE2   1 
ATOM   17503 C CE3   . TRP A 1 4093 ? 199.181 136.953 145.282 1.00 122.25 ? 4093 TRP A CE3   1 
ATOM   17504 C CZ2   . TRP A 1 4093 ? 198.048 134.494 144.469 1.00 122.25 ? 4093 TRP A CZ2   1 
ATOM   17505 C CZ3   . TRP A 1 4093 ? 199.374 135.795 146.007 1.00 122.25 ? 4093 TRP A CZ3   1 
ATOM   17506 C CH2   . TRP A 1 4093 ? 198.811 134.582 145.599 1.00 122.25 ? 4093 TRP A CH2   1 
ATOM   17507 N N     . VAL A 1 4094 ? 197.023 142.222 143.024 1.00 111.22 ? 4094 VAL A N     1 
ATOM   17508 C CA    . VAL A 1 4094 ? 197.118 143.630 143.386 1.00 111.22 ? 4094 VAL A CA    1 
ATOM   17509 C C     . VAL A 1 4094 ? 196.772 143.769 144.861 1.00 111.22 ? 4094 VAL A C     1 
ATOM   17510 O O     . VAL A 1 4094 ? 195.769 143.213 145.323 1.00 111.22 ? 4094 VAL A O     1 
ATOM   17511 C CB    . VAL A 1 4094 ? 196.190 144.503 142.521 1.00 111.22 ? 4094 VAL A CB    1 
ATOM   17512 C CG1   . VAL A 1 4094 ? 194.790 143.922 142.498 1.00 111.22 ? 4094 VAL A CG1   1 
ATOM   17513 C CG2   . VAL A 1 4094 ? 196.167 145.928 143.038 1.00 111.22 ? 4094 VAL A CG2   1 
ATOM   17514 N N     . MET A 1 4095 ? 197.605 144.499 145.598 1.00 112.13 ? 4095 MET A N     1 
ATOM   17515 C CA    . MET A 1 4095 ? 197.389 144.752 147.015 1.00 112.13 ? 4095 MET A CA    1 
ATOM   17516 C C     . MET A 1 4095 ? 197.441 146.253 147.245 1.00 112.13 ? 4095 MET A C     1 
ATOM   17517 O O     . MET A 1 4095 ? 198.317 146.937 146.710 1.00 112.13 ? 4095 MET A O     1 
ATOM   17518 C CB    . MET A 1 4095 ? 198.438 144.006 147.870 1.00 112.13 ? 4095 MET A CB    1 
ATOM   17519 C CG    . MET A 1 4095 ? 198.738 144.545 149.282 1.00 112.13 ? 4095 MET A CG    1 
ATOM   17520 S SD    . MET A 1 4095 ? 199.501 146.167 149.492 1.00 112.13 ? 4095 MET A SD    1 
ATOM   17521 C CE    . MET A 1 4095 ? 200.903 146.002 148.389 1.00 112.13 ? 4095 MET A CE    1 
ATOM   17522 N N     . LEU A 1 4096 ? 196.529 146.759 148.068 1.00 105.43 ? 4096 LEU A N     1 
ATOM   17523 C CA    . LEU A 1 4096 ? 196.362 148.193 148.262 1.00 105.43 ? 4096 LEU A CA    1 
ATOM   17524 C C     . LEU A 1 4096 ? 196.655 148.551 149.710 1.00 105.43 ? 4096 LEU A C     1 
ATOM   17525 O O     . LEU A 1 4096 ? 196.217 147.850 150.627 1.00 105.43 ? 4096 LEU A O     1 
ATOM   17526 C CB    . LEU A 1 4096 ? 194.951 148.634 147.876 1.00 105.43 ? 4096 LEU A CB    1 
ATOM   17527 C CG    . LEU A 1 4096 ? 194.624 148.610 146.382 1.00 105.43 ? 4096 LEU A CG    1 
ATOM   17528 C CD1   . LEU A 1 4096 ? 194.260 147.214 145.908 1.00 105.43 ? 4096 LEU A CD1   1 
ATOM   17529 C CD2   . LEU A 1 4096 ? 193.512 149.586 146.061 1.00 105.43 ? 4096 LEU A CD2   1 
ATOM   17530 N N     . LYS A 1 4097 ? 197.383 149.645 149.912 1.00 106.59 ? 4097 LYS A N     1 
ATOM   17531 C CA    . LYS A 1 4097 ? 197.891 150.020 151.224 1.00 106.59 ? 4097 LYS A CA    1 
ATOM   17532 C C     . LYS A 1 4097 ? 197.092 151.174 151.816 1.00 106.59 ? 4097 LYS A C     1 
ATOM   17533 O O     . LYS A 1 4097 ? 196.847 152.182 151.147 1.00 106.59 ? 4097 LYS A O     1 
ATOM   17534 C CB    . LYS A 1 4097 ? 199.367 150.407 151.133 1.00 106.59 ? 4097 LYS A CB    1 
ATOM   17535 C CG    . LYS A 1 4097 ? 200.142 149.613 150.099 1.00 106.59 ? 4097 LYS A CG    1 
ATOM   17536 C CD    . LYS A 1 4097 ? 201.537 150.178 149.876 1.00 106.59 ? 4097 LYS A CD    1 
ATOM   17537 C CE    . LYS A 1 4097 ? 202.309 150.302 151.178 1.00 106.59 ? 4097 LYS A CE    1 
ATOM   17538 N NZ    . LYS A 1 4097 ? 203.548 151.108 151.005 1.00 106.59 ? 4097 LYS A NZ    1 
ATOM   17539 N N     . ASN A 1 4098 ? 196.696 151.017 153.080 1.00 104.10 ? 4098 ASN A N     1 
ATOM   17540 C CA    . ASN A 1 4098 ? 196.051 152.078 153.856 1.00 104.10 ? 4098 ASN A CA    1 
ATOM   17541 C C     . ASN A 1 4098 ? 194.770 152.564 153.182 1.00 104.10 ? 4098 ASN A C     1 
ATOM   17542 O O     . ASN A 1 4098 ? 194.593 153.754 152.917 1.00 104.10 ? 4098 ASN A O     1 
ATOM   17543 C CB    . ASN A 1 4098 ? 197.015 153.242 154.092 1.00 104.10 ? 4098 ASN A CB    1 
ATOM   17544 C CG    . ASN A 1 4098 ? 198.390 152.781 154.519 1.00 104.10 ? 4098 ASN A CG    1 
ATOM   17545 O OD1   . ASN A 1 4098 ? 198.552 151.681 155.044 1.00 104.10 ? 4098 ASN A OD1   1 
ATOM   17546 N ND2   . ASN A 1 4098 ? 199.392 153.624 154.302 1.00 104.10 ? 4098 ASN A ND2   1 
ATOM   17547 N N     . VAL A 1 4099 ? 193.859 151.627 152.912 1.00 100.46 ? 4099 VAL A N     1 
ATOM   17548 C CA    . VAL A 1 4099 ? 192.625 151.977 152.212 1.00 100.46 ? 4099 VAL A CA    1 
ATOM   17549 C C     . VAL A 1 4099 ? 191.525 152.459 153.139 1.00 100.46 ? 4099 VAL A C     1 
ATOM   17550 O O     . VAL A 1 4099 ? 190.432 152.788 152.664 1.00 100.46 ? 4099 VAL A O     1 
ATOM   17551 C CB    . VAL A 1 4099 ? 192.084 150.786 151.404 1.00 100.46 ? 4099 VAL A CB    1 
ATOM   17552 C CG1   . VAL A 1 4099 ? 193.157 150.257 150.478 1.00 100.46 ? 4099 VAL A CG1   1 
ATOM   17553 C CG2   . VAL A 1 4099 ? 191.591 149.708 152.333 1.00 100.46 ? 4099 VAL A CG2   1 
ATOM   17554 N N     . HIS A 1 4100 ? 191.771 152.505 154.447 1.00 104.15 ? 4100 HIS A N     1 
ATOM   17555 C CA    . HIS A 1 4100 ? 190.751 152.982 155.370 1.00 104.15 ? 4100 HIS A CA    1 
ATOM   17556 C C     . HIS A 1 4100 ? 190.522 154.481 155.268 1.00 104.15 ? 4100 HIS A C     1 
ATOM   17557 O O     . HIS A 1 4100 ? 189.576 154.989 155.878 1.00 104.15 ? 4100 HIS A O     1 
ATOM   17558 C CB    . HIS A 1 4100 ? 191.124 152.611 156.804 1.00 104.15 ? 4100 HIS A CB    1 
ATOM   17559 C CG    . HIS A 1 4100 ? 192.466 153.116 157.229 1.00 104.15 ? 4100 HIS A CG    1 
ATOM   17560 N ND1   . HIS A 1 4100 ? 193.644 152.629 156.705 1.00 104.15 ? 4100 HIS A ND1   1 
ATOM   17561 C CD2   . HIS A 1 4100 ? 192.818 154.059 158.133 1.00 104.15 ? 4100 HIS A CD2   1 
ATOM   17562 C CE1   . HIS A 1 4100 ? 194.664 153.252 157.267 1.00 104.15 ? 4100 HIS A CE1   1 
ATOM   17563 N NE2   . HIS A 1 4100 ? 194.190 154.126 158.136 1.00 104.15 ? 4100 HIS A NE2   1 
ATOM   17564 N N     . LEU A 1 4101 ? 191.356 155.198 154.520 1.00 101.47 ? 4101 LEU A N     1 
ATOM   17565 C CA    . LEU A 1 4101 ? 191.236 156.645 154.414 1.00 101.47 ? 4101 LEU A CA    1 
ATOM   17566 C C     . LEU A 1 4101 ? 190.101 157.094 153.502 1.00 101.47 ? 4101 LEU A C     1 
ATOM   17567 O O     . LEU A 1 4101 ? 189.704 158.261 153.574 1.00 101.47 ? 4101 LEU A O     1 
ATOM   17568 C CB    . LEU A 1 4101 ? 192.552 157.246 153.911 1.00 101.47 ? 4101 LEU A CB    1 
ATOM   17569 C CG    . LEU A 1 4101 ? 193.727 157.382 154.885 1.00 101.47 ? 4101 LEU A CG    1 
ATOM   17570 C CD1   . LEU A 1 4101 ? 194.302 156.034 155.280 1.00 101.47 ? 4101 LEU A CD1   1 
ATOM   17571 C CD2   . LEU A 1 4101 ? 194.808 158.258 154.280 1.00 101.47 ? 4101 LEU A CD2   1 
ATOM   17572 N N     . ALA A 1 4102 ? 189.565 156.214 152.657 1.00 109.95 ? 4102 ALA A N     1 
ATOM   17573 C CA    . ALA A 1 4102 ? 188.558 156.583 151.661 1.00 109.95 ? 4102 ALA A CA    1 
ATOM   17574 C C     . ALA A 1 4102 ? 187.372 155.633 151.744 1.00 109.95 ? 4102 ALA A C     1 
ATOM   17575 O O     . ALA A 1 4102 ? 187.242 154.709 150.931 1.00 109.95 ? 4102 ALA A O     1 
ATOM   17576 C CB    . ALA A 1 4102 ? 189.154 156.585 150.253 1.00 109.95 ? 4102 ALA A CB    1 
ATOM   17577 N N     . PRO A 1 4103 ? 186.486 155.829 152.723 1.00 110.27 ? 4103 PRO A N     1 
ATOM   17578 C CA    . PRO A 1 4103 ? 185.329 154.925 152.848 1.00 110.27 ? 4103 PRO A CA    1 
ATOM   17579 C C     . PRO A 1 4103 ? 184.419 154.900 151.628 1.00 110.27 ? 4103 PRO A C     1 
ATOM   17580 O O     . PRO A 1 4103 ? 183.931 153.827 151.259 1.00 110.27 ? 4103 PRO A O     1 
ATOM   17581 C CB    . PRO A 1 4103 ? 184.602 155.466 154.087 1.00 110.27 ? 4103 PRO A CB    1 
ATOM   17582 C CG    . PRO A 1 4103 ? 185.650 156.209 154.852 1.00 110.27 ? 4103 PRO A CG    1 
ATOM   17583 C CD    . PRO A 1 4103 ? 186.555 156.803 153.824 1.00 110.27 ? 4103 PRO A CD    1 
ATOM   17584 N N     . GLY A 1 4104 ? 184.162 156.047 150.997 1.00 115.04 ? 4104 GLY A N     1 
ATOM   17585 C CA    . GLY A 1 4104 ? 183.258 156.061 149.854 1.00 115.04 ? 4104 GLY A CA    1 
ATOM   17586 C C     . GLY A 1 4104 ? 183.839 155.365 148.638 1.00 115.04 ? 4104 GLY A C     1 
ATOM   17587 O O     . GLY A 1 4104 ? 183.144 154.628 147.935 1.00 115.04 ? 4104 GLY A O     1 
ATOM   17588 N N     . TRP A 1 4105 ? 185.123 155.590 148.378 1.00 115.93 ? 4105 TRP A N     1 
ATOM   17589 C CA    . TRP A 1 4105 ? 185.827 154.845 147.341 1.00 115.93 ? 4105 TRP A CA    1 
ATOM   17590 C C     . TRP A 1 4105 ? 185.843 153.347 147.635 1.00 115.93 ? 4105 TRP A C     1 
ATOM   17591 O O     . TRP A 1 4105 ? 185.659 152.521 146.725 1.00 115.93 ? 4105 TRP A O     1 
ATOM   17592 C CB    . TRP A 1 4105 ? 187.221 155.462 147.193 1.00 115.93 ? 4105 TRP A CB    1 
ATOM   17593 C CG    . TRP A 1 4105 ? 188.136 154.860 146.213 1.00 115.93 ? 4105 TRP A CG    1 
ATOM   17594 C CD1   . TRP A 1 4105 ? 188.505 155.366 145.004 1.00 115.93 ? 4105 TRP A CD1   1 
ATOM   17595 C CD2   . TRP A 1 4105 ? 189.005 153.760 146.465 1.00 115.93 ? 4105 TRP A CD2   1 
ATOM   17596 N NE1   . TRP A 1 4105 ? 189.463 154.567 144.430 1.00 115.93 ? 4105 TRP A NE1   1 
ATOM   17597 C CE2   . TRP A 1 4105 ? 189.795 153.577 145.315 1.00 115.93 ? 4105 TRP A CE2   1 
ATOM   17598 C CE3   . TRP A 1 4105 ? 189.159 152.878 147.538 1.00 115.93 ? 4105 TRP A CE3   1 
ATOM   17599 C CZ2   . TRP A 1 4105 ? 190.719 152.544 145.204 1.00 115.93 ? 4105 TRP A CZ2   1 
ATOM   17600 C CZ3   . TRP A 1 4105 ? 190.071 151.855 147.427 1.00 115.93 ? 4105 TRP A CZ3   1 
ATOM   17601 C CH2   . TRP A 1 4105 ? 190.840 151.694 146.268 1.00 115.93 ? 4105 TRP A CH2   1 
ATOM   17602 N N     . LEU A 1 4106 ? 186.017 152.977 148.905 1.00 111.65 ? 4106 LEU A N     1 
ATOM   17603 C CA    . LEU A 1 4106 ? 185.916 151.573 149.285 1.00 111.65 ? 4106 LEU A CA    1 
ATOM   17604 C C     . LEU A 1 4106 ? 184.531 151.018 148.968 1.00 111.65 ? 4106 LEU A C     1 
ATOM   17605 O O     . LEU A 1 4106 ? 184.405 149.905 148.440 1.00 111.65 ? 4106 LEU A O     1 
ATOM   17606 C CB    . LEU A 1 4106 ? 186.243 151.418 150.769 1.00 111.65 ? 4106 LEU A CB    1 
ATOM   17607 C CG    . LEU A 1 4106 ? 187.207 150.280 151.092 1.00 111.65 ? 4106 LEU A CG    1 
ATOM   17608 C CD1   . LEU A 1 4106 ? 188.529 150.516 150.397 1.00 111.65 ? 4106 LEU A CD1   1 
ATOM   17609 C CD2   . LEU A 1 4106 ? 187.416 150.139 152.589 1.00 111.65 ? 4106 LEU A CD2   1 
ATOM   17610 N N     . MET A 1 4107 ? 183.485 151.791 149.264 1.00 117.78 ? 4107 MET A N     1 
ATOM   17611 C CA    . MET A 1 4107 ? 182.132 151.440 148.838 1.00 117.78 ? 4107 MET A CA    1 
ATOM   17612 C C     . MET A 1 4107 ? 182.071 151.223 147.331 1.00 117.78 ? 4107 MET A C     1 
ATOM   17613 O O     . MET A 1 4107 ? 181.444 150.270 146.847 1.00 117.78 ? 4107 MET A O     1 
ATOM   17614 C CB    . MET A 1 4107 ? 181.164 152.551 149.252 1.00 117.78 ? 4107 MET A CB    1 
ATOM   17615 C CG    . MET A 1 4107 ? 179.780 152.134 149.738 1.00 117.78 ? 4107 MET A CG    1 
ATOM   17616 S SD    . MET A 1 4107 ? 179.679 150.773 150.907 1.00 117.78 ? 4107 MET A SD    1 
ATOM   17617 C CE    . MET A 1 4107 ? 179.454 149.395 149.792 1.00 117.78 ? 4107 MET A CE    1 
ATOM   17618 N N     . GLN A 1 4108 ? 182.716 152.113 146.573 1.00 120.48 ? 4108 GLN A N     1 
ATOM   17619 C CA    . GLN A 1 4108 ? 182.625 152.058 145.118 1.00 120.48 ? 4108 GLN A CA    1 
ATOM   17620 C C     . GLN A 1 4108 ? 183.201 150.761 144.562 1.00 120.48 ? 4108 GLN A C     1 
ATOM   17621 O O     . GLN A 1 4108 ? 182.545 150.079 143.766 1.00 120.48 ? 4108 GLN A O     1 
ATOM   17622 C CB    . GLN A 1 4108 ? 183.317 153.268 144.490 1.00 120.48 ? 4108 GLN A CB    1 
ATOM   17623 C CG    . GLN A 1 4108 ? 182.343 154.340 144.018 1.00 120.48 ? 4108 GLN A CG    1 
ATOM   17624 C CD    . GLN A 1 4108 ? 183.029 155.600 143.531 1.00 120.48 ? 4108 GLN A CD    1 
ATOM   17625 O OE1   . GLN A 1 4108 ? 184.158 155.558 143.045 1.00 120.48 ? 4108 GLN A OE1   1 
ATOM   17626 N NE2   . GLN A 1 4108 ? 182.336 156.728 143.634 1.00 120.48 ? 4108 GLN A NE2   1 
ATOM   17627 N N     . LEU A 1 4109 ? 184.415 150.382 144.967 1.00 119.99 ? 4109 LEU A N     1 
ATOM   17628 C CA    . LEU A 1 4109 ? 184.918 149.100 144.459 1.00 119.99 ? 4109 LEU A CA    1 
ATOM   17629 C C     . LEU A 1 4109 ? 184.221 147.904 145.096 1.00 119.99 ? 4109 LEU A C     1 
ATOM   17630 O O     . LEU A 1 4109 ? 184.203 146.819 144.505 1.00 119.99 ? 4109 LEU A O     1 
ATOM   17631 C CB    . LEU A 1 4109 ? 186.436 148.942 144.573 1.00 119.99 ? 4109 LEU A CB    1 
ATOM   17632 C CG    . LEU A 1 4109 ? 187.451 150.015 144.201 1.00 119.99 ? 4109 LEU A CG    1 
ATOM   17633 C CD1   . LEU A 1 4109 ? 187.615 150.967 145.281 1.00 119.99 ? 4109 LEU A CD1   1 
ATOM   17634 C CD2   . LEU A 1 4109 ? 188.786 149.367 143.843 1.00 119.99 ? 4109 LEU A CD2   1 
ATOM   17635 N N     . GLU A 1 4110 ? 183.638 148.056 146.289 1.00 120.05 ? 4110 GLU A N     1 
ATOM   17636 C CA    . GLU A 1 4110 ? 182.825 146.950 146.784 1.00 120.05 ? 4110 GLU A CA    1 
ATOM   17637 C C     . GLU A 1 4110 ? 181.677 146.682 145.826 1.00 120.05 ? 4110 GLU A C     1 
ATOM   17638 O O     . GLU A 1 4110 ? 181.356 145.526 145.530 1.00 120.05 ? 4110 GLU A O     1 
ATOM   17639 C CB    . GLU A 1 4110 ? 182.278 147.233 148.181 1.00 120.05 ? 4110 GLU A CB    1 
ATOM   17640 C CG    . GLU A 1 4110 ? 181.686 145.982 148.846 1.00 120.05 ? 4110 GLU A CG    1 
ATOM   17641 C CD    . GLU A 1 4110 ? 180.238 145.707 148.469 1.00 120.05 ? 4110 GLU A CD    1 
ATOM   17642 O OE1   . GLU A 1 4110 ? 179.360 146.543 148.754 1.00 120.05 ? 4110 GLU A OE1   1 
ATOM   17643 O OE2   . GLU A 1 4110 ? 179.979 144.647 147.865 1.00 120.05 ? 4110 GLU A OE2   1 
ATOM   17644 N N     . LYS A 1 4111 ? 181.052 147.748 145.326 1.00 121.98 ? 4111 LYS A N     1 
ATOM   17645 C CA    . LYS A 1 4111 ? 180.054 147.587 144.276 1.00 121.98 ? 4111 LYS A CA    1 
ATOM   17646 C C     . LYS A 1 4111 ? 180.677 147.011 143.010 1.00 121.98 ? 4111 LYS A C     1 
ATOM   17647 O O     . LYS A 1 4111 ? 180.087 146.145 142.354 1.00 121.98 ? 4111 LYS A O     1 
ATOM   17648 C CB    . LYS A 1 4111 ? 179.387 148.927 143.974 1.00 121.98 ? 4111 LYS A CB    1 
ATOM   17649 C CG    . LYS A 1 4111 ? 178.835 149.631 145.193 1.00 121.98 ? 4111 LYS A CG    1 
ATOM   17650 C CD    . LYS A 1 4111 ? 178.912 151.135 145.026 1.00 121.98 ? 4111 LYS A CD    1 
ATOM   17651 C CE    . LYS A 1 4111 ? 178.553 151.845 146.315 1.00 121.98 ? 4111 LYS A CE    1 
ATOM   17652 N NZ    . LYS A 1 4111 ? 179.296 153.125 146.456 1.00 121.98 ? 4111 LYS A NZ    1 
ATOM   17653 N N     . LYS A 1 4112 ? 181.875 147.481 142.655 1.00 126.73 ? 4112 LYS A N     1 
ATOM   17654 C CA    . LYS A 1 4112 ? 182.437 147.170 141.343 1.00 126.73 ? 4112 LYS A CA    1 
ATOM   17655 C C     . LYS A 1 4112 ? 182.836 145.701 141.224 1.00 126.73 ? 4112 LYS A C     1 
ATOM   17656 O O     . LYS A 1 4112 ? 182.505 145.042 140.232 1.00 126.73 ? 4112 LYS A O     1 
ATOM   17657 C CB    . LYS A 1 4112 ? 183.634 148.077 141.055 1.00 126.73 ? 4112 LYS A CB    1 
ATOM   17658 C CG    . LYS A 1 4112 ? 184.753 147.401 140.274 1.00 126.73 ? 4112 LYS A CG    1 
ATOM   17659 C CD    . LYS A 1 4112 ? 185.695 148.416 139.649 1.00 126.73 ? 4112 LYS A CD    1 
ATOM   17660 C CE    . LYS A 1 4112 ? 186.639 147.753 138.657 1.00 126.73 ? 4112 LYS A CE    1 
ATOM   17661 N NZ    . LYS A 1 4112 ? 187.459 148.743 137.903 1.00 126.73 ? 4112 LYS A NZ    1 
ATOM   17662 N N     . LEU A 1 4113 ? 183.550 145.165 142.218 1.00 124.03 ? 4113 LEU A N     1 
ATOM   17663 C CA    . LEU A 1 4113 ? 184.041 143.797 142.072 1.00 124.03 ? 4113 LEU A CA    1 
ATOM   17664 C C     . LEU A 1 4113 ? 182.942 142.758 142.231 1.00 124.03 ? 4113 LEU A C     1 
ATOM   17665 O O     . LEU A 1 4113 ? 183.199 141.574 141.992 1.00 124.03 ? 4113 LEU A O     1 
ATOM   17666 C CB    . LEU A 1 4113 ? 185.174 143.497 143.059 1.00 124.03 ? 4113 LEU A CB    1 
ATOM   17667 C CG    . LEU A 1 4113 ? 185.152 143.986 144.506 1.00 124.03 ? 4113 LEU A CG    1 
ATOM   17668 C CD1   . LEU A 1 4113 ? 184.055 143.317 145.317 1.00 124.03 ? 4113 LEU A CD1   1 
ATOM   17669 C CD2   . LEU A 1 4113 ? 186.509 143.756 145.147 1.00 124.03 ? 4113 LEU A CD2   1 
ATOM   17670 N N     . HIS A 1 4114 ? 181.736 143.166 142.629 1.00 127.09 ? 4114 HIS A N     1 
ATOM   17671 C CA    . HIS A 1 4114 ? 180.625 142.228 142.717 1.00 127.09 ? 4114 HIS A CA    1 
ATOM   17672 C C     . HIS A 1 4114 ? 180.319 141.582 141.374 1.00 127.09 ? 4114 HIS A C     1 
ATOM   17673 O O     . HIS A 1 4114 ? 179.737 140.493 141.340 1.00 127.09 ? 4114 HIS A O     1 
ATOM   17674 C CB    . HIS A 1 4114 ? 179.384 142.941 143.252 1.00 127.09 ? 4114 HIS A CB    1 
ATOM   17675 C CG    . HIS A 1 4114 ? 178.488 142.065 144.070 1.00 127.09 ? 4114 HIS A CG    1 
ATOM   17676 N ND1   . HIS A 1 4114 ? 177.416 142.558 144.783 1.00 127.09 ? 4114 HIS A ND1   1 
ATOM   17677 C CD2   . HIS A 1 4114 ? 178.502 140.729 144.288 1.00 127.09 ? 4114 HIS A CD2   1 
ATOM   17678 C CE1   . HIS A 1 4114 ? 176.811 141.563 145.407 1.00 127.09 ? 4114 HIS A CE1   1 
ATOM   17679 N NE2   . HIS A 1 4114 ? 177.449 140.443 145.122 1.00 127.09 ? 4114 HIS A NE2   1 
ATOM   17680 N N     . SER A 1 4115 ? 180.698 142.225 140.274 1.00 128.19 ? 4115 SER A N     1 
ATOM   17681 C CA    . SER A 1 4115 ? 180.551 141.631 138.957 1.00 128.19 ? 4115 SER A CA    1 
ATOM   17682 C C     . SER A 1 4115 ? 181.513 140.458 138.792 1.00 128.19 ? 4115 SER A C     1 
ATOM   17683 O O     . SER A 1 4115 ? 182.491 140.310 139.530 1.00 128.19 ? 4115 SER A O     1 
ATOM   17684 C CB    . SER A 1 4115 ? 180.802 142.672 137.868 1.00 128.19 ? 4115 SER A CB    1 
ATOM   17685 O OG    . SER A 1 4115 ? 182.177 143.004 137.795 1.00 128.19 ? 4115 SER A OG    1 
ATOM   17686 N N     . LEU A 1 4116 ? 181.219 139.614 137.805 1.00 135.55 ? 4116 LEU A N     1 
ATOM   17687 C CA    . LEU A 1 4116 ? 182.020 138.419 137.576 1.00 135.55 ? 4116 LEU A CA    1 
ATOM   17688 C C     . LEU A 1 4116 ? 183.429 138.783 137.127 1.00 135.55 ? 4116 LEU A C     1 
ATOM   17689 O O     . LEU A 1 4116 ? 183.617 139.631 136.250 1.00 135.55 ? 4116 LEU A O     1 
ATOM   17690 C CB    . LEU A 1 4116 ? 181.350 137.529 136.528 1.00 135.55 ? 4116 LEU A CB    1 
ATOM   17691 C CG    . LEU A 1 4116 ? 182.232 136.441 135.911 1.00 135.55 ? 4116 LEU A CG    1 
ATOM   17692 C CD1   . LEU A 1 4116 ? 182.567 135.371 136.937 1.00 135.55 ? 4116 LEU A CD1   1 
ATOM   17693 C CD2   . LEU A 1 4116 ? 181.565 135.828 134.692 1.00 135.55 ? 4116 LEU A CD2   1 
ATOM   17694 N N     . GLN A 1 4117 ? 184.419 138.138 137.735 1.00 140.01 ? 4117 GLN A N     1 
ATOM   17695 C CA    . GLN A 1 4117 ? 185.786 138.311 137.264 1.00 140.01 ? 4117 GLN A CA    1 
ATOM   17696 C C     . GLN A 1 4117 ? 186.124 137.233 136.235 1.00 140.01 ? 4117 GLN A C     1 
ATOM   17697 O O     . GLN A 1 4117 ? 185.657 136.096 136.350 1.00 140.01 ? 4117 GLN A O     1 
ATOM   17698 C CB    . GLN A 1 4117 ? 186.772 138.250 138.427 1.00 140.01 ? 4117 GLN A CB    1 
ATOM   17699 C CG    . GLN A 1 4117 ? 187.166 136.850 138.864 1.00 140.01 ? 4117 GLN A CG    1 
ATOM   17700 C CD    . GLN A 1 4117 ? 186.005 136.072 139.448 1.00 140.01 ? 4117 GLN A CD    1 
ATOM   17701 O OE1   . GLN A 1 4117 ? 185.052 136.653 139.968 1.00 140.01 ? 4117 GLN A OE1   1 
ATOM   17702 N NE2   . GLN A 1 4117 ? 186.074 134.750 139.355 1.00 140.01 ? 4117 GLN A NE2   1 
ATOM   17703 N N     . PRO A 1 4118 ? 186.899 137.565 135.205 1.00 148.12 ? 4118 PRO A N     1 
ATOM   17704 C CA    . PRO A 1 4118 ? 187.208 136.569 134.171 1.00 148.12 ? 4118 PRO A CA    1 
ATOM   17705 C C     . PRO A 1 4118 ? 188.336 135.621 134.545 1.00 148.12 ? 4118 PRO A C     1 
ATOM   17706 O O     . PRO A 1 4118 ? 188.420 134.521 133.990 1.00 148.12 ? 4118 PRO A O     1 
ATOM   17707 C CB    . PRO A 1 4118 ? 187.586 137.431 132.960 1.00 148.12 ? 4118 PRO A CB    1 
ATOM   17708 C CG    . PRO A 1 4118 ? 188.082 138.702 133.544 1.00 148.12 ? 4118 PRO A CG    1 
ATOM   17709 C CD    . PRO A 1 4118 ? 187.307 138.923 134.811 1.00 148.12 ? 4118 PRO A CD    1 
ATOM   17710 N N     . HIS A 1 4119 ? 189.205 136.015 135.472 1.00 137.93 ? 4119 HIS A N     1 
ATOM   17711 C CA    . HIS A 1 4119 ? 190.376 135.222 135.817 1.00 137.93 ? 4119 HIS A CA    1 
ATOM   17712 C C     . HIS A 1 4119 ? 190.270 134.678 137.234 1.00 137.93 ? 4119 HIS A C     1 
ATOM   17713 O O     . HIS A 1 4119 ? 189.854 135.387 138.154 1.00 137.93 ? 4119 HIS A O     1 
ATOM   17714 C CB    . HIS A 1 4119 ? 191.660 136.038 135.679 1.00 137.93 ? 4119 HIS A CB    1 
ATOM   17715 C CG    . HIS A 1 4119 ? 192.836 135.228 135.238 1.00 137.93 ? 4119 HIS A CG    1 
ATOM   17716 N ND1   . HIS A 1 4119 ? 193.402 134.249 136.026 1.00 137.93 ? 4119 HIS A ND1   1 
ATOM   17717 C CD2   . HIS A 1 4119 ? 193.551 135.245 134.088 1.00 137.93 ? 4119 HIS A CD2   1 
ATOM   17718 C CE1   . HIS A 1 4119 ? 194.417 133.701 135.383 1.00 137.93 ? 4119 HIS A CE1   1 
ATOM   17719 N NE2   . HIS A 1 4119 ? 194.529 134.288 134.205 1.00 137.93 ? 4119 HIS A NE2   1 
ATOM   17720 N N     . ALA A 1 4120 ? 190.664 133.415 137.401 1.00 130.45 ? 4120 ALA A N     1 
ATOM   17721 C CA    . ALA A 1 4120 ? 190.624 132.759 138.699 1.00 130.45 ? 4120 ALA A CA    1 
ATOM   17722 C C     . ALA A 1 4120 ? 191.917 132.909 139.487 1.00 130.45 ? 4120 ALA A C     1 
ATOM   17723 O O     . ALA A 1 4120 ? 191.892 132.789 140.717 1.00 130.45 ? 4120 ALA A O     1 
ATOM   17724 C CB    . ALA A 1 4120 ? 190.310 131.270 138.530 1.00 130.45 ? 4120 ALA A CB    1 
ATOM   17725 N N     . CYS A 1 4121 ? 193.039 133.167 138.816 1.00 129.74 ? 4121 CYS A N     1 
ATOM   17726 C CA    . CYS A 1 4121 ? 194.312 133.327 139.504 1.00 129.74 ? 4121 CYS A CA    1 
ATOM   17727 C C     . CYS A 1 4121 ? 194.511 134.729 140.061 1.00 129.74 ? 4121 CYS A C     1 
ATOM   17728 O O     . CYS A 1 4121 ? 195.526 134.978 140.721 1.00 129.74 ? 4121 CYS A O     1 
ATOM   17729 C CB    . CYS A 1 4121 ? 195.466 132.980 138.561 1.00 129.74 ? 4121 CYS A CB    1 
ATOM   17730 S SG    . CYS A 1 4121 ? 196.987 132.476 139.395 1.00 129.74 ? 4121 CYS A SG    1 
ATOM   17731 N N     . PHE A 1 4122 ? 193.580 135.644 139.810 1.00 121.82 ? 4122 PHE A N     1 
ATOM   17732 C CA    . PHE A 1 4122 ? 193.675 136.998 140.334 1.00 121.82 ? 4122 PHE A CA    1 
ATOM   17733 C C     . PHE A 1 4122 ? 193.282 137.022 141.805 1.00 121.82 ? 4122 PHE A C     1 
ATOM   17734 O O     . PHE A 1 4122 ? 192.296 136.397 142.205 1.00 121.82 ? 4122 PHE A O     1 
ATOM   17735 C CB    . PHE A 1 4122 ? 192.779 137.937 139.529 1.00 121.82 ? 4122 PHE A CB    1 
ATOM   17736 C CG    . PHE A 1 4122 ? 192.195 139.058 140.333 1.00 121.82 ? 4122 PHE A CG    1 
ATOM   17737 C CD1   . PHE A 1 4122 ? 192.952 140.168 140.649 1.00 121.82 ? 4122 PHE A CD1   1 
ATOM   17738 C CD2   . PHE A 1 4122 ? 190.882 139.005 140.764 1.00 121.82 ? 4122 PHE A CD2   1 
ATOM   17739 C CE1   . PHE A 1 4122 ? 192.414 141.200 141.383 1.00 121.82 ? 4122 PHE A CE1   1 
ATOM   17740 C CE2   . PHE A 1 4122 ? 190.340 140.035 141.499 1.00 121.82 ? 4122 PHE A CE2   1 
ATOM   17741 C CZ    . PHE A 1 4122 ? 191.107 141.133 141.808 1.00 121.82 ? 4122 PHE A CZ    1 
ATOM   17742 N N     . ARG A 1 4123 ? 194.057 137.744 142.608 1.00 119.27 ? 4123 ARG A N     1 
ATOM   17743 C CA    . ARG A 1 4123 ? 193.795 137.888 144.033 1.00 119.27 ? 4123 ARG A CA    1 
ATOM   17744 C C     . ARG A 1 4123 ? 193.958 139.350 144.413 1.00 119.27 ? 4123 ARG A C     1 
ATOM   17745 O O     . ARG A 1 4123 ? 194.919 139.999 143.989 1.00 119.27 ? 4123 ARG A O     1 
ATOM   17746 C CB    . ARG A 1 4123 ? 194.740 137.017 144.861 1.00 119.27 ? 4123 ARG A CB    1 
ATOM   17747 C CG    . ARG A 1 4123 ? 194.524 135.528 144.685 1.00 119.27 ? 4123 ARG A CG    1 
ATOM   17748 C CD    . ARG A 1 4123 ? 193.214 135.080 145.294 1.00 119.27 ? 4123 ARG A CD    1 
ATOM   17749 N NE    . ARG A 1 4123 ? 193.098 133.628 145.289 1.00 119.27 ? 4123 ARG A NE    1 
ATOM   17750 C CZ    . ARG A 1 4123 ? 192.781 132.907 144.222 1.00 119.27 ? 4123 ARG A CZ    1 
ATOM   17751 N NH1   . ARG A 1 4123 ? 192.517 133.476 143.058 1.00 119.27 ? 4123 ARG A NH1   1 
ATOM   17752 N NH2   . ARG A 1 4123 ? 192.726 131.583 144.328 1.00 119.27 ? 4123 ARG A NH2   1 
ATOM   17753 N N     . LEU A 1 4124 ? 193.025 139.865 145.209 1.00 107.71 ? 4124 LEU A N     1 
ATOM   17754 C CA    . LEU A 1 4124 ? 193.038 141.257 145.635 1.00 107.71 ? 4124 LEU A CA    1 
ATOM   17755 C C     . LEU A 1 4124 ? 193.220 141.329 147.144 1.00 107.71 ? 4124 LEU A C     1 
ATOM   17756 O O     . LEU A 1 4124 ? 192.491 140.672 147.894 1.00 107.71 ? 4124 LEU A O     1 
ATOM   17757 C CB    . LEU A 1 4124 ? 191.750 141.969 145.221 1.00 107.71 ? 4124 LEU A CB    1 
ATOM   17758 C CG    . LEU A 1 4124 ? 191.612 143.424 145.666 1.00 107.71 ? 4124 LEU A CG    1 
ATOM   17759 C CD1   . LEU A 1 4124 ? 191.107 144.280 144.522 1.00 107.71 ? 4124 LEU A CD1   1 
ATOM   17760 C CD2   . LEU A 1 4124 ? 190.674 143.531 146.848 1.00 107.71 ? 4124 LEU A CD2   1 
ATOM   17761 N N     . PHE A 1 4125 ? 194.185 142.130 147.580 1.00 101.59 ? 4125 PHE A N     1 
ATOM   17762 C CA    . PHE A 1 4125 ? 194.479 142.334 148.990 1.00 101.59 ? 4125 PHE A CA    1 
ATOM   17763 C C     . PHE A 1 4125 ? 194.176 143.778 149.353 1.00 101.59 ? 4125 PHE A C     1 
ATOM   17764 O O     . PHE A 1 4125 ? 194.511 144.693 148.595 1.00 101.59 ? 4125 PHE A O     1 
ATOM   17765 C CB    . PHE A 1 4125 ? 195.944 142.037 149.298 1.00 101.59 ? 4125 PHE A CB    1 
ATOM   17766 C CG    . PHE A 1 4125 ? 196.364 140.641 148.983 1.00 101.59 ? 4125 PHE A CG    1 
ATOM   17767 C CD1   . PHE A 1 4125 ? 196.729 140.291 147.698 1.00 101.59 ? 4125 PHE A CD1   1 
ATOM   17768 C CD2   . PHE A 1 4125 ? 196.427 139.687 149.974 1.00 101.59 ? 4125 PHE A CD2   1 
ATOM   17769 C CE1   . PHE A 1 4125 ? 197.129 139.010 147.404 1.00 101.59 ? 4125 PHE A CE1   1 
ATOM   17770 C CE2   . PHE A 1 4125 ? 196.830 138.409 149.685 1.00 101.59 ? 4125 PHE A CE2   1 
ATOM   17771 C CZ    . PHE A 1 4125 ? 197.181 138.067 148.397 1.00 101.59 ? 4125 PHE A CZ    1 
ATOM   17772 N N     . LEU A 1 4126 ? 193.555 143.984 150.506 1.00 100.91 ? 4126 LEU A N     1 
ATOM   17773 C CA    . LEU A 1 4126 ? 193.344 145.319 151.045 1.00 100.91 ? 4126 LEU A CA    1 
ATOM   17774 C C     . LEU A 1 4126 ? 193.878 145.345 152.466 1.00 100.91 ? 4126 LEU A C     1 
ATOM   17775 O O     . LEU A 1 4126 ? 193.413 144.581 153.316 1.00 100.91 ? 4126 LEU A O     1 
ATOM   17776 C CB    . LEU A 1 4126 ? 191.865 145.702 151.018 1.00 100.91 ? 4126 LEU A CB    1 
ATOM   17777 C CG    . LEU A 1 4126 ? 191.233 145.816 149.634 1.00 100.91 ? 4126 LEU A CG    1 
ATOM   17778 C CD1   . LEU A 1 4126 ? 189.721 145.890 149.737 1.00 100.91 ? 4126 LEU A CD1   1 
ATOM   17779 C CD2   . LEU A 1 4126 ? 191.781 147.022 148.903 1.00 100.91 ? 4126 LEU A CD2   1 
ATOM   17780 N N     . THR A 1 4127 ? 194.845 146.219 152.724 1.00 103.21 ? 4127 THR A N     1 
ATOM   17781 C CA    . THR A 1 4127 ? 195.410 146.381 154.055 1.00 103.21 ? 4127 THR A CA    1 
ATOM   17782 C C     . THR A 1 4127 ? 195.120 147.788 154.557 1.00 103.21 ? 4127 THR A C     1 
ATOM   17783 O O     . THR A 1 4127 ? 195.158 148.754 153.788 1.00 103.21 ? 4127 THR A O     1 
ATOM   17784 C CB    . THR A 1 4127 ? 196.920 146.084 154.066 1.00 103.21 ? 4127 THR A CB    1 
ATOM   17785 O OG1   . THR A 1 4127 ? 197.327 145.729 155.393 1.00 103.21 ? 4127 THR A OG1   1 
ATOM   17786 C CG2   . THR A 1 4127 ? 197.737 147.274 153.591 1.00 103.21 ? 4127 THR A CG2   1 
ATOM   17787 N N     . MET A 1 4128 ? 194.779 147.894 155.838 1.00 105.49 ? 4128 MET A N     1 
ATOM   17788 C CA    . MET A 1 4128 ? 194.368 149.169 156.405 1.00 105.49 ? 4128 MET A CA    1 
ATOM   17789 C C     . MET A 1 4128 ? 194.419 149.074 157.924 1.00 105.49 ? 4128 MET A C     1 
ATOM   17790 O O     . MET A 1 4128 ? 194.887 148.081 158.490 1.00 105.49 ? 4128 MET A O     1 
ATOM   17791 C CB    . MET A 1 4128 ? 192.967 149.557 155.915 1.00 105.49 ? 4128 MET A CB    1 
ATOM   17792 C CG    . MET A 1 4128 ? 191.829 148.890 156.670 1.00 105.49 ? 4128 MET A CG    1 
ATOM   17793 S SD    . MET A 1 4128 ? 191.810 147.115 156.445 1.00 105.49 ? 4128 MET A SD    1 
ATOM   17794 C CE    . MET A 1 4128 ? 191.848 147.061 154.666 1.00 105.49 ? 4128 MET A CE    1 
ATOM   17795 N N     . GLU A 1 4129 ? 193.932 150.121 158.580 1.00 108.67 ? 4129 GLU A N     1 
ATOM   17796 C CA    . GLU A 1 4129 ? 193.816 150.197 160.026 1.00 108.67 ? 4129 GLU A CA    1 
ATOM   17797 C C     . GLU A 1 4129 ? 192.406 149.799 160.444 1.00 108.67 ? 4129 GLU A C     1 
ATOM   17798 O O     . GLU A 1 4129 ? 191.445 149.993 159.697 1.00 108.67 ? 4129 GLU A O     1 
ATOM   17799 C CB    . GLU A 1 4129 ? 194.119 151.618 160.500 1.00 108.67 ? 4129 GLU A CB    1 
ATOM   17800 C CG    . GLU A 1 4129 ? 194.640 151.738 161.911 1.00 108.67 ? 4129 GLU A CG    1 
ATOM   17801 C CD    . GLU A 1 4129 ? 195.094 153.151 162.224 1.00 108.67 ? 4129 GLU A CD    1 
ATOM   17802 O OE1   . GLU A 1 4129 ? 194.263 154.078 162.120 1.00 108.67 ? 4129 GLU A OE1   1 
ATOM   17803 O OE2   . GLU A 1 4129 ? 196.284 153.342 162.545 1.00 108.67 ? 4129 GLU A OE2   1 
ATOM   17804 N N     . ILE A 1 4130 ? 192.283 149.239 161.645 1.00 104.64 ? 4130 ILE A N     1 
ATOM   17805 C CA    . ILE A 1 4130 ? 190.967 148.879 162.168 1.00 104.64 ? 4130 ILE A CA    1 
ATOM   17806 C C     . ILE A 1 4130 ? 190.307 150.152 162.686 1.00 104.64 ? 4130 ILE A C     1 
ATOM   17807 O O     . ILE A 1 4130 ? 190.587 150.604 163.796 1.00 104.64 ? 4130 ILE A O     1 
ATOM   17808 C CB    . ILE A 1 4130 ? 191.045 147.807 163.255 1.00 104.64 ? 4130 ILE A CB    1 
ATOM   17809 C CG1   . ILE A 1 4130 ? 192.041 146.713 162.878 1.00 104.64 ? 4130 ILE A CG1   1 
ATOM   17810 C CG2   . ILE A 1 4130 ? 189.668 147.238 163.531 1.00 104.64 ? 4130 ILE A CG2   1 
ATOM   17811 C CD1   . ILE A 1 4130 ? 192.807 146.183 164.059 1.00 104.64 ? 4130 ILE A CD1   1 
ATOM   17812 N N     . ASN A 1 4131 ? 189.422 150.731 161.884 1.00 108.56 ? 4131 ASN A N     1 
ATOM   17813 C CA    . ASN A 1 4131 ? 188.632 151.884 162.278 1.00 108.56 ? 4131 ASN A CA    1 
ATOM   17814 C C     . ASN A 1 4131 ? 187.189 151.650 161.861 1.00 108.56 ? 4131 ASN A C     1 
ATOM   17815 O O     . ASN A 1 4131 ? 186.930 150.906 160.909 1.00 108.56 ? 4131 ASN A O     1 
ATOM   17816 C CB    . ASN A 1 4131 ? 189.160 153.181 161.643 1.00 108.56 ? 4131 ASN A CB    1 
ATOM   17817 C CG    . ASN A 1 4131 ? 189.207 153.115 160.132 1.00 108.56 ? 4131 ASN A CG    1 
ATOM   17818 O OD1   . ASN A 1 4131 ? 189.044 152.051 159.540 1.00 108.56 ? 4131 ASN A OD1   1 
ATOM   17819 N ND2   . ASN A 1 4131 ? 189.431 154.259 159.499 1.00 108.56 ? 4131 ASN A ND2   1 
ATOM   17820 N N     . PRO A 1 4132 ? 186.228 152.264 162.556 1.00 109.13 ? 4132 PRO A N     1 
ATOM   17821 C CA    . PRO A 1 4132 ? 184.818 152.073 162.188 1.00 109.13 ? 4132 PRO A CA    1 
ATOM   17822 C C     . PRO A 1 4132 ? 184.427 152.727 160.876 1.00 109.13 ? 4132 PRO A C     1 
ATOM   17823 O O     . PRO A 1 4132 ? 183.256 152.642 160.490 1.00 109.13 ? 4132 PRO A O     1 
ATOM   17824 C CB    . PRO A 1 4132 ? 184.064 152.711 163.363 1.00 109.13 ? 4132 PRO A CB    1 
ATOM   17825 C CG    . PRO A 1 4132 ? 185.016 153.702 163.923 1.00 109.13 ? 4132 PRO A CG    1 
ATOM   17826 C CD    . PRO A 1 4132 ? 186.377 153.098 163.760 1.00 109.13 ? 4132 PRO A CD    1 
ATOM   17827 N N     . LYS A 1 4133 ? 185.359 153.375 160.176 1.00 110.91 ? 4133 LYS A N     1 
ATOM   17828 C CA    . LYS A 1 4133 ? 185.024 154.066 158.939 1.00 110.91 ? 4133 LYS A CA    1 
ATOM   17829 C C     . LYS A 1 4133 ? 184.919 153.127 157.745 1.00 110.91 ? 4133 LYS A C     1 
ATOM   17830 O O     . LYS A 1 4133 ? 184.410 153.539 156.698 1.00 110.91 ? 4133 LYS A O     1 
ATOM   17831 C CB    . LYS A 1 4133 ? 186.061 155.152 158.646 1.00 110.91 ? 4133 LYS A CB    1 
ATOM   17832 C CG    . LYS A 1 4133 ? 186.305 156.115 159.801 1.00 110.91 ? 4133 LYS A CG    1 
ATOM   17833 C CD    . LYS A 1 4133 ? 185.003 156.606 160.412 1.00 110.91 ? 4133 LYS A CD    1 
ATOM   17834 C CE    . LYS A 1 4133 ? 184.473 157.820 159.675 1.00 110.91 ? 4133 LYS A CE    1 
ATOM   17835 N NZ    . LYS A 1 4133 ? 185.365 158.998 159.851 1.00 110.91 ? 4133 LYS A NZ    1 
ATOM   17836 N N     . VAL A 1 4134 ? 185.386 151.891 157.870 1.00 108.03 ? 4134 VAL A N     1 
ATOM   17837 C CA    . VAL A 1 4134 ? 185.296 150.950 156.747 1.00 108.03 ? 4134 VAL A CA    1 
ATOM   17838 C C     . VAL A 1 4134 ? 183.837 150.585 156.514 1.00 108.03 ? 4134 VAL A C     1 
ATOM   17839 O O     . VAL A 1 4134 ? 183.070 150.460 157.486 1.00 108.03 ? 4134 VAL A O     1 
ATOM   17840 C CB    . VAL A 1 4134 ? 186.137 149.704 157.025 1.00 108.03 ? 4134 VAL A CB    1 
ATOM   17841 C CG1   . VAL A 1 4134 ? 187.612 150.013 156.851 1.00 108.03 ? 4134 VAL A CG1   1 
ATOM   17842 C CG2   . VAL A 1 4134 ? 185.862 149.183 158.423 1.00 108.03 ? 4134 VAL A CG2   1 
ATOM   17843 N N     . PRO A 1 4135 ? 183.403 150.423 155.268 1.00 107.26 ? 4135 PRO A N     1 
ATOM   17844 C CA    . PRO A 1 4135 ? 182.010 150.039 155.020 1.00 107.26 ? 4135 PRO A CA    1 
ATOM   17845 C C     . PRO A 1 4135 ? 181.736 148.623 155.493 1.00 107.26 ? 4135 PRO A C     1 
ATOM   17846 O O     . PRO A 1 4135 ? 182.593 147.741 155.403 1.00 107.26 ? 4135 PRO A O     1 
ATOM   17847 C CB    . PRO A 1 4135 ? 181.872 150.153 153.498 1.00 107.26 ? 4135 PRO A CB    1 
ATOM   17848 C CG    . PRO A 1 4135 ? 183.071 150.924 153.042 1.00 107.26 ? 4135 PRO A CG    1 
ATOM   17849 C CD    . PRO A 1 4135 ? 184.151 150.619 154.020 1.00 107.26 ? 4135 PRO A CD    1 
ATOM   17850 N N     . VAL A 1 4136 ? 180.518 148.409 155.990 1.00 107.34 ? 4136 VAL A N     1 
ATOM   17851 C CA    . VAL A 1 4136 ? 180.141 147.089 156.481 1.00 107.34 ? 4136 VAL A CA    1 
ATOM   17852 C C     . VAL A 1 4136 ? 180.068 146.091 155.332 1.00 107.34 ? 4136 VAL A C     1 
ATOM   17853 O O     . VAL A 1 4136 ? 180.393 144.910 155.498 1.00 107.34 ? 4136 VAL A O     1 
ATOM   17854 C CB    . VAL A 1 4136 ? 178.813 147.170 157.254 1.00 107.34 ? 4136 VAL A CB    1 
ATOM   17855 C CG1   . VAL A 1 4136 ? 177.770 147.913 156.440 1.00 107.34 ? 4136 VAL A CG1   1 
ATOM   17856 C CG2   . VAL A 1 4136 ? 178.321 145.783 157.627 1.00 107.34 ? 4136 VAL A CG2   1 
ATOM   17857 N N     . ASN A 1 4137 ? 179.642 146.545 154.152 1.00 112.33 ? 4137 ASN A N     1 
ATOM   17858 C CA    . ASN A 1 4137 ? 179.442 145.626 153.037 1.00 112.33 ? 4137 ASN A CA    1 
ATOM   17859 C C     . ASN A 1 4137 ? 180.751 144.992 152.584 1.00 112.33 ? 4137 ASN A C     1 
ATOM   17860 O O     . ASN A 1 4137 ? 180.797 143.790 152.305 1.00 112.33 ? 4137 ASN A O     1 
ATOM   17861 C CB    . ASN A 1 4137 ? 178.765 146.347 151.875 1.00 112.33 ? 4137 ASN A CB    1 
ATOM   17862 C CG    . ASN A 1 4137 ? 177.284 146.549 152.104 1.00 112.33 ? 4137 ASN A CG    1 
ATOM   17863 O OD1   . ASN A 1 4137 ? 176.827 146.637 153.244 1.00 112.33 ? 4137 ASN A OD1   1 
ATOM   17864 N ND2   . ASN A 1 4137 ? 176.522 146.617 151.019 1.00 112.33 ? 4137 ASN A ND2   1 
ATOM   17865 N N     . LEU A 1 4138 ? 181.824 145.780 152.493 1.00 107.94 ? 4138 LEU A N     1 
ATOM   17866 C CA    . LEU A 1 4138 ? 183.110 145.205 152.110 1.00 107.94 ? 4138 LEU A CA    1 
ATOM   17867 C C     . LEU A 1 4138 ? 183.608 144.233 153.169 1.00 107.94 ? 4138 LEU A C     1 
ATOM   17868 O O     . LEU A 1 4138 ? 184.212 143.203 152.847 1.00 107.94 ? 4138 LEU A O     1 
ATOM   17869 C CB    . LEU A 1 4138 ? 184.140 146.304 151.867 1.00 107.94 ? 4138 LEU A CB    1 
ATOM   17870 C CG    . LEU A 1 4138 ? 185.395 145.815 151.142 1.00 107.94 ? 4138 LEU A CG    1 
ATOM   17871 C CD1   . LEU A 1 4138 ? 185.045 144.754 150.113 1.00 107.94 ? 4138 LEU A CD1   1 
ATOM   17872 C CD2   . LEU A 1 4138 ? 186.125 146.961 150.482 1.00 107.94 ? 4138 LEU A CD2   1 
ATOM   17873 N N     . LEU A 1 4139 ? 183.366 144.548 154.440 1.00 106.10 ? 4139 LEU A N     1 
ATOM   17874 C CA    . LEU A 1 4139 ? 183.707 143.627 155.516 1.00 106.10 ? 4139 LEU A CA    1 
ATOM   17875 C C     . LEU A 1 4139 ? 182.960 142.310 155.363 1.00 106.10 ? 4139 LEU A C     1 
ATOM   17876 O O     . LEU A 1 4139 ? 183.523 141.232 155.583 1.00 106.10 ? 4139 LEU A O     1 
ATOM   17877 C CB    . LEU A 1 4139 ? 183.378 144.277 156.857 1.00 106.10 ? 4139 LEU A CB    1 
ATOM   17878 C CG    . LEU A 1 4139 ? 184.535 144.812 157.690 1.00 106.10 ? 4139 LEU A CG    1 
ATOM   17879 C CD1   . LEU A 1 4139 ? 184.127 144.846 159.137 1.00 106.10 ? 4139 LEU A CD1   1 
ATOM   17880 C CD2   . LEU A 1 4139 ? 185.746 143.936 157.511 1.00 106.10 ? 4139 LEU A CD2   1 
ATOM   17881 N N     . ARG A 1 4140 ? 181.686 142.383 154.987 1.00 101.79 ? 4140 ARG A N     1 
ATOM   17882 C CA    . ARG A 1 4140 ? 180.880 141.181 154.840 1.00 101.79 ? 4140 ARG A CA    1 
ATOM   17883 C C     . ARG A 1 4140 ? 181.296 140.379 153.615 1.00 101.79 ? 4140 ARG A C     1 
ATOM   17884 O O     . ARG A 1 4140 ? 181.282 139.143 153.640 1.00 101.79 ? 4140 ARG A O     1 
ATOM   17885 C CB    . ARG A 1 4140 ? 179.405 141.569 154.768 1.00 101.79 ? 4140 ARG A CB    1 
ATOM   17886 C CG    . ARG A 1 4140 ? 178.535 140.629 153.969 1.00 101.79 ? 4140 ARG A CG    1 
ATOM   17887 C CD    . ARG A 1 4140 ? 177.056 140.921 154.182 1.00 101.79 ? 4140 ARG A CD    1 
ATOM   17888 N NE    . ARG A 1 4140 ? 176.637 140.706 155.563 1.00 101.79 ? 4140 ARG A NE    1 
ATOM   17889 C CZ    . ARG A 1 4140 ? 176.535 141.662 156.476 1.00 101.79 ? 4140 ARG A CZ    1 
ATOM   17890 N NH1   . ARG A 1 4140 ? 176.804 142.925 156.187 1.00 101.79 ? 4140 ARG A NH1   1 
ATOM   17891 N NH2   . ARG A 1 4140 ? 176.151 141.344 157.709 1.00 101.79 ? 4140 ARG A NH2   1 
ATOM   17892 N N     . ALA A 1 4141 ? 181.689 141.059 152.544 1.00 105.31 ? 4141 ALA A N     1 
ATOM   17893 C CA    . ALA A 1 4141 ? 181.879 140.413 151.253 1.00 105.31 ? 4141 ALA A CA    1 
ATOM   17894 C C     . ALA A 1 4141 ? 183.244 139.762 151.085 1.00 105.31 ? 4141 ALA A C     1 
ATOM   17895 O O     . ALA A 1 4141 ? 183.469 139.106 150.063 1.00 105.31 ? 4141 ALA A O     1 
ATOM   17896 C CB    . ALA A 1 4141 ? 181.658 141.425 150.127 1.00 105.31 ? 4141 ALA A CB    1 
ATOM   17897 N N     . GLY A 1 4142 ? 184.162 139.913 152.042 1.00 98.26  ? 4142 GLY A N     1 
ATOM   17898 C CA    . GLY A 1 4142 ? 185.496 139.378 151.897 1.00 98.26  ? 4142 GLY A CA    1 
ATOM   17899 C C     . GLY A 1 4142 ? 185.983 138.712 153.171 1.00 98.26  ? 4142 GLY A C     1 
ATOM   17900 O O     . GLY A 1 4142 ? 185.490 138.976 154.269 1.00 98.26  ? 4142 GLY A O     1 
ATOM   17901 N N     . ARG A 1 4143 ? 186.968 137.837 152.997 1.00 96.54  ? 4143 ARG A N     1 
ATOM   17902 C CA    . ARG A 1 4143 ? 187.666 137.227 154.117 1.00 96.54  ? 4143 ARG A CA    1 
ATOM   17903 C C     . ARG A 1 4143 ? 188.514 138.286 154.799 1.00 96.54  ? 4143 ARG A C     1 
ATOM   17904 O O     . ARG A 1 4143 ? 189.280 138.994 154.139 1.00 96.54  ? 4143 ARG A O     1 
ATOM   17905 C CB    . ARG A 1 4143 ? 188.550 136.072 153.648 1.00 96.54  ? 4143 ARG A CB    1 
ATOM   17906 C CG    . ARG A 1 4143 ? 187.803 134.793 153.350 1.00 96.54  ? 4143 ARG A CG    1 
ATOM   17907 C CD    . ARG A 1 4143 ? 187.451 134.071 154.634 1.00 96.54  ? 4143 ARG A CD    1 
ATOM   17908 N NE    . ARG A 1 4143 ? 188.383 132.991 154.940 1.00 96.54  ? 4143 ARG A NE    1 
ATOM   17909 C CZ    . ARG A 1 4143 ? 189.129 132.934 156.035 1.00 96.54  ? 4143 ARG A CZ    1 
ATOM   17910 N NH1   . ARG A 1 4143 ? 189.083 133.885 156.953 1.00 96.54  ? 4143 ARG A NH1   1 
ATOM   17911 N NH2   . ARG A 1 4143 ? 189.940 131.896 156.215 1.00 96.54  ? 4143 ARG A NH2   1 
ATOM   17912 N N     . ILE A 1 4144 ? 188.383 138.390 156.109 1.00 95.83  ? 4144 ILE A N     1 
ATOM   17913 C CA    . ILE A 1 4144 ? 189.092 139.403 156.876 1.00 95.83  ? 4144 ILE A CA    1 
ATOM   17914 C C     . ILE A 1 4144 ? 190.193 138.735 157.683 1.00 95.83  ? 4144 ILE A C     1 
ATOM   17915 O O     . ILE A 1 4144 ? 190.118 137.549 158.020 1.00 95.83  ? 4144 ILE A O     1 
ATOM   17916 C CB    . ILE A 1 4144 ? 188.121 140.193 157.776 1.00 95.83  ? 4144 ILE A CB    1 
ATOM   17917 C CG1   . ILE A 1 4144 ? 187.962 139.511 159.128 1.00 95.83  ? 4144 ILE A CG1   1 
ATOM   17918 C CG2   . ILE A 1 4144 ? 186.770 140.324 157.108 1.00 95.83  ? 4144 ILE A CG2   1 
ATOM   17919 C CD1   . ILE A 1 4144 ? 187.283 140.379 160.137 1.00 95.83  ? 4144 ILE A CD1   1 
ATOM   17920 N N     . PHE A 1 4145 ? 191.242 139.499 157.975 1.00 96.36  ? 4145 PHE A N     1 
ATOM   17921 C CA    . PHE A 1 4145 ? 192.397 138.994 158.707 1.00 96.36  ? 4145 PHE A CA    1 
ATOM   17922 C C     . PHE A 1 4145 ? 192.852 140.068 159.678 1.00 96.36  ? 4145 PHE A C     1 
ATOM   17923 O O     . PHE A 1 4145 ? 192.969 141.236 159.298 1.00 96.36  ? 4145 PHE A O     1 
ATOM   17924 C CB    . PHE A 1 4145 ? 193.529 138.617 157.753 1.00 96.36  ? 4145 PHE A CB    1 
ATOM   17925 C CG    . PHE A 1 4145 ? 193.299 137.332 157.024 1.00 96.36  ? 4145 PHE A CG    1 
ATOM   17926 C CD1   . PHE A 1 4145 ? 193.681 136.128 157.580 1.00 96.36  ? 4145 PHE A CD1   1 
ATOM   17927 C CD2   . PHE A 1 4145 ? 192.697 137.328 155.782 1.00 96.36  ? 4145 PHE A CD2   1 
ATOM   17928 C CE1   . PHE A 1 4145 ? 193.470 134.946 156.909 1.00 96.36  ? 4145 PHE A CE1   1 
ATOM   17929 C CE2   . PHE A 1 4145 ? 192.483 136.149 155.108 1.00 96.36  ? 4145 PHE A CE2   1 
ATOM   17930 C CZ    . PHE A 1 4145 ? 192.869 134.957 155.672 1.00 96.36  ? 4145 PHE A CZ    1 
ATOM   17931 N N     . VAL A 1 4146 ? 193.109 139.681 160.921 1.00 89.51  ? 4146 VAL A N     1 
ATOM   17932 C CA    . VAL A 1 4146 ? 193.506 140.619 161.963 1.00 89.51  ? 4146 VAL A CA    1 
ATOM   17933 C C     . VAL A 1 4146 ? 194.946 140.335 162.358 1.00 89.51  ? 4146 VAL A C     1 
ATOM   17934 O O     . VAL A 1 4146 ? 195.275 139.219 162.777 1.00 89.51  ? 4146 VAL A O     1 
ATOM   17935 C CB    . VAL A 1 4146 ? 192.576 140.523 163.180 1.00 89.51  ? 4146 VAL A CB    1 
ATOM   17936 C CG1   . VAL A 1 4146 ? 193.212 141.197 164.378 1.00 89.51  ? 4146 VAL A CG1   1 
ATOM   17937 C CG2   . VAL A 1 4146 ? 191.239 141.146 162.860 1.00 89.51  ? 4146 VAL A CG2   1 
ATOM   17938 N N     . PHE A 1 4147 ? 195.803 141.343 162.226 1.00 96.22  ? 4147 PHE A N     1 
ATOM   17939 C CA    . PHE A 1 4147 ? 197.202 141.241 162.615 1.00 96.22  ? 4147 PHE A CA    1 
ATOM   17940 C C     . PHE A 1 4147 ? 197.460 142.166 163.791 1.00 96.22  ? 4147 PHE A C     1 
ATOM   17941 O O     . PHE A 1 4147 ? 197.112 143.349 163.741 1.00 96.22  ? 4147 PHE A O     1 
ATOM   17942 C CB    . PHE A 1 4147 ? 198.136 141.598 161.458 1.00 96.22  ? 4147 PHE A CB    1 
ATOM   17943 C CG    . PHE A 1 4147 ? 198.231 140.538 160.407 1.00 96.22  ? 4147 PHE A CG    1 
ATOM   17944 C CD1   . PHE A 1 4147 ? 197.437 139.411 160.467 1.00 96.22  ? 4147 PHE A CD1   1 
ATOM   17945 C CD2   . PHE A 1 4147 ? 199.129 140.661 159.367 1.00 96.22  ? 4147 PHE A CD2   1 
ATOM   17946 C CE1   . PHE A 1 4147 ? 197.528 138.437 159.506 1.00 96.22  ? 4147 PHE A CE1   1 
ATOM   17947 C CE2   . PHE A 1 4147 ? 199.224 139.688 158.401 1.00 96.22  ? 4147 PHE A CE2   1 
ATOM   17948 C CZ    . PHE A 1 4147 ? 198.424 138.573 158.473 1.00 96.22  ? 4147 PHE A CZ    1 
ATOM   17949 N N     . GLU A 1 4148 ? 198.070 141.628 164.843 1.00 94.88  ? 4148 GLU A N     1 
ATOM   17950 C CA    . GLU A 1 4148 ? 198.436 142.420 166.001 1.00 94.88  ? 4148 GLU A CA    1 
ATOM   17951 C C     . GLU A 1 4148 ? 199.913 142.226 166.309 1.00 94.88  ? 4148 GLU A C     1 
ATOM   17952 O O     . GLU A 1 4148 ? 200.429 141.108 166.202 1.00 94.88  ? 4148 GLU A O     1 
ATOM   17953 C CB    . GLU A 1 4148 ? 197.604 142.030 167.228 1.00 94.88  ? 4148 GLU A CB    1 
ATOM   17954 C CG    . GLU A 1 4148 ? 196.167 141.679 166.921 1.00 94.88  ? 4148 GLU A CG    1 
ATOM   17955 C CD    . GLU A 1 4148 ? 195.559 140.772 167.970 1.00 94.88  ? 4148 GLU A CD    1 
ATOM   17956 O OE1   . GLU A 1 4148 ? 195.544 141.161 169.156 1.00 94.88  ? 4148 GLU A OE1   1 
ATOM   17957 O OE2   . GLU A 1 4148 ? 195.092 139.672 167.608 1.00 94.88  ? 4148 GLU A OE2   1 
ATOM   17958 N N     . PRO A 1 4149 ? 200.617 143.288 166.684 1.00 83.82  ? 4149 PRO A N     1 
ATOM   17959 C CA    . PRO A 1 4149 ? 202.002 143.137 167.120 1.00 83.82  ? 4149 PRO A CA    1 
ATOM   17960 C C     . PRO A 1 4149 ? 202.076 142.264 168.358 1.00 83.82  ? 4149 PRO A C     1 
ATOM   17961 O O     . PRO A 1 4149 ? 201.225 142.372 169.253 1.00 83.82  ? 4149 PRO A O     1 
ATOM   17962 C CB    . PRO A 1 4149 ? 202.436 144.578 167.426 1.00 83.82  ? 4149 PRO A CB    1 
ATOM   17963 C CG    . PRO A 1 4149 ? 201.165 145.316 167.657 1.00 83.82  ? 4149 PRO A CG    1 
ATOM   17964 C CD    . PRO A 1 4149 ? 200.164 144.685 166.749 1.00 83.82  ? 4149 PRO A CD    1 
ATOM   17965 N N     . PRO A 1 4150 ? 203.065 141.384 168.444 1.00 77.81  ? 4150 PRO A N     1 
ATOM   17966 C CA    . PRO A 1 4150 ? 203.182 140.518 169.613 1.00 77.81  ? 4150 PRO A CA    1 
ATOM   17967 C C     . PRO A 1 4150 ? 203.523 141.329 170.848 1.00 77.81  ? 4150 PRO A C     1 
ATOM   17968 O O     . PRO A 1 4150 ? 204.455 142.147 170.825 1.00 77.81  ? 4150 PRO A O     1 
ATOM   17969 C CB    . PRO A 1 4150 ? 204.328 139.566 169.239 1.00 77.81  ? 4150 PRO A CB    1 
ATOM   17970 C CG    . PRO A 1 4150 ? 204.458 139.674 167.758 1.00 77.81  ? 4150 PRO A CG    1 
ATOM   17971 C CD    . PRO A 1 4150 ? 204.080 141.077 167.427 1.00 77.81  ? 4150 PRO A CD    1 
ATOM   17972 N N     . PRO A 1 4151 ? 202.789 141.142 171.939 1.00 78.78  ? 4151 PRO A N     1 
ATOM   17973 C CA    . PRO A 1 4151 ? 203.119 141.855 173.175 1.00 78.78  ? 4151 PRO A CA    1 
ATOM   17974 C C     . PRO A 1 4151 ? 204.469 141.416 173.709 1.00 78.78  ? 4151 PRO A C     1 
ATOM   17975 O O     . PRO A 1 4151 ? 204.902 140.278 173.516 1.00 78.78  ? 4151 PRO A O     1 
ATOM   17976 C CB    . PRO A 1 4151 ? 201.987 141.462 174.133 1.00 78.78  ? 4151 PRO A CB    1 
ATOM   17977 C CG    . PRO A 1 4151 ? 200.920 140.863 173.270 1.00 78.78  ? 4151 PRO A CG    1 
ATOM   17978 C CD    . PRO A 1 4151 ? 201.622 140.263 172.100 1.00 78.78  ? 4151 PRO A CD    1 
ATOM   17979 N N     . GLY A 1 4152 ? 205.141 142.341 174.383 1.00 73.91  ? 4152 GLY A N     1 
ATOM   17980 C CA    . GLY A 1 4152 ? 206.436 142.038 174.954 1.00 73.91  ? 4152 GLY A CA    1 
ATOM   17981 C C     . GLY A 1 4152 ? 207.471 143.107 174.686 1.00 73.91  ? 4152 GLY A C     1 
ATOM   17982 O O     . GLY A 1 4152 ? 207.515 143.683 173.596 1.00 73.91  ? 4152 GLY A O     1 
ATOM   17983 N N     . VAL A 1 4153 ? 208.312 143.382 175.684 1.00 70.17  ? 4153 VAL A N     1 
ATOM   17984 C CA    . VAL A 1 4153 ? 209.376 144.362 175.504 1.00 70.17  ? 4153 VAL A CA    1 
ATOM   17985 C C     . VAL A 1 4153 ? 210.345 143.899 174.428 1.00 70.17  ? 4153 VAL A C     1 
ATOM   17986 O O     . VAL A 1 4153 ? 210.796 144.694 173.599 1.00 70.17  ? 4153 VAL A O     1 
ATOM   17987 C CB    . VAL A 1 4153 ? 210.093 144.623 176.841 1.00 70.17  ? 4153 VAL A CB    1 
ATOM   17988 C CG1   . VAL A 1 4153 ? 211.507 145.104 176.603 1.00 70.17  ? 4153 VAL A CG1   1 
ATOM   17989 C CG2   . VAL A 1 4153 ? 209.328 145.641 177.647 1.00 70.17  ? 4153 VAL A CG2   1 
ATOM   17990 N N     . LYS A 1 4154 ? 210.675 142.608 174.419 1.00 74.00  ? 4154 LYS A N     1 
ATOM   17991 C CA    . LYS A 1 4154 ? 211.654 142.095 173.466 1.00 74.00  ? 4154 LYS A CA    1 
ATOM   17992 C C     . LYS A 1 4154 ? 211.177 142.268 172.028 1.00 74.00  ? 4154 LYS A C     1 
ATOM   17993 O O     . LYS A 1 4154 ? 211.953 142.666 171.150 1.00 74.00  ? 4154 LYS A O     1 
ATOM   17994 C CB    . LYS A 1 4154 ? 211.942 140.627 173.771 1.00 74.00  ? 4154 LYS A CB    1 
ATOM   17995 C CG    . LYS A 1 4154 ? 212.770 139.903 172.731 1.00 74.00  ? 4154 LYS A CG    1 
ATOM   17996 C CD    . LYS A 1 4154 ? 213.151 138.516 173.232 1.00 74.00  ? 4154 LYS A CD    1 
ATOM   17997 C CE    . LYS A 1 4154 ? 213.438 137.560 172.088 1.00 74.00  ? 4154 LYS A CE    1 
ATOM   17998 N NZ    . LYS A 1 4154 ? 214.622 137.989 171.296 1.00 74.00  ? 4154 LYS A NZ    1 
ATOM   17999 N N     . ALA A 1 4155 ? 209.903 141.975 171.767 1.00 74.98  ? 4155 ALA A N     1 
ATOM   18000 C CA    . ALA A 1 4155 ? 209.376 142.130 170.415 1.00 74.98  ? 4155 ALA A CA    1 
ATOM   18001 C C     . ALA A 1 4155 ? 209.380 143.590 169.983 1.00 74.98  ? 4155 ALA A C     1 
ATOM   18002 O O     . ALA A 1 4155 ? 209.717 143.902 168.836 1.00 74.98  ? 4155 ALA A O     1 
ATOM   18003 C CB    . ALA A 1 4155 ? 207.967 141.549 170.330 1.00 74.98  ? 4155 ALA A CB    1 
ATOM   18004 N N     . ASN A 1 4156 ? 208.997 144.497 170.883 1.00 72.95  ? 4156 ASN A N     1 
ATOM   18005 C CA    . ASN A 1 4156 ? 209.040 145.919 170.564 1.00 72.95  ? 4156 ASN A CA    1 
ATOM   18006 C C     . ASN A 1 4156 ? 210.463 146.372 170.283 1.00 72.95  ? 4156 ASN A C     1 
ATOM   18007 O O     . ASN A 1 4156 ? 210.706 147.150 169.353 1.00 72.95  ? 4156 ASN A O     1 
ATOM   18008 C CB    . ASN A 1 4156 ? 208.439 146.727 171.712 1.00 72.95  ? 4156 ASN A CB    1 
ATOM   18009 C CG    . ASN A 1 4156 ? 207.965 148.089 171.274 1.00 72.95  ? 4156 ASN A CG    1 
ATOM   18010 O OD1   . ASN A 1 4156 ? 208.482 148.660 170.319 1.00 72.95  ? 4156 ASN A OD1   1 
ATOM   18011 N ND2   . ASN A 1 4156 ? 206.969 148.618 171.969 1.00 72.95  ? 4156 ASN A ND2   1 
ATOM   18012 N N     . MET A 1 4157 ? 211.414 145.900 171.085 1.00 71.99  ? 4157 MET A N     1 
ATOM   18013 C CA    . MET A 1 4157 ? 212.818 146.204 170.853 1.00 71.99  ? 4157 MET A CA    1 
ATOM   18014 C C     . MET A 1 4157 ? 213.239 145.769 169.460 1.00 71.99  ? 4157 MET A C     1 
ATOM   18015 O O     . MET A 1 4157 ? 213.849 146.540 168.709 1.00 71.99  ? 4157 MET A O     1 
ATOM   18016 C CB    . MET A 1 4157 ? 213.672 145.502 171.909 1.00 71.99  ? 4157 MET A CB    1 
ATOM   18017 C CG    . MET A 1 4157 ? 213.579 146.075 173.308 1.00 71.99  ? 4157 MET A CG    1 
ATOM   18018 S SD    . MET A 1 4157 ? 214.782 147.371 173.588 1.00 71.99  ? 4157 MET A SD    1 
ATOM   18019 C CE    . MET A 1 4157 ? 213.869 148.752 172.949 1.00 71.99  ? 4157 MET A CE    1 
ATOM   18020 N N     . LEU A 1 4158 ? 212.917 144.528 169.100 1.00 78.77  ? 4158 LEU A N     1 
ATOM   18021 C CA    . LEU A 1 4158 ? 213.320 144.015 167.798 1.00 78.77  ? 4158 LEU A CA    1 
ATOM   18022 C C     . LEU A 1 4158 ? 212.674 144.809 166.671 1.00 78.77  ? 4158 LEU A C     1 
ATOM   18023 O O     . LEU A 1 4158 ? 213.339 145.159 165.691 1.00 78.77  ? 4158 LEU A O     1 
ATOM   18024 C CB    . LEU A 1 4158 ? 212.968 142.534 167.689 1.00 78.77  ? 4158 LEU A CB    1 
ATOM   18025 C CG    . LEU A 1 4158 ? 213.847 141.712 166.746 1.00 78.77  ? 4158 LEU A CG    1 
ATOM   18026 C CD1   . LEU A 1 4158 ? 215.304 142.118 166.887 1.00 78.77  ? 4158 LEU A CD1   1 
ATOM   18027 C CD2   . LEU A 1 4158 ? 213.672 140.226 167.012 1.00 78.77  ? 4158 LEU A CD2   1 
ATOM   18028 N N     . ARG A 1 4159 ? 211.382 145.117 166.798 1.00 79.69  ? 4159 ARG A N     1 
ATOM   18029 C CA    . ARG A 1 4159 ? 210.693 145.859 165.746 1.00 79.69  ? 4159 ARG A CA    1 
ATOM   18030 C C     . ARG A 1 4159 ? 211.294 147.245 165.571 1.00 79.69  ? 4159 ARG A C     1 
ATOM   18031 O O     . ARG A 1 4159 ? 211.548 147.688 164.445 1.00 79.69  ? 4159 ARG A O     1 
ATOM   18032 C CB    . ARG A 1 4159 ? 209.203 145.963 166.064 1.00 79.69  ? 4159 ARG A CB    1 
ATOM   18033 C CG    . ARG A 1 4159 ? 208.403 144.721 165.737 1.00 79.69  ? 4159 ARG A CG    1 
ATOM   18034 C CD    . ARG A 1 4159 ? 206.937 144.945 166.037 1.00 79.69  ? 4159 ARG A CD    1 
ATOM   18035 N NE    . ARG A 1 4159 ? 206.619 144.593 167.415 1.00 79.69  ? 4159 ARG A NE    1 
ATOM   18036 C CZ    . ARG A 1 4159 ? 206.013 145.403 168.270 1.00 79.69  ? 4159 ARG A CZ    1 
ATOM   18037 N NH1   . ARG A 1 4159 ? 205.633 146.619 167.919 1.00 79.69  ? 4159 ARG A NH1   1 
ATOM   18038 N NH2   . ARG A 1 4159 ? 205.785 144.983 169.510 1.00 79.69  ? 4159 ARG A NH2   1 
ATOM   18039 N N     . THR A 1 4160 ? 211.531 147.949 166.680 1.00 77.44  ? 4160 THR A N     1 
ATOM   18040 C CA    . THR A 1 4160 ? 212.082 149.294 166.588 1.00 77.44  ? 4160 THR A CA    1 
ATOM   18041 C C     . THR A 1 4160 ? 213.484 149.274 166.002 1.00 77.44  ? 4160 THR A C     1 
ATOM   18042 O O     . THR A 1 4160 ? 213.819 150.102 165.148 1.00 77.44  ? 4160 THR A O     1 
ATOM   18043 C CB    . THR A 1 4160 ? 212.084 149.958 167.962 1.00 77.44  ? 4160 THR A CB    1 
ATOM   18044 O OG1   . THR A 1 4160 ? 210.749 150.343 168.304 1.00 77.44  ? 4160 THR A OG1   1 
ATOM   18045 C CG2   . THR A 1 4160 ? 212.968 151.188 167.953 1.00 77.44  ? 4160 THR A CG2   1 
ATOM   18046 N N     . PHE A 1 4161 ? 214.315 148.324 166.431 1.00 76.50  ? 4161 PHE A N     1 
ATOM   18047 C CA    . PHE A 1 4161 ? 215.677 148.279 165.919 1.00 76.50  ? 4161 PHE A CA    1 
ATOM   18048 C C     . PHE A 1 4161 ? 215.715 147.841 164.463 1.00 76.50  ? 4161 PHE A C     1 
ATOM   18049 O O     . PHE A 1 4161 ? 216.652 148.191 163.738 1.00 76.50  ? 4161 PHE A O     1 
ATOM   18050 C CB    . PHE A 1 4161 ? 216.528 147.354 166.782 1.00 76.50  ? 4161 PHE A CB    1 
ATOM   18051 C CG    . PHE A 1 4161 ? 217.206 148.051 167.920 1.00 76.50  ? 4161 PHE A CG    1 
ATOM   18052 C CD1   . PHE A 1 4161 ? 218.134 149.046 167.685 1.00 76.50  ? 4161 PHE A CD1   1 
ATOM   18053 C CD2   . PHE A 1 4161 ? 216.912 147.712 169.228 1.00 76.50  ? 4161 PHE A CD2   1 
ATOM   18054 C CE1   . PHE A 1 4161 ? 218.759 149.689 168.732 1.00 76.50  ? 4161 PHE A CE1   1 
ATOM   18055 C CE2   . PHE A 1 4161 ? 217.533 148.350 170.278 1.00 76.50  ? 4161 PHE A CE2   1 
ATOM   18056 C CZ    . PHE A 1 4161 ? 218.457 149.340 170.030 1.00 76.50  ? 4161 PHE A CZ    1 
ATOM   18057 N N     . SER A 1 4162 ? 214.721 147.073 164.016 1.00 83.51  ? 4162 SER A N     1 
ATOM   18058 C CA    . SER A 1 4162 ? 214.672 146.695 162.609 1.00 83.51  ? 4162 SER A CA    1 
ATOM   18059 C C     . SER A 1 4162 ? 214.161 147.841 161.746 1.00 83.51  ? 4162 SER A C     1 
ATOM   18060 O O     . SER A 1 4162 ? 214.603 148.008 160.604 1.00 83.51  ? 4162 SER A O     1 
ATOM   18061 C CB    . SER A 1 4162 ? 213.799 145.456 162.429 1.00 83.51  ? 4162 SER A CB    1 
ATOM   18062 O OG    . SER A 1 4162 ? 213.453 145.275 161.068 1.00 83.51  ? 4162 SER A OG    1 
ATOM   18063 N N     . SER A 1 4163 ? 213.223 148.634 162.267 1.00 86.20  ? 4163 SER A N     1 
ATOM   18064 C CA    . SER A 1 4163 ? 212.656 149.722 161.475 1.00 86.20  ? 4163 SER A CA    1 
ATOM   18065 C C     . SER A 1 4163 ? 213.681 150.819 161.212 1.00 86.20  ? 4163 SER A C     1 
ATOM   18066 O O     . SER A 1 4163 ? 213.738 151.369 160.107 1.00 86.20  ? 4163 SER A O     1 
ATOM   18067 C CB    . SER A 1 4163 ? 211.430 150.296 162.179 1.00 86.20  ? 4163 SER A CB    1 
ATOM   18068 O OG    . SER A 1 4163 ? 211.594 150.257 163.583 1.00 86.20  ? 4163 SER A OG    1 
ATOM   18069 N N     . ILE A 1 4164 ? 214.486 151.157 162.209 1.00 83.92  ? 4164 ILE A N     1 
ATOM   18070 C CA    . ILE A 1 4164 ? 215.485 152.217 162.036 1.00 83.92  ? 4164 ILE A CA    1 
ATOM   18071 C C     . ILE A 1 4164 ? 216.599 151.713 161.126 1.00 83.92  ? 4164 ILE A C     1 
ATOM   18072 O O     . ILE A 1 4164 ? 217.171 150.641 161.388 1.00 83.92  ? 4164 ILE A O     1 
ATOM   18073 C CB    . ILE A 1 4164 ? 216.037 152.652 163.389 1.00 83.92  ? 4164 ILE A CB    1 
ATOM   18074 C CG1   . ILE A 1 4164 ? 214.910 153.174 164.277 1.00 83.92  ? 4164 ILE A CG1   1 
ATOM   18075 C CG2   . ILE A 1 4164 ? 217.104 153.709 163.206 1.00 83.92  ? 4164 ILE A CG2   1 
ATOM   18076 C CD1   . ILE A 1 4164 ? 215.320 153.387 165.710 1.00 83.92  ? 4164 ILE A CD1   1 
ATOM   18077 N N     . PRO A 1 4165 ? 216.937 152.433 160.059 1.00 89.37  ? 4165 PRO A N     1 
ATOM   18078 C CA    . PRO A 1 4165 ? 218.000 151.968 159.161 1.00 89.37  ? 4165 PRO A CA    1 
ATOM   18079 C C     . PRO A 1 4165 ? 219.338 151.870 159.876 1.00 89.37  ? 4165 PRO A C     1 
ATOM   18080 O O     . PRO A 1 4165 ? 219.669 152.684 160.740 1.00 89.37  ? 4165 PRO A O     1 
ATOM   18081 C CB    . PRO A 1 4165 ? 218.032 153.037 158.063 1.00 89.37  ? 4165 PRO A CB    1 
ATOM   18082 C CG    . PRO A 1 4165 ? 216.705 153.715 158.144 1.00 89.37  ? 4165 PRO A CG    1 
ATOM   18083 C CD    . PRO A 1 4165 ? 216.319 153.681 159.587 1.00 89.37  ? 4165 PRO A CD    1 
ATOM   18084 N N     . VAL A 1 4166 ? 220.116 150.856 159.491 1.00 92.48  ? 4166 VAL A N     1 
ATOM   18085 C CA    . VAL A 1 4166 ? 221.424 150.643 160.102 1.00 92.48  ? 4166 VAL A CA    1 
ATOM   18086 C C     . VAL A 1 4166 ? 222.358 151.802 159.798 1.00 92.48  ? 4166 VAL A C     1 
ATOM   18087 O O     . VAL A 1 4166 ? 223.280 152.087 160.571 1.00 92.48  ? 4166 VAL A O     1 
ATOM   18088 C CB    . VAL A 1 4166 ? 222.019 149.307 159.628 1.00 92.48  ? 4166 VAL A CB    1 
ATOM   18089 C CG1   . VAL A 1 4166 ? 223.191 148.907 160.506 1.00 92.48  ? 4166 VAL A CG1   1 
ATOM   18090 C CG2   . VAL A 1 4166 ? 220.952 148.229 159.626 1.00 92.48  ? 4166 VAL A CG2   1 
ATOM   18091 N N     . SER A 1 4167 ? 222.144 152.487 158.674 1.00 96.21  ? 4167 SER A N     1 
ATOM   18092 C CA    . SER A 1 4167 ? 222.992 153.620 158.332 1.00 96.21  ? 4167 SER A CA    1 
ATOM   18093 C C     . SER A 1 4167 ? 222.881 154.721 159.375 1.00 96.21  ? 4167 SER A C     1 
ATOM   18094 O O     . SER A 1 4167 ? 223.882 155.349 159.735 1.00 96.21  ? 4167 SER A O     1 
ATOM   18095 C CB    . SER A 1 4167 ? 222.619 154.155 156.951 1.00 96.21  ? 4167 SER A CB    1 
ATOM   18096 O OG    . SER A 1 4167 ? 221.372 154.824 156.994 1.00 96.21  ? 4167 SER A OG    1 
ATOM   18097 N N     . ARG A 1 4168 ? 221.668 154.968 159.873 1.00 93.16  ? 4168 ARG A N     1 
ATOM   18098 C CA    . ARG A 1 4168 ? 221.475 156.030 160.853 1.00 93.16  ? 4168 ARG A CA    1 
ATOM   18099 C C     . ARG A 1 4168 ? 222.236 155.744 162.141 1.00 93.16  ? 4168 ARG A C     1 
ATOM   18100 O O     . ARG A 1 4168 ? 222.841 156.649 162.726 1.00 93.16  ? 4168 ARG A O     1 
ATOM   18101 C CB    . ARG A 1 4168 ? 219.987 156.211 161.138 1.00 93.16  ? 4168 ARG A CB    1 
ATOM   18102 C CG    . ARG A 1 4168 ? 219.245 156.967 160.054 1.00 93.16  ? 4168 ARG A CG    1 
ATOM   18103 C CD    . ARG A 1 4168 ? 217.775 157.100 160.397 1.00 93.16  ? 4168 ARG A CD    1 
ATOM   18104 N NE    . ARG A 1 4168 ? 217.576 157.748 161.686 1.00 93.16  ? 4168 ARG A NE    1 
ATOM   18105 C CZ    . ARG A 1 4168 ? 216.744 158.759 161.893 1.00 93.16  ? 4168 ARG A CZ    1 
ATOM   18106 N NH1   . ARG A 1 4168 ? 216.009 159.260 160.915 1.00 93.16  ? 4168 ARG A NH1   1 
ATOM   18107 N NH2   . ARG A 1 4168 ? 216.647 159.279 163.112 1.00 93.16  ? 4168 ARG A NH2   1 
ATOM   18108 N N     . ILE A 1 4169 ? 222.215 154.495 162.603 1.00 90.58  ? 4169 ILE A N     1 
ATOM   18109 C CA    . ILE A 1 4169 ? 222.899 154.163 163.848 1.00 90.58  ? 4169 ILE A CA    1 
ATOM   18110 C C     . ILE A 1 4169 ? 224.408 154.253 163.669 1.00 90.58  ? 4169 ILE A C     1 
ATOM   18111 O O     . ILE A 1 4169 ? 225.111 154.869 164.477 1.00 90.58  ? 4169 ILE A O     1 
ATOM   18112 C CB    . ILE A 1 4169 ? 222.479 152.769 164.341 1.00 90.58  ? 4169 ILE A CB    1 
ATOM   18113 C CG1   . ILE A 1 4169 ? 220.960 152.671 164.456 1.00 90.58  ? 4169 ILE A CG1   1 
ATOM   18114 C CG2   . ILE A 1 4169 ? 223.119 152.476 165.681 1.00 90.58  ? 4169 ILE A CG2   1 
ATOM   18115 C CD1   . ILE A 1 4169 ? 220.323 153.865 165.102 1.00 90.58  ? 4169 ILE A CD1   1 
ATOM   18116 N N     . CYS A 1 4170 ? 224.930 153.647 162.604 1.00 96.51  ? 4170 CYS A N     1 
ATOM   18117 C CA    . CYS A 1 4170 ? 226.373 153.605 162.375 1.00 96.51  ? 4170 CYS A CA    1 
ATOM   18118 C C     . CYS A 1 4170 ? 226.817 154.896 161.689 1.00 96.51  ? 4170 CYS A C     1 
ATOM   18119 O O     . CYS A 1 4170 ? 227.142 154.940 160.502 1.00 96.51  ? 4170 CYS A O     1 
ATOM   18120 C CB    . CYS A 1 4170 ? 226.750 152.376 161.558 1.00 96.51  ? 4170 CYS A CB    1 
ATOM   18121 S SG    . CYS A 1 4170 ? 225.828 150.881 161.967 1.00 96.51  ? 4170 CYS A SG    1 
ATOM   18122 N N     . LYS A 1 4171 ? 226.818 155.968 162.475 1.00 95.11  ? 4171 LYS A N     1 
ATOM   18123 C CA    . LYS A 1 4171 ? 227.231 157.273 161.982 1.00 95.11  ? 4171 LYS A CA    1 
ATOM   18124 C C     . LYS A 1 4171 ? 227.554 158.149 163.180 1.00 95.11  ? 4171 LYS A C     1 
ATOM   18125 O O     . LYS A 1 4171 ? 227.190 157.827 164.314 1.00 95.11  ? 4171 LYS A O     1 
ATOM   18126 C CB    . LYS A 1 4171 ? 226.143 157.914 161.117 1.00 95.11  ? 4171 LYS A CB    1 
ATOM   18127 C CG    . LYS A 1 4171 ? 226.660 158.920 160.107 1.00 95.11  ? 4171 LYS A CG    1 
ATOM   18128 C CD    . LYS A 1 4171 ? 225.545 159.426 159.207 1.00 95.11  ? 4171 LYS A CD    1 
ATOM   18129 C CE    . LYS A 1 4171 ? 224.675 158.287 158.696 1.00 95.11  ? 4171 LYS A CE    1 
ATOM   18130 N NZ    . LYS A 1 4171 ? 225.466 157.235 158.000 1.00 95.11  ? 4171 LYS A NZ    1 
ATOM   18131 N N     . SER A 1 4172 ? 228.264 159.252 162.917 1.00 96.38  ? 4172 SER A N     1 
ATOM   18132 C CA    . SER A 1 4172 ? 228.491 160.279 163.928 1.00 96.38  ? 4172 SER A CA    1 
ATOM   18133 C C     . SER A 1 4172 ? 229.292 159.694 165.090 1.00 96.38  ? 4172 SER A C     1 
ATOM   18134 O O     . SER A 1 4172 ? 229.870 158.611 164.939 1.00 96.38  ? 4172 SER A O     1 
ATOM   18135 C CB    . SER A 1 4172 ? 227.142 160.849 164.376 1.00 96.38  ? 4172 SER A CB    1 
ATOM   18136 O OG    . SER A 1 4172 ? 226.503 161.531 163.313 1.00 96.38  ? 4172 SER A OG    1 
ATOM   18137 N N     . PRO A 1 4173 ? 229.395 160.370 166.238 1.00 96.44  ? 4173 PRO A N     1 
ATOM   18138 C CA    . PRO A 1 4173 ? 229.996 159.718 167.404 1.00 96.44  ? 4173 PRO A CA    1 
ATOM   18139 C C     . PRO A 1 4173 ? 229.299 158.409 167.735 1.00 96.44  ? 4173 PRO A C     1 
ATOM   18140 O O     . PRO A 1 4173 ? 228.079 158.286 167.619 1.00 96.44  ? 4173 PRO A O     1 
ATOM   18141 C CB    . PRO A 1 4173 ? 229.802 160.749 168.514 1.00 96.44  ? 4173 PRO A CB    1 
ATOM   18142 C CG    . PRO A 1 4173 ? 229.888 162.031 167.824 1.00 96.44  ? 4173 PRO A CG    1 
ATOM   18143 C CD    . PRO A 1 4173 ? 229.397 161.836 166.411 1.00 96.44  ? 4173 PRO A CD    1 
ATOM   18144 N N     . ASN A 1 4174 ? 230.095 157.424 168.157 1.00 100.10 ? 4174 ASN A N     1 
ATOM   18145 C CA    . ASN A 1 4174 ? 229.562 156.099 168.445 1.00 100.10 ? 4174 ASN A CA    1 
ATOM   18146 C C     . ASN A 1 4174 ? 228.565 156.118 169.593 1.00 100.10 ? 4174 ASN A C     1 
ATOM   18147 O O     . ASN A 1 4174 ? 227.814 155.152 169.764 1.00 100.10 ? 4174 ASN A O     1 
ATOM   18148 C CB    . ASN A 1 4174 ? 230.702 155.136 168.764 1.00 100.10 ? 4174 ASN A CB    1 
ATOM   18149 C CG    . ASN A 1 4174 ? 231.942 155.418 167.950 1.00 100.10 ? 4174 ASN A CG    1 
ATOM   18150 O OD1   . ASN A 1 4174 ? 231.912 155.384 166.722 1.00 100.10 ? 4174 ASN A OD1   1 
ATOM   18151 N ND2   . ASN A 1 4174 ? 233.044 155.701 168.632 1.00 100.10 ? 4174 ASN A ND2   1 
ATOM   18152 N N     . GLU A 1 4175 ? 228.539 157.192 170.381 1.00 94.64  ? 4175 GLU A N     1 
ATOM   18153 C CA    . GLU A 1 4175 ? 227.532 157.326 171.423 1.00 94.64  ? 4175 GLU A CA    1 
ATOM   18154 C C     . GLU A 1 4175 ? 226.130 157.415 170.845 1.00 94.64  ? 4175 GLU A C     1 
ATOM   18155 O O     . GLU A 1 4175 ? 225.153 157.251 171.585 1.00 94.64  ? 4175 GLU A O     1 
ATOM   18156 C CB    . GLU A 1 4175 ? 227.826 158.559 172.274 1.00 94.64  ? 4175 GLU A CB    1 
ATOM   18157 C CG    . GLU A 1 4175 ? 229.095 158.456 173.103 1.00 94.64  ? 4175 GLU A CG    1 
ATOM   18158 C CD    . GLU A 1 4175 ? 230.353 158.678 172.288 1.00 94.64  ? 4175 GLU A CD    1 
ATOM   18159 O OE1   . GLU A 1 4175 ? 230.241 158.927 171.071 1.00 94.64  ? 4175 GLU A OE1   1 
ATOM   18160 O OE2   . GLU A 1 4175 ? 231.457 158.605 172.867 1.00 94.64  ? 4175 GLU A OE2   1 
ATOM   18161 N N     . ARG A 1 4176 ? 226.010 157.681 169.543 1.00 85.09  ? 4176 ARG A N     1 
ATOM   18162 C CA    . ARG A 1 4176 ? 224.696 157.718 168.914 1.00 85.09  ? 4176 ARG A CA    1 
ATOM   18163 C C     . ARG A 1 4176 ? 224.005 156.367 169.013 1.00 85.09  ? 4176 ARG A C     1 
ATOM   18164 O O     . ARG A 1 4176 ? 222.784 156.300 169.182 1.00 85.09  ? 4176 ARG A O     1 
ATOM   18165 C CB    . ARG A 1 4176 ? 224.823 158.146 167.455 1.00 85.09  ? 4176 ARG A CB    1 
ATOM   18166 C CG    . ARG A 1 4176 ? 223.495 158.270 166.741 1.00 85.09  ? 4176 ARG A CG    1 
ATOM   18167 C CD    . ARG A 1 4176 ? 223.676 158.785 165.330 1.00 85.09  ? 4176 ARG A CD    1 
ATOM   18168 N NE    . ARG A 1 4176 ? 224.080 160.183 165.307 1.00 85.09  ? 4176 ARG A NE    1 
ATOM   18169 C CZ    . ARG A 1 4176 ? 223.760 161.034 164.343 1.00 85.09  ? 4176 ARG A CZ    1 
ATOM   18170 N NH1   . ARG A 1 4176 ? 223.027 160.662 163.309 1.00 85.09  ? 4176 ARG A NH1   1 
ATOM   18171 N NH2   . ARG A 1 4176 ? 224.191 162.290 164.417 1.00 85.09  ? 4176 ARG A NH2   1 
ATOM   18172 N N     . ALA A 1 4177 ? 224.767 155.278 168.907 1.00 83.72  ? 4177 ALA A N     1 
ATOM   18173 C CA    . ALA A 1 4177 ? 224.175 153.950 169.024 1.00 83.72  ? 4177 ALA A CA    1 
ATOM   18174 C C     . ALA A 1 4177 ? 223.569 153.739 170.405 1.00 83.72  ? 4177 ALA A C     1 
ATOM   18175 O O     . ALA A 1 4177 ? 222.438 153.257 170.535 1.00 83.72  ? 4177 ALA A O     1 
ATOM   18176 C CB    . ALA A 1 4177 ? 225.225 152.882 168.727 1.00 83.72  ? 4177 ALA A CB    1 
ATOM   18177 N N     . ARG A 1 4178 ? 224.306 154.107 171.452 1.00 84.18  ? 4178 ARG A N     1 
ATOM   18178 C CA    . ARG A 1 4178 ? 223.779 153.954 172.803 1.00 84.18  ? 4178 ARG A CA    1 
ATOM   18179 C C     . ARG A 1 4178 ? 222.586 154.870 173.032 1.00 84.18  ? 4178 ARG A C     1 
ATOM   18180 O O     . ARG A 1 4178 ? 221.620 154.484 173.698 1.00 84.18  ? 4178 ARG A O     1 
ATOM   18181 C CB    . ARG A 1 4178 ? 224.874 154.224 173.831 1.00 84.18  ? 4178 ARG A CB    1 
ATOM   18182 C CG    . ARG A 1 4178 ? 224.368 154.308 175.256 1.00 84.18  ? 4178 ARG A CG    1 
ATOM   18183 C CD    . ARG A 1 4178 ? 225.436 153.918 176.257 1.00 84.18  ? 4178 ARG A CD    1 
ATOM   18184 N NE    . ARG A 1 4178 ? 225.306 152.535 176.697 1.00 84.18  ? 4178 ARG A NE    1 
ATOM   18185 C CZ    . ARG A 1 4178 ? 226.322 151.778 177.084 1.00 84.18  ? 4178 ARG A CZ    1 
ATOM   18186 N NH1   . ARG A 1 4178 ? 227.564 152.232 177.078 1.00 84.18  ? 4178 ARG A NH1   1 
ATOM   18187 N NH2   . ARG A 1 4178 ? 226.086 150.534 177.491 1.00 84.18  ? 4178 ARG A NH2   1 
ATOM   18188 N N     . LEU A 1 4179 ? 222.634 156.090 172.494 1.00 80.64  ? 4179 LEU A N     1 
ATOM   18189 C CA    . LEU A 1 4179 ? 221.495 156.990 172.634 1.00 80.64  ? 4179 LEU A CA    1 
ATOM   18190 C C     . LEU A 1 4179 ? 220.260 156.421 171.955 1.00 80.64  ? 4179 LEU A C     1 
ATOM   18191 O O     . LEU A 1 4179 ? 219.153 156.497 172.499 1.00 80.64  ? 4179 LEU A O     1 
ATOM   18192 C CB    . LEU A 1 4179 ? 221.829 158.362 172.060 1.00 80.64  ? 4179 LEU A CB    1 
ATOM   18193 C CG    . LEU A 1 4179 ? 222.544 159.298 173.025 1.00 80.64  ? 4179 LEU A CG    1 
ATOM   18194 C CD1   . LEU A 1 4179 ? 222.496 160.721 172.509 1.00 80.64  ? 4179 LEU A CD1   1 
ATOM   18195 C CD2   . LEU A 1 4179 ? 221.903 159.198 174.391 1.00 80.64  ? 4179 LEU A CD2   1 
ATOM   18196 N N     . TYR A 1 4180 ? 220.427 155.853 170.762 1.00 79.47  ? 4180 TYR A N     1 
ATOM   18197 C CA    . TYR A 1 4180 ? 219.296 155.245 170.076 1.00 79.47  ? 4180 TYR A CA    1 
ATOM   18198 C C     . TYR A 1 4180 ? 218.773 154.044 170.844 1.00 79.47  ? 4180 TYR A C     1 
ATOM   18199 O O     . TYR A 1 4180 ? 217.560 153.821 170.902 1.00 79.47  ? 4180 TYR A O     1 
ATOM   18200 C CB    . TYR A 1 4180 ? 219.691 154.850 168.660 1.00 79.47  ? 4180 TYR A CB    1 
ATOM   18201 C CG    . TYR A 1 4180 ? 219.294 155.869 167.626 1.00 79.47  ? 4180 TYR A CG    1 
ATOM   18202 C CD1   . TYR A 1 4180 ? 220.120 156.939 167.327 1.00 79.47  ? 4180 TYR A CD1   1 
ATOM   18203 C CD2   . TYR A 1 4180 ? 218.094 155.759 166.946 1.00 79.47  ? 4180 TYR A CD2   1 
ATOM   18204 C CE1   . TYR A 1 4180 ? 219.762 157.870 166.381 1.00 79.47  ? 4180 TYR A CE1   1 
ATOM   18205 C CE2   . TYR A 1 4180 ? 217.729 156.684 165.997 1.00 79.47  ? 4180 TYR A CE2   1 
ATOM   18206 C CZ    . TYR A 1 4180 ? 218.565 157.738 165.719 1.00 79.47  ? 4180 TYR A CZ    1 
ATOM   18207 O OH    . TYR A 1 4180 ? 218.197 158.663 164.771 1.00 79.47  ? 4180 TYR A OH    1 
ATOM   18208 N N     . PHE A 1 4181 ? 219.668 153.255 171.437 1.00 77.02  ? 4181 PHE A N     1 
ATOM   18209 C CA    . PHE A 1 4181 ? 219.216 152.136 172.256 1.00 77.02  ? 4181 PHE A CA    1 
ATOM   18210 C C     . PHE A 1 4181 ? 218.407 152.623 173.450 1.00 77.02  ? 4181 PHE A C     1 
ATOM   18211 O O     . PHE A 1 4181 ? 217.366 152.047 173.780 1.00 77.02  ? 4181 PHE A O     1 
ATOM   18212 C CB    . PHE A 1 4181 ? 220.406 151.307 172.728 1.00 77.02  ? 4181 PHE A CB    1 
ATOM   18213 C CG    . PHE A 1 4181 ? 220.069 150.339 173.823 1.00 77.02  ? 4181 PHE A CG    1 
ATOM   18214 C CD1   . PHE A 1 4181 ? 219.371 149.181 173.548 1.00 77.02  ? 4181 PHE A CD1   1 
ATOM   18215 C CD2   . PHE A 1 4181 ? 220.449 150.588 175.125 1.00 77.02  ? 4181 PHE A CD2   1 
ATOM   18216 C CE1   . PHE A 1 4181 ? 219.061 148.294 174.549 1.00 77.02  ? 4181 PHE A CE1   1 
ATOM   18217 C CE2   . PHE A 1 4181 ? 220.141 149.703 176.127 1.00 77.02  ? 4181 PHE A CE2   1 
ATOM   18218 C CZ    . PHE A 1 4181 ? 219.446 148.555 175.838 1.00 77.02  ? 4181 PHE A CZ    1 
ATOM   18219 N N     . LEU A 1 4182 ? 218.872 153.682 174.111 1.00 70.25  ? 4182 LEU A N     1 
ATOM   18220 C CA    . LEU A 1 4182 ? 218.129 154.225 175.241 1.00 70.25  ? 4182 LEU A CA    1 
ATOM   18221 C C     . LEU A 1 4182 ? 216.768 154.742 174.804 1.00 70.25  ? 4182 LEU A C     1 
ATOM   18222 O O     . LEU A 1 4182 ? 215.760 154.509 175.480 1.00 70.25  ? 4182 LEU A O     1 
ATOM   18223 C CB    . LEU A 1 4182 ? 218.930 155.338 175.910 1.00 70.25  ? 4182 LEU A CB    1 
ATOM   18224 C CG    . LEU A 1 4182 ? 219.883 154.894 177.012 1.00 70.25  ? 4182 LEU A CG    1 
ATOM   18225 C CD1   . LEU A 1 4182 ? 220.717 156.064 177.478 1.00 70.25  ? 4182 LEU A CD1   1 
ATOM   18226 C CD2   . LEU A 1 4182 ? 219.098 154.311 178.164 1.00 70.25  ? 4182 LEU A CD2   1 
ATOM   18227 N N     . LEU A 1 4183 ? 216.721 155.451 173.677 1.00 71.79  ? 4183 LEU A N     1 
ATOM   18228 C CA    . LEU A 1 4183 ? 215.451 155.978 173.194 1.00 71.79  ? 4183 LEU A CA    1 
ATOM   18229 C C     . LEU A 1 4183 ? 214.496 154.850 172.841 1.00 71.79  ? 4183 LEU A C     1 
ATOM   18230 O O     . LEU A 1 4183 ? 213.299 154.922 173.142 1.00 71.79  ? 4183 LEU A O     1 
ATOM   18231 C CB    . LEU A 1 4183 ? 215.690 156.895 171.995 1.00 71.79  ? 4183 LEU A CB    1 
ATOM   18232 C CG    . LEU A 1 4183 ? 214.542 157.314 171.076 1.00 71.79  ? 4183 LEU A CG    1 
ATOM   18233 C CD1   . LEU A 1 4183 ? 214.936 158.595 170.379 1.00 71.79  ? 4183 LEU A CD1   1 
ATOM   18234 C CD2   . LEU A 1 4183 ? 214.215 156.263 170.029 1.00 71.79  ? 4183 LEU A CD2   1 
ATOM   18235 N N     . ALA A 1 4184 ? 215.004 153.803 172.192 1.00 70.12  ? 4184 ALA A N     1 
ATOM   18236 C CA    . ALA A 1 4184 ? 214.167 152.658 171.867 1.00 70.12  ? 4184 ALA A CA    1 
ATOM   18237 C C     . ALA A 1 4184 ? 213.657 151.980 173.127 1.00 70.12  ? 4184 ALA A C     1 
ATOM   18238 O O     . ALA A 1 4184 ? 212.499 151.556 173.183 1.00 70.12  ? 4184 ALA A O     1 
ATOM   18239 C CB    . ALA A 1 4184 ? 214.943 151.669 171.002 1.00 70.12  ? 4184 ALA A CB    1 
ATOM   18240 N N     . TRP A 1 4185 ? 214.512 151.849 174.143 1.00 66.08  ? 4185 TRP A N     1 
ATOM   18241 C CA    . TRP A 1 4185 ? 214.076 151.245 175.395 1.00 66.08  ? 4185 TRP A CA    1 
ATOM   18242 C C     . TRP A 1 4185 ? 212.974 152.069 176.034 1.00 66.08  ? 4185 TRP A C     1 
ATOM   18243 O O     . TRP A 1 4185 ? 211.984 151.521 176.530 1.00 66.08  ? 4185 TRP A O     1 
ATOM   18244 C CB    . TRP A 1 4185 ? 215.253 151.105 176.353 1.00 66.08  ? 4185 TRP A CB    1 
ATOM   18245 C CG    . TRP A 1 4185 ? 214.842 150.679 177.714 1.00 66.08  ? 4185 TRP A CG    1 
ATOM   18246 C CD1   . TRP A 1 4185 ? 214.498 151.482 178.755 1.00 66.08  ? 4185 TRP A CD1   1 
ATOM   18247 C CD2   . TRP A 1 4185 ? 214.735 149.337 178.190 1.00 66.08  ? 4185 TRP A CD2   1 
ATOM   18248 N NE1   . TRP A 1 4185 ? 214.178 150.725 179.851 1.00 66.08  ? 4185 TRP A NE1   1 
ATOM   18249 C CE2   . TRP A 1 4185 ? 214.318 149.402 179.529 1.00 66.08  ? 4185 TRP A CE2   1 
ATOM   18250 C CE3   . TRP A 1 4185 ? 214.953 148.085 177.613 1.00 66.08  ? 4185 TRP A CE3   1 
ATOM   18251 C CZ2   . TRP A 1 4185 ? 214.112 148.267 180.300 1.00 66.08  ? 4185 TRP A CZ2   1 
ATOM   18252 C CZ3   . TRP A 1 4185 ? 214.749 146.961 178.378 1.00 66.08  ? 4185 TRP A CZ3   1 
ATOM   18253 C CH2   . TRP A 1 4185 ? 214.333 147.057 179.707 1.00 66.08  ? 4185 TRP A CH2   1 
ATOM   18254 N N     . PHE A 1 4186 ? 213.133 153.390 176.034 1.00 67.41  ? 4186 PHE A N     1 
ATOM   18255 C CA    . PHE A 1 4186 ? 212.093 154.254 176.573 1.00 67.41  ? 4186 PHE A CA    1 
ATOM   18256 C C     . PHE A 1 4186 ? 210.793 154.085 175.804 1.00 67.41  ? 4186 PHE A C     1 
ATOM   18257 O O     . PHE A 1 4186 ? 209.714 153.982 176.402 1.00 67.41  ? 4186 PHE A O     1 
ATOM   18258 C CB    . PHE A 1 4186 ? 212.552 155.706 176.530 1.00 67.41  ? 4186 PHE A CB    1 
ATOM   18259 C CG    . PHE A 1 4186 ? 211.490 156.677 176.909 1.00 67.41  ? 4186 PHE A CG    1 
ATOM   18260 C CD1   . PHE A 1 4186 ? 211.089 156.800 178.220 1.00 67.41  ? 4186 PHE A CD1   1 
ATOM   18261 C CD2   . PHE A 1 4186 ? 210.887 157.464 175.955 1.00 67.41  ? 4186 PHE A CD2   1 
ATOM   18262 C CE1   . PHE A 1 4186 ? 210.108 157.693 178.574 1.00 67.41  ? 4186 PHE A CE1   1 
ATOM   18263 C CE2   . PHE A 1 4186 ? 209.906 158.358 176.304 1.00 67.41  ? 4186 PHE A CE2   1 
ATOM   18264 C CZ    . PHE A 1 4186 ? 209.515 158.473 177.614 1.00 67.41  ? 4186 PHE A CZ    1 
ATOM   18265 N N     . HIS A 1 4187 ? 210.878 154.048 174.475 1.00 66.60  ? 4187 HIS A N     1 
ATOM   18266 C CA    . HIS A 1 4187 ? 209.677 153.886 173.666 1.00 66.60  ? 4187 HIS A CA    1 
ATOM   18267 C C     . HIS A 1 4187 ? 208.990 152.565 173.960 1.00 66.60  ? 4187 HIS A C     1 
ATOM   18268 O O     . HIS A 1 4187 ? 207.765 152.514 174.107 1.00 66.60  ? 4187 HIS A O     1 
ATOM   18269 C CB    . HIS A 1 4187 ? 210.019 153.975 172.186 1.00 66.60  ? 4187 HIS A CB    1 
ATOM   18270 C CG    . HIS A 1 4187 ? 208.824 153.889 171.296 1.00 66.60  ? 4187 HIS A CG    1 
ATOM   18271 N ND1   . HIS A 1 4187 ? 207.840 154.851 171.281 1.00 66.60  ? 4187 HIS A ND1   1 
ATOM   18272 C CD2   . HIS A 1 4187 ? 208.438 152.941 170.412 1.00 66.60  ? 4187 HIS A CD2   1 
ATOM   18273 C CE1   . HIS A 1 4187 ? 206.907 154.509 170.411 1.00 66.60  ? 4187 HIS A CE1   1 
ATOM   18274 N NE2   . HIS A 1 4187 ? 207.246 153.353 169.870 1.00 66.60  ? 4187 HIS A NE2   1 
ATOM   18275 N N     . ALA A 1 4188 ? 209.763 151.484 174.047 1.00 67.30  ? 4188 ALA A N     1 
ATOM   18276 C CA    . ALA A 1 4188 ? 209.175 150.179 174.317 1.00 67.30  ? 4188 ALA A CA    1 
ATOM   18277 C C     . ALA A 1 4188 ? 208.555 150.135 175.704 1.00 67.30  ? 4188 ALA A C     1 
ATOM   18278 O O     . ALA A 1 4188 ? 207.496 149.530 175.898 1.00 67.30  ? 4188 ALA A O     1 
ATOM   18279 C CB    . ALA A 1 4188 ? 210.226 149.084 174.158 1.00 67.30  ? 4188 ALA A CB    1 
ATOM   18280 N N     . ILE A 1 4189 ? 209.193 150.776 176.682 1.00 64.57  ? 4189 ILE A N     1 
ATOM   18281 C CA    . ILE A 1 4189 ? 208.634 150.810 178.029 1.00 64.57  ? 4189 ILE A CA    1 
ATOM   18282 C C     . ILE A 1 4189 ? 207.287 151.519 178.023 1.00 64.57  ? 4189 ILE A C     1 
ATOM   18283 O O     . ILE A 1 4189 ? 206.288 150.999 178.537 1.00 64.57  ? 4189 ILE A O     1 
ATOM   18284 C CB    . ILE A 1 4189 ? 209.619 151.484 178.998 1.00 64.57  ? 4189 ILE A CB    1 
ATOM   18285 C CG1   . ILE A 1 4189 ? 210.714 150.506 179.404 1.00 64.57  ? 4189 ILE A CG1   1 
ATOM   18286 C CG2   . ILE A 1 4189 ? 208.892 151.985 180.223 1.00 64.57  ? 4189 ILE A CG2   1 
ATOM   18287 C CD1   . ILE A 1 4189 ? 210.187 149.222 179.971 1.00 64.57  ? 4189 ILE A CD1   1 
ATOM   18288 N N     . ILE A 1 4190 ? 207.234 152.713 177.427 1.00 63.88  ? 4190 ILE A N     1 
ATOM   18289 C CA    . ILE A 1 4190 ? 205.986 153.466 177.456 1.00 63.88  ? 4190 ILE A CA    1 
ATOM   18290 C C     . ILE A 1 4190 ? 204.940 152.882 176.522 1.00 63.88  ? 4190 ILE A C     1 
ATOM   18291 O O     . ILE A 1 4190 ? 203.757 153.209 176.650 1.00 63.88  ? 4190 ILE A O     1 
ATOM   18292 C CB    . ILE A 1 4190 ? 206.212 154.951 177.128 1.00 63.88  ? 4190 ILE A CB    1 
ATOM   18293 C CG1   . ILE A 1 4190 ? 206.286 155.156 175.618 1.00 63.88  ? 4190 ILE A CG1   1 
ATOM   18294 C CG2   . ILE A 1 4190 ? 207.430 155.484 177.848 1.00 63.88  ? 4190 ILE A CG2   1 
ATOM   18295 C CD1   . ILE A 1 4190 ? 205.819 156.515 175.176 1.00 63.88  ? 4190 ILE A CD1   1 
ATOM   18296 N N     . GLN A 1 4191 ? 205.332 152.031 175.578 1.00 65.45  ? 4191 GLN A N     1 
ATOM   18297 C CA    . GLN A 1 4191 ? 204.323 151.356 174.774 1.00 65.45  ? 4191 GLN A CA    1 
ATOM   18298 C C     . GLN A 1 4191 ? 203.773 150.133 175.490 1.00 65.45  ? 4191 GLN A C     1 
ATOM   18299 O O     . GLN A 1 4191 ? 202.569 149.868 175.432 1.00 65.45  ? 4191 GLN A O     1 
ATOM   18300 C CB    . GLN A 1 4191 ? 204.900 150.958 173.419 1.00 65.45  ? 4191 GLN A CB    1 
ATOM   18301 C CG    . GLN A 1 4191 ? 204.577 151.920 172.303 1.00 65.45  ? 4191 GLN A CG    1 
ATOM   18302 C CD    . GLN A 1 4191 ? 204.403 151.217 170.979 1.00 65.45  ? 4191 GLN A CD    1 
ATOM   18303 O OE1   . GLN A 1 4191 ? 205.273 150.463 170.546 1.00 65.45  ? 4191 GLN A OE1   1 
ATOM   18304 N NE2   . GLN A 1 4191 ? 203.274 151.455 170.327 1.00 65.45  ? 4191 GLN A NE2   1 
ATOM   18305 N N     . GLU A 1 4192 ? 204.634 149.379 176.172 1.00 66.51  ? 4192 GLU A N     1 
ATOM   18306 C CA    . GLU A 1 4192 ? 204.162 148.203 176.885 1.00 66.51  ? 4192 GLU A CA    1 
ATOM   18307 C C     . GLU A 1 4192 ? 203.340 148.585 178.103 1.00 66.51  ? 4192 GLU A C     1 
ATOM   18308 O O     . GLU A 1 4192 ? 202.432 147.843 178.490 1.00 66.51  ? 4192 GLU A O     1 
ATOM   18309 C CB    . GLU A 1 4192 ? 205.338 147.324 177.291 1.00 66.51  ? 4192 GLU A CB    1 
ATOM   18310 C CG    . GLU A 1 4192 ? 206.012 146.631 176.126 1.00 66.51  ? 4192 GLU A CG    1 
ATOM   18311 C CD    . GLU A 1 4192 ? 205.052 145.789 175.319 1.00 66.51  ? 4192 GLU A CD    1 
ATOM   18312 O OE1   . GLU A 1 4192 ? 204.500 146.303 174.324 1.00 66.51  ? 4192 GLU A OE1   1 
ATOM   18313 O OE2   . GLU A 1 4192 ? 204.842 144.614 175.681 1.00 66.51  ? 4192 GLU A OE2   1 
ATOM   18314 N N     . ARG A 1 4193 ? 203.628 149.733 178.716 1.00 63.45  ? 4193 ARG A N     1 
ATOM   18315 C CA    . ARG A 1 4193 ? 202.800 150.172 179.829 1.00 63.45  ? 4193 ARG A CA    1 
ATOM   18316 C C     . ARG A 1 4193 ? 201.380 150.499 179.394 1.00 63.45  ? 4193 ARG A C     1 
ATOM   18317 O O     . ARG A 1 4193 ? 200.488 150.577 180.243 1.00 63.45  ? 4193 ARG A O     1 
ATOM   18318 C CB    . ARG A 1 4193 ? 203.421 151.387 180.510 1.00 63.45  ? 4193 ARG A CB    1 
ATOM   18319 C CG    . ARG A 1 4193 ? 204.651 151.081 181.327 1.00 63.45  ? 4193 ARG A CG    1 
ATOM   18320 C CD    . ARG A 1 4193 ? 205.106 152.314 182.066 1.00 63.45  ? 4193 ARG A CD    1 
ATOM   18321 N NE    . ARG A 1 4193 ? 204.121 152.739 183.050 1.00 63.45  ? 4193 ARG A NE    1 
ATOM   18322 C CZ    . ARG A 1 4193 ? 204.382 152.915 184.336 1.00 63.45  ? 4193 ARG A CZ    1 
ATOM   18323 N NH1   . ARG A 1 4193 ? 205.592 152.718 184.827 1.00 63.45  ? 4193 ARG A NH1   1 
ATOM   18324 N NH2   . ARG A 1 4193 ? 203.403 153.294 185.149 1.00 63.45  ? 4193 ARG A NH2   1 
ATOM   18325 N N     . LEU A 1 4194 ? 201.147 150.689 178.096 1.00 61.43  ? 4194 LEU A N     1 
ATOM   18326 C CA    . LEU A 1 4194 ? 199.813 151.053 177.640 1.00 61.43  ? 4194 LEU A CA    1 
ATOM   18327 C C     . LEU A 1 4194 ? 198.822 149.911 177.809 1.00 61.43  ? 4194 LEU A C     1 
ATOM   18328 O O     . LEU A 1 4194 ? 197.622 150.158 177.957 1.00 61.43  ? 4194 LEU A O     1 
ATOM   18329 C CB    . LEU A 1 4194 ? 199.859 151.496 176.182 1.00 61.43  ? 4194 LEU A CB    1 
ATOM   18330 C CG    . LEU A 1 4194 ? 200.263 152.948 175.956 1.00 61.43  ? 4194 LEU A CG    1 
ATOM   18331 C CD1   . LEU A 1 4194 ? 200.429 153.216 174.479 1.00 61.43  ? 4194 LEU A CD1   1 
ATOM   18332 C CD2   . LEU A 1 4194 ? 199.226 153.870 176.543 1.00 61.43  ? 4194 LEU A CD2   1 
ATOM   18333 N N     . ARG A 1 4195 ? 199.295 148.663 177.786 1.00 66.56  ? 4195 ARG A N     1 
ATOM   18334 C CA    . ARG A 1 4195 ? 198.383 147.534 177.933 1.00 66.56  ? 4195 ARG A CA    1 
ATOM   18335 C C     . ARG A 1 4195 ? 197.671 147.576 179.277 1.00 66.56  ? 4195 ARG A C     1 
ATOM   18336 O O     . ARG A 1 4195 ? 196.469 147.305 179.361 1.00 66.56  ? 4195 ARG A O     1 
ATOM   18337 C CB    . ARG A 1 4195 ? 199.136 146.218 177.764 1.00 66.56  ? 4195 ARG A CB    1 
ATOM   18338 C CG    . ARG A 1 4195 ? 199.659 145.990 176.362 1.00 66.56  ? 4195 ARG A CG    1 
ATOM   18339 C CD    . ARG A 1 4195 ? 200.132 144.562 176.174 1.00 66.56  ? 4195 ARG A CD    1 
ATOM   18340 N NE    . ARG A 1 4195 ? 201.252 144.243 177.051 1.00 66.56  ? 4195 ARG A NE    1 
ATOM   18341 C CZ    . ARG A 1 4195 ? 201.225 143.302 177.983 1.00 66.56  ? 4195 ARG A CZ    1 
ATOM   18342 N NH1   . ARG A 1 4195 ? 200.149 142.560 178.184 1.00 66.56  ? 4195 ARG A NH1   1 
ATOM   18343 N NH2   . ARG A 1 4195 ? 202.304 143.100 178.733 1.00 66.56  ? 4195 ARG A NH2   1 
ATOM   18344 N N     . TYR A 1 4196 ? 198.397 147.914 180.341 1.00 61.60  ? 4196 TYR A N     1 
ATOM   18345 C CA    . TYR A 1 4196 ? 197.801 148.128 181.657 1.00 61.60  ? 4196 TYR A CA    1 
ATOM   18346 C C     . TYR A 1 4196 ? 197.320 149.576 181.735 1.00 61.60  ? 4196 TYR A C     1 
ATOM   18347 O O     . TYR A 1 4196 ? 197.873 150.422 182.439 1.00 61.60  ? 4196 TYR A O     1 
ATOM   18348 C CB    . TYR A 1 4196 ? 198.801 147.794 182.752 1.00 61.60  ? 4196 TYR A CB    1 
ATOM   18349 C CG    . TYR A 1 4196 ? 199.673 146.609 182.413 1.00 61.60  ? 4196 TYR A CG    1 
ATOM   18350 C CD1   . TYR A 1 4196 ? 199.279 145.322 182.732 1.00 61.60  ? 4196 TYR A CD1   1 
ATOM   18351 C CD2   . TYR A 1 4196 ? 200.886 146.777 181.768 1.00 61.60  ? 4196 TYR A CD2   1 
ATOM   18352 C CE1   . TYR A 1 4196 ? 200.068 144.238 182.421 1.00 61.60  ? 4196 TYR A CE1   1 
ATOM   18353 C CE2   . TYR A 1 4196 ? 201.679 145.698 181.452 1.00 61.60  ? 4196 TYR A CE2   1 
ATOM   18354 C CZ    . TYR A 1 4196 ? 201.267 144.432 181.781 1.00 61.60  ? 4196 TYR A CZ    1 
ATOM   18355 O OH    . TYR A 1 4196 ? 202.059 143.354 181.468 1.00 61.60  ? 4196 TYR A OH    1 
ATOM   18356 N N     . ALA A 1 4197 ? 196.265 149.852 180.972 1.00 66.50  ? 4197 ALA A N     1 
ATOM   18357 C CA    . ALA A 1 4197 ? 195.833 151.232 180.764 1.00 66.50  ? 4197 ALA A CA    1 
ATOM   18358 C C     . ALA A 1 4197 ? 195.437 151.953 182.046 1.00 66.50  ? 4197 ALA A C     1 
ATOM   18359 O O     . ALA A 1 4197 ? 195.924 153.075 182.266 1.00 66.50  ? 4197 ALA A O     1 
ATOM   18360 C CB    . ALA A 1 4197 ? 194.696 151.263 179.739 1.00 66.50  ? 4197 ALA A CB    1 
ATOM   18361 N N     . PRO A 1 4198 ? 194.576 151.408 182.919 1.00 66.54  ? 4198 PRO A N     1 
ATOM   18362 C CA    . PRO A 1 4198 ? 194.181 152.178 184.105 1.00 66.54  ? 4198 PRO A CA    1 
ATOM   18363 C C     . PRO A 1 4198 ? 195.356 152.455 185.022 1.00 66.54  ? 4198 PRO A C     1 
ATOM   18364 O O     . PRO A 1 4198 ? 195.640 153.609 185.356 1.00 66.54  ? 4198 PRO A O     1 
ATOM   18365 C CB    . PRO A 1 4198 ? 193.141 151.279 184.786 1.00 66.54  ? 4198 PRO A CB    1 
ATOM   18366 C CG    . PRO A 1 4198 ? 192.728 150.305 183.748 1.00 66.54  ? 4198 PRO A CG    1 
ATOM   18367 C CD    . PRO A 1 4198 ? 193.932 150.086 182.906 1.00 66.54  ? 4198 PRO A CD    1 
ATOM   18368 N N     . LEU A 1 4199 ? 196.053 151.400 185.423 1.00 64.28  ? 4199 LEU A N     1 
ATOM   18369 C CA    . LEU A 1 4199 ? 197.207 151.505 186.306 1.00 64.28  ? 4199 LEU A CA    1 
ATOM   18370 C C     . LEU A 1 4199 ? 198.461 151.505 185.445 1.00 64.28  ? 4199 LEU A C     1 
ATOM   18371 O O     . LEU A 1 4199 ? 198.847 150.470 184.896 1.00 64.28  ? 4199 LEU A O     1 
ATOM   18372 C CB    . LEU A 1 4199 ? 197.226 150.358 187.313 1.00 64.28  ? 4199 LEU A CB    1 
ATOM   18373 C CG    . LEU A 1 4199 ? 198.579 149.988 187.917 1.00 64.28  ? 4199 LEU A CG    1 
ATOM   18374 C CD1   . LEU A 1 4199 ? 199.088 151.095 188.818 1.00 64.28  ? 4199 LEU A CD1   1 
ATOM   18375 C CD2   . LEU A 1 4199 ? 198.484 148.676 188.668 1.00 64.28  ? 4199 LEU A CD2   1 
ATOM   18376 N N     . GLY A 1 4200 ? 199.096 152.663 185.327 1.00 64.00  ? 4200 GLY A N     1 
ATOM   18377 C CA    . GLY A 1 4200 ? 200.299 152.760 184.532 1.00 64.00  ? 4200 GLY A CA    1 
ATOM   18378 C C     . GLY A 1 4200 ? 200.283 153.912 183.555 1.00 64.00  ? 4200 GLY A C     1 
ATOM   18379 O O     . GLY A 1 4200 ? 201.320 154.529 183.304 1.00 64.00  ? 4200 GLY A O     1 
ATOM   18380 N N     . TRP A 1 4201 ? 199.116 154.212 182.989 1.00 64.32  ? 4201 TRP A N     1 
ATOM   18381 C CA    . TRP A 1 4201 ? 199.000 155.339 182.076 1.00 64.32  ? 4201 TRP A CA    1 
ATOM   18382 C C     . TRP A 1 4201 ? 197.706 156.125 182.210 1.00 64.32  ? 4201 TRP A C     1 
ATOM   18383 O O     . TRP A 1 4201 ? 197.449 156.982 181.359 1.00 64.32  ? 4201 TRP A O     1 
ATOM   18384 C CB    . TRP A 1 4201 ? 199.142 154.872 180.624 1.00 64.32  ? 4201 TRP A CB    1 
ATOM   18385 C CG    . TRP A 1 4201 ? 200.542 154.879 180.126 1.00 64.32  ? 4201 TRP A CG    1 
ATOM   18386 C CD1   . TRP A 1 4201 ? 201.196 153.848 179.532 1.00 64.32  ? 4201 TRP A CD1   1 
ATOM   18387 C CD2   . TRP A 1 4201 ? 201.465 155.973 180.160 1.00 64.32  ? 4201 TRP A CD2   1 
ATOM   18388 N NE1   . TRP A 1 4201 ? 202.471 154.225 179.198 1.00 64.32  ? 4201 TRP A NE1   1 
ATOM   18389 C CE2   . TRP A 1 4201 ? 202.660 155.526 179.574 1.00 64.32  ? 4201 TRP A CE2   1 
ATOM   18390 C CE3   . TRP A 1 4201 ? 201.398 157.283 180.631 1.00 64.32  ? 4201 TRP A CE3   1 
ATOM   18391 C CZ2   . TRP A 1 4201 ? 203.776 156.338 179.448 1.00 64.32  ? 4201 TRP A CZ2   1 
ATOM   18392 C CZ3   . TRP A 1 4201 ? 202.506 158.085 180.504 1.00 64.32  ? 4201 TRP A CZ3   1 
ATOM   18393 C CH2   . TRP A 1 4201 ? 203.678 157.613 179.916 1.00 64.32  ? 4201 TRP A CH2   1 
ATOM   18394 N N     . SER A 1 4202 ? 196.874 155.849 183.215 1.00 69.38  ? 4202 SER A N     1 
ATOM   18395 C CA    . SER A 1 4202 ? 195.641 156.597 183.436 1.00 69.38  ? 4202 SER A CA    1 
ATOM   18396 C C     . SER A 1 4202 ? 194.696 156.472 182.248 1.00 69.38  ? 4202 SER A C     1 
ATOM   18397 O O     . SER A 1 4202 ? 193.613 155.891 182.367 1.00 69.38  ? 4202 SER A O     1 
ATOM   18398 C CB    . SER A 1 4202 ? 195.946 158.068 183.722 1.00 69.38  ? 4202 SER A CB    1 
ATOM   18399 O OG    . SER A 1 4202 ? 194.806 158.870 183.484 1.00 69.38  ? 4202 SER A OG    1 
ATOM   18400 N N     . LYS A 1 4203 ? 195.089 157.021 181.106 1.00 71.92  ? 4203 LYS A N     1 
ATOM   18401 C CA    . LYS A 1 4203 ? 194.333 156.916 179.869 1.00 71.92  ? 4203 LYS A CA    1 
ATOM   18402 C C     . LYS A 1 4203 ? 195.109 156.081 178.859 1.00 71.92  ? 4203 LYS A C     1 
ATOM   18403 O O     . LYS A 1 4203 ? 196.234 155.646 179.110 1.00 71.92  ? 4203 LYS A O     1 
ATOM   18404 C CB    . LYS A 1 4203 ? 194.034 158.304 179.297 1.00 71.92  ? 4203 LYS A CB    1 
ATOM   18405 C CG    . LYS A 1 4203 ? 192.772 158.946 179.839 1.00 71.92  ? 4203 LYS A CG    1 
ATOM   18406 C CD    . LYS A 1 4203 ? 192.422 160.217 179.078 1.00 71.92  ? 4203 LYS A CD    1 
ATOM   18407 C CE    . LYS A 1 4203 ? 192.576 160.048 177.571 1.00 71.92  ? 4203 LYS A CE    1 
ATOM   18408 N NZ    . LYS A 1 4203 ? 191.841 158.863 177.041 1.00 71.92  ? 4203 LYS A NZ    1 
ATOM   18409 N N     . LYS A 1 4204 ? 194.489 155.856 177.704 1.00 70.96  ? 4204 LYS A N     1 
ATOM   18410 C CA    . LYS A 1 4204 ? 195.092 155.073 176.628 1.00 70.96  ? 4204 LYS A CA    1 
ATOM   18411 C C     . LYS A 1 4204 ? 195.627 156.043 175.581 1.00 70.96  ? 4204 LYS A C     1 
ATOM   18412 O O     . LYS A 1 4204 ? 194.894 156.526 174.721 1.00 70.96  ? 4204 LYS A O     1 
ATOM   18413 C CB    . LYS A 1 4204 ? 194.084 154.101 176.030 1.00 70.96  ? 4204 LYS A CB    1 
ATOM   18414 C CG    . LYS A 1 4204 ? 194.641 153.266 174.893 1.00 70.96  ? 4204 LYS A CG    1 
ATOM   18415 C CD    . LYS A 1 4204 ? 193.742 152.081 174.584 1.00 70.96  ? 4204 LYS A CD    1 
ATOM   18416 C CE    . LYS A 1 4204 ? 193.387 151.312 175.843 1.00 70.96  ? 4204 LYS A CE    1 
ATOM   18417 N NZ    . LYS A 1 4204 ? 194.594 150.716 176.472 1.00 70.96  ? 4204 LYS A NZ    1 
ATOM   18418 N N     . TYR A 1 4205 ? 196.921 156.326 175.660 1.00 73.35  ? 4205 TYR A N     1 
ATOM   18419 C CA    . TYR A 1 4205 ? 197.547 157.274 174.755 1.00 73.35  ? 4205 TYR A CA    1 
ATOM   18420 C C     . TYR A 1 4205 ? 197.940 156.588 173.452 1.00 73.35  ? 4205 TYR A C     1 
ATOM   18421 O O     . TYR A 1 4205 ? 197.960 155.360 173.349 1.00 73.35  ? 4205 TYR A O     1 
ATOM   18422 C CB    . TYR A 1 4205 ? 198.770 157.908 175.411 1.00 73.35  ? 4205 TYR A CB    1 
ATOM   18423 C CG    . TYR A 1 4205 ? 198.447 158.828 176.565 1.00 73.35  ? 4205 TYR A CG    1 
ATOM   18424 C CD1   . TYR A 1 4205 ? 197.162 158.919 177.070 1.00 73.35  ? 4205 TYR A CD1   1 
ATOM   18425 C CD2   . TYR A 1 4205 ? 199.434 159.592 177.159 1.00 73.35  ? 4205 TYR A CD2   1 
ATOM   18426 C CE1   . TYR A 1 4205 ? 196.869 159.750 178.118 1.00 73.35  ? 4205 TYR A CE1   1 
ATOM   18427 C CE2   . TYR A 1 4205 ? 199.147 160.426 178.211 1.00 73.35  ? 4205 TYR A CE2   1 
ATOM   18428 C CZ    . TYR A 1 4205 ? 197.863 160.500 178.687 1.00 73.35  ? 4205 TYR A CZ    1 
ATOM   18429 O OH    . TYR A 1 4205 ? 197.568 161.332 179.740 1.00 73.35  ? 4205 TYR A OH    1 
ATOM   18430 N N     . GLU A 1 4206 ? 198.252 157.402 172.444 1.00 81.66  ? 4206 GLU A N     1 
ATOM   18431 C CA    . GLU A 1 4206 ? 198.608 156.850 171.141 1.00 81.66  ? 4206 GLU A CA    1 
ATOM   18432 C C     . GLU A 1 4206 ? 200.036 156.321 171.140 1.00 81.66  ? 4206 GLU A C     1 
ATOM   18433 O O     . GLU A 1 4206 ? 200.262 155.113 171.003 1.00 81.66  ? 4206 GLU A O     1 
ATOM   18434 C CB    . GLU A 1 4206 ? 198.424 157.908 170.055 1.00 81.66  ? 4206 GLU A CB    1 
ATOM   18435 C CG    . GLU A 1 4206 ? 196.991 158.369 169.883 1.00 81.66  ? 4206 GLU A CG    1 
ATOM   18436 C CD    . GLU A 1 4206 ? 196.234 157.545 168.861 1.00 81.66  ? 4206 GLU A CD    1 
ATOM   18437 O OE1   . GLU A 1 4206 ? 196.573 156.357 168.684 1.00 81.66  ? 4206 GLU A OE1   1 
ATOM   18438 O OE2   . GLU A 1 4206 ? 195.299 158.085 168.234 1.00 81.66  ? 4206 GLU A OE2   1 
ATOM   18439 N N     . PHE A 1 4207 ? 201.013 157.211 171.309 1.00 72.84  ? 4207 PHE A N     1 
ATOM   18440 C CA    . PHE A 1 4207 ? 202.425 156.838 171.372 1.00 72.84  ? 4207 PHE A CA    1 
ATOM   18441 C C     . PHE A 1 4207 ? 202.822 155.952 170.194 1.00 72.84  ? 4207 PHE A C     1 
ATOM   18442 O O     . PHE A 1 4207 ? 203.430 154.893 170.352 1.00 72.84  ? 4207 PHE A O     1 
ATOM   18443 C CB    . PHE A 1 4207 ? 202.741 156.161 172.701 1.00 72.84  ? 4207 PHE A CB    1 
ATOM   18444 C CG    . PHE A 1 4207 ? 202.705 157.093 173.866 1.00 72.84  ? 4207 PHE A CG    1 
ATOM   18445 C CD1   . PHE A 1 4207 ? 203.039 158.421 173.709 1.00 72.84  ? 4207 PHE A CD1   1 
ATOM   18446 C CD2   . PHE A 1 4207 ? 202.319 156.649 175.113 1.00 72.84  ? 4207 PHE A CD2   1 
ATOM   18447 C CE1   . PHE A 1 4207 ? 203.005 159.284 174.775 1.00 72.84  ? 4207 PHE A CE1   1 
ATOM   18448 C CE2   . PHE A 1 4207 ? 202.282 157.512 176.185 1.00 72.84  ? 4207 PHE A CE2   1 
ATOM   18449 C CZ    . PHE A 1 4207 ? 202.625 158.830 176.014 1.00 72.84  ? 4207 PHE A CZ    1 
ATOM   18450 N N     . GLY A 1 4208 ? 202.461 156.395 168.996 1.00 85.63  ? 4208 GLY A N     1 
ATOM   18451 C CA    . GLY A 1 4208 ? 202.712 155.631 167.796 1.00 85.63  ? 4208 GLY A CA    1 
ATOM   18452 C C     . GLY A 1 4208 ? 204.132 155.794 167.293 1.00 85.63  ? 4208 GLY A C     1 
ATOM   18453 O O     . GLY A 1 4208 ? 205.009 156.351 167.953 1.00 85.63  ? 4208 GLY A O     1 
ATOM   18454 N N     . GLU A 1 4209 ? 204.352 155.285 166.080 1.00 95.53  ? 4209 GLU A N     1 
ATOM   18455 C CA    . GLU A 1 4209 ? 205.682 155.336 165.484 1.00 95.53  ? 4209 GLU A CA    1 
ATOM   18456 C C     . GLU A 1 4209 ? 206.085 156.757 165.115 1.00 95.53  ? 4209 GLU A C     1 
ATOM   18457 O O     . GLU A 1 4209 ? 207.279 157.039 164.969 1.00 95.53  ? 4209 GLU A O     1 
ATOM   18458 C CB    . GLU A 1 4209 ? 205.735 154.430 164.255 1.00 95.53  ? 4209 GLU A CB    1 
ATOM   18459 C CG    . GLU A 1 4209 ? 205.343 155.115 162.960 1.00 95.53  ? 4209 GLU A CG    1 
ATOM   18460 C CD    . GLU A 1 4209 ? 205.216 154.145 161.803 1.00 95.53  ? 4209 GLU A CD    1 
ATOM   18461 O OE1   . GLU A 1 4209 ? 204.710 154.552 160.736 1.00 95.53  ? 4209 GLU A OE1   1 
ATOM   18462 O OE2   . GLU A 1 4209 ? 205.621 152.974 161.960 1.00 95.53  ? 4209 GLU A OE2   1 
ATOM   18463 N N     . SER A 1 4210 ? 205.116 157.659 164.957 1.00 92.06  ? 4210 SER A N     1 
ATOM   18464 C CA    . SER A 1 4210 ? 205.448 159.043 164.637 1.00 92.06  ? 4210 SER A CA    1 
ATOM   18465 C C     . SER A 1 4210 ? 206.234 159.693 165.767 1.00 92.06  ? 4210 SER A C     1 
ATOM   18466 O O     . SER A 1 4210 ? 207.184 160.446 165.523 1.00 92.06  ? 4210 SER A O     1 
ATOM   18467 C CB    . SER A 1 4210 ? 204.176 159.834 164.344 1.00 92.06  ? 4210 SER A CB    1 
ATOM   18468 O OG    . SER A 1 4210 ? 204.432 161.226 164.354 1.00 92.06  ? 4210 SER A OG    1 
ATOM   18469 N N     . ASP A 1 4211 ? 205.845 159.417 167.013 1.00 88.90  ? 4211 ASP A N     1 
ATOM   18470 C CA    . ASP A 1 4211 ? 206.579 159.954 168.152 1.00 88.90  ? 4211 ASP A CA    1 
ATOM   18471 C C     . ASP A 1 4211 ? 208.006 159.430 168.182 1.00 88.90  ? 4211 ASP A C     1 
ATOM   18472 O O     . ASP A 1 4211 ? 208.946 160.187 168.442 1.00 88.90  ? 4211 ASP A O     1 
ATOM   18473 C CB    . ASP A 1 4211 ? 205.851 159.609 169.447 1.00 88.90  ? 4211 ASP A CB    1 
ATOM   18474 C CG    . ASP A 1 4211 ? 204.432 160.123 169.464 1.00 88.90  ? 4211 ASP A CG    1 
ATOM   18475 O OD1   . ASP A 1 4211 ? 204.065 160.869 168.534 1.00 88.90  ? 4211 ASP A OD1   1 
ATOM   18476 O OD2   . ASP A 1 4211 ? 203.678 159.780 170.397 1.00 88.90  ? 4211 ASP A OD2   1 
ATOM   18477 N N     . LEU A 1 4212 ? 208.188 158.136 167.915 1.00 85.70  ? 4212 LEU A N     1 
ATOM   18478 C CA    . LEU A 1 4212 ? 209.535 157.580 167.864 1.00 85.70  ? 4212 LEU A CA    1 
ATOM   18479 C C     . LEU A 1 4212 ? 210.344 158.235 166.757 1.00 85.70  ? 4212 LEU A C     1 
ATOM   18480 O O     . LEU A 1 4212 ? 211.529 158.534 166.937 1.00 85.70  ? 4212 LEU A O     1 
ATOM   18481 C CB    . LEU A 1 4212 ? 209.462 156.061 167.678 1.00 85.70  ? 4212 LEU A CB    1 
ATOM   18482 C CG    . LEU A 1 4212 ? 210.680 155.131 167.583 1.00 85.70  ? 4212 LEU A CG    1 
ATOM   18483 C CD1   . LEU A 1 4212 ? 210.188 153.699 167.590 1.00 85.70  ? 4212 LEU A CD1   1 
ATOM   18484 C CD2   . LEU A 1 4212 ? 211.523 155.339 166.337 1.00 85.70  ? 4212 LEU A CD2   1 
ATOM   18485 N N     . ARG A 1 4213 ? 209.724 158.456 165.600 1.00 94.85  ? 4213 ARG A N     1 
ATOM   18486 C CA    . ARG A 1 4213 ? 210.436 159.083 164.495 1.00 94.85  ? 4213 ARG A CA    1 
ATOM   18487 C C     . ARG A 1 4213 ? 210.875 160.494 164.858 1.00 94.85  ? 4213 ARG A C     1 
ATOM   18488 O O     . ARG A 1 4213 ? 212.020 160.885 164.598 1.00 94.85  ? 4213 ARG A O     1 
ATOM   18489 C CB    . ARG A 1 4213 ? 209.551 159.099 163.254 1.00 94.85  ? 4213 ARG A CB    1 
ATOM   18490 C CG    . ARG A 1 4213 ? 210.313 159.014 161.953 1.00 94.85  ? 4213 ARG A CG    1 
ATOM   18491 C CD    . ARG A 1 4213 ? 210.977 157.655 161.816 1.00 94.85  ? 4213 ARG A CD    1 
ATOM   18492 N NE    . ARG A 1 4213 ? 210.037 156.632 161.377 1.00 94.85  ? 4213 ARG A NE    1 
ATOM   18493 C CZ    . ARG A 1 4213 ? 209.503 156.568 160.165 1.00 94.85  ? 4213 ARG A CZ    1 
ATOM   18494 N NH1   . ARG A 1 4213 ? 209.804 157.451 159.227 1.00 94.85  ? 4213 ARG A NH1   1 
ATOM   18495 N NH2   . ARG A 1 4213 ? 208.645 155.591 159.886 1.00 94.85  ? 4213 ARG A NH2   1 
ATOM   18496 N N     . SER A 1 4214 ? 209.980 161.271 165.468 1.00 91.08  ? 4214 SER A N     1 
ATOM   18497 C CA    . SER A 1 4214 ? 210.336 162.630 165.858 1.00 91.08  ? 4214 SER A CA    1 
ATOM   18498 C C     . SER A 1 4214 ? 211.417 162.629 166.928 1.00 91.08  ? 4214 SER A C     1 
ATOM   18499 O O     . SER A 1 4214 ? 212.324 163.469 166.903 1.00 91.08  ? 4214 SER A O     1 
ATOM   18500 C CB    . SER A 1 4214 ? 209.100 163.384 166.338 1.00 91.08  ? 4214 SER A CB    1 
ATOM   18501 O OG    . SER A 1 4214 ? 208.181 163.569 165.278 1.00 91.08  ? 4214 SER A OG    1 
ATOM   18502 N N     . ALA A 1 4215 ? 211.339 161.699 167.880 1.00 86.35  ? 4215 ALA A N     1 
ATOM   18503 C CA    . ALA A 1 4215 ? 212.370 161.614 168.905 1.00 86.35  ? 4215 ALA A CA    1 
ATOM   18504 C C     . ALA A 1 4215 ? 213.723 161.272 168.297 1.00 86.35  ? 4215 ALA A C     1 
ATOM   18505 O O     . ALA A 1 4215 ? 214.749 161.842 168.684 1.00 86.35  ? 4215 ALA A O     1 
ATOM   18506 C CB    . ALA A 1 4215 ? 211.976 160.583 169.958 1.00 86.35  ? 4215 ALA A CB    1 
ATOM   18507 N N     . CYS A 1 4216 ? 213.745 160.343 167.342 1.00 87.71  ? 4216 CYS A N     1 
ATOM   18508 C CA    . CYS A 1 4216 ? 214.996 160.004 166.677 1.00 87.71  ? 4216 CYS A CA    1 
ATOM   18509 C C     . CYS A 1 4216 ? 215.549 161.194 165.909 1.00 87.71  ? 4216 CYS A C     1 
ATOM   18510 O O     . CYS A 1 4216 ? 216.761 161.441 165.923 1.00 87.71  ? 4216 CYS A O     1 
ATOM   18511 C CB    . CYS A 1 4216 ? 214.789 158.814 165.746 1.00 87.71  ? 4216 CYS A CB    1 
ATOM   18512 S SG    . CYS A 1 4216 ? 214.435 157.273 166.601 1.00 87.71  ? 4216 CYS A SG    1 
ATOM   18513 N N     . ASP A 1 4217 ? 214.679 161.943 165.230 1.00 91.54  ? 4217 ASP A N     1 
ATOM   18514 C CA    . ASP A 1 4217 ? 215.142 163.131 164.520 1.00 91.54  ? 4217 ASP A CA    1 
ATOM   18515 C C     . ASP A 1 4217 ? 215.725 164.153 165.485 1.00 91.54  ? 4217 ASP A C     1 
ATOM   18516 O O     . ASP A 1 4217 ? 216.761 164.767 165.202 1.00 91.54  ? 4217 ASP A O     1 
ATOM   18517 C CB    . ASP A 1 4217 ? 213.999 163.746 163.715 1.00 91.54  ? 4217 ASP A CB    1 
ATOM   18518 C CG    . ASP A 1 4217 ? 213.607 162.900 162.524 1.00 91.54  ? 4217 ASP A CG    1 
ATOM   18519 O OD1   . ASP A 1 4217 ? 214.203 161.818 162.343 1.00 91.54  ? 4217 ASP A OD1   1 
ATOM   18520 O OD2   . ASP A 1 4217 ? 212.706 163.317 161.767 1.00 91.54  ? 4217 ASP A OD2   1 
ATOM   18521 N N     . THR A 1 4218 ? 215.069 164.354 166.628 1.00 84.41  ? 4218 THR A N     1 
ATOM   18522 C CA    . THR A 1 4218 ? 215.586 165.283 167.624 1.00 84.41  ? 4218 THR A CA    1 
ATOM   18523 C C     . THR A 1 4218 ? 216.948 164.837 168.136 1.00 84.41  ? 4218 THR A C     1 
ATOM   18524 O O     . THR A 1 4218 ? 217.873 165.652 168.263 1.00 84.41  ? 4218 THR A O     1 
ATOM   18525 C CB    . THR A 1 4218 ? 214.593 165.411 168.777 1.00 84.41  ? 4218 THR A CB    1 
ATOM   18526 O OG1   . THR A 1 4218 ? 213.516 166.269 168.384 1.00 84.41  ? 4218 THR A OG1   1 
ATOM   18527 C CG2   . THR A 1 4218 ? 215.266 165.980 170.008 1.00 84.41  ? 4218 THR A CG2   1 
ATOM   18528 N N     . VAL A 1 4219 ? 217.092 163.542 168.422 1.00 81.97  ? 4219 VAL A N     1 
ATOM   18529 C CA    . VAL A 1 4219 ? 218.371 163.023 168.897 1.00 81.97  ? 4219 VAL A CA    1 
ATOM   18530 C C     . VAL A 1 4219 ? 219.451 163.256 167.851 1.00 81.97  ? 4219 VAL A C     1 
ATOM   18531 O O     . VAL A 1 4219 ? 220.559 163.702 168.168 1.00 81.97  ? 4219 VAL A O     1 
ATOM   18532 C CB    . VAL A 1 4219 ? 218.248 161.531 169.253 1.00 81.97  ? 4219 VAL A CB    1 
ATOM   18533 C CG1   . VAL A 1 4219 ? 219.620 160.892 169.330 1.00 81.97  ? 4219 VAL A CG1   1 
ATOM   18534 C CG2   . VAL A 1 4219 ? 217.515 161.358 170.563 1.00 81.97  ? 4219 VAL A CG2   1 
ATOM   18535 N N     . ASP A 1 4220 ? 219.140 162.968 166.587 1.00 85.51  ? 4220 ASP A N     1 
ATOM   18536 C CA    . ASP A 1 4220 ? 220.119 163.154 165.524 1.00 85.51  ? 4220 ASP A CA    1 
ATOM   18537 C C     . ASP A 1 4220 ? 220.545 164.611 165.423 1.00 85.51  ? 4220 ASP A C     1 
ATOM   18538 O O     . ASP A 1 4220 ? 221.743 164.920 165.373 1.00 85.51  ? 4220 ASP A O     1 
ATOM   18539 C CB    . ASP A 1 4220 ? 219.542 162.676 164.193 1.00 85.51  ? 4220 ASP A CB    1 
ATOM   18540 C CG    . ASP A 1 4220 ? 219.739 161.195 163.972 1.00 85.51  ? 4220 ASP A CG    1 
ATOM   18541 O OD1   . ASP A 1 4220 ? 220.799 160.671 164.368 1.00 85.51  ? 4220 ASP A OD1   1 
ATOM   18542 O OD2   . ASP A 1 4220 ? 218.836 160.552 163.399 1.00 85.51  ? 4220 ASP A OD2   1 
ATOM   18543 N N     . THR A 1 4221 ? 219.573 165.525 165.404 1.00 85.93  ? 4221 THR A N     1 
ATOM   18544 C CA    . THR A 1 4221 ? 219.900 166.936 165.243 1.00 85.93  ? 4221 THR A CA    1 
ATOM   18545 C C     . THR A 1 4221 ? 220.746 167.437 166.400 1.00 85.93  ? 4221 THR A C     1 
ATOM   18546 O O     . THR A 1 4221 ? 221.749 168.129 166.191 1.00 85.93  ? 4221 THR A O     1 
ATOM   18547 C CB    . THR A 1 4221 ? 218.627 167.768 165.121 1.00 85.93  ? 4221 THR A CB    1 
ATOM   18548 O OG1   . THR A 1 4221 ? 217.735 167.431 166.189 1.00 85.93  ? 4221 THR A OG1   1 
ATOM   18549 C CG2   . THR A 1 4221 ? 217.945 167.506 163.789 1.00 85.93  ? 4221 THR A CG2   1 
ATOM   18550 N N     . TRP A 1 4222 ? 220.380 167.078 167.630 1.00 80.98  ? 4222 TRP A N     1 
ATOM   18551 C CA    . TRP A 1 4222 ? 221.122 167.602 168.770 1.00 80.98  ? 4222 TRP A CA    1 
ATOM   18552 C C     . TRP A 1 4222 ? 222.498 166.961 168.897 1.00 80.98  ? 4222 TRP A C     1 
ATOM   18553 O O     . TRP A 1 4222 ? 223.455 167.633 169.302 1.00 80.98  ? 4222 TRP A O     1 
ATOM   18554 C CB    . TRP A 1 4222 ? 220.304 167.427 170.042 1.00 80.98  ? 4222 TRP A CB    1 
ATOM   18555 C CG    . TRP A 1 4222 ? 219.240 168.457 170.128 1.00 80.98  ? 4222 TRP A CG    1 
ATOM   18556 C CD1   . TRP A 1 4222 ? 217.936 168.316 169.778 1.00 80.98  ? 4222 TRP A CD1   1 
ATOM   18557 C CD2   . TRP A 1 4222 ? 219.394 169.808 170.567 1.00 80.98  ? 4222 TRP A CD2   1 
ATOM   18558 N NE1   . TRP A 1 4222 ? 217.261 169.492 169.983 1.00 80.98  ? 4222 TRP A NE1   1 
ATOM   18559 C CE2   . TRP A 1 4222 ? 218.136 170.425 170.469 1.00 80.98  ? 4222 TRP A CE2   1 
ATOM   18560 C CE3   . TRP A 1 4222 ? 220.474 170.554 171.042 1.00 80.98  ? 4222 TRP A CE3   1 
ATOM   18561 C CZ2   . TRP A 1 4222 ? 217.927 171.750 170.826 1.00 80.98  ? 4222 TRP A CZ2   1 
ATOM   18562 C CZ3   . TRP A 1 4222 ? 220.264 171.870 171.396 1.00 80.98  ? 4222 TRP A CZ3   1 
ATOM   18563 C CH2   . TRP A 1 4222 ? 219.002 172.454 171.287 1.00 80.98  ? 4222 TRP A CH2   1 
ATOM   18564 N N     . LEU A 1 4223 ? 222.628 165.681 168.545 1.00 87.98  ? 4223 LEU A N     1 
ATOM   18565 C CA    . LEU A 1 4223 ? 223.946 165.062 168.528 1.00 87.98  ? 4223 LEU A CA    1 
ATOM   18566 C C     . LEU A 1 4223 ? 224.846 165.721 167.496 1.00 87.98  ? 4223 LEU A C     1 
ATOM   18567 O O     . LEU A 1 4223 ? 226.024 165.982 167.766 1.00 87.98  ? 4223 LEU A O     1 
ATOM   18568 C CB    . LEU A 1 4223 ? 223.817 163.568 168.251 1.00 87.98  ? 4223 LEU A CB    1 
ATOM   18569 C CG    . LEU A 1 4223 ? 223.644 162.694 169.489 1.00 87.98  ? 4223 LEU A CG    1 
ATOM   18570 C CD1   . LEU A 1 4223 ? 223.837 161.240 169.127 1.00 87.98  ? 4223 LEU A CD1   1 
ATOM   18571 C CD2   . LEU A 1 4223 ? 224.639 163.108 170.546 1.00 87.98  ? 4223 LEU A CD2   1 
ATOM   18572 N N     . ASP A 1 4224 ? 224.310 166.008 166.309 1.00 90.43  ? 4224 ASP A N     1 
ATOM   18573 C CA    . ASP A 1 4224 ? 225.104 166.710 165.310 1.00 90.43  ? 4224 ASP A CA    1 
ATOM   18574 C C     . ASP A 1 4224 ? 225.464 168.111 165.786 1.00 90.43  ? 4224 ASP A C     1 
ATOM   18575 O O     . ASP A 1 4224 ? 226.555 168.615 165.494 1.00 90.43  ? 4224 ASP A O     1 
ATOM   18576 C CB    . ASP A 1 4224 ? 224.353 166.768 163.980 1.00 90.43  ? 4224 ASP A CB    1 
ATOM   18577 C CG    . ASP A 1 4224 ? 224.408 165.455 163.218 1.00 90.43  ? 4224 ASP A CG    1 
ATOM   18578 O OD1   . ASP A 1 4224 ? 225.486 164.828 163.183 1.00 90.43  ? 4224 ASP A OD1   1 
ATOM   18579 O OD2   . ASP A 1 4224 ? 223.374 165.052 162.646 1.00 90.43  ? 4224 ASP A OD2   1 
ATOM   18580 N N     . ASP A 1 4225 ? 224.559 168.755 166.523 1.00 93.27  ? 4225 ASP A N     1 
ATOM   18581 C CA    . ASP A 1 4225 ? 224.817 170.110 166.994 1.00 93.27  ? 4225 ASP A CA    1 
ATOM   18582 C C     . ASP A 1 4225 ? 225.954 170.120 168.010 1.00 93.27  ? 4225 ASP A C     1 
ATOM   18583 O O     . ASP A 1 4225 ? 226.914 170.885 167.871 1.00 93.27  ? 4225 ASP A O     1 
ATOM   18584 C CB    . ASP A 1 4225 ? 223.521 170.691 167.578 1.00 93.27  ? 4225 ASP A CB    1 
ATOM   18585 C CG    . ASP A 1 4225 ? 223.697 172.057 168.253 1.00 93.27  ? 4225 ASP A CG    1 
ATOM   18586 O OD1   . ASP A 1 4225 ? 222.675 172.766 168.363 1.00 93.27  ? 4225 ASP A OD1   1 
ATOM   18587 O OD2   . ASP A 1 4225 ? 224.805 172.449 168.669 1.00 93.27  ? 4225 ASP A OD2   1 
ATOM   18588 N N     . THR A 1 4226 ? 225.871 169.270 169.036 1.00 92.60  ? 4226 THR A N     1 
ATOM   18589 C CA    . THR A 1 4226 ? 226.869 169.326 170.102 1.00 92.60  ? 4226 THR A CA    1 
ATOM   18590 C C     . THR A 1 4226 ? 228.206 168.753 169.650 1.00 92.60  ? 4226 THR A C     1 
ATOM   18591 O O     . THR A 1 4226 ? 229.259 169.347 169.910 1.00 92.60  ? 4226 THR A O     1 
ATOM   18592 C CB    . THR A 1 4226 ? 226.366 168.595 171.345 1.00 92.60  ? 4226 THR A CB    1 
ATOM   18593 O OG1   . THR A 1 4226 ? 225.283 169.333 171.922 1.00 92.60  ? 4226 THR A OG1   1 
ATOM   18594 C CG2   . THR A 1 4226 ? 227.479 168.465 172.374 1.00 92.60  ? 4226 THR A CG2   1 
ATOM   18595 N N     . ALA A 1 4227 ? 228.190 167.612 168.972 1.00 94.59  ? 4227 ALA A N     1 
ATOM   18596 C CA    . ALA A 1 4227 ? 229.408 166.950 168.514 1.00 94.59  ? 4227 ALA A CA    1 
ATOM   18597 C C     . ALA A 1 4227 ? 229.584 167.264 167.031 1.00 94.59  ? 4227 ALA A C     1 
ATOM   18598 O O     . ALA A 1 4227 ? 229.054 166.567 166.165 1.00 94.59  ? 4227 ALA A O     1 
ATOM   18599 C CB    . ALA A 1 4227 ? 229.344 165.452 168.770 1.00 94.59  ? 4227 ALA A CB    1 
ATOM   18600 N N     . LYS A 1 4228 ? 230.338 168.328 166.747 1.00 99.90  ? 4228 LYS A N     1 
ATOM   18601 C CA    . LYS A 1 4228 ? 230.559 168.730 165.362 1.00 99.90  ? 4228 LYS A CA    1 
ATOM   18602 C C     . LYS A 1 4228 ? 231.333 167.666 164.597 1.00 99.90  ? 4228 LYS A C     1 
ATOM   18603 O O     . LYS A 1 4228 ? 230.993 167.341 163.453 1.00 99.90  ? 4228 LYS A O     1 
ATOM   18604 C CB    . LYS A 1 4228 ? 231.303 170.063 165.316 1.00 99.90  ? 4228 LYS A CB    1 
ATOM   18605 C CG    . LYS A 1 4228 ? 231.128 170.923 166.559 1.00 99.90  ? 4228 LYS A CG    1 
ATOM   18606 C CD    . LYS A 1 4228 ? 229.757 171.575 166.612 1.00 99.90  ? 4228 LYS A CD    1 
ATOM   18607 C CE    . LYS A 1 4228 ? 229.574 172.585 165.494 1.00 99.90  ? 4228 LYS A CE    1 
ATOM   18608 N NZ    . LYS A 1 4228 ? 228.139 172.923 165.290 1.00 99.90  ? 4228 LYS A NZ    1 
ATOM   18609 N N     . GLY A 1 4229 ? 232.375 167.108 165.213 1.00 99.65  ? 4229 GLY A N     1 
ATOM   18610 C CA    . GLY A 1 4229 ? 233.196 166.122 164.549 1.00 99.65  ? 4229 GLY A CA    1 
ATOM   18611 C C     . GLY A 1 4229 ? 232.754 164.698 164.823 1.00 99.65  ? 4229 GLY A C     1 
ATOM   18612 O O     . GLY A 1 4229 ? 231.944 164.433 165.706 1.00 99.65  ? 4229 GLY A O     1 
ATOM   18613 N N     . ARG A 1 4230 ? 233.313 163.774 164.042 1.00 101.65 ? 4230 ARG A N     1 
ATOM   18614 C CA    . ARG A 1 4230 ? 232.979 162.363 164.188 1.00 101.65 ? 4230 ARG A CA    1 
ATOM   18615 C C     . ARG A 1 4230 ? 233.496 161.775 165.495 1.00 101.65 ? 4230 ARG A C     1 
ATOM   18616 O O     . ARG A 1 4230 ? 232.982 160.744 165.942 1.00 101.65 ? 4230 ARG A O     1 
ATOM   18617 C CB    . ARG A 1 4230 ? 233.539 161.574 163.003 1.00 101.65 ? 4230 ARG A CB    1 
ATOM   18618 C CG    . ARG A 1 4230 ? 233.122 160.112 162.954 1.00 101.65 ? 4230 ARG A CG    1 
ATOM   18619 C CD    . ARG A 1 4230 ? 234.334 159.197 162.882 1.00 101.65 ? 4230 ARG A CD    1 
ATOM   18620 N NE    . ARG A 1 4230 ? 235.157 159.258 164.085 1.00 101.65 ? 4230 ARG A NE    1 
ATOM   18621 C CZ    . ARG A 1 4230 ? 234.871 158.639 165.222 1.00 101.65 ? 4230 ARG A CZ    1 
ATOM   18622 N NH1   . ARG A 1 4230 ? 233.778 157.907 165.355 1.00 101.65 ? 4230 ARG A NH1   1 
ATOM   18623 N NH2   . ARG A 1 4230 ? 235.702 158.759 166.252 1.00 101.65 ? 4230 ARG A NH2   1 
ATOM   18624 N N     . GLN A 1 4231 ? 234.472 162.422 166.126 1.00 98.94  ? 4231 GLN A N     1 
ATOM   18625 C CA    . GLN A 1 4231 ? 235.121 161.860 167.303 1.00 98.94  ? 4231 GLN A CA    1 
ATOM   18626 C C     . GLN A 1 4231 ? 234.106 161.554 168.397 1.00 98.94  ? 4231 GLN A C     1 
ATOM   18627 O O     . GLN A 1 4231 ? 233.094 162.242 168.551 1.00 98.94  ? 4231 GLN A O     1 
ATOM   18628 C CB    . GLN A 1 4231 ? 236.191 162.822 167.824 1.00 98.94  ? 4231 GLN A CB    1 
ATOM   18629 C CG    . GLN A 1 4231 ? 235.647 164.065 168.511 1.00 98.94  ? 4231 GLN A CG    1 
ATOM   18630 C CD    . GLN A 1 4231 ? 235.040 165.054 167.536 1.00 98.94  ? 4231 GLN A CD    1 
ATOM   18631 O OE1   . GLN A 1 4231 ? 235.697 165.499 166.596 1.00 98.94  ? 4231 GLN A OE1   1 
ATOM   18632 N NE2   . GLN A 1 4231 ? 233.778 165.401 167.753 1.00 98.94  ? 4231 GLN A NE2   1 
ATOM   18633 N N     . ASN A 1 4232 ? 234.374 160.482 169.139 1.00 103.18 ? 4232 ASN A N     1 
ATOM   18634 C CA    . ASN A 1 4232 ? 233.499 160.082 170.232 1.00 103.18 ? 4232 ASN A CA    1 
ATOM   18635 C C     . ASN A 1 4232 ? 233.371 161.211 171.243 1.00 103.18 ? 4232 ASN A C     1 
ATOM   18636 O O     . ASN A 1 4232 ? 234.365 161.832 171.629 1.00 103.18 ? 4232 ASN A O     1 
ATOM   18637 C CB    . ASN A 1 4232 ? 234.044 158.828 170.910 1.00 103.18 ? 4232 ASN A CB    1 
ATOM   18638 C CG    . ASN A 1 4232 ? 235.543 158.878 171.097 1.00 103.18 ? 4232 ASN A CG    1 
ATOM   18639 O OD1   . ASN A 1 4232 ? 236.300 158.902 170.127 1.00 103.18 ? 4232 ASN A OD1   1 
ATOM   18640 N ND2   . ASN A 1 4232 ? 235.981 158.908 172.349 1.00 103.18 ? 4232 ASN A ND2   1 
ATOM   18641 N N     . ILE A 1 4233 ? 232.150 161.473 171.669 1.00 94.41  ? 4233 ILE A N     1 
ATOM   18642 C CA    . ILE A 1 4233 ? 231.849 162.624 172.506 1.00 94.41  ? 4233 ILE A CA    1 
ATOM   18643 C C     . ILE A 1 4233 ? 231.801 162.161 173.955 1.00 94.41  ? 4233 ILE A C     1 
ATOM   18644 O O     . ILE A 1 4233 ? 231.300 161.071 174.253 1.00 94.41  ? 4233 ILE A O     1 
ATOM   18645 C CB    . ILE A 1 4233 ? 230.521 163.268 172.068 1.00 94.41  ? 4233 ILE A CB    1 
ATOM   18646 C CG1   . ILE A 1 4233 ? 230.010 164.245 173.118 1.00 94.41  ? 4233 ILE A CG1   1 
ATOM   18647 C CG2   . ILE A 1 4233 ? 229.480 162.201 171.812 1.00 94.41  ? 4233 ILE A CG2   1 
ATOM   18648 C CD1   . ILE A 1 4233 ? 230.964 165.390 173.349 1.00 94.41  ? 4233 ILE A CD1   1 
ATOM   18649 N N     . SER A 1 4234 ? 232.331 162.982 174.859 1.00 93.39  ? 4234 SER A N     1 
ATOM   18650 C CA    . SER A 1 4234 ? 232.394 162.609 176.262 1.00 93.39  ? 4234 SER A CA    1 
ATOM   18651 C C     . SER A 1 4234 ? 230.990 162.394 176.824 1.00 93.39  ? 4234 SER A C     1 
ATOM   18652 O O     . SER A 1 4234 ? 230.044 163.089 176.443 1.00 93.39  ? 4234 SER A O     1 
ATOM   18653 C CB    . SER A 1 4234 ? 233.117 163.682 177.071 1.00 93.39  ? 4234 SER A CB    1 
ATOM   18654 O OG    . SER A 1 4234 ? 234.447 163.854 176.617 1.00 93.39  ? 4234 SER A OG    1 
ATOM   18655 N N     . PRO A 1 4235 ? 230.830 161.434 177.734 1.00 95.11  ? 4235 PRO A N     1 
ATOM   18656 C CA    . PRO A 1 4235 ? 229.489 161.126 178.252 1.00 95.11  ? 4235 PRO A CA    1 
ATOM   18657 C C     . PRO A 1 4235 ? 228.837 162.271 179.003 1.00 95.11  ? 4235 PRO A C     1 
ATOM   18658 O O     . PRO A 1 4235 ? 227.619 162.236 179.210 1.00 95.11  ? 4235 PRO A O     1 
ATOM   18659 C CB    . PRO A 1 4235 ? 229.737 159.926 179.175 1.00 95.11  ? 4235 PRO A CB    1 
ATOM   18660 C CG    . PRO A 1 4235 ? 231.025 159.343 178.709 1.00 95.11  ? 4235 PRO A CG    1 
ATOM   18661 C CD    . PRO A 1 4235 ? 231.846 160.499 178.237 1.00 95.11  ? 4235 PRO A CD    1 
ATOM   18662 N N     . ASP A 1 4236 ? 229.593 163.268 179.443 1.00 91.25  ? 4236 ASP A N     1 
ATOM   18663 C CA    . ASP A 1 4236 ? 229.013 164.381 180.181 1.00 91.25  ? 4236 ASP A CA    1 
ATOM   18664 C C     . ASP A 1 4236 ? 228.742 165.601 179.312 1.00 91.25  ? 4236 ASP A C     1 
ATOM   18665 O O     . ASP A 1 4236 ? 228.370 166.649 179.846 1.00 91.25  ? 4236 ASP A O     1 
ATOM   18666 C CB    . ASP A 1 4236 ? 229.924 164.770 181.347 1.00 91.25  ? 4236 ASP A CB    1 
ATOM   18667 C CG    . ASP A 1 4236 ? 231.316 165.147 180.895 1.00 91.25  ? 4236 ASP A CG    1 
ATOM   18668 O OD1   . ASP A 1 4236 ? 231.635 164.924 179.709 1.00 91.25  ? 4236 ASP A OD1   1 
ATOM   18669 O OD2   . ASP A 1 4236 ? 232.092 165.665 181.724 1.00 91.25  ? 4236 ASP A OD2   1 
ATOM   18670 N N     . LYS A 1 4237 ? 228.919 165.499 177.997 1.00 89.66  ? 4237 LYS A N     1 
ATOM   18671 C CA    . LYS A 1 4237 ? 228.761 166.649 177.119 1.00 89.66  ? 4237 LYS A CA    1 
ATOM   18672 C C     . LYS A 1 4237 ? 227.577 166.540 176.168 1.00 89.66  ? 4237 LYS A C     1 
ATOM   18673 O O     . LYS A 1 4237 ? 227.256 167.526 175.499 1.00 89.66  ? 4237 LYS A O     1 
ATOM   18674 C CB    . LYS A 1 4237 ? 230.040 166.872 176.308 1.00 89.66  ? 4237 LYS A CB    1 
ATOM   18675 C CG    . LYS A 1 4237 ? 231.078 167.733 176.996 1.00 89.66  ? 4237 LYS A CG    1 
ATOM   18676 C CD    . LYS A 1 4237 ? 230.465 169.013 177.529 1.00 89.66  ? 4237 LYS A CD    1 
ATOM   18677 C CE    . LYS A 1 4237 ? 231.517 169.895 178.180 1.00 89.66  ? 4237 LYS A CE    1 
ATOM   18678 N NZ    . LYS A 1 4237 ? 232.770 169.951 177.378 1.00 89.66  ? 4237 LYS A NZ    1 
ATOM   18679 N N     . ILE A 1 4238 ? 226.935 165.379 176.072 1.00 86.49  ? 4238 ILE A N     1 
ATOM   18680 C CA    . ILE A 1 4238 ? 225.705 165.316 175.274 1.00 86.49  ? 4238 ILE A CA    1 
ATOM   18681 C C     . ILE A 1 4238 ? 224.645 166.185 175.933 1.00 86.49  ? 4238 ILE A C     1 
ATOM   18682 O O     . ILE A 1 4238 ? 224.517 166.169 177.175 1.00 86.49  ? 4238 ILE A O     1 
ATOM   18683 C CB    . ILE A 1 4238 ? 225.209 163.866 175.120 1.00 86.49  ? 4238 ILE A CB    1 
ATOM   18684 C CG1   . ILE A 1 4238 ? 226.361 162.881 174.925 1.00 86.49  ? 4238 ILE A CG1   1 
ATOM   18685 C CG2   . ILE A 1 4238 ? 224.224 163.744 173.980 1.00 86.49  ? 4238 ILE A CG2   1 
ATOM   18686 C CD1   . ILE A 1 4238 ? 226.891 162.297 176.190 1.00 86.49  ? 4238 ILE A CD1   1 
ATOM   18687 N N     . PRO A 1 4239 ? 223.862 166.952 175.182 1.00 82.45  ? 4239 PRO A N     1 
ATOM   18688 C CA    . PRO A 1 4239 ? 222.873 167.829 175.817 1.00 82.45  ? 4239 PRO A CA    1 
ATOM   18689 C C     . PRO A 1 4239 ? 221.736 167.053 176.458 1.00 82.45  ? 4239 PRO A C     1 
ATOM   18690 O O     . PRO A 1 4239 ? 220.635 166.978 175.904 1.00 82.45  ? 4239 PRO A O     1 
ATOM   18691 C CB    . PRO A 1 4239 ? 222.378 168.695 174.653 1.00 82.45  ? 4239 PRO A CB    1 
ATOM   18692 C CG    . PRO A 1 4239 ? 222.647 167.882 173.440 1.00 82.45  ? 4239 PRO A CG    1 
ATOM   18693 C CD    . PRO A 1 4239 ? 223.916 167.150 173.725 1.00 82.45  ? 4239 PRO A CD    1 
ATOM   18694 N N     . TRP A 1 4240 ? 221.996 166.472 177.631 1.00 78.64  ? 4240 TRP A N     1 
ATOM   18695 C CA    . TRP A 1 4240 ? 220.973 165.687 178.310 1.00 78.64  ? 4240 TRP A CA    1 
ATOM   18696 C C     . TRP A 1 4240 ? 219.755 166.536 178.633 1.00 78.64  ? 4240 TRP A C     1 
ATOM   18697 O O     . TRP A 1 4240 ? 218.614 166.082 178.490 1.00 78.64  ? 4240 TRP A O     1 
ATOM   18698 C CB    . TRP A 1 4240 ? 221.540 165.075 179.587 1.00 78.64  ? 4240 TRP A CB    1 
ATOM   18699 C CG    . TRP A 1 4240 ? 222.577 164.051 179.334 1.00 78.64  ? 4240 TRP A CG    1 
ATOM   18700 C CD1   . TRP A 1 4240 ? 223.897 164.128 179.650 1.00 78.64  ? 4240 TRP A CD1   1 
ATOM   18701 C CD2   . TRP A 1 4240 ? 222.390 162.790 178.691 1.00 78.64  ? 4240 TRP A CD2   1 
ATOM   18702 N NE1   . TRP A 1 4240 ? 224.545 162.987 179.253 1.00 78.64  ? 4240 TRP A NE1   1 
ATOM   18703 C CE2   . TRP A 1 4240 ? 223.639 162.150 178.660 1.00 78.64  ? 4240 TRP A CE2   1 
ATOM   18704 C CE3   . TRP A 1 4240 ? 221.285 162.138 178.143 1.00 78.64  ? 4240 TRP A CE3   1 
ATOM   18705 C CZ2   . TRP A 1 4240 ? 223.816 160.893 178.102 1.00 78.64  ? 4240 TRP A CZ2   1 
ATOM   18706 C CZ3   . TRP A 1 4240 ? 221.461 160.892 177.591 1.00 78.64  ? 4240 TRP A CZ3   1 
ATOM   18707 C CH2   . TRP A 1 4240 ? 222.716 160.281 177.575 1.00 78.64  ? 4240 TRP A CH2   1 
ATOM   18708 N N     . SER A 1 4241 ? 219.977 167.771 179.077 1.00 76.77  ? 4241 SER A N     1 
ATOM   18709 C CA    . SER A 1 4241 ? 218.860 168.652 179.384 1.00 76.77  ? 4241 SER A CA    1 
ATOM   18710 C C     . SER A 1 4241 ? 218.008 168.901 178.149 1.00 76.77  ? 4241 SER A C     1 
ATOM   18711 O O     . SER A 1 4241 ? 216.774 168.886 178.225 1.00 76.77  ? 4241 SER A O     1 
ATOM   18712 C CB    . SER A 1 4241 ? 219.381 169.968 179.952 1.00 76.77  ? 4241 SER A CB    1 
ATOM   18713 O OG    . SER A 1 4241 ? 220.476 170.440 179.187 1.00 76.77  ? 4241 SER A OG    1 
ATOM   18714 N N     . ALA A 1 4242 ? 218.649 169.125 177.002 1.00 72.34  ? 4242 ALA A N     1 
ATOM   18715 C CA    . ALA A 1 4242 ? 217.905 169.378 175.773 1.00 72.34  ? 4242 ALA A CA    1 
ATOM   18716 C C     . ALA A 1 4242 ? 217.038 168.185 175.403 1.00 72.34  ? 4242 ALA A C     1 
ATOM   18717 O O     . ALA A 1 4242 ? 215.853 168.339 175.086 1.00 72.34  ? 4242 ALA A O     1 
ATOM   18718 C CB    . ALA A 1 4242 ? 218.868 169.709 174.636 1.00 72.34  ? 4242 ALA A CB    1 
ATOM   18719 N N     . LEU A 1 4243 ? 217.611 166.983 175.444 1.00 67.11  ? 4243 LEU A N     1 
ATOM   18720 C CA    . LEU A 1 4243 ? 216.847 165.794 175.089 1.00 67.11  ? 4243 LEU A CA    1 
ATOM   18721 C C     . LEU A 1 4243 ? 215.694 165.569 176.054 1.00 67.11  ? 4243 LEU A C     1 
ATOM   18722 O O     . LEU A 1 4243 ? 214.569 165.272 175.631 1.00 67.11  ? 4243 LEU A O     1 
ATOM   18723 C CB    . LEU A 1 4243 ? 217.764 164.577 175.062 1.00 67.11  ? 4243 LEU A CB    1 
ATOM   18724 C CG    . LEU A 1 4243 ? 218.155 164.147 173.656 1.00 67.11  ? 4243 LEU A CG    1 
ATOM   18725 C CD1   . LEU A 1 4243 ? 218.914 162.843 173.694 1.00 67.11  ? 4243 LEU A CD1   1 
ATOM   18726 C CD2   . LEU A 1 4243 ? 216.907 164.025 172.807 1.00 67.11  ? 4243 LEU A CD2   1 
ATOM   18727 N N     . LYS A 1 4244 ? 215.952 165.705 177.354 1.00 68.89  ? 4244 LYS A N     1 
ATOM   18728 C CA    . LYS A 1 4244 ? 214.900 165.490 178.338 1.00 68.89  ? 4244 LYS A CA    1 
ATOM   18729 C C     . LYS A 1 4244 ? 213.763 166.481 178.144 1.00 68.89  ? 4244 LYS A C     1 
ATOM   18730 O O     . LYS A 1 4244 ? 212.589 166.097 178.116 1.00 68.89  ? 4244 LYS A O     1 
ATOM   18731 C CB    . LYS A 1 4244 ? 215.475 165.594 179.748 1.00 68.89  ? 4244 LYS A CB    1 
ATOM   18732 C CG    . LYS A 1 4244 ? 216.269 164.380 180.175 1.00 68.89  ? 4244 LYS A CG    1 
ATOM   18733 C CD    . LYS A 1 4244 ? 216.506 164.382 181.667 1.00 68.89  ? 4244 LYS A CD    1 
ATOM   18734 C CE    . LYS A 1 4244 ? 217.333 165.582 182.075 1.00 68.89  ? 4244 LYS A CE    1 
ATOM   18735 N NZ    . LYS A 1 4244 ? 218.706 165.509 181.513 1.00 68.89  ? 4244 LYS A NZ    1 
ATOM   18736 N N     . THR A 1 4245 ? 214.092 167.764 177.990 1.00 68.13  ? 4245 THR A N     1 
ATOM   18737 C CA    . THR A 1 4245 ? 213.048 168.765 177.821 1.00 68.13  ? 4245 THR A CA    1 
ATOM   18738 C C     . THR A 1 4245 ? 212.272 168.540 176.534 1.00 68.13  ? 4245 THR A C     1 
ATOM   18739 O O     . THR A 1 4245 ? 211.042 168.655 176.515 1.00 68.13  ? 4245 THR A O     1 
ATOM   18740 C CB    . THR A 1 4245 ? 213.652 170.165 177.840 1.00 68.13  ? 4245 THR A CB    1 
ATOM   18741 O OG1   . THR A 1 4245 ? 214.398 170.345 179.049 1.00 68.13  ? 4245 THR A OG1   1 
ATOM   18742 C CG2   . THR A 1 4245 ? 212.560 171.212 177.768 1.00 68.13  ? 4245 THR A CG2   1 
ATOM   18743 N N     . LEU A 1 4246 ? 212.969 168.207 175.447 1.00 67.93  ? 4246 LEU A N     1 
ATOM   18744 C CA    . LEU A 1 4246 ? 212.285 168.007 174.177 1.00 67.93  ? 4246 LEU A CA    1 
ATOM   18745 C C     . LEU A 1 4246 ? 211.339 166.818 174.239 1.00 67.93  ? 4246 LEU A C     1 
ATOM   18746 O O     . LEU A 1 4246 ? 210.200 166.899 173.766 1.00 67.93  ? 4246 LEU A O     1 
ATOM   18747 C CB    . LEU A 1 4246 ? 213.303 167.823 173.057 1.00 67.93  ? 4246 LEU A CB    1 
ATOM   18748 C CG    . LEU A 1 4246 ? 213.522 169.065 172.203 1.00 67.93  ? 4246 LEU A CG    1 
ATOM   18749 C CD1   . LEU A 1 4246 ? 212.223 169.445 171.542 1.00 67.93  ? 4246 LEU A CD1   1 
ATOM   18750 C CD2   . LEU A 1 4246 ? 214.037 170.205 173.047 1.00 67.93  ? 4246 LEU A CD2   1 
ATOM   18751 N N     . MET A 1 4247 ? 211.781 165.708 174.827 1.00 69.69  ? 4247 MET A N     1 
ATOM   18752 C CA    . MET A 1 4247 ? 210.934 164.525 174.870 1.00 69.69  ? 4247 MET A CA    1 
ATOM   18753 C C     . MET A 1 4247 ? 209.905 164.571 175.988 1.00 69.69  ? 4247 MET A C     1 
ATOM   18754 O O     . MET A 1 4247 ? 209.005 163.727 176.009 1.00 69.69  ? 4247 MET A O     1 
ATOM   18755 C CB    . MET A 1 4247 ? 211.792 163.269 175.003 1.00 69.69  ? 4247 MET A CB    1 
ATOM   18756 C CG    . MET A 1 4247 ? 212.832 163.137 173.912 1.00 69.69  ? 4247 MET A CG    1 
ATOM   18757 S SD    . MET A 1 4247 ? 212.981 161.458 173.293 1.00 69.69  ? 4247 MET A SD    1 
ATOM   18758 C CE    . MET A 1 4247 ? 212.818 160.540 174.816 1.00 69.69  ? 4247 MET A CE    1 
ATOM   18759 N N     . ALA A 1 4248 ? 210.006 165.522 176.912 1.00 64.54  ? 4248 ALA A N     1 
ATOM   18760 C CA    . ALA A 1 4248 ? 208.986 165.658 177.944 1.00 64.54  ? 4248 ALA A CA    1 
ATOM   18761 C C     . ALA A 1 4248 ? 207.930 166.686 177.555 1.00 64.54  ? 4248 ALA A C     1 
ATOM   18762 O O     . ALA A 1 4248 ? 206.741 166.366 177.487 1.00 64.54  ? 4248 ALA A O     1 
ATOM   18763 C CB    . ALA A 1 4248 ? 209.636 166.037 179.277 1.00 64.54  ? 4248 ALA A CB    1 
ATOM   18764 N N     . GLN A 1 4249 ? 208.349 167.927 177.309 1.00 69.72  ? 4249 GLN A N     1 
ATOM   18765 C CA    . GLN A 1 4249 ? 207.392 168.976 176.979 1.00 69.72  ? 4249 GLN A CA    1 
ATOM   18766 C C     . GLN A 1 4249 ? 206.721 168.709 175.639 1.00 69.72  ? 4249 GLN A C     1 
ATOM   18767 O O     . GLN A 1 4249 ? 205.499 168.838 175.509 1.00 69.72  ? 4249 GLN A O     1 
ATOM   18768 C CB    . GLN A 1 4249 ? 208.089 170.334 176.973 1.00 69.72  ? 4249 GLN A CB    1 
ATOM   18769 C CG    . GLN A 1 4249 ? 208.866 170.625 178.236 1.00 69.72  ? 4249 GLN A CG    1 
ATOM   18770 C CD    . GLN A 1 4249 ? 208.045 170.382 179.483 1.00 69.72  ? 4249 GLN A CD    1 
ATOM   18771 O OE1   . GLN A 1 4249 ? 206.926 170.878 179.609 1.00 69.72  ? 4249 GLN A OE1   1 
ATOM   18772 N NE2   . GLN A 1 4249 ? 208.595 169.613 180.414 1.00 69.72  ? 4249 GLN A NE2   1 
ATOM   18773 N N     . SER A 1 4250 ? 207.498 168.333 174.636 1.00 69.84  ? 4250 SER A N     1 
ATOM   18774 C CA    . SER A 1 4250 ? 206.993 168.078 173.300 1.00 69.84  ? 4250 SER A CA    1 
ATOM   18775 C C     . SER A 1 4250 ? 207.182 166.605 172.951 1.00 69.84  ? 4250 SER A C     1 
ATOM   18776 O O     . SER A 1 4250 ? 207.574 165.792 173.795 1.00 69.84  ? 4250 SER A O     1 
ATOM   18777 C CB    . SER A 1 4250 ? 207.686 168.991 172.293 1.00 69.84  ? 4250 SER A CB    1 
ATOM   18778 O OG    . SER A 1 4250 ? 207.484 168.518 170.976 1.00 69.84  ? 4250 SER A OG    1 
ATOM   18779 N N     . ILE A 1 4251 ? 206.903 166.265 171.692 1.00 72.13  ? 4251 ILE A N     1 
ATOM   18780 C CA    . ILE A 1 4251 ? 207.009 164.898 171.186 1.00 72.13  ? 4251 ILE A CA    1 
ATOM   18781 C C     . ILE A 1 4251 ? 206.162 163.960 172.034 1.00 72.13  ? 4251 ILE A C     1 
ATOM   18782 O O     . ILE A 1 4251 ? 204.933 163.934 171.909 1.00 72.13  ? 4251 ILE A O     1 
ATOM   18783 C CB    . ILE A 1 4251 ? 208.469 164.412 171.132 1.00 72.13  ? 4251 ILE A CB    1 
ATOM   18784 C CG1   . ILE A 1 4251 ? 209.422 165.564 170.831 1.00 72.13  ? 4251 ILE A CG1   1 
ATOM   18785 C CG2   . ILE A 1 4251 ? 208.628 163.328 170.090 1.00 72.13  ? 4251 ILE A CG2   1 
ATOM   18786 C CD1   . ILE A 1 4251 ? 210.860 165.232 171.114 1.00 72.13  ? 4251 ILE A CD1   1 
ATOM   18787 N N     . TYR A 1 4252 ? 206.817 163.182 172.898 1.00 64.95  ? 4252 TYR A N     1 
ATOM   18788 C CA    . TYR A 1 4252 ? 206.102 162.182 173.683 1.00 64.95  ? 4252 TYR A CA    1 
ATOM   18789 C C     . TYR A 1 4252 ? 205.095 162.823 174.625 1.00 64.95  ? 4252 TYR A C     1 
ATOM   18790 O O     . TYR A 1 4252 ? 203.967 162.340 174.759 1.00 64.95  ? 4252 TYR A O     1 
ATOM   18791 C CB    . TYR A 1 4252 ? 207.093 161.325 174.463 1.00 64.95  ? 4252 TYR A CB    1 
ATOM   18792 C CG    . TYR A 1 4252 ? 207.604 160.151 173.676 1.00 64.95  ? 4252 TYR A CG    1 
ATOM   18793 C CD1   . TYR A 1 4252 ? 206.728 159.274 173.067 1.00 64.95  ? 4252 TYR A CD1   1 
ATOM   18794 C CD2   . TYR A 1 4252 ? 208.959 159.928 173.529 1.00 64.95  ? 4252 TYR A CD2   1 
ATOM   18795 C CE1   . TYR A 1 4252 ? 207.185 158.204 172.344 1.00 64.95  ? 4252 TYR A CE1   1 
ATOM   18796 C CE2   . TYR A 1 4252 ? 209.426 158.859 172.807 1.00 64.95  ? 4252 TYR A CE2   1 
ATOM   18797 C CZ    . TYR A 1 4252 ? 208.533 158.001 172.215 1.00 64.95  ? 4252 TYR A CZ    1 
ATOM   18798 O OH    . TYR A 1 4252 ? 208.988 156.929 171.489 1.00 64.95  ? 4252 TYR A OH    1 
ATOM   18799 N N     . GLY A 1 4253 ? 205.476 163.907 175.281 1.00 66.46  ? 4253 GLY A N     1 
ATOM   18800 C CA    . GLY A 1 4253 ? 204.570 164.523 176.221 1.00 66.46  ? 4253 GLY A CA    1 
ATOM   18801 C C     . GLY A 1 4253 ? 203.504 165.397 175.616 1.00 66.46  ? 4253 GLY A C     1 
ATOM   18802 O O     . GLY A 1 4253 ? 202.658 165.920 176.346 1.00 66.46  ? 4253 GLY A O     1 
ATOM   18803 N N     . GLY A 1 4254 ? 203.517 165.574 174.296 1.00 73.69  ? 4254 GLY A N     1 
ATOM   18804 C CA    . GLY A 1 4254 ? 202.528 166.434 173.671 1.00 73.69  ? 4254 GLY A CA    1 
ATOM   18805 C C     . GLY A 1 4254 ? 201.110 165.941 173.879 1.00 73.69  ? 4254 GLY A C     1 
ATOM   18806 O O     . GLY A 1 4254 ? 200.218 166.718 174.223 1.00 73.69  ? 4254 GLY A O     1 
ATOM   18807 N N     . ARG A 1 4255 ? 200.885 164.644 173.687 1.00 75.94  ? 4255 ARG A N     1 
ATOM   18808 C CA    . ARG A 1 4255 ? 199.557 164.084 173.884 1.00 75.94  ? 4255 ARG A CA    1 
ATOM   18809 C C     . ARG A 1 4255 ? 199.211 163.892 175.352 1.00 75.94  ? 4255 ARG A C     1 
ATOM   18810 O O     . ARG A 1 4255 ? 198.051 163.612 175.667 1.00 75.94  ? 4255 ARG A O     1 
ATOM   18811 C CB    . ARG A 1 4255 ? 199.435 162.753 173.146 1.00 75.94  ? 4255 ARG A CB    1 
ATOM   18812 C CG    . ARG A 1 4255 ? 200.761 162.087 172.878 1.00 75.94  ? 4255 ARG A CG    1 
ATOM   18813 C CD    . ARG A 1 4255 ? 200.570 160.790 172.127 1.00 75.94  ? 4255 ARG A CD    1 
ATOM   18814 N NE    . ARG A 1 4255 ? 199.881 160.992 170.861 1.00 75.94  ? 4255 ARG A NE    1 
ATOM   18815 C CZ    . ARG A 1 4255 ? 200.471 161.407 169.749 1.00 75.94  ? 4255 ARG A CZ    1 
ATOM   18816 N NH1   . ARG A 1 4255 ? 201.764 161.678 169.715 1.00 75.94  ? 4255 ARG A NH1   1 
ATOM   18817 N NH2   . ARG A 1 4255 ? 199.746 161.549 168.644 1.00 75.94  ? 4255 ARG A NH2   1 
ATOM   18818 N N     . VAL A 1 4256 ? 200.178 164.037 176.254 1.00 75.15  ? 4256 VAL A N     1 
ATOM   18819 C CA    . VAL A 1 4256 ? 199.898 163.898 177.675 1.00 75.15  ? 4256 VAL A CA    1 
ATOM   18820 C C     . VAL A 1 4256 ? 199.107 165.108 178.145 1.00 75.15  ? 4256 VAL A C     1 
ATOM   18821 O O     . VAL A 1 4256 ? 199.486 166.256 177.881 1.00 75.15  ? 4256 VAL A O     1 
ATOM   18822 C CB    . VAL A 1 4256 ? 201.202 163.746 178.466 1.00 75.15  ? 4256 VAL A CB    1 
ATOM   18823 C CG1   . VAL A 1 4256 ? 200.919 163.735 179.956 1.00 75.15  ? 4256 VAL A CG1   1 
ATOM   18824 C CG2   . VAL A 1 4256 ? 201.934 162.488 178.044 1.00 75.15  ? 4256 VAL A CG2   1 
ATOM   18825 N N     . ASP A 1 4257 ? 198.000 164.862 178.840 1.00 85.07  ? 4257 ASP A N     1 
ATOM   18826 C CA    . ASP A 1 4257 ? 197.147 165.938 179.324 1.00 85.07  ? 4257 ASP A CA    1 
ATOM   18827 C C     . ASP A 1 4257 ? 197.155 166.077 180.838 1.00 85.07  ? 4257 ASP A C     1 
ATOM   18828 O O     . ASP A 1 4257 ? 197.462 167.156 181.353 1.00 85.07  ? 4257 ASP A O     1 
ATOM   18829 C CB    . ASP A 1 4257 ? 195.712 165.736 178.817 1.00 85.07  ? 4257 ASP A CB    1 
ATOM   18830 C CG    . ASP A 1 4257 ? 195.173 164.354 179.114 1.00 85.07  ? 4257 ASP A CG    1 
ATOM   18831 O OD1   . ASP A 1 4257 ? 195.713 163.679 180.014 1.00 85.07  ? 4257 ASP A OD1   1 
ATOM   18832 O OD2   . ASP A 1 4257 ? 194.206 163.939 178.441 1.00 85.07  ? 4257 ASP A OD2   1 
ATOM   18833 N N     . ASN A 1 4258 ? 196.829 165.019 181.573 1.00 78.16  ? 4258 ASN A N     1 
ATOM   18834 C CA    . ASN A 1 4258 ? 196.813 165.112 183.024 1.00 78.16  ? 4258 ASN A CA    1 
ATOM   18835 C C     . ASN A 1 4258 ? 198.231 165.268 183.557 1.00 78.16  ? 4258 ASN A C     1 
ATOM   18836 O O     . ASN A 1 4258 ? 199.189 164.721 183.009 1.00 78.16  ? 4258 ASN A O     1 
ATOM   18837 C CB    . ASN A 1 4258 ? 196.155 163.880 183.634 1.00 78.16  ? 4258 ASN A CB    1 
ATOM   18838 C CG    . ASN A 1 4258 ? 196.628 162.603 182.995 1.00 78.16  ? 4258 ASN A CG    1 
ATOM   18839 O OD1   . ASN A 1 4258 ? 197.370 162.630 182.016 1.00 78.16  ? 4258 ASN A OD1   1 
ATOM   18840 N ND2   . ASN A 1 4258 ? 196.203 161.472 183.543 1.00 78.16  ? 4258 ASN A ND2   1 
ATOM   18841 N N     . GLU A 1 4259 ? 198.354 166.028 184.644 1.00 77.12  ? 4259 GLU A N     1 
ATOM   18842 C CA    . GLU A 1 4259 ? 199.673 166.378 185.154 1.00 77.12  ? 4259 GLU A CA    1 
ATOM   18843 C C     . GLU A 1 4259 ? 200.422 165.163 185.680 1.00 77.12  ? 4259 GLU A C     1 
ATOM   18844 O O     . GLU A 1 4259 ? 201.654 165.126 185.616 1.00 77.12  ? 4259 GLU A O     1 
ATOM   18845 C CB    . GLU A 1 4259 ? 199.541 167.438 186.246 1.00 77.12  ? 4259 GLU A CB    1 
ATOM   18846 C CG    . GLU A 1 4259 ? 200.829 168.179 186.566 1.00 77.12  ? 4259 GLU A CG    1 
ATOM   18847 C CD    . GLU A 1 4259 ? 201.723 167.429 187.532 1.00 77.12  ? 4259 GLU A CD    1 
ATOM   18848 O OE1   . GLU A 1 4259 ? 202.924 167.758 187.613 1.00 77.12  ? 4259 GLU A OE1   1 
ATOM   18849 O OE2   . GLU A 1 4259 ? 201.223 166.513 188.215 1.00 77.12  ? 4259 GLU A OE2   1 
ATOM   18850 N N     . PHE A 1 4260 ? 199.710 164.166 186.203 1.00 72.95  ? 4260 PHE A N     1 
ATOM   18851 C CA    . PHE A 1 4260 ? 200.390 163.045 186.843 1.00 72.95  ? 4260 PHE A CA    1 
ATOM   18852 C C     . PHE A 1 4260 ? 201.060 162.136 185.822 1.00 72.95  ? 4260 PHE A C     1 
ATOM   18853 O O     . PHE A 1 4260 ? 202.154 161.613 186.071 1.00 72.95  ? 4260 PHE A O     1 
ATOM   18854 C CB    . PHE A 1 4260 ? 199.404 162.279 187.714 1.00 72.95  ? 4260 PHE A CB    1 
ATOM   18855 C CG    . PHE A 1 4260 ? 198.870 163.092 188.847 1.00 72.95  ? 4260 PHE A CG    1 
ATOM   18856 C CD1   . PHE A 1 4260 ? 199.563 163.174 190.039 1.00 72.95  ? 4260 PHE A CD1   1 
ATOM   18857 C CD2   . PHE A 1 4260 ? 197.701 163.813 188.709 1.00 72.95  ? 4260 PHE A CD2   1 
ATOM   18858 C CE1   . PHE A 1 4260 ? 199.083 163.936 191.082 1.00 72.95  ? 4260 PHE A CE1   1 
ATOM   18859 C CE2   . PHE A 1 4260 ? 197.218 164.578 189.749 1.00 72.95  ? 4260 PHE A CE2   1 
ATOM   18860 C CZ    . PHE A 1 4260 ? 197.910 164.640 190.935 1.00 72.95  ? 4260 PHE A CZ    1 
ATOM   18861 N N     . ASP A 1 4261 ? 200.432 161.940 184.663 1.00 74.14  ? 4261 ASP A N     1 
ATOM   18862 C CA    . ASP A 1 4261 ? 201.110 161.217 183.595 1.00 74.14  ? 4261 ASP A CA    1 
ATOM   18863 C C     . ASP A 1 4261 ? 202.355 161.967 183.145 1.00 74.14  ? 4261 ASP A C     1 
ATOM   18864 O O     . ASP A 1 4261 ? 203.384 161.354 182.843 1.00 74.14  ? 4261 ASP A O     1 
ATOM   18865 C CB    . ASP A 1 4261 ? 200.158 160.986 182.426 1.00 74.14  ? 4261 ASP A CB    1 
ATOM   18866 C CG    . ASP A 1 4261 ? 199.001 160.088 182.795 1.00 74.14  ? 4261 ASP A CG    1 
ATOM   18867 O OD1   . ASP A 1 4261 ? 199.018 159.534 183.912 1.00 74.14  ? 4261 ASP A OD1   1 
ATOM   18868 O OD2   . ASP A 1 4261 ? 198.077 159.929 181.971 1.00 74.14  ? 4261 ASP A OD2   1 
ATOM   18869 N N     . GLN A 1 4262 ? 202.284 163.297 183.109 1.00 71.11  ? 4262 GLN A N     1 
ATOM   18870 C CA    . GLN A 1 4262 ? 203.466 164.089 182.794 1.00 71.11  ? 4262 GLN A CA    1 
ATOM   18871 C C     . GLN A 1 4262 ? 204.555 163.885 183.838 1.00 71.11  ? 4262 GLN A C     1 
ATOM   18872 O O     . GLN A 1 4262 ? 205.741 163.798 183.501 1.00 71.11  ? 4262 GLN A O     1 
ATOM   18873 C CB    . GLN A 1 4262 ? 203.091 165.564 182.693 1.00 71.11  ? 4262 GLN A CB    1 
ATOM   18874 C CG    . GLN A 1 4262 ? 204.254 166.462 182.366 1.00 71.11  ? 4262 GLN A CG    1 
ATOM   18875 C CD    . GLN A 1 4262 ? 204.707 166.297 180.941 1.00 71.11  ? 4262 GLN A CD    1 
ATOM   18876 O OE1   . GLN A 1 4262 ? 203.938 166.511 180.007 1.00 71.11  ? 4262 GLN A OE1   1 
ATOM   18877 N NE2   . GLN A 1 4262 ? 205.960 165.905 180.761 1.00 71.11  ? 4262 GLN A NE2   1 
ATOM   18878 N N     . ARG A 1 4263 ? 204.170 163.817 185.114 1.00 70.94  ? 4263 ARG A N     1 
ATOM   18879 C CA    . ARG A 1 4263 ? 205.142 163.563 186.171 1.00 70.94  ? 4263 ARG A CA    1 
ATOM   18880 C C     . ARG A 1 4263 ? 205.810 162.212 185.983 1.00 70.94  ? 4263 ARG A C     1 
ATOM   18881 O O     . ARG A 1 4263 ? 207.030 162.083 186.134 1.00 70.94  ? 4263 ARG A O     1 
ATOM   18882 C CB    . ARG A 1 4263 ? 204.461 163.626 187.533 1.00 70.94  ? 4263 ARG A CB    1 
ATOM   18883 C CG    . ARG A 1 4263 ? 205.367 164.058 188.663 1.00 70.94  ? 4263 ARG A CG    1 
ATOM   18884 C CD    . ARG A 1 4263 ? 204.632 163.986 189.991 1.00 70.94  ? 4263 ARG A CD    1 
ATOM   18885 N NE    . ARG A 1 4263 ? 203.762 162.818 190.059 1.00 70.94  ? 4263 ARG A NE    1 
ATOM   18886 C CZ    . ARG A 1 4263 ? 202.886 162.591 191.028 1.00 70.94  ? 4263 ARG A CZ    1 
ATOM   18887 N NH1   . ARG A 1 4263 ? 202.725 163.441 192.027 1.00 70.94  ? 4263 ARG A NH1   1 
ATOM   18888 N NH2   . ARG A 1 4263 ? 202.157 161.481 190.994 1.00 70.94  ? 4263 ARG A NH2   1 
ATOM   18889 N N     . LEU A 1 4264 ? 205.022 161.192 185.650 1.00 65.07  ? 4264 LEU A N     1 
ATOM   18890 C CA    . LEU A 1 4264 ? 205.593 159.868 185.434 1.00 65.07  ? 4264 LEU A CA    1 
ATOM   18891 C C     . LEU A 1 4264 ? 206.539 159.871 184.240 1.00 65.07  ? 4264 LEU A C     1 
ATOM   18892 O O     . LEU A 1 4264 ? 207.606 159.247 184.278 1.00 65.07  ? 4264 LEU A O     1 
ATOM   18893 C CB    . LEU A 1 4264 ? 204.469 158.848 185.251 1.00 65.07  ? 4264 LEU A CB    1 
ATOM   18894 C CG    . LEU A 1 4264 ? 204.722 157.456 184.674 1.00 65.07  ? 4264 LEU A CG    1 
ATOM   18895 C CD1   . LEU A 1 4264 ? 203.605 156.551 185.133 1.00 65.07  ? 4264 LEU A CD1   1 
ATOM   18896 C CD2   . LEU A 1 4264 ? 204.769 157.452 183.164 1.00 65.07  ? 4264 LEU A CD2   1 
ATOM   18897 N N     . LEU A 1 4265 ? 206.156 160.561 183.166 1.00 64.49  ? 4265 LEU A N     1 
ATOM   18898 C CA    . LEU A 1 4265 ? 207.007 160.629 181.983 1.00 64.49  ? 4265 LEU A CA    1 
ATOM   18899 C C     . LEU A 1 4265 ? 208.320 161.330 182.292 1.00 64.49  ? 4265 LEU A C     1 
ATOM   18900 O O     . LEU A 1 4265 ? 209.390 160.886 181.859 1.00 64.49  ? 4265 LEU A O     1 
ATOM   18901 C CB    . LEU A 1 4265 ? 206.267 161.342 180.857 1.00 64.49  ? 4265 LEU A CB    1 
ATOM   18902 C CG    . LEU A 1 4265 ? 206.791 161.103 179.451 1.00 64.49  ? 4265 LEU A CG    1 
ATOM   18903 C CD1   . LEU A 1 4265 ? 206.464 159.700 179.022 1.00 64.49  ? 4265 LEU A CD1   1 
ATOM   18904 C CD2   . LEU A 1 4265 ? 206.160 162.094 178.508 1.00 64.49  ? 4265 LEU A CD2   1 
ATOM   18905 N N     . ASN A 1 4266 ? 208.257 162.429 183.041 1.00 69.58  ? 4266 ASN A N     1 
ATOM   18906 C CA    . ASN A 1 4266 ? 209.479 163.110 183.445 1.00 69.58  ? 4266 ASN A CA    1 
ATOM   18907 C C     . ASN A 1 4266 ? 210.344 162.207 184.308 1.00 69.58  ? 4266 ASN A C     1 
ATOM   18908 O O     . ASN A 1 4266 ? 211.571 162.201 184.174 1.00 69.58  ? 4266 ASN A O     1 
ATOM   18909 C CB    . ASN A 1 4266 ? 209.143 164.400 184.187 1.00 69.58  ? 4266 ASN A CB    1 
ATOM   18910 C CG    . ASN A 1 4266 ? 208.940 165.568 183.254 1.00 69.58  ? 4266 ASN A CG    1 
ATOM   18911 O OD1   . ASN A 1 4266 ? 207.844 166.118 183.159 1.00 69.58  ? 4266 ASN A OD1   1 
ATOM   18912 N ND2   . ASN A 1 4266 ? 210.000 165.958 182.559 1.00 69.58  ? 4266 ASN A ND2   1 
ATOM   18913 N N     . THR A 1 4267 ? 209.723 161.440 185.206 1.00 72.07  ? 4267 THR A N     1 
ATOM   18914 C CA    . THR A 1 4267 ? 210.491 160.518 186.034 1.00 72.07  ? 4267 THR A CA    1 
ATOM   18915 C C     . THR A 1 4267 ? 211.213 159.487 185.180 1.00 72.07  ? 4267 THR A C     1 
ATOM   18916 O O     . THR A 1 4267 ? 212.402 159.217 185.389 1.00 72.07  ? 4267 THR A O     1 
ATOM   18917 C CB    . THR A 1 4267 ? 209.575 159.827 187.040 1.00 72.07  ? 4267 THR A CB    1 
ATOM   18918 O OG1   . THR A 1 4267 ? 209.098 160.785 187.991 1.00 72.07  ? 4267 THR A OG1   1 
ATOM   18919 C CG2   . THR A 1 4267 ? 210.325 158.731 187.769 1.00 72.07  ? 4267 THR A CG2   1 
ATOM   18920 N N     . PHE A 1 4268 ? 210.513 158.912 184.201 1.00 69.52  ? 4268 PHE A N     1 
ATOM   18921 C CA    . PHE A 1 4268 ? 211.146 157.935 183.321 1.00 69.52  ? 4268 PHE A CA    1 
ATOM   18922 C C     . PHE A 1 4268 ? 212.308 158.557 182.564 1.00 69.52  ? 4268 PHE A C     1 
ATOM   18923 O O     . PHE A 1 4268 ? 213.396 157.973 182.478 1.00 69.52  ? 4268 PHE A O     1 
ATOM   18924 C CB    . PHE A 1 4268 ? 210.129 157.363 182.338 1.00 69.52  ? 4268 PHE A CB    1 
ATOM   18925 C CG    . PHE A 1 4268 ? 209.541 156.063 182.770 1.00 69.52  ? 4268 PHE A CG    1 
ATOM   18926 C CD1   . PHE A 1 4268 ? 210.350 154.968 182.986 1.00 69.52  ? 4268 PHE A CD1   1 
ATOM   18927 C CD2   . PHE A 1 4268 ? 208.180 155.931 182.949 1.00 69.52  ? 4268 PHE A CD2   1 
ATOM   18928 C CE1   . PHE A 1 4268 ? 209.815 153.767 183.386 1.00 69.52  ? 4268 PHE A CE1   1 
ATOM   18929 C CE2   . PHE A 1 4268 ? 207.638 154.732 183.347 1.00 69.52  ? 4268 PHE A CE2   1 
ATOM   18930 C CZ    . PHE A 1 4268 ? 208.456 153.649 183.565 1.00 69.52  ? 4268 PHE A CZ    1 
ATOM   18931 N N     . LEU A 1 4269 ? 212.096 159.750 182.010 1.00 66.60  ? 4269 LEU A N     1 
ATOM   18932 C CA    . LEU A 1 4269 ? 213.147 160.386 181.227 1.00 66.60  ? 4269 LEU A CA    1 
ATOM   18933 C C     . LEU A 1 4269 ? 214.364 160.694 182.086 1.00 66.60  ? 4269 LEU A C     1 
ATOM   18934 O O     . LEU A 1 4269 ? 215.502 160.455 181.670 1.00 66.60  ? 4269 LEU A O     1 
ATOM   18935 C CB    . LEU A 1 4269 ? 212.611 161.654 180.570 1.00 66.60  ? 4269 LEU A CB    1 
ATOM   18936 C CG    . LEU A 1 4269 ? 211.738 161.394 179.347 1.00 66.60  ? 4269 LEU A CG    1 
ATOM   18937 C CD1   . LEU A 1 4269 ? 211.463 162.678 178.591 1.00 66.60  ? 4269 LEU A CD1   1 
ATOM   18938 C CD2   . LEU A 1 4269 ? 212.407 160.378 178.450 1.00 66.60  ? 4269 LEU A CD2   1 
ATOM   18939 N N     . GLU A 1 4270 ? 214.145 161.211 183.295 1.00 75.17  ? 4270 GLU A N     1 
ATOM   18940 C CA    . GLU A 1 4270 ? 215.269 161.543 184.159 1.00 75.17  ? 4270 GLU A CA    1 
ATOM   18941 C C     . GLU A 1 4270 ? 216.001 160.298 184.629 1.00 75.17  ? 4270 GLU A C     1 
ATOM   18942 O O     . GLU A 1 4270 ? 217.223 160.332 184.806 1.00 75.17  ? 4270 GLU A O     1 
ATOM   18943 C CB    . GLU A 1 4270 ? 214.791 162.363 185.354 1.00 75.17  ? 4270 GLU A CB    1 
ATOM   18944 C CG    . GLU A 1 4270 ? 214.186 163.699 184.971 1.00 75.17  ? 4270 GLU A CG    1 
ATOM   18945 C CD    . GLU A 1 4270 ? 214.201 164.693 186.109 1.00 75.17  ? 4270 GLU A CD    1 
ATOM   18946 O OE1   . GLU A 1 4270 ? 213.934 164.285 187.257 1.00 75.17  ? 4270 GLU A OE1   1 
ATOM   18947 O OE2   . GLU A 1 4270 ? 214.478 165.884 185.856 1.00 75.17  ? 4270 GLU A OE2   1 
ATOM   18948 N N     . ARG A 1 4271 ? 215.284 159.194 184.843 1.00 76.75  ? 4271 ARG A N     1 
ATOM   18949 C CA    . ARG A 1 4271 ? 215.961 157.969 185.250 1.00 76.75  ? 4271 ARG A CA    1 
ATOM   18950 C C     . ARG A 1 4271 ? 216.779 157.387 184.108 1.00 76.75  ? 4271 ARG A C     1 
ATOM   18951 O O     . ARG A 1 4271 ? 217.902 156.917 184.320 1.00 76.75  ? 4271 ARG A O     1 
ATOM   18952 C CB    . ARG A 1 4271 ? 214.950 156.944 185.760 1.00 76.75  ? 4271 ARG A CB    1 
ATOM   18953 C CG    . ARG A 1 4271 ? 215.582 155.812 186.552 1.00 76.75  ? 4271 ARG A CG    1 
ATOM   18954 C CD    . ARG A 1 4271 ? 214.544 154.823 187.050 1.00 76.75  ? 4271 ARG A CD    1 
ATOM   18955 N NE    . ARG A 1 4271 ? 214.260 153.787 186.065 1.00 76.75  ? 4271 ARG A NE    1 
ATOM   18956 C CZ    . ARG A 1 4271 ? 213.069 153.233 185.884 1.00 76.75  ? 4271 ARG A CZ    1 
ATOM   18957 N NH1   . ARG A 1 4271 ? 212.023 153.594 186.608 1.00 76.75  ? 4271 ARG A NH1   1 
ATOM   18958 N NH2   . ARG A 1 4271 ? 212.924 152.295 184.954 1.00 76.75  ? 4271 ARG A NH2   1 
ATOM   18959 N N     . LEU A 1 4272 ? 216.241 157.410 182.889 1.00 73.24  ? 4272 LEU A N     1 
ATOM   18960 C CA    . LEU A 1 4272 ? 216.954 156.805 181.770 1.00 73.24  ? 4272 LEU A CA    1 
ATOM   18961 C C     . LEU A 1 4272 ? 217.997 157.753 181.187 1.00 73.24  ? 4272 LEU A C     1 
ATOM   18962 O O     . LEU A 1 4272 ? 219.199 157.474 181.233 1.00 73.24  ? 4272 LEU A O     1 
ATOM   18963 C CB    . LEU A 1 4272 ? 215.964 156.369 180.691 1.00 73.24  ? 4272 LEU A CB    1 
ATOM   18964 C CG    . LEU A 1 4272 ? 215.165 155.110 181.014 1.00 73.24  ? 4272 LEU A CG    1 
ATOM   18965 C CD1   . LEU A 1 4272 ? 214.119 154.859 179.951 1.00 73.24  ? 4272 LEU A CD1   1 
ATOM   18966 C CD2   . LEU A 1 4272 ? 216.095 153.927 181.133 1.00 73.24  ? 4272 LEU A CD2   1 
ATOM   18967 N N     . PHE A 1 4273 ? 217.557 158.886 180.649 1.00 72.81  ? 4273 PHE A N     1 
ATOM   18968 C CA    . PHE A 1 4273 ? 218.441 159.782 179.906 1.00 72.81  ? 4273 PHE A CA    1 
ATOM   18969 C C     . PHE A 1 4273 ? 219.286 160.583 180.885 1.00 72.81  ? 4273 PHE A C     1 
ATOM   18970 O O     . PHE A 1 4273 ? 218.878 161.631 181.384 1.00 72.81  ? 4273 PHE A O     1 
ATOM   18971 C CB    . PHE A 1 4273 ? 217.633 160.699 179.001 1.00 72.81  ? 4273 PHE A CB    1 
ATOM   18972 C CG    . PHE A 1 4273 ? 217.137 160.034 177.762 1.00 72.81  ? 4273 PHE A CG    1 
ATOM   18973 C CD1   . PHE A 1 4273 ? 216.012 159.238 177.796 1.00 72.81  ? 4273 PHE A CD1   1 
ATOM   18974 C CD2   . PHE A 1 4273 ? 217.792 160.206 176.561 1.00 72.81  ? 4273 PHE A CD2   1 
ATOM   18975 C CE1   . PHE A 1 4273 ? 215.551 158.625 176.657 1.00 72.81  ? 4273 PHE A CE1   1 
ATOM   18976 C CE2   . PHE A 1 4273 ? 217.334 159.595 175.419 1.00 72.81  ? 4273 PHE A CE2   1 
ATOM   18977 C CZ    . PHE A 1 4273 ? 216.212 158.803 175.467 1.00 72.81  ? 4273 PHE A CZ    1 
ATOM   18978 N N     . THR A 1 4274 ? 220.489 160.088 181.152 1.00 81.46  ? 4274 THR A N     1 
ATOM   18979 C CA    . THR A 1 4274 ? 221.430 160.802 181.998 1.00 81.46  ? 4274 THR A CA    1 
ATOM   18980 C C     . THR A 1 4274 ? 222.840 160.362 181.638 1.00 81.46  ? 4274 THR A C     1 
ATOM   18981 O O     . THR A 1 4274 ? 223.045 159.323 181.008 1.00 81.46  ? 4274 THR A O     1 
ATOM   18982 C CB    . THR A 1 4274 ? 221.149 160.563 183.484 1.00 81.46  ? 4274 THR A CB    1 
ATOM   18983 O OG1   . THR A 1 4274 ? 221.763 161.598 184.261 1.00 81.46  ? 4274 THR A OG1   1 
ATOM   18984 C CG2   . THR A 1 4274 ? 221.694 159.219 183.920 1.00 81.46  ? 4274 THR A CG2   1 
ATOM   18985 N N     . THR A 1 4275 ? 223.817 161.174 182.045 1.00 83.49  ? 4275 THR A N     1 
ATOM   18986 C CA    . THR A 1 4275 ? 225.207 160.851 181.754 1.00 83.49  ? 4275 THR A CA    1 
ATOM   18987 C C     . THR A 1 4275 ? 225.653 159.566 182.432 1.00 83.49  ? 4275 THR A C     1 
ATOM   18988 O O     . THR A 1 4275 ? 226.572 158.906 181.937 1.00 83.49  ? 4275 THR A O     1 
ATOM   18989 C CB    . THR A 1 4275 ? 226.117 161.997 182.182 1.00 83.49  ? 4275 THR A CB    1 
ATOM   18990 O OG1   . THR A 1 4275 ? 227.480 161.561 182.139 1.00 83.49  ? 4275 THR A OG1   1 
ATOM   18991 C CG2   . THR A 1 4275 ? 225.777 162.446 183.592 1.00 83.49  ? 4275 THR A CG2   1 
ATOM   18992 N N     . ARG A 1 4276 ? 225.025 159.192 183.548 1.00 90.12  ? 4276 ARG A N     1 
ATOM   18993 C CA    . ARG A 1 4276 ? 225.377 157.948 184.218 1.00 90.12  ? 4276 ARG A CA    1 
ATOM   18994 C C     . ARG A 1 4276 ? 225.055 156.727 183.371 1.00 90.12  ? 4276 ARG A C     1 
ATOM   18995 O O     . ARG A 1 4276 ? 225.602 155.650 183.627 1.00 90.12  ? 4276 ARG A O     1 
ATOM   18996 C CB    . ARG A 1 4276 ? 224.652 157.842 185.559 1.00 90.12  ? 4276 ARG A CB    1 
ATOM   18997 C CG    . ARG A 1 4276 ? 224.882 159.014 186.489 1.00 90.12  ? 4276 ARG A CG    1 
ATOM   18998 C CD    . ARG A 1 4276 ? 223.593 159.410 187.190 1.00 90.12  ? 4276 ARG A CD    1 
ATOM   18999 N NE    . ARG A 1 4276 ? 222.802 158.253 187.597 1.00 90.12  ? 4276 ARG A NE    1 
ATOM   19000 C CZ    . ARG A 1 4276 ? 223.067 157.493 188.651 1.00 90.12  ? 4276 ARG A CZ    1 
ATOM   19001 N NH1   . ARG A 1 4276 ? 224.096 157.742 189.443 1.00 90.12  ? 4276 ARG A NH1   1 
ATOM   19002 N NH2   . ARG A 1 4276 ? 222.275 156.458 188.920 1.00 90.12  ? 4276 ARG A NH2   1 
ATOM   19003 N N     . SER A 1 4277 ? 224.184 156.871 182.371 1.00 85.73  ? 4277 SER A N     1 
ATOM   19004 C CA    . SER A 1 4277 ? 223.800 155.733 181.548 1.00 85.73  ? 4277 SER A CA    1 
ATOM   19005 C C     . SER A 1 4277 ? 224.977 155.143 180.792 1.00 85.73  ? 4277 SER A C     1 
ATOM   19006 O O     . SER A 1 4277 ? 224.911 153.983 180.373 1.00 85.73  ? 4277 SER A O     1 
ATOM   19007 C CB    . SER A 1 4277 ? 222.718 156.145 180.557 1.00 85.73  ? 4277 SER A CB    1 
ATOM   19008 O OG    . SER A 1 4277 ? 223.303 156.577 179.343 1.00 85.73  ? 4277 SER A OG    1 
ATOM   19009 N N     . PHE A 1 4278 ? 226.048 155.904 180.606 1.00 89.48  ? 4278 PHE A N     1 
ATOM   19010 C CA    . PHE A 1 4278 ? 227.218 155.420 179.893 1.00 89.48  ? 4278 PHE A CA    1 
ATOM   19011 C C     . PHE A 1 4278 ? 228.199 154.700 180.804 1.00 89.48  ? 4278 PHE A C     1 
ATOM   19012 O O     . PHE A 1 4278 ? 229.279 154.312 180.350 1.00 89.48  ? 4278 PHE A O     1 
ATOM   19013 C CB    . PHE A 1 4278 ? 227.908 156.579 179.177 1.00 89.48  ? 4278 PHE A CB    1 
ATOM   19014 C CG    . PHE A 1 4278 ? 227.241 156.970 177.895 1.00 89.48  ? 4278 PHE A CG    1 
ATOM   19015 C CD1   . PHE A 1 4278 ? 226.088 157.728 177.906 1.00 89.48  ? 4278 PHE A CD1   1 
ATOM   19016 C CD2   . PHE A 1 4278 ? 227.756 156.567 176.679 1.00 89.48  ? 4278 PHE A CD2   1 
ATOM   19017 C CE1   . PHE A 1 4278 ? 225.468 158.086 176.731 1.00 89.48  ? 4278 PHE A CE1   1 
ATOM   19018 C CE2   . PHE A 1 4278 ? 227.138 156.921 175.501 1.00 89.48  ? 4278 PHE A CE2   1 
ATOM   19019 C CZ    . PHE A 1 4278 ? 225.994 157.682 175.528 1.00 89.48  ? 4278 PHE A CZ    1 
ATOM   19020 N N     . ASP A 1 4279 ? 227.851 154.514 182.072 1.00 101.15 ? 4279 ASP A N     1 
ATOM   19021 C CA    . ASP A 1 4279 ? 228.668 153.756 183.005 1.00 101.15 ? 4279 ASP A CA    1 
ATOM   19022 C C     . ASP A 1 4279 ? 228.209 152.304 183.039 1.00 101.15 ? 4279 ASP A C     1 
ATOM   19023 O O     . ASP A 1 4279 ? 227.015 152.008 182.959 1.00 101.15 ? 4279 ASP A O     1 
ATOM   19024 C CB    . ASP A 1 4279 ? 228.601 154.365 184.405 1.00 101.15 ? 4279 ASP A CB    1 
ATOM   19025 C CG    . ASP A 1 4279 ? 229.393 155.652 184.515 1.00 101.15 ? 4279 ASP A CG    1 
ATOM   19026 O OD1   . ASP A 1 4279 ? 229.225 156.530 183.645 1.00 101.15 ? 4279 ASP A OD1   1 
ATOM   19027 O OD2   . ASP A 1 4279 ? 230.184 155.786 185.471 1.00 101.15 ? 4279 ASP A OD2   1 
ATOM   19028 N N     . SER A 1 4280 ? 229.179 151.398 183.171 1.00 106.30 ? 4280 SER A N     1 
ATOM   19029 C CA    . SER A 1 4280 ? 228.906 149.972 183.043 1.00 106.30 ? 4280 SER A CA    1 
ATOM   19030 C C     . SER A 1 4280 ? 227.980 149.442 184.129 1.00 106.30 ? 4280 SER A C     1 
ATOM   19031 O O     . SER A 1 4280 ? 227.385 148.374 183.949 1.00 106.30 ? 4280 SER A O     1 
ATOM   19032 C CB    . SER A 1 4280 ? 230.219 149.191 183.065 1.00 106.30 ? 4280 SER A CB    1 
ATOM   19033 O OG    . SER A 1 4280 ? 230.941 149.450 184.256 1.00 106.30 ? 4280 SER A OG    1 
ATOM   19034 N N     . GLU A 1 4281 ? 227.839 150.155 185.240 1.00 112.70 ? 4281 GLU A N     1 
ATOM   19035 C CA    . GLU A 1 4281 ? 227.061 149.680 186.374 1.00 112.70 ? 4281 GLU A CA    1 
ATOM   19036 C C     . GLU A 1 4281 ? 225.620 150.173 186.366 1.00 112.70 ? 4281 GLU A C     1 
ATOM   19037 O O     . GLU A 1 4281 ? 224.905 149.960 187.349 1.00 112.70 ? 4281 GLU A O     1 
ATOM   19038 C CB    . GLU A 1 4281 ? 227.743 150.092 187.683 1.00 112.70 ? 4281 GLU A CB    1 
ATOM   19039 C CG    . GLU A 1 4281 ? 228.110 151.564 187.753 1.00 112.70 ? 4281 GLU A CG    1 
ATOM   19040 C CD    . GLU A 1 4281 ? 226.989 152.422 188.304 1.00 112.70 ? 4281 GLU A CD    1 
ATOM   19041 O OE1   . GLU A 1 4281 ? 226.176 151.901 189.095 1.00 112.70 ? 4281 GLU A OE1   1 
ATOM   19042 O OE2   . GLU A 1 4281 ? 226.921 153.615 187.942 1.00 112.70 ? 4281 GLU A OE2   1 
ATOM   19043 N N     . PHE A 1 4282 ? 225.177 150.823 185.293 1.00 97.09  ? 4282 PHE A N     1 
ATOM   19044 C CA    . PHE A 1 4282 ? 223.821 151.350 185.247 1.00 97.09  ? 4282 PHE A CA    1 
ATOM   19045 C C     . PHE A 1 4282 ? 222.797 150.222 185.231 1.00 97.09  ? 4282 PHE A C     1 
ATOM   19046 O O     . PHE A 1 4282 ? 223.058 149.120 184.743 1.00 97.09  ? 4282 PHE A O     1 
ATOM   19047 C CB    . PHE A 1 4282 ? 223.631 152.241 184.021 1.00 97.09  ? 4282 PHE A CB    1 
ATOM   19048 C CG    . PHE A 1 4282 ? 222.478 153.191 184.141 1.00 97.09  ? 4282 PHE A CG    1 
ATOM   19049 C CD1   . PHE A 1 4282 ? 222.245 153.868 185.323 1.00 97.09  ? 4282 PHE A CD1   1 
ATOM   19050 C CD2   . PHE A 1 4282 ? 221.628 153.409 183.077 1.00 97.09  ? 4282 PHE A CD2   1 
ATOM   19051 C CE1   . PHE A 1 4282 ? 221.184 154.743 185.437 1.00 97.09  ? 4282 PHE A CE1   1 
ATOM   19052 C CE2   . PHE A 1 4282 ? 220.570 154.282 183.183 1.00 97.09  ? 4282 PHE A CE2   1 
ATOM   19053 C CZ    . PHE A 1 4282 ? 220.347 154.949 184.364 1.00 97.09  ? 4282 PHE A CZ    1 
ATOM   19054 N N     . LYS A 1 4283 ? 221.620 150.507 185.782 1.00 93.53  ? 4283 LYS A N     1 
ATOM   19055 C CA    . LYS A 1 4283 ? 220.530 149.543 185.866 1.00 93.53  ? 4283 LYS A CA    1 
ATOM   19056 C C     . LYS A 1 4283 ? 219.314 150.110 185.149 1.00 93.53  ? 4283 LYS A C     1 
ATOM   19057 O O     . LYS A 1 4283 ? 218.800 151.164 185.536 1.00 93.53  ? 4283 LYS A O     1 
ATOM   19058 C CB    . LYS A 1 4283 ? 220.193 149.228 187.322 1.00 93.53  ? 4283 LYS A CB    1 
ATOM   19059 C CG    . LYS A 1 4283 ? 221.383 149.309 188.256 1.00 93.53  ? 4283 LYS A CG    1 
ATOM   19060 C CD    . LYS A 1 4283 ? 222.352 148.169 188.011 1.00 93.53  ? 4283 LYS A CD    1 
ATOM   19061 C CE    . LYS A 1 4283 ? 221.772 146.855 188.497 1.00 93.53  ? 4283 LYS A CE    1 
ATOM   19062 N NZ    . LYS A 1 4283 ? 221.397 146.921 189.937 1.00 93.53  ? 4283 LYS A NZ    1 
ATOM   19063 N N     . LEU A 1 4284 ? 218.857 149.412 184.109 1.00 81.73  ? 4284 LEU A N     1 
ATOM   19064 C CA    . LEU A 1 4284 ? 217.684 149.875 183.377 1.00 81.73  ? 4284 LEU A CA    1 
ATOM   19065 C C     . LEU A 1 4284 ? 216.432 149.798 184.237 1.00 81.73  ? 4284 LEU A C     1 
ATOM   19066 O O     . LEU A 1 4284 ? 215.633 150.740 184.265 1.00 81.73  ? 4284 LEU A O     1 
ATOM   19067 C CB    . LEU A 1 4284 ? 217.505 149.060 182.100 1.00 81.73  ? 4284 LEU A CB    1 
ATOM   19068 C CG    . LEU A 1 4284 ? 218.455 149.379 180.948 1.00 81.73  ? 4284 LEU A CG    1 
ATOM   19069 C CD1   . LEU A 1 4284 ? 217.833 148.954 179.639 1.00 81.73  ? 4284 LEU A CD1   1 
ATOM   19070 C CD2   . LEU A 1 4284 ? 218.793 150.854 180.921 1.00 81.73  ? 4284 LEU A CD2   1 
ATOM   19071 N N     . ALA A 1 4285 ? 216.242 148.687 184.942 1.00 91.20  ? 4285 ALA A N     1 
ATOM   19072 C CA    . ALA A 1 4285 ? 215.106 148.516 185.835 1.00 91.20  ? 4285 ALA A CA    1 
ATOM   19073 C C     . ALA A 1 4285 ? 215.557 147.754 187.068 1.00 91.20  ? 4285 ALA A C     1 
ATOM   19074 O O     . ALA A 1 4285 ? 216.315 146.787 186.966 1.00 91.20  ? 4285 ALA A O     1 
ATOM   19075 C CB    . ALA A 1 4285 ? 213.956 147.776 185.149 1.00 91.20  ? 4285 ALA A CB    1 
ATOM   19076 N N     . CYS A 1 4286 ? 215.084 148.187 188.229 1.00 103.12 ? 4286 CYS A N     1 
ATOM   19077 C CA    . CYS A 1 4286 ? 215.488 147.608 189.498 1.00 103.12 ? 4286 CYS A CA    1 
ATOM   19078 C C     . CYS A 1 4286 ? 214.374 146.739 190.064 1.00 103.12 ? 4286 CYS A C     1 
ATOM   19079 O O     . CYS A 1 4286 ? 213.199 146.893 189.724 1.00 103.12 ? 4286 CYS A O     1 
ATOM   19080 C CB    . CYS A 1 4286 ? 215.862 148.699 190.505 1.00 103.12 ? 4286 CYS A CB    1 
ATOM   19081 S SG    . CYS A 1 4286 ? 216.563 150.187 189.766 1.00 103.12 ? 4286 CYS A SG    1 
ATOM   19082 N N     . LYS A 1 4287 ? 214.771 145.810 190.935 1.00 105.25 ? 4287 LYS A N     1 
ATOM   19083 C CA    . LYS A 1 4287 ? 213.845 144.927 191.645 1.00 105.25 ? 4287 LYS A CA    1 
ATOM   19084 C C     . LYS A 1 4287 ? 212.992 144.102 190.687 1.00 105.25 ? 4287 LYS A C     1 
ATOM   19085 O O     . LYS A 1 4287 ? 211.836 143.792 190.982 1.00 105.25 ? 4287 LYS A O     1 
ATOM   19086 C CB    . LYS A 1 4287 ? 212.951 145.716 192.606 1.00 105.25 ? 4287 LYS A CB    1 
ATOM   19087 C CG    . LYS A 1 4287 ? 213.692 146.748 193.440 1.00 105.25 ? 4287 LYS A CG    1 
ATOM   19088 C CD    . LYS A 1 4287 ? 214.439 146.099 194.593 1.00 105.25 ? 4287 LYS A CD    1 
ATOM   19089 C CE    . LYS A 1 4287 ? 215.173 147.136 195.426 1.00 105.25 ? 4287 LYS A CE    1 
ATOM   19090 N NZ    . LYS A 1 4287 ? 214.450 148.436 195.459 1.00 105.25 ? 4287 LYS A NZ    1 
ATOM   19091 N N     . VAL A 1 4288 ? 213.549 143.738 189.534 1.00 102.68 ? 4288 VAL A N     1 
ATOM   19092 C CA    . VAL A 1 4288 ? 212.834 142.873 188.604 1.00 102.68 ? 4288 VAL A CA    1 
ATOM   19093 C C     . VAL A 1 4288 ? 212.761 141.478 189.208 1.00 102.68 ? 4288 VAL A C     1 
ATOM   19094 O O     . VAL A 1 4288 ? 213.789 140.881 189.548 1.00 102.68 ? 4288 VAL A O     1 
ATOM   19095 C CB    . VAL A 1 4288 ? 213.517 142.854 187.231 1.00 102.68 ? 4288 VAL A CB    1 
ATOM   19096 C CG1   . VAL A 1 4288 ? 213.258 141.535 186.521 1.00 102.68 ? 4288 VAL A CG1   1 
ATOM   19097 C CG2   . VAL A 1 4288 ? 213.033 144.015 186.385 1.00 102.68 ? 4288 VAL A CG2   1 
ATOM   19098 N N     . ASP A 1 4289 ? 211.541 140.961 189.358 1.00 109.35 ? 4289 ASP A N     1 
ATOM   19099 C CA    . ASP A 1 4289 ? 211.309 139.662 189.988 1.00 109.35 ? 4289 ASP A CA    1 
ATOM   19100 C C     . ASP A 1 4289 ? 211.952 139.602 191.372 1.00 109.35 ? 4289 ASP A C     1 
ATOM   19101 O O     . ASP A 1 4289 ? 212.514 138.584 191.780 1.00 109.35 ? 4289 ASP A O     1 
ATOM   19102 C CB    . ASP A 1 4289 ? 211.808 138.519 189.102 1.00 109.35 ? 4289 ASP A CB    1 
ATOM   19103 N N     . GLY A 1 4290 ? 211.873 140.714 192.097 1.00 111.18 ? 4290 GLY A N     1 
ATOM   19104 C CA    . GLY A 1 4290 ? 212.409 140.781 193.441 1.00 111.18 ? 4290 GLY A CA    1 
ATOM   19105 C C     . GLY A 1 4290 ? 213.834 141.287 193.530 1.00 111.18 ? 4290 GLY A C     1 
ATOM   19106 O O     . GLY A 1 4290 ? 214.083 142.349 194.106 1.00 111.18 ? 4290 GLY A O     1 
ATOM   19107 N N     . HIS A 1 4291 ? 214.781 140.542 192.960 1.00 117.38 ? 4291 HIS A N     1 
ATOM   19108 C CA    . HIS A 1 4291 ? 216.192 140.862 193.139 1.00 117.38 ? 4291 HIS A CA    1 
ATOM   19109 C C     . HIS A 1 4291 ? 216.908 141.082 191.813 1.00 117.38 ? 4291 HIS A C     1 
ATOM   19110 O O     . HIS A 1 4291 ? 217.824 141.906 191.730 1.00 117.38 ? 4291 HIS A O     1 
ATOM   19111 C CB    . HIS A 1 4291 ? 216.886 139.751 193.930 1.00 117.38 ? 4291 HIS A CB    1 
ATOM   19112 C CG    . HIS A 1 4291 ? 218.288 139.474 193.484 1.00 117.38 ? 4291 HIS A CG    1 
ATOM   19113 N ND1   . HIS A 1 4291 ? 219.375 140.169 193.970 1.00 117.38 ? 4291 HIS A ND1   1 
ATOM   19114 C CD2   . HIS A 1 4291 ? 218.782 138.573 192.601 1.00 117.38 ? 4291 HIS A CD2   1 
ATOM   19115 C CE1   . HIS A 1 4291 ? 220.477 139.711 193.404 1.00 117.38 ? 4291 HIS A CE1   1 
ATOM   19116 N NE2   . HIS A 1 4291 ? 220.145 138.742 192.569 1.00 117.38 ? 4291 HIS A NE2   1 
ATOM   19117 N N     . LYS A 1 4292 ? 216.503 140.353 190.776 1.00 110.95 ? 4292 LYS A N     1 
ATOM   19118 C CA    . LYS A 1 4292 ? 217.171 140.454 189.485 1.00 110.95 ? 4292 LYS A CA    1 
ATOM   19119 C C     . LYS A 1 4292 ? 217.038 141.861 188.915 1.00 110.95 ? 4292 LYS A C     1 
ATOM   19120 O O     . LYS A 1 4292 ? 216.047 142.558 189.143 1.00 110.95 ? 4292 LYS A O     1 
ATOM   19121 C CB    . LYS A 1 4292 ? 216.589 139.438 188.505 1.00 110.95 ? 4292 LYS A CB    1 
ATOM   19122 C CG    . LYS A 1 4292 ? 217.445 138.201 188.313 1.00 110.95 ? 4292 LYS A CG    1 
ATOM   19123 C CD    . LYS A 1 4292 ? 216.656 137.078 187.658 1.00 110.95 ? 4292 LYS A CD    1 
ATOM   19124 C CE    . LYS A 1 4292 ? 215.756 137.598 186.545 1.00 110.95 ? 4292 LYS A CE    1 
ATOM   19125 N NZ    . LYS A 1 4292 ? 216.534 138.168 185.413 1.00 110.95 ? 4292 LYS A NZ    1 
ATOM   19126 N N     . ASP A 1 4293 ? 218.060 142.284 188.178 1.00 106.50 ? 4293 ASP A N     1 
ATOM   19127 C CA    . ASP A 1 4293 ? 218.084 143.615 187.593 1.00 106.50 ? 4293 ASP A CA    1 
ATOM   19128 C C     . ASP A 1 4293 ? 218.517 143.529 186.140 1.00 106.50 ? 4293 ASP A C     1 
ATOM   19129 O O     . ASP A 1 4293 ? 219.353 142.696 185.780 1.00 106.50 ? 4293 ASP A O     1 
ATOM   19130 C CB    . ASP A 1 4293 ? 219.024 144.542 188.363 1.00 106.50 ? 4293 ASP A CB    1 
ATOM   19131 C CG    . ASP A 1 4293 ? 218.795 144.485 189.855 1.00 106.50 ? 4293 ASP A CG    1 
ATOM   19132 O OD1   . ASP A 1 4293 ? 217.658 144.759 190.292 1.00 106.50 ? 4293 ASP A OD1   1 
ATOM   19133 O OD2   . ASP A 1 4293 ? 219.750 144.164 190.592 1.00 106.50 ? 4293 ASP A OD2   1 
ATOM   19134 N N     . ILE A 1 4294 ? 217.945 144.399 185.311 1.00 91.36  ? 4294 ILE A N     1 
ATOM   19135 C CA    . ILE A 1 4294 ? 218.256 144.433 183.889 1.00 91.36  ? 4294 ILE A CA    1 
ATOM   19136 C C     . ILE A 1 4294 ? 219.454 145.342 183.661 1.00 91.36  ? 4294 ILE A C     1 
ATOM   19137 O O     . ILE A 1 4294 ? 219.301 146.553 183.473 1.00 91.36  ? 4294 ILE A O     1 
ATOM   19138 C CB    . ILE A 1 4294 ? 217.046 144.907 183.068 1.00 91.36  ? 4294 ILE A CB    1 
ATOM   19139 C CG1   . ILE A 1 4294 ? 215.784 144.171 183.507 1.00 91.36  ? 4294 ILE A CG1   1 
ATOM   19140 C CG2   . ILE A 1 4294 ? 217.291 144.676 181.599 1.00 91.36  ? 4294 ILE A CG2   1 
ATOM   19141 C CD1   . ILE A 1 4294 ? 215.825 142.698 183.223 1.00 91.36  ? 4294 ILE A CD1   1 
ATOM   19142 N N     . GLN A 1 4295 ? 220.651 144.768 183.682 1.00 96.53  ? 4295 GLN A N     1 
ATOM   19143 C CA    . GLN A 1 4295 ? 221.856 145.556 183.475 1.00 96.53  ? 4295 GLN A CA    1 
ATOM   19144 C C     . GLN A 1 4295 ? 221.971 145.970 182.015 1.00 96.53  ? 4295 GLN A C     1 
ATOM   19145 O O     . GLN A 1 4295 ? 221.735 145.170 181.107 1.00 96.53  ? 4295 GLN A O     1 
ATOM   19146 C CB    . GLN A 1 4295 ? 223.086 144.755 183.891 1.00 96.53  ? 4295 GLN A CB    1 
ATOM   19147 C CG    . GLN A 1 4295 ? 224.300 145.606 184.189 1.00 96.53  ? 4295 GLN A CG    1 
ATOM   19148 C CD    . GLN A 1 4295 ? 224.417 145.939 185.664 1.00 96.53  ? 4295 GLN A CD    1 
ATOM   19149 O OE1   . GLN A 1 4295 ? 223.777 145.310 186.506 1.00 96.53  ? 4295 GLN A OE1   1 
ATOM   19150 N NE2   . GLN A 1 4295 ? 225.231 146.937 185.984 1.00 96.53  ? 4295 GLN A NE2   1 
ATOM   19151 N N     . MET A 1 4296 ? 222.331 147.227 181.787 1.00 91.83  ? 4296 MET A N     1 
ATOM   19152 C CA    . MET A 1 4296 ? 222.520 147.689 180.422 1.00 91.83  ? 4296 MET A CA    1 
ATOM   19153 C C     . MET A 1 4296 ? 223.757 147.035 179.813 1.00 91.83  ? 4296 MET A C     1 
ATOM   19154 O O     . MET A 1 4296 ? 224.804 146.960 180.462 1.00 91.83  ? 4296 MET A O     1 
ATOM   19155 C CB    . MET A 1 4296 ? 222.659 149.208 180.365 1.00 91.83  ? 4296 MET A CB    1 
ATOM   19156 C CG    . MET A 1 4296 ? 223.083 149.709 178.991 1.00 91.83  ? 4296 MET A CG    1 
ATOM   19157 S SD    . MET A 1 4296 ? 223.398 151.475 178.886 1.00 91.83  ? 4296 MET A SD    1 
ATOM   19158 C CE    . MET A 1 4296 ? 222.208 152.077 180.069 1.00 91.83  ? 4296 MET A CE    1 
ATOM   19159 N N     . PRO A 1 4297 ? 223.667 146.546 178.577 1.00 91.02  ? 4297 PRO A N     1 
ATOM   19160 C CA    . PRO A 1 4297 ? 224.848 145.976 177.925 1.00 91.02  ? 4297 PRO A CA    1 
ATOM   19161 C C     . PRO A 1 4297 ? 225.913 147.034 177.696 1.00 91.02  ? 4297 PRO A C     1 
ATOM   19162 O O     . PRO A 1 4297 ? 225.618 148.212 177.490 1.00 91.02  ? 4297 PRO A O     1 
ATOM   19163 C CB    . PRO A 1 4297 ? 224.298 145.443 176.600 1.00 91.02  ? 4297 PRO A CB    1 
ATOM   19164 C CG    . PRO A 1 4297 ? 223.079 146.259 176.354 1.00 91.02  ? 4297 PRO A CG    1 
ATOM   19165 C CD    . PRO A 1 4297 ? 222.484 146.497 177.705 1.00 91.02  ? 4297 PRO A CD    1 
ATOM   19166 N N     . ASP A 1 4298 ? 227.170 146.595 177.732 1.00 99.29  ? 4298 ASP A N     1 
ATOM   19167 C CA    . ASP A 1 4298 ? 228.314 147.484 177.553 1.00 99.29  ? 4298 ASP A CA    1 
ATOM   19168 C C     . ASP A 1 4298 ? 228.728 147.432 176.086 1.00 99.29  ? 4298 ASP A C     1 
ATOM   19169 O O     . ASP A 1 4298 ? 229.733 146.830 175.710 1.00 99.29  ? 4298 ASP A O     1 
ATOM   19170 C CB    . ASP A 1 4298 ? 229.451 147.078 178.481 1.00 99.29  ? 4298 ASP A CB    1 
ATOM   19171 C CG    . ASP A 1 4298 ? 228.964 146.722 179.868 1.00 99.29  ? 4298 ASP A CG    1 
ATOM   19172 O OD1   . ASP A 1 4298 ? 228.740 147.647 180.675 1.00 99.29  ? 4298 ASP A OD1   1 
ATOM   19173 O OD2   . ASP A 1 4298 ? 228.798 145.517 180.149 1.00 99.29  ? 4298 ASP A OD2   1 
ATOM   19174 N N     . GLY A 1 4299 ? 227.930 148.087 175.245 1.00 95.92  ? 4299 GLY A N     1 
ATOM   19175 C CA    . GLY A 1 4299 ? 228.156 148.063 173.820 1.00 95.92  ? 4299 GLY A CA    1 
ATOM   19176 C C     . GLY A 1 4299 ? 228.427 149.456 173.287 1.00 95.92  ? 4299 GLY A C     1 
ATOM   19177 O O     . GLY A 1 4299 ? 228.046 150.463 173.882 1.00 95.92  ? 4299 GLY A O     1 
ATOM   19178 N N     . ILE A 1 4300 ? 229.104 149.491 172.143 1.00 95.54  ? 4300 ILE A N     1 
ATOM   19179 C CA    . ILE A 1 4300 ? 229.457 150.749 171.498 1.00 95.54  ? 4300 ILE A CA    1 
ATOM   19180 C C     . ILE A 1 4300 ? 228.826 150.783 170.114 1.00 95.54  ? 4300 ILE A C     1 
ATOM   19181 O O     . ILE A 1 4300 ? 228.463 151.850 169.607 1.00 95.54  ? 4300 ILE A O     1 
ATOM   19182 C CB    . ILE A 1 4300 ? 230.986 150.915 171.429 1.00 95.54  ? 4300 ILE A CB    1 
ATOM   19183 C CG1   . ILE A 1 4300 ? 231.564 151.068 172.835 1.00 95.54  ? 4300 ILE A CG1   1 
ATOM   19184 C CG2   . ILE A 1 4300 ? 231.367 152.117 170.591 1.00 95.54  ? 4300 ILE A CG2   1 
ATOM   19185 C CD1   . ILE A 1 4300 ? 230.864 152.116 173.668 1.00 95.54  ? 4300 ILE A CD1   1 
ATOM   19186 N N     . ARG A 1 4301 ? 228.657 149.613 169.510 1.00 98.53  ? 4301 ARG A N     1 
ATOM   19187 C CA    . ARG A 1 4301 ? 228.073 149.492 168.185 1.00 98.53  ? 4301 ARG A CA    1 
ATOM   19188 C C     . ARG A 1 4301 ? 226.679 148.886 168.272 1.00 98.53  ? 4301 ARG A C     1 
ATOM   19189 O O     . ARG A 1 4301 ? 226.250 148.386 169.314 1.00 98.53  ? 4301 ARG A O     1 
ATOM   19190 C CB    . ARG A 1 4301 ? 228.966 148.649 167.268 1.00 98.53  ? 4301 ARG A CB    1 
ATOM   19191 C CG    . ARG A 1 4301 ? 229.878 149.468 166.372 1.00 98.53  ? 4301 ARG A CG    1 
ATOM   19192 C CD    . ARG A 1 4301 ? 231.277 148.881 166.303 1.00 98.53  ? 4301 ARG A CD    1 
ATOM   19193 N NE    . ARG A 1 4301 ? 231.890 148.756 167.620 1.00 98.53  ? 4301 ARG A NE    1 
ATOM   19194 C CZ    . ARG A 1 4301 ? 232.125 147.604 168.232 1.00 98.53  ? 4301 ARG A CZ    1 
ATOM   19195 N NH1   . ARG A 1 4301 ? 231.794 146.448 167.679 1.00 98.53  ? 4301 ARG A NH1   1 
ATOM   19196 N NH2   . ARG A 1 4301 ? 232.698 147.611 169.432 1.00 98.53  ? 4301 ARG A NH2   1 
ATOM   19197 N N     . ARG A 1 4302 ? 225.976 148.934 167.140 1.00 91.16  ? 4302 ARG A N     1 
ATOM   19198 C CA    . ARG A 1 4302 ? 224.591 148.479 167.099 1.00 91.16  ? 4302 ARG A CA    1 
ATOM   19199 C C     . ARG A 1 4302 ? 224.485 146.978 167.337 1.00 91.16  ? 4302 ARG A C     1 
ATOM   19200 O O     . ARG A 1 4302 ? 223.519 146.507 167.951 1.00 91.16  ? 4302 ARG A O     1 
ATOM   19201 C CB    . ARG A 1 4302 ? 223.968 148.855 165.758 1.00 91.16  ? 4302 ARG A CB    1 
ATOM   19202 C CG    . ARG A 1 4302 ? 222.652 148.177 165.474 1.00 91.16  ? 4302 ARG A CG    1 
ATOM   19203 C CD    . ARG A 1 4302 ? 222.435 148.032 163.988 1.00 91.16  ? 4302 ARG A CD    1 
ATOM   19204 N NE    . ARG A 1 4302 ? 221.382 147.071 163.694 1.00 91.16  ? 4302 ARG A NE    1 
ATOM   19205 C CZ    . ARG A 1 4302 ? 220.094 147.373 163.635 1.00 91.16  ? 4302 ARG A CZ    1 
ATOM   19206 N NH1   . ARG A 1 4302 ? 219.662 148.603 163.859 1.00 91.16  ? 4302 ARG A NH1   1 
ATOM   19207 N NH2   . ARG A 1 4302 ? 219.216 146.417 163.347 1.00 91.16  ? 4302 ARG A NH2   1 
ATOM   19208 N N     . GLU A 1 4303 ? 225.468 146.214 166.858 1.00 99.35  ? 4303 GLU A N     1 
ATOM   19209 C CA    . GLU A 1 4303 ? 225.370 144.761 166.927 1.00 99.35  ? 4303 GLU A CA    1 
ATOM   19210 C C     . GLU A 1 4303 ? 225.308 144.277 168.371 1.00 99.35  ? 4303 GLU A C     1 
ATOM   19211 O O     . GLU A 1 4303 ? 224.556 143.348 168.686 1.00 99.35  ? 4303 GLU A O     1 
ATOM   19212 C CB    . GLU A 1 4303 ? 226.536 144.120 166.167 1.00 99.35  ? 4303 GLU A CB    1 
ATOM   19213 C CG    . GLU A 1 4303 ? 227.824 143.933 166.956 1.00 99.35  ? 4303 GLU A CG    1 
ATOM   19214 C CD    . GLU A 1 4303 ? 229.061 143.945 166.073 1.00 99.35  ? 4303 GLU A CD    1 
ATOM   19215 O OE1   . GLU A 1 4303 ? 229.492 142.859 165.633 1.00 99.35  ? 4303 GLU A OE1   1 
ATOM   19216 O OE2   . GLU A 1 4303 ? 229.605 145.041 165.824 1.00 99.35  ? 4303 GLU A OE2   1 
ATOM   19217 N N     . GLU A 1 4304 ? 226.069 144.907 169.267 1.00 96.12  ? 4304 GLU A N     1 
ATOM   19218 C CA    . GLU A 1 4304 ? 226.040 144.504 170.669 1.00 96.12  ? 4304 GLU A CA    1 
ATOM   19219 C C     . GLU A 1 4304 ? 224.659 144.726 171.269 1.00 96.12  ? 4304 GLU A C     1 
ATOM   19220 O O     . GLU A 1 4304 ? 224.131 143.864 171.982 1.00 96.12  ? 4304 GLU A O     1 
ATOM   19221 C CB    . GLU A 1 4304 ? 227.097 145.273 171.457 1.00 96.12  ? 4304 GLU A CB    1 
ATOM   19222 C CG    . GLU A 1 4304 ? 228.515 144.990 171.014 1.00 96.12  ? 4304 GLU A CG    1 
ATOM   19223 C CD    . GLU A 1 4304 ? 229.154 146.181 170.335 1.00 96.12  ? 4304 GLU A CD    1 
ATOM   19224 O OE1   . GLU A 1 4304 ? 228.714 147.323 170.585 1.00 96.12  ? 4304 GLU A OE1   1 
ATOM   19225 O OE2   . GLU A 1 4304 ? 230.096 145.972 169.546 1.00 96.12  ? 4304 GLU A OE2   1 
ATOM   19226 N N     . PHE A 1 4305 ? 224.057 145.880 170.985 1.00 88.35  ? 4305 PHE A N     1 
ATOM   19227 C CA    . PHE A 1 4305 ? 222.739 146.175 171.531 1.00 88.35  ? 4305 PHE A CA    1 
ATOM   19228 C C     . PHE A 1 4305 ? 221.685 145.225 170.982 1.00 88.35  ? 4305 PHE A C     1 
ATOM   19229 O O     . PHE A 1 4305 ? 220.848 144.717 171.738 1.00 88.35  ? 4305 PHE A O     1 
ATOM   19230 C CB    . PHE A 1 4305 ? 222.366 147.625 171.235 1.00 88.35  ? 4305 PHE A CB    1 
ATOM   19231 C CG    . PHE A 1 4305 ? 223.226 148.619 171.948 1.00 88.35  ? 4305 PHE A CG    1 
ATOM   19232 C CD1   . PHE A 1 4305 ? 223.376 148.562 173.320 1.00 88.35  ? 4305 PHE A CD1   1 
ATOM   19233 C CD2   . PHE A 1 4305 ? 223.891 149.605 171.248 1.00 88.35  ? 4305 PHE A CD2   1 
ATOM   19234 C CE1   . PHE A 1 4305 ? 224.168 149.473 173.981 1.00 88.35  ? 4305 PHE A CE1   1 
ATOM   19235 C CE2   . PHE A 1 4305 ? 224.684 150.519 171.905 1.00 88.35  ? 4305 PHE A CE2   1 
ATOM   19236 C CZ    . PHE A 1 4305 ? 224.824 150.452 173.274 1.00 88.35  ? 4305 PHE A CZ    1 
ATOM   19237 N N     . VAL A 1 4306 ? 221.711 144.965 169.674 1.00 89.00  ? 4306 VAL A N     1 
ATOM   19238 C CA    . VAL A 1 4306 ? 220.700 144.079 169.110 1.00 89.00  ? 4306 VAL A CA    1 
ATOM   19239 C C     . VAL A 1 4306 ? 220.886 142.655 169.621 1.00 89.00  ? 4306 VAL A C     1 
ATOM   19240 O O     . VAL A 1 4306 ? 219.902 141.941 169.853 1.00 89.00  ? 4306 VAL A O     1 
ATOM   19241 C CB    . VAL A 1 4306 ? 220.700 144.154 167.572 1.00 89.00  ? 4306 VAL A CB    1 
ATOM   19242 C CG1   . VAL A 1 4306 ? 221.890 143.425 166.980 1.00 89.00  ? 4306 VAL A CG1   1 
ATOM   19243 C CG2   . VAL A 1 4306 ? 219.403 143.589 167.022 1.00 89.00  ? 4306 VAL A CG2   1 
ATOM   19244 N N     . GLN A 1 4307 ? 222.132 142.220 169.830 1.00 93.06  ? 4307 GLN A N     1 
ATOM   19245 C CA    . GLN A 1 4307 ? 222.352 140.885 170.369 1.00 93.06  ? 4307 GLN A CA    1 
ATOM   19246 C C     . GLN A 1 4307 ? 221.889 140.792 171.816 1.00 93.06  ? 4307 GLN A C     1 
ATOM   19247 O O     . GLN A 1 4307 ? 221.295 139.785 172.217 1.00 93.06  ? 4307 GLN A O     1 
ATOM   19248 C CB    . GLN A 1 4307 ? 223.826 140.503 170.248 1.00 93.06  ? 4307 GLN A CB    1 
ATOM   19249 C CG    . GLN A 1 4307 ? 224.198 139.223 170.977 1.00 93.06  ? 4307 GLN A CG    1 
ATOM   19250 C CD    . GLN A 1 4307 ? 223.714 137.971 170.265 1.00 93.06  ? 4307 GLN A CD    1 
ATOM   19251 O OE1   . GLN A 1 4307 ? 222.858 138.029 169.383 1.00 93.06  ? 4307 GLN A OE1   1 
ATOM   19252 N NE2   . GLN A 1 4307 ? 224.266 136.828 170.649 1.00 93.06  ? 4307 GLN A NE2   1 
ATOM   19253 N N     . TRP A 1 4308 ? 222.146 141.831 172.614 1.00 85.11  ? 4308 TRP A N     1 
ATOM   19254 C CA    . TRP A 1 4308 ? 221.656 141.831 173.987 1.00 85.11  ? 4308 TRP A CA    1 
ATOM   19255 C C     . TRP A 1 4308 ? 220.138 141.800 174.022 1.00 85.11  ? 4308 TRP A C     1 
ATOM   19256 O O     . TRP A 1 4308 ? 219.542 141.126 174.869 1.00 85.11  ? 4308 TRP A O     1 
ATOM   19257 C CB    . TRP A 1 4308 ? 222.178 143.051 174.739 1.00 85.11  ? 4308 TRP A CB    1 
ATOM   19258 C CG    . TRP A 1 4308 ? 221.645 143.150 176.130 1.00 85.11  ? 4308 TRP A CG    1 
ATOM   19259 C CD1   . TRP A 1 4308 ? 222.194 142.615 177.254 1.00 85.11  ? 4308 TRP A CD1   1 
ATOM   19260 C CD2   . TRP A 1 4308 ? 220.458 143.830 176.548 1.00 85.11  ? 4308 TRP A CD2   1 
ATOM   19261 N NE1   . TRP A 1 4308 ? 221.423 142.918 178.347 1.00 85.11  ? 4308 TRP A NE1   1 
ATOM   19262 C CE2   . TRP A 1 4308 ? 220.350 143.664 177.939 1.00 85.11  ? 4308 TRP A CE2   1 
ATOM   19263 C CE3   . TRP A 1 4308 ? 219.476 144.563 175.880 1.00 85.11  ? 4308 TRP A CE3   1 
ATOM   19264 C CZ2   . TRP A 1 4308 ? 219.303 144.202 178.673 1.00 85.11  ? 4308 TRP A CZ2   1 
ATOM   19265 C CZ3   . TRP A 1 4308 ? 218.437 145.097 176.612 1.00 85.11  ? 4308 TRP A CZ3   1 
ATOM   19266 C CH2   . TRP A 1 4308 ? 218.358 144.914 177.993 1.00 85.11  ? 4308 TRP A CH2   1 
ATOM   19267 N N     . VAL A 1 4309 ? 219.496 142.532 173.113 1.00 85.48  ? 4309 VAL A N     1 
ATOM   19268 C CA    . VAL A 1 4309 ? 218.040 142.492 173.023 1.00 85.48  ? 4309 VAL A CA    1 
ATOM   19269 C C     . VAL A 1 4309 ? 217.570 141.083 172.690 1.00 85.48  ? 4309 VAL A C     1 
ATOM   19270 O O     . VAL A 1 4309 ? 216.634 140.560 173.306 1.00 85.48  ? 4309 VAL A O     1 
ATOM   19271 C CB    . VAL A 1 4309 ? 217.541 143.513 171.988 1.00 85.48  ? 4309 VAL A CB    1 
ATOM   19272 C CG1   . VAL A 1 4309 ? 216.204 143.079 171.427 1.00 85.48  ? 4309 VAL A CG1   1 
ATOM   19273 C CG2   . VAL A 1 4309 ? 217.433 144.883 172.622 1.00 85.48  ? 4309 VAL A CG2   1 
ATOM   19274 N N     . GLU A 1 4310 ? 218.219 140.442 171.718 1.00 85.75  ? 4310 GLU A N     1 
ATOM   19275 C CA    . GLU A 1 4310 ? 217.840 139.078 171.373 1.00 85.75  ? 4310 GLU A CA    1 
ATOM   19276 C C     . GLU A 1 4310 ? 218.121 138.098 172.503 1.00 85.75  ? 4310 GLU A C     1 
ATOM   19277 O O     . GLU A 1 4310 ? 217.451 137.064 172.589 1.00 85.75  ? 4310 GLU A O     1 
ATOM   19278 C CB    . GLU A 1 4310 ? 218.565 138.632 170.107 1.00 85.75  ? 4310 GLU A CB    1 
ATOM   19279 C CG    . GLU A 1 4310 ? 218.092 139.333 168.854 1.00 85.75  ? 4310 GLU A CG    1 
ATOM   19280 C CD    . GLU A 1 4310 ? 218.458 138.577 167.598 1.00 85.75  ? 4310 GLU A CD    1 
ATOM   19281 O OE1   . GLU A 1 4310 ? 219.286 137.647 167.687 1.00 85.75  ? 4310 GLU A OE1   1 
ATOM   19282 O OE2   . GLU A 1 4310 ? 217.919 138.911 166.523 1.00 85.75  ? 4310 GLU A OE2   1 
ATOM   19283 N N     . LEU A 1 4311 ? 219.080 138.402 173.371 1.00 87.41  ? 4311 LEU A N     1 
ATOM   19284 C CA    . LEU A 1 4311 ? 219.412 137.545 174.500 1.00 87.41  ? 4311 LEU A CA    1 
ATOM   19285 C C     . LEU A 1 4311 ? 218.511 137.785 175.700 1.00 87.41  ? 4311 LEU A C     1 
ATOM   19286 O O     . LEU A 1 4311 ? 218.694 137.140 176.736 1.00 87.41  ? 4311 LEU A O     1 
ATOM   19287 C CB    . LEU A 1 4311 ? 220.872 137.752 174.908 1.00 87.41  ? 4311 LEU A CB    1 
ATOM   19288 C CG    . LEU A 1 4311 ? 221.917 137.055 174.040 1.00 87.41  ? 4311 LEU A CG    1 
ATOM   19289 C CD1   . LEU A 1 4311 ? 223.274 137.067 174.724 1.00 87.41  ? 4311 LEU A CD1   1 
ATOM   19290 C CD2   . LEU A 1 4311 ? 221.485 135.633 173.723 1.00 87.41  ? 4311 LEU A CD2   1 
ATOM   19291 N N     . LEU A 1 4312 ? 217.559 138.694 175.583 1.00 83.80  ? 4312 LEU A N     1 
ATOM   19292 C CA    . LEU A 1 4312 ? 216.681 139.010 176.697 1.00 83.80  ? 4312 LEU A CA    1 
ATOM   19293 C C     . LEU A 1 4312 ? 215.817 137.803 177.041 1.00 83.80  ? 4312 LEU A C     1 
ATOM   19294 O O     . LEU A 1 4312 ? 215.265 137.166 176.137 1.00 83.80  ? 4312 LEU A O     1 
ATOM   19295 C CB    . LEU A 1 4312 ? 215.810 140.203 176.334 1.00 83.80  ? 4312 LEU A CB    1 
ATOM   19296 C CG    . LEU A 1 4312 ? 214.970 140.855 177.422 1.00 83.80  ? 4312 LEU A CG    1 
ATOM   19297 C CD1   . LEU A 1 4312 ? 215.857 141.653 178.351 1.00 83.80  ? 4312 LEU A CD1   1 
ATOM   19298 C CD2   . LEU A 1 4312 ? 213.933 141.745 176.774 1.00 83.80  ? 4312 LEU A CD2   1 
ATOM   19299 N N     . PRO A 1 4313 ? 215.680 137.454 178.317 1.00 88.37  ? 4313 PRO A N     1 
ATOM   19300 C CA    . PRO A 1 4313 ? 214.858 136.296 178.680 1.00 88.37  ? 4313 PRO A CA    1 
ATOM   19301 C C     . PRO A 1 4313 ? 213.396 136.522 178.336 1.00 88.37  ? 4313 PRO A C     1 
ATOM   19302 O O     . PRO A 1 4313 ? 212.905 137.652 178.320 1.00 88.37  ? 4313 PRO A O     1 
ATOM   19303 C CB    . PRO A 1 4313 ? 215.062 136.173 180.193 1.00 88.37  ? 4313 PRO A CB    1 
ATOM   19304 C CG    . PRO A 1 4313 ? 215.464 137.540 180.628 1.00 88.37  ? 4313 PRO A CG    1 
ATOM   19305 C CD    . PRO A 1 4313 ? 216.269 138.106 179.497 1.00 88.37  ? 4313 PRO A CD    1 
ATOM   19306 N N     . ASP A 1 4314 ? 212.699 135.422 178.054 1.00 95.02  ? 4314 ASP A N     1 
ATOM   19307 C CA    . ASP A 1 4314 ? 211.292 135.514 177.684 1.00 95.02  ? 4314 ASP A CA    1 
ATOM   19308 C C     . ASP A 1 4314 ? 210.417 135.911 178.865 1.00 95.02  ? 4314 ASP A C     1 
ATOM   19309 O O     . ASP A 1 4314 ? 209.374 136.547 178.674 1.00 95.02  ? 4314 ASP A O     1 
ATOM   19310 C CB    . ASP A 1 4314 ? 210.819 134.185 177.101 1.00 95.02  ? 4314 ASP A CB    1 
ATOM   19311 C CG    . ASP A 1 4314 ? 209.405 134.254 176.568 1.00 95.02  ? 4314 ASP A CG    1 
ATOM   19312 O OD1   . ASP A 1 4314 ? 208.458 134.146 177.374 1.00 95.02  ? 4314 ASP A OD1   1 
ATOM   19313 O OD2   . ASP A 1 4314 ? 209.238 134.418 175.342 1.00 95.02  ? 4314 ASP A OD2   1 
ATOM   19314 N N     . THR A 1 4315 ? 210.819 135.560 180.084 1.00 95.57  ? 4315 THR A N     1 
ATOM   19315 C CA    . THR A 1 4315 ? 209.994 135.786 181.270 1.00 95.57  ? 4315 THR A CA    1 
ATOM   19316 C C     . THR A 1 4315 ? 210.003 137.271 181.626 1.00 95.57  ? 4315 THR A C     1 
ATOM   19317 O O     . THR A 1 4315 ? 210.696 137.729 182.538 1.00 95.57  ? 4315 THR A O     1 
ATOM   19318 C CB    . THR A 1 4315 ? 210.486 134.930 182.432 1.00 95.57  ? 4315 THR A CB    1 
ATOM   19319 O OG1   . THR A 1 4315 ? 209.909 135.402 183.656 1.00 95.57  ? 4315 THR A OG1   1 
ATOM   19320 C CG2   . THR A 1 4315 ? 212.008 134.959 182.529 1.00 95.57  ? 4315 THR A CG2   1 
ATOM   19321 N N     . GLN A 1 4316 ? 209.201 138.039 180.894 1.00 82.43  ? 4316 GLN A N     1 
ATOM   19322 C CA    . GLN A 1 4316 ? 209.059 139.468 181.146 1.00 82.43  ? 4316 GLN A CA    1 
ATOM   19323 C C     . GLN A 1 4316 ? 207.878 139.688 182.082 1.00 82.43  ? 4316 GLN A C     1 
ATOM   19324 O O     . GLN A 1 4316 ? 206.720 139.574 181.670 1.00 82.43  ? 4316 GLN A O     1 
ATOM   19325 C CB    . GLN A 1 4316 ? 208.864 140.241 179.846 1.00 82.43  ? 4316 GLN A CB    1 
ATOM   19326 C CG    . GLN A 1 4316 ? 208.488 141.693 180.071 1.00 82.43  ? 4316 GLN A CG    1 
ATOM   19327 C CD    . GLN A 1 4316 ? 207.457 142.190 179.085 1.00 82.43  ? 4316 GLN A CD    1 
ATOM   19328 O OE1   . GLN A 1 4316 ? 207.682 142.177 177.878 1.00 82.43  ? 4316 GLN A OE1   1 
ATOM   19329 N NE2   . GLN A 1 4316 ? 206.317 142.634 179.595 1.00 82.43  ? 4316 GLN A NE2   1 
ATOM   19330 N N     . THR A 1 4317 ? 208.168 139.997 183.325 1.00 81.70  ? 4317 THR A N     1 
ATOM   19331 C CA    . THR A 1 4317 ? 207.132 140.346 184.279 1.00 81.70  ? 4317 THR A CA    1 
ATOM   19332 C C     . THR A 1 4317 ? 206.830 141.834 184.200 1.00 81.70  ? 4317 THR A C     1 
ATOM   19333 O O     . THR A 1 4317 ? 207.657 142.622 183.732 1.00 81.70  ? 4317 THR A O     1 
ATOM   19334 C CB    . THR A 1 4317 ? 207.574 139.976 185.690 1.00 81.70  ? 4317 THR A CB    1 
ATOM   19335 O OG1   . THR A 1 4317 ? 208.295 141.072 186.265 1.00 81.70  ? 4317 THR A OG1   1 
ATOM   19336 C CG2   . THR A 1 4317 ? 208.476 138.757 185.655 1.00 81.70  ? 4317 THR A CG2   1 
ATOM   19337 N N     . PRO A 1 4318 ? 205.647 142.258 184.649 1.00 74.59  ? 4318 PRO A N     1 
ATOM   19338 C CA    . PRO A 1 4318 ? 205.336 143.694 184.640 1.00 74.59  ? 4318 PRO A CA    1 
ATOM   19339 C C     . PRO A 1 4318 ? 206.270 144.528 185.493 1.00 74.59  ? 4318 PRO A C     1 
ATOM   19340 O O     . PRO A 1 4318 ? 206.300 145.753 185.328 1.00 74.59  ? 4318 PRO A O     1 
ATOM   19341 C CB    . PRO A 1 4318 ? 203.900 143.742 185.169 1.00 74.59  ? 4318 PRO A CB    1 
ATOM   19342 C CG    . PRO A 1 4318 ? 203.337 142.431 184.790 1.00 74.59  ? 4318 PRO A CG    1 
ATOM   19343 C CD    . PRO A 1 4318 ? 204.456 141.447 184.942 1.00 74.59  ? 4318 PRO A CD    1 
ATOM   19344 N N     . SER A 1 4319 ? 207.028 143.917 186.404 1.00 75.26  ? 4319 SER A N     1 
ATOM   19345 C CA    . SER A 1 4319 ? 208.027 144.672 187.148 1.00 75.26  ? 4319 SER A CA    1 
ATOM   19346 C C     . SER A 1 4319 ? 209.087 145.264 186.234 1.00 75.26  ? 4319 SER A C     1 
ATOM   19347 O O     . SER A 1 4319 ? 209.778 146.205 186.633 1.00 75.26  ? 4319 SER A O     1 
ATOM   19348 C CB    . SER A 1 4319 ? 208.685 143.786 188.202 1.00 75.26  ? 4319 SER A CB    1 
ATOM   19349 O OG    . SER A 1 4319 ? 209.565 142.854 187.605 1.00 75.26  ? 4319 SER A OG    1 
ATOM   19350 N N     . TRP A 1 4320 ? 209.232 144.732 185.020 1.00 74.71  ? 4320 TRP A N     1 
ATOM   19351 C CA    . TRP A 1 4320 ? 210.152 145.323 184.058 1.00 74.71  ? 4320 TRP A CA    1 
ATOM   19352 C C     . TRP A 1 4320 ? 209.756 146.755 183.736 1.00 74.71  ? 4320 TRP A C     1 
ATOM   19353 O O     . TRP A 1 4320 ? 210.610 147.645 183.663 1.00 74.71  ? 4320 TRP A O     1 
ATOM   19354 C CB    . TRP A 1 4320 ? 210.180 144.492 182.779 1.00 74.71  ? 4320 TRP A CB    1 
ATOM   19355 C CG    . TRP A 1 4320 ? 210.796 143.151 182.926 1.00 74.71  ? 4320 TRP A CG    1 
ATOM   19356 C CD1   . TRP A 1 4320 ? 210.724 142.326 184.005 1.00 74.71  ? 4320 TRP A CD1   1 
ATOM   19357 C CD2   . TRP A 1 4320 ? 211.559 142.456 181.940 1.00 74.71  ? 4320 TRP A CD2   1 
ATOM   19358 N NE1   . TRP A 1 4320 ? 211.410 141.165 183.759 1.00 74.71  ? 4320 TRP A NE1   1 
ATOM   19359 C CE2   . TRP A 1 4320 ? 211.932 141.221 182.494 1.00 74.71  ? 4320 TRP A CE2   1 
ATOM   19360 C CE3   . TRP A 1 4320 ? 211.969 142.763 180.644 1.00 74.71  ? 4320 TRP A CE3   1 
ATOM   19361 C CZ2   . TRP A 1 4320 ? 212.694 140.294 181.798 1.00 74.71  ? 4320 TRP A CZ2   1 
ATOM   19362 C CZ3   . TRP A 1 4320 ? 212.721 141.846 179.958 1.00 74.71  ? 4320 TRP A CZ3   1 
ATOM   19363 C CH2   . TRP A 1 4320 ? 213.078 140.625 180.532 1.00 74.71  ? 4320 TRP A CH2   1 
ATOM   19364 N N     . LEU A 1 4321 ? 208.465 146.997 183.543 1.00 64.46  ? 4321 LEU A N     1 
ATOM   19365 C CA    . LEU A 1 4321 ? 207.983 148.324 183.199 1.00 64.46  ? 4321 LEU A CA    1 
ATOM   19366 C C     . LEU A 1 4321 ? 207.883 149.240 184.405 1.00 64.46  ? 4321 LEU A C     1 
ATOM   19367 O O     . LEU A 1 4321 ? 207.456 150.388 184.256 1.00 64.46  ? 4321 LEU A O     1 
ATOM   19368 C CB    . LEU A 1 4321 ? 206.616 148.228 182.520 1.00 64.46  ? 4321 LEU A CB    1 
ATOM   19369 C CG    . LEU A 1 4321 ? 206.358 147.041 181.595 1.00 64.46  ? 4321 LEU A CG    1 
ATOM   19370 C CD1   . LEU A 1 4321 ? 204.988 147.162 180.963 1.00 64.46  ? 4321 LEU A CD1   1 
ATOM   19371 C CD2   . LEU A 1 4321 ? 207.419 146.951 180.526 1.00 64.46  ? 4321 LEU A CD2   1 
ATOM   19372 N N     . GLY A 1 4322 ? 208.258 148.768 185.589 1.00 68.63  ? 4322 GLY A N     1 
ATOM   19373 C CA    . GLY A 1 4322 ? 208.071 149.522 186.802 1.00 68.63  ? 4322 GLY A CA    1 
ATOM   19374 C C     . GLY A 1 4322 ? 206.740 149.297 187.479 1.00 68.63  ? 4322 GLY A C     1 
ATOM   19375 O O     . GLY A 1 4322 ? 206.523 149.827 188.575 1.00 68.63  ? 4322 GLY A O     1 
ATOM   19376 N N     . LEU A 1 4323 ? 205.845 148.538 186.863 1.00 67.10  ? 4323 LEU A N     1 
ATOM   19377 C CA    . LEU A 1 4323 ? 204.562 148.209 187.458 1.00 67.10  ? 4323 LEU A CA    1 
ATOM   19378 C C     . LEU A 1 4323 ? 204.734 147.139 188.531 1.00 67.10  ? 4323 LEU A C     1 
ATOM   19379 O O     . LEU A 1 4323 ? 205.647 146.316 188.455 1.00 67.10  ? 4323 LEU A O     1 
ATOM   19380 C CB    . LEU A 1 4323 ? 203.594 147.700 186.399 1.00 67.10  ? 4323 LEU A CB    1 
ATOM   19381 C CG    . LEU A 1 4323 ? 202.848 148.693 185.511 1.00 67.10  ? 4323 LEU A CG    1 
ATOM   19382 C CD1   . LEU A 1 4323 ? 201.847 149.470 186.335 1.00 67.10  ? 4323 LEU A CD1   1 
ATOM   19383 C CD2   . LEU A 1 4323 ? 203.785 149.625 184.775 1.00 67.10  ? 4323 LEU A CD2   1 
ATOM   19384 N N     . PRO A 1 4324 ? 203.872 147.128 189.542 1.00 72.67  ? 4324 PRO A N     1 
ATOM   19385 C CA    . PRO A 1 4324 ? 203.847 145.988 190.459 1.00 72.67  ? 4324 PRO A CA    1 
ATOM   19386 C C     . PRO A 1 4324 ? 203.456 144.726 189.711 1.00 72.67  ? 4324 PRO A C     1 
ATOM   19387 O O     . PRO A 1 4324 ? 202.671 144.762 188.762 1.00 72.67  ? 4324 PRO A O     1 
ATOM   19388 C CB    . PRO A 1 4324 ? 202.788 146.384 191.493 1.00 72.67  ? 4324 PRO A CB    1 
ATOM   19389 C CG    . PRO A 1 4324 ? 201.944 147.394 190.801 1.00 72.67  ? 4324 PRO A CG    1 
ATOM   19390 C CD    . PRO A 1 4324 ? 202.866 148.141 189.891 1.00 72.67  ? 4324 PRO A CD    1 
ATOM   19391 N N     . ASN A 1 4325 ? 204.011 143.594 190.147 1.00 73.89  ? 4325 ASN A N     1 
ATOM   19392 C CA    . ASN A 1 4325 ? 203.799 142.351 189.415 1.00 73.89  ? 4325 ASN A CA    1 
ATOM   19393 C C     . ASN A 1 4325 ? 202.345 141.903 189.426 1.00 73.89  ? 4325 ASN A C     1 
ATOM   19394 O O     . ASN A 1 4325 ? 201.971 141.048 188.619 1.00 73.89  ? 4325 ASN A O     1 
ATOM   19395 C CB    . ASN A 1 4325 ? 204.691 141.248 189.979 1.00 73.89  ? 4325 ASN A CB    1 
ATOM   19396 C CG    . ASN A 1 4325 ? 206.161 141.580 189.862 1.00 73.89  ? 4325 ASN A CG    1 
ATOM   19397 O OD1   . ASN A 1 4325 ? 206.625 142.579 190.406 1.00 73.89  ? 4325 ASN A OD1   1 
ATOM   19398 N ND2   . ASN A 1 4325 ? 206.901 140.748 189.141 1.00 73.89  ? 4325 ASN A ND2   1 
ATOM   19399 N N     . ASN A 1 4326 ? 201.515 142.462 190.305 1.00 81.79  ? 4326 ASN A N     1 
ATOM   19400 C CA    . ASN A 1 4326 ? 200.100 142.121 190.296 1.00 81.79  ? 4326 ASN A CA    1 
ATOM   19401 C C     . ASN A 1 4326 ? 199.337 142.826 189.184 1.00 81.79  ? 4326 ASN A C     1 
ATOM   19402 O O     . ASN A 1 4326 ? 198.132 142.589 189.036 1.00 81.79  ? 4326 ASN A O     1 
ATOM   19403 C CB    . ASN A 1 4326 ? 199.468 142.452 191.647 1.00 81.79  ? 4326 ASN A CB    1 
ATOM   19404 C CG    . ASN A 1 4326 ? 199.724 143.878 192.073 1.00 81.79  ? 4326 ASN A CG    1 
ATOM   19405 O OD1   . ASN A 1 4326 ? 199.229 144.820 191.458 1.00 81.79  ? 4326 ASN A OD1   1 
ATOM   19406 N ND2   . ASN A 1 4326 ? 200.505 144.046 193.132 1.00 81.79  ? 4326 ASN A ND2   1 
ATOM   19407 N N     . ALA A 1 4327 ? 199.998 143.692 188.415 1.00 80.62  ? 4327 ALA A N     1 
ATOM   19408 C CA    . ALA A 1 4327 ? 199.317 144.358 187.312 1.00 80.62  ? 4327 ALA A CA    1 
ATOM   19409 C C     . ALA A 1 4327 ? 198.849 143.352 186.273 1.00 80.62  ? 4327 ALA A C     1 
ATOM   19410 O O     . ALA A 1 4327 ? 197.766 143.503 185.696 1.00 80.62  ? 4327 ALA A O     1 
ATOM   19411 C CB    . ALA A 1 4327 ? 200.235 145.398 186.675 1.00 80.62  ? 4327 ALA A CB    1 
ATOM   19412 N N     . GLU A 1 4328 ? 199.652 142.320 186.015 1.00 83.76  ? 4328 GLU A N     1 
ATOM   19413 C CA    . GLU A 1 4328 ? 199.234 141.286 185.076 1.00 83.76  ? 4328 GLU A CA    1 
ATOM   19414 C C     . GLU A 1 4328 ? 198.000 140.557 185.589 1.00 83.76  ? 4328 GLU A C     1 
ATOM   19415 O O     . GLU A 1 4328 ? 197.091 140.236 184.815 1.00 83.76  ? 4328 GLU A O     1 
ATOM   19416 C CB    . GLU A 1 4328 ? 200.392 140.319 184.815 1.00 83.76  ? 4328 GLU A CB    1 
ATOM   19417 C CG    . GLU A 1 4328 ? 200.009 138.936 184.302 1.00 83.76  ? 4328 GLU A CG    1 
ATOM   19418 C CD    . GLU A 1 4328 ? 199.627 137.970 185.407 1.00 83.76  ? 4328 GLU A CD    1 
ATOM   19419 O OE1   . GLU A 1 4328 ? 199.708 138.356 186.591 1.00 83.76  ? 4328 GLU A OE1   1 
ATOM   19420 O OE2   . GLU A 1 4328 ? 199.247 136.823 185.090 1.00 83.76  ? 4328 GLU A OE2   1 
ATOM   19421 N N     . ARG A 1 4329 ? 197.953 140.281 186.891 1.00 81.68  ? 4329 ARG A N     1 
ATOM   19422 C CA    . ARG A 1 4329 ? 196.774 139.649 187.468 1.00 81.68  ? 4329 ARG A CA    1 
ATOM   19423 C C     . ARG A 1 4329 ? 195.548 140.537 187.315 1.00 81.68  ? 4329 ARG A C     1 
ATOM   19424 O O     . ARG A 1 4329 ? 194.458 140.056 186.980 1.00 81.68  ? 4329 ARG A O     1 
ATOM   19425 C CB    . ARG A 1 4329 ? 197.030 139.329 188.938 1.00 81.68  ? 4329 ARG A CB    1 
ATOM   19426 C CG    . ARG A 1 4329 ? 195.781 139.114 189.765 1.00 81.68  ? 4329 ARG A CG    1 
ATOM   19427 C CD    . ARG A 1 4329 ? 196.129 138.933 191.230 1.00 81.68  ? 4329 ARG A CD    1 
ATOM   19428 N NE    . ARG A 1 4329 ? 196.687 137.612 191.483 1.00 81.68  ? 4329 ARG A NE    1 
ATOM   19429 C CZ    . ARG A 1 4329 ? 197.984 137.350 191.554 1.00 81.68  ? 4329 ARG A CZ    1 
ATOM   19430 N NH1   . ARG A 1 4329 ? 198.890 138.304 191.418 1.00 81.68  ? 4329 ARG A NH1   1 
ATOM   19431 N NH2   . ARG A 1 4329 ? 198.383 136.100 191.766 1.00 81.68  ? 4329 ARG A NH2   1 
ATOM   19432 N N     . VAL A 1 4330 ? 195.709 141.838 187.556 1.00 79.55  ? 4330 VAL A N     1 
ATOM   19433 C CA    . VAL A 1 4330 ? 194.591 142.763 187.391 1.00 79.55  ? 4330 VAL A CA    1 
ATOM   19434 C C     . VAL A 1 4330 ? 194.111 142.762 185.947 1.00 79.55  ? 4330 VAL A C     1 
ATOM   19435 O O     . VAL A 1 4330 ? 192.904 142.748 185.673 1.00 79.55  ? 4330 VAL A O     1 
ATOM   19436 C CB    . VAL A 1 4330 ? 194.989 144.175 187.851 1.00 79.55  ? 4330 VAL A CB    1 
ATOM   19437 C CG1   . VAL A 1 4330 ? 193.849 145.146 187.614 1.00 79.55  ? 4330 VAL A CG1   1 
ATOM   19438 C CG2   . VAL A 1 4330 ? 195.374 144.160 189.311 1.00 79.55  ? 4330 VAL A CG2   1 
ATOM   19439 N N     . LEU A 1 4331 ? 195.050 142.780 185.000 1.00 77.89  ? 4331 LEU A N     1 
ATOM   19440 C CA    . LEU A 1 4331 ? 194.681 142.775 183.590 1.00 77.89  ? 4331 LEU A CA    1 
ATOM   19441 C C     . LEU A 1 4331 ? 193.950 141.493 183.212 1.00 77.89  ? 4331 LEU A C     1 
ATOM   19442 O O     . LEU A 1 4331 ? 192.973 141.527 182.457 1.00 77.89  ? 4331 LEU A O     1 
ATOM   19443 C CB    . LEU A 1 4331 ? 195.925 142.952 182.727 1.00 77.89  ? 4331 LEU A CB    1 
ATOM   19444 C CG    . LEU A 1 4331 ? 195.657 142.892 181.229 1.00 77.89  ? 4331 LEU A CG    1 
ATOM   19445 C CD1   . LEU A 1 4331 ? 194.980 144.170 180.779 1.00 77.89  ? 4331 LEU A CD1   1 
ATOM   19446 C CD2   . LEU A 1 4331 ? 196.945 142.658 180.468 1.00 77.89  ? 4331 LEU A CD2   1 
ATOM   19447 N N     . LEU A 1 4332 ? 194.416 140.351 183.720 1.00 79.73  ? 4332 LEU A N     1 
ATOM   19448 C CA    . LEU A 1 4332 ? 193.743 139.089 183.431 1.00 79.73  ? 4332 LEU A CA    1 
ATOM   19449 C C     . LEU A 1 4332 ? 192.334 139.077 184.004 1.00 79.73  ? 4332 LEU A C     1 
ATOM   19450 O O     . LEU A 1 4332 ? 191.398 138.590 183.361 1.00 79.73  ? 4332 LEU A O     1 
ATOM   19451 C CB    . LEU A 1 4332 ? 194.554 137.919 183.980 1.00 79.73  ? 4332 LEU A CB    1 
ATOM   19452 C CG    . LEU A 1 4332 ? 195.778 137.510 183.165 1.00 79.73  ? 4332 LEU A CG    1 
ATOM   19453 C CD1   . LEU A 1 4332 ? 196.288 136.151 183.609 1.00 79.73  ? 4332 LEU A CD1   1 
ATOM   19454 C CD2   . LEU A 1 4332 ? 195.450 137.503 181.686 1.00 79.73  ? 4332 LEU A CD2   1 
ATOM   19455 N N     . THR A 1 4333 ? 192.164 139.606 185.216 1.00 84.73  ? 4333 THR A N     1 
ATOM   19456 C CA    . THR A 1 4333 ? 190.827 139.698 185.791 1.00 84.73  ? 4333 THR A CA    1 
ATOM   19457 C C     . THR A 1 4333 ? 189.924 140.576 184.936 1.00 84.73  ? 4333 THR A C     1 
ATOM   19458 O O     . THR A 1 4333 ? 188.760 140.236 184.689 1.00 84.73  ? 4333 THR A O     1 
ATOM   19459 C CB    . THR A 1 4333 ? 190.905 140.242 187.214 1.00 84.73  ? 4333 THR A CB    1 
ATOM   19460 O OG1   . THR A 1 4333 ? 191.804 139.437 187.984 1.00 84.73  ? 4333 THR A OG1   1 
ATOM   19461 C CG2   . THR A 1 4333 ? 189.534 140.225 187.865 1.00 84.73  ? 4333 THR A CG2   1 
ATOM   19462 N N     . THR A 1 4334 ? 190.448 141.712 184.474 1.00 84.92  ? 4334 THR A N     1 
ATOM   19463 C CA    . THR A 1 4334 ? 189.650 142.598 183.636 1.00 84.92  ? 4334 THR A CA    1 
ATOM   19464 C C     . THR A 1 4334 ? 189.265 141.917 182.330 1.00 84.92  ? 4334 THR A C     1 
ATOM   19465 O O     . THR A 1 4334 ? 188.130 142.053 181.862 1.00 84.92  ? 4334 THR A O     1 
ATOM   19466 C CB    . THR A 1 4334 ? 190.411 143.892 183.364 1.00 84.92  ? 4334 THR A CB    1 
ATOM   19467 O OG1   . THR A 1 4334 ? 190.728 144.526 184.608 1.00 84.92  ? 4334 THR A OG1   1 
ATOM   19468 C CG2   . THR A 1 4334 ? 189.570 144.836 182.525 1.00 84.92  ? 4334 THR A CG2   1 
ATOM   19469 N N     . GLN A 1 4335 ? 190.195 141.174 181.731 1.00 85.88  ? 4335 GLN A N     1 
ATOM   19470 C CA    . GLN A 1 4335 ? 189.884 140.472 180.489 1.00 85.88  ? 4335 GLN A CA    1 
ATOM   19471 C C     . GLN A 1 4335 ? 188.850 139.377 180.717 1.00 85.88  ? 4335 GLN A C     1 
ATOM   19472 O O     . GLN A 1 4335 ? 187.993 139.135 179.860 1.00 85.88  ? 4335 GLN A O     1 
ATOM   19473 C CB    . GLN A 1 4335 ? 191.157 139.897 179.874 1.00 85.88  ? 4335 GLN A CB    1 
ATOM   19474 C CG    . GLN A 1 4335 ? 191.909 140.886 179.009 1.00 85.88  ? 4335 GLN A CG    1 
ATOM   19475 C CD    . GLN A 1 4335 ? 193.232 140.346 178.530 1.00 85.88  ? 4335 GLN A CD    1 
ATOM   19476 O OE1   . GLN A 1 4335 ? 193.692 139.304 178.991 1.00 85.88  ? 4335 GLN A OE1   1 
ATOM   19477 N NE2   . GLN A 1 4335 ? 193.856 141.051 177.597 1.00 85.88  ? 4335 GLN A NE2   1 
ATOM   19478 N N     . GLY A 1 4336 ? 188.918 138.697 181.861 1.00 84.64  ? 4336 GLY A N     1 
ATOM   19479 C CA    . GLY A 1 4336 ? 187.893 137.717 182.182 1.00 84.64  ? 4336 GLY A CA    1 
ATOM   19480 C C     . GLY A 1 4336 ? 186.524 138.347 182.331 1.00 84.64  ? 4336 GLY A C     1 
ATOM   19481 O O     . GLY A 1 4336 ? 185.525 137.819 181.832 1.00 84.64  ? 4336 GLY A O     1 
ATOM   19482 N N     . VAL A 1 4337 ? 186.461 139.491 183.009 1.00 87.74  ? 4337 VAL A N     1 
ATOM   19483 C CA    . VAL A 1 4337 ? 185.195 140.206 183.130 1.00 87.74  ? 4337 VAL A CA    1 
ATOM   19484 C C     . VAL A 1 4337 ? 184.690 140.624 181.756 1.00 87.74  ? 4337 VAL A C     1 
ATOM   19485 O O     . VAL A 1 4337 ? 183.490 140.550 181.470 1.00 87.74  ? 4337 VAL A O     1 
ATOM   19486 C CB    . VAL A 1 4337 ? 185.351 141.412 184.072 1.00 87.74  ? 4337 VAL A CB    1 
ATOM   19487 C CG1   . VAL A 1 4337 ? 184.122 142.298 184.008 1.00 87.74  ? 4337 VAL A CG1   1 
ATOM   19488 C CG2   . VAL A 1 4337 ? 185.594 140.938 185.489 1.00 87.74  ? 4337 VAL A CG2   1 
ATOM   19489 N N     . ASP A 1 4338 ? 185.598 141.069 180.885 1.00 94.86  ? 4338 ASP A N     1 
ATOM   19490 C CA    . ASP A 1 4338 ? 185.199 141.476 179.540 1.00 94.86  ? 4338 ASP A CA    1 
ATOM   19491 C C     . ASP A 1 4338 ? 184.653 140.301 178.740 1.00 94.86  ? 4338 ASP A C     1 
ATOM   19492 O O     . ASP A 1 4338 ? 183.669 140.446 178.007 1.00 94.86  ? 4338 ASP A O     1 
ATOM   19493 C CB    . ASP A 1 4338 ? 186.379 142.112 178.809 1.00 94.86  ? 4338 ASP A CB    1 
ATOM   19494 C CG    . ASP A 1 4338 ? 186.366 143.623 178.889 1.00 94.86  ? 4338 ASP A CG    1 
ATOM   19495 O OD1   . ASP A 1 4338 ? 185.262 144.203 178.949 1.00 94.86  ? 4338 ASP A OD1   1 
ATOM   19496 O OD2   . ASP A 1 4338 ? 187.457 144.231 178.890 1.00 94.86  ? 4338 ASP A OD2   1 
ATOM   19497 N N     . MET A 1 4339 ? 185.290 139.135 178.848 1.00 90.59  ? 4339 MET A N     1 
ATOM   19498 C CA    . MET A 1 4339 ? 184.788 137.959 178.146 1.00 90.59  ? 4339 MET A CA    1 
ATOM   19499 C C     . MET A 1 4339 ? 183.418 137.557 178.674 1.00 90.59  ? 4339 MET A C     1 
ATOM   19500 O O     . MET A 1 4339 ? 182.526 137.196 177.897 1.00 90.59  ? 4339 MET A O     1 
ATOM   19501 C CB    . MET A 1 4339 ? 185.782 136.805 178.273 1.00 90.59  ? 4339 MET A CB    1 
ATOM   19502 C CG    . MET A 1 4339 ? 185.187 135.434 178.022 1.00 90.59  ? 4339 MET A CG    1 
ATOM   19503 S SD    . MET A 1 4339 ? 184.707 134.589 179.537 1.00 90.59  ? 4339 MET A SD    1 
ATOM   19504 C CE    . MET A 1 4339 ? 185.989 133.348 179.654 1.00 90.59  ? 4339 MET A CE    1 
ATOM   19505 N N     . ILE A 1 4340 ? 183.229 137.623 179.994 1.00 90.28  ? 4340 ILE A N     1 
ATOM   19506 C CA    . ILE A 1 4340 ? 181.916 137.346 180.571 1.00 90.28  ? 4340 ILE A CA    1 
ATOM   19507 C C     . ILE A 1 4340 ? 180.881 138.312 180.016 1.00 90.28  ? 4340 ILE A C     1 
ATOM   19508 O O     . ILE A 1 4340 ? 179.767 137.918 179.651 1.00 90.28  ? 4340 ILE A O     1 
ATOM   19509 C CB    . ILE A 1 4340 ? 181.978 137.421 182.106 1.00 90.28  ? 4340 ILE A CB    1 
ATOM   19510 C CG1   . ILE A 1 4340 ? 182.843 136.296 182.657 1.00 90.28  ? 4340 ILE A CG1   1 
ATOM   19511 C CG2   . ILE A 1 4340 ? 180.584 137.351 182.695 1.00 90.28  ? 4340 ILE A CG2   1 
ATOM   19512 C CD1   . ILE A 1 4340 ? 182.379 134.944 182.227 1.00 90.28  ? 4340 ILE A CD1   1 
ATOM   19513 N N     . SER A 1 4341 ? 181.233 139.596 179.956 1.00 96.50  ? 4341 SER A N     1 
ATOM   19514 C CA    . SER A 1 4341 ? 180.298 140.602 179.468 1.00 96.50  ? 4341 SER A CA    1 
ATOM   19515 C C     . SER A 1 4341 ? 179.949 140.371 178.004 1.00 96.50  ? 4341 SER A C     1 
ATOM   19516 O O     . SER A 1 4341 ? 178.786 140.501 177.609 1.00 96.50  ? 4341 SER A O     1 
ATOM   19517 C CB    . SER A 1 4341 ? 180.885 141.997 179.673 1.00 96.50  ? 4341 SER A CB    1 
ATOM   19518 O OG    . SER A 1 4341 ? 181.337 142.158 181.006 1.00 96.50  ? 4341 SER A OG    1 
ATOM   19519 N N     . LYS A 1 4342 ? 180.941 140.028 177.183 1.00 90.40  ? 4342 LYS A N     1 
ATOM   19520 C CA    . LYS A 1 4342 ? 180.670 139.729 175.781 1.00 90.40  ? 4342 LYS A CA    1 
ATOM   19521 C C     . LYS A 1 4342 ? 179.762 138.516 175.643 1.00 90.40  ? 4342 LYS A C     1 
ATOM   19522 O O     . LYS A 1 4342 ? 178.814 138.524 174.848 1.00 90.40  ? 4342 LYS A O     1 
ATOM   19523 C CB    . LYS A 1 4342 ? 181.979 139.497 175.033 1.00 90.40  ? 4342 LYS A CB    1 
ATOM   19524 C CG    . LYS A 1 4342 ? 182.821 140.740 174.846 1.00 90.40  ? 4342 LYS A CG    1 
ATOM   19525 C CD    . LYS A 1 4342 ? 184.224 140.378 174.396 1.00 90.40  ? 4342 LYS A CD    1 
ATOM   19526 C CE    . LYS A 1 4342 ? 185.241 141.372 174.912 1.00 90.40  ? 4342 LYS A CE    1 
ATOM   19527 N NZ    . LYS A 1 4342 ? 185.570 142.381 173.873 1.00 90.40  ? 4342 LYS A NZ    1 
ATOM   19528 N N     . MET A 1 4343 ? 180.034 137.464 176.414 1.00 93.31  ? 4343 MET A N     1 
ATOM   19529 C CA    . MET A 1 4343 ? 179.234 136.250 176.313 1.00 93.31  ? 4343 MET A CA    1 
ATOM   19530 C C     . MET A 1 4343 ? 177.808 136.490 176.785 1.00 93.31  ? 4343 MET A C     1 
ATOM   19531 O O     . MET A 1 4343 ? 176.862 135.890 176.262 1.00 93.31  ? 4343 MET A O     1 
ATOM   19532 C CB    . MET A 1 4343 ? 179.912 135.131 177.097 1.00 93.31  ? 4343 MET A CB    1 
ATOM   19533 C CG    . MET A 1 4343 ? 179.677 133.761 176.526 1.00 93.31  ? 4343 MET A CG    1 
ATOM   19534 S SD    . MET A 1 4343 ? 180.821 132.543 177.191 1.00 93.31  ? 4343 MET A SD    1 
ATOM   19535 C CE    . MET A 1 4343 ? 180.499 132.683 178.937 1.00 93.31  ? 4343 MET A CE    1 
ATOM   19536 N N     . LEU A 1 4344 ? 177.630 137.370 177.770 1.00 94.32  ? 4344 LEU A N     1 
ATOM   19537 C CA    . LEU A 1 4344 ? 176.283 137.774 178.156 1.00 94.32  ? 4344 LEU A CA    1 
ATOM   19538 C C     . LEU A 1 4344 ? 175.615 138.579 177.051 1.00 94.32  ? 4344 LEU A C     1 
ATOM   19539 O O     . LEU A 1 4344 ? 174.438 138.364 176.742 1.00 94.32  ? 4344 LEU A O     1 
ATOM   19540 C CB    . LEU A 1 4344 ? 176.327 138.575 179.453 1.00 94.32  ? 4344 LEU A CB    1 
ATOM   19541 C CG    . LEU A 1 4344 ? 175.699 137.875 180.653 1.00 94.32  ? 4344 LEU A CG    1 
ATOM   19542 C CD1   . LEU A 1 4344 ? 175.560 138.839 181.816 1.00 94.32  ? 4344 LEU A CD1   1 
ATOM   19543 C CD2   . LEU A 1 4344 ? 174.351 137.309 180.255 1.00 94.32  ? 4344 LEU A CD2   1 
ATOM   19544 N N     . LYS A 1 4345 ? 176.354 139.505 176.436 1.00 95.32  ? 4345 LYS A N     1 
ATOM   19545 C CA    . LYS A 1 4345 ? 175.829 140.302 175.335 1.00 95.32  ? 4345 LYS A CA    1 
ATOM   19546 C C     . LYS A 1 4345 ? 175.499 139.456 174.119 1.00 95.32  ? 4345 LYS A C     1 
ATOM   19547 O O     . LYS A 1 4345 ? 174.776 139.924 173.233 1.00 95.32  ? 4345 LYS A O     1 
ATOM   19548 C CB    . LYS A 1 4345 ? 176.834 141.386 174.945 1.00 95.32  ? 4345 LYS A CB    1 
ATOM   19549 C CG    . LYS A 1 4345 ? 176.214 142.590 174.259 1.00 95.32  ? 4345 LYS A CG    1 
ATOM   19550 C CD    . LYS A 1 4345 ? 177.259 143.639 173.946 1.00 95.32  ? 4345 LYS A CD    1 
ATOM   19551 C CE    . LYS A 1 4345 ? 178.008 143.284 172.674 1.00 95.32  ? 4345 LYS A CE    1 
ATOM   19552 N NZ    . LYS A 1 4345 ? 179.335 143.953 172.608 1.00 95.32  ? 4345 LYS A NZ    1 
ATOM   19553 N N     . MET A 1 4346 ? 176.013 138.233 174.056 1.00 97.00  ? 4346 MET A N     1 
ATOM   19554 C CA    . MET A 1 4346 ? 175.725 137.338 172.947 1.00 97.00  ? 4346 MET A CA    1 
ATOM   19555 C C     . MET A 1 4346 ? 174.662 136.318 173.324 1.00 97.00  ? 4346 MET A C     1 
ATOM   19556 O O     . MET A 1 4346 ? 174.719 135.165 172.886 1.00 97.00  ? 4346 MET A O     1 
ATOM   19557 C CB    . MET A 1 4346 ? 176.994 136.616 172.508 1.00 97.00  ? 4346 MET A CB    1 
ATOM   19558 C CG    . MET A 1 4346 ? 177.725 137.280 171.388 1.00 97.00  ? 4346 MET A CG    1 
ATOM   19559 S SD    . MET A 1 4346 ? 176.898 136.896 169.849 1.00 97.00  ? 4346 MET A SD    1 
ATOM   19560 C CE    . MET A 1 4346 ? 178.160 135.894 169.094 1.00 97.00  ? 4346 MET A CE    1 
ATOM   19561 N N     . GLN A 1 4347 ? 173.693 136.721 174.134 1.00 95.31  ? 4347 GLN A N     1 
ATOM   19562 C CA    . GLN A 1 4347 ? 172.651 135.791 174.531 1.00 95.31  ? 4347 GLN A CA    1 
ATOM   19563 C C     . GLN A 1 4347 ? 171.295 136.265 174.009 1.00 95.31  ? 4347 GLN A C     1 
ATOM   19564 O O     . GLN A 1 4347 ? 170.338 135.497 173.945 0.00 95.31  ? 4347 GLN A O     1 
ATOM   19565 C CB    . GLN A 1 4347 ? 172.621 135.634 176.050 1.00 95.31  ? 4347 GLN A CB    1 
ATOM   19566 C CG    . GLN A 1 4347 ? 171.953 134.361 176.513 1.00 95.31  ? 4347 GLN A CG    1 
ATOM   19567 C CD    . GLN A 1 4347 ? 172.935 133.206 176.611 1.00 95.31  ? 4347 GLN A CD    1 
ATOM   19568 O OE1   . GLN A 1 4347 ? 173.853 133.083 175.799 1.00 95.31  ? 4347 GLN A OE1   1 
ATOM   19569 N NE2   . GLN A 1 4347 ? 172.741 132.348 177.606 1.00 95.31  ? 4347 GLN A NE2   1 
ATOM   19570 N N     . ALA A 1 4375 ? 158.521 137.188 175.691 1.00 127.50 ? 4375 ALA A N     1 
ATOM   19571 C CA    . ALA A 1 4375 ? 159.045 136.309 176.729 1.00 127.50 ? 4375 ALA A CA    1 
ATOM   19572 C C     . ALA A 1 4375 ? 159.818 137.104 177.768 1.00 127.50 ? 4375 ALA A C     1 
ATOM   19573 O O     . ALA A 1 4375 ? 159.989 136.659 178.902 1.00 127.50 ? 4375 ALA A O     1 
ATOM   19574 C CB    . ALA A 1 4375 ? 159.928 135.235 176.121 1.00 127.50 ? 4375 ALA A CB    1 
ATOM   19575 N N     . TRP A 1 4376 ? 160.289 138.286 177.374 1.00 132.05 ? 4376 TRP A N     1 
ATOM   19576 C CA    . TRP A 1 4376 ? 161.033 139.139 178.289 1.00 132.05 ? 4376 TRP A CA    1 
ATOM   19577 C C     . TRP A 1 4376 ? 160.131 139.991 179.170 1.00 132.05 ? 4376 TRP A C     1 
ATOM   19578 O O     . TRP A 1 4376 ? 160.637 140.672 180.071 1.00 132.05 ? 4376 TRP A O     1 
ATOM   19579 C CB    . TRP A 1 4376 ? 161.993 140.038 177.507 1.00 132.05 ? 4376 TRP A CB    1 
ATOM   19580 C CG    . TRP A 1 4376 ? 161.347 140.779 176.386 1.00 132.05 ? 4376 TRP A CG    1 
ATOM   19581 C CD1   . TRP A 1 4376 ? 161.181 140.344 175.106 1.00 132.05 ? 4376 TRP A CD1   1 
ATOM   19582 C CD2   . TRP A 1 4376 ? 160.790 142.096 176.438 1.00 132.05 ? 4376 TRP A CD2   1 
ATOM   19583 N NE1   . TRP A 1 4376 ? 160.550 141.307 174.357 1.00 132.05 ? 4376 TRP A NE1   1 
ATOM   19584 C CE2   . TRP A 1 4376 ? 160.300 142.393 175.153 1.00 132.05 ? 4376 TRP A CE2   1 
ATOM   19585 C CE3   . TRP A 1 4376 ? 160.658 143.052 177.447 1.00 132.05 ? 4376 TRP A CE3   1 
ATOM   19586 C CZ2   . TRP A 1 4376 ? 159.687 143.605 174.850 1.00 132.05 ? 4376 TRP A CZ2   1 
ATOM   19587 C CZ3   . TRP A 1 4376 ? 160.052 144.254 177.145 1.00 132.05 ? 4376 TRP A CZ3   1 
ATOM   19588 C CH2   . TRP A 1 4376 ? 159.573 144.520 175.857 1.00 132.05 ? 4376 TRP A CH2   1 
ATOM   19589 N N     . MET A 1 4377 ? 158.817 139.959 178.942 1.00 129.85 ? 4377 MET A N     1 
ATOM   19590 C CA    . MET A 1 4377 ? 157.897 140.732 179.768 1.00 129.85 ? 4377 MET A CA    1 
ATOM   19591 C C     . MET A 1 4377 ? 158.014 140.338 181.234 1.00 129.85 ? 4377 MET A C     1 
ATOM   19592 O O     . MET A 1 4377 ? 158.136 141.197 182.113 1.00 129.85 ? 4377 MET A O     1 
ATOM   19593 C CB    . MET A 1 4377 ? 156.462 140.527 179.279 1.00 129.85 ? 4377 MET A CB    1 
ATOM   19594 C CG    . MET A 1 4377 ? 155.531 141.718 179.474 1.00 129.85 ? 4377 MET A CG    1 
ATOM   19595 S SD    . MET A 1 4377 ? 156.178 143.335 179.002 1.00 129.85 ? 4377 MET A SD    1 
ATOM   19596 C CE    . MET A 1 4377 ? 156.848 142.992 177.377 1.00 129.85 ? 4377 MET A CE    1 
ATOM   19597 N N     . ARG A 1 4378 ? 157.991 139.033 181.513 1.00 129.32 ? 4378 ARG A N     1 
ATOM   19598 C CA    . ARG A 1 4378 ? 157.964 138.565 182.895 1.00 129.32 ? 4378 ARG A CA    1 
ATOM   19599 C C     . ARG A 1 4378 ? 159.283 138.838 183.607 1.00 129.32 ? 4378 ARG A C     1 
ATOM   19600 O O     . ARG A 1 4378 ? 159.291 139.262 184.771 1.00 129.32 ? 4378 ARG A O     1 
ATOM   19601 C CB    . ARG A 1 4378 ? 157.619 137.074 182.938 1.00 129.32 ? 4378 ARG A CB    1 
ATOM   19602 C CG    . ARG A 1 4378 ? 156.324 136.700 182.212 1.00 129.32 ? 4378 ARG A CG    1 
ATOM   19603 C CD    . ARG A 1 4378 ? 156.547 136.382 180.736 1.00 129.32 ? 4378 ARG A CD    1 
ATOM   19604 N NE    . ARG A 1 4378 ? 155.302 136.069 180.043 1.00 129.32 ? 4378 ARG A NE    1 
ATOM   19605 C CZ    . ARG A 1 4378 ? 155.089 136.281 178.750 1.00 129.32 ? 4378 ARG A CZ    1 
ATOM   19606 N NH1   . ARG A 1 4378 ? 156.019 136.813 177.975 1.00 129.32 ? 4378 ARG A NH1   1 
ATOM   19607 N NH2   . ARG A 1 4378 ? 153.914 135.952 178.223 1.00 129.32 ? 4378 ARG A NH2   1 
ATOM   19608 N N     . THR A 1 4379 ? 160.410 138.597 182.933 1.00 130.55 ? 4379 THR A N     1 
ATOM   19609 C CA    . THR A 1 4379 ? 161.696 138.869 183.565 1.00 130.55 ? 4379 THR A CA    1 
ATOM   19610 C C     . THR A 1 4379 ? 161.895 140.364 183.779 1.00 130.55 ? 4379 THR A C     1 
ATOM   19611 O O     . THR A 1 4379 ? 162.433 140.781 184.811 1.00 130.55 ? 4379 THR A O     1 
ATOM   19612 C CB    . THR A 1 4379 ? 162.842 138.271 182.745 1.00 130.55 ? 4379 THR A CB    1 
ATOM   19613 O OG1   . THR A 1 4379 ? 164.095 138.623 183.346 1.00 130.55 ? 4379 THR A OG1   1 
ATOM   19614 C CG2   . THR A 1 4379 ? 162.819 138.771 181.320 1.00 130.55 ? 4379 THR A CG2   1 
ATOM   19615 N N     . LEU A 1 4380 ? 161.446 141.191 182.831 1.00 130.96 ? 4380 LEU A N     1 
ATOM   19616 C CA    . LEU A 1 4380 ? 161.514 142.632 183.041 1.00 130.96 ? 4380 LEU A CA    1 
ATOM   19617 C C     . LEU A 1 4380 ? 160.653 143.051 184.225 1.00 130.96 ? 4380 LEU A C     1 
ATOM   19618 O O     . LEU A 1 4380 ? 161.068 143.883 185.039 1.00 130.96 ? 4380 LEU A O     1 
ATOM   19619 C CB    . LEU A 1 4380 ? 161.085 143.375 181.778 1.00 130.96 ? 4380 LEU A CB    1 
ATOM   19620 C CG    . LEU A 1 4380 ? 161.248 144.893 181.853 1.00 130.96 ? 4380 LEU A CG    1 
ATOM   19621 C CD1   . LEU A 1 4380 ? 162.642 145.250 182.339 1.00 130.96 ? 4380 LEU A CD1   1 
ATOM   19622 C CD2   . LEU A 1 4380 ? 160.963 145.538 180.508 1.00 130.96 ? 4380 LEU A CD2   1 
ATOM   19623 N N     . HIS A 1 4381 ? 159.453 142.478 184.340 1.00 134.22 ? 4381 HIS A N     1 
ATOM   19624 C CA    . HIS A 1 4381 ? 158.577 142.801 185.459 1.00 134.22 ? 4381 HIS A CA    1 
ATOM   19625 C C     . HIS A 1 4381 ? 159.218 142.437 186.790 1.00 134.22 ? 4381 HIS A C     1 
ATOM   19626 O O     . HIS A 1 4381 ? 159.205 143.235 187.736 1.00 134.22 ? 4381 HIS A O     1 
ATOM   19627 C CB    . HIS A 1 4381 ? 157.236 142.087 185.297 1.00 134.22 ? 4381 HIS A CB    1 
ATOM   19628 C CG    . HIS A 1 4381 ? 156.125 142.704 186.086 1.00 134.22 ? 4381 HIS A CG    1 
ATOM   19629 N ND1   . HIS A 1 4381 ? 155.668 143.983 185.859 1.00 134.22 ? 4381 HIS A ND1   1 
ATOM   19630 C CD2   . HIS A 1 4381 ? 155.377 142.213 187.103 1.00 134.22 ? 4381 HIS A CD2   1 
ATOM   19631 C CE1   . HIS A 1 4381 ? 154.689 144.256 186.703 1.00 134.22 ? 4381 HIS A CE1   1 
ATOM   19632 N NE2   . HIS A 1 4381 ? 154.491 143.197 187.466 1.00 134.22 ? 4381 HIS A NE2   1 
ATOM   19633 N N     . THR A 1 4382 ? 159.783 141.233 186.887 1.00 129.67 ? 4382 THR A N     1 
ATOM   19634 C CA    . THR A 1 4382 ? 160.358 140.825 188.165 1.00 129.67 ? 4382 THR A CA    1 
ATOM   19635 C C     . THR A 1 4382 ? 161.610 141.633 188.489 1.00 129.67 ? 4382 THR A C     1 
ATOM   19636 O O     . THR A 1 4382 ? 161.850 141.968 189.654 1.00 129.67 ? 4382 THR A O     1 
ATOM   19637 C CB    . THR A 1 4382 ? 160.641 139.320 188.183 1.00 129.67 ? 4382 THR A CB    1 
ATOM   19638 O OG1   . THR A 1 4382 ? 161.023 138.925 189.506 1.00 129.67 ? 4382 THR A OG1   1 
ATOM   19639 C CG2   . THR A 1 4382 ? 161.742 138.940 187.210 1.00 129.67 ? 4382 THR A CG2   1 
ATOM   19640 N N     . THR A 1 4383 ? 162.402 141.990 187.472 1.00 124.62 ? 4383 THR A N     1 
ATOM   19641 C CA    . THR A 1 4383 ? 163.564 142.837 187.717 1.00 124.62 ? 4383 THR A CA    1 
ATOM   19642 C C     . THR A 1 4383 ? 163.144 144.217 188.203 1.00 124.62 ? 4383 THR A C     1 
ATOM   19643 O O     . THR A 1 4383 ? 163.746 144.766 189.134 1.00 124.62 ? 4383 THR A O     1 
ATOM   19644 C CB    . THR A 1 4383 ? 164.407 142.950 186.447 1.00 124.62 ? 4383 THR A CB    1 
ATOM   19645 O OG1   . THR A 1 4383 ? 164.532 141.659 185.840 1.00 124.62 ? 4383 THR A OG1   1 
ATOM   19646 C CG2   . THR A 1 4383 ? 165.790 143.481 186.776 1.00 124.62 ? 4383 THR A CG2   1 
ATOM   19647 N N     . ALA A 1 4384 ? 162.109 144.792 187.588 1.00 120.53 ? 4384 ALA A N     1 
ATOM   19648 C CA    . ALA A 1 4384 ? 161.636 146.105 188.009 1.00 120.53 ? 4384 ALA A CA    1 
ATOM   19649 C C     . ALA A 1 4384 ? 161.081 146.063 189.425 1.00 120.53 ? 4384 ALA A C     1 
ATOM   19650 O O     . ALA A 1 4384 ? 161.313 146.983 190.217 1.00 120.53 ? 4384 ALA A O     1 
ATOM   19651 C CB    . ALA A 1 4384 ? 160.582 146.621 187.032 1.00 120.53 ? 4384 ALA A CB    1 
ATOM   19652 N N     . SER A 1 4385 ? 160.340 145.007 189.763 1.00 125.42 ? 4385 SER A N     1 
ATOM   19653 C CA    . SER A 1 4385 ? 159.828 144.880 191.124 1.00 125.42 ? 4385 SER A CA    1 
ATOM   19654 C C     . SER A 1 4385 ? 160.967 144.732 192.126 1.00 125.42 ? 4385 SER A C     1 
ATOM   19655 O O     . SER A 1 4385 ? 160.928 145.320 193.215 1.00 125.42 ? 4385 SER A O     1 
ATOM   19656 C CB    . SER A 1 4385 ? 158.869 143.695 191.215 1.00 125.42 ? 4385 SER A CB    1 
ATOM   19657 O OG    . SER A 1 4385 ? 159.501 142.499 190.799 1.00 125.42 ? 4385 SER A OG    1 
ATOM   19658 N N     . ASN A 1 4386 ? 161.994 143.955 191.773 1.00 126.00 ? 4386 ASN A N     1 
ATOM   19659 C CA    . ASN A 1 4386 ? 163.151 143.821 192.650 1.00 126.00 ? 4386 ASN A CA    1 
ATOM   19660 C C     . ASN A 1 4386 ? 163.842 145.162 192.851 1.00 126.00 ? 4386 ASN A C     1 
ATOM   19661 O O     . ASN A 1 4386 ? 164.243 145.501 193.970 1.00 126.00 ? 4386 ASN A O     1 
ATOM   19662 C CB    . ASN A 1 4386 ? 164.128 142.796 192.077 1.00 126.00 ? 4386 ASN A CB    1 
ATOM   19663 C CG    . ASN A 1 4386 ? 163.596 141.382 192.151 1.00 126.00 ? 4386 ASN A CG    1 
ATOM   19664 O OD1   . ASN A 1 4386 ? 162.772 141.063 193.006 1.00 126.00 ? 4386 ASN A OD1   1 
ATOM   19665 N ND2   . ASN A 1 4386 ? 164.063 140.526 191.252 1.00 126.00 ? 4386 ASN A ND2   1 
ATOM   19666 N N     . TRP A 1 4387 ? 163.987 145.940 191.778 1.00 114.69 ? 4387 TRP A N     1 
ATOM   19667 C CA    . TRP A 1 4387 ? 164.630 147.244 191.898 1.00 114.69 ? 4387 TRP A CA    1 
ATOM   19668 C C     . TRP A 1 4387 ? 163.794 148.199 192.738 1.00 114.69 ? 4387 TRP A C     1 
ATOM   19669 O O     . TRP A 1 4387 ? 164.338 148.986 193.520 1.00 114.69 ? 4387 TRP A O     1 
ATOM   19670 C CB    . TRP A 1 4387 ? 164.893 147.826 190.514 1.00 114.69 ? 4387 TRP A CB    1 
ATOM   19671 C CG    . TRP A 1 4387 ? 165.995 147.125 189.813 1.00 114.69 ? 4387 TRP A CG    1 
ATOM   19672 C CD1   . TRP A 1 4387 ? 166.871 146.238 190.357 1.00 114.69 ? 4387 TRP A CD1   1 
ATOM   19673 C CD2   . TRP A 1 4387 ? 166.350 147.247 188.434 1.00 114.69 ? 4387 TRP A CD2   1 
ATOM   19674 N NE1   . TRP A 1 4387 ? 167.750 145.796 189.403 1.00 114.69 ? 4387 TRP A NE1   1 
ATOM   19675 C CE2   . TRP A 1 4387 ? 167.452 146.402 188.212 1.00 114.69 ? 4387 TRP A CE2   1 
ATOM   19676 C CE3   . TRP A 1 4387 ? 165.843 147.988 187.366 1.00 114.69 ? 4387 TRP A CE3   1 
ATOM   19677 C CZ2   . TRP A 1 4387 ? 168.056 146.277 186.966 1.00 114.69 ? 4387 TRP A CZ2   1 
ATOM   19678 C CZ3   . TRP A 1 4387 ? 166.444 147.864 186.131 1.00 114.69 ? 4387 TRP A CZ3   1 
ATOM   19679 C CH2   . TRP A 1 4387 ? 167.539 147.015 185.941 1.00 114.69 ? 4387 TRP A CH2   1 
ATOM   19680 N N     . LEU A 1 4388 ? 162.470 148.149 192.587 1.00 114.89 ? 4388 LEU A N     1 
ATOM   19681 C CA    . LEU A 1 4388 ? 161.607 148.971 193.424 1.00 114.89 ? 4388 LEU A CA    1 
ATOM   19682 C C     . LEU A 1 4388 ? 161.753 148.601 194.892 1.00 114.89 ? 4388 LEU A C     1 
ATOM   19683 O O     . LEU A 1 4388 ? 161.818 149.480 195.759 1.00 114.89 ? 4388 LEU A O     1 
ATOM   19684 C CB    . LEU A 1 4388 ? 160.155 148.832 192.977 1.00 114.89 ? 4388 LEU A CB    1 
ATOM   19685 C CG    . LEU A 1 4388 ? 159.841 149.499 191.642 1.00 114.89 ? 4388 LEU A CG    1 
ATOM   19686 C CD1   . LEU A 1 4388 ? 158.347 149.706 191.488 1.00 114.89 ? 4388 LEU A CD1   1 
ATOM   19687 C CD2   . LEU A 1 4388 ? 160.574 150.817 191.556 1.00 114.89 ? 4388 LEU A CD2   1 
ATOM   19688 N N     . HIS A 1 4389 ? 161.808 147.303 195.192 1.00 115.98 ? 4389 HIS A N     1 
ATOM   19689 C CA    . HIS A 1 4389 ? 162.052 146.890 196.570 1.00 115.98 ? 4389 HIS A CA    1 
ATOM   19690 C C     . HIS A 1 4389 ? 163.444 147.293 197.034 1.00 115.98 ? 4389 HIS A C     1 
ATOM   19691 O O     . HIS A 1 4389 ? 163.668 147.480 198.235 1.00 115.98 ? 4389 HIS A O     1 
ATOM   19692 C CB    . HIS A 1 4389 ? 161.862 145.382 196.715 1.00 115.98 ? 4389 HIS A CB    1 
ATOM   19693 C CG    . HIS A 1 4389 ? 161.340 144.969 198.055 1.00 115.98 ? 4389 HIS A CG    1 
ATOM   19694 N ND1   . HIS A 1 4389 ? 162.161 144.774 199.145 1.00 115.98 ? 4389 HIS A ND1   1 
ATOM   19695 C CD2   . HIS A 1 4389 ? 160.080 144.719 198.485 1.00 115.98 ? 4389 HIS A CD2   1 
ATOM   19696 C CE1   . HIS A 1 4389 ? 161.431 144.418 200.186 1.00 115.98 ? 4389 HIS A CE1   1 
ATOM   19697 N NE2   . HIS A 1 4389 ? 160.165 144.378 199.813 1.00 115.98 ? 4389 HIS A NE2   1 
ATOM   19698 N N     . LEU A 1 4390 ? 164.387 147.434 196.104 1.00 110.74 ? 4390 LEU A N     1 
ATOM   19699 C CA    . LEU A 1 4390 ? 165.763 147.744 196.472 1.00 110.74 ? 4390 LEU A CA    1 
ATOM   19700 C C     . LEU A 1 4390 ? 165.957 149.239 196.697 1.00 110.74 ? 4390 LEU A C     1 
ATOM   19701 O O     . LEU A 1 4390 ? 166.491 149.653 197.731 1.00 110.74 ? 4390 LEU A O     1 
ATOM   19702 C CB    . LEU A 1 4390 ? 166.712 147.217 195.391 1.00 110.74 ? 4390 LEU A CB    1 
ATOM   19703 C CG    . LEU A 1 4390 ? 168.216 147.488 195.451 1.00 110.74 ? 4390 LEU A CG    1 
ATOM   19704 C CD1   . LEU A 1 4390 ? 168.959 146.364 194.759 1.00 110.74 ? 4390 LEU A CD1   1 
ATOM   19705 C CD2   . LEU A 1 4390 ? 168.559 148.798 194.775 1.00 110.74 ? 4390 LEU A CD2   1 
ATOM   19706 N N     . ILE A 1 4391 ? 165.535 150.058 195.742 1.00 107.79 ? 4391 ILE A N     1 
ATOM   19707 C CA    . ILE A 1 4391 ? 165.722 151.509 195.858 1.00 107.79 ? 4391 ILE A CA    1 
ATOM   19708 C C     . ILE A 1 4391 ? 164.874 152.036 197.007 1.00 107.79 ? 4391 ILE A C     1 
ATOM   19709 O O     . ILE A 1 4391 ? 163.715 151.611 197.161 1.00 107.79 ? 4391 ILE A O     1 
ATOM   19710 C CB    . ILE A 1 4391 ? 165.352 152.197 194.544 1.00 107.79 ? 4391 ILE A CB    1 
ATOM   19711 C CG1   . ILE A 1 4391 ? 166.221 151.680 193.404 1.00 107.79 ? 4391 ILE A CG1   1 
ATOM   19712 C CG2   . ILE A 1 4391 ? 165.511 153.694 194.663 1.00 107.79 ? 4391 ILE A CG2   1 
ATOM   19713 C CD1   . ILE A 1 4391 ? 165.922 152.343 192.084 1.00 107.79 ? 4391 ILE A CD1   1 
ATOM   19714 N N     . PRO A 1 4392 ? 165.394 152.937 197.839 1.00 109.86 ? 4392 PRO A N     1 
ATOM   19715 C CA    . PRO A 1 4392 ? 164.546 153.578 198.847 1.00 109.86 ? 4392 PRO A CA    1 
ATOM   19716 C C     . PRO A 1 4392 ? 163.418 154.353 198.187 1.00 109.86 ? 4392 PRO A C     1 
ATOM   19717 O O     . PRO A 1 4392 ? 163.550 154.855 197.070 1.00 109.86 ? 4392 PRO A O     1 
ATOM   19718 C CB    . PRO A 1 4392 ? 165.512 154.509 199.585 1.00 109.86 ? 4392 PRO A CB    1 
ATOM   19719 C CG    . PRO A 1 4392 ? 166.848 153.896 199.371 1.00 109.86 ? 4392 PRO A CG    1 
ATOM   19720 C CD    . PRO A 1 4392 ? 166.809 153.306 197.996 1.00 109.86 ? 4392 PRO A CD    1 
ATOM   19721 N N     . GLN A 1 4393 ? 162.288 154.427 198.891 1.00 121.39 ? 4393 GLN A N     1 
ATOM   19722 C CA    . GLN A 1 4393 ? 161.077 154.980 198.296 1.00 121.39 ? 4393 GLN A CA    1 
ATOM   19723 C C     . GLN A 1 4393 ? 161.254 156.446 197.920 1.00 121.39 ? 4393 GLN A C     1 
ATOM   19724 O O     . GLN A 1 4393 ? 161.209 156.806 196.739 1.00 121.39 ? 4393 GLN A O     1 
ATOM   19725 C CB    . GLN A 1 4393 ? 159.901 154.799 199.254 1.00 121.39 ? 4393 GLN A CB    1 
ATOM   19726 C CG    . GLN A 1 4393 ? 159.518 153.346 199.472 1.00 121.39 ? 4393 GLN A CG    1 
ATOM   19727 C CD    . GLN A 1 4393 ? 159.758 152.493 198.240 1.00 121.39 ? 4393 GLN A CD    1 
ATOM   19728 O OE1   . GLN A 1 4393 ? 159.113 152.678 197.209 1.00 121.39 ? 4393 GLN A OE1   1 
ATOM   19729 N NE2   . GLN A 1 4393 ? 160.695 151.558 198.341 1.00 121.39 ? 4393 GLN A NE2   1 
ATOM   19730 N N     . THR A 1 4394 ? 161.460 157.311 198.911 1.00 128.18 ? 4394 THR A N     1 
ATOM   19731 C CA    . THR A 1 4394 ? 161.480 158.741 198.640 1.00 128.18 ? 4394 THR A CA    1 
ATOM   19732 C C     . THR A 1 4394 ? 162.251 159.462 199.735 1.00 128.18 ? 4394 THR A C     1 
ATOM   19733 O O     . THR A 1 4394 ? 162.122 159.131 200.915 1.00 128.18 ? 4394 THR A O     1 
ATOM   19734 C CB    . THR A 1 4394 ? 160.053 159.302 198.535 1.00 128.18 ? 4394 THR A CB    1 
ATOM   19735 O OG1   . THR A 1 4394 ? 159.380 158.701 197.422 1.00 128.18 ? 4394 THR A OG1   1 
ATOM   19736 C CG2   . THR A 1 4394 ? 160.073 160.813 198.342 1.00 128.18 ? 4394 THR A CG2   1 
ATOM   19737 N N     . LEU A 1 4395 ? 163.051 160.446 199.328 1.00 123.58 ? 4395 LEU A N     1 
ATOM   19738 C CA    . LEU A 1 4395 ? 163.760 161.335 200.237 1.00 123.58 ? 4395 LEU A CA    1 
ATOM   19739 C C     . LEU A 1 4395 ? 163.297 162.762 199.984 1.00 123.58 ? 4395 LEU A C     1 
ATOM   19740 O O     . LEU A 1 4395 ? 163.226 163.197 198.830 1.00 123.58 ? 4395 LEU A O     1 
ATOM   19741 C CB    . LEU A 1 4395 ? 165.272 161.225 200.046 1.00 123.58 ? 4395 LEU A CB    1 
ATOM   19742 C CG    . LEU A 1 4395 ? 166.101 162.371 200.622 1.00 123.58 ? 4395 LEU A CG    1 
ATOM   19743 C CD1   . LEU A 1 4395 ? 165.957 162.431 202.137 1.00 123.58 ? 4395 LEU A CD1   1 
ATOM   19744 C CD2   . LEU A 1 4395 ? 167.556 162.222 200.219 1.00 123.58 ? 4395 LEU A CD2   1 
ATOM   19745 N N     . SER A 1 4396 ? 162.989 163.487 201.054 1.00 123.06 ? 4396 SER A N     1 
ATOM   19746 C CA    . SER A 1 4396 ? 162.432 164.827 200.951 1.00 123.06 ? 4396 SER A CA    1 
ATOM   19747 C C     . SER A 1 4396 ? 163.501 165.884 201.201 1.00 123.06 ? 4396 SER A C     1 
ATOM   19748 O O     . SER A 1 4396 ? 164.486 165.647 201.904 1.00 123.06 ? 4396 SER A O     1 
ATOM   19749 C CB    . SER A 1 4396 ? 161.284 165.016 201.941 1.00 123.06 ? 4396 SER A CB    1 
ATOM   19750 O OG    . SER A 1 4396 ? 161.767 165.035 203.272 1.00 123.06 ? 4396 SER A OG    1 
ATOM   19751 N N     . HIS A 1 4397 ? 163.285 167.063 200.621 1.00 123.79 ? 4397 HIS A N     1 
ATOM   19752 C CA    . HIS A 1 4397 ? 164.207 168.187 200.766 1.00 123.79 ? 4397 HIS A CA    1 
ATOM   19753 C C     . HIS A 1 4397 ? 163.931 168.857 202.104 1.00 123.79 ? 4397 HIS A C     1 
ATOM   19754 O O     . HIS A 1 4397 ? 163.182 169.833 202.175 1.00 123.79 ? 4397 HIS A O     1 
ATOM   19755 C CB    . HIS A 1 4397 ? 164.032 169.197 199.637 1.00 123.79 ? 4397 HIS A CB    1 
ATOM   19756 C CG    . HIS A 1 4397 ? 163.792 168.590 198.291 1.00 123.79 ? 4397 HIS A CG    1 
ATOM   19757 N ND1   . HIS A 1 4397 ? 163.223 169.299 197.256 1.00 123.79 ? 4397 HIS A ND1   1 
ATOM   19758 C CD2   . HIS A 1 4397 ? 164.055 167.356 197.801 1.00 123.79 ? 4397 HIS A CD2   1 
ATOM   19759 C CE1   . HIS A 1 4397 ? 163.134 168.524 196.190 1.00 123.79 ? 4397 HIS A CE1   1 
ATOM   19760 N NE2   . HIS A 1 4397 ? 163.632 167.340 196.494 1.00 123.79 ? 4397 HIS A NE2   1 
ATOM   19761 N N     . LEU A 1 4398 ? 164.531 168.347 203.177 1.00 130.23 ? 4398 LEU A N     1 
ATOM   19762 C CA    . LEU A 1 4398 ? 164.407 168.986 204.486 1.00 130.23 ? 4398 LEU A CA    1 
ATOM   19763 C C     . LEU A 1 4398 ? 165.554 169.983 204.600 1.00 130.23 ? 4398 LEU A C     1 
ATOM   19764 O O     . LEU A 1 4398 ? 166.581 169.730 205.227 1.00 130.23 ? 4398 LEU A O     1 
ATOM   19765 C CB    . LEU A 1 4398 ? 164.420 167.956 205.612 1.00 130.23 ? 4398 LEU A CB    1 
ATOM   19766 C CG    . LEU A 1 4398 ? 164.051 168.523 206.987 1.00 130.23 ? 4398 LEU A CG    1 
ATOM   19767 C CD1   . LEU A 1 4398 ? 162.995 167.658 207.662 1.00 130.23 ? 4398 LEU A CD1   1 
ATOM   19768 C CD2   . LEU A 1 4398 ? 165.274 168.674 207.880 1.00 130.23 ? 4398 LEU A CD2   1 
ATOM   19769 N N     . LYS A 1 4399 ? 165.367 171.137 203.968 1.00 118.01 ? 4399 LYS A N     1 
ATOM   19770 C CA    . LYS A 1 4399 ? 166.453 172.084 203.781 1.00 118.01 ? 4399 LYS A CA    1 
ATOM   19771 C C     . LYS A 1 4399 ? 165.880 173.498 203.758 1.00 118.01 ? 4399 LYS A C     1 
ATOM   19772 O O     . LYS A 1 4399 ? 164.743 173.736 204.176 1.00 118.01 ? 4399 LYS A O     1 
ATOM   19773 C CB    . LYS A 1 4399 ? 167.221 171.755 202.494 1.00 118.01 ? 4399 LYS A CB    1 
ATOM   19774 C CG    . LYS A 1 4399 ? 168.160 170.563 202.600 1.00 118.01 ? 4399 LYS A CG    1 
ATOM   19775 C CD    . LYS A 1 4399 ? 169.122 170.718 203.760 1.00 118.01 ? 4399 LYS A CD    1 
ATOM   19776 C CE    . LYS A 1 4399 ? 169.824 169.412 204.055 1.00 118.01 ? 4399 LYS A CE    1 
ATOM   19777 N NZ    . LYS A 1 4399 ? 168.992 168.553 204.937 1.00 118.01 ? 4399 LYS A NZ    1 
ATOM   19778 N N     . ARG A 1 4400 ? 166.694 174.438 203.273 1.00 123.74 ? 4400 ARG A N     1 
ATOM   19779 C CA    . ARG A 1 4400 ? 166.300 175.832 203.058 1.00 123.74 ? 4400 ARG A CA    1 
ATOM   19780 C C     . ARG A 1 4400 ? 165.837 176.497 204.351 1.00 123.74 ? 4400 ARG A C     1 
ATOM   19781 O O     . ARG A 1 4400 ? 164.693 176.937 204.481 1.00 123.74 ? 4400 ARG A O     1 
ATOM   19782 C CB    . ARG A 1 4400 ? 165.235 175.945 201.966 1.00 123.74 ? 4400 ARG A CB    1 
ATOM   19783 C CG    . ARG A 1 4400 ? 165.275 177.274 201.230 1.00 123.74 ? 4400 ARG A CG    1 
ATOM   19784 C CD    . ARG A 1 4400 ? 164.843 177.129 199.782 1.00 123.74 ? 4400 ARG A CD    1 
ATOM   19785 N NE    . ARG A 1 4400 ? 165.717 176.231 199.039 1.00 123.74 ? 4400 ARG A NE    1 
ATOM   19786 C CZ    . ARG A 1 4400 ? 166.927 176.555 198.604 1.00 123.74 ? 4400 ARG A CZ    1 
ATOM   19787 N NH1   . ARG A 1 4400 ? 167.444 177.753 198.823 1.00 123.74 ? 4400 ARG A NH1   1 
ATOM   19788 N NH2   . ARG A 1 4400 ? 167.636 175.654 197.930 1.00 123.74 ? 4400 ARG A NH2   1 
ATOM   19789 N N     . THR A 1 4401 ? 166.745 176.570 205.316 1.00 120.74 ? 4401 THR A N     1 
ATOM   19790 C CA    . THR A 1 4401 ? 166.530 177.349 206.525 1.00 120.74 ? 4401 THR A CA    1 
ATOM   19791 C C     . THR A 1 4401 ? 167.241 178.687 206.382 1.00 120.74 ? 4401 THR A C     1 
ATOM   19792 O O     . THR A 1 4401 ? 168.423 178.731 206.026 1.00 120.74 ? 4401 THR A O     1 
ATOM   19793 C CB    . THR A 1 4401 ? 167.046 176.600 207.753 1.00 120.74 ? 4401 THR A CB    1 
ATOM   19794 O OG1   . THR A 1 4401 ? 166.563 175.251 207.727 1.00 120.74 ? 4401 THR A OG1   1 
ATOM   19795 C CG2   . THR A 1 4401 ? 166.576 177.282 209.026 1.00 120.74 ? 4401 THR A CG2   1 
ATOM   19796 N N     . VAL A 1 4402 ? 166.518 179.777 206.652 1.00 123.16 ? 4402 VAL A N     1 
ATOM   19797 C CA    . VAL A 1 4402 ? 167.103 181.107 206.504 1.00 123.16 ? 4402 VAL A CA    1 
ATOM   19798 C C     . VAL A 1 4402 ? 168.298 181.269 207.432 1.00 123.16 ? 4402 VAL A C     1 
ATOM   19799 O O     . VAL A 1 4402 ? 169.348 181.788 207.034 1.00 123.16 ? 4402 VAL A O     1 
ATOM   19800 C CB    . VAL A 1 4402 ? 166.041 182.193 206.752 1.00 123.16 ? 4402 VAL A CB    1 
ATOM   19801 C CG1   . VAL A 1 4402 ? 166.673 183.574 206.693 1.00 123.16 ? 4402 VAL A CG1   1 
ATOM   19802 C CG2   . VAL A 1 4402 ? 164.922 182.075 205.731 1.00 123.16 ? 4402 VAL A CG2   1 
ATOM   19803 N N     . GLU A 1 4403 ? 168.161 180.835 208.678 1.00 122.23 ? 4403 GLU A N     1 
ATOM   19804 C CA    . GLU A 1 4403 ? 169.297 180.805 209.581 1.00 122.23 ? 4403 GLU A CA    1 
ATOM   19805 C C     . GLU A 1 4403 ? 170.179 179.603 209.261 1.00 122.23 ? 4403 GLU A C     1 
ATOM   19806 O O     . GLU A 1 4403 ? 169.702 178.569 208.784 1.00 122.23 ? 4403 GLU A O     1 
ATOM   19807 C CB    . GLU A 1 4403 ? 168.819 180.767 211.035 1.00 122.23 ? 4403 GLU A CB    1 
ATOM   19808 C CG    . GLU A 1 4403 ? 169.903 180.532 212.082 1.00 122.23 ? 4403 GLU A CG    1 
ATOM   19809 C CD    . GLU A 1 4403 ? 171.035 181.552 212.045 1.00 122.23 ? 4403 GLU A CD    1 
ATOM   19810 O OE1   . GLU A 1 4403 ? 172.054 181.317 212.728 1.00 122.23 ? 4403 GLU A OE1   1 
ATOM   19811 O OE2   . GLU A 1 4403 ? 170.908 182.595 211.368 1.00 122.23 ? 4403 GLU A OE2   1 
ATOM   19812 N N     . ASN A 1 4404 ? 171.482 179.763 209.503 1.00 120.78 ? 4404 ASN A N     1 
ATOM   19813 C CA    . ASN A 1 4404 ? 172.534 178.804 209.169 1.00 120.78 ? 4404 ASN A CA    1 
ATOM   19814 C C     . ASN A 1 4404 ? 172.751 178.661 207.670 1.00 120.78 ? 4404 ASN A C     1 
ATOM   19815 O O     . ASN A 1 4404 ? 173.500 177.775 207.245 1.00 120.78 ? 4404 ASN A O     1 
ATOM   19816 C CB    . ASN A 1 4404 ? 172.282 177.419 209.778 1.00 120.78 ? 4404 ASN A CB    1 
ATOM   19817 C CG    . ASN A 1 4404 ? 172.241 177.447 211.291 1.00 120.78 ? 4404 ASN A CG    1 
ATOM   19818 O OD1   . ASN A 1 4404 ? 172.215 178.512 211.904 1.00 120.78 ? 4404 ASN A OD1   1 
ATOM   19819 N ND2   . ASN A 1 4404 ? 172.236 176.269 211.904 1.00 120.78 ? 4404 ASN A ND2   1 
ATOM   19820 N N     . ILE A 1 4405 ? 172.134 179.517 206.853 1.00 109.91 ? 4405 ILE A N     1 
ATOM   19821 C CA    . ILE A 1 4405 ? 172.387 179.479 205.420 1.00 109.91 ? 4405 ILE A CA    1 
ATOM   19822 C C     . ILE A 1 4405 ? 173.821 179.876 205.100 1.00 109.91 ? 4405 ILE A C     1 
ATOM   19823 O O     . ILE A 1 4405 ? 174.319 179.569 204.011 1.00 109.91 ? 4405 ILE A O     1 
ATOM   19824 C CB    . ILE A 1 4405 ? 171.388 180.385 204.676 1.00 109.91 ? 4405 ILE A CB    1 
ATOM   19825 C CG1   . ILE A 1 4405 ? 171.322 180.011 203.196 1.00 109.91 ? 4405 ILE A CG1   1 
ATOM   19826 C CG2   . ILE A 1 4405 ? 171.771 181.845 204.831 1.00 109.91 ? 4405 ILE A CG2   1 
ATOM   19827 C CD1   . ILE A 1 4405 ? 171.054 178.547 202.954 1.00 109.91 ? 4405 ILE A CD1   1 
ATOM   19828 N N     . LYS A 1 4406 ? 174.505 180.550 206.028 1.00 110.79 ? 4406 LYS A N     1 
ATOM   19829 C CA    . LYS A 1 4406 ? 175.882 180.966 205.790 1.00 110.79 ? 4406 LYS A CA    1 
ATOM   19830 C C     . LYS A 1 4406 ? 176.853 179.795 205.778 1.00 110.79 ? 4406 LYS A C     1 
ATOM   19831 O O     . LYS A 1 4406 ? 177.978 179.947 205.291 1.00 110.79 ? 4406 LYS A O     1 
ATOM   19832 C CB    . LYS A 1 4406 ? 176.318 181.980 206.847 1.00 110.79 ? 4406 LYS A CB    1 
ATOM   19833 C CG    . LYS A 1 4406 ? 175.759 181.718 208.236 1.00 110.79 ? 4406 LYS A CG    1 
ATOM   19834 C CD    . LYS A 1 4406 ? 176.075 182.870 209.179 1.00 110.79 ? 4406 LYS A CD    1 
ATOM   19835 C CE    . LYS A 1 4406 ? 175.142 182.882 210.377 1.00 110.79 ? 4406 LYS A CE    1 
ATOM   19836 N NZ    . LYS A 1 4406 ? 173.744 183.197 209.980 1.00 110.79 ? 4406 LYS A NZ    1 
ATOM   19837 N N     . ASP A 1 4407 ? 176.459 178.646 206.305 1.00 102.33 ? 4407 ASP A N     1 
ATOM   19838 C CA    . ASP A 1 4407 ? 177.350 177.495 206.302 1.00 102.33 ? 4407 ASP A CA    1 
ATOM   19839 C C     . ASP A 1 4407 ? 177.478 176.945 204.887 1.00 102.33 ? 4407 ASP A C     1 
ATOM   19840 O O     . ASP A 1 4407 ? 176.464 176.629 204.257 1.00 102.33 ? 4407 ASP A O     1 
ATOM   19841 C CB    . ASP A 1 4407 ? 176.835 176.417 207.246 1.00 102.33 ? 4407 ASP A CB    1 
ATOM   19842 C CG    . ASP A 1 4407 ? 177.586 175.112 207.101 1.00 102.33 ? 4407 ASP A CG    1 
ATOM   19843 O OD1   . ASP A 1 4407 ? 177.292 174.358 206.152 1.00 102.33 ? 4407 ASP A OD1   1 
ATOM   19844 O OD2   . ASP A 1 4407 ? 178.477 174.842 207.932 1.00 102.33 ? 4407 ASP A OD2   1 
ATOM   19845 N N     . PRO A 1 4408 ? 178.695 176.818 204.355 1.00 94.66  ? 4408 PRO A N     1 
ATOM   19846 C CA    . PRO A 1 4408 ? 178.831 176.312 202.980 1.00 94.66  ? 4408 PRO A CA    1 
ATOM   19847 C C     . PRO A 1 4408 ? 178.349 174.884 202.817 1.00 94.66  ? 4408 PRO A C     1 
ATOM   19848 O O     . PRO A 1 4408 ? 177.729 174.559 201.795 1.00 94.66  ? 4408 PRO A O     1 
ATOM   19849 C CB    . PRO A 1 4408 ? 180.336 176.441 202.708 1.00 94.66  ? 4408 PRO A CB    1 
ATOM   19850 C CG    . PRO A 1 4408 ? 180.853 177.363 203.773 1.00 94.66  ? 4408 PRO A CG    1 
ATOM   19851 C CD    . PRO A 1 4408 ? 179.995 177.130 204.962 1.00 94.66  ? 4408 PRO A CD    1 
ATOM   19852 N N     . LEU A 1 4409 ? 178.619 174.014 203.795 1.00 95.30  ? 4409 LEU A N     1 
ATOM   19853 C CA    . LEU A 1 4409 ? 178.135 172.643 203.693 1.00 95.30  ? 4409 LEU A CA    1 
ATOM   19854 C C     . LEU A 1 4409 ? 176.619 172.601 203.657 1.00 95.30  ? 4409 LEU A C     1 
ATOM   19855 O O     . LEU A 1 4409 ? 176.042 171.717 203.022 1.00 95.30  ? 4409 LEU A O     1 
ATOM   19856 C CB    . LEU A 1 4409 ? 178.644 171.791 204.853 1.00 95.30  ? 4409 LEU A CB    1 
ATOM   19857 C CG    . LEU A 1 4409 ? 180.136 171.777 205.155 1.00 95.30  ? 4409 LEU A CG    1 
ATOM   19858 C CD1   . LEU A 1 4409 ? 180.417 172.692 206.317 1.00 95.30  ? 4409 LEU A CD1   1 
ATOM   19859 C CD2   . LEU A 1 4409 ? 180.589 170.367 205.462 1.00 95.30  ? 4409 LEU A CD2   1 
ATOM   19860 N N     . PHE A 1 4410 ? 175.959 173.546 204.328 1.00 103.79 ? 4410 PHE A N     1 
ATOM   19861 C CA    . PHE A 1 4410 ? 174.505 173.597 204.266 1.00 103.79 ? 4410 PHE A CA    1 
ATOM   19862 C C     . PHE A 1 4410 ? 174.034 173.733 202.827 1.00 103.79 ? 4410 PHE A C     1 
ATOM   19863 O O     . PHE A 1 4410 ? 173.218 172.938 202.355 1.00 103.79 ? 4410 PHE A O     1 
ATOM   19864 C CB    . PHE A 1 4410 ? 173.979 174.753 205.115 1.00 103.79 ? 4410 PHE A CB    1 
ATOM   19865 C CG    . PHE A 1 4410 ? 172.500 174.690 205.376 1.00 103.79 ? 4410 PHE A CG    1 
ATOM   19866 C CD1   . PHE A 1 4410 ? 171.818 173.488 205.298 1.00 103.79 ? 4410 PHE A CD1   1 
ATOM   19867 C CD2   . PHE A 1 4410 ? 171.788 175.837 205.686 1.00 103.79 ? 4410 PHE A CD2   1 
ATOM   19868 C CE1   . PHE A 1 4410 ? 170.460 173.432 205.535 1.00 103.79 ? 4410 PHE A CE1   1 
ATOM   19869 C CE2   . PHE A 1 4410 ? 170.431 175.787 205.923 1.00 103.79 ? 4410 PHE A CE2   1 
ATOM   19870 C CZ    . PHE A 1 4410 ? 169.766 174.582 205.847 1.00 103.79 ? 4410 PHE A CZ    1 
ATOM   19871 N N     . ARG A 1 4411 ? 174.561 174.721 202.104 1.00 103.08 ? 4411 ARG A N     1 
ATOM   19872 C CA    . ARG A 1 4411 ? 174.140 174.922 200.722 1.00 103.08 ? 4411 ARG A CA    1 
ATOM   19873 C C     . ARG A 1 4411 ? 174.567 173.758 199.839 1.00 103.08 ? 4411 ARG A C     1 
ATOM   19874 O O     . ARG A 1 4411 ? 173.816 173.338 198.947 1.00 103.08 ? 4411 ARG A O     1 
ATOM   19875 C CB    . ARG A 1 4411 ? 174.704 176.236 200.187 1.00 103.08 ? 4411 ARG A CB    1 
ATOM   19876 C CG    . ARG A 1 4411 ? 174.499 177.420 201.114 1.00 103.08 ? 4411 ARG A CG    1 
ATOM   19877 C CD    . ARG A 1 4411 ? 175.125 178.668 200.534 1.00 103.08 ? 4411 ARG A CD    1 
ATOM   19878 N NE    . ARG A 1 4411 ? 176.305 179.081 201.280 1.00 103.08 ? 4411 ARG A NE    1 
ATOM   19879 C CZ    . ARG A 1 4411 ? 177.444 179.458 200.719 1.00 103.08 ? 4411 ARG A CZ    1 
ATOM   19880 N NH1   . ARG A 1 4411 ? 177.596 179.469 199.406 1.00 103.08 ? 4411 ARG A NH1   1 
ATOM   19881 N NH2   . ARG A 1 4411 ? 178.458 179.829 201.495 1.00 103.08 ? 4411 ARG A NH2   1 
ATOM   19882 N N     . PHE A 1 4412 ? 175.771 173.229 200.065 1.00 94.54  ? 4412 PHE A N     1 
ATOM   19883 C CA    . PHE A 1 4412 ? 176.231 172.107 199.257 1.00 94.54  ? 4412 PHE A CA    1 
ATOM   19884 C C     . PHE A 1 4412 ? 175.304 170.912 199.412 1.00 94.54  ? 4412 PHE A C     1 
ATOM   19885 O O     . PHE A 1 4412 ? 174.919 170.279 198.422 1.00 94.54  ? 4412 PHE A O     1 
ATOM   19886 C CB    . PHE A 1 4412 ? 177.657 171.727 199.644 1.00 94.54  ? 4412 PHE A CB    1 
ATOM   19887 C CG    . PHE A 1 4412 ? 178.078 170.379 199.141 1.00 94.54  ? 4412 PHE A CG    1 
ATOM   19888 C CD1   . PHE A 1 4412 ? 178.375 170.189 197.808 1.00 94.54  ? 4412 PHE A CD1   1 
ATOM   19889 C CD2   . PHE A 1 4412 ? 178.168 169.301 199.999 1.00 94.54  ? 4412 PHE A CD2   1 
ATOM   19890 C CE1   . PHE A 1 4412 ? 178.764 168.956 197.345 1.00 94.54  ? 4412 PHE A CE1   1 
ATOM   19891 C CE2   . PHE A 1 4412 ? 178.553 168.064 199.536 1.00 94.54  ? 4412 PHE A CE2   1 
ATOM   19892 C CZ    . PHE A 1 4412 ? 178.849 167.892 198.207 1.00 94.54  ? 4412 PHE A CZ    1 
ATOM   19893 N N     . PHE A 1 4413 ? 174.915 170.603 200.648 1.00 97.46  ? 4413 PHE A N     1 
ATOM   19894 C CA    . PHE A 1 4413 ? 174.038 169.467 200.877 1.00 97.46  ? 4413 PHE A CA    1 
ATOM   19895 C C     . PHE A 1 4413 ? 172.617 169.762 200.427 1.00 97.46  ? 4413 PHE A C     1 
ATOM   19896 O O     . PHE A 1 4413 ? 171.903 168.843 200.028 1.00 97.46  ? 4413 PHE A O     1 
ATOM   19897 C CB    . PHE A 1 4413 ? 174.075 169.067 202.348 1.00 97.46  ? 4413 PHE A CB    1 
ATOM   19898 C CG    . PHE A 1 4413 ? 175.321 168.329 202.734 1.00 97.46  ? 4413 PHE A CG    1 
ATOM   19899 C CD1   . PHE A 1 4413 ? 175.729 167.220 202.019 1.00 97.46  ? 4413 PHE A CD1   1 
ATOM   19900 C CD2   . PHE A 1 4413 ? 176.086 168.745 203.805 1.00 97.46  ? 4413 PHE A CD2   1 
ATOM   19901 C CE1   . PHE A 1 4413 ? 176.875 166.541 202.367 1.00 97.46  ? 4413 PHE A CE1   1 
ATOM   19902 C CE2   . PHE A 1 4413 ? 177.233 168.068 204.157 1.00 97.46  ? 4413 PHE A CE2   1 
ATOM   19903 C CZ    . PHE A 1 4413 ? 177.628 166.965 203.436 1.00 97.46  ? 4413 PHE A CZ    1 
ATOM   19904 N N     . GLU A 1 4414 ? 172.193 171.027 200.465 1.00 108.46 ? 4414 GLU A N     1 
ATOM   19905 C CA    . GLU A 1 4414 ? 170.912 171.382 199.864 1.00 108.46 ? 4414 GLU A CA    1 
ATOM   19906 C C     . GLU A 1 4414 ? 170.903 171.028 198.386 1.00 108.46 ? 4414 GLU A C     1 
ATOM   19907 O O     . GLU A 1 4414 ? 169.981 170.364 197.898 1.00 108.46 ? 4414 GLU A O     1 
ATOM   19908 C CB    . GLU A 1 4414 ? 170.624 172.872 200.049 1.00 108.46 ? 4414 GLU A CB    1 
ATOM   19909 C CG    . GLU A 1 4414 ? 170.350 173.302 201.473 1.00 108.46 ? 4414 GLU A CG    1 
ATOM   19910 C CD    . GLU A 1 4414 ? 169.936 174.756 201.567 1.00 108.46 ? 4414 GLU A CD    1 
ATOM   19911 O OE1   . GLU A 1 4414 ? 170.066 175.478 200.557 1.00 108.46 ? 4414 GLU A OE1   1 
ATOM   19912 O OE2   . GLU A 1 4414 ? 169.493 175.182 202.654 1.00 108.46 ? 4414 GLU A OE2   1 
ATOM   19913 N N     . ARG A 1 4415 ? 171.938 171.455 197.661 1.00 100.86 ? 4415 ARG A N     1 
ATOM   19914 C CA    . ARG A 1 4415 ? 172.024 171.148 196.237 1.00 100.86 ? 4415 ARG A CA    1 
ATOM   19915 C C     . ARG A 1 4415 ? 172.086 169.644 196.007 1.00 100.86 ? 4415 ARG A C     1 
ATOM   19916 O O     . ARG A 1 4415 ? 171.392 169.104 195.133 1.00 100.86 ? 4415 ARG A O     1 
ATOM   19917 C CB    . ARG A 1 4415 ? 173.245 171.833 195.629 1.00 100.86 ? 4415 ARG A CB    1 
ATOM   19918 C CG    . ARG A 1 4415 ? 173.238 171.876 194.113 1.00 100.86 ? 4415 ARG A CG    1 
ATOM   19919 C CD    . ARG A 1 4415 ? 174.430 172.653 193.575 1.00 100.86 ? 4415 ARG A CD    1 
ATOM   19920 N NE    . ARG A 1 4415 ? 174.636 173.904 194.295 1.00 100.86 ? 4415 ARG A NE    1 
ATOM   19921 C CZ    . ARG A 1 4415 ? 175.679 174.158 195.072 1.00 100.86 ? 4415 ARG A CZ    1 
ATOM   19922 N NH1   . ARG A 1 4415 ? 176.637 173.264 195.257 1.00 100.86 ? 4415 ARG A NH1   1 
ATOM   19923 N NH2   . ARG A 1 4415 ? 175.762 175.336 195.682 1.00 100.86 ? 4415 ARG A NH2   1 
ATOM   19924 N N     . GLU A 1 4416 ? 172.908 168.951 196.795 1.00 104.37 ? 4416 GLU A N     1 
ATOM   19925 C CA    . GLU A 1 4416 ? 173.066 167.513 196.621 1.00 104.37 ? 4416 GLU A CA    1 
ATOM   19926 C C     . GLU A 1 4416 ? 171.751 166.785 196.851 1.00 104.37 ? 4416 GLU A C     1 
ATOM   19927 O O     . GLU A 1 4416 ? 171.336 165.956 196.035 1.00 104.37 ? 4416 GLU A O     1 
ATOM   19928 C CB    . GLU A 1 4416 ? 174.139 166.992 197.572 1.00 104.37 ? 4416 GLU A CB    1 
ATOM   19929 C CG    . GLU A 1 4416 ? 175.011 165.921 196.966 1.00 104.37 ? 4416 GLU A CG    1 
ATOM   19930 C CD    . GLU A 1 4416 ? 175.937 166.479 195.910 1.00 104.37 ? 4416 GLU A CD    1 
ATOM   19931 O OE1   . GLU A 1 4416 ? 176.188 165.784 194.906 1.00 104.37 ? 4416 GLU A OE1   1 
ATOM   19932 O OE2   . GLU A 1 4416 ? 176.403 167.622 196.080 1.00 104.37 ? 4416 GLU A OE2   1 
ATOM   19933 N N     . VAL A 1 4417 ? 171.077 167.090 197.960 1.00 103.11 ? 4417 VAL A N     1 
ATOM   19934 C CA    . VAL A 1 4417 ? 169.830 166.418 198.294 1.00 103.11 ? 4417 VAL A CA    1 
ATOM   19935 C C     . VAL A 1 4417 ? 168.763 166.737 197.261 1.00 103.11 ? 4417 VAL A C     1 
ATOM   19936 O O     . VAL A 1 4417 ? 168.003 165.857 196.850 1.00 103.11 ? 4417 VAL A O     1 
ATOM   19937 C CB    . VAL A 1 4417 ? 169.382 166.802 199.715 1.00 103.11 ? 4417 VAL A CB    1 
ATOM   19938 C CG1   . VAL A 1 4417 ? 167.893 166.578 199.886 1.00 103.11 ? 4417 VAL A CG1   1 
ATOM   19939 C CG2   . VAL A 1 4417 ? 170.161 166.006 200.742 1.00 103.11 ? 4417 VAL A CG2   1 
ATOM   19940 N N     . LYS A 1 4418 ? 168.688 167.994 196.817 1.00 108.35 ? 4418 LYS A N     1 
ATOM   19941 C CA    . LYS A 1 4418 ? 167.684 168.354 195.823 1.00 108.35 ? 4418 LYS A CA    1 
ATOM   19942 C C     . LYS A 1 4418 ? 167.888 167.575 194.531 1.00 108.35 ? 4418 LYS A C     1 
ATOM   19943 O O     . LYS A 1 4418 ? 166.944 166.977 193.998 1.00 108.35 ? 4418 LYS A O     1 
ATOM   19944 C CB    . LYS A 1 4418 ? 167.721 169.858 195.556 1.00 108.35 ? 4418 LYS A CB    1 
ATOM   19945 C CG    . LYS A 1 4418 ? 167.105 170.256 194.226 1.00 108.35 ? 4418 LYS A CG    1 
ATOM   19946 C CD    . LYS A 1 4418 ? 166.361 171.575 194.327 1.00 108.35 ? 4418 LYS A CD    1 
ATOM   19947 C CE    . LYS A 1 4418 ? 167.302 172.717 194.656 1.00 108.35 ? 4418 LYS A CE    1 
ATOM   19948 N NZ    . LYS A 1 4418 ? 167.975 173.240 193.437 1.00 108.35 ? 4418 LYS A NZ    1 
ATOM   19949 N N     . MET A 1 4419 ? 169.121 167.555 194.018 1.00 106.91 ? 4419 MET A N     1 
ATOM   19950 C CA    . MET A 1 4419 ? 169.353 166.868 192.752 1.00 106.91 ? 4419 MET A CA    1 
ATOM   19951 C C     . MET A 1 4419 ? 169.151 165.366 192.910 1.00 106.91 ? 4419 MET A C     1 
ATOM   19952 O O     . MET A 1 4419 ? 168.563 164.716 192.035 1.00 106.91 ? 4419 MET A O     1 
ATOM   19953 C CB    . MET A 1 4419 ? 170.753 167.205 192.228 1.00 106.91 ? 4419 MET A CB    1 
ATOM   19954 C CG    . MET A 1 4419 ? 171.245 166.455 190.975 1.00 106.91 ? 4419 MET A CG    1 
ATOM   19955 S SD    . MET A 1 4419 ? 171.549 164.682 191.082 1.00 106.91 ? 4419 MET A SD    1 
ATOM   19956 C CE    . MET A 1 4419 ? 172.615 164.647 192.511 1.00 106.91 ? 4419 MET A CE    1 
ATOM   19957 N N     . GLY A 1 4420 ? 169.620 164.799 194.024 1.00 107.59 ? 4420 GLY A N     1 
ATOM   19958 C CA    . GLY A 1 4420 ? 169.444 163.376 194.243 1.00 107.59 ? 4420 GLY A CA    1 
ATOM   19959 C C     . GLY A 1 4420 ? 167.988 162.983 194.365 1.00 107.59 ? 4420 GLY A C     1 
ATOM   19960 O O     . GLY A 1 4420 ? 167.569 161.954 193.836 1.00 107.59 ? 4420 GLY A O     1 
ATOM   19961 N N     . ALA A 1 4421 ? 167.193 163.798 195.059 1.00 108.46 ? 4421 ALA A N     1 
ATOM   19962 C CA    . ALA A 1 4421 ? 165.772 163.512 195.185 1.00 108.46 ? 4421 ALA A CA    1 
ATOM   19963 C C     . ALA A 1 4421 ? 165.064 163.648 193.846 1.00 108.46 ? 4421 ALA A C     1 
ATOM   19964 O O     . ALA A 1 4421 ? 164.157 162.869 193.542 1.00 108.46 ? 4421 ALA A O     1 
ATOM   19965 C CB    . ALA A 1 4421 ? 165.140 164.431 196.226 1.00 108.46 ? 4421 ALA A CB    1 
ATOM   19966 N N     . LYS A 1 4422 ? 165.456 164.629 193.032 1.00 104.57 ? 4422 LYS A N     1 
ATOM   19967 C CA    . LYS A 1 4422 ? 164.872 164.736 191.699 1.00 104.57 ? 4422 LYS A CA    1 
ATOM   19968 C C     . LYS A 1 4422 ? 165.165 163.487 190.878 1.00 104.57 ? 4422 LYS A C     1 
ATOM   19969 O O     . LYS A 1 4422 ? 164.267 162.916 190.243 1.00 104.57 ? 4422 LYS A O     1 
ATOM   19970 C CB    . LYS A 1 4422 ? 165.400 165.982 190.990 1.00 104.57 ? 4422 LYS A CB    1 
ATOM   19971 C CG    . LYS A 1 4422 ? 165.231 165.950 189.479 1.00 104.57 ? 4422 LYS A CG    1 
ATOM   19972 C CD    . LYS A 1 4422 ? 164.898 167.325 188.922 1.00 104.57 ? 4422 LYS A CD    1 
ATOM   19973 C CE    . LYS A 1 4422 ? 165.910 168.368 189.367 1.00 104.57 ? 4422 LYS A CE    1 
ATOM   19974 N NZ    . LYS A 1 4422 ? 167.275 168.078 188.849 1.00 104.57 ? 4422 LYS A NZ    1 
ATOM   19975 N N     . LEU A 1 4423 ? 166.421 163.037 190.897 1.00 105.21 ? 4423 LEU A N     1 
ATOM   19976 C CA    . LEU A 1 4423 ? 166.780 161.835 190.153 1.00 105.21 ? 4423 LEU A CA    1 
ATOM   19977 C C     . LEU A 1 4423 ? 166.038 160.617 190.684 1.00 105.21 ? 4423 LEU A C     1 
ATOM   19978 O O     . LEU A 1 4423 ? 165.575 159.774 189.908 1.00 105.21 ? 4423 LEU A O     1 
ATOM   19979 C CB    . LEU A 1 4423 ? 168.290 161.610 190.212 1.00 105.21 ? 4423 LEU A CB    1 
ATOM   19980 C CG    . LEU A 1 4423 ? 168.915 160.961 188.976 1.00 105.21 ? 4423 LEU A CG    1 
ATOM   19981 C CD1   . LEU A 1 4423 ? 168.319 161.535 187.704 1.00 105.21 ? 4423 LEU A CD1   1 
ATOM   19982 C CD2   . LEU A 1 4423 ? 170.421 161.140 188.986 1.00 105.21 ? 4423 LEU A CD2   1 
ATOM   19983 N N     . LEU A 1 4424 ? 165.919 160.508 192.007 1.00 107.79 ? 4424 LEU A N     1 
ATOM   19984 C CA    . LEU A 1 4424 ? 165.215 159.379 192.602 1.00 107.79 ? 4424 LEU A CA    1 
ATOM   19985 C C     . LEU A 1 4424 ? 163.747 159.379 192.211 1.00 107.79 ? 4424 LEU A C     1 
ATOM   19986 O O     . LEU A 1 4424 ? 163.183 158.326 191.896 1.00 107.79 ? 4424 LEU A O     1 
ATOM   19987 C CB    . LEU A 1 4424 ? 165.362 159.418 194.121 1.00 107.79 ? 4424 LEU A CB    1 
ATOM   19988 C CG    . LEU A 1 4424 ? 164.320 158.642 194.918 1.00 107.79 ? 4424 LEU A CG    1 
ATOM   19989 C CD1   . LEU A 1 4424 ? 164.577 157.160 194.793 1.00 107.79 ? 4424 LEU A CD1   1 
ATOM   19990 C CD2   . LEU A 1 4424 ? 164.339 159.073 196.369 1.00 107.79 ? 4424 LEU A CD2   1 
ATOM   19991 N N     . GLN A 1 4425 ? 163.107 160.548 192.233 1.00 115.22 ? 4425 GLN A N     1 
ATOM   19992 C CA    . GLN A 1 4425 ? 161.709 160.639 191.832 1.00 115.22 ? 4425 GLN A CA    1 
ATOM   19993 C C     . GLN A 1 4425 ? 161.537 160.229 190.378 1.00 115.22 ? 4425 GLN A C     1 
ATOM   19994 O O     . GLN A 1 4425 ? 160.622 159.469 190.039 1.00 115.22 ? 4425 GLN A O     1 
ATOM   19995 C CB    . GLN A 1 4425 ? 161.193 162.059 192.055 1.00 115.22 ? 4425 GLN A CB    1 
ATOM   19996 C CG    . GLN A 1 4425 ? 159.756 162.271 191.620 1.00 115.22 ? 4425 GLN A CG    1 
ATOM   19997 C CD    . GLN A 1 4425 ? 159.372 163.737 191.584 1.00 115.22 ? 4425 GLN A CD    1 
ATOM   19998 O OE1   . GLN A 1 4425 ? 160.234 164.614 191.551 1.00 115.22 ? 4425 GLN A OE1   1 
ATOM   19999 N NE2   . GLN A 1 4425 ? 158.073 164.010 191.590 1.00 115.22 ? 4425 GLN A NE2   1 
ATOM   20000 N N     . ASP A 1 4426 ? 162.420 160.716 189.503 1.00 120.34 ? 4426 ASP A N     1 
ATOM   20001 C CA    . ASP A 1 4426 ? 162.330 160.344 188.095 1.00 120.34 ? 4426 ASP A CA    1 
ATOM   20002 C C     . ASP A 1 4426 ? 162.500 158.844 187.909 1.00 120.34 ? 4426 ASP A C     1 
ATOM   20003 O O     . ASP A 1 4426 ? 161.733 158.210 187.174 1.00 120.34 ? 4426 ASP A O     1 
ATOM   20004 C CB    . ASP A 1 4426 ? 163.373 161.105 187.281 1.00 120.34 ? 4426 ASP A CB    1 
ATOM   20005 C CG    . ASP A 1 4426 ? 162.863 162.441 186.793 1.00 120.34 ? 4426 ASP A CG    1 
ATOM   20006 O OD1   . ASP A 1 4426 ? 163.570 163.094 185.996 1.00 120.34 ? 4426 ASP A OD1   1 
ATOM   20007 O OD2   . ASP A 1 4426 ? 161.753 162.837 187.205 1.00 120.34 ? 4426 ASP A OD2   1 
ATOM   20008 N N     . VAL A 1 4427 ? 163.492 158.254 188.576 1.00 119.42 ? 4427 VAL A N     1 
ATOM   20009 C CA    . VAL A 1 4427 ? 163.748 156.829 188.411 1.00 119.42 ? 4427 VAL A CA    1 
ATOM   20010 C C     . VAL A 1 4427 ? 162.586 156.004 188.948 1.00 119.42 ? 4427 VAL A C     1 
ATOM   20011 O O     . VAL A 1 4427 ? 162.161 155.029 188.318 1.00 119.42 ? 4427 VAL A O     1 
ATOM   20012 C CB    . VAL A 1 4427 ? 165.079 156.449 189.081 1.00 119.42 ? 4427 VAL A CB    1 
ATOM   20013 C CG1   . VAL A 1 4427 ? 165.170 154.946 189.270 1.00 119.42 ? 4427 VAL A CG1   1 
ATOM   20014 C CG2   . VAL A 1 4427 ? 166.238 156.948 188.243 1.00 119.42 ? 4427 VAL A CG2   1 
ATOM   20015 N N     . ARG A 1 4428 ? 162.052 156.372 190.115 1.00 119.68 ? 4428 ARG A N     1 
ATOM   20016 C CA    . ARG A 1 4428 ? 160.925 155.635 190.671 1.00 119.68 ? 4428 ARG A CA    1 
ATOM   20017 C C     . ARG A 1 4428 ? 159.706 155.732 189.766 1.00 119.68 ? 4428 ARG A C     1 
ATOM   20018 O O     . ARG A 1 4428 ? 159.019 154.731 189.530 1.00 119.68 ? 4428 ARG A O     1 
ATOM   20019 C CB    . ARG A 1 4428 ? 160.590 156.154 192.068 1.00 119.68 ? 4428 ARG A CB    1 
ATOM   20020 C CG    . ARG A 1 4428 ? 161.621 155.817 193.129 1.00 119.68 ? 4428 ARG A CG    1 
ATOM   20021 C CD    . ARG A 1 4428 ? 161.520 154.378 193.587 1.00 119.68 ? 4428 ARG A CD    1 
ATOM   20022 N NE    . ARG A 1 4428 ? 160.152 153.880 193.548 1.00 119.68 ? 4428 ARG A NE    1 
ATOM   20023 C CZ    . ARG A 1 4428 ? 159.720 152.834 194.238 1.00 119.68 ? 4428 ARG A CZ    1 
ATOM   20024 N NH1   . ARG A 1 4428 ? 160.519 152.167 195.054 1.00 119.68 ? 4428 ARG A NH1   1 
ATOM   20025 N NH2   . ARG A 1 4428 ? 158.455 152.447 194.107 1.00 119.68 ? 4428 ARG A NH2   1 
ATOM   20026 N N     . GLN A 1 4429 ? 159.424 156.928 189.243 1.00 130.57 ? 4429 GLN A N     1 
ATOM   20027 C CA    . GLN A 1 4429 ? 158.280 157.086 188.352 1.00 130.57 ? 4429 GLN A CA    1 
ATOM   20028 C C     . GLN A 1 4429 ? 158.454 156.265 187.082 1.00 130.57 ? 4429 GLN A C     1 
ATOM   20029 O O     . GLN A 1 4429 ? 157.507 155.619 186.616 1.00 130.57 ? 4429 GLN A O     1 
ATOM   20030 C CB    . GLN A 1 4429 ? 158.081 158.564 188.016 1.00 130.57 ? 4429 GLN A CB    1 
ATOM   20031 C CG    . GLN A 1 4429 ? 157.094 158.831 186.891 1.00 130.57 ? 4429 GLN A CG    1 
ATOM   20032 C CD    . GLN A 1 4429 ? 157.764 158.919 185.531 1.00 130.57 ? 4429 GLN A CD    1 
ATOM   20033 O OE1   . GLN A 1 4429 ? 158.974 159.121 185.435 1.00 130.57 ? 4429 GLN A OE1   1 
ATOM   20034 N NE2   . GLN A 1 4429 ? 156.978 158.767 184.472 1.00 130.57 ? 4429 GLN A NE2   1 
ATOM   20035 N N     . ASP A 1 4430 ? 159.657 156.271 186.507 1.00 133.06 ? 4430 ASP A N     1 
ATOM   20036 C CA    . ASP A 1 4430 ? 159.878 155.525 185.274 1.00 133.06 ? 4430 ASP A CA    1 
ATOM   20037 C C     . ASP A 1 4430 ? 159.807 154.023 185.515 1.00 133.06 ? 4430 ASP A C     1 
ATOM   20038 O O     . ASP A 1 4430 ? 159.273 153.279 184.683 1.00 133.06 ? 4430 ASP A O     1 
ATOM   20039 C CB    . ASP A 1 4430 ? 161.218 155.917 184.664 1.00 133.06 ? 4430 ASP A CB    1 
ATOM   20040 C CG    . ASP A 1 4430 ? 161.144 157.223 183.903 1.00 133.06 ? 4430 ASP A CG    1 
ATOM   20041 O OD1   . ASP A 1 4430 ? 160.668 157.212 182.751 1.00 133.06 ? 4430 ASP A OD1   1 
ATOM   20042 O OD2   . ASP A 1 4430 ? 161.564 158.263 184.451 1.00 133.06 ? 4430 ASP A OD2   1 
ATOM   20043 N N     . LEU A 1 4431 ? 160.337 153.557 186.645 1.00 127.50 ? 4431 LEU A N     1 
ATOM   20044 C CA    . LEU A 1 4431 ? 160.212 152.147 186.988 1.00 127.50 ? 4431 LEU A CA    1 
ATOM   20045 C C     . LEU A 1 4431 ? 158.754 151.758 187.176 1.00 127.50 ? 4431 LEU A C     1 
ATOM   20046 O O     . LEU A 1 4431 ? 158.332 150.681 186.744 1.00 127.50 ? 4431 LEU A O     1 
ATOM   20047 C CB    . LEU A 1 4431 ? 161.012 151.837 188.249 1.00 127.50 ? 4431 LEU A CB    1 
ATOM   20048 C CG    . LEU A 1 4431 ? 162.421 151.276 188.073 1.00 127.50 ? 4431 LEU A CG    1 
ATOM   20049 C CD1   . LEU A 1 4431 ? 162.359 149.846 187.578 1.00 127.50 ? 4431 LEU A CD1   1 
ATOM   20050 C CD2   . LEU A 1 4431 ? 163.212 152.131 187.120 1.00 127.50 ? 4431 LEU A CD2   1 
ATOM   20051 N N     . ALA A 1 4432 ? 157.969 152.623 187.821 1.00 138.15 ? 4432 ALA A N     1 
ATOM   20052 C CA    . ALA A 1 4432 ? 156.545 152.347 187.971 1.00 138.15 ? 4432 ALA A CA    1 
ATOM   20053 C C     . ALA A 1 4432 ? 155.856 152.281 186.614 1.00 138.15 ? 4432 ALA A C     1 
ATOM   20054 O O     . ALA A 1 4432 ? 154.994 151.425 186.389 1.00 138.15 ? 4432 ALA A O     1 
ATOM   20055 C CB    . ALA A 1 4432 ? 155.893 153.407 188.856 1.00 138.15 ? 4432 ALA A CB    1 
ATOM   20056 N N     . ASP A 1 4433 ? 156.222 153.181 185.699 1.00 141.91 ? 4433 ASP A N     1 
ATOM   20057 C CA    . ASP A 1 4433 ? 155.640 153.152 184.361 1.00 141.91 ? 4433 ASP A CA    1 
ATOM   20058 C C     . ASP A 1 4433 ? 155.983 151.856 183.640 1.00 141.91 ? 4433 ASP A C     1 
ATOM   20059 O O     . ASP A 1 4433 ? 155.127 151.260 182.974 1.00 141.91 ? 4433 ASP A O     1 
ATOM   20060 C CB    . ASP A 1 4433 ? 156.119 154.356 183.552 1.00 141.91 ? 4433 ASP A CB    1 
ATOM   20061 C CG    . ASP A 1 4433 ? 155.387 155.629 183.917 1.00 141.91 ? 4433 ASP A CG    1 
ATOM   20062 O OD1   . ASP A 1 4433 ? 155.267 156.519 183.049 1.00 141.91 ? 4433 ASP A OD1   1 
ATOM   20063 O OD2   . ASP A 1 4433 ? 154.930 155.740 185.074 1.00 141.91 ? 4433 ASP A OD2   1 
ATOM   20064 N N     . VAL A 1 4434 ? 157.232 151.407 183.758 1.00 137.47 ? 4434 VAL A N     1 
ATOM   20065 C CA    . VAL A 1 4434 ? 157.624 150.143 183.141 1.00 137.47 ? 4434 VAL A CA    1 
ATOM   20066 C C     . VAL A 1 4434 ? 156.857 148.986 183.771 1.00 137.47 ? 4434 VAL A C     1 
ATOM   20067 O O     . VAL A 1 4434 ? 156.444 148.047 183.081 1.00 137.47 ? 4434 VAL A O     1 
ATOM   20068 C CB    . VAL A 1 4434 ? 159.147 149.946 183.245 1.00 137.47 ? 4434 VAL A CB    1 
ATOM   20069 C CG1   . VAL A 1 4434 ? 159.521 148.499 182.980 1.00 137.47 ? 4434 VAL A CG1   1 
ATOM   20070 C CG2   . VAL A 1 4434 ? 159.859 150.859 182.265 1.00 137.47 ? 4434 VAL A CG2   1 
ATOM   20071 N N     . VAL A 1 4435 ? 156.645 149.040 185.087 1.00 136.30 ? 4435 VAL A N     1 
ATOM   20072 C CA    . VAL A 1 4435 ? 155.875 147.999 185.761 1.00 136.30 ? 4435 VAL A CA    1 
ATOM   20073 C C     . VAL A 1 4435 ? 154.454 147.948 185.216 1.00 136.30 ? 4435 VAL A C     1 
ATOM   20074 O O     . VAL A 1 4435 ? 153.930 146.870 184.908 1.00 136.30 ? 4435 VAL A O     1 
ATOM   20075 C CB    . VAL A 1 4435 ? 155.890 148.228 187.284 1.00 136.30 ? 4435 VAL A CB    1 
ATOM   20076 C CG1   . VAL A 1 4435 ? 154.777 147.442 187.954 1.00 136.30 ? 4435 VAL A CG1   1 
ATOM   20077 C CG2   . VAL A 1 4435 ? 157.233 147.830 187.861 1.00 136.30 ? 4435 VAL A CG2   1 
ATOM   20078 N N     . GLN A 1 4436 ? 153.811 149.109 185.080 1.00 142.03 ? 4436 GLN A N     1 
ATOM   20079 C CA    . GLN A 1 4436 ? 152.447 149.132 184.559 1.00 142.03 ? 4436 GLN A CA    1 
ATOM   20080 C C     . GLN A 1 4436 ? 152.396 148.634 183.121 1.00 142.03 ? 4436 GLN A C     1 
ATOM   20081 O O     . GLN A 1 4436 ? 151.491 147.875 182.753 1.00 142.03 ? 4436 GLN A O     1 
ATOM   20082 C CB    . GLN A 1 4436 ? 151.852 150.538 184.653 1.00 142.03 ? 4436 GLN A CB    1 
ATOM   20083 C CG    . GLN A 1 4436 ? 151.991 151.235 186.004 1.00 142.03 ? 4436 GLN A CG    1 
ATOM   20084 C CD    . GLN A 1 4436 ? 151.707 150.341 187.201 1.00 142.03 ? 4436 GLN A CD    1 
ATOM   20085 O OE1   . GLN A 1 4436 ? 150.927 149.392 187.123 1.00 142.03 ? 4436 GLN A OE1   1 
ATOM   20086 N NE2   . GLN A 1 4436 ? 152.349 150.646 188.323 1.00 142.03 ? 4436 GLN A NE2   1 
ATOM   20087 N N     . VAL A 1 4437 ? 153.359 149.043 182.291 1.00 141.02 ? 4437 VAL A N     1 
ATOM   20088 C CA    . VAL A 1 4437 ? 153.339 148.617 180.898 1.00 141.02 ? 4437 VAL A CA    1 
ATOM   20089 C C     . VAL A 1 4437 ? 153.692 147.143 180.758 1.00 141.02 ? 4437 VAL A C     1 
ATOM   20090 O O     . VAL A 1 4437 ? 153.362 146.526 179.740 1.00 141.02 ? 4437 VAL A O     1 
ATOM   20091 C CB    . VAL A 1 4437 ? 154.278 149.488 180.043 1.00 141.02 ? 4437 VAL A CB    1 
ATOM   20092 C CG1   . VAL A 1 4437 ? 155.697 148.953 180.081 1.00 141.02 ? 4437 VAL A CG1   1 
ATOM   20093 C CG2   . VAL A 1 4437 ? 153.772 149.556 178.618 1.00 141.02 ? 4437 VAL A CG2   1 
ATOM   20094 N N     . CYS A 1 4438 ? 154.356 146.558 181.757 1.00 141.70 ? 4438 CYS A N     1 
ATOM   20095 C CA    . CYS A 1 4438 ? 154.670 145.135 181.695 1.00 141.70 ? 4438 CYS A CA    1 
ATOM   20096 C C     . CYS A 1 4438 ? 153.409 144.290 181.806 1.00 141.70 ? 4438 CYS A C     1 
ATOM   20097 O O     . CYS A 1 4438 ? 153.294 143.246 181.155 1.00 141.70 ? 4438 CYS A O     1 
ATOM   20098 C CB    . CYS A 1 4438 ? 155.663 144.767 182.794 1.00 141.70 ? 4438 CYS A CB    1 
ATOM   20099 S SG    . CYS A 1 4438 ? 157.397 144.813 182.290 1.00 141.70 ? 4438 CYS A SG    1 
ATOM   20100 N N     . GLU A 1 4439 ? 152.454 144.727 182.617 1.00 148.99 ? 4439 GLU A N     1 
ATOM   20101 C CA    . GLU A 1 4439 ? 151.180 144.039 182.754 1.00 148.99 ? 4439 GLU A CA    1 
ATOM   20102 C C     . GLU A 1 4439 ? 150.184 144.434 181.674 1.00 148.99 ? 4439 GLU A C     1 
ATOM   20103 O O     . GLU A 1 4439 ? 149.059 143.925 181.673 1.00 148.99 ? 4439 GLU A O     1 
ATOM   20104 C CB    . GLU A 1 4439 ? 150.580 144.316 184.136 1.00 148.99 ? 4439 GLU A CB    1 
ATOM   20105 C CG    . GLU A 1 4439 ? 151.563 144.133 185.277 1.00 148.99 ? 4439 GLU A CG    1 
ATOM   20106 C CD    . GLU A 1 4439 ? 151.981 142.687 185.447 1.00 148.99 ? 4439 GLU A CD    1 
ATOM   20107 O OE1   . GLU A 1 4439 ? 151.150 141.882 185.914 1.00 148.99 ? 4439 GLU A OE1   1 
ATOM   20108 O OE2   . GLU A 1 4439 ? 153.130 142.350 185.094 1.00 148.99 ? 4439 GLU A OE2   1 
ATOM   20109 N N     . GLY A 1 4440 ? 150.568 145.322 180.762 1.00 146.72 ? 4440 GLY A N     1 
ATOM   20110 C CA    . GLY A 1 4440 ? 149.637 145.799 179.763 1.00 146.72 ? 4440 GLY A CA    1 
ATOM   20111 C C     . GLY A 1 4440 ? 148.600 146.754 180.297 1.00 146.72 ? 4440 GLY A C     1 
ATOM   20112 O O     . GLY A 1 4440 ? 147.616 147.036 179.610 1.00 146.72 ? 4440 GLY A O     1 
ATOM   20113 N N     . LYS A 1 4441 ? 148.797 147.270 181.507 1.00 148.12 ? 4441 LYS A N     1 
ATOM   20114 C CA    . LYS A 1 4441 ? 147.838 148.159 182.144 1.00 148.12 ? 4441 LYS A CA    1 
ATOM   20115 C C     . LYS A 1 4441 ? 147.985 149.606 181.697 1.00 148.12 ? 4441 LYS A C     1 
ATOM   20116 O O     . LYS A 1 4441 ? 147.217 150.459 182.152 1.00 148.12 ? 4441 LYS A O     1 
ATOM   20117 C CB    . LYS A 1 4441 ? 147.977 148.081 183.667 1.00 148.12 ? 4441 LYS A CB    1 
ATOM   20118 C CG    . LYS A 1 4441 ? 147.320 146.864 184.294 1.00 148.12 ? 4441 LYS A CG    1 
ATOM   20119 C CD    . LYS A 1 4441 ? 147.830 146.636 185.708 1.00 148.12 ? 4441 LYS A CD    1 
ATOM   20120 C CE    . LYS A 1 4441 ? 146.737 146.094 186.614 1.00 148.12 ? 4441 LYS A CE    1 
ATOM   20121 N NZ    . LYS A 1 4441 ? 146.541 144.628 186.438 1.00 148.12 ? 4441 LYS A NZ    1 
ATOM   20122 N N     . LYS A 1 4442 ? 148.948 149.903 180.828 1.00 144.98 ? 4442 LYS A N     1 
ATOM   20123 C CA    . LYS A 1 4442 ? 149.169 151.270 180.385 1.00 144.98 ? 4442 LYS A CA    1 
ATOM   20124 C C     . LYS A 1 4442 ? 149.751 151.258 178.980 1.00 144.98 ? 4442 LYS A C     1 
ATOM   20125 O O     . LYS A 1 4442 ? 150.276 150.245 178.509 1.00 144.98 ? 4442 LYS A O     1 
ATOM   20126 C CB    . LYS A 1 4442 ? 150.092 152.028 181.347 1.00 144.98 ? 4442 LYS A CB    1 
ATOM   20127 C CG    . LYS A 1 4442 ? 151.572 151.829 181.082 1.00 144.98 ? 4442 LYS A CG    1 
ATOM   20128 C CD    . LYS A 1 4442 ? 152.400 152.886 181.792 1.00 144.98 ? 4442 LYS A CD    1 
ATOM   20129 C CE    . LYS A 1 4442 ? 151.834 154.278 181.556 1.00 144.98 ? 4442 LYS A CE    1 
ATOM   20130 N NZ    . LYS A 1 4442 ? 152.623 155.329 182.254 1.00 144.98 ? 4442 LYS A NZ    1 
ATOM   20131 N N     . LYS A 1 4443 ? 149.642 152.402 178.312 1.00 150.71 ? 4443 LYS A N     1 
ATOM   20132 C CA    . LYS A 1 4443 ? 150.135 152.546 176.951 1.00 150.71 ? 4443 LYS A CA    1 
ATOM   20133 C C     . LYS A 1 4443 ? 151.638 152.790 176.955 1.00 150.71 ? 4443 LYS A C     1 
ATOM   20134 O O     . LYS A 1 4443 ? 152.177 153.424 177.867 1.00 150.71 ? 4443 LYS A O     1 
ATOM   20135 C CB    . LYS A 1 4443 ? 149.405 153.694 176.249 1.00 150.71 ? 4443 LYS A CB    1 
ATOM   20136 C CG    . LYS A 1 4443 ? 149.722 153.863 174.768 1.00 150.71 ? 4443 LYS A CG    1 
ATOM   20137 C CD    . LYS A 1 4443 ? 150.782 154.929 174.535 1.00 150.71 ? 4443 LYS A CD    1 
ATOM   20138 C CE    . LYS A 1 4443 ? 150.954 155.220 173.055 1.00 150.71 ? 4443 LYS A CE    1 
ATOM   20139 N NZ    . LYS A 1 4443 ? 152.030 156.219 172.810 1.00 150.71 ? 4443 LYS A NZ    1 
ATOM   20140 N N     . GLN A 1 4444 ? 152.313 152.279 175.929 1.00 151.52 ? 4444 GLN A N     1 
ATOM   20141 C CA    . GLN A 1 4444 ? 153.757 152.412 175.790 1.00 151.52 ? 4444 GLN A CA    1 
ATOM   20142 C C     . GLN A 1 4444 ? 154.080 153.431 174.705 1.00 151.52 ? 4444 GLN A C     1 
ATOM   20143 O O     . GLN A 1 4444 ? 153.595 153.316 173.575 1.00 151.52 ? 4444 GLN A O     1 
ATOM   20144 C CB    . GLN A 1 4444 ? 154.393 151.061 175.462 1.00 151.52 ? 4444 GLN A CB    1 
ATOM   20145 C CG    . GLN A 1 4444 ? 155.700 151.139 174.700 1.00 151.52 ? 4444 GLN A CG    1 
ATOM   20146 C CD    . GLN A 1 4444 ? 156.012 149.850 173.966 1.00 151.52 ? 4444 GLN A CD    1 
ATOM   20147 O OE1   . GLN A 1 4444 ? 155.842 149.758 172.750 1.00 151.52 ? 4444 GLN A OE1   1 
ATOM   20148 N NE2   . GLN A 1 4444 ? 156.470 148.845 174.703 1.00 151.52 ? 4444 GLN A NE2   1 
ATOM   20149 N N     . THR A 1 4445 ? 154.896 154.419 175.051 1.00 149.86 ? 4445 THR A N     1 
ATOM   20150 C CA    . THR A 1 4445 ? 155.255 155.505 174.154 1.00 149.86 ? 4445 THR A CA    1 
ATOM   20151 C C     . THR A 1 4445 ? 156.690 155.335 173.671 1.00 149.86 ? 4445 THR A C     1 
ATOM   20152 O O     . THR A 1 4445 ? 157.361 154.340 173.958 1.00 149.86 ? 4445 THR A O     1 
ATOM   20153 C CB    . THR A 1 4445 ? 155.072 156.860 174.839 1.00 149.86 ? 4445 THR A CB    1 
ATOM   20154 O OG1   . THR A 1 4445 ? 155.522 157.902 173.965 1.00 149.86 ? 4445 THR A OG1   1 
ATOM   20155 C CG2   . THR A 1 4445 ? 155.867 156.912 176.132 1.00 149.86 ? 4445 THR A CG2   1 
ATOM   20156 N N     . ASN A 1 4446 ? 157.157 156.337 172.923 1.00 148.86 ? 4446 ASN A N     1 
ATOM   20157 C CA    . ASN A 1 4446 ? 158.486 156.272 172.324 1.00 148.86 ? 4446 ASN A CA    1 
ATOM   20158 C C     . ASN A 1 4446 ? 159.580 156.292 173.386 1.00 148.86 ? 4446 ASN A C     1 
ATOM   20159 O O     . ASN A 1 4446 ? 160.489 155.452 173.376 1.00 148.86 ? 4446 ASN A O     1 
ATOM   20160 C CB    . ASN A 1 4446 ? 158.658 157.429 171.343 1.00 148.86 ? 4446 ASN A CB    1 
ATOM   20161 C CG    . ASN A 1 4446 ? 158.479 158.780 172.004 1.00 148.86 ? 4446 ASN A CG    1 
ATOM   20162 O OD1   . ASN A 1 4446 ? 157.832 158.890 173.046 1.00 148.86 ? 4446 ASN A OD1   1 
ATOM   20163 N ND2   . ASN A 1 4446 ? 159.054 159.815 171.405 1.00 148.86 ? 4446 ASN A ND2   1 
ATOM   20164 N N     . TYR A 1 4447 ? 159.511 157.250 174.311 1.00 145.19 ? 4447 TYR A N     1 
ATOM   20165 C CA    . TYR A 1 4447 ? 160.525 157.343 175.354 1.00 145.19 ? 4447 TYR A CA    1 
ATOM   20166 C C     . TYR A 1 4447 ? 160.486 156.121 176.259 1.00 145.19 ? 4447 TYR A C     1 
ATOM   20167 O O     . TYR A 1 4447 ? 161.533 155.619 176.682 1.00 145.19 ? 4447 TYR A O     1 
ATOM   20168 C CB    . TYR A 1 4447 ? 160.328 158.634 176.150 1.00 145.19 ? 4447 TYR A CB    1 
ATOM   20169 C CG    . TYR A 1 4447 ? 160.881 158.617 177.558 1.00 145.19 ? 4447 TYR A CG    1 
ATOM   20170 C CD1   . TYR A 1 4447 ? 162.237 158.794 177.795 1.00 145.19 ? 4447 TYR A CD1   1 
ATOM   20171 C CD2   . TYR A 1 4447 ? 160.042 158.450 178.651 1.00 145.19 ? 4447 TYR A CD2   1 
ATOM   20172 C CE1   . TYR A 1 4447 ? 162.744 158.788 179.083 1.00 145.19 ? 4447 TYR A CE1   1 
ATOM   20173 C CE2   . TYR A 1 4447 ? 160.538 158.444 179.939 1.00 145.19 ? 4447 TYR A CE2   1 
ATOM   20174 C CZ    . TYR A 1 4447 ? 161.889 158.613 180.150 1.00 145.19 ? 4447 TYR A CZ    1 
ATOM   20175 O OH    . TYR A 1 4447 ? 162.388 158.607 181.432 1.00 145.19 ? 4447 TYR A OH    1 
ATOM   20176 N N     . LEU A 1 4448 ? 159.286 155.618 176.554 1.00 145.44 ? 4448 LEU A N     1 
ATOM   20177 C CA    . LEU A 1 4448 ? 159.169 154.364 177.288 1.00 145.44 ? 4448 LEU A CA    1 
ATOM   20178 C C     . LEU A 1 4448 ? 159.717 153.194 176.485 1.00 145.44 ? 4448 LEU A C     1 
ATOM   20179 O O     . LEU A 1 4448 ? 160.278 152.255 177.062 1.00 145.44 ? 4448 LEU A O     1 
ATOM   20180 C CB    . LEU A 1 4448 ? 157.711 154.108 177.666 1.00 145.44 ? 4448 LEU A CB    1 
ATOM   20181 C CG    . LEU A 1 4448 ? 157.313 154.558 179.070 1.00 145.44 ? 4448 LEU A CG    1 
ATOM   20182 C CD1   . LEU A 1 4448 ? 158.063 153.751 180.116 1.00 145.44 ? 4448 LEU A CD1   1 
ATOM   20183 C CD2   . LEU A 1 4448 ? 157.569 156.045 179.250 1.00 145.44 ? 4448 LEU A CD2   1 
ATOM   20184 N N     . ARG A 1 4449 ? 159.554 153.221 175.160 1.00 143.97 ? 4449 ARG A N     1 
ATOM   20185 C CA    . ARG A 1 4449 ? 160.161 152.188 174.328 1.00 143.97 ? 4449 ARG A CA    1 
ATOM   20186 C C     . ARG A 1 4449 ? 161.675 152.205 174.467 1.00 143.97 ? 4449 ARG A C     1 
ATOM   20187 O O     . ARG A 1 4449 ? 162.308 151.155 174.608 1.00 143.97 ? 4449 ARG A O     1 
ATOM   20188 C CB    . ARG A 1 4449 ? 159.750 152.371 172.867 1.00 143.97 ? 4449 ARG A CB    1 
ATOM   20189 C CG    . ARG A 1 4449 ? 158.571 151.512 172.460 1.00 143.97 ? 4449 ARG A CG    1 
ATOM   20190 C CD    . ARG A 1 4449 ? 158.357 151.475 170.952 1.00 143.97 ? 4449 ARG A CD    1 
ATOM   20191 N NE    . ARG A 1 4449 ? 157.675 152.658 170.440 1.00 143.97 ? 4449 ARG A NE    1 
ATOM   20192 C CZ    . ARG A 1 4449 ? 158.279 153.748 169.989 1.00 143.97 ? 4449 ARG A CZ    1 
ATOM   20193 N NH1   . ARG A 1 4449 ? 159.598 153.844 169.954 1.00 143.97 ? 4449 ARG A NH1   1 
ATOM   20194 N NH2   . ARG A 1 4449 ? 157.540 154.765 169.556 1.00 143.97 ? 4449 ARG A NH2   1 
ATOM   20195 N N     . THR A 1 4450 ? 162.272 153.398 174.445 1.00 140.85 ? 4450 THR A N     1 
ATOM   20196 C CA    . THR A 1 4450 ? 163.710 153.504 174.672 1.00 140.85 ? 4450 THR A CA    1 
ATOM   20197 C C     . THR A 1 4450 ? 164.081 153.004 176.063 1.00 140.85 ? 4450 THR A C     1 
ATOM   20198 O O     . THR A 1 4450 ? 165.065 152.277 176.231 1.00 140.85 ? 4450 THR A O     1 
ATOM   20199 C CB    . THR A 1 4450 ? 164.165 154.949 174.473 1.00 140.85 ? 4450 THR A CB    1 
ATOM   20200 O OG1   . THR A 1 4450 ? 163.541 155.777 175.457 1.00 140.85 ? 4450 THR A OG1   1 
ATOM   20201 C CG2   . THR A 1 4450 ? 163.792 155.450 173.080 1.00 140.85 ? 4450 THR A CG2   1 
ATOM   20202 N N     . LEU A 1 4451 ? 163.292 153.362 177.074 1.00 137.07 ? 4451 LEU A N     1 
ATOM   20203 C CA    . LEU A 1 4451 ? 163.595 152.909 178.426 1.00 137.07 ? 4451 LEU A CA    1 
ATOM   20204 C C     . LEU A 1 4451 ? 163.622 151.388 178.490 1.00 137.07 ? 4451 LEU A C     1 
ATOM   20205 O O     . LEU A 1 4451 ? 164.578 150.793 179.002 1.00 137.07 ? 4451 LEU A O     1 
ATOM   20206 C CB    . LEU A 1 4451 ? 162.589 153.482 179.416 1.00 137.07 ? 4451 LEU A CB    1 
ATOM   20207 C CG    . LEU A 1 4451 ? 163.200 153.938 180.736 1.00 137.07 ? 4451 LEU A CG    1 
ATOM   20208 C CD1   . LEU A 1 4451 ? 164.477 154.664 180.466 1.00 137.07 ? 4451 LEU A CD1   1 
ATOM   20209 C CD2   . LEU A 1 4451 ? 162.239 154.828 181.476 1.00 137.07 ? 4451 LEU A CD2   1 
ATOM   20210 N N     . ILE A 1 4452 ? 162.607 150.737 177.919 1.00 139.63 ? 4452 ILE A N     1 
ATOM   20211 C CA    . ILE A 1 4452 ? 162.555 149.281 178.002 1.00 139.63 ? 4452 ILE A CA    1 
ATOM   20212 C C     . ILE A 1 4452 ? 163.640 148.639 177.145 1.00 139.63 ? 4452 ILE A C     1 
ATOM   20213 O O     . ILE A 1 4452 ? 164.156 147.576 177.500 1.00 139.63 ? 4452 ILE A O     1 
ATOM   20214 C CB    . ILE A 1 4452 ? 161.154 148.748 177.643 1.00 139.63 ? 4452 ILE A CB    1 
ATOM   20215 C CG1   . ILE A 1 4452 ? 160.734 149.166 176.239 1.00 139.63 ? 4452 ILE A CG1   1 
ATOM   20216 C CG2   . ILE A 1 4452 ? 160.125 149.214 178.664 1.00 139.63 ? 4452 ILE A CG2   1 
ATOM   20217 C CD1   . ILE A 1 4452 ? 159.660 148.288 175.651 1.00 139.63 ? 4452 ILE A CD1   1 
ATOM   20218 N N     . ASN A 1 4453 ? 164.013 149.247 176.015 1.00 135.35 ? 4453 ASN A N     1 
ATOM   20219 C CA    . ASN A 1 4453 ? 165.077 148.652 175.207 1.00 135.35 ? 4453 ASN A CA    1 
ATOM   20220 C C     . ASN A 1 4453 ? 166.423 148.694 175.924 1.00 135.35 ? 4453 ASN A C     1 
ATOM   20221 O O     . ASN A 1 4453 ? 167.093 147.662 176.064 1.00 135.35 ? 4453 ASN A O     1 
ATOM   20222 C CB    . ASN A 1 4453 ? 165.156 149.335 173.843 1.00 135.35 ? 4453 ASN A CB    1 
ATOM   20223 C CG    . ASN A 1 4453 ? 163.845 149.280 173.092 1.00 135.35 ? 4453 ASN A CG    1 
ATOM   20224 O OD1   . ASN A 1 4453 ? 163.104 148.302 173.189 1.00 135.35 ? 4453 ASN A OD1   1 
ATOM   20225 N ND2   . ASN A 1 4453 ? 163.547 150.331 172.341 1.00 135.35 ? 4453 ASN A ND2   1 
ATOM   20226 N N     . GLU A 1 4454 ? 166.847 149.876 176.379 1.00 138.05 ? 4454 GLU A N     1 
ATOM   20227 C CA    . GLU A 1 4454 ? 168.089 149.923 177.154 1.00 138.05 ? 4454 GLU A CA    1 
ATOM   20228 C C     . GLU A 1 4454 ? 167.992 149.197 178.487 1.00 138.05 ? 4454 GLU A C     1 
ATOM   20229 O O     . GLU A 1 4454 ? 169.027 148.878 179.081 1.00 138.05 ? 4454 GLU A O     1 
ATOM   20230 C CB    . GLU A 1 4454 ? 168.597 151.356 177.353 1.00 138.05 ? 4454 GLU A CB    1 
ATOM   20231 C CG    . GLU A 1 4454 ? 168.963 152.191 176.111 1.00 138.05 ? 4454 GLU A CG    1 
ATOM   20232 C CD    . GLU A 1 4454 ? 167.832 152.586 175.208 1.00 138.05 ? 4454 GLU A CD    1 
ATOM   20233 O OE1   . GLU A 1 4454 ? 167.867 153.717 174.682 1.00 138.05 ? 4454 GLU A OE1   1 
ATOM   20234 O OE2   . GLU A 1 4454 ? 167.011 151.711 174.882 1.00 138.05 ? 4454 GLU A OE2   1 
ATOM   20235 N N     . LEU A 1 4455 ? 166.788 148.925 178.988 1.00 126.79 ? 4455 LEU A N     1 
ATOM   20236 C CA    . LEU A 1 4455 ? 166.706 148.056 180.157 1.00 126.79 ? 4455 LEU A CA    1 
ATOM   20237 C C     . LEU A 1 4455 ? 166.927 146.595 179.785 1.00 126.79 ? 4455 LEU A C     1 
ATOM   20238 O O     . LEU A 1 4455 ? 167.641 145.874 180.490 1.00 126.79 ? 4455 LEU A O     1 
ATOM   20239 C CB    . LEU A 1 4455 ? 165.370 148.244 180.868 1.00 126.79 ? 4455 LEU A CB    1 
ATOM   20240 C CG    . LEU A 1 4455 ? 165.330 149.475 181.770 1.00 126.79 ? 4455 LEU A CG    1 
ATOM   20241 C CD1   . LEU A 1 4455 ? 163.920 149.748 182.253 1.00 126.79 ? 4455 LEU A CD1   1 
ATOM   20242 C CD2   . LEU A 1 4455 ? 166.271 149.275 182.942 1.00 126.79 ? 4455 LEU A CD2   1 
ATOM   20243 N N     . VAL A 1 4456 ? 166.331 146.135 178.683 1.00 126.06 ? 4456 VAL A N     1 
ATOM   20244 C CA    . VAL A 1 4456 ? 166.451 144.720 178.353 1.00 126.06 ? 4456 VAL A CA    1 
ATOM   20245 C C     . VAL A 1 4456 ? 167.868 144.392 177.907 1.00 126.06 ? 4456 VAL A C     1 
ATOM   20246 O O     . VAL A 1 4456 ? 168.414 143.349 178.282 1.00 126.06 ? 4456 VAL A O     1 
ATOM   20247 C CB    . VAL A 1 4456 ? 165.398 144.282 177.314 1.00 126.06 ? 4456 VAL A CB    1 
ATOM   20248 C CG1   . VAL A 1 4456 ? 163.995 144.417 177.889 1.00 126.06 ? 4456 VAL A CG1   1 
ATOM   20249 C CG2   . VAL A 1 4456 ? 165.528 145.049 176.012 1.00 126.06 ? 4456 VAL A CG2   1 
ATOM   20250 N N     . LYS A 1 4457 ? 168.508 145.271 177.134 1.00 128.05 ? 4457 LYS A N     1 
ATOM   20251 C CA    . LYS A 1 4457 ? 169.876 144.945 176.747 1.00 128.05 ? 4457 LYS A CA    1 
ATOM   20252 C C     . LYS A 1 4457 ? 170.904 145.403 177.774 1.00 128.05 ? 4457 LYS A C     1 
ATOM   20253 O O     . LYS A 1 4457 ? 172.104 145.358 177.488 1.00 128.05 ? 4457 LYS A O     1 
ATOM   20254 C CB    . LYS A 1 4457 ? 170.240 145.505 175.366 1.00 128.05 ? 4457 LYS A CB    1 
ATOM   20255 C CG    . LYS A 1 4457 ? 169.096 145.719 174.399 1.00 128.05 ? 4457 LYS A CG    1 
ATOM   20256 C CD    . LYS A 1 4457 ? 169.571 146.550 173.209 1.00 128.05 ? 4457 LYS A CD    1 
ATOM   20257 C CE    . LYS A 1 4457 ? 169.935 147.973 173.563 1.00 128.05 ? 4457 LYS A CE    1 
ATOM   20258 N NZ    . LYS A 1 4457 ? 168.915 148.615 174.398 1.00 128.05 ? 4457 LYS A NZ    1 
ATOM   20259 N N     . GLY A 1 4458 ? 170.470 145.838 178.952 1.00 123.58 ? 4458 GLY A N     1 
ATOM   20260 C CA    . GLY A 1 4458 ? 171.386 146.092 180.044 1.00 123.58 ? 4458 GLY A CA    1 
ATOM   20261 C C     . GLY A 1 4458 ? 172.252 147.321 179.912 1.00 123.58 ? 4458 GLY A C     1 
ATOM   20262 O O     . GLY A 1 4458 ? 173.386 147.312 180.403 1.00 123.58 ? 4458 GLY A O     1 
ATOM   20263 N N     . ILE A 1 4459 ? 171.764 148.380 179.274 1.00 121.71 ? 4459 ILE A N     1 
ATOM   20264 C CA    . ILE A 1 4459 ? 172.494 149.638 179.162 1.00 121.71 ? 4459 ILE A CA    1 
ATOM   20265 C C     . ILE A 1 4459 ? 171.765 150.694 179.980 1.00 121.71 ? 4459 ILE A C     1 
ATOM   20266 O O     . ILE A 1 4459 ? 170.552 150.878 179.831 1.00 121.71 ? 4459 ILE A O     1 
ATOM   20267 C CB    . ILE A 1 4459 ? 172.636 150.074 177.694 1.00 121.71 ? 4459 ILE A CB    1 
ATOM   20268 C CG1   . ILE A 1 4459 ? 173.293 148.965 176.869 1.00 121.71 ? 4459 ILE A CG1   1 
ATOM   20269 C CG2   . ILE A 1 4459 ? 173.442 151.359 177.599 1.00 121.71 ? 4459 ILE A CG2   1 
ATOM   20270 C CD1   . ILE A 1 4459 ? 174.540 148.381 177.501 1.00 121.71 ? 4459 ILE A CD1   1 
ATOM   20271 N N     . LEU A 1 4460 ? 172.499 151.382 180.846 1.00 114.32 ? 4460 LEU A N     1 
ATOM   20272 C CA    . LEU A 1 4460 ? 171.874 152.346 181.738 1.00 114.32 ? 4460 LEU A CA    1 
ATOM   20273 C C     . LEU A 1 4460 ? 171.249 153.482 180.931 1.00 114.32 ? 4460 LEU A C     1 
ATOM   20274 O O     . LEU A 1 4460 ? 171.846 153.959 179.959 1.00 114.32 ? 4460 LEU A O     1 
ATOM   20275 C CB    . LEU A 1 4460 ? 172.902 152.875 182.744 1.00 114.32 ? 4460 LEU A CB    1 
ATOM   20276 C CG    . LEU A 1 4460 ? 173.868 154.022 182.432 1.00 114.32 ? 4460 LEU A CG    1 
ATOM   20277 C CD1   . LEU A 1 4460 ? 173.244 155.386 182.661 1.00 114.32 ? 4460 LEU A CD1   1 
ATOM   20278 C CD2   . LEU A 1 4460 ? 175.133 153.872 183.255 1.00 114.32 ? 4460 LEU A CD2   1 
ATOM   20279 N N     . PRO A 1 4461 ? 170.045 153.922 181.290 1.00 113.67 ? 4461 PRO A N     1 
ATOM   20280 C CA    . PRO A 1 4461 ? 169.352 154.931 180.483 1.00 113.67 ? 4461 PRO A CA    1 
ATOM   20281 C C     . PRO A 1 4461 ? 170.079 156.265 180.459 1.00 113.67 ? 4461 PRO A C     1 
ATOM   20282 O O     . PRO A 1 4461 ? 170.672 156.699 181.449 1.00 113.67 ? 4461 PRO A O     1 
ATOM   20283 C CB    . PRO A 1 4461 ? 167.990 155.060 181.174 1.00 113.67 ? 4461 PRO A CB    1 
ATOM   20284 C CG    . PRO A 1 4461 ? 167.835 153.791 181.947 1.00 113.67 ? 4461 PRO A CG    1 
ATOM   20285 C CD    . PRO A 1 4461 ? 169.211 153.435 182.397 1.00 113.67 ? 4461 PRO A CD    1 
ATOM   20286 N N     . ARG A 1 4462 ? 170.001 156.929 179.305 1.00 121.64 ? 4462 ARG A N     1 
ATOM   20287 C CA    . ARG A 1 4462 ? 170.680 158.209 179.141 1.00 121.64 ? 4462 ARG A CA    1 
ATOM   20288 C C     . ARG A 1 4462 ? 170.043 159.297 179.992 1.00 121.64 ? 4462 ARG A C     1 
ATOM   20289 O O     . ARG A 1 4462 ? 170.746 160.145 180.551 1.00 121.64 ? 4462 ARG A O     1 
ATOM   20290 C CB    . ARG A 1 4462 ? 170.680 158.615 177.669 1.00 121.64 ? 4462 ARG A CB    1 
ATOM   20291 C CG    . ARG A 1 4462 ? 171.299 157.593 176.716 1.00 121.64 ? 4462 ARG A CG    1 
ATOM   20292 C CD    . ARG A 1 4462 ? 172.560 156.895 177.259 1.00 121.64 ? 4462 ARG A CD    1 
ATOM   20293 N NE    . ARG A 1 4462 ? 173.475 157.762 178.002 1.00 121.64 ? 4462 ARG A NE    1 
ATOM   20294 C CZ    . ARG A 1 4462 ? 174.072 158.844 177.515 1.00 121.64 ? 4462 ARG A CZ    1 
ATOM   20295 N NH1   . ARG A 1 4462 ? 173.898 159.230 176.262 1.00 121.64 ? 4462 ARG A NH1   1 
ATOM   20296 N NH2   . ARG A 1 4462 ? 174.870 159.554 178.307 1.00 121.64 ? 4462 ARG A NH2   1 
ATOM   20297 N N     . SER A 1 4463 ? 168.716 159.291 180.109 1.00 123.93 ? 4463 SER A N     1 
ATOM   20298 C CA    . SER A 1 4463 ? 168.036 160.310 180.898 1.00 123.93 ? 4463 SER A CA    1 
ATOM   20299 C C     . SER A 1 4463 ? 168.236 160.133 182.395 1.00 123.93 ? 4463 SER A C     1 
ATOM   20300 O O     . SER A 1 4463 ? 167.609 160.858 183.174 1.00 123.93 ? 4463 SER A O     1 
ATOM   20301 C CB    . SER A 1 4463 ? 166.541 160.313 180.576 1.00 123.93 ? 4463 SER A CB    1 
ATOM   20302 O OG    . SER A 1 4463 ? 165.836 159.421 181.420 1.00 123.93 ? 4463 SER A OG    1 
ATOM   20303 N N     . TRP A 1 4464 ? 169.081 159.195 182.815 1.00 117.28 ? 4464 TRP A N     1 
ATOM   20304 C CA    . TRP A 1 4464 ? 169.318 158.937 184.227 1.00 117.28 ? 4464 TRP A CA    1 
ATOM   20305 C C     . TRP A 1 4464 ? 170.704 159.348 184.690 1.00 117.28 ? 4464 TRP A C     1 
ATOM   20306 O O     . TRP A 1 4464 ? 170.860 159.764 185.842 1.00 117.28 ? 4464 TRP A O     1 
ATOM   20307 C CB    . TRP A 1 4464 ? 169.121 157.450 184.530 1.00 117.28 ? 4464 TRP A CB    1 
ATOM   20308 C CG    . TRP A 1 4464 ? 167.730 156.959 184.316 1.00 117.28 ? 4464 TRP A CG    1 
ATOM   20309 C CD1   . TRP A 1 4464 ? 166.714 157.613 183.688 1.00 117.28 ? 4464 TRP A CD1   1 
ATOM   20310 C CD2   . TRP A 1 4464 ? 167.207 155.690 184.709 1.00 117.28 ? 4464 TRP A CD2   1 
ATOM   20311 N NE1   . TRP A 1 4464 ? 165.585 156.834 183.678 1.00 117.28 ? 4464 TRP A NE1   1 
ATOM   20312 C CE2   . TRP A 1 4464 ? 165.864 155.646 184.299 1.00 117.28 ? 4464 TRP A CE2   1 
ATOM   20313 C CE3   . TRP A 1 4464 ? 167.744 154.586 185.375 1.00 117.28 ? 4464 TRP A CE3   1 
ATOM   20314 C CZ2   . TRP A 1 4464 ? 165.052 154.546 184.530 1.00 117.28 ? 4464 TRP A CZ2   1 
ATOM   20315 C CZ3   . TRP A 1 4464 ? 166.938 153.497 185.602 1.00 117.28 ? 4464 TRP A CZ3   1 
ATOM   20316 C CH2   . TRP A 1 4464 ? 165.608 153.483 185.180 1.00 117.28 ? 4464 TRP A CH2   1 
ATOM   20317 N N     . SER A 1 4465 ? 171.709 159.245 183.826 1.00 112.74 ? 4465 SER A N     1 
ATOM   20318 C CA    . SER A 1 4465 ? 173.093 159.519 184.204 1.00 112.74 ? 4465 SER A CA    1 
ATOM   20319 C C     . SER A 1 4465 ? 173.282 161.024 184.327 1.00 112.74 ? 4465 SER A C     1 
ATOM   20320 O O     . SER A 1 4465 ? 173.778 161.690 183.419 1.00 112.74 ? 4465 SER A O     1 
ATOM   20321 C CB    . SER A 1 4465 ? 174.054 158.923 183.184 1.00 112.74 ? 4465 SER A CB    1 
ATOM   20322 O OG    . SER A 1 4465 ? 175.290 159.613 183.193 1.00 112.74 ? 4465 SER A OG    1 
ATOM   20323 N N     . HIS A 1 4466 ? 172.878 161.568 185.471 1.00 112.64 ? 4466 HIS A N     1 
ATOM   20324 C CA    . HIS A 1 4466 ? 173.068 162.980 185.766 1.00 112.64 ? 4466 HIS A CA    1 
ATOM   20325 C C     . HIS A 1 4466 ? 174.325 163.248 186.581 1.00 112.64 ? 4466 HIS A C     1 
ATOM   20326 O O     . HIS A 1 4466 ? 174.586 164.404 186.926 1.00 112.64 ? 4466 HIS A O     1 
ATOM   20327 C CB    . HIS A 1 4466 ? 171.846 163.536 186.499 1.00 112.64 ? 4466 HIS A CB    1 
ATOM   20328 C CG    . HIS A 1 4466 ? 170.689 163.828 185.598 1.00 112.64 ? 4466 HIS A CG    1 
ATOM   20329 N ND1   . HIS A 1 4466 ? 170.398 163.062 184.490 1.00 112.64 ? 4466 HIS A ND1   1 
ATOM   20330 C CD2   . HIS A 1 4466 ? 169.751 164.803 185.639 1.00 112.64 ? 4466 HIS A CD2   1 
ATOM   20331 C CE1   . HIS A 1 4466 ? 169.330 163.551 183.888 1.00 112.64 ? 4466 HIS A CE1   1 
ATOM   20332 N NE2   . HIS A 1 4466 ? 168.917 164.608 184.565 1.00 112.64 ? 4466 HIS A NE2   1 
ATOM   20333 N N     . TYR A 1 4467 ? 175.101 162.216 186.899 1.00 99.80  ? 4467 TYR A N     1 
ATOM   20334 C CA    . TYR A 1 4467 ? 176.360 162.372 187.610 1.00 99.80  ? 4467 TYR A CA    1 
ATOM   20335 C C     . TYR A 1 4467 ? 177.398 161.450 186.987 1.00 99.80  ? 4467 TYR A C     1 
ATOM   20336 O O     . TYR A 1 4467 ? 177.070 160.497 186.276 1.00 99.80  ? 4467 TYR A O     1 
ATOM   20337 C CB    . TYR A 1 4467 ? 176.201 162.082 189.108 1.00 99.80  ? 4467 TYR A CB    1 
ATOM   20338 C CG    . TYR A 1 4467 ? 175.659 160.711 189.421 1.00 99.80  ? 4467 TYR A CG    1 
ATOM   20339 C CD1   . TYR A 1 4467 ? 176.514 159.657 189.703 1.00 99.80  ? 4467 TYR A CD1   1 
ATOM   20340 C CD2   . TYR A 1 4467 ? 174.296 160.468 189.433 1.00 99.80  ? 4467 TYR A CD2   1 
ATOM   20341 C CE1   . TYR A 1 4467 ? 176.027 158.402 189.993 1.00 99.80  ? 4467 TYR A CE1   1 
ATOM   20342 C CE2   . TYR A 1 4467 ? 173.800 159.216 189.722 1.00 99.80  ? 4467 TYR A CE2   1 
ATOM   20343 C CZ    . TYR A 1 4467 ? 174.670 158.187 189.999 1.00 99.80  ? 4467 TYR A CZ    1 
ATOM   20344 O OH    . TYR A 1 4467 ? 174.181 156.934 190.285 1.00 99.80  ? 4467 TYR A OH    1 
ATOM   20345 N N     . THR A 1 4468 ? 178.666 161.751 187.259 1.00 94.97  ? 4468 THR A N     1 
ATOM   20346 C CA    . THR A 1 4468 ? 179.764 161.036 186.623 1.00 94.97  ? 4468 THR A CA    1 
ATOM   20347 C C     . THR A 1 4468 ? 179.741 159.559 186.992 1.00 94.97  ? 4468 THR A C     1 
ATOM   20348 O O     . THR A 1 4468 ? 179.586 159.198 188.161 1.00 94.97  ? 4468 THR A O     1 
ATOM   20349 C CB    . THR A 1 4468 ? 181.098 161.655 187.031 1.00 94.97  ? 4468 THR A CB    1 
ATOM   20350 O OG1   . THR A 1 4468 ? 180.949 163.074 187.148 1.00 94.97  ? 4468 THR A OG1   1 
ATOM   20351 C CG2   . THR A 1 4468 ? 182.160 161.346 185.994 1.00 94.97  ? 4468 THR A CG2   1 
ATOM   20352 N N     . VAL A 1 4469 ? 179.901 158.704 185.985 1.00 88.93  ? 4469 VAL A N     1 
ATOM   20353 C CA    . VAL A 1 4469 ? 179.893 157.257 186.196 1.00 88.93  ? 4469 VAL A CA    1 
ATOM   20354 C C     . VAL A 1 4469 ? 180.964 156.620 185.334 1.00 88.93  ? 4469 VAL A C     1 
ATOM   20355 O O     . VAL A 1 4469 ? 181.328 157.135 184.268 1.00 88.93  ? 4469 VAL A O     1 
ATOM   20356 C CB    . VAL A 1 4469 ? 178.524 156.640 185.855 1.00 88.93  ? 4469 VAL A CB    1 
ATOM   20357 C CG1   . VAL A 1 4469 ? 177.547 156.868 186.991 1.00 88.93  ? 4469 VAL A CG1   1 
ATOM   20358 C CG2   . VAL A 1 4469 ? 177.992 157.231 184.563 1.00 88.93  ? 4469 VAL A CG2   1 
ATOM   20359 N N     . PRO A 1 4470 ? 181.499 155.486 185.782 1.00 87.41  ? 4470 PRO A N     1 
ATOM   20360 C CA    . PRO A 1 4470 ? 182.497 154.778 184.975 1.00 87.41  ? 4470 PRO A CA    1 
ATOM   20361 C C     . PRO A 1 4470 ? 181.918 154.327 183.645 1.00 87.41  ? 4470 PRO A C     1 
ATOM   20362 O O     . PRO A 1 4470 ? 180.733 154.011 183.530 1.00 87.41  ? 4470 PRO A O     1 
ATOM   20363 C CB    . PRO A 1 4470 ? 182.881 153.581 185.850 1.00 87.41  ? 4470 PRO A CB    1 
ATOM   20364 C CG    . PRO A 1 4470 ? 182.513 153.981 187.230 1.00 87.41  ? 4470 PRO A CG    1 
ATOM   20365 C CD    . PRO A 1 4470 ? 181.313 154.862 187.102 1.00 87.41  ? 4470 PRO A CD    1 
ATOM   20366 N N     . ALA A 1 4471 ? 182.776 154.308 182.630 1.00 100.34 ? 4471 ALA A N     1 
ATOM   20367 C CA    . ALA A 1 4471 ? 182.351 153.899 181.300 1.00 100.34 ? 4471 ALA A CA    1 
ATOM   20368 C C     . ALA A 1 4471 ? 181.967 152.426 181.288 1.00 100.34 ? 4471 ALA A C     1 
ATOM   20369 O O     . ALA A 1 4471 ? 182.613 151.594 181.930 1.00 100.34 ? 4471 ALA A O     1 
ATOM   20370 C CB    . ALA A 1 4471 ? 183.461 154.157 180.284 1.00 100.34 ? 4471 ALA A CB    1 
ATOM   20371 N N     . GLY A 1 4472 ? 180.909 152.107 180.547 1.00 99.82  ? 4472 GLY A N     1 
ATOM   20372 C CA    . GLY A 1 4472 ? 180.454 150.736 180.436 1.00 99.82  ? 4472 GLY A CA    1 
ATOM   20373 C C     . GLY A 1 4472 ? 180.007 150.152 181.759 1.00 99.82  ? 4472 GLY A C     1 
ATOM   20374 O O     . GLY A 1 4472 ? 180.408 149.043 182.122 1.00 99.82  ? 4472 GLY A O     1 
ATOM   20375 N N     . MET A 1 4473 ? 179.186 150.893 182.496 1.00 102.71 ? 4473 MET A N     1 
ATOM   20376 C CA    . MET A 1 4473 ? 178.759 150.495 183.830 1.00 102.71 ? 4473 MET A CA    1 
ATOM   20377 C C     . MET A 1 4473 ? 177.362 149.895 183.742 1.00 102.71 ? 4473 MET A C     1 
ATOM   20378 O O     . MET A 1 4473 ? 176.431 150.543 183.252 1.00 102.71 ? 4473 MET A O     1 
ATOM   20379 C CB    . MET A 1 4473 ? 178.791 151.685 184.787 1.00 102.71 ? 4473 MET A CB    1 
ATOM   20380 C CG    . MET A 1 4473 ? 178.865 151.293 186.248 1.00 102.71 ? 4473 MET A CG    1 
ATOM   20381 S SD    . MET A 1 4473 ? 177.294 151.384 187.109 1.00 102.71 ? 4473 MET A SD    1 
ATOM   20382 C CE    . MET A 1 4473 ? 177.584 152.817 188.141 1.00 102.71 ? 4473 MET A CE    1 
ATOM   20383 N N     . THR A 1 4474 ? 177.225 148.664 184.221 1.00 102.75 ? 4474 THR A N     1 
ATOM   20384 C CA    . THR A 1 4474 ? 176.005 147.894 184.047 1.00 102.75 ? 4474 THR A CA    1 
ATOM   20385 C C     . THR A 1 4474 ? 174.875 148.473 184.900 1.00 102.75 ? 4474 THR A C     1 
ATOM   20386 O O     . THR A 1 4474 ? 175.099 149.088 185.946 1.00 102.75 ? 4474 THR A O     1 
ATOM   20387 C CB    . THR A 1 4474 ? 176.291 146.426 184.381 1.00 102.75 ? 4474 THR A CB    1 
ATOM   20388 O OG1   . THR A 1 4474 ? 176.893 145.796 183.244 1.00 102.75 ? 4474 THR A OG1   1 
ATOM   20389 C CG2   . THR A 1 4474 ? 175.041 145.660 184.760 1.00 102.75 ? 4474 THR A CG2   1 
ATOM   20390 N N     . VAL A 1 4475 ? 173.641 148.272 184.425 1.00 106.37 ? 4475 VAL A N     1 
ATOM   20391 C CA    . VAL A 1 4475 ? 172.474 148.884 185.054 1.00 106.37 ? 4475 VAL A CA    1 
ATOM   20392 C C     . VAL A 1 4475 ? 172.296 148.392 186.483 1.00 106.37 ? 4475 VAL A C     1 
ATOM   20393 O O     . VAL A 1 4475 ? 171.882 149.154 187.362 1.00 106.37 ? 4475 VAL A O     1 
ATOM   20394 C CB    . VAL A 1 4475 ? 171.214 148.611 184.215 1.00 106.37 ? 4475 VAL A CB    1 
ATOM   20395 C CG1   . VAL A 1 4475 ? 170.077 149.509 184.665 1.00 106.37 ? 4475 VAL A CG1   1 
ATOM   20396 C CG2   . VAL A 1 4475 ? 171.511 148.817 182.758 1.00 106.37 ? 4475 VAL A CG2   1 
ATOM   20397 N N     . ILE A 1 4476 ? 172.564 147.110 186.736 1.00 100.88 ? 4476 ILE A N     1 
ATOM   20398 C CA    . ILE A 1 4476 ? 172.425 146.604 188.099 1.00 100.88 ? 4476 ILE A CA    1 
ATOM   20399 C C     . ILE A 1 4476 ? 173.443 147.263 189.021 1.00 100.88 ? 4476 ILE A C     1 
ATOM   20400 O O     . ILE A 1 4476 ? 173.120 147.655 190.151 1.00 100.88 ? 4476 ILE A O     1 
ATOM   20401 C CB    . ILE A 1 4476 ? 172.531 145.069 188.134 1.00 100.88 ? 4476 ILE A CB    1 
ATOM   20402 C CG1   . ILE A 1 4476 ? 171.582 144.436 187.113 1.00 100.88 ? 4476 ILE A CG1   1 
ATOM   20403 C CG2   . ILE A 1 4476 ? 172.218 144.559 189.527 1.00 100.88 ? 4476 ILE A CG2   1 
ATOM   20404 C CD1   . ILE A 1 4476 ? 172.257 143.905 185.881 1.00 100.88 ? 4476 ILE A CD1   1 
ATOM   20405 N N     . GLN A 1 4477 ? 174.686 147.397 188.560 1.00 102.33 ? 4477 GLN A N     1 
ATOM   20406 C CA    . GLN A 1 4477 ? 175.667 148.130 189.350 1.00 102.33 ? 4477 GLN A CA    1 
ATOM   20407 C C     . GLN A 1 4477 ? 175.228 149.573 189.547 1.00 102.33 ? 4477 GLN A C     1 
ATOM   20408 O O     . GLN A 1 4477 ? 175.397 150.139 190.635 1.00 102.33 ? 4477 GLN A O     1 
ATOM   20409 C CB    . GLN A 1 4477 ? 177.041 148.064 188.685 1.00 102.33 ? 4477 GLN A CB    1 
ATOM   20410 C CG    . GLN A 1 4477 ? 177.355 146.735 188.020 1.00 102.33 ? 4477 GLN A CG    1 
ATOM   20411 C CD    . GLN A 1 4477 ? 178.468 146.843 186.994 1.00 102.33 ? 4477 GLN A CD    1 
ATOM   20412 O OE1   . GLN A 1 4477 ? 178.861 145.852 186.380 1.00 102.33 ? 4477 GLN A OE1   1 
ATOM   20413 N NE2   . GLN A 1 4477 ? 178.973 148.053 186.794 1.00 102.33 ? 4477 GLN A NE2   1 
ATOM   20414 N N     . TRP A 1 4478 ? 174.642 150.179 188.512 1.00 101.11 ? 4478 TRP A N     1 
ATOM   20415 C CA    . TRP A 1 4478 ? 174.190 151.561 188.625 1.00 101.11 ? 4478 TRP A CA    1 
ATOM   20416 C C     . TRP A 1 4478 ? 173.105 151.704 189.681 1.00 101.11 ? 4478 TRP A C     1 
ATOM   20417 O O     . TRP A 1 4478 ? 173.131 152.637 190.488 1.00 101.11 ? 4478 TRP A O     1 
ATOM   20418 C CB    . TRP A 1 4478 ? 173.687 152.068 187.276 1.00 101.11 ? 4478 TRP A CB    1 
ATOM   20419 C CG    . TRP A 1 4478 ? 173.422 153.541 187.269 1.00 101.11 ? 4478 TRP A CG    1 
ATOM   20420 C CD1   . TRP A 1 4478 ? 174.274 154.521 186.867 1.00 101.11 ? 4478 TRP A CD1   1 
ATOM   20421 C CD2   . TRP A 1 4478 ? 172.225 154.200 187.694 1.00 101.11 ? 4478 TRP A CD2   1 
ATOM   20422 N NE1   . TRP A 1 4478 ? 173.684 155.751 187.009 1.00 101.11 ? 4478 TRP A NE1   1 
ATOM   20423 C CE2   . TRP A 1 4478 ? 172.424 155.580 187.516 1.00 101.11 ? 4478 TRP A CE2   1 
ATOM   20424 C CE3   . TRP A 1 4478 ? 171.004 153.757 188.204 1.00 101.11 ? 4478 TRP A CE3   1 
ATOM   20425 C CZ2   . TRP A 1 4478 ? 171.449 156.520 187.828 1.00 101.11 ? 4478 TRP A CZ2   1 
ATOM   20426 C CZ3   . TRP A 1 4478 ? 170.038 154.691 188.515 1.00 101.11 ? 4478 TRP A CZ3   1 
ATOM   20427 C CH2   . TRP A 1 4478 ? 170.266 156.056 188.326 1.00 101.11 ? 4478 TRP A CH2   1 
ATOM   20428 N N     . VAL A 1 4479 ? 172.134 150.791 189.687 1.00 100.87 ? 4479 VAL A N     1 
ATOM   20429 C CA    . VAL A 1 4479 ? 171.030 150.918 190.630 1.00 100.87 ? 4479 VAL A CA    1 
ATOM   20430 C C     . VAL A 1 4479 ? 171.501 150.607 192.044 1.00 100.87 ? 4479 VAL A C     1 
ATOM   20431 O O     . VAL A 1 4479 ? 171.042 151.226 193.009 1.00 100.87 ? 4479 VAL A O     1 
ATOM   20432 C CB    . VAL A 1 4479 ? 169.839 150.038 190.206 1.00 100.87 ? 4479 VAL A CB    1 
ATOM   20433 C CG1   . VAL A 1 4479 ? 170.237 148.593 190.100 1.00 100.87 ? 4479 VAL A CG1   1 
ATOM   20434 C CG2   . VAL A 1 4479 ? 168.689 150.199 191.176 1.00 100.87 ? 4479 VAL A CG2   1 
ATOM   20435 N N     . SER A 1 4480 ? 172.432 149.663 192.197 1.00 102.57 ? 4480 SER A N     1 
ATOM   20436 C CA    . SER A 1 4480 ? 172.990 149.408 193.522 1.00 102.57 ? 4480 SER A CA    1 
ATOM   20437 C C     . SER A 1 4480 ? 173.724 150.637 194.049 1.00 102.57 ? 4480 SER A C     1 
ATOM   20438 O O     . SER A 1 4480 ? 173.553 151.033 195.211 1.00 102.57 ? 4480 SER A O     1 
ATOM   20439 C CB    . SER A 1 4480 ? 173.921 148.199 193.475 1.00 102.57 ? 4480 SER A CB    1 
ATOM   20440 O OG    . SER A 1 4480 ? 175.013 148.439 192.607 1.00 102.57 ? 4480 SER A OG    1 
ATOM   20441 N N     . ASP A 1 4481 ? 174.538 151.265 193.197 1.00 105.22 ? 4481 ASP A N     1 
ATOM   20442 C CA    . ASP A 1 4481 ? 175.238 152.475 193.609 1.00 105.22 ? 4481 ASP A CA    1 
ATOM   20443 C C     . ASP A 1 4481 ? 174.256 153.591 193.930 1.00 105.22 ? 4481 ASP A C     1 
ATOM   20444 O O     . ASP A 1 4481 ? 174.453 154.344 194.888 1.00 105.22 ? 4481 ASP A O     1 
ATOM   20445 C CB    . ASP A 1 4481 ? 176.210 152.921 192.522 1.00 105.22 ? 4481 ASP A CB    1 
ATOM   20446 C CG    . ASP A 1 4481 ? 176.957 154.181 192.898 1.00 105.22 ? 4481 ASP A CG    1 
ATOM   20447 O OD1   . ASP A 1 4481 ? 177.208 154.384 194.103 1.00 105.22 ? 4481 ASP A OD1   1 
ATOM   20448 O OD2   . ASP A 1 4481 ? 177.285 154.975 191.992 1.00 105.22 ? 4481 ASP A OD2   1 
ATOM   20449 N N     . PHE A 1 4482 ? 173.195 153.717 193.132 1.00 102.13 ? 4482 PHE A N     1 
ATOM   20450 C CA    . PHE A 1 4482 ? 172.185 154.733 193.397 1.00 102.13 ? 4482 PHE A CA    1 
ATOM   20451 C C     . PHE A 1 4482 ? 171.509 154.491 194.737 1.00 102.13 ? 4482 PHE A C     1 
ATOM   20452 O O     . PHE A 1 4482 ? 171.240 155.437 195.484 1.00 102.13 ? 4482 PHE A O     1 
ATOM   20453 C CB    . PHE A 1 4482 ? 171.154 154.748 192.272 1.00 102.13 ? 4482 PHE A CB    1 
ATOM   20454 C CG    . PHE A 1 4482 ? 170.282 155.962 192.272 1.00 102.13 ? 4482 PHE A CG    1 
ATOM   20455 C CD1   . PHE A 1 4482 ? 170.678 157.111 191.617 1.00 102.13 ? 4482 PHE A CD1   1 
ATOM   20456 C CD2   . PHE A 1 4482 ? 169.066 155.955 192.926 1.00 102.13 ? 4482 PHE A CD2   1 
ATOM   20457 C CE1   . PHE A 1 4482 ? 169.878 158.231 191.613 1.00 102.13 ? 4482 PHE A CE1   1 
ATOM   20458 C CE2   . PHE A 1 4482 ? 168.262 157.072 192.924 1.00 102.13 ? 4482 PHE A CE2   1 
ATOM   20459 C CZ    . PHE A 1 4482 ? 168.669 158.212 192.268 1.00 102.13 ? 4482 PHE A CZ    1 
ATOM   20460 N N     . SER A 1 4483 ? 171.225 153.229 195.055 1.00 102.26 ? 4483 SER A N     1 
ATOM   20461 C CA    . SER A 1 4483 ? 170.639 152.905 196.349 1.00 102.26 ? 4483 SER A CA    1 
ATOM   20462 C C     . SER A 1 4483 ? 171.569 153.300 197.485 1.00 102.26 ? 4483 SER A C     1 
ATOM   20463 O O     . SER A 1 4483 ? 171.129 153.884 198.483 1.00 102.26 ? 4483 SER A O     1 
ATOM   20464 C CB    . SER A 1 4483 ? 170.325 151.415 196.418 1.00 102.26 ? 4483 SER A CB    1 
ATOM   20465 O OG    . SER A 1 4483 ? 171.517 150.663 196.553 1.00 102.26 ? 4483 SER A OG    1 
ATOM   20466 N N     . GLU A 1 4484 ? 172.859 152.990 197.354 1.00 102.78 ? 4484 GLU A N     1 
ATOM   20467 C CA    . GLU A 1 4484 ? 173.805 153.380 198.396 1.00 102.78 ? 4484 GLU A CA    1 
ATOM   20468 C C     . GLU A 1 4484 ? 173.871 154.896 198.543 1.00 102.78 ? 4484 GLU A C     1 
ATOM   20469 O O     . GLU A 1 4484 ? 173.892 155.421 199.665 1.00 102.78 ? 4484 GLU A O     1 
ATOM   20470 C CB    . GLU A 1 4484 ? 175.188 152.811 198.096 1.00 102.78 ? 4484 GLU A CB    1 
ATOM   20471 C CG    . GLU A 1 4484 ? 175.193 151.322 197.847 1.00 102.78 ? 4484 GLU A CG    1 
ATOM   20472 C CD    . GLU A 1 4484 ? 175.451 150.532 199.109 1.00 102.78 ? 4484 GLU A CD    1 
ATOM   20473 O OE1   . GLU A 1 4484 ? 175.119 149.329 199.139 1.00 102.78 ? 4484 GLU A OE1   1 
ATOM   20474 O OE2   . GLU A 1 4484 ? 175.987 151.118 200.072 1.00 102.78 ? 4484 GLU A OE2   1 
ATOM   20475 N N     . ARG A 1 4485 ? 173.898 155.615 197.419 1.00 95.88  ? 4485 ARG A N     1 
ATOM   20476 C CA    . ARG A 1 4485 ? 173.944 157.071 197.477 1.00 95.88  ? 4485 ARG A CA    1 
ATOM   20477 C C     . ARG A 1 4485 ? 172.702 157.629 198.154 1.00 95.88  ? 4485 ARG A C     1 
ATOM   20478 O O     . ARG A 1 4485 ? 172.789 158.568 198.953 1.00 95.88  ? 4485 ARG A O     1 
ATOM   20479 C CB    . ARG A 1 4485 ? 174.084 157.654 196.072 1.00 95.88  ? 4485 ARG A CB    1 
ATOM   20480 C CG    . ARG A 1 4485 ? 175.351 157.261 195.343 1.00 95.88  ? 4485 ARG A CG    1 
ATOM   20481 C CD    . ARG A 1 4485 ? 175.340 157.811 193.925 1.00 95.88  ? 4485 ARG A CD    1 
ATOM   20482 N NE    . ARG A 1 4485 ? 176.436 157.293 193.117 1.00 95.88  ? 4485 ARG A NE    1 
ATOM   20483 C CZ    . ARG A 1 4485 ? 177.600 157.904 192.953 1.00 95.88  ? 4485 ARG A CZ    1 
ATOM   20484 N NH1   . ARG A 1 4485 ? 177.864 159.057 193.544 1.00 95.88  ? 4485 ARG A NH1   1 
ATOM   20485 N NH2   . ARG A 1 4485 ? 178.522 157.344 192.178 1.00 95.88  ? 4485 ARG A NH2   1 
ATOM   20486 N N     . ILE A 1 4486 ? 171.536 157.063 197.847 1.00 101.83 ? 4486 ILE A N     1 
ATOM   20487 C CA    . ILE A 1 4486 ? 170.302 157.559 198.440 1.00 101.83 ? 4486 ILE A CA    1 
ATOM   20488 C C     . ILE A 1 4486 ? 170.269 157.262 199.931 1.00 101.83 ? 4486 ILE A C     1 
ATOM   20489 O O     . ILE A 1 4486 ? 169.781 158.073 200.723 1.00 101.83 ? 4486 ILE A O     1 
ATOM   20490 C CB    . ILE A 1 4486 ? 169.086 156.971 197.708 1.00 101.83 ? 4486 ILE A CB    1 
ATOM   20491 C CG1   . ILE A 1 4486 ? 169.020 157.530 196.291 1.00 101.83 ? 4486 ILE A CG1   1 
ATOM   20492 C CG2   . ILE A 1 4486 ? 167.807 157.296 198.451 1.00 101.83 ? 4486 ILE A CG2   1 
ATOM   20493 C CD1   . ILE A 1 4486 ? 168.611 158.979 196.234 1.00 101.83 ? 4486 ILE A CD1   1 
ATOM   20494 N N     . LYS A 1 4487 ? 170.785 156.103 200.344 1.00 104.40 ? 4487 LYS A N     1 
ATOM   20495 C CA    . LYS A 1 4487 ? 170.870 155.820 201.774 1.00 104.40 ? 4487 LYS A CA    1 
ATOM   20496 C C     . LYS A 1 4487 ? 171.784 156.818 202.475 1.00 104.40 ? 4487 LYS A C     1 
ATOM   20497 O O     . LYS A 1 4487 ? 171.458 157.325 203.558 1.00 104.40 ? 4487 LYS A O     1 
ATOM   20498 C CB    . LYS A 1 4487 ? 171.359 154.391 202.004 1.00 104.40 ? 4487 LYS A CB    1 
ATOM   20499 C CG    . LYS A 1 4487 ? 170.421 153.319 201.483 1.00 104.40 ? 4487 LYS A CG    1 
ATOM   20500 C CD    . LYS A 1 4487 ? 171.055 151.943 201.582 1.00 104.40 ? 4487 LYS A CD    1 
ATOM   20501 C CE    . LYS A 1 4487 ? 170.020 150.869 201.864 1.00 104.40 ? 4487 LYS A CE    1 
ATOM   20502 N NZ    . LYS A 1 4487 ? 170.601 149.505 201.732 1.00 104.40 ? 4487 LYS A NZ    1 
ATOM   20503 N N     . GLN A 1 4488 ? 172.929 157.122 201.864 1.00 96.14  ? 4488 GLN A N     1 
ATOM   20504 C CA    . GLN A 1 4488 ? 173.834 158.102 202.451 1.00 96.14  ? 4488 GLN A CA    1 
ATOM   20505 C C     . GLN A 1 4488 ? 173.166 159.468 202.553 1.00 96.14  ? 4488 GLN A C     1 
ATOM   20506 O O     . GLN A 1 4488 ? 173.289 160.158 203.572 1.00 96.14  ? 4488 GLN A O     1 
ATOM   20507 C CB    . GLN A 1 4488 ? 175.114 158.183 201.625 1.00 96.14  ? 4488 GLN A CB    1 
ATOM   20508 C CG    . GLN A 1 4488 ? 176.061 159.283 202.045 1.00 96.14  ? 4488 GLN A CG    1 
ATOM   20509 C CD    . GLN A 1 4488 ? 177.345 159.268 201.248 1.00 96.14  ? 4488 GLN A CD    1 
ATOM   20510 O OE1   . GLN A 1 4488 ? 178.438 159.295 201.811 1.00 96.14  ? 4488 GLN A OE1   1 
ATOM   20511 N NE2   . GLN A 1 4488 ? 177.221 159.222 199.929 1.00 96.14  ? 4488 GLN A NE2   1 
ATOM   20512 N N     . LEU A 1 4489 ? 172.441 159.867 201.509 1.00 99.54  ? 4489 LEU A N     1 
ATOM   20513 C CA    . LEU A 1 4489 ? 171.762 161.156 201.531 1.00 99.54  ? 4489 LEU A CA    1 
ATOM   20514 C C     . LEU A 1 4489 ? 170.638 161.181 202.557 1.00 99.54  ? 4489 LEU A C     1 
ATOM   20515 O O     . LEU A 1 4489 ? 170.385 162.223 203.170 1.00 99.54  ? 4489 LEU A O     1 
ATOM   20516 C CB    . LEU A 1 4489 ? 171.230 161.487 200.139 1.00 99.54  ? 4489 LEU A CB    1 
ATOM   20517 C CG    . LEU A 1 4489 ? 172.303 161.785 199.092 1.00 99.54  ? 4489 LEU A CG    1 
ATOM   20518 C CD1   . LEU A 1 4489 ? 171.706 162.528 197.917 1.00 99.54  ? 4489 LEU A CD1   1 
ATOM   20519 C CD2   . LEU A 1 4489 ? 173.441 162.580 199.701 1.00 99.54  ? 4489 LEU A CD2   1 
ATOM   20520 N N     . GLN A 1 4490 ? 169.949 160.057 202.752 1.00 105.34 ? 4490 GLN A N     1 
ATOM   20521 C CA    . GLN A 1 4490 ? 168.941 159.981 203.802 1.00 105.34 ? 4490 GLN A CA    1 
ATOM   20522 C C     . GLN A 1 4490 ? 169.574 160.151 205.174 1.00 105.34 ? 4490 GLN A C     1 
ATOM   20523 O O     . GLN A 1 4490 ? 169.019 160.831 206.045 1.00 105.34 ? 4490 GLN A O     1 
ATOM   20524 C CB    . GLN A 1 4490 ? 168.193 158.653 203.723 1.00 105.34 ? 4490 GLN A CB    1 
ATOM   20525 C CG    . GLN A 1 4490 ? 166.938 158.696 202.877 1.00 105.34 ? 4490 GLN A CG    1 
ATOM   20526 C CD    . GLN A 1 4490 ? 166.468 157.315 202.478 1.00 105.34 ? 4490 GLN A CD    1 
ATOM   20527 O OE1   . GLN A 1 4490 ? 165.756 157.151 201.488 1.00 105.34 ? 4490 GLN A OE1   1 
ATOM   20528 N NE2   . GLN A 1 4490 ? 166.868 156.310 203.246 1.00 105.34 ? 4490 GLN A NE2   1 
ATOM   20529 N N     . ASN A 1 4491 ? 170.736 159.531 205.386 1.00 105.78 ? 4491 ASN A N     1 
ATOM   20530 C CA    . ASN A 1 4491 ? 171.451 159.734 206.642 1.00 105.78 ? 4491 ASN A CA    1 
ATOM   20531 C C     . ASN A 1 4491 ? 171.837 161.196 206.816 1.00 105.78 ? 4491 ASN A C     1 
ATOM   20532 O O     . ASN A 1 4491 ? 171.739 161.749 207.919 1.00 105.78 ? 4491 ASN A O     1 
ATOM   20533 C CB    . ASN A 1 4491 ? 172.687 158.839 206.694 1.00 105.78 ? 4491 ASN A CB    1 
ATOM   20534 C CG    . ASN A 1 4491 ? 172.713 157.956 207.921 1.00 105.78 ? 4491 ASN A CG    1 
ATOM   20535 O OD1   . ASN A 1 4491 ? 171.823 158.028 208.768 1.00 105.78 ? 4491 ASN A OD1   1 
ATOM   20536 N ND2   . ASN A 1 4491 ? 173.733 157.115 208.025 1.00 105.78 ? 4491 ASN A ND2   1 
ATOM   20537 N N     . ILE A 1 4492 ? 172.276 161.837 205.732 1.00 103.40 ? 4492 ILE A N     1 
ATOM   20538 C CA    . ILE A 1 4492 ? 172.626 163.254 205.786 1.00 103.40 ? 4492 ILE A CA    1 
ATOM   20539 C C     . ILE A 1 4492 ? 171.416 164.083 206.190 1.00 103.40 ? 4492 ILE A C     1 
ATOM   20540 O O     . ILE A 1 4492 ? 171.502 164.968 207.050 1.00 103.40 ? 4492 ILE A O     1 
ATOM   20541 C CB    . ILE A 1 4492 ? 173.191 163.716 204.433 1.00 103.40 ? 4492 ILE A CB    1 
ATOM   20542 C CG1   . ILE A 1 4492 ? 174.601 163.170 204.231 1.00 103.40 ? 4492 ILE A CG1   1 
ATOM   20543 C CG2   . ILE A 1 4492 ? 173.190 165.229 204.346 1.00 103.40 ? 4492 ILE A CG2   1 
ATOM   20544 C CD1   . ILE A 1 4492 ? 175.519 163.456 205.384 1.00 103.40 ? 4492 ILE A CD1   1 
ATOM   20545 N N     . SER A 1 4493 ? 170.270 163.813 205.565 1.00 107.87 ? 4493 SER A N     1 
ATOM   20546 C CA    . SER A 1 4493 ? 169.060 164.564 205.876 1.00 107.87 ? 4493 SER A CA    1 
ATOM   20547 C C     . SER A 1 4493 ? 168.637 164.349 207.321 1.00 107.87 ? 4493 SER A C     1 
ATOM   20548 O O     . SER A 1 4493 ? 168.217 165.293 207.999 1.00 107.87 ? 4493 SER A O     1 
ATOM   20549 C CB    . SER A 1 4493 ? 167.933 164.161 204.930 1.00 107.87 ? 4493 SER A CB    1 
ATOM   20550 O OG    . SER A 1 4493 ? 167.167 163.109 205.488 1.00 107.87 ? 4493 SER A OG    1 
ATOM   20551 N N     . LEU A 1 4494 ? 168.731 163.111 207.806 1.00 110.33 ? 4494 LEU A N     1 
ATOM   20552 C CA    . LEU A 1 4494 ? 168.365 162.831 209.189 1.00 110.33 ? 4494 LEU A CA    1 
ATOM   20553 C C     . LEU A 1 4494 ? 169.277 163.571 210.161 1.00 110.33 ? 4494 LEU A C     1 
ATOM   20554 O O     . LEU A 1 4494 ? 168.807 164.146 211.151 1.00 110.33 ? 4494 LEU A O     1 
ATOM   20555 C CB    . LEU A 1 4494 ? 168.410 161.325 209.443 1.00 110.33 ? 4494 LEU A CB    1 
ATOM   20556 C CG    . LEU A 1 4494 ? 168.128 160.837 210.864 1.00 110.33 ? 4494 LEU A CG    1 
ATOM   20557 C CD1   . LEU A 1 4494 ? 166.842 161.442 211.402 1.00 110.33 ? 4494 LEU A CD1   1 
ATOM   20558 C CD2   . LEU A 1 4494 ? 168.060 159.322 210.892 1.00 110.33 ? 4494 LEU A CD2   1 
ATOM   20559 N N     . ALA A 1 4495 ? 170.584 163.574 209.890 1.00 110.10 ? 4495 ALA A N     1 
ATOM   20560 C CA    . ALA A 1 4495 ? 171.512 164.289 210.759 1.00 110.10 ? 4495 ALA A CA    1 
ATOM   20561 C C     . ALA A 1 4495 ? 171.248 165.787 210.729 1.00 110.10 ? 4495 ALA A C     1 
ATOM   20562 O O     . ALA A 1 4495 ? 171.347 166.464 211.759 1.00 110.10 ? 4495 ALA A O     1 
ATOM   20563 C CB    . ALA A 1 4495 ? 172.953 163.989 210.351 1.00 110.10 ? 4495 ALA A CB    1 
ATOM   20564 N N     . ALA A 1 4496 ? 170.921 166.325 209.554 1.00 110.91 ? 4496 ALA A N     1 
ATOM   20565 C CA    . ALA A 1 4496 ? 170.588 167.742 209.459 1.00 110.91 ? 4496 ALA A CA    1 
ATOM   20566 C C     . ALA A 1 4496 ? 169.321 168.061 210.239 1.00 110.91 ? 4496 ALA A C     1 
ATOM   20567 O O     . ALA A 1 4496 ? 169.222 169.115 210.876 1.00 110.91 ? 4496 ALA A O     1 
ATOM   20568 C CB    . ALA A 1 4496 ? 170.434 168.149 207.996 1.00 110.91 ? 4496 ALA A CB    1 
ATOM   20569 N N     . ALA A 1 4497 ? 168.335 167.167 210.187 1.00 116.93 ? 4497 ALA A N     1 
ATOM   20570 C CA    . ALA A 1 4497 ? 167.093 167.391 210.918 1.00 116.93 ? 4497 ALA A CA    1 
ATOM   20571 C C     . ALA A 1 4497 ? 167.313 167.340 212.424 1.00 116.93 ? 4497 ALA A C     1 
ATOM   20572 O O     . ALA A 1 4497 ? 166.760 168.162 213.164 1.00 116.93 ? 4497 ALA A O     1 
ATOM   20573 C CB    . ALA A 1 4497 ? 166.047 166.360 210.498 1.00 116.93 ? 4497 ALA A CB    1 
ATOM   20574 N N     . SER A 1 4498 ? 168.116 166.384 212.897 1.00 122.80 ? 4498 SER A N     1 
ATOM   20575 C CA    . SER A 1 4498 ? 168.229 166.158 214.335 1.00 122.80 ? 4498 SER A CA    1 
ATOM   20576 C C     . SER A 1 4498 ? 168.896 167.332 215.042 1.00 122.80 ? 4498 SER A C     1 
ATOM   20577 O O     . SER A 1 4498 ? 168.378 167.841 216.043 1.00 122.80 ? 4498 SER A O     1 
ATOM   20578 C CB    . SER A 1 4498 ? 168.998 164.865 214.604 1.00 122.80 ? 4498 SER A CB    1 
ATOM   20579 O OG    . SER A 1 4498 ? 169.209 164.682 215.993 1.00 122.80 ? 4498 SER A OG    1 
ATOM   20580 N N     . GLY A 1 4499 ? 170.044 167.778 214.542 1.00 116.22 ? 4499 GLY A N     1 
ATOM   20581 C CA    . GLY A 1 4499 ? 170.809 168.787 215.247 1.00 116.22 ? 4499 GLY A CA    1 
ATOM   20582 C C     . GLY A 1 4499 ? 170.869 170.130 214.554 1.00 116.22 ? 4499 GLY A C     1 
ATOM   20583 O O     . GLY A 1 4499 ? 170.980 171.169 215.211 1.00 116.22 ? 4499 GLY A O     1 
ATOM   20584 N N     . GLY A 1 4500 ? 170.796 170.125 213.222 1.00 115.83 ? 4500 GLY A N     1 
ATOM   20585 C CA    . GLY A 1 4500 ? 170.898 171.336 212.436 1.00 115.83 ? 4500 GLY A CA    1 
ATOM   20586 C C     . GLY A 1 4500 ? 172.156 171.340 211.585 1.00 115.83 ? 4500 GLY A C     1 
ATOM   20587 O O     . GLY A 1 4500 ? 172.697 170.282 211.242 1.00 115.83 ? 4500 GLY A O     1 
ATOM   20588 N N     . ALA A 1 4501 ? 172.620 172.546 211.258 1.00 112.36 ? 4501 ALA A N     1 
ATOM   20589 C CA    . ALA A 1 4501 ? 173.819 172.689 210.443 1.00 112.36 ? 4501 ALA A CA    1 
ATOM   20590 C C     . ALA A 1 4501 ? 175.091 172.331 211.197 1.00 112.36 ? 4501 ALA A C     1 
ATOM   20591 O O     . ALA A 1 4501 ? 176.106 172.027 210.562 1.00 112.36 ? 4501 ALA A O     1 
ATOM   20592 C CB    . ALA A 1 4501 ? 173.927 174.117 209.908 1.00 112.36 ? 4501 ALA A CB    1 
ATOM   20593 N N     . LYS A 1 4502 ? 175.062 172.364 212.530 1.00 111.23 ? 4502 LYS A N     1 
ATOM   20594 C CA    . LYS A 1 4502 ? 176.251 172.020 213.302 1.00 111.23 ? 4502 LYS A CA    1 
ATOM   20595 C C     . LYS A 1 4502 ? 176.613 170.551 213.137 1.00 111.23 ? 4502 LYS A C     1 
ATOM   20596 O O     . LYS A 1 4502 ? 177.796 170.202 213.057 1.00 111.23 ? 4502 LYS A O     1 
ATOM   20597 C CB    . LYS A 1 4502 ? 176.037 172.354 214.775 1.00 111.23 ? 4502 LYS A CB    1 
ATOM   20598 C CG    . LYS A 1 4502 ? 177.256 172.106 215.637 1.00 111.23 ? 4502 LYS A CG    1 
ATOM   20599 C CD    . LYS A 1 4502 ? 178.402 173.013 215.229 1.00 111.23 ? 4502 LYS A CD    1 
ATOM   20600 C CE    . LYS A 1 4502 ? 177.989 174.475 215.282 1.00 111.23 ? 4502 LYS A CE    1 
ATOM   20601 N NZ    . LYS A 1 4502 ? 177.557 174.877 216.649 1.00 111.23 ? 4502 LYS A NZ    1 
ATOM   20602 N N     . GLU A 1 4503 ? 175.609 169.674 213.090 1.00 109.98 ? 4503 GLU A N     1 
ATOM   20603 C CA    . GLU A 1 4503 ? 175.873 168.250 212.929 1.00 109.98 ? 4503 GLU A CA    1 
ATOM   20604 C C     . GLU A 1 4503 ? 176.454 167.920 211.561 1.00 109.98 ? 4503 GLU A C     1 
ATOM   20605 O O     . GLU A 1 4503 ? 177.051 166.851 211.397 1.00 109.98 ? 4503 GLU A O     1 
ATOM   20606 C CB    . GLU A 1 4503 ? 174.590 167.451 213.161 1.00 109.98 ? 4503 GLU A CB    1 
ATOM   20607 C CG    . GLU A 1 4503 ? 174.787 165.950 213.362 1.00 109.98 ? 4503 GLU A CG    1 
ATOM   20608 C CD    . GLU A 1 4503 ? 175.886 165.610 214.358 1.00 109.98 ? 4503 GLU A CD    1 
ATOM   20609 O OE1   . GLU A 1 4503 ? 177.076 165.621 213.977 1.00 109.98 ? 4503 GLU A OE1   1 
ATOM   20610 O OE2   . GLU A 1 4503 ? 175.555 165.327 215.529 1.00 109.98 ? 4503 GLU A OE2   1 
ATOM   20611 N N     . LEU A 1 4504 ? 176.305 168.815 210.582 1.00 101.24 ? 4504 LEU A N     1 
ATOM   20612 C CA    . LEU A 1 4504 ? 176.826 168.548 209.246 1.00 101.24 ? 4504 LEU A CA    1 
ATOM   20613 C C     . LEU A 1 4504 ? 178.336 168.369 209.268 1.00 101.24 ? 4504 LEU A C     1 
ATOM   20614 O O     . LEU A 1 4504 ? 178.874 167.493 208.583 1.00 101.24 ? 4504 LEU A O     1 
ATOM   20615 C CB    . LEU A 1 4504 ? 176.439 169.682 208.301 1.00 101.24 ? 4504 LEU A CB    1 
ATOM   20616 C CG    . LEU A 1 4504 ? 174.954 169.777 207.964 1.00 101.24 ? 4504 LEU A CG    1 
ATOM   20617 C CD1   . LEU A 1 4504 ? 174.732 170.756 206.828 1.00 101.24 ? 4504 LEU A CD1   1 
ATOM   20618 C CD2   . LEU A 1 4504 ? 174.408 168.408 207.606 1.00 101.24 ? 4504 LEU A CD2   1 
ATOM   20619 N N     . LYS A 1 4505 ? 179.036 169.193 210.047 1.00 99.29  ? 4505 LYS A N     1 
ATOM   20620 C CA    . LYS A 1 4505 ? 180.490 169.103 210.098 1.00 99.29  ? 4505 LYS A CA    1 
ATOM   20621 C C     . LYS A 1 4505 ? 180.943 167.765 210.665 1.00 99.29  ? 4505 LYS A C     1 
ATOM   20622 O O     . LYS A 1 4505 ? 181.899 167.162 210.164 1.00 99.29  ? 4505 LYS A O     1 
ATOM   20623 C CB    . LYS A 1 4505 ? 181.055 170.259 210.924 1.00 99.29  ? 4505 LYS A CB    1 
ATOM   20624 C CG    . LYS A 1 4505 ? 182.571 170.283 211.013 1.00 99.29  ? 4505 LYS A CG    1 
ATOM   20625 C CD    . LYS A 1 4505 ? 183.066 169.812 212.368 1.00 99.29  ? 4505 LYS A CD    1 
ATOM   20626 C CE    . LYS A 1 4505 ? 184.571 169.619 212.358 1.00 99.29  ? 4505 LYS A CE    1 
ATOM   20627 N NZ    . LYS A 1 4505 ? 185.130 169.417 213.722 1.00 99.29  ? 4505 LYS A NZ    1 
ATOM   20628 N N     . ASN A 1 4506 ? 180.270 167.281 211.705 1.00 100.49 ? 4506 ASN A N     1 
ATOM   20629 C CA    . ASN A 1 4506 ? 180.667 166.040 212.370 1.00 100.49 ? 4506 ASN A CA    1 
ATOM   20630 C C     . ASN A 1 4506 ? 180.021 164.831 211.691 1.00 100.49 ? 4506 ASN A C     1 
ATOM   20631 O O     . ASN A 1 4506 ? 179.329 164.025 212.311 1.00 100.49 ? 4506 ASN A O     1 
ATOM   20632 C CB    . ASN A 1 4506 ? 180.307 166.100 213.849 1.00 100.49 ? 4506 ASN A CB    1 
ATOM   20633 C CG    . ASN A 1 4506 ? 180.878 167.322 214.539 1.00 100.49 ? 4506 ASN A CG    1 
ATOM   20634 O OD1   . ASN A 1 4506 ? 180.140 168.187 215.007 1.00 100.49 ? 4506 ASN A OD1   1 
ATOM   20635 N ND2   . ASN A 1 4506 ? 182.200 167.396 214.609 1.00 100.49 ? 4506 ASN A ND2   1 
ATOM   20636 N N     . ILE A 1 4507 ? 180.262 164.713 210.388 1.00 94.67  ? 4507 ILE A N     1 
ATOM   20637 C CA    . ILE A 1 4507 ? 179.723 163.622 209.586 1.00 94.67  ? 4507 ILE A CA    1 
ATOM   20638 C C     . ILE A 1 4507 ? 180.846 163.020 208.759 1.00 94.67  ? 4507 ILE A C     1 
ATOM   20639 O O     . ILE A 1 4507 ? 181.597 163.747 208.101 1.00 94.67  ? 4507 ILE A O     1 
ATOM   20640 C CB    . ILE A 1 4507 ? 178.576 164.093 208.673 1.00 94.67  ? 4507 ILE A CB    1 
ATOM   20641 C CG1   . ILE A 1 4507 ? 177.307 164.311 209.492 1.00 94.67  ? 4507 ILE A CG1   1 
ATOM   20642 C CG2   . ILE A 1 4507 ? 178.325 163.080 207.576 1.00 94.67  ? 4507 ILE A CG2   1 
ATOM   20643 C CD1   . ILE A 1 4507 ? 176.173 164.907 208.703 1.00 94.67  ? 4507 ILE A CD1   1 
ATOM   20644 N N     . HIS A 1 4508 ? 180.957 161.692 208.789 1.00 95.19  ? 4508 HIS A N     1 
ATOM   20645 C CA    . HIS A 1 4508 ? 181.951 160.977 207.993 1.00 95.19  ? 4508 HIS A CA    1 
ATOM   20646 C C     . HIS A 1 4508 ? 181.302 160.565 206.676 1.00 95.19  ? 4508 HIS A C     1 
ATOM   20647 O O     . HIS A 1 4508 ? 180.664 159.519 206.553 1.00 95.19  ? 4508 HIS A O     1 
ATOM   20648 C CB    . HIS A 1 4508 ? 182.494 159.782 208.764 1.00 95.19  ? 4508 HIS A CB    1 
ATOM   20649 C CG    . HIS A 1 4508 ? 183.185 160.154 210.037 1.00 95.19  ? 4508 HIS A CG    1 
ATOM   20650 N ND1   . HIS A 1 4508 ? 183.301 161.457 210.467 1.00 95.19  ? 4508 HIS A ND1   1 
ATOM   20651 C CD2   . HIS A 1 4508 ? 183.801 159.393 210.972 1.00 95.19  ? 4508 HIS A CD2   1 
ATOM   20652 C CE1   . HIS A 1 4508 ? 183.955 161.484 211.614 1.00 95.19  ? 4508 HIS A CE1   1 
ATOM   20653 N NE2   . HIS A 1 4508 ? 184.271 160.245 211.942 1.00 95.19  ? 4508 HIS A NE2   1 
ATOM   20654 N N     . VAL A 1 4509 ? 181.469 161.417 205.679 1.00 87.36  ? 4509 VAL A N     1 
ATOM   20655 C CA    . VAL A 1 4509 ? 180.877 161.220 204.363 1.00 87.36  ? 4509 VAL A CA    1 
ATOM   20656 C C     . VAL A 1 4509 ? 181.922 160.639 203.423 1.00 87.36  ? 4509 VAL A C     1 
ATOM   20657 O O     . VAL A 1 4509 ? 183.097 161.019 203.468 1.00 87.36  ? 4509 VAL A O     1 
ATOM   20658 C CB    . VAL A 1 4509 ? 180.315 162.548 203.824 1.00 87.36  ? 4509 VAL A CB    1 
ATOM   20659 C CG1   . VAL A 1 4509 ? 181.364 163.631 203.910 1.00 87.36  ? 4509 VAL A CG1   1 
ATOM   20660 C CG2   . VAL A 1 4509 ? 179.839 162.388 202.397 1.00 87.36  ? 4509 VAL A CG2   1 
ATOM   20661 N N     . CYS A 1 4510 ? 181.500 159.707 202.574 1.00 88.12  ? 4510 CYS A N     1 
ATOM   20662 C CA    . CYS A 1 4510 ? 182.370 159.118 201.566 1.00 88.12  ? 4510 CYS A CA    1 
ATOM   20663 C C     . CYS A 1 4510 ? 182.222 159.889 200.263 1.00 88.12  ? 4510 CYS A C     1 
ATOM   20664 O O     . CYS A 1 4510 ? 181.104 160.220 199.856 1.00 88.12  ? 4510 CYS A O     1 
ATOM   20665 C CB    . CYS A 1 4510 ? 182.049 157.638 201.348 1.00 88.12  ? 4510 CYS A CB    1 
ATOM   20666 S SG    . CYS A 1 4510 ? 180.461 157.295 200.559 1.00 88.12  ? 4510 CYS A SG    1 
ATOM   20667 N N     . LEU A 1 4511 ? 183.351 160.188 199.619 1.00 83.78  ? 4511 LEU A N     1 
ATOM   20668 C CA    . LEU A 1 4511 ? 183.298 160.932 198.368 1.00 83.78  ? 4511 LEU A CA    1 
ATOM   20669 C C     . LEU A 1 4511 ? 182.686 160.110 197.245 1.00 83.78  ? 4511 LEU A C     1 
ATOM   20670 O O     . LEU A 1 4511 ? 182.003 160.666 196.379 1.00 83.78  ? 4511 LEU A O     1 
ATOM   20671 C CB    . LEU A 1 4511 ? 184.692 161.404 197.961 1.00 83.78  ? 4511 LEU A CB    1 
ATOM   20672 C CG    . LEU A 1 4511 ? 185.291 162.592 198.711 1.00 83.78  ? 4511 LEU A CG    1 
ATOM   20673 C CD1   . LEU A 1 4511 ? 184.264 163.697 198.852 1.00 83.78  ? 4511 LEU A CD1   1 
ATOM   20674 C CD2   . LEU A 1 4511 ? 185.833 162.184 200.054 1.00 83.78  ? 4511 LEU A CD2   1 
ATOM   20675 N N     . GLY A 1 4512 ? 182.917 158.797 197.238 1.00 83.56  ? 4512 GLY A N     1 
ATOM   20676 C CA    . GLY A 1 4512 ? 182.417 157.979 196.146 1.00 83.56  ? 4512 GLY A CA    1 
ATOM   20677 C C     . GLY A 1 4512 ? 180.911 158.063 195.997 1.00 83.56  ? 4512 GLY A C     1 
ATOM   20678 O O     . GLY A 1 4512 ? 180.392 158.176 194.884 1.00 83.56  ? 4512 GLY A O     1 
ATOM   20679 N N     . GLY A 1 4513 ? 180.189 158.017 197.116 1.00 92.38  ? 4513 GLY A N     1 
ATOM   20680 C CA    . GLY A 1 4513 ? 178.745 158.159 197.053 1.00 92.38  ? 4513 GLY A CA    1 
ATOM   20681 C C     . GLY A 1 4513 ? 178.315 159.542 196.603 1.00 92.38  ? 4513 GLY A C     1 
ATOM   20682 O O     . GLY A 1 4513 ? 177.328 159.688 195.879 1.00 92.38  ? 4513 GLY A O     1 
ATOM   20683 N N     . LEU A 1 4514 ? 179.049 160.570 197.018 1.00 90.92  ? 4514 LEU A N     1 
ATOM   20684 C CA    . LEU A 1 4514 ? 178.701 161.930 196.639 1.00 90.92  ? 4514 LEU A CA    1 
ATOM   20685 C C     . LEU A 1 4514 ? 178.784 162.093 195.129 1.00 90.92  ? 4514 LEU A C     1 
ATOM   20686 O O     . LEU A 1 4514 ? 179.636 161.495 194.469 1.00 90.92  ? 4514 LEU A O     1 
ATOM   20687 C CB    . LEU A 1 4514 ? 179.629 162.926 197.327 1.00 90.92  ? 4514 LEU A CB    1 
ATOM   20688 C CG    . LEU A 1 4514 ? 179.403 163.146 198.819 1.00 90.92  ? 4514 LEU A CG    1 
ATOM   20689 C CD1   . LEU A 1 4514 ? 179.833 164.542 199.209 1.00 90.92  ? 4514 LEU A CD1   1 
ATOM   20690 C CD2   . LEU A 1 4514 ? 177.952 162.916 199.180 1.00 90.92  ? 4514 LEU A CD2   1 
ATOM   20691 N N     . PHE A 1 4515 ? 177.875 162.897 194.582 1.00 94.49  ? 4515 PHE A N     1 
ATOM   20692 C CA    . PHE A 1 4515 ? 177.823 163.071 193.135 1.00 94.49  ? 4515 PHE A CA    1 
ATOM   20693 C C     . PHE A 1 4515 ? 178.926 164.001 192.646 1.00 94.49  ? 4515 PHE A C     1 
ATOM   20694 O O     . PHE A 1 4515 ? 179.468 163.808 191.552 1.00 94.49  ? 4515 PHE A O     1 
ATOM   20695 C CB    . PHE A 1 4515 ? 176.448 163.594 192.727 1.00 94.49  ? 4515 PHE A CB    1 
ATOM   20696 C CG    . PHE A 1 4515 ? 175.307 162.780 193.269 1.00 94.49  ? 4515 PHE A CG    1 
ATOM   20697 C CD1   . PHE A 1 4515 ? 174.820 163.003 194.545 1.00 94.49  ? 4515 PHE A CD1   1 
ATOM   20698 C CD2   . PHE A 1 4515 ? 174.717 161.795 192.499 1.00 94.49  ? 4515 PHE A CD2   1 
ATOM   20699 C CE1   . PHE A 1 4515 ? 173.771 162.258 195.040 1.00 94.49  ? 4515 PHE A CE1   1 
ATOM   20700 C CE2   . PHE A 1 4515 ? 173.667 161.048 192.991 1.00 94.49  ? 4515 PHE A CE2   1 
ATOM   20701 C CZ    . PHE A 1 4515 ? 173.195 161.281 194.263 1.00 94.49  ? 4515 PHE A CZ    1 
ATOM   20702 N N     . VAL A 1 4516 ? 179.270 165.015 193.434 1.00 90.58  ? 4516 VAL A N     1 
ATOM   20703 C CA    . VAL A 1 4516 ? 180.303 165.976 193.057 1.00 90.58  ? 4516 VAL A CA    1 
ATOM   20704 C C     . VAL A 1 4516 ? 181.304 166.127 194.197 1.00 90.58  ? 4516 VAL A C     1 
ATOM   20705 O O     . VAL A 1 4516 ? 181.226 167.088 194.975 1.00 90.58  ? 4516 VAL A O     1 
ATOM   20706 C CB    . VAL A 1 4516 ? 179.681 167.324 192.661 1.00 90.58  ? 4516 VAL A CB    1 
ATOM   20707 C CG1   . VAL A 1 4516 ? 179.140 167.245 191.250 1.00 90.58  ? 4516 VAL A CG1   1 
ATOM   20708 C CG2   . VAL A 1 4516 ? 178.553 167.680 193.609 1.00 90.58  ? 4516 VAL A CG2   1 
ATOM   20709 N N     . PRO A 1 4517 ? 182.259 165.205 194.330 1.00 82.96  ? 4517 PRO A N     1 
ATOM   20710 C CA    . PRO A 1 4517 ? 183.204 165.287 195.456 1.00 82.96  ? 4517 PRO A CA    1 
ATOM   20711 C C     . PRO A 1 4517 ? 184.002 166.578 195.501 1.00 82.96  ? 4517 PRO A C     1 
ATOM   20712 O O     . PRO A 1 4517 ? 184.251 167.106 196.593 1.00 82.96  ? 4517 PRO A O     1 
ATOM   20713 C CB    . PRO A 1 4517 ? 184.113 164.072 195.228 1.00 82.96  ? 4517 PRO A CB    1 
ATOM   20714 C CG    . PRO A 1 4517 ? 183.320 163.153 194.370 1.00 82.96  ? 4517 PRO A CG    1 
ATOM   20715 C CD    . PRO A 1 4517 ? 182.490 164.020 193.492 1.00 82.96  ? 4517 PRO A CD    1 
ATOM   20716 N N     . GLU A 1 4518 ? 184.416 167.104 194.347 1.00 87.69  ? 4518 GLU A N     1 
ATOM   20717 C CA    . GLU A 1 4518 ? 185.179 168.346 194.352 1.00 87.69  ? 4518 GLU A CA    1 
ATOM   20718 C C     . GLU A 1 4518 ? 184.358 169.488 194.922 1.00 87.69  ? 4518 GLU A C     1 
ATOM   20719 O O     . GLU A 1 4518 ? 184.904 170.379 195.582 1.00 87.69  ? 4518 GLU A O     1 
ATOM   20720 C CB    . GLU A 1 4518 ? 185.661 168.686 192.942 1.00 87.69  ? 4518 GLU A CB    1 
ATOM   20721 C CG    . GLU A 1 4518 ? 184.589 168.619 191.876 1.00 87.69  ? 4518 GLU A CG    1 
ATOM   20722 C CD    . GLU A 1 4518 ? 184.523 167.262 191.207 1.00 87.69  ? 4518 GLU A CD    1 
ATOM   20723 O OE1   . GLU A 1 4518 ? 184.316 166.258 191.918 1.00 87.69  ? 4518 GLU A OE1   1 
ATOM   20724 O OE2   . GLU A 1 4518 ? 184.678 167.198 189.970 1.00 87.69  ? 4518 GLU A OE2   1 
ATOM   20725 N N     . ALA A 1 4519 ? 183.046 169.471 194.692 1.00 89.48  ? 4519 ALA A N     1 
ATOM   20726 C CA    . ALA A 1 4519 ? 182.184 170.458 195.325 1.00 89.48  ? 4519 ALA A CA    1 
ATOM   20727 C C     . ALA A 1 4519 ? 182.219 170.315 196.839 1.00 89.48  ? 4519 ALA A C     1 
ATOM   20728 O O     . ALA A 1 4519 ? 182.223 171.316 197.562 1.00 89.48  ? 4519 ALA A O     1 
ATOM   20729 C CB    . ALA A 1 4519 ? 180.757 170.325 194.800 1.00 89.48  ? 4519 ALA A CB    1 
ATOM   20730 N N     . TYR A 1 4520 ? 182.254 169.078 197.338 1.00 84.80  ? 4520 TYR A N     1 
ATOM   20731 C CA    . TYR A 1 4520 ? 182.358 168.879 198.779 1.00 84.80  ? 4520 TYR A CA    1 
ATOM   20732 C C     . TYR A 1 4520 ? 183.680 169.412 199.312 1.00 84.80  ? 4520 TYR A C     1 
ATOM   20733 O O     . TYR A 1 4520 ? 183.725 170.011 200.392 1.00 84.80  ? 4520 TYR A O     1 
ATOM   20734 C CB    . TYR A 1 4520 ? 182.211 167.401 199.129 1.00 84.80  ? 4520 TYR A CB    1 
ATOM   20735 C CG    . TYR A 1 4520 ? 182.391 167.130 200.602 1.00 84.80  ? 4520 TYR A CG    1 
ATOM   20736 C CD1   . TYR A 1 4520 ? 181.381 167.415 201.504 1.00 84.80  ? 4520 TYR A CD1   1 
ATOM   20737 C CD2   . TYR A 1 4520 ? 183.578 166.614 201.092 1.00 84.80  ? 4520 TYR A CD2   1 
ATOM   20738 C CE1   . TYR A 1 4520 ? 181.540 167.178 202.849 1.00 84.80  ? 4520 TYR A CE1   1 
ATOM   20739 C CE2   . TYR A 1 4520 ? 183.747 166.376 202.436 1.00 84.80  ? 4520 TYR A CE2   1 
ATOM   20740 C CZ    . TYR A 1 4520 ? 182.725 166.662 203.309 1.00 84.80  ? 4520 TYR A CZ    1 
ATOM   20741 O OH    . TYR A 1 4520 ? 182.888 166.425 204.651 1.00 84.80  ? 4520 TYR A OH    1 
ATOM   20742 N N     . ILE A 1 4521 ? 184.771 169.188 198.578 1.00 82.37  ? 4521 ILE A N     1 
ATOM   20743 C CA    . ILE A 1 4521 ? 186.068 169.697 199.017 1.00 82.37  ? 4521 ILE A CA    1 
ATOM   20744 C C     . ILE A 1 4521 ? 186.055 171.216 199.065 1.00 82.37  ? 4521 ILE A C     1 
ATOM   20745 O O     . ILE A 1 4521 ? 186.547 171.831 200.020 1.00 82.37  ? 4521 ILE A O     1 
ATOM   20746 C CB    . ILE A 1 4521 ? 187.186 169.176 198.100 1.00 82.37  ? 4521 ILE A CB    1 
ATOM   20747 C CG1   . ILE A 1 4521 ? 187.131 167.655 198.016 1.00 82.37  ? 4521 ILE A CG1   1 
ATOM   20748 C CG2   . ILE A 1 4521 ? 188.531 169.630 198.615 1.00 82.37  ? 4521 ILE A CG2   1 
ATOM   20749 C CD1   . ILE A 1 4521 ? 187.414 166.976 199.326 1.00 82.37  ? 4521 ILE A CD1   1 
ATOM   20750 N N     . THR A 1 4522 ? 185.493 171.846 198.034 1.00 85.06  ? 4522 THR A N     1 
ATOM   20751 C CA    . THR A 1 4522 ? 185.398 173.300 198.023 1.00 85.06  ? 4522 THR A CA    1 
ATOM   20752 C C     . THR A 1 4522 ? 184.535 173.802 199.173 1.00 85.06  ? 4522 THR A C     1 
ATOM   20753 O O     . THR A 1 4522 ? 184.861 174.812 199.807 1.00 85.06  ? 4522 THR A O     1 
ATOM   20754 C CB    . THR A 1 4522 ? 184.847 173.772 196.679 1.00 85.06  ? 4522 THR A CB    1 
ATOM   20755 O OG1   . THR A 1 4522 ? 185.906 173.796 195.715 1.00 85.06  ? 4522 THR A OG1   1 
ATOM   20756 C CG2   . THR A 1 4522 ? 184.245 175.158 196.797 1.00 85.06  ? 4522 THR A CG2   1 
ATOM   20757 N N     . ALA A 1 4523 ? 183.433 173.108 199.462 1.00 85.54  ? 4523 ALA A N     1 
ATOM   20758 C CA    . ALA A 1 4523 ? 182.585 173.503 200.581 1.00 85.54  ? 4523 ALA A CA    1 
ATOM   20759 C C     . ALA A 1 4523 ? 183.331 173.388 201.901 1.00 85.54  ? 4523 ALA A C     1 
ATOM   20760 O O     . ALA A 1 4523 ? 183.203 174.252 202.775 1.00 85.54  ? 4523 ALA A O     1 
ATOM   20761 C CB    . ALA A 1 4523 ? 181.317 172.652 200.606 1.00 85.54  ? 4523 ALA A CB    1 
ATOM   20762 N N     . THR A 1 4524 ? 184.111 172.321 202.067 1.00 82.13  ? 4524 THR A N     1 
ATOM   20763 C CA    . THR A 1 4524 ? 184.917 172.175 203.272 1.00 82.13  ? 4524 THR A CA    1 
ATOM   20764 C C     . THR A 1 4524 ? 185.908 173.320 203.404 1.00 82.13  ? 4524 THR A C     1 
ATOM   20765 O O     . THR A 1 4524 ? 186.082 173.886 204.491 1.00 82.13  ? 4524 THR A O     1 
ATOM   20766 C CB    . THR A 1 4524 ? 185.652 170.839 203.242 1.00 82.13  ? 4524 THR A CB    1 
ATOM   20767 O OG1   . THR A 1 4524 ? 184.707 169.780 203.054 1.00 82.13  ? 4524 THR A OG1   1 
ATOM   20768 C CG2   . THR A 1 4524 ? 186.401 170.619 204.532 1.00 82.13  ? 4524 THR A CG2   1 
ATOM   20769 N N     . ARG A 1 4525 ? 186.563 173.675 202.300 1.00 83.84  ? 4525 ARG A N     1 
ATOM   20770 C CA    . ARG A 1 4525 ? 187.508 174.784 202.319 1.00 83.84  ? 4525 ARG A CA    1 
ATOM   20771 C C     . ARG A 1 4525 ? 186.814 176.082 202.706 1.00 83.84  ? 4525 ARG A C     1 
ATOM   20772 O O     . ARG A 1 4525 ? 187.329 176.857 203.522 1.00 83.84  ? 4525 ARG A O     1 
ATOM   20773 C CB    . ARG A 1 4525 ? 188.167 174.910 200.949 1.00 83.84  ? 4525 ARG A CB    1 
ATOM   20774 C CG    . ARG A 1 4525 ? 189.519 175.578 200.938 1.00 83.84  ? 4525 ARG A CG    1 
ATOM   20775 C CD    . ARG A 1 4525 ? 190.067 175.588 199.523 1.00 83.84  ? 4525 ARG A CD    1 
ATOM   20776 N NE    . ARG A 1 4525 ? 191.466 175.987 199.467 1.00 83.84  ? 4525 ARG A NE    1 
ATOM   20777 C CZ    . ARG A 1 4525 ? 192.145 176.162 198.342 1.00 83.84  ? 4525 ARG A CZ    1 
ATOM   20778 N NH1   . ARG A 1 4525 ? 191.582 175.976 197.160 1.00 83.84  ? 4525 ARG A NH1   1 
ATOM   20779 N NH2   . ARG A 1 4525 ? 193.420 176.530 198.405 1.00 83.84  ? 4525 ARG A NH2   1 
ATOM   20780 N N     . GLN A 1 4526 ? 185.631 176.326 202.141 1.00 86.18  ? 4526 GLN A N     1 
ATOM   20781 C CA    . GLN A 1 4526 ? 184.889 177.538 202.465 1.00 86.18  ? 4526 GLN A CA    1 
ATOM   20782 C C     . GLN A 1 4526 ? 184.496 177.566 203.934 1.00 86.18  ? 4526 GLN A C     1 
ATOM   20783 O O     . GLN A 1 4526 ? 184.552 178.618 204.579 1.00 86.18  ? 4526 GLN A O     1 
ATOM   20784 C CB    . GLN A 1 4526 ? 183.650 177.654 201.580 1.00 86.18  ? 4526 GLN A CB    1 
ATOM   20785 C CG    . GLN A 1 4526 ? 183.944 177.901 200.114 1.00 86.18  ? 4526 GLN A CG    1 
ATOM   20786 C CD    . GLN A 1 4526 ? 182.690 177.893 199.268 1.00 86.18  ? 4526 GLN A CD    1 
ATOM   20787 O OE1   . GLN A 1 4526 ? 182.753 177.810 198.043 1.00 86.18  ? 4526 GLN A OE1   1 
ATOM   20788 N NE2   . GLN A 1 4526 ? 181.539 177.981 199.919 1.00 86.18  ? 4526 GLN A NE2   1 
ATOM   20789 N N     . TYR A 1 4527 ? 184.077 176.423 204.477 1.00 86.67  ? 4527 TYR A N     1 
ATOM   20790 C CA    . TYR A 1 4527 ? 183.704 176.376 205.886 1.00 86.67  ? 4527 TYR A CA    1 
ATOM   20791 C C     . TYR A 1 4527 ? 184.899 176.658 206.784 1.00 86.67  ? 4527 TYR A C     1 
ATOM   20792 O O     . TYR A 1 4527 ? 184.786 177.405 207.765 1.00 86.67  ? 4527 TYR A O     1 
ATOM   20793 C CB    . TYR A 1 4527 ? 183.099 175.018 206.222 1.00 86.67  ? 4527 TYR A CB    1 
ATOM   20794 C CG    . TYR A 1 4527 ? 182.769 174.845 207.685 1.00 86.67  ? 4527 TYR A CG    1 
ATOM   20795 C CD1   . TYR A 1 4527 ? 181.594 175.353 208.215 1.00 86.67  ? 4527 TYR A CD1   1 
ATOM   20796 C CD2   . TYR A 1 4527 ? 183.630 174.169 208.534 1.00 86.67  ? 4527 TYR A CD2   1 
ATOM   20797 C CE1   . TYR A 1 4527 ? 181.287 175.196 209.548 1.00 86.67  ? 4527 TYR A CE1   1 
ATOM   20798 C CE2   . TYR A 1 4527 ? 183.332 174.008 209.869 1.00 86.67  ? 4527 TYR A CE2   1 
ATOM   20799 C CZ    . TYR A 1 4527 ? 182.160 174.523 210.371 1.00 86.67  ? 4527 TYR A CZ    1 
ATOM   20800 O OH    . TYR A 1 4527 ? 181.859 174.364 211.702 1.00 86.67  ? 4527 TYR A OH    1 
ATOM   20801 N N     . VAL A 1 4528 ? 186.049 176.059 206.472 1.00 82.50  ? 4528 VAL A N     1 
ATOM   20802 C CA    . VAL A 1 4528 ? 187.228 176.293 207.295 1.00 82.50  ? 4528 VAL A CA    1 
ATOM   20803 C C     . VAL A 1 4528 ? 187.685 177.738 207.173 1.00 82.50  ? 4528 VAL A C     1 
ATOM   20804 O O     . VAL A 1 4528 ? 188.268 178.290 208.110 1.00 82.50  ? 4528 VAL A O     1 
ATOM   20805 C CB    . VAL A 1 4528 ? 188.349 175.306 206.927 1.00 82.50  ? 4528 VAL A CB    1 
ATOM   20806 C CG1   . VAL A 1 4528 ? 189.580 175.562 207.774 1.00 82.50  ? 4528 VAL A CG1   1 
ATOM   20807 C CG2   . VAL A 1 4528 ? 187.872 173.883 207.122 1.00 82.50  ? 4528 VAL A CG2   1 
ATOM   20808 N N     . ALA A 1 4529 ? 187.437 178.376 206.030 1.00 84.19  ? 4529 ALA A N     1 
ATOM   20809 C CA    . ALA A 1 4529 ? 187.745 179.798 205.912 1.00 84.19  ? 4529 ALA A CA    1 
ATOM   20810 C C     . ALA A 1 4529 ? 186.799 180.634 206.762 1.00 84.19  ? 4529 ALA A C     1 
ATOM   20811 O O     . ALA A 1 4529 ? 187.233 181.531 207.498 1.00 84.19  ? 4529 ALA A O     1 
ATOM   20812 C CB    . ALA A 1 4529 ? 187.676 180.230 204.449 1.00 84.19  ? 4529 ALA A CB    1 
ATOM   20813 N N     . GLN A 1 4530 ? 185.498 180.346 206.676 1.00 88.39  ? 4530 GLN A N     1 
ATOM   20814 C CA    . GLN A 1 4530 ? 184.508 181.125 207.412 1.00 88.39  ? 4530 GLN A CA    1 
ATOM   20815 C C     . GLN A 1 4530 ? 184.749 181.037 208.909 1.00 88.39  ? 4530 GLN A C     1 
ATOM   20816 O O     . GLN A 1 4530 ? 184.679 182.047 209.618 1.00 88.39  ? 4530 GLN A O     1 
ATOM   20817 C CB    . GLN A 1 4530 ? 183.101 180.650 207.062 1.00 88.39  ? 4530 GLN A CB    1 
ATOM   20818 C CG    . GLN A 1 4530 ? 182.377 181.563 206.094 1.00 88.39  ? 4530 GLN A CG    1 
ATOM   20819 C CD    . GLN A 1 4530 ? 180.874 181.427 206.179 1.00 88.39  ? 4530 GLN A CD    1 
ATOM   20820 O OE1   . GLN A 1 4530 ? 180.198 182.254 206.789 1.00 88.39  ? 4530 GLN A OE1   1 
ATOM   20821 N NE2   . GLN A 1 4530 ? 180.340 180.379 205.566 1.00 88.39  ? 4530 GLN A NE2   1 
ATOM   20822 N N     . ALA A 1 4531 ? 185.034 179.841 209.411 1.00 89.63  ? 4531 ALA A N     1 
ATOM   20823 C CA    . ALA A 1 4531 ? 185.594 179.740 210.748 1.00 89.63  ? 4531 ALA A CA    1 
ATOM   20824 C C     . ALA A 1 4531 ? 186.976 180.378 210.751 1.00 89.63  ? 4531 ALA A C     1 
ATOM   20825 O O     . ALA A 1 4531 ? 187.768 180.178 209.830 1.00 89.63  ? 4531 ALA A O     1 
ATOM   20826 C CB    . ALA A 1 4531 ? 185.676 178.283 211.193 1.00 89.63  ? 4531 ALA A CB    1 
ATOM   20827 N N     . ASN A 1 4532 ? 187.253 181.180 211.774 1.00 94.17  ? 4532 ASN A N     1 
ATOM   20828 C CA    . ASN A 1 4532 ? 188.492 181.936 211.936 1.00 94.17  ? 4532 ASN A CA    1 
ATOM   20829 C C     . ASN A 1 4532 ? 188.674 183.023 210.883 1.00 94.17  ? 4532 ASN A C     1 
ATOM   20830 O O     . ASN A 1 4532 ? 189.662 183.761 210.957 1.00 94.17  ? 4532 ASN A O     1 
ATOM   20831 C CB    . ASN A 1 4532 ? 189.743 181.043 211.931 1.00 94.17  ? 4532 ASN A CB    1 
ATOM   20832 C CG    . ASN A 1 4532 ? 189.503 179.697 212.579 1.00 94.17  ? 4532 ASN A CG    1 
ATOM   20833 O OD1   . ASN A 1 4532 ? 189.425 179.591 213.801 1.00 94.17  ? 4532 ASN A OD1   1 
ATOM   20834 N ND2   . ASN A 1 4532 ? 189.387 178.659 211.762 1.00 94.17  ? 4532 ASN A ND2   1 
ATOM   20835 N N     . SER A 1 4533 ? 187.766 183.152 209.912 1.00 92.18  ? 4533 SER A N     1 
ATOM   20836 C CA    . SER A 1 4533 ? 187.741 184.296 209.002 1.00 92.18  ? 4533 SER A CA    1 
ATOM   20837 C C     . SER A 1 4533 ? 189.073 184.456 208.265 1.00 92.18  ? 4533 SER A C     1 
ATOM   20838 O O     . SER A 1 4533 ? 189.780 185.456 208.403 1.00 92.18  ? 4533 SER A O     1 
ATOM   20839 C CB    . SER A 1 4533 ? 187.370 185.578 209.753 1.00 92.18  ? 4533 SER A CB    1 
ATOM   20840 O OG    . SER A 1 4533 ? 186.139 185.427 210.435 1.00 92.18  ? 4533 SER A OG    1 
ATOM   20841 N N     . TRP A 1 4534 ? 189.407 183.441 207.479 1.00 92.80  ? 4534 TRP A N     1 
ATOM   20842 C CA    . TRP A 1 4534 ? 190.582 183.458 206.621 1.00 92.80  ? 4534 TRP A CA    1 
ATOM   20843 C C     . TRP A 1 4534 ? 190.154 183.636 205.171 1.00 92.80  ? 4534 TRP A C     1 
ATOM   20844 O O     . TRP A 1 4534 ? 188.973 183.799 204.860 1.00 92.80  ? 4534 TRP A O     1 
ATOM   20845 C CB    . TRP A 1 4534 ? 191.393 182.168 206.781 1.00 92.80  ? 4534 TRP A CB    1 
ATOM   20846 C CG    . TRP A 1 4534 ? 192.156 182.097 208.056 1.00 92.80  ? 4534 TRP A CG    1 
ATOM   20847 C CD1   . TRP A 1 4534 ? 192.820 183.114 208.668 1.00 92.80  ? 4534 TRP A CD1   1 
ATOM   20848 C CD2   . TRP A 1 4534 ? 192.334 180.944 208.884 1.00 92.80  ? 4534 TRP A CD2   1 
ATOM   20849 N NE1   . TRP A 1 4534 ? 193.405 182.667 209.827 1.00 92.80  ? 4534 TRP A NE1   1 
ATOM   20850 C CE2   . TRP A 1 4534 ? 193.120 181.337 209.982 1.00 92.80  ? 4534 TRP A CE2   1 
ATOM   20851 C CE3   . TRP A 1 4534 ? 191.904 179.618 208.804 1.00 92.80  ? 4534 TRP A CE3   1 
ATOM   20852 C CZ2   . TRP A 1 4534 ? 193.486 180.453 210.991 1.00 92.80  ? 4534 TRP A CZ2   1 
ATOM   20853 C CZ3   . TRP A 1 4534 ? 192.269 178.742 209.806 1.00 92.80  ? 4534 TRP A CZ3   1 
ATOM   20854 C CH2   . TRP A 1 4534 ? 193.051 179.162 210.885 1.00 92.80  ? 4534 TRP A CH2   1 
ATOM   20855 N N     . SER A 1 4535 ? 191.134 183.612 204.279 1.00 83.79  ? 4535 SER A N     1 
ATOM   20856 C CA    . SER A 1 4535 ? 190.866 183.613 202.851 1.00 83.79  ? 4535 SER A CA    1 
ATOM   20857 C C     . SER A 1 4535 ? 191.214 182.253 202.265 1.00 83.79  ? 4535 SER A C     1 
ATOM   20858 O O     . SER A 1 4535 ? 192.102 181.555 202.759 1.00 83.79  ? 4535 SER A O     1 
ATOM   20859 C CB    . SER A 1 4535 ? 191.657 184.709 202.141 1.00 83.79  ? 4535 SER A CB    1 
ATOM   20860 O OG    . SER A 1 4535 ? 191.433 184.665 200.744 1.00 83.79  ? 4535 SER A OG    1 
ATOM   20861 N N     . LEU A 1 4536 ? 190.507 181.884 201.195 1.00 81.00  ? 4536 LEU A N     1 
ATOM   20862 C CA    . LEU A 1 4536 ? 190.657 180.545 200.635 1.00 81.00  ? 4536 LEU A CA    1 
ATOM   20863 C C     . LEU A 1 4536 ? 192.072 180.288 200.140 1.00 81.00  ? 4536 LEU A C     1 
ATOM   20864 O O     . LEU A 1 4536 ? 192.502 179.132 200.067 1.00 81.00  ? 4536 LEU A O     1 
ATOM   20865 C CB    . LEU A 1 4536 ? 189.661 180.338 199.500 1.00 81.00  ? 4536 LEU A CB    1 
ATOM   20866 C CG    . LEU A 1 4536 ? 188.412 179.549 199.876 1.00 81.00  ? 4536 LEU A CG    1 
ATOM   20867 C CD1   . LEU A 1 4536 ? 187.481 180.412 200.702 1.00 81.00  ? 4536 LEU A CD1   1 
ATOM   20868 C CD2   . LEU A 1 4536 ? 187.716 179.047 198.629 1.00 81.00  ? 4536 LEU A CD2   1 
ATOM   20869 N N     . GLU A 1 4537 ? 192.806 181.342 199.788 1.00 88.95  ? 4537 GLU A N     1 
ATOM   20870 C CA    . GLU A 1 4537 ? 194.182 181.164 199.339 1.00 88.95  ? 4537 GLU A CA    1 
ATOM   20871 C C     . GLU A 1 4537 ? 195.059 180.606 200.450 1.00 88.95  ? 4537 GLU A C     1 
ATOM   20872 O O     . GLU A 1 4537 ? 195.907 179.740 200.209 1.00 88.95  ? 4537 GLU A O     1 
ATOM   20873 C CB    . GLU A 1 4537 ? 194.743 182.492 198.853 1.00 88.95  ? 4537 GLU A CB    1 
ATOM   20874 C CG    . GLU A 1 4537 ? 194.284 183.664 199.691 1.00 88.95  ? 4537 GLU A CG    1 
ATOM   20875 C CD    . GLU A 1 4537 ? 194.253 184.947 198.905 1.00 88.95  ? 4537 GLU A CD    1 
ATOM   20876 O OE1   . GLU A 1 4537 ? 194.424 186.027 199.509 1.00 88.95  ? 4537 GLU A OE1   1 
ATOM   20877 O OE2   . GLU A 1 4537 ? 194.075 184.868 197.673 1.00 88.95  ? 4537 GLU A OE2   1 
ATOM   20878 N N     . GLU A 1 4538 ? 194.873 181.095 201.674 1.00 92.00  ? 4538 GLU A N     1 
ATOM   20879 C CA    . GLU A 1 4538 ? 195.742 180.734 202.784 1.00 92.00  ? 4538 GLU A CA    1 
ATOM   20880 C C     . GLU A 1 4538 ? 195.486 179.332 203.318 1.00 92.00  ? 4538 GLU A C     1 
ATOM   20881 O O     . GLU A 1 4538 ? 196.231 178.879 204.193 1.00 92.00  ? 4538 GLU A O     1 
ATOM   20882 C CB    . GLU A 1 4538 ? 195.591 181.751 203.914 1.00 92.00  ? 4538 GLU A CB    1 
ATOM   20883 C CG    . GLU A 1 4538 ? 195.625 183.192 203.446 1.00 92.00  ? 4538 GLU A CG    1 
ATOM   20884 C CD    . GLU A 1 4538 ? 194.829 184.115 204.346 1.00 92.00  ? 4538 GLU A CD    1 
ATOM   20885 O OE1   . GLU A 1 4538 ? 193.638 183.828 204.591 1.00 92.00  ? 4538 GLU A OE1   1 
ATOM   20886 O OE2   . GLU A 1 4538 ? 195.396 185.127 204.810 1.00 92.00  ? 4538 GLU A OE2   1 
ATOM   20887 N N     . LEU A 1 4539 ? 194.463 178.642 202.830 1.00 84.75  ? 4539 LEU A N     1 
ATOM   20888 C CA    . LEU A 1 4539 ? 194.139 177.302 203.294 1.00 84.75  ? 4539 LEU A CA    1 
ATOM   20889 C C     . LEU A 1 4539 ? 194.711 176.265 202.339 1.00 84.75  ? 4539 LEU A C     1 
ATOM   20890 O O     . LEU A 1 4539 ? 194.402 176.277 201.144 1.00 84.75  ? 4539 LEU A O     1 
ATOM   20891 C CB    . LEU A 1 4539 ? 192.628 177.122 203.421 1.00 84.75  ? 4539 LEU A CB    1 
ATOM   20892 C CG    . LEU A 1 4539 ? 191.946 178.109 204.362 1.00 84.75  ? 4539 LEU A CG    1 
ATOM   20893 C CD1   . LEU A 1 4539 ? 190.516 177.687 204.628 1.00 84.75  ? 4539 LEU A CD1   1 
ATOM   20894 C CD2   . LEU A 1 4539 ? 192.725 178.218 205.657 1.00 84.75  ? 4539 LEU A CD2   1 
ATOM   20895 N N     . CYS A 1 4540 ? 195.541 175.374 202.872 1.00 85.78  ? 4540 CYS A N     1 
ATOM   20896 C CA    . CYS A 1 4540 ? 196.070 174.240 202.135 1.00 85.78  ? 4540 CYS A CA    1 
ATOM   20897 C C     . CYS A 1 4540 ? 195.656 172.959 202.841 1.00 85.78  ? 4540 CYS A C     1 
ATOM   20898 O O     . CYS A 1 4540 ? 195.530 172.922 204.068 1.00 85.78  ? 4540 CYS A O     1 
ATOM   20899 C CB    . CYS A 1 4540 ? 197.592 174.307 202.015 1.00 85.78  ? 4540 CYS A CB    1 
ATOM   20900 S SG    . CYS A 1 4540 ? 198.469 174.098 203.574 1.00 85.78  ? 4540 CYS A SG    1 
ATOM   20901 N N     . LEU A 1 4541 ? 195.442 171.907 202.060 1.00 81.21  ? 4541 LEU A N     1 
ATOM   20902 C CA    . LEU A 1 4541 ? 194.870 170.674 202.579 1.00 81.21  ? 4541 LEU A CA    1 
ATOM   20903 C C     . LEU A 1 4541 ? 195.959 169.771 203.139 1.00 81.21  ? 4541 LEU A C     1 
ATOM   20904 O O     . LEU A 1 4541 ? 196.924 169.441 202.445 1.00 81.21  ? 4541 LEU A O     1 
ATOM   20905 C CB    . LEU A 1 4541 ? 194.091 169.941 201.489 1.00 81.21  ? 4541 LEU A CB    1 
ATOM   20906 C CG    . LEU A 1 4541 ? 193.738 168.481 201.768 1.00 81.21  ? 4541 LEU A CG    1 
ATOM   20907 C CD1   . LEU A 1 4541 ? 192.943 168.345 203.054 1.00 81.21  ? 4541 LEU A CD1   1 
ATOM   20908 C CD2   . LEU A 1 4541 ? 192.961 167.908 200.604 1.00 81.21  ? 4541 LEU A CD2   1 
ATOM   20909 N N     . GLU A 1 4542 ? 195.793 169.376 204.395 1.00 85.08  ? 4542 GLU A N     1 
ATOM   20910 C CA    . GLU A 1 4542 ? 196.636 168.388 205.049 1.00 85.08  ? 4542 GLU A CA    1 
ATOM   20911 C C     . GLU A 1 4542 ? 195.784 167.173 205.374 1.00 85.08  ? 4542 GLU A C     1 
ATOM   20912 O O     . GLU A 1 4542 ? 194.724 167.305 205.993 1.00 85.08  ? 4542 GLU A O     1 
ATOM   20913 C CB    . GLU A 1 4542 ? 197.256 168.956 206.324 1.00 85.08  ? 4542 GLU A CB    1 
ATOM   20914 C CG    . GLU A 1 4542 ? 198.014 167.943 207.151 1.00 85.08  ? 4542 GLU A CG    1 
ATOM   20915 C CD    . GLU A 1 4542 ? 198.336 168.462 208.537 1.00 85.08  ? 4542 GLU A CD    1 
ATOM   20916 O OE1   . GLU A 1 4542 ? 198.911 169.566 208.638 1.00 85.08  ? 4542 GLU A OE1   1 
ATOM   20917 O OE2   . GLU A 1 4542 ? 198.010 167.771 209.524 1.00 85.08  ? 4542 GLU A OE2   1 
ATOM   20918 N N     . VAL A 1 4543 ? 196.244 165.997 204.963 1.00 78.90  ? 4543 VAL A N     1 
ATOM   20919 C CA    . VAL A 1 4543 ? 195.480 164.764 205.095 1.00 78.90  ? 4543 VAL A CA    1 
ATOM   20920 C C     . VAL A 1 4543 ? 196.038 163.972 206.267 1.00 78.90  ? 4543 VAL A C     1 
ATOM   20921 O O     . VAL A 1 4543 ? 197.206 164.136 206.638 1.00 78.90  ? 4543 VAL A O     1 
ATOM   20922 C CB    . VAL A 1 4543 ? 195.514 163.937 203.800 1.00 78.90  ? 4543 VAL A CB    1 
ATOM   20923 C CG1   . VAL A 1 4543 ? 196.769 163.091 203.740 1.00 78.90  ? 4543 VAL A CG1   1 
ATOM   20924 C CG2   . VAL A 1 4543 ? 194.278 163.074 203.696 1.00 78.90  ? 4543 VAL A CG2   1 
ATOM   20925 N N     . ASN A 1 4544 ? 195.195 163.135 206.863 1.00 91.07  ? 4544 ASN A N     1 
ATOM   20926 C CA    . ASN A 1 4544 ? 195.575 162.309 208.000 1.00 91.07  ? 4544 ASN A CA    1 
ATOM   20927 C C     . ASN A 1 4544 ? 194.680 161.082 208.021 1.00 91.07  ? 4544 ASN A C     1 
ATOM   20928 O O     . ASN A 1 4544 ? 193.452 161.209 208.044 1.00 91.07  ? 4544 ASN A O     1 
ATOM   20929 C CB    . ASN A 1 4544 ? 195.454 163.090 209.309 1.00 91.07  ? 4544 ASN A CB    1 
ATOM   20930 C CG    . ASN A 1 4544 ? 195.661 162.220 210.527 1.00 91.07  ? 4544 ASN A CG    1 
ATOM   20931 O OD1   . ASN A 1 4544 ? 196.750 161.699 210.753 1.00 91.07  ? 4544 ASN A OD1   1 
ATOM   20932 N ND2   . ASN A 1 4544 ? 194.612 162.060 211.323 1.00 91.07  ? 4544 ASN A ND2   1 
ATOM   20933 N N     . VAL A 1 4545 ? 195.287 159.902 208.012 1.00 91.86  ? 4545 VAL A N     1 
ATOM   20934 C CA    . VAL A 1 4545 ? 194.556 158.642 208.016 1.00 91.86  ? 4545 VAL A CA    1 
ATOM   20935 C C     . VAL A 1 4545 ? 194.478 158.161 209.456 1.00 91.86  ? 4545 VAL A C     1 
ATOM   20936 O O     . VAL A 1 4545 ? 195.505 157.985 210.120 1.00 91.86  ? 4545 VAL A O     1 
ATOM   20937 C CB    . VAL A 1 4545 ? 195.220 157.595 207.115 1.00 91.86  ? 4545 VAL A CB    1 
ATOM   20938 C CG1   . VAL A 1 4545 ? 194.430 156.306 207.145 1.00 91.86  ? 4545 VAL A CG1   1 
ATOM   20939 C CG2   . VAL A 1 4545 ? 195.333 158.113 205.699 1.00 91.86  ? 4545 VAL A CG2   1 
ATOM   20940 N N     . THR A 1 4546 ? 193.265 157.951 209.944 1.00 104.75 ? 4546 THR A N     1 
ATOM   20941 C CA    . THR A 1 4546 ? 193.044 157.528 211.316 1.00 104.75 ? 4546 THR A CA    1 
ATOM   20942 C C     . THR A 1 4546 ? 192.420 156.139 211.343 1.00 104.75 ? 4546 THR A C     1 
ATOM   20943 O O     . THR A 1 4546 ? 191.488 155.840 210.593 1.00 104.75 ? 4546 THR A O     1 
ATOM   20944 C CB    . THR A 1 4546 ? 192.148 158.527 212.051 1.00 104.75 ? 4546 THR A CB    1 
ATOM   20945 O OG1   . THR A 1 4546 ? 192.907 159.700 212.370 1.00 104.75 ? 4546 THR A OG1   1 
ATOM   20946 C CG2   . THR A 1 4546 ? 191.603 157.923 213.335 1.00 104.75 ? 4546 THR A CG2   1 
ATOM   20947 N N     . THR A 1 4547 ? 192.960 155.284 212.213 1.00 118.60 ? 4547 THR A N     1 
ATOM   20948 C CA    . THR A 1 4547 ? 192.464 153.918 212.334 1.00 118.60 ? 4547 THR A CA    1 
ATOM   20949 C C     . THR A 1 4547 ? 191.018 153.876 212.813 1.00 118.60 ? 4547 THR A C     1 
ATOM   20950 O O     . THR A 1 4547 ? 190.212 153.098 212.290 1.00 118.60 ? 4547 THR A O     1 
ATOM   20951 C CB    . THR A 1 4547 ? 193.354 153.121 213.287 1.00 118.60 ? 4547 THR A CB    1 
ATOM   20952 O OG1   . THR A 1 4547 ? 194.731 153.350 212.963 1.00 118.60 ? 4547 THR A OG1   1 
ATOM   20953 C CG2   . THR A 1 4547 ? 193.053 151.635 213.174 1.00 118.60 ? 4547 THR A CG2   1 
ATOM   20954 N N     . SER A 1 4548 ? 190.670 154.695 213.802 1.00 124.91 ? 4548 SER A N     1 
ATOM   20955 C CA    . SER A 1 4548 ? 189.337 154.639 214.386 1.00 124.91 ? 4548 SER A CA    1 
ATOM   20956 C C     . SER A 1 4548 ? 188.302 155.187 213.413 1.00 124.91 ? 4548 SER A C     1 
ATOM   20957 O O     . SER A 1 4548 ? 188.485 156.260 212.832 1.00 124.91 ? 4548 SER A O     1 
ATOM   20958 C CB    . SER A 1 4548 ? 189.299 155.425 215.697 1.00 124.91 ? 4548 SER A CB    1 
ATOM   20959 O OG    . SER A 1 4548 ? 187.972 155.557 216.175 1.00 124.91 ? 4548 SER A OG    1 
ATOM   20960 N N     . GLN A 1 4549 ? 187.206 154.448 213.242 1.00 134.20 ? 4549 GLN A N     1 
ATOM   20961 C CA    . GLN A 1 4549 ? 186.122 154.882 212.371 1.00 134.20 ? 4549 GLN A CA    1 
ATOM   20962 C C     . GLN A 1 4549 ? 185.216 155.917 213.023 1.00 134.20 ? 4549 GLN A C     1 
ATOM   20963 O O     . GLN A 1 4549 ? 184.339 156.461 212.345 1.00 134.20 ? 4549 GLN A O     1 
ATOM   20964 C CB    . GLN A 1 4549 ? 185.283 153.681 211.927 1.00 134.20 ? 4549 GLN A CB    1 
ATOM   20965 C CG    . GLN A 1 4549 ? 185.869 152.902 210.760 1.00 134.20 ? 4549 GLN A CG    1 
ATOM   20966 C CD    . GLN A 1 4549 ? 186.987 151.969 211.180 1.00 134.20 ? 4549 GLN A CD    1 
ATOM   20967 O OE1   . GLN A 1 4549 ? 188.121 152.097 210.724 1.00 134.20 ? 4549 GLN A OE1   1 
ATOM   20968 N NE2   . GLN A 1 4549 ? 186.668 151.018 212.049 1.00 134.20 ? 4549 GLN A NE2   1 
ATOM   20969 N N     . GLY A 1 4550 ? 185.394 156.192 214.311 1.00 134.41 ? 4550 GLY A N     1 
ATOM   20970 C CA    . GLY A 1 4550 ? 184.599 157.194 214.992 1.00 134.41 ? 4550 GLY A CA    1 
ATOM   20971 C C     . GLY A 1 4550 ? 185.447 158.171 215.780 1.00 134.41 ? 4550 GLY A C     1 
ATOM   20972 O O     . GLY A 1 4550 ? 185.058 158.607 216.868 1.00 134.41 ? 4550 GLY A O     1 
ATOM   20973 N N     . ALA A 1 4551 ? 186.612 158.517 215.240 1.00 127.18 ? 4551 ALA A N     1 
ATOM   20974 C CA    . ALA A 1 4551 ? 187.536 159.398 215.934 1.00 127.18 ? 4551 ALA A CA    1 
ATOM   20975 C C     . ALA A 1 4551 ? 186.989 160.822 215.998 1.00 127.18 ? 4551 ALA A C     1 
ATOM   20976 O O     . ALA A 1 4551 ? 186.095 161.214 215.243 1.00 127.18 ? 4551 ALA A O     1 
ATOM   20977 C CB    . ALA A 1 4551 ? 188.901 159.393 215.250 1.00 127.18 ? 4551 ALA A CB    1 
ATOM   20978 N N     . THR A 1 4552 ? 187.548 161.599 216.921 1.00 120.88 ? 4552 THR A N     1 
ATOM   20979 C CA    . THR A 1 4552 ? 187.084 162.961 217.138 1.00 120.88 ? 4552 THR A CA    1 
ATOM   20980 C C     . THR A 1 4552 ? 187.494 163.872 215.988 1.00 120.88 ? 4552 THR A C     1 
ATOM   20981 O O     . THR A 1 4552 ? 188.600 163.771 215.453 1.00 120.88 ? 4552 THR A O     1 
ATOM   20982 C CB    . THR A 1 4552 ? 187.641 163.504 218.452 1.00 120.88 ? 4552 THR A CB    1 
ATOM   20983 O OG1   . THR A 1 4552 ? 189.073 163.528 218.390 1.00 120.88 ? 4552 THR A OG1   1 
ATOM   20984 C CG2   . THR A 1 4552 ? 187.204 162.629 219.617 1.00 120.88 ? 4552 THR A CG2   1 
ATOM   20985 N N     . LEU A 1 4553 ? 186.591 164.773 215.617 1.00 109.08 ? 4553 LEU A N     1 
ATOM   20986 C CA    . LEU A 1 4553 ? 186.857 165.810 214.630 1.00 109.08 ? 4553 LEU A CA    1 
ATOM   20987 C C     . LEU A 1 4553 ? 186.981 167.140 215.358 1.00 109.08 ? 4553 LEU A C     1 
ATOM   20988 O O     . LEU A 1 4553 ? 186.052 167.555 216.057 1.00 109.08 ? 4553 LEU A O     1 
ATOM   20989 C CB    . LEU A 1 4553 ? 185.745 165.878 213.586 1.00 109.08 ? 4553 LEU A CB    1 
ATOM   20990 C CG    . LEU A 1 4553 ? 185.567 164.671 212.669 1.00 109.08 ? 4553 LEU A CG    1 
ATOM   20991 C CD1   . LEU A 1 4553 ? 184.789 165.081 211.434 1.00 109.08 ? 4553 LEU A CD1   1 
ATOM   20992 C CD2   . LEU A 1 4553 ? 186.915 164.085 212.288 1.00 109.08 ? 4553 LEU A CD2   1 
ATOM   20993 N N     . ASP A 1 4554 ? 188.119 167.802 215.194 1.00 107.69 ? 4554 ASP A N     1 
ATOM   20994 C CA    . ASP A 1 4554 ? 188.396 169.057 215.878 1.00 107.69 ? 4554 ASP A CA    1 
ATOM   20995 C C     . ASP A 1 4554 ? 188.485 170.184 214.859 1.00 107.69 ? 4554 ASP A C     1 
ATOM   20996 O O     . ASP A 1 4554 ? 189.305 170.128 213.937 1.00 107.69 ? 4554 ASP A O     1 
ATOM   20997 C CB    . ASP A 1 4554 ? 189.685 168.957 216.691 1.00 107.69 ? 4554 ASP A CB    1 
ATOM   20998 C CG    . ASP A 1 4554 ? 190.878 168.590 215.843 1.00 107.69 ? 4554 ASP A CG    1 
ATOM   20999 O OD1   . ASP A 1 4554 ? 190.766 167.629 215.054 1.00 107.69 ? 4554 ASP A OD1   1 
ATOM   21000 O OD2   . ASP A 1 4554 ? 191.922 169.264 215.958 1.00 107.69 ? 4554 ASP A OD2   1 
ATOM   21001 N N     . ALA A 1 4555 ? 187.634 171.197 215.028 1.00 104.43 ? 4555 ALA A N     1 
ATOM   21002 C CA    . ALA A 1 4555 ? 187.703 172.429 214.252 1.00 104.43 ? 4555 ALA A CA    1 
ATOM   21003 C C     . ALA A 1 4555 ? 187.693 172.170 212.752 1.00 104.43 ? 4555 ALA A C     1 
ATOM   21004 O O     . ALA A 1 4555 ? 186.627 172.018 212.147 1.00 104.43 ? 4555 ALA A O     1 
ATOM   21005 C CB    . ALA A 1 4555 ? 188.950 173.228 214.637 1.00 104.43 ? 4555 ALA A CB    1 
ATOM   21006 N N     . CYS A 1 4556 ? 188.878 172.135 212.145 1.00 102.16 ? 4556 CYS A N     1 
ATOM   21007 C CA    . CYS A 1 4556 ? 189.004 172.025 210.699 1.00 102.16 ? 4556 CYS A CA    1 
ATOM   21008 C C     . CYS A 1 4556 ? 189.066 170.589 210.199 1.00 102.16 ? 4556 CYS A C     1 
ATOM   21009 O O     . CYS A 1 4556 ? 189.048 170.378 208.983 1.00 102.16 ? 4556 CYS A O     1 
ATOM   21010 C CB    . CYS A 1 4556 ? 190.253 172.772 210.235 1.00 102.16 ? 4556 CYS A CB    1 
ATOM   21011 S SG    . CYS A 1 4556 ? 190.572 174.301 211.137 1.00 102.16 ? 4556 CYS A SG    1 
ATOM   21012 N N     . SER A 1 4557 ? 189.145 169.602 211.085 1.00 98.68  ? 4557 SER A N     1 
ATOM   21013 C CA    . SER A 1 4557 ? 189.271 168.217 210.653 1.00 98.68  ? 4557 SER A CA    1 
ATOM   21014 C C     . SER A 1 4557 ? 187.916 167.669 210.225 1.00 98.68  ? 4557 SER A C     1 
ATOM   21015 O O     . SER A 1 4557 ? 186.925 167.807 210.947 1.00 98.68  ? 4557 SER A O     1 
ATOM   21016 C CB    . SER A 1 4557 ? 189.862 167.363 211.772 1.00 98.68  ? 4557 SER A CB    1 
ATOM   21017 O OG    . SER A 1 4557 ? 191.127 167.858 212.172 1.00 98.68  ? 4557 SER A OG    1 
ATOM   21018 N N     . PHE A 1 4558 ? 187.878 167.041 209.054 1.00 90.93  ? 4558 PHE A N     1 
ATOM   21019 C CA    . PHE A 1 4558 ? 186.657 166.482 208.496 1.00 90.93  ? 4558 PHE A CA    1 
ATOM   21020 C C     . PHE A 1 4558 ? 186.802 164.980 208.320 1.00 90.93  ? 4558 PHE A C     1 
ATOM   21021 O O     . PHE A 1 4558 ? 187.900 164.466 208.093 1.00 90.93  ? 4558 PHE A O     1 
ATOM   21022 C CB    . PHE A 1 4558 ? 186.313 167.118 207.150 1.00 90.93  ? 4558 PHE A CB    1 
ATOM   21023 C CG    . PHE A 1 4558 ? 185.694 168.472 207.265 1.00 90.93  ? 4558 PHE A CG    1 
ATOM   21024 C CD1   . PHE A 1 4558 ? 186.377 169.507 207.870 1.00 90.93  ? 4558 PHE A CD1   1 
ATOM   21025 C CD2   . PHE A 1 4558 ? 184.426 168.707 206.774 1.00 90.93  ? 4558 PHE A CD2   1 
ATOM   21026 C CE1   . PHE A 1 4558 ? 185.811 170.751 207.981 1.00 90.93  ? 4558 PHE A CE1   1 
ATOM   21027 C CE2   . PHE A 1 4558 ? 183.854 169.951 206.883 1.00 90.93  ? 4558 PHE A CE2   1 
ATOM   21028 C CZ    . PHE A 1 4558 ? 184.547 170.976 207.486 1.00 90.93  ? 4558 PHE A CZ    1 
ATOM   21029 N N     . GLY A 1 4559 ? 185.676 164.277 208.420 1.00 92.23  ? 4559 GLY A N     1 
ATOM   21030 C CA    . GLY A 1 4559 ? 185.671 162.835 208.288 1.00 92.23  ? 4559 GLY A CA    1 
ATOM   21031 C C     . GLY A 1 4559 ? 185.397 162.421 206.859 1.00 92.23  ? 4559 GLY A C     1 
ATOM   21032 O O     . GLY A 1 4559 ? 184.475 162.933 206.219 1.00 92.23  ? 4559 GLY A O     1 
ATOM   21033 N N     . VAL A 1 4560 ? 186.208 161.497 206.357 1.00 86.47  ? 4560 VAL A N     1 
ATOM   21034 C CA    . VAL A 1 4560 ? 186.044 160.961 205.013 1.00 86.47  ? 4560 VAL A CA    1 
ATOM   21035 C C     . VAL A 1 4560 ? 186.242 159.456 205.072 1.00 86.47  ? 4560 VAL A C     1 
ATOM   21036 O O     . VAL A 1 4560 ? 187.239 158.978 205.624 1.00 86.47  ? 4560 VAL A O     1 
ATOM   21037 C CB    . VAL A 1 4560 ? 187.031 161.603 204.022 1.00 86.47  ? 4560 VAL A CB    1 
ATOM   21038 C CG1   . VAL A 1 4560 ? 187.297 160.671 202.863 1.00 86.47  ? 4560 VAL A CG1   1 
ATOM   21039 C CG2   . VAL A 1 4560 ? 186.489 162.928 203.532 1.00 86.47  ? 4560 VAL A CG2   1 
ATOM   21040 N N     . THR A 1 4561 ? 185.299 158.711 204.509 1.00 88.20  ? 4561 THR A N     1 
ATOM   21041 C CA    . THR A 1 4561 ? 185.362 157.260 204.471 1.00 88.20  ? 4561 THR A CA    1 
ATOM   21042 C C     . THR A 1 4561 ? 185.376 156.783 203.027 1.00 88.20  ? 4561 THR A C     1 
ATOM   21043 O O     . THR A 1 4561 ? 185.159 157.552 202.090 1.00 88.20  ? 4561 THR A O     1 
ATOM   21044 C CB    . THR A 1 4561 ? 184.180 156.630 205.211 1.00 88.20  ? 4561 THR A CB    1 
ATOM   21045 O OG1   . THR A 1 4561 ? 182.963 156.969 204.537 1.00 88.20  ? 4561 THR A OG1   1 
ATOM   21046 C CG2   . THR A 1 4561 ? 184.118 157.133 206.639 1.00 88.20  ? 4561 THR A CG2   1 
ATOM   21047 N N     . GLY A 1 4562 ? 185.649 155.494 202.858 1.00 85.27  ? 4562 GLY A N     1 
ATOM   21048 C CA    . GLY A 1 4562 ? 185.566 154.866 201.560 1.00 85.27  ? 4562 GLY A CA    1 
ATOM   21049 C C     . GLY A 1 4562 ? 186.759 155.073 200.658 1.00 85.27  ? 4562 GLY A C     1 
ATOM   21050 O O     . GLY A 1 4562 ? 186.778 154.520 199.553 1.00 85.27  ? 4562 GLY A O     1 
ATOM   21051 N N     . LEU A 1 4563 ? 187.753 155.845 201.083 1.00 83.19  ? 4563 LEU A N     1 
ATOM   21052 C CA    . LEU A 1 4563 ? 188.946 156.020 200.269 1.00 83.19  ? 4563 LEU A CA    1 
ATOM   21053 C C     . LEU A 1 4563 ? 189.732 154.719 200.224 1.00 83.19  ? 4563 LEU A C     1 
ATOM   21054 O O     . LEU A 1 4563 ? 189.991 154.102 201.261 1.00 83.19  ? 4563 LEU A O     1 
ATOM   21055 C CB    . LEU A 1 4563 ? 189.812 157.142 200.831 1.00 83.19  ? 4563 LEU A CB    1 
ATOM   21056 C CG    . LEU A 1 4563 ? 189.279 158.553 200.606 1.00 83.19  ? 4563 LEU A CG    1 
ATOM   21057 C CD1   . LEU A 1 4563 ? 190.379 159.569 200.821 1.00 83.19  ? 4563 LEU A CD1   1 
ATOM   21058 C CD2   . LEU A 1 4563 ? 188.691 158.681 199.216 1.00 83.19  ? 4563 LEU A CD2   1 
ATOM   21059 N N     . LYS A 1 4564 ? 190.106 154.298 199.021 1.00 79.72  ? 4564 LYS A N     1 
ATOM   21060 C CA    . LYS A 1 4564 ? 190.891 153.090 198.826 1.00 79.72  ? 4564 LYS A CA    1 
ATOM   21061 C C     . LYS A 1 4564 ? 192.241 153.469 198.246 1.00 79.72  ? 4564 LYS A C     1 
ATOM   21062 O O     . LYS A 1 4564 ? 192.310 154.137 197.210 1.00 79.72  ? 4564 LYS A O     1 
ATOM   21063 C CB    . LYS A 1 4564 ? 190.177 152.103 197.905 1.00 79.72  ? 4564 LYS A CB    1 
ATOM   21064 C CG    . LYS A 1 4564 ? 188.671 152.083 198.067 1.00 79.72  ? 4564 LYS A CG    1 
ATOM   21065 C CD    . LYS A 1 4564 ? 188.058 150.831 197.452 1.00 79.72  ? 4564 LYS A CD    1 
ATOM   21066 C CE    . LYS A 1 4564 ? 188.780 150.422 196.177 1.00 79.72  ? 4564 LYS A CE    1 
ATOM   21067 N NZ    . LYS A 1 4564 ? 187.956 149.519 195.325 1.00 79.72  ? 4564 LYS A NZ    1 
ATOM   21068 N N     . LEU A 1 4565 ? 193.305 153.044 198.913 1.00 77.37  ? 4565 LEU A N     1 
ATOM   21069 C CA    . LEU A 1 4565 ? 194.666 153.313 198.479 1.00 77.37  ? 4565 LEU A CA    1 
ATOM   21070 C C     . LEU A 1 4565 ? 195.157 152.139 197.648 1.00 77.37  ? 4565 LEU A C     1 
ATOM   21071 O O     . LEU A 1 4565 ? 195.019 150.983 198.059 1.00 77.37  ? 4565 LEU A O     1 
ATOM   21072 C CB    . LEU A 1 4565 ? 195.582 153.535 199.680 1.00 77.37  ? 4565 LEU A CB    1 
ATOM   21073 C CG    . LEU A 1 4565 ? 197.020 153.924 199.365 1.00 77.37  ? 4565 LEU A CG    1 
ATOM   21074 C CD1   . LEU A 1 4565 ? 197.039 155.037 198.346 1.00 77.37  ? 4565 LEU A CD1   1 
ATOM   21075 C CD2   . LEU A 1 4565 ? 197.727 154.347 200.631 1.00 77.37  ? 4565 LEU A CD2   1 
ATOM   21076 N N     . GLN A 1 4566 ? 195.722 152.433 196.484 1.00 77.23  ? 4566 GLN A N     1 
ATOM   21077 C CA    . GLN A 1 4566 ? 196.152 151.409 195.546 1.00 77.23  ? 4566 GLN A CA    1 
ATOM   21078 C C     . GLN A 1 4566 ? 197.668 151.409 195.430 1.00 77.23  ? 4566 GLN A C     1 
ATOM   21079 O O     . GLN A 1 4566 ? 198.270 152.438 195.110 1.00 77.23  ? 4566 GLN A O     1 
ATOM   21080 C CB    . GLN A 1 4566 ? 195.517 151.633 194.175 1.00 77.23  ? 4566 GLN A CB    1 
ATOM   21081 C CG    . GLN A 1 4566 ? 194.057 151.248 194.124 1.00 77.23  ? 4566 GLN A CG    1 
ATOM   21082 C CD    . GLN A 1 4566 ? 193.668 150.653 192.793 1.00 77.23  ? 4566 GLN A CD    1 
ATOM   21083 O OE1   . GLN A 1 4566 ? 194.415 150.740 191.822 1.00 77.23  ? 4566 GLN A OE1   1 
ATOM   21084 N NE2   . GLN A 1 4566 ? 192.501 150.025 192.745 1.00 77.23  ? 4566 GLN A NE2   1 
ATOM   21085 N N     . GLY A 1 4567 ? 198.278 150.253 195.682 1.00 81.37  ? 4567 GLY A N     1 
ATOM   21086 C CA    . GLY A 1 4567 ? 199.702 150.082 195.515 1.00 81.37  ? 4567 GLY A CA    1 
ATOM   21087 C C     . GLY A 1 4567 ? 200.546 150.372 196.735 1.00 81.37  ? 4567 GLY A C     1 
ATOM   21088 O O     . GLY A 1 4567 ? 201.762 150.152 196.689 1.00 81.37  ? 4567 GLY A O     1 
ATOM   21089 N N     . ALA A 1 4568 ? 199.955 150.850 197.826 1.00 84.14  ? 4568 ALA A N     1 
ATOM   21090 C CA    . ALA A 1 4568 ? 200.735 151.178 199.008 1.00 84.14  ? 4568 ALA A CA    1 
ATOM   21091 C C     . ALA A 1 4568 ? 199.843 151.126 200.237 1.00 84.14  ? 4568 ALA A C     1 
ATOM   21092 O O     . ALA A 1 4568 ? 198.615 151.146 200.138 1.00 84.14  ? 4568 ALA A O     1 
ATOM   21093 C CB    . ALA A 1 4568 ? 201.386 152.557 198.881 1.00 84.14  ? 4568 ALA A CB    1 
ATOM   21094 N N     . THR A 1 4569 ? 200.480 151.060 201.402 1.00 88.85  ? 4569 THR A N     1 
ATOM   21095 C CA    . THR A 1 4569 ? 199.783 151.049 202.680 1.00 88.85  ? 4569 THR A CA    1 
ATOM   21096 C C     . THR A 1 4569 ? 200.233 152.235 203.517 1.00 88.85  ? 4569 THR A C     1 
ATOM   21097 O O     . THR A 1 4569 ? 201.399 152.637 203.467 1.00 88.85  ? 4569 THR A O     1 
ATOM   21098 C CB    . THR A 1 4569 ? 200.039 149.757 203.455 1.00 88.85  ? 4569 THR A CB    1 
ATOM   21099 O OG1   . THR A 1 4569 ? 201.389 149.746 203.933 1.00 88.85  ? 4569 THR A OG1   1 
ATOM   21100 C CG2   . THR A 1 4569 ? 199.808 148.547 202.569 1.00 88.85  ? 4569 THR A CG2   1 
ATOM   21101 N N     . CYS A 1 4570 ? 199.303 152.786 204.287 1.00 93.32  ? 4570 CYS A N     1 
ATOM   21102 C CA    . CYS A 1 4570 ? 199.564 153.932 205.144 1.00 93.32  ? 4570 CYS A CA    1 
ATOM   21103 C C     . CYS A 1 4570 ? 199.492 153.492 206.599 1.00 93.32  ? 4570 CYS A C     1 
ATOM   21104 O O     . CYS A 1 4570 ? 198.450 153.008 207.053 1.00 93.32  ? 4570 CYS A O     1 
ATOM   21105 C CB    . CYS A 1 4570 ? 198.561 155.052 204.877 1.00 93.32  ? 4570 CYS A CB    1 
ATOM   21106 S SG    . CYS A 1 4570 ? 198.382 156.208 206.244 1.00 93.32  ? 4570 CYS A SG    1 
ATOM   21107 N N     . ASN A 1 4571 ? 200.594 153.664 207.323 1.00 99.64  ? 4571 ASN A N     1 
ATOM   21108 C CA    . ASN A 1 4571 ? 200.658 153.405 208.756 1.00 99.64  ? 4571 ASN A CA    1 
ATOM   21109 C C     . ASN A 1 4571 ? 201.122 154.674 209.450 1.00 99.64  ? 4571 ASN A C     1 
ATOM   21110 O O     . ASN A 1 4571 ? 202.203 155.188 209.144 1.00 99.64  ? 4571 ASN A O     1 
ATOM   21111 C CB    . ASN A 1 4571 ? 201.604 152.246 209.072 1.00 99.64  ? 4571 ASN A CB    1 
ATOM   21112 C CG    . ASN A 1 4571 ? 200.933 150.897 208.949 1.00 99.64  ? 4571 ASN A CG    1 
ATOM   21113 O OD1   . ASN A 1 4571 ? 199.798 150.713 209.387 1.00 99.64  ? 4571 ASN A OD1   1 
ATOM   21114 N ND2   . ASN A 1 4571 ? 201.632 149.942 208.350 1.00 99.64  ? 4571 ASN A ND2   1 
ATOM   21115 N N     . ASN A 1 4572 ? 200.307 155.173 210.379 1.00 102.14 ? 4572 ASN A N     1 
ATOM   21116 C CA    . ASN A 1 4572 ? 200.630 156.376 211.145 1.00 102.14 ? 4572 ASN A CA    1 
ATOM   21117 C C     . ASN A 1 4572 ? 200.968 157.543 210.223 1.00 102.14 ? 4572 ASN A C     1 
ATOM   21118 O O     . ASN A 1 4572 ? 201.929 158.281 210.449 1.00 102.14 ? 4572 ASN A O     1 
ATOM   21119 C CB    . ASN A 1 4572 ? 201.774 156.110 212.123 1.00 102.14 ? 4572 ASN A CB    1 
ATOM   21120 C CG    . ASN A 1 4572 ? 201.332 155.313 213.328 1.00 102.14 ? 4572 ASN A CG    1 
ATOM   21121 O OD1   . ASN A 1 4572 ? 200.234 154.760 213.350 1.00 102.14 ? 4572 ASN A OD1   1 
ATOM   21122 N ND2   . ASN A 1 4572 ? 202.188 155.247 214.340 1.00 102.14 ? 4572 ASN A ND2   1 
ATOM   21123 N N     . ASN A 1 4573 ? 200.177 157.697 209.163 1.00 93.55  ? 4573 ASN A N     1 
ATOM   21124 C CA    . ASN A 1 4573 ? 200.313 158.754 208.165 1.00 93.55  ? 4573 ASN A CA    1 
ATOM   21125 C C     . ASN A 1 4573 ? 201.604 158.657 207.361 1.00 93.55  ? 4573 ASN A C     1 
ATOM   21126 O O     . ASN A 1 4573 ? 201.987 159.627 206.699 1.00 93.55  ? 4573 ASN A O     1 
ATOM   21127 C CB    . ASN A 1 4573 ? 200.207 160.146 208.799 1.00 93.55  ? 4573 ASN A CB    1 
ATOM   21128 C CG    . ASN A 1 4573 ? 198.792 160.667 208.817 1.00 93.55  ? 4573 ASN A CG    1 
ATOM   21129 O OD1   . ASN A 1 4573 ? 197.855 159.962 208.445 1.00 93.55  ? 4573 ASN A OD1   1 
ATOM   21130 N ND2   . ASN A 1 4573 ? 198.626 161.909 209.252 1.00 93.55  ? 4573 ASN A ND2   1 
ATOM   21131 N N     . LYS A 1 4574 ? 202.288 157.520 207.396 1.00 95.34  ? 4574 LYS A N     1 
ATOM   21132 C CA    . LYS A 1 4574 ? 203.481 157.302 206.593 1.00 95.34  ? 4574 LYS A CA    1 
ATOM   21133 C C     . LYS A 1 4574 ? 203.210 156.189 205.593 1.00 95.34  ? 4574 LYS A C     1 
ATOM   21134 O O     . LYS A 1 4574 ? 202.695 155.130 205.962 1.00 95.34  ? 4574 LYS A O     1 
ATOM   21135 C CB    . LYS A 1 4574 ? 204.685 156.953 207.468 1.00 95.34  ? 4574 LYS A CB    1 
ATOM   21136 C CG    . LYS A 1 4574 ? 204.672 157.601 208.839 1.00 95.34  ? 4574 LYS A CG    1 
ATOM   21137 C CD    . LYS A 1 4574 ? 205.646 156.911 209.782 1.00 95.34  ? 4574 LYS A CD    1 
ATOM   21138 C CE    . LYS A 1 4574 ? 204.988 155.764 210.527 1.00 95.34  ? 4574 LYS A CE    1 
ATOM   21139 N NZ    . LYS A 1 4574 ? 205.878 155.193 211.573 1.00 95.34  ? 4574 LYS A NZ    1 
ATOM   21140 N N     . LEU A 1 4575 ? 203.554 156.433 204.334 1.00 88.64  ? 4575 LEU A N     1 
ATOM   21141 C CA    . LEU A 1 4575 ? 203.280 155.474 203.276 1.00 88.64  ? 4575 LEU A CA    1 
ATOM   21142 C C     . LEU A 1 4575 ? 204.351 154.395 203.225 1.00 88.64  ? 4575 LEU A C     1 
ATOM   21143 O O     . LEU A 1 4575 ? 205.443 154.541 203.779 1.00 88.64  ? 4575 LEU A O     1 
ATOM   21144 C CB    . LEU A 1 4575 ? 203.196 156.177 201.924 1.00 88.64  ? 4575 LEU A CB    1 
ATOM   21145 C CG    . LEU A 1 4575 ? 201.872 156.877 201.635 1.00 88.64  ? 4575 LEU A CG    1 
ATOM   21146 C CD1   . LEU A 1 4575 ? 201.724 157.125 200.152 1.00 88.64  ? 4575 LEU A CD1   1 
ATOM   21147 C CD2   . LEU A 1 4575 ? 200.718 156.048 202.154 1.00 88.64  ? 4575 LEU A CD2   1 
ATOM   21148 N N     . SER A 1 4576 ? 204.019 153.297 202.550 1.00 88.51  ? 4576 SER A N     1 
ATOM   21149 C CA    . SER A 1 4576 ? 204.956 152.204 202.334 1.00 88.51  ? 4576 SER A CA    1 
ATOM   21150 C C     . SER A 1 4576 ? 204.493 151.400 201.131 1.00 88.51  ? 4576 SER A C     1 
ATOM   21151 O O     . SER A 1 4576 ? 203.318 151.036 201.045 1.00 88.51  ? 4576 SER A O     1 
ATOM   21152 C CB    . SER A 1 4576 ? 205.057 151.307 203.570 1.00 88.51  ? 4576 SER A CB    1 
ATOM   21153 O OG    . SER A 1 4576 ? 205.881 150.185 203.315 1.00 88.51  ? 4576 SER A OG    1 
ATOM   21154 N N     . LEU A 1 4577 ? 205.414 151.129 200.211 1.00 84.65  ? 4577 LEU A N     1 
ATOM   21155 C CA    . LEU A 1 4577 ? 205.073 150.361 199.023 1.00 84.65  ? 4577 LEU A CA    1 
ATOM   21156 C C     . LEU A 1 4577 ? 204.655 148.947 199.404 1.00 84.65  ? 4577 LEU A C     1 
ATOM   21157 O O     . LEU A 1 4577 ? 205.252 148.321 200.283 1.00 84.65  ? 4577 LEU A O     1 
ATOM   21158 C CB    . LEU A 1 4577 ? 206.262 150.313 198.065 1.00 84.65  ? 4577 LEU A CB    1 
ATOM   21159 C CG    . LEU A 1 4577 ? 206.228 151.248 196.858 1.00 84.65  ? 4577 LEU A CG    1 
ATOM   21160 C CD1   . LEU A 1 4577 ? 207.221 150.788 195.808 1.00 84.65  ? 4577 LEU A CD1   1 
ATOM   21161 C CD2   . LEU A 1 4577 ? 204.835 151.314 196.277 1.00 84.65  ? 4577 LEU A CD2   1 
ATOM   21162 N N     . SER A 1 4578 ? 203.618 148.443 198.738 1.00 90.31  ? 4578 SER A N     1 
ATOM   21163 C CA    . SER A 1 4578 ? 203.144 147.091 198.987 1.00 90.31  ? 4578 SER A CA    1 
ATOM   21164 C C     . SER A 1 4578 ? 202.650 146.478 197.687 1.00 90.31  ? 4578 SER A C     1 
ATOM   21165 O O     . SER A 1 4578 ? 202.213 147.185 196.776 1.00 90.31  ? 4578 SER A O     1 
ATOM   21166 C CB    . SER A 1 4578 ? 202.024 147.063 200.028 1.00 90.31  ? 4578 SER A CB    1 
ATOM   21167 O OG    . SER A 1 4578 ? 201.232 145.899 199.875 1.00 90.31  ? 4578 SER A OG    1 
ATOM   21168 N N     . ASN A 1 4579 ? 202.720 145.148 197.614 1.00 92.32  ? 4579 ASN A N     1 
ATOM   21169 C CA    . ASN A 1 4579 ? 202.228 144.440 196.439 1.00 92.32  ? 4579 ASN A CA    1 
ATOM   21170 C C     . ASN A 1 4579 ? 200.710 144.360 196.418 1.00 92.32  ? 4579 ASN A C     1 
ATOM   21171 O O     . ASN A 1 4579 ? 200.105 144.438 195.344 1.00 92.32  ? 4579 ASN A O     1 
ATOM   21172 C CB    . ASN A 1 4579 ? 202.817 143.031 196.387 1.00 92.32  ? 4579 ASN A CB    1 
ATOM   21173 C CG    . ASN A 1 4579 ? 204.316 143.036 196.220 1.00 92.32  ? 4579 ASN A CG    1 
ATOM   21174 O OD1   . ASN A 1 4579 ? 204.839 143.512 195.213 1.00 92.32  ? 4579 ASN A OD1   1 
ATOM   21175 N ND2   . ASN A 1 4579 ? 205.022 142.510 197.213 1.00 92.32  ? 4579 ASN A ND2   1 
ATOM   21176 N N     . ALA A 1 4580 ? 200.086 144.201 197.580 1.00 91.64  ? 4580 ALA A N     1 
ATOM   21177 C CA    . ALA A 1 4580 ? 198.639 144.074 197.640 1.00 91.64  ? 4580 ALA A CA    1 
ATOM   21178 C C     . ALA A 1 4580 ? 197.972 145.361 197.178 1.00 91.64  ? 4580 ALA A C     1 
ATOM   21179 O O     . ALA A 1 4580 ? 198.382 146.462 197.553 1.00 91.64  ? 4580 ALA A O     1 
ATOM   21180 C CB    . ALA A 1 4580 ? 198.193 143.729 199.060 1.00 91.64  ? 4580 ALA A CB    1 
ATOM   21181 N N     . ILE A 1 4581 ? 196.939 145.215 196.363 1.00 89.47  ? 4581 ILE A N     1 
ATOM   21182 C CA    . ILE A 1 4581 ? 196.223 146.347 195.812 1.00 89.47  ? 4581 ILE A CA    1 
ATOM   21183 C C     . ILE A 1 4581 ? 195.021 146.643 196.695 1.00 89.47  ? 4581 ILE A C     1 
ATOM   21184 O O     . ILE A 1 4581 ? 194.576 145.809 197.488 1.00 89.47  ? 4581 ILE A O     1 
ATOM   21185 C CB    . ILE A 1 4581 ? 195.782 146.080 194.360 1.00 89.47  ? 4581 ILE A CB    1 
ATOM   21186 C CG1   . ILE A 1 4581 ? 195.119 144.707 194.271 1.00 89.47  ? 4581 ILE A CG1   1 
ATOM   21187 C CG2   . ILE A 1 4581 ? 196.966 146.164 193.422 1.00 89.47  ? 4581 ILE A CG2   1 
ATOM   21188 C CD1   . ILE A 1 4581 ? 194.736 144.306 192.876 1.00 89.47  ? 4581 ILE A CD1   1 
ATOM   21189 N N     . SER A 1 4582 ? 194.490 147.856 196.557 1.00 88.07  ? 4582 SER A N     1 
ATOM   21190 C CA    . SER A 1 4582 ? 193.244 148.261 197.204 1.00 88.07  ? 4582 SER A CA    1 
ATOM   21191 C C     . SER A 1 4582 ? 193.337 148.141 198.726 1.00 88.07  ? 4582 SER A C     1 
ATOM   21192 O O     . SER A 1 4582 ? 192.568 147.426 199.370 1.00 88.07  ? 4582 SER A O     1 
ATOM   21193 C CB    . SER A 1 4582 ? 192.061 147.452 196.661 1.00 88.07  ? 4582 SER A CB    1 
ATOM   21194 O OG    . SER A 1 4582 ? 190.843 147.870 197.251 1.00 88.07  ? 4582 SER A OG    1 
ATOM   21195 N N     . THR A 1 4583 ? 194.297 148.860 199.296 1.00 85.71  ? 4583 THR A N     1 
ATOM   21196 C CA    . THR A 1 4583 ? 194.414 148.956 200.746 1.00 85.71  ? 4583 THR A CA    1 
ATOM   21197 C C     . THR A 1 4583 ? 193.458 150.037 201.230 1.00 85.71  ? 4583 THR A C     1 
ATOM   21198 O O     . THR A 1 4583 ? 193.738 151.230 201.090 1.00 85.71  ? 4583 THR A O     1 
ATOM   21199 C CB    . THR A 1 4583 ? 195.850 149.267 201.153 1.00 85.71  ? 4583 THR A CB    1 
ATOM   21200 O OG1   . THR A 1 4583 ? 196.707 148.202 200.726 1.00 85.71  ? 4583 THR A OG1   1 
ATOM   21201 C CG2   . THR A 1 4583 ? 195.953 149.418 202.662 1.00 85.71  ? 4583 THR A CG2   1 
ATOM   21202 N N     . ALA A 1 4584 ? 192.325 149.624 201.790 1.00 84.69  ? 4584 ALA A N     1 
ATOM   21203 C CA    . ALA A 1 4584 ? 191.297 150.577 202.180 1.00 84.69  ? 4584 ALA A CA    1 
ATOM   21204 C C     . ALA A 1 4584 ? 191.761 151.430 203.351 1.00 84.69  ? 4584 ALA A C     1 
ATOM   21205 O O     . ALA A 1 4584 ? 192.353 150.931 204.310 1.00 84.69  ? 4584 ALA A O     1 
ATOM   21206 C CB    . ALA A 1 4584 ? 190.007 149.845 202.545 1.00 84.69  ? 4584 ALA A CB    1 
ATOM   21207 N N     . LEU A 1 4585 ? 191.496 152.720 203.266 1.00 84.26  ? 4585 LEU A N     1 
ATOM   21208 C CA    . LEU A 1 4585 ? 191.781 153.601 204.390 1.00 84.26  ? 4585 LEU A CA    1 
ATOM   21209 C C     . LEU A 1 4585 ? 190.662 153.507 205.415 1.00 84.26  ? 4585 LEU A C     1 
ATOM   21210 O O     . LEU A 1 4585 ? 189.488 153.628 205.049 1.00 84.26  ? 4585 LEU A O     1 
ATOM   21211 C CB    . LEU A 1 4585 ? 191.936 155.043 203.937 1.00 84.26  ? 4585 LEU A CB    1 
ATOM   21212 C CG    . LEU A 1 4585 ? 193.182 155.376 203.118 1.00 84.26  ? 4585 LEU A CG    1 
ATOM   21213 C CD1   . LEU A 1 4585 ? 194.385 154.652 203.690 1.00 84.26  ? 4585 LEU A CD1   1 
ATOM   21214 C CD2   . LEU A 1 4585 ? 192.998 155.056 201.648 1.00 84.26  ? 4585 LEU A CD2   1 
ATOM   21215 N N     . PRO A 1 4586 ? 190.982 153.281 206.686 1.00 101.08 ? 4586 PRO A N     1 
ATOM   21216 C CA    . PRO A 1 4586 ? 189.937 153.201 207.715 1.00 101.08 ? 4586 PRO A CA    1 
ATOM   21217 C C     . PRO A 1 4586 ? 189.081 154.454 207.776 1.00 101.08 ? 4586 PRO A C     1 
ATOM   21218 O O     . PRO A 1 4586 ? 187.858 154.391 207.629 1.00 101.08 ? 4586 PRO A O     1 
ATOM   21219 C CB    . PRO A 1 4586 ? 190.737 153.008 209.009 1.00 101.08 ? 4586 PRO A CB    1 
ATOM   21220 C CG    . PRO A 1 4586 ? 192.039 152.432 208.570 1.00 101.08 ? 4586 PRO A CG    1 
ATOM   21221 C CD    . PRO A 1 4586 ? 192.326 153.040 207.235 1.00 101.08 ? 4586 PRO A CD    1 
ATOM   21222 N N     . LEU A 1 4587 ? 189.720 155.600 207.991 1.00 97.18  ? 4587 LEU A N     1 
ATOM   21223 C CA    . LEU A 1 4587 ? 189.024 156.878 208.022 1.00 97.18  ? 4587 LEU A CA    1 
ATOM   21224 C C     . LEU A 1 4587 ? 190.010 157.974 207.660 1.00 97.18  ? 4587 LEU A C     1 
ATOM   21225 O O     . LEU A 1 4587 ? 191.083 158.068 208.262 1.00 97.18  ? 4587 LEU A O     1 
ATOM   21226 C CB    . LEU A 1 4587 ? 188.413 157.153 209.396 1.00 97.18  ? 4587 LEU A CB    1 
ATOM   21227 C CG    . LEU A 1 4587 ? 187.885 158.575 209.569 1.00 97.18  ? 4587 LEU A CG    1 
ATOM   21228 C CD1   . LEU A 1 4587 ? 186.599 158.756 208.793 1.00 97.18  ? 4587 LEU A CD1   1 
ATOM   21229 C CD2   . LEU A 1 4587 ? 187.679 158.899 211.037 1.00 97.18  ? 4587 LEU A CD2   1 
ATOM   21230 N N     . THR A 1 4588 ? 189.643 158.795 206.686 1.00 91.37  ? 4588 THR A N     1 
ATOM   21231 C CA    . THR A 1 4588 ? 190.502 159.866 206.205 1.00 91.37  ? 4588 THR A CA    1 
ATOM   21232 C C     . THR A 1 4588 ? 190.076 161.183 206.836 1.00 91.37  ? 4588 THR A C     1 
ATOM   21233 O O     . THR A 1 4588 ? 188.905 161.567 206.754 1.00 91.37  ? 4588 THR A O     1 
ATOM   21234 C CB    . THR A 1 4588 ? 190.442 159.962 204.682 1.00 91.37  ? 4588 THR A CB    1 
ATOM   21235 O OG1   . THR A 1 4588 ? 190.386 158.644 204.126 1.00 91.37  ? 4588 THR A OG1   1 
ATOM   21236 C CG2   . THR A 1 4588 ? 191.667 160.670 204.150 1.00 91.37  ? 4588 THR A CG2   1 
ATOM   21237 N N     . GLN A 1 4589 ? 191.023 161.864 207.470 1.00 90.94  ? 4589 GLN A N     1 
ATOM   21238 C CA    . GLN A 1 4589 ? 190.770 163.144 208.114 1.00 90.94  ? 4589 GLN A CA    1 
ATOM   21239 C C     . GLN A 1 4589 ? 191.287 164.256 207.214 1.00 90.94  ? 4589 GLN A C     1 
ATOM   21240 O O     . GLN A 1 4589 ? 192.478 164.293 206.891 1.00 90.94  ? 4589 GLN A O     1 
ATOM   21241 C CB    . GLN A 1 4589 ? 191.445 163.207 209.483 1.00 90.94  ? 4589 GLN A CB    1 
ATOM   21242 C CG    . GLN A 1 4589 ? 190.770 162.369 210.549 1.00 90.94  ? 4589 GLN A CG    1 
ATOM   21243 C CD    . GLN A 1 4589 ? 190.883 162.985 211.925 1.00 90.94  ? 4589 GLN A CD    1 
ATOM   21244 O OE1   . GLN A 1 4589 ? 191.814 163.738 212.205 1.00 90.94  ? 4589 GLN A OE1   1 
ATOM   21245 N NE2   . GLN A 1 4589 ? 189.936 162.664 212.796 1.00 90.94  ? 4589 GLN A NE2   1 
ATOM   21246 N N     . LEU A 1 4590 ? 190.395 165.152 206.808 1.00 83.87  ? 4590 LEU A N     1 
ATOM   21247 C CA    . LEU A 1 4590 ? 190.755 166.311 206.001 1.00 83.87  ? 4590 LEU A CA    1 
ATOM   21248 C C     . LEU A 1 4590 ? 190.870 167.519 206.919 1.00 83.87  ? 4590 LEU A C     1 
ATOM   21249 O O     . LEU A 1 4590 ? 189.860 168.034 207.406 1.00 83.87  ? 4590 LEU A O     1 
ATOM   21250 C CB    . LEU A 1 4590 ? 189.722 166.559 204.907 1.00 83.87  ? 4590 LEU A CB    1 
ATOM   21251 C CG    . LEU A 1 4590 ? 189.537 165.428 203.905 1.00 83.87  ? 4590 LEU A CG    1 
ATOM   21252 C CD1   . LEU A 1 4590 ? 188.695 165.900 202.742 1.00 83.87  ? 4590 LEU A CD1   1 
ATOM   21253 C CD2   . LEU A 1 4590 ? 190.886 164.938 203.427 1.00 83.87  ? 4590 LEU A CD2   1 
ATOM   21254 N N     . ARG A 1 4591 ? 192.096 167.966 207.156 1.00 91.04  ? 4591 ARG A N     1 
ATOM   21255 C CA    . ARG A 1 4591 ? 192.355 169.155 207.954 1.00 91.04  ? 4591 ARG A CA    1 
ATOM   21256 C C     . ARG A 1 4591 ? 192.862 170.256 207.039 1.00 91.04  ? 4591 ARG A C     1 
ATOM   21257 O O     . ARG A 1 4591 ? 193.918 170.111 206.417 1.00 91.04  ? 4591 ARG A O     1 
ATOM   21258 C CB    . ARG A 1 4591 ? 193.369 168.869 209.059 1.00 91.04  ? 4591 ARG A CB    1 
ATOM   21259 C CG    . ARG A 1 4591 ? 193.755 170.098 209.864 1.00 91.04  ? 4591 ARG A CG    1 
ATOM   21260 C CD    . ARG A 1 4591 ? 194.632 169.735 211.048 1.00 91.04  ? 4591 ARG A CD    1 
ATOM   21261 N NE    . ARG A 1 4591 ? 193.981 168.755 211.908 1.00 91.04  ? 4591 ARG A NE    1 
ATOM   21262 C CZ    . ARG A 1 4591 ? 194.374 167.496 212.039 1.00 91.04  ? 4591 ARG A CZ    1 
ATOM   21263 N NH1   . ARG A 1 4591 ? 195.424 167.029 211.386 1.00 91.04  ? 4591 ARG A NH1   1 
ATOM   21264 N NH2   . ARG A 1 4591 ? 193.693 166.685 212.843 1.00 91.04  ? 4591 ARG A NH2   1 
ATOM   21265 N N     . TRP A 1 4592 ? 192.114 171.350 206.960 1.00 81.88  ? 4592 TRP A N     1 
ATOM   21266 C CA    . TRP A 1 4592 ? 192.529 172.516 206.192 1.00 81.88  ? 4592 TRP A CA    1 
ATOM   21267 C C     . TRP A 1 4592 ? 193.345 173.417 207.107 1.00 81.88  ? 4592 TRP A C     1 
ATOM   21268 O O     . TRP A 1 4592 ? 192.790 174.096 207.975 1.00 81.88  ? 4592 TRP A O     1 
ATOM   21269 C CB    . TRP A 1 4592 ? 191.321 173.255 205.629 1.00 81.88  ? 4592 TRP A CB    1 
ATOM   21270 C CG    . TRP A 1 4592 ? 190.715 172.598 204.443 1.00 81.88  ? 4592 TRP A CG    1 
ATOM   21271 C CD1   . TRP A 1 4592 ? 189.602 171.821 204.424 1.00 81.88  ? 4592 TRP A CD1   1 
ATOM   21272 C CD2   . TRP A 1 4592 ? 191.188 172.658 203.095 1.00 81.88  ? 4592 TRP A CD2   1 
ATOM   21273 N NE1   . TRP A 1 4592 ? 189.346 171.392 203.146 1.00 81.88  ? 4592 TRP A NE1   1 
ATOM   21274 C CE2   . TRP A 1 4592 ? 190.308 171.893 202.311 1.00 81.88  ? 4592 TRP A CE2   1 
ATOM   21275 C CE3   . TRP A 1 4592 ? 192.270 173.285 202.475 1.00 81.88  ? 4592 TRP A CE3   1 
ATOM   21276 C CZ2   . TRP A 1 4592 ? 190.475 171.737 200.942 1.00 81.88  ? 4592 TRP A CZ2   1 
ATOM   21277 C CZ3   . TRP A 1 4592 ? 192.433 173.130 201.115 1.00 81.88  ? 4592 TRP A CZ3   1 
ATOM   21278 C CH2   . TRP A 1 4592 ? 191.541 172.362 200.363 1.00 81.88  ? 4592 TRP A CH2   1 
ATOM   21279 N N     . VAL A 1 4593 ? 194.657 173.424 206.918 1.00 84.21  ? 4593 VAL A N     1 
ATOM   21280 C CA    . VAL A 1 4593 ? 195.552 174.208 207.755 1.00 84.21  ? 4593 VAL A CA    1 
ATOM   21281 C C     . VAL A 1 4593 ? 195.969 175.455 206.993 1.00 84.21  ? 4593 VAL A C     1 
ATOM   21282 O O     . VAL A 1 4593 ? 196.049 175.462 205.759 1.00 84.21  ? 4593 VAL A O     1 
ATOM   21283 C CB    . VAL A 1 4593 ? 196.783 173.391 208.199 1.00 84.21  ? 4593 VAL A CB    1 
ATOM   21284 C CG1   . VAL A 1 4593 ? 197.795 173.285 207.076 1.00 84.21  ? 4593 VAL A CG1   1 
ATOM   21285 C CG2   . VAL A 1 4593 ? 197.414 174.011 209.433 1.00 84.21  ? 4593 VAL A CG2   1 
ATOM   21286 N N     . LYS A 1 4594 ? 196.206 176.528 207.741 1.00 95.55  ? 4594 LYS A N     1 
ATOM   21287 C CA    . LYS A 1 4594 ? 196.698 177.762 207.147 1.00 95.55  ? 4594 LYS A CA    1 
ATOM   21288 C C     . LYS A 1 4594 ? 198.045 177.513 206.485 1.00 95.55  ? 4594 LYS A C     1 
ATOM   21289 O O     . LYS A 1 4594 ? 198.904 176.826 207.043 1.00 95.55  ? 4594 LYS A O     1 
ATOM   21290 C CB    . LYS A 1 4594 ? 196.817 178.848 208.215 1.00 95.55  ? 4594 LYS A CB    1 
ATOM   21291 C CG    . LYS A 1 4594 ? 197.696 180.018 207.818 1.00 95.55  ? 4594 LYS A CG    1 
ATOM   21292 C CD    . LYS A 1 4594 ? 197.344 181.277 208.592 1.00 95.55  ? 4594 LYS A CD    1 
ATOM   21293 C CE    . LYS A 1 4594 ? 196.175 182.009 207.962 1.00 95.55  ? 4594 LYS A CE    1 
ATOM   21294 N NZ    . LYS A 1 4594 ? 195.990 183.356 208.565 1.00 95.55  ? 4594 LYS A NZ    1 
ATOM   21295 N N     . GLN A 1 4595 ? 198.222 178.058 205.284 1.00 105.29 ? 4595 GLN A N     1 
ATOM   21296 C CA    . GLN A 1 4595 ? 199.466 177.856 204.557 1.00 105.29 ? 4595 GLN A CA    1 
ATOM   21297 C C     . GLN A 1 4595 ? 200.636 178.463 205.319 1.00 105.29 ? 4595 GLN A C     1 
ATOM   21298 O O     . GLN A 1 4595 ? 200.599 179.631 205.714 1.00 105.29 ? 4595 GLN A O     1 
ATOM   21299 C CB    . GLN A 1 4595 ? 199.368 178.471 203.162 1.00 105.29 ? 4595 GLN A CB    1 
ATOM   21300 C CG    . GLN A 1 4595 ? 200.593 178.237 202.304 1.00 105.29 ? 4595 GLN A CG    1 
ATOM   21301 C CD    . GLN A 1 4595 ? 201.234 176.893 202.568 1.00 105.29 ? 4595 GLN A CD    1 
ATOM   21302 O OE1   . GLN A 1 4595 ? 202.303 176.812 203.172 1.00 105.29 ? 4595 GLN A OE1   1 
ATOM   21303 N NE2   . GLN A 1 4595 ? 200.582 175.828 202.121 1.00 105.29 ? 4595 GLN A NE2   1 
ATOM   21304 N N     . THR A 1 4596 ? 201.681 177.661 205.518 1.00 119.19 ? 4596 THR A N     1 
ATOM   21305 C CA    . THR A 1 4596 ? 202.876 178.085 206.233 1.00 119.19 ? 4596 THR A CA    1 
ATOM   21306 C C     . THR A 1 4596 ? 204.054 178.334 205.299 1.00 119.19 ? 4596 THR A C     1 
ATOM   21307 O O     . THR A 1 4596 ? 205.205 178.204 205.729 1.00 119.19 ? 4596 THR A O     1 
ATOM   21308 C CB    . THR A 1 4596 ? 203.258 177.051 207.291 1.00 119.19 ? 4596 THR A CB    1 
ATOM   21309 O OG1   . THR A 1 4596 ? 204.037 176.012 206.687 1.00 119.19 ? 4596 THR A OG1   1 
ATOM   21310 C CG2   . THR A 1 4596 ? 202.015 176.442 207.913 1.00 119.19 ? 4596 THR A CG2   1 
ATOM   21311 N N     . ASN A 1 4597 ? 203.778 178.618 204.021 1.00 124.95 ? 4597 ASN A N     1 
ATOM   21312 C CA    . ASN A 1 4597 ? 204.721 179.045 202.983 1.00 124.95 ? 4597 ASN A CA    1 
ATOM   21313 C C     . ASN A 1 4597 ? 206.104 178.422 203.139 1.00 124.95 ? 4597 ASN A C     1 
ATOM   21314 O O     . ASN A 1 4597 ? 207.114 179.132 203.151 1.00 124.95 ? 4597 ASN A O     1 
ATOM   21315 C CB    . ASN A 1 4597 ? 204.821 180.580 202.903 1.00 124.95 ? 4597 ASN A CB    1 
ATOM   21316 C CG    . ASN A 1 4597 ? 205.195 181.251 204.223 1.00 124.95 ? 4597 ASN A CG    1 
ATOM   21317 O OD1   . ASN A 1 4597 ? 205.711 180.629 205.144 1.00 124.95 ? 4597 ASN A OD1   1 
ATOM   21318 N ND2   . ASN A 1 4597 ? 204.927 182.548 204.307 1.00 124.95 ? 4597 ASN A ND2   1 
ATOM   21319 N N     . THR A 1 4598 ? 206.158 177.099 203.251 1.00 127.94 ? 4598 THR A N     1 
ATOM   21320 C CA    . THR A 1 4598 ? 207.407 176.377 203.428 1.00 127.94 ? 4598 THR A CA    1 
ATOM   21321 C C     . THR A 1 4598 ? 207.531 175.327 202.335 1.00 127.94 ? 4598 THR A C     1 
ATOM   21322 O O     . THR A 1 4598 ? 206.528 174.821 201.823 1.00 127.94 ? 4598 THR A O     1 
ATOM   21323 C CB    . THR A 1 4598 ? 207.487 175.713 204.814 1.00 127.94 ? 4598 THR A CB    1 
ATOM   21324 O OG1   . THR A 1 4598 ? 207.011 176.625 205.810 1.00 127.94 ? 4598 THR A OG1   1 
ATOM   21325 C CG2   . THR A 1 4598 ? 208.921 175.328 205.146 1.00 127.94 ? 4598 THR A CG2   1 
ATOM   21326 N N     . GLU A 1 4599 ? 208.770 175.011 201.974 1.00 130.49 ? 4599 GLU A N     1 
ATOM   21327 C CA    . GLU A 1 4599 ? 209.015 174.079 200.883 1.00 130.49 ? 4599 GLU A CA    1 
ATOM   21328 C C     . GLU A 1 4599 ? 208.602 172.666 201.277 1.00 130.49 ? 4599 GLU A C     1 
ATOM   21329 O O     . GLU A 1 4599 ? 208.971 172.171 202.346 1.00 130.49 ? 4599 GLU A O     1 
ATOM   21330 C CB    . GLU A 1 4599 ? 210.488 174.106 200.482 1.00 130.49 ? 4599 GLU A CB    1 
ATOM   21331 C CG    . GLU A 1 4599 ? 210.868 173.043 199.465 1.00 130.49 ? 4599 GLU A CG    1 
ATOM   21332 C CD    . GLU A 1 4599 ? 210.011 173.101 198.213 1.00 130.49 ? 4599 GLU A CD    1 
ATOM   21333 O OE1   . GLU A 1 4599 ? 209.753 174.217 197.717 1.00 130.49 ? 4599 GLU A OE1   1 
ATOM   21334 O OE2   . GLU A 1 4599 ? 209.593 172.029 197.725 1.00 130.49 ? 4599 GLU A OE2   1 
ATOM   21335 N N     . LYS A 1 4600 ? 207.831 172.024 200.404 1.00 120.71 ? 4600 LYS A N     1 
ATOM   21336 C CA    . LYS A 1 4600 ? 207.493 170.618 200.576 1.00 120.71 ? 4600 LYS A CA    1 
ATOM   21337 C C     . LYS A 1 4600 ? 208.759 169.771 200.580 1.00 120.71 ? 4600 LYS A C     1 
ATOM   21338 O O     . LYS A 1 4600 ? 209.565 169.830 199.647 1.00 120.71 ? 4600 LYS A O     1 
ATOM   21339 C CB    . LYS A 1 4600 ? 206.540 170.192 199.456 1.00 120.71 ? 4600 LYS A CB    1 
ATOM   21340 C CG    . LYS A 1 4600 ? 206.673 168.766 198.950 1.00 120.71 ? 4600 LYS A CG    1 
ATOM   21341 C CD    . LYS A 1 4600 ? 205.550 168.463 197.963 1.00 120.71 ? 4600 LYS A CD    1 
ATOM   21342 C CE    . LYS A 1 4600 ? 205.819 167.210 197.144 1.00 120.71 ? 4600 LYS A CE    1 
ATOM   21343 N NZ    . LYS A 1 4600 ? 206.408 166.105 197.937 1.00 120.71 ? 4600 LYS A NZ    1 
ATOM   21344 N N     . LYS A 1 4601 ? 208.942 168.995 201.643 1.00 118.74 ? 4601 LYS A N     1 
ATOM   21345 C CA    . LYS A 1 4601 ? 210.169 168.235 201.805 1.00 118.74 ? 4601 LYS A CA    1 
ATOM   21346 C C     . LYS A 1 4601 ? 210.194 167.037 200.860 1.00 118.74 ? 4601 LYS A C     1 
ATOM   21347 O O     . LYS A 1 4601 ? 209.158 166.536 200.415 1.00 118.74 ? 4601 LYS A O     1 
ATOM   21348 C CB    . LYS A 1 4601 ? 210.335 167.774 203.252 1.00 118.74 ? 4601 LYS A CB    1 
ATOM   21349 C CG    . LYS A 1 4601 ? 209.078 167.217 203.878 1.00 118.74 ? 4601 LYS A CG    1 
ATOM   21350 C CD    . LYS A 1 4601 ? 209.272 166.996 205.366 1.00 118.74 ? 4601 LYS A CD    1 
ATOM   21351 C CE    . LYS A 1 4601 ? 210.500 166.145 205.634 1.00 118.74 ? 4601 LYS A CE    1 
ATOM   21352 N NZ    . LYS A 1 4601 ? 210.514 165.607 207.020 1.00 118.74 ? 4601 LYS A NZ    1 
ATOM   21353 N N     . ALA A 1 4602 ? 211.409 166.574 200.562 1.00 120.76 ? 4602 ALA A N     1 
ATOM   21354 C CA    . ALA A 1 4602 ? 211.610 165.534 199.561 1.00 120.76 ? 4602 ALA A CA    1 
ATOM   21355 C C     . ALA A 1 4602 ? 211.115 164.164 200.005 1.00 120.76 ? 4602 ALA A C     1 
ATOM   21356 O O     . ALA A 1 4602 ? 211.049 163.254 199.172 1.00 120.76 ? 4602 ALA A O     1 
ATOM   21357 C CB    . ALA A 1 4602 ? 213.092 165.448 199.191 1.00 120.76 ? 4602 ALA A CB    1 
ATOM   21358 N N     . SER A 1 4603 ? 210.767 163.986 201.276 1.00 107.60 ? 4603 SER A N     1 
ATOM   21359 C CA    . SER A 1 4603 ? 210.333 162.692 201.778 1.00 107.60 ? 4603 SER A CA    1 
ATOM   21360 C C     . SER A 1 4603 ? 208.825 162.506 201.698 1.00 107.60 ? 4603 SER A C     1 
ATOM   21361 O O     . SER A 1 4603 ? 208.312 161.488 202.173 1.00 107.60 ? 4603 SER A O     1 
ATOM   21362 C CB    . SER A 1 4603 ? 210.801 162.499 203.219 1.00 107.60 ? 4603 SER A CB    1 
ATOM   21363 O OG    . SER A 1 4603 ? 210.243 163.486 204.065 1.00 107.60 ? 4603 SER A OG    1 
ATOM   21364 N N     . VAL A 1 4604 ? 208.104 163.459 201.116 1.00 99.81  ? 4604 VAL A N     1 
ATOM   21365 C CA    . VAL A 1 4604 ? 206.658 163.358 200.974 1.00 99.81  ? 4604 VAL A CA    1 
ATOM   21366 C C     . VAL A 1 4604 ? 206.307 163.422 199.496 1.00 99.81  ? 4604 VAL A C     1 
ATOM   21367 O O     . VAL A 1 4604 ? 207.058 163.968 198.682 1.00 99.81  ? 4604 VAL A O     1 
ATOM   21368 C CB    . VAL A 1 4604 ? 205.917 164.456 201.766 1.00 99.81  ? 4604 VAL A CB    1 
ATOM   21369 C CG1   . VAL A 1 4604 ? 206.463 164.545 203.173 1.00 99.81  ? 4604 VAL A CG1   1 
ATOM   21370 C CG2   . VAL A 1 4604 ? 206.038 165.793 201.071 1.00 99.81  ? 4604 VAL A CG2   1 
ATOM   21371 N N     . VAL A 1 4605 ? 205.154 162.849 199.151 1.00 83.55  ? 4605 VAL A N     1 
ATOM   21372 C CA    . VAL A 1 4605 ? 204.711 162.749 197.769 1.00 83.55  ? 4605 VAL A CA    1 
ATOM   21373 C C     . VAL A 1 4605 ? 203.313 163.332 197.651 1.00 83.55  ? 4605 VAL A C     1 
ATOM   21374 O O     . VAL A 1 4605 ? 202.578 163.459 198.633 1.00 83.55  ? 4605 VAL A O     1 
ATOM   21375 C CB    . VAL A 1 4605 ? 204.712 161.297 197.255 1.00 83.55  ? 4605 VAL A CB    1 
ATOM   21376 C CG1   . VAL A 1 4605 ? 206.108 160.733 197.278 1.00 83.55  ? 4605 VAL A CG1   1 
ATOM   21377 C CG2   . VAL A 1 4605 ? 203.781 160.452 198.090 1.00 83.55  ? 4605 VAL A CG2   1 
ATOM   21378 N N     . THR A 1 4606 ? 202.950 163.682 196.424 1.00 76.65  ? 4606 THR A N     1 
ATOM   21379 C CA    . THR A 1 4606 ? 201.631 164.214 196.107 1.00 76.65  ? 4606 THR A CA    1 
ATOM   21380 C C     . THR A 1 4606 ? 200.895 163.161 195.289 1.00 76.65  ? 4606 THR A C     1 
ATOM   21381 O O     . THR A 1 4606 ? 201.218 162.931 194.121 1.00 76.65  ? 4606 THR A O     1 
ATOM   21382 C CB    . THR A 1 4606 ? 201.739 165.531 195.353 1.00 76.65  ? 4606 THR A CB    1 
ATOM   21383 O OG1   . THR A 1 4606 ? 202.579 166.430 196.086 1.00 76.65  ? 4606 THR A OG1   1 
ATOM   21384 C CG2   . THR A 1 4606 ? 200.370 166.153 195.191 1.00 76.65  ? 4606 THR A CG2   1 
ATOM   21385 N N     . LEU A 1 4607 ? 199.912 162.531 195.901 1.00 71.09  ? 4607 LEU A N     1 
ATOM   21386 C CA    . LEU A 1 4607 ? 199.203 161.420 195.278 1.00 71.09  ? 4607 LEU A CA    1 
ATOM   21387 C C     . LEU A 1 4607 ? 197.896 161.902 194.667 1.00 71.09  ? 4607 LEU A C     1 
ATOM   21388 O O     . LEU A 1 4607 ? 197.173 162.677 195.302 1.00 71.09  ? 4607 LEU A O     1 
ATOM   21389 C CB    . LEU A 1 4607 ? 198.916 160.334 196.296 1.00 71.09  ? 4607 LEU A CB    1 
ATOM   21390 C CG    . LEU A 1 4607 ? 200.116 159.476 196.676 1.00 71.09  ? 4607 LEU A CG    1 
ATOM   21391 C CD1   . LEU A 1 4607 ? 199.651 158.206 197.349 1.00 71.09  ? 4607 LEU A CD1   1 
ATOM   21392 C CD2   . LEU A 1 4607 ? 200.942 159.161 195.447 1.00 71.09  ? 4607 LEU A CD2   1 
ATOM   21393 N N     . PRO A 1 4608 ? 197.562 161.474 193.455 1.00 65.76  ? 4608 PRO A N     1 
ATOM   21394 C CA    . PRO A 1 4608 ? 196.273 161.847 192.874 1.00 65.76  ? 4608 PRO A CA    1 
ATOM   21395 C C     . PRO A 1 4608 ? 195.134 161.107 193.549 1.00 65.76  ? 4608 PRO A C     1 
ATOM   21396 O O     . PRO A 1 4608 ? 195.305 160.009 194.081 1.00 65.76  ? 4608 PRO A O     1 
ATOM   21397 C CB    . PRO A 1 4608 ? 196.413 161.423 191.412 1.00 65.76  ? 4608 PRO A CB    1 
ATOM   21398 C CG    . PRO A 1 4608 ? 197.349 160.275 191.468 1.00 65.76  ? 4608 PRO A CG    1 
ATOM   21399 C CD    . PRO A 1 4608 ? 198.323 160.574 192.576 1.00 65.76  ? 4608 PRO A CD    1 
ATOM   21400 N N     . VAL A 1 4609 ? 193.956 161.718 193.517 1.00 61.46  ? 4609 VAL A N     1 
ATOM   21401 C CA    . VAL A 1 4609 ? 192.744 161.115 194.054 1.00 61.46  ? 4609 VAL A CA    1 
ATOM   21402 C C     . VAL A 1 4609 ? 191.736 161.064 192.917 1.00 61.46  ? 4609 VAL A C     1 
ATOM   21403 O O     . VAL A 1 4609 ? 191.108 162.076 192.587 1.00 61.46  ? 4609 VAL A O     1 
ATOM   21404 C CB    . VAL A 1 4609 ? 192.189 161.887 195.252 1.00 61.46  ? 4609 VAL A CB    1 
ATOM   21405 C CG1   . VAL A 1 4609 ? 190.977 161.178 195.811 1.00 61.46  ? 4609 VAL A CG1   1 
ATOM   21406 C CG2   . VAL A 1 4609 ? 193.249 162.036 196.319 1.00 61.46  ? 4609 VAL A CG2   1 
ATOM   21407 N N     . TYR A 1 4610 ? 191.572 159.892 192.318 1.00 65.66  ? 4610 TYR A N     1 
ATOM   21408 C CA    . TYR A 1 4610 ? 190.626 159.713 191.231 1.00 65.66  ? 4610 TYR A CA    1 
ATOM   21409 C C     . TYR A 1 4610 ? 189.260 159.304 191.772 1.00 65.66  ? 4610 TYR A C     1 
ATOM   21410 O O     . TYR A 1 4610 ? 189.108 158.918 192.932 1.00 65.66  ? 4610 TYR A O     1 
ATOM   21411 C CB    . TYR A 1 4610 ? 191.142 158.673 190.242 1.00 65.66  ? 4610 TYR A CB    1 
ATOM   21412 C CG    . TYR A 1 4610 ? 192.347 159.124 189.460 1.00 65.66  ? 4610 TYR A CG    1 
ATOM   21413 C CD1   . TYR A 1 4610 ? 192.286 160.237 188.642 1.00 65.66  ? 4610 TYR A CD1   1 
ATOM   21414 C CD2   . TYR A 1 4610 ? 193.550 158.448 189.554 1.00 65.66  ? 4610 TYR A CD2   1 
ATOM   21415 C CE1   . TYR A 1 4610 ? 193.383 160.655 187.929 1.00 65.66  ? 4610 TYR A CE1   1 
ATOM   21416 C CE2   . TYR A 1 4610 ? 194.653 158.857 188.846 1.00 65.66  ? 4610 TYR A CE2   1 
ATOM   21417 C CZ    . TYR A 1 4610 ? 194.565 159.962 188.035 1.00 65.66  ? 4610 TYR A CZ    1 
ATOM   21418 O OH    . TYR A 1 4610 ? 195.665 160.378 187.325 1.00 65.66  ? 4610 TYR A OH    1 
ATOM   21419 N N     . LEU A 1 4611 ? 188.254 159.387 190.905 1.00 68.64  ? 4611 LEU A N     1 
ATOM   21420 C CA    . LEU A 1 4611 ? 186.892 159.083 191.325 1.00 68.64  ? 4611 LEU A CA    1 
ATOM   21421 C C     . LEU A 1 4611 ? 186.675 157.581 191.456 1.00 68.64  ? 4611 LEU A C     1 
ATOM   21422 O O     . LEU A 1 4611 ? 186.387 157.076 192.545 1.00 68.64  ? 4611 LEU A O     1 
ATOM   21423 C CB    . LEU A 1 4611 ? 185.891 159.681 190.338 1.00 68.64  ? 4611 LEU A CB    1 
ATOM   21424 C CG    . LEU A 1 4611 ? 184.438 159.627 190.798 1.00 68.64  ? 4611 LEU A CG    1 
ATOM   21425 C CD1   . LEU A 1 4611 ? 184.308 160.225 192.185 1.00 68.64  ? 4611 LEU A CD1   1 
ATOM   21426 C CD2   . LEU A 1 4611 ? 183.542 160.352 189.818 1.00 68.64  ? 4611 LEU A CD2   1 
ATOM   21427 N N     . ASN A 1 4612 ? 186.818 156.852 190.359 1.00 67.07  ? 4612 ASN A N     1 
ATOM   21428 C CA    . ASN A 1 4612 ? 186.582 155.418 190.330 1.00 67.07  ? 4612 ASN A CA    1 
ATOM   21429 C C     . ASN A 1 4612 ? 187.821 154.707 189.802 1.00 67.07  ? 4612 ASN A C     1 
ATOM   21430 O O     . ASN A 1 4612 ? 188.846 155.328 189.519 1.00 67.07  ? 4612 ASN A O     1 
ATOM   21431 C CB    . ASN A 1 4612 ? 185.355 155.095 189.480 1.00 67.07  ? 4612 ASN A CB    1 
ATOM   21432 C CG    . ASN A 1 4612 ? 185.363 155.826 188.164 1.00 67.07  ? 4612 ASN A CG    1 
ATOM   21433 O OD1   . ASN A 1 4612 ? 186.295 155.690 187.376 1.00 67.07  ? 4612 ASN A OD1   1 
ATOM   21434 N ND2   . ASN A 1 4612 ? 184.330 156.620 187.922 1.00 67.07  ? 4612 ASN A ND2   1 
ATOM   21435 N N     . PHE A 1 4613 ? 187.715 153.383 189.667 1.00 68.43  ? 4613 PHE A N     1 
ATOM   21436 C CA    . PHE A 1 4613 ? 188.869 152.592 189.256 1.00 68.43  ? 4613 PHE A CA    1 
ATOM   21437 C C     . PHE A 1 4613 ? 189.367 152.998 187.877 1.00 68.43  ? 4613 PHE A C     1 
ATOM   21438 O O     . PHE A 1 4613 ? 190.559 152.861 187.585 1.00 68.43  ? 4613 PHE A O     1 
ATOM   21439 C CB    . PHE A 1 4613 ? 188.529 151.102 189.281 1.00 68.43  ? 4613 PHE A CB    1 
ATOM   21440 C CG    . PHE A 1 4613 ? 187.588 150.675 188.195 1.00 68.43  ? 4613 PHE A CG    1 
ATOM   21441 C CD1   . PHE A 1 4613 ? 186.224 150.857 188.332 1.00 68.43  ? 4613 PHE A CD1   1 
ATOM   21442 C CD2   . PHE A 1 4613 ? 188.067 150.084 187.041 1.00 68.43  ? 4613 PHE A CD2   1 
ATOM   21443 C CE1   . PHE A 1 4613 ? 185.356 150.462 187.335 1.00 68.43  ? 4613 PHE A CE1   1 
ATOM   21444 C CE2   . PHE A 1 4613 ? 187.204 149.688 186.042 1.00 68.43  ? 4613 PHE A CE2   1 
ATOM   21445 C CZ    . PHE A 1 4613 ? 185.846 149.877 186.189 1.00 68.43  ? 4613 PHE A CZ    1 
ATOM   21446 N N     . THR A 1 4614 ? 188.481 153.491 187.020 1.00 66.70  ? 4614 THR A N     1 
ATOM   21447 C CA    . THR A 1 4614 ? 188.911 154.059 185.749 1.00 66.70  ? 4614 THR A CA    1 
ATOM   21448 C C     . THR A 1 4614 ? 189.461 155.452 186.010 1.00 66.70  ? 4614 THR A C     1 
ATOM   21449 O O     . THR A 1 4614 ? 188.704 156.390 186.279 1.00 66.70  ? 4614 THR A O     1 
ATOM   21450 C CB    . THR A 1 4614 ? 187.751 154.097 184.760 1.00 66.70  ? 4614 THR A CB    1 
ATOM   21451 O OG1   . THR A 1 4614 ? 187.502 152.773 184.273 1.00 66.70  ? 4614 THR A OG1   1 
ATOM   21452 C CG2   . THR A 1 4614 ? 188.085 154.993 183.582 1.00 66.70  ? 4614 THR A CG2   1 
ATOM   21453 N N     . ARG A 1 4615 ? 190.781 155.591 185.950 1.00 70.31  ? 4615 ARG A N     1 
ATOM   21454 C CA    . ARG A 1 4615 ? 191.438 156.847 186.298 1.00 70.31  ? 4615 ARG A CA    1 
ATOM   21455 C C     . ARG A 1 4615 ? 191.183 157.844 185.174 1.00 70.31  ? 4615 ARG A C     1 
ATOM   21456 O O     . ARG A 1 4615 ? 192.026 158.096 184.311 1.00 70.31  ? 4615 ARG A O     1 
ATOM   21457 C CB    . ARG A 1 4615 ? 192.927 156.629 186.520 1.00 70.31  ? 4615 ARG A CB    1 
ATOM   21458 C CG    . ARG A 1 4615 ? 193.286 155.237 187.004 1.00 70.31  ? 4615 ARG A CG    1 
ATOM   21459 C CD    . ARG A 1 4615 ? 193.601 155.224 188.481 1.00 70.31  ? 4615 ARG A CD    1 
ATOM   21460 N NE    . ARG A 1 4615 ? 194.360 154.040 188.854 1.00 70.31  ? 4615 ARG A NE    1 
ATOM   21461 C CZ    . ARG A 1 4615 ? 195.659 154.042 189.115 1.00 70.31  ? 4615 ARG A CZ    1 
ATOM   21462 N NH1   . ARG A 1 4615 ? 196.374 155.152 189.048 1.00 70.31  ? 4615 ARG A NH1   1 
ATOM   21463 N NH2   . ARG A 1 4615 ? 196.256 152.902 189.448 1.00 70.31  ? 4615 ARG A NH2   1 
ATOM   21464 N N     . ALA A 1 4616 ? 189.987 158.415 185.181 1.00 75.00  ? 4616 ALA A N     1 
ATOM   21465 C CA    . ALA A 1 4616 ? 189.599 159.387 184.173 1.00 75.00  ? 4616 ALA A CA    1 
ATOM   21466 C C     . ALA A 1 4616 ? 189.236 160.745 184.742 1.00 75.00  ? 4616 ALA A C     1 
ATOM   21467 O O     . ALA A 1 4616 ? 189.427 161.752 184.059 1.00 75.00  ? 4616 ALA A O     1 
ATOM   21468 C CB    . ALA A 1 4616 ? 188.412 158.864 183.352 1.00 75.00  ? 4616 ALA A CB    1 
ATOM   21469 N N     . ASP A 1 4617 ? 188.724 160.804 185.966 1.00 76.11  ? 4617 ASP A N     1 
ATOM   21470 C CA    . ASP A 1 4617 ? 188.331 162.054 186.595 1.00 76.11  ? 4617 ASP A CA    1 
ATOM   21471 C C     . ASP A 1 4617 ? 189.221 162.302 187.801 1.00 76.11  ? 4617 ASP A C     1 
ATOM   21472 O O     . ASP A 1 4617 ? 189.306 161.456 188.696 1.00 76.11  ? 4617 ASP A O     1 
ATOM   21473 C CB    . ASP A 1 4617 ? 186.867 162.011 187.020 1.00 76.11  ? 4617 ASP A CB    1 
ATOM   21474 C CG    . ASP A 1 4617 ? 185.980 161.400 185.963 1.00 76.11  ? 4617 ASP A CG    1 
ATOM   21475 O OD1   . ASP A 1 4617 ? 185.546 162.135 185.053 1.00 76.11  ? 4617 ASP A OD1   1 
ATOM   21476 O OD2   . ASP A 1 4617 ? 185.729 160.180 186.033 1.00 76.11  ? 4617 ASP A OD2   1 
ATOM   21477 N N     . LEU A 1 4618 ? 189.873 163.457 187.827 1.00 69.01  ? 4618 LEU A N     1 
ATOM   21478 C CA    . LEU A 1 4618 ? 190.746 163.839 188.925 1.00 69.01  ? 4618 LEU A CA    1 
ATOM   21479 C C     . LEU A 1 4618 ? 189.979 164.756 189.864 1.00 69.01  ? 4618 LEU A C     1 
ATOM   21480 O O     . LEU A 1 4618 ? 189.421 165.768 189.429 1.00 69.01  ? 4618 LEU A O     1 
ATOM   21481 C CB    . LEU A 1 4618 ? 192.005 164.532 188.408 1.00 69.01  ? 4618 LEU A CB    1 
ATOM   21482 C CG    . LEU A 1 4618 ? 192.874 165.207 189.466 1.00 69.01  ? 4618 LEU A CG    1 
ATOM   21483 C CD1   . LEU A 1 4618 ? 193.323 164.201 190.504 1.00 69.01  ? 4618 LEU A CD1   1 
ATOM   21484 C CD2   . LEU A 1 4618 ? 194.069 165.873 188.817 1.00 69.01  ? 4618 LEU A CD2   1 
ATOM   21485 N N     . ILE A 1 4619 ? 189.951 164.403 191.145 1.00 68.61  ? 4619 ILE A N     1 
ATOM   21486 C CA    . ILE A 1 4619 ? 189.187 165.169 192.121 1.00 68.61  ? 4619 ILE A CA    1 
ATOM   21487 C C     . ILE A 1 4619 ? 190.098 166.180 192.797 1.00 68.61  ? 4619 ILE A C     1 
ATOM   21488 O O     . ILE A 1 4619 ? 189.883 167.392 192.692 1.00 68.61  ? 4619 ILE A O     1 
ATOM   21489 C CB    . ILE A 1 4619 ? 188.523 164.246 193.156 1.00 68.61  ? 4619 ILE A CB    1 
ATOM   21490 C CG1   . ILE A 1 4619 ? 187.711 163.161 192.453 1.00 68.61  ? 4619 ILE A CG1   1 
ATOM   21491 C CG2   . ILE A 1 4619 ? 187.627 165.045 194.074 1.00 68.61  ? 4619 ILE A CG2   1 
ATOM   21492 C CD1   . ILE A 1 4619 ? 186.767 163.694 191.404 1.00 68.61  ? 4619 ILE A CD1   1 
ATOM   21493 N N     . PHE A 1 4620 ? 191.121 165.693 193.488 1.00 66.73  ? 4620 PHE A N     1 
ATOM   21494 C CA    . PHE A 1 4620 ? 192.077 166.560 194.161 1.00 66.73  ? 4620 PHE A CA    1 
ATOM   21495 C C     . PHE A 1 4620 ? 193.335 165.752 194.443 1.00 66.73  ? 4620 PHE A C     1 
ATOM   21496 O O     . PHE A 1 4620 ? 193.447 164.586 194.057 1.00 66.73  ? 4620 PHE A O     1 
ATOM   21497 C CB    . PHE A 1 4620 ? 191.488 167.158 195.441 1.00 66.73  ? 4620 PHE A CB    1 
ATOM   21498 C CG    . PHE A 1 4620 ? 191.238 166.153 196.529 1.00 66.73  ? 4620 PHE A CG    1 
ATOM   21499 C CD1   . PHE A 1 4620 ? 190.192 165.256 196.435 1.00 66.73  ? 4620 PHE A CD1   1 
ATOM   21500 C CD2   . PHE A 1 4620 ? 192.039 166.118 197.653 1.00 66.73  ? 4620 PHE A CD2   1 
ATOM   21501 C CE1   . PHE A 1 4620 ? 189.958 164.340 197.436 1.00 66.73  ? 4620 PHE A CE1   1 
ATOM   21502 C CE2   . PHE A 1 4620 ? 191.805 165.203 198.656 1.00 66.73  ? 4620 PHE A CE2   1 
ATOM   21503 C CZ    . PHE A 1 4620 ? 190.766 164.314 198.546 1.00 66.73  ? 4620 PHE A CZ    1 
ATOM   21504 N N     . THR A 1 4621 ? 194.290 166.385 195.117 1.00 69.59  ? 4621 THR A N     1 
ATOM   21505 C CA    . THR A 1 4621 ? 195.562 165.759 195.436 1.00 69.59  ? 4621 THR A CA    1 
ATOM   21506 C C     . THR A 1 4621 ? 195.795 165.806 196.938 1.00 69.59  ? 4621 THR A C     1 
ATOM   21507 O O     . THR A 1 4621 ? 195.290 166.689 197.634 1.00 69.59  ? 4621 THR A O     1 
ATOM   21508 C CB    . THR A 1 4621 ? 196.726 166.443 194.717 1.00 69.59  ? 4621 THR A CB    1 
ATOM   21509 O OG1   . THR A 1 4621 ? 197.102 167.623 195.436 1.00 69.59  ? 4621 THR A OG1   1 
ATOM   21510 C CG2   . THR A 1 4621 ? 196.332 166.824 193.304 1.00 69.59  ? 4621 THR A CG2   1 
ATOM   21511 N N     . VAL A 1 4622 ? 196.569 164.844 197.429 1.00 68.59  ? 4622 VAL A N     1 
ATOM   21512 C CA    . VAL A 1 4622 ? 196.892 164.740 198.844 1.00 68.59  ? 4622 VAL A CA    1 
ATOM   21513 C C     . VAL A 1 4622 ? 198.403 164.721 198.995 1.00 68.59  ? 4622 VAL A C     1 
ATOM   21514 O O     . VAL A 1 4622 ? 199.134 164.363 198.066 1.00 68.59  ? 4622 VAL A O     1 
ATOM   21515 C CB    . VAL A 1 4622 ? 196.275 163.482 199.481 1.00 68.59  ? 4622 VAL A CB    1 
ATOM   21516 C CG1   . VAL A 1 4622 ? 194.772 163.559 199.430 1.00 68.59  ? 4622 VAL A CG1   1 
ATOM   21517 C CG2   . VAL A 1 4622 ? 196.763 162.245 198.765 1.00 68.59  ? 4622 VAL A CG2   1 
ATOM   21518 N N     . ASP A 1 4623 ? 198.873 165.109 200.173 1.00 81.32  ? 4623 ASP A N     1 
ATOM   21519 C CA    . ASP A 1 4623 ? 200.295 165.114 200.493 1.00 81.32  ? 4623 ASP A CA    1 
ATOM   21520 C C     . ASP A 1 4623 ? 200.548 164.020 201.519 1.00 81.32  ? 4623 ASP A C     1 
ATOM   21521 O O     . ASP A 1 4623 ? 200.011 164.071 202.630 1.00 81.32  ? 4623 ASP A O     1 
ATOM   21522 C CB    . ASP A 1 4623 ? 200.728 166.478 201.020 1.00 81.32  ? 4623 ASP A CB    1 
ATOM   21523 C CG    . ASP A 1 4623 ? 201.063 167.447 199.910 1.00 81.32  ? 4623 ASP A CG    1 
ATOM   21524 O OD1   . ASP A 1 4623 ? 200.681 167.175 198.753 1.00 81.32  ? 4623 ASP A OD1   1 
ATOM   21525 O OD2   . ASP A 1 4623 ? 201.702 168.482 200.192 1.00 81.32  ? 4623 ASP A OD2   1 
ATOM   21526 N N     . PHE A 1 4624 ? 201.364 163.037 201.154 1.00 85.19  ? 4624 PHE A N     1 
ATOM   21527 C CA    . PHE A 1 4624 ? 201.618 161.879 201.997 1.00 85.19  ? 4624 PHE A CA    1 
ATOM   21528 C C     . PHE A 1 4624 ? 203.111 161.728 202.235 1.00 85.19  ? 4624 PHE A C     1 
ATOM   21529 O O     . PHE A 1 4624 ? 203.901 161.759 201.287 1.00 85.19  ? 4624 PHE A O     1 
ATOM   21530 C CB    . PHE A 1 4624 ? 201.066 160.607 201.355 1.00 85.19  ? 4624 PHE A CB    1 
ATOM   21531 C CG    . PHE A 1 4624 ? 199.699 160.234 201.831 1.00 85.19  ? 4624 PHE A CG    1 
ATOM   21532 C CD1   . PHE A 1 4624 ? 199.418 160.165 203.181 1.00 85.19  ? 4624 PHE A CD1   1 
ATOM   21533 C CD2   . PHE A 1 4624 ? 198.694 159.949 200.928 1.00 85.19  ? 4624 PHE A CD2   1 
ATOM   21534 C CE1   . PHE A 1 4624 ? 198.160 159.820 203.620 1.00 85.19  ? 4624 PHE A CE1   1 
ATOM   21535 C CE2   . PHE A 1 4624 ? 197.434 159.605 201.362 1.00 85.19  ? 4624 PHE A CE2   1 
ATOM   21536 C CZ    . PHE A 1 4624 ? 197.167 159.540 202.710 1.00 85.19  ? 4624 PHE A CZ    1 
ATOM   21537 N N     . GLU A 1 4625 ? 203.494 161.562 203.497 1.00 98.32  ? 4625 GLU A N     1 
ATOM   21538 C CA    . GLU A 1 4625 ? 204.857 161.167 203.812 1.00 98.32  ? 4625 GLU A CA    1 
ATOM   21539 C C     . GLU A 1 4625 ? 205.077 159.713 203.416 1.00 98.32  ? 4625 GLU A C     1 
ATOM   21540 O O     . GLU A 1 4625 ? 204.141 158.913 203.363 1.00 98.32  ? 4625 GLU A O     1 
ATOM   21541 C CB    . GLU A 1 4625 ? 205.142 161.341 205.303 1.00 98.32  ? 4625 GLU A CB    1 
ATOM   21542 C CG    . GLU A 1 4625 ? 204.997 162.759 205.813 1.00 98.32  ? 4625 GLU A CG    1 
ATOM   21543 C CD    . GLU A 1 4625 ? 206.235 163.238 206.544 1.00 98.32  ? 4625 GLU A CD    1 
ATOM   21544 O OE1   . GLU A 1 4625 ? 207.219 162.471 206.611 1.00 98.32  ? 4625 GLU A OE1   1 
ATOM   21545 O OE2   . GLU A 1 4625 ? 206.227 164.381 207.047 1.00 98.32  ? 4625 GLU A OE2   1 
ATOM   21546 N N     . ILE A 1 4626 ? 206.328 159.370 203.135 1.00 99.08  ? 4626 ILE A N     1 
ATOM   21547 C CA    . ILE A 1 4626 ? 206.686 158.003 202.792 1.00 99.08  ? 4626 ILE A CA    1 
ATOM   21548 C C     . ILE A 1 4626 ? 207.739 157.504 203.771 1.00 99.08  ? 4626 ILE A C     1 
ATOM   21549 O O     . ILE A 1 4626 ? 208.388 158.276 204.480 1.00 99.08  ? 4626 ILE A O     1 
ATOM   21550 C CB    . ILE A 1 4626 ? 207.189 157.881 201.342 1.00 99.08  ? 4626 ILE A CB    1 
ATOM   21551 C CG1   . ILE A 1 4626 ? 208.651 158.308 201.251 1.00 99.08  ? 4626 ILE A CG1   1 
ATOM   21552 C CG2   . ILE A 1 4626 ? 206.336 158.720 200.415 1.00 99.08  ? 4626 ILE A CG2   1 
ATOM   21553 C CD1   . ILE A 1 4626 ? 209.134 158.509 199.839 1.00 99.08  ? 4626 ILE A CD1   1 
ATOM   21554 N N     . ALA A 1 4627 ? 207.894 156.184 203.814 1.00 110.44 ? 4627 ALA A N     1 
ATOM   21555 C CA    . ALA A 1 4627 ? 208.951 155.587 204.613 1.00 110.44 ? 4627 ALA A CA    1 
ATOM   21556 C C     . ALA A 1 4627 ? 210.315 155.976 204.055 1.00 110.44 ? 4627 ALA A C     1 
ATOM   21557 O O     . ALA A 1 4627 ? 210.500 156.109 202.843 1.00 110.44 ? 4627 ALA A O     1 
ATOM   21558 C CB    . ALA A 1 4627 ? 208.809 154.067 204.644 1.00 110.44 ? 4627 ALA A CB    1 
ATOM   21559 N N     . THR A 1 4628 ? 211.278 156.159 204.961 1.00 119.62 ? 4628 THR A N     1 
ATOM   21560 C CA    . THR A 1 4628 ? 212.592 156.655 204.567 1.00 119.62 ? 4628 THR A CA    1 
ATOM   21561 C C     . THR A 1 4628 ? 213.303 155.725 203.593 1.00 119.62 ? 4628 THR A C     1 
ATOM   21562 O O     . THR A 1 4628 ? 214.121 156.193 202.795 1.00 119.62 ? 4628 THR A O     1 
ATOM   21563 C CB    . THR A 1 4628 ? 213.466 156.867 205.803 1.00 119.62 ? 4628 THR A CB    1 
ATOM   21564 O OG1   . THR A 1 4628 ? 213.281 155.775 206.713 1.00 119.62 ? 4628 THR A OG1   1 
ATOM   21565 C CG2   . THR A 1 4628 ? 213.096 158.168 206.498 1.00 119.62 ? 4628 THR A CG2   1 
ATOM   21566 N N     . LYS A 1 4629 ? 213.019 154.424 203.643 1.00 119.17 ? 4629 LYS A N     1 
ATOM   21567 C CA    . LYS A 1 4629 ? 213.653 153.502 202.709 1.00 119.17 ? 4629 LYS A CA    1 
ATOM   21568 C C     . LYS A 1 4629 ? 213.208 153.770 201.278 1.00 119.17 ? 4629 LYS A C     1 
ATOM   21569 O O     . LYS A 1 4629 ? 214.025 153.735 200.351 1.00 119.17 ? 4629 LYS A O     1 
ATOM   21570 C CB    . LYS A 1 4629 ? 213.344 152.057 203.101 1.00 119.17 ? 4629 LYS A CB    1 
ATOM   21571 C CG    . LYS A 1 4629 ? 213.395 151.781 204.594 1.00 119.17 ? 4629 LYS A CG    1 
ATOM   21572 C CD    . LYS A 1 4629 ? 214.716 152.225 205.208 1.00 119.17 ? 4629 LYS A CD    1 
ATOM   21573 C CE    . LYS A 1 4629 ? 215.890 151.453 204.625 1.00 119.17 ? 4629 LYS A CE    1 
ATOM   21574 N NZ    . LYS A 1 4629 ? 217.194 152.019 205.067 1.00 119.17 ? 4629 LYS A NZ    1 
ATOM   21575 N N     . GLU A 1 4630 ? 211.924 154.050 201.080 1.00 113.10 ? 4630 GLU A N     1 
ATOM   21576 C CA    . GLU A 1 4630 ? 211.387 154.214 199.741 1.00 113.10 ? 4630 GLU A CA    1 
ATOM   21577 C C     . GLU A 1 4630 ? 211.805 155.555 199.146 1.00 113.10 ? 4630 GLU A C     1 
ATOM   21578 O O     . GLU A 1 4630 ? 212.367 156.425 199.817 1.00 113.10 ? 4630 GLU A O     1 
ATOM   21579 C CB    . GLU A 1 4630 ? 209.866 154.085 199.757 1.00 113.10 ? 4630 GLU A CB    1 
ATOM   21580 C CG    . GLU A 1 4630 ? 209.372 152.687 199.442 1.00 113.10 ? 4630 GLU A CG    1 
ATOM   21581 C CD    . GLU A 1 4630 ? 209.425 151.771 200.641 1.00 113.10 ? 4630 GLU A CD    1 
ATOM   21582 O OE1   . GLU A 1 4630 ? 208.854 152.134 201.690 1.00 113.10 ? 4630 GLU A OE1   1 
ATOM   21583 O OE2   . GLU A 1 4630 ? 210.039 150.689 200.536 1.00 113.10 ? 4630 GLU A OE2   1 
ATOM   21584 N N     . ASP A 1 4631 ? 211.520 155.709 197.859 1.00 95.41  ? 4631 ASP A N     1 
ATOM   21585 C CA    . ASP A 1 4631 ? 211.882 156.877 197.077 1.00 95.41  ? 4631 ASP A CA    1 
ATOM   21586 C C     . ASP A 1 4631 ? 210.673 157.334 196.277 1.00 95.41  ? 4631 ASP A C     1 
ATOM   21587 O O     . ASP A 1 4631 ? 209.961 156.507 195.699 1.00 95.41  ? 4631 ASP A O     1 
ATOM   21588 C CB    . ASP A 1 4631 ? 213.055 156.545 196.142 1.00 95.41  ? 4631 ASP A CB    1 
ATOM   21589 C CG    . ASP A 1 4631 ? 213.182 157.507 194.983 1.00 95.41  ? 4631 ASP A CG    1 
ATOM   21590 O OD1   . ASP A 1 4631 ? 213.299 158.727 195.214 1.00 95.41  ? 4631 ASP A OD1   1 
ATOM   21591 O OD2   . ASP A 1 4631 ? 213.176 157.036 193.829 1.00 95.41  ? 4631 ASP A OD2   1 
ATOM   21592 N N     . PRO A 1 4632 ? 210.406 158.641 196.240 1.00 90.02  ? 4632 PRO A N     1 
ATOM   21593 C CA    . PRO A 1 4632 ? 209.192 159.120 195.559 1.00 90.02  ? 4632 PRO A CA    1 
ATOM   21594 C C     . PRO A 1 4632 ? 209.100 158.725 194.097 1.00 90.02  ? 4632 PRO A C     1 
ATOM   21595 O O     . PRO A 1 4632 ? 207.985 158.555 193.584 1.00 90.02  ? 4632 PRO A O     1 
ATOM   21596 C CB    . PRO A 1 4632 ? 209.278 160.645 195.727 1.00 90.02  ? 4632 PRO A CB    1 
ATOM   21597 C CG    . PRO A 1 4632 ? 210.678 160.920 196.197 1.00 90.02  ? 4632 PRO A CG    1 
ATOM   21598 C CD    . PRO A 1 4632 ? 211.062 159.723 196.986 1.00 90.02  ? 4632 PRO A CD    1 
ATOM   21599 N N     . ARG A 1 4633 ? 210.230 158.577 193.403 1.00 87.35  ? 4633 ARG A N     1 
ATOM   21600 C CA    . ARG A 1 4633 ? 210.174 158.143 192.012 1.00 87.35  ? 4633 ARG A CA    1 
ATOM   21601 C C     . ARG A 1 4633 ? 209.529 156.770 191.900 1.00 87.35  ? 4633 ARG A C     1 
ATOM   21602 O O     . ARG A 1 4633 ? 208.791 156.496 190.946 1.00 87.35  ? 4633 ARG A O     1 
ATOM   21603 C CB    . ARG A 1 4633 ? 211.573 158.121 191.407 1.00 87.35  ? 4633 ARG A CB    1 
ATOM   21604 C CG    . ARG A 1 4633 ? 212.221 159.481 191.279 1.00 87.35  ? 4633 ARG A CG    1 
ATOM   21605 C CD    . ARG A 1 4633 ? 213.720 159.318 191.175 1.00 87.35  ? 4633 ARG A CD    1 
ATOM   21606 N NE    . ARG A 1 4633 ? 214.170 158.173 191.956 1.00 87.35  ? 4633 ARG A NE    1 
ATOM   21607 C CZ    . ARG A 1 4633 ? 215.105 157.319 191.565 1.00 87.35  ? 4633 ARG A CZ    1 
ATOM   21608 N NH1   . ARG A 1 4633 ? 215.720 157.453 190.402 1.00 87.35  ? 4633 ARG A NH1   1 
ATOM   21609 N NH2   . ARG A 1 4633 ? 215.426 156.301 192.358 1.00 87.35  ? 4633 ARG A NH2   1 
ATOM   21610 N N     . SER A 1 4634 ? 209.797 155.893 192.869 1.00 84.42  ? 4634 SER A N     1 
ATOM   21611 C CA    . SER A 1 4634 ? 209.151 154.588 192.880 1.00 84.42  ? 4634 SER A CA    1 
ATOM   21612 C C     . SER A 1 4634 ? 207.641 154.730 192.978 1.00 84.42  ? 4634 SER A C     1 
ATOM   21613 O O     . SER A 1 4634 ? 206.899 154.049 192.264 1.00 84.42  ? 4634 SER A O     1 
ATOM   21614 C CB    . SER A 1 4634 ? 209.686 153.747 194.037 1.00 84.42  ? 4634 SER A CB    1 
ATOM   21615 O OG    . SER A 1 4634 ? 209.385 152.376 193.854 1.00 84.42  ? 4634 SER A OG    1 
ATOM   21616 N N     . PHE A 1 4635 ? 207.167 155.620 193.847 1.00 80.61  ? 4635 PHE A N     1 
ATOM   21617 C CA    . PHE A 1 4635 ? 205.730 155.838 193.951 1.00 80.61  ? 4635 PHE A CA    1 
ATOM   21618 C C     . PHE A 1 4635 ? 205.165 156.382 192.650 1.00 80.61  ? 4635 PHE A C     1 
ATOM   21619 O O     . PHE A 1 4635 ? 204.054 156.020 192.249 1.00 80.61  ? 4635 PHE A O     1 
ATOM   21620 C CB    . PHE A 1 4635 ? 205.424 156.784 195.107 1.00 80.61  ? 4635 PHE A CB    1 
ATOM   21621 C CG    . PHE A 1 4635 ? 205.365 156.106 196.439 1.00 80.61  ? 4635 PHE A CG    1 
ATOM   21622 C CD1   . PHE A 1 4635 ? 206.522 155.730 197.089 1.00 80.61  ? 4635 PHE A CD1   1 
ATOM   21623 C CD2   . PHE A 1 4635 ? 204.151 155.841 197.039 1.00 80.61  ? 4635 PHE A CD2   1 
ATOM   21624 C CE1   . PHE A 1 4635 ? 206.470 155.105 198.313 1.00 80.61  ? 4635 PHE A CE1   1 
ATOM   21625 C CE2   . PHE A 1 4635 ? 204.095 155.217 198.262 1.00 80.61  ? 4635 PHE A CE2   1 
ATOM   21626 C CZ    . PHE A 1 4635 ? 205.255 154.848 198.899 1.00 80.61  ? 4635 PHE A CZ    1 
ATOM   21627 N N     . TYR A 1 4636 ? 205.910 157.258 191.978 1.00 82.23  ? 4636 TYR A N     1 
ATOM   21628 C CA    . TYR A 1 4636 ? 205.422 157.816 190.723 1.00 82.23  ? 4636 TYR A CA    1 
ATOM   21629 C C     . TYR A 1 4636 ? 205.293 156.741 189.652 1.00 82.23  ? 4636 TYR A C     1 
ATOM   21630 O O     . TYR A 1 4636 ? 204.261 156.643 188.980 1.00 82.23  ? 4636 TYR A O     1 
ATOM   21631 C CB    . TYR A 1 4636 ? 206.346 158.934 190.244 1.00 82.23  ? 4636 TYR A CB    1 
ATOM   21632 C CG    . TYR A 1 4636 ? 206.395 160.137 191.153 1.00 82.23  ? 4636 TYR A CG    1 
ATOM   21633 C CD1   . TYR A 1 4636 ? 205.336 160.444 191.992 1.00 82.23  ? 4636 TYR A CD1   1 
ATOM   21634 C CD2   . TYR A 1 4636 ? 207.503 160.968 191.170 1.00 82.23  ? 4636 TYR A CD2   1 
ATOM   21635 C CE1   . TYR A 1 4636 ? 205.384 161.541 192.824 1.00 82.23  ? 4636 TYR A CE1   1 
ATOM   21636 C CE2   . TYR A 1 4636 ? 207.558 162.066 191.996 1.00 82.23  ? 4636 TYR A CE2   1 
ATOM   21637 C CZ    . TYR A 1 4636 ? 206.497 162.350 192.820 1.00 82.23  ? 4636 TYR A CZ    1 
ATOM   21638 O OH    . TYR A 1 4636 ? 206.554 163.448 193.644 1.00 82.23  ? 4636 TYR A OH    1 
ATOM   21639 N N     . GLU A 1 4637 ? 206.325 155.915 189.484 1.00 81.81  ? 4637 GLU A N     1 
ATOM   21640 C CA    . GLU A 1 4637 ? 206.344 154.990 188.358 1.00 81.81  ? 4637 GLU A CA    1 
ATOM   21641 C C     . GLU A 1 4637 ? 205.522 153.731 188.590 1.00 81.81  ? 4637 GLU A C     1 
ATOM   21642 O O     . GLU A 1 4637 ? 205.282 152.990 187.633 1.00 81.81  ? 4637 GLU A O     1 
ATOM   21643 C CB    . GLU A 1 4637 ? 207.780 154.598 188.009 1.00 81.81  ? 4637 GLU A CB    1 
ATOM   21644 C CG    . GLU A 1 4637 ? 208.535 153.896 189.119 1.00 81.81  ? 4637 GLU A CG    1 
ATOM   21645 C CD    . GLU A 1 4637 ? 210.023 154.190 189.083 1.00 81.81  ? 4637 GLU A CD    1 
ATOM   21646 O OE1   . GLU A 1 4637 ? 210.502 154.697 188.048 1.00 81.81  ? 4637 GLU A OE1   1 
ATOM   21647 O OE2   . GLU A 1 4637 ? 210.715 153.915 190.086 1.00 81.81  ? 4637 GLU A OE2   1 
ATOM   21648 N N     . ARG A 1 4638 ? 205.088 153.462 189.817 1.00 73.29  ? 4638 ARG A N     1 
ATOM   21649 C CA    . ARG A 1 4638 ? 204.267 152.293 190.095 1.00 73.29  ? 4638 ARG A CA    1 
ATOM   21650 C C     . ARG A 1 4638 ? 202.778 152.594 190.027 1.00 73.29  ? 4638 ARG A C     1 
ATOM   21651 O O     . ARG A 1 4638 ? 201.966 151.718 190.334 1.00 73.29  ? 4638 ARG A O     1 
ATOM   21652 C CB    . ARG A 1 4638 ? 204.621 151.707 191.463 1.00 73.29  ? 4638 ARG A CB    1 
ATOM   21653 C CG    . ARG A 1 4638 ? 206.025 151.134 191.535 1.00 73.29  ? 4638 ARG A CG    1 
ATOM   21654 C CD    . ARG A 1 4638 ? 206.022 149.671 191.931 1.00 73.29  ? 4638 ARG A CD    1 
ATOM   21655 N NE    . ARG A 1 4638 ? 205.358 149.444 193.207 1.00 73.29  ? 4638 ARG A NE    1 
ATOM   21656 C CZ    . ARG A 1 4638 ? 205.321 148.273 193.827 1.00 73.29  ? 4638 ARG A CZ    1 
ATOM   21657 N NH1   . ARG A 1 4638 ? 205.900 147.201 193.314 1.00 73.29  ? 4638 ARG A NH1   1 
ATOM   21658 N NH2   . ARG A 1 4638 ? 204.687 148.175 194.991 1.00 73.29  ? 4638 ARG A NH2   1 
ATOM   21659 N N     . GLY A 1 4639 ? 202.405 153.808 189.638 1.00 72.38  ? 4639 GLY A N     1 
ATOM   21660 C CA    . GLY A 1 4639 ? 200.999 154.149 189.495 1.00 72.38  ? 4639 GLY A CA    1 
ATOM   21661 C C     . GLY A 1 4639 ? 200.223 154.153 190.792 1.00 72.38  ? 4639 GLY A C     1 
ATOM   21662 O O     . GLY A 1 4639 ? 199.048 153.769 190.812 1.00 72.38  ? 4639 GLY A O     1 
ATOM   21663 N N     . VAL A 1 4640 ? 200.847 154.591 191.876 1.00 69.90  ? 4640 VAL A N     1 
ATOM   21664 C CA    . VAL A 1 4640 ? 200.170 154.662 193.164 1.00 69.90  ? 4640 VAL A CA    1 
ATOM   21665 C C     . VAL A 1 4640 ? 199.181 155.816 193.134 1.00 69.90  ? 4640 VAL A C     1 
ATOM   21666 O O     . VAL A 1 4640 ? 199.531 156.937 192.749 1.00 69.90  ? 4640 VAL A O     1 
ATOM   21667 C CB    . VAL A 1 4640 ? 201.186 154.830 194.300 1.00 69.90  ? 4640 VAL A CB    1 
ATOM   21668 C CG1   . VAL A 1 4640 ? 200.470 155.071 195.612 1.00 69.90  ? 4640 VAL A CG1   1 
ATOM   21669 C CG2   . VAL A 1 4640 ? 202.070 153.608 194.390 1.00 69.90  ? 4640 VAL A CG2   1 
ATOM   21670 N N     . ALA A 1 4641 ? 197.941 155.546 193.533 1.00 68.75  ? 4641 ALA A N     1 
ATOM   21671 C CA    . ALA A 1 4641 ? 196.902 156.562 193.504 1.00 68.75  ? 4641 ALA A CA    1 
ATOM   21672 C C     . ALA A 1 4641 ? 195.829 156.221 194.525 1.00 68.75  ? 4641 ALA A C     1 
ATOM   21673 O O     . ALA A 1 4641 ? 195.744 155.093 195.015 1.00 68.75  ? 4641 ALA A O     1 
ATOM   21674 C CB    . ALA A 1 4641 ? 196.288 156.695 192.108 1.00 68.75  ? 4641 ALA A CB    1 
ATOM   21675 N N     . VAL A 1 4642 ? 195.009 157.215 194.838 1.00 64.91  ? 4642 VAL A N     1 
ATOM   21676 C CA    . VAL A 1 4642 ? 193.892 157.069 195.763 1.00 64.91  ? 4642 VAL A CA    1 
ATOM   21677 C C     . VAL A 1 4642 ? 192.598 157.077 194.968 1.00 64.91  ? 4642 VAL A C     1 
ATOM   21678 O O     . VAL A 1 4642 ? 192.412 157.911 194.075 1.00 64.91  ? 4642 VAL A O     1 
ATOM   21679 C CB    . VAL A 1 4642 ? 193.897 158.188 196.818 1.00 64.91  ? 4642 VAL A CB    1 
ATOM   21680 C CG1   . VAL A 1 4642 ? 192.723 158.033 197.757 1.00 64.91  ? 4642 VAL A CG1   1 
ATOM   21681 C CG2   . VAL A 1 4642 ? 195.196 158.171 197.592 1.00 64.91  ? 4642 VAL A CG2   1 
ATOM   21682 N N     . LEU A 1 4643 ? 191.702 156.150 195.285 1.00 70.14  ? 4643 LEU A N     1 
ATOM   21683 C CA    . LEU A 1 4643 ? 190.428 156.030 194.594 1.00 70.14  ? 4643 LEU A CA    1 
ATOM   21684 C C     . LEU A 1 4643 ? 189.287 156.258 195.572 1.00 70.14  ? 4643 LEU A C     1 
ATOM   21685 O O     . LEU A 1 4643 ? 189.332 155.787 196.712 1.00 70.14  ? 4643 LEU A O     1 
ATOM   21686 C CB    . LEU A 1 4643 ? 190.283 154.663 193.945 1.00 70.14  ? 4643 LEU A CB    1 
ATOM   21687 C CG    . LEU A 1 4643 ? 191.337 154.351 192.894 1.00 70.14  ? 4643 LEU A CG    1 
ATOM   21688 C CD1   . LEU A 1 4643 ? 191.151 152.946 192.381 1.00 70.14  ? 4643 LEU A CD1   1 
ATOM   21689 C CD2   . LEU A 1 4643 ? 191.249 155.348 191.768 1.00 70.14  ? 4643 LEU A CD2   1 
ATOM   21690 N N     . CYS A 1 4644 ? 188.264 156.984 195.120 1.00 76.85  ? 4644 CYS A N     1 
ATOM   21691 C CA    . CYS A 1 4644 ? 187.129 157.273 195.988 1.00 76.85  ? 4644 CYS A CA    1 
ATOM   21692 C C     . CYS A 1 4644 ? 186.234 156.052 196.164 1.00 76.85  ? 4644 CYS A C     1 
ATOM   21693 O O     . CYS A 1 4644 ? 185.744 155.791 197.268 1.00 76.85  ? 4644 CYS A O     1 
ATOM   21694 C CB    . CYS A 1 4644 ? 186.330 158.449 195.432 1.00 76.85  ? 4644 CYS A CB    1 
ATOM   21695 S SG    . CYS A 1 4644 ? 187.234 160.010 195.393 1.00 76.85  ? 4644 CYS A SG    1 
ATOM   21696 N N     . THR A 1 4645 ? 186.006 155.296 195.097 1.00 74.22  ? 4645 THR A N     1 
ATOM   21697 C CA    . THR A 1 4645 ? 185.108 154.149 195.166 1.00 74.22  ? 4645 THR A CA    1 
ATOM   21698 C C     . THR A 1 4645 ? 185.869 152.836 195.249 1.00 74.22  ? 4645 THR A C     1 
ATOM   21699 O O     . THR A 1 4645 ? 186.911 152.664 194.621 0.00 74.22  ? 4645 THR A O     1 
ATOM   21700 C CB    . THR A 1 4645 ? 184.172 154.092 193.951 1.00 74.22  ? 4645 THR A CB    1 
ATOM   21701 O OG1   . THR A 1 4645 ? 184.907 153.657 192.801 1.00 74.22  ? 4645 THR A OG1   1 
ATOM   21702 C CG2   . THR A 1 4645 ? 183.575 155.459 193.678 1.00 74.22  ? 4645 THR A CG2   1 
HETATM 21703 P PB    . ADP B 2 .    ? 190.568 178.247 172.919 1.00 90.01  ? 4701 ADP A PB    1 
HETATM 21704 O O1B   . ADP B 2 .    ? 191.317 178.705 171.692 1.00 90.01  ? 4701 ADP A O1B   1 
HETATM 21705 O O2B   . ADP B 2 .    ? 191.384 177.336 173.798 1.00 90.01  ? 4701 ADP A O2B   1 
HETATM 21706 O O3B   . ADP B 2 .    ? 189.209 177.680 172.593 1.00 90.01  ? 4701 ADP A O3B   1 
HETATM 21707 P PA    . ADP B 2 .    ? 189.431 180.881 173.461 1.00 90.01  ? 4701 ADP A PA    1 
HETATM 21708 O O1A   . ADP B 2 .    ? 189.920 181.446 172.169 1.00 90.01  ? 4701 ADP A O1A   1 
HETATM 21709 O O2A   . ADP B 2 .    ? 187.983 180.542 173.587 1.00 90.01  ? 4701 ADP A O2A   1 
HETATM 21710 O O3A   . ADP B 2 .    ? 190.296 179.574 173.791 1.00 90.01  ? 4701 ADP A O3A   1 
HETATM 21711 O "O5'" . ADP B 2 .    ? 189.858 181.854 174.662 1.00 90.01  ? 4701 ADP A "O5'" 1 
HETATM 21712 C "C5'" . ADP B 2 .    ? 189.799 183.279 174.407 1.00 90.01  ? 4701 ADP A "C5'" 1 
HETATM 21713 C "C4'" . ADP B 2 .    ? 190.188 184.046 175.646 1.00 90.01  ? 4701 ADP A "C4'" 1 
HETATM 21714 O "O4'" . ADP B 2 .    ? 191.369 183.440 176.238 1.00 90.01  ? 4701 ADP A "O4'" 1 
HETATM 21715 C "C3'" . ADP B 2 .    ? 190.557 185.520 175.419 1.00 90.01  ? 4701 ADP A "C3'" 1 
HETATM 21716 O "O3'" . ADP B 2 .    ? 190.136 186.326 176.511 1.00 90.01  ? 4701 ADP A "O3'" 1 
HETATM 21717 C "C2'" . ADP B 2 .    ? 192.084 185.455 175.357 1.00 90.01  ? 4701 ADP A "C2'" 1 
HETATM 21718 O "O2'" . ADP B 2 .    ? 192.716 186.694 175.596 1.00 90.01  ? 4701 ADP A "O2'" 1 
HETATM 21719 C "C1'" . ADP B 2 .    ? 192.324 184.448 176.472 1.00 90.01  ? 4701 ADP A "C1'" 1 
HETATM 21720 N N9    . ADP B 2 .    ? 193.658 183.861 176.474 1.00 90.01  ? 4701 ADP A N9    1 
HETATM 21721 C C8    . ADP B 2 .    ? 194.043 182.680 175.892 1.00 90.01  ? 4701 ADP A C8    1 
HETATM 21722 N N7    . ADP B 2 .    ? 195.315 182.414 176.051 1.00 90.01  ? 4701 ADP A N7    1 
HETATM 21723 C C5    . ADP B 2 .    ? 195.805 183.492 176.774 1.00 90.01  ? 4701 ADP A C5    1 
HETATM 21724 C C6    . ADP B 2 .    ? 197.090 183.803 177.257 1.00 90.01  ? 4701 ADP A C6    1 
HETATM 21725 N N6    . ADP B 2 .    ? 198.156 183.029 177.076 1.00 90.01  ? 4701 ADP A N6    1 
HETATM 21726 N N1    . ADP B 2 .    ? 197.237 184.964 177.938 1.00 90.01  ? 4701 ADP A N1    1 
HETATM 21727 C C2    . ADP B 2 .    ? 196.161 185.739 178.117 1.00 90.01  ? 4701 ADP A C2    1 
HETATM 21728 N N3    . ADP B 2 .    ? 194.909 185.548 177.712 1.00 90.01  ? 4701 ADP A N3    1 
HETATM 21729 C C4    . ADP B 2 .    ? 194.793 184.393 177.037 1.00 90.01  ? 4701 ADP A C4    1 
HETATM 21730 P PG    . ATP C 3 .    ? 157.579 191.186 178.446 1.00 78.45  ? 4702 ATP A PG    1 
HETATM 21731 O O1G   . ATP C 3 .    ? 157.808 191.749 177.067 1.00 78.45  ? 4702 ATP A O1G   1 
HETATM 21732 O O2G   . ATP C 3 .    ? 156.374 190.282 178.512 1.00 78.45  ? 4702 ATP A O2G   1 
HETATM 21733 O O3G   . ATP C 3 .    ? 158.816 190.556 179.032 1.00 78.45  ? 4702 ATP A O3G   1 
HETATM 21734 P PB    . ATP C 3 .    ? 157.922 193.893 179.489 1.00 78.45  ? 4702 ATP A PB    1 
HETATM 21735 O O1B   . ATP C 3 .    ? 157.682 194.626 178.211 1.00 78.45  ? 4702 ATP A O1B   1 
HETATM 21736 O O2B   . ATP C 3 .    ? 159.316 193.719 179.990 1.00 78.45  ? 4702 ATP A O2B   1 
HETATM 21737 O O3B   . ATP C 3 .    ? 157.235 192.452 179.380 1.00 78.45  ? 4702 ATP A O3B   1 
HETATM 21738 P PA    . ATP C 3 .    ? 157.049 196.051 181.256 1.00 78.45  ? 4702 ATP A PA    1 
HETATM 21739 O O1A   . ATP C 3 .    ? 158.426 196.362 181.738 1.00 78.45  ? 4702 ATP A O1A   1 
HETATM 21740 O O2A   . ATP C 3 .    ? 156.410 196.978 180.276 1.00 78.45  ? 4702 ATP A O2A   1 
HETATM 21741 O O3A   . ATP C 3 .    ? 157.046 194.570 180.643 1.00 78.45  ? 4702 ATP A O3A   1 
HETATM 21742 O "O5'" . ATP C 3 .    ? 156.074 195.847 182.512 1.00 78.45  ? 4702 ATP A "O5'" 1 
HETATM 21743 C "C5'" . ATP C 3 .    ? 156.177 196.750 183.641 1.00 78.45  ? 4702 ATP A "C5'" 1 
HETATM 21744 C "C4'" . ATP C 3 .    ? 154.938 196.614 184.490 1.00 78.45  ? 4702 ATP A "C4'" 1 
HETATM 21745 O "O4'" . ATP C 3 .    ? 155.220 197.109 185.825 1.00 78.45  ? 4702 ATP A "O4'" 1 
HETATM 21746 C "C3'" . ATP C 3 .    ? 153.708 197.401 184.012 1.00 78.45  ? 4702 ATP A "C3'" 1 
HETATM 21747 O "O3'" . ATP C 3 .    ? 152.523 196.641 184.202 1.00 78.45  ? 4702 ATP A "O3'" 1 
HETATM 21748 C "C2'" . ATP C 3 .    ? 153.726 198.627 184.928 1.00 78.45  ? 4702 ATP A "C2'" 1 
HETATM 21749 O "O2'" . ATP C 3 .    ? 152.469 199.255 185.052 1.00 78.45  ? 4702 ATP A "O2'" 1 
HETATM 21750 C "C1'" . ATP C 3 .    ? 154.185 197.974 186.224 1.00 78.45  ? 4702 ATP A "C1'" 1 
HETATM 21751 N N9    . ATP C 3 .    ? 154.723 198.906 187.203 1.00 78.45  ? 4702 ATP A N9    1 
HETATM 21752 C C8    . ATP C 3 .    ? 154.072 199.470 188.272 1.00 78.45  ? 4702 ATP A C8    1 
HETATM 21753 N N7    . ATP C 3 .    ? 154.845 200.275 188.965 1.00 78.45  ? 4702 ATP A N7    1 
HETATM 21754 C C5    . ATP C 3 .    ? 156.069 200.238 188.308 1.00 78.45  ? 4702 ATP A C5    1 
HETATM 21755 C C6    . ATP C 3 .    ? 157.300 200.876 188.549 1.00 78.45  ? 4702 ATP A C6    1 
HETATM 21756 N N6    . ATP C 3 .    ? 157.517 201.712 189.560 1.00 78.45  ? 4702 ATP A N6    1 
HETATM 21757 N N1    . ATP C 3 .    ? 158.315 200.611 187.693 1.00 78.45  ? 4702 ATP A N1    1 
HETATM 21758 C C2    . ATP C 3 .    ? 158.094 199.768 186.677 1.00 78.45  ? 4702 ATP A C2    1 
HETATM 21759 N N3    . ATP C 3 .    ? 156.984 199.113 186.353 1.00 78.45  ? 4702 ATP A N3    1 
HETATM 21760 C C4    . ATP C 3 .    ? 156.000 199.396 187.220 1.00 78.45  ? 4702 ATP A C4    1 
HETATM 21761 P PG    . ATP D 3 .    ? 135.703 174.843 166.600 1.00 85.96  ? 4703 ATP A PG    1 
HETATM 21762 O O1G   . ATP D 3 .    ? 136.702 174.849 167.701 1.00 85.96  ? 4703 ATP A O1G   1 
HETATM 21763 O O2G   . ATP D 3 .    ? 135.810 176.052 165.674 1.00 85.96  ? 4703 ATP A O2G   1 
HETATM 21764 O O3G   . ATP D 3 .    ? 135.717 173.559 165.776 1.00 85.96  ? 4703 ATP A O3G   1 
HETATM 21765 P PB    . ATP D 3 .    ? 133.356 175.851 168.117 1.00 85.96  ? 4703 ATP A PB    1 
HETATM 21766 O O1B   . ATP D 3 .    ? 133.284 175.342 169.499 1.00 85.96  ? 4703 ATP A O1B   1 
HETATM 21767 O O2B   . ATP D 3 .    ? 133.889 177.271 167.945 1.00 85.96  ? 4703 ATP A O2B   1 
HETATM 21768 O O3B   . ATP D 3 .    ? 134.231 174.924 167.186 1.00 85.96  ? 4703 ATP A O3B   1 
HETATM 21769 P PA    . ATP D 3 .    ? 131.401 175.488 165.955 1.00 85.96  ? 4703 ATP A PA    1 
HETATM 21770 O O1A   . ATP D 3 .    ? 131.598 176.633 165.046 1.00 85.96  ? 4703 ATP A O1A   1 
HETATM 21771 O O2A   . ATP D 3 .    ? 132.054 174.182 165.510 1.00 85.96  ? 4703 ATP A O2A   1 
HETATM 21772 O O3A   . ATP D 3 .    ? 131.941 175.801 167.396 1.00 85.96  ? 4703 ATP A O3A   1 
HETATM 21773 O "O5'" . ATP D 3 .    ? 129.874 175.213 166.237 1.00 85.96  ? 4703 ATP A "O5'" 1 
HETATM 21774 C "C5'" . ATP D 3 .    ? 129.436 174.672 167.500 1.00 85.96  ? 4703 ATP A "C5'" 1 
HETATM 21775 C "C4'" . ATP D 3 .    ? 128.309 173.709 167.241 1.00 85.96  ? 4703 ATP A "C4'" 1 
HETATM 21776 O "O4'" . ATP D 3 .    ? 127.383 173.748 168.348 1.00 85.96  ? 4703 ATP A "O4'" 1 
HETATM 21777 C "C3'" . ATP D 3 .    ? 127.463 174.037 166.020 1.00 85.96  ? 4703 ATP A "C3'" 1 
HETATM 21778 O "O3'" . ATP D 3 .    ? 126.781 172.876 165.562 1.00 85.96  ? 4703 ATP A "O3'" 1 
HETATM 21779 C "C2'" . ATP D 3 .    ? 126.476 175.049 166.592 1.00 85.96  ? 4703 ATP A "C2'" 1 
HETATM 21780 O "O2'" . ATP D 3 .    ? 125.275 175.095 165.832 1.00 85.96  ? 4703 ATP A "O2'" 1 
HETATM 21781 C "C1'" . ATP D 3 .    ? 126.205 174.439 167.968 1.00 85.96  ? 4703 ATP A "C1'" 1 
HETATM 21782 N N9    . ATP D 3 .    ? 125.895 175.411 169.006 1.00 85.96  ? 4703 ATP A N9    1 
HETATM 21783 C C8    . ATP D 3 .    ? 126.452 175.479 170.255 1.00 85.96  ? 4703 ATP A C8    1 
HETATM 21784 N N7    . ATP D 3 .    ? 125.987 176.453 170.997 1.00 85.96  ? 4703 ATP A N7    1 
HETATM 21785 C C5    . ATP D 3 .    ? 125.055 177.071 170.178 1.00 85.96  ? 4703 ATP A C5    1 
HETATM 21786 C C6    . ATP D 3 .    ? 124.209 178.177 170.371 1.00 85.96  ? 4703 ATP A C6    1 
HETATM 21787 N N6    . ATP D 3 .    ? 124.162 178.888 171.502 1.00 85.96  ? 4703 ATP A N6    1 
HETATM 21788 N N1    . ATP D 3 .    ? 123.399 178.534 169.351 1.00 85.96  ? 4703 ATP A N1    1 
HETATM 21789 C C2    . ATP D 3 .    ? 123.442 177.827 168.220 1.00 85.96  ? 4703 ATP A C2    1 
HETATM 21790 N N3    . ATP D 3 .    ? 124.196 176.768 167.924 1.00 85.96  ? 4703 ATP A N3    1 
HETATM 21791 C C4    . ATP D 3 .    ? 124.987 176.438 168.948 1.00 85.96  ? 4703 ATP A C4    1 
HETATM 21792 P PB    . ADP E 2 .    ? 139.138 150.457 151.048 1.00 97.71  ? 4704 ADP A PB    1 
HETATM 21793 O O1B   . ADP E 2 .    ? 138.194 151.539 150.594 1.00 97.71  ? 4704 ADP A O1B   1 
HETATM 21794 O O2B   . ADP E 2 .    ? 138.930 150.002 152.469 1.00 97.71  ? 4704 ADP A O2B   1 
HETATM 21795 O O3B   . ADP E 2 .    ? 140.581 150.681 150.673 1.00 97.71  ? 4704 ADP A O3B   1 
HETATM 21796 P PA    . ADP E 2 .    ? 138.669 149.322 148.570 1.00 97.71  ? 4704 ADP A PA    1 
HETATM 21797 O O1A   . ADP E 2 .    ? 137.465 150.145 148.190 1.00 97.71  ? 4704 ADP A O1A   1 
HETATM 21798 O O2A   . ADP E 2 .    ? 140.051 149.722 148.120 1.00 97.71  ? 4704 ADP A O2A   1 
HETATM 21799 O O3A   . ADP E 2 .    ? 138.701 149.191 150.167 1.00 97.71  ? 4704 ADP A O3A   1 
HETATM 21800 O "O5'" . ADP E 2 .    ? 138.424 147.800 148.125 1.00 97.71  ? 4704 ADP A "O5'" 1 
HETATM 21801 C "C5'" . ADP E 2 .    ? 139.355 147.185 147.245 1.00 97.71  ? 4704 ADP A "C5'" 1 
HETATM 21802 C "C4'" . ADP E 2 .    ? 138.731 145.952 146.614 1.00 97.71  ? 4704 ADP A "C4'" 1 
HETATM 21803 O "O4'" . ADP E 2 .    ? 137.904 145.262 147.549 1.00 97.71  ? 4704 ADP A "O4'" 1 
HETATM 21804 C "C3'" . ADP E 2 .    ? 137.834 146.334 145.454 1.00 97.71  ? 4704 ADP A "C3'" 1 
HETATM 21805 O "O3'" . ADP E 2 .    ? 138.502 146.073 144.220 1.00 97.71  ? 4704 ADP A "O3'" 1 
HETATM 21806 C "C2'" . ADP E 2 .    ? 136.618 145.448 145.583 1.00 97.71  ? 4704 ADP A "C2'" 1 
HETATM 21807 O "O2'" . ADP E 2 .    ? 136.551 144.563 144.467 1.00 97.71  ? 4704 ADP A "O2'" 1 
HETATM 21808 C "C1'" . ADP E 2 .    ? 136.838 144.634 146.840 1.00 97.71  ? 4704 ADP A "C1'" 1 
HETATM 21809 N N9    . ADP E 2 .    ? 135.594 144.608 147.639 1.00 97.71  ? 4704 ADP A N9    1 
HETATM 21810 C C8    . ADP E 2 .    ? 135.289 145.417 148.664 1.00 97.71  ? 4704 ADP A C8    1 
HETATM 21811 N N7    . ADP E 2 .    ? 134.068 145.120 149.174 1.00 97.71  ? 4704 ADP A N7    1 
HETATM 21812 C C5    . ADP E 2 .    ? 133.574 144.096 148.463 1.00 97.71  ? 4704 ADP A C5    1 
HETATM 21813 C C6    . ADP E 2 .    ? 132.334 143.293 148.472 1.00 97.71  ? 4704 ADP A C6    1 
HETATM 21814 N N6    . ADP E 2 .    ? 131.350 143.532 149.370 1.00 97.71  ? 4704 ADP A N6    1 
HETATM 21815 N N1    . ADP E 2 .    ? 132.215 142.314 147.552 1.00 97.71  ? 4704 ADP A N1    1 
HETATM 21816 C C2    . ADP E 2 .    ? 133.187 142.067 146.657 1.00 97.71  ? 4704 ADP A C2    1 
HETATM 21817 N N3    . ADP E 2 .    ? 134.337 142.756 146.592 1.00 97.71  ? 4704 ADP A N3    1 
HETATM 21818 C C4    . ADP E 2 .    ? 134.584 143.764 147.454 1.00 97.71  ? 4704 ADP A C4    1 
# 
