data_9DH5
# 
_entry.id   9DH5 
# 
_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   9DH5         pdb_00009dh5 10.2210/pdb9dh5/pdb 
WWPDB D_1000288097 ?            ?                   
EMDB  EMD-46856    ?            ?                   
# 
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 FSC               1 0 2025-04-23 ? 
4 'Half map'        1 0 2025-04-23 1 
5 'Half map'        1 0 2025-04-23 2 
6 Image             1 0 2025-04-23 ? 
7 Mask              1 0 2025-04-23 1 
8 'Primary map'     1 0 2025-04-23 ? 
9 'Structure model' 1 1 2025-04-30 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 Mask              repository 'Initial release' ? ? 
8 8 '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 9 'Structure model' 'Data collection'     
2 9 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 9 'Structure model' citation        
2 9 'Structure model' citation_author 
3 9 'Structure model' em_admin        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 9 'Structure model' '_citation.country'                 
2 9 'Structure model' '_citation.journal_abbrev'          
3 9 'Structure model' '_citation.journal_id_CSD'          
4 9 'Structure model' '_citation.journal_id_ISSN'         
5 9 'Structure model' '_citation.pdbx_database_id_DOI'    
6 9 'Structure model' '_citation.pdbx_database_id_PubMed' 
7 9 'Structure model' '_citation.title'                   
8 9 'Structure model' '_citation.year'                    
9 9 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DH5 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-03 
_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-1 of the motor domain from full-length human dynein-1 in 5mM AMPPNP with 5mM Mg2+' 
_pdbx_database_related.db_id          EMD-46856 
_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    3 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"          507.181    1 ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                      24.305     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 
4 'MAGNESIUM ION'             MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    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               'fall armyworm' 
_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 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    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 1457 MET MET A . n 
A 1 1458 ALA 1458 1458 1458 ALA ALA A . n 
A 1 1459 LEU 1459 1459 1459 LEU LEU A . n 
A 1 1460 GLU 1460 1460 1460 GLU GLU A . n 
A 1 1461 GLU 1461 1461 1461 GLU GLU A . n 
A 1 1462 PHE 1462 1462 1462 PHE PHE A . n 
A 1 1463 LEU 1463 1463 1463 LEU LEU A . n 
A 1 1464 LYS 1464 1464 1464 LYS LYS A . n 
A 1 1465 GLN 1465 1465 1465 GLN GLN A . n 
A 1 1466 ILE 1466 1466 1466 ILE ILE A . n 
A 1 1467 ARG 1467 1467 1467 ARG ARG A . n 
A 1 1468 GLU 1468 1468 1468 GLU GLU A . n 
A 1 1469 VAL 1469 1469 1469 VAL VAL A . n 
A 1 1470 TRP 1470 1470 1470 TRP TRP A . n 
A 1 1471 ASN 1471 1471 1471 ASN ASN A . n 
A 1 1472 THR 1472 1472 1472 THR THR A . n 
A 1 1473 TYR 1473 1473 1473 TYR TYR A . n 
A 1 1474 GLU 1474 1474 1474 GLU GLU A . n 
A 1 1475 LEU 1475 1475 1475 LEU LEU A . n 
A 1 1476 ASP 1476 1476 1476 ASP ASP A . n 
A 1 1477 LEU 1477 1477 1477 LEU LEU A . n 
A 1 1478 VAL 1478 1478 1478 VAL VAL A . n 
A 1 1479 ASN 1479 1479 1479 ASN ASN A . n 
A 1 1480 TYR 1480 1480 1480 TYR TYR A . n 
A 1 1481 GLN 1481 1481 1481 GLN GLN A . n 
A 1 1482 ASN 1482 1482 1482 ASN ASN A . n 
A 1 1483 LYS 1483 1483 1483 LYS LYS A . n 
A 1 1484 CYS 1484 1484 1484 CYS CYS A . n 
A 1 1485 ARG 1485 1485 1485 ARG ARG A . n 
A 1 1486 LEU 1486 1486 1486 LEU LEU A . n 
A 1 1487 ILE 1487 1487 1487 ILE ILE A . n 
A 1 1488 ARG 1488 1488 1488 ARG ARG A . n 
A 1 1489 GLY 1489 1489 1489 GLY GLY A . n 
A 1 1490 TRP 1490 1490 1490 TRP TRP A . n 
A 1 1491 ASP 1491 1491 1491 ASP ASP A . n 
A 1 1492 ASP 1492 1492 1492 ASP ASP A . n 
A 1 1493 LEU 1493 1493 1493 LEU LEU A . n 
A 1 1494 PHE 1494 1494 1494 PHE PHE A . n 
A 1 1495 ASN 1495 1495 1495 ASN ASN A . n 
A 1 1496 LYS 1496 1496 1496 LYS LYS A . n 
A 1 1497 VAL 1497 1497 1497 VAL VAL A . n 
A 1 1498 LYS 1498 1498 1498 LYS LYS A . n 
A 1 1499 GLU 1499 1499 1499 GLU GLU A . n 
A 1 1500 HIS 1500 1500 1500 HIS HIS A . n 
A 1 1501 ILE 1501 1501 1501 ILE ILE A . n 
A 1 1502 ASN 1502 1502 1502 ASN ASN A . n 
A 1 1503 SER 1503 1503 1503 SER SER A . n 
A 1 1504 VAL 1504 1504 1504 VAL VAL A . n 
A 1 1505 SER 1505 1505 1505 SER SER A . n 
A 1 1506 ALA 1506 1506 1506 ALA ALA A . n 
A 1 1507 MET 1507 1507 1507 MET MET A . n 
A 1 1508 LYS 1508 1508 1508 LYS LYS A . n 
A 1 1509 LEU 1509 1509 1509 LEU LEU A . n 
A 1 1510 SER 1510 1510 1510 SER SER A . n 
A 1 1511 PRO 1511 1511 1511 PRO PRO A . n 
A 1 1512 TYR 1512 1512 1512 TYR TYR A . n 
A 1 1513 TYR 1513 1513 1513 TYR TYR A . n 
A 1 1514 LYS 1514 1514 1514 LYS LYS A . n 
A 1 1515 VAL 1515 1515 1515 VAL VAL A . n 
A 1 1516 PHE 1516 1516 1516 PHE PHE A . n 
A 1 1517 GLU 1517 1517 1517 GLU GLU A . n 
A 1 1518 GLU 1518 1518 1518 GLU GLU A . n 
A 1 1519 ASP 1519 1519 1519 ASP ASP A . n 
A 1 1520 ALA 1520 1520 1520 ALA ALA A . n 
A 1 1521 LEU 1521 1521 1521 LEU LEU A . n 
A 1 1522 SER 1522 1522 1522 SER SER A . n 
A 1 1523 TRP 1523 1523 1523 TRP TRP A . n 
A 1 1524 GLU 1524 1524 1524 GLU GLU A . n 
A 1 1525 ASP 1525 1525 1525 ASP ASP A . n 
A 1 1526 LYS 1526 1526 1526 LYS LYS A . n 
A 1 1527 LEU 1527 1527 1527 LEU LEU A . n 
A 1 1528 ASN 1528 1528 1528 ASN ASN A . n 
A 1 1529 ARG 1529 1529 1529 ARG ARG A . n 
A 1 1530 ILE 1530 1530 1530 ILE ILE A . n 
A 1 1531 MET 1531 1531 1531 MET MET A . n 
A 1 1532 ALA 1532 1532 1532 ALA ALA A . n 
A 1 1533 LEU 1533 1533 1533 LEU LEU A . n 
A 1 1534 PHE 1534 1534 1534 PHE PHE A . n 
A 1 1535 ASP 1535 1535 1535 ASP ASP A . n 
A 1 1536 VAL 1536 1536 1536 VAL VAL A . n 
A 1 1537 TRP 1537 1537 1537 TRP TRP A . n 
A 1 1538 ILE 1538 1538 1538 ILE ILE A . n 
A 1 1539 ASP 1539 1539 1539 ASP ASP A . n 
A 1 1540 VAL 1540 1540 1540 VAL VAL A . n 
A 1 1541 GLN 1541 1541 1541 GLN GLN A . n 
A 1 1542 ARG 1542 1542 1542 ARG ARG A . n 
A 1 1543 ARG 1543 1543 1543 ARG ARG A . n 
A 1 1544 TRP 1544 1544 1544 TRP TRP A . n 
A 1 1545 VAL 1545 1545 1545 VAL VAL A . n 
A 1 1546 TYR 1546 1546 1546 TYR TYR A . n 
A 1 1547 LEU 1547 1547 1547 LEU LEU A . n 
A 1 1548 GLU 1548 1548 1548 GLU GLU A . n 
A 1 1549 GLY 1549 1549 1549 GLY GLY A . n 
A 1 1550 ILE 1550 1550 1550 ILE ILE A . n 
A 1 1551 PHE 1551 1551 1551 PHE PHE A . n 
A 1 1552 THR 1552 1552 1552 THR THR A . n 
A 1 1553 GLY 1553 1553 1553 GLY GLY A . n 
A 1 1554 SER 1554 1554 1554 SER SER A . n 
A 1 1555 ALA 1555 1555 1555 ALA ALA A . n 
A 1 1556 ASP 1556 1556 1556 ASP ASP A . n 
A 1 1557 ILE 1557 1557 1557 ILE ILE A . n 
A 1 1558 LYS 1558 1558 1558 LYS LYS A . n 
A 1 1559 HIS 1559 1559 1559 HIS HIS A . n 
A 1 1560 LEU 1560 1560 1560 LEU LEU A . n 
A 1 1561 LEU 1561 1561 1561 LEU LEU A . n 
A 1 1562 PRO 1562 1562 1562 PRO PRO A . n 
A 1 1563 VAL 1563 1563 1563 VAL VAL A . n 
A 1 1564 GLU 1564 1564 1564 GLU GLU A . n 
A 1 1565 THR 1565 1565 1565 THR THR A . n 
A 1 1566 GLN 1566 1566 1566 GLN GLN A . n 
A 1 1567 ARG 1567 1567 1567 ARG ARG A . n 
A 1 1568 PHE 1568 1568 1568 PHE PHE A . n 
A 1 1569 GLN 1569 1569 1569 GLN GLN A . n 
A 1 1570 SER 1570 1570 1570 SER SER A . n 
A 1 1571 ILE 1571 1571 1571 ILE ILE A . n 
A 1 1572 SER 1572 1572 1572 SER SER A . n 
A 1 1573 THR 1573 1573 1573 THR THR A . n 
A 1 1574 GLU 1574 1574 1574 GLU GLU A . n 
A 1 1575 PHE 1575 1575 1575 PHE PHE A . n 
A 1 1576 LEU 1576 1576 1576 LEU LEU A . n 
A 1 1577 ALA 1577 1577 1577 ALA ALA A . n 
A 1 1578 LEU 1578 1578 1578 LEU LEU A . n 
A 1 1579 MET 1579 1579 1579 MET MET A . n 
A 1 1580 LYS 1580 1580 1580 LYS LYS A . n 
A 1 1581 LYS 1581 1581 1581 LYS LYS A . n 
A 1 1582 VAL 1582 1582 1582 VAL VAL A . n 
A 1 1583 SER 1583 1583 1583 SER SER A . n 
A 1 1584 LYS 1584 1584 1584 LYS LYS A . n 
A 1 1585 SER 1585 1585 1585 SER SER A . n 
A 1 1586 PRO 1586 1586 1586 PRO PRO A . n 
A 1 1587 LEU 1587 1587 1587 LEU LEU A . n 
A 1 1588 VAL 1588 1588 1588 VAL VAL A . n 
A 1 1589 MET 1589 1589 1589 MET MET A . n 
A 1 1590 ASP 1590 1590 1590 ASP ASP A . n 
A 1 1591 VAL 1591 1591 1591 VAL VAL A . n 
A 1 1592 LEU 1592 1592 1592 LEU LEU A . n 
A 1 1593 ASN 1593 1593 1593 ASN ASN A . n 
A 1 1594 ILE 1594 1594 1594 ILE ILE A . n 
A 1 1595 GLN 1595 1595 1595 GLN GLN A . n 
A 1 1596 GLY 1596 1596 1596 GLY GLY A . n 
A 1 1597 VAL 1597 1597 1597 VAL VAL A . n 
A 1 1598 GLN 1598 1598 1598 GLN GLN A . n 
A 1 1599 ARG 1599 1599 1599 ARG ARG A . n 
A 1 1600 SER 1600 1600 1600 SER SER A . n 
A 1 1601 LEU 1601 1601 1601 LEU LEU A . n 
A 1 1602 GLU 1602 1602 1602 GLU GLU A . n 
A 1 1603 ARG 1603 1603 1603 ARG ARG A . n 
A 1 1604 LEU 1604 1604 1604 LEU LEU A . n 
A 1 1605 ALA 1605 1605 1605 ALA ALA A . n 
A 1 1606 ASP 1606 1606 1606 ASP ASP A . n 
A 1 1607 LEU 1607 1607 1607 LEU LEU A . n 
A 1 1608 LEU 1608 1608 1608 LEU LEU A . n 
A 1 1609 GLY 1609 1609 1609 GLY GLY A . n 
A 1 1610 LYS 1610 1610 1610 LYS LYS A . n 
A 1 1611 ILE 1611 1611 1611 ILE ILE A . n 
A 1 1612 GLN 1612 1612 1612 GLN GLN A . n 
A 1 1613 LYS 1613 1613 1613 LYS LYS A . n 
A 1 1614 ALA 1614 1614 1614 ALA ALA A . n 
A 1 1615 LEU 1615 1615 1615 LEU LEU A . n 
A 1 1616 GLY 1616 1616 1616 GLY GLY A . n 
A 1 1617 GLU 1617 1617 1617 GLU GLU A . n 
A 1 1618 TYR 1618 1618 1618 TYR TYR A . n 
A 1 1619 LEU 1619 1619 1619 LEU LEU A . n 
A 1 1620 GLU 1620 1620 1620 GLU GLU A . n 
A 1 1621 ARG 1621 1621 1621 ARG ARG A . n 
A 1 1622 GLU 1622 1622 1622 GLU GLU A . n 
A 1 1623 ARG 1623 1623 1623 ARG ARG A . n 
A 1 1624 SER 1624 1624 1624 SER SER A . n 
A 1 1625 SER 1625 1625 1625 SER SER A . n 
A 1 1626 PHE 1626 1626 1626 PHE PHE A . n 
A 1 1627 PRO 1627 1627 1627 PRO PRO A . n 
A 1 1628 ARG 1628 1628 1628 ARG ARG A . n 
A 1 1629 PHE 1629 1629 1629 PHE PHE A . n 
A 1 1630 TYR 1630 1630 1630 TYR TYR A . n 
A 1 1631 PHE 1631 1631 1631 PHE PHE A . n 
A 1 1632 VAL 1632 1632 1632 VAL VAL A . n 
A 1 1633 GLY 1633 1633 1633 GLY GLY A . n 
A 1 1634 ASP 1634 1634 1634 ASP ASP A . n 
A 1 1635 GLU 1635 1635 1635 GLU GLU A . n 
A 1 1636 ASP 1636 1636 1636 ASP ASP A . n 
A 1 1637 LEU 1637 1637 1637 LEU LEU A . n 
A 1 1638 LEU 1638 1638 1638 LEU LEU A . n 
A 1 1639 GLU 1639 1639 1639 GLU GLU A . n 
A 1 1640 ILE 1640 1640 1640 ILE ILE A . n 
A 1 1641 ILE 1641 1641 1641 ILE ILE A . n 
A 1 1642 GLY 1642 1642 1642 GLY GLY A . n 
A 1 1643 ASN 1643 1643 1643 ASN ASN A . n 
A 1 1644 SER 1644 1644 1644 SER SER A . n 
A 1 1645 LYS 1645 1645 1645 LYS LYS A . n 
A 1 1646 ASN 1646 1646 1646 ASN ASN A . n 
A 1 1647 VAL 1647 1647 1647 VAL VAL A . n 
A 1 1648 ALA 1648 1648 1648 ALA ALA A . n 
A 1 1649 LYS 1649 1649 1649 LYS LYS A . n 
A 1 1650 LEU 1650 1650 1650 LEU LEU A . n 
A 1 1651 GLN 1651 1651 1651 GLN GLN A . n 
A 1 1652 LYS 1652 1652 1652 LYS LYS A . n 
A 1 1653 HIS 1653 1653 1653 HIS HIS A . n 
A 1 1654 PHE 1654 1654 1654 PHE PHE A . n 
A 1 1655 LYS 1655 1655 1655 LYS LYS A . n 
A 1 1656 LYS 1656 1656 1656 LYS LYS A . n 
A 1 1657 MET 1657 1657 1657 MET MET A . n 
A 1 1658 PHE 1658 1658 1658 PHE PHE A . n 
A 1 1659 ALA 1659 1659 1659 ALA ALA A . n 
A 1 1660 GLY 1660 1660 1660 GLY GLY A . n 
A 1 1661 VAL 1661 1661 1661 VAL VAL A . n 
A 1 1662 SER 1662 1662 1662 SER SER A . n 
A 1 1663 SER 1663 1663 1663 SER SER A . n 
A 1 1664 ILE 1664 1664 1664 ILE ILE A . n 
A 1 1665 ILE 1665 1665 1665 ILE ILE A . n 
A 1 1666 LEU 1666 1666 1666 LEU LEU A . n 
A 1 1667 ASN 1667 1667 1667 ASN ASN A . n 
A 1 1668 GLU 1668 1668 1668 GLU GLU A . n 
A 1 1669 ASP 1669 1669 1669 ASP ASP A . n 
A 1 1670 ASN 1670 1670 1670 ASN ASN A . n 
A 1 1671 SER 1671 1671 1671 SER SER A . n 
A 1 1672 VAL 1672 1672 1672 VAL VAL A . n 
A 1 1673 VAL 1673 1673 1673 VAL VAL A . n 
A 1 1674 LEU 1674 1674 1674 LEU LEU A . n 
A 1 1675 GLY 1675 1675 1675 GLY GLY A . n 
A 1 1676 ILE 1676 1676 1676 ILE ILE A . n 
A 1 1677 SER 1677 1677 1677 SER SER A . n 
A 1 1678 SER 1678 1678 1678 SER SER A . n 
A 1 1679 ARG 1679 1679 1679 ARG ARG A . n 
A 1 1680 GLU 1680 1680 1680 GLU GLU A . n 
A 1 1681 GLY 1681 1681 1681 GLY GLY A . n 
A 1 1682 GLU 1682 1682 1682 GLU GLU A . n 
A 1 1683 GLU 1683 1683 1683 GLU GLU A . n 
A 1 1684 VAL 1684 1684 1684 VAL VAL A . n 
A 1 1685 MET 1685 1685 1685 MET MET A . n 
A 1 1686 PHE 1686 1686 1686 PHE PHE A . n 
A 1 1687 LYS 1687 1687 1687 LYS LYS A . n 
A 1 1688 THR 1688 1688 1688 THR THR A . n 
A 1 1689 PRO 1689 1689 1689 PRO PRO A . n 
A 1 1690 VAL 1690 1690 1690 VAL VAL A . n 
A 1 1691 SER 1691 1691 1691 SER SER A . n 
A 1 1692 ILE 1692 1692 1692 ILE ILE A . n 
A 1 1693 THR 1693 1693 1693 THR THR A . n 
A 1 1694 GLU 1694 1694 1694 GLU GLU A . n 
A 1 1695 HIS 1695 1695 1695 HIS HIS A . n 
A 1 1696 PRO 1696 1696 1696 PRO PRO A . n 
A 1 1697 LYS 1697 1697 1697 LYS LYS A . n 
A 1 1698 ILE 1698 1698 1698 ILE ILE A . n 
A 1 1699 ASN 1699 1699 1699 ASN ASN A . n 
A 1 1700 GLU 1700 1700 1700 GLU GLU A . n 
A 1 1701 TRP 1701 1701 1701 TRP TRP A . n 
A 1 1702 LEU 1702 1702 1702 LEU LEU A . n 
A 1 1703 THR 1703 1703 1703 THR THR A . n 
A 1 1704 LEU 1704 1704 1704 LEU LEU A . n 
A 1 1705 VAL 1705 1705 1705 VAL VAL A . n 
A 1 1706 GLU 1706 1706 1706 GLU GLU A . n 
A 1 1707 LYS 1707 1707 1707 LYS LYS A . n 
A 1 1708 GLU 1708 1708 1708 GLU GLU A . n 
A 1 1709 MET 1709 1709 1709 MET MET A . n 
A 1 1710 ARG 1710 1710 1710 ARG ARG A . n 
A 1 1711 VAL 1711 1711 1711 VAL VAL A . n 
A 1 1712 THR 1712 1712 1712 THR THR A . n 
A 1 1713 LEU 1713 1713 1713 LEU LEU A . n 
A 1 1714 ALA 1714 1714 1714 ALA ALA A . n 
A 1 1715 LYS 1715 1715 1715 LYS LYS A . n 
A 1 1716 LEU 1716 1716 1716 LEU LEU A . n 
A 1 1717 LEU 1717 1717 1717 LEU LEU A . n 
A 1 1718 ALA 1718 1718 1718 ALA ALA A . n 
A 1 1719 GLU 1719 1719 1719 GLU GLU A . n 
A 1 1720 SER 1720 1720 1720 SER SER A . n 
A 1 1721 VAL 1721 1721 1721 VAL VAL A . n 
A 1 1722 THR 1722 1722 1722 THR THR A . n 
A 1 1723 GLU 1723 1723 1723 GLU GLU A . n 
A 1 1724 VAL 1724 1724 1724 VAL VAL A . n 
A 1 1725 GLU 1725 1725 1725 GLU GLU A . n 
A 1 1726 ILE 1726 1726 1726 ILE ILE A . n 
A 1 1727 PHE 1727 1727 1727 PHE PHE A . n 
A 1 1728 GLY 1728 1728 1728 GLY GLY A . n 
A 1 1729 LYS 1729 1729 1729 LYS LYS A . n 
A 1 1730 ALA 1730 1730 1730 ALA ALA A . n 
A 1 1731 THR 1731 1731 1731 THR THR A . n 
A 1 1732 SER 1732 1732 1732 SER SER A . n 
A 1 1733 ILE 1733 1733 1733 ILE ILE A . n 
A 1 1734 ASP 1734 1734 1734 ASP ASP A . n 
A 1 1735 PRO 1735 1735 1735 PRO PRO A . n 
A 1 1736 ASN 1736 1736 1736 ASN ASN A . n 
A 1 1737 THR 1737 1737 1737 THR THR A . n 
A 1 1738 TYR 1738 1738 1738 TYR TYR A . n 
A 1 1739 ILE 1739 1739 1739 ILE ILE A . n 
A 1 1740 THR 1740 1740 1740 THR THR A . n 
A 1 1741 TRP 1741 1741 1741 TRP TRP A . n 
A 1 1742 ILE 1742 1742 1742 ILE ILE A . n 
A 1 1743 ASP 1743 1743 1743 ASP ASP A . n 
A 1 1744 LYS 1744 1744 1744 LYS LYS A . n 
A 1 1745 TYR 1745 1745 1745 TYR TYR A . n 
A 1 1746 GLN 1746 1746 1746 GLN GLN A . n 
A 1 1747 ALA 1747 1747 1747 ALA ALA A . n 
A 1 1748 GLN 1748 1748 1748 GLN GLN A . n 
A 1 1749 LEU 1749 1749 1749 LEU LEU A . n 
A 1 1750 VAL 1750 1750 1750 VAL VAL A . n 
A 1 1751 VAL 1751 1751 1751 VAL VAL A . n 
A 1 1752 LEU 1752 1752 1752 LEU LEU A . n 
A 1 1753 SER 1753 1753 1753 SER SER A . n 
A 1 1754 ALA 1754 1754 1754 ALA ALA A . n 
A 1 1755 GLN 1755 1755 1755 GLN GLN A . n 
A 1 1756 ILE 1756 1756 1756 ILE ILE A . n 
A 1 1757 ALA 1757 1757 1757 ALA ALA A . n 
A 1 1758 TRP 1758 1758 1758 TRP TRP A . n 
A 1 1759 SER 1759 1759 1759 SER SER A . n 
A 1 1760 GLU 1760 1760 1760 GLU GLU A . n 
A 1 1761 ASN 1761 1761 1761 ASN ASN A . n 
A 1 1762 VAL 1762 1762 1762 VAL VAL A . n 
A 1 1763 GLU 1763 1763 1763 GLU GLU A . n 
A 1 1764 THR 1764 1764 1764 THR THR A . n 
A 1 1765 ALA 1765 1765 1765 ALA ALA A . n 
A 1 1766 LEU 1766 1766 1766 LEU LEU A . n 
A 1 1767 SER 1767 1767 1767 SER SER A . n 
A 1 1768 SER 1768 1768 1768 SER SER A . n 
A 1 1769 MET 1769 1769 1769 MET MET A . n 
A 1 1770 GLY 1770 1770 1770 GLY GLY A . n 
A 1 1771 GLY 1771 1771 1771 GLY GLY A . n 
A 1 1772 GLY 1772 1772 1772 GLY GLY A . n 
A 1 1773 GLY 1773 1773 1773 GLY GLY A . n 
A 1 1774 ASP 1774 1774 1774 ASP ASP A . n 
A 1 1775 ALA 1775 1775 1775 ALA ALA A . n 
A 1 1776 ALA 1776 1776 1776 ALA ALA A . n 
A 1 1777 PRO 1777 1777 1777 PRO PRO A . n 
A 1 1778 LEU 1778 1778 1778 LEU LEU A . n 
A 1 1779 HIS 1779 1779 1779 HIS HIS A . n 
A 1 1780 SER 1780 1780 1780 SER SER A . n 
A 1 1781 VAL 1781 1781 1781 VAL VAL A . n 
A 1 1782 LEU 1782 1782 1782 LEU LEU A . n 
A 1 1783 SER 1783 1783 1783 SER SER A . n 
A 1 1784 ASN 1784 1784 1784 ASN ASN A . n 
A 1 1785 VAL 1785 1785 1785 VAL VAL A . n 
A 1 1786 GLU 1786 1786 1786 GLU GLU A . n 
A 1 1787 VAL 1787 1787 1787 VAL VAL A . n 
A 1 1788 THR 1788 1788 1788 THR THR A . n 
A 1 1789 LEU 1789 1789 1789 LEU LEU A . n 
A 1 1790 ASN 1790 1790 1790 ASN ASN A . n 
A 1 1791 VAL 1791 1791 1791 VAL VAL A . n 
A 1 1792 LEU 1792 1792 1792 LEU LEU A . n 
A 1 1793 ALA 1793 1793 1793 ALA ALA A . n 
A 1 1794 ASP 1794 1794 1794 ASP ASP A . n 
A 1 1795 SER 1795 1795 1795 SER SER A . n 
A 1 1796 VAL 1796 1796 1796 VAL VAL A . n 
A 1 1797 LEU 1797 1797 1797 LEU LEU A . n 
A 1 1798 MET 1798 1798 1798 MET MET A . n 
A 1 1799 GLU 1799 1799 1799 GLU GLU A . n 
A 1 1800 GLN 1800 1800 1800 GLN GLN A . n 
A 1 1801 PRO 1801 1801 1801 PRO PRO A . n 
A 1 1802 PRO 1802 1802 1802 PRO PRO A . n 
A 1 1803 LEU 1803 1803 1803 LEU LEU A . n 
A 1 1804 ARG 1804 1804 1804 ARG ARG A . n 
A 1 1805 ARG 1805 1805 1805 ARG ARG A . n 
A 1 1806 ARG 1806 1806 1806 ARG ARG A . n 
A 1 1807 LYS 1807 1807 1807 LYS LYS A . n 
A 1 1808 LEU 1808 1808 1808 LEU LEU A . n 
A 1 1809 GLU 1809 1809 1809 GLU GLU A . n 
A 1 1810 HIS 1810 1810 1810 HIS HIS A . n 
A 1 1811 LEU 1811 1811 1811 LEU LEU A . n 
A 1 1812 ILE 1812 1812 1812 ILE ILE A . n 
A 1 1813 THR 1813 1813 1813 THR THR A . n 
A 1 1814 GLU 1814 1814 1814 GLU GLU A . n 
A 1 1815 LEU 1815 1815 1815 LEU LEU A . n 
A 1 1816 VAL 1816 1816 1816 VAL VAL A . n 
A 1 1817 HIS 1817 1817 1817 HIS HIS A . n 
A 1 1818 GLN 1818 1818 1818 GLN GLN A . n 
A 1 1819 ARG 1819 1819 1819 ARG ARG A . n 
A 1 1820 ASP 1820 1820 1820 ASP ASP A . n 
A 1 1821 VAL 1821 1821 1821 VAL VAL A . n 
A 1 1822 THR 1822 1822 1822 THR THR A . n 
A 1 1823 ARG 1823 1823 1823 ARG ARG A . n 
A 1 1824 SER 1824 1824 1824 SER SER A . n 
A 1 1825 LEU 1825 1825 1825 LEU LEU A . n 
A 1 1826 ILE 1826 1826 1826 ILE ILE A . n 
A 1 1827 LYS 1827 1827 1827 LYS LYS A . n 
A 1 1828 SER 1828 1828 1828 SER SER A . n 
A 1 1829 LYS 1829 1829 1829 LYS LYS A . n 
A 1 1830 ILE 1830 1830 1830 ILE ILE A . n 
A 1 1831 ASP 1831 1831 1831 ASP ASP A . n 
A 1 1832 ASN 1832 1832 1832 ASN ASN A . n 
A 1 1833 ALA 1833 1833 1833 ALA ALA A . n 
A 1 1834 LYS 1834 1834 1834 LYS LYS A . n 
A 1 1835 SER 1835 1835 1835 SER SER A . n 
A 1 1836 PHE 1836 1836 1836 PHE PHE A . n 
A 1 1837 GLU 1837 1837 1837 GLU GLU A . n 
A 1 1838 TRP 1838 1838 1838 TRP TRP A . n 
A 1 1839 LEU 1839 1839 1839 LEU LEU A . n 
A 1 1840 SER 1840 1840 1840 SER SER A . n 
A 1 1841 GLN 1841 1841 1841 GLN GLN A . n 
A 1 1842 MET 1842 1842 1842 MET MET A . n 
A 1 1843 ARG 1843 1843 1843 ARG ARG A . n 
A 1 1844 PHE 1844 1844 1844 PHE PHE A . n 
A 1 1845 TYR 1845 1845 1845 TYR TYR A . n 
A 1 1846 PHE 1846 1846 1846 PHE PHE A . n 
A 1 1847 ASP 1847 1847 1847 ASP ASP A . n 
A 1 1848 PRO 1848 1848 1848 PRO PRO A . n 
A 1 1849 LYS 1849 1849 1849 LYS LYS A . n 
A 1 1850 GLN 1850 1850 1850 GLN GLN A . n 
A 1 1851 THR 1851 1851 1851 THR THR A . n 
A 1 1852 ASP 1852 1852 1852 ASP ASP A . n 
A 1 1853 VAL 1853 1853 1853 VAL VAL A . n 
A 1 1854 LEU 1854 1854 1854 LEU LEU A . n 
A 1 1855 GLN 1855 1855 1855 GLN GLN A . n 
A 1 1856 GLN 1856 1856 1856 GLN GLN A . n 
A 1 1857 LEU 1857 1857 1857 LEU LEU A . n 
A 1 1858 SER 1858 1858 1858 SER SER A . n 
A 1 1859 ILE 1859 1859 1859 ILE ILE A . n 
A 1 1860 GLN 1860 1860 1860 GLN GLN A . n 
A 1 1861 MET 1861 1861 1861 MET MET A . n 
A 1 1862 ALA 1862 1862 1862 ALA ALA A . n 
A 1 1863 ASN 1863 1863 1863 ASN ASN A . n 
A 1 1864 ALA 1864 1864 1864 ALA ALA A . n 
A 1 1865 LYS 1865 1865 1865 LYS LYS A . n 
A 1 1866 PHE 1866 1866 1866 PHE PHE A . n 
A 1 1867 ASN 1867 1867 1867 ASN ASN A . n 
A 1 1868 TYR 1868 1868 1868 TYR TYR A . n 
A 1 1869 GLY 1869 1869 1869 GLY GLY A . n 
A 1 1870 PHE 1870 1870 1870 PHE PHE A . n 
A 1 1871 GLU 1871 1871 1871 GLU GLU A . n 
A 1 1872 TYR 1872 1872 1872 TYR TYR A . n 
A 1 1873 LEU 1873 1873 1873 LEU LEU A . n 
A 1 1874 GLY 1874 1874 1874 GLY GLY A . n 
A 1 1875 VAL 1875 1875 1875 VAL VAL A . n 
A 1 1876 GLN 1876 1876 1876 GLN GLN A . n 
A 1 1877 ASP 1877 1877 1877 ASP ASP A . n 
A 1 1878 LYS 1878 1878 1878 LYS LYS A . n 
A 1 1879 LEU 1879 1879 1879 LEU LEU A . n 
A 1 1880 VAL 1880 1880 1880 VAL VAL A . n 
A 1 1881 GLN 1881 1881 1881 GLN GLN A . n 
A 1 1882 THR 1882 1882 1882 THR THR A . n 
A 1 1883 PRO 1883 1883 1883 PRO PRO A . n 
A 1 1884 LEU 1884 1884 1884 LEU LEU A . n 
A 1 1885 THR 1885 1885 1885 THR THR A . n 
A 1 1886 ASP 1886 1886 1886 ASP ASP A . n 
A 1 1887 ARG 1887 1887 1887 ARG ARG A . n 
A 1 1888 CYS 1888 1888 1888 CYS CYS A . n 
A 1 1889 TYR 1889 1889 1889 TYR TYR A . n 
A 1 1890 LEU 1890 1890 1890 LEU LEU A . n 
A 1 1891 THR 1891 1891 1891 THR THR A . n 
A 1 1892 MET 1892 1892 1892 MET MET A . n 
A 1 1893 THR 1893 1893 1893 THR THR A . n 
A 1 1894 GLN 1894 1894 1894 GLN GLN A . n 
A 1 1895 ALA 1895 1895 1895 ALA ALA A . n 
A 1 1896 LEU 1896 1896 1896 LEU LEU A . n 
A 1 1897 GLU 1897 1897 1897 GLU GLU A . n 
A 1 1898 ALA 1898 1898 1898 ALA ALA A . n 
A 1 1899 ARG 1899 1899 1899 ARG ARG A . n 
A 1 1900 LEU 1900 1900 1900 LEU LEU A . n 
A 1 1901 GLY 1901 1901 1901 GLY GLY A . n 
A 1 1902 GLY 1902 1902 1902 GLY GLY A . n 
A 1 1903 SER 1903 1903 1903 SER SER A . n 
A 1 1904 PRO 1904 1904 1904 PRO PRO A . n 
A 1 1905 PHE 1905 1905 1905 PHE PHE A . n 
A 1 1906 GLY 1906 1906 1906 GLY GLY A . n 
A 1 1907 PRO 1907 1907 1907 PRO PRO A . n 
A 1 1908 ALA 1908 1908 1908 ALA ALA A . n 
A 1 1909 GLY 1909 1909 1909 GLY GLY A . n 
A 1 1910 THR 1910 1910 1910 THR THR A . n 
A 1 1911 GLY 1911 1911 1911 GLY GLY A . n 
A 1 1912 LYS 1912 1912 1912 LYS LYS A . n 
A 1 1913 THR 1913 1913 1913 THR THR A . n 
A 1 1914 GLU 1914 1914 1914 GLU GLU A . n 
A 1 1915 SER 1915 1915 1915 SER SER A . n 
A 1 1916 VAL 1916 1916 1916 VAL VAL A . n 
A 1 1917 LYS 1917 1917 1917 LYS LYS A . n 
A 1 1918 ALA 1918 1918 1918 ALA ALA A . n 
A 1 1919 LEU 1919 1919 1919 LEU LEU A . n 
A 1 1920 GLY 1920 1920 1920 GLY GLY A . n 
A 1 1921 HIS 1921 1921 1921 HIS HIS A . n 
A 1 1922 GLN 1922 1922 1922 GLN GLN A . n 
A 1 1923 LEU 1923 1923 1923 LEU LEU A . n 
A 1 1924 GLY 1924 1924 1924 GLY GLY A . n 
A 1 1925 ARG 1925 1925 1925 ARG ARG A . n 
A 1 1926 PHE 1926 1926 1926 PHE PHE A . n 
A 1 1927 VAL 1927 1927 1927 VAL VAL A . n 
A 1 1928 LEU 1928 1928 1928 LEU LEU A . n 
A 1 1929 VAL 1929 1929 1929 VAL VAL A . n 
A 1 1930 PHE 1930 1930 1930 PHE PHE A . n 
A 1 1931 ASN 1931 1931 1931 ASN ASN A . n 
A 1 1932 CYS 1932 1932 1932 CYS CYS A . n 
A 1 1933 ASP 1933 1933 1933 ASP ASP A . n 
A 1 1934 GLU 1934 1934 1934 GLU GLU A . n 
A 1 1935 THR 1935 1935 1935 THR THR A . n 
A 1 1936 PHE 1936 1936 1936 PHE PHE A . n 
A 1 1937 ASP 1937 1937 1937 ASP ASP A . n 
A 1 1938 PHE 1938 1938 1938 PHE PHE A . n 
A 1 1939 GLN 1939 1939 1939 GLN GLN A . n 
A 1 1940 ALA 1940 1940 1940 ALA ALA A . n 
A 1 1941 MET 1941 1941 1941 MET MET A . n 
A 1 1942 GLY 1942 1942 1942 GLY GLY A . n 
A 1 1943 ARG 1943 1943 1943 ARG ARG A . n 
A 1 1944 ILE 1944 1944 1944 ILE ILE A . n 
A 1 1945 PHE 1945 1945 1945 PHE PHE A . n 
A 1 1946 VAL 1946 1946 1946 VAL VAL A . n 
A 1 1947 GLY 1947 1947 1947 GLY GLY A . n 
A 1 1948 LEU 1948 1948 1948 LEU LEU A . n 
A 1 1949 CYS 1949 1949 1949 CYS CYS A . n 
A 1 1950 GLN 1950 1950 1950 GLN GLN A . n 
A 1 1951 VAL 1951 1951 1951 VAL VAL A . n 
A 1 1952 GLY 1952 1952 1952 GLY GLY A . n 
A 1 1953 ALA 1953 1953 1953 ALA ALA A . n 
A 1 1954 TRP 1954 1954 1954 TRP TRP A . n 
A 1 1955 GLY 1955 1955 1955 GLY GLY A . n 
A 1 1956 CYS 1956 1956 1956 CYS CYS A . n 
A 1 1957 PHE 1957 1957 1957 PHE PHE A . n 
A 1 1958 ASP 1958 1958 1958 ASP ASP A . n 
A 1 1959 GLU 1959 1959 1959 GLU GLU A . n 
A 1 1960 PHE 1960 1960 1960 PHE PHE A . n 
A 1 1961 ASN 1961 1961 1961 ASN ASN A . n 
A 1 1962 ARG 1962 1962 1962 ARG ARG A . n 
A 1 1963 LEU 1963 1963 1963 LEU LEU A . n 
A 1 1964 GLU 1964 1964 1964 GLU GLU A . n 
A 1 1965 GLU 1965 1965 1965 GLU GLU A . n 
A 1 1966 ARG 1966 1966 1966 ARG ARG A . n 
A 1 1967 MET 1967 1967 1967 MET MET A . n 
A 1 1968 LEU 1968 1968 1968 LEU LEU A . n 
A 1 1969 SER 1969 1969 1969 SER SER A . n 
A 1 1970 ALA 1970 1970 1970 ALA ALA A . n 
A 1 1971 VAL 1971 1971 1971 VAL VAL A . n 
A 1 1972 SER 1972 1972 1972 SER SER A . n 
A 1 1973 GLN 1973 1973 1973 GLN GLN A . n 
A 1 1974 GLN 1974 1974 1974 GLN GLN A . n 
A 1 1975 VAL 1975 1975 1975 VAL VAL A . n 
A 1 1976 GLN 1976 1976 1976 GLN GLN A . n 
A 1 1977 CYS 1977 1977 1977 CYS CYS A . n 
A 1 1978 ILE 1978 1978 1978 ILE ILE A . n 
A 1 1979 GLN 1979 1979 1979 GLN GLN A . n 
A 1 1980 GLU 1980 1980 1980 GLU GLU A . n 
A 1 1981 ALA 1981 1981 1981 ALA ALA A . n 
A 1 1982 LEU 1982 1982 1982 LEU LEU A . n 
A 1 1983 ARG 1983 1983 1983 ARG ARG A . n 
A 1 1984 GLU 1984 1984 1984 GLU GLU A . n 
A 1 1985 HIS 1985 1985 1985 HIS HIS A . n 
A 1 1986 SER 1986 1986 1986 SER SER A . n 
A 1 1987 ASN 1987 1987 1987 ASN ASN A . n 
A 1 1988 PRO 1988 1988 1988 PRO PRO A . n 
A 1 1989 ASN 1989 1989 1989 ASN ASN A . n 
A 1 1990 TYR 1990 1990 1990 TYR TYR A . n 
A 1 1991 ASP 1991 1991 1991 ASP ASP A . n 
A 1 1992 LYS 1992 1992 1992 LYS LYS A . n 
A 1 1993 THR 1993 1993 1993 THR THR A . n 
A 1 1994 SER 1994 1994 1994 SER SER A . n 
A 1 1995 ALA 1995 1995 1995 ALA ALA A . n 
A 1 1996 PRO 1996 1996 1996 PRO PRO A . n 
A 1 1997 ILE 1997 1997 1997 ILE ILE A . n 
A 1 1998 THR 1998 1998 1998 THR THR A . n 
A 1 1999 CYS 1999 1999 1999 CYS CYS A . n 
A 1 2000 GLU 2000 2000 2000 GLU GLU A . n 
A 1 2001 LEU 2001 2001 2001 LEU LEU A . n 
A 1 2002 LEU 2002 2002 2002 LEU LEU A . n 
A 1 2003 ASN 2003 2003 2003 ASN ASN A . n 
A 1 2004 LYS 2004 2004 2004 LYS LYS A . n 
A 1 2005 GLN 2005 2005 2005 GLN GLN A . n 
A 1 2006 VAL 2006 2006 2006 VAL VAL A . n 
A 1 2007 LYS 2007 2007 2007 LYS LYS A . n 
A 1 2008 VAL 2008 2008 2008 VAL VAL A . n 
A 1 2009 SER 2009 2009 2009 SER SER A . n 
A 1 2010 PRO 2010 2010 2010 PRO PRO A . n 
A 1 2011 ASP 2011 2011 2011 ASP ASP A . n 
A 1 2012 MET 2012 2012 2012 MET MET A . n 
A 1 2013 ALA 2013 2013 2013 ALA ALA A . n 
A 1 2014 ILE 2014 2014 2014 ILE ILE A . n 
A 1 2015 PHE 2015 2015 2015 PHE PHE A . n 
A 1 2016 ILE 2016 2016 2016 ILE ILE A . n 
A 1 2017 THR 2017 2017 2017 THR THR A . n 
A 1 2018 MET 2018 2018 2018 MET MET A . n 
A 1 2019 ASN 2019 2019 2019 ASN ASN A . n 
A 1 2020 PRO 2020 2020 2020 PRO PRO A . n 
A 1 2021 GLY 2021 2021 2021 GLY GLY A . n 
A 1 2022 TYR 2022 2022 2022 TYR TYR A . n 
A 1 2023 ALA 2023 2023 2023 ALA ALA A . n 
A 1 2024 GLY 2024 2024 2024 GLY GLY A . n 
A 1 2025 ARG 2025 2025 2025 ARG ARG A . n 
A 1 2026 SER 2026 2026 2026 SER SER 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 2115 LYS LYS A . n 
A 1 2116 GLU 2116 2116 2116 GLU GLU A . n 
A 1 2117 GLU 2117 2117 2117 GLU GLU A . n 
A 1 2118 ARG 2118 2118 2118 ARG ARG A . n 
A 1 2119 GLY 2119 2119 2119 GLY GLY A . n 
A 1 2120 GLU 2120 2120 2120 GLU GLU A . n 
A 1 2121 ALA 2121 2121 2121 ALA ALA A . n 
A 1 2122 VAL 2122 2122 2122 VAL VAL A . n 
A 1 2123 ASP 2123 2123 2123 ASP ASP A . n 
A 1 2124 GLU 2124 2124 2124 GLU GLU A . n 
A 1 2125 GLY 2125 2125 2125 GLY GLY A . n 
A 1 2126 GLU 2126 2126 2126 GLU GLU 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 MET 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 3071 SER SER A . n 
A 1 3072 SER 3072 3072 3072 SER SER A . n 
A 1 3073 GLU 3073 3073 3073 GLU GLU A . n 
A 1 3074 GLY 3074 3074 3074 GLY GLY A . n 
A 1 3075 LEU 3075 3075 3075 LEU LEU A . n 
A 1 3076 LYS 3076 3076 3076 LYS LYS A . n 
A 1 3077 ASP 3077 3077 3077 ASP ASP A . n 
A 1 3078 ARG 3078 3078 3078 ARG ARG A . n 
A 1 3079 ALA 3079 3079 3079 ALA ALA A . n 
A 1 3080 ALA 3080 3080 3080 ALA ALA A . n 
A 1 3081 THR 3081 3081 3081 THR THR 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 3221 ASP ASP A . n 
A 1 3222 LEU 3222 3222 3222 LEU LEU A . n 
A 1 3223 ARG 3223 3223 3223 ARG ARG A . n 
A 1 3224 ILE 3224 3224 3224 ILE ILE A . n 
A 1 3225 LYS 3225 3225 3225 LYS LYS A . n 
A 1 3226 SER 3226 3226 3226 SER SER A . n 
A 1 3227 GLN 3227 3227 3227 GLN GLN A . n 
A 1 3228 GLU 3228 3228 3228 GLU GLU A . n 
A 1 3229 LEU 3229 3229 3229 LEU LEU A . n 
A 1 3230 GLU 3230 3230 3230 GLU GLU A . n 
A 1 3231 VAL 3231 3231 3231 VAL VAL A . n 
A 1 3232 LYS 3232 3232 3232 LYS LYS A . n 
A 1 3233 ASN 3233 3233 3233 ASN ASN A . n 
A 1 3234 ALA 3234 3234 3234 ALA ALA A . n 
A 1 3235 ALA 3235 3235 3235 ALA ALA A . n 
A 1 3236 ALA 3236 3236 3236 ALA ALA A . n 
A 1 3237 ASN 3237 3237 3237 ASN ASN A . n 
A 1 3238 ASP 3238 3238 3238 ASP ASP A . n 
A 1 3239 LYS 3239 3239 3239 LYS LYS A . n 
A 1 3240 LEU 3240 3240 3240 LEU LEU A . n 
A 1 3241 LYS 3241 3241 3241 LYS LYS 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 3449 GLU GLU A . n 
A 1 3450 GLU 3450 3450 3450 GLU GLU A . n 
A 1 3451 TYR 3451 3451 3451 TYR TYR A . n 
A 1 3452 ALA 3452 3452 3452 ALA ALA A . n 
A 1 3453 VAL 3453 3453 3453 VAL VAL A . n 
A 1 3454 LEU 3454 3454 3454 LEU LEU A . n 
A 1 3455 ILE 3455 3455 3455 ILE ILE A . n 
A 1 3456 SER 3456 3456 3456 SER SER A . n 
A 1 3457 GLU 3457 3457 3457 GLU GLU A . n 
A 1 3458 ALA 3458 3458 3458 ALA ALA A . n 
A 1 3459 GLN 3459 3459 3459 GLN GLN A . n 
A 1 3460 ALA 3460 3460 3460 ALA ALA A . n 
A 1 3461 ILE 3461 3461 3461 ILE ILE A . n 
A 1 3462 LYS 3462 3462 3462 LYS LYS A . n 
A 1 3463 ALA 3463 3463 3463 ALA ALA A . n 
A 1 3464 ASP 3464 3464 3464 ASP ASP A . n 
A 1 3465 LEU 3465 3465 3465 LEU LEU A . n 
A 1 3466 ALA 3466 3466 3466 ALA ALA A . n 
A 1 3467 ALA 3467 3467 3467 ALA ALA A . n 
A 1 3468 VAL 3468 3468 3468 VAL VAL A . n 
A 1 3469 GLU 3469 3469 3469 GLU GLU A . n 
A 1 3470 ALA 3470 3470 3470 ALA ALA 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 ASP 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 4374 PRO PRO 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' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ADP 1 4701 4701 ADP ADP A . 
C 3 ATP 1 4702 4702 ATP ATP A . 
D 2 ADP 1 4703 4703 ADP ADP A . 
E 2 ADP 1 4704 4704 ADP ADP A . 
F 4 MG  1 4705 4705 MG  MG  A . 
G 4 MG  1 4706 4706 MG  MG  A . 
# 
_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                   9DH5 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9DH5 
_struct.title                        'State-1 of the motor domain from full-length human dynein-1 in 5mM AMPPNP with 5mM Mg2+' 
_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        9DH5 
_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 2 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_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              9DH5 
_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_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 MET A 1457 ? ASN A 1471 ? MET A 1457 ASN A 1471 1 ? 15 
HELX_P HELX_P2   AA2 GLY A 1489 ? LEU A 1509 ? GLY A 1489 LEU A 1509 1 ? 21 
HELX_P HELX_P3   AA3 SER A 1510 ? LYS A 1514 ? SER A 1510 LYS A 1514 5 ? 5  
HELX_P HELX_P4   AA4 PHE A 1516 ? SER A 1554 ? PHE A 1516 SER A 1554 1 ? 39 
HELX_P HELX_P5   AA5 ALA A 1555 ? LEU A 1561 ? ALA A 1555 LEU A 1561 1 ? 7  
HELX_P HELX_P6   AA6 LEU A 1561 ? SER A 1585 ? LEU A 1561 SER A 1585 1 ? 25 
HELX_P HELX_P7   AA7 LEU A 1587 ? ASN A 1593 ? LEU A 1587 ASN A 1593 1 ? 7  
HELX_P HELX_P8   AA8 GLY A 1596 ? ALA A 1614 ? GLY A 1596 ALA A 1614 1 ? 19 
HELX_P HELX_P9   AA9 LEU A 1615 ? PHE A 1626 ? LEU A 1615 PHE A 1626 1 ? 12 
HELX_P HELX_P10  AB1 PRO A 1627 ? VAL A 1632 ? PRO A 1627 VAL A 1632 5 ? 6  
HELX_P HELX_P11  AB2 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P12  AB3 ASN A 1646 ? LYS A 1652 ? ASN A 1646 LYS A 1652 5 ? 7  
HELX_P HELX_P13  AB4 HIS A 1653 ? PHE A 1658 ? HIS A 1653 PHE A 1658 1 ? 6  
HELX_P HELX_P14  AB5 LYS A 1697 ? GLY A 1728 ? LYS A 1697 GLY A 1728 1 ? 32 
HELX_P HELX_P15  AB6 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P16  AB7 GLN A 1746 ? MET A 1769 ? GLN A 1746 MET A 1769 1 ? 24 
HELX_P HELX_P17  AB8 GLY A 1770 ? GLY A 1772 ? GLY A 1770 GLY A 1772 5 ? 3  
HELX_P HELX_P18  AB9 PRO A 1777 ? LEU A 1797 ? PRO A 1777 LEU A 1797 1 ? 21 
HELX_P HELX_P19  AC1 PRO A 1801 ? SER A 1828 ? PRO A 1801 SER A 1828 1 ? 28 
HELX_P HELX_P20  AC2 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P21  AC3 ASP A 1852 ? GLN A 1855 ? ASP A 1852 GLN A 1855 5 ? 4  
HELX_P HELX_P22  AC4 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P23  AC5 GLY A 1911 ? LEU A 1923 ? GLY A 1911 LEU A 1923 1 ? 13 
HELX_P HELX_P24  AC6 ASP A 1937 ? GLY A 1952 ? ASP A 1937 GLY A 1952 1 ? 16 
HELX_P HELX_P25  AC7 PHE A 1960 ? LEU A 1963 ? PHE A 1960 LEU A 1963 5 ? 4  
HELX_P HELX_P26  AC8 GLU A 1964 ? ASN A 1987 ? GLU A 1964 ASN A 1987 1 ? 24 
HELX_P HELX_P27  AC9 PRO A 2029 ? LYS A 2034 ? PRO A 2029 LYS A 2034 1 ? 6  
HELX_P HELX_P28  AD1 ASP A 2045 ? GLY A 2058 ? ASP A 2045 GLY A 2058 1 ? 14 
HELX_P HELX_P29  AD2 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P30  AD3 GLY A 2089 ? GLU A 2117 ? GLY A 2089 GLU A 2117 1 ? 29 
HELX_P HELX_P31  AD4 ASP A 2123 ? ASN A 2130 ? ASP A 2123 ASN A 2130 1 ? 8  
HELX_P HELX_P32  AD5 PRO A 2132 ? VAL A 2146 ? PRO A 2132 VAL A 2146 1 ? 15 
HELX_P HELX_P33  AD6 PRO A 2147 ? LEU A 2149 ? PRO A 2147 LEU A 2149 5 ? 3  
HELX_P HELX_P34  AD7 VAL A 2150 ? GLU A 2152 ? VAL A 2150 GLU A 2152 5 ? 3  
HELX_P HELX_P35  AD8 ASP A 2153 ? PHE A 2165 ? ASP A 2153 PHE A 2165 1 ? 13 
HELX_P HELX_P36  AD9 MET A 2175 ? MET A 2189 ? MET A 2175 MET A 2189 1 ? 15 
HELX_P HELX_P37  AE1 GLY A 2200 ? GLN A 2215 ? GLY A 2200 GLN A 2215 1 ? 16 
HELX_P HELX_P38  AE2 GLY A 2229 ? GLY A 2246 ? GLY A 2229 GLY A 2246 1 ? 18 
HELX_P HELX_P39  AE3 ASP A 2255 ? ILE A 2259 ? ASP A 2255 ILE A 2259 5 ? 5  
HELX_P HELX_P40  AE4 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P41  AE5 GLY A 2278 ? SER A 2290 ? GLY A 2278 SER A 2290 1 ? 13 
HELX_P HELX_P42  AE6 GLY A 2293 ? LYS A 2297 ? GLY A 2293 LYS A 2297 5 ? 5  
HELX_P HELX_P43  AE7 ASP A 2308 ? GLU A 2313 ? ASP A 2308 GLU A 2313 1 ? 6  
HELX_P HELX_P44  AE8 LEU A 2315 ? ASP A 2320 ? LEU A 2315 ASP A 2320 1 ? 6  
HELX_P HELX_P45  AE9 THR A 2352 ? ARG A 2358 ? THR A 2352 ARG A 2358 1 ? 7  
HELX_P HELX_P46  AF1 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P47  AF2 PRO A 2411 ? GLN A 2424 ? PRO A 2411 GLN A 2424 1 ? 14 
HELX_P HELX_P48  AF3 PRO A 2425 ? THR A 2428 ? PRO A 2425 THR A 2428 5 ? 4  
HELX_P HELX_P49  AF4 GLY A 2431 ? LEU A 2443 ? GLY A 2431 LEU A 2443 1 ? 13 
HELX_P HELX_P50  AF5 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P51  AF6 GLN A 2482 ? GLY A 2504 ? GLN A 2482 GLY A 2504 1 ? 23 
HELX_P HELX_P52  AF7 ARG A 2507 ? THR A 2522 ? ARG A 2507 THR A 2522 1 ? 16 
HELX_P HELX_P53  AF8 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P54  AF9 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P55  AG1 GLU A 2558 ? VAL A 2562 ? GLU A 2558 VAL A 2562 5 ? 5  
HELX_P HELX_P56  AG2 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P57  AG3 GLY A 2600 ? ALA A 2611 ? GLY A 2600 ALA A 2611 1 ? 12 
HELX_P HELX_P58  AG4 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P59  AG5 GLN A 2677 ? HIS A 2689 ? GLN A 2677 HIS A 2689 1 ? 13 
HELX_P HELX_P60  AG6 SER A 2724 ? ARG A 2729 ? SER A 2724 ARG A 2729 1 ? 6  
HELX_P HELX_P61  AG7 GLY A 2740 ? LEU A 2756 ? GLY A 2740 LEU A 2756 1 ? 17 
HELX_P HELX_P62  AG8 ARG A 2757 ? LEU A 2758 ? ARG A 2757 LEU A 2758 5 ? 2  
HELX_P HELX_P63  AG9 ILE A 2759 ? THR A 2764 ? ILE A 2759 THR A 2764 5 ? 6  
HELX_P HELX_P64  AH1 TYR A 2765 ? PHE A 2784 ? TYR A 2765 PHE A 2784 1 ? 20 
HELX_P HELX_P65  AH2 SER A 2795 ? ALA A 2809 ? SER A 2795 ALA A 2809 1 ? 15 
HELX_P HELX_P66  AH3 PRO A 2817 ? GLN A 2834 ? PRO A 2817 GLN A 2834 1 ? 18 
HELX_P HELX_P67  AH4 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P68  AH5 ASP A 2862 ? SER A 2868 ? ASP A 2862 SER A 2868 1 ? 7  
HELX_P HELX_P69  AH6 ASP A 2885 ? GLU A 2904 ? ASP A 2885 GLU A 2904 1 ? 20 
HELX_P HELX_P70  AH7 PHE A 2912 ? ARG A 2927 ? PHE A 2912 ARG A 2927 1 ? 16 
HELX_P HELX_P71  AH8 GLY A 2942 ? ASN A 2954 ? GLY A 2942 ASN A 2954 1 ? 13 
HELX_P HELX_P72  AH9 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P73  AI1 SER A 2997 ? VAL A 2999 ? SER A 2997 VAL A 2999 5 ? 3  
HELX_P HELX_P74  AI2 ASP A 3001 ? GLY A 3015 ? ASP A 3001 GLY A 3015 1 ? 15 
HELX_P HELX_P75  AI3 GLY A 3023 ? GLU A 3040 ? GLY A 3023 GLU A 3040 1 ? 18 
HELX_P HELX_P76  AI4 SER A 3046 ? ASN A 3061 ? SER A 3046 ASN A 3061 1 ? 16 
HELX_P HELX_P77  AI5 SER A 3071 ? SER A 3082 ? SER A 3071 SER A 3082 1 ? 12 
HELX_P HELX_P78  AI6 PRO A 3083 ? ARG A 3088 ? PRO A 3083 ARG A 3088 1 ? 6  
HELX_P HELX_P79  AI7 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P80  AI8 SER A 3138 ? ARG A 3164 ? SER A 3138 ARG A 3164 1 ? 27 
HELX_P HELX_P81  AI9 THR A 3172 ? LYS A 3241 ? THR A 3172 LYS A 3241 1 ? 70 
HELX_P HELX_P82  AJ1 GLU A 3450 ? LEU A 3482 ? GLU A 3450 LEU A 3482 1 ? 33 
HELX_P HELX_P83  AJ2 LEU A 3482 ? THR A 3495 ? LEU A 3482 THR A 3495 1 ? 14 
HELX_P HELX_P84  AJ3 THR A 3495 ? ALA A 3517 ? THR A 3495 ALA A 3517 1 ? 23 
HELX_P HELX_P85  AJ4 GLY A 3518 ? PHE A 3520 ? GLY A 3518 PHE A 3520 5 ? 3  
HELX_P HELX_P86  AJ5 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P87  AJ6 ALA A 3548 ? LEU A 3553 ? ALA A 3548 LEU A 3553 1 ? 6  
HELX_P HELX_P88  AJ7 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P89  AJ8 ASP A 3570 ? PHE A 3583 ? ASP A 3570 PHE A 3583 1 ? 14 
HELX_P HELX_P90  AJ9 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P91  AK1 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P92  AK2 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P93  AK3 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P94  AK4 LEU A 3645 ? ASN A 3650 ? LEU A 3645 ASN A 3650 1 ? 6  
HELX_P HELX_P95  AK5 PRO A 3689 ? ARG A 3695 ? PRO A 3689 ARG A 3695 1 ? 7  
HELX_P HELX_P96  AK6 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P97  AK7 ARG A 3721 ? VAL A 3756 ? ARG A 3721 VAL A 3756 1 ? 36 
HELX_P HELX_P98  AK8 ASP A 3763 ? GLN A 3799 ? ASP A 3763 GLN A 3799 1 ? 37 
HELX_P HELX_P99  AK9 TYR A 3801 ? SER A 3817 ? TYR A 3801 SER A 3817 1 ? 17 
HELX_P HELX_P100 AL1 LEU A 3818 ? ILE A 3821 ? LEU A 3818 ILE A 3821 5 ? 4  
HELX_P HELX_P101 AL2 SER A 3828 ? GLU A 3842 ? SER A 3828 GLU A 3842 1 ? 15 
HELX_P HELX_P102 AL3 ASN A 3843 ? LYS A 3847 ? ASN A 3843 LYS A 3847 5 ? 5  
HELX_P HELX_P103 AL4 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P104 AL5 GLY A 3874 ? MET A 3875 ? GLY A 3874 MET A 3875 5 ? 2  
HELX_P HELX_P105 AL6 LEU A 3876 ? GLN A 3878 ? LEU A 3876 GLN A 3878 5 ? 3  
HELX_P HELX_P106 AL7 ASP A 3879 ? THR A 3895 ? ASP A 3879 THR A 3895 1 ? 17 
HELX_P HELX_P107 AL8 TYR A 3901 ? LEU A 3909 ? TYR A 3901 LEU A 3909 1 ? 9  
HELX_P HELX_P108 AL9 THR A 3928 ? SER A 3939 ? THR A 3928 SER A 3939 1 ? 12 
HELX_P HELX_P109 AM1 ASP A 3946 ? ASP A 3954 ? ASP A 3946 ASP A 3954 1 ? 9  
HELX_P HELX_P110 AM2 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P111 AM3 SER A 3965 ? THR A 3969 ? SER A 3965 THR A 3969 5 ? 5  
HELX_P HELX_P112 AM4 THR A 3981 ? ARG A 3997 ? THR A 3981 ARG A 3997 1 ? 17 
HELX_P HELX_P113 AM5 ARG A 4000 ? GLY A 4014 ? ARG A 4000 GLY A 4014 1 ? 15 
HELX_P HELX_P114 AM6 MET A 4018 ? GLN A 4023 ? MET A 4018 GLN A 4023 5 ? 6  
HELX_P HELX_P115 AM7 ASP A 4026 ? GLU A 4034 ? ASP A 4026 GLU A 4034 1 ? 9  
HELX_P HELX_P116 AM8 ALA A 4051 ? ASN A 4063 ? ALA A 4051 ASN A 4063 1 ? 13 
HELX_P HELX_P117 AM9 SER A 4073 ? VAL A 4088 ? SER A 4073 VAL A 4088 1 ? 16 
HELX_P HELX_P118 AN1 ASN A 4098 ? LEU A 4101 ? ASN A 4098 LEU A 4101 5 ? 4  
HELX_P HELX_P119 AN2 ALA A 4102 ? SER A 4115 ? ALA A 4102 SER A 4115 1 ? 14 
HELX_P HELX_P120 AN3 PRO A 4135 ? GLY A 4142 ? PRO A 4135 GLY A 4142 1 ? 8  
HELX_P HELX_P121 AN4 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P122 AN5 PRO A 4165 ? CYS A 4170 ? PRO A 4165 CYS A 4170 1 ? 6  
HELX_P HELX_P123 AN6 GLU A 4175 ? LEU A 4194 ? GLU A 4175 LEU A 4194 1 ? 20 
HELX_P HELX_P124 AN7 TYR A 4196 ? TRP A 4201 ? TYR A 4196 TRP A 4201 1 ? 6  
HELX_P HELX_P125 AN8 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P126 AN9 SER A 4234 ? ILE A 4238 ? SER A 4234 ILE A 4238 5 ? 5  
HELX_P HELX_P127 AO1 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P128 AO2 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P129 AO3 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P130 AO4 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P131 AO5 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
HELX_P HELX_P132 AO6 PRO A 4324 ? ALA A 4327 ? PRO A 4324 ALA A 4327 5 ? 4  
HELX_P HELX_P133 AO7 GLU A 4328 ? GLN A 4347 ? GLU A 4328 GLN A 4347 1 ? 20 
HELX_P HELX_P134 AO8 ALA A 4375 ? ILE A 4391 ? ALA A 4375 ILE A 4391 1 ? 17 
HELX_P HELX_P135 AO9 THR A 4401 ? LYS A 4406 ? THR A 4401 LYS A 4406 1 ? 6  
HELX_P HELX_P136 AP1 ASP A 4407 ? GLU A 4439 ? ASP A 4407 GLU A 4439 1 ? 33 
HELX_P HELX_P137 AP2 THR A 4445 ? GLY A 4458 ? THR A 4445 GLY A 4458 1 ? 14 
HELX_P HELX_P138 AP3 THR A 4474 ? SER A 4498 ? THR A 4474 SER A 4498 1 ? 25 
HELX_P HELX_P139 AP4 GLY A 4500 ? LYS A 4505 ? GLY A 4500 LYS A 4505 5 ? 6  
HELX_P HELX_P140 AP5 VAL A 4516 ? ASN A 4532 ? VAL A 4516 ASN A 4532 1 ? 17 
HELX_P HELX_P141 AP6 SER A 4535 ? GLU A 4537 ? SER A 4535 GLU A 4537 5 ? 3  
HELX_P HELX_P142 AP7 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_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A THR 1913 OG1 ? ? ? 1_555 F MG . MG ? ? A THR 1913 A MG 4705 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc2 metalc ? ? A SER 2231 OG  ? ? ? 1_555 G MG . MG ? ? A SER 2231 A MG 4706 1_555 ? ? ? ? ? ? ? 1.959 ? ? 
metalc3 metalc ? ? A GLU 2344 OE2 ? ? ? 1_555 G MG . MG ? ? A GLU 2344 A MG 4706 1_555 ? ? ? ? ? ? ? 1.745 ? ? 
metalc4 metalc ? ? B ADP .    O3B ? ? ? 1_555 F MG . MG ? ? A ADP 4701 A MG 4705 1_555 ? ? ? ? ? ? ? 2.103 ? ? 
metalc5 metalc ? ? C ATP .    O2G ? ? ? 1_555 G MG . MG ? ? A ATP 4702 A MG 4706 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc6 metalc ? ? C ATP .    O2B ? ? ? 1_555 G MG . MG ? ? A ATP 4702 A MG 4706 1_555 ? ? ? ? ? ? ? 2.138 ? ? 
metalc7 metalc ? ? C ATP .    O3B ? ? ? 1_555 G MG . MG ? ? A ATP 4702 A MG 4706 1_555 ? ? ? ? ? ? ? 2.957 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O3B ? B ADP .    ? A ADP 4701 ? 1_555 91.0  ? 
2  OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 89.2  ? 
3  OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 169.2 ? 
4  OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 89.0  ? 
5  OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 89.1  ? 
6  OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 101.3 ? 
7  O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 101.6 ? 
8  OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? C ATP .    ? A ATP 4702 ? 1_555 132.3 ? 
9  OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? C ATP .    ? A ATP 4702 ? 1_555 126.0 ? 
10 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? C ATP .    ? A ATP 4702 ? 1_555 56.1  ? 
11 O2B ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? C ATP .    ? A ATP 4702 ? 1_555 56.2  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 2 ? 
AB5 ? 5 ? 
AB6 ? 5 ? 
AB7 ? 3 ? 
AB8 ? 5 ? 
AB9 ? 2 ? 
AC1 ? 4 ? 
AC2 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? parallel      
AB2 3 4 ? parallel      
AB2 4 5 ? parallel      
AB3 1 2 ? anti-parallel 
AB3 2 3 ? parallel      
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? parallel      
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB6 4 5 ? parallel      
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB8 1 2 ? parallel      
AB8 2 3 ? parallel      
AB8 3 4 ? parallel      
AB8 4 5 ? parallel      
AB9 1 2 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? parallel      
AC2 3 4 ? anti-parallel 
AC2 4 5 ? parallel      
AC2 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 1477 ? TYR A 1480 ? LEU A 1477 TYR A 1480 
AA1 2 CYS A 1484 ? ILE A 1487 ? CYS A 1484 ILE A 1487 
AA2 1 SER A 1663 ? LEU A 1666 ? SER A 1663 LEU A 1666 
AA2 2 VAL A 1672 ? SER A 1677 ? VAL A 1672 SER A 1677 
AA2 3 GLU A 1683 ? SER A 1691 ? GLU A 1683 SER A 1691 
AA3 1 MET A 1842 ? PHE A 1846 ? MET A 1842 PHE A 1846 
AA3 2 LEU A 1857 ? MET A 1861 ? LEU A 1857 MET A 1861 
AA3 3 ALA A 1864 ? ASN A 1867 ? ALA A 1864 ASN A 1867 
AA4 1 GLY A 1901 ? PHE A 1905 ? GLY A 1901 PHE A 1905 
AA4 2 PHE A 2036 ? ALA A 2040 ? PHE A 2036 ALA A 2040 
AA5 1 VAL A 1927 ? ASN A 1931 ? VAL A 1927 ASN A 1931 
AA5 2 TRP A 1954 ? ASP A 1958 ? TRP A 1954 ASP A 1958 
AA5 3 ALA A 2013 ? THR A 2017 ? ALA A 2013 THR A 2017 
AA6 1 THR A 1998 ? LEU A 2001 ? THR A 1998 LEU A 2001 
AA6 2 LYS A 2004 ? LYS A 2007 ? LYS A 2004 LYS A 2007 
AA7 1 GLY A 2249 ? ILE A 2254 ? GLY A 2249 ILE A 2254 
AA7 2 ARG A 2298 ? ASP A 2304 ? ARG A 2298 ASP A 2304 
AA7 3 VAL A 2339 ? VAL A 2345 ? VAL A 2339 VAL A 2345 
AA7 4 GLY A 2219 ? VAL A 2223 ? GLY A 2219 VAL A 2223 
AA7 5 GLY A 2360 ? TRP A 2363 ? GLY A 2360 TRP A 2363 
AA8 1 GLY A 2266 ? LEU A 2268 ? GLY A 2266 LEU A 2268 
AA8 2 TRP A 2275 ? ASP A 2277 ? TRP A 2275 ASP A 2277 
AA9 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AA9 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AB1 1 TYR A 2537 ? VAL A 2539 ? TYR A 2537 VAL A 2539 
AB1 2 TRP A 2545 ? PRO A 2547 ? TRP A 2545 PRO A 2547 
AB2 1 MET A 2615 ? LEU A 2620 ? MET A 2615 LEU A 2620 
AB2 2 TRP A 2658 ? CYS A 2663 ? TRP A 2658 CYS A 2663 
AB2 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB2 4 LEU A 2591 ? CYS A 2594 ? LEU A 2591 CYS A 2594 
AB2 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB3 1 CYS A 2639 ? THR A 2644 ? CYS A 2639 THR A 2644 
AB3 2 GLY A 2647 ? PRO A 2652 ? GLY A 2647 PRO A 2652 
AB3 3 THR A 2699 ? LEU A 2703 ? THR A 2699 LEU A 2703 
AB3 4 GLY A 2691 ? ARG A 2694 ? GLY A 2691 ARG A 2694 
AB4 1 TYR A 2873 ? SER A 2874 ? TYR A 2873 SER A 2874 
AB4 2 ILE A 2882 ? PRO A 2883 ? ILE A 2882 PRO A 2883 
AB5 1 SER A 2957 ? TYR A 2959 ? SER A 2957 TYR A 2959 
AB5 2 ILE A 2990 ? ASP A 2995 ? ILE A 2990 ASP A 2995 
AB5 3 LEU A 3062 ? MET A 3068 ? LEU A 3062 MET A 3068 
AB5 4 HIS A 2932 ? GLY A 2937 ? HIS A 2932 GLY A 2937 
AB5 5 CYS A 3089 ? GLY A 3095 ? CYS A 3089 GLY A 3095 
AB6 1 THR A 3610 ? SER A 3613 ? THR A 3610 SER A 3613 
AB6 2 PRO A 3632 ? GLN A 3636 ? PRO A 3632 GLN A 3636 
AB6 3 VAL A 3676 ? THR A 3681 ? VAL A 3676 THR A 3681 
AB6 4 TYR A 3586 ? ILE A 3590 ? TYR A 3586 ILE A 3590 
AB6 5 VAL A 3696 ? ASN A 3700 ? VAL A 3696 ASN A 3700 
AB7 1 VAL A 3653 ? THR A 3656 ? VAL A 3653 THR A 3656 
AB7 2 ARG A 3659 ? LEU A 3664 ? ARG A 3659 LEU A 3664 
AB7 3 GLN A 3667 ? ASP A 3670 ? GLN A 3667 ASP A 3670 
AB8 1 ILE A 4066 ? ALA A 4070 ? ILE A 4066 ALA A 4070 
AB8 2 TRP A 4093 ? LYS A 4097 ? TRP A 4093 LYS A 4097 
AB8 3 ARG A 4123 ? GLU A 4129 ? ARG A 4123 GLU A 4129 
AB8 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB8 5 ARG A 4143 ? PHE A 4147 ? ARG A 4143 PHE A 4147 
AB9 1 LYS A 4283 ? ALA A 4285 ? LYS A 4283 ALA A 4285 
AB9 2 ILE A 4294 ? GLN A 4295 ? ILE A 4294 GLN A 4295 
AC1 1 VAL A 4509 ? CYS A 4510 ? VAL A 4509 CYS A 4510 
AC1 2 SER A 4557 ? THR A 4561 ? SER A 4557 THR A 4561 
AC1 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AC1 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AC2 1 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
AC2 2 LYS A 4574 ? ALA A 4584 ? LYS A 4574 ALA A 4584 
AC2 3 LEU A 4618 ? ILE A 4626 ? LEU A 4618 ILE A 4626 
AC2 4 VAL A 4604 ? TYR A 4610 ? VAL A 4604 TYR A 4610 
AC2 5 ALA A 4641 ? LEU A 4643 ? ALA A 4641 LEU A 4643 
AC2 6 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 1478 ? N VAL A 1478 O LEU A 1486 ? O LEU A 1486 
AA2 1 2 N SER A 1663 ? N SER A 1663 O SER A 1677 ? O SER A 1677 
AA2 2 3 N VAL A 1673 ? N VAL A 1673 O VAL A 1690 ? O VAL A 1690 
AA3 1 2 N ARG A 1843 ? N ARG A 1843 O GLN A 1860 ? O GLN A 1860 
AA3 2 3 N ILE A 1859 ? N ILE A 1859 O PHE A 1866 ? O PHE A 1866 
AA4 1 2 N GLY A 1901 ? N GLY A 1901 O ARG A 2037 ? O ARG A 2037 
AA5 1 2 N LEU A 1928 ? N LEU A 1928 O CYS A 1956 ? O CYS A 1956 
AA5 2 3 N PHE A 1957 ? N PHE A 1957 O PHE A 2015 ? O PHE A 2015 
AA6 1 2 N CYS A 1999 ? N CYS A 1999 O VAL A 2006 ? O VAL A 2006 
AA7 1 2 N ILE A 2254 ? N ILE A 2254 O VAL A 2302 ? O VAL A 2302 
AA7 2 3 N PHE A 2303 ? N PHE A 2303 O MET A 2342 ? O MET A 2342 
AA7 3 4 O PHE A 2343 ? O PHE A 2343 N MET A 2222 ? N MET A 2222 
AA7 4 5 N MET A 2221 ? N MET A 2221 O GLY A 2360 ? O GLY A 2360 
AA8 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA9 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AB1 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB2 1 2 N LEU A 2620 ? N LEU A 2620 O PHE A 2662 ? O PHE A 2662 
AB2 2 3 N CYS A 2663 ? N CYS A 2663 O ALA A 2711 ? O ALA A 2711 
AB2 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 2591 ? N LEU A 2591 
AB2 4 5 N CYS A 2594 ? N CYS A 2594 O VAL A 2734 ? O VAL A 2734 
AB3 1 2 N GLU A 2640 ? N GLU A 2640 O ALA A 2651 ? O ALA A 2651 
AB3 2 3 N LEU A 2650 ? N LEU A 2650 O LYS A 2702 ? O LYS A 2702 
AB3 3 4 O VAL A 2701 ? O VAL A 2701 N PHE A 2692 ? N PHE A 2692 
AB4 1 2 N SER A 2874 ? N SER A 2874 O ILE A 2882 ? O ILE A 2882 
AB5 1 2 N SER A 2957 ? N SER A 2957 O ALA A 2991 ? O ALA A 2991 
AB5 2 3 N PHE A 2992 ? N PHE A 2992 O HIS A 3063 ? O HIS A 3063 
AB5 3 4 O PHE A 3066 ? O PHE A 3066 N LEU A 2933 ? N LEU A 2933 
AB5 4 5 N HIS A 2932 ? N HIS A 2932 O VAL A 3090 ? O VAL A 3090 
AB6 1 2 N THR A 3612 ? N THR A 3612 O LEU A 3634 ? O LEU A 3634 
AB6 2 3 N VAL A 3635 ? N VAL A 3635 O PHE A 3678 ? O PHE A 3678 
AB6 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB6 4 5 N LEU A 3588 ? N LEU A 3588 O THR A 3697 ? O THR A 3697 
AB7 1 2 N ARG A 3654 ? N ARG A 3654 O LEU A 3661 ? O LEU A 3661 
AB7 2 3 N ILE A 3662 ? N ILE A 3662 O ILE A 3669 ? O ILE A 3669 
AB8 1 2 N THR A 4067 ? N THR A 4067 O MET A 4095 ? O MET A 4095 
AB8 2 3 N LEU A 4096 ? N LEU A 4096 O THR A 4127 ? O THR A 4127 
AB8 3 4 O LEU A 4126 ? O LEU A 4126 N MET A 4043 ? N MET A 4043 
AB8 4 5 N CYS A 4044 ? N CYS A 4044 O PHE A 4147 ? O PHE A 4147 
AB9 1 2 N ALA A 4285 ? N ALA A 4285 O ILE A 4294 ? O ILE A 4294 
AC1 1 2 N VAL A 4509 ? N VAL A 4509 O THR A 4561 ? O THR A 4561 
AC1 2 3 N PHE A 4558 ? N PHE A 4558 O LEU A 4590 ? O LEU A 4590 
AC1 3 4 O GLN A 4589 ? O GLN A 4589 N ASN A 4544 ? N ASN A 4544 
AC2 1 2 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
AC2 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AC2 3 4 O ILE A 4619 ? O ILE A 4619 N VAL A 4609 ? N VAL A 4609 
AC2 4 5 N TYR A 4610 ? N TYR A 4610 O VAL A 4642 ? O VAL A 4642 
AC2 5 6 O ALA A 4641 ? O ALA A 4641 N GLN A 4566 ? N GLN A 4566 
# 
_pdbx_entry_details.entry_id                   9DH5 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    2629 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   NZ 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   LYS 
_pdbx_validate_close_contact.auth_seq_id_2    2633 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.12 
# 
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 ASN A 1643 ? ? -99.36  32.64   
2  1 ASN A 1670 ? ? 71.11   33.12   
3  1 ALA A 1862 ? ? 58.11   -121.49 
4  1 THR A 2061 ? ? -99.14  38.36   
5  1 ALA A 2121 ? ? -98.97  37.02   
6  1 ASN A 2130 ? ? -101.16 75.71   
7  1 PRO A 2796 ? ? -59.73  -9.10   
8  1 SER A 3640 ? ? -103.10 40.37   
9  1 PRO A 3643 ? ? -66.61  2.25    
10 1 ARG A 3910 ? ? 52.77   -98.40  
11 1 ASP A 3946 ? ? -95.57  53.19   
12 1 GLU A 3977 ? ? -95.11  -60.67  
13 1 CYS A 4170 ? ? -90.33  30.17   
14 1 ALA A 4197 ? ? -20.69  -67.74  
15 1 GLU A 4206 ? ? -95.65  59.19   
16 1 TYR A 4252 ? ? 75.12   -9.71   
17 1 ASP A 4298 ? ? -92.17  48.95   
18 1 ASP A 4314 ? ? -90.65  31.07   
19 1 ASN A 4597 ? ? 35.06   47.87   
20 1 GLU A 4599 ? ? 59.28   -162.49 
21 1 ALA A 4602 ? ? 65.23   -0.59   
22 1 THR A 4628 ? ? 52.01   -142.77 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     4195 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.118 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9DH5 
_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                    9DH5 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   'BACK PROJECTION' 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.6 
_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               301002 
_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, 5 mM MgCl2, 5 mM DTT, 5 mM AMPPNP' 
_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-1 of the motor domain from full-length human dynein-1 in 5mM AMPPNP with 5mM Mg2+' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9DH5 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS GLACIOS' 
_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            200 
_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           45000 
_em_imaging.calibrated_magnification        45000 
_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              9DH5 
_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                9DH5 
_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 GLU 2389 ? A GLU 2389 
1458 1 Y 1 A GLY 2390 ? A GLY 2390 
1459 1 Y 1 A GLU 2391 ? A GLU 2391 
1460 1 Y 1 A ASP 2392 ? A ASP 2392 
1461 1 Y 1 A GLU 2393 ? A GLU 2393 
1462 1 Y 1 A ALA 2394 ? A ALA 2394 
1463 1 Y 1 A GLN 2395 ? A GLN 2395 
1464 1 Y 1 A ARG 2396 ? A ARG 2396 
1465 1 Y 1 A ARG 2397 ? A ARG 2397 
1466 1 Y 1 A ARG 2398 ? A ARG 2398 
1467 1 Y 1 A LYS 2399 ? A LYS 2399 
1468 1 Y 1 A GLY 2400 ? A GLY 2400 
1469 1 Y 1 A LYS 2401 ? A LYS 2401 
1470 1 Y 1 A GLU 2402 ? A GLU 2402 
1471 1 Y 1 A ASP 2403 ? A ASP 2403 
1472 1 Y 1 A GLU 2404 ? A GLU 2404 
1473 1 Y 1 A GLY 2405 ? A GLY 2405 
1474 1 Y 1 A GLU 2406 ? A GLU 2406 
1475 1 Y 1 A GLU 2407 ? A GLU 2407 
1476 1 Y 1 A ALA 2408 ? A ALA 2408 
1477 1 Y 1 A ALA 2409 ? A ALA 2409 
1478 1 Y 1 A LYS 3242 ? A LYS 3242 
1479 1 Y 1 A MET 3243 ? A MET 3243 
1480 1 Y 1 A VAL 3244 ? A VAL 3244 
1481 1 Y 1 A LYS 3245 ? A LYS 3245 
1482 1 Y 1 A ASP 3246 ? A ASP 3246 
1483 1 Y 1 A GLN 3247 ? A GLN 3247 
1484 1 Y 1 A GLN 3248 ? A GLN 3248 
1485 1 Y 1 A GLU 3249 ? A GLU 3249 
1486 1 Y 1 A ALA 3250 ? A ALA 3250 
1487 1 Y 1 A GLU 3251 ? A GLU 3251 
1488 1 Y 1 A LYS 3252 ? A LYS 3252 
1489 1 Y 1 A LYS 3253 ? A LYS 3253 
1490 1 Y 1 A LYS 3254 ? A LYS 3254 
1491 1 Y 1 A VAL 3255 ? A VAL 3255 
1492 1 Y 1 A MET 3256 ? A MET 3256 
1493 1 Y 1 A SER 3257 ? A SER 3257 
1494 1 Y 1 A GLN 3258 ? A GLN 3258 
1495 1 Y 1 A GLU 3259 ? A GLU 3259 
1496 1 Y 1 A ILE 3260 ? A ILE 3260 
1497 1 Y 1 A GLN 3261 ? A GLN 3261 
1498 1 Y 1 A GLU 3262 ? A GLU 3262 
1499 1 Y 1 A GLN 3263 ? A GLN 3263 
1500 1 Y 1 A LEU 3264 ? A LEU 3264 
1501 1 Y 1 A HIS 3265 ? A HIS 3265 
1502 1 Y 1 A LYS 3266 ? A LYS 3266 
1503 1 Y 1 A GLN 3267 ? A GLN 3267 
1504 1 Y 1 A GLN 3268 ? A GLN 3268 
1505 1 Y 1 A GLU 3269 ? A GLU 3269 
1506 1 Y 1 A VAL 3270 ? A VAL 3270 
1507 1 Y 1 A ILE 3271 ? A ILE 3271 
1508 1 Y 1 A ALA 3272 ? A ALA 3272 
1509 1 Y 1 A ASP 3273 ? A ASP 3273 
1510 1 Y 1 A LYS 3274 ? A LYS 3274 
1511 1 Y 1 A GLN 3275 ? A GLN 3275 
1512 1 Y 1 A MET 3276 ? A MET 3276 
1513 1 Y 1 A SER 3277 ? A SER 3277 
1514 1 Y 1 A VAL 3278 ? A VAL 3278 
1515 1 Y 1 A LYS 3279 ? A LYS 3279 
1516 1 Y 1 A GLU 3280 ? A GLU 3280 
1517 1 Y 1 A ASP 3281 ? A ASP 3281 
1518 1 Y 1 A LEU 3282 ? A LEU 3282 
1519 1 Y 1 A ASP 3283 ? A ASP 3283 
1520 1 Y 1 A LYS 3284 ? A LYS 3284 
1521 1 Y 1 A VAL 3285 ? A VAL 3285 
1522 1 Y 1 A GLU 3286 ? A GLU 3286 
1523 1 Y 1 A PRO 3287 ? A PRO 3287 
1524 1 Y 1 A ALA 3288 ? A ALA 3288 
1525 1 Y 1 A VAL 3289 ? A VAL 3289 
1526 1 Y 1 A ILE 3290 ? A ILE 3290 
1527 1 Y 1 A GLU 3291 ? A GLU 3291 
1528 1 Y 1 A ALA 3292 ? A ALA 3292 
1529 1 Y 1 A GLN 3293 ? A GLN 3293 
1530 1 Y 1 A ASN 3294 ? A ASN 3294 
1531 1 Y 1 A ALA 3295 ? A ALA 3295 
1532 1 Y 1 A VAL 3296 ? A VAL 3296 
1533 1 Y 1 A LYS 3297 ? A LYS 3297 
1534 1 Y 1 A SER 3298 ? A SER 3298 
1535 1 Y 1 A ILE 3299 ? A ILE 3299 
1536 1 Y 1 A LYS 3300 ? A LYS 3300 
1537 1 Y 1 A LYS 3301 ? A LYS 3301 
1538 1 Y 1 A GLN 3302 ? A GLN 3302 
1539 1 Y 1 A HIS 3303 ? A HIS 3303 
1540 1 Y 1 A LEU 3304 ? A LEU 3304 
1541 1 Y 1 A VAL 3305 ? A VAL 3305 
1542 1 Y 1 A GLU 3306 ? A GLU 3306 
1543 1 Y 1 A VAL 3307 ? A VAL 3307 
1544 1 Y 1 A ARG 3308 ? A ARG 3308 
1545 1 Y 1 A SER 3309 ? A SER 3309 
1546 1 Y 1 A MET 3310 ? A MET 3310 
1547 1 Y 1 A ALA 3311 ? A ALA 3311 
1548 1 Y 1 A ASN 3312 ? A ASN 3312 
1549 1 Y 1 A PRO 3313 ? A PRO 3313 
1550 1 Y 1 A PRO 3314 ? A PRO 3314 
1551 1 Y 1 A ALA 3315 ? A ALA 3315 
1552 1 Y 1 A ALA 3316 ? A ALA 3316 
1553 1 Y 1 A VAL 3317 ? A VAL 3317 
1554 1 Y 1 A LYS 3318 ? A LYS 3318 
1555 1 Y 1 A LEU 3319 ? A LEU 3319 
1556 1 Y 1 A ALA 3320 ? A ALA 3320 
1557 1 Y 1 A LEU 3321 ? A LEU 3321 
1558 1 Y 1 A GLU 3322 ? A GLU 3322 
1559 1 Y 1 A SER 3323 ? A SER 3323 
1560 1 Y 1 A ILE 3324 ? A ILE 3324 
1561 1 Y 1 A CYS 3325 ? A CYS 3325 
1562 1 Y 1 A LEU 3326 ? A LEU 3326 
1563 1 Y 1 A LEU 3327 ? A LEU 3327 
1564 1 Y 1 A LEU 3328 ? A LEU 3328 
1565 1 Y 1 A GLY 3329 ? A GLY 3329 
1566 1 Y 1 A GLU 3330 ? A GLU 3330 
1567 1 Y 1 A SER 3331 ? A SER 3331 
1568 1 Y 1 A THR 3332 ? A THR 3332 
1569 1 Y 1 A THR 3333 ? A THR 3333 
1570 1 Y 1 A ASP 3334 ? A ASP 3334 
1571 1 Y 1 A TRP 3335 ? A TRP 3335 
1572 1 Y 1 A LYS 3336 ? A LYS 3336 
1573 1 Y 1 A GLN 3337 ? A GLN 3337 
1574 1 Y 1 A ILE 3338 ? A ILE 3338 
1575 1 Y 1 A ARG 3339 ? A ARG 3339 
1576 1 Y 1 A SER 3340 ? A SER 3340 
1577 1 Y 1 A ILE 3341 ? A ILE 3341 
1578 1 Y 1 A ILE 3342 ? A ILE 3342 
1579 1 Y 1 A MET 3343 ? A MET 3343 
1580 1 Y 1 A ARG 3344 ? A ARG 3344 
1581 1 Y 1 A GLU 3345 ? A GLU 3345 
1582 1 Y 1 A ASN 3346 ? A ASN 3346 
1583 1 Y 1 A PHE 3347 ? A PHE 3347 
1584 1 Y 1 A ILE 3348 ? A ILE 3348 
1585 1 Y 1 A PRO 3349 ? A PRO 3349 
1586 1 Y 1 A THR 3350 ? A THR 3350 
1587 1 Y 1 A ILE 3351 ? A ILE 3351 
1588 1 Y 1 A VAL 3352 ? A VAL 3352 
1589 1 Y 1 A ASN 3353 ? A ASN 3353 
1590 1 Y 1 A PHE 3354 ? A PHE 3354 
1591 1 Y 1 A SER 3355 ? A SER 3355 
1592 1 Y 1 A ALA 3356 ? A ALA 3356 
1593 1 Y 1 A GLU 3357 ? A GLU 3357 
1594 1 Y 1 A GLU 3358 ? A GLU 3358 
1595 1 Y 1 A ILE 3359 ? A ILE 3359 
1596 1 Y 1 A SER 3360 ? A SER 3360 
1597 1 Y 1 A ASP 3361 ? A ASP 3361 
1598 1 Y 1 A ALA 3362 ? A ALA 3362 
1599 1 Y 1 A ILE 3363 ? A ILE 3363 
1600 1 Y 1 A ARG 3364 ? A ARG 3364 
1601 1 Y 1 A GLU 3365 ? A GLU 3365 
1602 1 Y 1 A LYS 3366 ? A LYS 3366 
1603 1 Y 1 A MET 3367 ? A MET 3367 
1604 1 Y 1 A LYS 3368 ? A LYS 3368 
1605 1 Y 1 A LYS 3369 ? A LYS 3369 
1606 1 Y 1 A ASN 3370 ? A ASN 3370 
1607 1 Y 1 A TYR 3371 ? A TYR 3371 
1608 1 Y 1 A MET 3372 ? A MET 3372 
1609 1 Y 1 A SER 3373 ? A SER 3373 
1610 1 Y 1 A ASN 3374 ? A ASN 3374 
1611 1 Y 1 A PRO 3375 ? A PRO 3375 
1612 1 Y 1 A SER 3376 ? A SER 3376 
1613 1 Y 1 A TYR 3377 ? A TYR 3377 
1614 1 Y 1 A ASN 3378 ? A ASN 3378 
1615 1 Y 1 A TYR 3379 ? A TYR 3379 
1616 1 Y 1 A GLU 3380 ? A GLU 3380 
1617 1 Y 1 A ILE 3381 ? A ILE 3381 
1618 1 Y 1 A VAL 3382 ? A VAL 3382 
1619 1 Y 1 A ASN 3383 ? A ASN 3383 
1620 1 Y 1 A ARG 3384 ? A ARG 3384 
1621 1 Y 1 A ALA 3385 ? A ALA 3385 
1622 1 Y 1 A SER 3386 ? A SER 3386 
1623 1 Y 1 A LEU 3387 ? A LEU 3387 
1624 1 Y 1 A ALA 3388 ? A ALA 3388 
1625 1 Y 1 A CYS 3389 ? A CYS 3389 
1626 1 Y 1 A GLY 3390 ? A GLY 3390 
1627 1 Y 1 A PRO 3391 ? A PRO 3391 
1628 1 Y 1 A MET 3392 ? A MET 3392 
1629 1 Y 1 A VAL 3393 ? A VAL 3393 
1630 1 Y 1 A LYS 3394 ? A LYS 3394 
1631 1 Y 1 A TRP 3395 ? A TRP 3395 
1632 1 Y 1 A ALA 3396 ? A ALA 3396 
1633 1 Y 1 A ILE 3397 ? A ILE 3397 
1634 1 Y 1 A ALA 3398 ? A ALA 3398 
1635 1 Y 1 A GLN 3399 ? A GLN 3399 
1636 1 Y 1 A LEU 3400 ? A LEU 3400 
1637 1 Y 1 A ASN 3401 ? A ASN 3401 
1638 1 Y 1 A TYR 3402 ? A TYR 3402 
1639 1 Y 1 A ALA 3403 ? A ALA 3403 
1640 1 Y 1 A ASP 3404 ? A ASP 3404 
1641 1 Y 1 A MET 3405 ? A MET 3405 
1642 1 Y 1 A LEU 3406 ? A LEU 3406 
1643 1 Y 1 A LYS 3407 ? A LYS 3407 
1644 1 Y 1 A ARG 3408 ? A ARG 3408 
1645 1 Y 1 A VAL 3409 ? A VAL 3409 
1646 1 Y 1 A GLU 3410 ? A GLU 3410 
1647 1 Y 1 A PRO 3411 ? A PRO 3411 
1648 1 Y 1 A LEU 3412 ? A LEU 3412 
1649 1 Y 1 A ARG 3413 ? A ARG 3413 
1650 1 Y 1 A ASN 3414 ? A ASN 3414 
1651 1 Y 1 A GLU 3415 ? A GLU 3415 
1652 1 Y 1 A LEU 3416 ? A LEU 3416 
1653 1 Y 1 A GLN 3417 ? A GLN 3417 
1654 1 Y 1 A LYS 3418 ? A LYS 3418 
1655 1 Y 1 A LEU 3419 ? A LEU 3419 
1656 1 Y 1 A GLU 3420 ? A GLU 3420 
1657 1 Y 1 A ASP 3421 ? A ASP 3421 
1658 1 Y 1 A ASP 3422 ? A ASP 3422 
1659 1 Y 1 A ALA 3423 ? A ALA 3423 
1660 1 Y 1 A LYS 3424 ? A LYS 3424 
1661 1 Y 1 A ASP 3425 ? A ASP 3425 
1662 1 Y 1 A ASN 3426 ? A ASN 3426 
1663 1 Y 1 A GLN 3427 ? A GLN 3427 
1664 1 Y 1 A GLN 3428 ? A GLN 3428 
1665 1 Y 1 A LYS 3429 ? A LYS 3429 
1666 1 Y 1 A ALA 3430 ? A ALA 3430 
1667 1 Y 1 A ASN 3431 ? A ASN 3431 
1668 1 Y 1 A GLU 3432 ? A GLU 3432 
1669 1 Y 1 A VAL 3433 ? A VAL 3433 
1670 1 Y 1 A GLU 3434 ? A GLU 3434 
1671 1 Y 1 A GLN 3435 ? A GLN 3435 
1672 1 Y 1 A MET 3436 ? A MET 3436 
1673 1 Y 1 A ILE 3437 ? A ILE 3437 
1674 1 Y 1 A ARG 3438 ? A ARG 3438 
1675 1 Y 1 A ASP 3439 ? A ASP 3439 
1676 1 Y 1 A LEU 3440 ? A LEU 3440 
1677 1 Y 1 A GLU 3441 ? A GLU 3441 
1678 1 Y 1 A ALA 3442 ? A ALA 3442 
1679 1 Y 1 A SER 3443 ? A SER 3443 
1680 1 Y 1 A ILE 3444 ? A ILE 3444 
1681 1 Y 1 A ALA 3445 ? A ALA 3445 
1682 1 Y 1 A ARG 3446 ? A ARG 3446 
1683 1 Y 1 A TYR 3447 ? A TYR 3447 
1684 1 Y 1 A LYS 3448 ? A LYS 3448 
1685 1 Y 1 A MET 4348 ? A MET 4348 
1686 1 Y 1 A LEU 4349 ? A LEU 4349 
1687 1 Y 1 A GLU 4350 ? A GLU 4350 
1688 1 Y 1 A ASP 4351 ? A ASP 4351 
1689 1 Y 1 A GLU 4352 ? A GLU 4352 
1690 1 Y 1 A ASP 4353 ? A ASP 4353 
1691 1 Y 1 A ASP 4354 ? A ASP 4354 
1692 1 Y 1 A LEU 4355 ? A LEU 4355 
1693 1 Y 1 A ALA 4356 ? A ALA 4356 
1694 1 Y 1 A TYR 4357 ? A TYR 4357 
1695 1 Y 1 A ALA 4358 ? A ALA 4358 
1696 1 Y 1 A GLU 4359 ? A GLU 4359 
1697 1 Y 1 A THR 4360 ? A THR 4360 
1698 1 Y 1 A GLU 4361 ? A GLU 4361 
1699 1 Y 1 A LYS 4362 ? A LYS 4362 
1700 1 Y 1 A LYS 4363 ? A LYS 4363 
1701 1 Y 1 A THR 4364 ? A THR 4364 
1702 1 Y 1 A ARG 4365 ? A ARG 4365 
1703 1 Y 1 A THR 4366 ? A THR 4366 
1704 1 Y 1 A ASP 4367 ? A ASP 4367 
1705 1 Y 1 A SER 4368 ? A SER 4368 
1706 1 Y 1 A THR 4369 ? A THR 4369 
1707 1 Y 1 A SER 4370 ? A SER 4370 
1708 1 Y 1 A ASP 4371 ? A ASP 4371 
1709 1 Y 1 A GLY 4372 ? A GLY 4372 
1710 1 Y 1 A ARG 4373 ? A ARG 4373 
1711 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 
MG  MG     MG N N 336 
PHE N      N  N N 337 
PHE CA     C  N S 338 
PHE C      C  N N 339 
PHE O      O  N N 340 
PHE CB     C  N N 341 
PHE CG     C  Y N 342 
PHE CD1    C  Y N 343 
PHE CD2    C  Y N 344 
PHE CE1    C  Y N 345 
PHE CE2    C  Y N 346 
PHE CZ     C  Y N 347 
PHE OXT    O  N N 348 
PHE H      H  N N 349 
PHE H2     H  N N 350 
PHE HA     H  N N 351 
PHE HB2    H  N N 352 
PHE HB3    H  N N 353 
PHE HD1    H  N N 354 
PHE HD2    H  N N 355 
PHE HE1    H  N N 356 
PHE HE2    H  N N 357 
PHE HZ     H  N N 358 
PHE HXT    H  N N 359 
PRO N      N  N N 360 
PRO CA     C  N S 361 
PRO C      C  N N 362 
PRO O      O  N N 363 
PRO CB     C  N N 364 
PRO CG     C  N N 365 
PRO CD     C  N N 366 
PRO OXT    O  N N 367 
PRO H      H  N N 368 
PRO HA     H  N N 369 
PRO HB2    H  N N 370 
PRO HB3    H  N N 371 
PRO HG2    H  N N 372 
PRO HG3    H  N N 373 
PRO HD2    H  N N 374 
PRO HD3    H  N N 375 
PRO HXT    H  N N 376 
SER N      N  N N 377 
SER CA     C  N S 378 
SER C      C  N N 379 
SER O      O  N N 380 
SER CB     C  N N 381 
SER OG     O  N N 382 
SER OXT    O  N N 383 
SER H      H  N N 384 
SER H2     H  N N 385 
SER HA     H  N N 386 
SER HB2    H  N N 387 
SER HB3    H  N N 388 
SER HG     H  N N 389 
SER HXT    H  N N 390 
THR N      N  N N 391 
THR CA     C  N S 392 
THR C      C  N N 393 
THR O      O  N N 394 
THR CB     C  N R 395 
THR OG1    O  N N 396 
THR CG2    C  N N 397 
THR OXT    O  N N 398 
THR H      H  N N 399 
THR H2     H  N N 400 
THR HA     H  N N 401 
THR HB     H  N N 402 
THR HG1    H  N N 403 
THR HG21   H  N N 404 
THR HG22   H  N N 405 
THR HG23   H  N N 406 
THR HXT    H  N N 407 
TRP N      N  N N 408 
TRP CA     C  N S 409 
TRP C      C  N N 410 
TRP O      O  N N 411 
TRP CB     C  N N 412 
TRP CG     C  Y N 413 
TRP CD1    C  Y N 414 
TRP CD2    C  Y N 415 
TRP NE1    N  Y N 416 
TRP CE2    C  Y N 417 
TRP CE3    C  Y N 418 
TRP CZ2    C  Y N 419 
TRP CZ3    C  Y N 420 
TRP CH2    C  Y N 421 
TRP OXT    O  N N 422 
TRP H      H  N N 423 
TRP H2     H  N N 424 
TRP HA     H  N N 425 
TRP HB2    H  N N 426 
TRP HB3    H  N N 427 
TRP HD1    H  N N 428 
TRP HE1    H  N N 429 
TRP HE3    H  N N 430 
TRP HZ2    H  N N 431 
TRP HZ3    H  N N 432 
TRP HH2    H  N N 433 
TRP HXT    H  N N 434 
TYR N      N  N N 435 
TYR CA     C  N S 436 
TYR C      C  N N 437 
TYR O      O  N N 438 
TYR CB     C  N N 439 
TYR CG     C  Y N 440 
TYR CD1    C  Y N 441 
TYR CD2    C  Y N 442 
TYR CE1    C  Y N 443 
TYR CE2    C  Y N 444 
TYR CZ     C  Y N 445 
TYR OH     O  N N 446 
TYR OXT    O  N N 447 
TYR H      H  N N 448 
TYR H2     H  N N 449 
TYR HA     H  N N 450 
TYR HB2    H  N N 451 
TYR HB3    H  N N 452 
TYR HD1    H  N N 453 
TYR HD2    H  N N 454 
TYR HE1    H  N N 455 
TYR HE2    H  N N 456 
TYR HH     H  N N 457 
TYR HXT    H  N N 458 
VAL N      N  N N 459 
VAL CA     C  N S 460 
VAL C      C  N N 461 
VAL O      O  N N 462 
VAL CB     C  N N 463 
VAL CG1    C  N N 464 
VAL CG2    C  N N 465 
VAL OXT    O  N N 466 
VAL H      H  N N 467 
VAL H2     H  N N 468 
VAL HA     H  N N 469 
VAL HB     H  N N 470 
VAL HG11   H  N N 471 
VAL HG12   H  N N 472 
VAL HG13   H  N N 473 
VAL HG21   H  N N 474 
VAL HG22   H  N N 475 
VAL HG23   H  N N 476 
VAL HXT    H  N N 477 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
ATP PG    O1G    doub N N 114 
ATP PG    O2G    sing N N 115 
ATP PG    O3G    sing N N 116 
ATP PG    O3B    sing N N 117 
ATP O2G   HOG2   sing N N 118 
ATP O3G   HOG3   sing N N 119 
ATP PB    O1B    doub N N 120 
ATP PB    O2B    sing N N 121 
ATP PB    O3B    sing N N 122 
ATP PB    O3A    sing N N 123 
ATP O2B   HOB2   sing N N 124 
ATP PA    O1A    doub N N 125 
ATP PA    O2A    sing N N 126 
ATP PA    O3A    sing N N 127 
ATP PA    "O5'"  sing N N 128 
ATP O2A   HOA2   sing N N 129 
ATP "O5'" "C5'"  sing N N 130 
ATP "C5'" "C4'"  sing N N 131 
ATP "C5'" "H5'1" sing N N 132 
ATP "C5'" "H5'2" sing N N 133 
ATP "C4'" "O4'"  sing N N 134 
ATP "C4'" "C3'"  sing N N 135 
ATP "C4'" "H4'"  sing N N 136 
ATP "O4'" "C1'"  sing N N 137 
ATP "C3'" "O3'"  sing N N 138 
ATP "C3'" "C2'"  sing N N 139 
ATP "C3'" "H3'"  sing N N 140 
ATP "O3'" "HO3'" sing N N 141 
ATP "C2'" "O2'"  sing N N 142 
ATP "C2'" "C1'"  sing N N 143 
ATP "C2'" "H2'"  sing N N 144 
ATP "O2'" "HO2'" sing N N 145 
ATP "C1'" N9     sing N N 146 
ATP "C1'" "H1'"  sing N N 147 
ATP N9    C8     sing Y N 148 
ATP N9    C4     sing Y N 149 
ATP C8    N7     doub Y N 150 
ATP C8    H8     sing N N 151 
ATP N7    C5     sing Y N 152 
ATP C5    C6     sing Y N 153 
ATP C5    C4     doub Y N 154 
ATP C6    N6     sing N N 155 
ATP C6    N1     doub Y N 156 
ATP N6    HN61   sing N N 157 
ATP N6    HN62   sing N N 158 
ATP N1    C2     sing Y N 159 
ATP C2    N3     doub Y N 160 
ATP C2    H2     sing N N 161 
ATP N3    C4     sing Y N 162 
CYS N     CA     sing N N 163 
CYS N     H      sing N N 164 
CYS N     H2     sing N N 165 
CYS CA    C      sing N N 166 
CYS CA    CB     sing N N 167 
CYS CA    HA     sing N N 168 
CYS C     O      doub N N 169 
CYS C     OXT    sing N N 170 
CYS CB    SG     sing N N 171 
CYS CB    HB2    sing N N 172 
CYS CB    HB3    sing N N 173 
CYS SG    HG     sing N N 174 
CYS OXT   HXT    sing N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-09-03 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9DH5 
_em_admin.last_update        2025-04-30 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-1 of the motor domain from full-length human dynein-1 in 5mM AMPPNP with 5mM Mg2+' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    YES 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                1.5 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         40 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ?         ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 SerialEM  4 
MASKING                         ? 3  ? ? ? ?         ? 
'CTF CORRECTION'                ? 4  1 ? ? ?         ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?         ? 
'MODEL FITTING'                 ? 7  ? ? ? ?         ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ?         ? 
OTHER                           ? 9  ? ? ? ?         ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ?         ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? cryoSPARC 4 
CLASSIFICATION                  ? 12 1 ? ? ?         ? 
RECONSTRUCTION                  ? 13 1 ? ? cryoSPARC 4 
'VOLUME SELECTION'              ? 14 1 1 1 ?         ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ?         ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ?         ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ?         ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ?         ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ?         ? 
# 
_em_specimen.concentration           2 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 'R35 GM142959' 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 'R35 GM139483' 2 
# 
_atom_sites.entry_id                    9DH5 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . MET A 1 1457 ? 223.200 209.500 144.134 1.00 36.31 ? 1457 MET A N     1 
ATOM   2     C  CA    . MET A 1 1457 ? 222.255 210.539 144.528 1.00 36.14 ? 1457 MET A CA    1 
ATOM   3     C  C     . MET A 1 1457 ? 221.021 209.932 145.187 1.00 36.56 ? 1457 MET A C     1 
ATOM   4     O  O     . MET A 1 1457 ? 220.072 210.644 145.518 1.00 37.52 ? 1457 MET A O     1 
ATOM   5     C  CB    . MET A 1 1457 ? 221.845 211.379 143.319 1.00 34.60 ? 1457 MET A CB    1 
ATOM   6     C  CG    . MET A 1 1457 ? 220.918 210.660 142.354 1.00 36.04 ? 1457 MET A CG    1 
ATOM   7     S  SD    . MET A 1 1457 ? 221.741 209.312 141.485 1.00 62.27 ? 1457 MET A SD    1 
ATOM   8     C  CE    . MET A 1 1457 ? 222.870 210.224 140.436 1.00 40.38 ? 1457 MET A CE    1 
ATOM   9     N  N     . ALA A 1 1458 ? 221.041 208.611 145.376 1.00 31.23 ? 1458 ALA A N     1 
ATOM   10    C  CA    . ALA A 1 1458 ? 219.934 207.949 146.057 1.00 31.23 ? 1458 ALA A CA    1 
ATOM   11    C  C     . ALA A 1 1458 ? 219.788 208.440 147.488 1.00 35.75 ? 1458 ALA A C     1 
ATOM   12    O  O     . ALA A 1 1458 ? 218.666 208.537 148.001 1.00 38.19 ? 1458 ALA A O     1 
ATOM   13    C  CB    . ALA A 1 1458 ? 220.132 206.433 146.030 1.00 30.17 ? 1458 ALA A CB    1 
ATOM   14    N  N     . LEU A 1 1459 ? 220.905 208.749 148.150 1.00 36.57 ? 1459 LEU A N     1 
ATOM   15    C  CA    . LEU A 1 1459 ? 220.840 209.348 149.478 1.00 32.87 ? 1459 LEU A CA    1 
ATOM   16    C  C     . LEU A 1 1459 ? 220.161 210.711 149.430 1.00 32.47 ? 1459 LEU A C     1 
ATOM   17    O  O     . LEU A 1 1459 ? 219.366 211.047 150.316 1.00 34.96 ? 1459 LEU A O     1 
ATOM   18    C  CB    . LEU A 1 1459 ? 222.242 209.471 150.071 1.00 25.11 ? 1459 LEU A CB    1 
ATOM   19    C  CG    . LEU A 1 1459 ? 222.996 208.186 150.417 1.00 32.15 ? 1459 LEU A CG    1 
ATOM   20    C  CD1   . LEU A 1 1459 ? 223.767 207.657 149.217 1.00 34.96 ? 1459 LEU A CD1   1 
ATOM   21    C  CD2   . LEU A 1 1459 ? 223.930 208.427 151.589 1.00 30.79 ? 1459 LEU A CD2   1 
ATOM   22    N  N     . GLU A 1 1460 ? 220.462 211.510 148.403 1.00 26.08 ? 1460 GLU A N     1 
ATOM   23    C  CA    . GLU A 1 1460 ? 219.835 212.821 148.281 1.00 30.66 ? 1460 GLU A CA    1 
ATOM   24    C  C     . GLU A 1 1460 ? 218.326 212.695 148.110 1.00 36.05 ? 1460 GLU A C     1 
ATOM   25    O  O     . GLU A 1 1460 ? 217.565 213.535 148.605 1.00 36.11 ? 1460 GLU A O     1 
ATOM   26    C  CB    . GLU A 1 1460 ? 220.451 213.592 147.111 1.00 30.79 ? 1460 GLU A CB    1 
ATOM   27    C  CG    . GLU A 1 1460 ? 219.822 214.952 146.858 1.00 31.46 ? 1460 GLU A CG    1 
ATOM   28    C  CD    . GLU A 1 1460 ? 220.404 215.649 145.643 1.00 42.28 ? 1460 GLU A CD    1 
ATOM   29    O  OE1   . GLU A 1 1460 ? 220.289 215.100 144.526 1.00 41.21 ? 1460 GLU A OE1   1 
ATOM   30    O  OE2   . GLU A 1 1460 ? 220.980 216.745 145.805 1.00 37.94 ? 1460 GLU A OE2   1 
ATOM   31    N  N     . GLU A 1 1461 ? 217.875 211.650 147.411 1.00 32.87 ? 1461 GLU A N     1 
ATOM   32    C  CA    . GLU A 1 1461 ? 216.440 211.434 147.250 1.00 29.66 ? 1461 GLU A CA    1 
ATOM   33    C  C     . GLU A 1 1461 ? 215.767 211.163 148.588 1.00 32.21 ? 1461 GLU A C     1 
ATOM   34    O  O     . GLU A 1 1461 ? 214.669 211.668 148.851 1.00 33.07 ? 1461 GLU A O     1 
ATOM   35    C  CB    . GLU A 1 1461 ? 216.188 210.282 146.278 1.00 27.72 ? 1461 GLU A CB    1 
ATOM   36    C  CG    . GLU A 1 1461 ? 216.925 210.415 144.957 1.00 33.58 ? 1461 GLU A CG    1 
ATOM   37    C  CD    . GLU A 1 1461 ? 216.865 211.824 144.399 1.00 40.13 ? 1461 GLU A CD    1 
ATOM   38    O  OE1   . GLU A 1 1461 ? 215.751 212.300 144.097 1.00 38.93 ? 1461 GLU A OE1   1 
ATOM   39    O  OE2   . GLU A 1 1461 ? 217.934 212.455 144.263 1.00 43.02 ? 1461 GLU A OE2   1 
ATOM   40    N  N     . PHE A 1 1462 ? 216.407 210.369 149.449 1.00 30.68 ? 1462 PHE A N     1 
ATOM   41    C  CA    . PHE A 1 1462 ? 215.830 210.082 150.758 1.00 26.41 ? 1462 PHE A CA    1 
ATOM   42    C  C     . PHE A 1 1462 ? 215.700 211.349 151.591 1.00 29.82 ? 1462 PHE A C     1 
ATOM   43    O  O     . PHE A 1 1462 ? 214.672 211.565 152.246 1.00 30.78 ? 1462 PHE A O     1 
ATOM   44    C  CB    . PHE A 1 1462 ? 216.669 209.036 151.490 1.00 27.55 ? 1462 PHE A CB    1 
ATOM   45    C  CG    . PHE A 1 1462 ? 216.660 207.680 150.837 1.00 37.74 ? 1462 PHE A CG    1 
ATOM   46    C  CD1   . PHE A 1 1462 ? 215.681 207.348 149.913 1.00 34.98 ? 1462 PHE A CD1   1 
ATOM   47    C  CD2   . PHE A 1 1462 ? 217.627 206.741 151.146 1.00 33.74 ? 1462 PHE A CD2   1 
ATOM   48    C  CE1   . PHE A 1 1462 ? 215.670 206.105 149.311 1.00 36.34 ? 1462 PHE A CE1   1 
ATOM   49    C  CE2   . PHE A 1 1462 ? 217.621 205.495 150.547 1.00 35.25 ? 1462 PHE A CE2   1 
ATOM   50    C  CZ    . PHE A 1 1462 ? 216.642 205.176 149.628 1.00 36.89 ? 1462 PHE A CZ    1 
ATOM   51    N  N     . LEU A 1 1463 ? 216.723 212.205 151.575 1.00 28.25 ? 1463 LEU A N     1 
ATOM   52    C  CA    . LEU A 1 1463 ? 216.628 213.473 152.291 1.00 25.26 ? 1463 LEU A CA    1 
ATOM   53    C  C     . LEU A 1 1463 ? 215.518 214.346 151.721 1.00 27.82 ? 1463 LEU A C     1 
ATOM   54    O  O     . LEU A 1 1463 ? 214.785 214.997 152.473 1.00 31.14 ? 1463 LEU A O     1 
ATOM   55    C  CB    . LEU A 1 1463 ? 217.963 214.218 152.249 1.00 28.03 ? 1463 LEU A CB    1 
ATOM   56    C  CG    . LEU A 1 1463 ? 219.042 213.862 153.276 1.00 28.14 ? 1463 LEU A CG    1 
ATOM   57    C  CD1   . LEU A 1 1463 ? 218.567 214.186 154.687 1.00 26.85 ? 1463 LEU A CD1   1 
ATOM   58    C  CD2   . LEU A 1 1463 ? 219.488 212.415 153.176 1.00 27.00 ? 1463 LEU A CD2   1 
ATOM   59    N  N     . LYS A 1 1464 ? 215.383 214.378 150.392 1.00 28.08 ? 1464 LYS A N     1 
ATOM   60    C  CA    . LYS A 1 1464 ? 214.315 215.157 149.776 1.00 25.69 ? 1464 LYS A CA    1 
ATOM   61    C  C     . LYS A 1 1464 ? 212.946 214.597 150.144 1.00 27.93 ? 1464 LYS A C     1 
ATOM   62    O  O     . LYS A 1 1464 ? 212.012 215.357 150.421 1.00 31.40 ? 1464 LYS A O     1 
ATOM   63    C  CB    . LYS A 1 1464 ? 214.500 215.188 148.259 1.00 27.40 ? 1464 LYS A CB    1 
ATOM   64    C  CG    . LYS A 1 1464 ? 213.505 216.070 147.524 1.00 24.34 ? 1464 LYS A CG    1 
ATOM   65    C  CD    . LYS A 1 1464 ? 213.762 217.544 147.802 1.00 28.00 ? 1464 LYS A CD    1 
ATOM   66    C  CE    . LYS A 1 1464 ? 212.837 218.429 146.982 1.00 32.94 ? 1464 LYS A CE    1 
ATOM   67    N  NZ    . LYS A 1 1464 ? 213.045 219.877 147.269 1.00 35.89 ? 1464 LYS A NZ    1 
ATOM   68    N  N     . GLN A 1 1465 ? 212.808 213.269 150.147 1.00 27.27 ? 1465 GLN A N     1 
ATOM   69    C  CA    . GLN A 1 1465 ? 211.544 212.658 150.545 1.00 23.93 ? 1465 GLN A CA    1 
ATOM   70    C  C     . GLN A 1 1465 ? 211.235 212.934 152.011 1.00 28.94 ? 1465 GLN A C     1 
ATOM   71    O  O     . GLN A 1 1465 ? 210.091 213.238 152.364 1.00 31.08 ? 1465 GLN A O     1 
ATOM   72    C  CB    . GLN A 1 1465 ? 211.577 211.153 150.279 1.00 24.02 ? 1465 GLN A CB    1 
ATOM   73    C  CG    . GLN A 1 1465 ? 211.573 210.780 148.809 1.00 27.05 ? 1465 GLN A CG    1 
ATOM   74    C  CD    . GLN A 1 1465 ? 212.052 209.363 148.566 1.00 33.71 ? 1465 GLN A CD    1 
ATOM   75    O  OE1   . GLN A 1 1465 ? 213.003 209.136 147.816 1.00 35.17 ? 1465 GLN A OE1   1 
ATOM   76    N  NE2   . GLN A 1 1465 ? 211.394 208.399 149.200 1.00 35.58 ? 1465 GLN A NE2   1 
ATOM   77    N  N     . ILE A 1 1466 ? 212.244 212.828 152.880 1.00 26.70 ? 1466 ILE A N     1 
ATOM   78    C  CA    . ILE A 1 1466 ? 212.044 213.138 154.291 1.00 23.10 ? 1466 ILE A CA    1 
ATOM   79    C  C     . ILE A 1 1466 ? 211.674 214.604 154.464 1.00 22.25 ? 1466 ILE A C     1 
ATOM   80    O  O     . ILE A 1 1466 ? 210.766 214.948 155.234 1.00 23.76 ? 1466 ILE A O     1 
ATOM   81    C  CB    . ILE A 1 1466 ? 213.299 212.770 155.104 1.00 18.36 ? 1466 ILE A CB    1 
ATOM   82    C  CG1   . ILE A 1 1466 ? 213.506 211.255 155.101 1.00 22.46 ? 1466 ILE A CG1   1 
ATOM   83    C  CG2   . ILE A 1 1466 ? 213.177 213.276 156.529 1.00 20.44 ? 1466 ILE A CG2   1 
ATOM   84    C  CD1   . ILE A 1 1466 ? 214.612 210.780 156.012 1.00 24.28 ? 1466 ILE A CD1   1 
ATOM   85    N  N     . ARG A 1 1467 ? 212.364 215.491 153.745 1.00 21.83 ? 1467 ARG A N     1 
ATOM   86    C  CA    . ARG A 1 1467 ? 212.059 216.916 153.818 1.00 25.61 ? 1467 ARG A CA    1 
ATOM   87    C  C     . ARG A 1 1467 ? 210.652 217.215 153.316 1.00 27.28 ? 1467 ARG A C     1 
ATOM   88    O  O     . ARG A 1 1467 ? 209.941 218.029 153.913 1.00 29.24 ? 1467 ARG A O     1 
ATOM   89    C  CB    . ARG A 1 1467 ? 213.098 217.706 153.020 1.00 26.41 ? 1467 ARG A CB    1 
ATOM   90    C  CG    . ARG A 1 1467 ? 212.765 219.173 152.802 1.00 29.22 ? 1467 ARG A CG    1 
ATOM   91    C  CD    . ARG A 1 1467 ? 212.866 219.960 154.096 1.00 25.69 ? 1467 ARG A CD    1 
ATOM   92    N  NE    . ARG A 1 1467 ? 214.179 219.841 154.719 1.00 26.52 ? 1467 ARG A NE    1 
ATOM   93    C  CZ    . ARG A 1 1467 ? 215.299 220.359 154.235 1.00 29.41 ? 1467 ARG A CZ    1 
ATOM   94    N  NH1   . ARG A 1 1467 ? 215.307 221.081 153.125 1.00 30.53 ? 1467 ARG A NH1   1 
ATOM   95    N  NH2   . ARG A 1 1467 ? 216.441 220.157 154.887 1.00 31.35 ? 1467 ARG A NH2   1 
ATOM   96    N  N     . GLU A 1 1468 ? 210.230 216.559 152.233 1.00 25.01 ? 1468 GLU A N     1 
ATOM   97    C  CA    . GLU A 1 1468 ? 208.905 216.808 151.673 1.00 25.54 ? 1468 GLU A CA    1 
ATOM   98    C  C     . GLU A 1 1468 ? 207.786 216.256 152.547 1.00 29.12 ? 1468 GLU A C     1 
ATOM   99    O  O     . GLU A 1 1468 ? 206.702 216.849 152.603 1.00 29.86 ? 1468 GLU A O     1 
ATOM   100   C  CB    . GLU A 1 1468 ? 208.808 216.213 150.267 1.00 23.03 ? 1468 GLU A CB    1 
ATOM   101   C  CG    . GLU A 1 1468 ? 209.493 217.040 149.190 1.00 29.41 ? 1468 GLU A CG    1 
ATOM   102   C  CD    . GLU A 1 1468 ? 208.727 218.302 148.832 1.00 38.60 ? 1468 GLU A CD    1 
ATOM   103   O  OE1   . GLU A 1 1468 ? 207.595 218.482 149.330 1.00 40.72 ? 1468 GLU A OE1   1 
ATOM   104   O  OE2   . GLU A 1 1468 ? 209.260 219.119 148.051 1.00 35.18 ? 1468 GLU A OE2   1 
ATOM   105   N  N     . VAL A 1 1469 ? 208.016 215.129 153.222 1.00 25.64 ? 1469 VAL A N     1 
ATOM   106   C  CA    . VAL A 1 1469 ? 206.983 214.550 154.075 1.00 19.91 ? 1469 VAL A CA    1 
ATOM   107   C  C     . VAL A 1 1469 ? 206.657 215.483 155.235 1.00 22.49 ? 1469 VAL A C     1 
ATOM   108   O  O     . VAL A 1 1469 ? 205.485 215.699 155.565 1.00 27.60 ? 1469 VAL A O     1 
ATOM   109   C  CB    . VAL A 1 1469 ? 207.417 213.158 154.571 1.00 19.91 ? 1469 VAL A CB    1 
ATOM   110   C  CG1   . VAL A 1 1469 ? 206.599 212.737 155.783 1.00 23.60 ? 1469 VAL A CG1   1 
ATOM   111   C  CG2   . VAL A 1 1469 ? 207.274 212.137 153.460 1.00 19.91 ? 1469 VAL A CG2   1 
ATOM   112   N  N     . TRP A 1 1470 ? 207.677 216.062 155.858 1.00 20.71 ? 1470 TRP A N     1 
ATOM   113   C  CA    . TRP A 1 1470 ? 207.502 216.868 157.058 1.00 20.44 ? 1470 TRP A CA    1 
ATOM   114   C  C     . TRP A 1 1470 ? 207.238 218.339 156.770 1.00 25.51 ? 1470 TRP A C     1 
ATOM   115   O  O     . TRP A 1 1470 ? 206.998 219.105 157.710 1.00 30.06 ? 1470 TRP A O     1 
ATOM   116   C  CB    . TRP A 1 1470 ? 208.725 216.718 157.966 1.00 18.98 ? 1470 TRP A CB    1 
ATOM   117   C  CG    . TRP A 1 1470 ? 208.858 215.328 158.491 1.00 16.07 ? 1470 TRP A CG    1 
ATOM   118   C  CD1   . TRP A 1 1470 ? 209.825 214.421 158.182 1.00 17.35 ? 1470 TRP A CD1   1 
ATOM   119   C  CD2   . TRP A 1 1470 ? 207.975 214.678 159.409 1.00 16.33 ? 1470 TRP A CD2   1 
ATOM   120   N  NE1   . TRP A 1 1470 ? 209.604 213.244 158.857 1.00 19.10 ? 1470 TRP A NE1   1 
ATOM   121   C  CE2   . TRP A 1 1470 ? 208.472 213.377 159.618 1.00 17.33 ? 1470 TRP A CE2   1 
ATOM   122   C  CE3   . TRP A 1 1470 ? 206.814 215.071 160.079 1.00 15.28 ? 1470 TRP A CE3   1 
ATOM   123   C  CZ2   . TRP A 1 1470 ? 207.849 212.470 160.469 1.00 14.09 ? 1470 TRP A CZ2   1 
ATOM   124   C  CZ3   . TRP A 1 1470 ? 206.198 214.169 160.921 1.00 16.23 ? 1470 TRP A CZ3   1 
ATOM   125   C  CH2   . TRP A 1 1470 ? 206.717 212.883 161.109 1.00 12.50 ? 1470 TRP A CH2   1 
ATOM   126   N  N     . ASN A 1 1471 ? 207.275 218.756 155.509 1.00 28.35 ? 1471 ASN A N     1 
ATOM   127   C  CA    . ASN A 1 1471 ? 206.879 220.109 155.151 1.00 25.48 ? 1471 ASN A CA    1 
ATOM   128   C  C     . ASN A 1 1471 ? 205.378 220.243 154.933 1.00 27.41 ? 1471 ASN A C     1 
ATOM   129   O  O     . ASN A 1 1471 ? 204.886 221.367 154.790 1.00 30.88 ? 1471 ASN A O     1 
ATOM   130   C  CB    . ASN A 1 1471 ? 207.623 220.562 153.891 1.00 23.08 ? 1471 ASN A CB    1 
ATOM   131   C  CG    . ASN A 1 1471 ? 209.079 220.886 154.159 1.00 32.94 ? 1471 ASN A CG    1 
ATOM   132   O  OD1   . ASN A 1 1471 ? 209.555 220.764 155.287 1.00 32.58 ? 1471 ASN A OD1   1 
ATOM   133   N  ND2   . ASN A 1 1471 ? 209.794 221.301 153.120 1.00 31.67 ? 1471 ASN A ND2   1 
ATOM   134   N  N     . THR A 1 1472 ? 204.646 219.129 154.904 1.00 22.40 ? 1472 THR A N     1 
ATOM   135   C  CA    . THR A 1 1472 ? 203.209 219.145 154.658 1.00 24.54 ? 1472 THR A CA    1 
ATOM   136   C  C     . THR A 1 1472 ? 202.392 218.361 155.672 1.00 30.25 ? 1472 THR A C     1 
ATOM   137   O  O     . THR A 1 1472 ? 201.192 218.632 155.802 1.00 31.66 ? 1472 THR A O     1 
ATOM   138   C  CB    . THR A 1 1472 ? 202.895 218.587 153.262 1.00 28.01 ? 1472 THR A CB    1 
ATOM   139   O  OG1   . THR A 1 1472 ? 203.312 217.219 153.190 1.00 27.75 ? 1472 THR A OG1   1 
ATOM   140   C  CG2   . THR A 1 1472 ? 203.612 219.389 152.184 1.00 28.19 ? 1472 THR A CG2   1 
ATOM   141   N  N     . TYR A 1 1473 ? 202.986 217.408 156.388 1.00 25.03 ? 1473 TYR A N     1 
ATOM   142   C  CA    . TYR A 1 1473 ? 202.219 216.529 157.259 1.00 21.26 ? 1473 TYR A CA    1 
ATOM   143   C  C     . TYR A 1 1473 ? 201.710 217.314 158.462 1.00 27.43 ? 1473 TYR A C     1 
ATOM   144   O  O     . TYR A 1 1473 ? 202.503 217.863 159.235 1.00 23.70 ? 1473 TYR A O     1 
ATOM   145   C  CB    . TYR A 1 1473 ? 203.084 215.355 157.706 1.00 18.63 ? 1473 TYR A CB    1 
ATOM   146   C  CG    . TYR A 1 1473 ? 202.366 214.350 158.576 1.00 23.06 ? 1473 TYR A CG    1 
ATOM   147   C  CD1   . TYR A 1 1473 ? 201.472 213.442 158.024 1.00 30.47 ? 1473 TYR A CD1   1 
ATOM   148   C  CD2   . TYR A 1 1473 ? 202.569 214.320 159.945 1.00 21.08 ? 1473 TYR A CD2   1 
ATOM   149   C  CE1   . TYR A 1 1473 ? 200.813 212.518 158.815 1.00 26.11 ? 1473 TYR A CE1   1 
ATOM   150   C  CE2   . TYR A 1 1473 ? 201.912 213.406 160.740 1.00 22.07 ? 1473 TYR A CE2   1 
ATOM   151   C  CZ    . TYR A 1 1473 ? 201.038 212.506 160.174 1.00 26.74 ? 1473 TYR A CZ    1 
ATOM   152   O  OH    . TYR A 1 1473 ? 200.386 211.597 160.973 1.00 23.25 ? 1473 TYR A OH    1 
ATOM   153   N  N     . GLU A 1 1474 ? 200.392 217.366 158.622 1.00 21.77 ? 1474 GLU A N     1 
ATOM   154   C  CA    . GLU A 1 1474 ? 199.755 218.133 159.680 1.00 19.81 ? 1474 GLU A CA    1 
ATOM   155   C  C     . GLU A 1 1474 ? 199.136 217.198 160.709 1.00 24.32 ? 1474 GLU A C     1 
ATOM   156   O  O     . GLU A 1 1474 ? 198.641 216.120 160.366 1.00 28.49 ? 1474 GLU A O     1 
ATOM   157   C  CB    . GLU A 1 1474 ? 198.677 219.062 159.113 1.00 20.98 ? 1474 GLU A CB    1 
ATOM   158   C  CG    . GLU A 1 1474 ? 199.221 220.256 158.350 1.00 22.04 ? 1474 GLU A CG    1 
ATOM   159   C  CD    . GLU A 1 1474 ? 198.142 221.254 157.983 1.00 30.16 ? 1474 GLU A CD    1 
ATOM   160   O  OE1   . GLU A 1 1474 ? 196.958 220.983 158.268 1.00 31.43 ? 1474 GLU A OE1   1 
ATOM   161   O  OE2   . GLU A 1 1474 ? 198.479 222.312 157.411 1.00 33.85 ? 1474 GLU A OE2   1 
ATOM   162   N  N     . LEU A 1 1475 ? 199.173 217.616 161.972 1.00 21.43 ? 1475 LEU A N     1 
ATOM   163   C  CA    . LEU A 1 1475 ? 198.504 216.874 163.031 1.00 17.40 ? 1475 LEU A CA    1 
ATOM   164   C  C     . LEU A 1 1475 ? 197.010 216.801 162.748 1.00 22.30 ? 1475 LEU A C     1 
ATOM   165   O  O     . LEU A 1 1475 ? 196.327 217.829 162.704 1.00 22.47 ? 1475 LEU A O     1 
ATOM   166   C  CB    . LEU A 1 1475 ? 198.763 217.534 164.382 1.00 12.85 ? 1475 LEU A CB    1 
ATOM   167   C  CG    . LEU A 1 1475 ? 200.194 217.428 164.909 1.00 16.69 ? 1475 LEU A CG    1 
ATOM   168   C  CD1   . LEU A 1 1475 ? 200.375 218.280 166.150 1.00 12.76 ? 1475 LEU A CD1   1 
ATOM   169   C  CD2   . LEU A 1 1475 ? 200.550 215.977 165.193 1.00 12.07 ? 1475 LEU A CD2   1 
ATOM   170   N  N     . ASP A 1 1476 ? 196.509 215.585 162.553 1.00 19.94 ? 1476 ASP A N     1 
ATOM   171   C  CA    . ASP A 1 1476 ? 195.102 215.385 162.231 1.00 17.67 ? 1476 ASP A CA    1 
ATOM   172   C  C     . ASP A 1 1476 ? 194.251 215.726 163.450 1.00 24.36 ? 1476 ASP A C     1 
ATOM   173   O  O     . ASP A 1 1476 ? 194.327 215.050 164.480 1.00 27.76 ? 1476 ASP A O     1 
ATOM   174   C  CB    . ASP A 1 1476 ? 194.874 213.945 161.781 1.00 26.96 ? 1476 ASP A CB    1 
ATOM   175   C  CG    . ASP A 1 1476 ? 193.478 213.709 161.245 1.00 36.95 ? 1476 ASP A CG    1 
ATOM   176   O  OD1   . ASP A 1 1476 ? 192.693 214.676 161.153 1.00 37.99 ? 1476 ASP A OD1   1 
ATOM   177   O  OD2   . ASP A 1 1476 ? 193.176 212.552 160.891 1.00 35.38 ? 1476 ASP A OD2   1 
ATOM   178   N  N     . LEU A 1 1477 ? 193.442 216.775 163.332 1.00 24.71 ? 1477 LEU A N     1 
ATOM   179   C  CA    . LEU A 1 1477 ? 192.701 217.320 164.459 1.00 17.60 ? 1477 LEU A CA    1 
ATOM   180   C  C     . LEU A 1 1477 ? 191.242 216.887 164.407 1.00 22.82 ? 1477 LEU A C     1 
ATOM   181   O  O     . LEU A 1 1477 ? 190.662 216.743 163.325 1.00 30.25 ? 1477 LEU A O     1 
ATOM   182   C  CB    . LEU A 1 1477 ? 192.785 218.846 164.483 1.00 18.09 ? 1477 LEU A CB    1 
ATOM   183   C  CG    . LEU A 1 1477 ? 194.153 219.437 164.827 1.00 19.44 ? 1477 LEU A CG    1 
ATOM   184   C  CD1   . LEU A 1 1477 ? 194.064 220.945 164.967 1.00 21.81 ? 1477 LEU A CD1   1 
ATOM   185   C  CD2   . LEU A 1 1477 ? 194.716 218.810 166.087 1.00 11.65 ? 1477 LEU A CD2   1 
ATOM   186   N  N     . VAL A 1 1478 ? 190.663 216.671 165.585 1.00 26.98 ? 1478 VAL A N     1 
ATOM   187   C  CA    . VAL A 1 1478 ? 189.249 216.357 165.741 1.00 21.35 ? 1478 VAL A CA    1 
ATOM   188   C  C     . VAL A 1 1478 ? 188.682 217.184 166.886 1.00 18.19 ? 1478 VAL A C     1 
ATOM   189   O  O     . VAL A 1 1478 ? 189.310 217.321 167.941 1.00 19.05 ? 1478 VAL A O     1 
ATOM   190   C  CB    . VAL A 1 1478 ? 189.013 214.849 165.983 1.00 22.35 ? 1478 VAL A CB    1 
ATOM   191   C  CG1   . VAL A 1 1478 ? 189.644 214.397 167.289 1.00 16.40 ? 1478 VAL A CG1   1 
ATOM   192   C  CG2   . VAL A 1 1478 ? 187.521 214.564 166.016 1.00 20.91 ? 1478 VAL A CG2   1 
ATOM   193   N  N     . ASN A 1 1479 ? 187.501 217.753 166.667 1.00 18.76 ? 1479 ASN A N     1 
ATOM   194   C  CA    . ASN A 1 1479 ? 186.813 218.469 167.731 1.00 18.15 ? 1479 ASN A CA    1 
ATOM   195   C  C     . ASN A 1 1479 ? 186.341 217.495 168.804 1.00 21.20 ? 1479 ASN A C     1 
ATOM   196   O  O     . ASN A 1 1479 ? 185.867 216.396 168.502 1.00 20.85 ? 1479 ASN A O     1 
ATOM   197   C  CB    . ASN A 1 1479 ? 185.628 219.248 167.170 1.00 19.14 ? 1479 ASN A CB    1 
ATOM   198   C  CG    . ASN A 1 1479 ? 184.787 219.886 168.254 1.00 18.96 ? 1479 ASN A CG    1 
ATOM   199   O  OD1   . ASN A 1 1479 ? 185.285 220.675 169.056 1.00 22.84 ? 1479 ASN A OD1   1 
ATOM   200   N  ND2   . ASN A 1 1479 ? 183.506 219.544 168.286 1.00 20.72 ? 1479 ASN A ND2   1 
ATOM   201   N  N     . TYR A 1 1480 ? 186.473 217.904 170.063 1.00 17.89 ? 1480 TYR A N     1 
ATOM   202   C  CA    . TYR A 1 1480 ? 186.078 217.082 171.203 1.00 20.18 ? 1480 TYR A CA    1 
ATOM   203   C  C     . TYR A 1 1480 ? 185.091 217.886 172.044 1.00 20.59 ? 1480 TYR A C     1 
ATOM   204   O  O     . TYR A 1 1480 ? 185.495 218.728 172.853 1.00 19.26 ? 1480 TYR A O     1 
ATOM   205   C  CB    . TYR A 1 1480 ? 187.301 216.650 172.011 1.00 16.84 ? 1480 TYR A CB    1 
ATOM   206   C  CG    . TYR A 1 1480 ? 186.978 215.957 173.317 1.00 13.44 ? 1480 TYR A CG    1 
ATOM   207   C  CD1   . TYR A 1 1480 ? 186.636 214.611 173.343 1.00 16.30 ? 1480 TYR A CD1   1 
ATOM   208   C  CD2   . TYR A 1 1480 ? 187.033 216.641 174.523 1.00 13.40 ? 1480 TYR A CD2   1 
ATOM   209   C  CE1   . TYR A 1 1480 ? 186.345 213.968 174.532 1.00 14.28 ? 1480 TYR A CE1   1 
ATOM   210   C  CE2   . TYR A 1 1480 ? 186.741 216.006 175.719 1.00 15.34 ? 1480 TYR A CE2   1 
ATOM   211   C  CZ    . TYR A 1 1480 ? 186.399 214.670 175.715 1.00 16.43 ? 1480 TYR A CZ    1 
ATOM   212   O  OH    . TYR A 1 1480 ? 186.112 214.032 176.900 1.00 20.91 ? 1480 TYR A OH    1 
ATOM   213   N  N     . GLN A 1 1481 ? 183.798 217.631 171.837 1.00 18.23 ? 1481 GLN A N     1 
ATOM   214   C  CA    . GLN A 1 1481 ? 182.718 218.245 172.614 1.00 19.36 ? 1481 GLN A CA    1 
ATOM   215   C  C     . GLN A 1 1481 ? 182.762 219.771 172.568 1.00 19.60 ? 1481 GLN A C     1 
ATOM   216   O  O     . GLN A 1 1481 ? 182.435 220.438 173.553 1.00 26.47 ? 1481 GLN A O     1 
ATOM   217   C  CB    . GLN A 1 1481 ? 182.737 217.762 174.067 1.00 22.87 ? 1481 GLN A CB    1 
ATOM   218   C  CG    . GLN A 1 1481 ? 182.852 216.258 174.224 1.00 17.83 ? 1481 GLN A CG    1 
ATOM   219   C  CD    . GLN A 1 1481 ? 183.129 215.850 175.653 1.00 18.21 ? 1481 GLN A CD    1 
ATOM   220   O  OE1   . GLN A 1 1481 ? 183.252 216.694 176.537 1.00 23.08 ? 1481 GLN A OE1   1 
ATOM   221   N  NE2   . GLN A 1 1481 ? 183.227 214.546 175.890 1.00 24.98 ? 1481 GLN A NE2   1 
ATOM   222   N  N     . ASN A 1 1482 ? 183.164 220.330 171.424 1.00 15.25 ? 1482 ASN A N     1 
ATOM   223   C  CA    . ASN A 1 1482 ? 183.217 221.780 171.217 1.00 17.77 ? 1482 ASN A CA    1 
ATOM   224   C  C     . ASN A 1 1482 ? 184.087 222.476 172.260 1.00 19.71 ? 1482 ASN A C     1 
ATOM   225   O  O     . ASN A 1 1482 ? 183.828 223.621 172.636 1.00 25.71 ? 1482 ASN A O     1 
ATOM   226   C  CB    . ASN A 1 1482 ? 181.814 222.392 171.199 1.00 20.52 ? 1482 ASN A CB    1 
ATOM   227   C  CG    . ASN A 1 1482 ? 180.970 221.882 170.048 1.00 29.09 ? 1482 ASN A CG    1 
ATOM   228   O  OD1   . ASN A 1 1482 ? 181.452 221.144 169.187 1.00 24.92 ? 1482 ASN A OD1   1 
ATOM   229   N  ND2   . ASN A 1 1482 ? 179.702 222.272 170.026 1.00 27.57 ? 1482 ASN A ND2   1 
ATOM   230   N  N     . LYS A 1 1483 ? 185.128 221.793 172.734 1.00 18.97 ? 1483 LYS A N     1 
ATOM   231   C  CA    . LYS A 1 1483 ? 186.057 222.361 173.699 1.00 18.04 ? 1483 LYS A CA    1 
ATOM   232   C  C     . LYS A 1 1483 ? 187.454 222.578 173.141 1.00 25.05 ? 1483 LYS A C     1 
ATOM   233   O  O     . LYS A 1 1483 ? 188.105 223.558 173.510 1.00 24.52 ? 1483 LYS A O     1 
ATOM   234   C  CB    . LYS A 1 1483 ? 186.161 221.464 174.938 1.00 17.46 ? 1483 LYS A CB    1 
ATOM   235   C  CG    . LYS A 1 1483 ? 184.841 221.171 175.633 1.00 24.86 ? 1483 LYS A CG    1 
ATOM   236   C  CD    . LYS A 1 1483 ? 184.935 219.897 176.466 1.00 25.37 ? 1483 LYS A CD    1 
ATOM   237   C  CE    . LYS A 1 1483 ? 183.762 219.763 177.424 1.00 24.38 ? 1483 LYS A CE    1 
ATOM   238   N  NZ    . LYS A 1 1483 ? 183.925 220.616 178.633 1.00 22.19 ? 1483 LYS A NZ    1 
ATOM   239   N  N     . CYS A 1 1484 ? 187.924 221.701 172.267 1.00 19.73 ? 1484 CYS A N     1 
ATOM   240   C  CA    . CYS A 1 1484 ? 189.285 221.757 171.742 1.00 16.99 ? 1484 CYS A CA    1 
ATOM   241   C  C     . CYS A 1 1484 ? 189.338 220.893 170.487 1.00 20.13 ? 1484 CYS A C     1 
ATOM   242   O  O     . CYS A 1 1484 ? 188.307 220.417 169.997 1.00 21.43 ? 1484 CYS A O     1 
ATOM   243   C  CB    . CYS A 1 1484 ? 190.299 221.312 172.796 1.00 14.22 ? 1484 CYS A CB    1 
ATOM   244   S  SG    . CYS A 1 1484 ? 190.174 219.573 173.249 1.00 42.47 ? 1484 CYS A SG    1 
ATOM   245   N  N     . ARG A 1 1485 ? 190.544 220.692 169.963 1.00 21.25 ? 1485 ARG A N     1 
ATOM   246   C  CA    . ARG A 1 1485 ? 190.756 219.903 168.753 1.00 17.36 ? 1485 ARG A CA    1 
ATOM   247   C  C     . ARG A 1 1485 ? 191.851 218.880 169.020 1.00 20.94 ? 1485 ARG A C     1 
ATOM   248   O  O     . ARG A 1 1485 ? 193.031 219.155 168.784 1.00 35.19 ? 1485 ARG A O     1 
ATOM   249   C  CB    . ARG A 1 1485 ? 191.122 220.796 167.568 1.00 17.47 ? 1485 ARG A CB    1 
ATOM   250   C  CG    . ARG A 1 1485 ? 190.084 221.855 167.248 1.00 20.08 ? 1485 ARG A CG    1 
ATOM   251   C  CD    . ARG A 1 1485 ? 189.122 221.370 166.176 1.00 21.80 ? 1485 ARG A CD    1 
ATOM   252   N  NE    . ARG A 1 1485 ? 189.809 220.943 164.964 1.00 17.82 ? 1485 ARG A NE    1 
ATOM   253   C  CZ    . ARG A 1 1485 ? 190.412 221.761 164.111 1.00 24.37 ? 1485 ARG A CZ    1 
ATOM   254   N  NH1   . ARG A 1 1485 ? 190.421 223.072 164.296 1.00 28.82 ? 1485 ARG A NH1   1 
ATOM   255   N  NH2   . ARG A 1 1485 ? 191.015 221.254 163.041 1.00 21.81 ? 1485 ARG A NH2   1 
ATOM   256   N  N     . LEU A 1 1486 ? 191.456 217.697 169.484 1.00 16.90 ? 1486 LEU A N     1 
ATOM   257   C  CA    . LEU A 1 1486 ? 192.391 216.643 169.846 1.00 14.60 ? 1486 LEU A CA    1 
ATOM   258   C  C     . LEU A 1 1486 ? 193.120 216.118 168.609 1.00 12.77 ? 1486 LEU A C     1 
ATOM   259   O  O     . LEU A 1 1486 ? 192.823 216.488 167.473 1.00 17.09 ? 1486 LEU A O     1 
ATOM   260   C  CB    . LEU A 1 1486 ? 191.658 215.504 170.548 1.00 13.15 ? 1486 LEU A CB    1 
ATOM   261   C  CG    . LEU A 1 1486 ? 191.131 215.765 171.957 1.00 9.95  ? 1486 LEU A CG    1 
ATOM   262   C  CD1   . LEU A 1 1486 ? 190.811 214.454 172.636 1.00 10.93 ? 1486 LEU A CD1   1 
ATOM   263   C  CD2   . LEU A 1 1486 ? 192.115 216.572 172.781 1.00 11.64 ? 1486 LEU A CD2   1 
ATOM   264   N  N     . ILE A 1 1487 ? 194.083 215.232 168.845 1.00 11.25 ? 1487 ILE A N     1 
ATOM   265   C  CA    . ILE A 1 1487 ? 194.927 214.672 167.794 1.00 13.94 ? 1487 ILE A CA    1 
ATOM   266   C  C     . ILE A 1 1487 ? 194.656 213.178 167.681 1.00 11.65 ? 1487 ILE A C     1 
ATOM   267   O  O     . ILE A 1 1487 ? 194.842 212.429 168.648 1.00 18.06 ? 1487 ILE A O     1 
ATOM   268   C  CB    . ILE A 1 1487 ? 196.415 214.939 168.069 1.00 12.50 ? 1487 ILE A CB    1 
ATOM   269   C  CG1   . ILE A 1 1487 ? 196.722 216.428 167.922 1.00 12.93 ? 1487 ILE A CG1   1 
ATOM   270   C  CG2   . ILE A 1 1487 ? 197.300 214.101 167.160 1.00 10.71 ? 1487 ILE A CG2   1 
ATOM   271   C  CD1   . ILE A 1 1487 ? 198.090 216.810 168.387 1.00 11.49 ? 1487 ILE A CD1   1 
ATOM   272   N  N     . ARG A 1 1488 ? 194.220 212.742 166.500 1.00 12.34 ? 1488 ARG A N     1 
ATOM   273   C  CA    . ARG A 1 1488 ? 194.133 211.328 166.182 1.00 14.96 ? 1488 ARG A CA    1 
ATOM   274   C  C     . ARG A 1 1488 ? 195.375 210.904 165.397 1.00 16.31 ? 1488 ARG A C     1 
ATOM   275   O  O     . ARG A 1 1488 ? 196.348 211.653 165.271 1.00 15.51 ? 1488 ARG A O     1 
ATOM   276   C  CB    . ARG A 1 1488 ? 192.868 210.992 165.386 1.00 15.81 ? 1488 ARG A CB    1 
ATOM   277   C  CG    . ARG A 1 1488 ? 192.851 211.577 163.984 1.00 27.26 ? 1488 ARG A CG    1 
ATOM   278   C  CD    . ARG A 1 1488 ? 191.549 211.305 163.236 1.00 28.09 ? 1488 ARG A CD    1 
ATOM   279   N  NE    . ARG A 1 1488 ? 190.367 211.983 163.745 1.00 28.35 ? 1488 ARG A NE    1 
ATOM   280   C  CZ    . ARG A 1 1488 ? 189.141 211.741 163.302 1.00 33.21 ? 1488 ARG A CZ    1 
ATOM   281   N  NH1   . ARG A 1 1488 ? 188.911 210.849 162.352 1.00 30.49 ? 1488 ARG A NH1   1 
ATOM   282   N  NH2   . ARG A 1 1488 ? 188.118 212.409 163.823 1.00 33.14 ? 1488 ARG A NH2   1 
ATOM   283   N  N     . GLY A 1 1489 ? 195.339 209.691 164.854 1.00 14.90 ? 1489 GLY A N     1 
ATOM   284   C  CA    . GLY A 1 1489 ? 196.402 209.216 163.983 1.00 15.69 ? 1489 GLY A CA    1 
ATOM   285   C  C     . GLY A 1 1489 ? 197.728 208.997 164.672 1.00 14.63 ? 1489 GLY A C     1 
ATOM   286   O  O     . GLY A 1 1489 ? 198.779 209.251 164.073 1.00 18.63 ? 1489 GLY A O     1 
ATOM   287   N  N     . TRP A 1 1490 ? 197.709 208.517 165.915 1.00 11.14 ? 1490 TRP A N     1 
ATOM   288   C  CA    . TRP A 1 1490 ? 198.954 208.245 166.624 1.00 11.84 ? 1490 TRP A CA    1 
ATOM   289   C  C     . TRP A 1 1490 ? 199.746 207.129 165.959 1.00 19.18 ? 1490 TRP A C     1 
ATOM   290   O  O     . TRP A 1 1490 ? 200.980 207.183 165.904 1.00 18.71 ? 1490 TRP A O     1 
ATOM   291   C  CB    . TRP A 1 1490 ? 198.661 207.905 168.080 1.00 11.07 ? 1490 TRP A CB    1 
ATOM   292   C  CG    . TRP A 1 1490 ? 198.106 209.057 168.811 1.00 11.13 ? 1490 TRP A CG    1 
ATOM   293   C  CD1   . TRP A 1 1490 ? 196.806 209.275 169.153 1.00 9.47  ? 1490 TRP A CD1   1 
ATOM   294   C  CD2   . TRP A 1 1490 ? 198.839 210.190 169.261 1.00 14.35 ? 1490 TRP A CD2   1 
ATOM   295   N  NE1   . TRP A 1 1490 ? 196.692 210.473 169.816 1.00 6.58  ? 1490 TRP A NE1   1 
ATOM   296   C  CE2   . TRP A 1 1490 ? 197.929 211.055 169.890 1.00 7.68  ? 1490 TRP A CE2   1 
ATOM   297   C  CE3   . TRP A 1 1490 ? 200.187 210.552 169.201 1.00 11.85 ? 1490 TRP A CE3   1 
ATOM   298   C  CZ2   . TRP A 1 1490 ? 198.323 212.256 170.455 1.00 8.25  ? 1490 TRP A CZ2   1 
ATOM   299   C  CZ3   . TRP A 1 1490 ? 200.573 211.740 169.758 1.00 10.92 ? 1490 TRP A CZ3   1 
ATOM   300   C  CH2   . TRP A 1 1490 ? 199.649 212.577 170.377 1.00 6.49  ? 1490 TRP A CH2   1 
ATOM   301   N  N     . ASP A 1 1491 ? 199.057 206.100 165.462 1.00 15.33 ? 1491 ASP A N     1 
ATOM   302   C  CA    . ASP A 1 1491 ? 199.755 205.040 164.747 1.00 15.57 ? 1491 ASP A CA    1 
ATOM   303   C  C     . ASP A 1 1491 ? 200.426 205.579 163.490 1.00 18.30 ? 1491 ASP A C     1 
ATOM   304   O  O     . ASP A 1 1491 ? 201.571 205.227 163.191 1.00 19.96 ? 1491 ASP A O     1 
ATOM   305   C  CB    . ASP A 1 1491 ? 198.783 203.911 164.407 1.00 18.07 ? 1491 ASP A CB    1 
ATOM   306   C  CG    . ASP A 1 1491 ? 198.604 202.935 165.554 1.00 27.14 ? 1491 ASP A CG    1 
ATOM   307   O  OD1   . ASP A 1 1491 ? 199.609 202.335 165.989 1.00 31.16 ? 1491 ASP A OD1   1 
ATOM   308   O  OD2   . ASP A 1 1491 ? 197.458 202.768 166.021 1.00 31.37 ? 1491 ASP A OD2   1 
ATOM   309   N  N     . ASP A 1 1492 ? 199.732 206.445 162.748 1.00 18.80 ? 1492 ASP A N     1 
ATOM   310   C  CA    . ASP A 1 1492 ? 200.328 207.030 161.550 1.00 17.93 ? 1492 ASP A CA    1 
ATOM   311   C  C     . ASP A 1 1492 ? 201.525 207.906 161.899 1.00 20.36 ? 1492 ASP A C     1 
ATOM   312   O  O     . ASP A 1 1492 ? 202.553 207.863 161.213 1.00 21.47 ? 1492 ASP A O     1 
ATOM   313   C  CB    . ASP A 1 1492 ? 199.280 207.835 160.782 1.00 17.72 ? 1492 ASP A CB    1 
ATOM   314   C  CG    . ASP A 1 1492 ? 198.135 206.978 160.292 1.00 26.87 ? 1492 ASP A CG    1 
ATOM   315   O  OD1   . ASP A 1 1492 ? 198.389 206.027 159.524 1.00 28.56 ? 1492 ASP A OD1   1 
ATOM   316   O  OD2   . ASP A 1 1492 ? 196.977 207.255 160.670 1.00 32.01 ? 1492 ASP A OD2   1 
ATOM   317   N  N     . LEU A 1 1493 ? 201.407 208.711 162.957 1.00 21.33 ? 1493 LEU A N     1 
ATOM   318   C  CA    . LEU A 1 1493 ? 202.511 209.571 163.375 1.00 13.89 ? 1493 LEU A CA    1 
ATOM   319   C  C     . LEU A 1 1493 ? 203.722 208.756 163.812 1.00 14.54 ? 1493 LEU A C     1 
ATOM   320   O  O     . LEU A 1 1493 ? 204.856 209.043 163.414 1.00 18.27 ? 1493 LEU A O     1 
ATOM   321   C  CB    . LEU A 1 1493 ? 202.049 210.489 164.507 1.00 16.99 ? 1493 LEU A CB    1 
ATOM   322   C  CG    . LEU A 1 1493 ? 202.942 211.659 164.930 1.00 13.36 ? 1493 LEU A CG    1 
ATOM   323   C  CD1   . LEU A 1 1493 ? 203.064 212.703 163.849 1.00 16.59 ? 1493 LEU A CD1   1 
ATOM   324   C  CD2   . LEU A 1 1493 ? 202.399 212.275 166.206 1.00 11.50 ? 1493 LEU A CD2   1 
ATOM   325   N  N     . PHE A 1 1494 ? 203.499 207.730 164.633 1.00 16.05 ? 1494 PHE A N     1 
ATOM   326   C  CA    . PHE A 1 1494 ? 204.620 207.007 165.225 1.00 15.92 ? 1494 PHE A CA    1 
ATOM   327   C  C     . PHE A 1 1494 ? 205.334 206.135 164.199 1.00 19.11 ? 1494 PHE A C     1 
ATOM   328   O  O     . PHE A 1 1494 ? 206.569 206.102 164.162 1.00 18.39 ? 1494 PHE A O     1 
ATOM   329   C  CB    . PHE A 1 1494 ? 204.135 206.175 166.409 1.00 14.24 ? 1494 PHE A CB    1 
ATOM   330   C  CG    . PHE A 1 1494 ? 203.838 206.990 167.633 1.00 13.35 ? 1494 PHE A CG    1 
ATOM   331   C  CD1   . PHE A 1 1494 ? 204.540 208.154 167.887 1.00 15.80 ? 1494 PHE A CD1   1 
ATOM   332   C  CD2   . PHE A 1 1494 ? 202.855 206.599 168.522 1.00 15.51 ? 1494 PHE A CD2   1 
ATOM   333   C  CE1   . PHE A 1 1494 ? 204.270 208.913 169.008 1.00 9.72  ? 1494 PHE A CE1   1 
ATOM   334   C  CE2   . PHE A 1 1494 ? 202.582 207.355 169.647 1.00 16.67 ? 1494 PHE A CE2   1 
ATOM   335   C  CZ    . PHE A 1 1494 ? 203.292 208.511 169.889 1.00 11.99 ? 1494 PHE A CZ    1 
ATOM   336   N  N     . ASN A 1 1495 ? 204.579 205.419 163.362 1.00 17.86 ? 1495 ASN A N     1 
ATOM   337   C  CA    . ASN A 1 1495 ? 205.210 204.594 162.336 1.00 19.36 ? 1495 ASN A CA    1 
ATOM   338   C  C     . ASN A 1 1495 ? 205.950 205.448 161.315 1.00 15.26 ? 1495 ASN A C     1 
ATOM   339   O  O     . ASN A 1 1495 ? 207.037 205.074 160.861 1.00 17.04 ? 1495 ASN A O     1 
ATOM   340   C  CB    . ASN A 1 1495 ? 204.174 203.709 161.646 1.00 15.38 ? 1495 ASN A CB    1 
ATOM   341   C  CG    . ASN A 1 1495 ? 203.294 202.970 162.628 1.00 19.26 ? 1495 ASN A CG    1 
ATOM   342   O  OD1   . ASN A 1 1495 ? 203.695 202.703 163.760 1.00 26.86 ? 1495 ASN A OD1   1 
ATOM   343   N  ND2   . ASN A 1 1495 ? 202.084 202.632 162.201 1.00 21.14 ? 1495 ASN A ND2   1 
ATOM   344   N  N     . LYS A 1 1496 ? 205.378 206.592 160.936 1.00 17.34 ? 1496 LYS A N     1 
ATOM   345   C  CA    . LYS A 1 1496 ? 206.056 207.469 159.985 1.00 15.65 ? 1496 LYS A CA    1 
ATOM   346   C  C     . LYS A 1 1496 ? 207.381 207.963 160.546 1.00 18.71 ? 1496 LYS A C     1 
ATOM   347   O  O     . LYS A 1 1496 ? 208.397 207.967 159.842 1.00 21.95 ? 1496 LYS A O     1 
ATOM   348   C  CB    . LYS A 1 1496 ? 205.157 208.649 159.618 1.00 18.19 ? 1496 LYS A CB    1 
ATOM   349   C  CG    . LYS A 1 1496 ? 205.758 209.594 158.591 1.00 19.28 ? 1496 LYS A CG    1 
ATOM   350   C  CD    . LYS A 1 1496 ? 206.009 208.894 157.264 1.00 21.64 ? 1496 LYS A CD    1 
ATOM   351   C  CE    . LYS A 1 1496 ? 204.712 208.464 156.607 1.00 23.20 ? 1496 LYS A CE    1 
ATOM   352   N  NZ    . LYS A 1 1496 ? 203.908 209.634 156.159 1.00 23.95 ? 1496 LYS A NZ    1 
ATOM   353   N  N     . VAL A 1 1497 ? 207.394 208.374 161.816 1.00 20.93 ? 1497 VAL A N     1 
ATOM   354   C  CA    . VAL A 1 1497 ? 208.635 208.831 162.435 1.00 14.33 ? 1497 VAL A CA    1 
ATOM   355   C  C     . VAL A 1 1497 ? 209.638 207.686 162.522 1.00 13.41 ? 1497 VAL A C     1 
ATOM   356   O  O     . VAL A 1 1497 ? 210.818 207.850 162.195 1.00 14.73 ? 1497 VAL A O     1 
ATOM   357   C  CB    . VAL A 1 1497 ? 208.353 209.445 163.819 1.00 15.55 ? 1497 VAL A CB    1 
ATOM   358   C  CG1   . VAL A 1 1497 ? 209.643 209.623 164.594 1.00 13.01 ? 1497 VAL A CG1   1 
ATOM   359   C  CG2   . VAL A 1 1497 ? 207.640 210.772 163.674 1.00 15.54 ? 1497 VAL A CG2   1 
ATOM   360   N  N     . LYS A 1 1498 ? 209.182 206.503 162.951 1.00 13.88 ? 1498 LYS A N     1 
ATOM   361   C  CA    . LYS A 1 1498 ? 210.080 205.356 163.048 1.00 15.82 ? 1498 LYS A CA    1 
ATOM   362   C  C     . LYS A 1 1498 ? 210.662 204.992 161.689 1.00 15.72 ? 1498 LYS A C     1 
ATOM   363   O  O     . LYS A 1 1498 ? 211.845 204.652 161.584 1.00 16.61 ? 1498 LYS A O     1 
ATOM   364   C  CB    . LYS A 1 1498 ? 209.354 204.149 163.644 1.00 16.07 ? 1498 LYS A CB    1 
ATOM   365   C  CG    . LYS A 1 1498 ? 208.992 204.257 165.115 1.00 16.84 ? 1498 LYS A CG    1 
ATOM   366   C  CD    . LYS A 1 1498 ? 208.159 203.051 165.536 1.00 23.95 ? 1498 LYS A CD    1 
ATOM   367   C  CE    . LYS A 1 1498 ? 207.054 203.416 166.516 1.00 18.30 ? 1498 LYS A CE    1 
ATOM   368   N  NZ    . LYS A 1 1498 ? 207.424 204.541 167.408 1.00 22.93 ? 1498 LYS A NZ    1 
ATOM   369   N  N     . GLU A 1 1499 ? 209.843 205.056 160.637 1.00 16.65 ? 1499 GLU A N     1 
ATOM   370   C  CA    . GLU A 1 1499 ? 210.317 204.695 159.306 1.00 16.38 ? 1499 GLU A CA    1 
ATOM   371   C  C     . GLU A 1 1499 ? 211.448 205.610 158.851 1.00 20.77 ? 1499 GLU A C     1 
ATOM   372   O  O     . GLU A 1 1499 ? 212.458 205.137 158.317 1.00 27.50 ? 1499 GLU A O     1 
ATOM   373   C  CB    . GLU A 1 1499 ? 209.155 204.726 158.315 1.00 15.68 ? 1499 GLU A CB    1 
ATOM   374   C  CG    . GLU A 1 1499 ? 209.456 204.122 156.951 1.00 26.35 ? 1499 GLU A CG    1 
ATOM   375   C  CD    . GLU A 1 1499 ? 210.132 205.097 156.008 1.00 33.58 ? 1499 GLU A CD    1 
ATOM   376   O  OE1   . GLU A 1 1499 ? 209.897 206.316 156.147 1.00 32.69 ? 1499 GLU A OE1   1 
ATOM   377   O  OE2   . GLU A 1 1499 ? 210.891 204.645 155.127 1.00 39.69 ? 1499 GLU A OE2   1 
ATOM   378   N  N     . HIS A 1 1500 ? 211.303 206.921 159.059 1.00 17.29 ? 1500 HIS A N     1 
ATOM   379   C  CA    . HIS A 1 1500 ? 212.375 207.836 158.688 1.00 16.37 ? 1500 HIS A CA    1 
ATOM   380   C  C     . HIS A 1 1500 ? 213.587 207.684 159.600 1.00 19.42 ? 1500 HIS A C     1 
ATOM   381   O  O     . HIS A 1 1500 ? 214.724 207.848 159.146 1.00 18.13 ? 1500 HIS A O     1 
ATOM   382   C  CB    . HIS A 1 1500 ? 211.876 209.281 158.709 1.00 15.95 ? 1500 HIS A CB    1 
ATOM   383   C  CG    . HIS A 1 1500 ? 210.817 209.568 157.690 1.00 21.08 ? 1500 HIS A CG    1 
ATOM   384   N  ND1   . HIS A 1 1500 ? 211.094 209.708 156.349 1.00 24.39 ? 1500 HIS A ND1   1 
ATOM   385   C  CD2   . HIS A 1 1500 ? 209.485 209.770 157.820 1.00 22.83 ? 1500 HIS A CD2   1 
ATOM   386   C  CE1   . HIS A 1 1500 ? 209.979 209.967 155.693 1.00 26.63 ? 1500 HIS A CE1   1 
ATOM   387   N  NE2   . HIS A 1 1500 ? 208.987 210.012 156.564 1.00 23.87 ? 1500 HIS A NE2   1 
ATOM   388   N  N     . ILE A 1 1501 ? 213.366 207.380 160.882 1.00 22.01 ? 1501 ILE A N     1 
ATOM   389   C  CA    . ILE A 1 1501 ? 214.481 207.183 161.804 1.00 16.17 ? 1501 ILE A CA    1 
ATOM   390   C  C     . ILE A 1 1501 ? 215.309 205.976 161.384 1.00 21.88 ? 1501 ILE A C     1 
ATOM   391   O  O     . ILE A 1 1501 ? 216.546 206.016 161.397 1.00 25.84 ? 1501 ILE A O     1 
ATOM   392   C  CB    . ILE A 1 1501 ? 213.964 207.052 163.248 1.00 17.81 ? 1501 ILE A CB    1 
ATOM   393   C  CG1   . ILE A 1 1501 ? 213.496 208.412 163.768 1.00 17.75 ? 1501 ILE A CG1   1 
ATOM   394   C  CG2   . ILE A 1 1501 ? 215.039 206.489 164.164 1.00 15.45 ? 1501 ILE A CG2   1 
ATOM   395   C  CD1   . ILE A 1 1501 ? 213.026 208.395 165.203 1.00 13.37 ? 1501 ILE A CD1   1 
ATOM   396   N  N     . ASN A 1 1502 ? 214.644 204.883 161.002 1.00 23.37 ? 1502 ASN A N     1 
ATOM   397   C  CA    . ASN A 1 1502 ? 215.366 203.720 160.502 1.00 21.43 ? 1502 ASN A CA    1 
ATOM   398   C  C     . ASN A 1 1502 ? 216.104 204.040 159.207 1.00 24.02 ? 1502 ASN A C     1 
ATOM   399   O  O     . ASN A 1 1502 ? 217.264 203.649 159.034 1.00 27.03 ? 1502 ASN A O     1 
ATOM   400   C  CB    . ASN A 1 1502 ? 214.404 202.549 160.291 1.00 18.68 ? 1502 ASN A CB    1 
ATOM   401   C  CG    . ASN A 1 1502 ? 213.626 202.207 161.542 1.00 24.55 ? 1502 ASN A CG    1 
ATOM   402   O  OD1   . ASN A 1 1502 ? 214.119 202.366 162.657 1.00 25.26 ? 1502 ASN A OD1   1 
ATOM   403   N  ND2   . ASN A 1 1502 ? 212.397 201.732 161.363 1.00 22.56 ? 1502 ASN A ND2   1 
ATOM   404   N  N     . SER A 1 1503 ? 215.448 204.753 158.286 1.00 19.19 ? 1503 SER A N     1 
ATOM   405   C  CA    . SER A 1 1503 ? 216.080 205.074 157.010 1.00 20.11 ? 1503 SER A CA    1 
ATOM   406   C  C     . SER A 1 1503 ? 217.306 205.958 157.207 1.00 26.76 ? 1503 SER A C     1 
ATOM   407   O  O     . SER A 1 1503 ? 218.333 205.764 156.546 1.00 33.17 ? 1503 SER A O     1 
ATOM   408   C  CB    . SER A 1 1503 ? 215.078 205.749 156.076 1.00 19.62 ? 1503 SER A CB    1 
ATOM   409   O  OG    . SER A 1 1503 ? 214.731 207.039 156.544 1.00 28.75 ? 1503 SER A OG    1 
ATOM   410   N  N     . VAL A 1 1504 ? 217.216 206.938 158.109 1.00 26.60 ? 1504 VAL A N     1 
ATOM   411   C  CA    . VAL A 1 1504 ? 218.379 207.762 158.428 1.00 26.03 ? 1504 VAL A CA    1 
ATOM   412   C  C     . VAL A 1 1504 ? 219.479 206.911 159.047 1.00 26.05 ? 1504 VAL A C     1 
ATOM   413   O  O     . VAL A 1 1504 ? 220.660 207.057 158.716 1.00 30.49 ? 1504 VAL A O     1 
ATOM   414   C  CB    . VAL A 1 1504 ? 217.972 208.928 159.349 1.00 22.86 ? 1504 VAL A CB    1 
ATOM   415   C  CG1   . VAL A 1 1504 ? 219.193 209.539 160.014 1.00 24.11 ? 1504 VAL A CG1   1 
ATOM   416   C  CG2   . VAL A 1 1504 ? 217.213 209.981 158.564 1.00 20.23 ? 1504 VAL A CG2   1 
ATOM   417   N  N     . SER A 1 1505 ? 219.113 206.012 159.963 1.00 24.67 ? 1505 SER A N     1 
ATOM   418   C  CA    . SER A 1 1505 ? 220.103 205.125 160.564 1.00 27.10 ? 1505 SER A CA    1 
ATOM   419   C  C     . SER A 1 1505 ? 220.696 204.177 159.529 1.00 26.74 ? 1505 SER A C     1 
ATOM   420   O  O     . SER A 1 1505 ? 221.910 203.944 159.505 1.00 32.01 ? 1505 SER A O     1 
ATOM   421   C  CB    . SER A 1 1505 ? 219.476 204.341 161.717 1.00 20.19 ? 1505 SER A CB    1 
ATOM   422   O  OG    . SER A 1 1505 ? 219.140 205.201 162.789 1.00 29.75 ? 1505 SER A OG    1 
ATOM   423   N  N     . ALA A 1 1506 ? 219.849 203.621 158.659 1.00 27.60 ? 1506 ALA A N     1 
ATOM   424   C  CA    . ALA A 1 1506 ? 220.323 202.672 157.657 1.00 27.27 ? 1506 ALA A CA    1 
ATOM   425   C  C     . ALA A 1 1506 ? 221.235 203.318 156.627 1.00 27.89 ? 1506 ALA A C     1 
ATOM   426   O  O     . ALA A 1 1506 ? 222.178 202.673 156.161 1.00 35.10 ? 1506 ALA A O     1 
ATOM   427   C  CB    . ALA A 1 1506 ? 219.138 202.011 156.951 1.00 24.23 ? 1506 ALA A CB    1 
ATOM   428   N  N     . MET A 1 1507 ? 220.977 204.576 156.263 1.00 27.58 ? 1507 MET A N     1 
ATOM   429   C  CA    . MET A 1 1507 ? 221.778 205.229 155.234 1.00 30.16 ? 1507 MET A CA    1 
ATOM   430   C  C     . MET A 1 1507 ? 223.166 205.602 155.743 1.00 33.07 ? 1507 MET A C     1 
ATOM   431   O  O     . MET A 1 1507 ? 224.035 205.964 154.945 1.00 34.13 ? 1507 MET A O     1 
ATOM   432   C  CB    . MET A 1 1507 ? 221.041 206.460 154.708 1.00 27.29 ? 1507 MET A CB    1 
ATOM   433   C  CG    . MET A 1 1507 ? 220.958 207.603 155.694 1.00 25.56 ? 1507 MET A CG    1 
ATOM   434   S  SD    . MET A 1 1507 ? 220.721 209.209 154.919 1.00 53.56 ? 1507 MET A SD    1 
ATOM   435   C  CE    . MET A 1 1507 ? 218.931 209.300 154.931 1.00 30.51 ? 1507 MET A CE    1 
ATOM   436   N  N     . LYS A 1 1508 ? 223.394 205.528 157.057 1.00 28.53 ? 1508 LYS A N     1 
ATOM   437   C  CA    . LYS A 1 1508 ? 224.749 205.720 157.571 1.00 28.50 ? 1508 LYS A CA    1 
ATOM   438   C  C     . LYS A 1 1508 ? 225.672 204.588 157.138 1.00 32.57 ? 1508 LYS A C     1 
ATOM   439   O  O     . LYS A 1 1508 ? 226.876 204.804 156.952 1.00 32.96 ? 1508 LYS A O     1 
ATOM   440   C  CB    . LYS A 1 1508 ? 224.735 205.842 159.094 1.00 29.08 ? 1508 LYS A CB    1 
ATOM   441   C  CG    . LYS A 1 1508 ? 223.748 206.860 159.629 1.00 30.77 ? 1508 LYS A CG    1 
ATOM   442   C  CD    . LYS A 1 1508 ? 223.630 206.775 161.141 1.00 28.69 ? 1508 LYS A CD    1 
ATOM   443   C  CE    . LYS A 1 1508 ? 222.559 207.718 161.662 1.00 31.74 ? 1508 LYS A CE    1 
ATOM   444   N  NZ    . LYS A 1 1508 ? 222.382 207.594 163.135 1.00 35.82 ? 1508 LYS A NZ    1 
ATOM   445   N  N     . LEU A 1 1509 ? 225.129 203.379 156.977 1.00 33.25 ? 1509 LEU A N     1 
ATOM   446   C  CA    . LEU A 1 1509 ? 225.938 202.247 156.539 1.00 34.76 ? 1509 LEU A CA    1 
ATOM   447   C  C     . LEU A 1 1509 ? 226.443 202.435 155.115 1.00 35.22 ? 1509 LEU A C     1 
ATOM   448   O  O     . LEU A 1 1509 ? 227.497 201.894 154.758 1.00 35.53 ? 1509 LEU A O     1 
ATOM   449   C  CB    . LEU A 1 1509 ? 225.130 200.955 156.645 1.00 27.17 ? 1509 LEU A CB    1 
ATOM   450   C  CG    . LEU A 1 1509 ? 224.347 200.745 157.942 1.00 34.56 ? 1509 LEU A CG    1 
ATOM   451   C  CD1   . LEU A 1 1509 ? 223.554 199.451 157.884 1.00 30.97 ? 1509 LEU A CD1   1 
ATOM   452   C  CD2   . LEU A 1 1509 ? 225.281 200.749 159.143 1.00 32.16 ? 1509 LEU A CD2   1 
ATOM   453   N  N     . SER A 1 1510 ? 225.712 203.178 154.295 1.00 33.88 ? 1510 SER A N     1 
ATOM   454   C  CA    . SER A 1 1510 ? 226.127 203.396 152.919 1.00 33.58 ? 1510 SER A CA    1 
ATOM   455   C  C     . SER A 1 1510 ? 227.431 204.188 152.885 1.00 36.02 ? 1510 SER A C     1 
ATOM   456   O  O     . SER A 1 1510 ? 227.611 205.127 153.672 1.00 35.85 ? 1510 SER A O     1 
ATOM   457   C  CB    . SER A 1 1510 ? 225.038 204.138 152.143 1.00 32.28 ? 1510 SER A CB    1 
ATOM   458   O  OG    . SER A 1 1510 ? 224.855 205.448 152.653 1.00 37.12 ? 1510 SER A OG    1 
ATOM   459   N  N     . PRO A 1 1511 ? 228.369 203.832 152.004 1.00 39.57 ? 1511 PRO A N     1 
ATOM   460   C  CA    . PRO A 1 1511 ? 229.639 204.573 151.947 1.00 33.73 ? 1511 PRO A CA    1 
ATOM   461   C  C     . PRO A 1 1511 ? 229.480 206.032 151.552 1.00 33.71 ? 1511 PRO A C     1 
ATOM   462   O  O     . PRO A 1 1511 ? 230.326 206.857 151.915 1.00 34.27 ? 1511 PRO A O     1 
ATOM   463   C  CB    . PRO A 1 1511 ? 230.453 203.789 150.910 1.00 33.68 ? 1511 PRO A CB    1 
ATOM   464   C  CG    . PRO A 1 1511 ? 229.426 203.112 150.064 1.00 35.73 ? 1511 PRO A CG    1 
ATOM   465   C  CD    . PRO A 1 1511 ? 228.315 202.752 151.005 1.00 35.16 ? 1511 PRO A CD    1 
ATOM   466   N  N     . TYR A 1 1512 ? 228.421 206.379 150.823 1.00 31.33 ? 1512 TYR A N     1 
ATOM   467   C  CA    . TYR A 1 1512 ? 228.209 207.746 150.360 1.00 31.89 ? 1512 TYR A CA    1 
ATOM   468   C  C     . TYR A 1 1512 ? 227.543 208.632 151.407 1.00 33.39 ? 1512 TYR A C     1 
ATOM   469   O  O     . TYR A 1 1512 ? 226.990 209.682 151.058 1.00 34.01 ? 1512 TYR A O     1 
ATOM   470   C  CB    . TYR A 1 1512 ? 227.380 207.745 149.074 1.00 33.09 ? 1512 TYR A CB    1 
ATOM   471   C  CG    . TYR A 1 1512 ? 227.891 206.799 148.008 1.00 32.65 ? 1512 TYR A CG    1 
ATOM   472   C  CD1   . TYR A 1 1512 ? 229.255 206.620 147.804 1.00 37.51 ? 1512 TYR A CD1   1 
ATOM   473   C  CD2   . TYR A 1 1512 ? 227.010 206.083 147.209 1.00 33.98 ? 1512 TYR A CD2   1 
ATOM   474   C  CE1   . TYR A 1 1512 ? 229.723 205.757 146.833 1.00 36.98 ? 1512 TYR A CE1   1 
ATOM   475   C  CE2   . TYR A 1 1512 ? 227.469 205.218 146.235 1.00 34.76 ? 1512 TYR A CE2   1 
ATOM   476   C  CZ    . TYR A 1 1512 ? 228.827 205.059 146.052 1.00 37.63 ? 1512 TYR A CZ    1 
ATOM   477   O  OH    . TYR A 1 1512 ? 229.289 204.198 145.083 1.00 41.90 ? 1512 TYR A OH    1 
ATOM   478   N  N     . TYR A 1 1513 ? 227.587 208.230 152.677 1.00 33.29 ? 1513 TYR A N     1 
ATOM   479   C  CA    . TYR A 1 1513 ? 226.932 208.974 153.744 1.00 28.07 ? 1513 TYR A CA    1 
ATOM   480   C  C     . TYR A 1 1513 ? 227.716 210.211 154.171 1.00 32.72 ? 1513 TYR A C     1 
ATOM   481   O  O     . TYR A 1 1513 ? 227.151 211.087 154.834 1.00 36.18 ? 1513 TYR A O     1 
ATOM   482   C  CB    . TYR A 1 1513 ? 226.709 208.046 154.943 1.00 27.16 ? 1513 TYR A CB    1 
ATOM   483   C  CG    . TYR A 1 1513 ? 226.110 208.707 156.165 1.00 31.72 ? 1513 TYR A CG    1 
ATOM   484   C  CD1   . TYR A 1 1513 ? 224.748 208.969 156.236 1.00 31.47 ? 1513 TYR A CD1   1 
ATOM   485   C  CD2   . TYR A 1 1513 ? 226.904 209.058 157.248 1.00 28.99 ? 1513 TYR A CD2   1 
ATOM   486   C  CE1   . TYR A 1 1513 ? 224.195 209.568 157.350 1.00 32.58 ? 1513 TYR A CE1   1 
ATOM   487   C  CE2   . TYR A 1 1513 ? 226.360 209.659 158.366 1.00 33.34 ? 1513 TYR A CE2   1 
ATOM   488   C  CZ    . TYR A 1 1513 ? 225.006 209.912 158.412 1.00 36.05 ? 1513 TYR A CZ    1 
ATOM   489   O  OH    . TYR A 1 1513 ? 224.460 210.509 159.522 1.00 36.12 ? 1513 TYR A OH    1 
ATOM   490   N  N     . LYS A 1 1514 ? 228.992 210.311 153.791 1.00 33.24 ? 1514 LYS A N     1 
ATOM   491   C  CA    . LYS A 1 1514 ? 229.826 211.412 154.268 1.00 30.67 ? 1514 LYS A CA    1 
ATOM   492   C  C     . LYS A 1 1514 ? 229.354 212.757 153.725 1.00 31.38 ? 1514 LYS A C     1 
ATOM   493   O  O     . LYS A 1 1514 ? 229.379 213.762 154.444 1.00 31.15 ? 1514 LYS A O     1 
ATOM   494   C  CB    . LYS A 1 1514 ? 231.286 211.163 153.887 1.00 26.75 ? 1514 LYS A CB    1 
ATOM   495   C  CG    . LYS A 1 1514 ? 232.256 212.187 154.453 1.00 29.41 ? 1514 LYS A CG    1 
ATOM   496   C  CD    . LYS A 1 1514 ? 232.103 212.322 155.961 1.00 32.02 ? 1514 LYS A CD    1 
ATOM   497   C  CE    . LYS A 1 1514 ? 233.018 213.404 156.511 1.00 33.10 ? 1514 LYS A CE    1 
ATOM   498   N  NZ    . LYS A 1 1514 ? 232.874 213.559 157.986 1.00 29.50 ? 1514 LYS A NZ    1 
ATOM   499   N  N     . VAL A 1 1515 ? 228.928 212.800 152.461 1.00 28.70 ? 1515 VAL A N     1 
ATOM   500   C  CA    . VAL A 1 1515 ? 228.558 214.073 151.849 1.00 29.08 ? 1515 VAL A CA    1 
ATOM   501   C  C     . VAL A 1 1515 ? 227.301 214.640 152.497 1.00 32.56 ? 1515 VAL A C     1 
ATOM   502   O  O     . VAL A 1 1515 ? 227.168 215.858 152.664 1.00 30.88 ? 1515 VAL A O     1 
ATOM   503   C  CB    . VAL A 1 1515 ? 228.396 213.907 150.325 1.00 30.50 ? 1515 VAL A CB    1 
ATOM   504   C  CG1   . VAL A 1 1515 ? 227.333 212.863 149.999 1.00 28.55 ? 1515 VAL A CG1   1 
ATOM   505   C  CG2   . VAL A 1 1515 ? 228.065 215.239 149.672 1.00 27.41 ? 1515 VAL A CG2   1 
ATOM   506   N  N     . PHE A 1 1516 ? 226.364 213.773 152.880 1.00 31.47 ? 1516 PHE A N     1 
ATOM   507   C  CA    . PHE A 1 1516 ? 225.097 214.190 153.468 1.00 26.65 ? 1516 PHE A CA    1 
ATOM   508   C  C     . PHE A 1 1516 ? 225.033 213.905 154.963 1.00 30.22 ? 1516 PHE A C     1 
ATOM   509   O  O     . PHE A 1 1516 ? 223.937 213.799 155.525 1.00 29.82 ? 1516 PHE A O     1 
ATOM   510   C  CB    . PHE A 1 1516 ? 223.935 213.505 152.749 1.00 28.61 ? 1516 PHE A CB    1 
ATOM   511   C  CG    . PHE A 1 1516 ? 223.944 213.698 151.261 1.00 29.63 ? 1516 PHE A CG    1 
ATOM   512   C  CD1   . PHE A 1 1516 ? 224.197 214.945 150.714 1.00 27.99 ? 1516 PHE A CD1   1 
ATOM   513   C  CD2   . PHE A 1 1516 ? 223.706 212.632 150.410 1.00 28.11 ? 1516 PHE A CD2   1 
ATOM   514   C  CE1   . PHE A 1 1516 ? 224.206 215.125 149.344 1.00 31.24 ? 1516 PHE A CE1   1 
ATOM   515   C  CE2   . PHE A 1 1516 ? 223.715 212.805 149.041 1.00 30.37 ? 1516 PHE A CE2   1 
ATOM   516   C  CZ    . PHE A 1 1516 ? 223.965 214.054 148.507 1.00 33.57 ? 1516 PHE A CZ    1 
ATOM   517   N  N     . GLU A 1 1517 ? 226.188 213.774 155.618 1.00 33.74 ? 1517 GLU A N     1 
ATOM   518   C  CA    . GLU A 1 1517 ? 226.208 213.405 157.030 1.00 30.12 ? 1517 GLU A CA    1 
ATOM   519   C  C     . GLU A 1 1517 ? 225.554 214.475 157.895 1.00 22.85 ? 1517 GLU A C     1 
ATOM   520   O  O     . GLU A 1 1517 ? 224.734 214.166 158.766 1.00 27.06 ? 1517 GLU A O     1 
ATOM   521   C  CB    . GLU A 1 1517 ? 227.646 213.153 157.484 1.00 30.75 ? 1517 GLU A CB    1 
ATOM   522   C  CG    . GLU A 1 1517 ? 227.787 212.845 158.964 1.00 36.80 ? 1517 GLU A CG    1 
ATOM   523   C  CD    . GLU A 1 1517 ? 229.186 212.396 159.334 1.00 42.87 ? 1517 GLU A CD    1 
ATOM   524   O  OE1   . GLU A 1 1517 ? 230.143 213.157 159.074 1.00 40.14 ? 1517 GLU A OE1   1 
ATOM   525   O  OE2   . GLU A 1 1517 ? 229.329 211.286 159.886 1.00 41.55 ? 1517 GLU A OE2   1 
ATOM   526   N  N     . GLU A 1 1518 ? 225.900 215.744 157.665 1.00 25.47 ? 1518 GLU A N     1 
ATOM   527   C  CA    . GLU A 1 1518 ? 225.369 216.813 158.505 1.00 28.74 ? 1518 GLU A CA    1 
ATOM   528   C  C     . GLU A 1 1518 ? 223.859 216.947 158.346 1.00 27.18 ? 1518 GLU A C     1 
ATOM   529   O  O     . GLU A 1 1518 ? 223.135 217.110 159.336 1.00 27.18 ? 1518 GLU A O     1 
ATOM   530   C  CB    . GLU A 1 1518 ? 226.064 218.134 158.177 1.00 21.77 ? 1518 GLU A CB    1 
ATOM   531   C  CG    . GLU A 1 1518 ? 225.588 219.309 159.019 1.00 26.03 ? 1518 GLU A CG    1 
ATOM   532   C  CD    . GLU A 1 1518 ? 226.008 220.647 158.445 1.00 37.53 ? 1518 GLU A CD    1 
ATOM   533   O  OE1   . GLU A 1 1518 ? 225.637 220.946 157.291 1.00 33.74 ? 1518 GLU A OE1   1 
ATOM   534   O  OE2   . GLU A 1 1518 ? 226.713 221.402 159.149 1.00 41.61 ? 1518 GLU A OE2   1 
ATOM   535   N  N     . ASP A 1 1519 ? 223.365 216.882 157.109 1.00 28.61 ? 1519 ASP A N     1 
ATOM   536   C  CA    . ASP A 1 1519 ? 221.929 217.004 156.879 1.00 23.74 ? 1519 ASP A CA    1 
ATOM   537   C  C     . ASP A 1 1519 ? 221.172 215.821 157.474 1.00 24.84 ? 1519 ASP A C     1 
ATOM   538   O  O     . ASP A 1 1519 ? 220.096 215.996 158.057 1.00 26.92 ? 1519 ASP A O     1 
ATOM   539   C  CB    . ASP A 1 1519 ? 221.652 217.138 155.384 1.00 19.53 ? 1519 ASP A CB    1 
ATOM   540   C  CG    . ASP A 1 1519 ? 220.265 217.678 155.095 1.00 33.87 ? 1519 ASP A CG    1 
ATOM   541   O  OD1   . ASP A 1 1519 ? 219.863 218.666 155.744 1.00 35.01 ? 1519 ASP A OD1   1 
ATOM   542   O  OD2   . ASP A 1 1519 ? 219.584 217.130 154.204 1.00 35.81 ? 1519 ASP A OD2   1 
ATOM   543   N  N     . ALA A 1 1520 ? 221.715 214.611 157.332 1.00 24.82 ? 1520 ALA A N     1 
ATOM   544   C  CA    . ALA A 1 1520 ? 221.086 213.446 157.944 1.00 21.70 ? 1520 ALA A CA    1 
ATOM   545   C  C     . ALA A 1 1520 ? 221.104 213.540 159.466 1.00 22.71 ? 1520 ALA A C     1 
ATOM   546   O  O     . ALA A 1 1520 ? 220.118 213.198 160.126 1.00 24.86 ? 1520 ALA A O     1 
ATOM   547   C  CB    . ALA A 1 1520 ? 221.778 212.167 157.476 1.00 18.51 ? 1520 ALA A CB    1 
ATOM   548   N  N     . LEU A 1 1521 ? 222.220 213.998 160.041 1.00 24.74 ? 1521 LEU A N     1 
ATOM   549   C  CA    . LEU A 1 1521 ? 222.288 214.166 161.489 1.00 21.46 ? 1521 LEU A CA    1 
ATOM   550   C  C     . LEU A 1 1521 ? 221.323 215.238 161.974 1.00 20.52 ? 1521 LEU A C     1 
ATOM   551   O  O     . LEU A 1 1521 ? 220.796 215.138 163.087 1.00 22.09 ? 1521 LEU A O     1 
ATOM   552   C  CB    . LEU A 1 1521 ? 223.714 214.505 161.919 1.00 22.69 ? 1521 LEU A CB    1 
ATOM   553   C  CG    . LEU A 1 1521 ? 224.719 213.356 161.908 1.00 23.11 ? 1521 LEU A CG    1 
ATOM   554   C  CD1   . LEU A 1 1521 ? 226.093 213.850 162.326 1.00 21.57 ? 1521 LEU A CD1   1 
ATOM   555   C  CD2   . LEU A 1 1521 ? 224.252 212.227 162.810 1.00 20.95 ? 1521 LEU A CD2   1 
ATOM   556   N  N     . SER A 1 1522 ? 221.092 216.272 161.163 1.00 17.37 ? 1522 SER A N     1 
ATOM   557   C  CA    . SER A 1 1522 ? 220.081 217.264 161.506 1.00 20.82 ? 1522 SER A CA    1 
ATOM   558   C  C     . SER A 1 1522 ? 218.695 216.633 161.558 1.00 19.94 ? 1522 SER A C     1 
ATOM   559   O  O     . SER A 1 1522 ? 217.898 216.941 162.451 1.00 18.55 ? 1522 SER A O     1 
ATOM   560   C  CB    . SER A 1 1522 ? 220.111 218.413 160.500 1.00 21.00 ? 1522 SER A CB    1 
ATOM   561   O  OG    . SER A 1 1522 ? 219.275 218.138 159.390 1.00 25.19 ? 1522 SER A OG    1 
ATOM   562   N  N     . TRP A 1 1523 ? 218.393 215.747 160.606 1.00 17.48 ? 1523 TRP A N     1 
ATOM   563   C  CA    . TRP A 1 1523 ? 217.087 215.100 160.591 1.00 18.82 ? 1523 TRP A CA    1 
ATOM   564   C  C     . TRP A 1 1523 ? 216.956 214.069 161.702 1.00 20.59 ? 1523 TRP A C     1 
ATOM   565   O  O     . TRP A 1 1523 ? 215.860 213.886 162.245 1.00 23.36 ? 1523 TRP A O     1 
ATOM   566   C  CB    . TRP A 1 1523 ? 216.832 214.463 159.227 1.00 15.19 ? 1523 TRP A CB    1 
ATOM   567   C  CG    . TRP A 1 1523 ? 216.268 215.435 158.254 1.00 21.84 ? 1523 TRP A CG    1 
ATOM   568   C  CD1   . TRP A 1 1523 ? 216.923 216.037 157.222 1.00 23.91 ? 1523 TRP A CD1   1 
ATOM   569   C  CD2   . TRP A 1 1523 ? 214.933 215.950 158.238 1.00 24.20 ? 1523 TRP A CD2   1 
ATOM   570   N  NE1   . TRP A 1 1523 ? 216.077 216.884 156.555 1.00 27.31 ? 1523 TRP A NE1   1 
ATOM   571   C  CE2   . TRP A 1 1523 ? 214.847 216.850 157.159 1.00 24.98 ? 1523 TRP A CE2   1 
ATOM   572   C  CE3   . TRP A 1 1523 ? 213.800 215.731 159.028 1.00 18.74 ? 1523 TRP A CE3   1 
ATOM   573   C  CZ2   . TRP A 1 1523 ? 213.675 217.531 156.849 1.00 22.52 ? 1523 TRP A CZ2   1 
ATOM   574   C  CZ3   . TRP A 1 1523 ? 212.639 216.407 158.718 1.00 18.94 ? 1523 TRP A CZ3   1 
ATOM   575   C  CH2   . TRP A 1 1523 ? 212.585 217.297 157.638 1.00 20.00 ? 1523 TRP A CH2   1 
ATOM   576   N  N     . GLU A 1 1524 ? 218.050 213.392 162.057 1.00 18.31 ? 1524 GLU A N     1 
ATOM   577   C  CA    . GLU A 1 1524 ? 218.012 212.468 163.185 1.00 15.60 ? 1524 GLU A CA    1 
ATOM   578   C  C     . GLU A 1 1524 ? 217.644 213.199 164.470 1.00 13.24 ? 1524 GLU A C     1 
ATOM   579   O  O     . GLU A 1 1524 ? 216.870 212.687 165.285 1.00 14.44 ? 1524 GLU A O     1 
ATOM   580   C  CB    . GLU A 1 1524 ? 219.360 211.764 163.333 1.00 19.96 ? 1524 GLU A CB    1 
ATOM   581   C  CG    . GLU A 1 1524 ? 219.487 210.921 164.592 1.00 21.81 ? 1524 GLU A CG    1 
ATOM   582   C  CD    . GLU A 1 1524 ? 220.925 210.570 164.913 1.00 28.07 ? 1524 GLU A CD    1 
ATOM   583   O  OE1   . GLU A 1 1524 ? 221.463 211.105 165.905 1.00 25.76 ? 1524 GLU A OE1   1 
ATOM   584   O  OE2   . GLU A 1 1524 ? 221.519 209.758 164.171 1.00 25.71 ? 1524 GLU A OE2   1 
ATOM   585   N  N     . ASP A 1 1525 ? 218.193 214.399 164.667 1.00 17.36 ? 1525 ASP A N     1 
ATOM   586   C  CA    . ASP A 1 1525 ? 217.829 215.200 165.828 1.00 14.17 ? 1525 ASP A CA    1 
ATOM   587   C  C     . ASP A 1 1525 ? 216.361 215.610 165.785 1.00 16.55 ? 1525 ASP A C     1 
ATOM   588   O  O     . ASP A 1 1525 ? 215.654 215.517 166.795 1.00 16.46 ? 1525 ASP A O     1 
ATOM   589   C  CB    . ASP A 1 1525 ? 218.728 216.429 165.916 1.00 16.01 ? 1525 ASP A CB    1 
ATOM   590   C  CG    . ASP A 1 1525 ? 218.496 217.231 167.175 1.00 24.99 ? 1525 ASP A CG    1 
ATOM   591   O  OD1   . ASP A 1 1525 ? 218.931 216.779 168.258 1.00 28.25 ? 1525 ASP A OD1   1 
ATOM   592   O  OD2   . ASP A 1 1525 ? 217.885 218.314 167.086 1.00 26.79 ? 1525 ASP A OD2   1 
ATOM   593   N  N     . LYS A 1 1526 ? 215.886 216.069 164.625 1.00 15.25 ? 1526 LYS A N     1 
ATOM   594   C  CA    . LYS A 1 1526 ? 214.497 216.509 164.519 1.00 11.45 ? 1526 LYS A CA    1 
ATOM   595   C  C     . LYS A 1 1526 ? 213.531 215.346 164.701 1.00 14.18 ? 1526 LYS A C     1 
ATOM   596   O  O     . LYS A 1 1526 ? 212.541 215.460 165.434 1.00 18.24 ? 1526 LYS A O     1 
ATOM   597   C  CB    . LYS A 1 1526 ? 214.263 217.202 163.173 1.00 14.52 ? 1526 LYS A CB    1 
ATOM   598   C  CG    . LYS A 1 1526 ? 215.003 218.517 163.020 1.00 15.76 ? 1526 LYS A CG    1 
ATOM   599   C  CD    . LYS A 1 1526 ? 214.612 219.241 161.744 1.00 14.10 ? 1526 LYS A CD    1 
ATOM   600   C  CE    . LYS A 1 1526 ? 215.215 218.575 160.523 1.00 21.22 ? 1526 LYS A CE    1 
ATOM   601   N  NZ    . LYS A 1 1526 ? 214.934 219.334 159.275 1.00 25.79 ? 1526 LYS A NZ    1 
ATOM   602   N  N     . LEU A 1 1527 ? 213.805 214.212 164.052 1.00 10.40 ? 1527 LEU A N     1 
ATOM   603   C  CA    . LEU A 1 1527 ? 212.925 213.057 164.188 1.00 10.88 ? 1527 LEU A CA    1 
ATOM   604   C  C     . LEU A 1 1527 ? 212.917 212.534 165.618 1.00 12.44 ? 1527 LEU A C     1 
ATOM   605   O  O     . LEU A 1 1527 ? 211.871 212.120 166.129 1.00 12.50 ? 1527 LEU A O     1 
ATOM   606   C  CB    . LEU A 1 1527 ? 213.346 211.956 163.216 1.00 13.84 ? 1527 LEU A CB    1 
ATOM   607   C  CG    . LEU A 1 1527 ? 213.149 212.235 161.726 1.00 11.76 ? 1527 LEU A CG    1 
ATOM   608   C  CD1   . LEU A 1 1527 ? 214.117 211.404 160.897 1.00 17.59 ? 1527 LEU A CD1   1 
ATOM   609   C  CD2   . LEU A 1 1527 ? 211.716 211.966 161.312 1.00 14.74 ? 1527 LEU A CD2   1 
ATOM   610   N  N     . ASN A 1 1528 ? 214.077 212.538 166.277 1.00 14.13 ? 1528 ASN A N     1 
ATOM   611   C  CA    . ASN A 1 1528 ? 214.130 212.126 167.676 1.00 9.47  ? 1528 ASN A CA    1 
ATOM   612   C  C     . ASN A 1 1528 ? 213.348 213.081 168.567 1.00 10.44 ? 1528 ASN A C     1 
ATOM   613   O  O     . ASN A 1 1528 ? 212.729 212.646 169.546 1.00 10.79 ? 1528 ASN A O     1 
ATOM   614   C  CB    . ASN A 1 1528 ? 215.579 212.034 168.143 1.00 11.99 ? 1528 ASN A CB    1 
ATOM   615   C  CG    . ASN A 1 1528 ? 216.222 210.712 167.787 1.00 10.33 ? 1528 ASN A CG    1 
ATOM   616   O  OD1   . ASN A 1 1528 ? 215.577 209.667 167.818 1.00 17.74 ? 1528 ASN A OD1   1 
ATOM   617   N  ND2   . ASN A 1 1528 ? 217.502 210.752 167.444 1.00 12.43 ? 1528 ASN A ND2   1 
ATOM   618   N  N     . ARG A 1 1529 ? 213.369 214.375 168.250 1.00 10.26 ? 1529 ARG A N     1 
ATOM   619   C  CA    . ARG A 1 1529 ? 212.608 215.346 169.030 1.00 8.91  ? 1529 ARG A CA    1 
ATOM   620   C  C     . ARG A 1 1529 ? 211.110 215.177 168.815 1.00 9.16  ? 1529 ARG A C     1 
ATOM   621   O  O     . ARG A 1 1529 ? 210.319 215.375 169.743 1.00 12.26 ? 1529 ARG A O     1 
ATOM   622   C  CB    . ARG A 1 1529 ? 213.056 216.763 168.674 1.00 10.19 ? 1529 ARG A CB    1 
ATOM   623   C  CG    . ARG A 1 1529 ? 214.333 217.186 169.373 1.00 10.35 ? 1529 ARG A CG    1 
ATOM   624   C  CD    . ARG A 1 1529 ? 214.997 218.369 168.689 1.00 12.03 ? 1529 ARG A CD    1 
ATOM   625   N  NE    . ARG A 1 1529 ? 214.071 219.472 168.464 1.00 14.92 ? 1529 ARG A NE    1 
ATOM   626   C  CZ    . ARG A 1 1529 ? 213.889 220.070 167.295 1.00 16.49 ? 1529 ARG A CZ    1 
ATOM   627   N  NH1   . ARG A 1 1529 ? 214.555 219.694 166.215 1.00 13.39 ? 1529 ARG A NH1   1 
ATOM   628   N  NH2   . ARG A 1 1529 ? 213.021 221.072 167.207 1.00 19.26 ? 1529 ARG A NH2   1 
ATOM   629   N  N     . ILE A 1 1530 ? 210.701 214.814 167.597 1.00 10.81 ? 1530 ILE A N     1 
ATOM   630   C  CA    . ILE A 1 1530 ? 209.293 214.532 167.334 1.00 7.03  ? 1530 ILE A CA    1 
ATOM   631   C  C     . ILE A 1 1530 ? 208.831 213.330 168.148 1.00 10.18 ? 1530 ILE A C     1 
ATOM   632   O  O     . ILE A 1 1530 ? 207.729 213.328 168.709 1.00 16.30 ? 1530 ILE A O     1 
ATOM   633   C  CB    . ILE A 1 1530 ? 209.058 214.319 165.826 1.00 10.65 ? 1530 ILE A CB    1 
ATOM   634   C  CG1   . ILE A 1 1530 ? 209.448 215.570 165.039 1.00 13.21 ? 1530 ILE A CG1   1 
ATOM   635   C  CG2   . ILE A 1 1530 ? 207.606 213.961 165.554 1.00 10.42 ? 1530 ILE A CG2   1 
ATOM   636   C  CD1   . ILE A 1 1530 ? 209.269 215.430 163.544 1.00 12.56 ? 1530 ILE A CD1   1 
ATOM   637   N  N     . MET A 1 1531 ? 209.664 212.288 168.221 1.00 9.69  ? 1531 MET A N     1 
ATOM   638   C  CA    . MET A 1 1531 ? 209.320 211.122 169.028 1.00 7.52  ? 1531 MET A CA    1 
ATOM   639   C  C     . MET A 1 1531 ? 209.179 211.480 170.501 1.00 8.87  ? 1531 MET A C     1 
ATOM   640   O  O     . MET A 1 1531 ? 208.225 211.056 171.160 1.00 16.22 ? 1531 MET A O     1 
ATOM   641   C  CB    . MET A 1 1531 ? 210.372 210.027 168.847 1.00 7.85  ? 1531 MET A CB    1 
ATOM   642   C  CG    . MET A 1 1531 ? 209.975 208.681 169.433 1.00 12.99 ? 1531 MET A CG    1 
ATOM   643   S  SD    . MET A 1 1531 ? 208.528 207.938 168.663 1.00 28.89 ? 1531 MET A SD    1 
ATOM   644   C  CE    . MET A 1 1531 ? 209.267 207.221 167.202 1.00 14.22 ? 1531 MET A CE    1 
ATOM   645   N  N     . ALA A 1 1532 ? 210.116 212.267 171.034 1.00 8.14  ? 1532 ALA A N     1 
ATOM   646   C  CA    . ALA A 1 1532 ? 210.098 212.568 172.461 1.00 6.82  ? 1532 ALA A CA    1 
ATOM   647   C  C     . ALA A 1 1532 ? 208.916 213.450 172.844 1.00 9.18  ? 1532 ALA A C     1 
ATOM   648   O  O     . ALA A 1 1532 ? 208.464 213.407 173.993 1.00 17.27 ? 1532 ALA A O     1 
ATOM   649   C  CB    . ALA A 1 1532 ? 211.413 213.229 172.873 1.00 9.67  ? 1532 ALA A CB    1 
ATOM   650   N  N     . LEU A 1 1533 ? 208.401 214.246 171.908 1.00 5.75  ? 1533 LEU A N     1 
ATOM   651   C  CA    . LEU A 1 1533 ? 207.297 215.143 172.225 1.00 8.03  ? 1533 LEU A CA    1 
ATOM   652   C  C     . LEU A 1 1533 ? 205.958 214.417 172.203 1.00 9.11  ? 1533 LEU A C     1 
ATOM   653   O  O     . LEU A 1 1533 ? 205.219 214.433 173.194 1.00 11.78 ? 1533 LEU A O     1 
ATOM   654   C  CB    . LEU A 1 1533 ? 207.279 216.323 171.251 1.00 9.61  ? 1533 LEU A CB    1 
ATOM   655   C  CG    . LEU A 1 1533 ? 206.138 217.327 171.433 1.00 9.12  ? 1533 LEU A CG    1 
ATOM   656   C  CD1   . LEU A 1 1533 ? 206.267 218.069 172.756 1.00 5.85  ? 1533 LEU A CD1   1 
ATOM   657   C  CD2   . LEU A 1 1533 ? 206.094 218.305 170.271 1.00 8.62  ? 1533 LEU A CD2   1 
ATOM   658   N  N     . PHE A 1 1534 ? 205.632 213.773 171.084 1.00 8.39  ? 1534 PHE A N     1 
ATOM   659   C  CA    . PHE A 1 1534 ? 204.323 213.156 170.921 1.00 9.54  ? 1534 PHE A CA    1 
ATOM   660   C  C     . PHE A 1 1534 ? 204.191 211.829 171.649 1.00 9.22  ? 1534 PHE A C     1 
ATOM   661   O  O     . PHE A 1 1534 ? 203.071 211.326 171.779 1.00 12.56 ? 1534 PHE A O     1 
ATOM   662   C  CB    . PHE A 1 1534 ? 204.021 212.985 169.432 1.00 8.13  ? 1534 PHE A CB    1 
ATOM   663   C  CG    . PHE A 1 1534 ? 203.951 214.286 168.692 1.00 7.93  ? 1534 PHE A CG    1 
ATOM   664   C  CD1   . PHE A 1 1534 ? 203.051 215.264 169.078 1.00 11.05 ? 1534 PHE A CD1   1 
ATOM   665   C  CD2   . PHE A 1 1534 ? 204.799 214.544 167.633 1.00 8.42  ? 1534 PHE A CD2   1 
ATOM   666   C  CE1   . PHE A 1 1534 ? 202.987 216.469 168.411 1.00 11.27 ? 1534 PHE A CE1   1 
ATOM   667   C  CE2   . PHE A 1 1534 ? 204.741 215.748 166.962 1.00 13.97 ? 1534 PHE A CE2   1 
ATOM   668   C  CZ    . PHE A 1 1534 ? 203.833 216.712 167.351 1.00 17.38 ? 1534 PHE A CZ    1 
ATOM   669   N  N     . ASP A 1 1535 ? 205.294 211.249 172.129 1.00 8.05  ? 1535 ASP A N     1 
ATOM   670   C  CA    . ASP A 1 1535 ? 205.174 210.135 173.062 1.00 9.38  ? 1535 ASP A CA    1 
ATOM   671   C  C     . ASP A 1 1535 ? 204.707 210.613 174.429 1.00 6.65  ? 1535 ASP A C     1 
ATOM   672   O  O     . ASP A 1 1535 ? 204.140 209.831 175.200 1.00 10.19 ? 1535 ASP A O     1 
ATOM   673   C  CB    . ASP A 1 1535 ? 206.503 209.392 173.183 1.00 7.98  ? 1535 ASP A CB    1 
ATOM   674   C  CG    . ASP A 1 1535 ? 206.330 207.970 173.668 1.00 11.73 ? 1535 ASP A CG    1 
ATOM   675   O  OD1   . ASP A 1 1535 ? 205.727 207.162 172.933 1.00 6.79  ? 1535 ASP A OD1   1 
ATOM   676   O  OD2   . ASP A 1 1535 ? 206.796 207.659 174.784 1.00 13.46 ? 1535 ASP A OD2   1 
ATOM   677   N  N     . VAL A 1 1536 ? 204.937 211.887 174.749 1.00 5.67  ? 1536 VAL A N     1 
ATOM   678   C  CA    . VAL A 1 1536 ? 204.395 212.458 175.976 1.00 6.78  ? 1536 VAL A CA    1 
ATOM   679   C  C     . VAL A 1 1536 ? 203.024 213.071 175.719 1.00 7.45  ? 1536 VAL A C     1 
ATOM   680   O  O     . VAL A 1 1536 ? 202.122 212.970 176.556 1.00 10.14 ? 1536 VAL A O     1 
ATOM   681   C  CB    . VAL A 1 1536 ? 205.377 213.488 176.565 1.00 7.01  ? 1536 VAL A CB    1 
ATOM   682   C  CG1   . VAL A 1 1536 ? 204.816 214.090 177.843 1.00 8.32  ? 1536 VAL A CG1   1 
ATOM   683   C  CG2   . VAL A 1 1536 ? 206.730 212.850 176.826 1.00 6.12  ? 1536 VAL A CG2   1 
ATOM   684   N  N     . TRP A 1 1537 ? 202.845 213.698 174.552 1.00 7.24  ? 1537 TRP A N     1 
ATOM   685   C  CA    . TRP A 1 1537 ? 201.574 214.341 174.227 1.00 5.40  ? 1537 TRP A CA    1 
ATOM   686   C  C     . TRP A 1 1537 ? 200.428 213.339 174.274 1.00 6.91  ? 1537 TRP A C     1 
ATOM   687   O  O     . TRP A 1 1537 ? 199.335 213.656 174.758 1.00 8.14  ? 1537 TRP A O     1 
ATOM   688   C  CB    . TRP A 1 1537 ? 201.647 214.977 172.840 1.00 7.43  ? 1537 TRP A CB    1 
ATOM   689   C  CG    . TRP A 1 1537 ? 200.410 215.740 172.432 1.00 11.98 ? 1537 TRP A CG    1 
ATOM   690   C  CD1   . TRP A 1 1537 ? 199.434 215.310 171.594 1.00 25.31 ? 1537 TRP A CD1   1 
ATOM   691   C  CD2   . TRP A 1 1537 ? 200.097 217.105 172.728 1.00 9.70  ? 1537 TRP A CD2   1 
ATOM   692   N  NE1   . TRP A 1 1537 ? 198.486 216.281 171.420 1.00 24.62 ? 1537 TRP A NE1   1 
ATOM   693   C  CE2   . TRP A 1 1537 ? 198.880 217.402 172.094 1.00 22.14 ? 1537 TRP A CE2   1 
ATOM   694   C  CE3   . TRP A 1 1537 ? 200.713 218.095 173.487 1.00 27.35 ? 1537 TRP A CE3   1 
ATOM   695   C  CZ2   . TRP A 1 1537 ? 198.271 218.642 172.195 1.00 28.08 ? 1537 TRP A CZ2   1 
ATOM   696   C  CZ3   . TRP A 1 1537 ? 200.101 219.322 173.596 1.00 28.15 ? 1537 TRP A CZ3   1 
ATOM   697   C  CH2   . TRP A 1 1537 ? 198.894 219.589 172.953 1.00 24.73 ? 1537 TRP A CH2   1 
ATOM   698   N  N     . ILE A 1 1538 ? 200.659 212.125 173.766 1.00 5.87  ? 1538 ILE A N     1 
ATOM   699   C  CA    . ILE A 1 1538 ? 199.600 211.122 173.692 1.00 5.92  ? 1538 ILE A CA    1 
ATOM   700   C  C     . ILE A 1 1538 ? 199.125 210.732 175.087 1.00 6.79  ? 1538 ILE A C     1 
ATOM   701   O  O     . ILE A 1 1538 ? 197.922 210.575 175.327 1.00 5.50  ? 1538 ILE A O     1 
ATOM   702   C  CB    . ILE A 1 1538 ? 200.069 209.901 172.875 1.00 7.65  ? 1538 ILE A CB    1 
ATOM   703   C  CG1   . ILE A 1 1538 ? 198.923 208.901 172.704 1.00 5.36  ? 1538 ILE A CG1   1 
ATOM   704   C  CG2   . ILE A 1 1538 ? 201.290 209.239 173.507 1.00 4.85  ? 1538 ILE A CG2   1 
ATOM   705   C  CD1   . ILE A 1 1538 ? 199.255 207.733 171.815 1.00 4.01  ? 1538 ILE A CD1   1 
ATOM   706   N  N     . ASP A 1 1539 ? 200.056 210.571 176.029 1.00 6.54  ? 1539 ASP A N     1 
ATOM   707   C  CA    . ASP A 1 1539 ? 199.673 210.260 177.401 1.00 4.82  ? 1539 ASP A CA    1 
ATOM   708   C  C     . ASP A 1 1539 ? 199.016 211.449 178.088 1.00 5.02  ? 1539 ASP A C     1 
ATOM   709   O  O     . ASP A 1 1539 ? 198.131 211.260 178.929 1.00 9.97  ? 1539 ASP A O     1 
ATOM   710   C  CB    . ASP A 1 1539 ? 200.893 209.799 178.197 1.00 5.60  ? 1539 ASP A CB    1 
ATOM   711   C  CG    . ASP A 1 1539 ? 201.229 208.342 177.955 1.00 8.94  ? 1539 ASP A CG    1 
ATOM   712   O  OD1   . ASP A 1 1539 ? 200.304 207.552 177.683 1.00 10.86 ? 1539 ASP A OD1   1 
ATOM   713   O  OD2   . ASP A 1 1539 ? 202.422 207.984 178.043 1.00 20.78 ? 1539 ASP A OD2   1 
ATOM   714   N  N     . VAL A 1 1540 ? 199.432 212.670 177.748 1.00 3.82  ? 1540 VAL A N     1 
ATOM   715   C  CA    . VAL A 1 1540 ? 198.831 213.858 178.345 1.00 2.70  ? 1540 VAL A CA    1 
ATOM   716   C  C     . VAL A 1 1540 ? 197.407 214.049 177.838 1.00 2.14  ? 1540 VAL A C     1 
ATOM   717   O  O     . VAL A 1 1540 ? 196.487 214.331 178.612 1.00 1.22  ? 1540 VAL A O     1 
ATOM   718   C  CB    . VAL A 1 1540 ? 199.706 215.095 178.065 1.00 3.42  ? 1540 VAL A CB    1 
ATOM   719   C  CG1   . VAL A 1 1540 ? 198.962 216.375 178.405 1.00 2.60  ? 1540 VAL A CG1   1 
ATOM   720   C  CG2   . VAL A 1 1540 ? 201.001 215.006 178.851 1.00 4.07  ? 1540 VAL A CG2   1 
ATOM   721   N  N     . GLN A 1 1541 ? 197.204 213.897 176.527 1.00 2.90  ? 1541 GLN A N     1 
ATOM   722   C  CA    . GLN A 1 1541 ? 195.864 214.040 175.966 1.00 1.92  ? 1541 GLN A CA    1 
ATOM   723   C  C     . GLN A 1 1541 ? 194.929 212.956 176.488 1.00 2.22  ? 1541 GLN A C     1 
ATOM   724   O  O     . GLN A 1 1541 ? 193.766 213.228 176.799 1.00 2.48  ? 1541 GLN A O     1 
ATOM   725   C  CB    . GLN A 1 1541 ? 195.925 214.011 174.440 1.00 1.93  ? 1541 GLN A CB    1 
ATOM   726   C  CG    . GLN A 1 1541 ? 194.564 214.016 173.767 1.00 3.18  ? 1541 GLN A CG    1 
ATOM   727   C  CD    . GLN A 1 1541 ? 194.649 214.234 172.273 1.00 6.88  ? 1541 GLN A CD    1 
ATOM   728   O  OE1   . GLN A 1 1541 ? 195.047 215.302 171.813 1.00 17.40 ? 1541 GLN A OE1   1 
ATOM   729   N  NE2   . GLN A 1 1541 ? 194.274 213.221 171.506 1.00 8.89  ? 1541 GLN A NE2   1 
ATOM   730   N  N     . ARG A 1 1542 ? 195.422 211.722 176.592 1.00 3.46  ? 1542 ARG A N     1 
ATOM   731   C  CA    . ARG A 1 1542 ? 194.600 210.632 177.108 1.00 3.22  ? 1542 ARG A CA    1 
ATOM   732   C  C     . ARG A 1 1542 ? 194.164 210.901 178.542 1.00 2.96  ? 1542 ARG A C     1 
ATOM   733   O  O     . ARG A 1 1542 ? 192.993 210.723 178.892 1.00 3.24  ? 1542 ARG A O     1 
ATOM   734   C  CB    . ARG A 1 1542 ? 195.371 209.316 177.015 1.00 2.97  ? 1542 ARG A CB    1 
ATOM   735   C  CG    . ARG A 1 1542 ? 194.722 208.153 177.732 1.00 3.75  ? 1542 ARG A CG    1 
ATOM   736   C  CD    . ARG A 1 1542 ? 195.496 206.872 177.477 1.00 4.12  ? 1542 ARG A CD    1 
ATOM   737   N  NE    . ARG A 1 1542 ? 196.816 206.904 178.095 1.00 5.72  ? 1542 ARG A NE    1 
ATOM   738   C  CZ    . ARG A 1 1542 ? 197.040 206.764 179.394 1.00 13.20 ? 1542 ARG A CZ    1 
ATOM   739   N  NH1   . ARG A 1 1542 ? 196.055 206.543 180.247 1.00 13.10 ? 1542 ARG A NH1   1 
ATOM   740   N  NH2   . ARG A 1 1542 ? 198.288 206.842 179.847 1.00 11.49 ? 1542 ARG A NH2   1 
ATOM   741   N  N     . ARG A 1 1543 ? 195.097 211.343 179.387 1.00 3.00  ? 1543 ARG A N     1 
ATOM   742   C  CA    . ARG A 1 1543 ? 194.773 211.582 180.790 1.00 2.97  ? 1543 ARG A CA    1 
ATOM   743   C  C     . ARG A 1 1543 ? 193.858 212.787 180.951 1.00 2.81  ? 1543 ARG A C     1 
ATOM   744   O  O     . ARG A 1 1543 ? 192.968 212.786 181.811 1.00 8.39  ? 1543 ARG A O     1 
ATOM   745   C  CB    . ARG A 1 1543 ? 196.053 211.761 181.601 1.00 2.67  ? 1543 ARG A CB    1 
ATOM   746   C  CG    . ARG A 1 1543 ? 196.747 210.453 181.911 1.00 6.13  ? 1543 ARG A CG    1 
ATOM   747   C  CD    . ARG A 1 1543 ? 198.056 210.665 182.634 1.00 7.52  ? 1543 ARG A CD    1 
ATOM   748   N  NE    . ARG A 1 1543 ? 198.988 209.578 182.367 1.00 15.67 ? 1543 ARG A NE    1 
ATOM   749   C  CZ    . ARG A 1 1543 ? 199.311 208.639 183.245 1.00 17.21 ? 1543 ARG A CZ    1 
ATOM   750   N  NH1   . ARG A 1 1543 ? 198.793 208.623 184.462 1.00 15.55 ? 1543 ARG A NH1   1 
ATOM   751   N  NH2   . ARG A 1 1543 ? 200.175 207.692 182.893 1.00 18.32 ? 1543 ARG A NH2   1 
ATOM   752   N  N     . TRP A 1 1544 ? 194.056 213.823 180.134 1.00 1.86  ? 1544 TRP A N     1 
ATOM   753   C  CA    . TRP A 1 1544 ? 193.200 214.999 180.220 1.00 1.67  ? 1544 TRP A CA    1 
ATOM   754   C  C     . TRP A 1 1544 ? 191.765 214.685 179.822 1.00 3.10  ? 1544 TRP A C     1 
ATOM   755   O  O     . TRP A 1 1544 ? 190.833 215.299 180.350 1.00 4.05  ? 1544 TRP A O     1 
ATOM   756   C  CB    . TRP A 1 1544 ? 193.750 216.125 179.345 1.00 2.52  ? 1544 TRP A CB    1 
ATOM   757   C  CG    . TRP A 1 1544 ? 192.925 217.373 179.412 1.00 2.02  ? 1544 TRP A CG    1 
ATOM   758   C  CD1   . TRP A 1 1544 ? 193.035 218.379 180.323 1.00 3.76  ? 1544 TRP A CD1   1 
ATOM   759   C  CD2   . TRP A 1 1544 ? 191.847 217.735 178.542 1.00 1.86  ? 1544 TRP A CD2   1 
ATOM   760   N  NE1   . TRP A 1 1544 ? 192.100 219.352 180.072 1.00 3.38  ? 1544 TRP A NE1   1 
ATOM   761   C  CE2   . TRP A 1 1544 ? 191.357 218.980 178.983 1.00 2.57  ? 1544 TRP A CE2   1 
ATOM   762   C  CE3   . TRP A 1 1544 ? 191.249 217.130 177.433 1.00 2.25  ? 1544 TRP A CE3   1 
ATOM   763   C  CZ2   . TRP A 1 1544 ? 190.302 219.630 178.352 1.00 3.63  ? 1544 TRP A CZ2   1 
ATOM   764   C  CZ3   . TRP A 1 1544 ? 190.204 217.777 176.810 1.00 2.54  ? 1544 TRP A CZ3   1 
ATOM   765   C  CH2   . TRP A 1 1544 ? 189.739 219.014 177.271 1.00 4.28  ? 1544 TRP A CH2   1 
ATOM   766   N  N     . VAL A 1 1545 ? 191.562 213.740 178.901 1.00 2.59  ? 1545 VAL A N     1 
ATOM   767   C  CA    . VAL A 1 1545 ? 190.213 213.450 178.424 1.00 3.50  ? 1545 VAL A CA    1 
ATOM   768   C  C     . VAL A 1 1545 ? 189.343 212.910 179.554 1.00 4.76  ? 1545 VAL A C     1 
ATOM   769   O  O     . VAL A 1 1545 ? 188.222 213.383 179.775 1.00 5.89  ? 1545 VAL A O     1 
ATOM   770   C  CB    . VAL A 1 1545 ? 190.261 212.480 177.229 1.00 2.80  ? 1545 VAL A CB    1 
ATOM   771   C  CG1   . VAL A 1 1545 ? 188.908 211.830 177.017 1.00 4.63  ? 1545 VAL A CG1   1 
ATOM   772   C  CG2   . VAL A 1 1545 ? 190.682 213.223 175.981 1.00 2.88  ? 1545 VAL A CG2   1 
ATOM   773   N  N     . TYR A 1 1546 ? 189.841 211.915 180.292 1.00 3.17  ? 1546 TYR A N     1 
ATOM   774   C  CA    . TYR A 1 1546 ? 189.008 211.326 181.333 1.00 3.90  ? 1546 TYR A CA    1 
ATOM   775   C  C     . TYR A 1 1546 ? 189.041 212.118 182.636 1.00 4.74  ? 1546 TYR A C     1 
ATOM   776   O  O     . TYR A 1 1546 ? 188.085 212.037 183.412 1.00 5.21  ? 1546 TYR A O     1 
ATOM   777   C  CB    . TYR A 1 1546 ? 189.389 209.857 181.574 1.00 3.64  ? 1546 TYR A CB    1 
ATOM   778   C  CG    . TYR A 1 1546 ? 190.777 209.577 182.112 1.00 2.81  ? 1546 TYR A CG    1 
ATOM   779   C  CD1   . TYR A 1 1546 ? 191.115 209.875 183.427 1.00 3.36  ? 1546 TYR A CD1   1 
ATOM   780   C  CD2   . TYR A 1 1546 ? 191.738 208.969 181.316 1.00 3.14  ? 1546 TYR A CD2   1 
ATOM   781   C  CE1   . TYR A 1 1546 ? 192.369 209.607 183.919 1.00 3.57  ? 1546 TYR A CE1   1 
ATOM   782   C  CE2   . TYR A 1 1546 ? 192.998 208.694 181.803 1.00 3.71  ? 1546 TYR A CE2   1 
ATOM   783   C  CZ    . TYR A 1 1546 ? 193.309 209.015 183.106 1.00 5.57  ? 1546 TYR A CZ    1 
ATOM   784   O  OH    . TYR A 1 1546 ? 194.562 208.743 183.604 1.00 6.15  ? 1546 TYR A OH    1 
ATOM   785   N  N     . LEU A 1 1547 ? 190.104 212.880 182.895 1.00 3.39  ? 1547 LEU A N     1 
ATOM   786   C  CA    . LEU A 1 1547 ? 190.079 213.780 184.043 1.00 3.42  ? 1547 LEU A CA    1 
ATOM   787   C  C     . LEU A 1 1547 ? 189.127 214.944 183.807 1.00 3.45  ? 1547 LEU A C     1 
ATOM   788   O  O     . LEU A 1 1547 ? 188.436 215.384 184.731 1.00 5.90  ? 1547 LEU A O     1 
ATOM   789   C  CB    . LEU A 1 1547 ? 191.484 214.290 184.358 1.00 3.30  ? 1547 LEU A CB    1 
ATOM   790   C  CG    . LEU A 1 1547 ? 192.403 213.314 185.091 1.00 4.25  ? 1547 LEU A CG    1 
ATOM   791   C  CD1   . LEU A 1 1547 ? 193.784 213.913 185.269 1.00 3.46  ? 1547 LEU A CD1   1 
ATOM   792   C  CD2   . LEU A 1 1547 ? 191.801 212.922 186.430 1.00 3.50  ? 1547 LEU A CD2   1 
ATOM   793   N  N     . GLU A 1 1548 ? 189.075 215.452 182.575 1.00 3.86  ? 1548 GLU A N     1 
ATOM   794   C  CA    . GLU A 1 1548 ? 188.140 216.525 182.254 1.00 8.25  ? 1548 GLU A CA    1 
ATOM   795   C  C     . GLU A 1 1548 ? 186.700 216.044 182.375 1.00 8.23  ? 1548 GLU A C     1 
ATOM   796   O  O     . GLU A 1 1548 ? 185.823 216.795 182.815 1.00 15.14 ? 1548 GLU A O     1 
ATOM   797   C  CB    . GLU A 1 1548 ? 188.424 217.061 180.849 1.00 6.33  ? 1548 GLU A CB    1 
ATOM   798   C  CG    . GLU A 1 1548 ? 187.791 218.402 180.512 1.00 8.34  ? 1548 GLU A CG    1 
ATOM   799   C  CD    . GLU A 1 1548 ? 186.312 218.297 180.201 1.00 18.95 ? 1548 GLU A CD    1 
ATOM   800   O  OE1   . GLU A 1 1548 ? 185.932 217.413 179.405 1.00 20.52 ? 1548 GLU A OE1   1 
ATOM   801   O  OE2   . GLU A 1 1548 ? 185.534 219.105 180.747 1.00 19.04 ? 1548 GLU A OE2   1 
ATOM   802   N  N     . GLY A 1 1549 ? 186.436 214.795 181.991 1.00 5.09  ? 1549 GLY A N     1 
ATOM   803   C  CA    . GLY A 1 1549 ? 185.095 214.255 182.138 1.00 7.58  ? 1549 GLY A CA    1 
ATOM   804   C  C     . GLY A 1 1549 ? 184.663 214.139 183.587 1.00 9.60  ? 1549 GLY A C     1 
ATOM   805   O  O     . GLY A 1 1549 ? 183.507 214.403 183.924 1.00 18.95 ? 1549 GLY A O     1 
ATOM   806   N  N     . ILE A 1 1550 ? 185.583 213.734 184.463 1.00 7.75  ? 1550 ILE A N     1 
ATOM   807   C  CA    . ILE A 1 1550 ? 185.256 213.606 185.879 1.00 8.58  ? 1550 ILE A CA    1 
ATOM   808   C  C     . ILE A 1 1550 ? 185.064 214.975 186.521 1.00 9.62  ? 1550 ILE A C     1 
ATOM   809   O  O     . ILE A 1 1550 ? 184.123 215.184 187.296 1.00 16.79 ? 1550 ILE A O     1 
ATOM   810   C  CB    . ILE A 1 1550 ? 186.334 212.781 186.602 1.00 7.60  ? 1550 ILE A CB    1 
ATOM   811   C  CG1   . ILE A 1 1550 ? 186.355 211.358 186.047 1.00 6.54  ? 1550 ILE A CG1   1 
ATOM   812   C  CG2   . ILE A 1 1550 ? 186.090 212.772 188.099 1.00 12.98 ? 1550 ILE A CG2   1 
ATOM   813   C  CD1   . ILE A 1 1550 ? 187.532 210.540 186.491 1.00 5.28  ? 1550 ILE A CD1   1 
ATOM   814   N  N     . PHE A 1 1551 ? 185.936 215.930 186.209 1.00 13.36 ? 1551 PHE A N     1 
ATOM   815   C  CA    . PHE A 1 1551 ? 185.871 217.249 186.828 1.00 11.02 ? 1551 PHE A CA    1 
ATOM   816   C  C     . PHE A 1 1551 ? 184.856 218.167 186.162 1.00 12.72 ? 1551 PHE A C     1 
ATOM   817   O  O     . PHE A 1 1551 ? 184.815 219.359 186.488 1.00 18.87 ? 1551 PHE A O     1 
ATOM   818   C  CB    . PHE A 1 1551 ? 187.252 217.908 186.820 1.00 5.47  ? 1551 PHE A CB    1 
ATOM   819   C  CG    . PHE A 1 1551 ? 188.183 217.370 187.867 1.00 6.44  ? 1551 PHE A CG    1 
ATOM   820   C  CD1   . PHE A 1 1551 ? 188.003 217.687 189.202 1.00 6.07  ? 1551 PHE A CD1   1 
ATOM   821   C  CD2   . PHE A 1 1551 ? 189.246 216.557 187.515 1.00 6.46  ? 1551 PHE A CD2   1 
ATOM   822   C  CE1   . PHE A 1 1551 ? 188.857 217.195 190.167 1.00 6.45  ? 1551 PHE A CE1   1 
ATOM   823   C  CE2   . PHE A 1 1551 ? 190.105 216.061 188.474 1.00 4.85  ? 1551 PHE A CE2   1 
ATOM   824   C  CZ    . PHE A 1 1551 ? 189.910 216.381 189.803 1.00 8.68  ? 1551 PHE A CZ    1 
ATOM   825   N  N     . THR A 1 1552 ? 184.052 217.653 185.239 1.00 10.81 ? 1552 THR A N     1 
ATOM   826   C  CA    . THR A 1 1552 ? 182.965 218.400 184.623 1.00 13.88 ? 1552 THR A CA    1 
ATOM   827   C  C     . THR A 1 1552 ? 181.606 217.752 184.837 1.00 22.61 ? 1552 THR A C     1 
ATOM   828   O  O     . THR A 1 1552 ? 180.632 218.451 185.131 1.00 25.35 ? 1552 THR A O     1 
ATOM   829   C  CB    . THR A 1 1552 ? 183.224 218.567 183.115 1.00 16.46 ? 1552 THR A CB    1 
ATOM   830   O  OG1   . THR A 1 1552 ? 184.333 219.452 182.916 1.00 20.13 ? 1552 THR A OG1   1 
ATOM   831   C  CG2   . THR A 1 1552 ? 182.003 219.134 182.410 1.00 16.02 ? 1552 THR A CG2   1 
ATOM   832   N  N     . GLY A 1 1553 ? 181.519 216.431 184.723 1.00 17.83 ? 1553 GLY A N     1 
ATOM   833   C  CA    . GLY A 1 1553 ? 180.274 215.706 184.854 1.00 21.23 ? 1553 GLY A CA    1 
ATOM   834   C  C     . GLY A 1 1553 ? 179.856 215.352 186.264 1.00 22.63 ? 1553 GLY A C     1 
ATOM   835   O  O     . GLY A 1 1553 ? 178.812 214.715 186.438 1.00 23.45 ? 1553 GLY A O     1 
ATOM   836   N  N     . SER A 1 1554 ? 180.628 215.740 187.281 1.00 22.22 ? 1554 SER A N     1 
ATOM   837   C  CA    . SER A 1 1554 ? 180.293 215.438 188.676 1.00 25.16 ? 1554 SER A CA    1 
ATOM   838   C  C     . SER A 1 1554 ? 180.594 216.683 189.509 1.00 21.72 ? 1554 SER A C     1 
ATOM   839   O  O     . SER A 1 1554 ? 181.732 216.900 189.931 1.00 27.12 ? 1554 SER A O     1 
ATOM   840   C  CB    . SER A 1 1554 ? 181.058 214.222 189.183 1.00 28.25 ? 1554 SER A CB    1 
ATOM   841   O  OG    . SER A 1 1554 ? 182.455 214.463 189.199 1.00 26.49 ? 1554 SER A OG    1 
ATOM   842   N  N     . ALA A 1 1555 ? 179.560 217.492 189.749 1.00 24.61 ? 1555 ALA A N     1 
ATOM   843   C  CA    . ALA A 1 1555 ? 179.742 218.714 190.526 1.00 27.79 ? 1555 ALA A CA    1 
ATOM   844   C  C     . ALA A 1 1555 ? 180.047 218.417 191.988 1.00 29.02 ? 1555 ALA A C     1 
ATOM   845   O  O     . ALA A 1 1555 ? 180.535 219.293 192.710 1.00 31.36 ? 1555 ALA A O     1 
ATOM   846   C  CB    . ALA A 1 1555 ? 178.500 219.598 190.411 1.00 24.79 ? 1555 ALA A CB    1 
ATOM   847   N  N     . ASP A 1 1556 ? 179.767 217.193 192.440 1.00 23.59 ? 1556 ASP A N     1 
ATOM   848   C  CA    . ASP A 1 1556 ? 180.021 216.840 193.835 1.00 26.60 ? 1556 ASP A CA    1 
ATOM   849   C  C     . ASP A 1 1556 ? 181.513 216.792 194.139 1.00 29.03 ? 1556 ASP A C     1 
ATOM   850   O  O     . ASP A 1 1556 ? 181.927 217.005 195.285 1.00 30.48 ? 1556 ASP A O     1 
ATOM   851   C  CB    . ASP A 1 1556 ? 179.370 215.495 194.159 1.00 23.24 ? 1556 ASP A CB    1 
ATOM   852   C  CG    . ASP A 1 1556 ? 179.653 214.445 193.105 1.00 30.49 ? 1556 ASP A CG    1 
ATOM   853   O  OD1   . ASP A 1 1556 ? 179.243 214.643 191.943 1.00 33.07 ? 1556 ASP A OD1   1 
ATOM   854   O  OD2   . ASP A 1 1556 ? 180.286 213.422 193.440 1.00 30.35 ? 1556 ASP A OD2   1 
ATOM   855   N  N     . ILE A 1 1557 ? 182.337 216.500 193.130 1.00 21.40 ? 1557 ILE A N     1 
ATOM   856   C  CA    . ILE A 1 1557 ? 183.769 216.344 193.366 1.00 19.12 ? 1557 ILE A CA    1 
ATOM   857   C  C     . ILE A 1 1557 ? 184.411 217.687 193.692 1.00 20.58 ? 1557 ILE A C     1 
ATOM   858   O  O     . ILE A 1 1557 ? 185.443 217.750 194.373 1.00 20.94 ? 1557 ILE A O     1 
ATOM   859   C  CB    . ILE A 1 1557 ? 184.442 215.661 192.158 1.00 18.46 ? 1557 ILE A CB    1 
ATOM   860   C  CG1   . ILE A 1 1557 ? 185.755 214.999 192.578 1.00 17.15 ? 1557 ILE A CG1   1 
ATOM   861   C  CG2   . ILE A 1 1557 ? 184.702 216.654 191.037 1.00 16.78 ? 1557 ILE A CG2   1 
ATOM   862   C  CD1   . ILE A 1 1557 ? 186.432 214.233 191.467 1.00 11.64 ? 1557 ILE A CD1   1 
ATOM   863   N  N     . LYS A 1 1558 ? 183.811 218.781 193.218 1.00 19.87 ? 1558 LYS A N     1 
ATOM   864   C  CA    . LYS A 1 1558 ? 184.358 220.106 193.494 1.00 17.94 ? 1558 LYS A CA    1 
ATOM   865   C  C     . LYS A 1 1558 ? 184.328 220.408 194.987 1.00 21.88 ? 1558 LYS A C     1 
ATOM   866   O  O     . LYS A 1 1558 ? 185.275 220.978 195.538 1.00 22.64 ? 1558 LYS A O     1 
ATOM   867   C  CB    . LYS A 1 1558 ? 183.582 221.163 192.710 1.00 17.70 ? 1558 LYS A CB    1 
ATOM   868   C  CG    . LYS A 1 1558 ? 184.084 222.582 192.917 1.00 21.23 ? 1558 LYS A CG    1 
ATOM   869   C  CD    . LYS A 1 1558 ? 183.314 223.569 192.058 1.00 27.20 ? 1558 LYS A CD    1 
ATOM   870   C  CE    . LYS A 1 1558 ? 183.876 224.974 192.195 1.00 29.05 ? 1558 LYS A CE    1 
ATOM   871   N  NZ    . LYS A 1 1558 ? 185.310 225.038 191.800 1.00 29.64 ? 1558 LYS A NZ    1 
ATOM   872   N  N     . HIS A 1 1559 ? 183.238 220.034 195.658 1.00 25.89 ? 1559 HIS A N     1 
ATOM   873   C  CA    . HIS A 1 1559 ? 183.168 220.207 197.105 1.00 26.69 ? 1559 HIS A CA    1 
ATOM   874   C  C     . HIS A 1 1559 ? 184.004 219.161 197.828 1.00 22.90 ? 1559 HIS A C     1 
ATOM   875   O  O     . HIS A 1 1559 ? 184.651 219.464 198.837 1.00 27.09 ? 1559 HIS A O     1 
ATOM   876   C  CB    . HIS A 1 1559 ? 181.714 220.142 197.568 1.00 25.11 ? 1559 HIS A CB    1 
ATOM   877   C  CG    . HIS A 1 1559 ? 180.867 221.266 197.057 1.00 31.11 ? 1559 HIS A CG    1 
ATOM   878   N  ND1   . HIS A 1 1559 ? 180.202 221.208 195.852 1.00 32.94 ? 1559 HIS A ND1   1 
ATOM   879   C  CD2   . HIS A 1 1559 ? 180.582 222.479 197.586 1.00 31.60 ? 1559 HIS A CD2   1 
ATOM   880   C  CE1   . HIS A 1 1559 ? 179.540 222.336 195.662 1.00 32.83 ? 1559 HIS A CE1   1 
ATOM   881   N  NE2   . HIS A 1 1559 ? 179.754 223.124 196.701 1.00 30.53 ? 1559 HIS A NE2   1 
ATOM   882   N  N     . LEU A 1 1560 ? 183.998 217.923 197.330 1.00 20.32 ? 1560 LEU A N     1 
ATOM   883   C  CA    . LEU A 1 1560 ? 184.726 216.848 197.999 1.00 18.85 ? 1560 LEU A CA    1 
ATOM   884   C  C     . LEU A 1 1560 ? 186.229 217.103 197.978 1.00 21.92 ? 1560 LEU A C     1 
ATOM   885   O  O     . LEU A 1 1560 ? 186.917 216.901 198.985 1.00 23.19 ? 1560 LEU A O     1 
ATOM   886   C  CB    . LEU A 1 1560 ? 184.391 215.510 197.342 1.00 20.91 ? 1560 LEU A CB    1 
ATOM   887   C  CG    . LEU A 1 1560 ? 185.194 214.290 197.795 1.00 24.67 ? 1560 LEU A CG    1 
ATOM   888   C  CD1   . LEU A 1 1560 ? 185.030 214.058 199.288 1.00 23.84 ? 1560 LEU A CD1   1 
ATOM   889   C  CD2   . LEU A 1 1560 ? 184.779 213.055 197.010 1.00 20.75 ? 1560 LEU A CD2   1 
ATOM   890   N  N     . LEU A 1 1561 ? 186.756 217.545 196.838 1.00 20.82 ? 1561 LEU A N     1 
ATOM   891   C  CA    . LEU A 1 1561 ? 188.181 217.822 196.668 1.00 19.12 ? 1561 LEU A CA    1 
ATOM   892   C  C     . LEU A 1 1561 ? 188.363 219.200 196.044 1.00 20.73 ? 1561 LEU A C     1 
ATOM   893   O  O     . LEU A 1 1561 ? 188.648 219.323 194.847 1.00 20.36 ? 1561 LEU A O     1 
ATOM   894   C  CB    . LEU A 1 1561 ? 188.850 216.741 195.821 1.00 19.66 ? 1561 LEU A CB    1 
ATOM   895   C  CG    . LEU A 1 1561 ? 188.680 215.318 196.341 1.00 19.74 ? 1561 LEU A CG    1 
ATOM   896   C  CD1   . LEU A 1 1561 ? 189.251 214.310 195.367 1.00 20.94 ? 1561 LEU A CD1   1 
ATOM   897   C  CD2   . LEU A 1 1561 ? 189.373 215.208 197.690 1.00 21.58 ? 1561 LEU A CD2   1 
ATOM   898   N  N     . PRO A 1 1562 ? 188.190 220.265 196.833 1.00 21.62 ? 1562 PRO A N     1 
ATOM   899   C  CA    . PRO A 1 1562 ? 188.351 221.618 196.268 1.00 18.01 ? 1562 PRO A CA    1 
ATOM   900   C  C     . PRO A 1 1562 ? 189.753 221.899 195.756 1.00 18.40 ? 1562 PRO A C     1 
ATOM   901   O  O     . PRO A 1 1562 ? 189.910 222.543 194.712 1.00 15.29 ? 1562 PRO A O     1 
ATOM   902   C  CB    . PRO A 1 1562 ? 187.974 222.527 197.447 1.00 15.95 ? 1562 PRO A CB    1 
ATOM   903   C  CG    . PRO A 1 1562 ? 187.167 221.659 198.362 1.00 18.51 ? 1562 PRO A CG    1 
ATOM   904   C  CD    . PRO A 1 1562 ? 187.786 220.305 198.247 1.00 13.87 ? 1562 PRO A CD    1 
ATOM   905   N  N     . VAL A 1 1563 ? 190.782 221.430 196.465 1.00 19.08 ? 1563 VAL A N     1 
ATOM   906   C  CA    . VAL A 1 1563 ? 192.157 221.718 196.061 1.00 15.54 ? 1563 VAL A CA    1 
ATOM   907   C  C     . VAL A 1 1563 ? 192.462 221.063 194.722 1.00 18.31 ? 1563 VAL A C     1 
ATOM   908   O  O     . VAL A 1 1563 ? 192.982 221.703 193.800 1.00 21.23 ? 1563 VAL A O     1 
ATOM   909   C  CB    . VAL A 1 1563 ? 193.146 221.262 197.149 1.00 22.66 ? 1563 VAL A CB    1 
ATOM   910   C  CG1   . VAL A 1 1563 ? 194.575 221.464 196.682 1.00 20.90 ? 1563 VAL A CG1   1 
ATOM   911   C  CG2   . VAL A 1 1563 ? 192.894 222.015 198.442 1.00 17.92 ? 1563 VAL A CG2   1 
ATOM   912   N  N     . GLU A 1 1564 ? 192.127 219.779 194.589 1.00 18.15 ? 1564 GLU A N     1 
ATOM   913   C  CA    . GLU A 1 1564 ? 192.365 219.073 193.335 1.00 15.43 ? 1564 GLU A CA    1 
ATOM   914   C  C     . GLU A 1 1564 ? 191.555 219.679 192.197 1.00 14.94 ? 1564 GLU A C     1 
ATOM   915   O  O     . GLU A 1 1564 ? 192.044 219.798 191.068 1.00 18.90 ? 1564 GLU A O     1 
ATOM   916   C  CB    . GLU A 1 1564 ? 192.040 217.587 193.503 1.00 13.11 ? 1564 GLU A CB    1 
ATOM   917   C  CG    . GLU A 1 1564 ? 192.938 216.841 194.487 1.00 15.93 ? 1564 GLU A CG    1 
ATOM   918   C  CD    . GLU A 1 1564 ? 192.648 217.156 195.946 1.00 29.21 ? 1564 GLU A CD    1 
ATOM   919   O  OE1   . GLU A 1 1564 ? 191.737 217.964 196.223 1.00 32.26 ? 1564 GLU A OE1   1 
ATOM   920   O  OE2   . GLU A 1 1564 ? 193.334 216.587 196.821 1.00 32.54 ? 1564 GLU A OE2   1 
ATOM   921   N  N     . THR A 1 1565 ? 190.308 220.066 192.477 1.00 12.02 ? 1565 THR A N     1 
ATOM   922   C  CA    . THR A 1 1565 ? 189.460 220.633 191.433 1.00 11.39 ? 1565 THR A CA    1 
ATOM   923   C  C     . THR A 1 1565 ? 190.025 221.949 190.911 1.00 16.98 ? 1565 THR A C     1 
ATOM   924   O  O     . THR A 1 1565 ? 190.034 222.191 189.698 1.00 14.75 ? 1565 THR A O     1 
ATOM   925   C  CB    . THR A 1 1565 ? 188.041 220.828 191.962 1.00 11.29 ? 1565 THR A CB    1 
ATOM   926   O  OG1   . THR A 1 1565 ? 187.517 219.566 192.390 1.00 20.80 ? 1565 THR A OG1   1 
ATOM   927   C  CG2   . THR A 1 1565 ? 187.144 221.399 190.878 1.00 8.58  ? 1565 THR A CG2   1 
ATOM   928   N  N     . GLN A 1 1566 ? 190.500 222.815 191.810 1.00 17.17 ? 1566 GLN A N     1 
ATOM   929   C  CA    . GLN A 1 1566 ? 191.115 224.063 191.365 1.00 17.29 ? 1566 GLN A CA    1 
ATOM   930   C  C     . GLN A 1 1566 ? 192.453 223.808 190.685 1.00 16.96 ? 1566 GLN A C     1 
ATOM   931   O  O     . GLN A 1 1566 ? 192.781 224.456 189.684 1.00 14.73 ? 1566 GLN A O     1 
ATOM   932   C  CB    . GLN A 1 1566 ? 191.273 225.030 192.541 1.00 19.36 ? 1566 GLN A CB    1 
ATOM   933   C  CG    . GLN A 1 1566 ? 189.989 225.377 193.306 1.00 27.13 ? 1566 GLN A CG    1 
ATOM   934   C  CD    . GLN A 1 1566 ? 188.856 225.891 192.422 1.00 32.83 ? 1566 GLN A CD    1 
ATOM   935   O  OE1   . GLN A 1 1566 ? 188.319 225.172 191.580 1.00 29.53 ? 1566 GLN A OE1   1 
ATOM   936   N  NE2   . GLN A 1 1566 ? 188.493 227.156 192.615 1.00 25.49 ? 1566 GLN A NE2   1 
ATOM   937   N  N     . ARG A 1 1567 ? 193.243 222.869 191.211 1.00 18.56 ? 1567 ARG A N     1 
ATOM   938   C  CA    . ARG A 1 1567 ? 194.511 222.545 190.563 1.00 11.63 ? 1567 ARG A CA    1 
ATOM   939   C  C     . ARG A 1 1567 ? 194.290 221.999 189.163 1.00 14.70 ? 1567 ARG A C     1 
ATOM   940   O  O     . ARG A 1 1567 ? 195.020 222.353 188.232 1.00 17.82 ? 1567 ARG A O     1 
ATOM   941   C  CB    . ARG A 1 1567 ? 195.320 221.560 191.407 1.00 9.54  ? 1567 ARG A CB    1 
ATOM   942   C  CG    . ARG A 1 1567 ? 195.828 222.142 192.713 1.00 23.84 ? 1567 ARG A CG    1 
ATOM   943   C  CD    . ARG A 1 1567 ? 196.599 221.119 193.533 1.00 27.89 ? 1567 ARG A CD    1 
ATOM   944   N  NE    . ARG A 1 1567 ? 197.840 220.707 192.891 1.00 25.24 ? 1567 ARG A NE    1 
ATOM   945   C  CZ    . ARG A 1 1567 ? 198.614 219.719 193.323 1.00 32.08 ? 1567 ARG A CZ    1 
ATOM   946   N  NH1   . ARG A 1 1567 ? 198.312 219.032 194.412 1.00 27.40 ? 1567 ARG A NH1   1 
ATOM   947   N  NH2   . ARG A 1 1567 ? 199.722 219.420 192.652 1.00 34.02 ? 1567 ARG A NH2   1 
ATOM   948   N  N     . PHE A 1 1568 ? 193.278 221.147 188.982 1.00 14.72 ? 1568 PHE A N     1 
ATOM   949   C  CA    . PHE A 1 1568 ? 192.996 220.645 187.643 1.00 8.90  ? 1568 PHE A CA    1 
ATOM   950   C  C     . PHE A 1 1568 ? 192.536 221.753 186.710 1.00 9.03  ? 1568 PHE A C     1 
ATOM   951   O  O     . PHE A 1 1568 ? 192.825 221.707 185.511 1.00 10.37 ? 1568 PHE A O     1 
ATOM   952   C  CB    . PHE A 1 1568 ? 191.943 219.537 187.677 1.00 11.30 ? 1568 PHE A CB    1 
ATOM   953   C  CG    . PHE A 1 1568 ? 191.530 219.075 186.312 1.00 9.49  ? 1568 PHE A CG    1 
ATOM   954   C  CD1   . PHE A 1 1568 ? 192.347 218.230 185.578 1.00 5.71  ? 1568 PHE A CD1   1 
ATOM   955   C  CD2   . PHE A 1 1568 ? 190.348 219.515 185.742 1.00 4.59  ? 1568 PHE A CD2   1 
ATOM   956   C  CE1   . PHE A 1 1568 ? 191.981 217.817 184.315 1.00 3.49  ? 1568 PHE A CE1   1 
ATOM   957   C  CE2   . PHE A 1 1568 ? 189.982 219.107 184.480 1.00 5.01  ? 1568 PHE A CE2   1 
ATOM   958   C  CZ    . PHE A 1 1568 ? 190.799 218.257 183.766 1.00 4.22  ? 1568 PHE A CZ    1 
ATOM   959   N  N     . GLN A 1 1569 ? 191.813 222.743 187.234 1.00 16.62 ? 1569 GLN A N     1 
ATOM   960   C  CA    . GLN A 1 1569 ? 191.359 223.846 186.394 1.00 15.79 ? 1569 GLN A CA    1 
ATOM   961   C  C     . GLN A 1 1569 ? 192.539 224.623 185.824 1.00 16.35 ? 1569 GLN A C     1 
ATOM   962   O  O     . GLN A 1 1569 ? 192.528 225.012 184.651 1.00 16.30 ? 1569 GLN A O     1 
ATOM   963   C  CB    . GLN A 1 1569 ? 190.445 224.771 187.196 1.00 17.71 ? 1569 GLN A CB    1 
ATOM   964   C  CG    . GLN A 1 1569 ? 189.864 225.907 186.380 1.00 20.36 ? 1569 GLN A CG    1 
ATOM   965   C  CD    . GLN A 1 1569 ? 188.989 225.405 185.250 1.00 27.04 ? 1569 GLN A CD    1 
ATOM   966   O  OE1   . GLN A 1 1569 ? 189.390 225.418 184.088 1.00 27.79 ? 1569 GLN A OE1   1 
ATOM   967   N  NE2   . GLN A 1 1569 ? 187.783 224.965 185.587 1.00 27.03 ? 1569 GLN A NE2   1 
ATOM   968   N  N     . SER A 1 1570 ? 193.566 224.859 186.644 1.00 15.62 ? 1570 SER A N     1 
ATOM   969   C  CA    . SER A 1 1570 ? 194.747 225.582 186.182 1.00 14.84 ? 1570 SER A CA    1 
ATOM   970   C  C     . SER A 1 1570 ? 195.489 224.800 185.104 1.00 18.37 ? 1570 SER A C     1 
ATOM   971   O  O     . SER A 1 1570 ? 195.904 225.364 184.086 1.00 24.02 ? 1570 SER A O     1 
ATOM   972   C  CB    . SER A 1 1570 ? 195.670 225.875 187.366 1.00 18.73 ? 1570 SER A CB    1 
ATOM   973   O  OG    . SER A 1 1570 ? 194.955 226.478 188.433 1.00 21.35 ? 1570 SER A OG    1 
ATOM   974   N  N     . ILE A 1 1571 ? 195.669 223.496 185.315 1.00 16.59 ? 1571 ILE A N     1 
ATOM   975   C  CA    . ILE A 1 1571 ? 196.333 222.666 184.315 1.00 11.82 ? 1571 ILE A CA    1 
ATOM   976   C  C     . ILE A 1 1571 ? 195.466 222.524 183.073 1.00 14.38 ? 1571 ILE A C     1 
ATOM   977   O  O     . ILE A 1 1571 ? 195.973 222.524 181.944 1.00 15.63 ? 1571 ILE A O     1 
ATOM   978   C  CB    . ILE A 1 1571 ? 196.696 221.299 184.920 1.00 10.56 ? 1571 ILE A CB    1 
ATOM   979   C  CG1   . ILE A 1 1571 ? 197.199 221.485 186.349 1.00 14.81 ? 1571 ILE A CG1   1 
ATOM   980   C  CG2   . ILE A 1 1571 ? 197.725 220.588 184.073 1.00 13.00 ? 1571 ILE A CG2   1 
ATOM   981   C  CD1   . ILE A 1 1571 ? 197.667 220.230 186.997 1.00 15.44 ? 1571 ILE A CD1   1 
ATOM   982   N  N     . SER A 1 1572 ? 194.151 222.401 183.256 1.00 11.55 ? 1572 SER A N     1 
ATOM   983   C  CA    . SER A 1 1572 ? 193.251 222.319 182.112 1.00 10.47 ? 1572 SER A CA    1 
ATOM   984   C  C     . SER A 1 1572 ? 193.271 223.604 181.296 1.00 14.57 ? 1572 SER A C     1 
ATOM   985   O  O     . SER A 1 1572 ? 192.952 223.585 180.102 1.00 15.68 ? 1572 SER A O     1 
ATOM   986   C  CB    . SER A 1 1572 ? 191.832 222.005 182.585 1.00 9.59  ? 1572 SER A CB    1 
ATOM   987   O  OG    . SER A 1 1572 ? 190.953 221.805 181.496 1.00 16.28 ? 1572 SER A OG    1 
ATOM   988   N  N     . THR A 1 1573 ? 193.630 224.729 181.918 1.00 18.01 ? 1573 THR A N     1 
ATOM   989   C  CA    . THR A 1 1573 ? 193.742 225.979 181.173 1.00 16.69 ? 1573 THR A CA    1 
ATOM   990   C  C     . THR A 1 1573 ? 194.983 225.987 180.288 1.00 15.79 ? 1573 THR A C     1 
ATOM   991   O  O     . THR A 1 1573 ? 194.911 226.363 179.114 1.00 15.68 ? 1573 THR A O     1 
ATOM   992   C  CB    . THR A 1 1573 ? 193.759 227.167 182.133 1.00 16.79 ? 1573 THR A CB    1 
ATOM   993   O  OG1   . THR A 1 1573 ? 192.621 227.096 183.000 1.00 23.67 ? 1573 THR A OG1   1 
ATOM   994   C  CG2   . THR A 1 1573 ? 193.705 228.472 181.360 1.00 12.10 ? 1573 THR A CG2   1 
ATOM   995   N  N     . GLU A 1 1574 ? 196.129 225.566 180.832 1.00 15.04 ? 1574 GLU A N     1 
ATOM   996   C  CA    . GLU A 1 1574 ? 197.357 225.556 180.044 1.00 12.26 ? 1574 GLU A CA    1 
ATOM   997   C  C     . GLU A 1 1574 ? 197.282 224.527 178.923 1.00 16.44 ? 1574 GLU A C     1 
ATOM   998   O  O     . GLU A 1 1574 ? 197.833 224.739 177.836 1.00 17.63 ? 1574 GLU A O     1 
ATOM   999   C  CB    . GLU A 1 1574 ? 198.563 225.291 180.947 1.00 12.79 ? 1574 GLU A CB    1 
ATOM   1000  C  CG    . GLU A 1 1574 ? 199.884 225.074 180.209 1.00 14.67 ? 1574 GLU A CG    1 
ATOM   1001  C  CD    . GLU A 1 1574 ? 200.221 226.187 179.223 1.00 23.49 ? 1574 GLU A CD    1 
ATOM   1002  O  OE1   . GLU A 1 1574 ? 199.857 227.356 179.477 1.00 27.07 ? 1574 GLU A OE1   1 
ATOM   1003  O  OE2   . GLU A 1 1574 ? 200.852 225.889 178.187 1.00 19.21 ? 1574 GLU A OE2   1 
ATOM   1004  N  N     . PHE A 1 1575 ? 196.607 223.402 179.168 1.00 12.44 ? 1575 PHE A N     1 
ATOM   1005  C  CA    . PHE A 1 1575 ? 196.425 222.408 178.116 1.00 11.32 ? 1575 PHE A CA    1 
ATOM   1006  C  C     . PHE A 1 1575 ? 195.608 222.978 176.964 1.00 10.68 ? 1575 PHE A C     1 
ATOM   1007  O  O     . PHE A 1 1575 ? 196.005 222.876 175.799 1.00 8.84  ? 1575 PHE A O     1 
ATOM   1008  C  CB    . PHE A 1 1575 ? 195.760 221.152 178.684 1.00 11.44 ? 1575 PHE A CB    1 
ATOM   1009  C  CG    . PHE A 1 1575 ? 195.359 220.153 177.637 1.00 8.88  ? 1575 PHE A CG    1 
ATOM   1010  C  CD1   . PHE A 1 1575 ? 196.285 219.255 177.129 1.00 9.87  ? 1575 PHE A CD1   1 
ATOM   1011  C  CD2   . PHE A 1 1575 ? 194.059 220.105 177.164 1.00 7.40  ? 1575 PHE A CD2   1 
ATOM   1012  C  CE1   . PHE A 1 1575 ? 195.922 218.335 176.167 1.00 7.42  ? 1575 PHE A CE1   1 
ATOM   1013  C  CE2   . PHE A 1 1575 ? 193.693 219.189 176.201 1.00 6.80  ? 1575 PHE A CE2   1 
ATOM   1014  C  CZ    . PHE A 1 1575 ? 194.625 218.301 175.705 1.00 6.24  ? 1575 PHE A CZ    1 
ATOM   1015  N  N     . LEU A 1 1576 ? 194.467 223.602 177.275 1.00 17.90 ? 1576 LEU A N     1 
ATOM   1016  C  CA    . LEU A 1 1576 ? 193.621 224.175 176.232 1.00 15.98 ? 1576 LEU A CA    1 
ATOM   1017  C  C     . LEU A 1 1576 ? 194.319 225.307 175.491 1.00 14.28 ? 1576 LEU A C     1 
ATOM   1018  O  O     . LEU A 1 1576 ? 194.125 225.463 174.280 1.00 16.74 ? 1576 LEU A O     1 
ATOM   1019  C  CB    . LEU A 1 1576 ? 192.303 224.667 176.831 1.00 14.71 ? 1576 LEU A CB    1 
ATOM   1020  C  CG    . LEU A 1 1576 ? 191.310 223.602 177.304 1.00 16.38 ? 1576 LEU A CG    1 
ATOM   1021  C  CD1   . LEU A 1 1576 ? 190.080 224.244 177.922 1.00 20.16 ? 1576 LEU A CD1   1 
ATOM   1022  C  CD2   . LEU A 1 1576 ? 190.909 222.695 176.154 1.00 18.87 ? 1576 LEU A CD2   1 
ATOM   1023  N  N     . ALA A 1 1577 ? 195.119 226.112 176.194 1.00 12.99 ? 1577 ALA A N     1 
ATOM   1024  C  CA    . ALA A 1 1577 ? 195.874 227.165 175.525 1.00 15.29 ? 1577 ALA A CA    1 
ATOM   1025  C  C     . ALA A 1 1577 ? 196.855 226.579 174.515 1.00 16.86 ? 1577 ALA A C     1 
ATOM   1026  O  O     . ALA A 1 1577 ? 196.992 227.091 173.399 1.00 17.89 ? 1577 ALA A O     1 
ATOM   1027  C  CB    . ALA A 1 1577 ? 196.609 228.020 176.555 1.00 11.88 ? 1577 ALA A CB    1 
ATOM   1028  N  N     . LEU A 1 1578 ? 197.536 225.496 174.890 1.00 12.69 ? 1578 LEU A N     1 
ATOM   1029  C  CA    . LEU A 1 1578 ? 198.453 224.844 173.964 1.00 14.46 ? 1578 LEU A CA    1 
ATOM   1030  C  C     . LEU A 1 1578 ? 197.699 224.137 172.846 1.00 14.39 ? 1578 LEU A C     1 
ATOM   1031  O  O     . LEU A 1 1578 ? 198.215 223.999 171.732 1.00 15.57 ? 1578 LEU A O     1 
ATOM   1032  C  CB    . LEU A 1 1578 ? 199.352 223.877 174.732 1.00 12.35 ? 1578 LEU A CB    1 
ATOM   1033  C  CG    . LEU A 1 1578 ? 200.445 223.113 173.997 1.00 12.57 ? 1578 LEU A CG    1 
ATOM   1034  C  CD1   . LEU A 1 1578 ? 201.465 224.060 173.400 1.00 16.56 ? 1578 LEU A CD1   1 
ATOM   1035  C  CD2   . LEU A 1 1578 ? 201.118 222.205 174.993 1.00 13.40 ? 1578 LEU A CD2   1 
ATOM   1036  N  N     . MET A 1 1579 ? 196.470 223.686 173.120 1.00 15.47 ? 1579 MET A N     1 
ATOM   1037  C  CA    . MET A 1 1579 ? 195.635 223.114 172.068 1.00 11.02 ? 1579 MET A CA    1 
ATOM   1038  C  C     . MET A 1 1579 ? 195.280 224.147 171.008 1.00 13.54 ? 1579 MET A C     1 
ATOM   1039  O  O     . MET A 1 1579 ? 195.277 223.831 169.813 1.00 16.69 ? 1579 MET A O     1 
ATOM   1040  C  CB    . MET A 1 1579 ? 194.355 222.531 172.666 1.00 14.90 ? 1579 MET A CB    1 
ATOM   1041  C  CG    . MET A 1 1579 ? 194.572 221.349 173.579 1.00 16.72 ? 1579 MET A CG    1 
ATOM   1042  S  SD    . MET A 1 1579 ? 195.340 219.955 172.753 1.00 33.42 ? 1579 MET A SD    1 
ATOM   1043  C  CE    . MET A 1 1579 ? 194.009 219.451 171.677 1.00 29.41 ? 1579 MET A CE    1 
ATOM   1044  N  N     . LYS A 1 1580 ? 194.968 225.376 171.426 1.00 14.74 ? 1580 LYS A N     1 
ATOM   1045  C  CA    . LYS A 1 1580 ? 194.581 226.411 170.472 1.00 18.01 ? 1580 LYS A CA    1 
ATOM   1046  C  C     . LYS A 1 1580 ? 195.735 226.763 169.541 1.00 19.21 ? 1580 LYS A C     1 
ATOM   1047  O  O     . LYS A 1 1580 ? 195.521 227.031 168.353 1.00 22.13 ? 1580 LYS A O     1 
ATOM   1048  C  CB    . LYS A 1 1580 ? 194.086 227.650 171.219 1.00 18.13 ? 1580 LYS A CB    1 
ATOM   1049  C  CG    . LYS A 1 1580 ? 193.524 228.737 170.318 1.00 24.69 ? 1580 LYS A CG    1 
ATOM   1050  C  CD    . LYS A 1 1580 ? 193.046 229.933 171.125 1.00 24.94 ? 1580 LYS A CD    1 
ATOM   1051  C  CE    . LYS A 1 1580 ? 191.781 229.607 171.902 1.00 25.59 ? 1580 LYS A CE    1 
ATOM   1052  N  NZ    . LYS A 1 1580 ? 190.621 229.369 171.000 1.00 31.76 ? 1580 LYS A NZ    1 
ATOM   1053  N  N     . LYS A 1 1581 ? 196.964 226.771 170.062 1.00 17.42 ? 1581 LYS A N     1 
ATOM   1054  C  CA    . LYS A 1 1581 ? 198.126 227.004 169.208 1.00 15.33 ? 1581 LYS A CA    1 
ATOM   1055  C  C     . LYS A 1 1581 ? 198.264 225.911 168.156 1.00 17.11 ? 1581 LYS A C     1 
ATOM   1056  O  O     . LYS A 1 1581 ? 198.579 226.195 166.995 1.00 21.18 ? 1581 LYS A O     1 
ATOM   1057  C  CB    . LYS A 1 1581 ? 199.397 227.089 170.051 1.00 13.19 ? 1581 LYS A CB    1 
ATOM   1058  C  CG    . LYS A 1 1581 ? 199.584 228.409 170.773 1.00 14.77 ? 1581 LYS A CG    1 
ATOM   1059  C  CD    . LYS A 1 1581 ? 200.844 228.393 171.620 1.00 14.64 ? 1581 LYS A CD    1 
ATOM   1060  C  CE    . LYS A 1 1581 ? 200.627 227.638 172.917 1.00 15.90 ? 1581 LYS A CE    1 
ATOM   1061  N  NZ    . LYS A 1 1581 ? 201.030 228.443 174.103 1.00 18.54 ? 1581 LYS A NZ    1 
ATOM   1062  N  N     . VAL A 1 1582 ? 198.036 224.656 168.546 1.00 13.57 ? 1582 VAL A N     1 
ATOM   1063  C  CA    . VAL A 1 1582 ? 198.111 223.549 167.599 1.00 12.49 ? 1582 VAL A CA    1 
ATOM   1064  C  C     . VAL A 1 1582 ? 197.058 223.712 166.512 1.00 16.49 ? 1582 VAL A C     1 
ATOM   1065  O  O     . VAL A 1 1582 ? 197.294 223.386 165.341 1.00 19.46 ? 1582 VAL A O     1 
ATOM   1066  C  CB    . VAL A 1 1582 ? 197.967 222.205 168.337 1.00 13.56 ? 1582 VAL A CB    1 
ATOM   1067  C  CG1   . VAL A 1 1582 ? 197.919 221.046 167.351 1.00 8.75  ? 1582 VAL A CG1   1 
ATOM   1068  C  CG2   . VAL A 1 1582 ? 199.106 222.019 169.328 1.00 10.43 ? 1582 VAL A CG2   1 
ATOM   1069  N  N     . SER A 1 1583 ? 195.878 224.220 166.878 1.00 19.90 ? 1583 SER A N     1 
ATOM   1070  C  CA    . SER A 1 1583 ? 194.821 224.424 165.893 1.00 18.38 ? 1583 SER A CA    1 
ATOM   1071  C  C     . SER A 1 1583 ? 195.236 225.443 164.836 1.00 25.58 ? 1583 SER A C     1 
ATOM   1072  O  O     . SER A 1 1583 ? 194.949 225.263 163.646 1.00 30.74 ? 1583 SER A O     1 
ATOM   1073  C  CB    . SER A 1 1583 ? 193.535 224.861 166.589 1.00 22.32 ? 1583 SER A CB    1 
ATOM   1074  O  OG    . SER A 1 1583 ? 192.453 224.907 165.675 1.00 32.97 ? 1583 SER A OG    1 
ATOM   1075  N  N     . LYS A 1 1584 ? 195.898 226.523 165.252 1.00 16.72 ? 1584 LYS A N     1 
ATOM   1076  C  CA    . LYS A 1 1584 ? 196.347 227.531 164.297 1.00 20.25 ? 1584 LYS A CA    1 
ATOM   1077  C  C     . LYS A 1 1584 ? 197.388 226.961 163.340 1.00 26.24 ? 1584 LYS A C     1 
ATOM   1078  O  O     . LYS A 1 1584 ? 197.320 227.178 162.126 1.00 23.81 ? 1584 LYS A O     1 
ATOM   1079  C  CB    . LYS A 1 1584 ? 196.908 228.746 165.038 1.00 20.52 ? 1584 LYS A CB    1 
ATOM   1080  C  CG    . LYS A 1 1584 ? 195.996 229.298 166.112 1.00 22.30 ? 1584 LYS A CG    1 
ATOM   1081  C  CD    . LYS A 1 1584 ? 194.669 229.751 165.528 1.00 27.61 ? 1584 LYS A CD    1 
ATOM   1082  C  CE    . LYS A 1 1584 ? 193.767 230.334 166.600 1.00 28.44 ? 1584 LYS A CE    1 
ATOM   1083  N  NZ    . LYS A 1 1584 ? 194.416 231.472 167.309 1.00 29.68 ? 1584 LYS A NZ    1 
ATOM   1084  N  N     . SER A 1 1585 ? 198.359 226.217 163.873 1.00 21.71 ? 1585 SER A N     1 
ATOM   1085  C  CA    . SER A 1 1585 ? 199.447 225.638 163.087 1.00 20.62 ? 1585 SER A CA    1 
ATOM   1086  C  C     . SER A 1 1585 ? 199.482 224.136 163.337 1.00 19.91 ? 1585 SER A C     1 
ATOM   1087  O  O     . SER A 1 1585 ? 200.254 223.655 164.180 1.00 21.97 ? 1585 SER A O     1 
ATOM   1088  C  CB    . SER A 1 1585 ? 200.785 226.283 163.441 1.00 23.16 ? 1585 SER A CB    1 
ATOM   1089  O  OG    . SER A 1 1585 ? 201.140 226.007 164.786 1.00 33.13 ? 1585 SER A OG    1 
ATOM   1090  N  N     . PRO A 1 1586 ? 198.665 223.356 162.627 1.00 18.84 ? 1586 PRO A N     1 
ATOM   1091  C  CA    . PRO A 1 1586 ? 198.671 221.903 162.828 1.00 19.19 ? 1586 PRO A CA    1 
ATOM   1092  C  C     . PRO A 1 1586 ? 199.864 221.199 162.205 1.00 22.49 ? 1586 PRO A C     1 
ATOM   1093  O  O     . PRO A 1 1586 ? 199.987 219.977 162.363 1.00 21.51 ? 1586 PRO A O     1 
ATOM   1094  C  CB    . PRO A 1 1586 ? 197.360 221.458 162.173 1.00 18.31 ? 1586 PRO A CB    1 
ATOM   1095  C  CG    . PRO A 1 1586 ? 197.110 222.472 161.108 1.00 16.40 ? 1586 PRO A CG    1 
ATOM   1096  C  CD    . PRO A 1 1586 ? 197.794 223.759 161.509 1.00 19.16 ? 1586 PRO A CD    1 
ATOM   1097  N  N     . LEU A 1 1587 ? 200.735 221.924 161.505 1.00 22.55 ? 1587 LEU A N     1 
ATOM   1098  C  CA    . LEU A 1 1587 ? 201.945 221.329 160.959 1.00 19.54 ? 1587 LEU A CA    1 
ATOM   1099  C  C     . LEU A 1 1587 ? 202.844 220.846 162.092 1.00 16.41 ? 1587 LEU A C     1 
ATOM   1100  O  O     . LEU A 1 1587 ? 203.023 221.537 163.099 1.00 18.74 ? 1587 LEU A O     1 
ATOM   1101  C  CB    . LEU A 1 1587 ? 202.685 222.347 160.089 1.00 20.35 ? 1587 LEU A CB    1 
ATOM   1102  C  CG    . LEU A 1 1587 ? 203.942 221.874 159.360 1.00 19.85 ? 1587 LEU A CG    1 
ATOM   1103  C  CD1   . LEU A 1 1587 ? 203.588 220.786 158.361 1.00 25.31 ? 1587 LEU A CD1   1 
ATOM   1104  C  CD2   . LEU A 1 1587 ? 204.640 223.035 158.669 1.00 23.70 ? 1587 LEU A CD2   1 
ATOM   1105  N  N     . VAL A 1 1588 ? 203.412 219.651 161.920 1.00 16.51 ? 1588 VAL A N     1 
ATOM   1106  C  CA    . VAL A 1 1588 ? 204.187 219.032 162.992 1.00 17.19 ? 1588 VAL A CA    1 
ATOM   1107  C  C     . VAL A 1 1588 ? 205.418 219.867 163.323 1.00 17.11 ? 1588 VAL A C     1 
ATOM   1108  O  O     . VAL A 1 1588 ? 205.757 220.059 164.498 1.00 19.31 ? 1588 VAL A O     1 
ATOM   1109  C  CB    . VAL A 1 1588 ? 204.563 217.587 162.613 1.00 14.66 ? 1588 VAL A CB    1 
ATOM   1110  C  CG1   . VAL A 1 1588 ? 205.519 216.999 163.637 1.00 10.48 ? 1588 VAL A CG1   1 
ATOM   1111  C  CG2   . VAL A 1 1588 ? 203.314 216.733 162.497 1.00 17.54 ? 1588 VAL A CG2   1 
ATOM   1112  N  N     . MET A 1 1589 ? 206.105 220.378 162.300 1.00 21.59 ? 1589 MET A N     1 
ATOM   1113  C  CA    . MET A 1 1589 ? 207.307 221.172 162.538 1.00 18.42 ? 1589 MET A CA    1 
ATOM   1114  C  C     . MET A 1 1589 ? 206.987 222.443 163.317 1.00 19.30 ? 1589 MET A C     1 
ATOM   1115  O  O     . MET A 1 1589 ? 207.747 222.839 164.208 1.00 19.82 ? 1589 MET A O     1 
ATOM   1116  C  CB    . MET A 1 1589 ? 207.986 221.505 161.212 1.00 14.14 ? 1589 MET A CB    1 
ATOM   1117  C  CG    . MET A 1 1589 ? 208.718 220.330 160.580 1.00 19.41 ? 1589 MET A CG    1 
ATOM   1118  S  SD    . MET A 1 1589 ? 209.543 219.275 161.789 1.00 39.80 ? 1589 MET A SD    1 
ATOM   1119  C  CE    . MET A 1 1589 ? 211.046 220.198 162.080 1.00 20.09 ? 1589 MET A CE    1 
ATOM   1120  N  N     . ASP A 1 1590 ? 205.867 223.095 162.996 1.00 20.15 ? 1590 ASP A N     1 
ATOM   1121  C  CA    . ASP A 1 1590 ? 205.465 224.281 163.746 1.00 17.25 ? 1590 ASP A CA    1 
ATOM   1122  C  C     . ASP A 1 1590 ? 205.181 223.945 165.204 1.00 17.46 ? 1590 ASP A C     1 
ATOM   1123  O  O     . ASP A 1 1590 ? 205.559 224.698 166.109 1.00 21.31 ? 1590 ASP A O     1 
ATOM   1124  C  CB    . ASP A 1 1590 ? 204.243 224.926 163.095 1.00 20.10 ? 1590 ASP A CB    1 
ATOM   1125  C  CG    . ASP A 1 1590 ? 204.558 225.546 161.749 1.00 32.95 ? 1590 ASP A CG    1 
ATOM   1126  O  OD1   . ASP A 1 1590 ? 205.713 225.979 161.548 1.00 35.20 ? 1590 ASP A OD1   1 
ATOM   1127  O  OD2   . ASP A 1 1590 ? 203.652 225.602 160.892 1.00 38.73 ? 1590 ASP A OD2   1 
ATOM   1128  N  N     . VAL A 1 1591 ? 204.508 222.818 165.453 1.00 12.12 ? 1591 VAL A N     1 
ATOM   1129  C  CA    . VAL A 1 1591 ? 204.275 222.384 166.826 1.00 12.26 ? 1591 VAL A CA    1 
ATOM   1130  C  C     . VAL A 1 1591 ? 205.595 222.046 167.506 1.00 14.88 ? 1591 VAL A C     1 
ATOM   1131  O  O     . VAL A 1 1591 ? 205.813 222.381 168.677 1.00 20.39 ? 1591 VAL A O     1 
ATOM   1132  C  CB    . VAL A 1 1591 ? 203.299 221.192 166.852 1.00 13.93 ? 1591 VAL A CB    1 
ATOM   1133  C  CG1   . VAL A 1 1591 ? 203.097 220.702 168.275 1.00 9.37  ? 1591 VAL A CG1   1 
ATOM   1134  C  CG2   . VAL A 1 1591 ? 201.969 221.583 166.234 1.00 13.86 ? 1591 VAL A CG2   1 
ATOM   1135  N  N     . LEU A 1 1592 ? 206.500 221.382 166.783 1.00 14.12 ? 1592 LEU A N     1 
ATOM   1136  C  CA    . LEU A 1 1592 ? 207.793 221.014 167.348 1.00 16.61 ? 1592 LEU A CA    1 
ATOM   1137  C  C     . LEU A 1 1592 ? 208.640 222.230 167.702 1.00 13.96 ? 1592 LEU A C     1 
ATOM   1138  O  O     . LEU A 1 1592 ? 209.499 222.136 168.585 1.00 15.26 ? 1592 LEU A O     1 
ATOM   1139  C  CB    . LEU A 1 1592 ? 208.551 220.113 166.368 1.00 19.30 ? 1592 LEU A CB    1 
ATOM   1140  C  CG    . LEU A 1 1592 ? 209.919 219.581 166.801 1.00 16.60 ? 1592 LEU A CG    1 
ATOM   1141  C  CD1   . LEU A 1 1592 ? 209.768 218.549 167.907 1.00 10.13 ? 1592 LEU A CD1   1 
ATOM   1142  C  CD2   . LEU A 1 1592 ? 210.677 219.005 165.618 1.00 15.51 ? 1592 LEU A CD2   1 
ATOM   1143  N  N     . ASN A 1 1593 ? 208.412 223.365 167.046 1.00 18.56 ? 1593 ASN A N     1 
ATOM   1144  C  CA    . ASN A 1 1593 ? 209.172 224.583 167.294 1.00 17.46 ? 1593 ASN A CA    1 
ATOM   1145  C  C     . ASN A 1 1593 ? 208.514 225.507 168.313 1.00 18.78 ? 1593 ASN A C     1 
ATOM   1146  O  O     . ASN A 1 1593 ? 209.038 226.594 168.568 1.00 22.36 ? 1593 ASN A O     1 
ATOM   1147  C  CB    . ASN A 1 1593 ? 209.389 225.342 165.981 1.00 17.85 ? 1593 ASN A CB    1 
ATOM   1148  C  CG    . ASN A 1 1593 ? 210.191 224.542 164.973 1.00 26.08 ? 1593 ASN A CG    1 
ATOM   1149  O  OD1   . ASN A 1 1593 ? 210.620 223.424 165.250 1.00 23.67 ? 1593 ASN A OD1   1 
ATOM   1150  N  ND2   . ASN A 1 1593 ? 210.391 225.112 163.790 1.00 24.55 ? 1593 ASN A ND2   1 
ATOM   1151  N  N     . ILE A 1 1594 ? 207.381 225.108 168.896 1.00 19.26 ? 1594 ILE A N     1 
ATOM   1152  C  CA    . ILE A 1 1594 ? 206.764 225.916 169.940 1.00 17.05 ? 1594 ILE A CA    1 
ATOM   1153  C  C     . ILE A 1 1594 ? 207.696 225.974 171.139 1.00 16.27 ? 1594 ILE A C     1 
ATOM   1154  O  O     . ILE A 1 1594 ? 208.240 224.951 171.569 1.00 21.73 ? 1594 ILE A O     1 
ATOM   1155  C  CB    . ILE A 1 1594 ? 205.383 225.346 170.313 1.00 14.12 ? 1594 ILE A CB    1 
ATOM   1156  C  CG1   . ILE A 1 1594 ? 204.446 225.398 169.105 1.00 12.79 ? 1594 ILE A CG1   1 
ATOM   1157  C  CG2   . ILE A 1 1594 ? 204.789 226.106 171.486 1.00 11.99 ? 1594 ILE A CG2   1 
ATOM   1158  C  CD1   . ILE A 1 1594 ? 203.064 224.860 169.374 1.00 10.90 ? 1594 ILE A CD1   1 
ATOM   1159  N  N     . GLN A 1 1595 ? 207.892 227.178 171.673 1.00 18.61 ? 1595 GLN A N     1 
ATOM   1160  C  CA    . GLN A 1 1595 ? 208.897 227.390 172.706 1.00 19.11 ? 1595 GLN A CA    1 
ATOM   1161  C  C     . GLN A 1 1595 ? 208.571 226.588 173.960 1.00 14.90 ? 1595 GLN A C     1 
ATOM   1162  O  O     . GLN A 1 1595 ? 207.492 226.730 174.543 1.00 13.42 ? 1595 GLN A O     1 
ATOM   1163  C  CB    . GLN A 1 1595 ? 208.997 228.876 173.043 1.00 17.32 ? 1595 GLN A CB    1 
ATOM   1164  C  CG    . GLN A 1 1595 ? 210.065 229.209 174.067 1.00 17.62 ? 1595 GLN A CG    1 
ATOM   1165  C  CD    . GLN A 1 1595 ? 210.141 230.693 174.366 1.00 30.99 ? 1595 GLN A CD    1 
ATOM   1166  O  OE1   . GLN A 1 1595 ? 209.385 231.491 173.809 1.00 31.14 ? 1595 GLN A OE1   1 
ATOM   1167  N  NE2   . GLN A 1 1595 ? 211.058 231.075 175.247 1.00 28.97 ? 1595 GLN A NE2   1 
ATOM   1168  N  N     . GLY A 1 1596 ? 209.514 225.743 174.369 1.00 18.89 ? 1596 GLY A N     1 
ATOM   1169  C  CA    . GLY A 1 1596 ? 209.357 224.952 175.575 1.00 15.15 ? 1596 GLY A CA    1 
ATOM   1170  C  C     . GLY A 1 1596 ? 208.244 223.935 175.523 1.00 17.14 ? 1596 GLY A C     1 
ATOM   1171  O  O     . GLY A 1 1596 ? 207.753 223.516 176.573 1.00 20.06 ? 1596 GLY A O     1 
ATOM   1172  N  N     . VAL A 1 1597 ? 207.832 223.519 174.325 1.00 17.81 ? 1597 VAL A N     1 
ATOM   1173  C  CA    . VAL A 1 1597 ? 206.717 222.583 174.210 1.00 12.72 ? 1597 VAL A CA    1 
ATOM   1174  C  C     . VAL A 1 1597 ? 207.084 221.235 174.820 1.00 12.64 ? 1597 VAL A C     1 
ATOM   1175  O  O     . VAL A 1 1597 ? 206.236 220.554 175.409 1.00 18.03 ? 1597 VAL A O     1 
ATOM   1176  C  CB    . VAL A 1 1597 ? 206.263 222.460 172.741 1.00 13.98 ? 1597 VAL A CB    1 
ATOM   1177  C  CG1   . VAL A 1 1597 ? 207.230 221.619 171.923 1.00 14.34 ? 1597 VAL A CG1   1 
ATOM   1178  C  CG2   . VAL A 1 1597 ? 204.857 221.883 172.669 1.00 16.70 ? 1597 VAL A CG2   1 
ATOM   1179  N  N     . GLN A 1 1598 ? 208.349 220.829 174.699 1.00 9.79  ? 1598 GLN A N     1 
ATOM   1180  C  CA    . GLN A 1 1598 ? 208.796 219.588 175.322 1.00 7.98  ? 1598 GLN A CA    1 
ATOM   1181  C  C     . GLN A 1 1598 ? 208.677 219.664 176.838 1.00 11.44 ? 1598 GLN A C     1 
ATOM   1182  O  O     . GLN A 1 1598 ? 208.183 218.734 177.485 1.00 14.46 ? 1598 GLN A O     1 
ATOM   1183  C  CB    . GLN A 1 1598 ? 210.234 219.283 174.910 1.00 9.93  ? 1598 GLN A CB    1 
ATOM   1184  C  CG    . GLN A 1 1598 ? 210.724 217.917 175.346 1.00 7.23  ? 1598 GLN A CG    1 
ATOM   1185  C  CD    . GLN A 1 1598 ? 209.878 216.793 174.795 1.00 9.60  ? 1598 GLN A CD    1 
ATOM   1186  O  OE1   . GLN A 1 1598 ? 209.747 216.643 173.583 1.00 18.28 ? 1598 GLN A OE1   1 
ATOM   1187  N  NE2   . GLN A 1 1598 ? 209.311 215.986 175.681 1.00 4.80  ? 1598 GLN A NE2   1 
ATOM   1188  N  N     . ARG A 1 1599 ? 209.124 220.776 177.423 1.00 16.93 ? 1599 ARG A N     1 
ATOM   1189  C  CA    . ARG A 1 1599 ? 209.061 220.913 178.873 1.00 14.36 ? 1599 ARG A CA    1 
ATOM   1190  C  C     . ARG A 1 1599 ? 207.633 221.165 179.340 1.00 13.39 ? 1599 ARG A C     1 
ATOM   1191  O  O     . ARG A 1 1599 ? 207.273 220.794 180.463 1.00 14.43 ? 1599 ARG A O     1 
ATOM   1192  C  CB    . ARG A 1 1599 ? 210.008 222.029 179.325 1.00 11.98 ? 1599 ARG A CB    1 
ATOM   1193  C  CG    . ARG A 1 1599 ? 210.196 222.166 180.834 1.00 17.19 ? 1599 ARG A CG    1 
ATOM   1194  C  CD    . ARG A 1 1599 ? 209.190 223.120 181.456 1.00 20.86 ? 1599 ARG A CD    1 
ATOM   1195  N  NE    . ARG A 1 1599 ? 209.315 224.470 180.922 1.00 26.89 ? 1599 ARG A NE    1 
ATOM   1196  C  CZ    . ARG A 1 1599 ? 208.390 225.412 181.049 1.00 35.27 ? 1599 ARG A CZ    1 
ATOM   1197  N  NH1   . ARG A 1 1599 ? 207.239 225.171 181.656 1.00 25.34 ? 1599 ARG A NH1   1 
ATOM   1198  N  NH2   . ARG A 1 1599 ? 208.623 226.622 180.549 1.00 24.13 ? 1599 ARG A NH2   1 
ATOM   1199  N  N     . SER A 1 1600 ? 206.805 221.781 178.494 1.00 11.11 ? 1600 SER A N     1 
ATOM   1200  C  CA    . SER A 1 1600 ? 205.406 221.994 178.851 1.00 10.83 ? 1600 SER A CA    1 
ATOM   1201  C  C     . SER A 1 1600 ? 204.672 220.669 179.005 1.00 17.03 ? 1600 SER A C     1 
ATOM   1202  O  O     . SER A 1 1600 ? 203.931 220.463 179.973 1.00 15.75 ? 1600 SER A O     1 
ATOM   1203  C  CB    . SER A 1 1600 ? 204.722 222.868 177.800 1.00 9.55  ? 1600 SER A CB    1 
ATOM   1204  O  OG    . SER A 1 1600 ? 205.291 224.164 177.761 1.00 16.20 ? 1600 SER A OG    1 
ATOM   1205  N  N     . LEU A 1 1601 ? 204.872 219.748 178.057 1.00 9.31  ? 1601 LEU A N     1 
ATOM   1206  C  CA    . LEU A 1 1601 ? 204.238 218.439 178.160 1.00 8.10  ? 1601 LEU A CA    1 
ATOM   1207  C  C     . LEU A 1 1601 ? 204.800 217.636 179.321 1.00 10.65 ? 1601 LEU A C     1 
ATOM   1208  O  O     . LEU A 1 1601 ? 204.060 216.907 179.991 1.00 16.00 ? 1601 LEU A O     1 
ATOM   1209  C  CB    . LEU A 1 1601 ? 204.391 217.651 176.859 1.00 11.69 ? 1601 LEU A CB    1 
ATOM   1210  C  CG    . LEU A 1 1601 ? 203.325 217.928 175.807 1.00 6.55  ? 1601 LEU A CG    1 
ATOM   1211  C  CD1   . LEU A 1 1601 ? 202.004 217.500 176.419 1.00 9.73  ? 1601 LEU A CD1   1 
ATOM   1212  C  CD2   . LEU A 1 1601 ? 203.284 219.370 175.357 1.00 11.63 ? 1601 LEU A CD2   1 
ATOM   1213  N  N     . GLU A 1 1602 ? 206.105 217.745 179.564 1.00 11.33 ? 1602 GLU A N     1 
ATOM   1214  C  CA    . GLU A 1 1602 ? 206.697 217.030 180.688 1.00 12.01 ? 1602 GLU A CA    1 
ATOM   1215  C  C     . GLU A 1 1602 ? 206.076 217.482 182.002 1.00 9.43  ? 1602 GLU A C     1 
ATOM   1216  O  O     . GLU A 1 1602 ? 205.811 216.661 182.887 1.00 7.47  ? 1602 GLU A O     1 
ATOM   1217  C  CB    . GLU A 1 1602 ? 208.211 217.234 180.698 1.00 14.88 ? 1602 GLU A CB    1 
ATOM   1218  C  CG    . GLU A 1 1602 ? 208.936 216.462 181.788 1.00 19.14 ? 1602 GLU A CG    1 
ATOM   1219  C  CD    . GLU A 1 1602 ? 210.439 216.649 181.735 1.00 28.04 ? 1602 GLU A CD    1 
ATOM   1220  O  OE1   . GLU A 1 1602 ? 210.918 217.402 180.858 1.00 31.37 ? 1602 GLU A OE1   1 
ATOM   1221  O  OE2   . GLU A 1 1602 ? 211.143 216.039 182.567 1.00 26.19 ? 1602 GLU A OE2   1 
ATOM   1222  N  N     . ARG A 1 1603 ? 205.820 218.784 182.140 1.00 6.55  ? 1603 ARG A N     1 
ATOM   1223  C  CA    . ARG A 1 1603 ? 205.153 219.279 183.338 1.00 10.71 ? 1603 ARG A CA    1 
ATOM   1224  C  C     . ARG A 1 1603 ? 203.682 218.878 183.354 1.00 11.16 ? 1603 ARG A C     1 
ATOM   1225  O  O     . ARG A 1 1603 ? 203.140 218.531 184.410 1.00 12.27 ? 1603 ARG A O     1 
ATOM   1226  C  CB    . ARG A 1 1603 ? 205.293 220.798 183.433 1.00 11.13 ? 1603 ARG A CB    1 
ATOM   1227  C  CG    . ARG A 1 1603 ? 204.607 221.388 184.649 1.00 12.89 ? 1603 ARG A CG    1 
ATOM   1228  C  CD    . ARG A 1 1603 ? 204.980 222.838 184.861 1.00 14.15 ? 1603 ARG A CD    1 
ATOM   1229  N  NE    . ARG A 1 1603 ? 203.816 223.645 185.208 1.00 20.57 ? 1603 ARG A NE    1 
ATOM   1230  C  CZ    . ARG A 1 1603 ? 203.033 224.251 184.327 1.00 16.67 ? 1603 ARG A CZ    1 
ATOM   1231  N  NH1   . ARG A 1 1603 ? 203.248 224.154 183.026 1.00 13.24 ? 1603 ARG A NH1   1 
ATOM   1232  N  NH2   . ARG A 1 1603 ? 202.006 224.974 184.764 1.00 16.85 ? 1603 ARG A NH2   1 
ATOM   1233  N  N     . LEU A 1 1604 ? 203.021 218.920 182.193 1.00 8.80  ? 1604 LEU A N     1 
ATOM   1234  C  CA    . LEU A 1 1604 ? 201.621 218.514 182.123 1.00 8.05  ? 1604 LEU A CA    1 
ATOM   1235  C  C     . LEU A 1 1604 ? 201.455 217.048 182.500 1.00 7.46  ? 1604 LEU A C     1 
ATOM   1236  O  O     . LEU A 1 1604 ? 200.515 216.687 183.216 1.00 10.07 ? 1604 LEU A O     1 
ATOM   1237  C  CB    . LEU A 1 1604 ? 201.065 218.768 180.722 1.00 7.90  ? 1604 LEU A CB    1 
ATOM   1238  C  CG    . LEU A 1 1604 ? 200.782 220.213 180.305 1.00 6.14  ? 1604 LEU A CG    1 
ATOM   1239  C  CD1   . LEU A 1 1604 ? 200.206 220.266 178.903 1.00 6.44  ? 1604 LEU A CD1   1 
ATOM   1240  C  CD2   . LEU A 1 1604 ? 199.860 220.902 181.286 1.00 8.77  ? 1604 LEU A CD2   1 
ATOM   1241  N  N     . ALA A 1 1605 ? 202.355 216.187 182.023 1.00 7.02  ? 1605 ALA A N     1 
ATOM   1242  C  CA    . ALA A 1 1605 ? 202.274 214.768 182.357 1.00 4.96  ? 1605 ALA A CA    1 
ATOM   1243  C  C     . ALA A 1 1605 ? 202.444 214.543 183.854 1.00 9.01  ? 1605 ALA A C     1 
ATOM   1244  O  O     . ALA A 1 1605 ? 201.681 213.792 184.471 1.00 11.78 ? 1605 ALA A O     1 
ATOM   1245  C  CB    . ALA A 1 1605 ? 203.327 213.986 181.571 1.00 3.33  ? 1605 ALA A CB    1 
ATOM   1246  N  N     . ASP A 1 1606 ? 203.443 215.194 184.455 1.00 9.93  ? 1606 ASP A N     1 
ATOM   1247  C  CA    . ASP A 1 1606 ? 203.670 215.031 185.887 1.00 8.31  ? 1606 ASP A CA    1 
ATOM   1248  C  C     . ASP A 1 1606 ? 202.517 215.604 186.702 1.00 10.08 ? 1606 ASP A C     1 
ATOM   1249  O  O     . ASP A 1 1606 ? 202.054 214.980 187.664 1.00 8.68  ? 1606 ASP A O     1 
ATOM   1250  C  CB    . ASP A 1 1606 ? 204.989 215.694 186.283 1.00 14.13 ? 1606 ASP A CB    1 
ATOM   1251  C  CG    . ASP A 1 1606 ? 205.194 215.730 187.785 1.00 26.68 ? 1606 ASP A CG    1 
ATOM   1252  O  OD1   . ASP A 1 1606 ? 205.315 214.648 188.396 1.00 20.89 ? 1606 ASP A OD1   1 
ATOM   1253  O  OD2   . ASP A 1 1606 ? 205.227 216.842 188.353 1.00 27.39 ? 1606 ASP A OD2   1 
ATOM   1254  N  N     . LEU A 1 1607 ? 202.040 216.793 186.328 1.00 9.15  ? 1607 LEU A N     1 
ATOM   1255  C  CA    . LEU A 1 1607 ? 200.966 217.432 187.079 1.00 6.26  ? 1607 LEU A CA    1 
ATOM   1256  C  C     . LEU A 1 1607 ? 199.664 216.645 186.980 1.00 8.87  ? 1607 LEU A C     1 
ATOM   1257  O  O     . LEU A 1 1607 ? 198.949 216.491 187.977 1.00 14.20 ? 1607 LEU A O     1 
ATOM   1258  C  CB    . LEU A 1 1607 ? 200.768 218.863 186.588 1.00 9.42  ? 1607 LEU A CB    1 
ATOM   1259  C  CG    . LEU A 1 1607 ? 201.783 219.923 187.018 1.00 13.56 ? 1607 LEU A CG    1 
ATOM   1260  C  CD1   . LEU A 1 1607 ? 201.296 221.300 186.599 1.00 11.09 ? 1607 LEU A CD1   1 
ATOM   1261  C  CD2   . LEU A 1 1607 ? 202.033 219.868 188.518 1.00 7.28  ? 1607 LEU A CD2   1 
ATOM   1262  N  N     . LEU A 1 1608 ? 199.332 216.149 185.784 1.00 8.79  ? 1608 LEU A N     1 
ATOM   1263  C  CA    . LEU A 1 1608 ? 198.114 215.358 185.630 1.00 5.20  ? 1608 LEU A CA    1 
ATOM   1264  C  C     . LEU A 1 1608 ? 198.200 214.046 186.396 1.00 7.48  ? 1608 LEU A C     1 
ATOM   1265  O  O     . LEU A 1 1608 ? 197.178 213.533 186.867 1.00 10.05 ? 1608 LEU A O     1 
ATOM   1266  C  CB    . LEU A 1 1608 ? 197.840 215.091 184.151 1.00 4.50  ? 1608 LEU A CB    1 
ATOM   1267  C  CG    . LEU A 1 1608 ? 197.255 216.243 183.332 1.00 4.15  ? 1608 LEU A CG    1 
ATOM   1268  C  CD1   . LEU A 1 1608 ? 197.353 215.943 181.844 1.00 2.84  ? 1608 LEU A CD1   1 
ATOM   1269  C  CD2   . LEU A 1 1608 ? 195.819 216.531 183.731 1.00 2.23  ? 1608 LEU A CD2   1 
ATOM   1270  N  N     . GLY A 1 1609 ? 199.403 213.486 186.529 1.00 6.18  ? 1609 GLY A N     1 
ATOM   1271  C  CA    . GLY A 1 1609 ? 199.569 212.288 187.331 1.00 6.39  ? 1609 GLY A CA    1 
ATOM   1272  C  C     . GLY A 1 1609 ? 199.295 212.516 188.803 1.00 12.73 ? 1609 GLY A C     1 
ATOM   1273  O  O     . GLY A 1 1609 ? 198.751 211.638 189.478 1.00 14.08 ? 1609 GLY A O     1 
ATOM   1274  N  N     . LYS A 1 1610 ? 199.671 213.685 189.323 1.00 13.97 ? 1610 LYS A N     1 
ATOM   1275  C  CA    . LYS A 1 1610 ? 199.398 213.997 190.722 1.00 11.36 ? 1610 LYS A CA    1 
ATOM   1276  C  C     . LYS A 1 1610 ? 197.902 214.105 190.983 1.00 11.53 ? 1610 LYS A C     1 
ATOM   1277  O  O     . LYS A 1 1610 ? 197.410 213.628 192.012 1.00 17.33 ? 1610 LYS A O     1 
ATOM   1278  C  CB    . LYS A 1 1610 ? 200.109 215.291 191.118 1.00 12.18 ? 1610 LYS A CB    1 
ATOM   1279  C  CG    . LYS A 1 1610 ? 201.618 215.237 190.976 1.00 12.37 ? 1610 LYS A CG    1 
ATOM   1280  C  CD    . LYS A 1 1610 ? 202.222 214.239 191.946 1.00 21.43 ? 1610 LYS A CD    1 
ATOM   1281  C  CE    . LYS A 1 1610 ? 203.740 214.300 191.930 1.00 26.49 ? 1610 LYS A CE    1 
ATOM   1282  N  NZ    . LYS A 1 1610 ? 204.302 213.793 190.651 1.00 25.01 ? 1610 LYS A NZ    1 
ATOM   1283  N  N     . ILE A 1 1611 ? 197.163 214.732 190.065 1.00 10.18 ? 1611 ILE A N     1 
ATOM   1284  C  CA    . ILE A 1 1611 ? 195.709 214.794 190.190 1.00 10.40 ? 1611 ILE A CA    1 
ATOM   1285  C  C     . ILE A 1 1611 ? 195.114 213.395 190.156 1.00 9.35  ? 1611 ILE A C     1 
ATOM   1286  O  O     . ILE A 1 1611 ? 194.174 213.085 190.898 1.00 16.46 ? 1611 ILE A O     1 
ATOM   1287  C  CB    . ILE A 1 1611 ? 195.118 215.684 189.083 1.00 8.32  ? 1611 ILE A CB    1 
ATOM   1288  C  CG1   . ILE A 1 1611 ? 195.619 217.115 189.232 1.00 8.55  ? 1611 ILE A CG1   1 
ATOM   1289  C  CG2   . ILE A 1 1611 ? 193.603 215.637 189.102 1.00 6.36  ? 1611 ILE A CG2   1 
ATOM   1290  C  CD1   . ILE A 1 1611 ? 195.291 217.965 188.053 1.00 11.94 ? 1611 ILE A CD1   1 
ATOM   1291  N  N     . GLN A 1 1612 ? 195.648 212.533 189.292 1.00 10.68 ? 1612 GLN A N     1 
ATOM   1292  C  CA    . GLN A 1 1612 ? 195.159 211.163 189.200 1.00 9.77  ? 1612 GLN A CA    1 
ATOM   1293  C  C     . GLN A 1 1612 ? 195.327 210.420 190.521 1.00 11.40 ? 1612 GLN A C     1 
ATOM   1294  O  O     . GLN A 1 1612 ? 194.415 209.717 190.966 1.00 15.52 ? 1612 GLN A O     1 
ATOM   1295  C  CB    . GLN A 1 1612 ? 195.889 210.439 188.074 1.00 9.54  ? 1612 GLN A CB    1 
ATOM   1296  C  CG    . GLN A 1 1612 ? 195.415 209.035 187.820 1.00 8.53  ? 1612 GLN A CG    1 
ATOM   1297  C  CD    . GLN A 1 1612 ? 196.134 208.396 186.660 1.00 9.42  ? 1612 GLN A CD    1 
ATOM   1298  O  OE1   . GLN A 1 1612 ? 197.023 208.996 186.058 1.00 14.71 ? 1612 GLN A OE1   1 
ATOM   1299  N  NE2   . GLN A 1 1612 ? 195.764 207.166 186.343 1.00 14.91 ? 1612 GLN A NE2   1 
ATOM   1300  N  N     . LYS A 1 1613 ? 196.483 210.574 191.167 1.00 11.65 ? 1613 LYS A N     1 
ATOM   1301  C  CA    . LYS A 1 1613 ? 196.739 209.895 192.430 1.00 9.94  ? 1613 LYS A CA    1 
ATOM   1302  C  C     . LYS A 1 1613 ? 195.990 210.516 193.600 1.00 12.63 ? 1613 LYS A C     1 
ATOM   1303  O  O     . LYS A 1 1613 ? 195.959 209.919 194.681 1.00 16.66 ? 1613 LYS A O     1 
ATOM   1304  C  CB    . LYS A 1 1613 ? 198.241 209.889 192.726 1.00 13.07 ? 1613 LYS A CB    1 
ATOM   1305  C  CG    . LYS A 1 1613 ? 199.087 209.302 191.611 1.00 14.05 ? 1613 LYS A CG    1 
ATOM   1306  C  CD    . LYS A 1 1613 ? 199.066 207.785 191.624 1.00 16.40 ? 1613 LYS A CD    1 
ATOM   1307  C  CE    . LYS A 1 1613 ? 199.900 207.216 190.486 1.00 17.64 ? 1613 LYS A CE    1 
ATOM   1308  N  NZ    . LYS A 1 1613 ? 199.974 208.152 189.328 1.00 15.29 ? 1613 LYS A NZ    1 
ATOM   1309  N  N     . ALA A 1 1614 ? 195.394 211.691 193.413 1.00 12.94 ? 1614 ALA A N     1 
ATOM   1310  C  CA    . ALA A 1 1614 ? 194.651 212.370 194.464 1.00 10.97 ? 1614 ALA A CA    1 
ATOM   1311  C  C     . ALA A 1 1614 ? 193.156 212.094 194.413 1.00 12.36 ? 1614 ALA A C     1 
ATOM   1312  O  O     . ALA A 1 1614 ? 192.416 212.615 195.252 1.00 13.63 ? 1614 ALA A O     1 
ATOM   1313  C  CB    . ALA A 1 1614 ? 194.902 213.877 194.389 1.00 12.92 ? 1614 ALA A CB    1 
ATOM   1314  N  N     . LEU A 1 1615 ? 192.693 211.291 193.457 1.00 11.34 ? 1615 LEU A N     1 
ATOM   1315  C  CA    . LEU A 1 1615 ? 191.282 210.958 193.325 1.00 8.71  ? 1615 LEU A CA    1 
ATOM   1316  C  C     . LEU A 1 1615 ? 190.945 209.593 193.910 1.00 8.65  ? 1615 LEU A C     1 
ATOM   1317  O  O     . LEU A 1 1615 ? 189.859 209.070 193.647 1.00 9.68  ? 1615 LEU A O     1 
ATOM   1318  C  CB    . LEU A 1 1615 ? 190.863 211.009 191.854 1.00 9.02  ? 1615 LEU A CB    1 
ATOM   1319  C  CG    . LEU A 1 1615 ? 190.974 212.356 191.137 1.00 9.65  ? 1615 LEU A CG    1 
ATOM   1320  C  CD1   . LEU A 1 1615 ? 190.125 212.367 189.877 1.00 8.91  ? 1615 LEU A CD1   1 
ATOM   1321  C  CD2   . LEU A 1 1615 ? 190.575 213.496 192.057 1.00 11.47 ? 1615 LEU A CD2   1 
ATOM   1322  N  N     . GLY A 1 1616 ? 191.851 209.008 194.696 1.00 11.00 ? 1616 GLY A N     1 
ATOM   1323  C  CA    . GLY A 1 1616 ? 191.633 207.660 195.191 1.00 6.14  ? 1616 GLY A CA    1 
ATOM   1324  C  C     . GLY A 1 1616 ? 190.405 207.535 196.073 1.00 11.83 ? 1616 GLY A C     1 
ATOM   1325  O  O     . GLY A 1 1616 ? 189.628 206.587 195.938 1.00 13.80 ? 1616 GLY A O     1 
ATOM   1326  N  N     . GLU A 1 1617 ? 190.211 208.486 196.990 1.00 9.88  ? 1617 GLU A N     1 
ATOM   1327  C  CA    . GLU A 1 1617 ? 189.055 208.404 197.879 1.00 12.16 ? 1617 GLU A CA    1 
ATOM   1328  C  C     . GLU A 1 1617 ? 187.762 208.671 197.120 1.00 10.40 ? 1617 GLU A C     1 
ATOM   1329  O  O     . GLU A 1 1617 ? 186.710 208.123 197.466 1.00 12.97 ? 1617 GLU A O     1 
ATOM   1330  C  CB    . GLU A 1 1617 ? 189.215 209.370 199.056 1.00 11.19 ? 1617 GLU A CB    1 
ATOM   1331  C  CG    . GLU A 1 1617 ? 189.312 210.833 198.676 1.00 23.65 ? 1617 GLU A CG    1 
ATOM   1332  C  CD    . GLU A 1 1617 ? 187.950 211.481 198.528 1.00 28.80 ? 1617 GLU A CD    1 
ATOM   1333  O  OE1   . GLU A 1 1617 ? 186.965 210.933 199.065 1.00 22.01 ? 1617 GLU A OE1   1 
ATOM   1334  O  OE2   . GLU A 1 1617 ? 187.860 212.523 197.853 1.00 30.63 ? 1617 GLU A OE2   1 
ATOM   1335  N  N     . TYR A 1 1618 ? 187.818 209.518 196.090 1.00 8.73  ? 1618 TYR A N     1 
ATOM   1336  C  CA    . TYR A 1 1618 ? 186.646 209.728 195.248 1.00 11.14 ? 1618 TYR A CA    1 
ATOM   1337  C  C     . TYR A 1 1618 ? 186.286 208.456 194.490 1.00 9.37  ? 1618 TYR A C     1 
ATOM   1338  O  O     . TYR A 1 1618 ? 185.102 208.147 194.309 1.00 9.99  ? 1618 TYR A O     1 
ATOM   1339  C  CB    . TYR A 1 1618 ? 186.896 210.884 194.276 1.00 6.90  ? 1618 TYR A CB    1 
ATOM   1340  C  CG    . TYR A 1 1618 ? 185.842 211.029 193.203 1.00 7.05  ? 1618 TYR A CG    1 
ATOM   1341  C  CD1   . TYR A 1 1618 ? 184.657 211.704 193.456 1.00 9.53  ? 1618 TYR A CD1   1 
ATOM   1342  C  CD2   . TYR A 1 1618 ? 186.033 210.494 191.935 1.00 8.56  ? 1618 TYR A CD2   1 
ATOM   1343  C  CE1   . TYR A 1 1618 ? 183.689 211.842 192.483 1.00 11.98 ? 1618 TYR A CE1   1 
ATOM   1344  C  CE2   . TYR A 1 1618 ? 185.070 210.625 190.954 1.00 10.95 ? 1618 TYR A CE2   1 
ATOM   1345  C  CZ    . TYR A 1 1618 ? 183.900 211.300 191.234 1.00 17.69 ? 1618 TYR A CZ    1 
ATOM   1346  O  OH    . TYR A 1 1618 ? 182.937 211.434 190.259 1.00 20.47 ? 1618 TYR A OH    1 
ATOM   1347  N  N     . LEU A 1 1619 ? 187.295 207.710 194.038 1.00 7.26  ? 1619 LEU A N     1 
ATOM   1348  C  CA    . LEU A 1 1619 ? 187.041 206.460 193.331 1.00 5.39  ? 1619 LEU A CA    1 
ATOM   1349  C  C     . LEU A 1 1619 ? 186.431 205.413 194.256 1.00 8.59  ? 1619 LEU A C     1 
ATOM   1350  O  O     . LEU A 1 1619 ? 185.570 204.633 193.835 1.00 12.23 ? 1619 LEU A O     1 
ATOM   1351  C  CB    . LEU A 1 1619 ? 188.334 205.941 192.710 1.00 5.37  ? 1619 LEU A CB    1 
ATOM   1352  C  CG    . LEU A 1 1619 ? 188.860 206.761 191.535 1.00 5.41  ? 1619 LEU A CG    1 
ATOM   1353  C  CD1   . LEU A 1 1619 ? 190.151 206.170 191.010 1.00 7.85  ? 1619 LEU A CD1   1 
ATOM   1354  C  CD2   . LEU A 1 1619 ? 187.818 206.855 190.434 1.00 3.74  ? 1619 LEU A CD2   1 
ATOM   1355  N  N     . GLU A 1 1620 ? 186.869 205.376 195.517 1.00 10.66 ? 1620 GLU A N     1 
ATOM   1356  C  CA    . GLU A 1 1620 ? 186.289 204.433 196.468 1.00 8.20  ? 1620 GLU A CA    1 
ATOM   1357  C  C     . GLU A 1 1620 ? 184.823 204.738 196.739 1.00 9.37  ? 1620 GLU A C     1 
ATOM   1358  O  O     . GLU A 1 1620 ? 184.054 203.835 197.084 1.00 17.73 ? 1620 GLU A O     1 
ATOM   1359  C  CB    . GLU A 1 1620 ? 187.087 204.445 197.773 1.00 8.22  ? 1620 GLU A CB    1 
ATOM   1360  C  CG    . GLU A 1 1620 ? 188.296 203.522 197.769 1.00 11.08 ? 1620 GLU A CG    1 
ATOM   1361  C  CD    . GLU A 1 1620 ? 187.920 202.058 197.620 1.00 16.73 ? 1620 GLU A CD    1 
ATOM   1362  O  OE1   . GLU A 1 1620 ? 187.346 201.488 198.569 1.00 14.17 ? 1620 GLU A OE1   1 
ATOM   1363  O  OE2   . GLU A 1 1620 ? 188.198 201.481 196.550 1.00 13.99 ? 1620 GLU A OE2   1 
ATOM   1364  N  N     . ARG A 1 1621 ? 184.417 206.000 196.589 1.00 5.92  ? 1621 ARG A N     1 
ATOM   1365  C  CA    . ARG A 1 1621 ? 183.014 206.349 196.776 1.00 7.99  ? 1621 ARG A CA    1 
ATOM   1366  C  C     . ARG A 1 1621 ? 182.168 205.898 195.592 1.00 10.96 ? 1621 ARG A C     1 
ATOM   1367  O  O     . ARG A 1 1621 ? 181.023 205.465 195.769 1.00 12.07 ? 1621 ARG A O     1 
ATOM   1368  C  CB    . ARG A 1 1621 ? 182.873 207.852 196.994 1.00 10.86 ? 1621 ARG A CB    1 
ATOM   1369  C  CG    . ARG A 1 1621 ? 181.567 208.265 197.647 1.00 12.45 ? 1621 ARG A CG    1 
ATOM   1370  C  CD    . ARG A 1 1621 ? 181.561 209.750 197.958 1.00 17.54 ? 1621 ARG A CD    1 
ATOM   1371  N  NE    . ARG A 1 1621 ? 181.833 210.551 196.771 1.00 19.51 ? 1621 ARG A NE    1 
ATOM   1372  C  CZ    . ARG A 1 1621 ? 180.899 211.024 195.957 1.00 28.20 ? 1621 ARG A CZ    1 
ATOM   1373  N  NH1   . ARG A 1 1621 ? 179.615 210.798 196.174 1.00 29.75 ? 1621 ARG A NH1   1 
ATOM   1374  N  NH2   . ARG A 1 1621 ? 181.264 211.743 194.899 1.00 24.97 ? 1621 ARG A NH2   1 
ATOM   1375  N  N     . GLU A 1 1622 ? 182.708 205.994 194.376 1.00 9.42  ? 1622 GLU A N     1 
ATOM   1376  C  CA    . GLU A 1 1622 ? 181.966 205.570 193.197 1.00 7.94  ? 1622 GLU A CA    1 
ATOM   1377  C  C     . GLU A 1 1622 ? 181.852 204.056 193.102 1.00 7.08  ? 1622 GLU A C     1 
ATOM   1378  O  O     . GLU A 1 1622 ? 180.908 203.557 192.480 1.00 8.88  ? 1622 GLU A O     1 
ATOM   1379  C  CB    . GLU A 1 1622 ? 182.627 206.124 191.932 1.00 9.64  ? 1622 GLU A CB    1 
ATOM   1380  C  CG    . GLU A 1 1622 ? 182.857 207.624 191.958 1.00 12.86 ? 1622 GLU A CG    1 
ATOM   1381  C  CD    . GLU A 1 1622 ? 181.643 208.409 191.500 1.00 21.05 ? 1622 GLU A CD    1 
ATOM   1382  O  OE1   . GLU A 1 1622 ? 181.222 208.235 190.337 1.00 23.33 ? 1622 GLU A OE1   1 
ATOM   1383  O  OE2   . GLU A 1 1622 ? 181.113 209.204 192.303 1.00 24.10 ? 1622 GLU A OE2   1 
ATOM   1384  N  N     . ARG A 1 1623 ? 182.787 203.318 193.705 1.00 5.47  ? 1623 ARG A N     1 
ATOM   1385  C  CA    . ARG A 1 1623 ? 182.737 201.862 193.644 1.00 4.57  ? 1623 ARG A CA    1 
ATOM   1386  C  C     . ARG A 1 1623 ? 181.505 201.311 194.352 1.00 7.04  ? 1623 ARG A C     1 
ATOM   1387  O  O     . ARG A 1 1623 ? 181.016 200.236 193.993 1.00 13.77 ? 1623 ARG A O     1 
ATOM   1388  C  CB    . ARG A 1 1623 ? 184.013 201.269 194.243 1.00 2.81  ? 1623 ARG A CB    1 
ATOM   1389  C  CG    . ARG A 1 1623 ? 185.200 201.269 193.291 1.00 2.95  ? 1623 ARG A CG    1 
ATOM   1390  C  CD    . ARG A 1 1623 ? 186.376 200.513 193.876 1.00 2.76  ? 1623 ARG A CD    1 
ATOM   1391  N  NE    . ARG A 1 1623 ? 187.655 201.148 193.570 1.00 7.80  ? 1623 ARG A NE    1 
ATOM   1392  C  CZ    . ARG A 1 1623 ? 188.299 201.033 192.418 1.00 5.90  ? 1623 ARG A CZ    1 
ATOM   1393  N  NH1   . ARG A 1 1623 ? 187.813 200.309 191.423 1.00 8.75  ? 1623 ARG A NH1   1 
ATOM   1394  N  NH2   . ARG A 1 1623 ? 189.464 201.652 192.261 1.00 3.39  ? 1623 ARG A NH2   1 
ATOM   1395  N  N     . SER A 1 1624 ? 180.994 202.028 195.352 1.00 5.92  ? 1624 SER A N     1 
ATOM   1396  C  CA    . SER A 1 1624 ? 179.770 201.596 196.022 1.00 6.62  ? 1624 SER A CA    1 
ATOM   1397  C  C     . SER A 1 1624 ? 178.566 201.681 195.092 1.00 8.39  ? 1624 SER A C     1 
ATOM   1398  O  O     . SER A 1 1624 ? 177.700 200.800 195.104 1.00 15.32 ? 1624 SER A O     1 
ATOM   1399  C  CB    . SER A 1 1624 ? 179.539 202.436 197.275 1.00 8.80  ? 1624 SER A CB    1 
ATOM   1400  O  OG    . SER A 1 1624 ? 180.577 202.235 198.218 1.00 20.17 ? 1624 SER A OG    1 
ATOM   1401  N  N     . SER A 1 1625 ? 178.497 202.734 194.273 1.00 8.23  ? 1625 SER A N     1 
ATOM   1402  C  CA    . SER A 1 1625 ? 177.342 202.939 193.406 1.00 7.20  ? 1625 SER A CA    1 
ATOM   1403  C  C     . SER A 1 1625 ? 177.228 201.877 192.321 1.00 9.41  ? 1625 SER A C     1 
ATOM   1404  O  O     . SER A 1 1625 ? 176.136 201.682 191.773 1.00 16.02 ? 1625 SER A O     1 
ATOM   1405  C  CB    . SER A 1 1625 ? 177.412 204.332 192.777 1.00 9.74  ? 1625 SER A CB    1 
ATOM   1406  O  OG    . SER A 1 1625 ? 178.463 204.412 191.830 1.00 16.69 ? 1625 SER A OG    1 
ATOM   1407  N  N     . PHE A 1 1626 ? 178.324 201.197 191.989 1.00 9.20  ? 1626 PHE A N     1 
ATOM   1408  C  CA    . PHE A 1 1626 ? 178.307 200.067 191.061 1.00 4.97  ? 1626 PHE A CA    1 
ATOM   1409  C  C     . PHE A 1 1626 ? 179.372 199.089 191.534 1.00 3.67  ? 1626 PHE A C     1 
ATOM   1410  O  O     . PHE A 1 1626 ? 180.544 199.191 191.152 1.00 2.61  ? 1626 PHE A O     1 
ATOM   1411  C  CB    . PHE A 1 1626 ? 178.550 200.516 189.620 1.00 2.87  ? 1626 PHE A CB    1 
ATOM   1412  C  CG    . PHE A 1 1626 ? 178.321 199.438 188.599 1.00 3.00  ? 1626 PHE A CG    1 
ATOM   1413  C  CD1   . PHE A 1 1626 ? 177.042 198.987 188.323 1.00 3.14  ? 1626 PHE A CD1   1 
ATOM   1414  C  CD2   . PHE A 1 1626 ? 179.385 198.887 187.905 1.00 3.57  ? 1626 PHE A CD2   1 
ATOM   1415  C  CE1   . PHE A 1 1626 ? 176.829 197.997 187.382 1.00 3.05  ? 1626 PHE A CE1   1 
ATOM   1416  C  CE2   . PHE A 1 1626 ? 179.180 197.899 186.962 1.00 2.72  ? 1626 PHE A CE2   1 
ATOM   1417  C  CZ    . PHE A 1 1626 ? 177.898 197.454 186.699 1.00 3.35  ? 1626 PHE A CZ    1 
ATOM   1418  N  N     . PRO A 1 1627 ? 178.996 198.119 192.373 1.00 4.42  ? 1627 PRO A N     1 
ATOM   1419  C  CA    . PRO A 1 1627 ? 180.009 197.322 193.088 1.00 3.28  ? 1627 PRO A CA    1 
ATOM   1420  C  C     . PRO A 1 1627 ? 180.920 196.498 192.195 1.00 2.11  ? 1627 PRO A C     1 
ATOM   1421  O  O     . PRO A 1 1627 ? 181.975 196.055 192.667 1.00 1.91  ? 1627 PRO A O     1 
ATOM   1422  C  CB    . PRO A 1 1627 ? 179.166 196.431 194.011 1.00 2.11  ? 1627 PRO A CB    1 
ATOM   1423  C  CG    . PRO A 1 1627 ? 177.798 196.437 193.420 1.00 3.67  ? 1627 PRO A CG    1 
ATOM   1424  C  CD    . PRO A 1 1627 ? 177.628 197.782 192.800 1.00 4.99  ? 1627 PRO A CD    1 
ATOM   1425  N  N     . ARG A 1 1628 ? 180.565 196.269 190.930 1.00 1.19  ? 1628 ARG A N     1 
ATOM   1426  C  CA    . ARG A 1 1628 ? 181.508 195.611 190.037 1.00 1.83  ? 1628 ARG A CA    1 
ATOM   1427  C  C     . ARG A 1 1628 ? 182.732 196.472 189.748 1.00 2.27  ? 1628 ARG A C     1 
ATOM   1428  O  O     . ARG A 1 1628 ? 183.718 195.953 189.216 1.00 1.78  ? 1628 ARG A O     1 
ATOM   1429  C  CB    . ARG A 1 1628 ? 180.818 195.214 188.731 1.00 1.99  ? 1628 ARG A CB    1 
ATOM   1430  C  CG    . ARG A 1 1628 ? 179.661 194.252 188.928 1.00 1.40  ? 1628 ARG A CG    1 
ATOM   1431  C  CD    . ARG A 1 1628 ? 179.002 193.881 187.618 1.00 1.88  ? 1628 ARG A CD    1 
ATOM   1432  N  NE    . ARG A 1 1628 ? 177.888 192.960 187.816 1.00 3.61  ? 1628 ARG A NE    1 
ATOM   1433  C  CZ    . ARG A 1 1628 ? 177.903 191.677 187.479 1.00 1.60  ? 1628 ARG A CZ    1 
ATOM   1434  N  NH1   . ARG A 1 1628 ? 178.973 191.118 186.936 1.00 2.65  ? 1628 ARG A NH1   1 
ATOM   1435  N  NH2   . ARG A 1 1628 ? 176.822 190.939 187.694 1.00 1.60  ? 1628 ARG A NH2   1 
ATOM   1436  N  N     . PHE A 1 1629 ? 182.693 197.763 190.091 1.00 2.35  ? 1629 PHE A N     1 
ATOM   1437  C  CA    . PHE A 1 1629 ? 183.880 198.604 190.007 1.00 1.76  ? 1629 PHE A CA    1 
ATOM   1438  C  C     . PHE A 1 1629 ? 184.936 198.220 191.035 1.00 1.09  ? 1629 PHE A C     1 
ATOM   1439  O  O     . PHE A 1 1629 ? 186.096 198.613 190.888 1.00 2.27  ? 1629 PHE A O     1 
ATOM   1440  C  CB    . PHE A 1 1629 ? 183.507 200.075 190.191 1.00 1.42  ? 1629 PHE A CB    1 
ATOM   1441  C  CG    . PHE A 1 1629 ? 182.807 200.678 189.010 1.00 0.84  ? 1629 PHE A CG    1 
ATOM   1442  C  CD1   . PHE A 1 1629 ? 182.972 200.148 187.742 1.00 1.09  ? 1629 PHE A CD1   1 
ATOM   1443  C  CD2   . PHE A 1 1629 ? 181.987 201.782 189.169 1.00 0.76  ? 1629 PHE A CD2   1 
ATOM   1444  C  CE1   . PHE A 1 1629 ? 182.327 200.707 186.657 1.00 1.43  ? 1629 PHE A CE1   1 
ATOM   1445  C  CE2   . PHE A 1 1629 ? 181.342 202.341 188.090 1.00 0.61  ? 1629 PHE A CE2   1 
ATOM   1446  C  CZ    . PHE A 1 1629 ? 181.512 201.806 186.833 1.00 1.63  ? 1629 PHE A CZ    1 
ATOM   1447  N  N     . TYR A 1 1630 ? 184.559 197.464 192.071 1.00 1.36  ? 1630 TYR A N     1 
ATOM   1448  C  CA    . TYR A 1 1630 ? 185.529 197.023 193.067 1.00 1.38  ? 1630 TYR A CA    1 
ATOM   1449  C  C     . TYR A 1 1630 ? 186.588 196.109 192.469 1.00 0.91  ? 1630 TYR A C     1 
ATOM   1450  O  O     . TYR A 1 1630 ? 187.648 195.925 193.075 1.00 0.89  ? 1630 TYR A O     1 
ATOM   1451  C  CB    . TYR A 1 1630 ? 184.823 196.309 194.220 1.00 0.68  ? 1630 TYR A CB    1 
ATOM   1452  C  CG    . TYR A 1 1630 ? 184.273 197.235 195.278 1.00 2.80  ? 1630 TYR A CG    1 
ATOM   1453  C  CD1   . TYR A 1 1630 ? 185.109 197.818 196.220 1.00 2.97  ? 1630 TYR A CD1   1 
ATOM   1454  C  CD2   . TYR A 1 1630 ? 182.917 197.522 195.340 1.00 4.03  ? 1630 TYR A CD2   1 
ATOM   1455  C  CE1   . TYR A 1 1630 ? 184.608 198.666 197.190 1.00 2.41  ? 1630 TYR A CE1   1 
ATOM   1456  C  CE2   . TYR A 1 1630 ? 182.408 198.367 196.301 1.00 3.27  ? 1630 TYR A CE2   1 
ATOM   1457  C  CZ    . TYR A 1 1630 ? 183.258 198.938 197.224 1.00 3.33  ? 1630 TYR A CZ    1 
ATOM   1458  O  OH    . TYR A 1 1630 ? 182.752 199.779 198.184 1.00 11.13 ? 1630 TYR A OH    1 
ATOM   1459  N  N     . PHE A 1 1631 ? 186.323 195.535 191.300 1.00 1.56  ? 1631 PHE A N     1 
ATOM   1460  C  CA    . PHE A 1 1631 ? 187.255 194.646 190.626 1.00 1.47  ? 1631 PHE A CA    1 
ATOM   1461  C  C     . PHE A 1 1631 ? 187.978 195.339 189.479 1.00 1.52  ? 1631 PHE A C     1 
ATOM   1462  O  O     . PHE A 1 1631 ? 188.502 194.670 188.585 1.00 5.97  ? 1631 PHE A O     1 
ATOM   1463  C  CB    . PHE A 1 1631 ? 186.513 193.403 190.142 1.00 2.03  ? 1631 PHE A CB    1 
ATOM   1464  C  CG    . PHE A 1 1631 ? 185.701 192.742 191.216 1.00 1.20  ? 1631 PHE A CG    1 
ATOM   1465  C  CD1   . PHE A 1 1631 ? 186.268 192.445 192.445 1.00 0.82  ? 1631 PHE A CD1   1 
ATOM   1466  C  CD2   . PHE A 1 1631 ? 184.365 192.447 191.012 1.00 1.70  ? 1631 PHE A CD2   1 
ATOM   1467  C  CE1   . PHE A 1 1631 ? 185.524 191.849 193.443 1.00 0.65  ? 1631 PHE A CE1   1 
ATOM   1468  C  CE2   . PHE A 1 1631 ? 183.613 191.851 192.006 1.00 1.45  ? 1631 PHE A CE2   1 
ATOM   1469  C  CZ    . PHE A 1 1631 ? 184.193 191.553 193.223 1.00 1.09  ? 1631 PHE A CZ    1 
ATOM   1470  N  N     . VAL A 1 1632 ? 188.017 196.667 189.499 1.00 1.98  ? 1632 VAL A N     1 
ATOM   1471  C  CA    . VAL A 1 1632 ? 188.674 197.477 188.482 1.00 2.31  ? 1632 VAL A CA    1 
ATOM   1472  C  C     . VAL A 1 1632 ? 189.717 198.346 189.167 1.00 1.71  ? 1632 VAL A C     1 
ATOM   1473  O  O     . VAL A 1 1632 ? 189.474 198.884 190.250 1.00 1.90  ? 1632 VAL A O     1 
ATOM   1474  C  CB    . VAL A 1 1632 ? 187.658 198.346 187.710 1.00 1.65  ? 1632 VAL A CB    1 
ATOM   1475  C  CG1   . VAL A 1 1632 ? 188.342 199.112 186.604 1.00 1.02  ? 1632 VAL A CG1   1 
ATOM   1476  C  CG2   . VAL A 1 1632 ? 186.537 197.491 187.152 1.00 1.59  ? 1632 VAL A CG2   1 
ATOM   1477  N  N     . GLY A 1 1633 ? 190.883 198.473 188.537 1.00 3.57  ? 1633 GLY A N     1 
ATOM   1478  C  CA    . GLY A 1 1633 ? 191.915 199.333 189.074 1.00 5.45  ? 1633 GLY A CA    1 
ATOM   1479  C  C     . GLY A 1 1633 ? 191.528 200.797 189.024 1.00 2.30  ? 1633 GLY A C     1 
ATOM   1480  O  O     . GLY A 1 1633 ? 190.583 201.203 188.346 1.00 1.39  ? 1633 GLY A O     1 
ATOM   1481  N  N     . ASP A 1 1634 ? 192.284 201.606 189.769 1.00 3.65  ? 1634 ASP A N     1 
ATOM   1482  C  CA    . ASP A 1 1634 ? 191.964 203.026 189.888 1.00 3.37  ? 1634 ASP A CA    1 
ATOM   1483  C  C     . ASP A 1 1634 ? 192.055 203.736 188.542 1.00 4.69  ? 1634 ASP A C     1 
ATOM   1484  O  O     . ASP A 1 1634 ? 191.169 204.517 188.181 1.00 3.87  ? 1634 ASP A O     1 
ATOM   1485  C  CB    . ASP A 1 1634 ? 192.888 203.688 190.908 1.00 3.64  ? 1634 ASP A CB    1 
ATOM   1486  C  CG    . ASP A 1 1634 ? 192.412 203.498 192.331 1.00 11.18 ? 1634 ASP A CG    1 
ATOM   1487  O  OD1   . ASP A 1 1634 ? 191.185 203.494 192.545 1.00 15.70 ? 1634 ASP A OD1   1 
ATOM   1488  O  OD2   . ASP A 1 1634 ? 193.262 203.356 193.234 1.00 18.07 ? 1634 ASP A OD2   1 
ATOM   1489  N  N     . GLU A 1 1635 ? 193.122 203.476 187.784 1.00 3.18  ? 1635 GLU A N     1 
ATOM   1490  C  CA    . GLU A 1 1635 ? 193.296 204.156 186.503 1.00 5.96  ? 1635 GLU A CA    1 
ATOM   1491  C  C     . GLU A 1 1635 ? 192.220 203.745 185.507 1.00 5.22  ? 1635 GLU A C     1 
ATOM   1492  O  O     . GLU A 1 1635 ? 191.678 204.590 184.785 1.00 7.73  ? 1635 GLU A O     1 
ATOM   1493  C  CB    . GLU A 1 1635 ? 194.688 203.878 185.937 1.00 14.55 ? 1635 GLU A CB    1 
ATOM   1494  C  CG    . GLU A 1 1635 ? 194.979 204.619 184.640 1.00 13.84 ? 1635 GLU A CG    1 
ATOM   1495  C  CD    . GLU A 1 1635 ? 196.382 204.370 184.125 1.00 25.41 ? 1635 GLU A CD    1 
ATOM   1496  O  OE1   . GLU A 1 1635 ? 197.128 203.600 184.766 1.00 32.31 ? 1635 GLU A OE1   1 
ATOM   1497  O  OE2   . GLU A 1 1635 ? 196.744 204.959 183.084 1.00 25.20 ? 1635 GLU A OE2   1 
ATOM   1498  N  N     . ASP A 1 1636 ? 191.898 202.453 185.454 1.00 5.40  ? 1636 ASP A N     1 
ATOM   1499  C  CA    . ASP A 1 1636 ? 190.847 201.994 184.553 1.00 5.52  ? 1636 ASP A CA    1 
ATOM   1500  C  C     . ASP A 1 1636 ? 189.491 202.553 184.961 1.00 3.14  ? 1636 ASP A C     1 
ATOM   1501  O  O     . ASP A 1 1636 ? 188.655 202.856 184.100 1.00 2.07  ? 1636 ASP A O     1 
ATOM   1502  C  CB    . ASP A 1 1636 ? 190.814 200.467 184.521 1.00 5.73  ? 1636 ASP A CB    1 
ATOM   1503  C  CG    . ASP A 1 1636 ? 192.030 199.872 183.849 1.00 13.75 ? 1636 ASP A CG    1 
ATOM   1504  O  OD1   . ASP A 1 1636 ? 192.605 200.531 182.957 1.00 18.09 ? 1636 ASP A OD1   1 
ATOM   1505  O  OD2   . ASP A 1 1636 ? 192.405 198.738 184.205 1.00 17.31 ? 1636 ASP A OD2   1 
ATOM   1506  N  N     . LEU A 1 1637 ? 189.248 202.680 186.267 1.00 2.06  ? 1637 LEU A N     1 
ATOM   1507  C  CA    . LEU A 1 1637 ? 187.991 203.254 186.736 1.00 1.98  ? 1637 LEU A CA    1 
ATOM   1508  C  C     . LEU A 1 1637 ? 187.862 204.717 186.327 1.00 2.75  ? 1637 LEU A C     1 
ATOM   1509  O  O     . LEU A 1 1637 ? 186.780 205.163 185.934 1.00 1.70  ? 1637 LEU A O     1 
ATOM   1510  C  CB    . LEU A 1 1637 ? 187.876 203.103 188.253 1.00 4.17  ? 1637 LEU A CB    1 
ATOM   1511  C  CG    . LEU A 1 1637 ? 186.564 203.581 188.881 1.00 1.77  ? 1637 LEU A CG    1 
ATOM   1512  C  CD1   . LEU A 1 1637 ? 185.368 202.963 188.178 1.00 0.61  ? 1637 LEU A CD1   1 
ATOM   1513  C  CD2   . LEU A 1 1637 ? 186.534 203.276 190.369 1.00 1.72  ? 1637 LEU A CD2   1 
ATOM   1514  N  N     . LEU A 1 1638 ? 188.956 205.479 186.415 1.00 4.51  ? 1638 LEU A N     1 
ATOM   1515  C  CA    . LEU A 1 1638 ? 188.932 206.864 185.954 1.00 2.73  ? 1638 LEU A CA    1 
ATOM   1516  C  C     . LEU A 1 1638 ? 188.622 206.939 184.466 1.00 2.75  ? 1638 LEU A C     1 
ATOM   1517  O  O     . LEU A 1 1638 ? 187.893 207.831 184.018 1.00 5.09  ? 1638 LEU A O     1 
ATOM   1518  C  CB    . LEU A 1 1638 ? 190.264 207.549 186.252 1.00 3.36  ? 1638 LEU A CB    1 
ATOM   1519  C  CG    . LEU A 1 1638 ? 190.673 207.705 187.715 1.00 4.20  ? 1638 LEU A CG    1 
ATOM   1520  C  CD1   . LEU A 1 1638 ? 192.175 207.601 187.843 1.00 4.72  ? 1638 LEU A CD1   1 
ATOM   1521  C  CD2   . LEU A 1 1638 ? 190.182 209.018 188.285 1.00 4.11  ? 1638 LEU A CD2   1 
ATOM   1522  N  N     . GLU A 1 1639 ? 189.175 206.012 183.682 1.00 2.13  ? 1639 GLU A N     1 
ATOM   1523  C  CA    . GLU A 1 1639 ? 188.840 205.948 182.266 1.00 3.25  ? 1639 GLU A CA    1 
ATOM   1524  C  C     . GLU A 1 1639 ? 187.361 205.637 182.067 1.00 4.68  ? 1639 GLU A C     1 
ATOM   1525  O  O     . GLU A 1 1639 ? 186.717 206.203 181.179 1.00 11.54 ? 1639 GLU A O     1 
ATOM   1526  C  CB    . GLU A 1 1639 ? 189.713 204.905 181.569 1.00 4.78  ? 1639 GLU A CB    1 
ATOM   1527  C  CG    . GLU A 1 1639 ? 189.497 204.812 180.069 1.00 12.64 ? 1639 GLU A CG    1 
ATOM   1528  C  CD    . GLU A 1 1639 ? 190.415 203.804 179.408 1.00 19.57 ? 1639 GLU A CD    1 
ATOM   1529  O  OE1   . GLU A 1 1639 ? 191.209 203.161 180.126 1.00 18.20 ? 1639 GLU A OE1   1 
ATOM   1530  O  OE2   . GLU A 1 1639 ? 190.337 203.651 178.173 1.00 18.93 ? 1639 GLU A OE2   1 
ATOM   1531  N  N     . ILE A 1 1640 ? 186.805 204.742 182.888 1.00 3.72  ? 1640 ILE A N     1 
ATOM   1532  C  CA    . ILE A 1 1640 ? 185.385 204.411 182.789 1.00 3.65  ? 1640 ILE A CA    1 
ATOM   1533  C  C     . ILE A 1 1640 ? 184.523 205.610 183.167 1.00 3.97  ? 1640 ILE A C     1 
ATOM   1534  O  O     . ILE A 1 1640 ? 183.585 205.969 182.447 1.00 5.97  ? 1640 ILE A O     1 
ATOM   1535  C  CB    . ILE A 1 1640 ? 185.061 203.181 183.657 1.00 5.39  ? 1640 ILE A CB    1 
ATOM   1536  C  CG1   . ILE A 1 1640 ? 185.734 201.928 183.091 1.00 2.93  ? 1640 ILE A CG1   1 
ATOM   1537  C  CG2   . ILE A 1 1640 ? 183.555 202.999 183.814 1.00 1.90  ? 1640 ILE A CG2   1 
ATOM   1538  C  CD1   . ILE A 1 1640 ? 185.952 200.833 184.113 1.00 1.08  ? 1640 ILE A CD1   1 
ATOM   1539  N  N     . ILE A 1 1641 ? 184.824 206.245 184.301 1.00 3.51  ? 1641 ILE A N     1 
ATOM   1540  C  CA    . ILE A 1 1641 ? 184.010 207.365 184.765 1.00 2.54  ? 1641 ILE A CA    1 
ATOM   1541  C  C     . ILE A 1 1641 ? 184.172 208.565 183.839 1.00 5.13  ? 1641 ILE A C     1 
ATOM   1542  O  O     . ILE A 1 1641 ? 183.188 209.195 183.433 1.00 3.33  ? 1641 ILE A O     1 
ATOM   1543  C  CB    . ILE A 1 1641 ? 184.369 207.728 186.218 1.00 4.04  ? 1641 ILE A CB    1 
ATOM   1544  C  CG1   . ILE A 1 1641 ? 184.228 206.513 187.138 1.00 3.74  ? 1641 ILE A CG1   1 
ATOM   1545  C  CG2   . ILE A 1 1641 ? 183.508 208.880 186.712 1.00 4.88  ? 1641 ILE A CG2   1 
ATOM   1546  C  CD1   . ILE A 1 1641 ? 182.871 205.875 187.113 1.00 4.94  ? 1641 ILE A CD1   1 
ATOM   1547  N  N     . GLY A 1 1642 ? 185.416 208.895 183.491 1.00 7.67  ? 1642 GLY A N     1 
ATOM   1548  C  CA    . GLY A 1 1642 ? 185.672 210.100 182.723 1.00 3.62  ? 1642 GLY A CA    1 
ATOM   1549  C  C     . GLY A 1 1642 ? 185.218 210.019 181.281 1.00 7.85  ? 1642 GLY A C     1 
ATOM   1550  O  O     . GLY A 1 1642 ? 184.896 211.043 180.673 1.00 12.58 ? 1642 GLY A O     1 
ATOM   1551  N  N     . ASN A 1 1643 ? 185.186 208.816 180.712 1.00 6.65  ? 1643 ASN A N     1 
ATOM   1552  C  CA    . ASN A 1 1643 ? 184.753 208.614 179.332 1.00 9.79  ? 1643 ASN A CA    1 
ATOM   1553  C  C     . ASN A 1 1643 ? 183.312 208.139 179.256 1.00 10.55 ? 1643 ASN A C     1 
ATOM   1554  O  O     . ASN A 1 1643 ? 182.944 207.391 178.348 1.00 13.27 ? 1643 ASN A O     1 
ATOM   1555  C  CB    . ASN A 1 1643 ? 185.680 207.631 178.624 1.00 12.12 ? 1643 ASN A CB    1 
ATOM   1556  C  CG    . ASN A 1 1643 ? 186.951 208.285 178.130 1.00 10.98 ? 1643 ASN A CG    1 
ATOM   1557  O  OD1   . ASN A 1 1643 ? 188.042 208.002 178.622 1.00 12.44 ? 1643 ASN A OD1   1 
ATOM   1558  N  ND2   . ASN A 1 1643 ? 186.816 209.164 177.145 1.00 18.29 ? 1643 ASN A ND2   1 
ATOM   1559  N  N     . SER A 1 1644 ? 182.471 208.578 180.195 1.00 14.82 ? 1644 SER A N     1 
ATOM   1560  C  CA    . SER A 1 1644 ? 181.090 208.114 180.242 1.00 12.05 ? 1644 SER A CA    1 
ATOM   1561  C  C     . SER A 1 1644 ? 180.304 208.500 178.996 1.00 16.26 ? 1644 SER A C     1 
ATOM   1562  O  O     . SER A 1 1644 ? 179.261 207.895 178.725 1.00 21.91 ? 1644 SER A O     1 
ATOM   1563  C  CB    . SER A 1 1644 ? 180.399 208.657 181.493 1.00 12.01 ? 1644 SER A CB    1 
ATOM   1564  O  OG    . SER A 1 1644 ? 180.121 210.040 181.364 1.00 19.22 ? 1644 SER A OG    1 
ATOM   1565  N  N     . LYS A 1 1645 ? 180.774 209.488 178.235 1.00 14.40 ? 1645 LYS A N     1 
ATOM   1566  C  CA    . LYS A 1 1645 ? 180.143 209.845 176.969 1.00 14.27 ? 1645 LYS A CA    1 
ATOM   1567  C  C     . LYS A 1 1645 ? 180.758 209.097 175.789 1.00 22.83 ? 1645 LYS A C     1 
ATOM   1568  O  O     . LYS A 1 1645 ? 180.049 208.756 174.836 1.00 29.58 ? 1645 LYS A O     1 
ATOM   1569  C  CB    . LYS A 1 1645 ? 180.239 211.353 176.742 1.00 19.21 ? 1645 LYS A CB    1 
ATOM   1570  C  CG    . LYS A 1 1645 ? 179.557 212.184 177.819 1.00 20.33 ? 1645 LYS A CG    1 
ATOM   1571  C  CD    . LYS A 1 1645 ? 179.929 213.652 177.715 1.00 17.79 ? 1645 LYS A CD    1 
ATOM   1572  C  CE    . LYS A 1 1645 ? 179.699 214.180 176.310 1.00 25.61 ? 1645 LYS A CE    1 
ATOM   1573  N  NZ    . LYS A 1 1645 ? 179.990 215.637 176.206 1.00 29.00 ? 1645 LYS A NZ    1 
ATOM   1574  N  N     . ASN A 1 1646 ? 182.062 208.832 175.834 1.00 19.73 ? 1646 ASN A N     1 
ATOM   1575  C  CA    . ASN A 1 1646 ? 182.745 208.065 174.791 1.00 15.10 ? 1646 ASN A CA    1 
ATOM   1576  C  C     . ASN A 1 1646 ? 182.631 206.588 175.146 1.00 17.60 ? 1646 ASN A C     1 
ATOM   1577  O  O     . ASN A 1 1646 ? 183.516 206.005 175.770 1.00 20.75 ? 1646 ASN A O     1 
ATOM   1578  C  CB    . ASN A 1 1646 ? 184.198 208.506 174.661 1.00 21.20 ? 1646 ASN A CB    1 
ATOM   1579  C  CG    . ASN A 1 1646 ? 184.335 209.991 174.402 1.00 27.11 ? 1646 ASN A CG    1 
ATOM   1580  O  OD1   . ASN A 1 1646 ? 184.831 210.738 175.246 1.00 25.19 ? 1646 ASN A OD1   1 
ATOM   1581  N  ND2   . ASN A 1 1646 ? 183.896 210.431 173.227 1.00 26.94 ? 1646 ASN A ND2   1 
ATOM   1582  N  N     . VAL A 1 1647 ? 181.519 205.977 174.733 1.00 19.86 ? 1647 VAL A N     1 
ATOM   1583  C  CA    . VAL A 1 1647 ? 181.225 204.601 175.121 1.00 13.13 ? 1647 VAL A CA    1 
ATOM   1584  C  C     . VAL A 1 1647 ? 182.173 203.609 174.458 1.00 13.07 ? 1647 VAL A C     1 
ATOM   1585  O  O     . VAL A 1 1647 ? 182.426 202.528 175.004 1.00 15.31 ? 1647 VAL A O     1 
ATOM   1586  C  CB    . VAL A 1 1647 ? 179.758 204.270 174.801 1.00 11.75 ? 1647 VAL A CB    1 
ATOM   1587  C  CG1   . VAL A 1 1647 ? 178.829 205.078 175.689 1.00 12.19 ? 1647 VAL A CG1   1 
ATOM   1588  C  CG2   . VAL A 1 1647 ? 179.479 204.570 173.345 1.00 15.93 ? 1647 VAL A CG2   1 
ATOM   1589  N  N     . ALA A 1 1648 ? 182.701 203.938 173.275 1.00 11.60 ? 1648 ALA A N     1 
ATOM   1590  C  CA    . ALA A 1 1648 ? 183.581 203.005 172.577 1.00 12.94 ? 1648 ALA A CA    1 
ATOM   1591  C  C     . ALA A 1 1648 ? 184.829 202.689 173.390 1.00 16.00 ? 1648 ALA A C     1 
ATOM   1592  O  O     . ALA A 1 1648 ? 185.403 201.603 173.250 1.00 19.00 ? 1648 ALA A O     1 
ATOM   1593  C  CB    . ALA A 1 1648 ? 183.967 203.565 171.209 1.00 13.52 ? 1648 ALA A CB    1 
ATOM   1594  N  N     . LYS A 1 1649 ? 185.265 203.615 174.242 1.00 13.41 ? 1649 LYS A N     1 
ATOM   1595  C  CA    . LYS A 1 1649 ? 186.411 203.373 175.105 1.00 13.88 ? 1649 LYS A CA    1 
ATOM   1596  C  C     . LYS A 1 1649 ? 186.072 202.502 176.307 1.00 10.71 ? 1649 LYS A C     1 
ATOM   1597  O  O     . LYS A 1 1649 ? 186.989 202.043 176.997 1.00 11.86 ? 1649 LYS A O     1 
ATOM   1598  C  CB    . LYS A 1 1649 ? 186.998 204.706 175.574 1.00 13.62 ? 1649 LYS A CB    1 
ATOM   1599  C  CG    . LYS A 1 1649 ? 187.563 205.543 174.443 1.00 14.38 ? 1649 LYS A CG    1 
ATOM   1600  C  CD    . LYS A 1 1649 ? 187.964 206.926 174.912 1.00 16.17 ? 1649 LYS A CD    1 
ATOM   1601  C  CE    . LYS A 1 1649 ? 188.061 207.881 173.738 1.00 25.68 ? 1649 LYS A CE    1 
ATOM   1602  N  NZ    . LYS A 1 1649 ? 186.878 207.759 172.841 1.00 27.12 ? 1649 LYS A NZ    1 
ATOM   1603  N  N     . LEU A 1 1650 ? 184.791 202.259 176.566 1.00 10.51 ? 1650 LEU A N     1 
ATOM   1604  C  CA    . LEU A 1 1650 ? 184.360 201.419 177.674 1.00 6.58  ? 1650 LEU A CA    1 
ATOM   1605  C  C     . LEU A 1 1650 ? 184.441 199.936 177.364 1.00 8.48  ? 1650 LEU A C     1 
ATOM   1606  O  O     . LEU A 1 1650 ? 184.368 199.122 178.291 1.00 8.19  ? 1650 LEU A O     1 
ATOM   1607  C  CB    . LEU A 1 1650 ? 182.920 201.760 178.077 1.00 6.59  ? 1650 LEU A CB    1 
ATOM   1608  C  CG    . LEU A 1 1650 ? 182.671 202.938 179.017 1.00 7.91  ? 1650 LEU A CG    1 
ATOM   1609  C  CD1   . LEU A 1 1650 ? 183.306 202.639 180.350 1.00 6.09  ? 1650 LEU A CD1   1 
ATOM   1610  C  CD2   . LEU A 1 1650 ? 183.205 204.239 178.458 1.00 14.10 ? 1650 LEU A CD2   1 
ATOM   1611  N  N     . GLN A 1 1651 ? 184.605 199.567 176.091 1.00 7.64  ? 1651 GLN A N     1 
ATOM   1612  C  CA    . GLN A 1 1651 ? 184.465 198.170 175.697 1.00 6.14  ? 1651 GLN A CA    1 
ATOM   1613  C  C     . GLN A 1 1651 ? 185.542 197.297 176.330 1.00 6.91  ? 1651 GLN A C     1 
ATOM   1614  O  O     . GLN A 1 1651 ? 185.263 196.173 176.758 1.00 10.76 ? 1651 GLN A O     1 
ATOM   1615  C  CB    . GLN A 1 1651 ? 184.503 198.056 174.172 1.00 7.16  ? 1651 GLN A CB    1 
ATOM   1616  C  CG    . GLN A 1 1651 ? 183.367 198.780 173.446 1.00 6.59  ? 1651 GLN A CG    1 
ATOM   1617  C  CD    . GLN A 1 1651 ? 182.011 198.109 173.599 1.00 5.74  ? 1651 GLN A CD    1 
ATOM   1618  O  OE1   . GLN A 1 1651 ? 181.818 197.248 174.453 1.00 13.69 ? 1651 GLN A OE1   1 
ATOM   1619  N  NE2   . GLN A 1 1651 ? 181.064 198.501 172.758 1.00 5.31  ? 1651 GLN A NE2   1 
ATOM   1620  N  N     . LYS A 1 1652 ? 186.774 197.802 176.414 1.00 6.78  ? 1652 LYS A N     1 
ATOM   1621  C  CA    . LYS A 1 1652 ? 187.883 197.001 176.917 1.00 7.13  ? 1652 LYS A CA    1 
ATOM   1622  C  C     . LYS A 1 1652 ? 187.771 196.680 178.402 1.00 5.35  ? 1652 LYS A C     1 
ATOM   1623  O  O     . LYS A 1 1652 ? 188.512 195.818 178.885 1.00 6.97  ? 1652 LYS A O     1 
ATOM   1624  C  CB    . LYS A 1 1652 ? 189.212 197.716 176.661 1.00 6.19  ? 1652 LYS A CB    1 
ATOM   1625  C  CG    . LYS A 1 1652 ? 189.370 199.023 177.418 1.00 8.77  ? 1652 LYS A CG    1 
ATOM   1626  C  CD    . LYS A 1 1652 ? 190.716 199.671 177.146 1.00 11.74 ? 1652 LYS A CD    1 
ATOM   1627  C  CE    . LYS A 1 1652 ? 190.782 200.267 175.754 1.00 20.05 ? 1652 LYS A CE    1 
ATOM   1628  N  NZ    . LYS A 1 1652 ? 192.050 201.014 175.539 1.00 18.11 ? 1652 LYS A NZ    1 
ATOM   1629  N  N     . HIS A 1 1653 ? 186.879 197.342 179.138 1.00 5.13  ? 1653 HIS A N     1 
ATOM   1630  C  CA    . HIS A 1 1653 ? 186.799 197.169 180.582 1.00 4.34  ? 1653 HIS A CA    1 
ATOM   1631  C  C     . HIS A 1 1653 ? 185.702 196.213 181.029 1.00 3.56  ? 1653 HIS A C     1 
ATOM   1632  O  O     . HIS A 1 1653 ? 185.657 195.867 182.214 1.00 3.80  ? 1653 HIS A O     1 
ATOM   1633  C  CB    . HIS A 1 1653 ? 186.586 198.524 181.266 1.00 4.91  ? 1653 HIS A CB    1 
ATOM   1634  C  CG    . HIS A 1 1653 ? 187.636 199.537 180.938 1.00 4.92  ? 1653 HIS A CG    1 
ATOM   1635  N  ND1   . HIS A 1 1653 ? 188.946 199.406 181.340 1.00 6.02  ? 1653 HIS A ND1   1 
ATOM   1636  C  CD2   . HIS A 1 1653 ? 187.568 200.700 180.251 1.00 5.71  ? 1653 HIS A CD2   1 
ATOM   1637  C  CE1   . HIS A 1 1653 ? 189.641 200.444 180.913 1.00 5.35  ? 1653 HIS A CE1   1 
ATOM   1638  N  NE2   . HIS A 1 1653 ? 188.829 201.245 180.248 1.00 8.73  ? 1653 HIS A NE2   1 
ATOM   1639  N  N     . PHE A 1 1654 ? 184.825 195.775 180.123 1.00 4.04  ? 1654 PHE A N     1 
ATOM   1640  C  CA    . PHE A 1 1654 ? 183.706 194.934 180.535 1.00 2.77  ? 1654 PHE A CA    1 
ATOM   1641  C  C     . PHE A 1 1654 ? 184.160 193.549 180.978 1.00 3.66  ? 1654 PHE A C     1 
ATOM   1642  O  O     . PHE A 1 1654 ? 183.509 192.934 181.829 1.00 8.33  ? 1654 PHE A O     1 
ATOM   1643  C  CB    . PHE A 1 1654 ? 182.681 194.822 179.408 1.00 3.46  ? 1654 PHE A CB    1 
ATOM   1644  C  CG    . PHE A 1 1654 ? 181.889 196.077 179.187 1.00 3.61  ? 1654 PHE A CG    1 
ATOM   1645  C  CD1   . PHE A 1 1654 ? 180.908 196.458 180.085 1.00 3.00  ? 1654 PHE A CD1   1 
ATOM   1646  C  CD2   . PHE A 1 1654 ? 182.127 196.876 178.083 1.00 4.30  ? 1654 PHE A CD2   1 
ATOM   1647  C  CE1   . PHE A 1 1654 ? 180.180 197.612 179.887 1.00 2.45  ? 1654 PHE A CE1   1 
ATOM   1648  C  CE2   . PHE A 1 1654 ? 181.399 198.033 177.879 1.00 3.39  ? 1654 PHE A CE2   1 
ATOM   1649  C  CZ    . PHE A 1 1654 ? 180.425 198.402 178.783 1.00 2.44  ? 1654 PHE A CZ    1 
ATOM   1650  N  N     . LYS A 1 1655 ? 185.266 193.040 180.425 1.00 3.52  ? 1655 LYS A N     1 
ATOM   1651  C  CA    . LYS A 1 1655 ? 185.745 191.725 180.833 1.00 2.95  ? 1655 LYS A CA    1 
ATOM   1652  C  C     . LYS A 1 1655 ? 186.188 191.702 182.288 1.00 2.52  ? 1655 LYS A C     1 
ATOM   1653  O  O     . LYS A 1 1655 ? 186.250 190.626 182.890 1.00 5.09  ? 1655 LYS A O     1 
ATOM   1654  C  CB    . LYS A 1 1655 ? 186.899 191.265 179.937 1.00 3.81  ? 1655 LYS A CB    1 
ATOM   1655  C  CG    . LYS A 1 1655 ? 188.156 192.114 180.042 1.00 8.87  ? 1655 LYS A CG    1 
ATOM   1656  C  CD    . LYS A 1 1655 ? 189.268 191.584 179.146 1.00 5.37  ? 1655 LYS A CD    1 
ATOM   1657  C  CE    . LYS A 1 1655 ? 188.990 191.862 177.682 1.00 11.01 ? 1655 LYS A CE    1 
ATOM   1658  N  NZ    . LYS A 1 1655 ? 190.132 191.463 176.815 1.00 18.02 ? 1655 LYS A NZ    1 
ATOM   1659  N  N     . LYS A 1 1656 ? 186.503 192.861 182.862 1.00 3.17  ? 1656 LYS A N     1 
ATOM   1660  C  CA    . LYS A 1 1656 ? 186.903 192.938 184.259 1.00 4.11  ? 1656 LYS A CA    1 
ATOM   1661  C  C     . LYS A 1 1656 ? 185.716 192.986 185.209 1.00 4.18  ? 1656 LYS A C     1 
ATOM   1662  O  O     . LYS A 1 1656 ? 185.837 192.551 186.359 1.00 9.50  ? 1656 LYS A O     1 
ATOM   1663  C  CB    . LYS A 1 1656 ? 187.788 194.166 184.482 1.00 5.14  ? 1656 LYS A CB    1 
ATOM   1664  C  CG    . LYS A 1 1656 ? 188.781 194.408 183.364 1.00 4.47  ? 1656 LYS A CG    1 
ATOM   1665  C  CD    . LYS A 1 1656 ? 189.526 195.717 183.542 1.00 4.07  ? 1656 LYS A CD    1 
ATOM   1666  C  CE    . LYS A 1 1656 ? 190.220 196.115 182.253 1.00 7.82  ? 1656 LYS A CE    1 
ATOM   1667  N  NZ    . LYS A 1 1656 ? 190.930 197.409 182.372 1.00 10.03 ? 1656 LYS A NZ    1 
ATOM   1668  N  N     . MET A 1 1657 ? 184.572 193.498 184.757 1.00 2.62  ? 1657 MET A N     1 
ATOM   1669  C  CA    . MET A 1 1657 ? 183.398 193.641 185.606 1.00 2.57  ? 1657 MET A CA    1 
ATOM   1670  C  C     . MET A 1 1657 ? 182.385 192.517 185.435 1.00 1.89  ? 1657 MET A C     1 
ATOM   1671  O  O     . MET A 1 1657 ? 181.451 192.423 186.237 1.00 2.24  ? 1657 MET A O     1 
ATOM   1672  C  CB    . MET A 1 1657 ? 182.700 194.979 185.331 1.00 3.82  ? 1657 MET A CB    1 
ATOM   1673  C  CG    . MET A 1 1657 ? 183.585 196.197 185.486 1.00 2.17  ? 1657 MET A CG    1 
ATOM   1674  S  SD    . MET A 1 1657 ? 182.757 197.706 184.958 1.00 12.66 ? 1657 MET A SD    1 
ATOM   1675  C  CE    . MET A 1 1657 ? 182.941 197.601 183.181 1.00 3.20  ? 1657 MET A CE    1 
ATOM   1676  N  N     . PHE A 1 1658 ? 182.539 191.669 184.425 1.00 2.95  ? 1658 PHE A N     1 
ATOM   1677  C  CA    . PHE A 1 1658 ? 181.553 190.646 184.120 1.00 2.74  ? 1658 PHE A CA    1 
ATOM   1678  C  C     . PHE A 1 1658 ? 182.249 189.317 183.857 1.00 4.08  ? 1658 PHE A C     1 
ATOM   1679  O  O     . PHE A 1 1658 ? 183.421 189.268 183.482 1.00 4.20  ? 1658 PHE A O     1 
ATOM   1680  C  CB    . PHE A 1 1658 ? 180.696 191.039 182.912 1.00 1.06  ? 1658 PHE A CB    1 
ATOM   1681  C  CG    . PHE A 1 1658 ? 179.728 192.152 183.188 1.00 1.49  ? 1658 PHE A CG    1 
ATOM   1682  C  CD1   . PHE A 1 1658 ? 180.121 193.477 183.075 1.00 2.11  ? 1658 PHE A CD1   1 
ATOM   1683  C  CD2   . PHE A 1 1658 ? 178.421 191.878 183.553 1.00 1.88  ? 1658 PHE A CD2   1 
ATOM   1684  C  CE1   . PHE A 1 1658 ? 179.231 194.504 183.326 1.00 2.12  ? 1658 PHE A CE1   1 
ATOM   1685  C  CE2   . PHE A 1 1658 ? 177.526 192.900 183.804 1.00 1.85  ? 1658 PHE A CE2   1 
ATOM   1686  C  CZ    . PHE A 1 1658 ? 177.932 194.216 183.691 1.00 2.21  ? 1658 PHE A CZ    1 
ATOM   1687  N  N     . ALA A 1 1659 ? 181.500 188.234 184.070 1.00 2.81  ? 1659 ALA A N     1 
ATOM   1688  C  CA    . ALA A 1 1659 ? 182.043 186.898 183.846 1.00 2.01  ? 1659 ALA A CA    1 
ATOM   1689  C  C     . ALA A 1 1659 ? 182.251 186.626 182.362 1.00 3.28  ? 1659 ALA A C     1 
ATOM   1690  O  O     . ALA A 1 1659 ? 183.310 186.136 181.954 1.00 8.38  ? 1659 ALA A O     1 
ATOM   1691  C  CB    . ALA A 1 1659 ? 181.118 185.848 184.459 1.00 1.97  ? 1659 ALA A CB    1 
ATOM   1692  N  N     . GLY A 1 1660 ? 181.256 186.940 181.537 1.00 1.99  ? 1660 GLY A N     1 
ATOM   1693  C  CA    . GLY A 1 1660 ? 181.327 186.613 180.129 1.00 2.02  ? 1660 GLY A CA    1 
ATOM   1694  C  C     . GLY A 1 1660 ? 180.901 187.721 179.188 1.00 2.48  ? 1660 GLY A C     1 
ATOM   1695  O  O     . GLY A 1 1660 ? 180.710 187.482 177.993 1.00 4.22  ? 1660 GLY A O     1 
ATOM   1696  N  N     . VAL A 1 1661 ? 180.747 188.936 179.702 1.00 2.50  ? 1661 VAL A N     1 
ATOM   1697  C  CA    . VAL A 1 1661 ? 180.417 190.087 178.874 1.00 2.39  ? 1661 VAL A CA    1 
ATOM   1698  C  C     . VAL A 1 1661 ? 181.724 190.755 178.468 1.00 4.28  ? 1661 VAL A C     1 
ATOM   1699  O  O     . VAL A 1 1661 ? 182.407 191.360 179.298 1.00 7.25  ? 1661 VAL A O     1 
ATOM   1700  C  CB    . VAL A 1 1661 ? 179.493 191.071 179.601 1.00 1.58  ? 1661 VAL A CB    1 
ATOM   1701  C  CG1   . VAL A 1 1661 ? 179.278 192.313 178.756 1.00 1.99  ? 1661 VAL A CG1   1 
ATOM   1702  C  CG2   . VAL A 1 1661 ? 178.170 190.409 179.943 1.00 1.37  ? 1661 VAL A CG2   1 
ATOM   1703  N  N     . SER A 1 1662 ? 182.078 190.638 177.192 1.00 4.88  ? 1662 SER A N     1 
ATOM   1704  C  CA    . SER A 1 1662 ? 183.280 191.283 176.685 1.00 5.43  ? 1662 SER A CA    1 
ATOM   1705  C  C     . SER A 1 1662 ? 182.992 192.638 176.055 1.00 4.98  ? 1662 SER A C     1 
ATOM   1706  O  O     . SER A 1 1662 ? 183.861 193.515 176.065 1.00 8.38  ? 1662 SER A O     1 
ATOM   1707  C  CB    . SER A 1 1662 ? 183.976 190.374 175.668 1.00 6.89  ? 1662 SER A CB    1 
ATOM   1708  O  OG    . SER A 1 1662 ? 185.135 190.990 175.141 1.00 17.85 ? 1662 SER A OG    1 
ATOM   1709  N  N     . SER A 1 1663 ? 181.791 192.828 175.517 1.00 4.24  ? 1663 SER A N     1 
ATOM   1710  C  CA    . SER A 1 1663 ? 181.412 194.093 174.907 1.00 3.36  ? 1663 SER A CA    1 
ATOM   1711  C  C     . SER A 1 1663 ? 179.897 194.206 174.915 1.00 5.02  ? 1663 SER A C     1 
ATOM   1712  O  O     . SER A 1 1663 ? 179.183 193.223 175.131 1.00 6.35  ? 1663 SER A O     1 
ATOM   1713  C  CB    . SER A 1 1663 ? 181.955 194.219 173.478 1.00 3.86  ? 1663 SER A CB    1 
ATOM   1714  O  OG    . SER A 1 1663 ? 181.342 193.283 172.610 1.00 6.12  ? 1663 SER A OG    1 
ATOM   1715  N  N     . ILE A 1 1664 ? 179.418 195.421 174.679 1.00 4.27  ? 1664 ILE A N     1 
ATOM   1716  C  CA    . ILE A 1 1664 ? 177.992 195.705 174.583 1.00 4.20  ? 1664 ILE A CA    1 
ATOM   1717  C  C     . ILE A 1 1664 ? 177.670 196.116 173.153 1.00 5.29  ? 1664 ILE A C     1 
ATOM   1718  O  O     . ILE A 1 1664 ? 178.518 196.660 172.437 1.00 8.38  ? 1664 ILE A O     1 
ATOM   1719  C  CB    . ILE A 1 1664 ? 177.561 196.799 175.585 1.00 5.62  ? 1664 ILE A CB    1 
ATOM   1720  C  CG1   . ILE A 1 1664 ? 178.384 198.071 175.373 1.00 6.31  ? 1664 ILE A CG1   1 
ATOM   1721  C  CG2   . ILE A 1 1664 ? 177.699 196.304 177.012 1.00 3.25  ? 1664 ILE A CG2   1 
ATOM   1722  C  CD1   . ILE A 1 1664 ? 177.965 199.219 176.252 1.00 3.56  ? 1664 ILE A CD1   1 
ATOM   1723  N  N     . ILE A 1 1665 ? 176.438 195.838 172.733 1.00 7.10  ? 1665 ILE A N     1 
ATOM   1724  C  CA    . ILE A 1 1665 ? 175.949 196.222 171.412 1.00 6.47  ? 1665 ILE A CA    1 
ATOM   1725  C  C     . ILE A 1 1665 ? 175.215 197.549 171.534 1.00 8.59  ? 1665 ILE A C     1 
ATOM   1726  O  O     . ILE A 1 1665 ? 174.367 197.725 172.418 1.00 10.07 ? 1665 ILE A O     1 
ATOM   1727  C  CB    . ILE A 1 1665 ? 175.039 195.144 170.796 1.00 5.59  ? 1665 ILE A CB    1 
ATOM   1728  C  CG1   . ILE A 1 1665 ? 175.813 193.853 170.533 1.00 6.45  ? 1665 ILE A CG1   1 
ATOM   1729  C  CG2   . ILE A 1 1665 ? 174.409 195.642 169.508 1.00 9.06  ? 1665 ILE A CG2   1 
ATOM   1730  C  CD1   . ILE A 1 1665 ? 175.810 192.893 171.668 1.00 6.63  ? 1665 ILE A CD1   1 
ATOM   1731  N  N     . LEU A 1 1666 ? 175.536 198.476 170.638 1.00 7.17  ? 1666 LEU A N     1 
ATOM   1732  C  CA    . LEU A 1 1666 ? 175.008 199.827 170.667 1.00 8.27  ? 1666 LEU A CA    1 
ATOM   1733  C  C     . LEU A 1 1666 ? 174.394 200.153 169.314 1.00 14.85 ? 1666 LEU A C     1 
ATOM   1734  O  O     . LEU A 1 1666 ? 174.772 199.586 168.286 1.00 22.13 ? 1666 LEU A O     1 
ATOM   1735  C  CB    . LEU A 1 1666 ? 176.117 200.827 171.007 1.00 11.27 ? 1666 LEU A CB    1 
ATOM   1736  C  CG    . LEU A 1 1666 ? 176.683 200.672 172.416 1.00 9.42  ? 1666 LEU A CG    1 
ATOM   1737  C  CD1   . LEU A 1 1666 ? 177.880 201.560 172.609 1.00 8.96  ? 1666 LEU A CD1   1 
ATOM   1738  C  CD2   . LEU A 1 1666 ? 175.611 201.025 173.426 1.00 10.33 ? 1666 LEU A CD2   1 
ATOM   1739  N  N     . ASN A 1 1667 ? 173.440 201.077 169.322 1.00 16.81 ? 1667 ASN A N     1 
ATOM   1740  C  CA    . ASN A 1 1667 ? 172.835 201.547 168.083 1.00 15.35 ? 1667 ASN A CA    1 
ATOM   1741  C  C     . ASN A 1 1667 ? 173.830 202.452 167.357 1.00 19.91 ? 1667 ASN A C     1 
ATOM   1742  O  O     . ASN A 1 1667 ? 174.977 202.631 167.778 1.00 26.20 ? 1667 ASN A O     1 
ATOM   1743  C  CB    . ASN A 1 1667 ? 171.511 202.254 168.363 1.00 9.73  ? 1667 ASN A CB    1 
ATOM   1744  C  CG    . ASN A 1 1667 ? 171.619 203.289 169.465 1.00 17.40 ? 1667 ASN A CG    1 
ATOM   1745  O  OD1   . ASN A 1 1667 ? 172.712 203.616 169.927 1.00 22.22 ? 1667 ASN A OD1   1 
ATOM   1746  N  ND2   . ASN A 1 1667 ? 170.479 203.827 169.880 1.00 14.38 ? 1667 ASN A ND2   1 
ATOM   1747  N  N     . GLU A 1 1668 ? 173.394 203.038 166.239 1.00 23.05 ? 1668 GLU A N     1 
ATOM   1748  C  CA    . GLU A 1 1668 ? 174.281 203.914 165.479 1.00 19.99 ? 1668 GLU A CA    1 
ATOM   1749  C  C     . GLU A 1 1668 ? 174.636 205.171 166.260 1.00 21.47 ? 1668 GLU A C     1 
ATOM   1750  O  O     . GLU A 1 1668 ? 175.725 205.726 166.080 1.00 25.89 ? 1668 GLU A O     1 
ATOM   1751  C  CB    . GLU A 1 1668 ? 173.638 204.274 164.134 1.00 24.72 ? 1668 GLU A CB    1 
ATOM   1752  C  CG    . GLU A 1 1668 ? 172.725 205.503 164.144 1.00 28.33 ? 1668 GLU A CG    1 
ATOM   1753  C  CD    . GLU A 1 1668 ? 171.466 205.329 164.981 1.00 31.91 ? 1668 GLU A CD    1 
ATOM   1754  O  OE1   . GLU A 1 1668 ? 171.212 204.214 165.481 1.00 26.16 ? 1668 GLU A OE1   1 
ATOM   1755  O  OE2   . GLU A 1 1668 ? 170.726 206.323 165.142 1.00 35.99 ? 1668 GLU A OE2   1 
ATOM   1756  N  N     . ASP A 1 1669 ? 173.737 205.630 167.132 1.00 21.81 ? 1669 ASP A N     1 
ATOM   1757  C  CA    . ASP A 1 1669 ? 173.992 206.839 167.907 1.00 19.95 ? 1669 ASP A CA    1 
ATOM   1758  C  C     . ASP A 1 1669 ? 174.951 206.544 169.058 1.00 19.83 ? 1669 ASP A C     1 
ATOM   1759  O  O     . ASP A 1 1669 ? 175.736 207.416 169.443 1.00 26.01 ? 1669 ASP A O     1 
ATOM   1760  C  CB    . ASP A 1 1669 ? 172.633 207.399 168.373 1.00 20.16 ? 1669 ASP A CB    1 
ATOM   1761  C  CG    . ASP A 1 1669 ? 172.725 208.561 169.374 1.00 27.55 ? 1669 ASP A CG    1 
ATOM   1762  O  OD1   . ASP A 1 1669 ? 171.696 209.257 169.498 1.00 34.17 ? 1669 ASP A OD1   1 
ATOM   1763  O  OD2   . ASP A 1 1669 ? 173.754 208.819 170.026 1.00 32.20 ? 1669 ASP A OD2   1 
ATOM   1764  N  N     . ASN A 1 1670 ? 174.956 205.298 169.551 1.00 21.18 ? 1670 ASN A N     1 
ATOM   1765  C  CA    . ASN A 1 1670 ? 175.636 204.897 170.786 1.00 18.64 ? 1670 ASN A CA    1 
ATOM   1766  C  C     . ASN A 1 1670 ? 174.927 205.449 172.017 1.00 18.00 ? 1670 ASN A C     1 
ATOM   1767  O  O     . ASN A 1 1670 ? 175.562 205.764 173.025 1.00 19.58 ? 1670 ASN A O     1 
ATOM   1768  C  CB    . ASN A 1 1670 ? 177.118 205.299 170.804 1.00 13.76 ? 1670 ASN A CB    1 
ATOM   1769  C  CG    . ASN A 1 1670 ? 177.924 204.611 169.724 1.00 21.67 ? 1670 ASN A CG    1 
ATOM   1770  O  OD1   . ASN A 1 1670 ? 178.090 203.391 169.736 1.00 23.09 ? 1670 ASN A OD1   1 
ATOM   1771  N  ND2   . ASN A 1 1670 ? 178.436 205.391 168.782 1.00 27.55 ? 1670 ASN A ND2   1 
ATOM   1772  N  N     . SER A 1 1671 ? 173.602 205.563 171.938 1.00 20.74 ? 1671 SER A N     1 
ATOM   1773  C  CA    . SER A 1 1671 ? 172.781 206.075 173.024 1.00 14.74 ? 1671 SER A CA    1 
ATOM   1774  C  C     . SER A 1 1671 ? 171.904 205.019 173.676 1.00 17.11 ? 1671 SER A C     1 
ATOM   1775  O  O     . SER A 1 1671 ? 171.368 205.269 174.758 1.00 17.35 ? 1671 SER A O     1 
ATOM   1776  C  CB    . SER A 1 1671 ? 171.886 207.212 172.516 1.00 15.89 ? 1671 SER A CB    1 
ATOM   1777  O  OG    . SER A 1 1671 ? 171.123 206.792 171.402 1.00 19.81 ? 1671 SER A OG    1 
ATOM   1778  N  N     . VAL A 1 1672 ? 171.729 203.863 173.044 1.00 15.80 ? 1672 VAL A N     1 
ATOM   1779  C  CA    . VAL A 1 1672 ? 170.925 202.777 173.588 1.00 11.13 ? 1672 VAL A CA    1 
ATOM   1780  C  C     . VAL A 1 1672 ? 171.761 201.506 173.562 1.00 9.86  ? 1672 VAL A C     1 
ATOM   1781  O  O     . VAL A 1 1672 ? 172.345 201.166 172.526 1.00 12.59 ? 1672 VAL A O     1 
ATOM   1782  C  CB    . VAL A 1 1672 ? 169.615 202.582 172.800 1.00 9.95  ? 1672 VAL A CB    1 
ATOM   1783  C  CG1   . VAL A 1 1672 ? 168.815 201.439 173.383 1.00 9.26  ? 1672 VAL A CG1   1 
ATOM   1784  C  CG2   . VAL A 1 1672 ? 168.796 203.861 172.801 1.00 8.61  ? 1672 VAL A CG2   1 
ATOM   1785  N  N     . VAL A 1 1673 ? 171.823 200.813 174.694 1.00 11.99 ? 1673 VAL A N     1 
ATOM   1786  C  CA    . VAL A 1 1673 ? 172.514 199.532 174.785 1.00 8.34  ? 1673 VAL A CA    1 
ATOM   1787  C  C     . VAL A 1 1673 ? 171.540 198.455 174.322 1.00 5.34  ? 1673 VAL A C     1 
ATOM   1788  O  O     . VAL A 1 1673 ? 170.579 198.132 175.023 1.00 8.78  ? 1673 VAL A O     1 
ATOM   1789  C  CB    . VAL A 1 1673 ? 173.014 199.259 176.208 1.00 7.74  ? 1673 VAL A CB    1 
ATOM   1790  C  CG1   . VAL A 1 1673 ? 173.535 197.832 176.325 1.00 7.30  ? 1673 VAL A CG1   1 
ATOM   1791  C  CG2   . VAL A 1 1673 ? 174.084 200.258 176.598 1.00 3.99  ? 1673 VAL A CG2   1 
ATOM   1792  N  N     . LEU A 1 1674 ? 171.778 197.914 173.127 1.00 6.54  ? 1674 LEU A N     1 
ATOM   1793  C  CA    . LEU A 1 1674 ? 170.892 196.894 172.579 1.00 6.78  ? 1674 LEU A CA    1 
ATOM   1794  C  C     . LEU A 1 1674 ? 171.121 195.525 173.208 1.00 4.74  ? 1674 LEU A C     1 
ATOM   1795  O  O     . LEU A 1 1674 ? 170.169 194.750 173.349 1.00 5.57  ? 1674 LEU A O     1 
ATOM   1796  C  CB    . LEU A 1 1674 ? 171.064 196.810 171.062 1.00 9.83  ? 1674 LEU A CB    1 
ATOM   1797  C  CG    . LEU A 1 1674 ? 170.477 197.974 170.265 1.00 6.70  ? 1674 LEU A CG    1 
ATOM   1798  C  CD1   . LEU A 1 1674 ? 170.583 197.714 168.776 1.00 12.02 ? 1674 LEU A CD1   1 
ATOM   1799  C  CD2   . LEU A 1 1674 ? 169.034 198.226 170.668 1.00 7.10  ? 1674 LEU A CD2   1 
ATOM   1800  N  N     . GLY A 1 1675 ? 172.354 195.204 173.582 1.00 5.55  ? 1675 GLY A N     1 
ATOM   1801  C  CA    . GLY A 1 1675 ? 172.627 193.903 174.158 1.00 3.25  ? 1675 GLY A CA    1 
ATOM   1802  C  C     . GLY A 1 1675 ? 174.074 193.779 174.580 1.00 4.30  ? 1675 GLY A C     1 
ATOM   1803  O  O     . GLY A 1 1675 ? 174.809 194.765 174.651 1.00 6.22  ? 1675 GLY A O     1 
ATOM   1804  N  N     . ILE A 1 1676 ? 174.473 192.538 174.862 1.00 3.43  ? 1676 ILE A N     1 
ATOM   1805  C  CA    . ILE A 1 1676 ? 175.823 192.220 175.302 1.00 3.56  ? 1676 ILE A CA    1 
ATOM   1806  C  C     . ILE A 1 1676 ? 176.385 191.122 174.411 1.00 2.91  ? 1676 ILE A C     1 
ATOM   1807  O  O     . ILE A 1 1676 ? 175.650 190.368 173.771 1.00 4.45  ? 1676 ILE A O     1 
ATOM   1808  C  CB    . ILE A 1 1676 ? 175.872 191.783 176.781 1.00 6.21  ? 1676 ILE A CB    1 
ATOM   1809  C  CG1   . ILE A 1 1676 ? 174.892 190.632 177.026 1.00 1.92  ? 1676 ILE A CG1   1 
ATOM   1810  C  CG2   . ILE A 1 1676 ? 175.588 192.964 177.697 1.00 1.09  ? 1676 ILE A CG2   1 
ATOM   1811  C  CD1   . ILE A 1 1676 ? 174.797 190.201 178.462 1.00 2.17  ? 1676 ILE A CD1   1 
ATOM   1812  N  N     . SER A 1 1677 ? 177.712 191.049 174.369 1.00 3.02  ? 1677 SER A N     1 
ATOM   1813  C  CA    . SER A 1 1677 ? 178.410 190.071 173.547 1.00 3.54  ? 1677 SER A CA    1 
ATOM   1814  C  C     . SER A 1 1677 ? 179.566 189.474 174.340 1.00 5.00  ? 1677 SER A C     1 
ATOM   1815  O  O     . SER A 1 1677 ? 180.091 190.087 175.271 1.00 4.97  ? 1677 SER A O     1 
ATOM   1816  C  CB    . SER A 1 1677 ? 178.921 190.696 172.244 1.00 4.60  ? 1677 SER A CB    1 
ATOM   1817  O  OG    . SER A 1 1677 ? 179.770 189.803 171.545 1.00 13.24 ? 1677 SER A OG    1 
ATOM   1818  N  N     . SER A 1 1678 ? 179.952 188.263 173.956 1.00 3.57  ? 1678 SER A N     1 
ATOM   1819  C  CA    . SER A 1 1678 ? 181.068 187.563 174.572 1.00 5.40  ? 1678 SER A CA    1 
ATOM   1820  C  C     . SER A 1 1678 ? 182.338 187.755 173.750 1.00 7.52  ? 1678 SER A C     1 
ATOM   1821  O  O     . SER A 1 1678 ? 182.325 188.316 172.652 1.00 7.15  ? 1678 SER A O     1 
ATOM   1822  C  CB    . SER A 1 1678 ? 180.752 186.072 174.720 1.00 5.51  ? 1678 SER A CB    1 
ATOM   1823  O  OG    . SER A 1 1678 ? 180.386 185.505 173.477 1.00 6.12  ? 1678 SER A OG    1 
ATOM   1824  N  N     . ARG A 1 1679 ? 183.451 187.269 174.301 1.00 8.18  ? 1679 ARG A N     1 
ATOM   1825  C  CA    . ARG A 1 1679 ? 184.730 187.370 173.607 1.00 6.56  ? 1679 ARG A CA    1 
ATOM   1826  C  C     . ARG A 1 1679 ? 184.787 186.493 172.362 1.00 9.23  ? 1679 ARG A C     1 
ATOM   1827  O  O     . ARG A 1 1679 ? 185.620 186.742 171.485 1.00 18.41 ? 1679 ARG A O     1 
ATOM   1828  C  CB    . ARG A 1 1679 ? 185.872 187.006 174.556 1.00 7.69  ? 1679 ARG A CB    1 
ATOM   1829  C  CG    . ARG A 1 1679 ? 185.878 185.555 174.996 1.00 12.11 ? 1679 ARG A CG    1 
ATOM   1830  C  CD    . ARG A 1 1679 ? 187.100 185.244 175.836 1.00 12.89 ? 1679 ARG A CD    1 
ATOM   1831  N  NE    . ARG A 1 1679 ? 187.204 186.133 176.988 1.00 20.97 ? 1679 ARG A NE    1 
ATOM   1832  C  CZ    . ARG A 1 1679 ? 188.238 186.168 177.817 1.00 25.86 ? 1679 ARG A CZ    1 
ATOM   1833  N  NH1   . ARG A 1 1679 ? 189.285 185.379 177.649 1.00 26.34 ? 1679 ARG A NH1   1 
ATOM   1834  N  NH2   . ARG A 1 1679 ? 188.221 187.018 178.840 1.00 20.13 ? 1679 ARG A NH2   1 
ATOM   1835  N  N     . GLU A 1 1680 ? 183.925 185.483 172.262 1.00 12.32 ? 1680 GLU A N     1 
ATOM   1836  C  CA    . GLU A 1 1680 ? 183.868 184.614 171.095 1.00 8.69  ? 1680 GLU A CA    1 
ATOM   1837  C  C     . GLU A 1 1680 ? 182.853 185.076 170.059 1.00 8.82  ? 1680 GLU A C     1 
ATOM   1838  O  O     . GLU A 1 1680 ? 182.682 184.405 169.037 1.00 18.63 ? 1680 GLU A O     1 
ATOM   1839  C  CB    . GLU A 1 1680 ? 183.547 183.176 171.515 1.00 9.22  ? 1680 GLU A CB    1 
ATOM   1840  C  CG    . GLU A 1 1680 ? 184.616 182.519 172.365 1.00 10.77 ? 1680 GLU A CG    1 
ATOM   1841  C  CD    . GLU A 1 1680 ? 184.240 182.451 173.829 1.00 17.15 ? 1680 GLU A CD    1 
ATOM   1842  O  OE1   . GLU A 1 1680 ? 184.978 181.808 174.604 1.00 20.03 ? 1680 GLU A OE1   1 
ATOM   1843  O  OE2   . GLU A 1 1680 ? 183.200 183.035 174.202 1.00 12.15 ? 1680 GLU A OE2   1 
ATOM   1844  N  N     . GLY A 1 1681 ? 182.173 186.194 170.296 1.00 7.06  ? 1681 GLY A N     1 
ATOM   1845  C  CA    . GLY A 1 1681 ? 181.229 186.743 169.348 1.00 6.50  ? 1681 GLY A CA    1 
ATOM   1846  C  C     . GLY A 1 1681 ? 179.775 186.426 169.622 1.00 10.26 ? 1681 GLY A C     1 
ATOM   1847  O  O     . GLY A 1 1681 ? 178.904 186.994 168.952 1.00 9.67  ? 1681 GLY A O     1 
ATOM   1848  N  N     . GLU A 1 1682 ? 179.484 185.541 170.572 1.00 8.82  ? 1682 GLU A N     1 
ATOM   1849  C  CA    . GLU A 1 1682 ? 178.100 185.218 170.890 1.00 8.50  ? 1682 GLU A CA    1 
ATOM   1850  C  C     . GLU A 1 1682 ? 177.401 186.434 171.486 1.00 6.39  ? 1682 GLU A C     1 
ATOM   1851  O  O     . GLU A 1 1682 ? 177.932 187.089 172.388 1.00 7.54  ? 1682 GLU A O     1 
ATOM   1852  C  CB    . GLU A 1 1682 ? 178.035 184.038 171.855 1.00 7.58  ? 1682 GLU A CB    1 
ATOM   1853  C  CG    . GLU A 1 1682 ? 176.626 183.541 172.123 1.00 5.61  ? 1682 GLU A CG    1 
ATOM   1854  C  CD    . GLU A 1 1682 ? 176.571 182.520 173.241 1.00 4.66  ? 1682 GLU A CD    1 
ATOM   1855  O  OE1   . GLU A 1 1682 ? 176.782 182.902 174.408 1.00 4.11  ? 1682 GLU A OE1   1 
ATOM   1856  O  OE2   . GLU A 1 1682 ? 176.318 181.334 172.950 1.00 8.20  ? 1682 GLU A OE2   1 
ATOM   1857  N  N     . GLU A 1 1683 ? 176.204 186.729 170.987 1.00 6.17  ? 1683 GLU A N     1 
ATOM   1858  C  CA    . GLU A 1 1683 ? 175.478 187.938 171.344 1.00 4.16  ? 1683 GLU A CA    1 
ATOM   1859  C  C     . GLU A 1 1683 ? 174.197 187.593 172.087 1.00 5.73  ? 1683 GLU A C     1 
ATOM   1860  O  O     . GLU A 1 1683 ? 173.526 186.607 171.766 1.00 9.60  ? 1683 GLU A O     1 
ATOM   1861  C  CB    . GLU A 1 1683 ? 175.137 188.764 170.102 1.00 5.09  ? 1683 GLU A CB    1 
ATOM   1862  C  CG    . GLU A 1 1683 ? 176.336 189.380 169.407 1.00 14.87 ? 1683 GLU A CG    1 
ATOM   1863  C  CD    . GLU A 1 1683 ? 175.935 190.278 168.253 1.00 21.56 ? 1683 GLU A CD    1 
ATOM   1864  O  OE1   . GLU A 1 1683 ? 174.720 190.412 167.998 1.00 21.86 ? 1683 GLU A OE1   1 
ATOM   1865  O  OE2   . GLU A 1 1683 ? 176.833 190.850 167.602 1.00 27.32 ? 1683 GLU A OE2   1 
ATOM   1866  N  N     . VAL A 1 1684 ? 173.865 188.411 173.079 1.00 2.80  ? 1684 VAL A N     1 
ATOM   1867  C  CA    . VAL A 1 1684 ? 172.576 188.362 173.758 1.00 2.91  ? 1684 VAL A CA    1 
ATOM   1868  C  C     . VAL A 1 1684 ? 171.879 189.688 173.496 1.00 4.25  ? 1684 VAL A C     1 
ATOM   1869  O  O     . VAL A 1 1684 ? 172.396 190.749 173.865 1.00 9.51  ? 1684 VAL A O     1 
ATOM   1870  C  CB    . VAL A 1 1684 ? 172.726 188.113 175.266 1.00 2.59  ? 1684 VAL A CB    1 
ATOM   1871  C  CG1   . VAL A 1 1684 ? 171.361 187.936 175.907 1.00 1.81  ? 1684 VAL A CG1   1 
ATOM   1872  C  CG2   . VAL A 1 1684 ? 173.610 186.904 175.528 1.00 2.41  ? 1684 VAL A CG2   1 
ATOM   1873  N  N     . MET A 1 1685 ? 170.714 189.632 172.861 1.00 2.97  ? 1685 MET A N     1 
ATOM   1874  C  CA    . MET A 1 1685 ? 169.939 190.824 172.543 1.00 3.82  ? 1685 MET A CA    1 
ATOM   1875  C  C     . MET A 1 1685 ? 168.905 191.045 173.639 1.00 5.34  ? 1685 MET A C     1 
ATOM   1876  O  O     . MET A 1 1685 ? 168.075 190.168 173.899 1.00 9.08  ? 1685 MET A O     1 
ATOM   1877  C  CB    . MET A 1 1685 ? 169.262 190.691 171.180 1.00 3.63  ? 1685 MET A CB    1 
ATOM   1878  C  CG    . MET A 1 1685 ? 170.199 190.876 170.000 1.00 8.21  ? 1685 MET A CG    1 
ATOM   1879  S  SD    . MET A 1 1685 ? 171.315 192.280 170.188 1.00 22.81 ? 1685 MET A SD    1 
ATOM   1880  C  CE    . MET A 1 1685 ? 170.380 193.562 169.360 1.00 7.18  ? 1685 MET A CE    1 
ATOM   1881  N  N     . PHE A 1 1686 ? 168.955 192.214 174.270 1.00 4.96  ? 1686 PHE A N     1 
ATOM   1882  C  CA    . PHE A 1 1686 ? 168.037 192.520 175.356 1.00 3.93  ? 1686 PHE A CA    1 
ATOM   1883  C  C     . PHE A 1 1686 ? 166.604 192.582 174.846 1.00 8.39  ? 1686 PHE A C     1 
ATOM   1884  O  O     . PHE A 1 1686 ? 166.339 193.062 173.741 1.00 14.47 ? 1686 PHE A O     1 
ATOM   1885  C  CB    . PHE A 1 1686 ? 168.407 193.848 176.015 1.00 3.42  ? 1686 PHE A CB    1 
ATOM   1886  C  CG    . PHE A 1 1686 ? 169.720 193.825 176.738 1.00 4.52  ? 1686 PHE A CG    1 
ATOM   1887  C  CD1   . PHE A 1 1686 ? 170.267 192.630 177.176 1.00 4.43  ? 1686 PHE A CD1   1 
ATOM   1888  C  CD2   . PHE A 1 1686 ? 170.405 195.003 176.988 1.00 2.76  ? 1686 PHE A CD2   1 
ATOM   1889  C  CE1   . PHE A 1 1686 ? 171.476 192.611 177.844 1.00 4.14  ? 1686 PHE A CE1   1 
ATOM   1890  C  CE2   . PHE A 1 1686 ? 171.611 194.989 177.655 1.00 2.47  ? 1686 PHE A CE2   1 
ATOM   1891  C  CZ    . PHE A 1 1686 ? 172.147 193.791 178.084 1.00 4.09  ? 1686 PHE A CZ    1 
ATOM   1892  N  N     . LYS A 1 1687 ? 165.672 192.078 175.656 1.00 7.07  ? 1687 LYS A N     1 
ATOM   1893  C  CA    . LYS A 1 1687 ? 164.261 192.195 175.306 1.00 11.41 ? 1687 LYS A CA    1 
ATOM   1894  C  C     . LYS A 1 1687 ? 163.793 193.640 175.422 1.00 12.19 ? 1687 LYS A C     1 
ATOM   1895  O  O     . LYS A 1 1687 ? 163.034 194.124 174.575 1.00 17.53 ? 1687 LYS A O     1 
ATOM   1896  C  CB    . LYS A 1 1687 ? 163.420 191.275 176.190 1.00 8.00  ? 1687 LYS A CB    1 
ATOM   1897  C  CG    . LYS A 1 1687 ? 164.146 190.019 176.641 1.00 9.26  ? 1687 LYS A CG    1 
ATOM   1898  C  CD    . LYS A 1 1687 ? 164.400 189.066 175.480 1.00 11.37 ? 1687 LYS A CD    1 
ATOM   1899  C  CE    . LYS A 1 1687 ? 163.198 188.186 175.194 1.00 12.80 ? 1687 LYS A CE    1 
ATOM   1900  N  NZ    . LYS A 1 1687 ? 163.352 187.447 173.912 1.00 8.20  ? 1687 LYS A NZ    1 
ATOM   1901  N  N     . THR A 1 1688 ? 164.235 194.341 176.459 1.00 11.10 ? 1688 THR A N     1 
ATOM   1902  C  CA    . THR A 1 1688 ? 163.968 195.768 176.626 1.00 11.02 ? 1688 THR A CA    1 
ATOM   1903  C  C     . THR A 1 1688 ? 165.291 196.521 176.609 1.00 9.88  ? 1688 THR A C     1 
ATOM   1904  O  O     . THR A 1 1688 ? 166.057 196.442 177.589 1.00 9.15  ? 1688 THR A O     1 
ATOM   1905  C  CB    . THR A 1 1688 ? 163.214 196.036 177.928 1.00 16.59 ? 1688 THR A CB    1 
ATOM   1906  O  OG1   . THR A 1 1688 ? 161.931 195.400 177.877 1.00 19.54 ? 1688 THR A OG1   1 
ATOM   1907  C  CG2   . THR A 1 1688 ? 163.016 197.526 178.131 1.00 16.74 ? 1688 THR A CG2   1 
ATOM   1908  N  N     . PRO A 1 1689 ? 165.613 197.244 175.537 1.00 14.05 ? 1689 PRO A N     1 
ATOM   1909  C  CA    . PRO A 1 1689 ? 166.914 197.916 175.459 1.00 11.88 ? 1689 PRO A CA    1 
ATOM   1910  C  C     . PRO A 1 1689 ? 167.065 199.014 176.503 1.00 7.01  ? 1689 PRO A C     1 
ATOM   1911  O  O     . PRO A 1 1689 ? 166.089 199.617 176.956 1.00 11.53 ? 1689 PRO A O     1 
ATOM   1912  C  CB    . PRO A 1 1689 ? 166.931 198.495 174.038 1.00 9.42  ? 1689 PRO A CB    1 
ATOM   1913  C  CG    . PRO A 1 1689 ? 165.890 197.719 173.294 1.00 12.52 ? 1689 PRO A CG    1 
ATOM   1914  C  CD    . PRO A 1 1689 ? 164.836 197.407 174.299 1.00 9.22  ? 1689 PRO A CD    1 
ATOM   1915  N  N     . VAL A 1 1690 ? 168.315 199.269 176.877 1.00 7.67  ? 1690 VAL A N     1 
ATOM   1916  C  CA    . VAL A 1 1690 ? 168.661 200.242 177.909 1.00 6.68  ? 1690 VAL A CA    1 
ATOM   1917  C  C     . VAL A 1 1690 ? 169.092 201.535 177.228 1.00 9.94  ? 1690 VAL A C     1 
ATOM   1918  O  O     . VAL A 1 1690 ? 170.040 201.542 176.436 1.00 10.26 ? 1690 VAL A O     1 
ATOM   1919  C  CB    . VAL A 1 1690 ? 169.772 199.710 178.826 1.00 6.18  ? 1690 VAL A CB    1 
ATOM   1920  C  CG1   . VAL A 1 1690 ? 170.222 200.785 179.799 1.00 5.15  ? 1690 VAL A CG1   1 
ATOM   1921  C  CG2   . VAL A 1 1690 ? 169.304 198.477 179.564 1.00 5.13  ? 1690 VAL A CG2   1 
ATOM   1922  N  N     . SER A 1 1691 ? 168.410 202.631 177.552 1.00 11.19 ? 1691 SER A N     1 
ATOM   1923  C  CA    . SER A 1 1691 ? 168.712 203.929 176.965 1.00 11.66 ? 1691 SER A CA    1 
ATOM   1924  C  C     . SER A 1 1691 ? 169.694 204.686 177.849 1.00 16.01 ? 1691 SER A C     1 
ATOM   1925  O  O     . SER A 1 1691 ? 169.437 204.890 179.038 1.00 9.06  ? 1691 SER A O     1 
ATOM   1926  C  CB    . SER A 1 1691 ? 167.434 204.747 176.776 1.00 15.36 ? 1691 SER A CB    1 
ATOM   1927  O  OG    . SER A 1 1691 ? 167.726 206.123 176.630 1.00 15.76 ? 1691 SER A OG    1 
ATOM   1928  N  N     . ILE A 1 1692 ? 170.817 205.099 177.261 1.00 14.01 ? 1692 ILE A N     1 
ATOM   1929  C  CA    . ILE A 1 1692 ? 171.803 205.860 178.015 1.00 13.05 ? 1692 ILE A CA    1 
ATOM   1930  C  C     . ILE A 1 1692 ? 171.381 207.321 178.146 1.00 17.20 ? 1692 ILE A C     1 
ATOM   1931  O  O     . ILE A 1 1692 ? 171.717 207.978 179.136 1.00 17.10 ? 1692 ILE A O     1 
ATOM   1932  C  CB    . ILE A 1 1692 ? 173.193 205.718 177.369 1.00 13.74 ? 1692 ILE A CB    1 
ATOM   1933  C  CG1   . ILE A 1 1692 ? 173.622 204.250 177.361 1.00 7.60  ? 1692 ILE A CG1   1 
ATOM   1934  C  CG2   . ILE A 1 1692 ? 174.230 206.558 178.100 1.00 10.10 ? 1692 ILE A CG2   1 
ATOM   1935  C  CD1   . ILE A 1 1692 ? 175.042 204.027 176.895 1.00 5.35  ? 1692 ILE A CD1   1 
ATOM   1936  N  N     . THR A 1 1693 ? 170.631 207.849 177.175 1.00 15.39 ? 1693 THR A N     1 
ATOM   1937  C  CA    . THR A 1 1693 ? 170.187 209.237 177.263 1.00 13.73 ? 1693 THR A CA    1 
ATOM   1938  C  C     . THR A 1 1693 ? 169.260 209.452 178.452 1.00 11.95 ? 1693 THR A C     1 
ATOM   1939  O  O     . THR A 1 1693 ? 169.363 210.466 179.152 1.00 16.07 ? 1693 THR A O     1 
ATOM   1940  C  CB    . THR A 1 1693 ? 169.491 209.662 175.970 1.00 17.18 ? 1693 THR A CB    1 
ATOM   1941  O  OG1   . THR A 1 1693 ? 168.307 208.878 175.781 1.00 16.12 ? 1693 THR A OG1   1 
ATOM   1942  C  CG2   . THR A 1 1693 ? 170.416 209.486 174.784 1.00 13.25 ? 1693 THR A CG2   1 
ATOM   1943  N  N     . GLU A 1 1694 ? 168.346 208.511 178.696 1.00 11.52 ? 1694 GLU A N     1 
ATOM   1944  C  CA    . GLU A 1 1694 ? 167.378 208.694 179.774 1.00 12.18 ? 1694 GLU A CA    1 
ATOM   1945  C  C     . GLU A 1 1694 ? 167.994 208.394 181.133 1.00 12.27 ? 1694 GLU A C     1 
ATOM   1946  O  O     . GLU A 1 1694 ? 167.452 208.796 182.169 1.00 10.23 ? 1694 GLU A O     1 
ATOM   1947  C  CB    . GLU A 1 1694 ? 166.149 207.822 179.523 1.00 12.49 ? 1694 GLU A CB    1 
ATOM   1948  C  CG    . GLU A 1 1694 ? 165.342 208.253 178.309 1.00 19.66 ? 1694 GLU A CG    1 
ATOM   1949  C  CD    . GLU A 1 1694 ? 164.137 207.370 178.057 1.00 29.82 ? 1694 GLU A CD    1 
ATOM   1950  O  OE1   . GLU A 1 1694 ? 163.992 206.345 178.752 1.00 32.02 ? 1694 GLU A OE1   1 
ATOM   1951  O  OE2   . GLU A 1 1694 ? 163.332 207.706 177.162 1.00 24.67 ? 1694 GLU A OE2   1 
ATOM   1952  N  N     . HIS A 1 1695 ? 169.124 207.685 181.154 1.00 16.72 ? 1695 HIS A N     1 
ATOM   1953  C  CA    . HIS A 1 1695 ? 169.889 207.420 182.368 1.00 12.77 ? 1695 HIS A CA    1 
ATOM   1954  C  C     . HIS A 1 1695 ? 171.346 207.758 182.091 1.00 13.44 ? 1695 HIS A C     1 
ATOM   1955  O  O     . HIS A 1 1695 ? 172.170 206.855 181.875 1.00 12.95 ? 1695 HIS A O     1 
ATOM   1956  C  CB    . HIS A 1 1695 ? 169.736 205.964 182.811 1.00 10.70 ? 1695 HIS A CB    1 
ATOM   1957  C  CG    . HIS A 1 1695 ? 168.312 205.519 182.928 1.00 13.46 ? 1695 HIS A CG    1 
ATOM   1958  N  ND1   . HIS A 1 1695 ? 167.600 205.608 184.103 1.00 10.90 ? 1695 HIS A ND1   1 
ATOM   1959  C  CD2   . HIS A 1 1695 ? 167.467 204.985 182.014 1.00 9.56  ? 1695 HIS A CD2   1 
ATOM   1960  C  CE1   . HIS A 1 1695 ? 166.377 205.146 183.911 1.00 15.86 ? 1695 HIS A CE1   1 
ATOM   1961  N  NE2   . HIS A 1 1695 ? 166.270 204.763 182.651 1.00 12.73 ? 1695 HIS A NE2   1 
ATOM   1962  N  N     . PRO A 1 1696 ? 171.717 209.041 182.082 1.00 12.94 ? 1696 PRO A N     1 
ATOM   1963  C  CA    . PRO A 1 1696 ? 173.041 209.414 181.557 1.00 9.45  ? 1696 PRO A CA    1 
ATOM   1964  C  C     . PRO A 1 1696 ? 174.203 208.938 182.406 1.00 9.46  ? 1696 PRO A C     1 
ATOM   1965  O  O     . PRO A 1 1696 ? 175.236 208.538 181.858 1.00 13.72 ? 1696 PRO A O     1 
ATOM   1966  C  CB    . PRO A 1 1696 ? 172.969 210.947 181.503 1.00 10.79 ? 1696 PRO A CB    1 
ATOM   1967  C  CG    . PRO A 1 1696 ? 171.501 211.262 181.533 1.00 12.59 ? 1696 PRO A CG    1 
ATOM   1968  C  CD    . PRO A 1 1696 ? 170.922 210.227 182.430 1.00 8.76  ? 1696 PRO A CD    1 
ATOM   1969  N  N     . LYS A 1 1697 ? 174.072 208.972 183.727 1.00 10.52 ? 1697 LYS A N     1 
ATOM   1970  C  CA    . LYS A 1 1697 ? 175.223 208.742 184.588 1.00 13.29 ? 1697 LYS A CA    1 
ATOM   1971  C  C     . LYS A 1 1697 ? 175.649 207.276 184.532 1.00 13.84 ? 1697 LYS A C     1 
ATOM   1972  O  O     . LYS A 1 1697 ? 174.820 206.373 184.399 1.00 11.92 ? 1697 LYS A O     1 
ATOM   1973  C  CB    . LYS A 1 1697 ? 174.897 209.190 186.014 1.00 13.28 ? 1697 LYS A CB    1 
ATOM   1974  C  CG    . LYS A 1 1697 ? 176.033 209.065 187.005 1.00 16.58 ? 1697 LYS A CG    1 
ATOM   1975  C  CD    . LYS A 1 1697 ? 175.638 209.644 188.352 1.00 17.30 ? 1697 LYS A CD    1 
ATOM   1976  C  CE    . LYS A 1 1697 ? 176.712 209.395 189.398 1.00 24.02 ? 1697 LYS A CE    1 
ATOM   1977  N  NZ    . LYS A 1 1697 ? 177.966 210.133 189.082 1.00 17.60 ? 1697 LYS A NZ    1 
ATOM   1978  N  N     . ILE A 1 1698 ? 176.963 207.053 184.626 1.00 17.56 ? 1698 ILE A N     1 
ATOM   1979  C  CA    . ILE A 1 1698 ? 177.560 205.784 184.216 1.00 8.39  ? 1698 ILE A CA    1 
ATOM   1980  C  C     . ILE A 1 1698 ? 177.077 204.628 185.089 1.00 9.55  ? 1698 ILE A C     1 
ATOM   1981  O  O     . ILE A 1 1698 ? 176.874 203.510 184.601 1.00 13.27 ? 1698 ILE A O     1 
ATOM   1982  C  CB    . ILE A 1 1698 ? 179.098 205.902 184.214 1.00 10.26 ? 1698 ILE A CB    1 
ATOM   1983  C  CG1   . ILE A 1 1698 ? 179.748 204.708 183.514 1.00 8.99  ? 1698 ILE A CG1   1 
ATOM   1984  C  CG2   . ILE A 1 1698 ? 179.643 206.076 185.617 1.00 11.30 ? 1698 ILE A CG2   1 
ATOM   1985  C  CD1   . ILE A 1 1698 ? 179.462 204.633 182.050 1.00 8.11  ? 1698 ILE A CD1   1 
ATOM   1986  N  N     . ASN A 1 1699 ? 176.889 204.868 186.387 1.00 11.41 ? 1699 ASN A N     1 
ATOM   1987  C  CA    . ASN A 1 1699 ? 176.615 203.768 187.305 1.00 8.39  ? 1699 ASN A CA    1 
ATOM   1988  C  C     . ASN A 1 1699 ? 175.159 203.319 187.288 1.00 10.89 ? 1699 ASN A C     1 
ATOM   1989  O  O     . ASN A 1 1699 ? 174.858 202.236 187.801 1.00 11.81 ? 1699 ASN A O     1 
ATOM   1990  C  CB    . ASN A 1 1699 ? 177.026 204.155 188.723 1.00 7.91  ? 1699 ASN A CB    1 
ATOM   1991  C  CG    . ASN A 1 1699 ? 176.161 205.251 189.296 1.00 12.30 ? 1699 ASN A CG    1 
ATOM   1992  O  OD1   . ASN A 1 1699 ? 176.135 206.362 188.779 1.00 14.28 ? 1699 ASN A OD1   1 
ATOM   1993  N  ND2   . ASN A 1 1699 ? 175.430 204.939 190.357 1.00 14.25 ? 1699 ASN A ND2   1 
ATOM   1994  N  N     . GLU A 1 1700 ? 174.248 204.111 186.724 1.00 8.63  ? 1700 GLU A N     1 
ATOM   1995  C  CA    . GLU A 1 1700 ? 172.849 203.698 186.678 1.00 9.77  ? 1700 GLU A CA    1 
ATOM   1996  C  C     . GLU A 1 1700 ? 172.534 202.863 185.443 1.00 9.92  ? 1700 GLU A C     1 
ATOM   1997  O  O     . GLU A 1 1700 ? 171.886 201.817 185.553 1.00 10.12 ? 1700 GLU A O     1 
ATOM   1998  C  CB    . GLU A 1 1700 ? 171.927 204.915 186.763 1.00 11.17 ? 1700 GLU A CB    1 
ATOM   1999  C  CG    . GLU A 1 1700 ? 171.968 205.619 188.109 1.00 15.69 ? 1700 GLU A CG    1 
ATOM   2000  C  CD    . GLU A 1 1700 ? 173.129 206.564 188.234 1.00 23.15 ? 1700 GLU A CD    1 
ATOM   2001  O  OE1   . GLU A 1 1700 ? 173.864 206.707 187.240 1.00 28.64 ? 1700 GLU A OE1   1 
ATOM   2002  O  OE2   . GLU A 1 1700 ? 173.309 207.160 189.315 1.00 26.40 ? 1700 GLU A OE2   1 
ATOM   2003  N  N     . TRP A 1 1701 ? 172.970 203.297 184.257 1.00 7.25  ? 1701 TRP A N     1 
ATOM   2004  C  CA    . TRP A 1 1701 ? 172.696 202.480 183.082 1.00 5.26  ? 1701 TRP A CA    1 
ATOM   2005  C  C     . TRP A 1 1701 ? 173.546 201.216 183.064 1.00 3.97  ? 1701 TRP A C     1 
ATOM   2006  O  O     . TRP A 1 1701 ? 173.122 200.209 182.491 1.00 6.63  ? 1701 TRP A O     1 
ATOM   2007  C  CB    . TRP A 1 1701 ? 172.887 203.279 181.783 1.00 7.28  ? 1701 TRP A CB    1 
ATOM   2008  C  CG    . TRP A 1 1701 ? 174.303 203.600 181.396 1.00 6.91  ? 1701 TRP A CG    1 
ATOM   2009  C  CD1   . TRP A 1 1701 ? 174.980 204.758 181.643 1.00 7.51  ? 1701 TRP A CD1   1 
ATOM   2010  C  CD2   . TRP A 1 1701 ? 175.204 202.762 180.660 1.00 6.72  ? 1701 TRP A CD2   1 
ATOM   2011  N  NE1   . TRP A 1 1701 ? 176.248 204.686 181.119 1.00 7.04  ? 1701 TRP A NE1   1 
ATOM   2012  C  CE2   . TRP A 1 1701 ? 176.410 203.470 180.512 1.00 6.09  ? 1701 TRP A CE2   1 
ATOM   2013  C  CE3   . TRP A 1 1701 ? 175.109 201.475 180.120 1.00 4.11  ? 1701 TRP A CE3   1 
ATOM   2014  C  CZ2   . TRP A 1 1701 ? 177.511 202.937 179.844 1.00 4.26  ? 1701 TRP A CZ2   1 
ATOM   2015  C  CZ3   . TRP A 1 1701 ? 176.203 200.950 179.463 1.00 4.32  ? 1701 TRP A CZ3   1 
ATOM   2016  C  CH2   . TRP A 1 1701 ? 177.388 201.679 179.331 1.00 3.71  ? 1701 TRP A CH2   1 
ATOM   2017  N  N     . LEU A 1 1702 ? 174.726 201.242 183.687 1.00 5.02  ? 1702 LEU A N     1 
ATOM   2018  C  CA    . LEU A 1 1702 ? 175.484 200.010 183.880 1.00 4.58  ? 1702 LEU A CA    1 
ATOM   2019  C  C     . LEU A 1 1702 ? 174.727 199.040 184.777 1.00 5.00  ? 1702 LEU A C     1 
ATOM   2020  O  O     . LEU A 1 1702 ? 174.750 197.826 184.552 1.00 7.45  ? 1702 LEU A O     1 
ATOM   2021  C  CB    . LEU A 1 1702 ? 176.860 200.320 184.469 1.00 4.79  ? 1702 LEU A CB    1 
ATOM   2022  C  CG    . LEU A 1 1702 ? 178.012 200.485 183.478 1.00 3.57  ? 1702 LEU A CG    1 
ATOM   2023  C  CD1   . LEU A 1 1702 ? 179.315 200.721 184.221 1.00 5.48  ? 1702 LEU A CD1   1 
ATOM   2024  C  CD2   . LEU A 1 1702 ? 178.122 199.271 182.571 1.00 3.15  ? 1702 LEU A CD2   1 
ATOM   2025  N  N     . THR A 1 1703 ? 174.058 199.563 185.810 1.00 3.80  ? 1703 THR A N     1 
ATOM   2026  C  CA    . THR A 1 1703 ? 173.203 198.725 186.641 1.00 3.97  ? 1703 THR A CA    1 
ATOM   2027  C  C     . THR A 1 1703 ? 172.020 198.185 185.846 1.00 4.14  ? 1703 THR A C     1 
ATOM   2028  O  O     . THR A 1 1703 ? 171.652 197.012 185.984 1.00 7.10  ? 1703 THR A O     1 
ATOM   2029  C  CB    . THR A 1 1703 ? 172.718 199.514 187.859 1.00 4.17  ? 1703 THR A CB    1 
ATOM   2030  O  OG1   . THR A 1 1703 ? 173.844 199.935 188.636 1.00 9.79  ? 1703 THR A OG1   1 
ATOM   2031  C  CG2   . THR A 1 1703 ? 171.807 198.662 188.728 1.00 6.69  ? 1703 THR A CG2   1 
ATOM   2032  N  N     . LEU A 1 1704 ? 171.414 199.023 185.000 1.00 2.91  ? 1704 LEU A N     1 
ATOM   2033  C  CA    . LEU A 1 1704 ? 170.292 198.566 184.186 1.00 3.42  ? 1704 LEU A CA    1 
ATOM   2034  C  C     . LEU A 1 1704 ? 170.735 197.528 183.162 1.00 5.82  ? 1704 LEU A C     1 
ATOM   2035  O  O     . LEU A 1 1704 ? 169.979 196.606 182.839 1.00 6.12  ? 1704 LEU A O     1 
ATOM   2036  C  CB    . LEU A 1 1704 ? 169.620 199.752 183.493 1.00 4.76  ? 1704 LEU A CB    1 
ATOM   2037  C  CG    . LEU A 1 1704 ? 169.045 200.844 184.398 1.00 4.11  ? 1704 LEU A CG    1 
ATOM   2038  C  CD1   . LEU A 1 1704 ? 168.528 202.006 183.572 1.00 7.46  ? 1704 LEU A CD1   1 
ATOM   2039  C  CD2   . LEU A 1 1704 ? 167.946 200.286 185.280 1.00 2.99  ? 1704 LEU A CD2   1 
ATOM   2040  N  N     . VAL A 1 1705 ? 171.952 197.668 182.631 1.00 5.56  ? 1705 VAL A N     1 
ATOM   2041  C  CA    . VAL A 1 1705 ? 172.490 196.656 181.727 1.00 4.64  ? 1705 VAL A CA    1 
ATOM   2042  C  C     . VAL A 1 1705 ? 172.675 195.333 182.460 1.00 3.42  ? 1705 VAL A C     1 
ATOM   2043  O  O     . VAL A 1 1705 ? 172.363 194.261 181.928 1.00 7.52  ? 1705 VAL A O     1 
ATOM   2044  C  CB    . VAL A 1 1705 ? 173.804 197.148 181.089 1.00 3.74  ? 1705 VAL A CB    1 
ATOM   2045  C  CG1   . VAL A 1 1705 ? 174.569 195.993 180.461 1.00 1.16  ? 1705 VAL A CG1   1 
ATOM   2046  C  CG2   . VAL A 1 1705 ? 173.510 198.207 180.043 1.00 1.88  ? 1705 VAL A CG2   1 
ATOM   2047  N  N     . GLU A 1 1706 ? 173.178 195.388 183.694 1.00 2.47  ? 1706 GLU A N     1 
ATOM   2048  C  CA    . GLU A 1 1706 ? 173.370 194.173 184.478 1.00 3.41  ? 1706 GLU A CA    1 
ATOM   2049  C  C     . GLU A 1 1706 ? 172.035 193.496 184.779 1.00 4.75  ? 1706 GLU A C     1 
ATOM   2050  O  O     . GLU A 1 1706 ? 171.945 192.263 184.811 1.00 4.04  ? 1706 GLU A O     1 
ATOM   2051  C  CB    . GLU A 1 1706 ? 174.127 194.510 185.767 1.00 3.73  ? 1706 GLU A CB    1 
ATOM   2052  C  CG    . GLU A 1 1706 ? 174.114 193.431 186.836 1.00 5.18  ? 1706 GLU A CG    1 
ATOM   2053  C  CD    . GLU A 1 1706 ? 174.573 193.950 188.188 1.00 14.52 ? 1706 GLU A CD    1 
ATOM   2054  O  OE1   . GLU A 1 1706 ? 173.961 194.913 188.694 1.00 17.36 ? 1706 GLU A OE1   1 
ATOM   2055  O  OE2   . GLU A 1 1706 ? 175.546 193.400 188.742 1.00 16.00 ? 1706 GLU A OE2   1 
ATOM   2056  N  N     . LYS A 1 1707 ? 170.983 194.287 185.000 1.00 5.29  ? 1707 LYS A N     1 
ATOM   2057  C  CA    . LYS A 1 1707 ? 169.666 193.714 185.265 1.00 3.69  ? 1707 LYS A CA    1 
ATOM   2058  C  C     . LYS A 1 1707 ? 169.040 193.142 183.997 1.00 4.13  ? 1707 LYS A C     1 
ATOM   2059  O  O     . LYS A 1 1707 ? 168.473 192.044 184.015 1.00 6.31  ? 1707 LYS A O     1 
ATOM   2060  C  CB    . LYS A 1 1707 ? 168.750 194.761 185.896 1.00 4.20  ? 1707 LYS A CB    1 
ATOM   2061  C  CG    . LYS A 1 1707 ? 169.169 195.180 187.292 1.00 6.63  ? 1707 LYS A CG    1 
ATOM   2062  C  CD    . LYS A 1 1707 ? 168.192 196.177 187.887 1.00 9.60  ? 1707 LYS A CD    1 
ATOM   2063  C  CE    . LYS A 1 1707 ? 168.660 196.653 189.249 1.00 10.73 ? 1707 LYS A CE    1 
ATOM   2064  N  NZ    . LYS A 1 1707 ? 168.620 195.559 190.255 1.00 12.77 ? 1707 LYS A NZ    1 
ATOM   2065  N  N     . GLU A 1 1708 ? 169.121 193.875 182.882 1.00 3.68  ? 1708 GLU A N     1 
ATOM   2066  C  CA    . GLU A 1 1708 ? 168.567 193.368 181.629 1.00 4.79  ? 1708 GLU A CA    1 
ATOM   2067  C  C     . GLU A 1 1708 ? 169.290 192.117 181.157 1.00 3.58  ? 1708 GLU A C     1 
ATOM   2068  O  O     . GLU A 1 1708 ? 168.688 191.257 180.506 1.00 3.51  ? 1708 GLU A O     1 
ATOM   2069  C  CB    . GLU A 1 1708 ? 168.603 194.441 180.542 1.00 3.60  ? 1708 GLU A CB    1 
ATOM   2070  C  CG    . GLU A 1 1708 ? 167.698 195.617 180.801 1.00 13.04 ? 1708 GLU A CG    1 
ATOM   2071  C  CD    . GLU A 1 1708 ? 166.236 195.231 180.751 1.00 26.25 ? 1708 GLU A CD    1 
ATOM   2072  O  OE1   . GLU A 1 1708 ? 165.890 194.309 179.980 1.00 18.34 ? 1708 GLU A OE1   1 
ATOM   2073  O  OE2   . GLU A 1 1708 ? 165.427 195.847 181.480 1.00 28.61 ? 1708 GLU A OE2   1 
ATOM   2074  N  N     . MET A 1 1709 ? 170.581 191.995 181.465 1.00 2.54  ? 1709 MET A N     1 
ATOM   2075  C  CA    . MET A 1 1709 ? 171.290 190.762 181.137 1.00 1.95  ? 1709 MET A CA    1 
ATOM   2076  C  C     . MET A 1 1709 ? 170.655 189.576 181.850 1.00 2.61  ? 1709 MET A C     1 
ATOM   2077  O  O     . MET A 1 1709 ? 170.429 188.522 181.246 1.00 2.79  ? 1709 MET A O     1 
ATOM   2078  C  CB    . MET A 1 1709 ? 172.770 190.892 181.494 1.00 1.85  ? 1709 MET A CB    1 
ATOM   2079  C  CG    . MET A 1 1709 ? 173.452 189.575 181.827 1.00 1.75  ? 1709 MET A CG    1 
ATOM   2080  S  SD    . MET A 1 1709 ? 175.043 189.778 182.647 1.00 3.45  ? 1709 MET A SD    1 
ATOM   2081  C  CE    . MET A 1 1709 ? 174.536 189.904 184.360 1.00 1.55  ? 1709 MET A CE    1 
ATOM   2082  N  N     . ARG A 1 1710 ? 170.332 189.743 183.133 1.00 3.35  ? 1710 ARG A N     1 
ATOM   2083  C  CA    . ARG A 1 1710 ? 169.712 188.662 183.892 1.00 1.72  ? 1710 ARG A CA    1 
ATOM   2084  C  C     . ARG A 1 1710 ? 168.278 188.414 183.436 1.00 1.87  ? 1710 ARG A C     1 
ATOM   2085  O  O     . ARG A 1 1710 ? 167.841 187.265 183.326 1.00 4.08  ? 1710 ARG A O     1 
ATOM   2086  C  CB    . ARG A 1 1710 ? 169.764 188.980 185.385 1.00 1.88  ? 1710 ARG A CB    1 
ATOM   2087  C  CG    . ARG A 1 1710 ? 171.169 188.996 185.953 1.00 1.11  ? 1710 ARG A CG    1 
ATOM   2088  C  CD    . ARG A 1 1710 ? 171.160 189.183 187.456 1.00 1.20  ? 1710 ARG A CD    1 
ATOM   2089  N  NE    . ARG A 1 1710 ? 172.503 189.114 188.018 1.00 4.42  ? 1710 ARG A NE    1 
ATOM   2090  C  CZ    . ARG A 1 1710 ? 173.088 190.099 188.687 1.00 7.30  ? 1710 ARG A CZ    1 
ATOM   2091  N  NH1   . ARG A 1 1710 ? 172.480 191.258 188.882 1.00 6.39  ? 1710 ARG A NH1   1 
ATOM   2092  N  NH2   . ARG A 1 1710 ? 174.313 189.917 189.169 1.00 3.52  ? 1710 ARG A NH2   1 
ATOM   2093  N  N     . VAL A 1 1711 ? 167.531 189.485 183.164 1.00 3.63  ? 1711 VAL A N     1 
ATOM   2094  C  CA    . VAL A 1 1711 ? 166.130 189.336 182.779 1.00 2.29  ? 1711 VAL A CA    1 
ATOM   2095  C  C     . VAL A 1 1711 ? 166.012 188.730 181.385 1.00 2.31  ? 1711 VAL A C     1 
ATOM   2096  O  O     . VAL A 1 1711 ? 165.160 187.869 181.138 1.00 4.75  ? 1711 VAL A O     1 
ATOM   2097  C  CB    . VAL A 1 1711 ? 165.405 190.692 182.881 1.00 2.99  ? 1711 VAL A CB    1 
ATOM   2098  C  CG1   . VAL A 1 1711 ? 164.030 190.617 182.243 1.00 3.20  ? 1711 VAL A CG1   1 
ATOM   2099  C  CG2   . VAL A 1 1711 ? 165.290 191.112 184.335 1.00 1.83  ? 1711 VAL A CG2   1 
ATOM   2100  N  N     . THR A 1 1712 ? 166.861 189.169 180.453 1.00 2.83  ? 1712 THR A N     1 
ATOM   2101  C  CA    . THR A 1 1712 ? 166.808 188.642 179.093 1.00 3.27  ? 1712 THR A CA    1 
ATOM   2102  C  C     . THR A 1 1712 ? 167.153 187.158 179.062 1.00 2.44  ? 1712 THR A C     1 
ATOM   2103  O  O     . THR A 1 1712 ? 166.492 186.369 178.378 1.00 2.44  ? 1712 THR A O     1 
ATOM   2104  C  CB    . THR A 1 1712 ? 167.755 189.432 178.186 1.00 3.30  ? 1712 THR A CB    1 
ATOM   2105  O  OG1   . THR A 1 1712 ? 167.322 190.795 178.112 1.00 5.33  ? 1712 THR A OG1   1 
ATOM   2106  C  CG2   . THR A 1 1712 ? 167.791 188.836 176.791 1.00 2.63  ? 1712 THR A CG2   1 
ATOM   2107  N  N     . LEU A 1 1713 ? 168.189 186.764 179.803 1.00 2.34  ? 1713 LEU A N     1 
ATOM   2108  C  CA    . LEU A 1 1713 ? 168.587 185.361 179.846 1.00 1.26  ? 1713 LEU A CA    1 
ATOM   2109  C  C     . LEU A 1 1713 ? 167.492 184.486 180.444 1.00 1.71  ? 1713 LEU A C     1 
ATOM   2110  O  O     . LEU A 1 1713 ? 167.243 183.377 179.958 1.00 5.23  ? 1713 LEU A O     1 
ATOM   2111  C  CB    . LEU A 1 1713 ? 169.883 185.216 180.638 1.00 1.28  ? 1713 LEU A CB    1 
ATOM   2112  C  CG    . LEU A 1 1713 ? 171.129 185.755 179.939 1.00 0.97  ? 1713 LEU A CG    1 
ATOM   2113  C  CD1   . LEU A 1 1713 ? 172.344 185.576 180.820 1.00 0.74  ? 1713 LEU A CD1   1 
ATOM   2114  C  CD2   . LEU A 1 1713 ? 171.318 185.056 178.604 1.00 0.88  ? 1713 LEU A CD2   1 
ATOM   2115  N  N     . ALA A 1 1714 ? 166.835 184.960 181.504 1.00 1.78  ? 1714 ALA A N     1 
ATOM   2116  C  CA    . ALA A 1 1714 ? 165.732 184.203 182.085 1.00 1.71  ? 1714 ALA A CA    1 
ATOM   2117  C  C     . ALA A 1 1714 ? 164.559 184.101 181.116 1.00 1.43  ? 1714 ALA A C     1 
ATOM   2118  O  O     . ALA A 1 1714 ? 163.935 183.039 181.000 1.00 2.02  ? 1714 ALA A O     1 
ATOM   2119  C  CB    . ALA A 1 1714 ? 165.296 184.839 183.405 1.00 1.80  ? 1714 ALA A CB    1 
ATOM   2120  N  N     . LYS A 1 1715 ? 164.236 185.194 180.422 1.00 1.96  ? 1715 LYS A N     1 
ATOM   2121  C  CA    . LYS A 1 1715 ? 163.196 185.138 179.399 1.00 3.08  ? 1715 LYS A CA    1 
ATOM   2122  C  C     . LYS A 1 1715 ? 163.604 184.232 178.245 1.00 2.29  ? 1715 LYS A C     1 
ATOM   2123  O  O     . LYS A 1 1715 ? 162.775 183.485 177.713 1.00 4.28  ? 1715 LYS A O     1 
ATOM   2124  C  CB    . LYS A 1 1715 ? 162.879 186.543 178.891 1.00 4.50  ? 1715 LYS A CB    1 
ATOM   2125  C  CG    . LYS A 1 1715 ? 162.084 187.391 179.860 1.00 4.13  ? 1715 LYS A CG    1 
ATOM   2126  C  CD    . LYS A 1 1715 ? 161.278 188.449 179.124 1.00 8.28  ? 1715 LYS A CD    1 
ATOM   2127  C  CE    . LYS A 1 1715 ? 161.196 189.739 179.919 1.00 8.15  ? 1715 LYS A CE    1 
ATOM   2128  N  NZ    . LYS A 1 1715 ? 161.056 189.485 181.375 1.00 14.34 ? 1715 LYS A NZ    1 
ATOM   2129  N  N     . LEU A 1 1716 ? 164.874 184.290 177.842 1.00 2.24  ? 1716 LEU A N     1 
ATOM   2130  C  CA    . LEU A 1 1716 ? 165.359 183.410 176.784 1.00 2.40  ? 1716 LEU A CA    1 
ATOM   2131  C  C     . LEU A 1 1716 ? 165.375 181.957 177.228 1.00 2.99  ? 1716 LEU A C     1 
ATOM   2132  O  O     . LEU A 1 1716 ? 165.148 181.058 176.412 1.00 3.89  ? 1716 LEU A O     1 
ATOM   2133  C  CB    . LEU A 1 1716 ? 166.753 183.847 176.337 1.00 1.89  ? 1716 LEU A CB    1 
ATOM   2134  C  CG    . LEU A 1 1716 ? 166.839 184.975 175.310 1.00 1.79  ? 1716 LEU A CG    1 
ATOM   2135  C  CD1   . LEU A 1 1716 ? 168.275 185.427 175.146 1.00 2.16  ? 1716 LEU A CD1   1 
ATOM   2136  C  CD2   . LEU A 1 1716 ? 166.258 184.535 173.977 1.00 1.94  ? 1716 LEU A CD2   1 
ATOM   2137  N  N     . LEU A 1 1717 ? 165.652 181.703 178.512 1.00 2.51  ? 1717 LEU A N     1 
ATOM   2138  C  CA    . LEU A 1 1717 ? 165.608 180.339 179.023 1.00 2.06  ? 1717 LEU A CA    1 
ATOM   2139  C  C     . LEU A 1 1717 ? 164.203 179.760 178.926 1.00 3.72  ? 1717 LEU A C     1 
ATOM   2140  O  O     . LEU A 1 1717 ? 164.029 178.599 178.544 1.00 4.98  ? 1717 LEU A O     1 
ATOM   2141  C  CB    . LEU A 1 1717 ? 166.104 180.300 180.468 1.00 2.18  ? 1717 LEU A CB    1 
ATOM   2142  C  CG    . LEU A 1 1717 ? 166.084 178.927 181.145 1.00 2.54  ? 1717 LEU A CG    1 
ATOM   2143  C  CD1   . LEU A 1 1717 ? 167.038 177.962 180.454 1.00 0.99  ? 1717 LEU A CD1   1 
ATOM   2144  C  CD2   . LEU A 1 1717 ? 166.412 179.044 182.623 1.00 0.56  ? 1717 LEU A CD2   1 
ATOM   2145  N  N     . ALA A 1 1718 ? 163.186 180.560 179.257 1.00 3.21  ? 1718 ALA A N     1 
ATOM   2146  C  CA    . ALA A 1 1718 ? 161.812 180.072 179.202 1.00 4.07  ? 1718 ALA A CA    1 
ATOM   2147  C  C     . ALA A 1 1718 ? 161.420 179.685 177.781 1.00 9.25  ? 1718 ALA A C     1 
ATOM   2148  O  O     . ALA A 1 1718 ? 160.754 178.665 177.569 1.00 12.28 ? 1718 ALA A O     1 
ATOM   2149  C  CB    . ALA A 1 1718 ? 160.856 181.127 179.754 1.00 4.53  ? 1718 ALA A CB    1 
ATOM   2150  N  N     . GLU A 1 1719 ? 161.817 180.491 176.797 1.00 11.23 ? 1719 GLU A N     1 
ATOM   2151  C  CA    . GLU A 1 1719 ? 161.552 180.145 175.406 1.00 7.40  ? 1719 GLU A CA    1 
ATOM   2152  C  C     . GLU A 1 1719 ? 162.314 178.893 174.992 1.00 5.98  ? 1719 GLU A C     1 
ATOM   2153  O  O     . GLU A 1 1719 ? 161.782 178.046 174.263 1.00 10.63 ? 1719 GLU A O     1 
ATOM   2154  C  CB    . GLU A 1 1719 ? 161.908 181.321 174.498 1.00 7.58  ? 1719 GLU A CB    1 
ATOM   2155  C  CG    . GLU A 1 1719 ? 161.059 182.556 174.741 1.00 10.73 ? 1719 GLU A CG    1 
ATOM   2156  C  CD    . GLU A 1 1719 ? 161.829 183.846 174.543 1.00 15.34 ? 1719 GLU A CD    1 
ATOM   2157  O  OE1   . GLU A 1 1719 ? 163.057 183.780 174.333 1.00 12.12 ? 1719 GLU A OE1   1 
ATOM   2158  O  OE2   . GLU A 1 1719 ? 161.207 184.925 174.602 1.00 21.21 ? 1719 GLU A OE2   1 
ATOM   2159  N  N     . SER A 1 1720 ? 163.564 178.759 175.442 1.00 4.41  ? 1720 SER A N     1 
ATOM   2160  C  CA    . SER A 1 1720 ? 164.358 177.583 175.104 1.00 4.18  ? 1720 SER A CA    1 
ATOM   2161  C  C     . SER A 1 1720 ? 163.793 176.321 175.748 1.00 5.91  ? 1720 SER A C     1 
ATOM   2162  O  O     . SER A 1 1720 ? 163.769 175.259 175.119 1.00 6.55  ? 1720 SER A O     1 
ATOM   2163  C  CB    . SER A 1 1720 ? 165.812 177.797 175.523 1.00 3.80  ? 1720 SER A CB    1 
ATOM   2164  O  OG    . SER A 1 1720 ? 166.640 176.752 175.047 1.00 2.89  ? 1720 SER A OG    1 
ATOM   2165  N  N     . VAL A 1 1721 ? 163.347 176.415 177.004 1.00 8.31  ? 1721 VAL A N     1 
ATOM   2166  C  CA    . VAL A 1 1721 ? 162.772 175.253 177.681 1.00 6.90  ? 1721 VAL A CA    1 
ATOM   2167  C  C     . VAL A 1 1721 ? 161.531 174.763 176.945 1.00 8.77  ? 1721 VAL A C     1 
ATOM   2168  O  O     . VAL A 1 1721 ? 161.288 173.555 176.846 1.00 13.84 ? 1721 VAL A O     1 
ATOM   2169  C  CB    . VAL A 1 1721 ? 162.473 175.579 179.158 1.00 4.75  ? 1721 VAL A CB    1 
ATOM   2170  C  CG1   . VAL A 1 1721 ? 161.744 174.427 179.823 1.00 4.39  ? 1721 VAL A CG1   1 
ATOM   2171  C  CG2   . VAL A 1 1721 ? 163.763 175.847 179.907 1.00 3.22  ? 1721 VAL A CG2   1 
ATOM   2172  N  N     . THR A 1 1722 ? 160.732 175.688 176.411 1.00 9.65  ? 1722 THR A N     1 
ATOM   2173  C  CA    . THR A 1 1722 ? 159.535 175.295 175.675 1.00 9.57  ? 1722 THR A CA    1 
ATOM   2174  C  C     . THR A 1 1722 ? 159.884 174.449 174.458 1.00 12.77 ? 1722 THR A C     1 
ATOM   2175  O  O     . THR A 1 1722 ? 159.224 173.440 174.182 1.00 21.37 ? 1722 THR A O     1 
ATOM   2176  C  CB    . THR A 1 1722 ? 158.745 176.535 175.253 1.00 9.43  ? 1722 THR A CB    1 
ATOM   2177  O  OG1   . THR A 1 1722 ? 158.356 177.274 176.416 1.00 13.35 ? 1722 THR A OG1   1 
ATOM   2178  C  CG2   . THR A 1 1722 ? 157.503 176.140 174.477 1.00 11.12 ? 1722 THR A CG2   1 
ATOM   2179  N  N     . GLU A 1 1723 ? 160.922 174.843 173.718 1.00 14.69 ? 1723 GLU A N     1 
ATOM   2180  C  CA    . GLU A 1 1723 ? 161.288 174.117 172.506 1.00 10.67 ? 1723 GLU A CA    1 
ATOM   2181  C  C     . GLU A 1 1723 ? 161.989 172.801 172.822 1.00 13.66 ? 1723 GLU A C     1 
ATOM   2182  O  O     . GLU A 1 1723 ? 161.731 171.784 172.167 1.00 14.51 ? 1723 GLU A O     1 
ATOM   2183  C  CB    . GLU A 1 1723 ? 162.171 174.995 171.619 1.00 9.23  ? 1723 GLU A CB    1 
ATOM   2184  C  CG    . GLU A 1 1723 ? 161.522 176.302 171.204 1.00 11.53 ? 1723 GLU A CG    1 
ATOM   2185  C  CD    . GLU A 1 1723 ? 162.382 177.099 170.243 1.00 19.15 ? 1723 GLU A CD    1 
ATOM   2186  O  OE1   . GLU A 1 1723 ? 163.437 176.584 169.820 1.00 20.25 ? 1723 GLU A OE1   1 
ATOM   2187  O  OE2   . GLU A 1 1723 ? 162.002 178.242 169.914 1.00 22.31 ? 1723 GLU A OE2   1 
ATOM   2188  N  N     . VAL A 1 1724 ? 162.885 172.797 173.814 1.00 11.52 ? 1724 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 1724 ? 163.680 171.604 174.090 1.00 10.02 ? 1724 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 1724 ? 162.818 170.475 174.641 1.00 14.44 ? 1724 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 1724 ? 163.195 169.301 174.524 1.00 17.05 ? 1724 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 1724 ? 164.840 171.934 175.051 1.00 7.76  ? 1724 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 1724 ? 164.319 172.314 176.423 1.00 8.94  ? 1724 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 1724 ? 165.831 170.780 175.138 1.00 7.84  ? 1724 VAL A CG2   1 
ATOM   2195  N  N     . GLU A 1 1725 ? 161.662 170.792 175.232 1.00 15.45 ? 1725 GLU A N     1 
ATOM   2196  C  CA    . GLU A 1 1725 ? 160.779 169.748 175.742 1.00 15.42 ? 1725 GLU A CA    1 
ATOM   2197  C  C     . GLU A 1 1725 ? 160.263 168.851 174.626 1.00 19.09 ? 1725 GLU A C     1 
ATOM   2198  O  O     . GLU A 1 1725 ? 160.016 167.661 174.855 1.00 25.85 ? 1725 GLU A O     1 
ATOM   2199  C  CB    . GLU A 1 1725 ? 159.609 170.366 176.504 1.00 16.20 ? 1725 GLU A CB    1 
ATOM   2200  C  CG    . GLU A 1 1725 ? 159.965 170.863 177.893 1.00 16.10 ? 1725 GLU A CG    1 
ATOM   2201  C  CD    . GLU A 1 1725 ? 158.848 171.664 178.526 1.00 20.93 ? 1725 GLU A CD    1 
ATOM   2202  O  OE1   . GLU A 1 1725 ? 158.411 172.663 177.915 1.00 21.02 ? 1725 GLU A OE1   1 
ATOM   2203  O  OE2   . GLU A 1 1725 ? 158.414 171.302 179.638 1.00 25.87 ? 1725 GLU A OE2   1 
ATOM   2204  N  N     . ILE A 1 1726 ? 160.090 169.398 173.420 1.00 17.01 ? 1726 ILE A N     1 
ATOM   2205  C  CA    . ILE A 1 1726 ? 159.684 168.578 172.282 1.00 17.32 ? 1726 ILE A CA    1 
ATOM   2206  C  C     . ILE A 1 1726 ? 160.744 167.528 171.979 1.00 18.31 ? 1726 ILE A C     1 
ATOM   2207  O  O     . ILE A 1 1726 ? 160.430 166.363 171.710 1.00 23.06 ? 1726 ILE A O     1 
ATOM   2208  C  CB    . ILE A 1 1726 ? 159.404 169.466 171.055 1.00 14.34 ? 1726 ILE A CB    1 
ATOM   2209  C  CG1   . ILE A 1 1726 ? 158.556 170.679 171.451 1.00 15.25 ? 1726 ILE A CG1   1 
ATOM   2210  C  CG2   . ILE A 1 1726 ? 158.727 168.665 169.959 1.00 20.38 ? 1726 ILE A CG2   1 
ATOM   2211  C  CD1   . ILE A 1 1726 ? 157.230 170.328 172.079 1.00 17.83 ? 1726 ILE A CD1   1 
ATOM   2212  N  N     . PHE A 1 1727 ? 162.019 167.924 172.019 1.00 17.18 ? 1727 PHE A N     1 
ATOM   2213  C  CA    . PHE A 1 1727 ? 163.105 166.975 171.803 1.00 12.42 ? 1727 PHE A CA    1 
ATOM   2214  C  C     . PHE A 1 1727 ? 163.130 165.907 172.888 1.00 15.14 ? 1727 PHE A C     1 
ATOM   2215  O  O     . PHE A 1 1727 ? 163.378 164.729 172.603 1.00 20.89 ? 1727 PHE A O     1 
ATOM   2216  C  CB    . PHE A 1 1727 ? 164.439 167.717 171.748 1.00 9.29  ? 1727 PHE A CB    1 
ATOM   2217  C  CG    . PHE A 1 1727 ? 164.507 168.756 170.672 1.00 11.17 ? 1727 PHE A CG    1 
ATOM   2218  C  CD1   . PHE A 1 1727 ? 163.956 168.515 169.424 1.00 10.85 ? 1727 PHE A CD1   1 
ATOM   2219  C  CD2   . PHE A 1 1727 ? 165.108 169.981 170.911 1.00 10.28 ? 1727 PHE A CD2   1 
ATOM   2220  C  CE1   . PHE A 1 1727 ? 164.016 169.473 168.431 1.00 9.54  ? 1727 PHE A CE1   1 
ATOM   2221  C  CE2   . PHE A 1 1727 ? 165.171 170.940 169.921 1.00 6.55  ? 1727 PHE A CE2   1 
ATOM   2222  C  CZ    . PHE A 1 1727 ? 164.624 170.686 168.680 1.00 7.84  ? 1727 PHE A CZ    1 
ATOM   2223  N  N     . GLY A 1 1728 ? 162.890 166.300 174.137 1.00 17.30 ? 1728 GLY A N     1 
ATOM   2224  C  CA    . GLY A 1 1728 ? 162.799 165.326 175.204 1.00 14.30 ? 1728 GLY A CA    1 
ATOM   2225  C  C     . GLY A 1 1728 ? 161.601 164.413 175.036 1.00 17.64 ? 1728 GLY A C     1 
ATOM   2226  O  O     . GLY A 1 1728 ? 160.580 164.789 174.459 1.00 21.32 ? 1728 GLY A O     1 
ATOM   2227  N  N     . LYS A 1 1729 ? 161.741 163.195 175.559 1.00 21.43 ? 1729 LYS A N     1 
ATOM   2228  C  CA    . LYS A 1 1729 ? 160.758 162.111 175.427 1.00 28.16 ? 1729 LYS A CA    1 
ATOM   2229  C  C     . LYS A 1 1729 ? 160.153 162.068 174.022 1.00 31.58 ? 1729 LYS A C     1 
ATOM   2230  O  O     . LYS A 1 1729 ? 158.937 161.981 173.831 1.00 33.40 ? 1729 LYS A O     1 
ATOM   2231  C  CB    . LYS A 1 1729 ? 159.673 162.198 176.511 1.00 26.95 ? 1729 LYS A CB    1 
ATOM   2232  C  CG    . LYS A 1 1729 ? 158.854 163.484 176.568 1.00 26.27 ? 1729 LYS A CG    1 
ATOM   2233  C  CD    . LYS A 1 1729 ? 157.879 163.472 177.734 1.00 26.35 ? 1729 LYS A CD    1 
ATOM   2234  C  CE    . LYS A 1 1729 ? 158.595 163.206 179.050 1.00 21.55 ? 1729 LYS A CE    1 
ATOM   2235  N  NZ    . LYS A 1 1729 ? 157.660 163.235 180.207 1.00 28.31 ? 1729 LYS A NZ    1 
ATOM   2236  N  N     . ALA A 1 1730 ? 161.032 162.123 173.025 1.00 27.64 ? 1730 ALA A N     1 
ATOM   2237  C  CA    . ALA A 1 1730 ? 160.665 161.979 171.625 1.00 22.32 ? 1730 ALA A CA    1 
ATOM   2238  C  C     . ALA A 1 1730 ? 161.430 160.805 171.031 1.00 28.85 ? 1730 ALA A C     1 
ATOM   2239  O  O     . ALA A 1 1730 ? 162.622 160.628 171.303 1.00 28.80 ? 1730 ALA A O     1 
ATOM   2240  C  CB    . ALA A 1 1730 ? 160.961 163.254 170.835 1.00 21.40 ? 1730 ALA A CB    1 
ATOM   2241  N  N     . THR A 1 1731 ? 160.733 159.995 170.230 1.00 22.58 ? 1731 THR A N     1 
ATOM   2242  C  CA    . THR A 1 1731 ? 161.347 158.788 169.685 1.00 22.61 ? 1731 THR A CA    1 
ATOM   2243  C  C     . THR A 1 1731 ? 162.477 159.120 168.717 1.00 28.23 ? 1731 THR A C     1 
ATOM   2244  O  O     . THR A 1 1731 ? 163.539 158.488 168.756 1.00 31.87 ? 1731 THR A O     1 
ATOM   2245  C  CB    . THR A 1 1731 ? 160.288 157.928 168.992 1.00 26.53 ? 1731 THR A CB    1 
ATOM   2246  O  OG1   . THR A 1 1731 ? 159.707 158.660 167.906 1.00 34.17 ? 1731 THR A OG1   1 
ATOM   2247  C  CG2   . THR A 1 1731 ? 159.195 157.540 169.976 1.00 26.01 ? 1731 THR A CG2   1 
ATOM   2248  N  N     . SER A 1 1732 ? 162.273 160.101 167.842 1.00 22.50 ? 1732 SER A N     1 
ATOM   2249  C  CA    . SER A 1 1732 ? 163.254 160.454 166.827 1.00 21.66 ? 1732 SER A CA    1 
ATOM   2250  C  C     . SER A 1 1732 ? 163.423 161.963 166.773 1.00 18.44 ? 1732 SER A C     1 
ATOM   2251  O  O     . SER A 1 1732 ? 162.442 162.710 166.816 1.00 24.75 ? 1732 SER A O     1 
ATOM   2252  C  CB    . SER A 1 1732 ? 162.841 159.928 165.446 1.00 26.47 ? 1732 SER A CB    1 
ATOM   2253  O  OG    . SER A 1 1732 ? 161.605 160.487 165.040 1.00 28.51 ? 1732 SER A OG    1 
ATOM   2254  N  N     . ILE A 1 1733 ? 164.672 162.405 166.662 1.00 11.92 ? 1733 ILE A N     1 
ATOM   2255  C  CA    . ILE A 1 1733 ? 165.006 163.819 166.575 1.00 9.78  ? 1733 ILE A CA    1 
ATOM   2256  C  C     . ILE A 1 1733 ? 165.578 164.096 165.192 1.00 14.54 ? 1733 ILE A C     1 
ATOM   2257  O  O     . ILE A 1 1733 ? 166.549 163.454 164.773 1.00 21.41 ? 1733 ILE A O     1 
ATOM   2258  C  CB    . ILE A 1 1733 ? 165.995 164.238 167.672 1.00 11.45 ? 1733 ILE A CB    1 
ATOM   2259  C  CG1   . ILE A 1 1733 ? 165.371 164.020 169.050 1.00 15.99 ? 1733 ILE A CG1   1 
ATOM   2260  C  CG2   . ILE A 1 1733 ? 166.427 165.687 167.477 1.00 11.73 ? 1733 ILE A CG2   1 
ATOM   2261  C  CD1   . ILE A 1 1733 ? 166.176 164.596 170.173 1.00 6.96  ? 1733 ILE A CD1   1 
ATOM   2262  N  N     . ASP A 1 1734 ? 164.976 165.042 164.491 1.00 12.84 ? 1734 ASP A N     1 
ATOM   2263  C  CA    . ASP A 1 1734 ? 165.524 165.507 163.225 1.00 14.99 ? 1734 ASP A CA    1 
ATOM   2264  C  C     . ASP A 1 1734 ? 166.745 166.375 163.494 1.00 16.62 ? 1734 ASP A C     1 
ATOM   2265  O  O     . ASP A 1 1734 ? 166.644 167.351 164.249 1.00 11.68 ? 1734 ASP A O     1 
ATOM   2266  C  CB    . ASP A 1 1734 ? 164.470 166.291 162.451 1.00 14.86 ? 1734 ASP A CB    1 
ATOM   2267  C  CG    . ASP A 1 1734 ? 165.059 167.087 161.308 1.00 23.09 ? 1734 ASP A CG    1 
ATOM   2268  O  OD1   . ASP A 1 1734 ? 165.716 166.482 160.435 1.00 23.14 ? 1734 ASP A OD1   1 
ATOM   2269  O  OD2   . ASP A 1 1734 ? 164.871 168.320 161.284 1.00 23.56 ? 1734 ASP A OD2   1 
ATOM   2270  N  N     . PRO A 1 1735 ? 167.909 166.061 162.919 1.00 12.79 ? 1735 PRO A N     1 
ATOM   2271  C  CA    . PRO A 1 1735 ? 169.098 166.884 163.195 1.00 13.66 ? 1735 PRO A CA    1 
ATOM   2272  C  C     . PRO A 1 1735 ? 168.939 168.342 162.805 1.00 15.25 ? 1735 PRO A C     1 
ATOM   2273  O  O     . PRO A 1 1735 ? 169.448 169.221 163.510 1.00 12.35 ? 1735 PRO A O     1 
ATOM   2274  C  CB    . PRO A 1 1735 ? 170.197 166.188 162.377 1.00 15.58 ? 1735 PRO A CB    1 
ATOM   2275  C  CG    . PRO A 1 1735 ? 169.723 164.781 162.235 1.00 15.36 ? 1735 PRO A CG    1 
ATOM   2276  C  CD    . PRO A 1 1735 ? 168.232 164.876 162.106 1.00 15.16 ? 1735 PRO A CD    1 
ATOM   2277  N  N     . ASN A 1 1736 ? 168.237 168.629 161.705 1.00 15.85 ? 1736 ASN A N     1 
ATOM   2278  C  CA    . ASN A 1 1736 ? 168.101 170.012 161.257 1.00 15.86 ? 1736 ASN A CA    1 
ATOM   2279  C  C     . ASN A 1 1736 ? 167.350 170.859 162.277 1.00 14.77 ? 1736 ASN A C     1 
ATOM   2280  O  O     . ASN A 1 1736 ? 167.751 171.993 162.566 1.00 15.92 ? 1736 ASN A O     1 
ATOM   2281  C  CB    . ASN A 1 1736 ? 167.401 170.056 159.899 1.00 17.75 ? 1736 ASN A CB    1 
ATOM   2282  C  CG    . ASN A 1 1736 ? 168.104 169.213 158.855 1.00 21.48 ? 1736 ASN A CG    1 
ATOM   2283  O  OD1   . ASN A 1 1736 ? 169.313 169.333 158.657 1.00 16.05 ? 1736 ASN A OD1   1 
ATOM   2284  N  ND2   . ASN A 1 1736 ? 167.348 168.356 158.176 1.00 23.53 ? 1736 ASN A ND2   1 
ATOM   2285  N  N     . THR A 1 1737 ? 166.261 170.330 162.836 1.00 12.21 ? 1737 THR A N     1 
ATOM   2286  C  CA    . THR A 1 1737 ? 165.540 171.057 163.872 1.00 12.35 ? 1737 THR A CA    1 
ATOM   2287  C  C     . THR A 1 1737 ? 166.389 171.214 165.129 1.00 10.27 ? 1737 THR A C     1 
ATOM   2288  O  O     . THR A 1 1737 ? 166.424 172.294 165.732 1.00 13.14 ? 1737 THR A O     1 
ATOM   2289  C  CB    . THR A 1 1737 ? 164.225 170.344 164.197 1.00 12.11 ? 1737 THR A CB    1 
ATOM   2290  O  OG1   . THR A 1 1737 ? 163.438 170.229 163.007 1.00 19.77 ? 1737 THR A OG1   1 
ATOM   2291  C  CG2   . THR A 1 1737 ? 163.441 171.123 165.237 1.00 12.83 ? 1737 THR A CG2   1 
ATOM   2292  N  N     . TYR A 1 1738 ? 167.085 170.150 165.534 1.00 9.11  ? 1738 TYR A N     1 
ATOM   2293  C  CA    . TYR A 1 1738 ? 167.902 170.202 166.742 1.00 4.63  ? 1738 TYR A CA    1 
ATOM   2294  C  C     . TYR A 1 1738 ? 169.073 171.165 166.585 1.00 7.83  ? 1738 TYR A C     1 
ATOM   2295  O  O     . TYR A 1 1738 ? 169.390 171.920 167.511 1.00 8.58  ? 1738 TYR A O     1 
ATOM   2296  C  CB    . TYR A 1 1738 ? 168.395 168.799 167.092 1.00 7.86  ? 1738 TYR A CB    1 
ATOM   2297  C  CG    . TYR A 1 1738 ? 168.912 168.667 168.500 1.00 6.57  ? 1738 TYR A CG    1 
ATOM   2298  C  CD1   . TYR A 1 1738 ? 168.061 168.788 169.587 1.00 4.11  ? 1738 TYR A CD1   1 
ATOM   2299  C  CD2   . TYR A 1 1738 ? 170.253 168.414 168.745 1.00 4.93  ? 1738 TYR A CD2   1 
ATOM   2300  C  CE1   . TYR A 1 1738 ? 168.530 168.668 170.878 1.00 6.24  ? 1738 TYR A CE1   1 
ATOM   2301  C  CE2   . TYR A 1 1738 ? 170.733 168.292 170.031 1.00 4.22  ? 1738 TYR A CE2   1 
ATOM   2302  C  CZ    . TYR A 1 1738 ? 169.866 168.420 171.093 1.00 3.73  ? 1738 TYR A CZ    1 
ATOM   2303  O  OH    . TYR A 1 1738 ? 170.342 168.299 172.376 1.00 8.03  ? 1738 TYR A OH    1 
ATOM   2304  N  N     . ILE A 1 1739 ? 169.732 171.150 165.425 1.00 10.79 ? 1739 ILE A N     1 
ATOM   2305  C  CA    . ILE A 1 1739 ? 170.823 172.088 165.179 1.00 7.67  ? 1739 ILE A CA    1 
ATOM   2306  C  C     . ILE A 1 1739 ? 170.292 173.515 165.118 1.00 8.32  ? 1739 ILE A C     1 
ATOM   2307  O  O     . ILE A 1 1739 ? 170.956 174.459 165.564 1.00 10.64 ? 1739 ILE A O     1 
ATOM   2308  C  CB    . ILE A 1 1739 ? 171.581 171.695 163.896 1.00 9.38  ? 1739 ILE A CB    1 
ATOM   2309  C  CG1   . ILE A 1 1739 ? 172.315 170.368 164.095 1.00 10.41 ? 1739 ILE A CG1   1 
ATOM   2310  C  CG2   . ILE A 1 1739 ? 172.557 172.781 163.485 1.00 4.52  ? 1739 ILE A CG2   1 
ATOM   2311  C  CD1   . ILE A 1 1739 ? 173.501 170.455 165.029 1.00 10.71 ? 1739 ILE A CD1   1 
ATOM   2312  N  N     . THR A 1 1740 ? 169.085 173.694 164.580 1.00 8.94  ? 1740 THR A N     1 
ATOM   2313  C  CA    . THR A 1 1740 ? 168.470 175.016 164.558 1.00 7.45  ? 1740 THR A CA    1 
ATOM   2314  C  C     . THR A 1 1740 ? 168.252 175.546 165.970 1.00 7.87  ? 1740 THR A C     1 
ATOM   2315  O  O     . THR A 1 1740 ? 168.513 176.722 166.246 1.00 10.21 ? 1740 THR A O     1 
ATOM   2316  C  CB    . THR A 1 1740 ? 167.147 174.965 163.794 1.00 5.41  ? 1740 THR A CB    1 
ATOM   2317  O  OG1   . THR A 1 1740 ? 167.390 174.549 162.445 1.00 16.90 ? 1740 THR A OG1   1 
ATOM   2318  C  CG2   . THR A 1 1740 ? 166.478 176.329 163.781 1.00 6.76  ? 1740 THR A CG2   1 
ATOM   2319  N  N     . TRP A 1 1741 ? 167.782 174.689 166.880 1.00 4.95  ? 1741 TRP A N     1 
ATOM   2320  C  CA    . TRP A 1 1741 ? 167.556 175.121 168.256 1.00 3.49  ? 1741 TRP A CA    1 
ATOM   2321  C  C     . TRP A 1 1741 ? 168.872 175.428 168.968 1.00 4.02  ? 1741 TRP A C     1 
ATOM   2322  O  O     . TRP A 1 1741 ? 168.942 176.358 169.775 1.00 5.66  ? 1741 TRP A O     1 
ATOM   2323  C  CB    . TRP A 1 1741 ? 166.762 174.060 169.015 1.00 3.58  ? 1741 TRP A CB    1 
ATOM   2324  C  CG    . TRP A 1 1741 ? 166.817 174.228 170.503 1.00 3.16  ? 1741 TRP A CG    1 
ATOM   2325  C  CD1   . TRP A 1 1741 ? 166.032 175.041 171.262 1.00 3.11  ? 1741 TRP A CD1   1 
ATOM   2326  C  CD2   . TRP A 1 1741 ? 167.703 173.565 171.408 1.00 2.23  ? 1741 TRP A CD2   1 
ATOM   2327  N  NE1   . TRP A 1 1741 ? 166.376 174.929 172.584 1.00 2.57  ? 1741 TRP A NE1   1 
ATOM   2328  C  CE2   . TRP A 1 1741 ? 167.402 174.028 172.701 1.00 2.98  ? 1741 TRP A CE2   1 
ATOM   2329  C  CE3   . TRP A 1 1741 ? 168.725 172.624 171.252 1.00 1.89  ? 1741 TRP A CE3   1 
ATOM   2330  C  CZ2   . TRP A 1 1741 ? 168.082 173.584 173.831 1.00 3.79  ? 1741 TRP A CZ2   1 
ATOM   2331  C  CZ3   . TRP A 1 1741 ? 169.399 172.187 172.373 1.00 2.09  ? 1741 TRP A CZ3   1 
ATOM   2332  C  CH2   . TRP A 1 1741 ? 169.075 172.665 173.647 1.00 2.15  ? 1741 TRP A CH2   1 
ATOM   2333  N  N     . ILE A 1 1742 ? 169.921 174.652 168.685 1.00 3.62  ? 1742 ILE A N     1 
ATOM   2334  C  CA    . ILE A 1 1742 ? 171.227 174.920 169.283 1.00 5.15  ? 1742 ILE A CA    1 
ATOM   2335  C  C     . ILE A 1 1742 ? 171.753 176.276 168.830 1.00 7.02  ? 1742 ILE A C     1 
ATOM   2336  O  O     . ILE A 1 1742 ? 172.287 177.053 169.631 1.00 8.89  ? 1742 ILE A O     1 
ATOM   2337  C  CB    . ILE A 1 1742 ? 172.215 173.789 168.939 1.00 6.09  ? 1742 ILE A CB    1 
ATOM   2338  C  CG1   . ILE A 1 1742 ? 171.772 172.475 169.584 1.00 5.11  ? 1742 ILE A CG1   1 
ATOM   2339  C  CG2   . ILE A 1 1742 ? 173.623 174.151 169.377 1.00 2.42  ? 1742 ILE A CG2   1 
ATOM   2340  C  CD1   . ILE A 1 1742 ? 172.516 171.270 169.074 1.00 5.05  ? 1742 ILE A CD1   1 
ATOM   2341  N  N     . ASP A 1 1743 ? 171.608 176.582 167.540 1.00 7.45  ? 1743 ASP A N     1 
ATOM   2342  C  CA    . ASP A 1 1743 ? 172.134 177.831 167.004 1.00 7.90  ? 1743 ASP A CA    1 
ATOM   2343  C  C     . ASP A 1 1743 ? 171.357 179.042 167.504 1.00 8.85  ? 1743 ASP A C     1 
ATOM   2344  O  O     . ASP A 1 1743 ? 171.924 180.134 167.622 1.00 8.39  ? 1743 ASP A O     1 
ATOM   2345  C  CB    . ASP A 1 1743 ? 172.114 177.785 165.476 1.00 9.39  ? 1743 ASP A CB    1 
ATOM   2346  C  CG    . ASP A 1 1743 ? 173.362 177.162 164.899 1.00 9.58  ? 1743 ASP A CG    1 
ATOM   2347  O  OD1   . ASP A 1 1743 ? 174.373 177.081 165.623 1.00 16.11 ? 1743 ASP A OD1   1 
ATOM   2348  O  OD2   . ASP A 1 1743 ? 173.330 176.752 163.721 1.00 17.24 ? 1743 ASP A OD2   1 
ATOM   2349  N  N     . LYS A 1 1744 ? 170.066 178.872 167.797 1.00 4.92  ? 1744 LYS A N     1 
ATOM   2350  C  CA    . LYS A 1 1744 ? 169.226 180.010 168.155 1.00 4.39  ? 1744 LYS A CA    1 
ATOM   2351  C  C     . LYS A 1 1744 ? 169.533 180.538 169.552 1.00 4.59  ? 1744 LYS A C     1 
ATOM   2352  O  O     . LYS A 1 1744 ? 169.447 181.749 169.783 1.00 6.72  ? 1744 LYS A O     1 
ATOM   2353  C  CB    . LYS A 1 1744 ? 167.753 179.621 168.041 1.00 5.91  ? 1744 LYS A CB    1 
ATOM   2354  C  CG    . LYS A 1 1744 ? 166.771 180.705 168.462 1.00 6.08  ? 1744 LYS A CG    1 
ATOM   2355  C  CD    . LYS A 1 1744 ? 165.357 180.157 168.535 1.00 4.76  ? 1744 LYS A CD    1 
ATOM   2356  C  CE    . LYS A 1 1744 ? 164.336 181.176 168.069 1.00 11.22 ? 1744 LYS A CE    1 
ATOM   2357  N  NZ    . LYS A 1 1744 ? 163.709 181.901 169.208 1.00 17.50 ? 1744 LYS A NZ    1 
ATOM   2358  N  N     . TYR A 1 1745 ? 169.892 179.666 170.488 1.00 5.10  ? 1745 TYR A N     1 
ATOM   2359  C  CA    . TYR A 1 1745 ? 170.066 180.064 171.878 1.00 3.17  ? 1745 TYR A CA    1 
ATOM   2360  C  C     . TYR A 1 1745 ? 171.532 180.001 172.284 1.00 2.67  ? 1745 TYR A C     1 
ATOM   2361  O  O     . TYR A 1 1745 ? 172.361 179.372 171.622 1.00 6.02  ? 1745 TYR A O     1 
ATOM   2362  C  CB    . TYR A 1 1745 ? 169.217 179.186 172.803 1.00 1.41  ? 1745 TYR A CB    1 
ATOM   2363  C  CG    . TYR A 1 1745 ? 167.738 179.372 172.581 1.00 2.37  ? 1745 TYR A CG    1 
ATOM   2364  C  CD1   . TYR A 1 1745 ? 167.068 180.464 173.113 1.00 2.99  ? 1745 TYR A CD1   1 
ATOM   2365  C  CD2   . TYR A 1 1745 ? 167.015 178.465 171.823 1.00 3.44  ? 1745 TYR A CD2   1 
ATOM   2366  C  CE1   . TYR A 1 1745 ? 165.719 180.643 172.902 1.00 3.27  ? 1745 TYR A CE1   1 
ATOM   2367  C  CE2   . TYR A 1 1745 ? 165.665 178.635 171.609 1.00 4.37  ? 1745 TYR A CE2   1 
ATOM   2368  C  CZ    . TYR A 1 1745 ? 165.022 179.725 172.148 1.00 4.22  ? 1745 TYR A CZ    1 
ATOM   2369  O  OH    . TYR A 1 1745 ? 163.675 179.895 171.935 1.00 8.63  ? 1745 TYR A OH    1 
ATOM   2370  N  N     . GLN A 1 1746 ? 171.837 180.677 173.387 1.00 1.77  ? 1746 GLN A N     1 
ATOM   2371  C  CA    . GLN A 1 1746 ? 173.206 180.805 173.855 1.00 2.31  ? 1746 GLN A CA    1 
ATOM   2372  C  C     . GLN A 1 1746 ? 173.718 179.476 174.402 1.00 2.83  ? 1746 GLN A C     1 
ATOM   2373  O  O     . GLN A 1 1746 ? 172.949 178.585 174.770 1.00 9.22  ? 1746 GLN A O     1 
ATOM   2374  C  CB    . GLN A 1 1746 ? 173.302 181.896 174.920 1.00 2.86  ? 1746 GLN A CB    1 
ATOM   2375  C  CG    . GLN A 1 1746 ? 173.304 183.307 174.357 1.00 3.02  ? 1746 GLN A CG    1 
ATOM   2376  C  CD    . GLN A 1 1746 ? 171.926 183.781 173.931 1.00 2.72  ? 1746 GLN A CD    1 
ATOM   2377  O  OE1   . GLN A 1 1746 ? 170.926 183.100 174.152 1.00 3.36  ? 1746 GLN A OE1   1 
ATOM   2378  N  NE2   . GLN A 1 1746 ? 171.870 184.950 173.308 1.00 2.86  ? 1746 GLN A NE2   1 
ATOM   2379  N  N     . ALA A 1 1747 ? 175.046 179.354 174.453 1.00 2.13  ? 1747 ALA A N     1 
ATOM   2380  C  CA    . ALA A 1 1747 ? 175.659 178.097 174.867 1.00 2.42  ? 1747 ALA A CA    1 
ATOM   2381  C  C     . ALA A 1 1747 ? 175.265 177.725 176.291 1.00 2.30  ? 1747 ALA A C     1 
ATOM   2382  O  O     . ALA A 1 1747 ? 174.950 176.563 176.571 1.00 3.36  ? 1747 ALA A O     1 
ATOM   2383  C  CB    . ALA A 1 1747 ? 177.179 178.188 174.738 1.00 2.00  ? 1747 ALA A CB    1 
ATOM   2384  N  N     . GLN A 1 1748 ? 175.275 178.697 177.202 1.00 2.49  ? 1748 GLN A N     1 
ATOM   2385  C  CA    . GLN A 1 1748 ? 174.899 178.419 178.584 1.00 1.66  ? 1748 GLN A CA    1 
ATOM   2386  C  C     . GLN A 1 1748 ? 173.439 177.991 178.701 1.00 1.77  ? 1748 GLN A C     1 
ATOM   2387  O  O     . GLN A 1 1748 ? 173.120 177.107 179.505 1.00 1.58  ? 1748 GLN A O     1 
ATOM   2388  C  CB    . GLN A 1 1748 ? 175.188 179.642 179.455 1.00 1.32  ? 1748 GLN A CB    1 
ATOM   2389  C  CG    . GLN A 1 1748 ? 174.364 180.866 179.111 1.00 3.37  ? 1748 GLN A CG    1 
ATOM   2390  C  CD    . GLN A 1 1748 ? 174.724 182.066 179.953 1.00 4.22  ? 1748 GLN A CD    1 
ATOM   2391  O  OE1   . GLN A 1 1748 ? 175.563 181.985 180.845 1.00 2.39  ? 1748 GLN A OE1   1 
ATOM   2392  N  NE2   . GLN A 1 1748 ? 174.109 183.197 179.653 1.00 7.74  ? 1748 GLN A NE2   1 
ATOM   2393  N  N     . LEU A 1 1749 ? 172.545 178.594 177.919 1.00 2.51  ? 1749 LEU A N     1 
ATOM   2394  C  CA    . LEU A 1 1749 ? 171.133 178.242 177.989 1.00 2.00  ? 1749 LEU A CA    1 
ATOM   2395  C  C     . LEU A 1 1749 ? 170.835 176.915 177.305 1.00 2.42  ? 1749 LEU A C     1 
ATOM   2396  O  O     . LEU A 1 1749 ? 169.895 176.219 177.701 1.00 1.95  ? 1749 LEU A O     1 
ATOM   2397  C  CB    . LEU A 1 1749 ? 170.287 179.350 177.364 1.00 2.45  ? 1749 LEU A CB    1 
ATOM   2398  C  CG    . LEU A 1 1749 ? 170.309 180.700 178.076 1.00 3.73  ? 1749 LEU A CG    1 
ATOM   2399  C  CD1   . LEU A 1 1749 ? 169.177 181.567 177.572 1.00 2.90  ? 1749 LEU A CD1   1 
ATOM   2400  C  CD2   . LEU A 1 1749 ? 170.218 180.520 179.583 1.00 2.60  ? 1749 LEU A CD2   1 
ATOM   2401  N  N     . VAL A 1 1750 ? 171.612 176.558 176.281 1.00 2.19  ? 1750 VAL A N     1 
ATOM   2402  C  CA    . VAL A 1 1750 ? 171.396 175.297 175.578 1.00 2.05  ? 1750 VAL A CA    1 
ATOM   2403  C  C     . VAL A 1 1750 ? 171.671 174.118 176.503 1.00 1.28  ? 1750 VAL A C     1 
ATOM   2404  O  O     . VAL A 1 1750 ? 170.890 173.162 176.572 1.00 2.74  ? 1750 VAL A O     1 
ATOM   2405  C  CB    . VAL A 1 1750 ? 172.261 175.246 174.306 1.00 2.38  ? 1750 VAL A CB    1 
ATOM   2406  C  CG1   . VAL A 1 1750 ? 172.393 173.831 173.809 1.00 2.46  ? 1750 VAL A CG1   1 
ATOM   2407  C  CG2   . VAL A 1 1750 ? 171.655 176.121 173.226 1.00 1.81  ? 1750 VAL A CG2   1 
ATOM   2408  N  N     . VAL A 1 1751 ? 172.786 174.168 177.234 1.00 1.11  ? 1751 VAL A N     1 
ATOM   2409  C  CA    . VAL A 1 1751 ? 173.083 173.118 178.201 1.00 1.66  ? 1751 VAL A CA    1 
ATOM   2410  C  C     . VAL A 1 1751 ? 172.093 173.164 179.357 1.00 0.96  ? 1751 VAL A C     1 
ATOM   2411  O  O     . VAL A 1 1751 ? 171.638 172.124 179.844 1.00 1.65  ? 1751 VAL A O     1 
ATOM   2412  C  CB    . VAL A 1 1751 ? 174.539 173.237 178.686 1.00 1.74  ? 1751 VAL A CB    1 
ATOM   2413  C  CG1   . VAL A 1 1751 ? 174.790 172.313 179.868 1.00 2.06  ? 1751 VAL A CG1   1 
ATOM   2414  C  CG2   . VAL A 1 1751 ? 175.489 172.915 177.554 1.00 0.98  ? 1751 VAL A CG2   1 
ATOM   2415  N  N     . LEU A 1 1752 ? 171.733 174.369 179.800 1.00 1.04  ? 1752 LEU A N     1 
ATOM   2416  C  CA    . LEU A 1 1752 ? 170.752 174.512 180.870 1.00 0.76  ? 1752 LEU A CA    1 
ATOM   2417  C  C     . LEU A 1 1752 ? 169.398 173.947 180.458 1.00 0.79  ? 1752 LEU A C     1 
ATOM   2418  O  O     . LEU A 1 1752 ? 168.717 173.301 181.261 1.00 0.96  ? 1752 LEU A O     1 
ATOM   2419  C  CB    . LEU A 1 1752 ? 170.630 175.983 181.257 1.00 0.79  ? 1752 LEU A CB    1 
ATOM   2420  C  CG    . LEU A 1 1752 ? 170.102 176.335 182.644 1.00 0.52  ? 1752 LEU A CG    1 
ATOM   2421  C  CD1   . LEU A 1 1752 ? 170.922 175.653 183.723 1.00 0.34  ? 1752 LEU A CD1   1 
ATOM   2422  C  CD2   . LEU A 1 1752 ? 170.120 177.841 182.820 1.00 0.38  ? 1752 LEU A CD2   1 
ATOM   2423  N  N     . SER A 1 1753 ? 168.987 174.187 179.212 1.00 2.29  ? 1753 SER A N     1 
ATOM   2424  C  CA    . SER A 1 1753 ? 167.720 173.646 178.732 1.00 2.08  ? 1753 SER A CA    1 
ATOM   2425  C  C     . SER A 1 1753 ? 167.750 172.125 178.676 1.00 1.26  ? 1753 SER A C     1 
ATOM   2426  O  O     . SER A 1 1753 ? 166.753 171.465 178.994 1.00 0.99  ? 1753 SER A O     1 
ATOM   2427  C  CB    . SER A 1 1753 ? 167.388 174.229 177.360 1.00 1.23  ? 1753 SER A CB    1 
ATOM   2428  O  OG    . SER A 1 1753 ? 167.070 175.601 177.466 1.00 4.35  ? 1753 SER A OG    1 
ATOM   2429  N  N     . ALA A 1 1754 ? 168.879 171.549 178.261 1.00 1.21  ? 1754 ALA A N     1 
ATOM   2430  C  CA    . ALA A 1 1754 ? 168.995 170.096 178.221 1.00 1.45  ? 1754 ALA A CA    1 
ATOM   2431  C  C     . ALA A 1 1754 ? 168.910 169.495 179.618 1.00 1.20  ? 1754 ALA A C     1 
ATOM   2432  O  O     . ALA A 1 1754 ? 168.283 168.447 179.812 1.00 1.96  ? 1754 ALA A O     1 
ATOM   2433  C  CB    . ALA A 1 1754 ? 170.302 169.691 177.539 1.00 1.12  ? 1754 ALA A CB    1 
ATOM   2434  N  N     . GLN A 1 1755 ? 169.542 170.138 180.601 1.00 0.73  ? 1755 GLN A N     1 
ATOM   2435  C  CA    . GLN A 1 1755 ? 169.485 169.636 181.970 1.00 0.60  ? 1755 GLN A CA    1 
ATOM   2436  C  C     . GLN A 1 1755 ? 168.073 169.719 182.532 1.00 0.94  ? 1755 GLN A C     1 
ATOM   2437  O  O     . GLN A 1 1755 ? 167.626 168.811 183.242 1.00 8.31  ? 1755 GLN A O     1 
ATOM   2438  C  CB    . GLN A 1 1755 ? 170.465 170.408 182.853 1.00 0.57  ? 1755 GLN A CB    1 
ATOM   2439  C  CG    . GLN A 1 1755 ? 171.908 170.269 182.422 1.00 1.52  ? 1755 GLN A CG    1 
ATOM   2440  C  CD    . GLN A 1 1755 ? 172.858 171.091 183.266 1.00 0.85  ? 1755 GLN A CD    1 
ATOM   2441  O  OE1   . GLN A 1 1755 ? 172.722 172.307 183.368 1.00 0.88  ? 1755 GLN A OE1   1 
ATOM   2442  N  NE2   . GLN A 1 1755 ? 173.836 170.429 183.869 1.00 0.83  ? 1755 GLN A NE2   1 
ATOM   2443  N  N     . ILE A 1 1756 ? 167.355 170.803 182.228 1.00 0.68  ? 1756 ILE A N     1 
ATOM   2444  C  CA    . ILE A 1 1756 ? 165.984 170.956 182.709 1.00 0.74  ? 1756 ILE A CA    1 
ATOM   2445  C  C     . ILE A 1 1756 ? 165.093 169.866 182.129 1.00 1.46  ? 1756 ILE A C     1 
ATOM   2446  O  O     . ILE A 1 1756 ? 164.307 169.234 182.844 1.00 10.69 ? 1756 ILE A O     1 
ATOM   2447  C  CB    . ILE A 1 1756 ? 165.453 172.361 182.373 1.00 2.05  ? 1756 ILE A CB    1 
ATOM   2448  C  CG1   . ILE A 1 1756 ? 166.136 173.415 183.244 1.00 1.17  ? 1756 ILE A CG1   1 
ATOM   2449  C  CG2   . ILE A 1 1756 ? 163.944 172.424 182.548 1.00 1.00  ? 1756 ILE A CG2   1 
ATOM   2450  C  CD1   . ILE A 1 1756 ? 166.087 174.804 182.665 1.00 1.08  ? 1756 ILE A CD1   1 
ATOM   2451  N  N     . ALA A 1 1757 ? 165.204 169.628 180.820 1.00 1.41  ? 1757 ALA A N     1 
ATOM   2452  C  CA    . ALA A 1 1757 ? 164.359 168.630 180.175 1.00 1.19  ? 1757 ALA A CA    1 
ATOM   2453  C  C     . ALA A 1 1757 ? 164.635 167.233 180.717 1.00 2.71  ? 1757 ALA A C     1 
ATOM   2454  O  O     . ALA A 1 1757 ? 163.703 166.464 180.975 1.00 3.43  ? 1757 ALA A O     1 
ATOM   2455  C  CB    . ALA A 1 1757 ? 164.563 168.670 178.662 1.00 1.60  ? 1757 ALA A CB    1 
ATOM   2456  N  N     . TRP A 1 1758 ? 165.912 166.891 180.903 1.00 2.30  ? 1758 TRP A N     1 
ATOM   2457  C  CA    . TRP A 1 1758 ? 166.255 165.570 181.417 1.00 2.20  ? 1758 TRP A CA    1 
ATOM   2458  C  C     . TRP A 1 1758 ? 165.756 165.383 182.845 1.00 3.83  ? 1758 TRP A C     1 
ATOM   2459  O  O     . TRP A 1 1758 ? 165.253 164.310 183.196 1.00 6.83  ? 1758 TRP A O     1 
ATOM   2460  C  CB    . TRP A 1 1758 ? 167.764 165.356 181.339 1.00 2.35  ? 1758 TRP A CB    1 
ATOM   2461  C  CG    . TRP A 1 1758 ? 168.228 164.104 182.004 1.00 1.59  ? 1758 TRP A CG    1 
ATOM   2462  C  CD1   . TRP A 1 1758 ? 168.041 162.827 181.566 1.00 1.39  ? 1758 TRP A CD1   1 
ATOM   2463  C  CD2   . TRP A 1 1758 ? 168.956 164.005 183.231 1.00 1.18  ? 1758 TRP A CD2   1 
ATOM   2464  N  NE1   . TRP A 1 1758 ? 168.608 161.939 182.444 1.00 1.34  ? 1758 TRP A NE1   1 
ATOM   2465  C  CE2   . TRP A 1 1758 ? 169.177 162.637 183.476 1.00 0.93  ? 1758 TRP A CE2   1 
ATOM   2466  C  CE3   . TRP A 1 1758 ? 169.442 164.941 184.148 1.00 1.61  ? 1758 TRP A CE3   1 
ATOM   2467  C  CZ2   . TRP A 1 1758 ? 169.863 162.182 184.597 1.00 1.03  ? 1758 TRP A CZ2   1 
ATOM   2468  C  CZ3   . TRP A 1 1758 ? 170.122 164.488 185.258 1.00 4.21  ? 1758 TRP A CZ3   1 
ATOM   2469  C  CH2   . TRP A 1 1758 ? 170.326 163.122 185.474 1.00 1.53  ? 1758 TRP A CH2   1 
ATOM   2470  N  N     . SER A 1 1759 ? 165.888 166.415 183.682 1.00 2.90  ? 1759 SER A N     1 
ATOM   2471  C  CA    . SER A 1 1759 ? 165.429 166.309 185.065 1.00 2.08  ? 1759 SER A CA    1 
ATOM   2472  C  C     . SER A 1 1759 ? 163.926 166.075 185.133 1.00 3.65  ? 1759 SER A C     1 
ATOM   2473  O  O     . SER A 1 1759 ? 163.458 165.224 185.897 1.00 8.14  ? 1759 SER A O     1 
ATOM   2474  C  CB    . SER A 1 1759 ? 165.808 167.566 185.847 1.00 1.98  ? 1759 SER A CB    1 
ATOM   2475  O  OG    . SER A 1 1759 ? 167.161 167.531 186.258 1.00 2.60  ? 1759 SER A OG    1 
ATOM   2476  N  N     . GLU A 1 1760 ? 163.152 166.814 184.336 1.00 3.75  ? 1760 GLU A N     1 
ATOM   2477  C  CA    . GLU A 1 1760 ? 161.703 166.651 184.363 1.00 5.90  ? 1760 GLU A CA    1 
ATOM   2478  C  C     . GLU A 1 1760 ? 161.275 165.300 183.806 1.00 6.57  ? 1760 GLU A C     1 
ATOM   2479  O  O     . GLU A 1 1760 ? 160.259 164.749 184.241 1.00 11.28 ? 1760 GLU A O     1 
ATOM   2480  C  CB    . GLU A 1 1760 ? 161.031 167.791 183.597 1.00 12.09 ? 1760 GLU A CB    1 
ATOM   2481  C  CG    . GLU A 1 1760 ? 161.192 169.151 184.264 1.00 14.69 ? 1760 GLU A CG    1 
ATOM   2482  C  CD    . GLU A 1 1760 ? 160.534 170.275 183.485 1.00 22.63 ? 1760 GLU A CD    1 
ATOM   2483  O  OE1   . GLU A 1 1760 ? 160.056 170.027 182.360 1.00 27.85 ? 1760 GLU A OE1   1 
ATOM   2484  O  OE2   . GLU A 1 1760 ? 160.490 171.410 184.006 1.00 20.37 ? 1760 GLU A OE2   1 
ATOM   2485  N  N     . ASN A 1 1761 ? 162.025 164.756 182.845 1.00 4.52  ? 1761 ASN A N     1 
ATOM   2486  C  CA    . ASN A 1 1761 ? 161.728 163.415 182.348 1.00 6.68  ? 1761 ASN A CA    1 
ATOM   2487  C  C     . ASN A 1 1761 ? 161.946 162.362 183.426 1.00 7.45  ? 1761 ASN A C     1 
ATOM   2488  O  O     . ASN A 1 1761 ? 161.135 161.442 183.576 1.00 8.59  ? 1761 ASN A O     1 
ATOM   2489  C  CB    . ASN A 1 1761 ? 162.581 163.108 181.119 1.00 6.94  ? 1761 ASN A CB    1 
ATOM   2490  C  CG    . ASN A 1 1761 ? 162.153 163.897 179.901 1.00 7.72  ? 1761 ASN A CG    1 
ATOM   2491  O  OD1   . ASN A 1 1761 ? 161.251 164.729 179.973 1.00 8.66  ? 1761 ASN A OD1   1 
ATOM   2492  N  ND2   . ASN A 1 1761 ? 162.803 163.642 178.773 1.00 10.51 ? 1761 ASN A ND2   1 
ATOM   2493  N  N     . VAL A 1 1762 ? 163.040 162.476 184.185 1.00 4.60  ? 1762 VAL A N     1 
ATOM   2494  C  CA    . VAL A 1 1762 ? 163.303 161.523 185.260 1.00 4.41  ? 1762 VAL A CA    1 
ATOM   2495  C  C     . VAL A 1 1762 ? 162.257 161.665 186.359 1.00 9.61  ? 1762 VAL A C     1 
ATOM   2496  O  O     . VAL A 1 1762 ? 161.749 160.668 186.888 1.00 9.97  ? 1762 VAL A O     1 
ATOM   2497  C  CB    . VAL A 1 1762 ? 164.729 161.710 185.807 1.00 2.37  ? 1762 VAL A CB    1 
ATOM   2498  C  CG1   . VAL A 1 1762 ? 164.948 160.828 187.029 1.00 2.08  ? 1762 VAL A CG1   1 
ATOM   2499  C  CG2   . VAL A 1 1762 ? 165.756 161.407 184.729 1.00 1.73  ? 1762 VAL A CG2   1 
ATOM   2500  N  N     . GLU A 1 1763 ? 161.912 162.906 186.712 1.00 5.49  ? 1763 GLU A N     1 
ATOM   2501  C  CA    . GLU A 1 1763 ? 160.842 163.141 187.679 1.00 6.26  ? 1763 GLU A CA    1 
ATOM   2502  C  C     . GLU A 1 1763 ? 159.532 162.522 187.208 1.00 8.26  ? 1763 GLU A C     1 
ATOM   2503  O  O     . GLU A 1 1763 ? 158.792 161.926 188.000 1.00 7.29  ? 1763 GLU A O     1 
ATOM   2504  C  CB    . GLU A 1 1763 ? 160.661 164.640 187.919 1.00 5.57  ? 1763 GLU A CB    1 
ATOM   2505  C  CG    . GLU A 1 1763 ? 161.808 165.342 188.622 1.00 7.83  ? 1763 GLU A CG    1 
ATOM   2506  C  CD    . GLU A 1 1763 ? 161.967 164.905 190.063 1.00 8.32  ? 1763 GLU A CD    1 
ATOM   2507  O  OE1   . GLU A 1 1763 ? 160.947 164.570 190.697 1.00 13.81 ? 1763 GLU A OE1   1 
ATOM   2508  O  OE2   . GLU A 1 1763 ? 163.107 164.913 190.569 1.00 9.77  ? 1763 GLU A OE2   1 
ATOM   2509  N  N     . THR A 1 1764 ? 159.218 162.670 185.919 1.00 6.52  ? 1764 THR A N     1 
ATOM   2510  C  CA    . THR A 1 1764 ? 157.989 162.094 185.384 1.00 7.22  ? 1764 THR A CA    1 
ATOM   2511  C  C     . THR A 1 1764 ? 158.027 160.572 185.437 1.00 9.29  ? 1764 THR A C     1 
ATOM   2512  O  O     . THR A 1 1764 ? 157.039 159.926 185.805 1.00 12.82 ? 1764 THR A O     1 
ATOM   2513  C  CB    . THR A 1 1764 ? 157.764 162.579 183.953 1.00 10.22 ? 1764 THR A CB    1 
ATOM   2514  O  OG1   . THR A 1 1764 ? 157.855 164.007 183.912 1.00 16.82 ? 1764 THR A OG1   1 
ATOM   2515  C  CG2   . THR A 1 1764 ? 156.394 162.155 183.458 1.00 9.48  ? 1764 THR A CG2   1 
ATOM   2516  N  N     . ALA A 1 1765 ? 159.165 159.980 185.070 1.00 11.83 ? 1765 ALA A N     1 
ATOM   2517  C  CA    . ALA A 1 1765 ? 159.282 158.526 185.063 1.00 11.36 ? 1765 ALA A CA    1 
ATOM   2518  C  C     . ALA A 1 1765 ? 159.204 157.955 186.473 1.00 13.10 ? 1765 ALA A C     1 
ATOM   2519  O  O     . ALA A 1 1765 ? 158.496 156.972 186.719 1.00 20.54 ? 1765 ALA A O     1 
ATOM   2520  C  CB    . ALA A 1 1765 ? 160.586 158.110 184.384 1.00 11.00 ? 1765 ALA A CB    1 
ATOM   2521  N  N     . LEU A 1 1766 ? 159.926 158.565 187.417 1.00 9.85  ? 1766 LEU A N     1 
ATOM   2522  C  CA    . LEU A 1 1766 ? 159.922 158.064 188.787 1.00 12.00 ? 1766 LEU A CA    1 
ATOM   2523  C  C     . LEU A 1 1766 ? 158.542 158.196 189.422 1.00 14.04 ? 1766 LEU A C     1 
ATOM   2524  O  O     . LEU A 1 1766 ? 158.153 157.371 190.257 1.00 25.31 ? 1766 LEU A O     1 
ATOM   2525  C  CB    . LEU A 1 1766 ? 160.969 158.802 189.622 1.00 7.75  ? 1766 LEU A CB    1 
ATOM   2526  C  CG    . LEU A 1 1766 ? 162.434 158.589 189.232 1.00 9.42  ? 1766 LEU A CG    1 
ATOM   2527  C  CD1   . LEU A 1 1766 ? 163.358 159.358 190.161 1.00 4.86  ? 1766 LEU A CD1   1 
ATOM   2528  C  CD2   . LEU A 1 1766 ? 162.785 157.114 189.223 1.00 6.76  ? 1766 LEU A CD2   1 
ATOM   2529  N  N     . SER A 1 1767 ? 157.789 159.225 189.036 1.00 16.34 ? 1767 SER A N     1 
ATOM   2530  C  CA    . SER A 1 1767 ? 156.440 159.392 189.563 1.00 18.16 ? 1767 SER A CA    1 
ATOM   2531  C  C     . SER A 1 1767 ? 155.529 158.249 189.128 1.00 19.92 ? 1767 SER A C     1 
ATOM   2532  O  O     . SER A 1 1767 ? 154.689 157.784 189.905 1.00 31.60 ? 1767 SER A O     1 
ATOM   2533  C  CB    . SER A 1 1767 ? 155.868 160.737 189.120 1.00 12.28 ? 1767 SER A CB    1 
ATOM   2534  O  OG    . SER A 1 1767 ? 156.727 161.795 189.497 1.00 20.45 ? 1767 SER A OG    1 
ATOM   2535  N  N     . SER A 1 1768 ? 155.679 157.788 187.885 1.00 17.12 ? 1768 SER A N     1 
ATOM   2536  C  CA    . SER A 1 1768 ? 154.873 156.677 187.394 1.00 15.79 ? 1768 SER A CA    1 
ATOM   2537  C  C     . SER A 1 1768 ? 155.239 155.353 188.054 1.00 22.01 ? 1768 SER A C     1 
ATOM   2538  O  O     . SER A 1 1768 ? 154.409 154.440 188.079 1.00 32.39 ? 1768 SER A O     1 
ATOM   2539  C  CB    . SER A 1 1768 ? 155.019 156.560 185.877 1.00 16.95 ? 1768 SER A CB    1 
ATOM   2540  O  OG    . SER A 1 1768 ? 154.273 155.463 185.377 1.00 27.82 ? 1768 SER A OG    1 
ATOM   2541  N  N     . MET A 1 1769 ? 156.456 155.230 188.583 1.00 21.03 ? 1769 MET A N     1 
ATOM   2542  C  CA    . MET A 1 1769 ? 156.926 154.003 189.207 1.00 19.47 ? 1769 MET A CA    1 
ATOM   2543  C  C     . MET A 1 1769 ? 156.590 153.935 190.693 1.00 31.11 ? 1769 MET A C     1 
ATOM   2544  O  O     . MET A 1 1769 ? 157.251 153.197 191.436 1.00 27.33 ? 1769 MET A O     1 
ATOM   2545  C  CB    . MET A 1 1769 ? 158.435 153.859 189.003 1.00 16.99 ? 1769 MET A CB    1 
ATOM   2546  C  CG    . MET A 1 1769 ? 158.841 153.646 187.556 1.00 22.78 ? 1769 MET A CG    1 
ATOM   2547  S  SD    . MET A 1 1769 ? 160.624 153.560 187.311 1.00 29.22 ? 1769 MET A SD    1 
ATOM   2548  C  CE    . MET A 1 1769 ? 160.993 151.981 188.070 1.00 19.12 ? 1769 MET A CE    1 
ATOM   2549  N  N     . GLY A 1 1770 ? 155.579 154.685 191.138 1.00 29.81 ? 1770 GLY A N     1 
ATOM   2550  C  CA    . GLY A 1 1770 ? 155.263 154.731 192.557 1.00 28.22 ? 1770 GLY A CA    1 
ATOM   2551  C  C     . GLY A 1 1770 ? 154.845 153.384 193.118 1.00 30.97 ? 1770 GLY A C     1 
ATOM   2552  O  O     . GLY A 1 1770 ? 155.104 153.080 194.285 1.00 34.45 ? 1770 GLY A O     1 
ATOM   2553  N  N     . GLY A 1 1771 ? 154.193 152.560 192.296 1.00 26.85 ? 1771 GLY A N     1 
ATOM   2554  C  CA    . GLY A 1 1771 ? 153.753 151.255 192.756 1.00 29.71 ? 1771 GLY A CA    1 
ATOM   2555  C  C     . GLY A 1 1771 ? 154.872 150.253 192.934 1.00 33.83 ? 1771 GLY A C     1 
ATOM   2556  O  O     . GLY A 1 1771 ? 154.646 149.183 193.506 1.00 34.74 ? 1771 GLY A O     1 
ATOM   2557  N  N     . GLY A 1 1772 ? 156.074 150.575 192.460 1.00 31.66 ? 1772 GLY A N     1 
ATOM   2558  C  CA    . GLY A 1 1772 ? 157.202 149.676 192.592 1.00 26.99 ? 1772 GLY A CA    1 
ATOM   2559  C  C     . GLY A 1 1772 ? 157.253 148.626 191.502 1.00 29.59 ? 1772 GLY A C     1 
ATOM   2560  O  O     . GLY A 1 1772 ? 158.203 148.582 190.714 1.00 28.45 ? 1772 GLY A O     1 
ATOM   2561  N  N     . GLY A 1 1773 ? 156.228 147.774 191.446 1.00 28.66 ? 1773 GLY A N     1 
ATOM   2562  C  CA    . GLY A 1 1773 ? 156.171 146.739 190.429 1.00 29.05 ? 1773 GLY A CA    1 
ATOM   2563  C  C     . GLY A 1 1773 ? 155.743 147.243 189.068 1.00 32.40 ? 1773 GLY A C     1 
ATOM   2564  O  O     . GLY A 1 1773 ? 155.724 146.465 188.107 1.00 34.91 ? 1773 GLY A O     1 
ATOM   2565  N  N     . ASP A 1 1774 ? 155.390 148.523 188.961 1.00 32.76 ? 1774 ASP A N     1 
ATOM   2566  C  CA    . ASP A 1 1774 ? 155.002 149.091 187.678 1.00 31.61 ? 1774 ASP A CA    1 
ATOM   2567  C  C     . ASP A 1 1774 ? 156.181 149.077 186.715 1.00 32.34 ? 1774 ASP A C     1 
ATOM   2568  O  O     . ASP A 1 1774 ? 157.344 149.107 187.124 1.00 34.35 ? 1774 ASP A O     1 
ATOM   2569  C  CB    . ASP A 1 1774 ? 154.491 150.521 187.860 1.00 28.77 ? 1774 ASP A CB    1 
ATOM   2570  C  CG    . ASP A 1 1774 ? 153.168 150.580 188.597 1.00 32.36 ? 1774 ASP A CG    1 
ATOM   2571  O  OD1   . ASP A 1 1774 ? 152.385 149.613 188.493 1.00 31.94 ? 1774 ASP A OD1   1 
ATOM   2572  O  OD2   . ASP A 1 1774 ? 152.913 151.592 189.281 1.00 33.75 ? 1774 ASP A OD2   1 
ATOM   2573  N  N     . ALA A 1 1775 ? 155.869 149.021 185.420 1.00 35.06 ? 1775 ALA A N     1 
ATOM   2574  C  CA    . ALA A 1 1775 ? 156.910 149.045 184.406 1.00 31.24 ? 1775 ALA A CA    1 
ATOM   2575  C  C     . ALA A 1 1775 ? 157.727 150.326 184.520 1.00 29.71 ? 1775 ALA A C     1 
ATOM   2576  O  O     . ALA A 1 1775 ? 157.232 151.368 184.956 1.00 28.77 ? 1775 ALA A O     1 
ATOM   2577  C  CB    . ALA A 1 1775 ? 156.300 148.931 183.009 1.00 18.84 ? 1775 ALA A CB    1 
ATOM   2578  N  N     . ALA A 1 1776 ? 158.996 150.237 184.129 1.00 25.64 ? 1776 ALA A N     1 
ATOM   2579  C  CA    . ALA A 1 1776 ? 159.915 151.358 184.275 1.00 22.88 ? 1776 ALA A CA    1 
ATOM   2580  C  C     . ALA A 1 1776 ? 159.941 152.173 182.989 1.00 24.85 ? 1776 ALA A C     1 
ATOM   2581  O  O     . ALA A 1 1776 ? 160.430 151.673 181.963 1.00 17.50 ? 1776 ALA A O     1 
ATOM   2582  C  CB    . ALA A 1 1776 ? 161.312 150.862 184.617 1.00 10.48 ? 1776 ALA A CB    1 
ATOM   2583  N  N     . PRO A 1 1777 ? 159.435 153.410 182.986 1.00 25.88 ? 1777 PRO A N     1 
ATOM   2584  C  CA    . PRO A 1 1777 ? 159.664 154.307 181.849 1.00 22.25 ? 1777 PRO A CA    1 
ATOM   2585  C  C     . PRO A 1 1777 ? 160.989 155.046 181.917 1.00 17.80 ? 1777 PRO A C     1 
ATOM   2586  O  O     . PRO A 1 1777 ? 161.223 155.938 181.094 1.00 19.08 ? 1777 PRO A O     1 
ATOM   2587  C  CB    . PRO A 1 1777 ? 158.482 155.286 181.936 1.00 21.51 ? 1777 PRO A CB    1 
ATOM   2588  C  CG    . PRO A 1 1777 ? 157.983 155.202 183.345 1.00 21.51 ? 1777 PRO A CG    1 
ATOM   2589  C  CD    . PRO A 1 1777 ? 158.640 154.047 184.045 1.00 24.16 ? 1777 PRO A CD    1 
ATOM   2590  N  N     . LEU A 1 1778 ? 161.847 154.713 182.885 1.00 14.87 ? 1778 LEU A N     1 
ATOM   2591  C  CA    . LEU A 1 1778 ? 163.193 155.273 182.915 1.00 10.55 ? 1778 LEU A CA    1 
ATOM   2592  C  C     . LEU A 1 1778 ? 163.988 154.873 181.683 1.00 12.93 ? 1778 LEU A C     1 
ATOM   2593  O  O     . LEU A 1 1778 ? 164.881 155.613 181.253 1.00 14.00 ? 1778 LEU A O     1 
ATOM   2594  C  CB    . LEU A 1 1778 ? 163.927 154.818 184.175 1.00 11.85 ? 1778 LEU A CB    1 
ATOM   2595  C  CG    . LEU A 1 1778 ? 163.996 155.766 185.367 1.00 10.67 ? 1778 LEU A CG    1 
ATOM   2596  C  CD1   . LEU A 1 1778 ? 164.895 155.167 186.433 1.00 11.41 ? 1778 LEU A CD1   1 
ATOM   2597  C  CD2   . LEU A 1 1778 ? 164.503 157.130 184.940 1.00 7.15  ? 1778 LEU A CD2   1 
ATOM   2598  N  N     . HIS A 1 1779 ? 163.685 153.707 181.110 1.00 11.80 ? 1779 HIS A N     1 
ATOM   2599  C  CA    . HIS A 1 1779 ? 164.374 153.273 179.902 1.00 10.52 ? 1779 HIS A CA    1 
ATOM   2600  C  C     . HIS A 1 1779 ? 164.107 154.230 178.748 1.00 9.40  ? 1779 HIS A C     1 
ATOM   2601  O  O     . HIS A 1 1779 ? 164.984 154.462 177.908 1.00 8.86  ? 1779 HIS A O     1 
ATOM   2602  C  CB    . HIS A 1 1779 ? 163.950 151.850 179.543 1.00 15.84 ? 1779 HIS A CB    1 
ATOM   2603  C  CG    . HIS A 1 1779 ? 164.578 150.799 180.404 1.00 18.31 ? 1779 HIS A CG    1 
ATOM   2604  N  ND1   . HIS A 1 1779 ? 163.923 150.218 181.467 1.00 15.35 ? 1779 HIS A ND1   1 
ATOM   2605  C  CD2   . HIS A 1 1779 ? 165.808 150.232 180.365 1.00 17.66 ? 1779 HIS A CD2   1 
ATOM   2606  C  CE1   . HIS A 1 1779 ? 164.719 149.336 182.044 1.00 15.02 ? 1779 HIS A CE1   1 
ATOM   2607  N  NE2   . HIS A 1 1779 ? 165.868 149.324 181.394 1.00 19.76 ? 1779 HIS A NE2   1 
ATOM   2608  N  N     . SER A 1 1780 ? 162.899 154.794 178.690 1.00 11.95 ? 1780 SER A N     1 
ATOM   2609  C  CA    . SER A 1 1780 ? 162.605 155.809 177.683 1.00 12.29 ? 1780 SER A CA    1 
ATOM   2610  C  C     . SER A 1 1780 ? 163.432 157.070 177.909 1.00 9.91  ? 1780 SER A C     1 
ATOM   2611  O  O     . SER A 1 1780 ? 163.880 157.705 176.948 1.00 12.35 ? 1780 SER A O     1 
ATOM   2612  C  CB    . SER A 1 1780 ? 161.113 156.134 177.684 1.00 8.27  ? 1780 SER A CB    1 
ATOM   2613  O  OG    . SER A 1 1780 ? 160.352 155.002 177.303 1.00 15.65 ? 1780 SER A OG    1 
ATOM   2614  N  N     . VAL A 1 1781 ? 163.634 157.454 179.172 1.00 7.48  ? 1781 VAL A N     1 
ATOM   2615  C  CA    . VAL A 1 1781 ? 164.507 158.585 179.472 1.00 7.66  ? 1781 VAL A CA    1 
ATOM   2616  C  C     . VAL A 1 1781 ? 165.919 158.299 178.984 1.00 8.76  ? 1781 VAL A C     1 
ATOM   2617  O  O     . VAL A 1 1781 ? 166.564 159.149 178.358 1.00 12.45 ? 1781 VAL A O     1 
ATOM   2618  C  CB    . VAL A 1 1781 ? 164.482 158.904 180.978 1.00 8.46  ? 1781 VAL A CB    1 
ATOM   2619  C  CG1   . VAL A 1 1781 ? 165.576 159.903 181.332 1.00 4.93  ? 1781 VAL A CG1   1 
ATOM   2620  C  CG2   . VAL A 1 1781 ? 163.121 159.433 181.387 1.00 7.96  ? 1781 VAL A CG2   1 
ATOM   2621  N  N     . LEU A 1 1782 ? 166.419 157.092 179.254 1.00 8.39  ? 1782 LEU A N     1 
ATOM   2622  C  CA    . LEU A 1 1782 ? 167.695 156.674 178.689 1.00 5.07  ? 1782 LEU A CA    1 
ATOM   2623  C  C     . LEU A 1 1782 ? 167.628 156.628 177.168 1.00 8.81  ? 1782 LEU A C     1 
ATOM   2624  O  O     . LEU A 1 1782 ? 168.570 157.045 176.486 1.00 10.99 ? 1782 LEU A O     1 
ATOM   2625  C  CB    . LEU A 1 1782 ? 168.095 155.313 179.254 1.00 4.39  ? 1782 LEU A CB    1 
ATOM   2626  C  CG    . LEU A 1 1782 ? 169.443 154.742 178.816 1.00 8.75  ? 1782 LEU A CG    1 
ATOM   2627  C  CD1   . LEU A 1 1782 ? 170.576 155.694 179.169 1.00 4.29  ? 1782 LEU A CD1   1 
ATOM   2628  C  CD2   . LEU A 1 1782 ? 169.669 153.377 179.439 1.00 5.19  ? 1782 LEU A CD2   1 
ATOM   2629  N  N     . SER A 1 1783 ? 166.512 156.136 176.622 1.00 7.84  ? 1783 SER A N     1 
ATOM   2630  C  CA    . SER A 1 1783 ? 166.362 156.048 175.174 1.00 7.18  ? 1783 SER A CA    1 
ATOM   2631  C  C     . SER A 1 1783 ? 166.448 157.422 174.520 1.00 10.83 ? 1783 SER A C     1 
ATOM   2632  O  O     . SER A 1 1783 ? 167.098 157.582 173.480 1.00 11.93 ? 1783 SER A O     1 
ATOM   2633  C  CB    . SER A 1 1783 ? 165.033 155.376 174.827 1.00 10.93 ? 1783 SER A CB    1 
ATOM   2634  O  OG    . SER A 1 1783 ? 164.840 155.310 173.426 1.00 19.10 ? 1783 SER A OG    1 
ATOM   2635  N  N     . ASN A 1 1784 ? 165.792 158.423 175.110 1.00 12.67 ? 1784 ASN A N     1 
ATOM   2636  C  CA    . ASN A 1 1784 ? 165.856 159.772 174.559 1.00 8.07  ? 1784 ASN A CA    1 
ATOM   2637  C  C     . ASN A 1 1784 ? 167.276 160.319 174.602 1.00 6.67  ? 1784 ASN A C     1 
ATOM   2638  O  O     . ASN A 1 1784 ? 167.722 160.983 173.660 1.00 10.41 ? 1784 ASN A O     1 
ATOM   2639  C  CB    . ASN A 1 1784 ? 164.903 160.695 175.318 1.00 12.41 ? 1784 ASN A CB    1 
ATOM   2640  C  CG    . ASN A 1 1784 ? 164.804 162.071 174.692 1.00 16.13 ? 1784 ASN A CG    1 
ATOM   2641  O  OD1   . ASN A 1 1784 ? 165.270 163.058 175.260 1.00 16.09 ? 1784 ASN A OD1   1 
ATOM   2642  N  ND2   . ASN A 1 1784 ? 164.191 162.146 173.519 1.00 12.25 ? 1784 ASN A ND2   1 
ATOM   2643  N  N     . VAL A 1 1785 ? 167.998 160.055 175.691 1.00 8.78  ? 1785 VAL A N     1 
ATOM   2644  C  CA    . VAL A 1 1785 ? 169.380 160.514 175.799 1.00 7.52  ? 1785 VAL A CA    1 
ATOM   2645  C  C     . VAL A 1 1785 ? 170.261 159.815 174.768 1.00 9.17  ? 1785 VAL A C     1 
ATOM   2646  O  O     . VAL A 1 1785 ? 171.129 160.443 174.152 1.00 8.48  ? 1785 VAL A O     1 
ATOM   2647  C  CB    . VAL A 1 1785 ? 169.899 160.308 177.233 1.00 4.90  ? 1785 VAL A CB    1 
ATOM   2648  C  CG1   . VAL A 1 1785 ? 171.376 160.637 177.320 1.00 3.63  ? 1785 VAL A CG1   1 
ATOM   2649  C  CG2   . VAL A 1 1785 ? 169.107 161.166 178.206 1.00 3.89  ? 1785 VAL A CG2   1 
ATOM   2650  N  N     . GLU A 1 1786 ? 170.055 158.510 174.562 1.00 8.69  ? 1786 GLU A N     1 
ATOM   2651  C  CA    . GLU A 1 1786 ? 170.816 157.789 173.545 1.00 10.00 ? 1786 GLU A CA    1 
ATOM   2652  C  C     . GLU A 1 1786 ? 170.582 158.380 172.161 1.00 9.42  ? 1786 GLU A C     1 
ATOM   2653  O  O     . GLU A 1 1786 ? 171.531 158.598 171.399 1.00 10.04 ? 1786 GLU A O     1 
ATOM   2654  C  CB    . GLU A 1 1786 ? 170.442 156.306 173.552 1.00 12.51 ? 1786 GLU A CB    1 
ATOM   2655  C  CG    . GLU A 1 1786 ? 170.739 155.571 174.837 1.00 12.34 ? 1786 GLU A CG    1 
ATOM   2656  C  CD    . GLU A 1 1786 ? 172.206 155.251 174.986 1.00 17.86 ? 1786 GLU A CD    1 
ATOM   2657  O  OE1   . GLU A 1 1786 ? 172.684 154.308 174.319 1.00 24.63 ? 1786 GLU A OE1   1 
ATOM   2658  O  OE2   . GLU A 1 1786 ? 172.884 155.945 175.765 1.00 19.94 ? 1786 GLU A OE2   1 
ATOM   2659  N  N     . VAL A 1 1787 ? 169.321 158.645 171.819 1.00 8.09  ? 1787 VAL A N     1 
ATOM   2660  C  CA    . VAL A 1 1787 ? 169.000 159.169 170.495 1.00 8.56  ? 1787 VAL A CA    1 
ATOM   2661  C  C     . VAL A 1 1787 ? 169.598 160.559 170.316 1.00 7.69  ? 1787 VAL A C     1 
ATOM   2662  O  O     . VAL A 1 1787 ? 170.216 160.861 169.288 1.00 9.68  ? 1787 VAL A O     1 
ATOM   2663  C  CB    . VAL A 1 1787 ? 167.476 159.178 170.277 1.00 7.88  ? 1787 VAL A CB    1 
ATOM   2664  C  CG1   . VAL A 1 1787 ? 167.099 160.131 169.152 1.00 12.36 ? 1787 VAL A CG1   1 
ATOM   2665  C  CG2   . VAL A 1 1787 ? 166.972 157.775 169.991 1.00 10.99 ? 1787 VAL A CG2   1 
ATOM   2666  N  N     . THR A 1 1788 ? 169.436 161.420 171.322 1.00 5.68  ? 1788 THR A N     1 
ATOM   2667  C  CA    . THR A 1 1788 ? 169.941 162.783 171.220 1.00 6.05  ? 1788 THR A CA    1 
ATOM   2668  C  C     . THR A 1 1788 ? 171.462 162.792 171.144 1.00 6.37  ? 1788 THR A C     1 
ATOM   2669  O  O     . THR A 1 1788 ? 172.052 163.588 170.404 1.00 7.49  ? 1788 THR A O     1 
ATOM   2670  C  CB    . THR A 1 1788 ? 169.461 163.607 172.414 1.00 4.91  ? 1788 THR A CB    1 
ATOM   2671  O  OG1   . THR A 1 1788 ? 168.031 163.624 172.434 1.00 10.17 ? 1788 THR A OG1   1 
ATOM   2672  C  CG2   . THR A 1 1788 ? 169.937 165.040 172.284 1.00 5.16  ? 1788 THR A CG2   1 
ATOM   2673  N  N     . LEU A 1 1789 ? 172.114 161.906 171.898 1.00 7.87  ? 1789 LEU A N     1 
ATOM   2674  C  CA    . LEU A 1 1789 ? 173.571 161.866 171.911 1.00 5.42  ? 1789 LEU A CA    1 
ATOM   2675  C  C     . LEU A 1 1789 ? 174.118 161.352 170.585 1.00 6.15  ? 1789 LEU A C     1 
ATOM   2676  O  O     . LEU A 1 1789 ? 175.208 161.752 170.159 1.00 12.34 ? 1789 LEU A O     1 
ATOM   2677  C  CB    . LEU A 1 1789 ? 174.047 161.003 173.080 1.00 4.71  ? 1789 LEU A CB    1 
ATOM   2678  C  CG    . LEU A 1 1789 ? 175.543 160.862 173.349 1.00 10.58 ? 1789 LEU A CG    1 
ATOM   2679  C  CD1   . LEU A 1 1789 ? 176.132 162.218 173.693 1.00 3.22  ? 1789 LEU A CD1   1 
ATOM   2680  C  CD2   . LEU A 1 1789 ? 175.775 159.875 174.479 1.00 11.13 ? 1789 LEU A CD2   1 
ATOM   2681  N  N     . ASN A 1 1790 ? 173.379 160.461 169.916 1.00 8.19  ? 1790 ASN A N     1 
ATOM   2682  C  CA    . ASN A 1 1790 ? 173.803 159.989 168.599 1.00 6.82  ? 1790 ASN A CA    1 
ATOM   2683  C  C     . ASN A 1 1790 ? 173.781 161.113 167.571 1.00 9.00  ? 1790 ASN A C     1 
ATOM   2684  O  O     . ASN A 1 1790 ? 174.679 161.205 166.727 1.00 12.22 ? 1790 ASN A O     1 
ATOM   2685  C  CB    . ASN A 1 1790 ? 172.923 158.826 168.143 1.00 9.08  ? 1790 ASN A CB    1 
ATOM   2686  C  CG    . ASN A 1 1790 ? 173.219 157.542 168.894 1.00 15.43 ? 1790 ASN A CG    1 
ATOM   2687  O  OD1   . ASN A 1 1790 ? 174.371 157.246 169.208 1.00 15.45 ? 1790 ASN A OD1   1 
ATOM   2688  N  ND2   . ASN A 1 1790 ? 172.177 156.773 169.186 1.00 15.76 ? 1790 ASN A ND2   1 
ATOM   2689  N  N     . VAL A 1 1791 ? 172.759 161.970 167.620 1.00 7.09  ? 1791 VAL A N     1 
ATOM   2690  C  CA    . VAL A 1 1791 ? 172.709 163.120 166.721 1.00 7.92  ? 1791 VAL A CA    1 
ATOM   2691  C  C     . VAL A 1 1791 ? 173.854 164.079 167.019 1.00 9.05  ? 1791 VAL A C     1 
ATOM   2692  O  O     . VAL A 1 1791 ? 174.495 164.606 166.100 1.00 9.79  ? 1791 VAL A O     1 
ATOM   2693  C  CB    . VAL A 1 1791 ? 171.340 163.816 166.823 1.00 7.99  ? 1791 VAL A CB    1 
ATOM   2694  C  CG1   . VAL A 1 1791 ? 171.328 165.090 165.999 1.00 8.22  ? 1791 VAL A CG1   1 
ATOM   2695  C  CG2   . VAL A 1 1791 ? 170.238 162.881 166.369 1.00 9.48  ? 1791 VAL A CG2   1 
ATOM   2696  N  N     . LEU A 1 1792 ? 174.124 164.328 168.302 1.00 7.13  ? 1792 LEU A N     1 
ATOM   2697  C  CA    . LEU A 1 1792 ? 175.242 165.191 168.668 1.00 6.49  ? 1792 LEU A CA    1 
ATOM   2698  C  C     . LEU A 1 1792 ? 176.568 164.597 168.211 1.00 6.90  ? 1792 LEU A C     1 
ATOM   2699  O  O     . LEU A 1 1792 ? 177.431 165.312 167.691 1.00 6.51  ? 1792 LEU A O     1 
ATOM   2700  C  CB    . LEU A 1 1792 ? 175.252 165.421 170.178 1.00 5.35  ? 1792 LEU A CB    1 
ATOM   2701  C  CG    . LEU A 1 1792 ? 174.092 166.223 170.765 1.00 4.54  ? 1792 LEU A CG    1 
ATOM   2702  C  CD1   . LEU A 1 1792 ? 174.114 166.147 172.282 1.00 5.27  ? 1792 LEU A CD1   1 
ATOM   2703  C  CD2   . LEU A 1 1792 ? 174.156 167.662 170.301 1.00 3.55  ? 1792 LEU A CD2   1 
ATOM   2704  N  N     . ALA A 1 1793 ? 176.742 163.287 168.397 1.00 9.29  ? 1793 ALA A N     1 
ATOM   2705  C  CA    . ALA A 1 1793 ? 177.974 162.634 167.961 1.00 7.06  ? 1793 ALA A CA    1 
ATOM   2706  C  C     . ALA A 1 1793 ? 178.117 162.683 166.446 1.00 10.20 ? 1793 ALA A C     1 
ATOM   2707  O  O     . ALA A 1 1793 ? 179.224 162.857 165.926 1.00 13.31 ? 1793 ALA A O     1 
ATOM   2708  C  CB    . ALA A 1 1793 ? 178.007 161.191 168.460 1.00 8.94  ? 1793 ALA A CB    1 
ATOM   2709  N  N     . ASP A 1 1794 ? 177.008 162.522 165.719 1.00 10.20 ? 1794 ASP A N     1 
ATOM   2710  C  CA    . ASP A 1 1794 ? 177.058 162.621 164.264 1.00 9.32  ? 1794 ASP A CA    1 
ATOM   2711  C  C     . ASP A 1 1794 ? 177.415 164.033 163.815 1.00 11.24 ? 1794 ASP A C     1 
ATOM   2712  O  O     . ASP A 1 1794 ? 178.138 164.211 162.827 1.00 15.83 ? 1794 ASP A O     1 
ATOM   2713  C  CB    . ASP A 1 1794 ? 175.722 162.190 163.660 1.00 11.93 ? 1794 ASP A CB    1 
ATOM   2714  C  CG    . ASP A 1 1794 ? 175.644 160.694 163.433 1.00 27.37 ? 1794 ASP A CG    1 
ATOM   2715  O  OD1   . ASP A 1 1794 ? 176.633 159.994 163.735 1.00 27.98 ? 1794 ASP A OD1   1 
ATOM   2716  O  OD2   . ASP A 1 1794 ? 174.596 160.217 162.951 1.00 36.78 ? 1794 ASP A OD2   1 
ATOM   2717  N  N     . SER A 1 1795 ? 176.912 165.048 164.521 1.00 12.77 ? 1795 SER A N     1 
ATOM   2718  C  CA    . SER A 1 1795 ? 177.174 166.428 164.127 1.00 7.04  ? 1795 SER A CA    1 
ATOM   2719  C  C     . SER A 1 1795 ? 178.654 166.775 164.247 1.00 9.16  ? 1795 SER A C     1 
ATOM   2720  O  O     . SER A 1 1795 ? 179.202 167.484 163.394 1.00 13.57 ? 1795 SER A O     1 
ATOM   2721  C  CB    . SER A 1 1795 ? 176.327 167.383 164.967 1.00 6.40  ? 1795 SER A CB    1 
ATOM   2722  O  OG    . SER A 1 1795 ? 174.946 167.126 164.791 1.00 6.97  ? 1795 SER A OG    1 
ATOM   2723  N  N     . VAL A 1 1796 ? 179.319 166.288 165.299 1.00 6.87  ? 1796 VAL A N     1 
ATOM   2724  C  CA    . VAL A 1 1796 ? 180.732 166.608 165.500 1.00 8.42  ? 1796 VAL A CA    1 
ATOM   2725  C  C     . VAL A 1 1796 ? 181.655 165.745 164.657 1.00 11.49 ? 1796 VAL A C     1 
ATOM   2726  O  O     . VAL A 1 1796 ? 182.869 165.986 164.646 1.00 11.10 ? 1796 VAL A O     1 
ATOM   2727  C  CB    . VAL A 1 1796 ? 181.128 166.486 166.987 1.00 7.18  ? 1796 VAL A CB    1 
ATOM   2728  C  CG1   . VAL A 1 1796 ? 180.316 167.454 167.830 1.00 6.80  ? 1796 VAL A CG1   1 
ATOM   2729  C  CG2   . VAL A 1 1796 ? 180.954 165.064 167.477 1.00 7.10  ? 1796 VAL A CG2   1 
ATOM   2730  N  N     . LEU A 1 1797 ? 181.123 164.750 163.947 1.00 11.56 ? 1797 LEU A N     1 
ATOM   2731  C  CA    . LEU A 1 1797 ? 181.933 163.973 163.017 1.00 12.29 ? 1797 LEU A CA    1 
ATOM   2732  C  C     . LEU A 1 1797 ? 182.209 164.724 161.722 1.00 13.60 ? 1797 LEU A C     1 
ATOM   2733  O  O     . LEU A 1 1797 ? 183.052 164.284 160.934 1.00 19.65 ? 1797 LEU A O     1 
ATOM   2734  C  CB    . LEU A 1 1797 ? 181.250 162.641 162.703 1.00 10.82 ? 1797 LEU A CB    1 
ATOM   2735  C  CG    . LEU A 1 1797 ? 181.235 161.589 163.812 1.00 13.89 ? 1797 LEU A CG    1 
ATOM   2736  C  CD1   . LEU A 1 1797 ? 180.366 160.404 163.421 1.00 14.02 ? 1797 LEU A CD1   1 
ATOM   2737  C  CD2   . LEU A 1 1797 ? 182.640 161.134 164.143 1.00 10.60 ? 1797 LEU A CD2   1 
ATOM   2738  N  N     . MET A 1 1798 ? 181.524 165.835 161.491 1.00 9.56  ? 1798 MET A N     1 
ATOM   2739  C  CA    . MET A 1 1798 ? 181.674 166.652 160.297 1.00 13.28 ? 1798 MET A CA    1 
ATOM   2740  C  C     . MET A 1 1798 ? 182.025 168.082 160.700 1.00 17.10 ? 1798 MET A C     1 
ATOM   2741  O  O     . MET A 1 1798 ? 182.022 168.440 161.878 1.00 18.54 ? 1798 MET A O     1 
ATOM   2742  C  CB    . MET A 1 1798 ? 180.401 166.598 159.451 1.00 16.62 ? 1798 MET A CB    1 
ATOM   2743  C  CG    . MET A 1 1798 ? 179.188 167.216 160.119 1.00 15.56 ? 1798 MET A CG    1 
ATOM   2744  S  SD    . MET A 1 1798 ? 177.698 167.084 159.115 1.00 45.47 ? 1798 MET A SD    1 
ATOM   2745  C  CE    . MET A 1 1798 ? 176.497 167.873 160.184 1.00 19.16 ? 1798 MET A CE    1 
ATOM   2746  N  N     . GLU A 1 1799 ? 182.341 168.901 159.699 1.00 16.65 ? 1799 GLU A N     1 
ATOM   2747  C  CA    . GLU A 1 1799 ? 182.741 170.277 159.959 1.00 15.09 ? 1799 GLU A CA    1 
ATOM   2748  C  C     . GLU A 1 1799 ? 181.553 171.100 160.436 1.00 18.76 ? 1799 GLU A C     1 
ATOM   2749  O  O     . GLU A 1 1799 ? 180.434 170.957 159.937 1.00 17.67 ? 1799 GLU A O     1 
ATOM   2750  C  CB    . GLU A 1 1799 ? 183.346 170.902 158.702 1.00 17.27 ? 1799 GLU A CB    1 
ATOM   2751  C  CG    . GLU A 1 1799 ? 184.413 171.947 158.985 1.00 21.08 ? 1799 GLU A CG    1 
ATOM   2752  C  CD    . GLU A 1 1799 ? 184.738 172.789 157.769 1.00 31.32 ? 1799 GLU A CD    1 
ATOM   2753  O  OE1   . GLU A 1 1799 ? 184.109 172.580 156.712 1.00 33.21 ? 1799 GLU A OE1   1 
ATOM   2754  O  OE2   . GLU A 1 1799 ? 185.621 173.666 157.873 1.00 31.00 ? 1799 GLU A OE2   1 
ATOM   2755  N  N     . GLN A 1 1800 ? 181.800 171.958 161.417 1.00 18.46 ? 1800 GLN A N     1 
ATOM   2756  C  CA    . GLN A 1 1800 ? 180.778 172.799 162.018 1.00 13.34 ? 1800 GLN A CA    1 
ATOM   2757  C  C     . GLN A 1 1800 ? 181.355 174.185 162.252 1.00 9.35  ? 1800 GLN A C     1 
ATOM   2758  O  O     . GLN A 1 1800 ? 182.577 174.351 162.330 1.00 13.04 ? 1800 GLN A O     1 
ATOM   2759  C  CB    . GLN A 1 1800 ? 180.272 172.217 163.348 1.00 6.19  ? 1800 GLN A CB    1 
ATOM   2760  C  CG    . GLN A 1 1800 ? 179.658 170.831 163.251 1.00 7.26  ? 1800 GLN A CG    1 
ATOM   2761  C  CD    . GLN A 1 1800 ? 178.219 170.854 162.773 1.00 10.95 ? 1800 GLN A CD    1 
ATOM   2762  O  OE1   . GLN A 1 1800 ? 177.692 171.900 162.398 1.00 12.66 ? 1800 GLN A OE1   1 
ATOM   2763  N  NE2   . GLN A 1 1800 ? 177.576 169.695 162.784 1.00 8.50  ? 1800 GLN A NE2   1 
ATOM   2764  N  N     . PRO A 1 1801 ? 180.501 175.202 162.355 1.00 7.87  ? 1801 PRO A N     1 
ATOM   2765  C  CA    . PRO A 1 1801 ? 180.986 176.519 162.756 1.00 6.11  ? 1801 PRO A CA    1 
ATOM   2766  C  C     . PRO A 1 1801 ? 181.619 176.457 164.129 1.00 7.83  ? 1801 PRO A C     1 
ATOM   2767  O  O     . PRO A 1 1801 ? 181.208 175.652 164.988 1.00 9.68  ? 1801 PRO A O     1 
ATOM   2768  C  CB    . PRO A 1 1801 ? 179.715 177.377 162.759 1.00 8.23  ? 1801 PRO A CB    1 
ATOM   2769  C  CG    . PRO A 1 1801 ? 178.802 176.697 161.806 1.00 8.98  ? 1801 PRO A CG    1 
ATOM   2770  C  CD    . PRO A 1 1801 ? 179.089 175.232 161.936 1.00 8.36  ? 1801 PRO A CD    1 
ATOM   2771  N  N     . PRO A 1 1802 ? 182.641 177.281 164.384 1.00 9.92  ? 1802 PRO A N     1 
ATOM   2772  C  CA    . PRO A 1 1802 ? 183.370 177.172 165.661 1.00 7.14  ? 1802 PRO A CA    1 
ATOM   2773  C  C     . PRO A 1 1802 ? 182.501 177.367 166.890 1.00 7.93  ? 1802 PRO A C     1 
ATOM   2774  O  O     . PRO A 1 1802 ? 182.719 176.695 167.905 1.00 7.70  ? 1802 PRO A O     1 
ATOM   2775  C  CB    . PRO A 1 1802 ? 184.442 178.265 165.540 1.00 4.10  ? 1802 PRO A CB    1 
ATOM   2776  C  CG    . PRO A 1 1802 ? 184.588 178.493 164.072 1.00 7.22  ? 1802 PRO A CG    1 
ATOM   2777  C  CD    . PRO A 1 1802 ? 183.212 178.321 163.513 1.00 8.68  ? 1802 PRO A CD    1 
ATOM   2778  N  N     . LEU A 1 1803 ? 181.521 178.270 166.836 1.00 7.70  ? 1803 LEU A N     1 
ATOM   2779  C  CA    . LEU A 1 1803 ? 180.641 178.459 167.984 1.00 4.47  ? 1803 LEU A CA    1 
ATOM   2780  C  C     . LEU A 1 1803 ? 179.695 177.278 168.153 1.00 6.48  ? 1803 LEU A C     1 
ATOM   2781  O  O     . LEU A 1 1803 ? 179.481 176.804 169.274 1.00 6.66  ? 1803 LEU A O     1 
ATOM   2782  C  CB    . LEU A 1 1803 ? 179.854 179.760 167.839 1.00 5.03  ? 1803 LEU A CB    1 
ATOM   2783  C  CG    . LEU A 1 1803 ? 178.881 180.075 168.977 1.00 4.14  ? 1803 LEU A CG    1 
ATOM   2784  C  CD1   . LEU A 1 1803 ? 179.639 180.425 170.246 1.00 5.42  ? 1803 LEU A CD1   1 
ATOM   2785  C  CD2   . LEU A 1 1803 ? 177.932 181.194 168.588 1.00 5.94  ? 1803 LEU A CD2   1 
ATOM   2786  N  N     . ARG A 1 1804 ? 179.121 176.787 167.051 1.00 4.83  ? 1804 ARG A N     1 
ATOM   2787  C  CA    . ARG A 1 1804 ? 178.220 175.644 167.136 1.00 5.42  ? 1804 ARG A CA    1 
ATOM   2788  C  C     . ARG A 1 1804 ? 178.960 174.384 167.568 1.00 4.98  ? 1804 ARG A C     1 
ATOM   2789  O  O     . ARG A 1 1804 ? 178.434 173.590 168.357 1.00 5.51  ? 1804 ARG A O     1 
ATOM   2790  C  CB    . ARG A 1 1804 ? 177.520 175.420 165.798 1.00 6.50  ? 1804 ARG A CB    1 
ATOM   2791  C  CG    . ARG A 1 1804 ? 176.507 174.292 165.827 1.00 5.32  ? 1804 ARG A CG    1 
ATOM   2792  C  CD    . ARG A 1 1804 ? 176.188 173.793 164.436 1.00 8.25  ? 1804 ARG A CD    1 
ATOM   2793  N  NE    . ARG A 1 1804 ? 175.489 174.789 163.633 1.00 9.28  ? 1804 ARG A NE    1 
ATOM   2794  C  CZ    . ARG A 1 1804 ? 175.219 174.648 162.343 1.00 7.97  ? 1804 ARG A CZ    1 
ATOM   2795  N  NH1   . ARG A 1 1804 ? 175.603 173.575 161.671 1.00 10.18 ? 1804 ARG A NH1   1 
ATOM   2796  N  NH2   . ARG A 1 1804 ? 174.545 175.604 161.714 1.00 12.05 ? 1804 ARG A NH2   1 
ATOM   2797  N  N     . ARG A 1 1805 ? 180.182 174.189 167.067 1.00 4.98  ? 1805 ARG A N     1 
ATOM   2798  C  CA    . ARG A 1 1805 ? 180.953 173.006 167.434 1.00 3.59  ? 1805 ARG A CA    1 
ATOM   2799  C  C     . ARG A 1 1805 ? 181.211 172.962 168.933 1.00 5.69  ? 1805 ARG A C     1 
ATOM   2800  O  O     . ARG A 1 1805 ? 181.111 171.899 169.558 1.00 8.79  ? 1805 ARG A O     1 
ATOM   2801  C  CB    . ARG A 1 1805 ? 182.274 172.981 166.665 1.00 7.31  ? 1805 ARG A CB    1 
ATOM   2802  C  CG    . ARG A 1 1805 ? 183.102 171.735 166.914 1.00 6.51  ? 1805 ARG A CG    1 
ATOM   2803  C  CD    . ARG A 1 1805 ? 184.583 172.003 166.736 1.00 8.33  ? 1805 ARG A CD    1 
ATOM   2804  N  NE    . ARG A 1 1805 ? 185.165 172.652 167.903 1.00 15.89 ? 1805 ARG A NE    1 
ATOM   2805  C  CZ    . ARG A 1 1805 ? 185.909 173.748 167.859 1.00 15.22 ? 1805 ARG A CZ    1 
ATOM   2806  N  NH1   . ARG A 1 1805 ? 186.196 174.345 166.713 1.00 10.75 ? 1805 ARG A NH1   1 
ATOM   2807  N  NH2   . ARG A 1 1805 ? 186.384 174.256 168.991 1.00 13.50 ? 1805 ARG A NH2   1 
ATOM   2808  N  N     . ARG A 1 1806 ? 181.556 174.104 169.526 1.00 4.95  ? 1806 ARG A N     1 
ATOM   2809  C  CA    . ARG A 1 1806 ? 181.752 174.145 170.970 1.00 5.47  ? 1806 ARG A CA    1 
ATOM   2810  C  C     . ARG A 1 1806 ? 180.444 173.901 171.715 1.00 3.31  ? 1806 ARG A C     1 
ATOM   2811  O  O     . ARG A 1 1806 ? 180.434 173.161 172.703 1.00 3.38  ? 1806 ARG A O     1 
ATOM   2812  C  CB    . ARG A 1 1806 ? 182.396 175.474 171.367 1.00 7.90  ? 1806 ARG A CB    1 
ATOM   2813  C  CG    . ARG A 1 1806 ? 183.784 175.627 170.759 1.00 6.29  ? 1806 ARG A CG    1 
ATOM   2814  C  CD    . ARG A 1 1806 ? 184.507 176.891 171.180 1.00 8.28  ? 1806 ARG A CD    1 
ATOM   2815  N  NE    . ARG A 1 1806 ? 184.923 176.863 172.576 1.00 16.56 ? 1806 ARG A NE    1 
ATOM   2816  C  CZ    . ARG A 1 1806 ? 184.827 177.896 173.403 1.00 14.10 ? 1806 ARG A CZ    1 
ATOM   2817  N  NH1   . ARG A 1 1806 ? 184.353 179.064 172.999 1.00 14.28 ? 1806 ARG A NH1   1 
ATOM   2818  N  NH2   . ARG A 1 1806 ? 185.227 177.757 174.664 1.00 7.76  ? 1806 ARG A NH2   1 
ATOM   2819  N  N     . LYS A 1 1807 ? 179.334 174.469 171.237 1.00 4.25  ? 1807 LYS A N     1 
ATOM   2820  C  CA    . LYS A 1 1807 ? 178.032 174.165 171.825 1.00 2.22  ? 1807 LYS A CA    1 
ATOM   2821  C  C     . LYS A 1 1807 ? 177.739 172.673 171.776 1.00 2.45  ? 1807 LYS A C     1 
ATOM   2822  O  O     . LYS A 1 1807 ? 177.228 172.099 172.745 1.00 2.44  ? 1807 LYS A O     1 
ATOM   2823  C  CB    . LYS A 1 1807 ? 176.926 174.931 171.102 1.00 1.97  ? 1807 LYS A CB    1 
ATOM   2824  C  CG    . LYS A 1 1807 ? 176.797 176.391 171.462 1.00 1.23  ? 1807 LYS A CG    1 
ATOM   2825  C  CD    . LYS A 1 1807 ? 175.702 177.025 170.627 1.00 1.80  ? 1807 LYS A CD    1 
ATOM   2826  C  CE    . LYS A 1 1807 ? 175.446 178.461 171.021 1.00 3.79  ? 1807 LYS A CE    1 
ATOM   2827  N  NZ    . LYS A 1 1807 ? 174.478 179.102 170.092 1.00 4.51  ? 1807 LYS A NZ    1 
ATOM   2828  N  N     . LEU A 1 1808 ? 178.042 172.030 170.646 1.00 5.73  ? 1808 LEU A N     1 
ATOM   2829  C  CA    . LEU A 1 1808 ? 177.844 170.592 170.533 1.00 2.31  ? 1808 LEU A CA    1 
ATOM   2830  C  C     . LEU A 1 1808 ? 178.743 169.835 171.503 1.00 2.56  ? 1808 LEU A C     1 
ATOM   2831  O  O     . LEU A 1 1808 ? 178.339 168.808 172.060 1.00 3.25  ? 1808 LEU A O     1 
ATOM   2832  C  CB    . LEU A 1 1808 ? 178.100 170.144 169.095 1.00 3.41  ? 1808 LEU A CB    1 
ATOM   2833  C  CG    . LEU A 1 1808 ? 177.148 170.689 168.030 1.00 3.34  ? 1808 LEU A CG    1 
ATOM   2834  C  CD1   . LEU A 1 1808 ? 177.816 170.687 166.663 1.00 2.19  ? 1808 LEU A CD1   1 
ATOM   2835  C  CD2   . LEU A 1 1808 ? 175.861 169.889 167.998 1.00 6.37  ? 1808 LEU A CD2   1 
ATOM   2836  N  N     . GLU A 1 1809 ? 179.967 170.320 171.711 1.00 3.05  ? 1809 GLU A N     1 
ATOM   2837  C  CA    . GLU A 1 1809 ? 180.859 169.685 172.675 1.00 3.11  ? 1809 GLU A CA    1 
ATOM   2838  C  C     . GLU A 1 1809 ? 180.314 169.805 174.092 1.00 2.25  ? 1809 GLU A C     1 
ATOM   2839  O  O     . GLU A 1 1809 ? 180.453 168.879 174.898 1.00 1.92  ? 1809 GLU A O     1 
ATOM   2840  C  CB    . GLU A 1 1809 ? 182.259 170.292 172.581 1.00 3.01  ? 1809 GLU A CB    1 
ATOM   2841  C  CG    . GLU A 1 1809 ? 183.043 169.847 171.363 1.00 6.73  ? 1809 GLU A CG    1 
ATOM   2842  C  CD    . GLU A 1 1809 ? 184.177 170.793 171.015 1.00 18.94 ? 1809 GLU A CD    1 
ATOM   2843  O  OE1   . GLU A 1 1809 ? 184.290 171.853 171.662 1.00 18.24 ? 1809 GLU A OE1   1 
ATOM   2844  O  OE2   . GLU A 1 1809 ? 184.957 170.474 170.094 1.00 16.97 ? 1809 GLU A OE2   1 
ATOM   2845  N  N     . HIS A 1 1810 ? 179.700 170.945 174.421 1.00 5.35  ? 1810 HIS A N     1 
ATOM   2846  C  CA    . HIS A 1 1810 ? 179.116 171.102 175.750 1.00 2.59  ? 1810 HIS A CA    1 
ATOM   2847  C  C     . HIS A 1 1810 ? 177.932 170.162 175.942 1.00 2.16  ? 1810 HIS A C     1 
ATOM   2848  O  O     . HIS A 1 1810 ? 177.761 169.577 177.016 1.00 2.70  ? 1810 HIS A O     1 
ATOM   2849  C  CB    . HIS A 1 1810 ? 178.683 172.549 175.985 1.00 2.91  ? 1810 HIS A CB    1 
ATOM   2850  C  CG    . HIS A 1 1810 ? 179.813 173.531 175.994 1.00 5.44  ? 1810 HIS A CG    1 
ATOM   2851  N  ND1   . HIS A 1 1810 ? 180.689 173.646 177.047 1.00 13.33 ? 1810 HIS A ND1   1 
ATOM   2852  C  CD2   . HIS A 1 1810 ? 180.156 174.500 175.115 1.00 12.89 ? 1810 HIS A CD2   1 
ATOM   2853  C  CE1   . HIS A 1 1810 ? 181.564 174.602 176.791 1.00 10.44 ? 1810 HIS A CE1   1 
ATOM   2854  N  NE2   . HIS A 1 1810 ? 181.260 175.138 175.625 1.00 11.52 ? 1810 HIS A NE2   1 
ATOM   2855  N  N     . LEU A 1 1811 ? 177.101 170.012 174.909 1.00 1.60  ? 1811 LEU A N     1 
ATOM   2856  C  CA    . LEU A 1 1811 ? 175.932 169.145 175.013 1.00 1.25  ? 1811 LEU A CA    1 
ATOM   2857  C  C     . LEU A 1 1811 ? 176.331 167.683 175.140 1.00 1.62  ? 1811 LEU A C     1 
ATOM   2858  O  O     . LEU A 1 1811 ? 175.705 166.929 175.894 1.00 3.19  ? 1811 LEU A O     1 
ATOM   2859  C  CB    . LEU A 1 1811 ? 175.024 169.348 173.802 1.00 1.34  ? 1811 LEU A CB    1 
ATOM   2860  C  CG    . LEU A 1 1811 ? 174.049 170.522 173.876 1.00 2.56  ? 1811 LEU A CG    1 
ATOM   2861  C  CD1   . LEU A 1 1811 ? 173.288 170.635 172.574 1.00 4.83  ? 1811 LEU A CD1   1 
ATOM   2862  C  CD2   . LEU A 1 1811 ? 173.095 170.360 175.046 1.00 1.68  ? 1811 LEU A CD2   1 
ATOM   2863  N  N     . ILE A 1 1812 ? 177.361 167.261 174.404 1.00 1.41  ? 1812 ILE A N     1 
ATOM   2864  C  CA    . ILE A 1 1812 ? 177.830 165.883 174.502 1.00 1.11  ? 1812 ILE A CA    1 
ATOM   2865  C  C     . ILE A 1 1812 ? 178.313 165.590 175.916 1.00 1.11  ? 1812 ILE A C     1 
ATOM   2866  O  O     . ILE A 1 1812 ? 178.002 164.540 176.490 1.00 1.25  ? 1812 ILE A O     1 
ATOM   2867  C  CB    . ILE A 1 1812 ? 178.929 165.616 173.457 1.00 1.64  ? 1812 ILE A CB    1 
ATOM   2868  C  CG1   . ILE A 1 1812 ? 178.318 165.475 172.063 1.00 2.70  ? 1812 ILE A CG1   1 
ATOM   2869  C  CG2   . ILE A 1 1812 ? 179.724 164.371 173.814 1.00 1.58  ? 1812 ILE A CG2   1 
ATOM   2870  C  CD1   . ILE A 1 1812 ? 179.337 165.437 170.948 1.00 2.56  ? 1812 ILE A CD1   1 
ATOM   2871  N  N     . THR A 1 1813 ? 179.068 166.521 176.503 1.00 1.18  ? 1813 THR A N     1 
ATOM   2872  C  CA    . THR A 1 1813 ? 179.557 166.329 177.863 1.00 0.96  ? 1813 THR A CA    1 
ATOM   2873  C  C     . THR A 1 1813 ? 178.406 166.250 178.859 1.00 1.12  ? 1813 THR A C     1 
ATOM   2874  O  O     . THR A 1 1813 ? 178.422 165.418 179.772 1.00 1.56  ? 1813 THR A O     1 
ATOM   2875  C  CB    . THR A 1 1813 ? 180.518 167.459 178.234 1.00 1.66  ? 1813 THR A CB    1 
ATOM   2876  O  OG1   . THR A 1 1813 ? 181.523 167.582 177.221 1.00 6.45  ? 1813 THR A OG1   1 
ATOM   2877  C  CG2   . THR A 1 1813 ? 181.192 167.180 179.567 1.00 1.09  ? 1813 THR A CG2   1 
ATOM   2878  N  N     . GLU A 1 1814 ? 177.396 167.106 178.695 1.00 1.65  ? 1814 GLU A N     1 
ATOM   2879  C  CA    . GLU A 1 1814 ? 176.244 167.081 179.588 1.00 1.53  ? 1814 GLU A CA    1 
ATOM   2880  C  C     . GLU A 1 1814 ? 175.453 165.785 179.448 1.00 1.66  ? 1814 GLU A C     1 
ATOM   2881  O  O     . GLU A 1 1814 ? 175.025 165.204 180.451 1.00 1.24  ? 1814 GLU A O     1 
ATOM   2882  C  CB    . GLU A 1 1814 ? 175.344 168.286 179.314 1.00 1.92  ? 1814 GLU A CB    1 
ATOM   2883  C  CG    . GLU A 1 1814 ? 174.190 168.433 180.290 1.00 1.84  ? 1814 GLU A CG    1 
ATOM   2884  C  CD    . GLU A 1 1814 ? 174.597 168.158 181.726 1.00 9.63  ? 1814 GLU A CD    1 
ATOM   2885  O  OE1   . GLU A 1 1814 ? 175.535 168.820 182.217 1.00 5.65  ? 1814 GLU A OE1   1 
ATOM   2886  O  OE2   . GLU A 1 1814 ? 173.978 167.281 182.363 1.00 15.45 ? 1814 GLU A OE2   1 
ATOM   2887  N  N     . LEU A 1 1815 ? 175.245 165.320 178.215 1.00 1.27  ? 1815 LEU A N     1 
ATOM   2888  C  CA    . LEU A 1 1815 ? 174.406 164.144 178.008 1.00 1.05  ? 1815 LEU A CA    1 
ATOM   2889  C  C     . LEU A 1 1815 ? 175.116 162.852 178.385 1.00 0.86  ? 1815 LEU A C     1 
ATOM   2890  O  O     . LEU A 1 1815 ? 174.459 161.892 178.803 1.00 0.96  ? 1815 LEU A O     1 
ATOM   2891  C  CB    . LEU A 1 1815 ? 173.927 164.083 176.562 1.00 0.98  ? 1815 LEU A CB    1 
ATOM   2892  C  CG    . LEU A 1 1815 ? 172.541 164.681 176.321 1.00 2.21  ? 1815 LEU A CG    1 
ATOM   2893  C  CD1   . LEU A 1 1815 ? 172.469 166.160 176.691 1.00 2.11  ? 1815 LEU A CD1   1 
ATOM   2894  C  CD2   . LEU A 1 1815 ? 172.143 164.463 174.888 1.00 3.02  ? 1815 LEU A CD2   1 
ATOM   2895  N  N     . VAL A 1 1816 ? 176.441 162.796 178.239 1.00 1.00  ? 1816 VAL A N     1 
ATOM   2896  C  CA    . VAL A 1 1816 ? 177.179 161.621 178.693 1.00 1.99  ? 1816 VAL A CA    1 
ATOM   2897  C  C     . VAL A 1 1816 ? 176.981 161.425 180.189 1.00 2.34  ? 1816 VAL A C     1 
ATOM   2898  O  O     . VAL A 1 1816 ? 176.814 160.296 180.668 1.00 3.57  ? 1816 VAL A O     1 
ATOM   2899  C  CB    . VAL A 1 1816 ? 178.668 161.745 178.317 1.00 1.98  ? 1816 VAL A CB    1 
ATOM   2900  C  CG1   . VAL A 1 1816 ? 179.516 160.796 179.145 1.00 3.54  ? 1816 VAL A CG1   1 
ATOM   2901  C  CG2   . VAL A 1 1816 ? 178.859 161.455 176.840 1.00 1.02  ? 1816 VAL A CG2   1 
ATOM   2902  N  N     . HIS A 1 1817 ? 176.977 162.522 180.949 1.00 1.14  ? 1817 HIS A N     1 
ATOM   2903  C  CA    . HIS A 1 1817 ? 176.688 162.429 182.374 1.00 0.78  ? 1817 HIS A CA    1 
ATOM   2904  C  C     . HIS A 1 1817 ? 175.243 162.014 182.628 1.00 0.97  ? 1817 HIS A C     1 
ATOM   2905  O  O     . HIS A 1 1817 ? 174.977 161.182 183.501 1.00 2.93  ? 1817 HIS A O     1 
ATOM   2906  C  CB    . HIS A 1 1817 ? 177.001 163.758 183.059 1.00 0.95  ? 1817 HIS A CB    1 
ATOM   2907  C  CG    . HIS A 1 1817 ? 176.614 163.794 184.502 1.00 0.96  ? 1817 HIS A CG    1 
ATOM   2908  N  ND1   . HIS A 1 1817 ? 177.308 163.111 185.476 1.00 1.27  ? 1817 HIS A ND1   1 
ATOM   2909  C  CD2   . HIS A 1 1817 ? 175.613 164.447 185.140 1.00 0.96  ? 1817 HIS A CD2   1 
ATOM   2910  C  CE1   . HIS A 1 1817 ? 176.745 163.331 186.650 1.00 1.81  ? 1817 HIS A CE1   1 
ATOM   2911  N  NE2   . HIS A 1 1817 ? 175.717 164.140 186.475 1.00 2.28  ? 1817 HIS A NE2   1 
ATOM   2912  N  N     . GLN A 1 1818 ? 174.294 162.583 181.879 1.00 1.09  ? 1818 GLN A N     1 
ATOM   2913  C  CA    . GLN A 1 1818 ? 172.897 162.193 182.042 1.00 0.66  ? 1818 GLN A CA    1 
ATOM   2914  C  C     . GLN A 1 1818 ? 172.690 160.732 181.671 1.00 1.57  ? 1818 GLN A C     1 
ATOM   2915  O  O     . GLN A 1 1818 ? 171.897 160.028 182.306 1.00 3.24  ? 1818 GLN A O     1 
ATOM   2916  C  CB    . GLN A 1 1818 ? 171.988 163.090 181.199 1.00 0.67  ? 1818 GLN A CB    1 
ATOM   2917  C  CG    . GLN A 1 1818 ? 171.967 164.544 181.622 1.00 1.39  ? 1818 GLN A CG    1 
ATOM   2918  C  CD    . GLN A 1 1818 ? 171.164 165.409 180.672 1.00 2.55  ? 1818 GLN A CD    1 
ATOM   2919  O  OE1   . GLN A 1 1818 ? 170.675 164.934 179.649 1.00 2.65  ? 1818 GLN A OE1   1 
ATOM   2920  N  NE2   . GLN A 1 1818 ? 171.019 166.683 181.008 1.00 1.89  ? 1818 GLN A NE2   1 
ATOM   2921  N  N     . ARG A 1 1819 ? 173.392 160.260 180.640 1.00 1.29  ? 1819 ARG A N     1 
ATOM   2922  C  CA    . ARG A 1 1819 ? 173.342 158.846 180.292 1.00 1.67  ? 1819 ARG A CA    1 
ATOM   2923  C  C     . ARG A 1 1819 ? 173.870 157.978 181.428 1.00 2.38  ? 1819 ARG A C     1 
ATOM   2924  O  O     . ARG A 1 1819 ? 173.291 156.932 181.740 1.00 2.08  ? 1819 ARG A O     1 
ATOM   2925  C  CB    . ARG A 1 1819 ? 174.143 158.599 179.015 1.00 4.06  ? 1819 ARG A CB    1 
ATOM   2926  C  CG    . ARG A 1 1819 ? 174.155 157.157 178.557 1.00 2.42  ? 1819 ARG A CG    1 
ATOM   2927  C  CD    . ARG A 1 1819 ? 175.202 156.943 177.489 1.00 2.98  ? 1819 ARG A CD    1 
ATOM   2928  N  NE    . ARG A 1 1819 ? 176.536 157.323 177.935 1.00 4.61  ? 1819 ARG A NE    1 
ATOM   2929  C  CZ    . ARG A 1 1819 ? 177.589 157.412 177.134 1.00 5.88  ? 1819 ARG A CZ    1 
ATOM   2930  N  NH1   . ARG A 1 1819 ? 177.491 157.171 175.837 1.00 3.55  ? 1819 ARG A NH1   1 
ATOM   2931  N  NH2   . ARG A 1 1819 ? 178.768 157.753 177.646 1.00 10.95 ? 1819 ARG A NH2   1 
ATOM   2932  N  N     . ASP A 1 1820 ? 174.970 158.399 182.054 1.00 3.03  ? 1820 ASP A N     1 
ATOM   2933  C  CA    . ASP A 1 1820 ? 175.551 157.623 183.144 1.00 1.86  ? 1820 ASP A CA    1 
ATOM   2934  C  C     . ASP A 1 1820 ? 174.650 157.624 184.372 1.00 3.14  ? 1820 ASP A C     1 
ATOM   2935  O  O     . ASP A 1 1820 ? 174.496 156.592 185.035 1.00 6.39  ? 1820 ASP A O     1 
ATOM   2936  C  CB    . ASP A 1 1820 ? 176.935 158.169 183.490 1.00 2.84  ? 1820 ASP A CB    1 
ATOM   2937  C  CG    . ASP A 1 1820 ? 177.992 157.751 182.487 1.00 18.99 ? 1820 ASP A CG    1 
ATOM   2938  O  OD1   . ASP A 1 1820 ? 177.717 156.839 181.678 1.00 14.57 ? 1820 ASP A OD1   1 
ATOM   2939  O  OD2   . ASP A 1 1820 ? 179.096 158.335 182.504 1.00 18.58 ? 1820 ASP A OD2   1 
ATOM   2940  N  N     . VAL A 1 1821 ? 174.054 158.772 184.697 1.00 2.17  ? 1821 VAL A N     1 
ATOM   2941  C  CA    . VAL A 1 1821 ? 173.167 158.849 185.853 1.00 3.15  ? 1821 VAL A CA    1 
ATOM   2942  C  C     . VAL A 1 1821 ? 171.913 158.014 185.621 1.00 2.36  ? 1821 VAL A C     1 
ATOM   2943  O  O     . VAL A 1 1821 ? 171.460 157.291 186.517 1.00 3.78  ? 1821 VAL A O     1 
ATOM   2944  C  CB    . VAL A 1 1821 ? 172.824 160.315 186.167 1.00 1.38  ? 1821 VAL A CB    1 
ATOM   2945  C  CG1   . VAL A 1 1821 ? 171.723 160.394 187.209 1.00 0.98  ? 1821 VAL A CG1   1 
ATOM   2946  C  CG2   . VAL A 1 1821 ? 174.061 161.053 186.641 1.00 0.83  ? 1821 VAL A CG2   1 
ATOM   2947  N  N     . THR A 1 1822 ? 171.334 158.096 184.423 1.00 1.85  ? 1822 THR A N     1 
ATOM   2948  C  CA    . THR A 1 1822 ? 170.131 157.328 184.129 1.00 2.75  ? 1822 THR A CA    1 
ATOM   2949  C  C     . THR A 1 1822 ? 170.421 155.832 184.148 1.00 4.43  ? 1822 THR A C     1 
ATOM   2950  O  O     . THR A 1 1822 ? 169.603 155.040 184.630 1.00 5.29  ? 1822 THR A O     1 
ATOM   2951  C  CB    . THR A 1 1822 ? 169.552 157.752 182.779 1.00 3.48  ? 1822 THR A CB    1 
ATOM   2952  O  OG1   . THR A 1 1822 ? 169.233 159.146 182.818 1.00 2.37  ? 1822 THR A OG1   1 
ATOM   2953  C  CG2   . THR A 1 1822 ? 168.281 156.977 182.482 1.00 3.59  ? 1822 THR A CG2   1 
ATOM   2954  N  N     . ARG A 1 1823 ? 171.584 155.427 183.631 1.00 4.29  ? 1823 ARG A N     1 
ATOM   2955  C  CA    . ARG A 1 1823 ? 171.978 154.024 183.700 1.00 3.32  ? 1823 ARG A CA    1 
ATOM   2956  C  C     . ARG A 1 1823 ? 172.140 153.570 185.146 1.00 4.90  ? 1823 ARG A C     1 
ATOM   2957  O  O     . ARG A 1 1823 ? 171.730 152.459 185.504 1.00 7.16  ? 1823 ARG A O     1 
ATOM   2958  C  CB    . ARG A 1 1823 ? 173.275 153.803 182.924 1.00 2.35  ? 1823 ARG A CB    1 
ATOM   2959  C  CG    . ARG A 1 1823 ? 173.086 153.583 181.438 1.00 2.35  ? 1823 ARG A CG    1 
ATOM   2960  C  CD    . ARG A 1 1823 ? 174.408 153.694 180.705 1.00 3.10  ? 1823 ARG A CD    1 
ATOM   2961  N  NE    . ARG A 1 1823 ? 174.276 153.379 179.290 1.00 4.73  ? 1823 ARG A NE    1 
ATOM   2962  C  CZ    . ARG A 1 1823 ? 175.234 153.553 178.391 1.00 6.95  ? 1823 ARG A CZ    1 
ATOM   2963  N  NH1   . ARG A 1 1823 ? 176.415 154.046 178.726 1.00 8.96  ? 1823 ARG A NH1   1 
ATOM   2964  N  NH2   . ARG A 1 1823 ? 175.003 153.225 177.123 1.00 7.45  ? 1823 ARG A NH2   1 
ATOM   2965  N  N     . SER A 1 1824 ? 172.737 154.415 185.987 1.00 3.47  ? 1824 SER A N     1 
ATOM   2966  C  CA    . SER A 1 1824 ? 172.875 154.083 187.401 1.00 4.42  ? 1824 SER A CA    1 
ATOM   2967  C  C     . SER A 1 1824 ? 171.512 153.964 188.073 1.00 7.58  ? 1824 SER A C     1 
ATOM   2968  O  O     . SER A 1 1824 ? 171.303 153.087 188.918 1.00 11.73 ? 1824 SER A O     1 
ATOM   2969  C  CB    . SER A 1 1824 ? 173.732 155.135 188.103 1.00 3.23  ? 1824 SER A CB    1 
ATOM   2970  O  OG    . SER A 1 1824 ? 173.861 154.858 189.483 1.00 9.74  ? 1824 SER A OG    1 
ATOM   2971  N  N     . LEU A 1 1825 ? 170.571 154.840 187.711 1.00 5.86  ? 1825 LEU A N     1 
ATOM   2972  C  CA    . LEU A 1 1825 ? 169.229 154.768 188.278 1.00 5.48  ? 1825 LEU A CA    1 
ATOM   2973  C  C     . LEU A 1 1825 ? 168.524 153.479 187.870 1.00 7.49  ? 1825 LEU A C     1 
ATOM   2974  O  O     . LEU A 1 1825 ? 167.829 152.860 188.683 1.00 14.42 ? 1825 LEU A O     1 
ATOM   2975  C  CB    . LEU A 1 1825 ? 168.412 155.985 187.844 1.00 6.90  ? 1825 LEU A CB    1 
ATOM   2976  C  CG    . LEU A 1 1825 ? 168.818 157.346 188.415 1.00 5.73  ? 1825 LEU A CG    1 
ATOM   2977  C  CD1   . LEU A 1 1825 ? 167.857 158.425 187.953 1.00 4.53  ? 1825 LEU A CD1   1 
ATOM   2978  C  CD2   . LEU A 1 1825 ? 168.894 157.307 189.932 1.00 4.29  ? 1825 LEU A CD2   1 
ATOM   2979  N  N     . ILE A 1 1826 ? 168.679 153.066 186.612 1.00 6.93  ? 1826 ILE A N     1 
ATOM   2980  C  CA    . ILE A 1 1826 ? 168.044 151.836 186.150 1.00 8.93  ? 1826 ILE A CA    1 
ATOM   2981  C  C     . ILE A 1 1826 ? 168.693 150.619 186.798 1.00 10.05 ? 1826 ILE A C     1 
ATOM   2982  O  O     . ILE A 1 1826 ? 168.005 149.678 187.209 1.00 14.34 ? 1826 ILE A O     1 
ATOM   2983  C  CB    . ILE A 1 1826 ? 168.094 151.756 184.612 1.00 5.49  ? 1826 ILE A CB    1 
ATOM   2984  C  CG1   . ILE A 1 1826 ? 167.273 152.887 183.994 1.00 8.76  ? 1826 ILE A CG1   1 
ATOM   2985  C  CG2   . ILE A 1 1826 ? 167.591 150.406 184.130 1.00 6.70  ? 1826 ILE A CG2   1 
ATOM   2986  C  CD1   . ILE A 1 1826 ? 167.420 152.999 182.492 1.00 8.85  ? 1826 ILE A CD1   1 
ATOM   2987  N  N     . LYS A 1 1827 ? 170.024 150.619 186.903 1.00 9.27  ? 1827 LYS A N     1 
ATOM   2988  C  CA    . LYS A 1 1827 ? 170.724 149.478 187.484 1.00 11.25 ? 1827 LYS A CA    1 
ATOM   2989  C  C     . LYS A 1 1827 ? 170.385 149.303 188.958 1.00 13.65 ? 1827 LYS A C     1 
ATOM   2990  O  O     . LYS A 1 1827 ? 170.368 148.174 189.462 1.00 26.04 ? 1827 LYS A O     1 
ATOM   2991  C  CB    . LYS A 1 1827 ? 172.233 149.645 187.294 1.00 11.68 ? 1827 LYS A CB    1 
ATOM   2992  C  CG    . LYS A 1 1827 ? 173.074 148.498 187.823 1.00 15.20 ? 1827 LYS A CG    1 
ATOM   2993  C  CD    . LYS A 1 1827 ? 174.554 148.766 187.614 1.00 19.01 ? 1827 LYS A CD    1 
ATOM   2994  C  CE    . LYS A 1 1827 ? 175.391 147.532 187.899 1.00 24.37 ? 1827 LYS A CE    1 
ATOM   2995  N  NZ    . LYS A 1 1827 ? 175.027 146.397 187.007 1.00 26.27 ? 1827 LYS A NZ    1 
ATOM   2996  N  N     . SER A 1 1828 ? 170.100 150.395 189.659 1.00 9.67  ? 1828 SER A N     1 
ATOM   2997  C  CA    . SER A 1 1828 ? 169.781 150.351 191.079 1.00 9.97  ? 1828 SER A CA    1 
ATOM   2998  C  C     . SER A 1 1828 ? 168.292 150.195 191.351 1.00 12.33 ? 1828 SER A C     1 
ATOM   2999  O  O     . SER A 1 1828 ? 167.890 150.204 192.519 1.00 13.57 ? 1828 SER A O     1 
ATOM   3000  C  CB    . SER A 1 1828 ? 170.302 151.611 191.772 1.00 12.06 ? 1828 SER A CB    1 
ATOM   3001  O  OG    . SER A 1 1828 ? 171.712 151.578 191.887 1.00 17.76 ? 1828 SER A OG    1 
ATOM   3002  N  N     . LYS A 1 1829 ? 167.473 150.060 190.307 1.00 12.57 ? 1829 LYS A N     1 
ATOM   3003  C  CA    . LYS A 1 1829 ? 166.036 149.813 190.440 1.00 13.56 ? 1829 LYS A CA    1 
ATOM   3004  C  C     . LYS A 1 1829 ? 165.352 150.890 191.279 1.00 13.48 ? 1829 LYS A C     1 
ATOM   3005  O  O     . LYS A 1 1829 ? 164.538 150.598 192.156 1.00 18.40 ? 1829 LYS A O     1 
ATOM   3006  C  CB    . LYS A 1 1829 ? 165.772 148.422 191.021 1.00 17.20 ? 1829 LYS A CB    1 
ATOM   3007  C  CG    . LYS A 1 1829 ? 166.295 147.286 190.161 1.00 17.40 ? 1829 LYS A CG    1 
ATOM   3008  C  CD    . LYS A 1 1829 ? 165.624 147.272 188.798 1.00 22.57 ? 1829 LYS A CD    1 
ATOM   3009  C  CE    . LYS A 1 1829 ? 164.148 146.930 188.911 1.00 25.41 ? 1829 LYS A CE    1 
ATOM   3010  N  NZ    . LYS A 1 1829 ? 163.942 145.544 189.416 1.00 25.49 ? 1829 LYS A NZ    1 
ATOM   3011  N  N     . ILE A 1 1830 ? 165.679 152.152 191.003 1.00 14.28 ? 1830 ILE A N     1 
ATOM   3012  C  CA    . ILE A 1 1830 ? 165.046 153.261 191.705 1.00 14.28 ? 1830 ILE A CA    1 
ATOM   3013  C  C     . ILE A 1 1830 ? 163.667 153.515 191.112 1.00 15.88 ? 1830 ILE A C     1 
ATOM   3014  O  O     . ILE A 1 1830 ? 163.517 153.698 189.897 1.00 28.09 ? 1830 ILE A O     1 
ATOM   3015  C  CB    . ILE A 1 1830 ? 165.925 154.517 191.636 1.00 11.75 ? 1830 ILE A CB    1 
ATOM   3016  C  CG1   . ILE A 1 1830 ? 167.288 154.232 192.265 1.00 11.39 ? 1830 ILE A CG1   1 
ATOM   3017  C  CG2   . ILE A 1 1830 ? 165.241 155.687 192.318 1.00 12.46 ? 1830 ILE A CG2   1 
ATOM   3018  C  CD1   . ILE A 1 1830 ? 167.203 153.848 193.721 1.00 17.42 ? 1830 ILE A CD1   1 
ATOM   3019  N  N     . ASP A 1 1831 ? 162.650 153.529 191.974 1.00 14.65 ? 1831 ASP A N     1 
ATOM   3020  C  CA    . ASP A 1 1831 ? 161.270 153.699 191.542 1.00 14.17 ? 1831 ASP A CA    1 
ATOM   3021  C  C     . ASP A 1 1831 ? 160.569 154.851 192.254 1.00 17.66 ? 1831 ASP A C     1 
ATOM   3022  O  O     . ASP A 1 1831 ? 159.374 155.067 192.025 1.00 18.17 ? 1831 ASP A O     1 
ATOM   3023  C  CB    . ASP A 1 1831 ? 160.485 152.400 191.752 1.00 19.15 ? 1831 ASP A CB    1 
ATOM   3024  C  CG    . ASP A 1 1831 ? 160.616 151.862 193.164 1.00 24.02 ? 1831 ASP A CG    1 
ATOM   3025  O  OD1   . ASP A 1 1831 ? 161.261 152.524 194.002 1.00 27.24 ? 1831 ASP A OD1   1 
ATOM   3026  O  OD2   . ASP A 1 1831 ? 160.076 150.771 193.437 1.00 30.63 ? 1831 ASP A OD2   1 
ATOM   3027  N  N     . ASN A 1 1832 ? 161.274 155.590 193.104 1.00 11.71 ? 1832 ASN A N     1 
ATOM   3028  C  CA    . ASN A 1 1832 ? 160.688 156.679 193.867 1.00 10.36 ? 1832 ASN A CA    1 
ATOM   3029  C  C     . ASN A 1 1832 ? 161.500 157.946 193.643 1.00 11.76 ? 1832 ASN A C     1 
ATOM   3030  O  O     . ASN A 1 1832 ? 162.733 157.911 193.638 1.00 10.05 ? 1832 ASN A O     1 
ATOM   3031  C  CB    . ASN A 1 1832 ? 160.636 156.329 195.361 1.00 10.08 ? 1832 ASN A CB    1 
ATOM   3032  C  CG    . ASN A 1 1832 ? 160.292 157.518 196.231 1.00 16.86 ? 1832 ASN A CG    1 
ATOM   3033  O  OD1   . ASN A 1 1832 ? 159.512 158.386 195.841 1.00 21.15 ? 1832 ASN A OD1   1 
ATOM   3034  N  ND2   . ASN A 1 1832 ? 160.871 157.559 197.425 1.00 22.79 ? 1832 ASN A ND2   1 
ATOM   3035  N  N     . ALA A 1 1833 ? 160.798 159.065 193.453 1.00 10.49 ? 1833 ALA A N     1 
ATOM   3036  C  CA    . ALA A 1 1833 ? 161.468 160.344 193.254 1.00 5.75  ? 1833 ALA A CA    1 
ATOM   3037  C  C     . ALA A 1 1833 ? 162.152 160.843 194.519 1.00 8.77  ? 1833 ALA A C     1 
ATOM   3038  O  O     . ALA A 1 1833 ? 163.063 161.672 194.428 1.00 7.74  ? 1833 ALA A O     1 
ATOM   3039  C  CB    . ALA A 1 1833 ? 160.474 161.392 192.757 1.00 9.91  ? 1833 ALA A CB    1 
ATOM   3040  N  N     . LYS A 1 1834 ? 161.740 160.359 195.687 1.00 10.01 ? 1834 LYS A N     1 
ATOM   3041  C  CA    . LYS A 1 1834 ? 162.337 160.765 196.951 1.00 9.38  ? 1834 LYS A CA    1 
ATOM   3042  C  C     . LYS A 1 1834 ? 163.506 159.880 197.362 1.00 8.27  ? 1834 LYS A C     1 
ATOM   3043  O  O     . LYS A 1 1834 ? 164.058 160.075 198.448 1.00 9.56  ? 1834 LYS A O     1 
ATOM   3044  C  CB    . LYS A 1 1834 ? 161.278 160.773 198.055 1.00 12.02 ? 1834 LYS A CB    1 
ATOM   3045  C  CG    . LYS A 1 1834 ? 160.272 161.906 197.939 1.00 10.81 ? 1834 LYS A CG    1 
ATOM   3046  C  CD    . LYS A 1 1834 ? 160.958 163.257 197.941 1.00 14.12 ? 1834 LYS A CD    1 
ATOM   3047  C  CE    . LYS A 1 1834 ? 160.119 164.301 197.220 1.00 18.17 ? 1834 LYS A CE    1 
ATOM   3048  N  NZ    . LYS A 1 1834 ? 160.206 164.163 195.739 1.00 17.47 ? 1834 LYS A NZ    1 
ATOM   3049  N  N     . SER A 1 1835 ? 163.884 158.914 196.529 1.00 7.91  ? 1835 SER A N     1 
ATOM   3050  C  CA    . SER A 1 1835 ? 165.068 158.113 196.797 1.00 5.86  ? 1835 SER A CA    1 
ATOM   3051  C  C     . SER A 1 1835 ? 166.310 158.990 196.765 1.00 5.75  ? 1835 SER A C     1 
ATOM   3052  O  O     . SER A 1 1835 ? 166.419 159.913 195.953 1.00 9.82  ? 1835 SER A O     1 
ATOM   3053  C  CB    . SER A 1 1835 ? 165.193 156.989 195.771 1.00 8.25  ? 1835 SER A CB    1 
ATOM   3054  O  OG    . SER A 1 1835 ? 166.429 156.312 195.904 1.00 18.09 ? 1835 SER A OG    1 
ATOM   3055  N  N     . PHE A 1 1836 ? 167.256 158.702 197.662 1.00 5.33  ? 1836 PHE A N     1 
ATOM   3056  C  CA    . PHE A 1 1836 ? 168.431 159.551 197.773 1.00 3.41  ? 1836 PHE A CA    1 
ATOM   3057  C  C     . PHE A 1 1836 ? 169.349 159.452 196.564 1.00 2.95  ? 1836 PHE A C     1 
ATOM   3058  O  O     . PHE A 1 1836 ? 170.041 160.425 196.253 1.00 2.55  ? 1836 PHE A O     1 
ATOM   3059  C  CB    . PHE A 1 1836 ? 169.217 159.227 199.041 1.00 1.70  ? 1836 PHE A CB    1 
ATOM   3060  C  CG    . PHE A 1 1836 ? 170.261 160.246 199.366 1.00 1.26  ? 1836 PHE A CG    1 
ATOM   3061  C  CD1   . PHE A 1 1836 ? 169.899 161.516 199.782 1.00 1.37  ? 1836 PHE A CD1   1 
ATOM   3062  C  CD2   . PHE A 1 1836 ? 171.603 159.951 199.232 1.00 0.67  ? 1836 PHE A CD2   1 
ATOM   3063  C  CE1   . PHE A 1 1836 ? 170.855 162.463 200.073 1.00 1.25  ? 1836 PHE A CE1   1 
ATOM   3064  C  CE2   . PHE A 1 1836 ? 172.563 160.896 199.521 1.00 0.60  ? 1836 PHE A CE2   1 
ATOM   3065  C  CZ    . PHE A 1 1836 ? 172.191 162.149 199.942 1.00 0.80  ? 1836 PHE A CZ    1 
ATOM   3066  N  N     . GLU A 1 1837 ? 169.377 158.307 195.877 1.00 5.61  ? 1837 GLU A N     1 
ATOM   3067  C  CA    . GLU A 1 1837 ? 170.226 158.194 194.697 1.00 6.29  ? 1837 GLU A CA    1 
ATOM   3068  C  C     . GLU A 1 1837 ? 169.760 159.117 193.580 1.00 3.36  ? 1837 GLU A C     1 
ATOM   3069  O  O     . GLU A 1 1837 ? 170.537 159.433 192.673 1.00 6.01  ? 1837 GLU A O     1 
ATOM   3070  C  CB    . GLU A 1 1837 ? 170.284 156.743 194.220 1.00 7.14  ? 1837 GLU A CB    1 
ATOM   3071  C  CG    . GLU A 1 1837 ? 170.994 155.822 195.194 1.00 12.13 ? 1837 GLU A CG    1 
ATOM   3072  C  CD    . GLU A 1 1837 ? 171.032 154.387 194.724 1.00 27.37 ? 1837 GLU A CD    1 
ATOM   3073  O  OE1   . GLU A 1 1837 ? 170.394 154.084 193.696 1.00 30.75 ? 1837 GLU A OE1   1 
ATOM   3074  O  OE2   . GLU A 1 1837 ? 171.697 153.561 195.382 1.00 28.26 ? 1837 GLU A OE2   1 
ATOM   3075  N  N     . TRP A 1 1838 ? 168.504 159.560 193.625 1.00 3.13  ? 1838 TRP A N     1 
ATOM   3076  C  CA    . TRP A 1 1838 ? 168.044 160.622 192.739 1.00 2.07  ? 1838 TRP A CA    1 
ATOM   3077  C  C     . TRP A 1 1838 ? 168.207 162.001 193.368 1.00 2.34  ? 1838 TRP A C     1 
ATOM   3078  O  O     . TRP A 1 1838 ? 168.580 162.954 192.676 1.00 2.56  ? 1838 TRP A O     1 
ATOM   3079  C  CB    . TRP A 1 1838 ? 166.580 160.396 192.353 1.00 1.90  ? 1838 TRP A CB    1 
ATOM   3080  C  CG    . TRP A 1 1838 ? 165.994 161.496 191.510 1.00 1.51  ? 1838 TRP A CG    1 
ATOM   3081  C  CD1   . TRP A 1 1838 ? 164.836 162.175 191.747 1.00 1.58  ? 1838 TRP A CD1   1 
ATOM   3082  C  CD2   . TRP A 1 1838 ? 166.529 162.033 190.292 1.00 1.42  ? 1838 TRP A CD2   1 
ATOM   3083  N  NE1   . TRP A 1 1838 ? 164.620 163.103 190.762 1.00 1.49  ? 1838 TRP A NE1   1 
ATOM   3084  C  CE2   . TRP A 1 1838 ? 165.644 163.036 189.854 1.00 1.68  ? 1838 TRP A CE2   1 
ATOM   3085  C  CE3   . TRP A 1 1838 ? 167.671 161.766 189.529 1.00 1.04  ? 1838 TRP A CE3   1 
ATOM   3086  C  CZ2   . TRP A 1 1838 ? 165.864 163.774 188.693 1.00 1.44  ? 1838 TRP A CZ2   1 
ATOM   3087  C  CZ3   . TRP A 1 1838 ? 167.887 162.496 188.379 1.00 0.90  ? 1838 TRP A CZ3   1 
ATOM   3088  C  CH2   . TRP A 1 1838 ? 166.988 163.489 187.972 1.00 1.12  ? 1838 TRP A CH2   1 
ATOM   3089  N  N     . LEU A 1 1839 ? 167.937 162.126 194.669 1.00 2.11  ? 1839 LEU A N     1 
ATOM   3090  C  CA    . LEU A 1 1839 ? 168.083 163.417 195.335 1.00 1.06  ? 1839 LEU A CA    1 
ATOM   3091  C  C     . LEU A 1 1839 ? 169.538 163.864 195.371 1.00 0.79  ? 1839 LEU A C     1 
ATOM   3092  O  O     . LEU A 1 1839 ? 169.824 165.063 195.279 1.00 3.16  ? 1839 LEU A O     1 
ATOM   3093  C  CB    . LEU A 1 1839 ? 167.509 163.353 196.750 1.00 2.00  ? 1839 LEU A CB    1 
ATOM   3094  C  CG    . LEU A 1 1839 ? 166.000 163.154 196.883 1.00 1.91  ? 1839 LEU A CG    1 
ATOM   3095  C  CD1   . LEU A 1 1839 ? 165.621 163.035 198.345 1.00 1.91  ? 1839 LEU A CD1   1 
ATOM   3096  C  CD2   . LEU A 1 1839 ? 165.238 164.290 196.218 1.00 1.57  ? 1839 LEU A CD2   1 
ATOM   3097  N  N     . SER A 1 1840 ? 170.470 162.919 195.508 1.00 1.00  ? 1840 SER A N     1 
ATOM   3098  C  CA    . SER A 1 1840 ? 171.887 163.263 195.499 1.00 0.96  ? 1840 SER A CA    1 
ATOM   3099  C  C     . SER A 1 1840 ? 172.342 163.811 194.154 1.00 1.17  ? 1840 SER A C     1 
ATOM   3100  O  O     . SER A 1 1840 ? 173.347 164.526 194.099 1.00 1.77  ? 1840 SER A O     1 
ATOM   3101  C  CB    . SER A 1 1840 ? 172.726 162.043 195.879 1.00 0.95  ? 1840 SER A CB    1 
ATOM   3102  O  OG    . SER A 1 1840 ? 172.468 160.956 195.007 1.00 2.33  ? 1840 SER A OG    1 
ATOM   3103  N  N     . GLN A 1 1841 ? 171.634 163.490 193.074 1.00 0.92  ? 1841 GLN A N     1 
ATOM   3104  C  CA    . GLN A 1 1841 ? 171.939 164.064 191.773 1.00 0.82  ? 1841 GLN A CA    1 
ATOM   3105  C  C     . GLN A 1 1841 ? 171.550 165.537 191.730 1.00 0.65  ? 1841 GLN A C     1 
ATOM   3106  O  O     . GLN A 1 1841 ? 170.634 165.981 192.427 1.00 0.81  ? 1841 GLN A O     1 
ATOM   3107  C  CB    . GLN A 1 1841 ? 171.205 163.304 190.667 1.00 0.80  ? 1841 GLN A CB    1 
ATOM   3108  C  CG    . GLN A 1 1841 ? 171.487 161.817 190.632 1.00 1.09  ? 1841 GLN A CG    1 
ATOM   3109  C  CD    . GLN A 1 1841 ? 172.967 161.501 190.652 1.00 1.17  ? 1841 GLN A CD    1 
ATOM   3110  O  OE1   . GLN A 1 1841 ? 173.726 161.986 189.816 1.00 3.71  ? 1841 GLN A OE1   1 
ATOM   3111  N  NE2   . GLN A 1 1841 ? 173.384 160.685 191.607 1.00 2.23  ? 1841 GLN A NE2   1 
ATOM   3112  N  N     . MET A 1 1842 ? 172.259 166.297 190.902 1.00 0.53  ? 1842 MET A N     1 
ATOM   3113  C  CA    . MET A 1 1842 ? 171.923 167.697 190.682 1.00 0.39  ? 1842 MET A CA    1 
ATOM   3114  C  C     . MET A 1 1842 ? 170.720 167.780 189.749 1.00 0.25  ? 1842 MET A C     1 
ATOM   3115  O  O     . MET A 1 1842 ? 170.786 167.329 188.601 1.00 0.40  ? 1842 MET A O     1 
ATOM   3116  C  CB    . MET A 1 1842 ? 173.114 168.451 190.101 1.00 0.33  ? 1842 MET A CB    1 
ATOM   3117  C  CG    . MET A 1 1842 ? 172.846 169.922 189.855 1.00 0.44  ? 1842 MET A CG    1 
ATOM   3118  S  SD    . MET A 1 1842 ? 174.351 170.909 189.846 1.00 7.95  ? 1842 MET A SD    1 
ATOM   3119  C  CE    . MET A 1 1842 ? 174.584 171.190 191.595 1.00 0.14  ? 1842 MET A CE    1 
ATOM   3120  N  N     . ARG A 1 1843 ? 169.626 168.346 190.242 1.00 0.35  ? 1843 ARG A N     1 
ATOM   3121  C  CA    . ARG A 1 1843 ? 168.363 168.375 189.525 1.00 0.35  ? 1843 ARG A CA    1 
ATOM   3122  C  C     . ARG A 1 1843 ? 167.985 169.807 189.174 1.00 0.25  ? 1843 ARG A C     1 
ATOM   3123  O  O     . ARG A 1 1843 ? 168.476 170.770 189.768 1.00 0.45  ? 1843 ARG A O     1 
ATOM   3124  C  CB    . ARG A 1 1843 ? 167.260 167.707 190.351 1.00 0.90  ? 1843 ARG A CB    1 
ATOM   3125  C  CG    . ARG A 1 1843 ? 167.692 166.380 190.958 1.00 1.11  ? 1843 ARG A CG    1 
ATOM   3126  C  CD    . ARG A 1 1843 ? 166.571 165.698 191.719 1.00 3.31  ? 1843 ARG A CD    1 
ATOM   3127  N  NE    . ARG A 1 1843 ? 165.970 166.553 192.737 1.00 4.30  ? 1843 ARG A NE    1 
ATOM   3128  C  CZ    . ARG A 1 1843 ? 166.553 166.897 193.877 1.00 1.73  ? 1843 ARG A CZ    1 
ATOM   3129  N  NH1   . ARG A 1 1843 ? 167.762 166.465 194.195 1.00 0.53  ? 1843 ARG A NH1   1 
ATOM   3130  N  NH2   . ARG A 1 1843 ? 165.906 167.693 194.720 1.00 6.16  ? 1843 ARG A NH2   1 
ATOM   3131  N  N     . PHE A 1 1844 ? 167.113 169.937 188.177 1.00 0.60  ? 1844 PHE A N     1 
ATOM   3132  C  CA    . PHE A 1 1844 ? 166.755 171.228 187.600 1.00 0.54  ? 1844 PHE A CA    1 
ATOM   3133  C  C     . PHE A 1 1844 ? 165.246 171.276 187.412 1.00 0.65  ? 1844 PHE A C     1 
ATOM   3134  O  O     . PHE A 1 1844 ? 164.704 170.592 186.539 1.00 1.21  ? 1844 PHE A O     1 
ATOM   3135  C  CB    . PHE A 1 1844 ? 167.478 171.457 186.270 1.00 0.36  ? 1844 PHE A CB    1 
ATOM   3136  C  CG    . PHE A 1 1844 ? 168.970 171.343 186.368 1.00 0.21  ? 1844 PHE A CG    1 
ATOM   3137  C  CD1   . PHE A 1 1844 ? 169.592 170.104 186.321 1.00 0.33  ? 1844 PHE A CD1   1 
ATOM   3138  C  CD2   . PHE A 1 1844 ? 169.751 172.471 186.516 1.00 0.14  ? 1844 PHE A CD2   1 
ATOM   3139  C  CE1   . PHE A 1 1844 ? 170.962 170.000 186.420 1.00 0.34  ? 1844 PHE A CE1   1 
ATOM   3140  C  CE2   . PHE A 1 1844 ? 171.120 172.371 186.614 1.00 0.27  ? 1844 PHE A CE2   1 
ATOM   3141  C  CZ    . PHE A 1 1844 ? 171.728 171.134 186.565 1.00 0.23  ? 1844 PHE A CZ    1 
ATOM   3142  N  N     . TYR A 1 1845 ? 164.575 172.086 188.225 1.00 0.80  ? 1845 TYR A N     1 
ATOM   3143  C  CA    . TYR A 1 1845 ? 163.128 172.242 188.174 1.00 1.88  ? 1845 TYR A CA    1 
ATOM   3144  C  C     . TYR A 1 1845 ? 162.793 173.619 187.622 1.00 2.09  ? 1845 TYR A C     1 
ATOM   3145  O  O     . TYR A 1 1845 ? 163.341 174.627 188.078 1.00 1.20  ? 1845 TYR A O     1 
ATOM   3146  C  CB    . TYR A 1 1845 ? 162.507 172.054 189.559 1.00 1.27  ? 1845 TYR A CB    1 
ATOM   3147  C  CG    . TYR A 1 1845 ? 162.814 170.711 190.173 1.00 5.55  ? 1845 TYR A CG    1 
ATOM   3148  C  CD1   . TYR A 1 1845 ? 163.979 170.510 190.901 1.00 3.88  ? 1845 TYR A CD1   1 
ATOM   3149  C  CD2   . TYR A 1 1845 ? 161.945 169.642 190.015 1.00 5.52  ? 1845 TYR A CD2   1 
ATOM   3150  C  CE1   . TYR A 1 1845 ? 164.264 169.282 191.458 1.00 3.21  ? 1845 TYR A CE1   1 
ATOM   3151  C  CE2   . TYR A 1 1845 ? 162.223 168.413 190.569 1.00 4.27  ? 1845 TYR A CE2   1 
ATOM   3152  C  CZ    . TYR A 1 1845 ? 163.384 168.238 191.288 1.00 5.26  ? 1845 TYR A CZ    1 
ATOM   3153  O  OH    . TYR A 1 1845 ? 163.663 167.012 191.842 1.00 8.64  ? 1845 TYR A OH    1 
ATOM   3154  N  N     . PHE A 1 1846 ? 161.897 173.657 186.642 1.00 2.42  ? 1846 PHE A N     1 
ATOM   3155  C  CA    . PHE A 1 1846 ? 161.509 174.889 185.974 1.00 2.93  ? 1846 PHE A CA    1 
ATOM   3156  C  C     . PHE A 1 1846 ? 160.007 175.078 186.135 1.00 6.37  ? 1846 PHE A C     1 
ATOM   3157  O  O     . PHE A 1 1846 ? 159.224 174.198 185.767 1.00 11.03 ? 1846 PHE A O     1 
ATOM   3158  C  CB    . PHE A 1 1846 ? 161.905 174.849 184.497 1.00 5.37  ? 1846 PHE A CB    1 
ATOM   3159  C  CG    . PHE A 1 1846 ? 161.612 176.116 183.751 1.00 5.86  ? 1846 PHE A CG    1 
ATOM   3160  C  CD1   . PHE A 1 1846 ? 162.549 177.134 183.701 1.00 4.14  ? 1846 PHE A CD1   1 
ATOM   3161  C  CD2   . PHE A 1 1846 ? 160.412 176.284 183.084 1.00 7.15  ? 1846 PHE A CD2   1 
ATOM   3162  C  CE1   . PHE A 1 1846 ? 162.288 178.297 183.011 1.00 5.08  ? 1846 PHE A CE1   1 
ATOM   3163  C  CE2   . PHE A 1 1846 ? 160.146 177.445 182.392 1.00 9.00  ? 1846 PHE A CE2   1 
ATOM   3164  C  CZ    . PHE A 1 1846 ? 161.086 178.452 182.356 1.00 7.51  ? 1846 PHE A CZ    1 
ATOM   3165  N  N     . ASP A 1 1847 ? 159.609 176.223 186.683 1.00 10.09 ? 1847 ASP A N     1 
ATOM   3166  C  CA    . ASP A 1 1847 ? 158.197 176.551 186.853 1.00 11.44 ? 1847 ASP A CA    1 
ATOM   3167  C  C     . ASP A 1 1847 ? 157.839 177.690 185.911 1.00 15.94 ? 1847 ASP A C     1 
ATOM   3168  O  O     . ASP A 1 1847 ? 158.167 178.854 186.190 1.00 18.69 ? 1847 ASP A O     1 
ATOM   3169  C  CB    . ASP A 1 1847 ? 157.899 176.937 188.306 1.00 9.03  ? 1847 ASP A CB    1 
ATOM   3170  C  CG    . ASP A 1 1847 ? 156.431 177.253 188.542 1.00 19.23 ? 1847 ASP A CG    1 
ATOM   3171  O  OD1   . ASP A 1 1847 ? 155.606 177.023 187.633 1.00 20.38 ? 1847 ASP A OD1   1 
ATOM   3172  O  OD2   . ASP A 1 1847 ? 156.098 177.736 189.643 1.00 29.45 ? 1847 ASP A OD2   1 
ATOM   3173  N  N     . PRO A 1 1848 ? 157.179 177.415 184.784 1.00 15.62 ? 1848 PRO A N     1 
ATOM   3174  C  CA    . PRO A 1 1848 ? 156.763 178.507 183.892 1.00 16.66 ? 1848 PRO A CA    1 
ATOM   3175  C  C     . PRO A 1 1848 ? 155.715 179.423 184.500 1.00 18.44 ? 1848 PRO A C     1 
ATOM   3176  O  O     . PRO A 1 1848 ? 155.575 180.562 184.042 1.00 25.89 ? 1848 PRO A O     1 
ATOM   3177  C  CB    . PRO A 1 1848 ? 156.215 177.763 182.668 1.00 16.22 ? 1848 PRO A CB    1 
ATOM   3178  C  CG    . PRO A 1 1848 ? 155.722 176.472 183.236 1.00 12.56 ? 1848 PRO A CG    1 
ATOM   3179  C  CD    . PRO A 1 1848 ? 156.750 176.102 184.273 1.00 12.01 ? 1848 PRO A CD    1 
ATOM   3180  N  N     . LYS A 1 1849 ? 154.977 178.964 185.511 1.00 19.46 ? 1849 LYS A N     1 
ATOM   3181  C  CA    . LYS A 1 1849 ? 153.922 179.765 186.119 1.00 18.49 ? 1849 LYS A CA    1 
ATOM   3182  C  C     . LYS A 1 1849 ? 154.451 180.784 187.119 1.00 18.36 ? 1849 LYS A C     1 
ATOM   3183  O  O     . LYS A 1 1849 ? 153.678 181.635 187.572 1.00 22.58 ? 1849 LYS A O     1 
ATOM   3184  C  CB    . LYS A 1 1849 ? 152.906 178.851 186.809 1.00 23.29 ? 1849 LYS A CB    1 
ATOM   3185  C  CG    . LYS A 1 1849 ? 152.083 178.008 185.851 1.00 23.84 ? 1849 LYS A CG    1 
ATOM   3186  C  CD    . LYS A 1 1849 ? 151.148 177.072 186.600 1.00 28.39 ? 1849 LYS A CD    1 
ATOM   3187  C  CE    . LYS A 1 1849 ? 150.020 177.839 187.271 1.00 30.91 ? 1849 LYS A CE    1 
ATOM   3188  N  NZ    . LYS A 1 1849 ? 149.091 178.440 186.274 1.00 32.11 ? 1849 LYS A NZ    1 
ATOM   3189  N  N     . GLN A 1 1850 ? 155.731 180.716 187.472 1.00 19.23 ? 1850 GLN A N     1 
ATOM   3190  C  CA    . GLN A 1 1850 ? 156.303 181.652 188.431 1.00 16.59 ? 1850 GLN A CA    1 
ATOM   3191  C  C     . GLN A 1 1850 ? 156.295 183.064 187.853 1.00 18.17 ? 1850 GLN A C     1 
ATOM   3192  O  O     . GLN A 1 1850 ? 156.661 183.274 186.694 1.00 18.24 ? 1850 GLN A O     1 
ATOM   3193  C  CB    . GLN A 1 1850 ? 157.725 181.218 188.787 1.00 18.49 ? 1850 GLN A CB    1 
ATOM   3194  C  CG    . GLN A 1 1850 ? 158.542 182.237 189.552 1.00 15.20 ? 1850 GLN A CG    1 
ATOM   3195  C  CD    . GLN A 1 1850 ? 158.036 182.451 190.962 1.00 17.90 ? 1850 GLN A CD    1 
ATOM   3196  O  OE1   . GLN A 1 1850 ? 157.321 183.413 191.235 1.00 26.19 ? 1850 GLN A OE1   1 
ATOM   3197  N  NE2   . GLN A 1 1850 ? 158.396 181.547 191.866 1.00 15.40 ? 1850 GLN A NE2   1 
ATOM   3198  N  N     . THR A 1 1851 ? 155.865 184.031 188.667 1.00 21.34 ? 1851 THR A N     1 
ATOM   3199  C  CA    . THR A 1 1851 ? 155.728 185.402 188.179 1.00 16.84 ? 1851 THR A CA    1 
ATOM   3200  C  C     . THR A 1 1851 ? 157.087 186.049 187.935 1.00 21.27 ? 1851 THR A C     1 
ATOM   3201  O  O     . THR A 1 1851 ? 157.288 186.714 186.913 1.00 22.79 ? 1851 THR A O     1 
ATOM   3202  C  CB    . THR A 1 1851 ? 154.913 186.234 189.169 1.00 20.70 ? 1851 THR A CB    1 
ATOM   3203  O  OG1   . THR A 1 1851 ? 155.731 186.573 190.296 1.00 28.68 ? 1851 THR A OG1   1 
ATOM   3204  C  CG2   . THR A 1 1851 ? 153.702 185.450 189.650 1.00 19.70 ? 1851 THR A CG2   1 
ATOM   3205  N  N     . ASP A 1 1852 ? 158.025 185.872 188.859 1.00 21.01 ? 1852 ASP A N     1 
ATOM   3206  C  CA    . ASP A 1 1852 ? 159.362 186.435 188.708 1.00 14.10 ? 1852 ASP A CA    1 
ATOM   3207  C  C     . ASP A 1 1852 ? 160.183 185.532 187.793 1.00 16.09 ? 1852 ASP A C     1 
ATOM   3208  O  O     . ASP A 1 1852 ? 160.384 184.352 188.096 1.00 16.59 ? 1852 ASP A O     1 
ATOM   3209  C  CB    . ASP A 1 1852 ? 160.033 186.586 190.071 1.00 10.57 ? 1852 ASP A CB    1 
ATOM   3210  C  CG    . ASP A 1 1852 ? 161.380 187.289 189.991 1.00 20.30 ? 1852 ASP A CG    1 
ATOM   3211  O  OD1   . ASP A 1 1852 ? 161.764 187.741 188.892 1.00 23.53 ? 1852 ASP A OD1   1 
ATOM   3212  O  OD2   . ASP A 1 1852 ? 162.058 187.387 191.035 1.00 17.09 ? 1852 ASP A OD2   1 
ATOM   3213  N  N     . VAL A 1 1853 ? 160.654 186.085 186.675 1.00 11.92 ? 1853 VAL A N     1 
ATOM   3214  C  CA    . VAL A 1 1853 ? 161.410 185.287 185.714 1.00 9.66  ? 1853 VAL A CA    1 
ATOM   3215  C  C     . VAL A 1 1853 ? 162.730 184.821 186.310 1.00 9.24  ? 1853 VAL A C     1 
ATOM   3216  O  O     . VAL A 1 1853 ? 163.264 183.777 185.916 1.00 13.75 ? 1853 VAL A O     1 
ATOM   3217  C  CB    . VAL A 1 1853 ? 161.628 186.079 184.411 1.00 11.20 ? 1853 VAL A CB    1 
ATOM   3218  C  CG1   . VAL A 1 1853 ? 160.326 186.188 183.639 1.00 9.75  ? 1853 VAL A CG1   1 
ATOM   3219  C  CG2   . VAL A 1 1853 ? 162.199 187.457 184.707 1.00 10.33 ? 1853 VAL A CG2   1 
ATOM   3220  N  N     . LEU A 1 1854 ? 163.274 185.570 187.268 1.00 8.13  ? 1854 LEU A N     1 
ATOM   3221  C  CA    . LEU A 1 1854 ? 164.551 185.221 187.873 1.00 6.96  ? 1854 LEU A CA    1 
ATOM   3222  C  C     . LEU A 1 1854 ? 164.461 184.047 188.838 1.00 8.12  ? 1854 LEU A C     1 
ATOM   3223  O  O     . LEU A 1 1854 ? 165.502 183.548 189.273 1.00 9.37  ? 1854 LEU A O     1 
ATOM   3224  C  CB    . LEU A 1 1854 ? 165.134 186.435 188.599 1.00 7.19  ? 1854 LEU A CB    1 
ATOM   3225  C  CG    . LEU A 1 1854 ? 165.592 187.590 187.707 1.00 6.21  ? 1854 LEU A CG    1 
ATOM   3226  C  CD1   . LEU A 1 1854 ? 166.320 188.637 188.524 1.00 3.50  ? 1854 LEU A CD1   1 
ATOM   3227  C  CD2   . LEU A 1 1854 ? 166.473 187.081 186.575 1.00 3.04  ? 1854 LEU A CD2   1 
ATOM   3228  N  N     . GLN A 1 1855 ? 163.253 183.594 189.181 1.00 9.55  ? 1855 GLN A N     1 
ATOM   3229  C  CA    . GLN A 1 1855 ? 163.075 182.491 190.119 1.00 4.85  ? 1855 GLN A CA    1 
ATOM   3230  C  C     . GLN A 1 1855 ? 162.320 181.319 189.501 1.00 5.99  ? 1855 GLN A C     1 
ATOM   3231  O  O     . GLN A 1 1855 ? 161.831 180.451 190.229 1.00 9.99  ? 1855 GLN A O     1 
ATOM   3232  C  CB    . GLN A 1 1855 ? 162.359 182.972 191.383 1.00 6.81  ? 1855 GLN A CB    1 
ATOM   3233  C  CG    . GLN A 1 1855 ? 163.127 184.015 192.180 1.00 5.71  ? 1855 GLN A CG    1 
ATOM   3234  C  CD    . GLN A 1 1855 ? 164.473 183.511 192.662 1.00 11.73 ? 1855 GLN A CD    1 
ATOM   3235  O  OE1   . GLN A 1 1855 ? 164.594 182.375 193.120 1.00 17.39 ? 1855 GLN A OE1   1 
ATOM   3236  N  NE2   . GLN A 1 1855 ? 165.494 184.353 192.556 1.00 14.36 ? 1855 GLN A NE2   1 
ATOM   3237  N  N     . GLN A 1 1856 ? 162.219 181.271 188.171 1.00 4.79  ? 1856 GLN A N     1 
ATOM   3238  C  CA    . GLN A 1 1856 ? 161.535 180.150 187.532 1.00 5.53  ? 1856 GLN A CA    1 
ATOM   3239  C  C     . GLN A 1 1856 ? 162.376 178.881 187.562 1.00 4.47  ? 1856 GLN A C     1 
ATOM   3240  O  O     . GLN A 1 1856 ? 161.826 177.776 187.554 1.00 5.84  ? 1856 GLN A O     1 
ATOM   3241  C  CB    . GLN A 1 1856 ? 161.167 180.499 186.091 1.00 8.26  ? 1856 GLN A CB    1 
ATOM   3242  C  CG    . GLN A 1 1856 ? 160.386 181.790 185.939 1.00 9.33  ? 1856 GLN A CG    1 
ATOM   3243  C  CD    . GLN A 1 1856 ? 159.594 181.843 184.648 1.00 14.22 ? 1856 GLN A CD    1 
ATOM   3244  O  OE1   . GLN A 1 1856 ? 160.130 181.615 183.564 1.00 17.79 ? 1856 GLN A OE1   1 
ATOM   3245  N  NE2   . GLN A 1 1856 ? 158.308 182.149 184.757 1.00 20.48 ? 1856 GLN A NE2   1 
ATOM   3246  N  N     . LEU A 1 1857 ? 163.696 179.017 187.604 1.00 3.21  ? 1857 LEU A N     1 
ATOM   3247  C  CA    . LEU A 1 1857 ? 164.597 177.874 187.598 1.00 0.91  ? 1857 LEU A CA    1 
ATOM   3248  C  C     . LEU A 1 1857 ? 165.129 177.625 189.000 1.00 1.05  ? 1857 LEU A C     1 
ATOM   3249  O  O     . LEU A 1 1857 ? 165.672 178.532 189.637 1.00 1.47  ? 1857 LEU A O     1 
ATOM   3250  C  CB    . LEU A 1 1857 ? 165.757 178.099 186.628 1.00 0.87  ? 1857 LEU A CB    1 
ATOM   3251  C  CG    . LEU A 1 1857 ? 166.833 177.015 186.658 1.00 0.69  ? 1857 LEU A CG    1 
ATOM   3252  C  CD1   . LEU A 1 1857 ? 166.237 175.665 186.292 1.00 0.60  ? 1857 LEU A CD1   1 
ATOM   3253  C  CD2   . LEU A 1 1857 ? 167.977 177.369 185.732 1.00 0.59  ? 1857 LEU A CD2   1 
ATOM   3254  N  N     . SER A 1 1858 ? 164.968 176.394 189.476 1.00 1.37  ? 1858 SER A N     1 
ATOM   3255  C  CA    . SER A 1 1858 ? 165.490 175.968 190.765 1.00 0.76  ? 1858 SER A CA    1 
ATOM   3256  C  C     . SER A 1 1858 ? 166.432 174.792 190.552 1.00 0.58  ? 1858 SER A C     1 
ATOM   3257  O  O     . SER A 1 1858 ? 166.065 173.808 189.904 1.00 0.78  ? 1858 SER A O     1 
ATOM   3258  C  CB    . SER A 1 1858 ? 164.353 175.582 191.718 1.00 1.02  ? 1858 SER A CB    1 
ATOM   3259  O  OG    . SER A 1 1858 ? 164.855 175.214 192.990 1.00 7.58  ? 1858 SER A OG    1 
ATOM   3260  N  N     . ILE A 1 1859 ? 167.642 174.902 191.088 1.00 0.45  ? 1859 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 1859 ? 168.642 173.844 191.018 1.00 0.45  ? 1859 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 1859 ? 168.786 173.251 192.409 1.00 0.62  ? 1859 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 1859 ? 169.116 173.962 193.365 1.00 0.94  ? 1859 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 1859 ? 169.987 174.365 190.491 1.00 0.29  ? 1859 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 1859 ? 169.815 174.952 189.089 1.00 0.31  ? 1859 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 1859 ? 171.024 173.256 190.485 1.00 0.22  ? 1859 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 1859 ? 170.776 176.067 188.776 1.00 0.14  ? 1859 ILE A CD1   1 
ATOM   3268  N  N     . GLN A 1 1860 ? 168.536 171.950 192.526 1.00 1.11  ? 1860 GLN A N     1 
ATOM   3269  C  CA    . GLN A 1 1860 ? 168.528 171.272 193.814 1.00 0.86  ? 1860 GLN A CA    1 
ATOM   3270  C  C     . GLN A 1 1860 ? 169.461 170.073 193.775 1.00 0.36  ? 1860 GLN A C     1 
ATOM   3271  O  O     . GLN A 1 1860 ? 169.416 169.276 192.835 1.00 0.36  ? 1860 GLN A O     1 
ATOM   3272  C  CB    . GLN A 1 1860 ? 167.113 170.833 194.194 1.00 1.95  ? 1860 GLN A CB    1 
ATOM   3273  C  CG    . GLN A 1 1860 ? 166.075 171.928 194.050 1.00 2.27  ? 1860 GLN A CG    1 
ATOM   3274  C  CD    . GLN A 1 1860 ? 164.689 171.467 194.434 1.00 3.40  ? 1860 GLN A CD    1 
ATOM   3275  O  OE1   . GLN A 1 1860 ? 164.493 170.321 194.831 1.00 9.91  ? 1860 GLN A OE1   1 
ATOM   3276  N  NE2   . GLN A 1 1860 ? 163.715 172.360 194.318 1.00 6.24  ? 1860 GLN A NE2   1 
ATOM   3277  N  N     . MET A 1 1861 ? 170.309 169.960 194.793 1.00 0.78  ? 1861 MET A N     1 
ATOM   3278  C  CA    . MET A 1 1861 ? 171.180 168.806 194.983 1.00 0.90  ? 1861 MET A CA    1 
ATOM   3279  C  C     . MET A 1 1861 ? 171.091 168.388 196.443 1.00 0.46  ? 1861 MET A C     1 
ATOM   3280  O  O     . MET A 1 1861 ? 171.468 169.159 197.331 1.00 0.46  ? 1861 MET A O     1 
ATOM   3281  C  CB    . MET A 1 1861 ? 172.625 169.127 194.594 1.00 0.70  ? 1861 MET A CB    1 
ATOM   3282  C  CG    . MET A 1 1861 ? 173.453 167.909 194.224 1.00 0.38  ? 1861 MET A CG    1 
ATOM   3283  S  SD    . MET A 1 1861 ? 175.155 168.314 193.804 1.00 4.29  ? 1861 MET A SD    1 
ATOM   3284  C  CE    . MET A 1 1861 ? 175.785 166.703 193.349 1.00 0.70  ? 1861 MET A CE    1 
ATOM   3285  N  N     . ALA A 1 1862 ? 170.592 167.173 196.684 1.00 1.52  ? 1862 ALA A N     1 
ATOM   3286  C  CA    . ALA A 1 1862 ? 170.263 166.671 198.026 1.00 0.93  ? 1862 ALA A CA    1 
ATOM   3287  C  C     . ALA A 1 1862 ? 169.247 167.630 198.632 1.00 1.39  ? 1862 ALA A C     1 
ATOM   3288  O  O     . ALA A 1 1862 ? 168.174 167.819 198.032 1.00 4.48  ? 1862 ALA A O     1 
ATOM   3289  C  CB    . ALA A 1 1862 ? 171.546 166.456 198.831 1.00 0.67  ? 1862 ALA A CB    1 
ATOM   3290  N  N     . ASN A 1 1863 ? 169.516 168.252 199.777 1.00 0.67  ? 1863 ASN A N     1 
ATOM   3291  C  CA    . ASN A 1 1863 ? 168.603 169.232 200.346 1.00 0.97  ? 1863 ASN A CA    1 
ATOM   3292  C  C     . ASN A 1 1863 ? 168.943 170.659 199.942 1.00 2.36  ? 1863 ASN A C     1 
ATOM   3293  O  O     . ASN A 1 1863 ? 168.161 171.570 200.230 1.00 5.67  ? 1863 ASN A O     1 
ATOM   3294  C  CB    . ASN A 1 1863 ? 168.590 169.130 201.876 1.00 1.16  ? 1863 ASN A CB    1 
ATOM   3295  C  CG    . ASN A 1 1863 ? 169.976 169.200 202.476 1.00 2.69  ? 1863 ASN A CG    1 
ATOM   3296  O  OD1   . ASN A 1 1863 ? 170.826 168.351 202.209 1.00 4.08  ? 1863 ASN A OD1   1 
ATOM   3297  N  ND2   . ASN A 1 1863 ? 170.214 170.221 203.287 1.00 2.59  ? 1863 ASN A ND2   1 
ATOM   3298  N  N     . ALA A 1 1864 ? 170.080 170.873 199.288 1.00 1.44  ? 1864 ALA A N     1 
ATOM   3299  C  CA    . ALA A 1 1864 ? 170.480 172.215 198.892 1.00 1.06  ? 1864 ALA A CA    1 
ATOM   3300  C  C     . ALA A 1 1864 ? 169.653 172.687 197.704 1.00 1.07  ? 1864 ALA A C     1 
ATOM   3301  O  O     . ALA A 1 1864 ? 169.504 171.968 196.713 1.00 2.13  ? 1864 ALA A O     1 
ATOM   3302  C  CB    . ALA A 1 1864 ? 171.968 172.244 198.551 1.00 0.52  ? 1864 ALA A CB    1 
ATOM   3303  N  N     . LYS A 1 1865 ? 169.110 173.895 197.810 1.00 1.18  ? 1865 LYS A N     1 
ATOM   3304  C  CA    . LYS A 1 1865 ? 168.361 174.527 196.735 1.00 1.21  ? 1865 LYS A CA    1 
ATOM   3305  C  C     . LYS A 1 1865 ? 169.015 175.851 196.380 1.00 0.48  ? 1865 LYS A C     1 
ATOM   3306  O  O     . LYS A 1 1865 ? 169.422 176.611 197.263 1.00 0.82  ? 1865 LYS A O     1 
ATOM   3307  C  CB    . LYS A 1 1865 ? 166.898 174.756 197.125 1.00 0.93  ? 1865 LYS A CB    1 
ATOM   3308  C  CG    . LYS A 1 1865 ? 166.117 173.484 197.323 1.00 2.91  ? 1865 LYS A CG    1 
ATOM   3309  C  CD    . LYS A 1 1865 ? 164.675 173.762 197.692 1.00 5.71  ? 1865 LYS A CD    1 
ATOM   3310  C  CE    . LYS A 1 1865 ? 163.902 172.462 197.796 1.00 11.88 ? 1865 LYS A CE    1 
ATOM   3311  N  NZ    . LYS A 1 1865 ? 164.390 171.644 198.940 1.00 7.30  ? 1865 LYS A NZ    1 
ATOM   3312  N  N     . PHE A 1 1866 ? 169.118 176.118 195.084 1.00 0.37  ? 1866 PHE A N     1 
ATOM   3313  C  CA    . PHE A 1 1866 ? 169.766 177.322 194.598 1.00 0.50  ? 1866 PHE A CA    1 
ATOM   3314  C  C     . PHE A 1 1866 ? 168.912 177.956 193.514 1.00 0.33  ? 1866 PHE A C     1 
ATOM   3315  O  O     . PHE A 1 1866 ? 168.226 177.266 192.755 1.00 0.58  ? 1866 PHE A O     1 
ATOM   3316  C  CB    . PHE A 1 1866 ? 171.163 177.029 194.040 1.00 0.29  ? 1866 PHE A CB    1 
ATOM   3317  C  CG    . PHE A 1 1866 ? 172.091 176.400 195.030 1.00 0.27  ? 1866 PHE A CG    1 
ATOM   3318  C  CD1   . PHE A 1 1866 ? 172.857 177.184 195.871 1.00 0.24  ? 1866 PHE A CD1   1 
ATOM   3319  C  CD2   . PHE A 1 1866 ? 172.196 175.023 195.122 1.00 0.10  ? 1866 PHE A CD2   1 
ATOM   3320  C  CE1   . PHE A 1 1866 ? 173.713 176.606 196.782 1.00 1.31  ? 1866 PHE A CE1   1 
ATOM   3321  C  CE2   . PHE A 1 1866 ? 173.046 174.442 196.030 1.00 0.11  ? 1866 PHE A CE2   1 
ATOM   3322  C  CZ    . PHE A 1 1866 ? 173.806 175.231 196.864 1.00 0.34  ? 1866 PHE A CZ    1 
ATOM   3323  N  N     . ASN A 1 1867 ? 168.957 179.279 193.455 1.00 0.43  ? 1867 ASN A N     1 
ATOM   3324  C  CA    . ASN A 1 1867 ? 168.455 180.008 192.307 1.00 0.64  ? 1867 ASN A CA    1 
ATOM   3325  C  C     . ASN A 1 1867 ? 169.572 180.163 191.285 1.00 0.40  ? 1867 ASN A C     1 
ATOM   3326  O  O     . ASN A 1 1867 ? 170.756 180.175 191.628 1.00 0.32  ? 1867 ASN A O     1 
ATOM   3327  C  CB    . ASN A 1 1867 ? 167.925 181.382 192.718 1.00 1.57  ? 1867 ASN A CB    1 
ATOM   3328  C  CG    . ASN A 1 1867 ? 169.036 182.346 193.093 1.00 5.27  ? 1867 ASN A CG    1 
ATOM   3329  O  OD1   . ASN A 1 1867 ? 169.808 182.091 194.016 1.00 6.31  ? 1867 ASN A OD1   1 
ATOM   3330  N  ND2   . ASN A 1 1867 ? 169.126 183.456 192.373 1.00 6.76  ? 1867 ASN A ND2   1 
ATOM   3331  N  N     . TYR A 1 1868 ? 169.186 180.271 190.021 1.00 0.40  ? 1868 TYR A N     1 
ATOM   3332  C  CA    . TYR A 1 1868 ? 170.148 180.532 188.963 1.00 0.24  ? 1868 TYR A CA    1 
ATOM   3333  C  C     . TYR A 1 1868 ? 170.463 182.023 188.921 1.00 0.53  ? 1868 TYR A C     1 
ATOM   3334  O  O     . TYR A 1 1868 ? 169.554 182.858 188.872 1.00 1.01  ? 1868 TYR A O     1 
ATOM   3335  C  CB    . TYR A 1 1868 ? 169.601 180.055 187.619 1.00 0.33  ? 1868 TYR A CB    1 
ATOM   3336  C  CG    . TYR A 1 1868 ? 170.650 179.876 186.548 1.00 0.44  ? 1868 TYR A CG    1 
ATOM   3337  C  CD1   . TYR A 1 1868 ? 171.563 178.830 186.605 1.00 0.19  ? 1868 TYR A CD1   1 
ATOM   3338  C  CD2   . TYR A 1 1868 ? 170.720 180.749 185.473 1.00 0.13  ? 1868 TYR A CD2   1 
ATOM   3339  C  CE1   . TYR A 1 1868 ? 172.520 178.668 185.624 1.00 0.16  ? 1868 TYR A CE1   1 
ATOM   3340  C  CE2   . TYR A 1 1868 ? 171.669 180.593 184.491 1.00 0.10  ? 1868 TYR A CE2   1 
ATOM   3341  C  CZ    . TYR A 1 1868 ? 172.568 179.554 184.567 1.00 0.17  ? 1868 TYR A CZ    1 
ATOM   3342  O  OH    . TYR A 1 1868 ? 173.511 179.401 183.581 1.00 1.26  ? 1868 TYR A OH    1 
ATOM   3343  N  N     . GLY A 1 1869 ? 171.754 182.358 188.959 1.00 0.15  ? 1869 GLY A N     1 
ATOM   3344  C  CA    . GLY A 1 1869 ? 172.145 183.755 189.013 1.00 0.62  ? 1869 GLY A CA    1 
ATOM   3345  C  C     . GLY A 1 1869 ? 171.911 184.504 187.718 1.00 0.81  ? 1869 GLY A C     1 
ATOM   3346  O  O     . GLY A 1 1869 ? 171.752 185.727 187.726 1.00 1.90  ? 1869 GLY A O     1 
ATOM   3347  N  N     . PHE A 1 1870 ? 171.879 183.785 186.595 1.00 0.51  ? 1870 PHE A N     1 
ATOM   3348  C  CA    . PHE A 1 1870 ? 171.675 184.363 185.265 1.00 0.63  ? 1870 PHE A CA    1 
ATOM   3349  C  C     . PHE A 1 1870 ? 172.750 185.390 184.919 1.00 0.84  ? 1870 PHE A C     1 
ATOM   3350  O  O     . PHE A 1 1870 ? 172.488 186.376 184.231 1.00 1.71  ? 1870 PHE A O     1 
ATOM   3351  C  CB    . PHE A 1 1870 ? 170.273 184.966 185.129 1.00 0.53  ? 1870 PHE A CB    1 
ATOM   3352  C  CG    . PHE A 1 1870 ? 169.199 183.934 184.963 1.00 0.73  ? 1870 PHE A CG    1 
ATOM   3353  C  CD1   . PHE A 1 1870 ? 169.093 183.209 183.789 1.00 0.46  ? 1870 PHE A CD1   1 
ATOM   3354  C  CD2   . PHE A 1 1870 ? 168.310 183.668 185.990 1.00 0.67  ? 1870 PHE A CD2   1 
ATOM   3355  C  CE1   . PHE A 1 1870 ? 168.118 182.250 183.637 1.00 0.52  ? 1870 PHE A CE1   1 
ATOM   3356  C  CE2   . PHE A 1 1870 ? 167.329 182.712 185.842 1.00 0.66  ? 1870 PHE A CE2   1 
ATOM   3357  C  CZ    . PHE A 1 1870 ? 167.233 182.001 184.662 1.00 0.77  ? 1870 PHE A CZ    1 
ATOM   3358  N  N     . GLU A 1 1871 ? 173.965 185.155 185.405 1.00 1.04  ? 1871 GLU A N     1 
ATOM   3359  C  CA    . GLU A 1 1871 ? 175.129 185.872 184.911 1.00 0.66  ? 1871 GLU A CA    1 
ATOM   3360  C  C     . GLU A 1 1871 ? 175.478 185.362 183.520 1.00 1.02  ? 1871 GLU A C     1 
ATOM   3361  O  O     . GLU A 1 1871 ? 175.537 184.150 183.295 1.00 4.28  ? 1871 GLU A O     1 
ATOM   3362  C  CB    . GLU A 1 1871 ? 176.310 185.674 185.861 1.00 0.47  ? 1871 GLU A CB    1 
ATOM   3363  C  CG    . GLU A 1 1871 ? 177.589 186.379 185.451 1.00 1.52  ? 1871 GLU A CG    1 
ATOM   3364  C  CD    . GLU A 1 1871 ? 177.606 187.846 185.835 1.00 2.34  ? 1871 GLU A CD    1 
ATOM   3365  O  OE1   . GLU A 1 1871 ? 176.610 188.332 186.410 1.00 4.13  ? 1871 GLU A OE1   1 
ATOM   3366  O  OE2   . GLU A 1 1871 ? 178.622 188.516 185.566 1.00 2.87  ? 1871 GLU A OE2   1 
ATOM   3367  N  N     . TYR A 1 1872 ? 175.698 186.276 182.580 1.00 1.29  ? 1872 TYR A N     1 
ATOM   3368  C  CA    . TYR A 1 1872 ? 176.110 185.870 181.242 1.00 0.95  ? 1872 TYR A CA    1 
ATOM   3369  C  C     . TYR A 1 1872 ? 177.521 185.305 181.319 1.00 1.52  ? 1872 TYR A C     1 
ATOM   3370  O  O     . TYR A 1 1872 ? 178.475 186.034 181.604 1.00 3.19  ? 1872 TYR A O     1 
ATOM   3371  C  CB    . TYR A 1 1872 ? 176.058 187.041 180.266 1.00 1.20  ? 1872 TYR A CB    1 
ATOM   3372  C  CG    . TYR A 1 1872 ? 176.413 186.625 178.857 1.00 1.56  ? 1872 TYR A CG    1 
ATOM   3373  C  CD1   . TYR A 1 1872 ? 175.933 185.435 178.327 1.00 2.45  ? 1872 TYR A CD1   1 
ATOM   3374  C  CD2   . TYR A 1 1872 ? 177.270 187.388 178.077 1.00 2.02  ? 1872 TYR A CD2   1 
ATOM   3375  C  CE1   . TYR A 1 1872 ? 176.260 185.036 177.052 1.00 2.24  ? 1872 TYR A CE1   1 
ATOM   3376  C  CE2   . TYR A 1 1872 ? 177.607 186.994 176.796 1.00 3.35  ? 1872 TYR A CE2   1 
ATOM   3377  C  CZ    . TYR A 1 1872 ? 177.099 185.815 176.290 1.00 2.82  ? 1872 TYR A CZ    1 
ATOM   3378  O  OH    . TYR A 1 1872 ? 177.429 185.414 175.019 1.00 4.17  ? 1872 TYR A OH    1 
ATOM   3379  N  N     . LEU A 1 1873 ? 177.659 184.005 181.077 1.00 1.74  ? 1873 LEU A N     1 
ATOM   3380  C  CA    . LEU A 1 1873 ? 178.954 183.351 181.152 1.00 2.52  ? 1873 LEU A CA    1 
ATOM   3381  C  C     . LEU A 1 1873 ? 179.666 183.266 179.812 1.00 2.77  ? 1873 LEU A C     1 
ATOM   3382  O  O     . LEU A 1 1873 ? 180.835 182.873 179.776 1.00 8.63  ? 1873 LEU A O     1 
ATOM   3383  C  CB    . LEU A 1 1873 ? 178.796 181.946 181.740 1.00 3.27  ? 1873 LEU A CB    1 
ATOM   3384  C  CG    . LEU A 1 1873 ? 178.083 181.897 183.091 1.00 1.26  ? 1873 LEU A CG    1 
ATOM   3385  C  CD1   . LEU A 1 1873 ? 177.832 180.468 183.508 1.00 0.97  ? 1873 LEU A CD1   1 
ATOM   3386  C  CD2   . LEU A 1 1873 ? 178.894 182.631 184.147 1.00 1.94  ? 1873 LEU A CD2   1 
ATOM   3387  N  N     . GLY A 1 1874 ? 179.008 183.645 178.720 1.00 2.90  ? 1874 GLY A N     1 
ATOM   3388  C  CA    . GLY A 1 1874 ? 179.615 183.461 177.415 1.00 2.79  ? 1874 GLY A CA    1 
ATOM   3389  C  C     . GLY A 1 1874 ? 179.749 181.990 177.087 1.00 2.52  ? 1874 GLY A C     1 
ATOM   3390  O  O     . GLY A 1 1874 ? 178.831 181.193 177.302 1.00 5.46  ? 1874 GLY A O     1 
ATOM   3391  N  N     . VAL A 1 1875 ? 180.909 181.616 176.554 1.00 3.75  ? 1875 VAL A N     1 
ATOM   3392  C  CA    . VAL A 1 1875 ? 181.175 180.218 176.241 1.00 4.60  ? 1875 VAL A CA    1 
ATOM   3393  C  C     . VAL A 1 1875 ? 182.355 179.743 177.076 1.00 6.45  ? 1875 VAL A C     1 
ATOM   3394  O  O     . VAL A 1 1875 ? 183.513 179.869 176.665 1.00 14.61 ? 1875 VAL A O     1 
ATOM   3395  C  CB    . VAL A 1 1875 ? 181.442 180.022 174.737 1.00 5.42  ? 1875 VAL A CB    1 
ATOM   3396  C  CG1   . VAL A 1 1875 ? 181.384 178.548 174.376 1.00 7.29  ? 1875 VAL A CG1   1 
ATOM   3397  C  CG2   . VAL A 1 1875 ? 180.451 180.820 173.907 1.00 3.87  ? 1875 VAL A CG2   1 
ATOM   3398  N  N     . GLN A 1 1876 ? 182.069 179.189 178.251 1.00 8.23  ? 1876 GLN A N     1 
ATOM   3399  C  CA    . GLN A 1 1876 ? 183.101 178.666 179.135 1.00 8.32  ? 1876 GLN A CA    1 
ATOM   3400  C  C     . GLN A 1 1876 ? 183.271 177.173 178.904 1.00 10.80 ? 1876 GLN A C     1 
ATOM   3401  O  O     . GLN A 1 1876 ? 182.293 176.424 178.898 1.00 16.32 ? 1876 GLN A O     1 
ATOM   3402  C  CB    . GLN A 1 1876 ? 182.747 178.915 180.603 1.00 11.71 ? 1876 GLN A CB    1 
ATOM   3403  C  CG    . GLN A 1 1876 ? 182.279 180.322 180.926 1.00 8.82  ? 1876 GLN A CG    1 
ATOM   3404  C  CD    . GLN A 1 1876 ? 183.405 181.224 181.391 1.00 15.16 ? 1876 GLN A CD    1 
ATOM   3405  O  OE1   . GLN A 1 1876 ? 184.557 180.804 181.479 1.00 15.84 ? 1876 GLN A OE1   1 
ATOM   3406  N  NE2   . GLN A 1 1876 ? 183.073 182.473 181.698 1.00 17.28 ? 1876 GLN A NE2   1 
ATOM   3407  N  N     . ASP A 1 1877 ? 184.520 176.748 178.721 1.00 15.75 ? 1877 ASP A N     1 
ATOM   3408  C  CA    . ASP A 1 1877 ? 184.810 175.328 178.561 1.00 11.76 ? 1877 ASP A CA    1 
ATOM   3409  C  C     . ASP A 1 1877 ? 184.335 174.556 179.786 1.00 9.17  ? 1877 ASP A C     1 
ATOM   3410  O  O     . ASP A 1 1877 ? 184.630 174.928 180.923 1.00 8.57  ? 1877 ASP A O     1 
ATOM   3411  C  CB    . ASP A 1 1877 ? 186.308 175.115 178.350 1.00 9.20  ? 1877 ASP A CB    1 
ATOM   3412  C  CG    . ASP A 1 1877 ? 186.767 175.524 176.966 1.00 19.38 ? 1877 ASP A CG    1 
ATOM   3413  O  OD1   . ASP A 1 1877 ? 186.105 175.141 175.977 1.00 23.13 ? 1877 ASP A OD1   1 
ATOM   3414  O  OD2   . ASP A 1 1877 ? 187.790 176.232 176.865 1.00 22.81 ? 1877 ASP A OD2   1 
ATOM   3415  N  N     . LYS A 1 1878 ? 183.598 173.476 179.547 1.00 10.44 ? 1878 LYS A N     1 
ATOM   3416  C  CA    . LYS A 1 1878 ? 183.024 172.695 180.633 1.00 7.91  ? 1878 LYS A CA    1 
ATOM   3417  C  C     . LYS A 1 1878 ? 183.908 171.515 181.003 1.00 6.68  ? 1878 LYS A C     1 
ATOM   3418  O  O     . LYS A 1 1878 ? 184.657 170.991 180.175 1.00 10.83 ? 1878 LYS A O     1 
ATOM   3419  C  CB    . LYS A 1 1878 ? 181.625 172.197 180.278 1.00 6.53  ? 1878 LYS A CB    1 
ATOM   3420  C  CG    . LYS A 1 1878 ? 180.600 173.300 180.159 1.00 11.96 ? 1878 LYS A CG    1 
ATOM   3421  C  CD    . LYS A 1 1878 ? 179.227 172.733 179.861 1.00 13.09 ? 1878 LYS A CD    1 
ATOM   3422  C  CE    . LYS A 1 1878 ? 178.213 173.835 179.664 1.00 10.49 ? 1878 LYS A CE    1 
ATOM   3423  N  NZ    . LYS A 1 1878 ? 177.959 174.580 180.921 1.00 13.13 ? 1878 LYS A NZ    1 
ATOM   3424  N  N     . LEU A 1 1879 ? 183.808 171.109 182.262 1.00 4.10  ? 1879 LEU A N     1 
ATOM   3425  C  CA    . LEU A 1 1879 ? 184.533 169.960 182.766 1.00 1.26  ? 1879 LEU A CA    1 
ATOM   3426  C  C     . LEU A 1 1879 ? 183.749 168.688 182.478 1.00 1.24  ? 1879 LEU A C     1 
ATOM   3427  O  O     . LEU A 1 1879 ? 182.518 168.699 182.398 1.00 1.93  ? 1879 LEU A O     1 
ATOM   3428  C  CB    . LEU A 1 1879 ? 184.761 170.096 184.271 1.00 0.53  ? 1879 LEU A CB    1 
ATOM   3429  C  CG    . LEU A 1 1879 ? 185.751 171.145 184.775 1.00 0.46  ? 1879 LEU A CG    1 
ATOM   3430  C  CD1   . LEU A 1 1879 ? 186.042 170.921 186.250 1.00 0.11  ? 1879 LEU A CD1   1 
ATOM   3431  C  CD2   . LEU A 1 1879 ? 187.032 171.151 183.961 1.00 0.51  ? 1879 LEU A CD2   1 
ATOM   3432  N  N     . VAL A 1 1880 ? 184.473 167.582 182.319 1.00 0.78  ? 1880 VAL A N     1 
ATOM   3433  C  CA    . VAL A 1 1880 ? 183.818 166.283 182.275 1.00 0.65  ? 1880 VAL A CA    1 
ATOM   3434  C  C     . VAL A 1 1880 ? 183.300 165.958 183.668 1.00 0.80  ? 1880 VAL A C     1 
ATOM   3435  O  O     . VAL A 1 1880 ? 184.043 166.022 184.654 1.00 0.93  ? 1880 VAL A O     1 
ATOM   3436  C  CB    . VAL A 1 1880 ? 184.782 165.202 181.763 1.00 0.94  ? 1880 VAL A CB    1 
ATOM   3437  C  CG1   . VAL A 1 1880 ? 184.150 163.821 181.901 1.00 0.37  ? 1880 VAL A CG1   1 
ATOM   3438  C  CG2   . VAL A 1 1880 ? 185.168 165.479 180.322 1.00 0.69  ? 1880 VAL A CG2   1 
ATOM   3439  N  N     . GLN A 1 1881 ? 182.020 165.624 183.756 1.00 1.33  ? 1881 GLN A N     1 
ATOM   3440  C  CA    . GLN A 1 1881 ? 181.352 165.472 185.045 1.00 2.16  ? 1881 GLN A CA    1 
ATOM   3441  C  C     . GLN A 1 1881 ? 181.666 164.079 185.582 1.00 1.63  ? 1881 GLN A C     1 
ATOM   3442  O  O     . GLN A 1 1881 ? 180.900 163.133 185.387 1.00 3.96  ? 1881 GLN A O     1 
ATOM   3443  C  CB    . GLN A 1 1881 ? 179.856 165.703 184.871 1.00 2.73  ? 1881 GLN A CB    1 
ATOM   3444  C  CG    . GLN A 1 1881 ? 179.023 165.688 186.135 1.00 2.55  ? 1881 GLN A CG    1 
ATOM   3445  C  CD    . GLN A 1 1881 ? 179.391 166.789 187.107 1.00 3.71  ? 1881 GLN A CD    1 
ATOM   3446  O  OE1   . GLN A 1 1881 ? 180.031 166.544 188.124 1.00 5.66  ? 1881 GLN A OE1   1 
ATOM   3447  N  NE2   . GLN A 1 1881 ? 178.989 168.013 186.793 1.00 7.50  ? 1881 GLN A NE2   1 
ATOM   3448  N  N     . THR A 1 1882 ? 182.812 163.948 186.255 1.00 1.92  ? 1882 THR A N     1 
ATOM   3449  C  CA    . THR A 1 1882 ? 183.353 162.703 186.779 1.00 0.95  ? 1882 THR A CA    1 
ATOM   3450  C  C     . THR A 1 1882 ? 182.825 162.416 188.178 1.00 1.21  ? 1882 THR A C     1 
ATOM   3451  O  O     . THR A 1 1882 ? 182.275 163.301 188.838 1.00 1.59  ? 1882 THR A O     1 
ATOM   3452  C  CB    . THR A 1 1882 ? 184.887 162.761 186.809 1.00 1.09  ? 1882 THR A CB    1 
ATOM   3453  O  OG1   . THR A 1 1882 ? 185.320 163.630 187.864 1.00 1.32  ? 1882 THR A OG1   1 
ATOM   3454  C  CG2   . THR A 1 1882 ? 185.430 163.259 185.487 1.00 0.70  ? 1882 THR A CG2   1 
ATOM   3455  N  N     . PRO A 1 1883 ? 182.960 161.173 188.657 1.00 3.02  ? 1883 PRO A N     1 
ATOM   3456  C  CA    . PRO A 1 1883 ? 182.565 160.876 190.045 1.00 1.11  ? 1883 PRO A CA    1 
ATOM   3457  C  C     . PRO A 1 1883 ? 183.251 161.747 191.087 1.00 1.13  ? 1883 PRO A C     1 
ATOM   3458  O  O     . PRO A 1 1883 ? 182.622 162.101 192.091 1.00 1.74  ? 1883 PRO A O     1 
ATOM   3459  C  CB    . PRO A 1 1883 ? 182.954 159.401 190.189 1.00 0.92  ? 1883 PRO A CB    1 
ATOM   3460  C  CG    . PRO A 1 1883 ? 182.744 158.859 188.827 1.00 1.97  ? 1883 PRO A CG    1 
ATOM   3461  C  CD    . PRO A 1 1883 ? 183.256 159.935 187.910 1.00 1.04  ? 1883 PRO A CD    1 
ATOM   3462  N  N     . LEU A 1 1884 ? 184.523 162.096 190.888 1.00 1.22  ? 1884 LEU A N     1 
ATOM   3463  C  CA    . LEU A 1 1884 ? 185.165 163.062 191.775 1.00 0.72  ? 1884 LEU A CA    1 
ATOM   3464  C  C     . LEU A 1 1884 ? 184.473 164.416 191.692 1.00 0.58  ? 1884 LEU A C     1 
ATOM   3465  O  O     . LEU A 1 1884 ? 184.252 165.078 192.711 1.00 0.79  ? 1884 LEU A O     1 
ATOM   3466  C  CB    . LEU A 1 1884 ? 186.650 163.196 191.434 1.00 1.16  ? 1884 LEU A CB    1 
ATOM   3467  C  CG    . LEU A 1 1884 ? 187.453 164.136 192.339 1.00 1.60  ? 1884 LEU A CG    1 
ATOM   3468  C  CD1   . LEU A 1 1884 ? 187.332 163.733 193.806 1.00 1.41  ? 1884 LEU A CD1   1 
ATOM   3469  C  CD2   . LEU A 1 1884 ? 188.911 164.205 191.915 1.00 0.57  ? 1884 LEU A CD2   1 
ATOM   3470  N  N     . THR A 1 1885 ? 184.112 164.836 190.478 1.00 1.33  ? 1885 THR A N     1 
ATOM   3471  C  CA    . THR A 1 1885 ? 183.415 166.105 190.312 1.00 1.11  ? 1885 THR A CA    1 
ATOM   3472  C  C     . THR A 1 1885 ? 182.011 166.032 190.904 1.00 0.91  ? 1885 THR A C     1 
ATOM   3473  O  O     . THR A 1 1885 ? 181.518 167.012 191.473 1.00 0.78  ? 1885 THR A O     1 
ATOM   3474  C  CB    . THR A 1 1885 ? 183.361 166.481 188.830 1.00 0.66  ? 1885 THR A CB    1 
ATOM   3475  O  OG1   . THR A 1 1885 ? 184.692 166.543 188.307 1.00 3.34  ? 1885 THR A OG1   1 
ATOM   3476  C  CG2   . THR A 1 1885 ? 182.738 167.854 188.658 1.00 0.60  ? 1885 THR A CG2   1 
ATOM   3477  N  N     . ASP A 1 1886 ? 181.357 164.874 190.783 1.00 0.82  ? 1886 ASP A N     1 
ATOM   3478  C  CA    . ASP A 1 1886 ? 180.062 164.676 191.425 1.00 0.62  ? 1886 ASP A CA    1 
ATOM   3479  C  C     . ASP A 1 1886 ? 180.181 164.802 192.937 1.00 0.37  ? 1886 ASP A C     1 
ATOM   3480  O  O     . ASP A 1 1886 ? 179.360 165.457 193.588 1.00 0.18  ? 1886 ASP A O     1 
ATOM   3481  C  CB    . ASP A 1 1886 ? 179.492 163.304 191.056 1.00 1.01  ? 1886 ASP A CB    1 
ATOM   3482  C  CG    . ASP A 1 1886 ? 178.780 163.303 189.724 1.00 3.60  ? 1886 ASP A CG    1 
ATOM   3483  O  OD1   . ASP A 1 1886 ? 179.185 164.069 188.832 1.00 6.31  ? 1886 ASP A OD1   1 
ATOM   3484  O  OD2   . ASP A 1 1886 ? 177.812 162.530 189.566 1.00 11.07 ? 1886 ASP A OD2   1 
ATOM   3485  N  N     . ARG A 1 1887 ? 181.208 164.173 193.509 1.00 0.35  ? 1887 ARG A N     1 
ATOM   3486  C  CA    . ARG A 1 1887 ? 181.442 164.288 194.942 1.00 0.14  ? 1887 ARG A CA    1 
ATOM   3487  C  C     . ARG A 1 1887 ? 181.782 165.723 195.326 1.00 0.15  ? 1887 ARG A C     1 
ATOM   3488  O  O     . ARG A 1 1887 ? 181.374 166.205 196.388 1.00 0.16  ? 1887 ARG A O     1 
ATOM   3489  C  CB    . ARG A 1 1887 ? 182.560 163.330 195.354 1.00 0.25  ? 1887 ARG A CB    1 
ATOM   3490  C  CG    . ARG A 1 1887 ? 182.810 163.238 196.841 1.00 0.44  ? 1887 ARG A CG    1 
ATOM   3491  C  CD    . ARG A 1 1887 ? 184.055 162.420 197.118 1.00 0.64  ? 1887 ARG A CD    1 
ATOM   3492  N  NE    . ARG A 1 1887 ? 184.335 162.315 198.544 1.00 1.91  ? 1887 ARG A NE    1 
ATOM   3493  C  CZ    . ARG A 1 1887 ? 184.468 161.172 199.200 1.00 1.02  ? 1887 ARG A CZ    1 
ATOM   3494  N  NH1   . ARG A 1 1887 ? 184.395 160.008 198.578 1.00 2.43  ? 1887 ARG A NH1   1 
ATOM   3495  N  NH2   . ARG A 1 1887 ? 184.687 161.196 200.510 1.00 1.21  ? 1887 ARG A NH2   1 
ATOM   3496  N  N     . CYS A 1 1888 ? 182.529 166.422 194.466 1.00 0.22  ? 1888 CYS A N     1 
ATOM   3497  C  CA    . CYS A 1 1888 ? 182.825 167.829 194.720 1.00 0.23  ? 1888 CYS A CA    1 
ATOM   3498  C  C     . CYS A 1 1888 ? 181.556 168.666 194.727 1.00 0.07  ? 1888 CYS A C     1 
ATOM   3499  O  O     . CYS A 1 1888 ? 181.374 169.526 195.596 1.00 0.06  ? 1888 CYS A O     1 
ATOM   3500  C  CB    . CYS A 1 1888 ? 183.818 168.353 193.681 1.00 0.24  ? 1888 CYS A CB    1 
ATOM   3501  S  SG    . CYS A 1 1888 ? 184.486 169.992 194.041 1.00 6.60  ? 1888 CYS A SG    1 
ATOM   3502  N  N     . TYR A 1 1889 ? 180.657 168.420 193.775 1.00 0.10  ? 1889 TYR A N     1 
ATOM   3503  C  CA    . TYR A 1 1889 ? 179.406 169.170 193.718 1.00 0.13  ? 1889 TYR A CA    1 
ATOM   3504  C  C     . TYR A 1 1889 ? 178.563 168.927 194.963 1.00 0.07  ? 1889 TYR A C     1 
ATOM   3505  O  O     . TYR A 1 1889 ? 177.992 169.863 195.533 1.00 0.04  ? 1889 TYR A O     1 
ATOM   3506  C  CB    . TYR A 1 1889 ? 178.625 168.787 192.460 1.00 0.12  ? 1889 TYR A CB    1 
ATOM   3507  C  CG    . TYR A 1 1889 ? 179.044 169.521 191.210 1.00 0.14  ? 1889 TYR A CG    1 
ATOM   3508  C  CD1   . TYR A 1 1889 ? 180.338 169.999 191.059 1.00 0.19  ? 1889 TYR A CD1   1 
ATOM   3509  C  CD2   . TYR A 1 1889 ? 178.145 169.720 190.170 1.00 0.42  ? 1889 TYR A CD2   1 
ATOM   3510  C  CE1   . TYR A 1 1889 ? 180.722 170.666 189.913 1.00 0.26  ? 1889 TYR A CE1   1 
ATOM   3511  C  CE2   . TYR A 1 1889 ? 178.521 170.383 189.020 1.00 0.69  ? 1889 TYR A CE2   1 
ATOM   3512  C  CZ    . TYR A 1 1889 ? 179.810 170.853 188.897 1.00 0.52  ? 1889 TYR A CZ    1 
ATOM   3513  O  OH    . TYR A 1 1889 ? 180.189 171.514 187.755 1.00 0.51  ? 1889 TYR A OH    1 
ATOM   3514  N  N     . LEU A 1 1890 ? 178.475 167.671 195.400 1.00 0.07  ? 1890 LEU A N     1 
ATOM   3515  C  CA    . LEU A 1 1890 ? 177.657 167.344 196.562 1.00 0.05  ? 1890 LEU A CA    1 
ATOM   3516  C  C     . LEU A 1 1890 ? 178.198 168.007 197.822 1.00 0.07  ? 1890 LEU A C     1 
ATOM   3517  O  O     . LEU A 1 1890 ? 177.442 168.580 198.613 1.00 0.07  ? 1890 LEU A O     1 
ATOM   3518  C  CB    . LEU A 1 1890 ? 177.587 165.829 196.733 1.00 0.14  ? 1890 LEU A CB    1 
ATOM   3519  C  CG    . LEU A 1 1890 ? 176.702 165.307 197.864 1.00 0.06  ? 1890 LEU A CG    1 
ATOM   3520  C  CD1   . LEU A 1 1890 ? 175.248 165.639 197.600 1.00 0.03  ? 1890 LEU A CD1   1 
ATOM   3521  C  CD2   . LEU A 1 1890 ? 176.899 163.811 198.042 1.00 0.09  ? 1890 LEU A CD2   1 
ATOM   3522  N  N     . THR A 1 1891 ? 179.516 167.951 198.017 1.00 0.06  ? 1891 THR A N     1 
ATOM   3523  C  CA    . THR A 1 1891 ? 180.112 168.490 199.235 1.00 0.05  ? 1891 THR A CA    1 
ATOM   3524  C  C     . THR A 1 1891 ? 180.007 170.010 199.276 1.00 0.04  ? 1891 THR A C     1 
ATOM   3525  O  O     . THR A 1 1891 ? 179.626 170.590 200.298 1.00 0.09  ? 1891 THR A O     1 
ATOM   3526  C  CB    . THR A 1 1891 ? 181.571 168.044 199.339 1.00 0.12  ? 1891 THR A CB    1 
ATOM   3527  O  OG1   . THR A 1 1891 ? 181.653 166.629 199.133 1.00 1.63  ? 1891 THR A OG1   1 
ATOM   3528  C  CG2   . THR A 1 1891 ? 182.141 168.383 200.704 1.00 0.11  ? 1891 THR A CG2   1 
ATOM   3529  N  N     . MET A 1 1892 ? 180.340 170.675 198.168 1.00 0.05  ? 1892 MET A N     1 
ATOM   3530  C  CA    . MET A 1 1892 ? 180.316 172.134 198.152 1.00 0.03  ? 1892 MET A CA    1 
ATOM   3531  C  C     . MET A 1 1892 ? 178.898 172.675 198.292 1.00 0.03  ? 1892 MET A C     1 
ATOM   3532  O  O     . MET A 1 1892 ? 178.680 173.677 198.982 1.00 0.02  ? 1892 MET A O     1 
ATOM   3533  C  CB    . MET A 1 1892 ? 180.978 172.664 196.881 1.00 0.03  ? 1892 MET A CB    1 
ATOM   3534  C  CG    . MET A 1 1892 ? 182.414 172.217 196.686 1.00 0.02  ? 1892 MET A CG    1 
ATOM   3535  S  SD    . MET A 1 1892 ? 183.537 172.791 197.968 1.00 2.09  ? 1892 MET A SD    1 
ATOM   3536  C  CE    . MET A 1 1892 ? 183.921 171.261 198.812 1.00 0.06  ? 1892 MET A CE    1 
ATOM   3537  N  N     . THR A 1 1893 ? 177.919 172.032 197.653 1.00 0.03  ? 1893 THR A N     1 
ATOM   3538  C  CA    . THR A 1 1893 ? 176.542 172.495 197.793 1.00 0.04  ? 1893 THR A CA    1 
ATOM   3539  C  C     . THR A 1 1893 ? 176.008 172.252 199.199 1.00 0.06  ? 1893 THR A C     1 
ATOM   3540  O  O     . THR A 1 1893 ? 175.141 172.999 199.663 1.00 0.10  ? 1893 THR A O     1 
ATOM   3541  C  CB    . THR A 1 1893 ? 175.634 171.829 196.756 1.00 0.05  ? 1893 THR A CB    1 
ATOM   3542  O  OG1   . THR A 1 1893 ? 175.761 170.403 196.835 1.00 0.13  ? 1893 THR A OG1   1 
ATOM   3543  C  CG2   . THR A 1 1893 ? 175.987 172.298 195.358 1.00 0.03  ? 1893 THR A CG2   1 
ATOM   3544  N  N     . GLN A 1 1894 ? 176.499 171.219 199.886 1.00 0.06  ? 1894 GLN A N     1 
ATOM   3545  C  CA    . GLN A 1 1894 ? 176.157 171.053 201.295 1.00 0.08  ? 1894 GLN A CA    1 
ATOM   3546  C  C     . GLN A 1 1894 ? 176.702 172.205 202.125 1.00 0.17  ? 1894 GLN A C     1 
ATOM   3547  O  O     . GLN A 1 1894 ? 176.021 172.706 203.027 1.00 0.37  ? 1894 GLN A O     1 
ATOM   3548  C  CB    . GLN A 1 1894 ? 176.681 169.715 201.820 1.00 0.26  ? 1894 GLN A CB    1 
ATOM   3549  C  CG    . GLN A 1 1894 ? 175.872 168.509 201.386 1.00 0.07  ? 1894 GLN A CG    1 
ATOM   3550  C  CD    . GLN A 1 1894 ? 174.481 168.492 201.981 1.00 0.23  ? 1894 GLN A CD    1 
ATOM   3551  O  OE1   . GLN A 1 1894 ? 174.315 168.469 203.200 1.00 4.51  ? 1894 GLN A OE1   1 
ATOM   3552  N  NE2   . GLN A 1 1894 ? 173.470 168.504 201.123 1.00 0.34  ? 1894 GLN A NE2   1 
ATOM   3553  N  N     . ALA A 1 1895 ? 177.929 172.641 201.832 1.00 0.18  ? 1895 ALA A N     1 
ATOM   3554  C  CA    . ALA A 1 1895 ? 178.496 173.795 202.522 1.00 0.11  ? 1895 ALA A CA    1 
ATOM   3555  C  C     . ALA A 1 1895 ? 177.716 175.064 202.208 1.00 0.15  ? 1895 ALA A C     1 
ATOM   3556  O  O     . ALA A 1 1895 ? 177.513 175.907 203.090 1.00 0.28  ? 1895 ALA A O     1 
ATOM   3557  C  CB    . ALA A 1 1895 ? 179.967 173.960 202.145 1.00 0.08  ? 1895 ALA A CB    1 
ATOM   3558  N  N     . LEU A 1 1896 ? 177.282 175.223 200.957 1.00 0.11  ? 1896 LEU A N     1 
ATOM   3559  C  CA    . LEU A 1 1896 ? 176.513 176.405 200.581 1.00 0.14  ? 1896 LEU A CA    1 
ATOM   3560  C  C     . LEU A 1 1896 ? 175.171 176.445 201.301 1.00 0.78  ? 1896 LEU A C     1 
ATOM   3561  O  O     . LEU A 1 1896 ? 174.728 177.514 201.735 1.00 2.98  ? 1896 LEU A O     1 
ATOM   3562  C  CB    . LEU A 1 1896 ? 176.316 176.441 199.069 1.00 0.19  ? 1896 LEU A CB    1 
ATOM   3563  C  CG    . LEU A 1 1896 ? 177.574 176.619 198.216 1.00 0.13  ? 1896 LEU A CG    1 
ATOM   3564  C  CD1   . LEU A 1 1896 ? 177.258 176.436 196.744 1.00 0.14  ? 1896 LEU A CD1   1 
ATOM   3565  C  CD2   . LEU A 1 1896 ? 178.205 177.971 198.466 1.00 0.07  ? 1896 LEU A CD2   1 
ATOM   3566  N  N     . GLU A 1 1897 ? 174.503 175.297 201.427 1.00 0.34  ? 1897 GLU A N     1 
ATOM   3567  C  CA    . GLU A 1 1897 ? 173.253 175.255 202.175 1.00 0.67  ? 1897 GLU A CA    1 
ATOM   3568  C  C     . GLU A 1 1897 ? 173.475 175.547 203.653 1.00 1.18  ? 1897 GLU A C     1 
ATOM   3569  O  O     . GLU A 1 1897 ? 172.642 176.205 204.287 1.00 2.16  ? 1897 GLU A O     1 
ATOM   3570  C  CB    . GLU A 1 1897 ? 172.570 173.897 201.995 1.00 0.88  ? 1897 GLU A CB    1 
ATOM   3571  C  CG    . GLU A 1 1897 ? 171.074 173.911 202.295 1.00 1.08  ? 1897 GLU A CG    1 
ATOM   3572  C  CD    . GLU A 1 1897 ? 170.261 174.718 201.294 1.00 6.36  ? 1897 GLU A CD    1 
ATOM   3573  O  OE1   . GLU A 1 1897 ? 170.837 175.254 200.324 1.00 9.21  ? 1897 GLU A OE1   1 
ATOM   3574  O  OE2   . GLU A 1 1897 ? 169.031 174.821 201.481 1.00 11.59 ? 1897 GLU A OE2   1 
ATOM   3575  N  N     . ALA A 1 1898 ? 174.582 175.074 204.216 1.00 0.64  ? 1898 ALA A N     1 
ATOM   3576  C  CA    . ALA A 1 1898 ? 174.945 175.373 205.593 1.00 0.48  ? 1898 ALA A CA    1 
ATOM   3577  C  C     . ALA A 1 1898 ? 175.544 176.763 205.752 1.00 0.89  ? 1898 ALA A C     1 
ATOM   3578  O  O     . ALA A 1 1898 ? 175.977 177.111 206.855 1.00 1.04  ? 1898 ALA A O     1 
ATOM   3579  C  CB    . ALA A 1 1898 ? 175.926 174.322 206.120 1.00 0.35  ? 1898 ALA A CB    1 
ATOM   3580  N  N     . ARG A 1 1899 ? 175.576 177.548 204.674 1.00 0.97  ? 1899 ARG A N     1 
ATOM   3581  C  CA    . ARG A 1 1899 ? 176.174 178.884 204.674 1.00 1.08  ? 1899 ARG A CA    1 
ATOM   3582  C  C     . ARG A 1 1899 ? 177.631 178.827 205.124 1.00 0.81  ? 1899 ARG A C     1 
ATOM   3583  O  O     . ARG A 1 1899 ? 178.113 179.693 205.853 1.00 1.93  ? 1899 ARG A O     1 
ATOM   3584  C  CB    . ARG A 1 1899 ? 175.367 179.868 205.528 1.00 2.01  ? 1899 ARG A CB    1 
ATOM   3585  C  CG    . ARG A 1 1899 ? 174.165 180.497 204.823 1.00 3.90  ? 1899 ARG A CG    1 
ATOM   3586  C  CD    . ARG A 1 1899 ? 173.185 179.463 204.291 1.00 4.57  ? 1899 ARG A CD    1 
ATOM   3587  N  NE    . ARG A 1 1899 ? 172.312 179.999 203.256 1.00 12.14 ? 1899 ARG A NE    1 
ATOM   3588  C  CZ    . ARG A 1 1899 ? 171.365 179.302 202.642 1.00 10.75 ? 1899 ARG A CZ    1 
ATOM   3589  N  NH1   . ARG A 1 1899 ? 171.142 178.033 202.933 1.00 5.98  ? 1899 ARG A NH1   1 
ATOM   3590  N  NH2   . ARG A 1 1899 ? 170.626 179.895 201.707 1.00 12.71 ? 1899 ARG A NH2   1 
ATOM   3591  N  N     . LEU A 1 1900 ? 178.330 177.788 204.688 1.00 0.86  ? 1900 LEU A N     1 
ATOM   3592  C  CA    . LEU A 1 1900 ? 179.745 177.606 204.947 1.00 0.17  ? 1900 LEU A CA    1 
ATOM   3593  C  C     . LEU A 1 1900 ? 180.521 177.723 203.646 1.00 0.15  ? 1900 LEU A C     1 
ATOM   3594  O  O     . LEU A 1 1900 ? 179.961 177.635 202.550 1.00 0.19  ? 1900 LEU A O     1 
ATOM   3595  C  CB    . LEU A 1 1900 ? 180.016 176.243 205.597 1.00 0.48  ? 1900 LEU A CB    1 
ATOM   3596  C  CG    . LEU A 1 1900 ? 179.570 176.061 207.048 1.00 1.57  ? 1900 LEU A CG    1 
ATOM   3597  C  CD1   . LEU A 1 1900 ? 179.722 174.611 207.476 1.00 1.01  ? 1900 LEU A CD1   1 
ATOM   3598  C  CD2   . LEU A 1 1900 ? 180.353 176.980 207.969 1.00 0.46  ? 1900 LEU A CD2   1 
ATOM   3599  N  N     . GLY A 1 1901 ? 181.822 177.934 203.776 1.00 0.12  ? 1901 GLY A N     1 
ATOM   3600  C  CA    . GLY A 1 1901 ? 182.676 177.954 202.615 1.00 0.05  ? 1901 GLY A CA    1 
ATOM   3601  C  C     . GLY A 1 1901 ? 183.097 176.565 202.183 1.00 0.06  ? 1901 GLY A C     1 
ATOM   3602  O  O     . GLY A 1 1901 ? 183.070 175.604 202.949 1.00 0.12  ? 1901 GLY A O     1 
ATOM   3603  N  N     . GLY A 1 1902 ? 183.486 176.461 200.919 1.00 0.03  ? 1902 GLY A N     1 
ATOM   3604  C  CA    . GLY A 1 1902 ? 184.030 175.229 200.376 1.00 0.03  ? 1902 GLY A CA    1 
ATOM   3605  C  C     . GLY A 1 1902 ? 185.548 175.268 200.398 1.00 0.02  ? 1902 GLY A C     1 
ATOM   3606  O  O     . GLY A 1 1902 ? 186.157 176.289 200.082 1.00 0.03  ? 1902 GLY A O     1 
ATOM   3607  N  N     . SER A 1 1903 ? 186.149 174.148 200.783 1.00 0.04  ? 1903 SER A N     1 
ATOM   3608  C  CA    . SER A 1 1903 ? 187.604 174.030 200.887 1.00 0.03  ? 1903 SER A CA    1 
ATOM   3609  C  C     . SER A 1 1903 ? 188.088 172.749 200.218 1.00 0.06  ? 1903 SER A C     1 
ATOM   3610  O  O     . SER A 1 1903 ? 188.492 171.795 200.893 1.00 0.09  ? 1903 SER A O     1 
ATOM   3611  C  CB    . SER A 1 1903 ? 188.046 174.080 202.349 1.00 0.05  ? 1903 SER A CB    1 
ATOM   3612  O  OG    . SER A 1 1903 ? 189.454 173.973 202.453 1.00 5.69  ? 1903 SER A OG    1 
ATOM   3613  N  N     . PRO A 1 1904 ? 188.073 172.693 198.887 1.00 0.06  ? 1904 PRO A N     1 
ATOM   3614  C  CA    . PRO A 1 1904 ? 188.717 171.566 198.197 1.00 0.05  ? 1904 PRO A CA    1 
ATOM   3615  C  C     . PRO A 1 1904 ? 190.226 171.613 198.394 1.00 0.06  ? 1904 PRO A C     1 
ATOM   3616  O  O     . PRO A 1 1904 ? 190.859 172.652 198.195 1.00 0.31  ? 1904 PRO A O     1 
ATOM   3617  C  CB    . PRO A 1 1904 ? 188.329 171.775 196.727 1.00 0.05  ? 1904 PRO A CB    1 
ATOM   3618  C  CG    . PRO A 1 1904 ? 187.182 172.737 196.760 1.00 0.05  ? 1904 PRO A CG    1 
ATOM   3619  C  CD    . PRO A 1 1904 ? 187.444 173.617 197.930 1.00 0.05  ? 1904 PRO A CD    1 
ATOM   3620  N  N     . PHE A 1 1905 ? 190.799 170.482 198.795 1.00 0.06  ? 1905 PHE A N     1 
ATOM   3621  C  CA    . PHE A 1 1905 ? 192.225 170.388 199.062 1.00 0.11  ? 1905 PHE A CA    1 
ATOM   3622  C  C     . PHE A 1 1905 ? 192.795 169.142 198.400 1.00 0.07  ? 1905 PHE A C     1 
ATOM   3623  O  O     . PHE A 1 1905 ? 192.108 168.128 198.252 1.00 0.14  ? 1905 PHE A O     1 
ATOM   3624  C  CB    . PHE A 1 1905 ? 192.518 170.362 200.573 1.00 0.17  ? 1905 PHE A CB    1 
ATOM   3625  C  CG    . PHE A 1 1905 ? 192.022 169.128 201.268 1.00 0.08  ? 1905 PHE A CG    1 
ATOM   3626  C  CD1   . PHE A 1 1905 ? 190.733 169.070 201.767 1.00 0.08  ? 1905 PHE A CD1   1 
ATOM   3627  C  CD2   . PHE A 1 1905 ? 192.849 168.031 201.437 1.00 0.09  ? 1905 PHE A CD2   1 
ATOM   3628  C  CE1   . PHE A 1 1905 ? 190.277 167.941 202.409 1.00 0.15  ? 1905 PHE A CE1   1 
ATOM   3629  C  CE2   . PHE A 1 1905 ? 192.395 166.901 202.078 1.00 0.19  ? 1905 PHE A CE2   1 
ATOM   3630  C  CZ    . PHE A 1 1905 ? 191.108 166.856 202.566 1.00 0.38  ? 1905 PHE A CZ    1 
ATOM   3631  N  N     . GLY A 1 1906 ? 194.061 169.229 198.008 1.00 0.10  ? 1906 GLY A N     1 
ATOM   3632  C  CA    . GLY A 1 1906 ? 194.748 168.121 197.395 1.00 0.35  ? 1906 GLY A CA    1 
ATOM   3633  C  C     . GLY A 1 1906 ? 196.010 168.555 196.684 1.00 0.74  ? 1906 GLY A C     1 
ATOM   3634  O  O     . GLY A 1 1906 ? 196.398 169.726 196.712 1.00 0.86  ? 1906 GLY A O     1 
ATOM   3635  N  N     . PRO A 1 1907 ? 196.723 167.617 196.016 1.00 2.28  ? 1907 PRO A N     1 
ATOM   3636  C  CA    . PRO A 1 1907 ? 197.915 167.971 195.260 1.00 1.36  ? 1907 PRO A CA    1 
ATOM   3637  C  C     . PRO A 1 1907 ? 197.564 168.777 194.019 1.00 1.94  ? 1907 PRO A C     1 
ATOM   3638  O  O     . PRO A 1 1907 ? 196.369 168.926 193.703 1.00 2.30  ? 1907 PRO A O     1 
ATOM   3639  C  CB    . PRO A 1 1907 ? 198.518 166.604 194.920 1.00 1.18  ? 1907 PRO A CB    1 
ATOM   3640  C  CG    . PRO A 1 1907 ? 197.316 165.696 194.824 1.00 1.62  ? 1907 PRO A CG    1 
ATOM   3641  C  CD    . PRO A 1 1907 ? 196.412 166.188 195.938 1.00 1.12  ? 1907 PRO A CD    1 
ATOM   3642  N  N     . ALA A 1 1908 ? 198.580 169.277 193.317 1.00 2.83  ? 1908 ALA A N     1 
ATOM   3643  C  CA    . ALA A 1 1908 ? 198.344 170.142 192.136 1.00 2.35  ? 1908 ALA A CA    1 
ATOM   3644  C  C     . ALA A 1 1908 ? 197.791 169.344 190.953 1.00 1.69  ? 1908 ALA A C     1 
ATOM   3645  O  O     . ALA A 1 1908 ? 198.147 168.159 190.799 1.00 4.60  ? 1908 ALA A O     1 
ATOM   3646  C  CB    . ALA A 1 1908 ? 199.632 170.841 191.766 1.00 3.80  ? 1908 ALA A CB    1 
ATOM   3647  N  N     . GLY A 1 1909 ? 196.948 169.981 190.140 1.00 0.67  ? 1909 GLY A N     1 
ATOM   3648  C  CA    . GLY A 1 1909 ? 196.427 169.336 188.922 1.00 0.90  ? 1909 GLY A CA    1 
ATOM   3649  C  C     . GLY A 1 1909 ? 195.370 168.294 189.216 1.00 0.99  ? 1909 GLY A C     1 
ATOM   3650  O  O     . GLY A 1 1909 ? 195.337 167.278 188.499 1.00 1.51  ? 1909 GLY A O     1 
ATOM   3651  N  N     . THR A 1 1910 ? 194.523 168.524 190.218 1.00 1.20  ? 1910 THR A N     1 
ATOM   3652  C  CA    . THR A 1 1910 ? 193.447 167.574 190.452 1.00 0.93  ? 1910 THR A CA    1 
ATOM   3653  C  C     . THR A 1 1910 ? 192.071 168.131 190.117 1.00 0.49  ? 1910 THR A C     1 
ATOM   3654  O  O     . THR A 1 1910 ? 191.077 167.422 190.299 1.00 2.75  ? 1910 THR A O     1 
ATOM   3655  C  CB    . THR A 1 1910 ? 193.456 167.095 191.913 1.00 1.13  ? 1910 THR A CB    1 
ATOM   3656  O  OG1   . THR A 1 1910 ? 193.447 168.222 192.796 1.00 1.66  ? 1910 THR A OG1   1 
ATOM   3657  C  CG2   . THR A 1 1910 ? 194.688 166.253 192.185 1.00 0.63  ? 1910 THR A CG2   1 
ATOM   3658  N  N     . GLY A 1 1911 ? 191.991 169.363 189.629 1.00 0.15  ? 1911 GLY A N     1 
ATOM   3659  C  CA    . GLY A 1 1911 ? 190.726 169.964 189.274 1.00 0.11  ? 1911 GLY A CA    1 
ATOM   3660  C  C     . GLY A 1 1911 ? 190.062 170.777 190.358 1.00 0.12  ? 1911 GLY A C     1 
ATOM   3661  O  O     . GLY A 1 1911 ? 188.877 171.091 190.223 1.00 0.16  ? 1911 GLY A O     1 
ATOM   3662  N  N     . LYS A 1 1912 ? 190.792 171.123 191.413 1.00 0.22  ? 1912 LYS A N     1 
ATOM   3663  C  CA    . LYS A 1 1912 ? 190.192 171.853 192.559 1.00 0.08  ? 1912 LYS A CA    1 
ATOM   3664  C  C     . LYS A 1 1912 ? 189.582 173.186 192.089 1.00 0.06  ? 1912 LYS A C     1 
ATOM   3665  O  O     . LYS A 1 1912 ? 188.381 173.399 192.342 1.00 0.05  ? 1912 LYS A O     1 
ATOM   3666  C  CB    . LYS A 1 1912 ? 191.252 172.060 193.645 1.00 0.25  ? 1912 LYS A CB    1 
ATOM   3667  C  CG    . LYS A 1 1912 ? 191.719 170.797 194.351 1.00 0.19  ? 1912 LYS A CG    1 
ATOM   3668  C  CD    . LYS A 1 1912 ? 192.678 171.077 195.501 1.00 0.12  ? 1912 LYS A CD    1 
ATOM   3669  C  CE    . LYS A 1 1912 ? 193.895 171.831 195.073 1.00 0.22  ? 1912 LYS A CE    1 
ATOM   3670  N  NZ    . LYS A 1 1912 ? 194.666 171.100 194.064 1.00 0.47  ? 1912 LYS A NZ    1 
ATOM   3671  N  N     . THR A 1 1913 ? 190.368 174.035 191.423 1.00 0.09  ? 1913 THR A N     1 
ATOM   3672  C  CA    . THR A 1 1913 ? 189.889 175.375 191.010 1.00 0.11  ? 1913 THR A CA    1 
ATOM   3673  C  C     . THR A 1 1913 ? 188.833 175.251 189.934 1.00 0.08  ? 1913 THR A C     1 
ATOM   3674  O  O     . THR A 1 1913 ? 187.816 175.969 190.022 1.00 0.05  ? 1913 THR A O     1 
ATOM   3675  C  CB    . THR A 1 1913 ? 191.084 176.208 190.540 1.00 0.18  ? 1913 THR A CB    1 
ATOM   3676  O  OG1   . THR A 1 1913 ? 192.030 176.161 191.604 1.00 0.46  ? 1913 THR A OG1   1 
ATOM   3677  C  CG2   . THR A 1 1913 ? 190.709 177.645 190.228 1.00 0.41  ? 1913 THR A CG2   1 
ATOM   3678  N  N     . GLU A 1 1914 ? 189.048 174.370 188.959 1.00 0.05  ? 1914 GLU A N     1 
ATOM   3679  C  CA    . GLU A 1 1914 ? 188.107 174.248 187.816 1.00 0.09  ? 1914 GLU A CA    1 
ATOM   3680  C  C     . GLU A 1 1914 ? 186.752 173.718 188.312 1.00 0.03  ? 1914 GLU A C     1 
ATOM   3681  O  O     . GLU A 1 1914 ? 185.718 174.140 187.765 1.00 0.04  ? 1914 GLU A O     1 
ATOM   3682  C  CB    . GLU A 1 1914 ? 188.722 173.370 186.726 1.00 0.91  ? 1914 GLU A CB    1 
ATOM   3683  C  CG    . GLU A 1 1914 ? 189.958 173.998 186.092 1.00 0.99  ? 1914 GLU A CG    1 
ATOM   3684  C  CD    . GLU A 1 1914 ? 189.821 175.489 185.842 1.00 4.12  ? 1914 GLU A CD    1 
ATOM   3685  O  OE1   . GLU A 1 1914 ? 188.921 175.882 185.069 1.00 4.40  ? 1914 GLU A OE1   1 
ATOM   3686  O  OE2   . GLU A 1 1914 ? 190.613 176.259 186.425 1.00 5.58  ? 1914 GLU A OE2   1 
ATOM   3687  N  N     . SER A 1 1915 ? 186.768 172.848 189.320 1.00 0.06  ? 1915 SER A N     1 
ATOM   3688  C  CA    . SER A 1 1915 ? 185.513 172.315 189.836 1.00 0.04  ? 1915 SER A CA    1 
ATOM   3689  C  C     . SER A 1 1915 ? 184.697 173.396 190.533 1.00 0.02  ? 1915 SER A C     1 
ATOM   3690  O  O     . SER A 1 1915 ? 183.468 173.433 190.406 1.00 0.04  ? 1915 SER A O     1 
ATOM   3691  C  CB    . SER A 1 1915 ? 185.787 171.152 190.787 1.00 0.06  ? 1915 SER A CB    1 
ATOM   3692  O  OG    . SER A 1 1915 ? 186.511 170.129 190.135 1.00 0.30  ? 1915 SER A OG    1 
ATOM   3693  N  N     . VAL A 1 1916 ? 185.364 174.280 191.278 1.00 0.04  ? 1916 VAL A N     1 
ATOM   3694  C  CA    . VAL A 1 1916 ? 184.663 175.376 191.940 1.00 0.05  ? 1916 VAL A CA    1 
ATOM   3695  C  C     . VAL A 1 1916 ? 184.035 176.302 190.906 1.00 0.05  ? 1916 VAL A C     1 
ATOM   3696  O  O     . VAL A 1 1916 ? 182.874 176.706 191.033 1.00 0.02  ? 1916 VAL A O     1 
ATOM   3697  C  CB    . VAL A 1 1916 ? 185.617 176.137 192.880 1.00 0.03  ? 1916 VAL A CB    1 
ATOM   3698  C  CG1   . VAL A 1 1916 ? 184.974 177.427 193.372 1.00 0.02  ? 1916 VAL A CG1   1 
ATOM   3699  C  CG2   . VAL A 1 1916 ? 186.017 175.261 194.052 1.00 0.06  ? 1916 VAL A CG2   1 
ATOM   3700  N  N     . LYS A 1 1917 ? 184.794 176.648 189.862 1.00 0.02  ? 1917 LYS A N     1 
ATOM   3701  C  CA    . LYS A 1 1917 ? 184.240 177.480 188.799 1.00 0.03  ? 1917 LYS A CA    1 
ATOM   3702  C  C     . LYS A 1 1917 ? 183.131 176.755 188.055 1.00 0.03  ? 1917 LYS A C     1 
ATOM   3703  O  O     . LYS A 1 1917 ? 182.118 177.362 187.691 1.00 0.03  ? 1917 LYS A O     1 
ATOM   3704  C  CB    . LYS A 1 1917 ? 185.337 177.922 187.829 1.00 0.06  ? 1917 LYS A CB    1 
ATOM   3705  C  CG    . LYS A 1 1917 ? 186.374 178.843 188.438 1.00 1.09  ? 1917 LYS A CG    1 
ATOM   3706  C  CD    . LYS A 1 1917 ? 187.201 179.542 187.371 1.00 2.82  ? 1917 LYS A CD    1 
ATOM   3707  C  CE    . LYS A 1 1917 ? 187.914 178.561 186.472 1.00 2.41  ? 1917 LYS A CE    1 
ATOM   3708  N  NZ    . LYS A 1 1917 ? 188.651 179.241 185.375 1.00 1.21  ? 1917 LYS A NZ    1 
ATOM   3709  N  N     . ALA A 1 1918 ? 183.305 175.453 187.814 1.00 0.02  ? 1918 ALA A N     1 
ATOM   3710  C  CA    . ALA A 1 1918 ? 182.279 174.687 187.118 1.00 0.03  ? 1918 ALA A CA    1 
ATOM   3711  C  C     . ALA A 1 1918 ? 180.973 174.687 187.903 1.00 0.04  ? 1918 ALA A C     1 
ATOM   3712  O  O     . ALA A 1 1918 ? 179.893 174.870 187.333 1.00 0.02  ? 1918 ALA A O     1 
ATOM   3713  C  CB    . ALA A 1 1918 ? 182.767 173.260 186.869 1.00 0.03  ? 1918 ALA A CB    1 
ATOM   3714  N  N     . LEU A 1 1919 ? 181.055 174.498 189.221 1.00 0.03  ? 1919 LEU A N     1 
ATOM   3715  C  CA    . LEU A 1 1919 ? 179.860 174.553 190.052 1.00 0.04  ? 1919 LEU A CA    1 
ATOM   3716  C  C     . LEU A 1 1919 ? 179.237 175.944 190.019 1.00 0.06  ? 1919 LEU A C     1 
ATOM   3717  O  O     . LEU A 1 1919 ? 178.013 176.088 189.929 1.00 0.01  ? 1919 LEU A O     1 
ATOM   3718  C  CB    . LEU A 1 1919 ? 180.192 174.144 191.487 1.00 0.08  ? 1919 LEU A CB    1 
ATOM   3719  C  CG    . LEU A 1 1919 ? 179.019 174.207 192.466 1.00 0.02  ? 1919 LEU A CG    1 
ATOM   3720  C  CD1   . LEU A 1 1919 ? 177.852 173.364 191.966 1.00 0.01  ? 1919 LEU A CD1   1 
ATOM   3721  C  CD2   . LEU A 1 1919 ? 179.447 173.770 193.849 1.00 0.03  ? 1919 LEU A CD2   1 
ATOM   3722  N  N     . GLY A 1 1920 ? 180.072 176.982 190.087 1.00 0.20  ? 1920 GLY A N     1 
ATOM   3723  C  CA    . GLY A 1 1920 ? 179.559 178.338 189.986 1.00 0.03  ? 1920 GLY A CA    1 
ATOM   3724  C  C     . GLY A 1 1920 ? 178.910 178.621 188.646 1.00 0.05  ? 1920 GLY A C     1 
ATOM   3725  O  O     . GLY A 1 1920 ? 177.844 179.233 188.575 1.00 0.04  ? 1920 GLY A O     1 
ATOM   3726  N  N     . HIS A 1 1921 ? 179.551 178.181 187.561 1.00 0.03  ? 1921 HIS A N     1 
ATOM   3727  C  CA    . HIS A 1 1921 ? 178.960 178.356 186.239 1.00 0.07  ? 1921 HIS A CA    1 
ATOM   3728  C  C     . HIS A 1 1921 ? 177.699 177.518 186.087 1.00 0.03  ? 1921 HIS A C     1 
ATOM   3729  O  O     . HIS A 1 1921 ? 176.770 177.905 185.369 1.00 0.07  ? 1921 HIS A O     1 
ATOM   3730  C  CB    . HIS A 1 1921 ? 179.976 178.008 185.149 1.00 0.21  ? 1921 HIS A CB    1 
ATOM   3731  C  CG    . HIS A 1 1921 ? 181.224 178.831 185.206 1.00 1.28  ? 1921 HIS A CG    1 
ATOM   3732  N  ND1   . HIS A 1 1921 ? 182.375 178.483 184.532 1.00 11.11 ? 1921 HIS A ND1   1 
ATOM   3733  C  CD2   . HIS A 1 1921 ? 181.503 179.986 185.854 1.00 0.52  ? 1921 HIS A CD2   1 
ATOM   3734  C  CE1   . HIS A 1 1921 ? 183.308 179.391 184.762 1.00 5.25  ? 1921 HIS A CE1   1 
ATOM   3735  N  NE2   . HIS A 1 1921 ? 182.805 180.312 185.562 1.00 5.25  ? 1921 HIS A NE2   1 
ATOM   3736  N  N     . GLN A 1 1922 ? 177.649 176.365 186.754 1.00 0.04  ? 1922 GLN A N     1 
ATOM   3737  C  CA    . GLN A 1 1922 ? 176.431 175.566 186.767 1.00 0.05  ? 1922 GLN A CA    1 
ATOM   3738  C  C     . GLN A 1 1922 ? 175.277 176.337 187.394 1.00 0.03  ? 1922 GLN A C     1 
ATOM   3739  O  O     . GLN A 1 1922 ? 174.137 176.260 186.923 1.00 0.05  ? 1922 GLN A O     1 
ATOM   3740  C  CB    . GLN A 1 1922 ? 176.672 174.258 187.519 1.00 0.09  ? 1922 GLN A CB    1 
ATOM   3741  C  CG    . GLN A 1 1922 ? 175.478 173.335 187.534 1.00 0.21  ? 1922 GLN A CG    1 
ATOM   3742  C  CD    . GLN A 1 1922 ? 175.090 172.873 186.149 1.00 0.61  ? 1922 GLN A CD    1 
ATOM   3743  O  OE1   . GLN A 1 1922 ? 175.799 172.087 185.524 1.00 0.41  ? 1922 GLN A OE1   1 
ATOM   3744  N  NE2   . GLN A 1 1922 ? 173.970 173.378 185.651 1.00 1.07  ? 1922 GLN A NE2   1 
ATOM   3745  N  N     . LEU A 1 1923 ? 175.557 177.088 188.453 1.00 0.04  ? 1923 LEU A N     1 
ATOM   3746  C  CA    . LEU A 1 1923 ? 174.550 177.872 189.151 1.00 0.05  ? 1923 LEU A CA    1 
ATOM   3747  C  C     . LEU A 1 1923 ? 174.395 179.276 188.582 1.00 0.09  ? 1923 LEU A C     1 
ATOM   3748  O  O     . LEU A 1 1923 ? 173.642 180.077 189.147 1.00 0.31  ? 1923 LEU A O     1 
ATOM   3749  C  CB    . LEU A 1 1923 ? 174.889 177.949 190.642 1.00 0.12  ? 1923 LEU A CB    1 
ATOM   3750  C  CG    . LEU A 1 1923 ? 174.979 176.604 191.373 1.00 0.05  ? 1923 LEU A CG    1 
ATOM   3751  C  CD1   . LEU A 1 1923 ? 175.162 176.802 192.867 1.00 0.03  ? 1923 LEU A CD1   1 
ATOM   3752  C  CD2   . LEU A 1 1923 ? 173.757 175.747 191.087 1.00 0.02  ? 1923 LEU A CD2   1 
ATOM   3753  N  N     . GLY A 1 1924 ? 175.079 179.591 187.487 1.00 0.09  ? 1924 GLY A N     1 
ATOM   3754  C  CA    . GLY A 1 1924 ? 174.988 180.906 186.875 1.00 0.09  ? 1924 GLY A CA    1 
ATOM   3755  C  C     . GLY A 1 1924 ? 175.569 182.023 187.713 1.00 0.09  ? 1924 GLY A C     1 
ATOM   3756  O  O     . GLY A 1 1924 ? 175.047 183.144 187.691 1.00 0.26  ? 1924 GLY A O     1 
ATOM   3757  N  N     . ARG A 1 1925 ? 176.641 181.751 188.442 1.00 0.05  ? 1925 ARG A N     1 
ATOM   3758  C  CA    . ARG A 1 1925 ? 177.258 182.731 189.318 1.00 0.07  ? 1925 ARG A CA    1 
ATOM   3759  C  C     . ARG A 1 1925 ? 178.517 183.302 188.683 1.00 0.06  ? 1925 ARG A C     1 
ATOM   3760  O  O     . ARG A 1 1925 ? 179.184 182.649 187.878 1.00 0.06  ? 1925 ARG A O     1 
ATOM   3761  C  CB    . ARG A 1 1925 ? 177.601 182.112 190.676 1.00 0.06  ? 1925 ARG A CB    1 
ATOM   3762  C  CG    . ARG A 1 1925 ? 176.426 181.475 191.385 1.00 0.06  ? 1925 ARG A CG    1 
ATOM   3763  C  CD    . ARG A 1 1925 ? 175.660 182.490 192.214 1.00 0.19  ? 1925 ARG A CD    1 
ATOM   3764  N  NE    . ARG A 1 1925 ? 174.687 181.863 193.100 1.00 0.39  ? 1925 ARG A NE    1 
ATOM   3765  C  CZ    . ARG A 1 1925 ? 173.565 181.282 192.699 1.00 0.63  ? 1925 ARG A CZ    1 
ATOM   3766  N  NH1   . ARG A 1 1925 ? 173.226 181.235 191.421 1.00 0.42  ? 1925 ARG A NH1   1 
ATOM   3767  N  NH2   . ARG A 1 1925 ? 172.757 180.738 193.603 1.00 0.51  ? 1925 ARG A NH2   1 
ATOM   3768  N  N     . PHE A 1 1926 ? 178.831 184.539 189.056 1.00 0.10  ? 1926 PHE A N     1 
ATOM   3769  C  CA    . PHE A 1 1926 ? 180.087 185.171 188.675 1.00 0.11  ? 1926 PHE A CA    1 
ATOM   3770  C  C     . PHE A 1 1926 ? 181.170 184.665 189.624 1.00 0.03  ? 1926 PHE A C     1 
ATOM   3771  O  O     . PHE A 1 1926 ? 181.173 185.005 190.809 1.00 0.04  ? 1926 PHE A O     1 
ATOM   3772  C  CB    . PHE A 1 1926 ? 179.940 186.691 188.730 1.00 0.22  ? 1926 PHE A CB    1 
ATOM   3773  C  CG    . PHE A 1 1926 ? 181.142 187.454 188.246 1.00 0.33  ? 1926 PHE A CG    1 
ATOM   3774  C  CD1   . PHE A 1 1926 ? 182.184 186.822 187.588 1.00 0.25  ? 1926 PHE A CD1   1 
ATOM   3775  C  CD2   . PHE A 1 1926 ? 181.217 188.825 188.437 1.00 0.53  ? 1926 PHE A CD2   1 
ATOM   3776  C  CE1   . PHE A 1 1926 ? 183.279 187.536 187.145 1.00 0.36  ? 1926 PHE A CE1   1 
ATOM   3777  C  CE2   . PHE A 1 1926 ? 182.309 189.544 187.995 1.00 1.08  ? 1926 PHE A CE2   1 
ATOM   3778  C  CZ    . PHE A 1 1926 ? 183.341 188.901 187.348 1.00 1.25  ? 1926 PHE A CZ    1 
ATOM   3779  N  N     . VAL A 1 1927 ? 182.079 183.846 189.109 1.00 0.02  ? 1927 VAL A N     1 
ATOM   3780  C  CA    . VAL A 1 1927 ? 183.145 183.247 189.902 1.00 0.02  ? 1927 VAL A CA    1 
ATOM   3781  C  C     . VAL A 1 1927 ? 184.422 184.038 189.657 1.00 0.02  ? 1927 VAL A C     1 
ATOM   3782  O  O     . VAL A 1 1927 ? 184.864 184.176 188.510 1.00 0.05  ? 1927 VAL A O     1 
ATOM   3783  C  CB    . VAL A 1 1927 ? 183.343 181.763 189.553 1.00 0.03  ? 1927 VAL A CB    1 
ATOM   3784  C  CG1   . VAL A 1 1927 ? 184.366 181.126 190.484 1.00 0.02  ? 1927 VAL A CG1   1 
ATOM   3785  C  CG2   . VAL A 1 1927 ? 182.025 181.019 189.612 1.00 0.02  ? 1927 VAL A CG2   1 
ATOM   3786  N  N     . LEU A 1 1928 ? 185.015 184.554 190.726 1.00 0.03  ? 1928 LEU A N     1 
ATOM   3787  C  CA    . LEU A 1 1928 ? 186.273 185.281 190.652 1.00 0.03  ? 1928 LEU A CA    1 
ATOM   3788  C  C     . LEU A 1 1928 ? 187.368 184.463 191.319 1.00 0.04  ? 1928 LEU A C     1 
ATOM   3789  O  O     . LEU A 1 1928 ? 187.221 184.037 192.468 1.00 0.09  ? 1928 LEU A O     1 
ATOM   3790  C  CB    . LEU A 1 1928 ? 186.178 186.658 191.311 1.00 0.19  ? 1928 LEU A CB    1 
ATOM   3791  C  CG    . LEU A 1 1928 ? 185.477 187.781 190.543 1.00 0.21  ? 1928 LEU A CG    1 
ATOM   3792  C  CD1   . LEU A 1 1928 ? 183.973 187.580 190.524 1.00 0.11  ? 1928 LEU A CD1   1 
ATOM   3793  C  CD2   . LEU A 1 1928 ? 185.844 189.144 191.099 1.00 0.29  ? 1928 LEU A CD2   1 
ATOM   3794  N  N     . VAL A 1 1929 ? 188.456 184.252 190.595 1.00 0.09  ? 1929 VAL A N     1 
ATOM   3795  C  CA    . VAL A 1 1929 ? 189.609 183.508 191.081 1.00 0.12  ? 1929 VAL A CA    1 
ATOM   3796  C  C     . VAL A 1 1929 ? 190.653 184.507 191.551 1.00 0.11  ? 1929 VAL A C     1 
ATOM   3797  O  O     . VAL A 1 1929 ? 190.912 185.509 190.876 1.00 0.32  ? 1929 VAL A O     1 
ATOM   3798  C  CB    . VAL A 1 1929 ? 190.170 182.585 189.984 1.00 0.29  ? 1929 VAL A CB    1 
ATOM   3799  C  CG1   . VAL A 1 1929 ? 191.575 182.129 190.320 1.00 0.93  ? 1929 VAL A CG1   1 
ATOM   3800  C  CG2   . VAL A 1 1929 ? 189.252 181.396 189.779 1.00 0.16  ? 1929 VAL A CG2   1 
ATOM   3801  N  N     . PHE A 1 1930 ? 191.233 184.253 192.720 1.00 0.16  ? 1930 PHE A N     1 
ATOM   3802  C  CA    . PHE A 1 1930 ? 192.320 185.068 193.248 1.00 0.14  ? 1930 PHE A CA    1 
ATOM   3803  C  C     . PHE A 1 1930 ? 193.505 184.165 193.552 1.00 0.56  ? 1930 PHE A C     1 
ATOM   3804  O  O     . PHE A 1 1930 ? 193.362 183.169 194.267 1.00 0.89  ? 1930 PHE A O     1 
ATOM   3805  C  CB    . PHE A 1 1930 ? 191.884 185.833 194.500 1.00 0.16  ? 1930 PHE A CB    1 
ATOM   3806  C  CG    . PHE A 1 1930 ? 190.707 186.736 194.273 1.00 0.08  ? 1930 PHE A CG    1 
ATOM   3807  C  CD1   . PHE A 1 1930 ? 190.893 188.046 193.874 1.00 0.07  ? 1930 PHE A CD1   1 
ATOM   3808  C  CD2   . PHE A 1 1930 ? 189.417 186.272 194.451 1.00 0.07  ? 1930 PHE A CD2   1 
ATOM   3809  C  CE1   . PHE A 1 1930 ? 189.816 188.877 193.659 1.00 0.12  ? 1930 PHE A CE1   1 
ATOM   3810  C  CE2   . PHE A 1 1930 ? 188.337 187.099 194.235 1.00 0.07  ? 1930 PHE A CE2   1 
ATOM   3811  C  CZ    . PHE A 1 1930 ? 188.537 188.404 193.839 1.00 0.09  ? 1930 PHE A CZ    1 
ATOM   3812  N  N     . ASN A 1 1931 ? 194.663 184.504 192.995 1.00 0.66  ? 1931 ASN A N     1 
ATOM   3813  C  CA    . ASN A 1 1931 ? 195.912 183.810 193.298 1.00 0.48  ? 1931 ASN A CA    1 
ATOM   3814  C  C     . ASN A 1 1931 ? 196.493 184.470 194.542 1.00 0.69  ? 1931 ASN A C     1 
ATOM   3815  O  O     . ASN A 1 1931 ? 197.126 185.523 194.466 1.00 1.68  ? 1931 ASN A O     1 
ATOM   3816  C  CB    . ASN A 1 1931 ? 196.867 183.880 192.112 1.00 0.55  ? 1931 ASN A CB    1 
ATOM   3817  C  CG    . ASN A 1 1931 ? 198.136 183.073 192.316 1.00 0.90  ? 1931 ASN A CG    1 
ATOM   3818  O  OD1   . ASN A 1 1931 ? 198.715 183.043 193.401 1.00 2.32  ? 1931 ASN A OD1   1 
ATOM   3819  N  ND2   . ASN A 1 1931 ? 198.587 182.428 191.254 1.00 0.41  ? 1931 ASN A ND2   1 
ATOM   3820  N  N     . CYS A 1 1932 ? 196.272 183.848 195.693 1.00 0.93  ? 1932 CYS A N     1 
ATOM   3821  C  CA    . CYS A 1 1932 ? 196.646 184.439 196.967 1.00 0.95  ? 1932 CYS A CA    1 
ATOM   3822  C  C     . CYS A 1 1932 ? 198.144 184.322 197.217 1.00 1.38  ? 1932 CYS A C     1 
ATOM   3823  O  O     . CYS A 1 1932 ? 198.793 183.359 196.801 1.00 2.62  ? 1932 CYS A O     1 
ATOM   3824  C  CB    . CYS A 1 1932 ? 195.881 183.762 198.103 1.00 1.06  ? 1932 CYS A CB    1 
ATOM   3825  S  SG    . CYS A 1 1932 ? 194.096 183.983 198.047 1.00 4.43  ? 1932 CYS A SG    1 
ATOM   3826  N  N     . ASP A 1 1933 ? 198.693 185.322 197.904 1.00 1.07  ? 1933 ASP A N     1 
ATOM   3827  C  CA    . ASP A 1 1933 ? 200.052 185.248 198.418 1.00 1.60  ? 1933 ASP A CA    1 
ATOM   3828  C  C     . ASP A 1 1933 ? 200.093 185.934 199.778 1.00 1.91  ? 1933 ASP A C     1 
ATOM   3829  O  O     . ASP A 1 1933 ? 199.059 186.305 200.341 1.00 1.69  ? 1933 ASP A O     1 
ATOM   3830  C  CB    . ASP A 1 1933 ? 201.070 185.854 197.440 1.00 3.07  ? 1933 ASP A CB    1 
ATOM   3831  C  CG    . ASP A 1 1933 ? 200.858 187.340 197.190 1.00 3.55  ? 1933 ASP A CG    1 
ATOM   3832  O  OD1   . ASP A 1 1933 ? 199.903 187.931 197.727 1.00 3.23  ? 1933 ASP A OD1   1 
ATOM   3833  O  OD2   . ASP A 1 1933 ? 201.674 187.929 196.453 1.00 14.37 ? 1933 ASP A OD2   1 
ATOM   3834  N  N     . GLU A 1 1934 ? 201.308 186.106 200.303 1.00 4.84  ? 1934 GLU A N     1 
ATOM   3835  C  CA    . GLU A 1 1934 ? 201.487 186.716 201.615 1.00 2.66  ? 1934 GLU A CA    1 
ATOM   3836  C  C     . GLU A 1 1934 ? 201.093 188.187 201.647 1.00 3.13  ? 1934 GLU A C     1 
ATOM   3837  O  O     . GLU A 1 1934 ? 200.946 188.746 202.738 1.00 7.03  ? 1934 GLU A O     1 
ATOM   3838  C  CB    . GLU A 1 1934 ? 202.939 186.554 202.070 1.00 6.08  ? 1934 GLU A CB    1 
ATOM   3839  C  CG    . GLU A 1 1934 ? 203.933 187.429 201.322 1.00 6.68  ? 1934 GLU A CG    1 
ATOM   3840  C  CD    . GLU A 1 1934 ? 204.309 186.863 199.967 1.00 12.71 ? 1934 GLU A CD    1 
ATOM   3841  O  OE1   . GLU A 1 1934 ? 203.906 185.719 199.666 1.00 14.46 ? 1934 GLU A OE1   1 
ATOM   3842  O  OE2   . GLU A 1 1934 ? 205.005 187.563 199.205 1.00 16.55 ? 1934 GLU A OE2   1 
ATOM   3843  N  N     . THR A 1 1935 ? 200.920 188.827 200.490 1.00 3.17  ? 1935 THR A N     1 
ATOM   3844  C  CA    . THR A 1 1935 ? 200.494 190.220 200.452 1.00 1.70  ? 1935 THR A CA    1 
ATOM   3845  C  C     . THR A 1 1935 ? 198.985 190.384 200.576 1.00 2.03  ? 1935 THR A C     1 
ATOM   3846  O  O     . THR A 1 1935 ? 198.511 191.519 200.682 1.00 2.71  ? 1935 THR A O     1 
ATOM   3847  C  CB    . THR A 1 1935 ? 200.982 190.888 199.165 1.00 2.23  ? 1935 THR A CB    1 
ATOM   3848  O  OG1   . THR A 1 1935 ? 200.312 190.311 198.038 1.00 3.63  ? 1935 THR A OG1   1 
ATOM   3849  C  CG2   . THR A 1 1935 ? 202.480 190.706 199.010 1.00 1.80  ? 1935 THR A CG2   1 
ATOM   3850  N  N     . PHE A 1 1936 ? 198.224 189.293 200.560 1.00 2.58  ? 1936 PHE A N     1 
ATOM   3851  C  CA    . PHE A 1 1936 ? 196.782 189.341 200.797 1.00 1.66  ? 1936 PHE A CA    1 
ATOM   3852  C  C     . PHE A 1 1936 ? 196.563 189.431 202.301 1.00 2.39  ? 1936 PHE A C     1 
ATOM   3853  O  O     . PHE A 1 1936 ? 196.396 188.424 202.990 1.00 7.19  ? 1936 PHE A O     1 
ATOM   3854  C  CB    . PHE A 1 1936 ? 196.092 188.119 200.202 1.00 1.07  ? 1936 PHE A CB    1 
ATOM   3855  C  CG    . PHE A 1 1936 ? 195.846 188.218 198.726 1.00 1.33  ? 1936 PHE A CG    1 
ATOM   3856  C  CD1   . PHE A 1 1936 ? 196.901 188.199 197.829 1.00 0.91  ? 1936 PHE A CD1   1 
ATOM   3857  C  CD2   . PHE A 1 1936 ? 194.556 188.324 198.231 1.00 0.94  ? 1936 PHE A CD2   1 
ATOM   3858  C  CE1   . PHE A 1 1936 ? 196.675 188.288 196.473 1.00 0.72  ? 1936 PHE A CE1   1 
ATOM   3859  C  CE2   . PHE A 1 1936 ? 194.325 188.412 196.875 1.00 0.72  ? 1936 PHE A CE2   1 
ATOM   3860  C  CZ    . PHE A 1 1936 ? 195.386 188.394 195.995 1.00 0.70  ? 1936 PHE A CZ    1 
ATOM   3861  N  N     . ASP A 1 1937 ? 196.574 190.653 202.820 1.00 2.36  ? 1937 ASP A N     1 
ATOM   3862  C  CA    . ASP A 1 1937 ? 196.475 190.877 204.253 1.00 1.54  ? 1937 ASP A CA    1 
ATOM   3863  C  C     . ASP A 1 1937 ? 195.014 191.062 204.663 1.00 1.66  ? 1937 ASP A C     1 
ATOM   3864  O  O     . ASP A 1 1937 ? 194.087 190.854 203.877 1.00 1.63  ? 1937 ASP A O     1 
ATOM   3865  C  CB    . ASP A 1 1937 ? 197.356 192.059 204.661 1.00 1.79  ? 1937 ASP A CB    1 
ATOM   3866  C  CG    . ASP A 1 1937 ? 197.004 193.347 203.930 1.00 4.32  ? 1937 ASP A CG    1 
ATOM   3867  O  OD1   . ASP A 1 1937 ? 195.849 193.517 203.490 1.00 3.36  ? 1937 ASP A OD1   1 
ATOM   3868  O  OD2   . ASP A 1 1937 ? 197.902 194.203 203.796 1.00 15.10 ? 1937 ASP A OD2   1 
ATOM   3869  N  N     . PHE A 1 1938 ? 194.804 191.460 205.919 1.00 1.70  ? 1938 PHE A N     1 
ATOM   3870  C  CA    . PHE A 1 1938 ? 193.453 191.635 206.442 1.00 1.11  ? 1938 PHE A CA    1 
ATOM   3871  C  C     . PHE A 1 1938 ? 192.703 192.731 205.691 1.00 0.87  ? 1938 PHE A C     1 
ATOM   3872  O  O     . PHE A 1 1938 ? 191.517 192.583 205.375 1.00 0.60  ? 1938 PHE A O     1 
ATOM   3873  C  CB    . PHE A 1 1938 ? 193.524 191.939 207.940 1.00 1.17  ? 1938 PHE A CB    1 
ATOM   3874  C  CG    . PHE A 1 1938 ? 192.203 192.292 208.557 1.00 0.83  ? 1938 PHE A CG    1 
ATOM   3875  C  CD1   . PHE A 1 1938 ? 191.330 191.304 208.969 1.00 0.62  ? 1938 PHE A CD1   1 
ATOM   3876  C  CD2   . PHE A 1 1938 ? 191.851 193.616 208.755 1.00 0.77  ? 1938 PHE A CD2   1 
ATOM   3877  C  CE1   . PHE A 1 1938 ? 190.121 191.627 209.547 1.00 0.71  ? 1938 PHE A CE1   1 
ATOM   3878  C  CE2   . PHE A 1 1938 ? 190.643 193.944 209.332 1.00 1.14  ? 1938 PHE A CE2   1 
ATOM   3879  C  CZ    . PHE A 1 1938 ? 189.777 192.947 209.727 1.00 0.73  ? 1938 PHE A CZ    1 
ATOM   3880  N  N     . GLN A 1 1939 ? 193.381 193.840 205.399 1.00 1.57  ? 1939 GLN A N     1 
ATOM   3881  C  CA    . GLN A 1 1939 ? 192.723 194.947 204.712 1.00 1.68  ? 1939 GLN A CA    1 
ATOM   3882  C  C     . GLN A 1 1939 ? 192.429 194.607 203.255 1.00 1.62  ? 1939 GLN A C     1 
ATOM   3883  O  O     . GLN A 1 1939 ? 191.386 194.997 202.722 1.00 1.37  ? 1939 GLN A O     1 
ATOM   3884  C  CB    . GLN A 1 1939 ? 193.580 196.206 204.816 1.00 2.99  ? 1939 GLN A CB    1 
ATOM   3885  C  CG    . GLN A 1 1939 ? 193.793 196.681 206.243 1.00 2.47  ? 1939 GLN A CG    1 
ATOM   3886  C  CD    . GLN A 1 1939 ? 194.673 197.910 206.327 1.00 12.51 ? 1939 GLN A CD    1 
ATOM   3887  O  OE1   . GLN A 1 1939 ? 194.339 198.964 205.788 1.00 17.23 ? 1939 GLN A OE1   1 
ATOM   3888  N  NE2   . GLN A 1 1939 ? 195.808 197.779 207.001 1.00 13.50 ? 1939 GLN A NE2   1 
ATOM   3889  N  N     . ALA A 1 1940 ? 193.341 193.891 202.592 1.00 1.22  ? 1940 ALA A N     1 
ATOM   3890  C  CA    . ALA A 1 1940 ? 193.128 193.534 201.194 1.00 0.76  ? 1940 ALA A CA    1 
ATOM   3891  C  C     . ALA A 1 1940 ? 192.001 192.519 201.051 1.00 0.53  ? 1940 ALA A C     1 
ATOM   3892  O  O     . ALA A 1 1940 ? 191.139 192.652 200.175 1.00 0.28  ? 1940 ALA A O     1 
ATOM   3893  C  CB    . ALA A 1 1940 ? 194.422 192.995 200.583 1.00 0.98  ? 1940 ALA A CB    1 
ATOM   3894  N  N     . MET A 1 1941 ? 191.988 191.495 201.909 1.00 0.72  ? 1941 MET A N     1 
ATOM   3895  C  CA    . MET A 1 1941 ? 190.936 190.486 201.852 1.00 0.64  ? 1941 MET A CA    1 
ATOM   3896  C  C     . MET A 1 1941 ? 189.570 191.094 202.130 1.00 0.58  ? 1941 MET A C     1 
ATOM   3897  O  O     . MET A 1 1941 ? 188.582 190.742 201.475 1.00 2.65  ? 1941 MET A O     1 
ATOM   3898  C  CB    . MET A 1 1941 ? 191.233 189.362 202.845 1.00 0.48  ? 1941 MET A CB    1 
ATOM   3899  C  CG    . MET A 1 1941 ? 192.409 188.482 202.459 1.00 0.94  ? 1941 MET A CG    1 
ATOM   3900  S  SD    . MET A 1 1941 ? 192.107 187.523 200.963 1.00 4.37  ? 1941 MET A SD    1 
ATOM   3901  C  CE    . MET A 1 1941 ? 190.745 186.490 201.493 1.00 0.55  ? 1941 MET A CE    1 
ATOM   3902  N  N     . GLY A 1 1942 ? 189.493 192.011 203.095 1.00 0.27  ? 1942 GLY A N     1 
ATOM   3903  C  CA    . GLY A 1 1942 ? 188.215 192.616 203.428 1.00 0.38  ? 1942 GLY A CA    1 
ATOM   3904  C  C     . GLY A 1 1942 ? 187.628 193.406 202.277 1.00 0.53  ? 1942 GLY A C     1 
ATOM   3905  O  O     . GLY A 1 1942 ? 186.428 193.332 202.005 1.00 0.82  ? 1942 GLY A O     1 
ATOM   3906  N  N     . ARG A 1 1943 ? 188.468 194.174 201.583 1.00 0.45  ? 1943 ARG A N     1 
ATOM   3907  C  CA    . ARG A 1 1943 ? 187.991 194.938 200.435 1.00 0.29  ? 1943 ARG A CA    1 
ATOM   3908  C  C     . ARG A 1 1943 ? 187.502 194.019 199.325 1.00 0.22  ? 1943 ARG A C     1 
ATOM   3909  O  O     . ARG A 1 1943 ? 186.505 194.313 198.659 1.00 0.49  ? 1943 ARG A O     1 
ATOM   3910  C  CB    . ARG A 1 1943 ? 189.096 195.868 199.932 1.00 0.78  ? 1943 ARG A CB    1 
ATOM   3911  C  CG    . ARG A 1 1943 ? 188.635 196.846 198.875 1.00 0.65  ? 1943 ARG A CG    1 
ATOM   3912  C  CD    . ARG A 1 1943 ? 189.642 197.966 198.684 1.00 2.98  ? 1943 ARG A CD    1 
ATOM   3913  N  NE    . ARG A 1 1943 ? 189.382 198.751 197.480 1.00 7.82  ? 1943 ARG A NE    1 
ATOM   3914  C  CZ    . ARG A 1 1943 ? 189.439 198.281 196.241 1.00 4.73  ? 1943 ARG A CZ    1 
ATOM   3915  N  NH1   . ARG A 1 1943 ? 189.803 197.035 195.988 1.00 1.92  ? 1943 ARG A NH1   1 
ATOM   3916  N  NH2   . ARG A 1 1943 ? 189.137 199.086 195.228 1.00 6.80  ? 1943 ARG A NH2   1 
ATOM   3917  N  N     . ILE A 1 1944 ? 188.196 192.901 199.109 1.00 0.16  ? 1944 ILE A N     1 
ATOM   3918  C  CA    . ILE A 1 1944 ? 187.734 191.912 198.138 1.00 0.18  ? 1944 ILE A CA    1 
ATOM   3919  C  C     . ILE A 1 1944 ? 186.391 191.334 198.568 1.00 0.21  ? 1944 ILE A C     1 
ATOM   3920  O  O     . ILE A 1 1944 ? 185.499 191.117 197.738 1.00 0.18  ? 1944 ILE A O     1 
ATOM   3921  C  CB    . ILE A 1 1944 ? 188.799 190.818 197.942 1.00 0.19  ? 1944 ILE A CB    1 
ATOM   3922  C  CG1   . ILE A 1 1944 ? 190.082 191.423 197.367 1.00 0.16  ? 1944 ILE A CG1   1 
ATOM   3923  C  CG2   . ILE A 1 1944 ? 188.276 189.703 197.055 1.00 0.09  ? 1944 ILE A CG2   1 
ATOM   3924  C  CD1   . ILE A 1 1944 ? 191.206 190.427 197.191 1.00 0.19  ? 1944 ILE A CD1   1 
ATOM   3925  N  N     . PHE A 1 1945 ? 186.224 191.080 199.868 1.00 0.21  ? 1945 PHE A N     1 
ATOM   3926  C  CA    . PHE A 1 1945 ? 184.944 190.592 200.367 1.00 0.19  ? 1945 PHE A CA    1 
ATOM   3927  C  C     . PHE A 1 1945 ? 183.838 191.617 200.150 1.00 0.17  ? 1945 PHE A C     1 
ATOM   3928  O  O     . PHE A 1 1945 ? 182.702 191.254 199.827 1.00 0.24  ? 1945 PHE A O     1 
ATOM   3929  C  CB    . PHE A 1 1945 ? 185.056 190.233 201.849 1.00 0.28  ? 1945 PHE A CB    1 
ATOM   3930  C  CG    . PHE A 1 1945 ? 185.824 188.973 202.111 1.00 0.18  ? 1945 PHE A CG    1 
ATOM   3931  C  CD1   . PHE A 1 1945 ? 185.728 187.896 201.246 1.00 0.12  ? 1945 PHE A CD1   1 
ATOM   3932  C  CD2   . PHE A 1 1945 ? 186.645 188.865 203.219 1.00 0.20  ? 1945 PHE A CD2   1 
ATOM   3933  C  CE1   . PHE A 1 1945 ? 186.437 186.736 201.484 1.00 0.08  ? 1945 PHE A CE1   1 
ATOM   3934  C  CE2   . PHE A 1 1945 ? 187.355 187.709 203.461 1.00 0.20  ? 1945 PHE A CE2   1 
ATOM   3935  C  CZ    . PHE A 1 1945 ? 187.251 186.641 202.591 1.00 0.12  ? 1945 PHE A CZ    1 
ATOM   3936  N  N     . VAL A 1 1946 ? 184.153 192.901 200.328 1.00 0.32  ? 1946 VAL A N     1 
ATOM   3937  C  CA    . VAL A 1 1946 ? 183.157 193.950 200.131 1.00 0.51  ? 1946 VAL A CA    1 
ATOM   3938  C  C     . VAL A 1 1946 ? 182.640 193.925 198.699 1.00 0.29  ? 1946 VAL A C     1 
ATOM   3939  O  O     . VAL A 1 1946 ? 181.432 194.004 198.454 1.00 0.95  ? 1946 VAL A O     1 
ATOM   3940  C  CB    . VAL A 1 1946 ? 183.750 195.326 200.498 1.00 0.39  ? 1946 VAL A CB    1 
ATOM   3941  C  CG1   . VAL A 1 1946 ? 182.823 196.445 200.060 1.00 0.18  ? 1946 VAL A CG1   1 
ATOM   3942  C  CG2   . VAL A 1 1946 ? 184.011 195.407 201.988 1.00 0.32  ? 1946 VAL A CG2   1 
ATOM   3943  N  N     . GLY A 1 1947 ? 183.551 193.804 197.732 1.00 0.21  ? 1947 GLY A N     1 
ATOM   3944  C  CA    . GLY A 1 1947 ? 183.127 193.684 196.348 1.00 0.23  ? 1947 GLY A CA    1 
ATOM   3945  C  C     . GLY A 1 1947 ? 182.331 192.420 196.086 1.00 0.32  ? 1947 GLY A C     1 
ATOM   3946  O  O     . GLY A 1 1947 ? 181.303 192.453 195.406 1.00 0.77  ? 1947 GLY A O     1 
ATOM   3947  N  N     . LEU A 1 1948 ? 182.793 191.289 196.624 1.00 0.16  ? 1948 LEU A N     1 
ATOM   3948  C  CA    . LEU A 1 1948 ? 182.082 190.030 196.424 1.00 0.33  ? 1948 LEU A CA    1 
ATOM   3949  C  C     . LEU A 1 1948 ? 180.692 190.070 197.046 1.00 0.42  ? 1948 LEU A C     1 
ATOM   3950  O  O     . LEU A 1 1948 ? 179.725 189.580 196.451 1.00 0.69  ? 1948 LEU A O     1 
ATOM   3951  C  CB    . LEU A 1 1948 ? 182.890 188.872 197.008 1.00 0.28  ? 1948 LEU A CB    1 
ATOM   3952  C  CG    . LEU A 1 1948 ? 184.152 188.414 196.277 1.00 0.21  ? 1948 LEU A CG    1 
ATOM   3953  C  CD1   . LEU A 1 1948 ? 184.948 187.470 197.164 1.00 0.05  ? 1948 LEU A CD1   1 
ATOM   3954  C  CD2   . LEU A 1 1948 ? 183.810 187.754 194.952 1.00 0.05  ? 1948 LEU A CD2   1 
ATOM   3955  N  N     . CYS A 1 1949 ? 180.573 190.643 198.246 1.00 0.28  ? 1949 CYS A N     1 
ATOM   3956  C  CA    . CYS A 1 1949 ? 179.293 190.643 198.948 1.00 0.60  ? 1949 CYS A CA    1 
ATOM   3957  C  C     . CYS A 1 1949 ? 178.246 191.476 198.218 1.00 0.83  ? 1949 CYS A C     1 
ATOM   3958  O  O     . CYS A 1 1949 ? 177.094 191.050 198.085 1.00 1.32  ? 1949 CYS A O     1 
ATOM   3959  C  CB    . CYS A 1 1949 ? 179.478 191.147 200.379 1.00 0.99  ? 1949 CYS A CB    1 
ATOM   3960  S  SG    . CYS A 1 1949 ? 180.240 189.951 201.495 1.00 0.74  ? 1949 CYS A SG    1 
ATOM   3961  N  N     . GLN A 1 1950 ? 178.620 192.664 197.746 1.00 1.14  ? 1950 GLN A N     1 
ATOM   3962  C  CA    . GLN A 1 1950 ? 177.640 193.533 197.102 1.00 1.75  ? 1950 GLN A CA    1 
ATOM   3963  C  C     . GLN A 1 1950 ? 177.286 193.042 195.705 1.00 1.44  ? 1950 GLN A C     1 
ATOM   3964  O  O     . GLN A 1 1950 ? 176.124 193.123 195.289 1.00 4.63  ? 1950 GLN A O     1 
ATOM   3965  C  CB    . GLN A 1 1950 ? 178.156 194.967 197.052 1.00 2.93  ? 1950 GLN A CB    1 
ATOM   3966  C  CG    . GLN A 1 1950 ? 178.508 195.550 198.400 1.00 2.78  ? 1950 GLN A CG    1 
ATOM   3967  C  CD    . GLN A 1 1950 ? 178.771 197.035 198.332 1.00 4.90  ? 1950 GLN A CD    1 
ATOM   3968  O  OE1   . GLN A 1 1950 ? 177.860 197.825 198.092 1.00 14.99 ? 1950 GLN A OE1   1 
ATOM   3969  N  NE2   . GLN A 1 1950 ? 180.022 197.425 198.534 1.00 5.68  ? 1950 GLN A NE2   1 
ATOM   3970  N  N     . VAL A 1 1951 ? 178.272 192.539 194.963 1.00 1.14  ? 1951 VAL A N     1 
ATOM   3971  C  CA    . VAL A 1 1951 ? 178.003 192.021 193.625 1.00 0.69  ? 1951 VAL A CA    1 
ATOM   3972  C  C     . VAL A 1 1951 ? 177.169 190.749 193.702 1.00 0.51  ? 1951 VAL A C     1 
ATOM   3973  O  O     . VAL A 1 1951 ? 176.279 190.521 192.875 1.00 1.32  ? 1951 VAL A O     1 
ATOM   3974  C  CB    . VAL A 1 1951 ? 179.325 191.792 192.865 1.00 1.03  ? 1951 VAL A CB    1 
ATOM   3975  C  CG1   . VAL A 1 1951 ? 179.091 190.977 191.604 1.00 0.46  ? 1951 VAL A CG1   1 
ATOM   3976  C  CG2   . VAL A 1 1951 ? 179.974 193.121 192.525 1.00 0.62  ? 1951 VAL A CG2   1 
ATOM   3977  N  N     . GLY A 1 1952 ? 177.423 189.915 194.705 1.00 1.01  ? 1952 GLY A N     1 
ATOM   3978  C  CA    . GLY A 1 1952 ? 176.844 188.591 194.739 1.00 0.64  ? 1952 GLY A CA    1 
ATOM   3979  C  C     . GLY A 1 1952 ? 177.683 187.554 194.040 1.00 0.28  ? 1952 GLY A C     1 
ATOM   3980  O  O     . GLY A 1 1952 ? 177.145 186.554 193.554 1.00 3.14  ? 1952 GLY A O     1 
ATOM   3981  N  N     . ALA A 1 1953 ? 178.988 187.766 193.965 1.00 0.26  ? 1953 ALA A N     1 
ATOM   3982  C  CA    . ALA A 1 1953 ? 179.896 186.913 193.218 1.00 0.32  ? 1953 ALA A CA    1 
ATOM   3983  C  C     . ALA A 1 1953 ? 180.592 185.922 194.142 1.00 0.09  ? 1953 ALA A C     1 
ATOM   3984  O  O     . ALA A 1 1953 ? 180.713 186.135 195.349 1.00 0.30  ? 1953 ALA A O     1 
ATOM   3985  C  CB    . ALA A 1 1953 ? 180.929 187.761 192.476 1.00 0.19  ? 1953 ALA A CB    1 
ATOM   3986  N  N     . TRP A 1 1954 ? 181.045 184.824 193.550 1.00 0.07  ? 1954 TRP A N     1 
ATOM   3987  C  CA    . TRP A 1 1954 ? 181.787 183.799 194.269 1.00 0.03  ? 1954 TRP A CA    1 
ATOM   3988  C  C     . TRP A 1 1954 ? 183.269 184.146 194.270 1.00 0.03  ? 1954 TRP A C     1 
ATOM   3989  O  O     . TRP A 1 1954 ? 183.828 184.507 193.231 1.00 0.04  ? 1954 TRP A O     1 
ATOM   3990  C  CB    . TRP A 1 1954 ? 181.573 182.426 193.632 1.00 0.04  ? 1954 TRP A CB    1 
ATOM   3991  C  CG    . TRP A 1 1954 ? 180.265 181.783 193.959 1.00 0.06  ? 1954 TRP A CG    1 
ATOM   3992  C  CD1   . TRP A 1 1954 ? 179.137 182.401 194.400 1.00 0.03  ? 1954 TRP A CD1   1 
ATOM   3993  C  CD2   . TRP A 1 1954 ? 179.947 180.394 193.851 1.00 0.05  ? 1954 TRP A CD2   1 
ATOM   3994  N  NE1   . TRP A 1 1954 ? 178.137 181.482 194.581 1.00 0.01  ? 1954 TRP A NE1   1 
ATOM   3995  C  CE2   . TRP A 1 1954 ? 178.609 180.242 194.249 1.00 0.02  ? 1954 TRP A CE2   1 
ATOM   3996  C  CE3   . TRP A 1 1954 ? 180.667 179.263 193.455 1.00 0.00  ? 1954 TRP A CE3   1 
ATOM   3997  C  CZ2   . TRP A 1 1954 ? 177.974 179.005 194.268 1.00 0.02  ? 1954 TRP A CZ2   1 
ATOM   3998  C  CZ3   . TRP A 1 1954 ? 180.036 178.039 193.473 1.00 0.02  ? 1954 TRP A CZ3   1 
ATOM   3999  C  CH2   . TRP A 1 1954 ? 178.703 177.919 193.874 1.00 0.02  ? 1954 TRP A CH2   1 
ATOM   4000  N  N     . GLY A 1 1955 ? 183.896 184.036 195.433 1.00 0.03  ? 1955 GLY A N     1 
ATOM   4001  C  CA    . GLY A 1 1955 ? 185.327 184.213 195.530 1.00 0.03  ? 1955 GLY A CA    1 
ATOM   4002  C  C     . GLY A 1 1955 ? 186.052 182.898 195.707 1.00 0.05  ? 1955 GLY A C     1 
ATOM   4003  O  O     . GLY A 1 1955 ? 185.907 182.236 196.739 1.00 0.03  ? 1955 GLY A O     1 
ATOM   4004  N  N     . CYS A 1 1956 ? 186.820 182.495 194.700 1.00 0.03  ? 1956 CYS A N     1 
ATOM   4005  C  CA    . CYS A 1 1956 ? 187.642 181.293 194.772 1.00 0.02  ? 1956 CYS A CA    1 
ATOM   4006  C  C     . CYS A 1 1956 ? 189.073 181.736 195.051 1.00 0.05  ? 1956 CYS A C     1 
ATOM   4007  O  O     . CYS A 1 1956 ? 189.779 182.199 194.153 1.00 0.25  ? 1956 CYS A O     1 
ATOM   4008  C  CB    . CYS A 1 1956 ? 187.540 180.479 193.485 1.00 0.08  ? 1956 CYS A CB    1 
ATOM   4009  S  SG    . CYS A 1 1956 ? 188.590 179.008 193.452 1.00 2.56  ? 1956 CYS A SG    1 
ATOM   4010  N  N     . PHE A 1 1957 ? 189.483 181.603 196.312 1.00 0.05  ? 1957 PHE A N     1 
ATOM   4011  C  CA    . PHE A 1 1957 ? 190.850 182.004 196.733 1.00 0.17  ? 1957 PHE A CA    1 
ATOM   4012  C  C     . PHE A 1 1957 ? 191.779 180.797 196.657 1.00 0.26  ? 1957 PHE A C     1 
ATOM   4013  O  O     . PHE A 1 1957 ? 191.807 179.981 197.596 1.00 0.40  ? 1957 PHE A O     1 
ATOM   4014  C  CB    . PHE A 1 1957 ? 190.725 182.618 198.131 1.00 0.09  ? 1957 PHE A CB    1 
ATOM   4015  C  CG    . PHE A 1 1957 ? 189.869 183.875 198.172 1.00 0.03  ? 1957 PHE A CG    1 
ATOM   4016  C  CD1   . PHE A 1 1957 ? 188.493 183.795 198.343 1.00 0.02  ? 1957 PHE A CD1   1 
ATOM   4017  C  CD2   . PHE A 1 1957 ? 190.445 185.133 198.034 1.00 0.04  ? 1957 PHE A CD2   1 
ATOM   4018  C  CE1   . PHE A 1 1957 ? 187.716 184.940 198.377 1.00 0.02  ? 1957 PHE A CE1   1 
ATOM   4019  C  CE2   . PHE A 1 1957 ? 189.662 186.276 198.069 1.00 0.04  ? 1957 PHE A CE2   1 
ATOM   4020  C  CZ    . PHE A 1 1957 ? 188.302 186.176 198.242 1.00 0.04  ? 1957 PHE A CZ    1 
ATOM   4021  N  N     . ASP A 1 1958 ? 192.543 180.699 195.567 1.00 0.76  ? 1958 ASP A N     1 
ATOM   4022  C  CA    . ASP A 1 1958 ? 193.483 179.564 195.369 1.00 0.59  ? 1958 ASP A CA    1 
ATOM   4023  C  C     . ASP A 1 1958 ? 194.782 179.827 196.137 1.00 1.43  ? 1958 ASP A C     1 
ATOM   4024  O  O     . ASP A 1 1958 ? 195.069 181.007 196.419 1.00 1.92  ? 1958 ASP A O     1 
ATOM   4025  C  CB    . ASP A 1 1958 ? 193.701 179.313 193.886 1.00 1.44  ? 1958 ASP A CB    1 
ATOM   4026  C  CG    . ASP A 1 1958 ? 192.429 179.100 193.079 1.00 4.14  ? 1958 ASP A CG    1 
ATOM   4027  O  OD1   . ASP A 1 1958 ? 191.671 178.168 193.415 1.00 5.32  ? 1958 ASP A OD1   1 
ATOM   4028  O  OD2   . ASP A 1 1958 ? 192.204 179.870 192.125 1.00 8.53  ? 1958 ASP A OD2   1 
ATOM   4029  N  N     . GLU A 1 1959 ? 195.534 178.768 196.455 1.00 2.33  ? 1959 GLU A N     1 
ATOM   4030  C  CA    . GLU A 1 1959 ? 196.781 178.919 197.252 1.00 1.70  ? 1959 GLU A CA    1 
ATOM   4031  C  C     . GLU A 1 1959 ? 196.455 179.787 198.476 1.00 1.12  ? 1959 GLU A C     1 
ATOM   4032  O  O     . GLU A 1 1959 ? 197.276 180.663 198.817 1.00 1.35  ? 1959 GLU A O     1 
ATOM   4033  C  CB    . GLU A 1 1959 ? 197.899 179.469 196.366 1.00 1.90  ? 1959 GLU A CB    1 
ATOM   4034  C  CG    . GLU A 1 1959 ? 198.234 178.549 195.196 1.00 6.64  ? 1959 GLU A CG    1 
ATOM   4035  C  CD    . GLU A 1 1959 ? 197.472 178.834 193.914 1.00 13.61 ? 1959 GLU A CD    1 
ATOM   4036  O  OE1   . GLU A 1 1959 ? 196.779 179.871 193.848 1.00 15.15 ? 1959 GLU A OE1   1 
ATOM   4037  O  OE2   . GLU A 1 1959 ? 197.557 178.002 192.986 1.00 17.15 ? 1959 GLU A OE2   1 
ATOM   4038  N  N     . PHE A 1 1960 ? 195.305 179.542 199.109 1.00 0.92  ? 1960 PHE A N     1 
ATOM   4039  C  CA    . PHE A 1 1960 ? 194.861 180.349 200.239 1.00 0.53  ? 1960 PHE A CA    1 
ATOM   4040  C  C     . PHE A 1 1960 ? 195.772 180.189 201.449 1.00 0.92  ? 1960 PHE A C     1 
ATOM   4041  O  O     . PHE A 1 1960 ? 195.846 181.093 202.289 1.00 0.71  ? 1960 PHE A O     1 
ATOM   4042  C  CB    . PHE A 1 1960 ? 193.417 179.982 200.580 1.00 0.29  ? 1960 PHE A CB    1 
ATOM   4043  C  CG    . PHE A 1 1960 ? 192.835 180.757 201.722 1.00 0.22  ? 1960 PHE A CG    1 
ATOM   4044  C  CD1   . PHE A 1 1960 ? 192.398 182.056 201.544 1.00 0.16  ? 1960 PHE A CD1   1 
ATOM   4045  C  CD2   . PHE A 1 1960 ? 192.667 180.163 202.961 1.00 0.14  ? 1960 PHE A CD2   1 
ATOM   4046  C  CE1   . PHE A 1 1960 ? 191.846 182.762 202.586 1.00 0.08  ? 1960 PHE A CE1   1 
ATOM   4047  C  CE2   . PHE A 1 1960 ? 192.108 180.866 204.005 1.00 0.19  ? 1960 PHE A CE2   1 
ATOM   4048  C  CZ    . PHE A 1 1960 ? 191.699 182.167 203.817 1.00 0.11  ? 1960 PHE A CZ    1 
ATOM   4049  N  N     . ASN A 1 1961 ? 196.485 179.068 201.548 1.00 1.41  ? 1961 ASN A N     1 
ATOM   4050  C  CA    . ASN A 1 1961 ? 197.426 178.866 202.641 1.00 0.73  ? 1961 ASN A CA    1 
ATOM   4051  C  C     . ASN A 1 1961 ? 198.770 179.536 202.394 1.00 0.67  ? 1961 ASN A C     1 
ATOM   4052  O  O     . ASN A 1 1961 ? 199.704 179.318 203.171 1.00 1.22  ? 1961 ASN A O     1 
ATOM   4053  C  CB    . ASN A 1 1961 ? 197.626 177.371 202.909 1.00 1.83  ? 1961 ASN A CB    1 
ATOM   4054  C  CG    . ASN A 1 1961 ? 198.051 176.600 201.674 1.00 3.10  ? 1961 ASN A CG    1 
ATOM   4055  O  OD1   . ASN A 1 1961 ? 198.152 177.153 200.581 1.00 3.73  ? 1961 ASN A OD1   1 
ATOM   4056  N  ND2   . ASN A 1 1961 ? 198.315 175.313 201.850 1.00 4.09  ? 1961 ASN A ND2   1 
ATOM   4057  N  N     . ARG A 1 1962 ? 198.900 180.324 201.327 1.00 1.53  ? 1962 ARG A N     1 
ATOM   4058  C  CA    . ARG A 1 1962 ? 200.089 181.146 201.147 1.00 1.42  ? 1962 ARG A CA    1 
ATOM   4059  C  C     . ARG A 1 1962 ? 200.005 182.456 201.917 1.00 1.11  ? 1962 ARG A C     1 
ATOM   4060  O  O     . ARG A 1 1962 ? 201.008 183.172 202.003 1.00 2.11  ? 1962 ARG A O     1 
ATOM   4061  C  CB    . ARG A 1 1962 ? 200.323 181.413 199.656 1.00 1.05  ? 1962 ARG A CB    1 
ATOM   4062  C  CG    . ARG A 1 1962 ? 200.601 180.138 198.871 1.00 2.36  ? 1962 ARG A CG    1 
ATOM   4063  C  CD    . ARG A 1 1962 ? 201.566 180.323 197.707 1.00 2.73  ? 1962 ARG A CD    1 
ATOM   4064  N  NE    . ARG A 1 1962 ? 201.135 181.334 196.750 1.00 2.07  ? 1962 ARG A NE    1 
ATOM   4065  C  CZ    . ARG A 1 1962 ? 201.877 182.361 196.359 1.00 1.25  ? 1962 ARG A CZ    1 
ATOM   4066  N  NH1   . ARG A 1 1962 ? 203.110 182.530 196.806 1.00 1.16  ? 1962 ARG A NH1   1 
ATOM   4067  N  NH2   . ARG A 1 1962 ? 201.374 183.231 195.490 1.00 1.68  ? 1962 ARG A NH2   1 
ATOM   4068  N  N     . LEU A 1 1963 ? 198.844 182.779 202.481 1.00 1.04  ? 1963 LEU A N     1 
ATOM   4069  C  CA    . LEU A 1 1963 ? 198.736 183.892 203.411 1.00 0.79  ? 1963 LEU A CA    1 
ATOM   4070  C  C     . LEU A 1 1963 ? 199.516 183.592 204.684 1.00 1.58  ? 1963 LEU A C     1 
ATOM   4071  O  O     . LEU A 1 1963 ? 199.727 182.435 205.049 1.00 1.90  ? 1963 LEU A O     1 
ATOM   4072  C  CB    . LEU A 1 1963 ? 197.274 184.161 203.768 1.00 0.90  ? 1963 LEU A CB    1 
ATOM   4073  C  CG    . LEU A 1 1963 ? 196.427 185.102 202.911 1.00 0.94  ? 1963 LEU A CG    1 
ATOM   4074  C  CD1   . LEU A 1 1963 ? 196.238 184.560 201.512 1.00 1.10  ? 1963 LEU A CD1   1 
ATOM   4075  C  CD2   . LEU A 1 1963 ? 195.086 185.346 203.578 1.00 0.43  ? 1963 LEU A CD2   1 
ATOM   4076  N  N     . GLU A 1 1964 ? 199.951 184.650 205.359 1.00 3.93  ? 1964 GLU A N     1 
ATOM   4077  C  CA    . GLU A 1 1964 ? 200.584 184.474 206.657 1.00 3.14  ? 1964 GLU A CA    1 
ATOM   4078  C  C     . GLU A 1 1964 ? 199.573 183.957 207.674 1.00 1.54  ? 1964 GLU A C     1 
ATOM   4079  O  O     . GLU A 1 1964 ? 198.368 184.199 207.564 1.00 1.90  ? 1964 GLU A O     1 
ATOM   4080  C  CB    . GLU A 1 1964 ? 201.201 185.789 207.132 1.00 3.99  ? 1964 GLU A CB    1 
ATOM   4081  C  CG    . GLU A 1 1964 ? 202.360 186.258 206.276 1.00 4.24  ? 1964 GLU A CG    1 
ATOM   4082  C  CD    . GLU A 1 1964 ? 203.556 185.326 206.372 1.00 19.53 ? 1964 GLU A CD    1 
ATOM   4083  O  OE1   . GLU A 1 1964 ? 203.756 184.726 207.449 1.00 20.69 ? 1964 GLU A OE1   1 
ATOM   4084  O  OE2   . GLU A 1 1964 ? 204.293 185.193 205.375 1.00 21.24 ? 1964 GLU A OE2   1 
ATOM   4085  N  N     . GLU A 1 1965 ? 200.075 183.223 208.670 1.00 1.82  ? 1965 GLU A N     1 
ATOM   4086  C  CA    . GLU A 1 1965 ? 199.190 182.632 209.669 1.00 1.11  ? 1965 GLU A CA    1 
ATOM   4087  C  C     . GLU A 1 1965 ? 198.443 183.703 210.453 1.00 0.94  ? 1965 GLU A C     1 
ATOM   4088  O  O     . GLU A 1 1965 ? 197.261 183.534 210.775 1.00 1.12  ? 1965 GLU A O     1 
ATOM   4089  C  CB    . GLU A 1 1965 ? 199.980 181.728 210.614 1.00 1.75  ? 1965 GLU A CB    1 
ATOM   4090  C  CG    . GLU A 1 1965 ? 200.566 180.503 209.945 1.00 5.18  ? 1965 GLU A CG    1 
ATOM   4091  C  CD    . GLU A 1 1965 ? 200.961 179.423 210.932 1.00 15.33 ? 1965 GLU A CD    1 
ATOM   4092  O  OE1   . GLU A 1 1965 ? 201.396 178.341 210.484 1.00 7.57  ? 1965 GLU A OE1   1 
ATOM   4093  O  OE2   . GLU A 1 1965 ? 200.835 179.654 212.152 1.00 21.70 ? 1965 GLU A OE2   1 
ATOM   4094  N  N     . ARG A 1 1966 ? 199.112 184.815 210.772 1.00 0.99  ? 1966 ARG A N     1 
ATOM   4095  C  CA    . ARG A 1 1966 ? 198.429 185.904 211.461 1.00 1.26  ? 1966 ARG A CA    1 
ATOM   4096  C  C     . ARG A 1 1966 ? 197.311 186.493 210.610 1.00 1.08  ? 1966 ARG A C     1 
ATOM   4097  O  O     . ARG A 1 1966 ? 196.264 186.876 211.144 1.00 0.81  ? 1966 ARG A O     1 
ATOM   4098  C  CB    . ARG A 1 1966 ? 199.431 186.987 211.869 1.00 3.39  ? 1966 ARG A CB    1 
ATOM   4099  C  CG    . ARG A 1 1966 ? 200.133 187.699 210.720 1.00 2.10  ? 1966 ARG A CG    1 
ATOM   4100  C  CD    . ARG A 1 1966 ? 201.319 188.508 211.224 1.00 5.63  ? 1966 ARG A CD    1 
ATOM   4101  N  NE    . ARG A 1 1966 ? 201.868 189.391 210.201 1.00 6.89  ? 1966 ARG A NE    1 
ATOM   4102  C  CZ    . ARG A 1 1966 ? 201.622 190.692 210.123 1.00 8.93  ? 1966 ARG A CZ    1 
ATOM   4103  N  NH1   . ARG A 1 1966 ? 200.832 191.299 210.993 1.00 7.37  ? 1966 ARG A NH1   1 
ATOM   4104  N  NH2   . ARG A 1 1966 ? 202.178 191.399 209.145 1.00 23.47 ? 1966 ARG A NH2   1 
ATOM   4105  N  N     . MET A 1 1967 ? 197.502 186.560 209.292 1.00 2.25  ? 1967 MET A N     1 
ATOM   4106  C  CA    . MET A 1 1967 ? 196.452 187.082 208.424 1.00 1.16  ? 1967 MET A CA    1 
ATOM   4107  C  C     . MET A 1 1967 ? 195.289 186.106 208.295 1.00 0.46  ? 1967 MET A C     1 
ATOM   4108  O  O     . MET A 1 1967 ? 194.136 186.533 208.183 1.00 0.30  ? 1967 MET A O     1 
ATOM   4109  C  CB    . MET A 1 1967 ? 197.026 187.416 207.048 1.00 0.95  ? 1967 MET A CB    1 
ATOM   4110  C  CG    . MET A 1 1967 ? 197.759 188.739 206.998 1.00 1.19  ? 1967 MET A CG    1 
ATOM   4111  S  SD    . MET A 1 1967 ? 196.985 190.003 208.024 1.00 8.49  ? 1967 MET A SD    1 
ATOM   4112  C  CE    . MET A 1 1967 ? 198.327 191.173 208.185 1.00 2.70  ? 1967 MET A CE    1 
ATOM   4113  N  N     . LEU A 1 1968 ? 195.569 184.802 208.310 1.00 0.87  ? 1968 LEU A N     1 
ATOM   4114  C  CA    . LEU A 1 1968 ? 194.498 183.814 208.245 1.00 0.64  ? 1968 LEU A CA    1 
ATOM   4115  C  C     . LEU A 1 1968 ? 193.580 183.917 209.454 1.00 0.55  ? 1968 LEU A C     1 
ATOM   4116  O  O     . LEU A 1 1968 ? 192.354 183.830 209.321 1.00 0.53  ? 1968 LEU A O     1 
ATOM   4117  C  CB    . LEU A 1 1968 ? 195.084 182.407 208.132 1.00 0.73  ? 1968 LEU A CB    1 
ATOM   4118  C  CG    . LEU A 1 1968 ? 195.854 182.115 206.846 1.00 0.85  ? 1968 LEU A CG    1 
ATOM   4119  C  CD1   . LEU A 1 1968 ? 196.642 180.823 206.972 1.00 1.58  ? 1968 LEU A CD1   1 
ATOM   4120  C  CD2   . LEU A 1 1968 ? 194.911 182.063 205.657 1.00 0.47  ? 1968 LEU A CD2   1 
ATOM   4121  N  N     . SER A 1 1969 ? 194.156 184.100 210.645 1.00 0.67  ? 1969 SER A N     1 
ATOM   4122  C  CA    . SER A 1 1969 ? 193.343 184.284 211.841 1.00 0.56  ? 1969 SER A CA    1 
ATOM   4123  C  C     . SER A 1 1969 ? 192.487 185.539 211.736 1.00 0.61  ? 1969 SER A C     1 
ATOM   4124  O  O     . SER A 1 1969 ? 191.288 185.509 212.034 1.00 1.29  ? 1969 SER A O     1 
ATOM   4125  C  CB    . SER A 1 1969 ? 194.239 184.345 213.077 1.00 0.49  ? 1969 SER A CB    1 
ATOM   4126  O  OG    . SER A 1 1969 ? 193.525 184.802 214.210 1.00 2.22  ? 1969 SER A OG    1 
ATOM   4127  N  N     . ALA A 1 1970 ? 193.084 186.647 211.291 1.00 0.83  ? 1970 ALA A N     1 
ATOM   4128  C  CA    . ALA A 1 1970 ? 192.344 187.899 211.177 1.00 0.95  ? 1970 ALA A CA    1 
ATOM   4129  C  C     . ALA A 1 1970 ? 191.213 187.789 210.160 1.00 0.52  ? 1970 ALA A C     1 
ATOM   4130  O  O     . ALA A 1 1970 ? 190.111 188.300 210.389 1.00 1.09  ? 1970 ALA A O     1 
ATOM   4131  C  CB    . ALA A 1 1970 ? 193.295 189.031 210.800 1.00 0.91  ? 1970 ALA A CB    1 
ATOM   4132  N  N     . VAL A 1 1971 ? 191.472 187.129 209.030 1.00 0.33  ? 1971 VAL A N     1 
ATOM   4133  C  CA    . VAL A 1 1971 ? 190.464 187.008 207.982 1.00 0.74  ? 1971 VAL A CA    1 
ATOM   4134  C  C     . VAL A 1 1971 ? 189.278 186.177 208.460 1.00 0.50  ? 1971 VAL A C     1 
ATOM   4135  O  O     . VAL A 1 1971 ? 188.138 186.409 208.039 1.00 0.41  ? 1971 VAL A O     1 
ATOM   4136  C  CB    . VAL A 1 1971 ? 191.111 186.432 206.706 1.00 0.38  ? 1971 VAL A CB    1 
ATOM   4137  C  CG1   . VAL A 1 1971 ? 190.071 185.828 205.774 1.00 0.39  ? 1971 VAL A CG1   1 
ATOM   4138  C  CG2   . VAL A 1 1971 ? 191.891 187.516 205.987 1.00 0.31  ? 1971 VAL A CG2   1 
ATOM   4139  N  N     . SER A 1 1972 ? 189.517 185.222 209.365 1.00 0.41  ? 1972 SER A N     1 
ATOM   4140  C  CA    . SER A 1 1972 ? 188.441 184.374 209.872 1.00 0.61  ? 1972 SER A CA    1 
ATOM   4141  C  C     . SER A 1 1972 ? 187.306 185.190 210.481 1.00 0.85  ? 1972 SER A C     1 
ATOM   4142  O  O     . SER A 1 1972 ? 186.148 184.763 210.438 1.00 0.69  ? 1972 SER A O     1 
ATOM   4143  C  CB    . SER A 1 1972 ? 188.997 183.390 210.900 1.00 0.46  ? 1972 SER A CB    1 
ATOM   4144  O  OG    . SER A 1 1972 ? 189.489 184.069 212.040 1.00 0.58  ? 1972 SER A OG    1 
ATOM   4145  N  N     . GLN A 1 1973 ? 187.615 186.354 211.054 1.00 2.07  ? 1973 GLN A N     1 
ATOM   4146  C  CA    . GLN A 1 1973 ? 186.561 187.214 211.581 1.00 1.39  ? 1973 GLN A CA    1 
ATOM   4147  C  C     . GLN A 1 1973 ? 185.665 187.741 210.465 1.00 1.71  ? 1973 GLN A C     1 
ATOM   4148  O  O     . GLN A 1 1973 ? 184.437 187.762 210.606 1.00 1.23  ? 1973 GLN A O     1 
ATOM   4149  C  CB    . GLN A 1 1973 ? 187.177 188.366 212.374 1.00 1.77  ? 1973 GLN A CB    1 
ATOM   4150  C  CG    . GLN A 1 1973 ? 186.209 189.067 213.314 1.00 5.21  ? 1973 GLN A CG    1 
ATOM   4151  C  CD    . GLN A 1 1973 ? 185.357 190.103 212.611 1.00 13.53 ? 1973 GLN A CD    1 
ATOM   4152  O  OE1   . GLN A 1 1973 ? 185.874 191.053 212.025 1.00 16.89 ? 1973 GLN A OE1   1 
ATOM   4153  N  NE2   . GLN A 1 1973 ? 184.041 189.927 212.668 1.00 13.25 ? 1973 GLN A NE2   1 
ATOM   4154  N  N     . GLN A 1 1974 ? 186.260 188.173 209.351 1.00 3.26  ? 1974 GLN A N     1 
ATOM   4155  C  CA    . GLN A 1 1974 ? 185.461 188.673 208.236 1.00 0.79  ? 1974 GLN A CA    1 
ATOM   4156  C  C     . GLN A 1 1974 ? 184.638 187.559 207.603 1.00 0.68  ? 1974 GLN A C     1 
ATOM   4157  O  O     . GLN A 1 1974 ? 183.474 187.770 207.241 1.00 1.35  ? 1974 GLN A O     1 
ATOM   4158  C  CB    . GLN A 1 1974 ? 186.364 189.330 207.193 1.00 0.65  ? 1974 GLN A CB    1 
ATOM   4159  C  CG    . GLN A 1 1974 ? 187.408 190.254 207.784 1.00 0.95  ? 1974 GLN A CG    1 
ATOM   4160  C  CD    . GLN A 1 1974 ? 188.290 190.893 206.731 1.00 0.56  ? 1974 GLN A CD    1 
ATOM   4161  O  OE1   . GLN A 1 1974 ? 188.416 192.115 206.671 1.00 0.90  ? 1974 GLN A OE1   1 
ATOM   4162  N  NE2   . GLN A 1 1974 ? 188.908 190.069 205.899 1.00 0.74  ? 1974 GLN A NE2   1 
ATOM   4163  N  N     . VAL A 1 1975 ? 185.223 186.370 207.453 1.00 1.01  ? 1975 VAL A N     1 
ATOM   4164  C  CA    . VAL A 1 1975 ? 184.490 185.252 206.868 1.00 0.78  ? 1975 VAL A CA    1 
ATOM   4165  C  C     . VAL A 1 1975 ? 183.299 184.889 207.742 1.00 1.13  ? 1975 VAL A C     1 
ATOM   4166  O  O     . VAL A 1 1975 ? 182.210 184.584 207.241 1.00 1.64  ? 1975 VAL A O     1 
ATOM   4167  C  CB    . VAL A 1 1975 ? 185.427 184.049 206.654 1.00 0.57  ? 1975 VAL A CB    1 
ATOM   4168  C  CG1   . VAL A 1 1975 ? 184.636 182.817 206.226 1.00 0.38  ? 1975 VAL A CG1   1 
ATOM   4169  C  CG2   . VAL A 1 1975 ? 186.495 184.384 205.627 1.00 0.17  ? 1975 VAL A CG2   1 
ATOM   4170  N  N     . GLN A 1 1976 ? 183.483 184.931 209.062 1.00 1.11  ? 1976 GLN A N     1 
ATOM   4171  C  CA    . GLN A 1 1976 ? 182.404 184.568 209.972 1.00 0.95  ? 1976 GLN A CA    1 
ATOM   4172  C  C     . GLN A 1 1976 ? 181.240 185.550 209.892 1.00 2.25  ? 1976 GLN A C     1 
ATOM   4173  O  O     . GLN A 1 1976 ? 180.077 185.134 209.830 1.00 5.66  ? 1976 GLN A O     1 
ATOM   4174  C  CB    . GLN A 1 1976 ? 182.935 184.474 211.399 1.00 2.48  ? 1976 GLN A CB    1 
ATOM   4175  C  CG    . GLN A 1 1976 ? 182.053 183.664 212.328 1.00 6.04  ? 1976 GLN A CG    1 
ATOM   4176  C  CD    . GLN A 1 1976 ? 182.730 183.354 213.645 1.00 9.92  ? 1976 GLN A CD    1 
ATOM   4177  O  OE1   . GLN A 1 1976 ? 182.967 182.192 213.976 1.00 14.40 ? 1976 GLN A OE1   1 
ATOM   4178  N  NE2   . GLN A 1 1976 ? 183.055 184.395 214.402 1.00 9.01  ? 1976 GLN A NE2   1 
ATOM   4179  N  N     . CYS A 1 1977 ? 181.525 186.855 209.882 1.00 2.64  ? 1977 CYS A N     1 
ATOM   4180  C  CA    . CYS A 1 1977 ? 180.439 187.834 209.913 1.00 2.24  ? 1977 CYS A CA    1 
ATOM   4181  C  C     . CYS A 1 1977 ? 179.624 187.795 208.626 1.00 2.34  ? 1977 CYS A C     1 
ATOM   4182  O  O     . CYS A 1 1977 ? 178.405 188.001 208.650 1.00 4.43  ? 1977 CYS A O     1 
ATOM   4183  C  CB    . CYS A 1 1977 ? 180.984 189.242 210.165 1.00 2.19  ? 1977 CYS A CB    1 
ATOM   4184  S  SG    . CYS A 1 1977 ? 182.051 189.916 208.880 1.00 32.26 ? 1977 CYS A SG    1 
ATOM   4185  N  N     . ILE A 1 1978 ? 180.277 187.534 207.492 1.00 1.44  ? 1978 ILE A N     1 
ATOM   4186  C  CA    . ILE A 1 1978 ? 179.546 187.355 206.242 1.00 1.78  ? 1978 ILE A CA    1 
ATOM   4187  C  C     . ILE A 1 1978 ? 178.635 186.138 206.331 1.00 1.89  ? 1978 ILE A C     1 
ATOM   4188  O  O     . ILE A 1 1978 ? 177.478 186.176 205.900 1.00 2.66  ? 1978 ILE A O     1 
ATOM   4189  C  CB    . ILE A 1 1978 ? 180.523 187.247 205.055 1.00 2.64  ? 1978 ILE A CB    1 
ATOM   4190  C  CG1   . ILE A 1 1978 ? 181.260 188.571 204.839 1.00 0.59  ? 1978 ILE A CG1   1 
ATOM   4191  C  CG2   . ILE A 1 1978 ? 179.794 186.820 203.791 1.00 1.17  ? 1978 ILE A CG2   1 
ATOM   4192  C  CD1   . ILE A 1 1978 ? 182.621 188.411 204.207 1.00 0.55  ? 1978 ILE A CD1   1 
ATOM   4193  N  N     . GLN A 1 1979 ? 179.142 185.044 206.902 1.00 2.08  ? 1979 GLN A N     1 
ATOM   4194  C  CA    . GLN A 1 1979 ? 178.359 183.817 206.987 1.00 2.23  ? 1979 GLN A CA    1 
ATOM   4195  C  C     . GLN A 1 1979 ? 177.137 183.995 207.882 1.00 3.88  ? 1979 GLN A C     1 
ATOM   4196  O  O     . GLN A 1 1979 ? 176.069 183.440 207.597 1.00 7.10  ? 1979 GLN A O     1 
ATOM   4197  C  CB    . GLN A 1 1979 ? 179.240 182.671 207.479 1.00 2.01  ? 1979 GLN A CB    1 
ATOM   4198  C  CG    . GLN A 1 1979 ? 180.155 182.117 206.402 1.00 1.73  ? 1979 GLN A CG    1 
ATOM   4199  C  CD    . GLN A 1 1979 ? 181.085 181.041 206.911 1.00 0.81  ? 1979 GLN A CD    1 
ATOM   4200  O  OE1   . GLN A 1 1979 ? 181.117 180.742 208.100 1.00 2.86  ? 1979 GLN A OE1   1 
ATOM   4201  N  NE2   . GLN A 1 1979 ? 181.850 180.450 206.007 1.00 0.42  ? 1979 GLN A NE2   1 
ATOM   4202  N  N     . GLU A 1 1980 ? 177.272 184.758 208.972 1.00 3.87  ? 1980 GLU A N     1 
ATOM   4203  C  CA    . GLU A 1 1980 ? 176.103 185.073 209.789 1.00 4.48  ? 1980 GLU A CA    1 
ATOM   4204  C  C     . GLU A 1 1980 ? 175.092 185.898 209.004 1.00 4.99  ? 1980 GLU A C     1 
ATOM   4205  O  O     . GLU A 1 1980 ? 173.879 185.695 209.133 1.00 12.64 ? 1980 GLU A O     1 
ATOM   4206  C  CB    . GLU A 1 1980 ? 176.516 185.810 211.066 1.00 7.85  ? 1980 GLU A CB    1 
ATOM   4207  C  CG    . GLU A 1 1980 ? 177.699 185.226 211.857 1.00 9.75  ? 1980 GLU A CG    1 
ATOM   4208  C  CD    . GLU A 1 1980 ? 177.650 183.716 212.093 1.00 21.30 ? 1980 GLU A CD    1 
ATOM   4209  O  OE1   . GLU A 1 1980 ? 178.678 183.171 212.547 1.00 23.90 ? 1980 GLU A OE1   1 
ATOM   4210  O  OE2   . GLU A 1 1980 ? 176.597 183.074 211.884 1.00 23.70 ? 1980 GLU A OE2   1 
ATOM   4211  N  N     . ALA A 1 1981 ? 175.573 186.837 208.188 1.00 4.68  ? 1981 ALA A N     1 
ATOM   4212  C  CA    . ALA A 1 1981 ? 174.672 187.607 207.339 1.00 7.79  ? 1981 ALA A CA    1 
ATOM   4213  C  C     . ALA A 1 1981 ? 173.984 186.716 206.313 1.00 10.75 ? 1981 ALA A C     1 
ATOM   4214  O  O     . ALA A 1 1981 ? 172.798 186.900 206.014 1.00 14.61 ? 1981 ALA A O     1 
ATOM   4215  C  CB    . ALA A 1 1981 ? 175.441 188.732 206.646 1.00 4.97  ? 1981 ALA A CB    1 
ATOM   4216  N  N     . LEU A 1 1982 ? 174.713 185.744 205.760 1.00 6.70  ? 1982 LEU A N     1 
ATOM   4217  C  CA    . LEU A 1 1982 ? 174.122 184.846 204.773 1.00 6.02  ? 1982 LEU A CA    1 
ATOM   4218  C  C     . LEU A 1 1982 ? 172.979 184.040 205.373 1.00 6.85  ? 1982 LEU A C     1 
ATOM   4219  O  O     . LEU A 1 1982 ? 171.974 183.778 204.701 1.00 10.83 ? 1982 LEU A O     1 
ATOM   4220  C  CB    . LEU A 1 1982 ? 175.192 183.919 204.202 1.00 6.16  ? 1982 LEU A CB    1 
ATOM   4221  C  CG    . LEU A 1 1982 ? 176.188 184.547 203.228 1.00 5.09  ? 1982 LEU A CG    1 
ATOM   4222  C  CD1   . LEU A 1 1982 ? 177.320 183.581 202.928 1.00 3.47  ? 1982 LEU A CD1   1 
ATOM   4223  C  CD2   . LEU A 1 1982 ? 175.486 184.971 201.953 1.00 6.20  ? 1982 LEU A CD2   1 
ATOM   4224  N  N     . ARG A 1 1983 ? 173.113 183.634 206.637 1.00 6.28  ? 1983 ARG A N     1 
ATOM   4225  C  CA    . ARG A 1 1983 ? 172.035 182.920 207.306 1.00 8.05  ? 1983 ARG A CA    1 
ATOM   4226  C  C     . ARG A 1 1983 ? 170.814 183.800 207.545 1.00 12.61 ? 1983 ARG A C     1 
ATOM   4227  O  O     . ARG A 1 1983 ? 169.713 183.269 207.735 1.00 17.07 ? 1983 ARG A O     1 
ATOM   4228  C  CB    . ARG A 1 1983 ? 172.537 182.336 208.626 1.00 4.13  ? 1983 ARG A CB    1 
ATOM   4229  C  CG    . ARG A 1 1983 ? 173.469 181.160 208.429 1.00 3.77  ? 1983 ARG A CG    1 
ATOM   4230  C  CD    . ARG A 1 1983 ? 174.189 180.762 209.698 1.00 2.86  ? 1983 ARG A CD    1 
ATOM   4231  N  NE    . ARG A 1 1983 ? 175.296 179.862 209.401 1.00 4.23  ? 1983 ARG A NE    1 
ATOM   4232  C  CZ    . ARG A 1 1983 ? 176.574 180.151 209.603 1.00 8.83  ? 1983 ARG A CZ    1 
ATOM   4233  N  NH1   . ARG A 1 1983 ? 176.946 181.299 210.146 1.00 6.33  ? 1983 ARG A NH1   1 
ATOM   4234  N  NH2   . ARG A 1 1983 ? 177.502 179.266 209.250 1.00 4.06  ? 1983 ARG A NH2   1 
ATOM   4235  N  N     . GLU A 1 1984 ? 170.976 185.126 207.541 1.00 14.21 ? 1984 GLU A N     1 
ATOM   4236  C  CA    . GLU A 1 1984 ? 169.819 186.003 207.664 1.00 14.62 ? 1984 GLU A CA    1 
ATOM   4237  C  C     . GLU A 1 1984 ? 168.944 185.960 206.415 1.00 16.85 ? 1984 GLU A C     1 
ATOM   4238  O  O     . GLU A 1 1984 ? 167.724 186.132 206.514 1.00 25.98 ? 1984 GLU A O     1 
ATOM   4239  C  CB    . GLU A 1 1984 ? 170.267 187.433 207.966 1.00 14.79 ? 1984 GLU A CB    1 
ATOM   4240  C  CG    . GLU A 1 1984 ? 170.620 187.663 209.427 1.00 17.93 ? 1984 GLU A CG    1 
ATOM   4241  C  CD    . GLU A 1 1984 ? 171.707 188.701 209.622 1.00 24.96 ? 1984 GLU A CD    1 
ATOM   4242  O  OE1   . GLU A 1 1984 ? 171.787 189.647 208.809 1.00 22.89 ? 1984 GLU A OE1   1 
ATOM   4243  O  OE2   . GLU A 1 1984 ? 172.485 188.573 210.592 1.00 20.49 ? 1984 GLU A OE2   1 
ATOM   4244  N  N     . HIS A 1 1985 ? 169.539 185.738 205.240 1.00 14.72 ? 1985 HIS A N     1 
ATOM   4245  C  CA    . HIS A 1 1985 ? 168.736 185.498 204.045 1.00 22.10 ? 1985 HIS A CA    1 
ATOM   4246  C  C     . HIS A 1 1985 ? 167.914 184.226 204.189 1.00 22.48 ? 1985 HIS A C     1 
ATOM   4247  O  O     . HIS A 1 1985 ? 166.737 184.190 203.813 1.00 28.86 ? 1985 HIS A O     1 
ATOM   4248  C  CB    . HIS A 1 1985 ? 169.630 185.397 202.807 1.00 16.88 ? 1985 HIS A CB    1 
ATOM   4249  C  CG    . HIS A 1 1985 ? 170.300 186.680 202.430 1.00 13.32 ? 1985 HIS A CG    1 
ATOM   4250  N  ND1   . HIS A 1 1985 ? 171.588 186.985 202.812 1.00 21.81 ? 1985 HIS A ND1   1 
ATOM   4251  C  CD2   . HIS A 1 1985 ? 169.869 187.726 201.686 1.00 14.41 ? 1985 HIS A CD2   1 
ATOM   4252  C  CE1   . HIS A 1 1985 ? 171.917 188.170 202.331 1.00 17.15 ? 1985 HIS A CE1   1 
ATOM   4253  N  NE2   . HIS A 1 1985 ? 170.892 188.642 201.645 1.00 15.76 ? 1985 HIS A NE2   1 
ATOM   4254  N  N     . SER A 1 1986 ? 168.523 183.171 204.730 1.00 18.84 ? 1986 SER A N     1 
ATOM   4255  C  CA    . SER A 1 1986 ? 167.885 181.866 204.827 1.00 16.57 ? 1986 SER A CA    1 
ATOM   4256  C  C     . SER A 1 1986 ? 166.783 181.812 205.876 1.00 21.08 ? 1986 SER A C     1 
ATOM   4257  O  O     . SER A 1 1986 ? 166.059 180.814 205.931 1.00 25.65 ? 1986 SER A O     1 
ATOM   4258  C  CB    . SER A 1 1986 ? 168.941 180.802 205.127 1.00 11.54 ? 1986 SER A CB    1 
ATOM   4259  O  OG    . SER A 1 1986 ? 169.272 180.783 206.502 1.00 10.33 ? 1986 SER A OG    1 
ATOM   4260  N  N     . ASN A 1 1987 ? 166.642 182.838 206.702 1.00 20.32 ? 1987 ASN A N     1 
ATOM   4261  C  CA    . ASN A 1 1987 ? 165.600 182.840 207.721 1.00 26.31 ? 1987 ASN A CA    1 
ATOM   4262  C  C     . ASN A 1 1987 ? 164.233 183.018 207.071 1.00 34.08 ? 1987 ASN A C     1 
ATOM   4263  O  O     . ASN A 1 1987 ? 164.021 184.008 206.357 1.00 33.54 ? 1987 ASN A O     1 
ATOM   4264  C  CB    . ASN A 1 1987 ? 165.850 183.947 208.740 1.00 26.54 ? 1987 ASN A CB    1 
ATOM   4265  C  CG    . ASN A 1 1987 ? 166.980 183.616 209.695 1.00 32.46 ? 1987 ASN A CG    1 
ATOM   4266  O  OD1   . ASN A 1 1987 ? 167.979 184.331 209.767 1.00 32.94 ? 1987 ASN A OD1   1 
ATOM   4267  N  ND2   . ASN A 1 1987 ? 166.826 182.525 210.437 1.00 27.84 ? 1987 ASN A ND2   1 
ATOM   4268  N  N     . PRO A 1 1988 ? 163.291 182.093 207.273 1.00 36.24 ? 1988 PRO A N     1 
ATOM   4269  C  CA    . PRO A 1 1988 ? 161.945 182.284 206.706 1.00 32.06 ? 1988 PRO A CA    1 
ATOM   4270  C  C     . PRO A 1 1988 ? 161.223 183.498 207.259 1.00 38.08 ? 1988 PRO A C     1 
ATOM   4271  O  O     . PRO A 1 1988 ? 160.388 184.084 206.558 1.00 38.56 ? 1988 PRO A O     1 
ATOM   4272  C  CB    . PRO A 1 1988 ? 161.225 180.979 207.070 1.00 31.33 ? 1988 PRO A CB    1 
ATOM   4273  C  CG    . PRO A 1 1988 ? 161.961 180.465 208.266 1.00 36.74 ? 1988 PRO A CG    1 
ATOM   4274  C  CD    . PRO A 1 1988 ? 163.396 180.847 208.049 1.00 33.08 ? 1988 PRO A CD    1 
ATOM   4275  N  N     . ASN A 1 1989 ? 161.513 183.889 208.503 1.00 36.11 ? 1989 ASN A N     1 
ATOM   4276  C  CA    . ASN A 1 1989 ? 160.841 185.042 209.095 1.00 33.21 ? 1989 ASN A CA    1 
ATOM   4277  C  C     . ASN A 1 1989 ? 161.199 186.327 208.359 1.00 38.35 ? 1989 ASN A C     1 
ATOM   4278  O  O     . ASN A 1 1989 ? 160.366 187.235 208.241 1.00 41.94 ? 1989 ASN A O     1 
ATOM   4279  C  CB    . ASN A 1 1989 ? 161.196 185.152 210.578 1.00 33.84 ? 1989 ASN A CB    1 
ATOM   4280  C  CG    . ASN A 1 1989 ? 162.688 185.043 210.831 1.00 37.31 ? 1989 ASN A CG    1 
ATOM   4281  O  OD1   . ASN A 1 1989 ? 163.465 185.902 210.416 1.00 36.74 ? 1989 ASN A OD1   1 
ATOM   4282  N  ND2   . ASN A 1 1989 ? 163.095 183.980 211.517 1.00 32.03 ? 1989 ASN A ND2   1 
ATOM   4283  N  N     . TYR A 1 1990 ? 162.432 186.426 207.870 1.00 37.09 ? 1990 TYR A N     1 
ATOM   4284  C  CA    . TYR A 1 1990 ? 162.850 187.604 207.122 1.00 35.42 ? 1990 TYR A CA    1 
ATOM   4285  C  C     . TYR A 1 1990 ? 162.046 187.739 205.834 1.00 35.54 ? 1990 TYR A C     1 
ATOM   4286  O  O     . TYR A 1 1990 ? 161.797 186.757 205.131 1.00 37.17 ? 1990 TYR A O     1 
ATOM   4287  C  CB    . TYR A 1 1990 ? 164.346 187.526 206.810 1.00 31.14 ? 1990 TYR A CB    1 
ATOM   4288  C  CG    . TYR A 1 1990 ? 164.760 188.311 205.587 1.00 28.66 ? 1990 TYR A CG    1 
ATOM   4289  C  CD1   . TYR A 1 1990 ? 164.917 189.689 205.642 1.00 32.85 ? 1990 TYR A CD1   1 
ATOM   4290  C  CD2   . TYR A 1 1990 ? 165.000 187.673 204.376 1.00 29.58 ? 1990 TYR A CD2   1 
ATOM   4291  C  CE1   . TYR A 1 1990 ? 165.298 190.410 204.525 1.00 29.00 ? 1990 TYR A CE1   1 
ATOM   4292  C  CE2   . TYR A 1 1990 ? 165.379 188.383 203.255 1.00 30.60 ? 1990 TYR A CE2   1 
ATOM   4293  C  CZ    . TYR A 1 1990 ? 165.522 189.751 203.335 1.00 33.49 ? 1990 TYR A CZ    1 
ATOM   4294  O  OH    . TYR A 1 1990 ? 165.903 190.464 202.222 1.00 31.16 ? 1990 TYR A OH    1 
ATOM   4295  N  N     . ASP A 1 1991 ? 161.640 188.969 205.531 1.00 36.37 ? 1991 ASP A N     1 
ATOM   4296  C  CA    . ASP A 1 1991 ? 160.877 189.277 204.333 1.00 34.31 ? 1991 ASP A CA    1 
ATOM   4297  C  C     . ASP A 1 1991 ? 161.693 190.169 203.407 1.00 37.55 ? 1991 ASP A C     1 
ATOM   4298  O  O     . ASP A 1 1991 ? 162.404 191.073 203.856 1.00 39.00 ? 1991 ASP A O     1 
ATOM   4299  C  CB    . ASP A 1 1991 ? 159.553 189.962 204.685 1.00 34.13 ? 1991 ASP A CB    1 
ATOM   4300  C  CG    . ASP A 1 1991 ? 159.750 191.258 205.446 1.00 40.53 ? 1991 ASP A CG    1 
ATOM   4301  O  OD1   . ASP A 1 1991 ? 160.424 191.236 206.497 1.00 35.72 ? 1991 ASP A OD1   1 
ATOM   4302  O  OD2   . ASP A 1 1991 ? 159.231 192.300 204.991 1.00 39.15 ? 1991 ASP A OD2   1 
ATOM   4303  N  N     . LYS A 1 1992 ? 161.579 189.905 202.102 1.00 36.78 ? 1992 LYS A N     1 
ATOM   4304  C  CA    . LYS A 1 1992 ? 162.372 190.641 201.121 1.00 36.15 ? 1992 LYS A CA    1 
ATOM   4305  C  C     . LYS A 1 1992 ? 162.059 192.132 201.139 1.00 37.35 ? 1992 LYS A C     1 
ATOM   4306  O  O     . LYS A 1 1992 ? 162.905 192.946 200.753 1.00 35.95 ? 1992 LYS A O     1 
ATOM   4307  C  CB    . LYS A 1 1992 ? 162.136 190.068 199.723 1.00 33.61 ? 1992 LYS A CB    1 
ATOM   4308  C  CG    . LYS A 1 1992 ? 162.516 188.602 199.581 1.00 31.44 ? 1992 LYS A CG    1 
ATOM   4309  C  CD    . LYS A 1 1992 ? 162.106 188.054 198.225 1.00 27.57 ? 1992 LYS A CD    1 
ATOM   4310  C  CE    . LYS A 1 1992 ? 160.599 188.125 198.032 1.00 31.43 ? 1992 LYS A CE    1 
ATOM   4311  N  NZ    . LYS A 1 1992 ? 160.178 187.557 196.723 1.00 35.79 ? 1992 LYS A NZ    1 
ATOM   4312  N  N     . THR A 1 1993 ? 160.861 192.509 201.580 1.00 36.86 ? 1993 THR A N     1 
ATOM   4313  C  CA    . THR A 1 1993 ? 160.475 193.917 201.669 1.00 34.59 ? 1993 THR A CA    1 
ATOM   4314  C  C     . THR A 1 1993 ? 160.785 194.471 203.062 1.00 37.64 ? 1993 THR A C     1 
ATOM   4315  O  O     . THR A 1 1993 ? 159.904 194.876 203.820 1.00 39.64 ? 1993 THR A O     1 
ATOM   4316  C  CB    . THR A 1 1993 ? 159.000 194.084 201.322 1.00 33.83 ? 1993 THR A CB    1 
ATOM   4317  O  OG1   . THR A 1 1993 ? 158.205 193.294 202.215 1.00 38.43 ? 1993 THR A OG1   1 
ATOM   4318  C  CG2   . THR A 1 1993 ? 158.737 193.640 199.891 1.00 30.20 ? 1993 THR A CG2   1 
ATOM   4319  N  N     . SER A 1 1994 ? 162.075 194.478 203.391 1.00 35.89 ? 1994 SER A N     1 
ATOM   4320  C  CA    . SER A 1 1994 ? 162.546 194.959 204.682 1.00 36.86 ? 1994 SER A CA    1 
ATOM   4321  C  C     . SER A 1 1994 ? 163.930 195.568 204.491 1.00 35.04 ? 1994 SER A C     1 
ATOM   4322  O  O     . SER A 1 1994 ? 164.388 195.786 203.364 1.00 35.45 ? 1994 SER A O     1 
ATOM   4323  C  CB    . SER A 1 1994 ? 162.550 193.827 205.717 1.00 32.32 ? 1994 SER A CB    1 
ATOM   4324  O  OG    . SER A 1 1994 ? 163.673 192.982 205.536 1.00 34.24 ? 1994 SER A OG    1 
ATOM   4325  N  N     . ALA A 1 1995 ? 164.599 195.848 205.604 1.00 29.07 ? 1995 ALA A N     1 
ATOM   4326  C  CA    . ALA A 1 1995 ? 165.959 196.365 205.548 1.00 30.67 ? 1995 ALA A CA    1 
ATOM   4327  C  C     . ALA A 1 1995 ? 166.896 195.295 205.000 1.00 32.34 ? 1995 ALA A C     1 
ATOM   4328  O  O     . ALA A 1 1995 ? 166.837 194.143 205.442 1.00 31.78 ? 1995 ALA A O     1 
ATOM   4329  C  CB    . ALA A 1 1995 ? 166.421 196.816 206.931 1.00 23.28 ? 1995 ALA A CB    1 
ATOM   4330  N  N     . PRO A 1 1996 ? 167.761 195.628 204.042 1.00 31.17 ? 1996 PRO A N     1 
ATOM   4331  C  CA    . PRO A 1 1996 ? 168.643 194.609 203.460 1.00 26.67 ? 1996 PRO A CA    1 
ATOM   4332  C  C     . PRO A 1 1996 ? 169.597 194.031 204.494 1.00 23.01 ? 1996 PRO A C     1 
ATOM   4333  O  O     . PRO A 1 1996 ? 170.016 194.708 205.434 1.00 23.69 ? 1996 PRO A O     1 
ATOM   4334  C  CB    . PRO A 1 1996 ? 169.402 195.379 202.371 1.00 24.40 ? 1996 PRO A CB    1 
ATOM   4335  C  CG    . PRO A 1 1996 ? 168.545 196.568 202.071 1.00 28.36 ? 1996 PRO A CG    1 
ATOM   4336  C  CD    . PRO A 1 1996 ? 167.905 196.932 203.376 1.00 23.52 ? 1996 PRO A CD    1 
ATOM   4337  N  N     . ILE A 1 1997 ? 169.929 192.753 204.310 1.00 20.51 ? 1997 ILE A N     1 
ATOM   4338  C  CA    . ILE A 1 1997 ? 170.919 192.105 205.161 1.00 13.33 ? 1997 ILE A CA    1 
ATOM   4339  C  C     . ILE A 1 1997 ? 172.266 192.787 204.974 1.00 14.71 ? 1997 ILE A C     1 
ATOM   4340  O  O     . ILE A 1 1997 ? 172.669 193.108 203.849 1.00 15.18 ? 1997 ILE A O     1 
ATOM   4341  C  CB    . ILE A 1 1997 ? 171.012 190.601 204.854 1.00 13.82 ? 1997 ILE A CB    1 
ATOM   4342  C  CG1   . ILE A 1 1997 ? 169.691 189.892 205.158 1.00 18.14 ? 1997 ILE A CG1   1 
ATOM   4343  C  CG2   . ILE A 1 1997 ? 172.150 189.967 205.620 1.00 13.51 ? 1997 ILE A CG2   1 
ATOM   4344  C  CD1   . ILE A 1 1997 ? 168.735 189.866 204.008 1.00 22.05 ? 1997 ILE A CD1   1 
ATOM   4345  N  N     . THR A 1 1998 ? 172.963 193.014 206.081 1.00 11.05 ? 1998 THR A N     1 
ATOM   4346  C  CA    . THR A 1 1998 ? 174.215 193.748 206.079 1.00 9.46  ? 1998 THR A CA    1 
ATOM   4347  C  C     . THR A 1 1998 ? 175.154 193.160 207.123 1.00 10.55 ? 1998 THR A C     1 
ATOM   4348  O  O     . THR A 1 1998 ? 174.738 192.816 208.232 1.00 17.98 ? 1998 THR A O     1 
ATOM   4349  C  CB    . THR A 1 1998 ? 173.964 195.243 206.355 1.00 11.57 ? 1998 THR A CB    1 
ATOM   4350  O  OG1   . THR A 1 1998 ? 173.360 195.849 205.207 1.00 12.97 ? 1998 THR A OG1   1 
ATOM   4351  C  CG2   . THR A 1 1998 ? 175.249 195.953 206.656 1.00 12.64 ? 1998 THR A CG2   1 
ATOM   4352  N  N     . CYS A 1 1999 ? 176.426 193.031 206.755 1.00 6.20  ? 1999 CYS A N     1 
ATOM   4353  C  CA    . CYS A 1 1999 ? 177.474 192.648 207.688 1.00 9.31  ? 1999 CYS A CA    1 
ATOM   4354  C  C     . CYS A 1 1999 ? 178.519 193.755 207.751 1.00 8.55  ? 1999 CYS A C     1 
ATOM   4355  O  O     . CYS A 1 1999 ? 178.609 194.605 206.863 1.00 8.23  ? 1999 CYS A O     1 
ATOM   4356  C  CB    . CYS A 1 1999 ? 178.131 191.320 207.291 1.00 5.31  ? 1999 CYS A CB    1 
ATOM   4357  S  SG    . CYS A 1 1999 ? 179.400 191.453 206.020 1.00 18.41 ? 1999 CYS A SG    1 
ATOM   4358  N  N     . GLU A 1 2000 ? 179.307 193.743 208.821 1.00 6.03  ? 2000 GLU A N     1 
ATOM   4359  C  CA    . GLU A 1 2000 ? 180.320 194.768 209.040 1.00 9.76  ? 2000 GLU A CA    1 
ATOM   4360  C  C     . GLU A 1 2000 ? 181.644 194.303 208.447 1.00 7.29  ? 2000 GLU A C     1 
ATOM   4361  O  O     . GLU A 1 2000 ? 182.271 193.369 208.957 1.00 4.76  ? 2000 GLU A O     1 
ATOM   4362  C  CB    . GLU A 1 2000 ? 180.463 195.083 210.526 1.00 11.36 ? 2000 GLU A CB    1 
ATOM   4363  C  CG    . GLU A 1 2000 ? 181.160 196.402 210.797 1.00 8.78  ? 2000 GLU A CG    1 
ATOM   4364  C  CD    . GLU A 1 2000 ? 181.433 196.630 212.269 1.00 19.53 ? 2000 GLU A CD    1 
ATOM   4365  O  OE1   . GLU A 1 2000 ? 181.056 195.765 213.086 1.00 24.32 ? 2000 GLU A OE1   1 
ATOM   4366  O  OE2   . GLU A 1 2000 ? 182.025 197.674 212.606 1.00 17.40 ? 2000 GLU A OE2   1 
ATOM   4367  N  N     . LEU A 1 2001 ? 182.072 194.960 207.373 1.00 5.34  ? 2001 LEU A N     1 
ATOM   4368  C  CA    . LEU A 1 2001 ? 183.362 194.705 206.747 1.00 4.39  ? 2001 LEU A CA    1 
ATOM   4369  C  C     . LEU A 1 2001 ? 184.174 195.989 206.781 1.00 6.61  ? 2001 LEU A C     1 
ATOM   4370  O  O     . LEU A 1 2001 ? 183.714 197.029 206.298 1.00 11.59 ? 2001 LEU A O     1 
ATOM   4371  C  CB    . LEU A 1 2001 ? 183.189 194.208 205.311 1.00 5.03  ? 2001 LEU A CB    1 
ATOM   4372  C  CG    . LEU A 1 2001 ? 182.710 192.764 205.160 1.00 1.22  ? 2001 LEU A CG    1 
ATOM   4373  C  CD1   . LEU A 1 2001 ? 182.505 192.409 203.695 1.00 0.84  ? 2001 LEU A CD1   1 
ATOM   4374  C  CD2   . LEU A 1 2001 ? 183.699 191.814 205.814 1.00 1.08  ? 2001 LEU A CD2   1 
ATOM   4375  N  N     . LEU A 1 2002 ? 185.376 195.913 207.353 1.00 6.28  ? 2002 LEU A N     1 
ATOM   4376  C  CA    . LEU A 1 2002 ? 186.285 197.055 207.449 1.00 4.87  ? 2002 LEU A CA    1 
ATOM   4377  C  C     . LEU A 1 2002 ? 185.609 198.246 208.126 1.00 7.84  ? 2002 LEU A C     1 
ATOM   4378  O  O     . LEU A 1 2002 ? 185.700 199.389 207.675 1.00 12.90 ? 2002 LEU A O     1 
ATOM   4379  C  CB    . LEU A 1 2002 ? 186.826 197.435 206.069 1.00 3.80  ? 2002 LEU A CB    1 
ATOM   4380  C  CG    . LEU A 1 2002 ? 187.651 196.348 205.378 1.00 4.18  ? 2002 LEU A CG    1 
ATOM   4381  C  CD1   . LEU A 1 2002 ? 188.169 196.824 204.033 1.00 0.98  ? 2002 LEU A CD1   1 
ATOM   4382  C  CD2   . LEU A 1 2002 ? 188.798 195.897 206.270 1.00 4.44  ? 2002 LEU A CD2   1 
ATOM   4383  N  N     . ASN A 1 2003 ? 184.906 197.954 209.224 1.00 8.02  ? 2003 ASN A N     1 
ATOM   4384  C  CA    . ASN A 1 2003 ? 184.236 198.964 210.049 1.00 9.87  ? 2003 ASN A CA    1 
ATOM   4385  C  C     . ASN A 1 2003 ? 183.184 199.741 209.258 1.00 9.53  ? 2003 ASN A C     1 
ATOM   4386  O  O     . ASN A 1 2003 ? 182.900 200.904 209.548 1.00 18.08 ? 2003 ASN A O     1 
ATOM   4387  C  CB    . ASN A 1 2003 ? 185.245 199.921 210.688 1.00 9.20  ? 2003 ASN A CB    1 
ATOM   4388  C  CG    . ASN A 1 2003 ? 186.336 199.196 211.442 1.00 14.24 ? 2003 ASN A CG    1 
ATOM   4389  O  OD1   . ASN A 1 2003 ? 187.511 199.277 211.085 1.00 18.00 ? 2003 ASN A OD1   1 
ATOM   4390  N  ND2   . ASN A 1 2003 ? 185.954 198.476 212.490 1.00 15.10 ? 2003 ASN A ND2   1 
ATOM   4391  N  N     . LYS A 1 2004 ? 182.598 199.093 208.255 1.00 9.11  ? 2004 LYS A N     1 
ATOM   4392  C  CA    . LYS A 1 2004 ? 181.523 199.692 207.479 1.00 6.90  ? 2004 LYS A CA    1 
ATOM   4393  C  C     . LYS A 1 2004 ? 180.415 198.667 207.298 1.00 9.50  ? 2004 LYS A C     1 
ATOM   4394  O  O     . LYS A 1 2004 ? 180.680 197.466 207.214 1.00 8.49  ? 2004 LYS A O     1 
ATOM   4395  C  CB    . LYS A 1 2004 ? 182.012 200.188 206.112 1.00 5.75  ? 2004 LYS A CB    1 
ATOM   4396  C  CG    . LYS A 1 2004 ? 183.067 201.270 206.181 1.00 14.03 ? 2004 LYS A CG    1 
ATOM   4397  C  CD    . LYS A 1 2004 ? 182.493 202.555 206.752 1.00 18.93 ? 2004 LYS A CD    1 
ATOM   4398  C  CE    . LYS A 1 2004 ? 183.521 203.671 206.755 1.00 20.39 ? 2004 LYS A CE    1 
ATOM   4399  N  NZ    . LYS A 1 2004 ? 182.968 204.917 207.353 1.00 24.34 ? 2004 LYS A NZ    1 
ATOM   4400  N  N     . GLN A 1 2005 ? 179.180 199.151 207.235 1.00 9.65  ? 2005 GLN A N     1 
ATOM   4401  C  CA    . GLN A 1 2005 ? 178.025 198.282 207.046 1.00 8.00  ? 2005 GLN A CA    1 
ATOM   4402  C  C     . GLN A 1 2005 ? 177.852 197.998 205.558 1.00 7.23  ? 2005 GLN A C     1 
ATOM   4403  O  O     . GLN A 1 2005 ? 177.538 198.904 204.780 1.00 12.46 ? 2005 GLN A O     1 
ATOM   4404  C  CB    . GLN A 1 2005 ? 176.774 198.933 207.631 1.00 7.17  ? 2005 GLN A CB    1 
ATOM   4405  C  CG    . GLN A 1 2005 ? 176.741 198.968 209.156 1.00 8.99  ? 2005 GLN A CG    1 
ATOM   4406  C  CD    . GLN A 1 2005 ? 176.971 197.608 209.792 1.00 11.22 ? 2005 GLN A CD    1 
ATOM   4407  O  OE1   . GLN A 1 2005 ? 176.237 196.657 209.535 1.00 12.49 ? 2005 GLN A OE1   1 
ATOM   4408  N  NE2   . GLN A 1 2005 ? 178.000 197.513 210.627 1.00 16.18 ? 2005 GLN A NE2   1 
ATOM   4409  N  N     . VAL A 1 2006 ? 178.051 196.742 205.164 1.00 5.10  ? 2006 VAL A N     1 
ATOM   4410  C  CA    . VAL A 1 2006 ? 178.079 196.343 203.762 1.00 5.95  ? 2006 VAL A CA    1 
ATOM   4411  C  C     . VAL A 1 2006 ? 176.922 195.391 203.496 1.00 5.28  ? 2006 VAL A C     1 
ATOM   4412  O  O     . VAL A 1 2006 ? 176.761 194.391 204.202 1.00 9.19  ? 2006 VAL A O     1 
ATOM   4413  C  CB    . VAL A 1 2006 ? 179.420 195.684 203.393 1.00 5.20  ? 2006 VAL A CB    1 
ATOM   4414  C  CG1   . VAL A 1 2006 ? 179.444 195.307 201.922 1.00 4.16  ? 2006 VAL A CG1   1 
ATOM   4415  C  CG2   . VAL A 1 2006 ? 180.579 196.608 203.730 1.00 5.05  ? 2006 VAL A CG2   1 
ATOM   4416  N  N     . LYS A 1 2007 ? 176.123 195.699 202.477 1.00 4.23  ? 2007 LYS A N     1 
ATOM   4417  C  CA    . LYS A 1 2007 ? 175.044 194.806 202.077 1.00 9.07  ? 2007 LYS A CA    1 
ATOM   4418  C  C     . LYS A 1 2007 ? 175.612 193.510 201.511 1.00 8.91  ? 2007 LYS A C     1 
ATOM   4419  O  O     . LYS A 1 2007 ? 176.626 193.510 200.809 1.00 4.13  ? 2007 LYS A O     1 
ATOM   4420  C  CB    . LYS A 1 2007 ? 174.147 195.480 201.040 1.00 7.62  ? 2007 LYS A CB    1 
ATOM   4421  C  CG    . LYS A 1 2007 ? 173.416 196.707 201.549 1.00 14.99 ? 2007 LYS A CG    1 
ATOM   4422  C  CD    . LYS A 1 2007 ? 172.493 197.279 200.484 1.00 25.32 ? 2007 LYS A CD    1 
ATOM   4423  C  CE    . LYS A 1 2007 ? 173.285 197.917 199.354 1.00 21.89 ? 2007 LYS A CE    1 
ATOM   4424  N  NZ    . LYS A 1 2007 ? 174.036 199.120 199.802 1.00 24.86 ? 2007 LYS A NZ    1 
ATOM   4425  N  N     . VAL A 1 2008 ? 174.950 192.400 201.821 1.00 8.28  ? 2008 VAL A N     1 
ATOM   4426  C  CA    . VAL A 1 2008 ? 175.402 191.074 201.423 1.00 3.48  ? 2008 VAL A CA    1 
ATOM   4427  C  C     . VAL A 1 2008 ? 174.368 190.470 200.486 1.00 5.70  ? 2008 VAL A C     1 
ATOM   4428  O  O     . VAL A 1 2008 ? 173.191 190.350 200.843 1.00 14.38 ? 2008 VAL A O     1 
ATOM   4429  C  CB    . VAL A 1 2008 ? 175.635 190.169 202.647 1.00 4.05  ? 2008 VAL A CB    1 
ATOM   4430  C  CG1   . VAL A 1 2008 ? 176.130 188.800 202.211 1.00 5.44  ? 2008 VAL A CG1   1 
ATOM   4431  C  CG2   . VAL A 1 2008 ? 176.622 190.818 203.605 1.00 3.11  ? 2008 VAL A CG2   1 
ATOM   4432  N  N     . SER A 1 2009 ? 174.803 190.104 199.286 1.00 7.41  ? 2009 SER A N     1 
ATOM   4433  C  CA    . SER A 1 2009 ? 173.871 189.418 198.403 1.00 6.28  ? 2009 SER A CA    1 
ATOM   4434  C  C     . SER A 1 2009 ? 173.847 187.927 198.725 1.00 7.74  ? 2009 SER A C     1 
ATOM   4435  O  O     . SER A 1 2009 ? 174.895 187.339 199.009 1.00 10.04 ? 2009 SER A O     1 
ATOM   4436  C  CB    . SER A 1 2009 ? 174.257 189.623 196.943 1.00 4.52  ? 2009 SER A CB    1 
ATOM   4437  O  OG    . SER A 1 2009 ? 173.379 188.925 196.075 1.00 9.84  ? 2009 SER A OG    1 
ATOM   4438  N  N     . PRO A 1 2010 ? 172.670 187.299 198.702 1.00 7.09  ? 2010 PRO A N     1 
ATOM   4439  C  CA    . PRO A 1 2010 ? 172.599 185.866 199.038 1.00 6.71  ? 2010 PRO A CA    1 
ATOM   4440  C  C     . PRO A 1 2010 ? 173.353 184.971 198.071 1.00 4.83  ? 2010 PRO A C     1 
ATOM   4441  O  O     . PRO A 1 2010 ? 173.662 183.828 198.424 1.00 8.75  ? 2010 PRO A O     1 
ATOM   4442  C  CB    . PRO A 1 2010 ? 171.090 185.575 199.010 1.00 7.80  ? 2010 PRO A CB    1 
ATOM   4443  C  CG    . PRO A 1 2010 ? 170.502 186.670 198.187 1.00 4.18  ? 2010 PRO A CG    1 
ATOM   4444  C  CD    . PRO A 1 2010 ? 171.342 187.875 198.449 1.00 6.49  ? 2010 PRO A CD    1 
ATOM   4445  N  N     . ASP A 1 2011 ? 173.659 185.449 196.866 1.00 4.36  ? 2011 ASP A N     1 
ATOM   4446  C  CA    . ASP A 1 2011 ? 174.314 184.620 195.864 1.00 2.57  ? 2011 ASP A CA    1 
ATOM   4447  C  C     . ASP A 1 2011 ? 175.819 184.501 196.060 1.00 1.54  ? 2011 ASP A C     1 
ATOM   4448  O  O     . ASP A 1 2011 ? 176.442 183.664 195.398 1.00 1.35  ? 2011 ASP A O     1 
ATOM   4449  C  CB    . ASP A 1 2011 ? 174.029 185.159 194.462 1.00 1.51  ? 2011 ASP A CB    1 
ATOM   4450  C  CG    . ASP A 1 2011 ? 172.629 184.830 193.982 1.00 8.19  ? 2011 ASP A CG    1 
ATOM   4451  O  OD1   . ASP A 1 2011 ? 171.834 184.294 194.783 1.00 9.79  ? 2011 ASP A OD1   1 
ATOM   4452  O  OD2   . ASP A 1 2011 ? 172.328 185.095 192.803 1.00 9.55  ? 2011 ASP A OD2   1 
ATOM   4453  N  N     . MET A 1 2012 ? 176.420 185.300 196.936 1.00 1.07  ? 2012 MET A N     1 
ATOM   4454  C  CA    . MET A 1 2012 ? 177.868 185.272 197.077 1.00 0.68  ? 2012 MET A CA    1 
ATOM   4455  C  C     . MET A 1 2012 ? 178.311 184.059 197.884 1.00 1.02  ? 2012 MET A C     1 
ATOM   4456  O  O     . MET A 1 2012 ? 177.575 183.551 198.735 1.00 4.09  ? 2012 MET A O     1 
ATOM   4457  C  CB    . MET A 1 2012 ? 178.370 186.569 197.719 1.00 0.62  ? 2012 MET A CB    1 
ATOM   4458  C  CG    . MET A 1 2012 ? 178.061 186.760 199.199 1.00 1.57  ? 2012 MET A CG    1 
ATOM   4459  S  SD    . MET A 1 2012 ? 179.196 185.905 200.312 1.00 16.39 ? 2012 MET A SD    1 
ATOM   4460  C  CE    . MET A 1 2012 ? 180.763 186.589 199.786 1.00 0.61  ? 2012 MET A CE    1 
ATOM   4461  N  N     . ALA A 1 2013 ? 179.530 183.597 197.616 1.00 0.17  ? 2013 ALA A N     1 
ATOM   4462  C  CA    . ALA A 1 2013 ? 180.085 182.438 198.293 1.00 0.03  ? 2013 ALA A CA    1 
ATOM   4463  C  C     . ALA A 1 2013 ? 181.597 182.581 198.349 1.00 0.04  ? 2013 ALA A C     1 
ATOM   4464  O  O     . ALA A 1 2013 ? 182.200 183.312 197.561 1.00 0.06  ? 2013 ALA A O     1 
ATOM   4465  C  CB    . ALA A 1 2013 ? 179.691 181.132 197.594 1.00 0.01  ? 2013 ALA A CB    1 
ATOM   4466  N  N     . ILE A 1 2014 ? 182.206 181.868 199.294 1.00 0.06  ? 2014 ILE A N     1 
ATOM   4467  C  CA    . ILE A 1 2014 ? 183.649 181.895 199.502 1.00 0.03  ? 2014 ILE A CA    1 
ATOM   4468  C  C     . ILE A 1 2014 ? 184.185 180.478 199.365 1.00 0.03  ? 2014 ILE A C     1 
ATOM   4469  O  O     . ILE A 1 2014 ? 183.684 179.552 200.012 1.00 0.04  ? 2014 ILE A O     1 
ATOM   4470  C  CB    . ILE A 1 2014 ? 184.017 182.486 200.876 1.00 0.04  ? 2014 ILE A CB    1 
ATOM   4471  C  CG1   . ILE A 1 2014 ? 183.312 183.825 201.093 1.00 0.04  ? 2014 ILE A CG1   1 
ATOM   4472  C  CG2   . ILE A 1 2014 ? 185.520 182.651 201.001 1.00 0.03  ? 2014 ILE A CG2   1 
ATOM   4473  C  CD1   . ILE A 1 2014 ? 183.588 184.451 202.443 1.00 0.12  ? 2014 ILE A CD1   1 
ATOM   4474  N  N     . PHE A 1 2015 ? 185.198 180.310 198.523 1.00 0.03  ? 2015 PHE A N     1 
ATOM   4475  C  CA    . PHE A 1 2015 ? 185.854 179.026 198.328 1.00 0.04  ? 2015 PHE A CA    1 
ATOM   4476  C  C     . PHE A 1 2015 ? 187.359 179.209 198.431 1.00 0.10  ? 2015 PHE A C     1 
ATOM   4477  O  O     . PHE A 1 2015 ? 187.905 180.210 197.960 1.00 0.03  ? 2015 PHE A O     1 
ATOM   4478  C  CB    . PHE A 1 2015 ? 185.498 178.408 196.971 1.00 0.00  ? 2015 PHE A CB    1 
ATOM   4479  C  CG    . PHE A 1 2015 ? 184.100 177.882 196.891 1.00 0.02  ? 2015 PHE A CG    1 
ATOM   4480  C  CD1   . PHE A 1 2015 ? 183.045 178.725 196.578 1.00 0.00  ? 2015 PHE A CD1   1 
ATOM   4481  C  CD2   . PHE A 1 2015 ? 183.834 176.544 197.122 1.00 0.02  ? 2015 PHE A CD2   1 
ATOM   4482  C  CE1   . PHE A 1 2015 ? 181.758 178.245 196.501 1.00 0.03  ? 2015 PHE A CE1   1 
ATOM   4483  C  CE2   . PHE A 1 2015 ? 182.544 176.057 197.044 1.00 0.01  ? 2015 PHE A CE2   1 
ATOM   4484  C  CZ    . PHE A 1 2015 ? 181.505 176.909 196.734 1.00 0.03  ? 2015 PHE A CZ    1 
ATOM   4485  N  N     . ILE A 1 2016 ? 188.014 178.233 199.053 1.00 0.02  ? 2016 ILE A N     1 
ATOM   4486  C  CA    . ILE A 1 2016 ? 189.496 178.264 199.180 1.00 0.03  ? 2016 ILE A CA    1 
ATOM   4487  C  C     . ILE A 1 2016 ? 190.018 176.914 198.672 1.00 0.05  ? 2016 ILE A C     1 
ATOM   4488  O  O     . ILE A 1 2016 ? 189.448 175.875 199.049 1.00 0.07  ? 2016 ILE A O     1 
ATOM   4489  C  CB    . ILE A 1 2016 ? 189.921 178.556 200.631 1.00 0.07  ? 2016 ILE A CB    1 
ATOM   4490  C  CG1   . ILE A 1 2016 ? 189.438 177.471 201.594 1.00 0.05  ? 2016 ILE A CG1   1 
ATOM   4491  C  CG2   . ILE A 1 2016 ? 189.450 179.945 201.066 1.00 0.02  ? 2016 ILE A CG2   1 
ATOM   4492  C  CD1   . ILE A 1 2016 ? 189.830 177.703 203.042 1.00 0.04  ? 2016 ILE A CD1   1 
ATOM   4493  N  N     . THR A 1 2017 ? 191.031 176.944 197.808 1.00 0.32  ? 2017 THR A N     1 
ATOM   4494  C  CA    . THR A 1 2017 ? 191.635 175.697 197.299 1.00 0.57  ? 2017 THR A CA    1 
ATOM   4495  C  C     . THR A 1 2017 ? 193.060 175.674 197.782 1.00 0.90  ? 2017 THR A C     1 
ATOM   4496  O  O     . THR A 1 2017 ? 193.749 176.701 197.624 1.00 1.63  ? 2017 THR A O     1 
ATOM   4497  C  CB    . THR A 1 2017 ? 191.532 175.643 195.774 1.00 0.87  ? 2017 THR A CB    1 
ATOM   4498  O  OG1   . THR A 1 2017 ? 192.349 176.708 195.298 1.00 3.57  ? 2017 THR A OG1   1 
ATOM   4499  C  CG2   . THR A 1 2017 ? 190.106 175.817 195.280 1.00 0.50  ? 2017 THR A CG2   1 
ATOM   4500  N  N     . MET A 1 2018 ? 193.496 174.562 198.370 1.00 1.32  ? 2018 MET A N     1 
ATOM   4501  C  CA    . MET A 1 2018 ? 194.852 174.552 198.970 1.00 1.11  ? 2018 MET A CA    1 
ATOM   4502  C  C     . MET A 1 2018 ? 195.538 173.196 198.790 1.00 1.13  ? 2018 MET A C     1 
ATOM   4503  O  O     . MET A 1 2018 ? 194.829 172.184 198.632 1.00 1.16  ? 2018 MET A O     1 
ATOM   4504  C  CB    . MET A 1 2018 ? 194.782 174.821 200.477 1.00 2.20  ? 2018 MET A CB    1 
ATOM   4505  C  CG    . MET A 1 2018 ? 194.136 176.136 200.858 1.00 3.50  ? 2018 MET A CG    1 
ATOM   4506  S  SD    . MET A 1 2018 ? 193.945 176.271 202.646 1.00 12.11 ? 2018 MET A SD    1 
ATOM   4507  C  CE    . MET A 1 2018 ? 192.837 174.895 202.979 1.00 3.47  ? 2018 MET A CE    1 
ATOM   4508  N  N     . ASN A 1 2019 ? 196.870 173.196 198.792 1.00 5.67  ? 2019 ASN A N     1 
ATOM   4509  C  CA    . ASN A 1 2019 ? 197.645 171.927 198.756 1.00 4.41  ? 2019 ASN A CA    1 
ATOM   4510  C  C     . ASN A 1 2019 ? 198.244 171.756 200.153 1.00 5.25  ? 2019 ASN A C     1 
ATOM   4511  O  O     . ASN A 1 2019 ? 199.332 172.315 200.408 1.00 13.56 ? 2019 ASN A O     1 
ATOM   4512  C  CB    . ASN A 1 2019 ? 198.680 171.917 197.640 1.00 4.15  ? 2019 ASN A CB    1 
ATOM   4513  C  CG    . ASN A 1 2019 ? 199.375 170.582 197.512 1.00 7.05  ? 2019 ASN A CG    1 
ATOM   4514  O  OD1   . ASN A 1 2019 ? 199.169 169.685 198.337 1.00 6.37  ? 2019 ASN A OD1   1 
ATOM   4515  N  ND2   . ASN A 1 2019 ? 200.207 170.434 196.491 1.00 8.07  ? 2019 ASN A ND2   1 
ATOM   4516  N  N     . PRO A 1 2020 ? 197.578 171.032 201.075 1.00 6.95  ? 2020 PRO A N     1 
ATOM   4517  C  CA    . PRO A 1 2020 ? 198.060 170.921 202.448 1.00 10.02 ? 2020 PRO A CA    1 
ATOM   4518  C  C     . PRO A 1 2020 ? 199.371 170.158 202.548 1.00 12.98 ? 2020 PRO A C     1 
ATOM   4519  O  O     . PRO A 1 2020 ? 199.970 170.134 203.638 1.00 16.50 ? 2020 PRO A O     1 
ATOM   4520  C  CB    . PRO A 1 2020 ? 196.904 170.191 203.162 1.00 7.98  ? 2020 PRO A CB    1 
ATOM   4521  C  CG    . PRO A 1 2020 ? 195.730 170.327 202.219 1.00 5.77  ? 2020 PRO A CG    1 
ATOM   4522  C  CD    . PRO A 1 2020 ? 196.345 170.308 200.833 1.00 6.46  ? 2020 PRO A CD    1 
ATOM   4523  N  N     . GLY A 1 2021 ? 199.809 169.551 201.444 1.00 13.70 ? 2021 GLY A N     1 
ATOM   4524  C  CA    . GLY A 1 2021 ? 201.047 168.751 201.454 1.00 10.66 ? 2021 GLY A CA    1 
ATOM   4525  C  C     . GLY A 1 2021 ? 202.271 169.600 201.185 1.00 15.83 ? 2021 GLY A C     1 
ATOM   4526  O  O     . GLY A 1 2021 ? 203.393 169.090 201.371 1.00 31.39 ? 2021 GLY A O     1 
ATOM   4527  N  N     . TYR A 1 2022 ? 202.076 170.846 200.753 1.00 12.15 ? 2022 TYR A N     1 
ATOM   4528  C  CA    . TYR A 1 2022 ? 203.231 171.716 200.405 1.00 10.72 ? 2022 TYR A CA    1 
ATOM   4529  C  C     . TYR A 1 2022 ? 203.891 172.187 201.700 1.00 11.13 ? 2022 TYR A C     1 
ATOM   4530  O  O     . TYR A 1 2022 ? 203.213 172.821 202.534 1.00 13.67 ? 2022 TYR A O     1 
ATOM   4531  C  CB    . TYR A 1 2022 ? 202.784 172.861 199.485 1.00 9.99  ? 2022 TYR A CB    1 
ATOM   4532  C  CG    . TYR A 1 2022 ? 202.912 172.547 198.001 1.00 12.46 ? 2022 TYR A CG    1 
ATOM   4533  C  CD1   . TYR A 1 2022 ? 203.002 171.235 197.550 1.00 12.68 ? 2022 TYR A CD1   1 
ATOM   4534  C  CD2   . TYR A 1 2022 ? 202.917 173.557 197.049 1.00 9.93  ? 2022 TYR A CD2   1 
ATOM   4535  C  CE1   . TYR A 1 2022 ? 203.117 170.941 196.202 1.00 11.85 ? 2022 TYR A CE1   1 
ATOM   4536  C  CE2   . TYR A 1 2022 ? 203.027 173.276 195.697 1.00 11.56 ? 2022 TYR A CE2   1 
ATOM   4537  C  CZ    . TYR A 1 2022 ? 203.124 171.964 195.272 1.00 16.51 ? 2022 TYR A CZ    1 
ATOM   4538  O  OH    . TYR A 1 2022 ? 203.231 171.678 193.942 1.00 14.04 ? 2022 TYR A OH    1 
ATOM   4539  N  N     . ALA A 1 2023 ? 205.178 171.870 201.869 1.00 15.43 ? 2023 ALA A N     1 
ATOM   4540  C  CA    . ALA A 1 2023 ? 205.925 172.324 203.065 1.00 17.43 ? 2023 ALA A CA    1 
ATOM   4541  C  C     . ALA A 1 2023 ? 206.152 173.835 202.981 1.00 13.89 ? 2023 ALA A C     1 
ATOM   4542  O  O     . ALA A 1 2023 ? 206.226 174.369 201.853 1.00 12.85 ? 2023 ALA A O     1 
ATOM   4543  C  CB    . ALA A 1 2023 ? 207.228 171.574 203.172 1.00 18.72 ? 2023 ALA A CB    1 
ATOM   4544  N  N     . GLY A 1 2024 ? 206.255 174.504 204.132 1.00 13.04 ? 2024 GLY A N     1 
ATOM   4545  C  CA    . GLY A 1 2024 ? 206.425 175.939 204.137 1.00 11.72 ? 2024 GLY A CA    1 
ATOM   4546  C  C     . GLY A 1 2024 ? 205.133 176.725 204.082 1.00 12.80 ? 2024 GLY A C     1 
ATOM   4547  O  O     . GLY A 1 2024 ? 205.154 177.939 204.315 1.00 17.73 ? 2024 GLY A O     1 
ATOM   4548  N  N     . ARG A 1 2025 ? 204.015 176.071 203.780 1.00 9.60  ? 2025 ARG A N     1 
ATOM   4549  C  CA    . ARG A 1 2025 ? 202.730 176.747 203.761 1.00 6.76  ? 2025 ARG A CA    1 
ATOM   4550  C  C     . ARG A 1 2025 ? 202.269 177.053 205.184 1.00 6.77  ? 2025 ARG A C     1 
ATOM   4551  O  O     . ARG A 1 2025 ? 202.751 176.480 206.164 1.00 15.69 ? 2025 ARG A O     1 
ATOM   4552  C  CB    . ARG A 1 2025 ? 201.685 175.897 203.039 1.00 9.96  ? 2025 ARG A CB    1 
ATOM   4553  C  CG    . ARG A 1 2025 ? 201.985 175.656 201.578 1.00 5.05  ? 2025 ARG A CG    1 
ATOM   4554  C  CD    . ARG A 1 2025 ? 201.681 176.882 200.739 1.00 4.47  ? 2025 ARG A CD    1 
ATOM   4555  N  NE    . ARG A 1 2025 ? 202.384 176.846 199.464 1.00 9.38  ? 2025 ARG A NE    1 
ATOM   4556  C  CZ    . ARG A 1 2025 ? 201.794 176.733 198.283 1.00 8.70  ? 2025 ARG A CZ    1 
ATOM   4557  N  NH1   . ARG A 1 2025 ? 200.483 176.607 198.174 1.00 8.81  ? 2025 ARG A NH1   1 
ATOM   4558  N  NH2   . ARG A 1 2025 ? 202.539 176.739 197.183 1.00 9.38  ? 2025 ARG A NH2   1 
ATOM   4559  N  N     . SER A 1 2026 ? 201.319 177.972 205.286 1.00 4.03  ? 2026 SER A N     1 
ATOM   4560  C  CA    . SER A 1 2026 ? 200.756 178.353 206.571 1.00 3.87  ? 2026 SER A CA    1 
ATOM   4561  C  C     . SER A 1 2026 ? 199.664 177.376 206.975 1.00 5.47  ? 2026 SER A C     1 
ATOM   4562  O  O     . SER A 1 2026 ? 198.837 176.971 206.154 1.00 7.08  ? 2026 SER A O     1 
ATOM   4563  C  CB    . SER A 1 2026 ? 200.185 179.768 206.514 1.00 2.81  ? 2026 SER A CB    1 
ATOM   4564  O  OG    . SER A 1 2026 ? 201.109 180.679 205.952 1.00 3.64  ? 2026 SER A OG    1 
ATOM   4565  N  N     . ASN A 1 2027 ? 199.667 176.997 208.248 1.00 6.24  ? 2027 ASN A N     1 
ATOM   4566  C  CA    . ASN A 1 2027 ? 198.597 176.180 208.794 1.00 5.44  ? 2027 ASN A CA    1 
ATOM   4567  C  C     . ASN A 1 2027 ? 197.408 177.065 209.136 1.00 4.37  ? 2027 ASN A C     1 
ATOM   4568  O  O     . ASN A 1 2027 ? 197.565 178.114 209.767 1.00 15.28 ? 2027 ASN A O     1 
ATOM   4569  C  CB    . ASN A 1 2027 ? 199.076 175.424 210.033 1.00 4.99  ? 2027 ASN A CB    1 
ATOM   4570  C  CG    . ASN A 1 2027 ? 200.135 174.394 209.709 1.00 10.79 ? 2027 ASN A CG    1 
ATOM   4571  O  OD1   . ASN A 1 2027 ? 199.973 173.588 208.791 1.00 10.92 ? 2027 ASN A OD1   1 
ATOM   4572  N  ND2   . ASN A 1 2027 ? 201.232 174.416 210.456 1.00 13.46 ? 2027 ASN A ND2   1 
ATOM   4573  N  N     . LEU A 1 2028 ? 196.229 176.657 208.704 1.00 2.77  ? 2028 LEU A N     1 
ATOM   4574  C  CA    . LEU A 1 2028 ? 195.030 177.419 209.016 1.00 3.18  ? 2028 LEU A CA    1 
ATOM   4575  C  C     . LEU A 1 2028 ? 194.665 177.231 210.484 1.00 6.30  ? 2028 LEU A C     1 
ATOM   4576  O  O     . LEU A 1 2028 ? 194.668 176.098 210.975 1.00 16.40 ? 2028 LEU A O     1 
ATOM   4577  C  CB    . LEU A 1 2028 ? 193.867 176.988 208.128 1.00 2.33  ? 2028 LEU A CB    1 
ATOM   4578  C  CG    . LEU A 1 2028 ? 193.658 177.744 206.815 1.00 2.90  ? 2028 LEU A CG    1 
ATOM   4579  C  CD1   . LEU A 1 2028 ? 194.890 177.678 205.921 1.00 0.79  ? 2028 LEU A CD1   1 
ATOM   4580  C  CD2   . LEU A 1 2028 ? 192.423 177.232 206.100 1.00 1.57  ? 2028 LEU A CD2   1 
ATOM   4581  N  N     . PRO A 1 2029 ? 194.369 178.303 211.214 1.00 5.15  ? 2029 PRO A N     1 
ATOM   4582  C  CA    . PRO A 1 2029 ? 193.844 178.138 212.573 1.00 2.93  ? 2029 PRO A CA    1 
ATOM   4583  C  C     . PRO A 1 2029 ? 192.496 177.433 212.551 1.00 2.10  ? 2029 PRO A C     1 
ATOM   4584  O  O     . PRO A 1 2029 ? 191.733 177.535 211.589 1.00 3.74  ? 2029 PRO A O     1 
ATOM   4585  C  CB    . PRO A 1 2029 ? 193.723 179.577 213.088 1.00 2.47  ? 2029 PRO A CB    1 
ATOM   4586  C  CG    . PRO A 1 2029 ? 193.716 180.432 211.863 1.00 1.67  ? 2029 PRO A CG    1 
ATOM   4587  C  CD    . PRO A 1 2029 ? 194.564 179.718 210.858 1.00 2.63  ? 2029 PRO A CD    1 
ATOM   4588  N  N     . ASP A 1 2030 ? 192.212 176.704 213.634 1.00 3.11  ? 2030 ASP A N     1 
ATOM   4589  C  CA    . ASP A 1 2030 ? 191.013 175.873 213.680 1.00 2.46  ? 2030 ASP A CA    1 
ATOM   4590  C  C     . ASP A 1 2030 ? 189.744 176.707 213.563 1.00 1.81  ? 2030 ASP A C     1 
ATOM   4591  O  O     . ASP A 1 2030 ? 188.771 176.279 212.932 1.00 2.95  ? 2030 ASP A O     1 
ATOM   4592  C  CB    . ASP A 1 2030 ? 190.992 175.048 214.965 1.00 4.40  ? 2030 ASP A CB    1 
ATOM   4593  C  CG    . ASP A 1 2030 ? 192.084 174.005 215.006 1.00 11.93 ? 2030 ASP A CG    1 
ATOM   4594  O  OD1   . ASP A 1 2030 ? 192.578 173.704 216.112 1.00 10.73 ? 2030 ASP A OD1   1 
ATOM   4595  O  OD2   . ASP A 1 2030 ? 192.452 173.481 213.933 1.00 19.27 ? 2030 ASP A OD2   1 
ATOM   4596  N  N     . ASN A 1 2031 ? 189.729 177.895 214.170 1.00 2.58  ? 2031 ASN A N     1 
ATOM   4597  C  CA    . ASN A 1 2031 ? 188.542 178.741 214.095 1.00 1.12  ? 2031 ASN A CA    1 
ATOM   4598  C  C     . ASN A 1 2031 ? 188.238 179.155 212.660 1.00 1.86  ? 2031 ASN A C     1 
ATOM   4599  O  O     . ASN A 1 2031 ? 187.074 179.388 212.317 1.00 2.37  ? 2031 ASN A O     1 
ATOM   4600  C  CB    . ASN A 1 2031 ? 188.713 179.970 214.989 1.00 0.79  ? 2031 ASN A CB    1 
ATOM   4601  C  CG    . ASN A 1 2031 ? 189.620 181.015 214.377 1.00 0.77  ? 2031 ASN A CG    1 
ATOM   4602  O  OD1   . ASN A 1 2031 ? 190.770 180.738 214.046 1.00 1.25  ? 2031 ASN A OD1   1 
ATOM   4603  N  ND2   . ASN A 1 2031 ? 189.105 182.228 214.228 1.00 0.60  ? 2031 ASN A ND2   1 
ATOM   4604  N  N     . LEU A 1 2032 ? 189.263 179.259 211.812 1.00 1.30  ? 2032 LEU A N     1 
ATOM   4605  C  CA    . LEU A 1 2032 ? 189.023 179.504 210.396 1.00 0.70  ? 2032 LEU A CA    1 
ATOM   4606  C  C     . LEU A 1 2032 ? 188.554 178.240 209.686 1.00 1.04  ? 2032 LEU A C     1 
ATOM   4607  O  O     . LEU A 1 2032 ? 187.664 178.294 208.830 1.00 0.52  ? 2032 LEU A O     1 
ATOM   4608  C  CB    . LEU A 1 2032 ? 190.287 180.053 209.735 1.00 1.27  ? 2032 LEU A CB    1 
ATOM   4609  C  CG    . LEU A 1 2032 ? 190.237 180.281 208.222 1.00 0.58  ? 2032 LEU A CG    1 
ATOM   4610  C  CD1   . LEU A 1 2032 ? 189.208 181.336 207.861 1.00 0.24  ? 2032 LEU A CD1   1 
ATOM   4611  C  CD2   . LEU A 1 2032 ? 191.608 180.660 207.692 1.00 0.36  ? 2032 LEU A CD2   1 
ATOM   4612  N  N     . LYS A 1 2033 ? 189.132 177.089 210.040 1.00 1.77  ? 2033 LYS A N     1 
ATOM   4613  C  CA    . LYS A 1 2033 ? 188.807 175.845 209.353 1.00 1.12  ? 2033 LYS A CA    1 
ATOM   4614  C  C     . LYS A 1 2033 ? 187.369 175.409 209.603 1.00 0.73  ? 2033 LYS A C     1 
ATOM   4615  O  O     . LYS A 1 2033 ? 186.756 174.789 208.728 1.00 0.73  ? 2033 LYS A O     1 
ATOM   4616  C  CB    . LYS A 1 2033 ? 189.778 174.741 209.774 1.00 1.54  ? 2033 LYS A CB    1 
ATOM   4617  C  CG    . LYS A 1 2033 ? 191.179 174.941 209.234 1.00 1.79  ? 2033 LYS A CG    1 
ATOM   4618  C  CD    . LYS A 1 2033 ? 191.983 173.656 209.219 1.00 3.69  ? 2033 LYS A CD    1 
ATOM   4619  C  CE    . LYS A 1 2033 ? 192.807 173.496 210.480 1.00 8.61  ? 2033 LYS A CE    1 
ATOM   4620  N  NZ    . LYS A 1 2033 ? 193.980 172.614 210.250 1.00 8.17  ? 2033 LYS A NZ    1 
ATOM   4621  N  N     . LYS A 1 2034 ? 186.809 175.725 210.773 1.00 1.06  ? 2034 LYS A N     1 
ATOM   4622  C  CA    . LYS A 1 2034 ? 185.428 175.342 211.046 1.00 1.24  ? 2034 LYS A CA    1 
ATOM   4623  C  C     . LYS A 1 2034 ? 184.437 176.101 210.173 1.00 0.62  ? 2034 LYS A C     1 
ATOM   4624  O  O     . LYS A 1 2034 ? 183.269 175.709 210.100 1.00 0.72  ? 2034 LYS A O     1 
ATOM   4625  C  CB    . LYS A 1 2034 ? 185.087 175.563 212.521 1.00 1.37  ? 2034 LYS A CB    1 
ATOM   4626  C  CG    . LYS A 1 2034 ? 185.101 177.011 212.960 1.00 2.46  ? 2034 LYS A CG    1 
ATOM   4627  C  CD    . LYS A 1 2034 ? 184.800 177.141 214.439 1.00 3.23  ? 2034 LYS A CD    1 
ATOM   4628  C  CE    . LYS A 1 2034 ? 184.798 178.596 214.879 1.00 9.18  ? 2034 LYS A CE    1 
ATOM   4629  N  NZ    . LYS A 1 2034 ? 184.509 178.721 216.335 1.00 9.61  ? 2034 LYS A NZ    1 
ATOM   4630  N  N     . LEU A 1 2035 ? 184.873 177.170 209.515 1.00 0.52  ? 2035 LEU A N     1 
ATOM   4631  C  CA    . LEU A 1 2035 ? 184.023 177.934 208.616 1.00 0.23  ? 2035 LEU A CA    1 
ATOM   4632  C  C     . LEU A 1 2035 ? 183.978 177.353 207.209 1.00 0.14  ? 2035 LEU A C     1 
ATOM   4633  O  O     . LEU A 1 2035 ? 183.243 177.872 206.364 1.00 0.08  ? 2035 LEU A O     1 
ATOM   4634  C  CB    . LEU A 1 2035 ? 184.497 179.387 208.553 1.00 0.44  ? 2035 LEU A CB    1 
ATOM   4635  C  CG    . LEU A 1 2035 ? 184.623 180.121 209.887 1.00 0.51  ? 2035 LEU A CG    1 
ATOM   4636  C  CD1   . LEU A 1 2035 ? 185.277 181.479 209.687 1.00 0.23  ? 2035 LEU A CD1   1 
ATOM   4637  C  CD2   . LEU A 1 2035 ? 183.266 180.264 210.555 1.00 0.87  ? 2035 LEU A CD2   1 
ATOM   4638  N  N     . PHE A 1 2036 ? 184.740 176.299 206.940 1.00 0.13  ? 2036 PHE A N     1 
ATOM   4639  C  CA    . PHE A 1 2036 ? 184.820 175.720 205.610 1.00 0.11  ? 2036 PHE A CA    1 
ATOM   4640  C  C     . PHE A 1 2036 ? 184.592 174.221 205.682 1.00 0.14  ? 2036 PHE A C     1 
ATOM   4641  O  O     . PHE A 1 2036 ? 185.044 173.556 206.617 1.00 0.43  ? 2036 PHE A O     1 
ATOM   4642  C  CB    . PHE A 1 2036 ? 186.181 176.008 204.962 1.00 0.06  ? 2036 PHE A CB    1 
ATOM   4643  C  CG    . PHE A 1 2036 ? 186.405 177.456 204.648 1.00 0.05  ? 2036 PHE A CG    1 
ATOM   4644  C  CD1   . PHE A 1 2036 ? 186.983 178.298 205.582 1.00 0.06  ? 2036 PHE A CD1   1 
ATOM   4645  C  CD2   . PHE A 1 2036 ? 186.028 177.979 203.424 1.00 0.05  ? 2036 PHE A CD2   1 
ATOM   4646  C  CE1   . PHE A 1 2036 ? 187.187 179.632 205.298 1.00 0.08  ? 2036 PHE A CE1   1 
ATOM   4647  C  CE2   . PHE A 1 2036 ? 186.228 179.313 203.136 1.00 0.05  ? 2036 PHE A CE2   1 
ATOM   4648  C  CZ    . PHE A 1 2036 ? 186.809 180.141 204.076 1.00 0.06  ? 2036 PHE A CZ    1 
ATOM   4649  N  N     . ARG A 1 2037 ? 183.878 173.695 204.693 1.00 0.25  ? 2037 ARG A N     1 
ATOM   4650  C  CA    . ARG A 1 2037 ? 183.740 172.259 204.515 1.00 0.18  ? 2037 ARG A CA    1 
ATOM   4651  C  C     . ARG A 1 2037 ? 184.783 171.796 203.507 1.00 0.06  ? 2037 ARG A C     1 
ATOM   4652  O  O     . ARG A 1 2037 ? 184.835 172.303 202.384 1.00 0.13  ? 2037 ARG A O     1 
ATOM   4653  C  CB    . ARG A 1 2037 ? 182.331 171.901 204.047 1.00 0.11  ? 2037 ARG A CB    1 
ATOM   4654  C  CG    . ARG A 1 2037 ? 181.258 172.179 205.086 1.00 0.77  ? 2037 ARG A CG    1 
ATOM   4655  C  CD    . ARG A 1 2037 ? 181.273 171.135 206.193 1.00 0.83  ? 2037 ARG A CD    1 
ATOM   4656  N  NE    . ARG A 1 2037 ? 180.774 169.843 205.737 1.00 2.91  ? 2037 ARG A NE    1 
ATOM   4657  C  CZ    . ARG A 1 2037 ? 179.534 169.613 205.327 1.00 5.59  ? 2037 ARG A CZ    1 
ATOM   4658  N  NH1   . ARG A 1 2037 ? 178.594 170.542 205.402 1.00 3.42  ? 2037 ARG A NH1   1 
ATOM   4659  N  NH2   . ARG A 1 2037 ? 179.223 168.414 204.845 1.00 4.13  ? 2037 ARG A NH2   1 
ATOM   4660  N  N     . SER A 1 2038 ? 185.618 170.850 203.915 1.00 0.10  ? 2038 SER A N     1 
ATOM   4661  C  CA    . SER A 1 2038 ? 186.754 170.424 203.117 1.00 0.09  ? 2038 SER A CA    1 
ATOM   4662  C  C     . SER A 1 2038 ? 186.443 169.123 202.391 1.00 0.15  ? 2038 SER A C     1 
ATOM   4663  O  O     . SER A 1 2038 ? 185.738 168.257 202.916 1.00 0.65  ? 2038 SER A O     1 
ATOM   4664  C  CB    . SER A 1 2038 ? 188.000 170.257 203.988 1.00 0.12  ? 2038 SER A CB    1 
ATOM   4665  O  OG    . SER A 1 2038 ? 187.872 169.152 204.863 1.00 1.00  ? 2038 SER A OG    1 
ATOM   4666  N  N     . LEU A 1 2039 ? 186.965 168.999 201.174 1.00 0.15  ? 2039 LEU A N     1 
ATOM   4667  C  CA    . LEU A 1 2039 ? 186.858 167.774 200.395 1.00 0.15  ? 2039 LEU A CA    1 
ATOM   4668  C  C     . LEU A 1 2039 ? 188.207 167.454 199.778 1.00 0.15  ? 2039 LEU A C     1 
ATOM   4669  O  O     . LEU A 1 2039 ? 188.849 168.332 199.195 1.00 0.10  ? 2039 LEU A O     1 
ATOM   4670  C  CB    . LEU A 1 2039 ? 185.804 167.897 199.293 1.00 0.22  ? 2039 LEU A CB    1 
ATOM   4671  C  CG    . LEU A 1 2039 ? 185.637 166.602 198.497 1.00 0.53  ? 2039 LEU A CG    1 
ATOM   4672  C  CD1   . LEU A 1 2039 ? 185.136 165.471 199.371 1.00 0.76  ? 2039 LEU A CD1   1 
ATOM   4673  C  CD2   . LEU A 1 2039 ? 184.720 166.816 197.340 1.00 0.34  ? 2039 LEU A CD2   1 
ATOM   4674  N  N     . ALA A 1 2040 ? 188.631 166.201 199.903 1.00 0.25  ? 2040 ALA A N     1 
ATOM   4675  C  CA    . ALA A 1 2040 ? 189.894 165.765 199.323 1.00 0.30  ? 2040 ALA A CA    1 
ATOM   4676  C  C     . ALA A 1 2040 ? 189.696 165.448 197.845 1.00 0.35  ? 2040 ALA A C     1 
ATOM   4677  O  O     . ALA A 1 2040 ? 188.895 164.578 197.491 1.00 0.32  ? 2040 ALA A O     1 
ATOM   4678  C  CB    . ALA A 1 2040 ? 190.432 164.545 200.067 1.00 0.36  ? 2040 ALA A CB    1 
ATOM   4679  N  N     . MET A 1 2041 ? 190.414 166.162 196.990 1.00 0.42  ? 2041 MET A N     1 
ATOM   4680  C  CA    . MET A 1 2041 ? 190.441 165.901 195.555 1.00 0.56  ? 2041 MET A CA    1 
ATOM   4681  C  C     . MET A 1 2041 ? 191.864 165.468 195.225 1.00 0.66  ? 2041 MET A C     1 
ATOM   4682  O  O     . MET A 1 2041 ? 192.743 166.306 195.008 1.00 2.12  ? 2041 MET A O     1 
ATOM   4683  C  CB    . MET A 1 2041 ? 190.011 167.132 194.760 1.00 0.52  ? 2041 MET A CB    1 
ATOM   4684  C  CG    . MET A 1 2041 ? 188.595 167.599 195.071 1.00 0.32  ? 2041 MET A CG    1 
ATOM   4685  S  SD    . MET A 1 2041 ? 188.008 168.935 194.015 1.00 13.17 ? 2041 MET A SD    1 
ATOM   4686  C  CE    . MET A 1 2041 ? 188.200 168.208 192.390 1.00 0.39  ? 2041 MET A CE    1 
ATOM   4687  N  N     . THR A 1 2042 ? 192.091 164.159 195.208 1.00 1.07  ? 2042 THR A N     1 
ATOM   4688  C  CA    . THR A 1 2042 ? 193.433 163.601 195.091 1.00 1.48  ? 2042 THR A CA    1 
ATOM   4689  C  C     . THR A 1 2042 ? 193.650 162.796 193.824 1.00 2.68  ? 2042 THR A C     1 
ATOM   4690  O  O     . THR A 1 2042 ? 194.711 162.905 193.208 1.00 7.08  ? 2042 THR A O     1 
ATOM   4691  C  CB    . THR A 1 2042 ? 193.744 162.720 196.315 1.00 2.46  ? 2042 THR A CB    1 
ATOM   4692  O  OG1   . THR A 1 2042 ? 193.437 163.437 197.515 1.00 1.77  ? 2042 THR A OG1   1 
ATOM   4693  C  CG2   . THR A 1 2042 ? 195.211 162.330 196.334 1.00 3.33  ? 2042 THR A CG2   1 
ATOM   4694  N  N     . LYS A 1 2043 ? 192.675 161.984 193.410 1.00 4.61  ? 2043 LYS A N     1 
ATOM   4695  C  CA    . LYS A 1 2043 ? 192.799 161.117 192.240 1.00 2.91  ? 2043 LYS A CA    1 
ATOM   4696  C  C     . LYS A 1 2043 ? 191.737 161.492 191.216 1.00 3.08  ? 2043 LYS A C     1 
ATOM   4697  O  O     . LYS A 1 2043 ? 190.596 161.008 191.284 1.00 4.38  ? 2043 LYS A O     1 
ATOM   4698  C  CB    . LYS A 1 2043 ? 192.678 159.645 192.630 1.00 4.17  ? 2043 LYS A CB    1 
ATOM   4699  C  CG    . LYS A 1 2043 ? 193.750 159.155 193.584 1.00 9.55  ? 2043 LYS A CG    1 
ATOM   4700  C  CD    . LYS A 1 2043 ? 195.120 159.142 192.928 1.00 17.76 ? 2043 LYS A CD    1 
ATOM   4701  C  CE    . LYS A 1 2043 ? 196.173 158.576 193.865 1.00 18.43 ? 2043 LYS A CE    1 
ATOM   4702  N  NZ    . LYS A 1 2043 ? 197.531 158.593 193.255 1.00 27.99 ? 2043 LYS A NZ    1 
ATOM   4703  N  N     . PRO A 1 2044 ? 192.063 162.348 190.251 1.00 3.94  ? 2044 PRO A N     1 
ATOM   4704  C  CA    . PRO A 1 2044 ? 191.108 162.644 189.178 1.00 1.50  ? 2044 PRO A CA    1 
ATOM   4705  C  C     . PRO A 1 2044 ? 190.853 161.423 188.311 1.00 2.89  ? 2044 PRO A C     1 
ATOM   4706  O  O     . PRO A 1 2044 ? 191.718 160.560 188.138 1.00 3.65  ? 2044 PRO A O     1 
ATOM   4707  C  CB    . PRO A 1 2044 ? 191.793 163.760 188.380 1.00 1.66  ? 2044 PRO A CB    1 
ATOM   4708  C  CG    . PRO A 1 2044 ? 192.925 164.231 189.229 1.00 1.11  ? 2044 PRO A CG    1 
ATOM   4709  C  CD    . PRO A 1 2044 ? 193.320 163.093 190.098 1.00 1.97  ? 2044 PRO A CD    1 
ATOM   4710  N  N     . ASP A 1 2045 ? 189.642 161.357 187.761 1.00 2.67  ? 2045 ASP A N     1 
ATOM   4711  C  CA    . ASP A 1 2045 ? 189.215 160.229 186.934 1.00 1.85  ? 2045 ASP A CA    1 
ATOM   4712  C  C     . ASP A 1 2045 ? 189.676 160.476 185.498 1.00 2.15  ? 2045 ASP A C     1 
ATOM   4713  O  O     . ASP A 1 2045 ? 188.920 160.911 184.627 1.00 1.78  ? 2045 ASP A O     1 
ATOM   4714  C  CB    . ASP A 1 2045 ? 187.707 160.043 187.034 1.00 1.92  ? 2045 ASP A CB    1 
ATOM   4715  C  CG    . ASP A 1 2045 ? 187.227 159.963 188.474 1.00 5.47  ? 2045 ASP A CG    1 
ATOM   4716  O  OD1   . ASP A 1 2045 ? 187.835 159.210 189.263 1.00 7.47  ? 2045 ASP A OD1   1 
ATOM   4717  O  OD2   . ASP A 1 2045 ? 186.246 160.650 188.820 1.00 3.83  ? 2045 ASP A OD2   1 
ATOM   4718  N  N     . ARG A 1 2046 ? 190.956 160.173 185.258 1.00 2.04  ? 2046 ARG A N     1 
ATOM   4719  C  CA    . ARG A 1 2046 ? 191.599 160.553 184.003 1.00 1.11  ? 2046 ARG A CA    1 
ATOM   4720  C  C     . ARG A 1 2046 ? 190.984 159.841 182.804 1.00 1.58  ? 2046 ARG A C     1 
ATOM   4721  O  O     . ARG A 1 2046 ? 190.769 160.461 181.757 1.00 1.58  ? 2046 ARG A O     1 
ATOM   4722  C  CB    . ARG A 1 2046 ? 193.096 160.267 184.073 1.00 1.29  ? 2046 ARG A CB    1 
ATOM   4723  C  CG    . ARG A 1 2046 ? 193.849 161.138 185.051 1.00 1.68  ? 2046 ARG A CG    1 
ATOM   4724  C  CD    . ARG A 1 2046 ? 195.321 160.789 185.061 1.00 4.45  ? 2046 ARG A CD    1 
ATOM   4725  N  NE    . ARG A 1 2046 ? 196.066 161.603 186.012 1.00 7.45  ? 2046 ARG A NE    1 
ATOM   4726  C  CZ    . ARG A 1 2046 ? 197.361 161.465 186.259 1.00 13.73 ? 2046 ARG A CZ    1 
ATOM   4727  N  NH1   . ARG A 1 2046 ? 198.090 160.554 185.634 1.00 18.46 ? 2046 ARG A NH1   1 
ATOM   4728  N  NH2   . ARG A 1 2046 ? 197.938 162.260 187.153 1.00 13.74 ? 2046 ARG A NH2   1 
ATOM   4729  N  N     . GLN A 1 2047 ? 190.702 158.544 182.931 1.00 1.69  ? 2047 GLN A N     1 
ATOM   4730  C  CA    . GLN A 1 2047 ? 190.220 157.789 181.779 1.00 1.95  ? 2047 GLN A CA    1 
ATOM   4731  C  C     . GLN A 1 2047 ? 188.832 158.252 181.351 1.00 3.78  ? 2047 GLN A C     1 
ATOM   4732  O  O     . GLN A 1 2047 ? 188.506 158.226 180.158 1.00 5.04  ? 2047 GLN A O     1 
ATOM   4733  C  CB    . GLN A 1 2047 ? 190.246 156.287 182.085 1.00 4.94  ? 2047 GLN A CB    1 
ATOM   4734  C  CG    . GLN A 1 2047 ? 189.346 155.817 183.219 1.00 17.03 ? 2047 GLN A CG    1 
ATOM   4735  C  CD    . GLN A 1 2047 ? 187.915 155.569 182.783 1.00 15.99 ? 2047 GLN A CD    1 
ATOM   4736  O  OE1   . GLN A 1 2047 ? 187.658 155.212 181.633 1.00 15.01 ? 2047 GLN A OE1   1 
ATOM   4737  N  NE2   . GLN A 1 2047 ? 186.975 155.752 183.704 1.00 14.33 ? 2047 GLN A NE2   1 
ATOM   4738  N  N     . LEU A 1 2048 ? 188.003 158.688 182.300 1.00 2.91  ? 2048 LEU A N     1 
ATOM   4739  C  CA    . LEU A 1 2048 ? 186.690 159.214 181.940 1.00 1.28  ? 2048 LEU A CA    1 
ATOM   4740  C  C     . LEU A 1 2048 ? 186.810 160.579 181.270 1.00 1.89  ? 2048 LEU A C     1 
ATOM   4741  O  O     . LEU A 1 2048 ? 186.109 160.862 180.292 1.00 5.01  ? 2048 LEU A O     1 
ATOM   4742  C  CB    . LEU A 1 2048 ? 185.792 159.293 183.175 1.00 2.77  ? 2048 LEU A CB    1 
ATOM   4743  C  CG    . LEU A 1 2048 ? 184.384 159.836 182.915 1.00 2.13  ? 2048 LEU A CG    1 
ATOM   4744  C  CD1   . LEU A 1 2048 ? 183.648 158.973 181.900 1.00 0.47  ? 2048 LEU A CD1   1 
ATOM   4745  C  CD2   . LEU A 1 2048 ? 183.595 159.944 184.205 1.00 1.33  ? 2048 LEU A CD2   1 
ATOM   4746  N  N     . ILE A 1 2049 ? 187.691 161.441 181.784 1.00 1.14  ? 2049 ILE A N     1 
ATOM   4747  C  CA    . ILE A 1 2049 ? 187.907 162.747 181.162 1.00 1.08  ? 2049 ILE A CA    1 
ATOM   4748  C  C     . ILE A 1 2049 ? 188.421 162.576 179.739 1.00 1.82  ? 2049 ILE A C     1 
ATOM   4749  O  O     . ILE A 1 2049 ? 187.958 163.245 178.809 1.00 5.93  ? 2049 ILE A O     1 
ATOM   4750  C  CB    . ILE A 1 2049 ? 188.872 163.599 182.009 1.00 1.06  ? 2049 ILE A CB    1 
ATOM   4751  C  CG1   . ILE A 1 2049 ? 188.322 163.806 183.419 1.00 0.88  ? 2049 ILE A CG1   1 
ATOM   4752  C  CG2   . ILE A 1 2049 ? 189.153 164.927 181.327 1.00 0.39  ? 2049 ILE A CG2   1 
ATOM   4753  C  CD1   . ILE A 1 2049 ? 189.300 164.459 184.371 1.00 0.41  ? 2049 ILE A CD1   1 
ATOM   4754  N  N     . ALA A 1 2050 ? 189.388 161.677 179.550 1.00 1.65  ? 2050 ALA A N     1 
ATOM   4755  C  CA    . ALA A 1 2050 ? 189.939 161.451 178.220 1.00 0.94  ? 2050 ALA A CA    1 
ATOM   4756  C  C     . ALA A 1 2050 ? 188.886 160.893 177.271 1.00 1.50  ? 2050 ALA A C     1 
ATOM   4757  O  O     . ALA A 1 2050 ? 188.814 161.298 176.106 1.00 2.66  ? 2050 ALA A O     1 
ATOM   4758  C  CB    . ALA A 1 2050 ? 191.142 160.514 178.303 1.00 1.10  ? 2050 ALA A CB    1 
ATOM   4759  N  N     . GLN A 1 2051 ? 188.056 159.965 177.754 1.00 2.70  ? 2051 GLN A N     1 
ATOM   4760  C  CA    . GLN A 1 2051 ? 187.070 159.330 176.886 1.00 2.22  ? 2051 GLN A CA    1 
ATOM   4761  C  C     . GLN A 1 2051 ? 186.013 160.328 176.430 1.00 2.37  ? 2051 GLN A C     1 
ATOM   4762  O  O     . GLN A 1 2051 ? 185.642 160.361 175.252 1.00 5.03  ? 2051 GLN A O     1 
ATOM   4763  C  CB    . GLN A 1 2051 ? 186.432 158.143 177.611 1.00 4.15  ? 2051 GLN A CB    1 
ATOM   4764  C  CG    . GLN A 1 2051 ? 185.527 157.276 176.747 1.00 6.67  ? 2051 GLN A CG    1 
ATOM   4765  C  CD    . GLN A 1 2051 ? 184.104 157.792 176.670 1.00 14.94 ? 2051 GLN A CD    1 
ATOM   4766  O  OE1   . GLN A 1 2051 ? 183.608 158.428 177.599 1.00 12.11 ? 2051 GLN A OE1   1 
ATOM   4767  N  NE2   . GLN A 1 2051 ? 183.440 157.526 175.551 1.00 12.72 ? 2051 GLN A NE2   1 
ATOM   4768  N  N     . VAL A 1 2052 ? 185.518 161.156 177.351 1.00 3.92  ? 2052 VAL A N     1 
ATOM   4769  C  CA    . VAL A 1 2052 ? 184.461 162.103 177.007 1.00 2.55  ? 2052 VAL A CA    1 
ATOM   4770  C  C     . VAL A 1 2052 ? 184.996 163.210 176.108 1.00 2.53  ? 2052 VAL A C     1 
ATOM   4771  O  O     . VAL A 1 2052 ? 184.332 163.624 175.151 1.00 4.60  ? 2052 VAL A O     1 
ATOM   4772  C  CB    . VAL A 1 2052 ? 183.811 162.662 178.287 1.00 1.70  ? 2052 VAL A CB    1 
ATOM   4773  C  CG1   . VAL A 1 2052 ? 182.781 163.728 177.949 1.00 0.92  ? 2052 VAL A CG1   1 
ATOM   4774  C  CG2   . VAL A 1 2052 ? 183.167 161.539 179.077 1.00 2.27  ? 2052 VAL A CG2   1 
ATOM   4775  N  N     . MET A 1 2053 ? 186.202 163.711 176.395 1.00 2.37  ? 2053 MET A N     1 
ATOM   4776  C  CA    . MET A 1 2053 ? 186.773 164.775 175.573 1.00 2.69  ? 2053 MET A CA    1 
ATOM   4777  C  C     . MET A 1 2053 ? 187.028 164.309 174.145 1.00 4.77  ? 2053 MET A C     1 
ATOM   4778  O  O     . MET A 1 2053 ? 186.721 165.026 173.187 1.00 7.56  ? 2053 MET A O     1 
ATOM   4779  C  CB    . MET A 1 2053 ? 188.069 165.293 176.192 1.00 3.62  ? 2053 MET A CB    1 
ATOM   4780  C  CG    . MET A 1 2053 ? 187.875 166.250 177.344 1.00 3.14  ? 2053 MET A CG    1 
ATOM   4781  S  SD    . MET A 1 2053 ? 189.452 166.669 178.097 1.00 27.24 ? 2053 MET A SD    1 
ATOM   4782  C  CE    . MET A 1 2053 ? 190.106 167.782 176.855 1.00 4.88  ? 2053 MET A CE    1 
ATOM   4783  N  N     . LEU A 1 2054 ? 187.598 163.114 173.982 1.00 2.71  ? 2054 LEU A N     1 
ATOM   4784  C  CA    . LEU A 1 2054 ? 187.838 162.595 172.640 1.00 3.26  ? 2054 LEU A CA    1 
ATOM   4785  C  C     . LEU A 1 2054 ? 186.534 162.287 171.920 1.00 6.25  ? 2054 LEU A C     1 
ATOM   4786  O  O     . LEU A 1 2054 ? 186.442 162.461 170.701 1.00 11.18 ? 2054 LEU A O     1 
ATOM   4787  C  CB    . LEU A 1 2054 ? 188.723 161.351 172.702 1.00 3.68  ? 2054 LEU A CB    1 
ATOM   4788  C  CG    . LEU A 1 2054 ? 190.180 161.581 173.101 1.00 4.09  ? 2054 LEU A CG    1 
ATOM   4789  C  CD1   . LEU A 1 2054 ? 190.870 160.265 173.405 1.00 3.38  ? 2054 LEU A CD1   1 
ATOM   4790  C  CD2   . LEU A 1 2054 ? 190.928 162.348 172.020 1.00 3.13  ? 2054 LEU A CD2   1 
ATOM   4791  N  N     . TYR A 1 2055 ? 185.520 161.831 172.657 1.00 3.89  ? 2055 TYR A N     1 
ATOM   4792  C  CA    . TYR A 1 2055 ? 184.221 161.561 172.057 1.00 4.62  ? 2055 TYR A CA    1 
ATOM   4793  C  C     . TYR A 1 2055 ? 183.505 162.848 171.664 1.00 3.62  ? 2055 TYR A C     1 
ATOM   4794  O  O     . TYR A 1 2055 ? 182.798 162.878 170.651 1.00 4.60  ? 2055 TYR A O     1 
ATOM   4795  C  CB    . TYR A 1 2055 ? 183.377 160.732 173.025 1.00 5.17  ? 2055 TYR A CB    1 
ATOM   4796  C  CG    . TYR A 1 2055 ? 181.961 160.460 172.579 1.00 3.43  ? 2055 TYR A CG    1 
ATOM   4797  C  CD1   . TYR A 1 2055 ? 181.697 159.593 171.530 1.00 3.14  ? 2055 TYR A CD1   1 
ATOM   4798  C  CD2   . TYR A 1 2055 ? 180.886 161.040 173.234 1.00 4.61  ? 2055 TYR A CD2   1 
ATOM   4799  C  CE1   . TYR A 1 2055 ? 180.403 159.333 171.128 1.00 6.43  ? 2055 TYR A CE1   1 
ATOM   4800  C  CE2   . TYR A 1 2055 ? 179.589 160.783 172.844 1.00 6.62  ? 2055 TYR A CE2   1 
ATOM   4801  C  CZ    . TYR A 1 2055 ? 179.352 159.928 171.790 1.00 11.52 ? 2055 TYR A CZ    1 
ATOM   4802  O  OH    . TYR A 1 2055 ? 178.061 159.673 171.399 1.00 15.46 ? 2055 TYR A OH    1 
ATOM   4803  N  N     . SER A 1 2056 ? 183.676 163.917 172.446 1.00 4.56  ? 2056 SER A N     1 
ATOM   4804  C  CA    . SER A 1 2056 ? 183.050 165.192 172.111 1.00 3.88  ? 2056 SER A CA    1 
ATOM   4805  C  C     . SER A 1 2056 ? 183.759 165.891 170.959 1.00 6.78  ? 2056 SER A C     1 
ATOM   4806  O  O     . SER A 1 2056 ? 183.148 166.716 170.273 1.00 10.39 ? 2056 SER A O     1 
ATOM   4807  C  CB    . SER A 1 2056 ? 183.022 166.102 173.338 1.00 3.73  ? 2056 SER A CB    1 
ATOM   4808  O  OG    . SER A 1 2056 ? 184.330 166.390 173.791 1.00 6.92  ? 2056 SER A OG    1 
ATOM   4809  N  N     . GLN A 1 2057 ? 185.036 165.582 170.735 1.00 7.76  ? 2057 GLN A N     1 
ATOM   4810  C  CA    . GLN A 1 2057 ? 185.783 166.175 169.638 1.00 4.29  ? 2057 GLN A CA    1 
ATOM   4811  C  C     . GLN A 1 2057 ? 185.534 165.481 168.306 1.00 7.81  ? 2057 GLN A C     1 
ATOM   4812  O  O     . GLN A 1 2057 ? 185.938 166.013 167.266 1.00 12.93 ? 2057 GLN A O     1 
ATOM   4813  C  CB    . GLN A 1 2057 ? 187.280 166.159 169.951 1.00 5.99  ? 2057 GLN A CB    1 
ATOM   4814  C  CG    . GLN A 1 2057 ? 187.778 167.388 170.692 1.00 4.59  ? 2057 GLN A CG    1 
ATOM   4815  C  CD    . GLN A 1 2057 ? 188.915 167.072 171.647 1.00 10.09 ? 2057 GLN A CD    1 
ATOM   4816  O  OE1   . GLN A 1 2057 ? 189.589 166.051 171.509 1.00 11.76 ? 2057 GLN A OE1   1 
ATOM   4817  N  NE2   . GLN A 1 2057 ? 189.135 167.950 172.618 1.00 9.17  ? 2057 GLN A NE2   1 
ATOM   4818  N  N     . GLY A 1 2058 ? 184.884 164.322 168.305 1.00 6.71  ? 2058 GLY A N     1 
ATOM   4819  C  CA    . GLY A 1 2058 ? 184.575 163.612 167.084 1.00 5.10  ? 2058 GLY A CA    1 
ATOM   4820  C  C     . GLY A 1 2058 ? 185.428 162.398 166.785 1.00 6.46  ? 2058 GLY A C     1 
ATOM   4821  O  O     . GLY A 1 2058 ? 185.325 161.855 165.680 1.00 13.86 ? 2058 GLY A O     1 
ATOM   4822  N  N     . PHE A 1 2059 ? 186.264 161.955 167.719 1.00 6.12  ? 2059 PHE A N     1 
ATOM   4823  C  CA    . PHE A 1 2059 ? 187.062 160.754 167.503 1.00 6.06  ? 2059 PHE A CA    1 
ATOM   4824  C  C     . PHE A 1 2059 ? 186.167 159.523 167.591 1.00 8.97  ? 2059 PHE A C     1 
ATOM   4825  O  O     . PHE A 1 2059 ? 185.532 159.284 168.622 1.00 14.60 ? 2059 PHE A O     1 
ATOM   4826  C  CB    . PHE A 1 2059 ? 188.186 160.672 168.532 1.00 6.26  ? 2059 PHE A CB    1 
ATOM   4827  C  CG    . PHE A 1 2059 ? 189.295 161.658 168.307 1.00 5.96  ? 2059 PHE A CG    1 
ATOM   4828  C  CD1   . PHE A 1 2059 ? 189.198 162.952 168.790 1.00 6.16  ? 2059 PHE A CD1   1 
ATOM   4829  C  CD2   . PHE A 1 2059 ? 190.444 161.286 167.630 1.00 6.56  ? 2059 PHE A CD2   1 
ATOM   4830  C  CE1   . PHE A 1 2059 ? 190.220 163.857 168.594 1.00 4.99  ? 2059 PHE A CE1   1 
ATOM   4831  C  CE2   . PHE A 1 2059 ? 191.468 162.188 167.431 1.00 8.47  ? 2059 PHE A CE2   1 
ATOM   4832  C  CZ    . PHE A 1 2059 ? 191.356 163.475 167.913 1.00 4.52  ? 2059 PHE A CZ    1 
ATOM   4833  N  N     . ARG A 1 2060 ? 186.116 158.741 166.512 1.00 9.33  ? 2060 ARG A N     1 
ATOM   4834  C  CA    . ARG A 1 2060 ? 185.247 157.568 166.496 1.00 10.77 ? 2060 ARG A CA    1 
ATOM   4835  C  C     . ARG A 1 2060 ? 185.733 156.488 167.455 1.00 11.56 ? 2060 ARG A C     1 
ATOM   4836  O  O     . ARG A 1 2060 ? 184.917 155.776 168.050 1.00 18.41 ? 2060 ARG A O     1 
ATOM   4837  C  CB    . ARG A 1 2060 ? 185.139 157.011 165.078 1.00 17.09 ? 2060 ARG A CB    1 
ATOM   4838  C  CG    . ARG A 1 2060 ? 184.150 155.861 164.937 1.00 31.01 ? 2060 ARG A CG    1 
ATOM   4839  C  CD    . ARG A 1 2060 ? 184.041 155.398 163.493 1.00 26.81 ? 2060 ARG A CD    1 
ATOM   4840  N  NE    . ARG A 1 2060 ? 185.295 154.835 163.008 1.00 28.91 ? 2060 ARG A NE    1 
ATOM   4841  C  CZ    . ARG A 1 2060 ? 186.041 155.381 162.058 1.00 32.99 ? 2060 ARG A CZ    1 
ATOM   4842  N  NH1   . ARG A 1 2060 ? 185.691 156.514 161.472 1.00 34.63 ? 2060 ARG A NH1   1 
ATOM   4843  N  NH2   . ARG A 1 2060 ? 187.167 154.775 161.689 1.00 30.16 ? 2060 ARG A NH2   1 
ATOM   4844  N  N     . THR A 1 2061 ? 187.047 156.357 167.628 1.00 12.96 ? 2061 THR A N     1 
ATOM   4845  C  CA    . THR A 1 2061 ? 187.643 155.350 168.505 1.00 8.63  ? 2061 THR A CA    1 
ATOM   4846  C  C     . THR A 1 2061 ? 188.027 155.933 169.855 1.00 10.97 ? 2061 THR A C     1 
ATOM   4847  O  O     . THR A 1 2061 ? 189.068 155.583 170.419 1.00 14.27 ? 2061 THR A O     1 
ATOM   4848  C  CB    . THR A 1 2061 ? 188.857 154.713 167.835 1.00 10.84 ? 2061 THR A CB    1 
ATOM   4849  O  OG1   . THR A 1 2061 ? 189.723 155.737 167.334 1.00 16.03 ? 2061 THR A OG1   1 
ATOM   4850  C  CG2   . THR A 1 2061 ? 188.422 153.821 166.686 1.00 10.17 ? 2061 THR A CG2   1 
ATOM   4851  N  N     . ALA A 1 2062 ? 187.197 156.836 170.391 1.00 12.82 ? 2062 ALA A N     1 
ATOM   4852  C  CA    . ALA A 1 2062 ? 187.535 157.529 171.630 1.00 7.76  ? 2062 ALA A CA    1 
ATOM   4853  C  C     . ALA A 1 2062 ? 187.753 156.556 172.781 1.00 10.48 ? 2062 ALA A C     1 
ATOM   4854  O  O     . ALA A 1 2062 ? 188.646 156.759 173.612 1.00 15.71 ? 2062 ALA A O     1 
ATOM   4855  C  CB    . ALA A 1 2062 ? 186.440 158.535 171.981 1.00 6.50  ? 2062 ALA A CB    1 
ATOM   4856  N  N     . GLU A 1 2063 ? 186.943 155.496 172.857 1.00 13.62 ? 2063 GLU A N     1 
ATOM   4857  C  CA    . GLU A 1 2063 ? 187.126 154.512 173.919 1.00 13.57 ? 2063 GLU A CA    1 
ATOM   4858  C  C     . GLU A 1 2063 ? 188.463 153.794 173.786 1.00 10.19 ? 2063 GLU A C     1 
ATOM   4859  O  O     . GLU A 1 2063 ? 189.158 153.572 174.784 1.00 13.54 ? 2063 GLU A O     1 
ATOM   4860  C  CB    . GLU A 1 2063 ? 185.973 153.508 173.913 1.00 19.83 ? 2063 GLU A CB    1 
ATOM   4861  C  CG    . GLU A 1 2063 ? 184.632 154.106 174.293 1.00 24.31 ? 2063 GLU A CG    1 
ATOM   4862  C  CD    . GLU A 1 2063 ? 183.508 153.087 174.259 1.00 32.31 ? 2063 GLU A CD    1 
ATOM   4863  O  OE1   . GLU A 1 2063 ? 183.752 151.946 173.817 1.00 32.55 ? 2063 GLU A OE1   1 
ATOM   4864  O  OE2   . GLU A 1 2063 ? 182.382 153.431 174.675 1.00 31.55 ? 2063 GLU A OE2   1 
ATOM   4865  N  N     . VAL A 1 2064 ? 188.837 153.417 172.563 1.00 10.91 ? 2064 VAL A N     1 
ATOM   4866  C  CA    . VAL A 1 2064 ? 190.135 152.785 172.350 1.00 10.75 ? 2064 VAL A CA    1 
ATOM   4867  C  C     . VAL A 1 2064 ? 191.261 153.762 172.655 1.00 10.59 ? 2064 VAL A C     1 
ATOM   4868  O  O     . VAL A 1 2064 ? 192.241 153.414 173.322 1.00 11.66 ? 2064 VAL A O     1 
ATOM   4869  C  CB    . VAL A 1 2064 ? 190.232 152.232 170.917 1.00 10.61 ? 2064 VAL A CB    1 
ATOM   4870  C  CG1   . VAL A 1 2064 ? 191.628 151.695 170.648 1.00 14.71 ? 2064 VAL A CG1   1 
ATOM   4871  C  CG2   . VAL A 1 2064 ? 189.191 151.153 170.694 1.00 8.63  ? 2064 VAL A CG2   1 
ATOM   4872  N  N     . LEU A 1 2065 ? 191.139 155.004 172.179 1.00 10.29 ? 2065 LEU A N     1 
ATOM   4873  C  CA    . LEU A 1 2065 ? 192.188 155.993 172.405 1.00 9.12  ? 2065 LEU A CA    1 
ATOM   4874  C  C     . LEU A 1 2065 ? 192.338 156.322 173.885 1.00 7.05  ? 2065 LEU A C     1 
ATOM   4875  O  O     . LEU A 1 2065 ? 193.461 156.465 174.383 1.00 11.71 ? 2065 LEU A O     1 
ATOM   4876  C  CB    . LEU A 1 2065 ? 191.893 157.258 171.601 1.00 9.40  ? 2065 LEU A CB    1 
ATOM   4877  C  CG    . LEU A 1 2065 ? 191.922 157.103 170.081 1.00 7.86  ? 2065 LEU A CG    1 
ATOM   4878  C  CD1   . LEU A 1 2065 ? 191.529 158.402 169.408 1.00 9.76  ? 2065 LEU A CD1   1 
ATOM   4879  C  CD2   . LEU A 1 2065 ? 193.288 156.647 169.615 1.00 9.46  ? 2065 LEU A CD2   1 
ATOM   4880  N  N     . ALA A 1 2066 ? 191.221 156.448 174.604 1.00 7.94  ? 2066 ALA A N     1 
ATOM   4881  C  CA    . ALA A 1 2066 ? 191.291 156.768 176.026 1.00 8.57  ? 2066 ALA A CA    1 
ATOM   4882  C  C     . ALA A 1 2066 ? 191.916 155.630 176.823 1.00 10.13 ? 2066 ALA A C     1 
ATOM   4883  O  O     . ALA A 1 2066 ? 192.664 155.872 177.777 1.00 9.25  ? 2066 ALA A O     1 
ATOM   4884  C  CB    . ALA A 1 2066 ? 189.898 157.098 176.558 1.00 6.43  ? 2066 ALA A CB    1 
ATOM   4885  N  N     . ASN A 1 2067 ? 191.621 154.383 176.449 1.00 11.48 ? 2067 ASN A N     1 
ATOM   4886  C  CA    . ASN A 1 2067 ? 192.202 153.234 177.135 1.00 11.35 ? 2067 ASN A CA    1 
ATOM   4887  C  C     . ASN A 1 2067 ? 193.693 153.085 176.882 1.00 10.35 ? 2067 ASN A C     1 
ATOM   4888  O  O     . ASN A 1 2067 ? 194.340 152.285 177.565 1.00 21.44 ? 2067 ASN A O     1 
ATOM   4889  C  CB    . ASN A 1 2067 ? 191.487 151.947 176.722 1.00 14.99 ? 2067 ASN A CB    1 
ATOM   4890  C  CG    . ASN A 1 2067 ? 190.153 151.778 177.408 1.00 19.25 ? 2067 ASN A CG    1 
ATOM   4891  O  OD1   . ASN A 1 2067 ? 190.070 151.779 178.635 1.00 20.75 ? 2067 ASN A OD1   1 
ATOM   4892  N  ND2   . ASN A 1 2067 ? 189.098 151.621 176.619 1.00 18.18 ? 2067 ASN A ND2   1 
ATOM   4893  N  N     . LYS A 1 2068 ? 194.248 153.814 175.921 1.00 7.27  ? 2068 LYS A N     1 
ATOM   4894  C  CA    . LYS A 1 2068 ? 195.677 153.784 175.641 1.00 7.43  ? 2068 LYS A CA    1 
ATOM   4895  C  C     . LYS A 1 2068 ? 196.415 155.013 176.141 1.00 7.73  ? 2068 LYS A C     1 
ATOM   4896  O  O     . LYS A 1 2068 ? 197.504 154.882 176.702 1.00 7.07  ? 2068 LYS A O     1 
ATOM   4897  C  CB    . LYS A 1 2068 ? 195.915 153.636 174.134 1.00 8.69  ? 2068 LYS A CB    1 
ATOM   4898  C  CG    . LYS A 1 2068 ? 195.291 152.400 173.522 1.00 12.08 ? 2068 LYS A CG    1 
ATOM   4899  C  CD    . LYS A 1 2068 ? 195.537 152.343 172.028 1.00 8.23  ? 2068 LYS A CD    1 
ATOM   4900  C  CE    . LYS A 1 2068 ? 195.281 150.949 171.485 1.00 13.83 ? 2068 LYS A CE    1 
ATOM   4901  N  NZ    . LYS A 1 2068 ? 196.119 149.930 172.172 1.00 15.60 ? 2068 LYS A NZ    1 
ATOM   4902  N  N     . ILE A 1 2069 ? 195.844 156.205 175.958 1.00 5.57  ? 2069 ILE A N     1 
ATOM   4903  C  CA    . ILE A 1 2069 ? 196.563 157.430 176.290 1.00 4.69  ? 2069 ILE A CA    1 
ATOM   4904  C  C     . ILE A 1 2069 ? 196.744 157.590 177.797 1.00 5.90  ? 2069 ILE A C     1 
ATOM   4905  O  O     . ILE A 1 2069 ? 197.787 158.071 178.252 1.00 6.80  ? 2069 ILE A O     1 
ATOM   4906  C  CB    . ILE A 1 2069 ? 195.860 158.650 175.658 1.00 5.22  ? 2069 ILE A CB    1 
ATOM   4907  C  CG1   . ILE A 1 2069 ? 196.768 159.877 175.740 1.00 8.52  ? 2069 ILE A CG1   1 
ATOM   4908  C  CG2   . ILE A 1 2069 ? 194.508 158.918 176.305 1.00 3.08  ? 2069 ILE A CG2   1 
ATOM   4909  C  CD1   . ILE A 1 2069 ? 198.017 159.741 174.921 1.00 4.49  ? 2069 ILE A CD1   1 
ATOM   4910  N  N     . VAL A 1 2070 ? 195.756 157.195 178.593 1.00 4.55  ? 2070 VAL A N     1 
ATOM   4911  C  CA    . VAL A 1 2070 ? 195.818 157.387 180.040 1.00 4.65  ? 2070 VAL A CA    1 
ATOM   4912  C  C     . VAL A 1 2070 ? 196.829 156.421 180.656 1.00 5.22  ? 2070 VAL A C     1 
ATOM   4913  O  O     . VAL A 1 2070 ? 197.659 156.856 181.468 1.00 4.50  ? 2070 VAL A O     1 
ATOM   4914  C  CB    . VAL A 1 2070 ? 194.427 157.252 180.682 1.00 4.41  ? 2070 VAL A CB    1 
ATOM   4915  C  CG1   . VAL A 1 2070 ? 194.520 157.381 182.193 1.00 1.77  ? 2070 VAL A CG1   1 
ATOM   4916  C  CG2   . VAL A 1 2070 ? 193.490 158.299 180.115 1.00 3.10  ? 2070 VAL A CG2   1 
ATOM   4917  N  N     . PRO A 1 2071 ? 196.813 155.121 180.330 1.00 5.52  ? 2071 PRO A N     1 
ATOM   4918  C  CA    . PRO A 1 2071 ? 197.915 154.261 180.793 1.00 5.87  ? 2071 PRO A CA    1 
ATOM   4919  C  C     . PRO A 1 2071 ? 199.272 154.679 180.260 1.00 6.02  ? 2071 PRO A C     1 
ATOM   4920  O  O     . PRO A 1 2071 ? 200.280 154.487 180.951 1.00 7.32  ? 2071 PRO A O     1 
ATOM   4921  C  CB    . PRO A 1 2071 ? 197.509 152.872 180.281 1.00 5.43  ? 2071 PRO A CB    1 
ATOM   4922  C  CG    . PRO A 1 2071 ? 196.046 152.945 180.152 1.00 9.00  ? 2071 PRO A CG    1 
ATOM   4923  C  CD    . PRO A 1 2071 ? 195.781 154.323 179.646 1.00 5.26  ? 2071 PRO A CD    1 
ATOM   4924  N  N     . PHE A 1 2072 ? 199.330 155.241 179.050 1.00 5.02  ? 2072 PHE A N     1 
ATOM   4925  C  CA    . PHE A 1 2072 ? 200.609 155.670 178.493 1.00 6.14  ? 2072 PHE A CA    1 
ATOM   4926  C  C     . PHE A 1 2072 ? 201.241 156.765 179.341 1.00 8.45  ? 2072 PHE A C     1 
ATOM   4927  O  O     . PHE A 1 2072 ? 202.456 156.762 179.569 1.00 11.58 ? 2072 PHE A O     1 
ATOM   4928  C  CB    . PHE A 1 2072 ? 200.423 156.149 177.054 1.00 5.26  ? 2072 PHE A CB    1 
ATOM   4929  C  CG    . PHE A 1 2072 ? 201.632 156.824 176.483 1.00 9.58  ? 2072 PHE A CG    1 
ATOM   4930  C  CD1   . PHE A 1 2072 ? 202.697 156.079 176.008 1.00 7.77  ? 2072 PHE A CD1   1 
ATOM   4931  C  CD2   . PHE A 1 2072 ? 201.707 158.207 176.419 1.00 8.01  ? 2072 PHE A CD2   1 
ATOM   4932  C  CE1   . PHE A 1 2072 ? 203.811 156.698 175.485 1.00 6.86  ? 2072 PHE A CE1   1 
ATOM   4933  C  CE2   . PHE A 1 2072 ? 202.819 158.829 175.897 1.00 5.59  ? 2072 PHE A CE2   1 
ATOM   4934  C  CZ    . PHE A 1 2072 ? 203.871 158.076 175.428 1.00 7.07  ? 2072 PHE A CZ    1 
ATOM   4935  N  N     . PHE A 1 2073 ? 200.432 157.719 179.808 1.00 6.61  ? 2073 PHE A N     1 
ATOM   4936  C  CA    . PHE A 1 2073 ? 200.948 158.759 180.689 1.00 5.86  ? 2073 PHE A CA    1 
ATOM   4937  C  C     . PHE A 1 2073 ? 201.420 158.167 182.011 1.00 8.65  ? 2073 PHE A C     1 
ATOM   4938  O  O     . PHE A 1 2073 ? 202.416 158.619 182.583 1.00 14.94 ? 2073 PHE A O     1 
ATOM   4939  C  CB    . PHE A 1 2073 ? 199.876 159.823 180.924 1.00 5.31  ? 2073 PHE A CB    1 
ATOM   4940  C  CG    . PHE A 1 2073 ? 199.960 160.984 179.982 1.00 3.55  ? 2073 PHE A CG    1 
ATOM   4941  C  CD1   . PHE A 1 2073 ? 199.612 160.839 178.651 1.00 3.19  ? 2073 PHE A CD1   1 
ATOM   4942  C  CD2   . PHE A 1 2073 ? 200.379 162.224 180.428 1.00 3.49  ? 2073 PHE A CD2   1 
ATOM   4943  C  CE1   . PHE A 1 2073 ? 199.690 161.905 177.781 1.00 3.72  ? 2073 PHE A CE1   1 
ATOM   4944  C  CE2   . PHE A 1 2073 ? 200.456 163.295 179.563 1.00 3.05  ? 2073 PHE A CE2   1 
ATOM   4945  C  CZ    . PHE A 1 2073 ? 200.111 163.135 178.238 1.00 3.57  ? 2073 PHE A CZ    1 
ATOM   4946  N  N     . LYS A 1 2074 ? 200.701 157.160 182.513 1.00 9.57  ? 2074 LYS A N     1 
ATOM   4947  C  CA    . LYS A 1 2074 ? 201.127 156.472 183.726 1.00 9.23  ? 2074 LYS A CA    1 
ATOM   4948  C  C     . LYS A 1 2074 ? 202.465 155.774 183.508 1.00 8.60  ? 2074 LYS A C     1 
ATOM   4949  O  O     . LYS A 1 2074 ? 203.351 155.829 184.368 1.00 9.62  ? 2074 LYS A O     1 
ATOM   4950  C  CB    . LYS A 1 2074 ? 200.044 155.475 184.149 1.00 11.02 ? 2074 LYS A CB    1 
ATOM   4951  C  CG    . LYS A 1 2074 ? 200.412 154.489 185.256 1.00 13.27 ? 2074 LYS A CG    1 
ATOM   4952  C  CD    . LYS A 1 2074 ? 201.094 155.164 186.437 1.00 16.45 ? 2074 LYS A CD    1 
ATOM   4953  C  CE    . LYS A 1 2074 ? 200.882 154.372 187.717 1.00 21.16 ? 2074 LYS A CE    1 
ATOM   4954  N  NZ    . LYS A 1 2074 ? 201.275 152.944 187.565 1.00 23.18 ? 2074 LYS A NZ    1 
ATOM   4955  N  N     . LEU A 1 2075 ? 202.636 155.128 182.351 1.00 8.23  ? 2075 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 2075 ? 203.897 154.457 182.050 1.00 7.77  ? 2075 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 2075 ? 205.047 155.450 181.939 1.00 11.58 ? 2075 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 2075 ? 206.161 155.168 182.393 1.00 20.27 ? 2075 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 2075 ? 203.767 153.644 180.763 1.00 10.92 ? 2075 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 2075 ? 203.080 152.283 180.859 1.00 14.09 ? 2075 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 2075 ? 202.384 151.946 179.549 1.00 11.03 ? 2075 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 2075 ? 204.080 151.199 181.232 1.00 19.61 ? 2075 LEU A CD2   1 
ATOM   4963  N  N     . CYS A 1 2076 ? 204.800 156.615 181.336 1.00 10.88 ? 2076 CYS A N     1 
ATOM   4964  C  CA    . CYS A 1 2076 ? 205.862 157.609 181.187 1.00 10.70 ? 2076 CYS A CA    1 
ATOM   4965  C  C     . CYS A 1 2076 ? 206.359 158.095 182.542 1.00 7.53  ? 2076 CYS A C     1 
ATOM   4966  O  O     . CYS A 1 2076 ? 207.561 158.306 182.731 1.00 8.20  ? 2076 CYS A O     1 
ATOM   4967  C  CB    . CYS A 1 2076 ? 205.372 158.784 180.343 1.00 5.44  ? 2076 CYS A CB    1 
ATOM   4968  S  SG    . CYS A 1 2076 ? 205.283 158.432 178.578 1.00 14.32 ? 2076 CYS A SG    1 
ATOM   4969  N  N     . ASP A 1 2077 ? 205.446 158.273 183.498 1.00 10.07 ? 2077 ASP A N     1 
ATOM   4970  C  CA    . ASP A 1 2077 ? 205.831 158.722 184.829 1.00 6.99  ? 2077 ASP A CA    1 
ATOM   4971  C  C     . ASP A 1 2077 ? 206.719 157.718 185.551 1.00 8.24  ? 2077 ASP A C     1 
ATOM   4972  O  O     . ASP A 1 2077 ? 207.417 158.098 186.497 1.00 15.61 ? 2077 ASP A O     1 
ATOM   4973  C  CB    . ASP A 1 2077 ? 204.583 159.001 185.664 1.00 8.21  ? 2077 ASP A CB    1 
ATOM   4974  C  CG    . ASP A 1 2077 ? 204.870 159.872 186.864 1.00 15.30 ? 2077 ASP A CG    1 
ATOM   4975  O  OD1   . ASP A 1 2077 ? 205.752 160.750 186.766 1.00 21.89 ? 2077 ASP A OD1   1 
ATOM   4976  O  OD2   . ASP A 1 2077 ? 204.217 159.675 187.910 1.00 26.87 ? 2077 ASP A OD2   1 
ATOM   4977  N  N     . GLU A 1 2078 ? 206.715 156.457 185.132 1.00 12.88 ? 2078 GLU A N     1 
ATOM   4978  C  CA    . GLU A 1 2078 ? 207.494 155.415 185.789 1.00 11.52 ? 2078 GLU A CA    1 
ATOM   4979  C  C     . GLU A 1 2078 ? 208.597 154.837 184.919 1.00 12.03 ? 2078 GLU A C     1 
ATOM   4980  O  O     . GLU A 1 2078 ? 209.695 154.589 185.417 1.00 20.90 ? 2078 GLU A O     1 
ATOM   4981  C  CB    . GLU A 1 2078 ? 206.570 154.285 186.249 1.00 13.80 ? 2078 GLU A CB    1 
ATOM   4982  C  CG    . GLU A 1 2078 ? 205.920 154.542 187.593 1.00 17.10 ? 2078 GLU A CG    1 
ATOM   4983  C  CD    . GLU A 1 2078 ? 204.523 153.969 187.684 1.00 24.30 ? 2078 GLU A CD    1 
ATOM   4984  O  OE1   . GLU A 1 2078 ? 204.061 153.369 186.693 1.00 23.66 ? 2078 GLU A OE1   1 
ATOM   4985  O  OE2   . GLU A 1 2078 ? 203.887 154.120 188.747 1.00 21.72 ? 2078 GLU A OE2   1 
ATOM   4986  N  N     . GLN A 1 2079 ? 208.337 154.619 183.629 1.00 10.28 ? 2079 GLN A N     1 
ATOM   4987  C  CA    . GLN A 1 2079 ? 209.348 154.016 182.768 1.00 12.77 ? 2079 GLN A CA    1 
ATOM   4988  C  C     . GLN A 1 2079 ? 210.468 155.002 182.452 1.00 18.17 ? 2079 GLN A C     1 
ATOM   4989  O  O     . GLN A 1 2079 ? 211.638 154.613 182.366 1.00 28.19 ? 2079 GLN A O     1 
ATOM   4990  C  CB    . GLN A 1 2079 ? 208.700 153.504 181.481 1.00 13.59 ? 2079 GLN A CB    1 
ATOM   4991  C  CG    . GLN A 1 2079 ? 207.661 152.412 181.697 1.00 18.28 ? 2079 GLN A CG    1 
ATOM   4992  C  CD    . GLN A 1 2079 ? 208.250 151.128 182.243 1.00 19.07 ? 2079 GLN A CD    1 
ATOM   4993  O  OE1   . GLN A 1 2079 ? 209.338 150.717 181.854 1.00 22.18 ? 2079 GLN A OE1   1 
ATOM   4994  N  NE2   . GLN A 1 2079 ? 207.529 150.489 183.154 1.00 25.48 ? 2079 GLN A NE2   1 
ATOM   4995  N  N     . LEU A 1 2080 ? 210.132 156.276 182.269 1.00 15.20 ? 2080 LEU A N     1 
ATOM   4996  C  CA    . LEU A 1 2080 ? 211.127 157.291 181.958 1.00 11.40 ? 2080 LEU A CA    1 
ATOM   4997  C  C     . LEU A 1 2080 ? 211.890 157.703 183.213 1.00 12.42 ? 2080 LEU A C     1 
ATOM   4998  O  O     . LEU A 1 2080 ? 211.422 157.535 184.342 1.00 20.15 ? 2080 LEU A O     1 
ATOM   4999  C  CB    . LEU A 1 2080 ? 210.470 158.523 181.335 1.00 7.64  ? 2080 LEU A CB    1 
ATOM   5000  C  CG    . LEU A 1 2080 ? 209.652 158.332 180.061 1.00 5.16  ? 2080 LEU A CG    1 
ATOM   5001  C  CD1   . LEU A 1 2080 ? 209.027 159.651 179.638 1.00 11.77 ? 2080 LEU A CD1   1 
ATOM   5002  C  CD2   . LEU A 1 2080 ? 210.510 157.755 178.954 1.00 7.21  ? 2080 LEU A CD2   1 
ATOM   5003  N  N     . SER A 1 2081 ? 213.072 158.269 182.997 1.00 9.64  ? 2081 SER A N     1 
ATOM   5004  C  CA    . SER A 1 2081 ? 213.901 158.722 184.102 1.00 11.11 ? 2081 SER A CA    1 
ATOM   5005  C  C     . SER A 1 2081 ? 213.218 159.861 184.856 1.00 10.41 ? 2081 SER A C     1 
ATOM   5006  O  O     . SER A 1 2081 ? 212.297 160.511 184.359 1.00 11.95 ? 2081 SER A O     1 
ATOM   5007  C  CB    . SER A 1 2081 ? 215.270 159.177 183.601 1.00 13.05 ? 2081 SER A CB    1 
ATOM   5008  O  OG    . SER A 1 2081 ? 215.210 160.489 183.067 1.00 7.32  ? 2081 SER A OG    1 
ATOM   5009  N  N     . SER A 1 2082 ? 213.688 160.096 186.075 1.00 11.93 ? 2082 SER A N     1 
ATOM   5010  C  CA    . SER A 1 2082 ? 213.109 161.109 186.945 1.00 9.57  ? 2082 SER A CA    1 
ATOM   5011  C  C     . SER A 1 2082 ? 213.830 162.434 186.729 1.00 10.41 ? 2082 SER A C     1 
ATOM   5012  O  O     . SER A 1 2082 ? 215.050 162.521 186.911 1.00 8.62  ? 2082 SER A O     1 
ATOM   5013  C  CB    . SER A 1 2082 ? 213.196 160.677 188.406 1.00 13.77 ? 2082 SER A CB    1 
ATOM   5014  O  OG    . SER A 1 2082 ? 212.423 159.512 188.633 1.00 17.42 ? 2082 SER A OG    1 
ATOM   5015  N  N     . GLN A 1 2083 ? 213.077 163.458 186.333 1.00 13.08 ? 2083 GLN A N     1 
ATOM   5016  C  CA    . GLN A 1 2083 ? 213.600 164.800 186.135 1.00 4.84  ? 2083 GLN A CA    1 
ATOM   5017  C  C     . GLN A 1 2083 ? 212.671 165.803 186.803 1.00 2.56  ? 2083 GLN A C     1 
ATOM   5018  O  O     . GLN A 1 2083 ? 211.459 165.590 186.883 1.00 2.65  ? 2083 GLN A O     1 
ATOM   5019  C  CB    . GLN A 1 2083 ? 213.747 165.132 184.643 1.00 2.80  ? 2083 GLN A CB    1 
ATOM   5020  C  CG    . GLN A 1 2083 ? 214.454 164.061 183.827 1.00 2.11  ? 2083 GLN A CG    1 
ATOM   5021  C  CD    . GLN A 1 2083 ? 215.957 164.067 184.018 1.00 3.35  ? 2083 GLN A CD    1 
ATOM   5022  O  OE1   . GLN A 1 2083 ? 216.513 164.967 184.644 1.00 7.37  ? 2083 GLN A OE1   1 
ATOM   5023  N  NE2   . GLN A 1 2083 ? 216.624 163.053 183.484 1.00 3.80  ? 2083 GLN A NE2   1 
ATOM   5024  N  N     . SER A 1 2084 ? 213.250 166.904 187.287 1.00 6.58  ? 2084 SER A N     1 
ATOM   5025  C  CA    . SER A 1 2084 ? 212.448 167.930 187.945 1.00 5.44  ? 2084 SER A CA    1 
ATOM   5026  C  C     . SER A 1 2084 ? 211.508 168.643 186.980 1.00 3.58  ? 2084 SER A C     1 
ATOM   5027  O  O     . SER A 1 2084 ? 210.491 169.191 187.417 1.00 5.75  ? 2084 SER A O     1 
ATOM   5028  C  CB    . SER A 1 2084 ? 213.352 168.947 188.641 1.00 4.17  ? 2084 SER A CB    1 
ATOM   5029  O  OG    . SER A 1 2084 ? 214.426 169.343 187.808 1.00 19.36 ? 2084 SER A OG    1 
ATOM   5030  N  N     . HIS A 1 2085 ? 211.816 168.642 185.684 1.00 1.87  ? 2085 HIS A N     1 
ATOM   5031  C  CA    . HIS A 1 2085 ? 210.986 169.290 184.679 1.00 2.26  ? 2085 HIS A CA    1 
ATOM   5032  C  C     . HIS A 1 2085 ? 210.051 168.311 183.977 1.00 3.03  ? 2085 HIS A C     1 
ATOM   5033  O  O     . HIS A 1 2085 ? 209.627 168.570 182.847 1.00 7.04  ? 2085 HIS A O     1 
ATOM   5034  C  CB    . HIS A 1 2085 ? 211.864 170.009 183.656 1.00 1.31  ? 2085 HIS A CB    1 
ATOM   5035  C  CG    . HIS A 1 2085 ? 212.725 169.092 182.845 1.00 1.29  ? 2085 HIS A CG    1 
ATOM   5036  N  ND1   . HIS A 1 2085 ? 213.923 168.593 183.306 1.00 0.98  ? 2085 HIS A ND1   1 
ATOM   5037  C  CD2   . HIS A 1 2085 ? 212.563 168.589 181.599 1.00 1.52  ? 2085 HIS A CD2   1 
ATOM   5038  C  CE1   . HIS A 1 2085 ? 214.460 167.818 182.382 1.00 0.68  ? 2085 HIS A CE1   1 
ATOM   5039  N  NE2   . HIS A 1 2085 ? 213.654 167.799 181.336 1.00 0.74  ? 2085 HIS A NE2   1 
ATOM   5040  N  N     . TYR A 1 2086 ? 209.722 167.198 184.621 1.00 2.15  ? 2086 TYR A N     1 
ATOM   5041  C  CA    . TYR A 1 2086 ? 208.841 166.192 184.049 1.00 2.08  ? 2086 TYR A CA    1 
ATOM   5042  C  C     . TYR A 1 2086 ? 207.472 166.281 184.708 1.00 4.27  ? 2086 TYR A C     1 
ATOM   5043  O  O     . TYR A 1 2086 ? 207.369 166.286 185.937 1.00 7.91  ? 2086 TYR A O     1 
ATOM   5044  C  CB    . TYR A 1 2086 ? 209.419 164.788 184.229 1.00 2.54  ? 2086 TYR A CB    1 
ATOM   5045  C  CG    . TYR A 1 2086 ? 210.395 164.372 183.154 1.00 3.00  ? 2086 TYR A CG    1 
ATOM   5046  C  CD1   . TYR A 1 2086 ? 210.962 165.307 182.300 1.00 2.22  ? 2086 TYR A CD1   1 
ATOM   5047  C  CD2   . TYR A 1 2086 ? 210.762 163.041 183.005 1.00 3.25  ? 2086 TYR A CD2   1 
ATOM   5048  C  CE1   . TYR A 1 2086 ? 211.855 164.929 181.321 1.00 1.48  ? 2086 TYR A CE1   1 
ATOM   5049  C  CE2   . TYR A 1 2086 ? 211.658 162.655 182.031 1.00 2.90  ? 2086 TYR A CE2   1 
ATOM   5050  C  CZ    . TYR A 1 2086 ? 212.202 163.601 181.191 1.00 3.26  ? 2086 TYR A CZ    1 
ATOM   5051  O  OH    . TYR A 1 2086 ? 213.094 163.220 180.218 1.00 2.03  ? 2086 TYR A OH    1 
ATOM   5052  N  N     . ASP A 1 2087 ? 206.429 166.362 183.887 1.00 4.41  ? 2087 ASP A N     1 
ATOM   5053  C  CA    . ASP A 1 2087 ? 205.059 166.335 184.375 1.00 5.71  ? 2087 ASP A CA    1 
ATOM   5054  C  C     . ASP A 1 2087 ? 204.224 165.467 183.451 1.00 4.65  ? 2087 ASP A C     1 
ATOM   5055  O  O     . ASP A 1 2087 ? 204.228 165.667 182.233 1.00 6.17  ? 2087 ASP A O     1 
ATOM   5056  C  CB    . ASP A 1 2087 ? 204.453 167.739 184.454 1.00 9.48  ? 2087 ASP A CB    1 
ATOM   5057  C  CG    . ASP A 1 2087 ? 203.026 167.723 184.955 1.00 15.26 ? 2087 ASP A CG    1 
ATOM   5058  O  OD1   . ASP A 1 2087 ? 202.789 167.186 186.059 1.00 14.36 ? 2087 ASP A OD1   1 
ATOM   5059  O  OD2   . ASP A 1 2087 ? 202.136 168.221 184.234 1.00 11.62 ? 2087 ASP A OD2   1 
ATOM   5060  N  N     . PHE A 1 2088 ? 203.516 164.507 184.032 1.00 4.44  ? 2088 PHE A N     1 
ATOM   5061  C  CA    . PHE A 1 2088 ? 202.627 163.625 183.293 1.00 4.26  ? 2088 PHE A CA    1 
ATOM   5062  C  C     . PHE A 1 2088 ? 201.274 163.553 183.979 1.00 5.05  ? 2088 PHE A C     1 
ATOM   5063  O  O     . PHE A 1 2088 ? 200.602 162.519 183.973 1.00 11.90 ? 2088 PHE A O     1 
ATOM   5064  C  CB    . PHE A 1 2088 ? 203.246 162.239 183.139 1.00 6.92  ? 2088 PHE A CB    1 
ATOM   5065  C  CG    . PHE A 1 2088 ? 204.581 162.250 182.453 1.00 7.02  ? 2088 PHE A CG    1 
ATOM   5066  C  CD1   . PHE A 1 2088 ? 204.669 162.422 181.083 1.00 5.92  ? 2088 PHE A CD1   1 
ATOM   5067  C  CD2   . PHE A 1 2088 ? 205.750 162.098 183.179 1.00 6.16  ? 2088 PHE A CD2   1 
ATOM   5068  C  CE1   . PHE A 1 2088 ? 205.898 162.438 180.449 1.00 7.20  ? 2088 PHE A CE1   1 
ATOM   5069  C  CE2   . PHE A 1 2088 ? 206.979 162.113 182.551 1.00 4.03  ? 2088 PHE A CE2   1 
ATOM   5070  C  CZ    . PHE A 1 2088 ? 207.053 162.285 181.186 1.00 5.37  ? 2088 PHE A CZ    1 
ATOM   5071  N  N     . GLY A 1 2089 ? 200.858 164.664 184.577 1.00 3.10  ? 2089 GLY A N     1 
ATOM   5072  C  CA    . GLY A 1 2089 ? 199.609 164.743 185.302 1.00 3.28  ? 2089 GLY A CA    1 
ATOM   5073  C  C     . GLY A 1 2089 ? 198.443 165.122 184.416 1.00 2.43  ? 2089 GLY A C     1 
ATOM   5074  O  O     . GLY A 1 2089 ? 198.485 164.986 183.191 1.00 4.68  ? 2089 GLY A O     1 
ATOM   5075  N  N     . LEU A 1 2090 ? 197.379 165.608 185.058 1.00 2.09  ? 2090 LEU A N     1 
ATOM   5076  C  CA    . LEU A 1 2090 ? 196.144 165.892 184.334 1.00 1.49  ? 2090 LEU A CA    1 
ATOM   5077  C  C     . LEU A 1 2090 ? 196.299 167.085 183.396 1.00 1.33  ? 2090 LEU A C     1 
ATOM   5078  O  O     . LEU A 1 2090 ? 195.704 167.102 182.314 1.00 0.99  ? 2090 LEU A O     1 
ATOM   5079  C  CB    . LEU A 1 2090 ? 194.998 166.118 185.318 1.00 1.86  ? 2090 LEU A CB    1 
ATOM   5080  C  CG    . LEU A 1 2090 ? 193.607 166.205 184.689 1.00 1.72  ? 2090 LEU A CG    1 
ATOM   5081  C  CD1   . LEU A 1 2090 ? 193.352 165.010 183.786 1.00 0.95  ? 2090 LEU A CD1   1 
ATOM   5082  C  CD2   . LEU A 1 2090 ? 192.543 166.297 185.762 1.00 0.72  ? 2090 LEU A CD2   1 
ATOM   5083  N  N     . ARG A 1 2091 ? 197.083 168.094 183.790 1.00 1.30  ? 2091 ARG A N     1 
ATOM   5084  C  CA    . ARG A 1 2091 ? 197.340 169.213 182.885 1.00 0.87  ? 2091 ARG A CA    1 
ATOM   5085  C  C     . ARG A 1 2091 ? 198.028 168.741 181.613 1.00 1.18  ? 2091 ARG A C     1 
ATOM   5086  O  O     . ARG A 1 2091 ? 197.660 169.158 180.508 1.00 1.03  ? 2091 ARG A O     1 
ATOM   5087  C  CB    . ARG A 1 2091 ? 198.191 170.282 183.570 1.00 0.71  ? 2091 ARG A CB    1 
ATOM   5088  C  CG    . ARG A 1 2091 ? 197.523 171.029 184.701 1.00 1.30  ? 2091 ARG A CG    1 
ATOM   5089  C  CD    . ARG A 1 2091 ? 198.446 172.124 185.226 1.00 2.23  ? 2091 ARG A CD    1 
ATOM   5090  N  NE    . ARG A 1 2091 ? 198.083 172.579 186.561 1.00 4.96  ? 2091 ARG A NE    1 
ATOM   5091  C  CZ    . ARG A 1 2091 ? 196.953 173.199 186.872 1.00 1.30  ? 2091 ARG A CZ    1 
ATOM   5092  N  NH1   . ARG A 1 2091 ? 196.085 173.564 185.943 1.00 0.99  ? 2091 ARG A NH1   1 
ATOM   5093  N  NH2   . ARG A 1 2091 ? 196.696 173.476 188.145 1.00 0.80  ? 2091 ARG A NH2   1 
ATOM   5094  N  N     . ALA A 1 2092 ? 199.031 167.874 181.750 1.00 1.04  ? 2092 ALA A N     1 
ATOM   5095  C  CA    . ALA A 1 2092 ? 199.710 167.328 180.579 1.00 1.00  ? 2092 ALA A CA    1 
ATOM   5096  C  C     . ALA A 1 2092 ? 198.753 166.507 179.726 1.00 0.99  ? 2092 ALA A C     1 
ATOM   5097  O  O     . ALA A 1 2092 ? 198.752 166.613 178.496 1.00 1.08  ? 2092 ALA A O     1 
ATOM   5098  C  CB    . ALA A 1 2092 ? 200.909 166.488 181.017 1.00 2.69  ? 2092 ALA A CB    1 
ATOM   5099  N  N     . LEU A 1 2093 ? 197.923 165.680 180.370 1.00 1.29  ? 2093 LEU A N     1 
ATOM   5100  C  CA    . LEU A 1 2093 ? 196.925 164.909 179.637 1.00 1.06  ? 2093 LEU A CA    1 
ATOM   5101  C  C     . LEU A 1 2093 ? 195.915 165.823 178.956 1.00 0.81  ? 2093 LEU A C     1 
ATOM   5102  O  O     . LEU A 1 2093 ? 195.560 165.617 177.793 1.00 0.97  ? 2093 LEU A O     1 
ATOM   5103  C  CB    . LEU A 1 2093 ? 196.216 163.936 180.581 1.00 0.93  ? 2093 LEU A CB    1 
ATOM   5104  C  CG    . LEU A 1 2093 ? 195.102 163.099 179.947 1.00 0.61  ? 2093 LEU A CG    1 
ATOM   5105  C  CD1   . LEU A 1 2093 ? 195.657 162.182 178.864 1.00 1.07  ? 2093 LEU A CD1   1 
ATOM   5106  C  CD2   . LEU A 1 2093 ? 194.352 162.307 181.002 1.00 0.94  ? 2093 LEU A CD2   1 
ATOM   5107  N  N     . LYS A 1 2094 ? 195.447 166.848 179.674 1.00 0.91  ? 2094 LYS A N     1 
ATOM   5108  C  CA    . LYS A 1 2094 ? 194.500 167.794 179.092 1.00 0.79  ? 2094 LYS A CA    1 
ATOM   5109  C  C     . LYS A 1 2094 ? 195.108 168.517 177.899 1.00 1.04  ? 2094 LYS A C     1 
ATOM   5110  O  O     . LYS A 1 2094 ? 194.431 168.745 176.890 1.00 1.13  ? 2094 LYS A O     1 
ATOM   5111  C  CB    . LYS A 1 2094 ? 194.051 168.797 180.155 1.00 1.68  ? 2094 LYS A CB    1 
ATOM   5112  C  CG    . LYS A 1 2094 ? 192.842 169.627 179.769 1.00 1.24  ? 2094 LYS A CG    1 
ATOM   5113  C  CD    . LYS A 1 2094 ? 191.551 168.886 180.051 1.00 2.00  ? 2094 LYS A CD    1 
ATOM   5114  C  CE    . LYS A 1 2094 ? 190.343 169.770 179.795 1.00 2.26  ? 2094 LYS A CE    1 
ATOM   5115  N  NZ    . LYS A 1 2094 ? 190.316 170.951 180.693 1.00 2.64  ? 2094 LYS A NZ    1 
ATOM   5116  N  N     . SER A 1 2095 ? 196.387 168.891 178.001 1.00 1.29  ? 2095 SER A N     1 
ATOM   5117  C  CA    . SER A 1 2095 ? 197.062 169.574 176.903 1.00 0.60  ? 2095 SER A CA    1 
ATOM   5118  C  C     . SER A 1 2095 ? 197.097 168.705 175.651 1.00 1.25  ? 2095 SER A C     1 
ATOM   5119  O  O     . SER A 1 2095 ? 196.827 169.180 174.543 1.00 2.03  ? 2095 SER A O     1 
ATOM   5120  C  CB    . SER A 1 2095 ? 198.477 169.963 177.330 1.00 1.16  ? 2095 SER A CB    1 
ATOM   5121  O  OG    . SER A 1 2095 ? 199.215 170.495 176.243 1.00 15.11 ? 2095 SER A OG    1 
ATOM   5122  N  N     . VAL A 1 2096 ? 197.432 167.424 175.812 1.00 0.95  ? 2096 VAL A N     1 
ATOM   5123  C  CA    . VAL A 1 2096 ? 197.469 166.515 174.671 1.00 1.45  ? 2096 VAL A CA    1 
ATOM   5124  C  C     . VAL A 1 2096 ? 196.072 166.319 174.095 1.00 1.63  ? 2096 VAL A C     1 
ATOM   5125  O  O     . VAL A 1 2096 ? 195.884 166.319 172.873 1.00 2.83  ? 2096 VAL A O     1 
ATOM   5126  C  CB    . VAL A 1 2096 ? 198.112 165.175 175.078 1.00 2.90  ? 2096 VAL A CB    1 
ATOM   5127  C  CG1   . VAL A 1 2096 ? 197.975 164.155 173.965 1.00 1.97  ? 2096 VAL A CG1   1 
ATOM   5128  C  CG2   . VAL A 1 2096 ? 199.574 165.380 175.437 1.00 3.70  ? 2096 VAL A CG2   1 
ATOM   5129  N  N     . LEU A 1 2097 ? 195.071 166.149 174.964 1.00 1.52  ? 2097 LEU A N     1 
ATOM   5130  C  CA    . LEU A 1 2097 ? 193.706 165.926 174.496 1.00 1.44  ? 2097 LEU A CA    1 
ATOM   5131  C  C     . LEU A 1 2097 ? 193.175 167.129 173.726 1.00 4.36  ? 2097 LEU A C     1 
ATOM   5132  O  O     . LEU A 1 2097 ? 192.537 166.971 172.679 1.00 5.99  ? 2097 LEU A O     1 
ATOM   5133  C  CB    . LEU A 1 2097 ? 192.794 165.607 175.679 1.00 1.58  ? 2097 LEU A CB    1 
ATOM   5134  C  CG    . LEU A 1 2097 ? 193.035 164.283 176.407 1.00 1.04  ? 2097 LEU A CG    1 
ATOM   5135  C  CD1   . LEU A 1 2097 ? 192.181 164.209 177.661 1.00 0.93  ? 2097 LEU A CD1   1 
ATOM   5136  C  CD2   . LEU A 1 2097 ? 192.764 163.103 175.493 1.00 1.00  ? 2097 LEU A CD2   1 
ATOM   5137  N  N     . VAL A 1 2098 ? 193.414 168.339 174.235 1.00 2.74  ? 2098 VAL A N     1 
ATOM   5138  C  CA    . VAL A 1 2098 ? 192.991 169.539 173.524 1.00 2.59  ? 2098 VAL A CA    1 
ATOM   5139  C  C     . VAL A 1 2098 ? 193.753 169.677 172.212 1.00 3.41  ? 2098 VAL A C     1 
ATOM   5140  O  O     . VAL A 1 2098 ? 193.170 170.000 171.171 1.00 2.84  ? 2098 VAL A O     1 
ATOM   5141  C  CB    . VAL A 1 2098 ? 193.164 170.779 174.422 1.00 3.33  ? 2098 VAL A CB    1 
ATOM   5142  C  CG1   . VAL A 1 2098 ? 193.029 172.058 173.611 1.00 0.96  ? 2098 VAL A CG1   1 
ATOM   5143  C  CG2   . VAL A 1 2098 ? 192.148 170.755 175.551 1.00 5.01  ? 2098 VAL A CG2   1 
ATOM   5144  N  N     . SER A 1 2099 ? 195.065 169.426 172.242 1.00 3.62  ? 2099 SER A N     1 
ATOM   5145  C  CA    . SER A 1 2099 ? 195.859 169.470 171.019 1.00 2.22  ? 2099 SER A CA    1 
ATOM   5146  C  C     . SER A 1 2099 ? 195.416 168.407 170.024 1.00 2.37  ? 2099 SER A C     1 
ATOM   5147  O  O     . SER A 1 2099 ? 195.516 168.616 168.810 1.00 5.26  ? 2099 SER A O     1 
ATOM   5148  C  CB    . SER A 1 2099 ? 197.342 169.302 171.358 1.00 3.76  ? 2099 SER A CB    1 
ATOM   5149  O  OG    . SER A 1 2099 ? 198.158 169.517 170.222 1.00 13.31 ? 2099 SER A OG    1 
ATOM   5150  N  N     . ALA A 1 2100 ? 194.923 167.267 170.513 1.00 3.50  ? 2100 ALA A N     1 
ATOM   5151  C  CA    . ALA A 1 2100 ? 194.447 166.219 169.615 1.00 5.12  ? 2100 ALA A CA    1 
ATOM   5152  C  C     . ALA A 1 2100 ? 193.283 166.709 168.764 1.00 6.50  ? 2100 ALA A C     1 
ATOM   5153  O  O     . ALA A 1 2100 ? 193.220 166.427 167.562 1.00 7.64  ? 2100 ALA A O     1 
ATOM   5154  C  CB    . ALA A 1 2100 ? 194.045 164.982 170.415 1.00 5.02  ? 2100 ALA A CB    1 
ATOM   5155  N  N     . GLY A 1 2101 ? 192.348 167.443 169.369 1.00 5.27  ? 2101 GLY A N     1 
ATOM   5156  C  CA    . GLY A 1 2101 ? 191.247 168.000 168.600 1.00 3.95  ? 2101 GLY A CA    1 
ATOM   5157  C  C     . GLY A 1 2101 ? 191.708 169.024 167.582 1.00 5.71  ? 2101 GLY A C     1 
ATOM   5158  O  O     . GLY A 1 2101 ? 191.187 169.084 166.466 1.00 7.10  ? 2101 GLY A O     1 
ATOM   5159  N  N     . ASN A 1 2102 ? 192.687 169.851 167.956 1.00 6.60  ? 2102 ASN A N     1 
ATOM   5160  C  CA    . ASN A 1 2102 ? 193.229 170.827 167.018 1.00 4.73  ? 2102 ASN A CA    1 
ATOM   5161  C  C     . ASN A 1 2102 ? 193.940 170.143 165.855 1.00 6.22  ? 2102 ASN A C     1 
ATOM   5162  O  O     . ASN A 1 2102 ? 193.798 170.559 164.701 1.00 11.52 ? 2102 ASN A O     1 
ATOM   5163  C  CB    . ASN A 1 2102 ? 194.172 171.783 167.744 1.00 7.16  ? 2102 ASN A CB    1 
ATOM   5164  C  CG    . ASN A 1 2102 ? 193.433 172.802 168.586 1.00 10.57 ? 2102 ASN A CG    1 
ATOM   5165  O  OD1   . ASN A 1 2102 ? 192.480 173.426 168.126 1.00 20.08 ? 2102 ASN A OD1   1 
ATOM   5166  N  ND2   . ASN A 1 2102 ? 193.871 172.976 169.826 1.00 6.35  ? 2102 ASN A ND2   1 
ATOM   5167  N  N     . VAL A 1 2103 ? 194.706 169.088 166.142 1.00 5.62  ? 2103 VAL A N     1 
ATOM   5168  C  CA    . VAL A 1 2103 ? 195.404 168.366 165.080 1.00 6.51  ? 2103 VAL A CA    1 
ATOM   5169  C  C     . VAL A 1 2103 ? 194.408 167.654 164.174 1.00 8.78  ? 2103 VAL A C     1 
ATOM   5170  O  O     . VAL A 1 2103 ? 194.603 167.567 162.955 1.00 10.36 ? 2103 VAL A O     1 
ATOM   5171  C  CB    . VAL A 1 2103 ? 196.432 167.389 165.680 1.00 7.40  ? 2103 VAL A CB    1 
ATOM   5172  C  CG1   . VAL A 1 2103 ? 197.009 166.489 164.603 1.00 5.14  ? 2103 VAL A CG1   1 
ATOM   5173  C  CG2   . VAL A 1 2103 ? 197.545 168.150 166.379 1.00 9.10  ? 2103 VAL A CG2   1 
ATOM   5174  N  N     . LYS A 1 2104 ? 193.327 167.123 164.747 1.00 8.22  ? 2104 LYS A N     1 
ATOM   5175  C  CA    . LYS A 1 2104 ? 192.323 166.458 163.923 1.00 8.04  ? 2104 LYS A CA    1 
ATOM   5176  C  C     . LYS A 1 2104 ? 191.646 167.441 162.975 1.00 7.42  ? 2104 LYS A C     1 
ATOM   5177  O  O     . LYS A 1 2104 ? 191.377 167.108 161.817 1.00 8.16  ? 2104 LYS A O     1 
ATOM   5178  C  CB    . LYS A 1 2104 ? 191.288 165.760 164.804 1.00 10.76 ? 2104 LYS A CB    1 
ATOM   5179  C  CG    . LYS A 1 2104 ? 190.378 164.819 164.033 1.00 7.28  ? 2104 LYS A CG    1 
ATOM   5180  C  CD    . LYS A 1 2104 ? 189.566 163.932 164.955 1.00 9.35  ? 2104 LYS A CD    1 
ATOM   5181  C  CE    . LYS A 1 2104 ? 188.368 164.671 165.524 1.00 11.58 ? 2104 LYS A CE    1 
ATOM   5182  N  NZ    . LYS A 1 2104 ? 187.249 164.744 164.546 1.00 8.13  ? 2104 LYS A NZ    1 
ATOM   5183  N  N     . ARG A 1 2105 ? 191.366 168.657 163.449 1.00 11.36 ? 2105 ARG A N     1 
ATOM   5184  C  CA    . ARG A 1 2105 ? 190.710 169.648 162.602 1.00 7.24  ? 2105 ARG A CA    1 
ATOM   5185  C  C     . ARG A 1 2105 ? 191.605 170.079 161.445 1.00 12.17 ? 2105 ARG A C     1 
ATOM   5186  O  O     . ARG A 1 2105 ? 191.126 170.258 160.321 1.00 19.50 ? 2105 ARG A O     1 
ATOM   5187  C  CB    . ARG A 1 2105 ? 190.287 170.857 163.436 1.00 7.44  ? 2105 ARG A CB    1 
ATOM   5188  C  CG    . ARG A 1 2105 ? 189.004 170.649 164.230 1.00 7.54  ? 2105 ARG A CG    1 
ATOM   5189  C  CD    . ARG A 1 2105 ? 188.530 171.947 164.862 1.00 7.28  ? 2105 ARG A CD    1 
ATOM   5190  N  NE    . ARG A 1 2105 ? 189.319 172.305 166.035 1.00 12.29 ? 2105 ARG A NE    1 
ATOM   5191  C  CZ    . ARG A 1 2105 ? 189.224 171.711 167.216 1.00 10.33 ? 2105 ARG A CZ    1 
ATOM   5192  N  NH1   . ARG A 1 2105 ? 188.354 170.739 167.435 1.00 13.33 ? 2105 ARG A NH1   1 
ATOM   5193  N  NH2   . ARG A 1 2105 ? 190.023 172.102 168.206 1.00 10.63 ? 2105 ARG A NH2   1 
ATOM   5194  N  N     . GLU A 1 2106 ? 192.906 170.254 161.698 1.00 11.75 ? 2106 GLU A N     1 
ATOM   5195  C  CA    . GLU A 1 2106 ? 193.799 170.708 160.636 1.00 15.98 ? 2106 GLU A CA    1 
ATOM   5196  C  C     . GLU A 1 2106 ? 193.995 169.630 159.574 1.00 18.30 ? 2106 GLU A C     1 
ATOM   5197  O  O     . GLU A 1 2106 ? 194.107 169.939 158.382 1.00 25.56 ? 2106 GLU A O     1 
ATOM   5198  C  CB    . GLU A 1 2106 ? 195.143 171.156 161.220 1.00 9.17  ? 2106 GLU A CB    1 
ATOM   5199  C  CG    . GLU A 1 2106 ? 195.957 170.053 161.863 1.00 20.32 ? 2106 GLU A CG    1 
ATOM   5200  C  CD    . GLU A 1 2106 ? 197.245 170.551 162.486 1.00 24.14 ? 2106 GLU A CD    1 
ATOM   5201  O  OE1   . GLU A 1 2106 ? 197.499 171.771 162.439 1.00 19.37 ? 2106 GLU A OE1   1 
ATOM   5202  O  OE2   . GLU A 1 2106 ? 198.002 169.716 163.023 1.00 26.25 ? 2106 GLU A OE2   1 
ATOM   5203  N  N     . ARG A 1 2107 ? 194.043 168.358 159.982 1.00 11.15 ? 2107 ARG A N     1 
ATOM   5204  C  CA    . ARG A 1 2107 ? 194.148 167.280 159.002 1.00 12.30 ? 2107 ARG A CA    1 
ATOM   5205  C  C     . ARG A 1 2107 ? 192.911 167.205 158.120 1.00 17.32 ? 2107 ARG A C     1 
ATOM   5206  O  O     . ARG A 1 2107 ? 193.021 167.011 156.904 1.00 24.87 ? 2107 ARG A O     1 
ATOM   5207  C  CB    . ARG A 1 2107 ? 194.382 165.941 159.695 1.00 12.89 ? 2107 ARG A CB    1 
ATOM   5208  C  CG    . ARG A 1 2107 ? 195.717 165.802 160.384 1.00 13.49 ? 2107 ARG A CG    1 
ATOM   5209  C  CD    . ARG A 1 2107 ? 195.816 164.421 160.987 1.00 19.09 ? 2107 ARG A CD    1 
ATOM   5210  N  NE    . ARG A 1 2107 ? 197.040 164.215 161.749 1.00 26.59 ? 2107 ARG A NE    1 
ATOM   5211  C  CZ    . ARG A 1 2107 ? 198.174 163.769 161.228 1.00 18.53 ? 2107 ARG A CZ    1 
ATOM   5212  N  NH1   . ARG A 1 2107 ? 198.271 163.466 159.944 1.00 21.26 ? 2107 ARG A NH1   1 
ATOM   5213  N  NH2   . ARG A 1 2107 ? 199.233 163.612 162.018 1.00 21.63 ? 2107 ARG A NH2   1 
ATOM   5214  N  N     . ILE A 1 2108 ? 191.723 167.345 158.711 1.00 16.89 ? 2108 ILE A N     1 
ATOM   5215  C  CA    . ILE A 1 2108 ? 190.500 167.332 157.915 1.00 17.81 ? 2108 ILE A CA    1 
ATOM   5216  C  C     . ILE A 1 2108 ? 190.507 168.491 156.928 1.00 22.63 ? 2108 ILE A C     1 
ATOM   5217  O  O     . ILE A 1 2108 ? 190.146 168.330 155.756 1.00 27.37 ? 2108 ILE A O     1 
ATOM   5218  C  CB    . ILE A 1 2108 ? 189.261 167.364 158.829 1.00 16.22 ? 2108 ILE A CB    1 
ATOM   5219  C  CG1   . ILE A 1 2108 ? 189.202 166.097 159.681 1.00 15.13 ? 2108 ILE A CG1   1 
ATOM   5220  C  CG2   . ILE A 1 2108 ? 187.990 167.510 158.007 1.00 14.40 ? 2108 ILE A CG2   1 
ATOM   5221  C  CD1   . ILE A 1 2108 ? 187.998 166.026 160.593 1.00 10.67 ? 2108 ILE A CD1   1 
ATOM   5222  N  N     . GLN A 1 2109 ? 190.930 169.673 157.382 1.00 22.48 ? 2109 GLN A N     1 
ATOM   5223  C  CA    . GLN A 1 2109 ? 191.077 170.804 156.474 1.00 23.03 ? 2109 GLN A CA    1 
ATOM   5224  C  C     . GLN A 1 2109 ? 192.153 170.545 155.429 1.00 27.26 ? 2109 GLN A C     1 
ATOM   5225  O  O     . GLN A 1 2109 ? 192.023 170.985 154.282 1.00 28.54 ? 2109 GLN A O     1 
ATOM   5226  C  CB    . GLN A 1 2109 ? 191.401 172.073 157.262 1.00 20.57 ? 2109 GLN A CB    1 
ATOM   5227  C  CG    . GLN A 1 2109 ? 190.230 172.616 158.057 1.00 23.10 ? 2109 GLN A CG    1 
ATOM   5228  C  CD    . GLN A 1 2109 ? 189.053 172.977 157.178 1.00 33.36 ? 2109 GLN A CD    1 
ATOM   5229  O  OE1   . GLN A 1 2109 ? 188.013 172.320 157.214 1.00 36.67 ? 2109 GLN A OE1   1 
ATOM   5230  N  NE2   . GLN A 1 2109 ? 189.210 174.027 156.381 1.00 29.37 ? 2109 GLN A NE2   1 
ATOM   5231  N  N     . LYS A 1 2110 ? 193.224 169.843 155.806 1.00 21.09 ? 2110 LYS A N     1 
ATOM   5232  C  CA    . LYS A 1 2110 ? 194.281 169.530 154.849 1.00 21.20 ? 2110 LYS A CA    1 
ATOM   5233  C  C     . LYS A 1 2110 ? 193.825 168.484 153.838 1.00 22.79 ? 2110 LYS A C     1 
ATOM   5234  O  O     . LYS A 1 2110 ? 194.166 168.573 152.652 1.00 26.93 ? 2110 LYS A O     1 
ATOM   5235  C  CB    . LYS A 1 2110 ? 195.533 169.056 155.587 1.00 20.08 ? 2110 LYS A CB    1 
ATOM   5236  C  CG    . LYS A 1 2110 ? 196.666 168.621 154.681 1.00 22.38 ? 2110 LYS A CG    1 
ATOM   5237  C  CD    . LYS A 1 2110 ? 197.566 167.610 155.370 1.00 28.08 ? 2110 LYS A CD    1 
ATOM   5238  C  CE    . LYS A 1 2110 ? 198.985 167.677 154.832 1.00 25.18 ? 2110 LYS A CE    1 
ATOM   5239  N  NZ    . LYS A 1 2110 ? 199.060 167.227 153.415 1.00 29.23 ? 2110 LYS A NZ    1 
ATOM   5240  N  N     . ILE A 1 2111 ? 193.062 167.485 154.285 1.00 24.44 ? 2111 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 2111 ? 192.610 166.428 153.381 1.00 22.73 ? 2111 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 2111 ? 191.708 167.003 152.298 1.00 26.33 ? 2111 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 2111 ? 191.864 166.701 151.108 1.00 31.89 ? 2111 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 2111 ? 191.899 165.312 154.169 1.00 17.58 ? 2111 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 2111 ? 192.904 164.518 155.003 1.00 18.51 ? 2111 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 2111 ? 191.144 164.389 153.228 1.00 16.08 ? 2111 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 2111 ? 192.265 163.479 155.893 1.00 15.26 ? 2111 ILE A CD1   1 
ATOM   5248  N  N     . LYS A 1 2112 ? 190.753 167.847 152.691 1.00 26.96 ? 2112 LYS A N     1 
ATOM   5249  C  CA    . LYS A 1 2112 ? 189.861 168.448 151.707 1.00 25.62 ? 2112 LYS A CA    1 
ATOM   5250  C  C     . LYS A 1 2112 ? 190.577 169.492 150.861 1.00 30.51 ? 2112 LYS A C     1 
ATOM   5251  O  O     . LYS A 1 2112 ? 190.208 169.703 149.702 1.00 31.27 ? 2112 LYS A O     1 
ATOM   5252  C  CB    . LYS A 1 2112 ? 188.637 169.054 152.397 1.00 26.28 ? 2112 LYS A CB    1 
ATOM   5253  C  CG    . LYS A 1 2112 ? 188.946 170.116 153.429 1.00 26.94 ? 2112 LYS A CG    1 
ATOM   5254  C  CD    . LYS A 1 2112 ? 187.680 170.552 154.147 1.00 34.18 ? 2112 LYS A CD    1 
ATOM   5255  C  CE    . LYS A 1 2112 ? 186.994 169.370 154.819 1.00 33.16 ? 2112 LYS A CE    1 
ATOM   5256  N  NZ    . LYS A 1 2112 ? 185.789 169.789 155.586 1.00 29.39 ? 2112 LYS A NZ    1 
ATOM   5257  N  N     . ARG A 1 2113 ? 191.602 170.150 151.414 1.00 31.95 ? 2113 ARG A N     1 
ATOM   5258  C  CA    . ARG A 1 2113 ? 192.406 171.066 150.609 1.00 24.50 ? 2113 ARG A CA    1 
ATOM   5259  C  C     . ARG A 1 2113 ? 193.103 170.323 149.477 1.00 30.48 ? 2113 ARG A C     1 
ATOM   5260  O  O     . ARG A 1 2113 ? 193.203 170.838 148.356 1.00 36.67 ? 2113 ARG A O     1 
ATOM   5261  C  CB    . ARG A 1 2113 ? 193.425 171.792 151.484 1.00 25.63 ? 2113 ARG A CB    1 
ATOM   5262  C  CG    . ARG A 1 2113 ? 192.966 173.157 151.969 1.00 27.63 ? 2113 ARG A CG    1 
ATOM   5263  C  CD    . ARG A 1 2113 ? 193.958 173.755 152.956 1.00 23.86 ? 2113 ARG A CD    1 
ATOM   5264  N  NE    . ARG A 1 2113 ? 193.972 173.035 154.224 1.00 29.43 ? 2113 ARG A NE    1 
ATOM   5265  C  CZ    . ARG A 1 2113 ? 194.750 173.344 155.251 1.00 32.04 ? 2113 ARG A CZ    1 
ATOM   5266  N  NH1   . ARG A 1 2113 ? 195.599 174.358 155.196 1.00 28.59 ? 2113 ARG A NH1   1 
ATOM   5267  N  NH2   . ARG A 1 2113 ? 194.677 172.618 156.364 1.00 27.16 ? 2113 ARG A NH2   1 
ATOM   5268  N  N     . GLU A 1 2114 ? 193.597 169.114 149.752 1.00 27.41 ? 2114 GLU A N     1 
ATOM   5269  C  CA    . GLU A 1 2114 ? 194.101 168.265 148.678 1.00 30.91 ? 2114 GLU A CA    1 
ATOM   5270  C  C     . GLU A 1 2114 ? 192.987 167.863 147.725 1.00 32.05 ? 2114 GLU A C     1 
ATOM   5271  O  O     . GLU A 1 2114 ? 193.230 167.678 146.526 1.00 34.94 ? 2114 GLU A O     1 
ATOM   5272  C  CB    . GLU A 1 2114 ? 194.775 167.020 149.258 1.00 29.20 ? 2114 GLU A CB    1 
ATOM   5273  C  CG    . GLU A 1 2114 ? 195.875 167.310 150.262 1.00 28.95 ? 2114 GLU A CG    1 
ATOM   5274  C  CD    . GLU A 1 2114 ? 196.750 168.477 149.852 1.00 36.16 ? 2114 GLU A CD    1 
ATOM   5275  O  OE1   . GLU A 1 2114 ? 197.387 168.395 148.779 1.00 35.67 ? 2114 GLU A OE1   1 
ATOM   5276  O  OE2   . GLU A 1 2114 ? 196.800 169.476 150.599 1.00 32.65 ? 2114 GLU A OE2   1 
ATOM   5277  N  N     . LYS A 1 2115 ? 191.763 167.717 148.235 1.00 29.75 ? 2115 LYS A N     1 
ATOM   5278  C  CA    . LYS A 1 2115 ? 190.651 167.311 147.384 1.00 29.63 ? 2115 LYS A CA    1 
ATOM   5279  C  C     . LYS A 1 2115 ? 190.226 168.435 146.445 1.00 31.36 ? 2115 LYS A C     1 
ATOM   5280  O  O     . LYS A 1 2115 ? 189.748 168.170 145.336 1.00 35.74 ? 2115 LYS A O     1 
ATOM   5281  C  CB    . LYS A 1 2115 ? 189.474 166.851 148.242 1.00 27.31 ? 2115 LYS A CB    1 
ATOM   5282  C  CG    . LYS A 1 2115 ? 189.633 165.448 148.809 1.00 29.44 ? 2115 LYS A CG    1 
ATOM   5283  C  CD    . LYS A 1 2115 ? 188.302 164.898 149.290 1.00 32.62 ? 2115 LYS A CD    1 
ATOM   5284  C  CE    . LYS A 1 2115 ? 188.393 163.416 149.598 1.00 25.41 ? 2115 LYS A CE    1 
ATOM   5285  N  NZ    . LYS A 1 2115 ? 189.250 163.140 150.782 1.00 27.16 ? 2115 LYS A NZ    1 
ATOM   5286  N  N     . GLU A 1 2116 ? 190.384 169.692 146.868 1.00 30.58 ? 2116 GLU A N     1 
ATOM   5287  C  CA    . GLU A 1 2116 ? 190.024 170.810 145.999 1.00 33.35 ? 2116 GLU A CA    1 
ATOM   5288  C  C     . GLU A 1 2116 ? 190.860 170.807 144.725 1.00 34.61 ? 2116 GLU A C     1 
ATOM   5289  O  O     . GLU A 1 2116 ? 190.342 171.066 143.632 1.00 32.25 ? 2116 GLU A O     1 
ATOM   5290  C  CB    . GLU A 1 2116 ? 190.185 172.138 146.740 1.00 30.92 ? 2116 GLU A CB    1 
ATOM   5291  C  CG    . GLU A 1 2116 ? 189.397 172.244 148.032 1.00 33.61 ? 2116 GLU A CG    1 
ATOM   5292  C  CD    . GLU A 1 2116 ? 187.999 171.669 147.917 1.00 38.58 ? 2116 GLU A CD    1 
ATOM   5293  O  OE1   . GLU A 1 2116 ? 187.227 172.146 147.059 1.00 36.56 ? 2116 GLU A OE1   1 
ATOM   5294  O  OE2   . GLU A 1 2116 ? 187.673 170.742 148.687 1.00 36.31 ? 2116 GLU A OE2   1 
ATOM   5295  N  N     . GLU A 1 2117 ? 192.151 170.516 144.844 1.00 32.59 ? 2117 GLU A N     1 
ATOM   5296  C  CA    . GLU A 1 2117 ? 193.042 170.439 143.694 1.00 35.78 ? 2117 GLU A CA    1 
ATOM   5297  C  C     . GLU A 1 2117 ? 193.113 169.042 143.086 1.00 33.63 ? 2117 GLU A C     1 
ATOM   5298  O  O     . GLU A 1 2117 ? 193.808 168.856 142.083 1.00 37.81 ? 2117 GLU A O     1 
ATOM   5299  C  CB    . GLU A 1 2117 ? 194.441 170.933 144.086 1.00 33.84 ? 2117 GLU A CB    1 
ATOM   5300  C  CG    . GLU A 1 2117 ? 195.123 170.153 145.207 1.00 38.80 ? 2117 GLU A CG    1 
ATOM   5301  C  CD    . GLU A 1 2117 ? 195.894 168.945 144.717 1.00 41.34 ? 2117 GLU A CD    1 
ATOM   5302  O  OE1   . GLU A 1 2117 ? 196.228 168.895 143.516 1.00 41.46 ? 2117 GLU A OE1   1 
ATOM   5303  O  OE2   . GLU A 1 2117 ? 196.176 168.048 145.541 1.00 40.60 ? 2117 GLU A OE2   1 
ATOM   5304  N  N     . ARG A 1 2118 ? 192.409 168.065 143.660 1.00 33.84 ? 2118 ARG A N     1 
ATOM   5305  C  CA    . ARG A 1 2118 ? 192.287 166.720 143.091 1.00 34.76 ? 2118 ARG A CA    1 
ATOM   5306  C  C     . ARG A 1 2118 ? 190.806 166.348 143.072 1.00 34.74 ? 2118 ARG A C     1 
ATOM   5307  O  O     . ARG A 1 2118 ? 190.301 165.724 144.010 1.00 40.30 ? 2118 ARG A O     1 
ATOM   5308  C  CB    . ARG A 1 2118 ? 193.107 165.698 143.881 1.00 31.25 ? 2118 ARG A CB    1 
ATOM   5309  C  CG    . ARG A 1 2118 ? 194.609 165.893 143.801 1.00 32.04 ? 2118 ARG A CG    1 
ATOM   5310  C  CD    . ARG A 1 2118 ? 195.090 165.905 142.359 1.00 36.32 ? 2118 ARG A CD    1 
ATOM   5311  N  NE    . ARG A 1 2118 ? 194.617 164.744 141.616 1.00 37.68 ? 2118 ARG A NE    1 
ATOM   5312  C  CZ    . ARG A 1 2118 ? 193.874 164.806 140.519 1.00 38.37 ? 2118 ARG A CZ    1 
ATOM   5313  N  NH1   . ARG A 1 2118 ? 193.497 165.965 140.005 1.00 37.83 ? 2118 ARG A NH1   1 
ATOM   5314  N  NH2   . ARG A 1 2118 ? 193.502 163.677 139.922 1.00 38.94 ? 2118 ARG A NH2   1 
ATOM   5315  N  N     . GLY A 1 2119 ? 190.114 166.728 142.002 1.00 32.94 ? 2119 GLY A N     1 
ATOM   5316  C  CA    . GLY A 1 2119 ? 188.720 166.375 141.842 1.00 33.75 ? 2119 GLY A CA    1 
ATOM   5317  C  C     . GLY A 1 2119 ? 187.784 167.217 142.690 1.00 37.03 ? 2119 GLY A C     1 
ATOM   5318  O  O     . GLY A 1 2119 ? 188.119 168.303 143.172 1.00 36.93 ? 2119 GLY A O     1 
ATOM   5319  N  N     . GLU A 1 2120 ? 186.568 166.703 142.846 1.00 32.73 ? 2120 GLU A N     1 
ATOM   5320  C  CA    . GLU A 1 2120 ? 185.525 167.347 143.641 1.00 36.90 ? 2120 GLU A CA    1 
ATOM   5321  C  C     . GLU A 1 2120 ? 184.780 166.300 144.463 1.00 36.07 ? 2120 GLU A C     1 
ATOM   5322  O  O     . GLU A 1 2120 ? 183.548 166.264 144.505 1.00 35.87 ? 2120 GLU A O     1 
ATOM   5323  C  CB    . GLU A 1 2120 ? 184.568 168.141 142.750 1.00 34.90 ? 2120 GLU A CB    1 
ATOM   5324  C  CG    . GLU A 1 2120 ? 185.123 169.478 142.286 1.00 34.48 ? 2120 GLU A CG    1 
ATOM   5325  C  CD    . GLU A 1 2120 ? 184.113 170.285 141.496 1.00 40.32 ? 2120 GLU A CD    1 
ATOM   5326  O  OE1   . GLU A 1 2120 ? 183.025 170.575 142.038 1.00 40.28 ? 2120 GLU A OE1   1 
ATOM   5327  O  OE2   . GLU A 1 2120 ? 184.407 170.634 140.333 1.00 38.65 ? 2120 GLU A OE2   1 
ATOM   5328  N  N     . ALA A 1 2121 ? 185.532 165.427 145.129 1.00 32.58 ? 2121 ALA A N     1 
ATOM   5329  C  CA    . ALA A 1 2121 ? 184.977 164.275 145.837 1.00 31.17 ? 2121 ALA A CA    1 
ATOM   5330  C  C     . ALA A 1 2121 ? 184.830 164.525 147.335 1.00 30.95 ? 2121 ALA A C     1 
ATOM   5331  O  O     . ALA A 1 2121 ? 185.053 163.617 148.140 1.00 31.13 ? 2121 ALA A O     1 
ATOM   5332  C  CB    . ALA A 1 2121 ? 185.836 163.041 145.585 1.00 28.92 ? 2121 ALA A CB    1 
ATOM   5333  N  N     . VAL A 1 2122 ? 184.464 165.743 147.736 1.00 32.16 ? 2122 VAL A N     1 
ATOM   5334  C  CA    . VAL A 1 2122 ? 184.279 166.062 149.148 1.00 29.19 ? 2122 VAL A CA    1 
ATOM   5335  C  C     . VAL A 1 2122 ? 183.147 165.210 149.710 1.00 31.49 ? 2122 VAL A C     1 
ATOM   5336  O  O     . VAL A 1 2122 ? 181.981 165.379 149.339 1.00 34.92 ? 2122 VAL A O     1 
ATOM   5337  C  CB    . VAL A 1 2122 ? 183.998 167.561 149.352 1.00 29.90 ? 2122 VAL A CB    1 
ATOM   5338  C  CG1   . VAL A 1 2122 ? 183.611 167.835 150.798 1.00 31.01 ? 2122 VAL A CG1   1 
ATOM   5339  C  CG2   . VAL A 1 2122 ? 185.210 168.388 148.952 1.00 23.11 ? 2122 VAL A CG2   1 
ATOM   5340  N  N     . ASP A 1 2123 ? 183.492 164.285 150.603 1.00 28.74 ? 2123 ASP A N     1 
ATOM   5341  C  CA    . ASP A 1 2123 ? 182.553 163.316 151.160 1.00 31.15 ? 2123 ASP A CA    1 
ATOM   5342  C  C     . ASP A 1 2123 ? 182.752 163.196 152.666 1.00 33.58 ? 2123 ASP A C     1 
ATOM   5343  O  O     . ASP A 1 2123 ? 182.974 162.101 153.194 1.00 32.73 ? 2123 ASP A O     1 
ATOM   5344  C  CB    . ASP A 1 2123 ? 182.688 161.956 150.478 1.00 28.62 ? 2123 ASP A CB    1 
ATOM   5345  C  CG    . ASP A 1 2123 ? 181.454 161.092 150.656 1.00 35.25 ? 2123 ASP A CG    1 
ATOM   5346  O  OD1   . ASP A 1 2123 ? 180.357 161.537 150.258 1.00 36.80 ? 2123 ASP A OD1   1 
ATOM   5347  O  OD2   . ASP A 1 2123 ? 181.576 159.968 151.182 1.00 39.28 ? 2123 ASP A OD2   1 
ATOM   5348  N  N     . GLU A 1 2124 ? 182.682 164.332 153.369 1.00 31.81 ? 2124 GLU A N     1 
ATOM   5349  C  CA    . GLU A 1 2124 ? 183.099 164.507 154.762 1.00 26.78 ? 2124 GLU A CA    1 
ATOM   5350  C  C     . GLU A 1 2124 ? 182.845 163.294 155.653 1.00 27.01 ? 2124 GLU A C     1 
ATOM   5351  O  O     . GLU A 1 2124 ? 183.693 162.948 156.483 1.00 32.86 ? 2124 GLU A O     1 
ATOM   5352  C  CB    . GLU A 1 2124 ? 182.410 165.735 155.371 1.00 27.87 ? 2124 GLU A CB    1 
ATOM   5353  C  CG    . GLU A 1 2124 ? 180.885 165.762 155.260 1.00 29.75 ? 2124 GLU A CG    1 
ATOM   5354  C  CD    . GLU A 1 2124 ? 180.387 166.178 153.886 1.00 38.06 ? 2124 GLU A CD    1 
ATOM   5355  O  OE1   . GLU A 1 2124 ? 181.224 166.481 153.012 1.00 35.37 ? 2124 GLU A OE1   1 
ATOM   5356  O  OE2   . GLU A 1 2124 ? 179.154 166.203 153.686 1.00 35.94 ? 2124 GLU A OE2   1 
ATOM   5357  N  N     . GLY A 1 2125 ? 181.686 162.655 155.513 1.00 27.26 ? 2125 GLY A N     1 
ATOM   5358  C  CA    . GLY A 1 2125 ? 181.407 161.449 156.266 1.00 31.48 ? 2125 GLY A CA    1 
ATOM   5359  C  C     . GLY A 1 2125 ? 182.432 160.357 156.041 1.00 30.12 ? 2125 GLY A C     1 
ATOM   5360  O  O     . GLY A 1 2125 ? 182.909 159.738 156.995 1.00 30.74 ? 2125 GLY A O     1 
ATOM   5361  N  N     . GLU A 1 2126 ? 182.792 160.117 154.776 1.00 31.54 ? 2126 GLU A N     1 
ATOM   5362  C  CA    . GLU A 1 2126 ? 183.840 159.148 154.478 1.00 32.31 ? 2126 GLU A CA    1 
ATOM   5363  C  C     . GLU A 1 2126 ? 185.216 159.677 154.868 1.00 31.18 ? 2126 GLU A C     1 
ATOM   5364  O  O     . GLU A 1 2126 ? 186.121 158.889 155.163 1.00 27.23 ? 2126 GLU A O     1 
ATOM   5365  C  CB    . GLU A 1 2126 ? 183.811 158.779 152.995 1.00 30.95 ? 2126 GLU A CB    1 
ATOM   5366  C  CG    . GLU A 1 2126 ? 184.867 157.772 152.565 1.00 34.83 ? 2126 GLU A CG    1 
ATOM   5367  C  CD    . GLU A 1 2126 ? 184.785 157.436 151.089 1.00 39.85 ? 2126 GLU A CD    1 
ATOM   5368  O  OE1   . GLU A 1 2126 ? 183.903 157.988 150.399 1.00 41.60 ? 2126 GLU A OE1   1 
ATOM   5369  O  OE2   . GLU A 1 2126 ? 185.605 156.619 150.619 1.00 38.08 ? 2126 GLU A OE2   1 
ATOM   5370  N  N     . ILE A 1 2127 ? 185.387 161.000 154.878 1.00 26.91 ? 2127 ILE A N     1 
ATOM   5371  C  CA    . ILE A 1 2127 ? 186.665 161.582 155.277 1.00 26.88 ? 2127 ILE A CA    1 
ATOM   5372  C  C     . ILE A 1 2127 ? 186.993 161.208 156.715 1.00 26.21 ? 2127 ILE A C     1 
ATOM   5373  O  O     . ILE A 1 2127 ? 188.149 160.912 157.049 1.00 29.68 ? 2127 ILE A O     1 
ATOM   5374  C  CB    . ILE A 1 2127 ? 186.642 163.109 155.074 1.00 28.03 ? 2127 ILE A CB    1 
ATOM   5375  C  CG1   . ILE A 1 2127 ? 186.329 163.445 153.614 1.00 29.69 ? 2127 ILE A CG1   1 
ATOM   5376  C  CG2   . ILE A 1 2127 ? 187.965 163.728 155.496 1.00 17.59 ? 2127 ILE A CG2   1 
ATOM   5377  C  CD1   . ILE A 1 2127 ? 186.447 164.917 153.281 1.00 28.35 ? 2127 ILE A CD1   1 
ATOM   5378  N  N     . ALA A 1 2128 ? 185.986 161.206 157.588 1.00 28.28 ? 2128 ALA A N     1 
ATOM   5379  C  CA    . ALA A 1 2128 ? 186.192 160.786 158.969 1.00 27.22 ? 2128 ALA A CA    1 
ATOM   5380  C  C     . ALA A 1 2128 ? 186.340 159.277 159.106 1.00 30.44 ? 2128 ALA A C     1 
ATOM   5381  O  O     . ALA A 1 2128 ? 186.859 158.812 160.127 1.00 26.69 ? 2128 ALA A O     1 
ATOM   5382  C  CB    . ALA A 1 2128 ? 185.035 161.270 159.846 1.00 19.35 ? 2128 ALA A CB    1 
ATOM   5383  N  N     . GLU A 1 2129 ? 185.894 158.504 158.115 1.00 27.80 ? 2129 GLU A N     1 
ATOM   5384  C  CA    . GLU A 1 2129 ? 186.032 157.052 158.188 1.00 25.08 ? 2129 GLU A CA    1 
ATOM   5385  C  C     . GLU A 1 2129 ? 187.492 156.634 158.077 1.00 27.84 ? 2129 GLU A C     1 
ATOM   5386  O  O     . GLU A 1 2129 ? 187.980 155.827 158.875 1.00 29.48 ? 2129 GLU A O     1 
ATOM   5387  C  CB    . GLU A 1 2129 ? 185.196 156.387 157.094 1.00 29.17 ? 2129 GLU A CB    1 
ATOM   5388  C  CG    . GLU A 1 2129 ? 183.692 156.542 157.272 1.00 29.91 ? 2129 GLU A CG    1 
ATOM   5389  C  CD    . GLU A 1 2129 ? 183.133 155.662 158.376 1.00 39.25 ? 2129 GLU A CD    1 
ATOM   5390  O  OE1   . GLU A 1 2129 ? 183.893 154.843 158.935 1.00 38.03 ? 2129 GLU A OE1   1 
ATOM   5391  O  OE2   . GLU A 1 2129 ? 181.931 155.789 158.687 1.00 46.44 ? 2129 GLU A OE2   1 
ATOM   5392  N  N     . ASN A 1 2130 ? 188.205 157.167 157.084 1.00 27.93 ? 2130 ASN A N     1 
ATOM   5393  C  CA    . ASN A 1 2130 ? 189.625 156.881 156.897 1.00 23.14 ? 2130 ASN A CA    1 
ATOM   5394  C  C     . ASN A 1 2130 ? 190.428 158.059 157.442 1.00 26.02 ? 2130 ASN A C     1 
ATOM   5395  O  O     . ASN A 1 2130 ? 190.962 158.884 156.703 1.00 30.02 ? 2130 ASN A O     1 
ATOM   5396  C  CB    . ASN A 1 2130 ? 189.929 156.615 155.427 1.00 23.75 ? 2130 ASN A CB    1 
ATOM   5397  C  CG    . ASN A 1 2130 ? 189.221 155.384 154.900 1.00 28.63 ? 2130 ASN A CG    1 
ATOM   5398  O  OD1   . ASN A 1 2130 ? 188.354 155.477 154.032 1.00 31.77 ? 2130 ASN A OD1   1 
ATOM   5399  N  ND2   . ASN A 1 2130 ? 189.586 154.221 155.428 1.00 30.36 ? 2130 ASN A ND2   1 
ATOM   5400  N  N     . LEU A 1 2131 ? 190.511 158.127 158.769 1.00 25.48 ? 2131 LEU A N     1 
ATOM   5401  C  CA    . LEU A 1 2131 ? 191.267 159.174 159.448 1.00 19.45 ? 2131 LEU A CA    1 
ATOM   5402  C  C     . LEU A 1 2131 ? 192.131 158.520 160.517 1.00 21.54 ? 2131 LEU A C     1 
ATOM   5403  O  O     . LEU A 1 2131 ? 191.591 157.863 161.431 1.00 25.32 ? 2131 LEU A O     1 
ATOM   5404  C  CB    . LEU A 1 2131 ? 190.337 160.225 160.059 1.00 21.90 ? 2131 LEU A CB    1 
ATOM   5405  C  CG    . LEU A 1 2131 ? 191.038 161.401 160.736 1.00 21.06 ? 2131 LEU A CG    1 
ATOM   5406  C  CD1   . LEU A 1 2131 ? 191.857 162.177 159.716 1.00 20.44 ? 2131 LEU A CD1   1 
ATOM   5407  C  CD2   . LEU A 1 2131 ? 190.035 162.307 161.428 1.00 11.21 ? 2131 LEU A CD2   1 
ATOM   5408  N  N     . PRO A 1 2132 ? 193.457 158.666 160.458 1.00 22.99 ? 2132 PRO A N     1 
ATOM   5409  C  CA    . PRO A 1 2132 ? 194.324 157.987 161.430 1.00 17.69 ? 2132 PRO A CA    1 
ATOM   5410  C  C     . PRO A 1 2132 ? 194.238 158.608 162.814 1.00 15.57 ? 2132 PRO A C     1 
ATOM   5411  O  O     . PRO A 1 2132 ? 195.091 159.418 163.192 1.00 18.31 ? 2132 PRO A O     1 
ATOM   5412  C  CB    . PRO A 1 2132 ? 195.725 158.154 160.827 1.00 20.17 ? 2132 PRO A CB    1 
ATOM   5413  C  CG    . PRO A 1 2132 ? 195.492 158.529 159.391 1.00 17.17 ? 2132 PRO A CG    1 
ATOM   5414  C  CD    . PRO A 1 2132 ? 194.236 159.327 159.403 1.00 16.91 ? 2132 PRO A CD    1 
ATOM   5415  N  N     . GLU A 1 2133 ? 193.209 158.232 163.575 1.00 14.55 ? 2133 GLU A N     1 
ATOM   5416  C  CA    . GLU A 1 2133 ? 192.983 158.845 164.880 1.00 13.32 ? 2133 GLU A CA    1 
ATOM   5417  C  C     . GLU A 1 2133 ? 194.129 158.555 165.842 1.00 12.83 ? 2133 GLU A C     1 
ATOM   5418  O  O     . GLU A 1 2133 ? 194.513 159.423 166.634 1.00 18.99 ? 2133 GLU A O     1 
ATOM   5419  C  CB    . GLU A 1 2133 ? 191.652 158.366 165.460 1.00 17.62 ? 2133 GLU A CB    1 
ATOM   5420  C  CG    . GLU A 1 2133 ? 190.444 159.001 164.801 1.00 13.78 ? 2133 GLU A CG    1 
ATOM   5421  C  CD    . GLU A 1 2133 ? 189.136 158.527 165.397 1.00 14.39 ? 2133 GLU A CD    1 
ATOM   5422  O  OE1   . GLU A 1 2133 ? 189.173 157.723 166.349 1.00 13.59 ? 2133 GLU A OE1   1 
ATOM   5423  O  OE2   . GLU A 1 2133 ? 188.070 158.959 164.911 1.00 17.42 ? 2133 GLU A OE2   1 
ATOM   5424  N  N     . GLN A 1 2134 ? 194.679 157.340 165.800 1.00 11.11 ? 2134 GLN A N     1 
ATOM   5425  C  CA    . GLN A 1 2134 ? 195.836 157.033 166.635 1.00 12.27 ? 2134 GLN A CA    1 
ATOM   5426  C  C     . GLN A 1 2134 ? 197.036 157.892 166.252 1.00 11.08 ? 2134 GLN A C     1 
ATOM   5427  O  O     . GLN A 1 2134 ? 197.750 158.389 167.127 1.00 10.94 ? 2134 GLN A O     1 
ATOM   5428  C  CB    . GLN A 1 2134 ? 196.182 155.549 166.544 1.00 12.15 ? 2134 GLN A CB    1 
ATOM   5429  C  CG    . GLN A 1 2134 ? 195.197 154.643 167.259 1.00 11.02 ? 2134 GLN A CG    1 
ATOM   5430  C  CD    . GLN A 1 2134 ? 195.811 153.330 167.686 1.00 15.46 ? 2134 GLN A CD    1 
ATOM   5431  O  OE1   . GLN A 1 2134 ? 197.014 153.115 167.541 1.00 18.09 ? 2134 GLN A OE1   1 
ATOM   5432  N  NE2   . GLN A 1 2134 ? 194.986 152.438 168.221 1.00 20.27 ? 2134 GLN A NE2   1 
ATOM   5433  N  N     . GLU A 1 2135 ? 197.265 158.082 164.951 1.00 14.21 ? 2135 GLU A N     1 
ATOM   5434  C  CA    . GLU A 1 2135 ? 198.377 158.917 164.510 1.00 10.79 ? 2135 GLU A CA    1 
ATOM   5435  C  C     . GLU A 1 2135 ? 198.189 160.369 164.930 1.00 9.89  ? 2135 GLU A C     1 
ATOM   5436  O  O     . GLU A 1 2135 ? 199.172 161.062 165.219 1.00 12.07 ? 2135 GLU A O     1 
ATOM   5437  C  CB    . GLU A 1 2135 ? 198.542 158.813 162.993 1.00 13.69 ? 2135 GLU A CB    1 
ATOM   5438  C  CG    . GLU A 1 2135 ? 199.776 159.500 162.446 1.00 15.51 ? 2135 GLU A CG    1 
ATOM   5439  C  CD    . GLU A 1 2135 ? 199.545 160.112 161.080 1.00 28.13 ? 2135 GLU A CD    1 
ATOM   5440  O  OE1   . GLU A 1 2135 ? 200.526 160.263 160.321 1.00 34.51 ? 2135 GLU A OE1   1 
ATOM   5441  O  OE2   . GLU A 1 2135 ? 198.383 160.444 160.761 1.00 29.61 ? 2135 GLU A OE2   1 
ATOM   5442  N  N     . ILE A 1 2136 ? 196.942 160.844 164.972 1.00 12.21 ? 2136 ILE A N     1 
ATOM   5443  C  CA    . ILE A 1 2136 ? 196.668 162.197 165.443 1.00 6.73  ? 2136 ILE A CA    1 
ATOM   5444  C  C     . ILE A 1 2136 ? 197.077 162.338 166.904 1.00 6.53  ? 2136 ILE A C     1 
ATOM   5445  O  O     . ILE A 1 2136 ? 197.718 163.320 167.298 1.00 8.12  ? 2136 ILE A O     1 
ATOM   5446  C  CB    . ILE A 1 2136 ? 195.181 162.541 165.239 1.00 10.11 ? 2136 ILE A CB    1 
ATOM   5447  C  CG1   . ILE A 1 2136 ? 194.847 162.587 163.751 1.00 10.12 ? 2136 ILE A CG1   1 
ATOM   5448  C  CG2   . ILE A 1 2136 ? 194.836 163.862 165.907 1.00 7.71  ? 2136 ILE A CG2   1 
ATOM   5449  C  CD1   . ILE A 1 2136 ? 193.371 162.678 163.456 1.00 12.24 ? 2136 ILE A CD1   1 
ATOM   5450  N  N     . LEU A 1 2137 ? 196.714 161.352 167.727 1.00 6.93  ? 2137 LEU A N     1 
ATOM   5451  C  CA    . LEU A 1 2137 ? 197.040 161.407 169.148 1.00 5.61  ? 2137 LEU A CA    1 
ATOM   5452  C  C     . LEU A 1 2137 ? 198.546 161.338 169.377 1.00 7.31  ? 2137 LEU A C     1 
ATOM   5453  O  O     . LEU A 1 2137 ? 199.073 161.997 170.281 1.00 8.78  ? 2137 LEU A O     1 
ATOM   5454  C  CB    . LEU A 1 2137 ? 196.325 160.278 169.889 1.00 4.85  ? 2137 LEU A CB    1 
ATOM   5455  C  CG    . LEU A 1 2137 ? 196.283 160.349 171.417 1.00 5.21  ? 2137 LEU A CG    1 
ATOM   5456  C  CD1   . LEU A 1 2137 ? 195.691 161.665 171.884 1.00 7.96  ? 2137 LEU A CD1   1 
ATOM   5457  C  CD2   . LEU A 1 2137 ? 195.495 159.179 171.977 1.00 8.36  ? 2137 LEU A CD2   1 
ATOM   5458  N  N     . ILE A 1 2138 ? 199.254 160.541 168.574 1.00 4.68  ? 2138 ILE A N     1 
ATOM   5459  C  CA    . ILE A 1 2138 ? 200.702 160.427 168.729 1.00 6.73  ? 2138 ILE A CA    1 
ATOM   5460  C  C     . ILE A 1 2138 ? 201.378 161.754 168.409 1.00 7.23  ? 2138 ILE A C     1 
ATOM   5461  O  O     . ILE A 1 2138 ? 202.340 162.153 169.079 1.00 7.92  ? 2138 ILE A O     1 
ATOM   5462  C  CB    . ILE A 1 2138 ? 201.249 159.286 167.852 1.00 8.89  ? 2138 ILE A CB    1 
ATOM   5463  C  CG1   . ILE A 1 2138 ? 200.594 157.963 168.238 1.00 10.31 ? 2138 ILE A CG1   1 
ATOM   5464  C  CG2   . ILE A 1 2138 ? 202.755 159.181 167.987 1.00 8.07  ? 2138 ILE A CG2   1 
ATOM   5465  C  CD1   . ILE A 1 2138 ? 200.845 157.556 169.652 1.00 11.52 ? 2138 ILE A CD1   1 
ATOM   5466  N  N     . GLN A 1 2139 ? 200.892 162.453 167.383 1.00 5.41  ? 2139 GLN A N     1 
ATOM   5467  C  CA    . GLN A 1 2139 ? 201.460 163.749 167.030 1.00 5.14  ? 2139 GLN A CA    1 
ATOM   5468  C  C     . GLN A 1 2139 ? 201.314 164.745 168.173 1.00 6.97  ? 2139 GLN A C     1 
ATOM   5469  O  O     . GLN A 1 2139 ? 202.253 165.487 168.481 1.00 10.73 ? 2139 GLN A O     1 
ATOM   5470  C  CB    . GLN A 1 2139 ? 200.794 164.279 165.761 1.00 4.83  ? 2139 GLN A CB    1 
ATOM   5471  C  CG    . GLN A 1 2139 ? 201.429 165.533 165.204 1.00 7.20  ? 2139 GLN A CG    1 
ATOM   5472  C  CD    . GLN A 1 2139 ? 200.607 166.159 164.096 1.00 7.50  ? 2139 GLN A CD    1 
ATOM   5473  O  OE1   . GLN A 1 2139 ? 200.151 165.470 163.185 1.00 15.19 ? 2139 GLN A OE1   1 
ATOM   5474  N  NE2   . GLN A 1 2139 ? 200.418 167.469 164.166 1.00 7.80  ? 2139 GLN A NE2   1 
ATOM   5475  N  N     . SER A 1 2140 ? 200.148 164.770 168.820 1.00 6.37  ? 2140 SER A N     1 
ATOM   5476  C  CA    . SER A 1 2140 ? 199.953 165.665 169.954 1.00 5.01  ? 2140 SER A CA    1 
ATOM   5477  C  C     . SER A 1 2140 ? 200.877 165.304 171.111 1.00 4.73  ? 2140 SER A C     1 
ATOM   5478  O  O     . SER A 1 2140 ? 201.411 166.191 171.785 1.00 11.23 ? 2140 SER A O     1 
ATOM   5479  C  CB    . SER A 1 2140 ? 198.495 165.635 170.403 1.00 4.86  ? 2140 SER A CB    1 
ATOM   5480  O  OG    . SER A 1 2140 ? 197.634 165.889 169.309 1.00 13.49 ? 2140 SER A OG    1 
ATOM   5481  N  N     . VAL A 1 2141 ? 201.072 164.007 171.358 1.00 5.72  ? 2141 VAL A N     1 
ATOM   5482  C  CA    . VAL A 1 2141 ? 201.967 163.573 172.427 1.00 5.94  ? 2141 VAL A CA    1 
ATOM   5483  C  C     . VAL A 1 2141 ? 203.395 164.017 172.135 1.00 4.61  ? 2141 VAL A C     1 
ATOM   5484  O  O     . VAL A 1 2141 ? 204.082 164.571 172.999 1.00 5.90  ? 2141 VAL A O     1 
ATOM   5485  C  CB    . VAL A 1 2141 ? 201.879 162.048 172.613 1.00 3.60  ? 2141 VAL A CB    1 
ATOM   5486  C  CG1   . VAL A 1 2141 ? 203.025 161.548 173.477 1.00 6.72  ? 2141 VAL A CG1   1 
ATOM   5487  C  CG2   . VAL A 1 2141 ? 200.549 161.667 173.224 1.00 2.79  ? 2141 VAL A CG2   1 
ATOM   5488  N  N     . CYS A 1 2142 ? 203.856 163.791 170.904 1.00 3.26  ? 2142 CYS A N     1 
ATOM   5489  C  CA    . CYS A 1 2142 ? 205.244 164.092 170.573 1.00 4.89  ? 2142 CYS A CA    1 
ATOM   5490  C  C     . CYS A 1 2142 ? 205.492 165.595 170.504 1.00 6.87  ? 2142 CYS A C     1 
ATOM   5491  O  O     . CYS A 1 2142 ? 206.558 166.070 170.908 1.00 6.28  ? 2142 CYS A O     1 
ATOM   5492  C  CB    . CYS A 1 2142 ? 205.618 163.416 169.256 1.00 5.03  ? 2142 CYS A CB    1 
ATOM   5493  S  SG    . CYS A 1 2142 ? 205.748 161.617 169.377 1.00 12.58 ? 2142 CYS A SG    1 
ATOM   5494  N  N     . GLU A 1 2143 ? 204.522 166.359 169.999 1.00 4.56  ? 2143 GLU A N     1 
ATOM   5495  C  CA    . GLU A 1 2143 ? 204.661 167.809 169.971 1.00 3.61  ? 2143 GLU A CA    1 
ATOM   5496  C  C     . GLU A 1 2143 ? 204.693 168.419 171.366 1.00 4.70  ? 2143 GLU A C     1 
ATOM   5497  O  O     . GLU A 1 2143 ? 205.132 169.562 171.517 1.00 10.31 ? 2143 GLU A O     1 
ATOM   5498  C  CB    . GLU A 1 2143 ? 203.519 168.431 169.167 1.00 6.66  ? 2143 GLU A CB    1 
ATOM   5499  C  CG    . GLU A 1 2143 ? 203.588 168.189 167.670 1.00 7.68  ? 2143 GLU A CG    1 
ATOM   5500  C  CD    . GLU A 1 2143 ? 202.746 169.177 166.892 1.00 14.43 ? 2143 GLU A CD    1 
ATOM   5501  O  OE1   . GLU A 1 2143 ? 201.996 168.747 165.993 1.00 11.66 ? 2143 GLU A OE1   1 
ATOM   5502  O  OE2   . GLU A 1 2143 ? 202.819 170.384 167.194 1.00 26.55 ? 2143 GLU A OE2   1 
ATOM   5503  N  N     . THR A 1 2144 ? 204.249 167.684 172.384 1.00 4.52  ? 2144 THR A N     1 
ATOM   5504  C  CA    . THR A 1 2144 ? 204.108 168.227 173.726 1.00 2.78  ? 2144 THR A CA    1 
ATOM   5505  C  C     . THR A 1 2144 ? 205.019 167.562 174.749 1.00 4.20  ? 2144 THR A C     1 
ATOM   5506  O  O     . THR A 1 2144 ? 205.547 168.251 175.624 1.00 8.85  ? 2144 THR A O     1 
ATOM   5507  C  CB    . THR A 1 2144 ? 202.645 168.109 174.181 1.00 6.98  ? 2144 THR A CB    1 
ATOM   5508  O  OG1   . THR A 1 2144 ? 201.838 169.024 173.433 1.00 10.96 ? 2144 THR A OG1   1 
ATOM   5509  C  CG2   . THR A 1 2144 ? 202.496 168.463 175.640 1.00 13.09 ? 2144 THR A CG2   1 
ATOM   5510  N  N     . MET A 1 2145 ? 205.242 166.251 174.645 1.00 5.64  ? 2145 MET A N     1 
ATOM   5511  C  CA    . MET A 1 2145 ? 206.110 165.510 175.555 1.00 3.42  ? 2145 MET A CA    1 
ATOM   5512  C  C     . MET A 1 2145 ? 207.568 165.447 175.124 1.00 2.02  ? 2145 MET A C     1 
ATOM   5513  O  O     . MET A 1 2145 ? 208.449 165.500 175.982 1.00 2.57  ? 2145 MET A O     1 
ATOM   5514  C  CB    . MET A 1 2145 ? 205.599 164.073 175.728 1.00 6.37  ? 2145 MET A CB    1 
ATOM   5515  C  CG    . MET A 1 2145 ? 204.249 163.905 176.416 1.00 8.61  ? 2145 MET A CG    1 
ATOM   5516  S  SD    . MET A 1 2145 ? 204.208 164.504 178.119 1.00 38.89 ? 2145 MET A SD    1 
ATOM   5517  C  CE    . MET A 1 2145 ? 203.368 166.068 177.955 1.00 11.11 ? 2145 MET A CE    1 
ATOM   5518  N  N     . VAL A 1 2146 ? 207.844 165.315 173.824 1.00 1.64  ? 2146 VAL A N     1 
ATOM   5519  C  CA    . VAL A 1 2146 ? 209.220 165.092 173.373 1.00 1.91  ? 2146 VAL A CA    1 
ATOM   5520  C  C     . VAL A 1 2146 ? 210.163 166.235 173.742 1.00 1.17  ? 2146 VAL A C     1 
ATOM   5521  O  O     . VAL A 1 2146 ? 211.278 165.955 174.214 1.00 1.65  ? 2146 VAL A O     1 
ATOM   5522  C  CB    . VAL A 1 2146 ? 209.238 164.773 171.868 1.00 1.92  ? 2146 VAL A CB    1 
ATOM   5523  C  CG1   . VAL A 1 2146 ? 210.613 165.040 171.271 1.00 1.13  ? 2146 VAL A CG1   1 
ATOM   5524  C  CG2   . VAL A 1 2146 ? 208.826 163.330 171.633 1.00 1.37  ? 2146 VAL A CG2   1 
ATOM   5525  N  N     . PRO A 1 2147 ? 209.807 167.514 173.563 1.00 1.78  ? 2147 PRO A N     1 
ATOM   5526  C  CA    . PRO A 1 2147 ? 210.779 168.583 173.855 1.00 1.55  ? 2147 PRO A CA    1 
ATOM   5527  C  C     . PRO A 1 2147 ? 211.264 168.620 175.294 1.00 0.78  ? 2147 PRO A C     1 
ATOM   5528  O  O     . PRO A 1 2147 ? 212.338 169.176 175.550 1.00 1.55  ? 2147 PRO A O     1 
ATOM   5529  C  CB    . PRO A 1 2147 ? 210.008 169.860 173.493 1.00 1.21  ? 2147 PRO A CB    1 
ATOM   5530  C  CG    . PRO A 1 2147 ? 209.042 169.414 172.473 1.00 0.93  ? 2147 PRO A CG    1 
ATOM   5531  C  CD    . PRO A 1 2147 ? 208.585 168.077 172.959 1.00 0.88  ? 2147 PRO A CD    1 
ATOM   5532  N  N     . LYS A 1 2148 ? 210.514 168.060 176.243 1.00 1.15  ? 2148 LYS A N     1 
ATOM   5533  C  CA    . LYS A 1 2148 ? 210.942 168.048 177.637 1.00 1.07  ? 2148 LYS A CA    1 
ATOM   5534  C  C     . LYS A 1 2148 ? 211.899 166.908 177.958 1.00 1.05  ? 2148 LYS A C     1 
ATOM   5535  O  O     . LYS A 1 2148 ? 212.479 166.898 179.048 1.00 2.51  ? 2148 LYS A O     1 
ATOM   5536  C  CB    . LYS A 1 2148 ? 209.723 167.961 178.559 1.00 1.17  ? 2148 LYS A CB    1 
ATOM   5537  C  CG    . LYS A 1 2148 ? 209.290 166.544 178.896 1.00 2.46  ? 2148 LYS A CG    1 
ATOM   5538  C  CD    . LYS A 1 2148 ? 208.170 166.526 179.918 1.00 4.09  ? 2148 LYS A CD    1 
ATOM   5539  C  CE    . LYS A 1 2148 ? 206.975 167.328 179.436 1.00 10.67 ? 2148 LYS A CE    1 
ATOM   5540  N  NZ    . LYS A 1 2148 ? 205.809 167.188 180.344 1.00 13.03 ? 2148 LYS A NZ    1 
ATOM   5541  N  N     . LEU A 1 2149 ? 212.089 165.967 177.043 1.00 1.23  ? 2149 LEU A N     1 
ATOM   5542  C  CA    . LEU A 1 2149 ? 212.822 164.748 177.348 1.00 1.46  ? 2149 LEU A CA    1 
ATOM   5543  C  C     . LEU A 1 2149 ? 214.326 164.962 177.264 1.00 1.66  ? 2149 LEU A C     1 
ATOM   5544  O  O     . LEU A 1 2149 ? 214.819 165.689 176.399 1.00 2.61  ? 2149 LEU A O     1 
ATOM   5545  C  CB    . LEU A 1 2149 ? 212.409 163.636 176.389 1.00 2.22  ? 2149 LEU A CB    1 
ATOM   5546  C  CG    . LEU A 1 2149 ? 210.964 163.163 176.502 1.00 2.04  ? 2149 LEU A CG    1 
ATOM   5547  C  CD1   . LEU A 1 2149 ? 210.712 162.073 175.483 1.00 2.12  ? 2149 LEU A CD1   1 
ATOM   5548  C  CD2   . LEU A 1 2149 ? 210.652 162.688 177.909 1.00 1.35  ? 2149 LEU A CD2   1 
ATOM   5549  N  N     . VAL A 1 2150 ? 215.056 164.315 178.171 1.00 2.37  ? 2150 VAL A N     1 
ATOM   5550  C  CA    . VAL A 1 2150 ? 216.507 164.234 178.066 1.00 3.63  ? 2150 VAL A CA    1 
ATOM   5551  C  C     . VAL A 1 2150 ? 216.829 163.225 176.973 1.00 4.30  ? 2150 VAL A C     1 
ATOM   5552  O  O     . VAL A 1 2150 ? 215.948 162.487 176.522 1.00 5.12  ? 2150 VAL A O     1 
ATOM   5553  C  CB    . VAL A 1 2150 ? 217.161 163.852 179.407 1.00 3.13  ? 2150 VAL A CB    1 
ATOM   5554  C  CG1   . VAL A 1 2150 ? 216.875 164.918 180.459 1.00 1.27  ? 2150 VAL A CG1   1 
ATOM   5555  C  CG2   . VAL A 1 2150 ? 216.685 162.483 179.871 1.00 4.94  ? 2150 VAL A CG2   1 
ATOM   5556  N  N     . ALA A 1 2151 ? 218.091 163.189 176.541 1.00 4.58  ? 2151 ALA A N     1 
ATOM   5557  C  CA    . ALA A 1 2151 ? 218.448 162.408 175.360 1.00 5.03  ? 2151 ALA A CA    1 
ATOM   5558  C  C     . ALA A 1 2151 ? 218.172 160.921 175.557 1.00 9.15  ? 2151 ALA A C     1 
ATOM   5559  O  O     . ALA A 1 2151 ? 217.701 160.246 174.635 1.00 6.90  ? 2151 ALA A O     1 
ATOM   5560  C  CB    . ALA A 1 2151 ? 219.917 162.636 175.005 1.00 2.84  ? 2151 ALA A CB    1 
ATOM   5561  N  N     . GLU A 1 2152 ? 218.459 160.392 176.748 1.00 9.65  ? 2152 GLU A N     1 
ATOM   5562  C  CA    . GLU A 1 2152 ? 218.323 158.954 176.958 1.00 7.48  ? 2152 GLU A CA    1 
ATOM   5563  C  C     . GLU A 1 2152 ? 216.872 158.530 177.162 1.00 10.18 ? 2152 GLU A C     1 
ATOM   5564  O  O     . GLU A 1 2152 ? 216.565 157.338 177.085 1.00 15.40 ? 2152 GLU A O     1 
ATOM   5565  C  CB    . GLU A 1 2152 ? 219.205 158.515 178.130 1.00 13.18 ? 2152 GLU A CB    1 
ATOM   5566  C  CG    . GLU A 1 2152 ? 218.899 159.176 179.465 1.00 18.37 ? 2152 GLU A CG    1 
ATOM   5567  C  CD    . GLU A 1 2152 ? 217.816 158.473 180.253 1.00 15.11 ? 2152 GLU A CD    1 
ATOM   5568  O  OE1   . GLU A 1 2152 ? 217.536 157.288 179.974 1.00 14.57 ? 2152 GLU A OE1   1 
ATOM   5569  O  OE2   . GLU A 1 2152 ? 217.256 159.107 181.168 1.00 18.37 ? 2152 GLU A OE2   1 
ATOM   5570  N  N     . ASP A 1 2153 ? 215.967 159.480 177.409 1.00 8.57  ? 2153 ASP A N     1 
ATOM   5571  C  CA    . ASP A 1 2153 ? 214.549 159.149 177.510 1.00 6.93  ? 2153 ASP A CA    1 
ATOM   5572  C  C     . ASP A 1 2153 ? 213.832 159.175 176.166 1.00 7.08  ? 2153 ASP A C     1 
ATOM   5573  O  O     . ASP A 1 2153 ? 212.750 158.590 176.052 1.00 11.98 ? 2153 ASP A O     1 
ATOM   5574  C  CB    . ASP A 1 2153 ? 213.843 160.100 178.476 1.00 6.88  ? 2153 ASP A CB    1 
ATOM   5575  C  CG    . ASP A 1 2153 ? 214.082 159.745 179.926 1.00 7.65  ? 2153 ASP A CG    1 
ATOM   5576  O  OD1   . ASP A 1 2153 ? 214.645 158.666 180.192 1.00 17.44 ? 2153 ASP A OD1   1 
ATOM   5577  O  OD2   . ASP A 1 2153 ? 213.705 160.545 180.803 1.00 8.94  ? 2153 ASP A OD2   1 
ATOM   5578  N  N     . ILE A 1 2154 ? 214.403 159.835 175.157 1.00 6.07  ? 2154 ILE A N     1 
ATOM   5579  C  CA    . ILE A 1 2154 ? 213.733 159.920 173.857 1.00 6.47  ? 2154 ILE A CA    1 
ATOM   5580  C  C     . ILE A 1 2154 ? 213.511 158.544 173.233 1.00 8.54  ? 2154 ILE A C     1 
ATOM   5581  O  O     . ILE A 1 2154 ? 212.377 158.259 172.814 1.00 15.53 ? 2154 ILE A O     1 
ATOM   5582  C  CB    . ILE A 1 2154 ? 214.499 160.881 172.930 1.00 4.66  ? 2154 ILE A CB    1 
ATOM   5583  C  CG1   . ILE A 1 2154 ? 214.577 162.275 173.557 1.00 4.93  ? 2154 ILE A CG1   1 
ATOM   5584  C  CG2   . ILE A 1 2154 ? 213.836 160.951 171.565 1.00 7.09  ? 2154 ILE A CG2   1 
ATOM   5585  C  CD1   . ILE A 1 2154 ? 215.506 163.216 172.836 1.00 6.31  ? 2154 ILE A CD1   1 
ATOM   5586  N  N     . PRO A 1 2155 ? 214.512 157.659 173.133 1.00 11.39 ? 2155 PRO A N     1 
ATOM   5587  C  CA    . PRO A 1 2155 ? 214.221 156.308 172.626 1.00 7.72  ? 2155 PRO A CA    1 
ATOM   5588  C  C     . PRO A 1 2155 ? 213.269 155.526 173.513 1.00 9.70  ? 2155 PRO A C     1 
ATOM   5589  O  O     . PRO A 1 2155 ? 212.507 154.696 173.003 1.00 14.45 ? 2155 PRO A O     1 
ATOM   5590  C  CB    . PRO A 1 2155 ? 215.607 155.651 172.562 1.00 8.53  ? 2155 PRO A CB    1 
ATOM   5591  C  CG    . PRO A 1 2155 ? 216.564 156.783 172.535 1.00 7.15  ? 2155 PRO A CG    1 
ATOM   5592  C  CD    . PRO A 1 2155 ? 215.950 157.814 173.415 1.00 6.89  ? 2155 PRO A CD    1 
ATOM   5593  N  N     . LEU A 1 2156 ? 213.299 155.759 174.828 1.00 9.84  ? 2156 LEU A N     1 
ATOM   5594  C  CA    . LEU A 1 2156 ? 212.399 155.051 175.732 1.00 7.57  ? 2156 LEU A CA    1 
ATOM   5595  C  C     . LEU A 1 2156 ? 210.942 155.364 175.425 1.00 8.33  ? 2156 LEU A C     1 
ATOM   5596  O  O     . LEU A 1 2156 ? 210.103 154.458 175.364 1.00 12.54 ? 2156 LEU A O     1 
ATOM   5597  C  CB    . LEU A 1 2156 ? 212.720 155.410 177.182 1.00 9.17  ? 2156 LEU A CB    1 
ATOM   5598  C  CG    . LEU A 1 2156 ? 214.022 154.915 177.809 1.00 10.17 ? 2156 LEU A CG    1 
ATOM   5599  C  CD1   . LEU A 1 2156 ? 213.920 154.974 179.319 1.00 18.59 ? 2156 LEU A CD1   1 
ATOM   5600  C  CD2   . LEU A 1 2156 ? 214.315 153.496 177.366 1.00 16.54 ? 2156 LEU A CD2   1 
ATOM   5601  N  N     . LEU A 1 2157 ? 210.621 156.643 175.221 1.00 14.38 ? 2157 LEU A N     1 
ATOM   5602  C  CA    . LEU A 1 2157 ? 209.229 157.026 175.009 1.00 9.54  ? 2157 LEU A CA    1 
ATOM   5603  C  C     . LEU A 1 2157 ? 208.708 156.509 173.673 1.00 6.90  ? 2157 LEU A C     1 
ATOM   5604  O  O     . LEU A 1 2157 ? 207.532 156.148 173.559 1.00 10.75 ? 2157 LEU A O     1 
ATOM   5605  C  CB    . LEU A 1 2157 ? 209.083 158.547 175.130 1.00 10.59 ? 2157 LEU A CB    1 
ATOM   5606  C  CG    . LEU A 1 2157 ? 207.677 159.158 175.120 1.00 6.08  ? 2157 LEU A CG    1 
ATOM   5607  C  CD1   . LEU A 1 2157 ? 207.642 160.430 175.930 1.00 10.97 ? 2157 LEU A CD1   1 
ATOM   5608  C  CD2   . LEU A 1 2157 ? 207.267 159.482 173.705 1.00 2.43  ? 2157 LEU A CD2   1 
ATOM   5609  N  N     . PHE A 1 2158 ? 209.567 156.457 172.654 1.00 5.67  ? 2158 PHE A N     1 
ATOM   5610  C  CA    . PHE A 1 2158 ? 209.134 155.904 171.376 1.00 10.33 ? 2158 PHE A CA    1 
ATOM   5611  C  C     . PHE A 1 2158 ? 208.957 154.393 171.442 1.00 9.33  ? 2158 PHE A C     1 
ATOM   5612  O  O     . PHE A 1 2158 ? 208.085 153.845 170.760 1.00 10.60 ? 2158 PHE A O     1 
ATOM   5613  C  CB    . PHE A 1 2158 ? 210.115 156.293 170.272 1.00 9.26  ? 2158 PHE A CB    1 
ATOM   5614  C  CG    . PHE A 1 2158 ? 209.916 157.691 169.766 1.00 11.29 ? 2158 PHE A CG    1 
ATOM   5615  C  CD1   . PHE A 1 2158 ? 208.872 157.983 168.908 1.00 8.97  ? 2158 PHE A CD1   1 
ATOM   5616  C  CD2   . PHE A 1 2158 ? 210.760 158.713 170.160 1.00 13.54 ? 2158 PHE A CD2   1 
ATOM   5617  C  CE1   . PHE A 1 2158 ? 208.679 159.268 168.446 1.00 12.44 ? 2158 PHE A CE1   1 
ATOM   5618  C  CE2   . PHE A 1 2158 ? 210.572 160.000 169.700 1.00 10.58 ? 2158 PHE A CE2   1 
ATOM   5619  C  CZ    . PHE A 1 2158 ? 209.530 160.277 168.843 1.00 10.41 ? 2158 PHE A CZ    1 
ATOM   5620  N  N     . SER A 1 2159 ? 209.767 153.702 172.249 1.00 10.44 ? 2159 SER A N     1 
ATOM   5621  C  CA    . SER A 1 2159 ? 209.501 152.292 172.508 1.00 11.54 ? 2159 SER A CA    1 
ATOM   5622  C  C     . SER A 1 2159 ? 208.172 152.117 173.229 1.00 11.59 ? 2159 SER A C     1 
ATOM   5623  O  O     . SER A 1 2159 ? 207.388 151.223 172.893 1.00 12.09 ? 2159 SER A O     1 
ATOM   5624  C  CB    . SER A 1 2159 ? 210.641 151.678 173.318 1.00 13.23 ? 2159 SER A CB    1 
ATOM   5625  O  OG    . SER A 1 2159 ? 211.845 151.695 172.578 1.00 24.39 ? 2159 SER A OG    1 
ATOM   5626  N  N     . LEU A 1 2160 ? 207.898 152.976 174.214 1.00 9.10  ? 2160 LEU A N     1 
ATOM   5627  C  CA    . LEU A 1 2160 ? 206.597 152.959 174.874 1.00 7.99  ? 2160 LEU A CA    1 
ATOM   5628  C  C     . LEU A 1 2160 ? 205.481 153.283 173.891 1.00 10.55 ? 2160 LEU A C     1 
ATOM   5629  O  O     . LEU A 1 2160 ? 204.391 152.705 173.964 1.00 14.47 ? 2160 LEU A O     1 
ATOM   5630  C  CB    . LEU A 1 2160 ? 206.584 153.948 176.037 1.00 6.72  ? 2160 LEU A CB    1 
ATOM   5631  C  CG    . LEU A 1 2160 ? 207.322 153.558 177.316 1.00 9.46  ? 2160 LEU A CG    1 
ATOM   5632  C  CD1   . LEU A 1 2160 ? 207.334 154.727 178.281 1.00 11.44 ? 2160 LEU A CD1   1 
ATOM   5633  C  CD2   . LEU A 1 2160 ? 206.678 152.342 177.956 1.00 14.22 ? 2160 LEU A CD2   1 
ATOM   5634  N  N     . LEU A 1 2161 ? 205.730 154.219 172.971 1.00 9.39  ? 2161 LEU A N     1 
ATOM   5635  C  CA    . LEU A 1 2161 ? 204.722 154.553 171.972 1.00 7.58  ? 2161 LEU A CA    1 
ATOM   5636  C  C     . LEU A 1 2161 ? 204.426 153.365 171.069 1.00 9.68  ? 2161 LEU A C     1 
ATOM   5637  O  O     . LEU A 1 2161 ? 203.264 153.096 170.743 1.00 13.76 ? 2161 LEU A O     1 
ATOM   5638  C  CB    . LEU A 1 2161 ? 205.174 155.747 171.135 1.00 10.31 ? 2161 LEU A CB    1 
ATOM   5639  C  CG    . LEU A 1 2161 ? 204.990 157.141 171.729 1.00 10.31 ? 2161 LEU A CG    1 
ATOM   5640  C  CD1   . LEU A 1 2161 ? 205.697 158.167 170.853 1.00 11.11 ? 2161 LEU A CD1   1 
ATOM   5641  C  CD2   . LEU A 1 2161 ? 203.524 157.478 171.918 1.00 6.13  ? 2161 LEU A CD2   1 
ATOM   5642  N  N     . SER A 1 2162 ? 205.467 152.643 170.647 1.00 10.62 ? 2162 SER A N     1 
ATOM   5643  C  CA    . SER A 1 2162 ? 205.251 151.456 169.832 1.00 12.91 ? 2162 SER A CA    1 
ATOM   5644  C  C     . SER A 1 2162 ? 204.567 150.356 170.628 1.00 12.45 ? 2162 SER A C     1 
ATOM   5645  O  O     . SER A 1 2162 ? 203.840 149.537 170.056 1.00 19.69 ? 2162 SER A O     1 
ATOM   5646  C  CB    . SER A 1 2162 ? 206.578 150.957 169.260 1.00 12.04 ? 2162 SER A CB    1 
ATOM   5647  O  OG    . SER A 1 2162 ? 207.435 150.499 170.289 1.00 17.71 ? 2162 SER A OG    1 
ATOM   5648  N  N     . ASP A 1 2163 ? 204.788 150.324 171.943 1.00 14.38 ? 2163 ASP A N     1 
ATOM   5649  C  CA    . ASP A 1 2163 ? 204.152 149.316 172.785 1.00 10.15 ? 2163 ASP A CA    1 
ATOM   5650  C  C     . ASP A 1 2163 ? 202.647 149.538 172.879 1.00 11.84 ? 2163 ASP A C     1 
ATOM   5651  O  O     . ASP A 1 2163 ? 201.863 148.587 172.797 1.00 21.61 ? 2163 ASP A O     1 
ATOM   5652  C  CB    . ASP A 1 2163 ? 204.786 149.326 174.175 1.00 12.00 ? 2163 ASP A CB    1 
ATOM   5653  C  CG    . ASP A 1 2163 ? 206.067 148.522 174.232 1.00 27.22 ? 2163 ASP A CG    1 
ATOM   5654  O  OD1   . ASP A 1 2163 ? 206.017 147.311 173.937 1.00 37.14 ? 2163 ASP A OD1   1 
ATOM   5655  O  OD2   . ASP A 1 2163 ? 207.122 149.092 174.581 1.00 25.82 ? 2163 ASP A OD2   1 
ATOM   5656  N  N     . VAL A 1 2164 ? 202.225 150.788 173.051 1.00 9.57  ? 2164 VAL A N     1 
ATOM   5657  C  CA    . VAL A 1 2164 ? 200.811 151.081 173.252 1.00 11.14 ? 2164 VAL A CA    1 
ATOM   5658  C  C     . VAL A 1 2164 ? 200.099 151.403 171.938 1.00 11.33 ? 2164 VAL A C     1 
ATOM   5659  O  O     . VAL A 1 2164 ? 198.883 151.216 171.832 1.00 13.59 ? 2164 VAL A O     1 
ATOM   5660  C  CB    . VAL A 1 2164 ? 200.660 152.227 174.268 1.00 10.44 ? 2164 VAL A CB    1 
ATOM   5661  C  CG1   . VAL A 1 2164 ? 199.211 152.392 174.683 1.00 10.44 ? 2164 VAL A CG1   1 
ATOM   5662  C  CG2   . VAL A 1 2164 ? 201.528 151.969 175.487 1.00 10.34 ? 2164 VAL A CG2   1 
ATOM   5663  N  N     . PHE A 1 2165 ? 200.829 151.872 170.929 1.00 9.57  ? 2165 PHE A N     1 
ATOM   5664  C  CA    . PHE A 1 2165 ? 200.261 152.232 169.630 1.00 9.42  ? 2165 PHE A CA    1 
ATOM   5665  C  C     . PHE A 1 2165 ? 201.074 151.551 168.537 1.00 14.88 ? 2165 PHE A C     1 
ATOM   5666  O  O     . PHE A 1 2165 ? 201.868 152.200 167.841 1.00 18.52 ? 2165 PHE A O     1 
ATOM   5667  C  CB    . PHE A 1 2165 ? 200.242 153.748 169.436 1.00 11.24 ? 2165 PHE A CB    1 
ATOM   5668  C  CG    . PHE A 1 2165 ? 199.475 154.492 170.497 1.00 13.02 ? 2165 PHE A CG    1 
ATOM   5669  C  CD1   . PHE A 1 2165 ? 200.079 154.844 171.694 1.00 13.35 ? 2165 PHE A CD1   1 
ATOM   5670  C  CD2   . PHE A 1 2165 ? 198.157 154.859 170.287 1.00 10.20 ? 2165 PHE A CD2   1 
ATOM   5671  C  CE1   . PHE A 1 2165 ? 199.381 155.535 172.662 1.00 8.48  ? 2165 PHE A CE1   1 
ATOM   5672  C  CE2   . PHE A 1 2165 ? 197.454 155.551 171.253 1.00 11.20 ? 2165 PHE A CE2   1 
ATOM   5673  C  CZ    . PHE A 1 2165 ? 198.067 155.890 172.442 1.00 8.14  ? 2165 PHE A CZ    1 
ATOM   5674  N  N     . PRO A 1 2166 ? 200.905 150.240 168.357 1.00 16.23 ? 2166 PRO A N     1 
ATOM   5675  C  CA    . PRO A 1 2166 ? 201.718 149.519 167.369 1.00 12.19 ? 2166 PRO A CA    1 
ATOM   5676  C  C     . PRO A 1 2166 ? 201.472 150.023 165.954 1.00 11.87 ? 2166 PRO A C     1 
ATOM   5677  O  O     . PRO A 1 2166 ? 200.344 150.346 165.573 1.00 20.90 ? 2166 PRO A O     1 
ATOM   5678  C  CB    . PRO A 1 2166 ? 201.262 148.064 167.531 1.00 10.89 ? 2166 PRO A CB    1 
ATOM   5679  C  CG    . PRO A 1 2166 ? 200.617 148.006 168.874 1.00 15.39 ? 2166 PRO A CG    1 
ATOM   5680  C  CD    . PRO A 1 2166 ? 199.976 149.342 169.058 1.00 14.12 ? 2166 PRO A CD    1 
ATOM   5681  N  N     . GLY A 1 2167 ? 202.546 150.081 165.170 1.00 15.71 ? 2167 GLY A N     1 
ATOM   5682  C  CA    . GLY A 1 2167 ? 202.442 150.438 163.771 1.00 14.06 ? 2167 GLY A CA    1 
ATOM   5683  C  C     . GLY A 1 2167 ? 202.135 151.889 163.491 1.00 18.50 ? 2167 GLY A C     1 
ATOM   5684  O  O     . GLY A 1 2167 ? 201.796 152.226 162.354 1.00 20.81 ? 2167 GLY A O     1 
ATOM   5685  N  N     . VAL A 1 2168 ? 202.239 152.761 164.488 1.00 19.67 ? 2168 VAL A N     1 
ATOM   5686  C  CA    . VAL A 1 2168 ? 201.929 154.177 164.338 1.00 12.17 ? 2168 VAL A CA    1 
ATOM   5687  C  C     . VAL A 1 2168 ? 203.232 154.951 164.461 1.00 16.70 ? 2168 VAL A C     1 
ATOM   5688  O  O     . VAL A 1 2168 ? 203.940 154.834 165.468 1.00 20.07 ? 2168 VAL A O     1 
ATOM   5689  C  CB    . VAL A 1 2168 ? 200.900 154.642 165.380 1.00 16.67 ? 2168 VAL A CB    1 
ATOM   5690  C  CG1   . VAL A 1 2168 ? 200.540 156.097 165.150 1.00 20.12 ? 2168 VAL A CG1   1 
ATOM   5691  C  CG2   . VAL A 1 2168 ? 199.664 153.762 165.326 1.00 15.34 ? 2168 VAL A CG2   1 
ATOM   5692  N  N     . GLN A 1 2169 ? 203.543 155.746 163.443 1.00 22.56 ? 2169 GLN A N     1 
ATOM   5693  C  CA    . GLN A 1 2169 ? 204.816 156.442 163.352 1.00 22.19 ? 2169 GLN A CA    1 
ATOM   5694  C  C     . GLN A 1 2169 ? 204.615 157.945 163.473 1.00 22.13 ? 2169 GLN A C     1 
ATOM   5695  O  O     . GLN A 1 2169 ? 203.598 158.487 163.033 1.00 24.66 ? 2169 GLN A O     1 
ATOM   5696  C  CB    . GLN A 1 2169 ? 205.526 156.116 162.035 1.00 25.10 ? 2169 GLN A CB    1 
ATOM   5697  C  CG    . GLN A 1 2169 ? 206.052 154.699 161.960 1.00 21.92 ? 2169 GLN A CG    1 
ATOM   5698  C  CD    . GLN A 1 2169 ? 206.828 154.305 163.201 1.00 27.14 ? 2169 GLN A CD    1 
ATOM   5699  O  OE1   . GLN A 1 2169 ? 206.424 153.408 163.942 1.00 27.71 ? 2169 GLN A OE1   1 
ATOM   5700  N  NE2   . GLN A 1 2169 ? 207.949 154.975 163.436 1.00 30.02 ? 2169 GLN A NE2   1 
ATOM   5701  N  N     . TYR A 1 2170 ? 205.596 158.611 164.074 1.00 18.95 ? 2170 TYR A N     1 
ATOM   5702  C  CA    . TYR A 1 2170 ? 205.594 160.056 164.235 1.00 14.15 ? 2170 TYR A CA    1 
ATOM   5703  C  C     . TYR A 1 2170 ? 206.500 160.678 163.183 1.00 17.76 ? 2170 TYR A C     1 
ATOM   5704  O  O     . TYR A 1 2170 ? 207.660 160.277 163.044 1.00 24.84 ? 2170 TYR A O     1 
ATOM   5705  C  CB    . TYR A 1 2170 ? 206.070 160.450 165.633 1.00 17.46 ? 2170 TYR A CB    1 
ATOM   5706  C  CG    . TYR A 1 2170 ? 206.216 161.940 165.825 1.00 17.47 ? 2170 TYR A CG    1 
ATOM   5707  C  CD1   . TYR A 1 2170 ? 205.162 162.798 165.548 1.00 13.24 ? 2170 TYR A CD1   1 
ATOM   5708  C  CD2   . TYR A 1 2170 ? 207.412 162.491 166.264 1.00 15.46 ? 2170 TYR A CD2   1 
ATOM   5709  C  CE1   . TYR A 1 2170 ? 205.289 164.162 165.715 1.00 16.12 ? 2170 TYR A CE1   1 
ATOM   5710  C  CE2   . TYR A 1 2170 ? 207.550 163.856 166.432 1.00 13.92 ? 2170 TYR A CE2   1 
ATOM   5711  C  CZ    . TYR A 1 2170 ? 206.485 164.687 166.157 1.00 13.97 ? 2170 TYR A CZ    1 
ATOM   5712  O  OH    . TYR A 1 2170 ? 206.611 166.045 166.325 1.00 15.59 ? 2170 TYR A OH    1 
ATOM   5713  N  N     . HIS A 1 2171 ? 205.975 161.652 162.448 1.00 20.64 ? 2171 HIS A N     1 
ATOM   5714  C  CA    . HIS A 1 2171 ? 206.753 162.353 161.431 1.00 24.69 ? 2171 HIS A CA    1 
ATOM   5715  C  C     . HIS A 1 2171 ? 206.498 163.845 161.571 1.00 20.64 ? 2171 HIS A C     1 
ATOM   5716  O  O     . HIS A 1 2171 ? 205.383 164.314 161.327 1.00 28.49 ? 2171 HIS A O     1 
ATOM   5717  C  CB    . HIS A 1 2171 ? 206.400 161.865 160.027 1.00 24.25 ? 2171 HIS A CB    1 
ATOM   5718  C  CG    . HIS A 1 2171 ? 206.888 160.481 159.731 1.00 29.93 ? 2171 HIS A CG    1 
ATOM   5719  N  ND1   . HIS A 1 2171 ? 206.172 159.352 160.065 1.00 33.77 ? 2171 HIS A ND1   1 
ATOM   5720  C  CD2   . HIS A 1 2171 ? 208.024 160.045 159.139 1.00 31.87 ? 2171 HIS A CD2   1 
ATOM   5721  C  CE1   . HIS A 1 2171 ? 206.845 158.280 159.685 1.00 34.58 ? 2171 HIS A CE1   1 
ATOM   5722  N  NE2   . HIS A 1 2171 ? 207.973 158.672 159.121 1.00 37.66 ? 2171 HIS A NE2   1 
ATOM   5723  N  N     . ARG A 1 2172 ? 207.530 164.586 161.966 1.00 19.61 ? 2172 ARG A N     1 
ATOM   5724  C  CA    . ARG A 1 2172 ? 207.415 166.031 162.071 1.00 19.22 ? 2172 ARG A CA    1 
ATOM   5725  C  C     . ARG A 1 2172 ? 207.212 166.648 160.694 1.00 24.60 ? 2172 ARG A C     1 
ATOM   5726  O  O     . ARG A 1 2172 ? 207.691 166.135 159.679 1.00 27.84 ? 2172 ARG A O     1 
ATOM   5727  C  CB    . ARG A 1 2172 ? 208.667 166.626 162.710 1.00 18.59 ? 2172 ARG A CB    1 
ATOM   5728  C  CG    . ARG A 1 2172 ? 208.906 166.222 164.149 1.00 17.40 ? 2172 ARG A CG    1 
ATOM   5729  C  CD    . ARG A 1 2172 ? 210.182 166.856 164.674 1.00 24.76 ? 2172 ARG A CD    1 
ATOM   5730  N  NE    . ARG A 1 2172 ? 210.056 168.305 164.765 1.00 33.48 ? 2172 ARG A NE    1 
ATOM   5731  C  CZ    . ARG A 1 2172 ? 210.685 169.166 163.974 1.00 28.34 ? 2172 ARG A CZ    1 
ATOM   5732  N  NH1   . ARG A 1 2172 ? 211.492 168.757 163.010 1.00 24.62 ? 2172 ARG A NH1   1 
ATOM   5733  N  NH2   . ARG A 1 2172 ? 210.492 170.469 164.153 1.00 20.70 ? 2172 ARG A NH2   1 
ATOM   5734  N  N     . GLY A 1 2173 ? 206.488 167.763 160.664 1.00 24.60 ? 2173 GLY A N     1 
ATOM   5735  C  CA    . GLY A 1 2173 ? 206.409 168.544 159.445 1.00 24.19 ? 2173 GLY A CA    1 
ATOM   5736  C  C     . GLY A 1 2173 ? 207.752 169.176 159.126 1.00 25.34 ? 2173 GLY A C     1 
ATOM   5737  O  O     . GLY A 1 2173 ? 208.428 169.727 159.996 1.00 23.29 ? 2173 GLY A O     1 
ATOM   5738  N  N     . GLU A 1 2174 ? 208.147 169.083 157.858 1.00 25.07 ? 2174 GLU A N     1 
ATOM   5739  C  CA    . GLU A 1 2174 ? 209.410 169.665 157.409 1.00 22.23 ? 2174 GLU A CA    1 
ATOM   5740  C  C     . GLU A 1 2174 ? 209.131 171.139 157.148 1.00 23.57 ? 2174 GLU A C     1 
ATOM   5741  O  O     . GLU A 1 2174 ? 208.656 171.531 156.082 1.00 30.47 ? 2174 GLU A O     1 
ATOM   5742  C  CB    . GLU A 1 2174 ? 209.939 168.938 156.177 1.00 21.06 ? 2174 GLU A CB    1 
ATOM   5743  C  CG    . GLU A 1 2174 ? 211.367 169.305 155.793 1.00 25.77 ? 2174 GLU A CG    1 
ATOM   5744  C  CD    . GLU A 1 2174 ? 211.460 170.557 154.944 1.00 33.66 ? 2174 GLU A CD    1 
ATOM   5745  O  OE1   . GLU A 1 2174 ? 210.503 170.848 154.199 1.00 32.19 ? 2174 GLU A OE1   1 
ATOM   5746  O  OE2   . GLU A 1 2174 ? 212.493 171.254 155.027 1.00 31.02 ? 2174 GLU A OE2   1 
ATOM   5747  N  N     . MET A 1 2175 ? 209.414 171.968 158.154 1.00 17.16 ? 2175 MET A N     1 
ATOM   5748  C  CA    . MET A 1 2175 ? 209.026 173.379 158.145 1.00 14.11 ? 2175 MET A CA    1 
ATOM   5749  C  C     . MET A 1 2175 ? 210.054 174.202 157.368 1.00 12.22 ? 2175 MET A C     1 
ATOM   5750  O  O     . MET A 1 2175 ? 210.885 174.919 157.925 1.00 15.29 ? 2175 MET A O     1 
ATOM   5751  C  CB    . MET A 1 2175 ? 208.858 173.887 159.570 1.00 17.31 ? 2175 MET A CB    1 
ATOM   5752  C  CG    . MET A 1 2175 ? 207.695 173.250 160.308 1.00 17.62 ? 2175 MET A CG    1 
ATOM   5753  S  SD    . MET A 1 2175 ? 207.460 173.895 161.971 1.00 31.78 ? 2175 MET A SD    1 
ATOM   5754  C  CE    . MET A 1 2175 ? 208.824 173.123 162.835 1.00 10.52 ? 2175 MET A CE    1 
ATOM   5755  N  N     . THR A 1 2176 ? 209.959 174.106 156.038 1.00 13.50 ? 2176 THR A N     1 
ATOM   5756  C  CA    . THR A 1 2176 ? 210.912 174.791 155.172 1.00 12.13 ? 2176 THR A CA    1 
ATOM   5757  C  C     . THR A 1 2176 ? 210.869 176.300 155.369 1.00 8.37  ? 2176 THR A C     1 
ATOM   5758  O  O     . THR A 1 2176 ? 211.917 176.952 155.439 1.00 13.65 ? 2176 THR A O     1 
ATOM   5759  C  CB    . THR A 1 2176 ? 210.635 174.444 153.707 1.00 12.67 ? 2176 THR A CB    1 
ATOM   5760  O  OG1   . THR A 1 2176 ? 210.763 173.033 153.517 1.00 12.42 ? 2176 THR A OG1   1 
ATOM   5761  C  CG2   . THR A 1 2176 ? 211.611 175.162 152.793 1.00 18.41 ? 2176 THR A CG2   1 
ATOM   5762  N  N     . ALA A 1 2177 ? 209.668 176.873 155.465 1.00 10.21 ? 2177 ALA A N     1 
ATOM   5763  C  CA    . ALA A 1 2177 ? 209.543 178.323 155.540 1.00 7.15  ? 2177 ALA A CA    1 
ATOM   5764  C  C     . ALA A 1 2177 ? 210.233 178.882 156.779 1.00 8.66  ? 2177 ALA A C     1 
ATOM   5765  O  O     . ALA A 1 2177 ? 210.948 179.887 156.701 1.00 14.35 ? 2177 ALA A O     1 
ATOM   5766  C  CB    . ALA A 1 2177 ? 208.069 178.724 155.518 1.00 8.01  ? 2177 ALA A CB    1 
ATOM   5767  N  N     . LEU A 1 2178 ? 210.039 178.241 157.933 1.00 6.86  ? 2178 LEU A N     1 
ATOM   5768  C  CA    . LEU A 1 2178 ? 210.681 178.725 159.150 1.00 8.23  ? 2178 LEU A CA    1 
ATOM   5769  C  C     . LEU A 1 2178 ? 212.176 178.438 159.141 1.00 8.33  ? 2178 LEU A C     1 
ATOM   5770  O  O     . LEU A 1 2178 ? 212.976 179.268 159.589 1.00 8.62  ? 2178 LEU A O     1 
ATOM   5771  C  CB    . LEU A 1 2178 ? 210.021 178.109 160.383 1.00 7.39  ? 2178 LEU A CB    1 
ATOM   5772  C  CG    . LEU A 1 2178 ? 210.594 178.558 161.730 1.00 3.75  ? 2178 LEU A CG    1 
ATOM   5773  C  CD1   . LEU A 1 2178 ? 210.506 180.068 161.883 1.00 5.69  ? 2178 LEU A CD1   1 
ATOM   5774  C  CD2   . LEU A 1 2178 ? 209.885 177.866 162.877 1.00 2.36  ? 2178 LEU A CD2   1 
ATOM   5775  N  N     . ARG A 1 2179 ? 212.577 177.272 158.626 1.00 9.14  ? 2179 ARG A N     1 
ATOM   5776  C  CA    . ARG A 1 2179 ? 213.994 176.920 158.613 1.00 7.08  ? 2179 ARG A CA    1 
ATOM   5777  C  C     . ARG A 1 2179 ? 214.799 177.864 157.727 1.00 8.97  ? 2179 ARG A C     1 
ATOM   5778  O  O     . ARG A 1 2179 ? 215.946 178.194 158.047 1.00 11.58 ? 2179 ARG A O     1 
ATOM   5779  C  CB    . ARG A 1 2179 ? 214.181 175.470 158.172 1.00 5.82  ? 2179 ARG A CB    1 
ATOM   5780  C  CG    . ARG A 1 2179 ? 213.634 174.447 159.152 1.00 7.66  ? 2179 ARG A CG    1 
ATOM   5781  C  CD    . ARG A 1 2179 ? 213.955 173.031 158.715 1.00 7.11  ? 2179 ARG A CD    1 
ATOM   5782  N  NE    . ARG A 1 2179 ? 215.239 172.591 159.245 1.00 12.27 ? 2179 ARG A NE    1 
ATOM   5783  C  CZ    . ARG A 1 2179 ? 215.393 171.583 160.093 1.00 15.53 ? 2179 ARG A CZ    1 
ATOM   5784  N  NH1   . ARG A 1 2179 ? 214.364 170.861 160.504 1.00 10.20 ? 2179 ARG A NH1   1 
ATOM   5785  N  NH2   . ARG A 1 2179 ? 216.613 171.290 160.536 1.00 18.22 ? 2179 ARG A NH2   1 
ATOM   5786  N  N     . GLU A 1 2180 ? 214.226 178.299 156.601 1.00 7.57  ? 2180 GLU A N     1 
ATOM   5787  C  CA    . GLU A 1 2180 ? 214.928 179.257 155.751 1.00 8.49  ? 2180 GLU A CA    1 
ATOM   5788  C  C     . GLU A 1 2180 ? 215.159 180.576 156.478 1.00 8.71  ? 2180 GLU A C     1 
ATOM   5789  O  O     . GLU A 1 2180 ? 216.248 181.154 156.394 1.00 11.37 ? 2180 GLU A O     1 
ATOM   5790  C  CB    . GLU A 1 2180 ? 214.162 179.486 154.449 1.00 9.56  ? 2180 GLU A CB    1 
ATOM   5791  C  CG    . GLU A 1 2180 ? 214.091 178.275 153.539 1.00 15.89 ? 2180 GLU A CG    1 
ATOM   5792  C  CD    . GLU A 1 2180 ? 215.449 177.882 152.986 1.00 29.07 ? 2180 GLU A CD    1 
ATOM   5793  O  OE1   . GLU A 1 2180 ? 216.292 178.780 152.779 1.00 27.91 ? 2180 GLU A OE1   1 
ATOM   5794  O  OE2   . GLU A 1 2180 ? 215.672 176.675 152.751 1.00 32.87 ? 2180 GLU A OE2   1 
ATOM   5795  N  N     . GLU A 1 2181 ? 214.150 181.067 157.199 1.00 9.57  ? 2181 GLU A N     1 
ATOM   5796  C  CA    . GLU A 1 2181 ? 214.325 182.306 157.947 1.00 5.66  ? 2181 GLU A CA    1 
ATOM   5797  C  C     . GLU A 1 2181 ? 215.299 182.122 159.105 1.00 6.52  ? 2181 GLU A C     1 
ATOM   5798  O  O     . GLU A 1 2181 ? 216.090 183.024 159.402 1.00 9.74  ? 2181 GLU A O     1 
ATOM   5799  C  CB    . GLU A 1 2181 ? 212.976 182.821 158.451 1.00 6.39  ? 2181 GLU A CB    1 
ATOM   5800  C  CG    . GLU A 1 2181 ? 211.985 183.190 157.352 1.00 8.57  ? 2181 GLU A CG    1 
ATOM   5801  C  CD    . GLU A 1 2181 ? 212.340 184.473 156.610 1.00 16.99 ? 2181 GLU A CD    1 
ATOM   5802  O  OE1   . GLU A 1 2181 ? 213.456 185.001 156.797 1.00 23.65 ? 2181 GLU A OE1   1 
ATOM   5803  O  OE2   . GLU A 1 2181 ? 211.493 184.957 155.833 1.00 15.64 ? 2181 GLU A OE2   1 
ATOM   5804  N  N     . LEU A 1 2182 ? 215.259 180.963 159.766 1.00 5.57  ? 2182 LEU A N     1 
ATOM   5805  C  CA    . LEU A 1 2182 ? 216.205 180.695 160.846 1.00 4.66  ? 2182 LEU A CA    1 
ATOM   5806  C  C     . LEU A 1 2182 ? 217.638 180.676 160.329 1.00 6.82  ? 2182 LEU A C     1 
ATOM   5807  O  O     . LEU A 1 2182 ? 218.549 181.193 160.983 1.00 6.91  ? 2182 LEU A O     1 
ATOM   5808  C  CB    . LEU A 1 2182 ? 215.866 179.370 161.528 1.00 2.27  ? 2182 LEU A CB    1 
ATOM   5809  C  CG    . LEU A 1 2182 ? 214.601 179.319 162.384 1.00 3.10  ? 2182 LEU A CG    1 
ATOM   5810  C  CD1   . LEU A 1 2182 ? 214.228 177.882 162.702 1.00 2.03  ? 2182 LEU A CD1   1 
ATOM   5811  C  CD2   . LEU A 1 2182 ? 214.778 180.120 163.660 1.00 1.67  ? 2182 LEU A CD2   1 
ATOM   5812  N  N     . LYS A 1 2183 ? 217.852 180.082 159.154 1.00 7.71  ? 2183 LYS A N     1 
ATOM   5813  C  CA    . LYS A 1 2183 ? 219.192 180.018 158.583 1.00 6.60  ? 2183 LYS A CA    1 
ATOM   5814  C  C     . LYS A 1 2183 ? 219.726 181.412 158.268 1.00 7.19  ? 2183 LYS A C     1 
ATOM   5815  O  O     . LYS A 1 2183 ? 220.912 181.693 158.479 1.00 7.74  ? 2183 LYS A O     1 
ATOM   5816  C  CB    . LYS A 1 2183 ? 219.179 179.140 157.334 1.00 6.02  ? 2183 LYS A CB    1 
ATOM   5817  C  CG    . LYS A 1 2183 ? 220.529 178.948 156.682 1.00 10.83 ? 2183 LYS A CG    1 
ATOM   5818  C  CD    . LYS A 1 2183 ? 220.435 177.975 155.522 1.00 12.13 ? 2183 LYS A CD    1 
ATOM   5819  C  CE    . LYS A 1 2183 ? 221.750 177.890 154.772 1.00 17.30 ? 2183 LYS A CE    1 
ATOM   5820  N  NZ    . LYS A 1 2183 ? 222.821 177.297 155.615 1.00 22.55 ? 2183 LYS A NZ    1 
ATOM   5821  N  N     . LYS A 1 2184 ? 218.866 182.300 157.764 1.00 7.11  ? 2184 LYS A N     1 
ATOM   5822  C  CA    . LYS A 1 2184 ? 219.290 183.670 157.491 1.00 5.95  ? 2184 LYS A CA    1 
ATOM   5823  C  C     . LYS A 1 2184 ? 219.560 184.442 158.779 1.00 5.76  ? 2184 LYS A C     1 
ATOM   5824  O  O     . LYS A 1 2184 ? 220.524 185.211 158.856 1.00 8.59  ? 2184 LYS A O     1 
ATOM   5825  C  CB    . LYS A 1 2184 ? 218.239 184.387 156.646 1.00 6.95  ? 2184 LYS A CB    1 
ATOM   5826  C  CG    . LYS A 1 2184 ? 218.414 184.196 155.148 1.00 9.51  ? 2184 LYS A CG    1 
ATOM   5827  C  CD    . LYS A 1 2184 ? 217.076 184.018 154.446 1.00 14.16 ? 2184 LYS A CD    1 
ATOM   5828  C  CE    . LYS A 1 2184 ? 216.132 185.164 154.759 1.00 17.88 ? 2184 LYS A CE    1 
ATOM   5829  N  NZ    . LYS A 1 2184 ? 214.994 185.229 153.804 1.00 27.38 ? 2184 LYS A NZ    1 
ATOM   5830  N  N     . VAL A 1 2185 ? 218.715 184.258 159.796 1.00 5.20  ? 2185 VAL A N     1 
ATOM   5831  C  CA    . VAL A 1 2185 ? 218.914 184.958 161.062 1.00 2.99  ? 2185 VAL A CA    1 
ATOM   5832  C  C     . VAL A 1 2185 ? 220.204 184.495 161.730 1.00 3.45  ? 2185 VAL A C     1 
ATOM   5833  O  O     . VAL A 1 2185 ? 220.927 185.295 162.335 1.00 6.35  ? 2185 VAL A O     1 
ATOM   5834  C  CB    . VAL A 1 2185 ? 217.689 184.765 161.978 1.00 4.89  ? 2185 VAL A CB    1 
ATOM   5835  C  CG1   . VAL A 1 2185 ? 217.988 185.239 163.395 1.00 3.24  ? 2185 VAL A CG1   1 
ATOM   5836  C  CG2   . VAL A 1 2185 ? 216.493 185.512 161.420 1.00 3.14  ? 2185 VAL A CG2   1 
ATOM   5837  N  N     . CYS A 1 2186 ? 220.518 183.202 161.620 1.00 6.11  ? 2186 CYS A N     1 
ATOM   5838  C  CA    . CYS A 1 2186 ? 221.760 182.686 162.187 1.00 3.73  ? 2186 CYS A CA    1 
ATOM   5839  C  C     . CYS A 1 2186 ? 222.978 183.301 161.508 1.00 2.76  ? 2186 CYS A C     1 
ATOM   5840  O  O     . CYS A 1 2186 ? 223.972 183.618 162.171 1.00 4.17  ? 2186 CYS A O     1 
ATOM   5841  C  CB    . CYS A 1 2186 ? 221.796 181.163 162.075 1.00 3.23  ? 2186 CYS A CB    1 
ATOM   5842  S  SG    . CYS A 1 2186 ? 220.858 180.296 163.350 1.00 4.91  ? 2186 CYS A SG    1 
ATOM   5843  N  N     . GLN A 1 2187 ? 222.919 183.472 160.185 1.00 5.43  ? 2187 GLN A N     1 
ATOM   5844  C  CA    . GLN A 1 2187 ? 224.029 184.086 159.461 1.00 5.05  ? 2187 GLN A CA    1 
ATOM   5845  C  C     . GLN A 1 2187 ? 224.258 185.523 159.915 1.00 6.17  ? 2187 GLN A C     1 
ATOM   5846  O  O     . GLN A 1 2187 ? 225.405 185.962 160.059 1.00 9.63  ? 2187 GLN A O     1 
ATOM   5847  C  CB    . GLN A 1 2187 ? 223.761 184.034 157.958 1.00 3.81  ? 2187 GLN A CB    1 
ATOM   5848  C  CG    . GLN A 1 2187 ? 224.880 184.584 157.082 1.00 10.33 ? 2187 GLN A CG    1 
ATOM   5849  C  CD    . GLN A 1 2187 ? 226.178 183.814 157.219 1.00 17.08 ? 2187 GLN A CD    1 
ATOM   5850  O  OE1   . GLN A 1 2187 ? 227.124 184.275 157.856 1.00 12.83 ? 2187 GLN A OE1   1 
ATOM   5851  N  NE2   . GLN A 1 2187 ? 226.229 182.630 156.619 1.00 16.54 ? 2187 GLN A NE2   1 
ATOM   5852  N  N     . GLU A 1 2188 ? 223.179 186.273 160.142 1.00 5.25  ? 2188 GLU A N     1 
ATOM   5853  C  CA    . GLU A 1 2188 ? 223.321 187.659 160.570 1.00 6.95  ? 2188 GLU A CA    1 
ATOM   5854  C  C     . GLU A 1 2188 ? 223.764 187.753 162.025 1.00 4.34  ? 2188 GLU A C     1 
ATOM   5855  O  O     . GLU A 1 2188 ? 224.332 188.771 162.436 1.00 4.06  ? 2188 GLU A O     1 
ATOM   5856  C  CB    . GLU A 1 2188 ? 222.005 188.408 160.346 1.00 7.42  ? 2188 GLU A CB    1 
ATOM   5857  C  CG    . GLU A 1 2188 ? 222.032 189.886 160.711 1.00 14.22 ? 2188 GLU A CG    1 
ATOM   5858  C  CD    . GLU A 1 2188 ? 222.973 190.695 159.835 1.00 31.58 ? 2188 GLU A CD    1 
ATOM   5859  O  OE1   . GLU A 1 2188 ? 223.227 190.280 158.684 1.00 29.77 ? 2188 GLU A OE1   1 
ATOM   5860  O  OE2   . GLU A 1 2188 ? 223.461 191.747 160.299 1.00 26.99 ? 2188 GLU A OE2   1 
ATOM   5861  N  N     . MET A 1 2189 ? 223.535 186.701 162.809 1.00 5.71  ? 2189 MET A N     1 
ATOM   5862  C  CA    . MET A 1 2189 ? 223.915 186.666 164.214 1.00 3.93  ? 2189 MET A CA    1 
ATOM   5863  C  C     . MET A 1 2189 ? 225.165 185.833 164.467 1.00 2.41  ? 2189 MET A C     1 
ATOM   5864  O  O     . MET A 1 2189 ? 225.456 185.511 165.624 1.00 5.21  ? 2189 MET A O     1 
ATOM   5865  C  CB    . MET A 1 2189 ? 222.751 186.140 165.055 1.00 2.26  ? 2189 MET A CB    1 
ATOM   5866  C  CG    . MET A 1 2189 ? 221.644 187.158 165.265 1.00 2.49  ? 2189 MET A CG    1 
ATOM   5867  S  SD    . MET A 1 2189 ? 220.237 186.516 166.189 1.00 8.11  ? 2189 MET A SD    1 
ATOM   5868  C  CE    . MET A 1 2189 ? 220.871 186.560 167.860 1.00 4.97  ? 2189 MET A CE    1 
ATOM   5869  N  N     . TYR A 1 2190 ? 225.905 185.476 163.414 1.00 2.48  ? 2190 TYR A N     1 
ATOM   5870  C  CA    . TYR A 1 2190 ? 227.149 184.707 163.528 1.00 2.61  ? 2190 TYR A CA    1 
ATOM   5871  C  C     . TYR A 1 2190 ? 226.926 183.378 164.246 1.00 2.83  ? 2190 TYR A C     1 
ATOM   5872  O  O     . TYR A 1 2190 ? 227.777 182.912 165.006 1.00 2.38  ? 2190 TYR A O     1 
ATOM   5873  C  CB    . TYR A 1 2190 ? 228.242 185.521 164.227 1.00 2.39  ? 2190 TYR A CB    1 
ATOM   5874  C  CG    . TYR A 1 2190 ? 228.416 186.911 163.671 1.00 3.88  ? 2190 TYR A CG    1 
ATOM   5875  C  CD1   . TYR A 1 2190 ? 229.126 187.127 162.498 1.00 3.40  ? 2190 TYR A CD1   1 
ATOM   5876  C  CD2   . TYR A 1 2190 ? 227.864 188.008 164.316 1.00 2.78  ? 2190 TYR A CD2   1 
ATOM   5877  C  CE1   . TYR A 1 2190 ? 229.282 188.394 161.986 1.00 4.21  ? 2190 TYR A CE1   1 
ATOM   5878  C  CE2   . TYR A 1 2190 ? 228.015 189.282 163.810 1.00 4.37  ? 2190 TYR A CE2   1 
ATOM   5879  C  CZ    . TYR A 1 2190 ? 228.724 189.469 162.646 1.00 7.09  ? 2190 TYR A CZ    1 
ATOM   5880  O  OH    . TYR A 1 2190 ? 228.879 190.738 162.138 1.00 12.24 ? 2190 TYR A OH    1 
ATOM   5881  N  N     . LEU A 1 2191 ? 225.782 182.756 163.996 1.00 3.74  ? 2191 LEU A N     1 
ATOM   5882  C  CA    . LEU A 1 2191 ? 225.433 181.494 164.623 1.00 0.96  ? 2191 LEU A CA    1 
ATOM   5883  C  C     . LEU A 1 2191 ? 225.537 180.357 163.616 1.00 2.27  ? 2191 LEU A C     1 
ATOM   5884  O  O     . LEU A 1 2191 ? 225.500 180.563 162.400 1.00 7.52  ? 2191 LEU A O     1 
ATOM   5885  C  CB    . LEU A 1 2191 ? 224.024 181.543 165.217 1.00 1.14  ? 2191 LEU A CB    1 
ATOM   5886  C  CG    . LEU A 1 2191 ? 223.846 182.442 166.440 1.00 0.95  ? 2191 LEU A CG    1 
ATOM   5887  C  CD1   . LEU A 1 2191 ? 222.526 182.148 167.119 1.00 2.24  ? 2191 LEU A CD1   1 
ATOM   5888  C  CD2   . LEU A 1 2191 ? 224.998 182.281 167.415 1.00 0.50  ? 2191 LEU A CD2   1 
ATOM   5889  N  N     . THR A 1 2192 ? 225.676 179.148 164.145 1.00 2.35  ? 2192 THR A N     1 
ATOM   5890  C  CA    . THR A 1 2192 ? 225.792 177.953 163.324 1.00 3.05  ? 2192 THR A CA    1 
ATOM   5891  C  C     . THR A 1 2192 ? 224.421 177.315 163.155 1.00 3.02  ? 2192 THR A C     1 
ATOM   5892  O  O     . THR A 1 2192 ? 223.738 177.021 164.140 1.00 1.86  ? 2192 THR A O     1 
ATOM   5893  C  CB    . THR A 1 2192 ? 226.768 176.956 163.951 1.00 3.63  ? 2192 THR A CB    1 
ATOM   5894  O  OG1   . THR A 1 2192 ? 228.078 177.532 163.993 1.00 3.95  ? 2192 THR A OG1   1 
ATOM   5895  C  CG2   . THR A 1 2192 ? 226.808 175.672 163.143 1.00 2.55  ? 2192 THR A CG2   1 
ATOM   5896  N  N     . TYR A 1 2193 ? 224.024 177.110 161.904 1.00 6.46  ? 2193 TYR A N     1 
ATOM   5897  C  CA    . TYR A 1 2193 ? 222.764 176.464 161.568 1.00 3.34  ? 2193 TYR A CA    1 
ATOM   5898  C  C     . TYR A 1 2193 ? 223.056 175.098 160.964 1.00 4.13  ? 2193 TYR A C     1 
ATOM   5899  O  O     . TYR A 1 2193 ? 223.935 174.969 160.106 1.00 9.17  ? 2193 TYR A O     1 
ATOM   5900  C  CB    . TYR A 1 2193 ? 221.950 177.321 160.596 1.00 2.30  ? 2193 TYR A CB    1 
ATOM   5901  C  CG    . TYR A 1 2193 ? 220.685 176.657 160.098 1.00 4.63  ? 2193 TYR A CG    1 
ATOM   5902  C  CD1   . TYR A 1 2193 ? 220.698 175.850 158.968 1.00 6.43  ? 2193 TYR A CD1   1 
ATOM   5903  C  CD2   . TYR A 1 2193 ? 219.480 176.835 160.760 1.00 4.19  ? 2193 TYR A CD2   1 
ATOM   5904  C  CE1   . TYR A 1 2193 ? 219.554 175.241 158.515 1.00 5.08  ? 2193 TYR A CE1   1 
ATOM   5905  C  CE2   . TYR A 1 2193 ? 218.325 176.226 160.312 1.00 5.33  ? 2193 TYR A CE2   1 
ATOM   5906  C  CZ    . TYR A 1 2193 ? 218.370 175.431 159.188 1.00 8.80  ? 2193 TYR A CZ    1 
ATOM   5907  O  OH    . TYR A 1 2193 ? 217.228 174.821 158.732 1.00 16.73 ? 2193 TYR A OH    1 
ATOM   5908  N  N     . GLY A 1 2194 ? 222.313 174.083 161.412 1.00 4.57  ? 2194 GLY A N     1 
ATOM   5909  C  CA    . GLY A 1 2194 ? 222.452 172.747 160.881 1.00 4.76  ? 2194 GLY A CA    1 
ATOM   5910  C  C     . GLY A 1 2194 ? 221.091 172.129 160.615 1.00 8.77  ? 2194 GLY A C     1 
ATOM   5911  O  O     . GLY A 1 2194 ? 220.056 172.635 161.053 1.00 10.51 ? 2194 GLY A O     1 
ATOM   5912  N  N     . ASP A 1 2195 ? 221.115 171.017 159.884 1.00 15.66 ? 2195 ASP A N     1 
ATOM   5913  C  CA    . ASP A 1 2195 ? 219.908 170.278 159.528 1.00 11.01 ? 2195 ASP A CA    1 
ATOM   5914  C  C     . ASP A 1 2195 ? 220.161 168.801 159.786 1.00 12.34 ? 2195 ASP A C     1 
ATOM   5915  O  O     . ASP A 1 2195 ? 220.953 168.171 159.079 1.00 16.82 ? 2195 ASP A O     1 
ATOM   5916  C  CB    . ASP A 1 2195 ? 219.523 170.525 158.069 1.00 8.25  ? 2195 ASP A CB    1 
ATOM   5917  C  CG    . ASP A 1 2195 ? 218.599 171.713 157.903 1.00 18.56 ? 2195 ASP A CG    1 
ATOM   5918  O  OD1   . ASP A 1 2195 ? 218.154 172.271 158.928 1.00 18.53 ? 2195 ASP A OD1   1 
ATOM   5919  O  OD2   . ASP A 1 2195 ? 218.319 172.094 156.748 1.00 24.58 ? 2195 ASP A OD2   1 
ATOM   5920  N  N     . GLY A 1 2196 ? 219.493 168.250 160.795 1.00 11.23 ? 2196 GLY A N     1 
ATOM   5921  C  CA    . GLY A 1 2196 ? 219.645 166.847 161.124 1.00 12.41 ? 2196 GLY A CA    1 
ATOM   5922  C  C     . GLY A 1 2196 ? 220.852 166.555 161.990 1.00 17.87 ? 2196 GLY A C     1 
ATOM   5923  O  O     . GLY A 1 2196 ? 220.936 167.025 163.130 1.00 19.15 ? 2196 GLY A O     1 
ATOM   5924  N  N     . GLU A 1 2197 ? 221.791 165.775 161.464 1.00 14.76 ? 2197 GLU A N     1 
ATOM   5925  C  CA    . GLU A 1 2197 ? 222.991 165.396 162.197 1.00 14.53 ? 2197 GLU A CA    1 
ATOM   5926  C  C     . GLU A 1 2197 ? 224.166 166.327 161.930 1.00 15.10 ? 2197 GLU A C     1 
ATOM   5927  O  O     . GLU A 1 2197 ? 225.264 166.072 162.433 1.00 13.53 ? 2197 GLU A O     1 
ATOM   5928  C  CB    . GLU A 1 2197 ? 223.388 163.956 161.854 1.00 22.40 ? 2197 GLU A CB    1 
ATOM   5929  C  CG    . GLU A 1 2197 ? 222.265 162.950 162.019 1.00 19.86 ? 2197 GLU A CG    1 
ATOM   5930  C  CD    . GLU A 1 2197 ? 221.444 163.194 163.271 1.00 24.32 ? 2197 GLU A CD    1 
ATOM   5931  O  OE1   . GLU A 1 2197 ? 221.932 162.871 164.374 1.00 29.01 ? 2197 GLU A OE1   1 
ATOM   5932  O  OE2   . GLU A 1 2197 ? 220.312 163.710 163.152 1.00 31.31 ? 2197 GLU A OE2   1 
ATOM   5933  N  N     . GLU A 1 2198 ? 223.965 167.391 161.159 1.00 11.56 ? 2198 GLU A N     1 
ATOM   5934  C  CA    . GLU A 1 2198 ? 225.027 168.348 160.910 1.00 9.35  ? 2198 GLU A CA    1 
ATOM   5935  C  C     . GLU A 1 2198 ? 225.351 169.130 162.183 1.00 10.24 ? 2198 GLU A C     1 
ATOM   5936  O  O     . GLU A 1 2198 ? 224.669 169.021 163.207 1.00 9.47  ? 2198 GLU A O     1 
ATOM   5937  C  CB    . GLU A 1 2198 ? 224.633 169.309 159.789 1.00 8.30  ? 2198 GLU A CB    1 
ATOM   5938  C  CG    . GLU A 1 2198 ? 224.113 168.630 158.538 1.00 8.62  ? 2198 GLU A CG    1 
ATOM   5939  C  CD    . GLU A 1 2198 ? 223.434 169.601 157.591 1.00 20.11 ? 2198 GLU A CD    1 
ATOM   5940  O  OE1   . GLU A 1 2198 ? 223.546 170.825 157.812 1.00 17.01 ? 2198 GLU A OE1   1 
ATOM   5941  O  OE2   . GLU A 1 2198 ? 222.789 169.140 156.628 1.00 24.94 ? 2198 GLU A OE2   1 
ATOM   5942  N  N     . VAL A 1 2199 ? 226.417 169.923 162.110 1.00 10.21 ? 2199 VAL A N     1 
ATOM   5943  C  CA    . VAL A 1 2199 ? 226.778 170.787 163.226 1.00 5.10  ? 2199 VAL A CA    1 
ATOM   5944  C  C     . VAL A 1 2199 ? 225.674 171.814 163.419 1.00 4.05  ? 2199 VAL A C     1 
ATOM   5945  O  O     . VAL A 1 2199 ? 225.299 172.527 162.480 1.00 9.15  ? 2199 VAL A O     1 
ATOM   5946  C  CB    . VAL A 1 2199 ? 228.136 171.454 162.980 1.00 6.05  ? 2199 VAL A CB    1 
ATOM   5947  C  CG1   . VAL A 1 2199 ? 228.512 172.347 164.151 1.00 5.02  ? 2199 VAL A CG1   1 
ATOM   5948  C  CG2   . VAL A 1 2199 ? 229.206 170.405 162.740 1.00 4.85  ? 2199 VAL A CG2   1 
ATOM   5949  N  N     . GLY A 1 2200 ? 225.143 171.891 164.635 1.00 2.84  ? 2200 GLY A N     1 
ATOM   5950  C  CA    . GLY A 1 2200 ? 224.037 172.776 164.930 1.00 2.94  ? 2200 GLY A CA    1 
ATOM   5951  C  C     . GLY A 1 2200 ? 222.664 172.191 164.695 1.00 2.52  ? 2200 GLY A C     1 
ATOM   5952  O  O     . GLY A 1 2200 ? 221.668 172.861 164.995 1.00 1.74  ? 2200 GLY A O     1 
ATOM   5953  N  N     . GLY A 1 2201 ? 222.575 170.964 164.177 1.00 5.07  ? 2201 GLY A N     1 
ATOM   5954  C  CA    . GLY A 1 2201 ? 221.275 170.380 163.896 1.00 4.36  ? 2201 GLY A CA    1 
ATOM   5955  C  C     . GLY A 1 2201 ? 220.445 170.149 165.145 1.00 1.73  ? 2201 GLY A C     1 
ATOM   5956  O  O     . GLY A 1 2201 ? 219.232 170.372 165.145 1.00 1.12  ? 2201 GLY A O     1 
ATOM   5957  N  N     . MET A 1 2202 ? 221.084 169.693 166.224 1.00 2.99  ? 2202 MET A N     1 
ATOM   5958  C  CA    . MET A 1 2202 ? 220.365 169.489 167.477 1.00 1.24  ? 2202 MET A CA    1 
ATOM   5959  C  C     . MET A 1 2202 ? 219.802 170.801 168.006 1.00 1.11  ? 2202 MET A C     1 
ATOM   5960  O  O     . MET A 1 2202 ? 218.671 170.849 168.501 1.00 1.36  ? 2202 MET A O     1 
ATOM   5961  C  CB    . MET A 1 2202 ? 221.285 168.850 168.514 1.00 2.64  ? 2202 MET A CB    1 
ATOM   5962  C  CG    . MET A 1 2202 ? 221.545 167.371 168.300 1.00 4.47  ? 2202 MET A CG    1 
ATOM   5963  S  SD    . MET A 1 2202 ? 222.329 166.606 169.732 1.00 32.34 ? 2202 MET A SD    1 
ATOM   5964  C  CE    . MET A 1 2202 ? 224.058 166.831 169.335 1.00 13.18 ? 2202 MET A CE    1 
ATOM   5965  N  N     . TRP A 1 2203 ? 220.583 171.878 167.907 1.00 1.15  ? 2203 TRP A N     1 
ATOM   5966  C  CA    . TRP A 1 2203 ? 220.124 173.183 168.366 1.00 0.52  ? 2203 TRP A CA    1 
ATOM   5967  C  C     . TRP A 1 2203 ? 218.961 173.695 167.525 1.00 0.46  ? 2203 TRP A C     1 
ATOM   5968  O  O     . TRP A 1 2203 ? 218.021 174.291 168.058 1.00 0.56  ? 2203 TRP A O     1 
ATOM   5969  C  CB    . TRP A 1 2203 ? 221.293 174.167 168.352 1.00 0.58  ? 2203 TRP A CB    1 
ATOM   5970  C  CG    . TRP A 1 2203 ? 220.939 175.553 168.767 1.00 0.25  ? 2203 TRP A CG    1 
ATOM   5971  C  CD1   . TRP A 1 2203 ? 220.846 176.028 170.037 1.00 0.13  ? 2203 TRP A CD1   1 
ATOM   5972  C  CD2   . TRP A 1 2203 ? 220.648 176.655 167.902 1.00 0.11  ? 2203 TRP A CD2   1 
ATOM   5973  N  NE1   . TRP A 1 2203 ? 220.507 177.356 170.022 1.00 0.06  ? 2203 TRP A NE1   1 
ATOM   5974  C  CE2   . TRP A 1 2203 ? 220.379 177.766 168.721 1.00 0.08  ? 2203 TRP A CE2   1 
ATOM   5975  C  CE3   . TRP A 1 2203 ? 220.585 176.808 166.515 1.00 0.13  ? 2203 TRP A CE3   1 
ATOM   5976  C  CZ2   . TRP A 1 2203 ? 220.052 179.014 168.200 1.00 0.10  ? 2203 TRP A CZ2   1 
ATOM   5977  C  CZ3   . TRP A 1 2203 ? 220.262 178.045 166.000 1.00 0.35  ? 2203 TRP A CZ3   1 
ATOM   5978  C  CH2   . TRP A 1 2203 ? 220.000 179.133 166.840 1.00 0.97  ? 2203 TRP A CH2   1 
ATOM   5979  N  N     . VAL A 1 2204 ? 219.006 173.468 166.210 1.00 0.40  ? 2204 VAL A N     1 
ATOM   5980  C  CA    . VAL A 1 2204 ? 217.925 173.920 165.337 1.00 0.50  ? 2204 VAL A CA    1 
ATOM   5981  C  C     . VAL A 1 2204 ? 216.637 173.162 165.641 1.00 0.88  ? 2204 VAL A C     1 
ATOM   5982  O  O     . VAL A 1 2204 ? 215.541 173.731 165.588 1.00 0.81  ? 2204 VAL A O     1 
ATOM   5983  C  CB    . VAL A 1 2204 ? 218.341 173.781 163.861 1.00 1.08  ? 2204 VAL A CB    1 
ATOM   5984  C  CG1   . VAL A 1 2204 ? 217.156 174.029 162.938 1.00 1.94  ? 2204 VAL A CG1   1 
ATOM   5985  C  CG2   . VAL A 1 2204 ? 219.469 174.744 163.542 1.00 0.88  ? 2204 VAL A CG2   1 
ATOM   5986  N  N     . GLU A 1 2205 ? 216.747 171.874 165.973 1.00 1.18  ? 2205 GLU A N     1 
ATOM   5987  C  CA    . GLU A 1 2205 ? 215.570 171.118 166.387 1.00 0.82  ? 2205 GLU A CA    1 
ATOM   5988  C  C     . GLU A 1 2205 ? 214.950 171.708 167.648 1.00 1.17  ? 2205 GLU A C     1 
ATOM   5989  O  O     . GLU A 1 2205 ? 213.723 171.771 167.774 1.00 1.52  ? 2205 GLU A O     1 
ATOM   5990  C  CB    . GLU A 1 2205 ? 215.934 169.649 166.607 1.00 1.39  ? 2205 GLU A CB    1 
ATOM   5991  C  CG    . GLU A 1 2205 ? 216.348 168.905 165.348 1.00 7.33  ? 2205 GLU A CG    1 
ATOM   5992  C  CD    . GLU A 1 2205 ? 215.211 168.748 164.357 1.00 17.92 ? 2205 GLU A CD    1 
ATOM   5993  O  OE1   . GLU A 1 2205 ? 214.046 168.641 164.794 1.00 15.45 ? 2205 GLU A OE1   1 
ATOM   5994  O  OE2   . GLU A 1 2205 ? 215.483 168.729 163.139 1.00 22.07 ? 2205 GLU A OE2   1 
ATOM   5995  N  N     . LYS A 1 2206 ? 215.785 172.148 168.594 1.00 0.84  ? 2206 LYS A N     1 
ATOM   5996  C  CA    . LYS A 1 2206 ? 215.262 172.752 169.814 1.00 0.38  ? 2206 LYS A CA    1 
ATOM   5997  C  C     . LYS A 1 2206 ? 214.576 174.082 169.527 1.00 0.35  ? 2206 LYS A C     1 
ATOM   5998  O  O     . LYS A 1 2206 ? 213.588 174.428 170.184 1.00 1.51  ? 2206 LYS A O     1 
ATOM   5999  C  CB    . LYS A 1 2206 ? 216.383 172.926 170.837 1.00 0.41  ? 2206 LYS A CB    1 
ATOM   6000  C  CG    . LYS A 1 2206 ? 216.795 171.627 171.502 1.00 0.53  ? 2206 LYS A CG    1 
ATOM   6001  C  CD    . LYS A 1 2206 ? 215.616 170.994 172.212 1.00 0.82  ? 2206 LYS A CD    1 
ATOM   6002  C  CE    . LYS A 1 2206 ? 215.912 169.573 172.638 1.00 0.27  ? 2206 LYS A CE    1 
ATOM   6003  N  NZ    . LYS A 1 2206 ? 214.818 169.021 173.471 1.00 0.13  ? 2206 LYS A NZ    1 
ATOM   6004  N  N     . VAL A 1 2207 ? 215.087 174.844 168.560 1.00 0.50  ? 2207 VAL A N     1 
ATOM   6005  C  CA    . VAL A 1 2207 ? 214.411 176.072 168.153 1.00 0.41  ? 2207 VAL A CA    1 
ATOM   6006  C  C     . VAL A 1 2207 ? 213.043 175.754 167.564 1.00 0.48  ? 2207 VAL A C     1 
ATOM   6007  O  O     . VAL A 1 2207 ? 212.049 176.422 167.869 1.00 0.45  ? 2207 VAL A O     1 
ATOM   6008  C  CB    . VAL A 1 2207 ? 215.285 176.866 167.165 1.00 0.37  ? 2207 VAL A CB    1 
ATOM   6009  C  CG1   . VAL A 1 2207 ? 214.574 178.130 166.721 1.00 0.27  ? 2207 VAL A CG1   1 
ATOM   6010  C  CG2   . VAL A 1 2207 ? 216.630 177.200 167.788 1.00 0.16  ? 2207 VAL A CG2   1 
ATOM   6011  N  N     . LEU A 1 2208 ? 212.971 174.729 166.713 1.00 0.62  ? 2208 LEU A N     1 
ATOM   6012  C  CA    . LEU A 1 2208 ? 211.694 174.328 166.132 1.00 0.53  ? 2208 LEU A CA    1 
ATOM   6013  C  C     . LEU A 1 2208 ? 210.752 173.766 167.190 1.00 0.31  ? 2208 LEU A C     1 
ATOM   6014  O  O     . LEU A 1 2208 ? 209.546 174.027 167.152 1.00 0.91  ? 2208 LEU A O     1 
ATOM   6015  C  CB    . LEU A 1 2208 ? 211.928 173.309 165.019 1.00 0.94  ? 2208 LEU A CB    1 
ATOM   6016  C  CG    . LEU A 1 2208 ? 212.753 173.821 163.841 1.00 1.25  ? 2208 LEU A CG    1 
ATOM   6017  C  CD1   . LEU A 1 2208 ? 213.076 172.692 162.887 1.00 1.85  ? 2208 LEU A CD1   1 
ATOM   6018  C  CD2   . LEU A 1 2208 ? 212.020 174.936 163.122 1.00 1.74  ? 2208 LEU A CD2   1 
ATOM   6019  N  N     . GLN A 1 2209 ? 211.282 172.986 168.134 1.00 0.34  ? 2209 GLN A N     1 
ATOM   6020  C  CA    . GLN A 1 2209 ? 210.456 172.486 169.228 1.00 0.37  ? 2209 GLN A CA    1 
ATOM   6021  C  C     . GLN A 1 2209 ? 209.926 173.630 170.080 1.00 0.41  ? 2209 GLN A C     1 
ATOM   6022  O  O     . GLN A 1 2209 ? 208.769 173.607 170.517 1.00 0.46  ? 2209 GLN A O     1 
ATOM   6023  C  CB    . GLN A 1 2209 ? 211.254 171.509 170.090 1.00 0.34  ? 2209 GLN A CB    1 
ATOM   6024  C  CG    . GLN A 1 2209 ? 211.547 170.176 169.430 1.00 0.32  ? 2209 GLN A CG    1 
ATOM   6025  C  CD    . GLN A 1 2209 ? 212.372 169.265 170.315 1.00 0.53  ? 2209 GLN A CD    1 
ATOM   6026  O  OE1   . GLN A 1 2209 ? 212.716 169.621 171.438 1.00 0.80  ? 2209 GLN A OE1   1 
ATOM   6027  N  NE2   . GLN A 1 2209 ? 212.695 168.082 169.809 1.00 1.31  ? 2209 GLN A NE2   1 
ATOM   6028  N  N     . LEU A 1 2210 ? 210.761 174.642 170.325 1.00 0.55  ? 2210 LEU A N     1 
ATOM   6029  C  CA    . LEU A 1 2210 ? 210.320 175.807 171.083 1.00 0.25  ? 2210 LEU A CA    1 
ATOM   6030  C  C     . LEU A 1 2210 ? 209.188 176.534 170.367 1.00 0.42  ? 2210 LEU A C     1 
ATOM   6031  O  O     . LEU A 1 2210 ? 208.255 177.029 171.008 1.00 0.47  ? 2210 LEU A O     1 
ATOM   6032  C  CB    . LEU A 1 2210 ? 211.505 176.741 171.323 1.00 0.24  ? 2210 LEU A CB    1 
ATOM   6033  C  CG    . LEU A 1 2210 ? 211.226 178.104 171.950 1.00 0.25  ? 2210 LEU A CG    1 
ATOM   6034  C  CD1   . LEU A 1 2210 ? 210.848 177.949 173.412 1.00 0.17  ? 2210 LEU A CD1   1 
ATOM   6035  C  CD2   . LEU A 1 2210 ? 212.436 179.009 171.793 1.00 0.04  ? 2210 LEU A CD2   1 
ATOM   6036  N  N     . TYR A 1 2211 ? 209.254 176.610 169.034 1.00 0.51  ? 2211 TYR A N     1 
ATOM   6037  C  CA    . TYR A 1 2211 ? 208.180 177.236 168.272 1.00 0.43  ? 2211 TYR A CA    1 
ATOM   6038  C  C     . TYR A 1 2211 ? 206.874 176.469 168.427 1.00 1.15  ? 2211 TYR A C     1 
ATOM   6039  O  O     . TYR A 1 2211 ? 205.803 177.072 168.545 1.00 2.06  ? 2211 TYR A O     1 
ATOM   6040  C  CB    . TYR A 1 2211 ? 208.564 177.337 166.797 1.00 0.48  ? 2211 TYR A CB    1 
ATOM   6041  C  CG    . TYR A 1 2211 ? 207.475 177.927 165.931 1.00 2.19  ? 2211 TYR A CG    1 
ATOM   6042  C  CD1   . TYR A 1 2211 ? 207.023 177.264 164.798 1.00 3.54  ? 2211 TYR A CD1   1 
ATOM   6043  C  CD2   . TYR A 1 2211 ? 206.898 179.149 166.248 1.00 2.44  ? 2211 TYR A CD2   1 
ATOM   6044  C  CE1   . TYR A 1 2211 ? 206.030 177.804 164.008 1.00 5.61  ? 2211 TYR A CE1   1 
ATOM   6045  C  CE2   . TYR A 1 2211 ? 205.905 179.693 165.466 1.00 4.05  ? 2211 TYR A CE2   1 
ATOM   6046  C  CZ    . TYR A 1 2211 ? 205.475 179.019 164.347 1.00 7.52  ? 2211 TYR A CZ    1 
ATOM   6047  O  OH    . TYR A 1 2211 ? 204.485 179.563 163.566 1.00 12.72 ? 2211 TYR A OH    1 
ATOM   6048  N  N     . GLN A 1 2212 ? 206.945 175.137 168.418 1.00 2.08  ? 2212 GLN A N     1 
ATOM   6049  C  CA    . GLN A 1 2212 ? 205.739 174.333 168.581 1.00 1.82  ? 2212 GLN A CA    1 
ATOM   6050  C  C     . GLN A 1 2212 ? 205.098 174.576 169.941 1.00 2.18  ? 2212 GLN A C     1 
ATOM   6051  O  O     . GLN A 1 2212 ? 203.870 174.652 170.049 1.00 6.82  ? 2212 GLN A O     1 
ATOM   6052  C  CB    . GLN A 1 2212 ? 206.069 172.853 168.399 1.00 4.65  ? 2212 GLN A CB    1 
ATOM   6053  C  CG    . GLN A 1 2212 ? 206.566 172.487 167.010 1.00 7.60  ? 2212 GLN A CG    1 
ATOM   6054  C  CD    . GLN A 1 2212 ? 205.513 172.667 165.938 1.00 19.68 ? 2212 GLN A CD    1 
ATOM   6055  O  OE1   . GLN A 1 2212 ? 204.336 172.378 166.152 1.00 13.60 ? 2212 GLN A OE1   1 
ATOM   6056  N  NE2   . GLN A 1 2212 ? 205.931 173.145 164.771 1.00 27.07 ? 2212 GLN A NE2   1 
ATOM   6057  N  N     . ILE A 1 2213 ? 205.915 174.705 170.988 1.00 1.13  ? 2213 ILE A N     1 
ATOM   6058  C  CA    . ILE A 1 2213 ? 205.385 174.953 172.324 1.00 1.44  ? 2213 ILE A CA    1 
ATOM   6059  C  C     . ILE A 1 2213 ? 204.739 176.332 172.400 1.00 1.99  ? 2213 ILE A C     1 
ATOM   6060  O  O     . ILE A 1 2213 ? 203.736 176.520 173.097 1.00 2.03  ? 2213 ILE A O     1 
ATOM   6061  C  CB    . ILE A 1 2213 ? 206.499 174.778 173.375 1.00 2.33  ? 2213 ILE A CB    1 
ATOM   6062  C  CG1   . ILE A 1 2213 ? 207.095 173.373 173.281 1.00 1.38  ? 2213 ILE A CG1   1 
ATOM   6063  C  CG2   . ILE A 1 2213 ? 205.965 175.031 174.775 1.00 1.55  ? 2213 ILE A CG2   1 
ATOM   6064  C  CD1   . ILE A 1 2213 ? 206.163 172.279 173.751 1.00 1.20  ? 2213 ILE A CD1   1 
ATOM   6065  N  N     . THR A 1 2214 ? 205.293 177.316 171.685 1.00 1.42  ? 2214 THR A N     1 
ATOM   6066  C  CA    . THR A 1 2214 ? 204.704 178.653 171.681 1.00 2.18  ? 2214 THR A CA    1 
ATOM   6067  C  C     . THR A 1 2214 ? 203.305 178.664 171.086 1.00 2.24  ? 2214 THR A C     1 
ATOM   6068  O  O     . THR A 1 2214 ? 202.516 179.559 171.405 1.00 4.84  ? 2214 THR A O     1 
ATOM   6069  C  CB    . THR A 1 2214 ? 205.582 179.638 170.903 1.00 0.97  ? 2214 THR A CB    1 
ATOM   6070  O  OG1   . THR A 1 2214 ? 205.884 179.101 169.609 1.00 6.74  ? 2214 THR A OG1   1 
ATOM   6071  C  CG2   . THR A 1 2214 ? 206.867 179.907 171.639 1.00 0.41  ? 2214 THR A CG2   1 
ATOM   6072  N  N     . GLN A 1 2215 ? 202.984 177.703 170.225 1.00 2.26  ? 2215 GLN A N     1 
ATOM   6073  C  CA    . GLN A 1 2215 ? 201.676 177.637 169.588 1.00 2.87  ? 2215 GLN A CA    1 
ATOM   6074  C  C     . GLN A 1 2215 ? 200.656 176.842 170.391 1.00 4.36  ? 2215 GLN A C     1 
ATOM   6075  O  O     . GLN A 1 2215 ? 199.479 176.826 170.018 1.00 10.99 ? 2215 GLN A O     1 
ATOM   6076  C  CB    . GLN A 1 2215 ? 201.808 177.028 168.189 1.00 2.53  ? 2215 GLN A CB    1 
ATOM   6077  C  CG    . GLN A 1 2215 ? 202.699 177.827 167.251 1.00 3.66  ? 2215 GLN A CG    1 
ATOM   6078  C  CD    . GLN A 1 2215 ? 203.098 177.043 166.017 1.00 8.07  ? 2215 GLN A CD    1 
ATOM   6079  O  OE1   . GLN A 1 2215 ? 203.798 176.036 166.106 1.00 16.96 ? 2215 GLN A OE1   1 
ATOM   6080  N  NE2   . GLN A 1 2215 ? 202.655 177.506 164.855 1.00 8.39  ? 2215 GLN A NE2   1 
ATOM   6081  N  N     . ILE A 1 2216 ? 201.072 176.187 171.474 1.00 3.89  ? 2216 ILE A N     1 
ATOM   6082  C  CA    . ILE A 1 2216 ? 200.172 175.352 172.261 1.00 3.94  ? 2216 ILE A CA    1 
ATOM   6083  C  C     . ILE A 1 2216 ? 200.043 175.914 173.671 1.00 3.33  ? 2216 ILE A C     1 
ATOM   6084  O  O     . ILE A 1 2216 ? 198.988 175.798 174.303 1.00 7.84  ? 2216 ILE A O     1 
ATOM   6085  C  CB    . ILE A 1 2216 ? 200.671 173.894 172.289 1.00 4.59  ? 2216 ILE A CB    1 
ATOM   6086  C  CG1   . ILE A 1 2216 ? 200.761 173.338 170.869 1.00 6.15  ? 2216 ILE A CG1   1 
ATOM   6087  C  CG2   . ILE A 1 2216 ? 199.763 173.024 173.140 1.00 10.78 ? 2216 ILE A CG2   1 
ATOM   6088  C  CD1   . ILE A 1 2216 ? 199.443 173.313 170.141 1.00 7.56  ? 2216 ILE A CD1   1 
ATOM   6089  N  N     . ASN A 1 2217 ? 201.102 176.548 174.162 1.00 1.90  ? 2217 ASN A N     1 
ATOM   6090  C  CA    . ASN A 1 2217 ? 201.150 177.054 175.526 1.00 1.83  ? 2217 ASN A CA    1 
ATOM   6091  C  C     . ASN A 1 2217 ? 201.365 178.558 175.519 1.00 1.28  ? 2217 ASN A C     1 
ATOM   6092  O  O     . ASN A 1 2217 ? 202.100 179.087 174.680 1.00 7.05  ? 2217 ASN A O     1 
ATOM   6093  C  CB    . ASN A 1 2217 ? 202.270 176.384 176.337 1.00 1.18  ? 2217 ASN A CB    1 
ATOM   6094  C  CG    . ASN A 1 2217 ? 202.292 174.878 176.174 1.00 1.52  ? 2217 ASN A CG    1 
ATOM   6095  O  OD1   . ASN A 1 2217 ? 202.508 174.362 175.078 1.00 6.31  ? 2217 ASN A OD1   1 
ATOM   6096  N  ND2   . ASN A 1 2217 ? 202.067 174.164 177.267 1.00 1.66  ? 2217 ASN A ND2   1 
ATOM   6097  N  N     . HIS A 1 2218 ? 200.707 179.246 176.448 1.00 0.57  ? 2218 HIS A N     1 
ATOM   6098  C  CA    . HIS A 1 2218 ? 201.007 180.647 176.700 1.00 0.43  ? 2218 HIS A CA    1 
ATOM   6099  C  C     . HIS A 1 2218 ? 202.095 180.827 177.751 1.00 0.28  ? 2218 HIS A C     1 
ATOM   6100  O  O     . HIS A 1 2218 ? 202.616 181.937 177.902 1.00 0.16  ? 2218 HIS A O     1 
ATOM   6101  C  CB    . HIS A 1 2218 ? 199.741 181.397 177.125 1.00 0.27  ? 2218 HIS A CB    1 
ATOM   6102  C  CG    . HIS A 1 2218 ? 199.114 180.870 178.375 1.00 0.37  ? 2218 HIS A CG    1 
ATOM   6103  N  ND1   . HIS A 1 2218 ? 198.136 179.900 178.364 1.00 0.60  ? 2218 HIS A ND1   1 
ATOM   6104  C  CD2   . HIS A 1 2218 ? 199.322 181.178 179.676 1.00 0.49  ? 2218 HIS A CD2   1 
ATOM   6105  C  CE1   . HIS A 1 2218 ? 197.771 179.631 179.604 1.00 0.59  ? 2218 HIS A CE1   1 
ATOM   6106  N  NE2   . HIS A 1 2218 ? 198.476 180.395 180.420 1.00 0.53  ? 2218 HIS A NE2   1 
ATOM   6107  N  N     . GLY A 1 2219 ? 202.445 179.762 178.467 1.00 0.27  ? 2219 GLY A N     1 
ATOM   6108  C  CA    . GLY A 1 2219 ? 203.552 179.769 179.402 1.00 0.15  ? 2219 GLY A CA    1 
ATOM   6109  C  C     . GLY A 1 2219 ? 204.464 178.579 179.182 1.00 0.26  ? 2219 GLY A C     1 
ATOM   6110  O  O     . GLY A 1 2219 ? 203.995 177.440 179.117 1.00 0.54  ? 2219 GLY A O     1 
ATOM   6111  N  N     . LEU A 1 2220 ? 205.766 178.823 179.058 1.00 0.17  ? 2220 LEU A N     1 
ATOM   6112  C  CA    . LEU A 1 2220 ? 206.710 177.764 178.740 1.00 0.12  ? 2220 LEU A CA    1 
ATOM   6113  C  C     . LEU A 1 2220 ? 208.050 178.034 179.405 1.00 0.10  ? 2220 LEU A C     1 
ATOM   6114  O  O     . LEU A 1 2220 ? 208.419 179.182 179.655 1.00 0.08  ? 2220 LEU A O     1 
ATOM   6115  C  CB    . LEU A 1 2220 ? 206.877 177.616 177.221 1.00 0.29  ? 2220 LEU A CB    1 
ATOM   6116  C  CG    . LEU A 1 2220 ? 207.411 178.785 176.385 1.00 0.21  ? 2220 LEU A CG    1 
ATOM   6117  C  CD1   . LEU A 1 2220 ? 208.930 178.912 176.412 1.00 0.14  ? 2220 LEU A CD1   1 
ATOM   6118  C  CD2   . LEU A 1 2220 ? 206.911 178.655 174.963 1.00 1.35  ? 2220 LEU A CD2   1 
ATOM   6119  N  N     . MET A 1 2221 ? 208.784 176.957 179.679 1.00 0.26  ? 2221 MET A N     1 
ATOM   6120  C  CA    . MET A 1 2221 ? 210.114 177.045 180.264 1.00 0.05  ? 2221 MET A CA    1 
ATOM   6121  C  C     . MET A 1 2221 ? 211.133 176.408 179.337 1.00 0.04  ? 2221 MET A C     1 
ATOM   6122  O  O     . MET A 1 2221 ? 210.893 175.327 178.789 1.00 0.05  ? 2221 MET A O     1 
ATOM   6123  C  CB    . MET A 1 2221 ? 210.178 176.390 181.645 1.00 0.08  ? 2221 MET A CB    1 
ATOM   6124  C  CG    . MET A 1 2221 ? 209.381 177.122 182.685 1.00 0.18  ? 2221 MET A CG    1 
ATOM   6125  S  SD    . MET A 1 2221 ? 209.429 176.390 184.321 1.00 26.23 ? 2221 MET A SD    1 
ATOM   6126  C  CE    . MET A 1 2221 ? 208.314 177.505 185.162 1.00 2.54  ? 2221 MET A CE    1 
ATOM   6127  N  N     . MET A 1 2222 ? 212.262 177.087 179.165 1.00 0.07  ? 2222 MET A N     1 
ATOM   6128  C  CA    . MET A 1 2222 ? 213.446 176.520 178.534 1.00 0.02  ? 2222 MET A CA    1 
ATOM   6129  C  C     . MET A 1 2222 ? 214.421 176.162 179.647 1.00 0.02  ? 2222 MET A C     1 
ATOM   6130  O  O     . MET A 1 2222 ? 214.958 177.047 180.318 1.00 0.04  ? 2222 MET A O     1 
ATOM   6131  C  CB    . MET A 1 2222 ? 214.055 177.518 177.554 1.00 0.03  ? 2222 MET A CB    1 
ATOM   6132  C  CG    . MET A 1 2222 ? 213.124 177.912 176.431 1.00 0.05  ? 2222 MET A CG    1 
ATOM   6133  S  SD    . MET A 1 2222 ? 213.709 179.326 175.488 1.00 0.09  ? 2222 MET A SD    1 
ATOM   6134  C  CE    . MET A 1 2222 ? 212.941 180.654 176.410 1.00 0.03  ? 2222 MET A CE    1 
ATOM   6135  N  N     . VAL A 1 2223 ? 214.635 174.868 179.857 1.00 0.03  ? 2223 VAL A N     1 
ATOM   6136  C  CA    . VAL A 1 2223 ? 215.430 174.371 180.972 1.00 0.03  ? 2223 VAL A CA    1 
ATOM   6137  C  C     . VAL A 1 2223 ? 216.676 173.697 180.420 1.00 0.04  ? 2223 VAL A C     1 
ATOM   6138  O  O     . VAL A 1 2223 ? 216.587 172.839 179.536 1.00 0.09  ? 2223 VAL A O     1 
ATOM   6139  C  CB    . VAL A 1 2223 ? 214.623 173.397 181.847 1.00 0.03  ? 2223 VAL A CB    1 
ATOM   6140  C  CG1   . VAL A 1 2223 ? 215.417 173.025 183.087 1.00 0.07  ? 2223 VAL A CG1   1 
ATOM   6141  C  CG2   . VAL A 1 2223 ? 213.280 174.004 182.217 1.00 0.05  ? 2223 VAL A CG2   1 
ATOM   6142  N  N     . GLY A 1 2224 ? 217.833 174.082 180.944 1.00 0.06  ? 2224 GLY A N     1 
ATOM   6143  C  CA    . GLY A 1 2224 ? 219.080 173.482 180.547 1.00 0.10  ? 2224 GLY A CA    1 
ATOM   6144  C  C     . GLY A 1 2224 ? 220.271 174.117 181.226 1.00 0.18  ? 2224 GLY A C     1 
ATOM   6145  O  O     . GLY A 1 2224 ? 220.217 175.262 181.676 1.00 0.22  ? 2224 GLY A O     1 
ATOM   6146  N  N     . PRO A 1 2225 ? 221.384 173.387 181.290 1.00 0.55  ? 2225 PRO A N     1 
ATOM   6147  C  CA    . PRO A 1 2225 ? 222.578 173.912 181.960 1.00 0.21  ? 2225 PRO A CA    1 
ATOM   6148  C  C     . PRO A 1 2225 ? 223.063 175.195 181.303 1.00 0.30  ? 2225 PRO A C     1 
ATOM   6149  O  O     . PRO A 1 2225 ? 222.760 175.488 180.146 1.00 0.43  ? 2225 PRO A O     1 
ATOM   6150  C  CB    . PRO A 1 2225 ? 223.604 172.784 181.795 1.00 0.52  ? 2225 PRO A CB    1 
ATOM   6151  C  CG    . PRO A 1 2225 ? 222.788 171.564 181.555 1.00 0.46  ? 2225 PRO A CG    1 
ATOM   6152  C  CD    . PRO A 1 2225 ? 221.592 172.020 180.787 1.00 0.20  ? 2225 PRO A CD    1 
ATOM   6153  N  N     . SER A 1 2226 ? 223.822 175.971 182.072 1.00 0.48  ? 2226 SER A N     1 
ATOM   6154  C  CA    . SER A 1 2226 ? 224.329 177.241 181.574 1.00 0.26  ? 2226 SER A CA    1 
ATOM   6155  C  C     . SER A 1 2226 ? 225.203 177.010 180.349 1.00 0.38  ? 2226 SER A C     1 
ATOM   6156  O  O     . SER A 1 2226 ? 226.147 176.213 180.384 1.00 1.35  ? 2226 SER A O     1 
ATOM   6157  C  CB    . SER A 1 2226 ? 225.111 177.964 182.670 1.00 0.45  ? 2226 SER A CB    1 
ATOM   6158  O  OG    . SER A 1 2226 ? 225.808 179.081 182.151 1.00 0.45  ? 2226 SER A OG    1 
ATOM   6159  N  N     . GLY A 1 2227 ? 224.879 177.697 179.260 1.00 0.15  ? 2227 GLY A N     1 
ATOM   6160  C  CA    . GLY A 1 2227 ? 225.600 177.530 178.016 1.00 0.17  ? 2227 GLY A CA    1 
ATOM   6161  C  C     . GLY A 1 2227 ? 225.067 176.401 177.160 1.00 0.54  ? 2227 GLY A C     1 
ATOM   6162  O  O     . GLY A 1 2227 ? 225.838 175.647 176.563 1.00 1.46  ? 2227 GLY A O     1 
ATOM   6163  N  N     . SER A 1 2228 ? 223.744 176.271 177.101 1.00 1.05  ? 2228 SER A N     1 
ATOM   6164  C  CA    . SER A 1 2228 ? 223.089 175.250 176.294 1.00 0.65  ? 2228 SER A CA    1 
ATOM   6165  C  C     . SER A 1 2228 ? 222.419 175.831 175.057 1.00 0.33  ? 2228 SER A C     1 
ATOM   6166  O  O     . SER A 1 2228 ? 221.779 175.091 174.305 1.00 0.42  ? 2228 SER A O     1 
ATOM   6167  C  CB    . SER A 1 2228 ? 222.063 174.490 177.134 1.00 0.37  ? 2228 SER A CB    1 
ATOM   6168  O  OG    . SER A 1 2228 ? 222.692 173.785 178.187 1.00 1.93  ? 2228 SER A OG    1 
ATOM   6169  N  N     . GLY A 1 2229 ? 222.550 177.135 174.833 1.00 0.06  ? 2229 GLY A N     1 
ATOM   6170  C  CA    . GLY A 1 2229 ? 221.920 177.762 173.693 1.00 0.04  ? 2229 GLY A CA    1 
ATOM   6171  C  C     . GLY A 1 2229 ? 220.472 178.135 173.884 1.00 0.05  ? 2229 GLY A C     1 
ATOM   6172  O  O     . GLY A 1 2229 ? 219.760 178.316 172.895 1.00 0.03  ? 2229 GLY A O     1 
ATOM   6173  N  N     . LYS A 1 2230 ? 220.028 178.199 175.133 1.00 0.01  ? 2230 LYS A N     1 
ATOM   6174  C  CA    . LYS A 1 2230 ? 218.604 178.511 175.412 1.00 0.05  ? 2230 LYS A CA    1 
ATOM   6175  C  C     . LYS A 1 2230 ? 218.308 179.951 174.954 1.00 0.02  ? 2230 LYS A C     1 
ATOM   6176  O  O     . LYS A 1 2230 ? 217.317 180.138 174.223 1.00 0.03  ? 2230 LYS A O     1 
ATOM   6177  C  CB    . LYS A 1 2230 ? 218.291 178.265 176.893 1.00 0.00  ? 2230 LYS A CB    1 
ATOM   6178  C  CG    . LYS A 1 2230 ? 218.687 176.916 177.457 1.00 0.04  ? 2230 LYS A CG    1 
ATOM   6179  C  CD    . LYS A 1 2230 ? 218.318 176.782 178.929 1.00 0.02  ? 2230 LYS A CD    1 
ATOM   6180  C  CE    . LYS A 1 2230 ? 218.930 177.848 179.783 1.00 0.02  ? 2230 LYS A CE    1 
ATOM   6181  N  NZ    . LYS A 1 2230 ? 220.394 177.823 179.746 1.00 0.02  ? 2230 LYS A NZ    1 
ATOM   6182  N  N     . SER A 1 2231 ? 219.140 180.919 175.341 1.00 0.03  ? 2231 SER A N     1 
ATOM   6183  C  CA    . SER A 1 2231 ? 218.879 182.346 175.003 1.00 0.03  ? 2231 SER A CA    1 
ATOM   6184  C  C     . SER A 1 2231 ? 218.876 182.547 173.484 1.00 0.05  ? 2231 SER A C     1 
ATOM   6185  O  O     . SER A 1 2231 ? 217.927 183.182 172.973 1.00 0.12  ? 2231 SER A O     1 
ATOM   6186  C  CB    . SER A 1 2231 ? 219.876 183.266 175.663 1.00 0.02  ? 2231 SER A CB    1 
ATOM   6187  O  OG    . SER A 1 2231 ? 219.740 183.257 177.074 1.00 0.08  ? 2231 SER A OG    1 
ATOM   6188  N  N     . MET A 1 2232 ? 219.887 182.024 172.798 1.00 0.04  ? 2232 MET A N     1 
ATOM   6189  C  CA    . MET A 1 2232 ? 219.997 182.207 171.330 1.00 0.04  ? 2232 MET A CA    1 
ATOM   6190  C  C     . MET A 1 2232 ? 218.820 181.503 170.640 1.00 0.05  ? 2232 MET A C     1 
ATOM   6191  O  O     . MET A 1 2232 ? 218.396 181.992 169.578 1.00 0.13  ? 2232 MET A O     1 
ATOM   6192  C  CB    . MET A 1 2232 ? 221.342 181.684 170.811 1.00 0.12  ? 2232 MET A CB    1 
ATOM   6193  C  CG    . MET A 1 2232 ? 222.541 182.498 171.254 1.00 0.11  ? 2232 MET A CG    1 
ATOM   6194  S  SD    . MET A 1 2232 ? 222.388 184.243 170.822 1.00 13.92 ? 2232 MET A SD    1 
ATOM   6195  C  CE    . MET A 1 2232 ? 224.063 184.810 171.150 1.00 6.08  ? 2232 MET A CE    1 
ATOM   6196  N  N     . ALA A 1 2233 ? 218.300 180.425 171.239 1.00 0.05  ? 2233 ALA A N     1 
ATOM   6197  C  CA    . ALA A 1 2233 ? 217.195 179.689 170.634 1.00 0.04  ? 2233 ALA A CA    1 
ATOM   6198  C  C     . ALA A 1 2233 ? 215.942 180.549 170.529 1.00 0.09  ? 2233 ALA A C     1 
ATOM   6199  O  O     . ALA A 1 2233 ? 215.256 180.528 169.501 1.00 1.04  ? 2233 ALA A O     1 
ATOM   6200  C  CB    . ALA A 1 2233 ? 216.906 178.419 171.430 1.00 0.05  ? 2233 ALA A CB    1 
ATOM   6201  N  N     . TRP A 1 2234 ? 215.622 181.309 171.574 1.00 0.04  ? 2234 TRP A N     1 
ATOM   6202  C  CA    . TRP A 1 2234 ? 214.429 182.143 171.526 1.00 0.06  ? 2234 TRP A CA    1 
ATOM   6203  C  C     . TRP A 1 2234 ? 214.694 183.527 170.952 1.00 0.23  ? 2234 TRP A C     1 
ATOM   6204  O  O     . TRP A 1 2234 ? 213.761 184.150 170.435 1.00 3.72  ? 2234 TRP A O     1 
ATOM   6205  C  CB    . TRP A 1 2234 ? 213.782 182.255 172.915 1.00 0.04  ? 2234 TRP A CB    1 
ATOM   6206  C  CG    . TRP A 1 2234 ? 214.508 183.091 173.941 1.00 0.04  ? 2234 TRP A CG    1 
ATOM   6207  C  CD1   . TRP A 1 2234 ? 215.243 182.632 174.989 1.00 0.02  ? 2234 TRP A CD1   1 
ATOM   6208  C  CD2   . TRP A 1 2234 ? 214.526 184.520 174.039 1.00 0.04  ? 2234 TRP A CD2   1 
ATOM   6209  N  NE1   . TRP A 1 2234 ? 215.731 183.677 175.723 1.00 0.02  ? 2234 TRP A NE1   1 
ATOM   6210  C  CE2   . TRP A 1 2234 ? 215.308 184.851 175.160 1.00 0.03  ? 2234 TRP A CE2   1 
ATOM   6211  C  CE3   . TRP A 1 2234 ? 213.966 185.553 173.281 1.00 0.02  ? 2234 TRP A CE3   1 
ATOM   6212  C  CZ2   . TRP A 1 2234 ? 215.546 186.167 175.542 1.00 0.04  ? 2234 TRP A CZ2   1 
ATOM   6213  C  CZ3   . TRP A 1 2234 ? 214.206 186.855 173.659 1.00 0.02  ? 2234 TRP A CZ3   1 
ATOM   6214  C  CH2   . TRP A 1 2234 ? 214.987 187.152 174.781 1.00 0.04  ? 2234 TRP A CH2   1 
ATOM   6215  N  N     . ARG A 1 2235 ? 215.930 184.024 171.029 1.00 0.11  ? 2235 ARG A N     1 
ATOM   6216  C  CA    . ARG A 1 2235 ? 216.245 185.290 170.376 1.00 0.11  ? 2235 ARG A CA    1 
ATOM   6217  C  C     . ARG A 1 2235 ? 216.244 185.142 168.859 1.00 0.28  ? 2235 ARG A C     1 
ATOM   6218  O  O     . ARG A 1 2235 ? 215.789 186.040 168.143 1.00 0.58  ? 2235 ARG A O     1 
ATOM   6219  C  CB    . ARG A 1 2235 ? 217.592 185.821 170.870 1.00 0.30  ? 2235 ARG A CB    1 
ATOM   6220  C  CG    . ARG A 1 2235 ? 217.562 186.404 172.275 1.00 0.75  ? 2235 ARG A CG    1 
ATOM   6221  C  CD    . ARG A 1 2235 ? 218.944 186.880 172.707 1.00 2.79  ? 2235 ARG A CD    1 
ATOM   6222  N  NE    . ARG A 1 2235 ? 218.909 187.721 173.901 1.00 6.27  ? 2235 ARG A NE    1 
ATOM   6223  C  CZ    . ARG A 1 2235 ? 218.362 188.929 173.963 1.00 6.85  ? 2235 ARG A CZ    1 
ATOM   6224  N  NH1   . ARG A 1 2235 ? 217.806 189.493 172.904 1.00 8.50  ? 2235 ARG A NH1   1 
ATOM   6225  N  NH2   . ARG A 1 2235 ? 218.381 189.590 175.114 1.00 2.92  ? 2235 ARG A NH2   1 
ATOM   6226  N  N     . VAL A 1 2236 ? 216.759 184.022 168.351 1.00 0.32  ? 2236 VAL A N     1 
ATOM   6227  C  CA    . VAL A 1 2236 ? 216.737 183.776 166.912 1.00 0.45  ? 2236 VAL A CA    1 
ATOM   6228  C  C     . VAL A 1 2236 ? 215.317 183.492 166.437 1.00 0.40  ? 2236 VAL A C     1 
ATOM   6229  O  O     . VAL A 1 2236 ? 214.896 183.974 165.380 1.00 0.33  ? 2236 VAL A O     1 
ATOM   6230  C  CB    . VAL A 1 2236 ? 217.701 182.631 166.552 1.00 0.29  ? 2236 VAL A CB    1 
ATOM   6231  C  CG1   . VAL A 1 2236 ? 217.415 182.092 165.166 1.00 0.58  ? 2236 VAL A CG1   1 
ATOM   6232  C  CG2   . VAL A 1 2236 ? 219.132 183.110 166.641 1.00 0.53  ? 2236 VAL A CG2   1 
ATOM   6233  N  N     . LEU A 1 2237 ? 214.557 182.712 167.211 1.00 0.48  ? 2237 LEU A N     1 
ATOM   6234  C  CA    . LEU A 1 2237 ? 213.186 182.399 166.822 1.00 0.32  ? 2237 LEU A CA    1 
ATOM   6235  C  C     . LEU A 1 2237 ? 212.331 183.657 166.761 1.00 0.42  ? 2237 LEU A C     1 
ATOM   6236  O  O     . LEU A 1 2237 ? 211.499 183.806 165.860 1.00 0.50  ? 2237 LEU A O     1 
ATOM   6237  C  CB    . LEU A 1 2237 ? 212.580 181.385 167.794 1.00 0.26  ? 2237 LEU A CB    1 
ATOM   6238  C  CG    . LEU A 1 2237 ? 211.116 180.999 167.553 1.00 0.20  ? 2237 LEU A CG    1 
ATOM   6239  C  CD1   . LEU A 1 2237 ? 210.925 180.395 166.169 1.00 0.23  ? 2237 LEU A CD1   1 
ATOM   6240  C  CD2   . LEU A 1 2237 ? 210.619 180.050 168.626 1.00 0.15  ? 2237 LEU A CD2   1 
ATOM   6241  N  N     . LEU A 1 2238 ? 212.524 184.576 167.711 1.00 0.58  ? 2238 LEU A N     1 
ATOM   6242  C  CA    . LEU A 1 2238 ? 211.748 185.811 167.720 1.00 0.24  ? 2238 LEU A CA    1 
ATOM   6243  C  C     . LEU A 1 2238 ? 212.010 186.639 166.469 1.00 0.64  ? 2238 LEU A C     1 
ATOM   6244  O  O     . LEU A 1 2238 ? 211.075 187.182 165.869 1.00 1.45  ? 2238 LEU A O     1 
ATOM   6245  C  CB    . LEU A 1 2238 ? 212.063 186.618 168.979 1.00 0.26  ? 2238 LEU A CB    1 
ATOM   6246  C  CG    . LEU A 1 2238 ? 211.166 187.819 169.291 1.00 0.32  ? 2238 LEU A CG    1 
ATOM   6247  C  CD1   . LEU A 1 2238 ? 209.715 187.390 169.444 1.00 0.18  ? 2238 LEU A CD1   1 
ATOM   6248  C  CD2   . LEU A 1 2238 ? 211.645 188.535 170.539 1.00 0.09  ? 2238 LEU A CD2   1 
ATOM   6249  N  N     . LYS A 1 2239 ? 213.275 186.750 166.058 1.00 0.71  ? 2239 LYS A N     1 
ATOM   6250  C  CA    . LYS A 1 2239 ? 213.595 187.475 164.832 1.00 0.80  ? 2239 LYS A CA    1 
ATOM   6251  C  C     . LYS A 1 2239 ? 213.070 186.749 163.601 1.00 0.84  ? 2239 LYS A C     1 
ATOM   6252  O  O     . LYS A 1 2239 ? 212.584 187.385 162.660 1.00 2.68  ? 2239 LYS A O     1 
ATOM   6253  C  CB    . LYS A 1 2239 ? 215.107 187.687 164.726 1.00 1.15  ? 2239 LYS A CB    1 
ATOM   6254  C  CG    . LYS A 1 2239 ? 215.683 188.564 165.814 1.00 4.57  ? 2239 LYS A CG    1 
ATOM   6255  C  CD    . LYS A 1 2239 ? 217.201 188.548 165.798 1.00 4.44  ? 2239 LYS A CD    1 
ATOM   6256  C  CE    . LYS A 1 2239 ? 217.769 189.589 166.748 1.00 3.45  ? 2239 LYS A CE    1 
ATOM   6257  N  NZ    . LYS A 1 2239 ? 219.251 189.543 166.803 1.00 5.59  ? 2239 LYS A NZ    1 
ATOM   6258  N  N     . ALA A 1 2240 ? 213.170 185.417 163.583 1.00 0.74  ? 2240 ALA A N     1 
ATOM   6259  C  CA    . ALA A 1 2240 ? 212.711 184.652 162.429 1.00 1.65  ? 2240 ALA A CA    1 
ATOM   6260  C  C     . ALA A 1 2240 ? 211.206 184.789 162.234 1.00 1.82  ? 2240 ALA A C     1 
ATOM   6261  O  O     . ALA A 1 2240 ? 210.730 184.913 161.100 1.00 2.83  ? 2240 ALA A O     1 
ATOM   6262  C  CB    . ALA A 1 2240 ? 213.103 183.184 162.583 1.00 1.08  ? 2240 ALA A CB    1 
ATOM   6263  N  N     . LEU A 1 2241 ? 210.444 184.764 163.328 1.00 1.03  ? 2241 LEU A N     1 
ATOM   6264  C  CA    . LEU A 1 2241 ? 208.999 184.932 163.222 1.00 1.23  ? 2241 LEU A CA    1 
ATOM   6265  C  C     . LEU A 1 2241 ? 208.629 186.330 162.751 1.00 3.25  ? 2241 LEU A C     1 
ATOM   6266  O  O     . LEU A 1 2241 ? 207.606 186.505 162.081 1.00 6.83  ? 2241 LEU A O     1 
ATOM   6267  C  CB    . LEU A 1 2241 ? 208.336 184.624 164.562 1.00 0.74  ? 2241 LEU A CB    1 
ATOM   6268  C  CG    . LEU A 1 2241 ? 208.491 183.176 165.028 1.00 0.74  ? 2241 LEU A CG    1 
ATOM   6269  C  CD1   . LEU A 1 2241 ? 207.919 182.980 166.422 1.00 0.31  ? 2241 LEU A CD1   1 
ATOM   6270  C  CD2   . LEU A 1 2241 ? 207.851 182.227 164.033 1.00 1.61  ? 2241 LEU A CD2   1 
ATOM   6271  N  N     . GLU A 1 2242 ? 209.440 187.335 163.090 1.00 2.33  ? 2242 GLU A N     1 
ATOM   6272  C  CA    . GLU A 1 2242 ? 209.196 188.681 162.582 1.00 2.72  ? 2242 GLU A CA    1 
ATOM   6273  C  C     . GLU A 1 2242 ? 209.315 188.724 161.066 1.00 3.92  ? 2242 GLU A C     1 
ATOM   6274  O  O     . GLU A 1 2242 ? 208.518 189.383 160.391 1.00 7.12  ? 2242 GLU A O     1 
ATOM   6275  C  CB    . GLU A 1 2242 ? 210.167 189.671 163.225 1.00 3.40  ? 2242 GLU A CB    1 
ATOM   6276  C  CG    . GLU A 1 2242 ? 209.974 191.108 162.775 1.00 3.06  ? 2242 GLU A CG    1 
ATOM   6277  C  CD    . GLU A 1 2242 ? 210.393 192.115 163.826 1.00 9.97  ? 2242 GLU A CD    1 
ATOM   6278  O  OE1   . GLU A 1 2242 ? 210.798 191.695 164.930 1.00 6.50  ? 2242 GLU A OE1   1 
ATOM   6279  O  OE2   . GLU A 1 2242 ? 210.314 193.331 163.549 1.00 15.04 ? 2242 GLU A OE2   1 
ATOM   6280  N  N     . ARG A 1 2243 ? 210.310 188.030 160.515 1.00 4.39  ? 2243 ARG A N     1 
ATOM   6281  C  CA    . ARG A 1 2243 ? 210.508 188.015 159.071 1.00 6.62  ? 2243 ARG A CA    1 
ATOM   6282  C  C     . ARG A 1 2243 ? 209.498 187.106 158.381 1.00 5.58  ? 2243 ARG A C     1 
ATOM   6283  O  O     . ARG A 1 2243 ? 209.002 187.433 157.298 1.00 11.87 ? 2243 ARG A O     1 
ATOM   6284  C  CB    . ARG A 1 2243 ? 211.932 187.564 158.756 1.00 6.18  ? 2243 ARG A CB    1 
ATOM   6285  C  CG    . ARG A 1 2243 ? 212.991 188.551 159.201 1.00 9.13  ? 2243 ARG A CG    1 
ATOM   6286  C  CD    . ARG A 1 2243 ? 214.380 188.051 158.868 1.00 15.54 ? 2243 ARG A CD    1 
ATOM   6287  N  NE    . ARG A 1 2243 ? 215.418 188.975 159.309 1.00 15.19 ? 2243 ARG A NE    1 
ATOM   6288  C  CZ    . ARG A 1 2243 ? 216.718 188.748 159.189 1.00 17.32 ? 2243 ARG A CZ    1 
ATOM   6289  N  NH1   . ARG A 1 2243 ? 217.177 187.651 158.615 1.00 15.71 ? 2243 ARG A NH1   1 
ATOM   6290  N  NH2   . ARG A 1 2243 ? 217.580 189.647 159.656 1.00 18.06 ? 2243 ARG A NH2   1 
ATOM   6291  N  N     . LEU A 1 2244 ? 209.184 185.967 158.999 1.00 5.98  ? 2244 LEU A N     1 
ATOM   6292  C  CA    . LEU A 1 2244 ? 208.276 185.005 158.387 1.00 5.10  ? 2244 LEU A CA    1 
ATOM   6293  C  C     . LEU A 1 2244 ? 206.841 185.517 158.377 1.00 5.80  ? 2244 LEU A C     1 
ATOM   6294  O  O     . LEU A 1 2244 ? 206.151 185.442 157.355 1.00 9.92  ? 2244 LEU A O     1 
ATOM   6295  C  CB    . LEU A 1 2244 ? 208.363 183.672 159.130 1.00 4.03  ? 2244 LEU A CB    1 
ATOM   6296  C  CG    . LEU A 1 2244 ? 207.548 182.511 158.560 1.00 6.94  ? 2244 LEU A CG    1 
ATOM   6297  C  CD1   . LEU A 1 2244 ? 208.281 181.868 157.401 1.00 8.76  ? 2244 LEU A CD1   1 
ATOM   6298  C  CD2   . LEU A 1 2244 ? 207.236 181.490 159.643 1.00 5.34  ? 2244 LEU A CD2   1 
ATOM   6299  N  N     . GLU A 1 2245 ? 206.377 186.047 159.509 1.00 5.53  ? 2245 GLU A N     1 
ATOM   6300  C  CA    . GLU A 1 2245 ? 204.975 186.395 159.687 1.00 4.32  ? 2245 GLU A CA    1 
ATOM   6301  C  C     . GLU A 1 2245 ? 204.689 187.880 159.509 1.00 6.88  ? 2245 GLU A C     1 
ATOM   6302  O  O     . GLU A 1 2245 ? 203.521 188.256 159.375 1.00 12.02 ? 2245 GLU A O     1 
ATOM   6303  C  CB    . GLU A 1 2245 ? 204.506 185.957 161.080 1.00 8.25  ? 2245 GLU A CB    1 
ATOM   6304  C  CG    . GLU A 1 2245 ? 204.472 184.452 161.278 1.00 10.42 ? 2245 GLU A CG    1 
ATOM   6305  C  CD    . GLU A 1 2245 ? 204.024 184.061 162.671 1.00 18.32 ? 2245 GLU A CD    1 
ATOM   6306  O  OE1   . GLU A 1 2245 ? 203.860 184.962 163.519 1.00 14.97 ? 2245 GLU A OE1   1 
ATOM   6307  O  OE2   . GLU A 1 2245 ? 203.837 182.850 162.918 1.00 24.07 ? 2245 GLU A OE2   1 
ATOM   6308  N  N     . GLY A 1 2246 ? 205.717 188.724 159.507 1.00 3.41  ? 2246 GLY A N     1 
ATOM   6309  C  CA    . GLY A 1 2246 ? 205.521 190.154 159.420 1.00 2.66  ? 2246 GLY A CA    1 
ATOM   6310  C  C     . GLY A 1 2246 ? 205.157 190.830 160.723 1.00 5.58  ? 2246 GLY A C     1 
ATOM   6311  O  O     . GLY A 1 2246 ? 204.967 192.053 160.734 1.00 6.50  ? 2246 GLY A O     1 
ATOM   6312  N  N     . VAL A 1 2247 ? 205.063 190.083 161.817 1.00 4.94  ? 2247 VAL A N     1 
ATOM   6313  C  CA    . VAL A 1 2247 ? 204.678 190.630 163.111 1.00 5.05  ? 2247 VAL A CA    1 
ATOM   6314  C  C     . VAL A 1 2247 ? 205.936 190.964 163.898 1.00 3.76  ? 2247 VAL A C     1 
ATOM   6315  O  O     . VAL A 1 2247 ? 206.808 190.109 164.086 1.00 5.16  ? 2247 VAL A O     1 
ATOM   6316  C  CB    . VAL A 1 2247 ? 203.789 189.640 163.881 1.00 3.09  ? 2247 VAL A CB    1 
ATOM   6317  C  CG1   . VAL A 1 2247 ? 203.435 190.189 165.251 1.00 1.74  ? 2247 VAL A CG1   1 
ATOM   6318  C  CG2   . VAL A 1 2247 ? 202.533 189.328 163.081 1.00 2.19  ? 2247 VAL A CG2   1 
ATOM   6319  N  N     . GLU A 1 2248 ? 206.032 192.209 164.357 1.00 3.62  ? 2248 GLU A N     1 
ATOM   6320  C  CA    . GLU A 1 2248 ? 207.189 192.640 165.128 1.00 3.76  ? 2248 GLU A CA    1 
ATOM   6321  C  C     . GLU A 1 2248 ? 207.252 191.892 166.455 1.00 4.10  ? 2248 GLU A C     1 
ATOM   6322  O  O     . GLU A 1 2248 ? 206.242 191.751 167.150 1.00 5.35  ? 2248 GLU A O     1 
ATOM   6323  C  CB    . GLU A 1 2248 ? 207.132 194.146 165.369 1.00 4.99  ? 2248 GLU A CB    1 
ATOM   6324  C  CG    . GLU A 1 2248 ? 208.144 194.657 166.380 1.00 7.63  ? 2248 GLU A CG    1 
ATOM   6325  C  CD    . GLU A 1 2248 ? 208.003 196.142 166.642 1.00 21.10 ? 2248 GLU A CD    1 
ATOM   6326  O  OE1   . GLU A 1 2248 ? 207.173 196.789 165.970 1.00 22.87 ? 2248 GLU A OE1   1 
ATOM   6327  O  OE2   . GLU A 1 2248 ? 208.720 196.663 167.521 1.00 23.85 ? 2248 GLU A OE2   1 
ATOM   6328  N  N     . GLY A 1 2249 ? 208.442 191.410 166.803 1.00 3.47  ? 2249 GLY A N     1 
ATOM   6329  C  CA    . GLY A 1 2249 ? 208.648 190.669 168.032 1.00 1.25  ? 2249 GLY A CA    1 
ATOM   6330  C  C     . GLY A 1 2249 ? 209.370 191.515 169.063 1.00 0.97  ? 2249 GLY A C     1 
ATOM   6331  O  O     . GLY A 1 2249 ? 210.413 192.107 168.779 1.00 3.91  ? 2249 GLY A O     1 
ATOM   6332  N  N     . VAL A 1 2250 ? 208.798 191.567 170.261 1.00 0.76  ? 2250 VAL A N     1 
ATOM   6333  C  CA    . VAL A 1 2250 ? 209.342 192.346 171.365 1.00 0.31  ? 2250 VAL A CA    1 
ATOM   6334  C  C     . VAL A 1 2250 ? 209.531 191.419 172.554 1.00 0.17  ? 2250 VAL A C     1 
ATOM   6335  O  O     . VAL A 1 2250 ? 208.600 190.708 172.947 1.00 0.24  ? 2250 VAL A O     1 
ATOM   6336  C  CB    . VAL A 1 2250 ? 208.423 193.525 171.737 1.00 0.27  ? 2250 VAL A CB    1 
ATOM   6337  C  CG1   . VAL A 1 2250 ? 208.931 194.225 172.989 1.00 0.20  ? 2250 VAL A CG1   1 
ATOM   6338  C  CG2   . VAL A 1 2250 ? 208.319 194.498 170.578 1.00 1.41  ? 2250 VAL A CG2   1 
ATOM   6339  N  N     . ALA A 1 2251 ? 210.730 191.427 173.126 1.00 0.12  ? 2251 ALA A N     1 
ATOM   6340  C  CA    . ALA A 1 2251 ? 211.049 190.617 174.292 1.00 0.03  ? 2251 ALA A CA    1 
ATOM   6341  C  C     . ALA A 1 2251 ? 211.360 191.525 175.473 1.00 0.04  ? 2251 ALA A C     1 
ATOM   6342  O  O     . ALA A 1 2251 ? 212.183 192.437 175.360 1.00 0.08  ? 2251 ALA A O     1 
ATOM   6343  C  CB    . ALA A 1 2251 ? 212.232 189.690 174.015 1.00 0.02  ? 2251 ALA A CB    1 
ATOM   6344  N  N     . HIS A 1 2252 ? 210.693 191.277 176.595 1.00 0.03  ? 2252 HIS A N     1 
ATOM   6345  C  CA    . HIS A 1 2252 ? 210.990 191.932 177.863 1.00 0.02  ? 2252 HIS A CA    1 
ATOM   6346  C  C     . HIS A 1 2252 ? 211.653 190.893 178.754 1.00 0.03  ? 2252 HIS A C     1 
ATOM   6347  O  O     . HIS A 1 2252 ? 210.991 189.966 179.232 1.00 0.06  ? 2252 HIS A O     1 
ATOM   6348  C  CB    . HIS A 1 2252 ? 209.722 192.482 178.515 1.00 0.03  ? 2252 HIS A CB    1 
ATOM   6349  C  CG    . HIS A 1 2252 ? 208.903 193.350 177.612 1.00 0.05  ? 2252 HIS A CG    1 
ATOM   6350  N  ND1   . HIS A 1 2252 ? 209.000 194.724 177.609 1.00 0.05  ? 2252 HIS A ND1   1 
ATOM   6351  C  CD2   . HIS A 1 2252 ? 207.963 193.037 176.690 1.00 0.11  ? 2252 HIS A CD2   1 
ATOM   6352  C  CE1   . HIS A 1 2252 ? 208.158 195.221 176.720 1.00 0.04  ? 2252 HIS A CE1   1 
ATOM   6353  N  NE2   . HIS A 1 2252 ? 207.517 194.219 176.149 1.00 0.07  ? 2252 HIS A NE2   1 
ATOM   6354  N  N     . ILE A 1 2253 ? 212.955 191.035 178.966 1.00 0.03  ? 2253 ILE A N     1 
ATOM   6355  C  CA    . ILE A 1 2253 ? 213.718 190.068 179.744 1.00 0.01  ? 2253 ILE A CA    1 
ATOM   6356  C  C     . ILE A 1 2253 ? 213.811 190.578 181.175 1.00 0.05  ? 2253 ILE A C     1 
ATOM   6357  O  O     . ILE A 1 2253 ? 214.264 191.699 181.416 1.00 0.03  ? 2253 ILE A O     1 
ATOM   6358  C  CB    . ILE A 1 2253 ? 215.114 189.836 179.146 1.00 0.06  ? 2253 ILE A CB    1 
ATOM   6359  C  CG1   . ILE A 1 2253 ? 215.018 189.241 177.740 1.00 0.04  ? 2253 ILE A CG1   1 
ATOM   6360  C  CG2   . ILE A 1 2253 ? 215.907 188.896 180.025 1.00 0.04  ? 2253 ILE A CG2   1 
ATOM   6361  C  CD1   . ILE A 1 2253 ? 214.919 190.261 176.632 1.00 0.03  ? 2253 ILE A CD1   1 
ATOM   6362  N  N     . ILE A 1 2254 ? 213.379 189.755 182.125 1.00 0.07  ? 2254 ILE A N     1 
ATOM   6363  C  CA    . ILE A 1 2254 ? 213.329 190.120 183.534 1.00 0.07  ? 2254 ILE A CA    1 
ATOM   6364  C  C     . ILE A 1 2254 ? 214.148 189.112 184.324 1.00 0.07  ? 2254 ILE A C     1 
ATOM   6365  O  O     . ILE A 1 2254 ? 214.016 187.902 184.117 1.00 0.15  ? 2254 ILE A O     1 
ATOM   6366  C  CB    . ILE A 1 2254 ? 211.881 190.172 184.057 1.00 0.05  ? 2254 ILE A CB    1 
ATOM   6367  C  CG1   . ILE A 1 2254 ? 211.084 191.252 183.326 1.00 0.02  ? 2254 ILE A CG1   1 
ATOM   6368  C  CG2   . ILE A 1 2254 ? 211.858 190.404 185.562 1.00 0.07  ? 2254 ILE A CG2   1 
ATOM   6369  C  CD1   . ILE A 1 2254 ? 209.635 191.323 183.740 1.00 0.01  ? 2254 ILE A CD1   1 
ATOM   6370  N  N     . ASP A 1 2255 ? 215.002 189.609 185.220 1.00 0.13  ? 2255 ASP A N     1 
ATOM   6371  C  CA    . ASP A 1 2255 ? 215.624 188.749 186.216 1.00 0.15  ? 2255 ASP A CA    1 
ATOM   6372  C  C     . ASP A 1 2255 ? 214.773 188.815 187.476 1.00 0.17  ? 2255 ASP A C     1 
ATOM   6373  O  O     . ASP A 1 2255 ? 214.884 189.784 188.243 1.00 0.19  ? 2255 ASP A O     1 
ATOM   6374  C  CB    . ASP A 1 2255 ? 217.062 189.180 186.507 1.00 0.13  ? 2255 ASP A CB    1 
ATOM   6375  C  CG    . ASP A 1 2255 ? 217.880 188.077 187.158 1.00 1.35  ? 2255 ASP A CG    1 
ATOM   6376  O  OD1   . ASP A 1 2255 ? 217.321 187.314 187.971 1.00 0.50  ? 2255 ASP A OD1   1 
ATOM   6377  O  OD2   . ASP A 1 2255 ? 219.087 187.974 186.856 1.00 6.11  ? 2255 ASP A OD2   1 
ATOM   6378  N  N     . PRO A 1 2256 ? 213.901 187.835 187.724 1.00 0.20  ? 2256 PRO A N     1 
ATOM   6379  C  CA    . PRO A 1 2256 ? 212.980 187.942 188.865 1.00 0.31  ? 2256 PRO A CA    1 
ATOM   6380  C  C     . PRO A 1 2256 ? 213.666 187.971 190.220 1.00 0.36  ? 2256 PRO A C     1 
ATOM   6381  O  O     . PRO A 1 2256 ? 213.145 188.601 191.145 1.00 1.42  ? 2256 PRO A O     1 
ATOM   6382  C  CB    . PRO A 1 2256 ? 212.094 186.701 188.704 1.00 0.08  ? 2256 PRO A CB    1 
ATOM   6383  C  CG    . PRO A 1 2256 ? 212.966 185.735 187.986 1.00 0.07  ? 2256 PRO A CG    1 
ATOM   6384  C  CD    . PRO A 1 2256 ? 213.772 186.545 187.030 1.00 0.11  ? 2256 PRO A CD    1 
ATOM   6385  N  N     . LYS A 1 2257 ? 214.806 187.304 190.374 1.00 0.29  ? 2257 LYS A N     1 
ATOM   6386  C  CA    . LYS A 1 2257 ? 215.488 187.227 191.659 1.00 0.32  ? 2257 LYS A CA    1 
ATOM   6387  C  C     . LYS A 1 2257 ? 216.559 188.294 191.836 1.00 0.35  ? 2257 LYS A C     1 
ATOM   6388  O  O     . LYS A 1 2257 ? 217.193 188.345 192.893 1.00 0.61  ? 2257 LYS A O     1 
ATOM   6389  C  CB    . LYS A 1 2257 ? 216.103 185.838 191.848 1.00 0.62  ? 2257 LYS A CB    1 
ATOM   6390  C  CG    . LYS A 1 2257 ? 215.081 184.723 191.983 1.00 0.36  ? 2257 LYS A CG    1 
ATOM   6391  C  CD    . LYS A 1 2257 ? 214.381 184.768 193.327 1.00 0.36  ? 2257 LYS A CD    1 
ATOM   6392  C  CE    . LYS A 1 2257 ? 215.315 184.384 194.462 1.00 2.08  ? 2257 LYS A CE    1 
ATOM   6393  N  NZ    . LYS A 1 2257 ? 215.327 182.918 194.714 1.00 0.55  ? 2257 LYS A NZ    1 
ATOM   6394  N  N     . ALA A 1 2258 ? 216.781 189.141 190.832 1.00 0.28  ? 2258 ALA A N     1 
ATOM   6395  C  CA    . ALA A 1 2258 ? 217.685 190.272 190.986 1.00 0.18  ? 2258 ALA A CA    1 
ATOM   6396  C  C     . ALA A 1 2258 ? 217.043 191.429 191.735 1.00 0.37  ? 2258 ALA A C     1 
ATOM   6397  O  O     . ALA A 1 2258 ? 217.744 192.374 192.108 1.00 0.65  ? 2258 ALA A O     1 
ATOM   6398  C  CB    . ALA A 1 2258 ? 218.173 190.752 189.617 1.00 0.08  ? 2258 ALA A CB    1 
ATOM   6399  N  N     . ILE A 1 2259 ? 215.732 191.370 191.957 1.00 0.66  ? 2259 ILE A N     1 
ATOM   6400  C  CA    . ILE A 1 2259 ? 214.982 192.399 192.657 1.00 0.61  ? 2259 ILE A CA    1 
ATOM   6401  C  C     . ILE A 1 2259 ? 214.117 191.721 193.710 1.00 0.56  ? 2259 ILE A C     1 
ATOM   6402  O  O     . ILE A 1 2259 ? 213.919 190.505 193.696 1.00 1.15  ? 2259 ILE A O     1 
ATOM   6403  C  CB    . ILE A 1 2259 ? 214.113 193.239 191.697 1.00 0.35  ? 2259 ILE A CB    1 
ATOM   6404  C  CG1   . ILE A 1 2259 ? 213.048 192.354 191.042 1.00 0.15  ? 2259 ILE A CG1   1 
ATOM   6405  C  CG2   . ILE A 1 2259 ? 214.976 193.912 190.644 1.00 0.07  ? 2259 ILE A CG2   1 
ATOM   6406  C  CD1   . ILE A 1 2259 ? 212.173 193.070 190.053 1.00 0.09  ? 2259 ILE A CD1   1 
ATOM   6407  N  N     . SER A 1 2260 ? 213.604 192.524 194.636 1.00 0.44  ? 2260 SER A N     1 
ATOM   6408  C  CA    . SER A 1 2260 ? 212.685 191.995 195.631 1.00 0.83  ? 2260 SER A CA    1 
ATOM   6409  C  C     . SER A 1 2260 ? 211.359 191.615 194.977 1.00 0.65  ? 2260 SER A C     1 
ATOM   6410  O  O     . SER A 1 2260 ? 210.990 192.122 193.914 1.00 0.47  ? 2260 SER A O     1 
ATOM   6411  C  CB    . SER A 1 2260 ? 212.453 193.014 196.746 1.00 1.54  ? 2260 SER A CB    1 
ATOM   6412  O  OG    . SER A 1 2260 ? 211.771 194.157 196.267 1.00 1.54  ? 2260 SER A OG    1 
ATOM   6413  N  N     . LYS A 1 2261 ? 210.645 190.691 195.624 1.00 0.33  ? 2261 LYS A N     1 
ATOM   6414  C  CA    . LYS A 1 2261 ? 209.330 190.305 195.126 1.00 0.62  ? 2261 LYS A CA    1 
ATOM   6415  C  C     . LYS A 1 2261 ? 208.363 191.481 195.150 1.00 0.60  ? 2261 LYS A C     1 
ATOM   6416  O  O     . LYS A 1 2261 ? 207.447 191.552 194.325 1.00 0.36  ? 2261 LYS A O     1 
ATOM   6417  C  CB    . LYS A 1 2261 ? 208.779 189.137 195.942 1.00 1.32  ? 2261 LYS A CB    1 
ATOM   6418  C  CG    . LYS A 1 2261 ? 207.457 188.598 195.436 1.00 0.71  ? 2261 LYS A CG    1 
ATOM   6419  C  CD    . LYS A 1 2261 ? 206.884 187.573 196.385 1.00 2.98  ? 2261 LYS A CD    1 
ATOM   6420  C  CE    . LYS A 1 2261 ? 205.517 187.107 195.928 1.00 2.60  ? 2261 LYS A CE    1 
ATOM   6421  N  NZ    . LYS A 1 2261 ? 204.939 186.124 196.881 1.00 4.46  ? 2261 LYS A NZ    1 
ATOM   6422  N  N     . ASP A 1 2262 ? 208.560 192.416 196.082 1.00 1.37  ? 2262 ASP A N     1 
ATOM   6423  C  CA    . ASP A 1 2262 ? 207.776 193.644 196.085 1.00 0.98  ? 2262 ASP A CA    1 
ATOM   6424  C  C     . ASP A 1 2262 ? 208.013 194.449 194.813 1.00 1.19  ? 2262 ASP A C     1 
ATOM   6425  O  O     . ASP A 1 2262 ? 207.081 195.048 194.265 1.00 1.33  ? 2262 ASP A O     1 
ATOM   6426  C  CB    . ASP A 1 2262 ? 208.122 194.480 197.316 1.00 5.15  ? 2262 ASP A CB    1 
ATOM   6427  C  CG    . ASP A 1 2262 ? 207.643 193.845 198.605 1.00 11.26 ? 2262 ASP A CG    1 
ATOM   6428  O  OD1   . ASP A 1 2262 ? 206.629 193.119 198.576 1.00 15.74 ? 2262 ASP A OD1   1 
ATOM   6429  O  OD2   . ASP A 1 2262 ? 208.281 194.079 199.653 1.00 13.74 ? 2262 ASP A OD2   1 
ATOM   6430  N  N     . HIS A 1 2263 ? 209.256 194.482 194.333 1.00 1.28  ? 2263 HIS A N     1 
ATOM   6431  C  CA    . HIS A 1 2263 ? 209.572 195.216 193.116 1.00 0.55  ? 2263 HIS A CA    1 
ATOM   6432  C  C     . HIS A 1 2263 ? 209.204 194.449 191.852 1.00 0.17  ? 2263 HIS A C     1 
ATOM   6433  O  O     . HIS A 1 2263 ? 209.153 195.047 190.774 1.00 0.13  ? 2263 HIS A O     1 
ATOM   6434  C  CB    . HIS A 1 2263 ? 211.060 195.572 193.093 1.00 0.40  ? 2263 HIS A CB    1 
ATOM   6435  C  CG    . HIS A 1 2263 ? 211.424 196.694 194.013 1.00 0.89  ? 2263 HIS A CG    1 
ATOM   6436  N  ND1   . HIS A 1 2263 ? 212.668 196.809 194.592 1.00 3.07  ? 2263 HIS A ND1   1 
ATOM   6437  C  CD2   . HIS A 1 2263 ? 210.704 197.752 194.454 1.00 1.74  ? 2263 HIS A CD2   1 
ATOM   6438  C  CE1   . HIS A 1 2263 ? 212.700 197.889 195.350 1.00 2.37  ? 2263 HIS A CE1   1 
ATOM   6439  N  NE2   . HIS A 1 2263 ? 211.521 198.479 195.284 1.00 4.37  ? 2263 HIS A NE2   1 
ATOM   6440  N  N     . LEU A 1 2264 ? 208.940 193.147 191.961 1.00 0.21  ? 2264 LEU A N     1 
ATOM   6441  C  CA    . LEU A 1 2264 ? 208.560 192.361 190.791 1.00 0.09  ? 2264 LEU A CA    1 
ATOM   6442  C  C     . LEU A 1 2264 ? 207.075 192.505 190.480 1.00 0.03  ? 2264 LEU A C     1 
ATOM   6443  O  O     . LEU A 1 2264 ? 206.694 192.736 189.329 1.00 0.05  ? 2264 LEU A O     1 
ATOM   6444  C  CB    . LEU A 1 2264 ? 208.926 190.891 191.009 1.00 0.09  ? 2264 LEU A CB    1 
ATOM   6445  C  CG    . LEU A 1 2264 ? 208.589 189.908 189.886 1.00 0.03  ? 2264 LEU A CG    1 
ATOM   6446  C  CD1   . LEU A 1 2264 ? 209.313 190.279 188.598 1.00 0.04  ? 2264 LEU A CD1   1 
ATOM   6447  C  CD2   . LEU A 1 2264 ? 208.936 188.490 190.305 1.00 0.04  ? 2264 LEU A CD2   1 
ATOM   6448  N  N     . TYR A 1 2265 ? 206.224 192.384 191.494 1.00 0.04  ? 2265 TYR A N     1 
ATOM   6449  C  CA    . TYR A 1 2265 ? 204.782 192.410 191.296 1.00 0.11  ? 2265 TYR A CA    1 
ATOM   6450  C  C     . TYR A 1 2265 ? 204.114 193.692 191.763 1.00 0.09  ? 2265 TYR A C     1 
ATOM   6451  O  O     . TYR A 1 2265 ? 203.059 194.046 191.238 1.00 0.08  ? 2265 TYR A O     1 
ATOM   6452  C  CB    . TYR A 1 2265 ? 204.127 191.226 192.011 1.00 0.04  ? 2265 TYR A CB    1 
ATOM   6453  C  CG    . TYR A 1 2265 ? 204.526 189.888 191.446 1.00 0.02  ? 2265 TYR A CG    1 
ATOM   6454  C  CD1   . TYR A 1 2265 ? 204.143 189.515 190.166 1.00 0.05  ? 2265 TYR A CD1   1 
ATOM   6455  C  CD2   . TYR A 1 2265 ? 205.286 188.996 192.190 1.00 0.04  ? 2265 TYR A CD2   1 
ATOM   6456  C  CE1   . TYR A 1 2265 ? 204.502 188.293 189.644 1.00 0.09  ? 2265 TYR A CE1   1 
ATOM   6457  C  CE2   . TYR A 1 2265 ? 205.650 187.773 191.677 1.00 0.08  ? 2265 TYR A CE2   1 
ATOM   6458  C  CZ    . TYR A 1 2265 ? 205.256 187.426 190.402 1.00 0.09  ? 2265 TYR A CZ    1 
ATOM   6459  O  OH    . TYR A 1 2265 ? 205.616 186.207 189.884 1.00 0.18  ? 2265 TYR A OH    1 
ATOM   6460  N  N     . GLY A 1 2266 ? 204.691 194.388 192.730 1.00 0.15  ? 2266 GLY A N     1 
ATOM   6461  C  CA    . GLY A 1 2266 ? 204.126 195.614 193.247 1.00 0.21  ? 2266 GLY A CA    1 
ATOM   6462  C  C     . GLY A 1 2266 ? 203.787 195.505 194.719 1.00 0.30  ? 2266 GLY A C     1 
ATOM   6463  O  O     . GLY A 1 2266 ? 203.862 194.441 195.333 1.00 0.81  ? 2266 GLY A O     1 
ATOM   6464  N  N     . THR A 1 2267 ? 203.410 196.648 195.284 1.00 0.53  ? 2267 THR A N     1 
ATOM   6465  C  CA    . THR A 1 2267 ? 203.081 196.748 196.697 1.00 0.95  ? 2267 THR A CA    1 
ATOM   6466  C  C     . THR A 1 2267 ? 201.770 197.496 196.861 1.00 0.84  ? 2267 THR A C     1 
ATOM   6467  O  O     . THR A 1 2267 ? 201.426 198.367 196.059 1.00 0.50  ? 2267 THR A O     1 
ATOM   6468  C  CB    . THR A 1 2267 ? 204.165 197.477 197.505 1.00 0.89  ? 2267 THR A CB    1 
ATOM   6469  O  OG1   . THR A 1 2267 ? 204.343 198.802 196.987 1.00 3.36  ? 2267 THR A OG1   1 
ATOM   6470  C  CG2   . THR A 1 2267 ? 205.476 196.735 197.443 1.00 1.16  ? 2267 THR A CG2   1 
ATOM   6471  N  N     . LEU A 1 2268 ? 201.047 197.143 197.915 1.00 1.28  ? 2268 LEU A N     1 
ATOM   6472  C  CA    . LEU A 1 2268 ? 199.870 197.877 198.353 1.00 2.88  ? 2268 LEU A CA    1 
ATOM   6473  C  C     . LEU A 1 2268 ? 200.272 198.696 199.573 1.00 3.37  ? 2268 LEU A C     1 
ATOM   6474  O  O     . LEU A 1 2268 ? 200.807 198.144 200.540 1.00 5.11  ? 2268 LEU A O     1 
ATOM   6475  C  CB    . LEU A 1 2268 ? 198.725 196.918 198.673 1.00 1.78  ? 2268 LEU A CB    1 
ATOM   6476  C  CG    . LEU A 1 2268 ? 197.300 197.463 198.676 1.00 3.22  ? 2268 LEU A CG    1 
ATOM   6477  C  CD1   . LEU A 1 2268 ? 197.047 198.312 197.446 1.00 2.67  ? 2268 LEU A CD1   1 
ATOM   6478  C  CD2   . LEU A 1 2268 ? 196.320 196.306 198.734 1.00 3.29  ? 2268 LEU A CD2   1 
ATOM   6479  N  N     . ASP A 1 2269 ? 200.035 200.001 199.518 1.00 6.89  ? 2269 ASP A N     1 
ATOM   6480  C  CA    . ASP A 1 2269 ? 200.476 200.891 200.580 1.00 9.55  ? 2269 ASP A CA    1 
ATOM   6481  C  C     . ASP A 1 2269 ? 199.768 200.535 201.887 1.00 10.89 ? 2269 ASP A C     1 
ATOM   6482  O  O     . ASP A 1 2269 ? 198.534 200.406 201.901 1.00 14.07 ? 2269 ASP A O     1 
ATOM   6483  C  CB    . ASP A 1 2269 ? 200.206 202.348 200.208 1.00 10.28 ? 2269 ASP A CB    1 
ATOM   6484  C  CG    . ASP A 1 2269 ? 200.760 203.332 201.228 1.00 17.95 ? 2269 ASP A CG    1 
ATOM   6485  O  OD1   . ASP A 1 2269 ? 200.323 203.311 202.399 1.00 20.87 ? 2269 ASP A OD1   1 
ATOM   6486  O  OD2   . ASP A 1 2269 ? 201.643 204.132 200.857 1.00 20.12 ? 2269 ASP A OD2   1 
ATOM   6487  N  N     . PRO A 1 2270 ? 200.501 200.364 202.986 1.00 9.63  ? 2270 PRO A N     1 
ATOM   6488  C  CA    . PRO A 1 2270 ? 199.857 199.980 204.254 1.00 11.30 ? 2270 PRO A CA    1 
ATOM   6489  C  C     . PRO A 1 2270 ? 198.817 200.969 204.751 1.00 17.32 ? 2270 PRO A C     1 
ATOM   6490  O  O     . PRO A 1 2270 ? 197.839 200.553 205.387 1.00 20.01 ? 2270 PRO A O     1 
ATOM   6491  C  CB    . PRO A 1 2270 ? 201.042 199.880 205.224 1.00 14.74 ? 2270 PRO A CB    1 
ATOM   6492  C  CG    . PRO A 1 2270 ? 202.224 199.614 204.352 1.00 11.63 ? 2270 PRO A CG    1 
ATOM   6493  C  CD    . PRO A 1 2270 ? 201.969 200.380 203.090 1.00 10.19 ? 2270 PRO A CD    1 
ATOM   6494  N  N     . ASN A 1 2271 ? 198.983 202.263 204.476 1.00 14.30 ? 2271 ASN A N     1 
ATOM   6495  C  CA    . ASN A 1 2271 ? 198.115 203.291 205.035 1.00 15.08 ? 2271 ASN A CA    1 
ATOM   6496  C  C     . ASN A 1 2271 ? 197.194 203.909 203.992 1.00 15.35 ? 2271 ASN A C     1 
ATOM   6497  O  O     . ASN A 1 2271 ? 195.972 203.887 204.160 1.00 20.30 ? 2271 ASN A O     1 
ATOM   6498  C  CB    . ASN A 1 2271 ? 198.965 204.376 205.708 1.00 18.90 ? 2271 ASN A CB    1 
ATOM   6499  C  CG    . ASN A 1 2271 ? 200.084 203.799 206.549 1.00 20.87 ? 2271 ASN A CG    1 
ATOM   6500  O  OD1   . ASN A 1 2271 ? 199.840 203.048 207.495 1.00 27.50 ? 2271 ASN A OD1   1 
ATOM   6501  N  ND2   . ASN A 1 2271 ? 201.318 204.144 206.209 1.00 16.21 ? 2271 ASN A ND2   1 
ATOM   6502  N  N     . THR A 1 2272 ? 197.745 204.457 202.906 1.00 12.52 ? 2272 THR A N     1 
ATOM   6503  C  CA    . THR A 1 2272 ? 196.899 205.067 201.887 1.00 10.79 ? 2272 THR A CA    1 
ATOM   6504  C  C     . THR A 1 2272 ? 196.204 204.025 201.022 1.00 8.23  ? 2272 THR A C     1 
ATOM   6505  O  O     . THR A 1 2272 ? 195.281 204.372 200.280 1.00 12.41 ? 2272 THR A O     1 
ATOM   6506  C  CB    . THR A 1 2272 ? 197.715 206.011 201.001 1.00 16.85 ? 2272 THR A CB    1 
ATOM   6507  O  OG1   . THR A 1 2272 ? 198.734 205.276 200.316 1.00 20.55 ? 2272 THR A OG1   1 
ATOM   6508  C  CG2   . THR A 1 2272 ? 198.372 207.093 201.845 1.00 20.17 ? 2272 THR A CG2   1 
ATOM   6509  N  N     . ARG A 1 2273 ? 196.628 202.762 201.108 1.00 11.14 ? 2273 ARG A N     1 
ATOM   6510  C  CA    . ARG A 1 2273 ? 196.071 201.662 200.317 1.00 9.47  ? 2273 ARG A CA    1 
ATOM   6511  C  C     . ARG A 1 2273 ? 196.200 201.921 198.818 1.00 11.07 ? 2273 ARG A C     1 
ATOM   6512  O  O     . ARG A 1 2273 ? 195.376 201.468 198.023 1.00 11.71 ? 2273 ARG A O     1 
ATOM   6513  C  CB    . ARG A 1 2273 ? 194.612 201.378 200.691 1.00 10.71 ? 2273 ARG A CB    1 
ATOM   6514  C  CG    . ARG A 1 2273 ? 194.331 201.446 202.186 1.00 12.43 ? 2273 ARG A CG    1 
ATOM   6515  C  CD    . ARG A 1 2273 ? 195.114 200.402 202.963 1.00 10.91 ? 2273 ARG A CD    1 
ATOM   6516  N  NE    . ARG A 1 2273 ? 194.942 199.058 202.430 1.00 9.57  ? 2273 ARG A NE    1 
ATOM   6517  C  CZ    . ARG A 1 2273 ? 195.769 198.049 202.667 1.00 8.03  ? 2273 ARG A CZ    1 
ATOM   6518  N  NH1   . ARG A 1 2273 ? 196.845 198.202 203.421 1.00 9.25  ? 2273 ARG A NH1   1 
ATOM   6519  N  NH2   . ARG A 1 2273 ? 195.511 196.858 202.134 1.00 5.73  ? 2273 ARG A NH2   1 
ATOM   6520  N  N     . GLU A 1 2274 ? 197.239 202.654 198.429 1.00 11.61 ? 2274 GLU A N     1 
ATOM   6521  C  CA    . GLU A 1 2274 ? 197.521 202.926 197.028 1.00 9.80  ? 2274 GLU A CA    1 
ATOM   6522  C  C     . GLU A 1 2274 ? 198.370 201.803 196.451 1.00 7.42  ? 2274 GLU A C     1 
ATOM   6523  O  O     . GLU A 1 2274 ? 199.296 201.311 197.101 1.00 6.47  ? 2274 GLU A O     1 
ATOM   6524  C  CB    . GLU A 1 2274 ? 198.244 204.264 196.879 1.00 11.19 ? 2274 GLU A CB    1 
ATOM   6525  C  CG    . GLU A 1 2274 ? 198.548 204.663 195.446 1.00 12.76 ? 2274 GLU A CG    1 
ATOM   6526  C  CD    . GLU A 1 2274 ? 197.296 204.917 194.627 1.00 21.38 ? 2274 GLU A CD    1 
ATOM   6527  O  OE1   . GLU A 1 2274 ? 196.254 205.265 195.222 1.00 27.20 ? 2274 GLU A OE1   1 
ATOM   6528  O  OE2   . GLU A 1 2274 ? 197.357 204.770 193.389 1.00 21.89 ? 2274 GLU A OE2   1 
ATOM   6529  N  N     . TRP A 1 2275 ? 198.050 201.395 195.227 1.00 4.40  ? 2275 TRP A N     1 
ATOM   6530  C  CA    . TRP A 1 2275 ? 198.770 200.312 194.576 1.00 2.13  ? 2275 TRP A CA    1 
ATOM   6531  C  C     . TRP A 1 2275 ? 199.852 200.865 193.658 1.00 2.66  ? 2275 TRP A C     1 
ATOM   6532  O  O     . TRP A 1 2275 ? 199.585 201.731 192.820 1.00 6.86  ? 2275 TRP A O     1 
ATOM   6533  C  CB    . TRP A 1 2275 ? 197.822 199.418 193.778 1.00 1.50  ? 2275 TRP A CB    1 
ATOM   6534  C  CG    . TRP A 1 2275 ? 198.560 198.396 192.980 1.00 0.90  ? 2275 TRP A CG    1 
ATOM   6535  C  CD1   . TRP A 1 2275 ? 198.814 198.425 191.643 1.00 0.41  ? 2275 TRP A CD1   1 
ATOM   6536  C  CD2   . TRP A 1 2275 ? 199.181 197.207 193.480 1.00 0.39  ? 2275 TRP A CD2   1 
ATOM   6537  N  NE1   . TRP A 1 2275 ? 199.540 197.320 191.276 1.00 0.32  ? 2275 TRP A NE1   1 
ATOM   6538  C  CE2   . TRP A 1 2275 ? 199.779 196.556 192.385 1.00 0.23  ? 2275 TRP A CE2   1 
ATOM   6539  C  CE3   . TRP A 1 2275 ? 199.286 196.627 194.748 1.00 0.45  ? 2275 TRP A CE3   1 
ATOM   6540  C  CZ2   . TRP A 1 2275 ? 200.466 195.354 192.518 1.00 0.17  ? 2275 TRP A CZ2   1 
ATOM   6541  C  CZ3   . TRP A 1 2275 ? 199.969 195.433 194.877 1.00 0.71  ? 2275 TRP A CZ3   1 
ATOM   6542  C  CH2   . TRP A 1 2275 ? 200.550 194.809 193.768 1.00 0.40  ? 2275 TRP A CH2   1 
ATOM   6543  N  N     . THR A 1 2276 ? 201.068 200.360 193.825 1.00 0.80  ? 2276 THR A N     1 
ATOM   6544  C  CA    . THR A 1 2276 ? 202.183 200.658 192.938 1.00 0.93  ? 2276 THR A CA    1 
ATOM   6545  C  C     . THR A 1 2276 ? 202.526 199.397 192.159 1.00 0.53  ? 2276 THR A C     1 
ATOM   6546  O  O     . THR A 1 2276 ? 202.685 198.326 192.752 1.00 0.46  ? 2276 THR A O     1 
ATOM   6547  C  CB    . THR A 1 2276 ? 203.405 201.147 193.720 1.00 1.11  ? 2276 THR A CB    1 
ATOM   6548  O  OG1   . THR A 1 2276 ? 203.098 202.387 194.367 1.00 6.66  ? 2276 THR A OG1   1 
ATOM   6549  C  CG2   . THR A 1 2276 ? 204.588 201.349 192.789 1.00 0.48  ? 2276 THR A CG2   1 
ATOM   6550  N  N     . ASP A 1 2277 ? 202.623 199.520 190.840 1.00 0.39  ? 2277 ASP A N     1 
ATOM   6551  C  CA    . ASP A 1 2277 ? 202.942 198.368 190.008 1.00 0.20  ? 2277 ASP A CA    1 
ATOM   6552  C  C     . ASP A 1 2277 ? 204.396 197.955 190.185 1.00 0.43  ? 2277 ASP A C     1 
ATOM   6553  O  O     . ASP A 1 2277 ? 205.289 198.794 190.327 1.00 0.20  ? 2277 ASP A O     1 
ATOM   6554  C  CB    . ASP A 1 2277 ? 202.671 198.677 188.536 1.00 0.15  ? 2277 ASP A CB    1 
ATOM   6555  C  CG    . ASP A 1 2277 ? 201.258 198.341 188.121 1.00 0.35  ? 2277 ASP A CG    1 
ATOM   6556  O  OD1   . ASP A 1 2277 ? 200.490 197.838 188.965 1.00 6.03  ? 2277 ASP A OD1   1 
ATOM   6557  O  OD2   . ASP A 1 2277 ? 200.913 198.578 186.947 1.00 0.78  ? 2277 ASP A OD2   1 
ATOM   6558  N  N     . GLY A 1 2278 ? 204.628 196.646 190.178 1.00 2.24  ? 2278 GLY A N     1 
ATOM   6559  C  CA    . GLY A 1 2278 ? 205.965 196.105 190.102 1.00 0.06  ? 2278 GLY A CA    1 
ATOM   6560  C  C     . GLY A 1 2278 ? 206.442 196.033 188.668 1.00 0.03  ? 2278 GLY A C     1 
ATOM   6561  O  O     . GLY A 1 2278 ? 205.800 196.516 187.737 1.00 0.04  ? 2278 GLY A O     1 
ATOM   6562  N  N     . LEU A 1 2279 ? 207.603 195.403 188.493 1.00 0.04  ? 2279 LEU A N     1 
ATOM   6563  C  CA    . LEU A 1 2279 ? 208.218 195.339 187.169 1.00 0.03  ? 2279 LEU A CA    1 
ATOM   6564  C  C     . LEU A 1 2279 ? 207.379 194.511 186.203 1.00 0.01  ? 2279 LEU A C     1 
ATOM   6565  O  O     . LEU A 1 2279 ? 207.071 194.961 185.095 1.00 0.03  ? 2279 LEU A O     1 
ATOM   6566  C  CB    . LEU A 1 2279 ? 209.634 194.778 187.282 1.00 0.04  ? 2279 LEU A CB    1 
ATOM   6567  C  CG    . LEU A 1 2279 ? 210.393 194.539 185.977 1.00 0.02  ? 2279 LEU A CG    1 
ATOM   6568  C  CD1   . LEU A 1 2279 ? 210.433 195.798 185.129 1.00 0.03  ? 2279 LEU A CD1   1 
ATOM   6569  C  CD2   . LEU A 1 2279 ? 211.793 194.050 186.280 1.00 0.04  ? 2279 LEU A CD2   1 
ATOM   6570  N  N     . PHE A 1 2280 ? 206.994 193.298 186.606 1.00 0.02  ? 2280 PHE A N     1 
ATOM   6571  C  CA    . PHE A 1 2280 ? 206.207 192.451 185.714 1.00 0.05  ? 2280 PHE A CA    1 
ATOM   6572  C  C     . PHE A 1 2280 ? 204.803 193.007 185.514 1.00 0.15  ? 2280 PHE A C     1 
ATOM   6573  O  O     . PHE A 1 2280 ? 204.271 192.975 184.400 1.00 0.05  ? 2280 PHE A O     1 
ATOM   6574  C  CB    . PHE A 1 2280 ? 206.145 191.023 186.254 1.00 0.02  ? 2280 PHE A CB    1 
ATOM   6575  C  CG    . PHE A 1 2280 ? 205.157 190.151 185.537 1.00 0.05  ? 2280 PHE A CG    1 
ATOM   6576  C  CD1   . PHE A 1 2280 ? 205.426 189.682 184.262 1.00 0.02  ? 2280 PHE A CD1   1 
ATOM   6577  C  CD2   . PHE A 1 2280 ? 203.957 189.806 186.133 1.00 0.01  ? 2280 PHE A CD2   1 
ATOM   6578  C  CE1   . PHE A 1 2280 ? 204.520 188.881 183.598 1.00 0.02  ? 2280 PHE A CE1   1 
ATOM   6579  C  CE2   . PHE A 1 2280 ? 203.047 189.007 185.473 1.00 0.04  ? 2280 PHE A CE2   1 
ATOM   6580  C  CZ    . PHE A 1 2280 ? 203.328 188.543 184.204 1.00 0.26  ? 2280 PHE A CZ    1 
ATOM   6581  N  N     . THR A 1 2281 ? 204.188 193.517 186.583 1.00 0.05  ? 2281 THR A N     1 
ATOM   6582  C  CA    . THR A 1 2281 ? 202.841 194.067 186.470 1.00 0.05  ? 2281 THR A CA    1 
ATOM   6583  C  C     . THR A 1 2281 ? 202.815 195.277 185.548 1.00 0.04  ? 2281 THR A C     1 
ATOM   6584  O  O     . THR A 1 2281 ? 201.875 195.451 184.768 1.00 0.05  ? 2281 THR A O     1 
ATOM   6585  C  CB    . THR A 1 2281 ? 202.306 194.434 187.855 1.00 0.10  ? 2281 THR A CB    1 
ATOM   6586  O  OG1   . THR A 1 2281 ? 202.594 193.373 188.774 1.00 0.14  ? 2281 THR A OG1   1 
ATOM   6587  C  CG2   . THR A 1 2281 ? 200.808 194.661 187.805 1.00 0.06  ? 2281 THR A CG2   1 
ATOM   6588  N  N     . HIS A 1 2282 ? 203.843 196.126 185.626 1.00 0.05  ? 2282 HIS A N     1 
ATOM   6589  C  CA    . HIS A 1 2282 ? 203.908 197.298 184.761 1.00 0.05  ? 2282 HIS A CA    1 
ATOM   6590  C  C     . HIS A 1 2282 ? 204.040 196.900 183.295 1.00 0.04  ? 2282 HIS A C     1 
ATOM   6591  O  O     . HIS A 1 2282 ? 203.390 197.490 182.425 1.00 0.09  ? 2282 HIS A O     1 
ATOM   6592  C  CB    . HIS A 1 2282 ? 205.071 198.193 185.188 1.00 0.08  ? 2282 HIS A CB    1 
ATOM   6593  C  CG    . HIS A 1 2282 ? 205.476 199.203 184.160 1.00 0.24  ? 2282 HIS A CG    1 
ATOM   6594  N  ND1   . HIS A 1 2282 ? 206.499 198.983 183.264 1.00 0.41  ? 2282 HIS A ND1   1 
ATOM   6595  C  CD2   . HIS A 1 2282 ? 204.999 200.440 183.891 1.00 0.16  ? 2282 HIS A CD2   1 
ATOM   6596  C  CE1   . HIS A 1 2282 ? 206.632 200.040 182.484 1.00 2.18  ? 2282 HIS A CE1   1 
ATOM   6597  N  NE2   . HIS A 1 2282 ? 205.733 200.939 182.843 1.00 1.40  ? 2282 HIS A NE2   1 
ATOM   6598  N  N     . VAL A 1 2283 ? 204.880 195.905 183.003 1.00 0.03  ? 2283 VAL A N     1 
ATOM   6599  C  CA    . VAL A 1 2283 ? 205.085 195.480 181.619 1.00 0.04  ? 2283 VAL A CA    1 
ATOM   6600  C  C     . VAL A 1 2283 ? 203.799 194.898 181.045 1.00 0.07  ? 2283 VAL A C     1 
ATOM   6601  O  O     . VAL A 1 2283 ? 203.383 195.241 179.932 1.00 0.11  ? 2283 VAL A O     1 
ATOM   6602  C  CB    . VAL A 1 2283 ? 206.246 194.472 181.535 1.00 0.06  ? 2283 VAL A CB    1 
ATOM   6603  C  CG1   . VAL A 1 2283 ? 206.292 193.817 180.162 1.00 0.05  ? 2283 VAL A CG1   1 
ATOM   6604  C  CG2   . VAL A 1 2283 ? 207.565 195.157 181.842 1.00 0.05  ? 2283 VAL A CG2   1 
ATOM   6605  N  N     . LEU A 1 2284 ? 203.147 194.014 181.801 1.00 0.06  ? 2284 LEU A N     1 
ATOM   6606  C  CA    . LEU A 1 2284 ? 201.920 193.388 181.324 1.00 0.08  ? 2284 LEU A CA    1 
ATOM   6607  C  C     . LEU A 1 2284 ? 200.798 194.406 181.178 1.00 0.10  ? 2284 LEU A C     1 
ATOM   6608  O  O     . LEU A 1 2284 ? 200.019 194.345 180.220 1.00 0.38  ? 2284 LEU A O     1 
ATOM   6609  C  CB    . LEU A 1 2284 ? 201.513 192.255 182.264 1.00 0.10  ? 2284 LEU A CB    1 
ATOM   6610  C  CG    . LEU A 1 2284 ? 200.137 191.616 182.068 1.00 0.10  ? 2284 LEU A CG    1 
ATOM   6611  C  CD1   . LEU A 1 2284 ? 200.017 190.994 180.686 1.00 1.57  ? 2284 LEU A CD1   1 
ATOM   6612  C  CD2   . LEU A 1 2284 ? 199.885 190.583 183.144 1.00 0.28  ? 2284 LEU A CD2   1 
ATOM   6613  N  N     . ARG A 1 2285 ? 200.698 195.354 182.114 1.00 0.08  ? 2285 ARG A N     1 
ATOM   6614  C  CA    . ARG A 1 2285 ? 199.667 196.380 182.019 1.00 0.20  ? 2285 ARG A CA    1 
ATOM   6615  C  C     . ARG A 1 2285 ? 199.898 197.299 180.826 1.00 0.50  ? 2285 ARG A C     1 
ATOM   6616  O  O     . ARG A 1 2285 ? 198.936 197.763 180.206 1.00 0.59  ? 2285 ARG A O     1 
ATOM   6617  C  CB    . ARG A 1 2285 ? 199.612 197.192 183.312 1.00 0.17  ? 2285 ARG A CB    1 
ATOM   6618  C  CG    . ARG A 1 2285 ? 198.404 198.101 183.421 1.00 0.40  ? 2285 ARG A CG    1 
ATOM   6619  C  CD    . ARG A 1 2285 ? 198.562 199.084 184.564 1.00 0.40  ? 2285 ARG A CD    1 
ATOM   6620  N  NE    . ARG A 1 2285 ? 198.630 198.415 185.858 1.00 0.35  ? 2285 ARG A NE    1 
ATOM   6621  C  CZ    . ARG A 1 2285 ? 197.591 197.889 186.492 1.00 0.50  ? 2285 ARG A CZ    1 
ATOM   6622  N  NH1   . ARG A 1 2285 ? 196.373 197.940 185.983 1.00 0.57  ? 2285 ARG A NH1   1 
ATOM   6623  N  NH2   . ARG A 1 2285 ? 197.780 197.299 187.667 1.00 0.64  ? 2285 ARG A NH2   1 
ATOM   6624  N  N     . LYS A 1 2286 ? 201.161 197.574 180.494 1.00 0.39  ? 2286 LYS A N     1 
ATOM   6625  C  CA    . LYS A 1 2286 ? 201.465 198.384 179.319 1.00 0.48  ? 2286 LYS A CA    1 
ATOM   6626  C  C     . LYS A 1 2286 ? 201.005 197.691 178.040 1.00 0.42  ? 2286 LYS A C     1 
ATOM   6627  O  O     . LYS A 1 2286 ? 200.525 198.347 177.110 1.00 0.86  ? 2286 LYS A O     1 
ATOM   6628  C  CB    . LYS A 1 2286 ? 202.963 198.679 179.268 1.00 1.01  ? 2286 LYS A CB    1 
ATOM   6629  C  CG    . LYS A 1 2286 ? 203.325 199.986 178.588 1.00 1.49  ? 2286 LYS A CG    1 
ATOM   6630  C  CD    . LYS A 1 2286 ? 204.820 200.073 178.342 1.00 2.54  ? 2286 LYS A CD    1 
ATOM   6631  C  CE    . LYS A 1 2286 ? 205.273 201.510 178.158 1.00 5.81  ? 2286 LYS A CE    1 
ATOM   6632  N  NZ    . LYS A 1 2286 ? 204.232 202.351 177.508 1.00 12.57 ? 2286 LYS A NZ    1 
ATOM   6633  N  N     . ILE A 1 2287 ? 201.148 196.366 177.976 1.00 0.32  ? 2287 ILE A N     1 
ATOM   6634  C  CA    . ILE A 1 2287 ? 200.714 195.621 176.796 1.00 0.53  ? 2287 ILE A CA    1 
ATOM   6635  C  C     . ILE A 1 2287 ? 199.192 195.595 176.702 1.00 0.73  ? 2287 ILE A C     1 
ATOM   6636  O  O     . ILE A 1 2287 ? 198.625 195.733 175.613 1.00 2.52  ? 2287 ILE A O     1 
ATOM   6637  C  CB    . ILE A 1 2287 ? 201.310 194.203 176.815 1.00 0.39  ? 2287 ILE A CB    1 
ATOM   6638  C  CG1   . ILE A 1 2287 ? 202.838 194.268 176.801 1.00 0.29  ? 2287 ILE A CG1   1 
ATOM   6639  C  CG2   . ILE A 1 2287 ? 200.796 193.386 175.642 1.00 0.34  ? 2287 ILE A CG2   1 
ATOM   6640  C  CD1   . ILE A 1 2287 ? 203.511 192.958 177.126 1.00 0.09  ? 2287 ILE A CD1   1 
ATOM   6641  N  N     . ILE A 1 2288 ? 198.509 195.412 177.833 1.00 0.55  ? 2288 ILE A N     1 
ATOM   6642  C  CA    . ILE A 1 2288 ? 197.049 195.376 177.828 1.00 0.67  ? 2288 ILE A CA    1 
ATOM   6643  C  C     . ILE A 1 2288 ? 196.475 196.731 177.429 1.00 0.95  ? 2288 ILE A C     1 
ATOM   6644  O  O     . ILE A 1 2288 ? 195.521 196.810 176.649 1.00 1.45  ? 2288 ILE A O     1 
ATOM   6645  C  CB    . ILE A 1 2288 ? 196.522 194.918 179.200 1.00 0.84  ? 2288 ILE A CB    1 
ATOM   6646  C  CG1   . ILE A 1 2288 ? 197.001 193.501 179.514 1.00 0.45  ? 2288 ILE A CG1   1 
ATOM   6647  C  CG2   . ILE A 1 2288 ? 195.004 194.998 179.251 1.00 0.52  ? 2288 ILE A CG2   1 
ATOM   6648  C  CD1   . ILE A 1 2288 ? 196.892 193.131 180.975 1.00 0.27  ? 2288 ILE A CD1   1 
ATOM   6649  N  N     . ASP A 1 2289 ? 197.043 197.817 177.963 1.00 1.46  ? 2289 ASP A N     1 
ATOM   6650  C  CA    . ASP A 1 2289 ? 196.540 199.151 177.646 1.00 1.45  ? 2289 ASP A CA    1 
ATOM   6651  C  C     . ASP A 1 2289 ? 196.717 199.473 176.169 1.00 3.91  ? 2289 ASP A C     1 
ATOM   6652  O  O     . ASP A 1 2289 ? 195.856 200.123 175.564 1.00 6.57  ? 2289 ASP A O     1 
ATOM   6653  C  CB    . ASP A 1 2289 ? 197.236 200.192 178.519 1.00 2.88  ? 2289 ASP A CB    1 
ATOM   6654  C  CG    . ASP A 1 2289 ? 196.815 200.103 179.973 1.00 17.56 ? 2289 ASP A CG    1 
ATOM   6655  O  OD1   . ASP A 1 2289 ? 197.606 200.507 180.851 1.00 12.95 ? 2289 ASP A OD1   1 
ATOM   6656  O  OD2   . ASP A 1 2289 ? 195.691 199.628 180.240 1.00 20.02 ? 2289 ASP A OD2   1 
ATOM   6657  N  N     . SER A 1 2290 ? 197.825 199.030 175.578 1.00 2.59  ? 2290 SER A N     1 
ATOM   6658  C  CA    . SER A 1 2290 ? 198.066 199.121 174.138 1.00 2.23  ? 2290 SER A CA    1 
ATOM   6659  C  C     . SER A 1 2290 ? 197.981 200.565 173.644 1.00 3.05  ? 2290 SER A C     1 
ATOM   6660  O  O     . SER A 1 2290 ? 197.346 200.868 172.631 1.00 3.00  ? 2290 SER A O     1 
ATOM   6661  C  CB    . SER A 1 2290 ? 197.105 198.220 173.365 1.00 2.88  ? 2290 SER A CB    1 
ATOM   6662  O  OG    . SER A 1 2290 ? 197.526 198.064 172.022 1.00 5.46  ? 2290 SER A OG    1 
ATOM   6663  N  N     . VAL A 1 2291 ? 198.639 201.464 174.377 1.00 3.64  ? 2291 VAL A N     1 
ATOM   6664  C  CA    . VAL A 1 2291 ? 198.704 202.857 173.960 1.00 3.01  ? 2291 VAL A CA    1 
ATOM   6665  C  C     . VAL A 1 2291 ? 199.507 203.014 172.676 1.00 3.47  ? 2291 VAL A C     1 
ATOM   6666  O  O     . VAL A 1 2291 ? 199.158 203.840 171.825 1.00 5.28  ? 2291 VAL A O     1 
ATOM   6667  C  CB    . VAL A 1 2291 ? 199.280 203.714 175.104 1.00 3.34  ? 2291 VAL A CB    1 
ATOM   6668  C  CG1   . VAL A 1 2291 ? 199.689 205.093 174.608 1.00 1.94  ? 2291 VAL A CG1   1 
ATOM   6669  C  CG2   . VAL A 1 2291 ? 198.269 203.824 176.238 1.00 2.58  ? 2291 VAL A CG2   1 
ATOM   6670  N  N     . ARG A 1 2292 ? 200.561 202.222 172.498 1.00 2.56  ? 2292 ARG A N     1 
ATOM   6671  C  CA    . ARG A 1 2292 ? 201.448 202.319 171.345 1.00 4.01  ? 2292 ARG A CA    1 
ATOM   6672  C  C     . ARG A 1 2292 ? 201.423 201.039 170.518 1.00 5.07  ? 2292 ARG A C     1 
ATOM   6673  O  O     . ARG A 1 2292 ? 202.441 200.609 169.971 1.00 7.52  ? 2292 ARG A O     1 
ATOM   6674  C  CB    . ARG A 1 2292 ? 202.868 202.651 171.796 1.00 3.30  ? 2292 ARG A CB    1 
ATOM   6675  C  CG    . ARG A 1 2292 ? 202.945 203.938 172.587 1.00 2.55  ? 2292 ARG A CG    1 
ATOM   6676  C  CD    . ARG A 1 2292 ? 204.323 204.169 173.177 1.00 2.75  ? 2292 ARG A CD    1 
ATOM   6677  N  NE    . ARG A 1 2292 ? 204.387 205.403 173.955 1.00 5.24  ? 2292 ARG A NE    1 
ATOM   6678  C  CZ    . ARG A 1 2292 ? 203.692 205.643 175.060 1.00 5.20  ? 2292 ARG A CZ    1 
ATOM   6679  N  NH1   . ARG A 1 2292 ? 202.912 204.723 175.604 1.00 8.30  ? 2292 ARG A NH1   1 
ATOM   6680  N  NH2   . ARG A 1 2292 ? 203.794 206.834 175.644 1.00 3.33  ? 2292 ARG A NH2   1 
ATOM   6681  N  N     . GLY A 1 2293 ? 200.253 200.417 170.414 1.00 3.89  ? 2293 GLY A N     1 
ATOM   6682  C  CA    . GLY A 1 2293 ? 200.077 199.243 169.574 1.00 2.52  ? 2293 GLY A CA    1 
ATOM   6683  C  C     . GLY A 1 2293 ? 200.825 198.002 170.017 1.00 4.79  ? 2293 GLY A C     1 
ATOM   6684  O  O     . GLY A 1 2293 ? 201.345 197.266 169.171 1.00 7.38  ? 2293 GLY A O     1 
ATOM   6685  N  N     . GLU A 1 2294 ? 200.882 197.745 171.325 1.00 3.29  ? 2294 GLU A N     1 
ATOM   6686  C  CA    . GLU A 1 2294 ? 201.535 196.539 171.822 1.00 2.48  ? 2294 GLU A CA    1 
ATOM   6687  C  C     . GLU A 1 2294 ? 200.716 195.277 171.584 1.00 3.28  ? 2294 GLU A C     1 
ATOM   6688  O  O     . GLU A 1 2294 ? 201.289 194.183 171.581 1.00 5.36  ? 2294 GLU A O     1 
ATOM   6689  C  CB    . GLU A 1 2294 ? 201.860 196.680 173.315 1.00 1.89  ? 2294 GLU A CB    1 
ATOM   6690  C  CG    . GLU A 1 2294 ? 202.752 197.866 173.709 1.00 1.35  ? 2294 GLU A CG    1 
ATOM   6691  C  CD    . GLU A 1 2294 ? 202.092 199.230 173.595 1.00 4.52  ? 2294 GLU A CD    1 
ATOM   6692  O  OE1   . GLU A 1 2294 ? 200.944 199.317 173.124 1.00 6.64  ? 2294 GLU A OE1   1 
ATOM   6693  O  OE2   . GLU A 1 2294 ? 202.736 200.224 173.984 1.00 10.17 ? 2294 GLU A OE2   1 
ATOM   6694  N  N     . LEU A 1 2295 ? 199.404 195.391 171.375 1.00 2.67  ? 2295 LEU A N     1 
ATOM   6695  C  CA    . LEU A 1 2295 ? 198.588 194.206 171.134 1.00 1.91  ? 2295 LEU A CA    1 
ATOM   6696  C  C     . LEU A 1 2295 ? 198.725 193.657 169.722 1.00 2.32  ? 2295 LEU A C     1 
ATOM   6697  O  O     . LEU A 1 2295 ? 198.280 192.533 169.470 1.00 4.56  ? 2295 LEU A O     1 
ATOM   6698  C  CB    . LEU A 1 2295 ? 197.114 194.497 171.419 1.00 2.02  ? 2295 LEU A CB    1 
ATOM   6699  C  CG    . LEU A 1 2295 ? 196.727 194.727 172.878 1.00 1.70  ? 2295 LEU A CG    1 
ATOM   6700  C  CD1   . LEU A 1 2295 ? 195.261 195.116 172.988 1.00 0.97  ? 2295 LEU A CD1   1 
ATOM   6701  C  CD2   . LEU A 1 2295 ? 197.027 193.495 173.710 1.00 0.77  ? 2295 LEU A CD2   1 
ATOM   6702  N  N     . GLN A 1 2296 ? 199.316 194.413 168.800 1.00 3.88  ? 2296 GLN A N     1 
ATOM   6703  C  CA    . GLN A 1 2296 ? 199.532 193.947 167.439 1.00 3.13  ? 2296 GLN A CA    1 
ATOM   6704  C  C     . GLN A 1 2296 ? 200.914 193.343 167.243 1.00 3.15  ? 2296 GLN A C     1 
ATOM   6705  O  O     . GLN A 1 2296 ? 201.250 192.945 166.124 1.00 6.55  ? 2296 GLN A O     1 
ATOM   6706  C  CB    . GLN A 1 2296 ? 199.321 195.093 166.444 1.00 3.20  ? 2296 GLN A CB    1 
ATOM   6707  C  CG    . GLN A 1 2296 ? 198.186 196.042 166.799 1.00 3.53  ? 2296 GLN A CG    1 
ATOM   6708  C  CD    . GLN A 1 2296 ? 196.907 195.325 167.179 1.00 6.03  ? 2296 GLN A CD    1 
ATOM   6709  O  OE1   . GLN A 1 2296 ? 196.372 195.522 168.269 1.00 3.37  ? 2296 GLN A OE1   1 
ATOM   6710  N  NE2   . GLN A 1 2296 ? 196.411 194.483 166.281 1.00 9.85  ? 2296 GLN A NE2   1 
ATOM   6711  N  N     . LYS A 1 2297 ? 201.714 193.260 168.299 1.00 4.38  ? 2297 LYS A N     1 
ATOM   6712  C  CA    . LYS A 1 2297 ? 203.063 192.729 168.234 1.00 2.36  ? 2297 LYS A CA    1 
ATOM   6713  C  C     . LYS A 1 2297 ? 203.149 191.442 169.042 1.00 1.22  ? 2297 LYS A C     1 
ATOM   6714  O  O     . LYS A 1 2297 ? 202.341 191.193 169.940 1.00 2.06  ? 2297 LYS A O     1 
ATOM   6715  C  CB    . LYS A 1 2297 ? 204.085 193.739 168.769 1.00 3.38  ? 2297 LYS A CB    1 
ATOM   6716  C  CG    . LYS A 1 2297 ? 204.011 195.107 168.127 1.00 7.13  ? 2297 LYS A CG    1 
ATOM   6717  C  CD    . LYS A 1 2297 ? 204.989 196.064 168.780 1.00 9.48  ? 2297 LYS A CD    1 
ATOM   6718  C  CE    . LYS A 1 2297 ? 204.830 197.474 168.241 1.00 10.26 ? 2297 LYS A CE    1 
ATOM   6719  N  NZ    . LYS A 1 2297 ? 205.815 198.406 168.849 1.00 14.54 ? 2297 LYS A NZ    1 
ATOM   6720  N  N     . ARG A 1 2298 ? 204.137 190.621 168.706 1.00 1.22  ? 2298 ARG A N     1 
ATOM   6721  C  CA    . ARG A 1 2298 ? 204.441 189.441 169.502 1.00 0.62  ? 2298 ARG A CA    1 
ATOM   6722  C  C     . ARG A 1 2298 ? 205.205 189.878 170.747 1.00 0.66  ? 2298 ARG A C     1 
ATOM   6723  O  O     . ARG A 1 2298 ? 206.307 190.429 170.646 1.00 1.08  ? 2298 ARG A O     1 
ATOM   6724  C  CB    . ARG A 1 2298 ? 205.244 188.438 168.680 1.00 0.36  ? 2298 ARG A CB    1 
ATOM   6725  C  CG    . ARG A 1 2298 ? 205.841 187.298 169.479 1.00 0.35  ? 2298 ARG A CG    1 
ATOM   6726  C  CD    . ARG A 1 2298 ? 206.393 186.217 168.567 1.00 0.52  ? 2298 ARG A CD    1 
ATOM   6727  N  NE    . ARG A 1 2298 ? 205.340 185.388 167.994 1.00 1.08  ? 2298 ARG A NE    1 
ATOM   6728  C  CZ    . ARG A 1 2298 ? 204.989 185.396 166.716 1.00 1.09  ? 2298 ARG A CZ    1 
ATOM   6729  N  NH1   . ARG A 1 2298 ? 205.581 186.191 165.841 1.00 0.65  ? 2298 ARG A NH1   1 
ATOM   6730  N  NH2   . ARG A 1 2298 ? 204.016 184.589 166.306 1.00 1.18  ? 2298 ARG A NH2   1 
ATOM   6731  N  N     . GLN A 1 2299 ? 204.615 189.651 171.917 1.00 0.40  ? 2299 GLN A N     1 
ATOM   6732  C  CA    . GLN A 1 2299 ? 205.170 190.112 173.186 1.00 0.17  ? 2299 GLN A CA    1 
ATOM   6733  C  C     . GLN A 1 2299 ? 205.622 188.903 173.992 1.00 0.05  ? 2299 GLN A C     1 
ATOM   6734  O  O     . GLN A 1 2299 ? 204.798 188.088 174.416 1.00 0.16  ? 2299 GLN A O     1 
ATOM   6735  C  CB    . GLN A 1 2299 ? 204.142 190.933 173.958 1.00 0.21  ? 2299 GLN A CB    1 
ATOM   6736  C  CG    . GLN A 1 2299 ? 203.677 192.181 173.234 1.00 0.28  ? 2299 GLN A CG    1 
ATOM   6737  C  CD    . GLN A 1 2299 ? 204.654 193.329 173.357 1.00 0.50  ? 2299 GLN A CD    1 
ATOM   6738  O  OE1   . GLN A 1 2299 ? 205.696 193.206 173.998 1.00 0.47  ? 2299 GLN A OE1   1 
ATOM   6739  N  NE2   . GLN A 1 2299 ? 204.326 194.452 172.739 1.00 3.23  ? 2299 GLN A NE2   1 
ATOM   6740  N  N     . TRP A 1 2300 ? 206.927 188.792 174.210 1.00 0.04  ? 2300 TRP A N     1 
ATOM   6741  C  CA    . TRP A 1 2300 ? 207.501 187.709 174.997 1.00 0.03  ? 2300 TRP A CA    1 
ATOM   6742  C  C     . TRP A 1 2300 ? 208.083 188.288 176.279 1.00 0.03  ? 2300 TRP A C     1 
ATOM   6743  O  O     . TRP A 1 2300 ? 208.941 189.173 176.232 1.00 0.04  ? 2300 TRP A O     1 
ATOM   6744  C  CB    . TRP A 1 2300 ? 208.573 186.960 174.206 1.00 0.05  ? 2300 TRP A CB    1 
ATOM   6745  C  CG    . TRP A 1 2300 ? 208.013 186.070 173.136 1.00 0.04  ? 2300 TRP A CG    1 
ATOM   6746  C  CD1   . TRP A 1 2300 ? 206.702 185.918 172.803 1.00 0.03  ? 2300 TRP A CD1   1 
ATOM   6747  C  CD2   . TRP A 1 2300 ? 208.750 185.208 172.266 1.00 0.05  ? 2300 TRP A CD2   1 
ATOM   6748  N  NE1   . TRP A 1 2300 ? 206.576 185.017 171.780 1.00 0.05  ? 2300 TRP A NE1   1 
ATOM   6749  C  CE2   . TRP A 1 2300 ? 207.819 184.565 171.430 1.00 0.07  ? 2300 TRP A CE2   1 
ATOM   6750  C  CE3   . TRP A 1 2300 ? 210.109 184.917 172.111 1.00 0.06  ? 2300 TRP A CE3   1 
ATOM   6751  C  CZ2   . TRP A 1 2300 ? 208.201 183.651 170.455 1.00 0.07  ? 2300 TRP A CZ2   1 
ATOM   6752  C  CZ3   . TRP A 1 2300 ? 210.484 184.010 171.145 1.00 0.09  ? 2300 TRP A CZ3   1 
ATOM   6753  C  CH2   . TRP A 1 2300 ? 209.534 183.387 170.327 1.00 0.14  ? 2300 TRP A CH2   1 
ATOM   6754  N  N     . ILE A 1 2301 ? 207.613 187.791 177.416 1.00 0.04  ? 2301 ILE A N     1 
ATOM   6755  C  CA    . ILE A 1 2301 ? 208.139 188.174 178.719 1.00 0.05  ? 2301 ILE A CA    1 
ATOM   6756  C  C     . ILE A 1 2301 ? 208.988 187.015 179.216 1.00 0.06  ? 2301 ILE A C     1 
ATOM   6757  O  O     . ILE A 1 2301 ? 208.464 185.968 179.612 1.00 0.05  ? 2301 ILE A O     1 
ATOM   6758  C  CB    . ILE A 1 2301 ? 207.016 188.527 179.703 1.00 0.02  ? 2301 ILE A CB    1 
ATOM   6759  C  CG1   . ILE A 1 2301 ? 206.147 189.645 179.125 1.00 0.08  ? 2301 ILE A CG1   1 
ATOM   6760  C  CG2   . ILE A 1 2301 ? 207.598 188.935 181.047 1.00 0.02  ? 2301 ILE A CG2   1 
ATOM   6761  C  CD1   . ILE A 1 2301 ? 204.908 189.940 179.924 1.00 0.02  ? 2301 ILE A CD1   1 
ATOM   6762  N  N     . VAL A 1 2302 ? 210.301 187.195 179.194 1.00 0.04  ? 2302 VAL A N     1 
ATOM   6763  C  CA    . VAL A 1 2302 ? 211.246 186.136 179.510 1.00 0.03  ? 2302 VAL A CA    1 
ATOM   6764  C  C     . VAL A 1 2302 ? 211.765 186.361 180.922 1.00 0.06  ? 2302 VAL A C     1 
ATOM   6765  O  O     . VAL A 1 2302 ? 212.440 187.358 181.194 1.00 0.04  ? 2302 VAL A O     1 
ATOM   6766  C  CB    . VAL A 1 2302 ? 212.400 186.097 178.495 1.00 0.04  ? 2302 VAL A CB    1 
ATOM   6767  C  CG1   . VAL A 1 2302 ? 213.308 184.906 178.763 1.00 0.03  ? 2302 VAL A CG1   1 
ATOM   6768  C  CG2   . VAL A 1 2302 ? 211.854 186.056 177.076 1.00 0.03  ? 2302 VAL A CG2   1 
ATOM   6769  N  N     . PHE A 1 2303 ? 211.438 185.424 181.811 1.00 0.05  ? 2303 PHE A N     1 
ATOM   6770  C  CA    . PHE A 1 2303 ? 211.992 185.483 183.188 1.00 0.03  ? 2303 PHE A CA    1 
ATOM   6771  C  C     . PHE A 1 2303 ? 213.315 184.722 183.165 1.00 0.03  ? 2303 PHE A C     1 
ATOM   6772  O  O     . PHE A 1 2303 ? 213.306 183.498 183.372 1.00 0.11  ? 2303 PHE A O     1 
ATOM   6773  C  CB    . PHE A 1 2303 ? 210.996 184.930 184.211 1.00 0.03  ? 2303 PHE A CB    1 
ATOM   6774  C  CG    . PHE A 1 2303 ? 209.730 185.748 184.424 1.00 0.03  ? 2303 PHE A CG    1 
ATOM   6775  C  CD1   . PHE A 1 2303 ? 209.720 186.830 185.297 1.00 0.04  ? 2303 PHE A CD1   1 
ATOM   6776  C  CD2   . PHE A 1 2303 ? 208.546 185.412 183.780 1.00 0.02  ? 2303 PHE A CD2   1 
ATOM   6777  C  CE1   . PHE A 1 2303 ? 208.566 187.567 185.498 1.00 0.02  ? 2303 PHE A CE1   1 
ATOM   6778  C  CE2   . PHE A 1 2303 ? 207.393 186.152 183.986 1.00 0.02  ? 2303 PHE A CE2   1 
ATOM   6779  C  CZ    . PHE A 1 2303 ? 207.406 187.224 184.846 1.00 0.02  ? 2303 PHE A CZ    1 
ATOM   6780  N  N     . ASP A 1 2304 ? 214.417 185.423 182.879 1.00 0.07  ? 2304 ASP A N     1 
ATOM   6781  C  CA    . ASP A 1 2304 ? 215.764 184.790 182.843 1.00 0.12  ? 2304 ASP A CA    1 
ATOM   6782  C  C     . ASP A 1 2304 ? 216.375 184.834 184.246 1.00 0.16  ? 2304 ASP A C     1 
ATOM   6783  O  O     . ASP A 1 2304 ? 216.937 185.884 184.619 1.00 0.31  ? 2304 ASP A O     1 
ATOM   6784  C  CB    . ASP A 1 2304 ? 216.663 185.437 181.802 1.00 0.12  ? 2304 ASP A CB    1 
ATOM   6785  C  CG    . ASP A 1 2304 ? 218.006 184.759 181.575 1.00 0.13  ? 2304 ASP A CG    1 
ATOM   6786  O  OD1   . ASP A 1 2304 ? 218.251 183.713 182.209 1.00 0.18  ? 2304 ASP A OD1   1 
ATOM   6787  O  OD2   . ASP A 1 2304 ? 218.798 185.289 180.770 1.00 0.35  ? 2304 ASP A OD2   1 
ATOM   6788  N  N     . GLY A 1 2305 ? 216.275 183.731 184.984 1.00 0.11  ? 2305 GLY A N     1 
ATOM   6789  C  CA    . GLY A 1 2305 ? 216.776 183.704 186.366 1.00 0.29  ? 2305 GLY A CA    1 
ATOM   6790  C  C     . GLY A 1 2305 ? 216.300 182.476 187.109 1.00 0.45  ? 2305 GLY A C     1 
ATOM   6791  O  O     . GLY A 1 2305 ? 215.728 181.579 186.464 1.00 0.91  ? 2305 GLY A O     1 
ATOM   6792  N  N     . ASP A 1 2306 ? 216.522 182.437 188.420 1.00 0.53  ? 2306 ASP A N     1 
ATOM   6793  C  CA    . ASP A 1 2306 ? 216.161 181.288 189.236 1.00 0.66  ? 2306 ASP A CA    1 
ATOM   6794  C  C     . ASP A 1 2306 ? 214.662 181.253 189.503 1.00 0.66  ? 2306 ASP A C     1 
ATOM   6795  O  O     . ASP A 1 2306 ? 214.019 182.291 189.673 1.00 2.88  ? 2306 ASP A O     1 
ATOM   6796  C  CB    . ASP A 1 2306 ? 216.921 181.310 190.561 1.00 1.42  ? 2306 ASP A CB    1 
ATOM   6797  C  CG    . ASP A 1 2306 ? 218.407 181.113 190.379 1.00 3.42  ? 2306 ASP A CG    1 
ATOM   6798  O  OD1   . ASP A 1 2306 ? 218.813 180.602 189.314 1.00 6.30  ? 2306 ASP A OD1   1 
ATOM   6799  O  OD2   . ASP A 1 2306 ? 219.169 181.457 191.303 1.00 6.01  ? 2306 ASP A OD2   1 
ATOM   6800  N  N     . VAL A 1 2307 ? 214.112 180.045 189.547 1.00 0.51  ? 2307 VAL A N     1 
ATOM   6801  C  CA    . VAL A 1 2307 ? 212.702 179.831 189.845 1.00 0.68  ? 2307 VAL A CA    1 
ATOM   6802  C  C     . VAL A 1 2307 ? 212.589 179.290 191.263 1.00 1.14  ? 2307 VAL A C     1 
ATOM   6803  O  O     . VAL A 1 2307 ? 213.187 178.259 191.594 1.00 2.95  ? 2307 VAL A O     1 
ATOM   6804  C  CB    . VAL A 1 2307 ? 212.050 178.872 188.836 1.00 0.83  ? 2307 VAL A CB    1 
ATOM   6805  C  CG1   . VAL A 1 2307 ? 210.736 178.339 189.385 1.00 0.72  ? 2307 VAL A CG1   1 
ATOM   6806  C  CG2   . VAL A 1 2307 ? 211.813 179.572 187.510 1.00 0.18  ? 2307 VAL A CG2   1 
ATOM   6807  N  N     . ASP A 1 2308 ? 211.836 179.986 192.102 1.00 0.63  ? 2308 ASP A N     1 
ATOM   6808  C  CA    . ASP A 1 2308 ? 211.496 179.524 193.439 1.00 1.00  ? 2308 ASP A CA    1 
ATOM   6809  C  C     . ASP A 1 2308 ? 210.003 179.701 193.662 1.00 1.15  ? 2308 ASP A C     1 
ATOM   6810  O  O     . ASP A 1 2308 ? 209.366 180.543 193.022 1.00 0.68  ? 2308 ASP A O     1 
ATOM   6811  C  CB    . ASP A 1 2308 ? 212.342 180.244 194.510 1.00 1.10  ? 2308 ASP A CB    1 
ATOM   6812  C  CG    . ASP A 1 2308 ? 211.905 181.688 194.816 1.00 2.03  ? 2308 ASP A CG    1 
ATOM   6813  O  OD1   . ASP A 1 2308 ? 210.781 182.132 194.520 1.00 2.91  ? 2308 ASP A OD1   1 
ATOM   6814  O  OD2   . ASP A 1 2308 ? 212.742 182.413 195.388 1.00 4.65  ? 2308 ASP A OD2   1 
ATOM   6815  N  N     . PRO A 1 2309 ? 209.402 178.891 194.538 1.00 1.66  ? 2309 PRO A N     1 
ATOM   6816  C  CA    . PRO A 1 2309 ? 207.945 178.978 194.726 1.00 1.09  ? 2309 PRO A CA    1 
ATOM   6817  C  C     . PRO A 1 2309 ? 207.472 180.317 195.261 1.00 1.33  ? 2309 PRO A C     1 
ATOM   6818  O  O     . PRO A 1 2309 ? 206.296 180.652 195.085 1.00 1.14  ? 2309 PRO A O     1 
ATOM   6819  C  CB    . PRO A 1 2309 ? 207.652 177.843 195.718 1.00 1.34  ? 2309 PRO A CB    1 
ATOM   6820  C  CG    . PRO A 1 2309 ? 208.951 177.571 196.383 1.00 1.99  ? 2309 PRO A CG    1 
ATOM   6821  C  CD    . PRO A 1 2309 ? 209.995 177.818 195.349 1.00 1.85  ? 2309 PRO A CD    1 
ATOM   6822  N  N     . GLU A 1 2310 ? 208.348 181.098 195.897 1.00 2.34  ? 2310 GLU A N     1 
ATOM   6823  C  CA    . GLU A 1 2310 ? 207.908 182.338 196.528 1.00 1.85  ? 2310 GLU A CA    1 
ATOM   6824  C  C     . GLU A 1 2310 ? 207.378 183.336 195.503 1.00 3.47  ? 2310 GLU A C     1 
ATOM   6825  O  O     . GLU A 1 2310 ? 206.365 183.999 195.744 1.00 8.90  ? 2310 GLU A O     1 
ATOM   6826  C  CB    . GLU A 1 2310 ? 209.049 182.950 197.339 1.00 5.17  ? 2310 GLU A CB    1 
ATOM   6827  C  CG    . GLU A 1 2310 ? 208.654 184.207 198.097 1.00 10.72 ? 2310 GLU A CG    1 
ATOM   6828  C  CD    . GLU A 1 2310 ? 209.786 184.769 198.936 1.00 26.61 ? 2310 GLU A CD    1 
ATOM   6829  O  OE1   . GLU A 1 2310 ? 210.894 184.191 198.913 1.00 24.30 ? 2310 GLU A OE1   1 
ATOM   6830  O  OE2   . GLU A 1 2310 ? 209.567 185.792 199.621 1.00 27.51 ? 2310 GLU A OE2   1 
ATOM   6831  N  N     . TRP A 1 2311 ? 208.041 183.459 194.352 1.00 1.52  ? 2311 TRP A N     1 
ATOM   6832  C  CA    . TRP A 1 2311 ? 207.609 184.433 193.358 1.00 0.59  ? 2311 TRP A CA    1 
ATOM   6833  C  C     . TRP A 1 2311 ? 206.846 183.828 192.186 1.00 0.44  ? 2311 TRP A C     1 
ATOM   6834  O  O     . TRP A 1 2311 ? 205.926 184.471 191.676 1.00 3.71  ? 2311 TRP A O     1 
ATOM   6835  C  CB    . TRP A 1 2311 ? 208.805 185.240 192.827 1.00 0.31  ? 2311 TRP A CB    1 
ATOM   6836  C  CG    . TRP A 1 2311 ? 209.690 184.517 191.853 1.00 0.33  ? 2311 TRP A CG    1 
ATOM   6837  C  CD1   . TRP A 1 2311 ? 210.837 183.843 192.138 1.00 0.17  ? 2311 TRP A CD1   1 
ATOM   6838  C  CD2   . TRP A 1 2311 ? 209.504 184.402 190.437 1.00 0.14  ? 2311 TRP A CD2   1 
ATOM   6839  N  NE1   . TRP A 1 2311 ? 211.371 183.311 190.997 1.00 0.17  ? 2311 TRP A NE1   1 
ATOM   6840  C  CE2   . TRP A 1 2311 ? 210.576 183.646 189.936 1.00 0.08  ? 2311 TRP A CE2   1 
ATOM   6841  C  CE3   . TRP A 1 2311 ? 208.535 184.868 189.546 1.00 0.04  ? 2311 TRP A CE3   1 
ATOM   6842  C  CZ2   . TRP A 1 2311 ? 210.698 183.329 188.588 1.00 0.04  ? 2311 TRP A CZ2   1 
ATOM   6843  C  CZ3   . TRP A 1 2311 ? 208.665 184.560 188.211 1.00 0.03  ? 2311 TRP A CZ3   1 
ATOM   6844  C  CH2   . TRP A 1 2311 ? 209.739 183.801 187.743 1.00 0.02  ? 2311 TRP A CH2   1 
ATOM   6845  N  N     . VAL A 1 2312 ? 207.180 182.613 191.741 1.00 0.23  ? 2312 VAL A N     1 
ATOM   6846  C  CA    . VAL A 1 2312 ? 206.546 182.106 190.526 1.00 0.38  ? 2312 VAL A CA    1 
ATOM   6847  C  C     . VAL A 1 2312 ? 205.119 181.636 190.785 1.00 0.38  ? 2312 VAL A C     1 
ATOM   6848  O  O     . VAL A 1 2312 ? 204.301 181.621 189.859 1.00 0.37  ? 2312 VAL A O     1 
ATOM   6849  C  CB    . VAL A 1 2312 ? 207.359 180.966 189.887 1.00 0.24  ? 2312 VAL A CB    1 
ATOM   6850  C  CG1   . VAL A 1 2312 ? 207.344 179.712 190.762 1.00 0.47  ? 2312 VAL A CG1   1 
ATOM   6851  C  CG2   . VAL A 1 2312 ? 206.901 180.689 188.461 1.00 0.13  ? 2312 VAL A CG2   1 
ATOM   6852  N  N     . GLU A 1 2313 ? 204.790 181.262 192.020 1.00 0.27  ? 2313 GLU A N     1 
ATOM   6853  C  CA    . GLU A 1 2313 ? 203.434 180.838 192.341 1.00 0.50  ? 2313 GLU A CA    1 
ATOM   6854  C  C     . GLU A 1 2313 ? 202.435 181.987 192.343 1.00 0.79  ? 2313 GLU A C     1 
ATOM   6855  O  O     . GLU A 1 2313 ? 201.230 181.734 192.427 1.00 2.49  ? 2313 GLU A O     1 
ATOM   6856  C  CB    . GLU A 1 2313 ? 203.420 180.106 193.683 1.00 1.35  ? 2313 GLU A CB    1 
ATOM   6857  C  CG    . GLU A 1 2313 ? 204.161 178.781 193.627 1.00 2.65  ? 2313 GLU A CG    1 
ATOM   6858  C  CD    . GLU A 1 2313 ? 204.178 178.055 194.948 1.00 15.99 ? 2313 GLU A CD    1 
ATOM   6859  O  OE1   . GLU A 1 2313 ? 203.721 178.638 195.956 1.00 16.62 ? 2313 GLU A OE1   1 
ATOM   6860  O  OE2   . GLU A 1 2313 ? 204.647 176.898 194.983 1.00 14.66 ? 2313 GLU A OE2   1 
ATOM   6861  N  N     . ASN A 1 2314 ? 202.900 183.235 192.258 1.00 0.89  ? 2314 ASN A N     1 
ATOM   6862  C  CA    . ASN A 1 2314 ? 202.018 184.346 191.925 1.00 0.44  ? 2314 ASN A CA    1 
ATOM   6863  C  C     . ASN A 1 2314 ? 201.521 184.274 190.490 1.00 0.26  ? 2314 ASN A C     1 
ATOM   6864  O  O     . ASN A 1 2314 ? 200.560 184.969 190.147 1.00 0.39  ? 2314 ASN A O     1 
ATOM   6865  C  CB    . ASN A 1 2314 ? 202.730 185.682 192.145 1.00 0.66  ? 2314 ASN A CB    1 
ATOM   6866  C  CG    . ASN A 1 2314 ? 202.806 186.071 193.606 1.00 1.40  ? 2314 ASN A CG    1 
ATOM   6867  O  OD1   . ASN A 1 2314 ? 203.111 185.247 194.465 1.00 4.16  ? 2314 ASN A OD1   1 
ATOM   6868  N  ND2   . ASN A 1 2314 ? 202.532 187.335 193.894 1.00 0.26  ? 2314 ASN A ND2   1 
ATOM   6869  N  N     . LEU A 1 2315 ? 202.154 183.457 189.651 1.00 0.29  ? 2315 LEU A N     1 
ATOM   6870  C  CA    . LEU A 1 2315 ? 201.779 183.293 188.255 1.00 0.23  ? 2315 LEU A CA    1 
ATOM   6871  C  C     . LEU A 1 2315 ? 200.957 182.036 188.011 1.00 0.26  ? 2315 LEU A C     1 
ATOM   6872  O  O     . LEU A 1 2315 ? 200.747 181.666 186.854 1.00 0.37  ? 2315 LEU A O     1 
ATOM   6873  C  CB    . LEU A 1 2315 ? 203.032 183.268 187.377 1.00 0.17  ? 2315 LEU A CB    1 
ATOM   6874  C  CG    . LEU A 1 2315 ? 203.932 184.503 187.408 1.00 0.11  ? 2315 LEU A CG    1 
ATOM   6875  C  CD1   . LEU A 1 2315 ? 205.220 184.237 186.647 1.00 0.08  ? 2315 LEU A CD1   1 
ATOM   6876  C  CD2   . LEU A 1 2315 ? 203.207 185.706 186.836 1.00 0.07  ? 2315 LEU A CD2   1 
ATOM   6877  N  N     . ASN A 1 2316 ? 200.494 181.368 189.071 1.00 0.51  ? 2316 ASN A N     1 
ATOM   6878  C  CA    . ASN A 1 2316 ? 199.711 180.148 188.890 1.00 0.49  ? 2316 ASN A CA    1 
ATOM   6879  C  C     . ASN A 1 2316 ? 198.442 180.427 188.097 1.00 0.38  ? 2316 ASN A C     1 
ATOM   6880  O  O     . ASN A 1 2316 ? 198.098 179.680 187.176 1.00 0.78  ? 2316 ASN A O     1 
ATOM   6881  C  CB    . ASN A 1 2316 ? 199.378 179.524 190.246 1.00 0.84  ? 2316 ASN A CB    1 
ATOM   6882  C  CG    . ASN A 1 2316 ? 200.495 178.656 190.780 1.00 1.45  ? 2316 ASN A CG    1 
ATOM   6883  O  OD1   . ASN A 1 2316 ? 201.514 178.459 190.122 1.00 3.04  ? 2316 ASN A OD1   1 
ATOM   6884  N  ND2   . ASN A 1 2316 ? 200.308 178.129 191.984 1.00 1.99  ? 2316 ASN A ND2   1 
ATOM   6885  N  N     . SER A 1 2317 ? 197.741 181.512 188.428 1.00 0.41  ? 2317 SER A N     1 
ATOM   6886  C  CA    . SER A 1 2317 ? 196.554 181.880 187.666 1.00 0.47  ? 2317 SER A CA    1 
ATOM   6887  C  C     . SER A 1 2317 ? 196.901 182.475 186.307 1.00 0.36  ? 2317 SER A C     1 
ATOM   6888  O  O     . SER A 1 2317 ? 196.027 182.555 185.439 1.00 0.81  ? 2317 SER A O     1 
ATOM   6889  C  CB    . SER A 1 2317 ? 195.690 182.857 188.467 1.00 0.44  ? 2317 SER A CB    1 
ATOM   6890  O  OG    . SER A 1 2317 ? 196.406 184.033 188.795 1.00 0.44  ? 2317 SER A OG    1 
ATOM   6891  N  N     . VAL A 1 2318 ? 198.149 182.904 186.106 1.00 0.32  ? 2318 VAL A N     1 
ATOM   6892  C  CA    . VAL A 1 2318 ? 198.577 183.380 184.795 1.00 0.34  ? 2318 VAL A CA    1 
ATOM   6893  C  C     . VAL A 1 2318 ? 198.879 182.207 183.871 1.00 0.26  ? 2318 VAL A C     1 
ATOM   6894  O  O     . VAL A 1 2318 ? 198.489 182.202 182.698 1.00 0.32  ? 2318 VAL A O     1 
ATOM   6895  C  CB    . VAL A 1 2318 ? 199.797 184.312 184.932 1.00 0.37  ? 2318 VAL A CB    1 
ATOM   6896  C  CG1   . VAL A 1 2318 ? 200.264 184.787 183.565 1.00 0.12  ? 2318 VAL A CG1   1 
ATOM   6897  C  CG2   . VAL A 1 2318 ? 199.472 185.494 185.823 1.00 0.14  ? 2318 VAL A CG2   1 
ATOM   6898  N  N     . LEU A 1 2319 ? 199.576 181.198 184.386 1.00 0.40  ? 2319 LEU A N     1 
ATOM   6899  C  CA    . LEU A 1 2319 ? 200.041 180.088 183.568 1.00 0.45  ? 2319 LEU A CA    1 
ATOM   6900  C  C     . LEU A 1 2319 ? 198.978 179.023 183.320 1.00 1.13  ? 2319 LEU A C     1 
ATOM   6901  O  O     . LEU A 1 2319 ? 199.159 178.200 182.418 1.00 2.26  ? 2319 LEU A O     1 
ATOM   6902  C  CB    . LEU A 1 2319 ? 201.267 179.450 184.221 1.00 0.65  ? 2319 LEU A CB    1 
ATOM   6903  C  CG    . LEU A 1 2319 ? 202.447 180.396 184.458 1.00 0.22  ? 2319 LEU A CG    1 
ATOM   6904  C  CD1   . LEU A 1 2319 ? 203.534 179.720 185.271 1.00 0.57  ? 2319 LEU A CD1   1 
ATOM   6905  C  CD2   . LEU A 1 2319 ? 203.000 180.917 183.142 1.00 0.12  ? 2319 LEU A CD2   1 
ATOM   6906  N  N     . ASP A 1 2320 ? 197.882 179.010 184.076 1.00 1.03  ? 2320 ASP A N     1 
ATOM   6907  C  CA    . ASP A 1 2320 ? 196.820 178.045 183.832 1.00 1.94  ? 2320 ASP A CA    1 
ATOM   6908  C  C     . ASP A 1 2320 ? 195.793 178.654 182.878 1.00 2.18  ? 2320 ASP A C     1 
ATOM   6909  O  O     . ASP A 1 2320 ? 196.029 179.688 182.248 1.00 1.99  ? 2320 ASP A O     1 
ATOM   6910  C  CB    . ASP A 1 2320 ? 196.189 177.570 185.143 1.00 1.62  ? 2320 ASP A CB    1 
ATOM   6911  C  CG    . ASP A 1 2320 ? 195.634 178.702 185.985 1.00 3.28  ? 2320 ASP A CG    1 
ATOM   6912  O  OD1   . ASP A 1 2320 ? 195.469 179.825 185.470 1.00 5.47  ? 2320 ASP A OD1   1 
ATOM   6913  O  OD2   . ASP A 1 2320 ? 195.356 178.462 187.178 1.00 3.08  ? 2320 ASP A OD2   1 
ATOM   6914  N  N     . ASP A 1 2321 ? 194.633 178.007 182.758 1.00 3.05  ? 2321 ASP A N     1 
ATOM   6915  C  CA    . ASP A 1 2321 ? 193.623 178.445 181.803 1.00 3.82  ? 2321 ASP A CA    1 
ATOM   6916  C  C     . ASP A 1 2321 ? 192.931 179.738 182.218 1.00 2.35  ? 2321 ASP A C     1 
ATOM   6917  O  O     . ASP A 1 2321 ? 192.237 180.341 181.394 1.00 6.83  ? 2321 ASP A O     1 
ATOM   6918  C  CB    . ASP A 1 2321 ? 192.596 177.330 181.588 1.00 7.51  ? 2321 ASP A CB    1 
ATOM   6919  C  CG    . ASP A 1 2321 ? 191.828 176.980 182.854 1.00 18.61 ? 2321 ASP A CG    1 
ATOM   6920  O  OD1   . ASP A 1 2321 ? 192.106 177.563 183.923 1.00 18.02 ? 2321 ASP A OD1   1 
ATOM   6921  O  OD2   . ASP A 1 2321 ? 190.941 176.104 182.778 1.00 19.22 ? 2321 ASP A OD2   1 
ATOM   6922  N  N     . ASN A 1 2322 ? 193.099 180.177 183.469 1.00 2.15  ? 2322 ASN A N     1 
ATOM   6923  C  CA    . ASN A 1 2322 ? 192.537 181.458 183.885 1.00 1.66  ? 2322 ASN A CA    1 
ATOM   6924  C  C     . ASN A 1 2322 ? 193.156 182.613 183.106 1.00 1.24  ? 2322 ASN A C     1 
ATOM   6925  O  O     . ASN A 1 2322 ? 192.452 183.553 182.719 1.00 1.18  ? 2322 ASN A O     1 
ATOM   6926  C  CB    . ASN A 1 2322 ? 192.733 181.668 185.386 1.00 2.04  ? 2322 ASN A CB    1 
ATOM   6927  C  CG    . ASN A 1 2322 ? 191.885 180.737 186.222 1.00 1.54  ? 2322 ASN A CG    1 
ATOM   6928  O  OD1   . ASN A 1 2322 ? 190.658 180.789 186.171 1.00 1.84  ? 2322 ASN A OD1   1 
ATOM   6929  N  ND2   . ASN A 1 2322 ? 192.533 179.880 186.997 1.00 2.39  ? 2322 ASN A ND2   1 
ATOM   6930  N  N     . LYS A 1 2323 ? 194.468 182.556 182.867 1.00 1.10  ? 2323 LYS A N     1 
ATOM   6931  C  CA    . LYS A 1 2323 ? 195.196 183.608 182.153 1.00 0.89  ? 2323 LYS A CA    1 
ATOM   6932  C  C     . LYS A 1 2323 ? 194.981 184.968 182.808 1.00 0.41  ? 2323 LYS A C     1 
ATOM   6933  O  O     . LYS A 1 2323 ? 194.780 185.982 182.141 1.00 0.55  ? 2323 LYS A O     1 
ATOM   6934  C  CB    . LYS A 1 2323 ? 194.804 183.645 180.676 1.00 1.08  ? 2323 LYS A CB    1 
ATOM   6935  C  CG    . LYS A 1 2323 ? 195.207 182.414 179.889 1.00 1.22  ? 2323 LYS A CG    1 
ATOM   6936  C  CD    . LYS A 1 2323 ? 194.663 182.470 178.474 1.00 1.89  ? 2323 LYS A CD    1 
ATOM   6937  C  CE    . LYS A 1 2323 ? 195.077 181.250 177.673 1.00 8.95  ? 2323 LYS A CE    1 
ATOM   6938  N  NZ    . LYS A 1 2323 ? 194.645 181.341 176.255 1.00 14.75 ? 2323 LYS A NZ    1 
ATOM   6939  N  N     . LEU A 1 2324 ? 195.014 184.986 184.138 1.00 0.57  ? 2324 LEU A N     1 
ATOM   6940  C  CA    . LEU A 1 2324 ? 194.732 186.184 184.912 1.00 0.43  ? 2324 LEU A CA    1 
ATOM   6941  C  C     . LEU A 1 2324 ? 195.844 186.411 185.924 1.00 0.27  ? 2324 LEU A C     1 
ATOM   6942  O  O     . LEU A 1 2324 ? 196.227 185.487 186.645 1.00 0.61  ? 2324 LEU A O     1 
ATOM   6943  C  CB    . LEU A 1 2324 ? 193.387 186.064 185.633 1.00 0.87  ? 2324 LEU A CB    1 
ATOM   6944  C  CG    . LEU A 1 2324 ? 192.126 186.368 184.825 1.00 0.65  ? 2324 LEU A CG    1 
ATOM   6945  C  CD1   . LEU A 1 2324 ? 190.898 185.930 185.598 1.00 0.98  ? 2324 LEU A CD1   1 
ATOM   6946  C  CD2   . LEU A 1 2324 ? 192.046 187.843 184.472 1.00 0.50  ? 2324 LEU A CD2   1 
ATOM   6947  N  N     . LEU A 1 2325 ? 196.357 187.634 185.970 1.00 0.24  ? 2325 LEU A N     1 
ATOM   6948  C  CA    . LEU A 1 2325 ? 197.236 188.075 187.046 1.00 0.15  ? 2325 LEU A CA    1 
ATOM   6949  C  C     . LEU A 1 2325 ? 196.365 188.767 188.085 1.00 0.24  ? 2325 LEU A C     1 
ATOM   6950  O  O     . LEU A 1 2325 ? 195.806 189.836 187.822 1.00 0.66  ? 2325 LEU A O     1 
ATOM   6951  C  CB    . LEU A 1 2325 ? 198.329 189.008 186.530 1.00 0.15  ? 2325 LEU A CB    1 
ATOM   6952  C  CG    . LEU A 1 2325 ? 199.240 189.613 187.603 1.00 0.10  ? 2325 LEU A CG    1 
ATOM   6953  C  CD1   . LEU A 1 2325 ? 200.137 188.554 188.221 1.00 0.08  ? 2325 LEU A CD1   1 
ATOM   6954  C  CD2   . LEU A 1 2325 ? 200.063 190.762 187.039 1.00 0.15  ? 2325 LEU A CD2   1 
ATOM   6955  N  N     . THR A 1 2326 ? 196.232 188.152 189.253 1.00 0.15  ? 2326 THR A N     1 
ATOM   6956  C  CA    . THR A 1 2326 ? 195.393 188.685 190.315 1.00 0.56  ? 2326 THR A CA    1 
ATOM   6957  C  C     . THR A 1 2326 ? 196.259 189.440 191.312 1.00 0.45  ? 2326 THR A C     1 
ATOM   6958  O  O     . THR A 1 2326 ? 197.285 188.926 191.769 1.00 0.66  ? 2326 THR A O     1 
ATOM   6959  C  CB    . THR A 1 2326 ? 194.612 187.575 191.020 1.00 0.57  ? 2326 THR A CB    1 
ATOM   6960  O  OG1   . THR A 1 2326 ? 195.526 186.653 191.622 1.00 2.00  ? 2326 THR A OG1   1 
ATOM   6961  C  CG2   . THR A 1 2326 ? 193.737 186.835 190.026 1.00 0.17  ? 2326 THR A CG2   1 
ATOM   6962  N  N     . LEU A 1 2327 ? 195.846 190.647 191.637 1.00 0.44  ? 2327 LEU A N     1 
ATOM   6963  C  CA    . LEU A 1 2327 ? 196.588 191.506 192.532 1.00 0.80  ? 2327 LEU A CA    1 
ATOM   6964  C  C     . LEU A 1 2327 ? 195.833 191.676 193.847 1.00 1.14  ? 2327 LEU A C     1 
ATOM   6965  O  O     . LEU A 1 2327 ? 194.601 191.604 193.873 1.00 1.69  ? 2327 LEU A O     1 
ATOM   6966  C  CB    . LEU A 1 2327 ? 196.821 192.875 191.883 1.00 2.60  ? 2327 LEU A CB    1 
ATOM   6967  C  CG    . LEU A 1 2327 ? 197.734 192.907 190.655 1.00 0.94  ? 2327 LEU A CG    1 
ATOM   6968  C  CD1   . LEU A 1 2327 ? 197.938 194.334 190.176 1.00 0.47  ? 2327 LEU A CD1   1 
ATOM   6969  C  CD2   . LEU A 1 2327 ? 199.066 192.235 190.940 1.00 0.18  ? 2327 LEU A CD2   1 
ATOM   6970  N  N     . PRO A 1 2328 ? 196.541 191.895 194.958 1.00 1.93  ? 2328 PRO A N     1 
ATOM   6971  C  CA    . PRO A 1 2328 ? 195.848 192.039 196.250 1.00 0.97  ? 2328 PRO A CA    1 
ATOM   6972  C  C     . PRO A 1 2328 ? 194.896 193.225 196.326 1.00 2.40  ? 2328 PRO A C     1 
ATOM   6973  O  O     . PRO A 1 2328 ? 194.028 193.235 197.207 1.00 6.57  ? 2328 PRO A O     1 
ATOM   6974  C  CB    . PRO A 1 2328 ? 197.002 192.167 197.254 1.00 0.90  ? 2328 PRO A CB    1 
ATOM   6975  C  CG    . PRO A 1 2328 ? 198.173 192.601 196.433 1.00 1.07  ? 2328 PRO A CG    1 
ATOM   6976  C  CD    . PRO A 1 2328 ? 198.002 191.875 195.134 1.00 1.31  ? 2328 PRO A CD    1 
ATOM   6977  N  N     . ASN A 1 2329 ? 195.017 194.221 195.448 1.00 1.43  ? 2329 ASN A N     1 
ATOM   6978  C  CA    . ASN A 1 2329 ? 194.036 195.300 195.427 1.00 1.50  ? 2329 ASN A CA    1 
ATOM   6979  C  C     . ASN A 1 2329 ? 192.734 194.906 194.740 1.00 1.37  ? 2329 ASN A C     1 
ATOM   6980  O  O     . ASN A 1 2329 ? 191.887 195.773 194.515 1.00 1.89  ? 2329 ASN A O     1 
ATOM   6981  C  CB    . ASN A 1 2329 ? 194.613 196.555 194.759 1.00 2.63  ? 2329 ASN A CB    1 
ATOM   6982  C  CG    . ASN A 1 2329 ? 194.936 196.353 193.283 1.00 2.23  ? 2329 ASN A CG    1 
ATOM   6983  O  OD1   . ASN A 1 2329 ? 194.801 195.259 192.741 1.00 3.17  ? 2329 ASN A OD1   1 
ATOM   6984  N  ND2   . ASN A 1 2329 ? 195.364 197.424 192.629 1.00 3.69  ? 2329 ASN A ND2   1 
ATOM   6985  N  N     . GLY A 1 2330 ? 192.558 193.629 194.401 1.00 1.22  ? 2330 GLY A N     1 
ATOM   6986  C  CA    . GLY A 1 2330 ? 191.360 193.156 193.746 1.00 1.01  ? 2330 GLY A CA    1 
ATOM   6987  C  C     . GLY A 1 2330 ? 191.392 193.216 192.234 1.00 1.69  ? 2330 GLY A C     1 
ATOM   6988  O  O     . GLY A 1 2330 ? 190.479 192.688 191.591 1.00 2.17  ? 2330 GLY A O     1 
ATOM   6989  N  N     . GLU A 1 2331 ? 192.414 193.833 191.651 1.00 1.94  ? 2331 GLU A N     1 
ATOM   6990  C  CA    . GLU A 1 2331 ? 192.506 193.971 190.207 1.00 1.85  ? 2331 GLU A CA    1 
ATOM   6991  C  C     . GLU A 1 2331 ? 192.925 192.651 189.569 1.00 1.53  ? 2331 GLU A C     1 
ATOM   6992  O  O     . GLU A 1 2331 ? 193.721 191.896 190.133 1.00 1.36  ? 2331 GLU A O     1 
ATOM   6993  C  CB    . GLU A 1 2331 ? 193.502 195.073 189.849 1.00 1.47  ? 2331 GLU A CB    1 
ATOM   6994  C  CG    . GLU A 1 2331 ? 193.129 195.887 188.632 1.00 3.79  ? 2331 GLU A CG    1 
ATOM   6995  C  CD    . GLU A 1 2331 ? 194.269 196.765 188.154 1.00 11.08 ? 2331 GLU A CD    1 
ATOM   6996  O  OE1   . GLU A 1 2331 ? 194.968 197.347 189.011 1.00 8.31  ? 2331 GLU A OE1   1 
ATOM   6997  O  OE2   . GLU A 1 2331 ? 194.462 196.874 186.926 1.00 18.23 ? 2331 GLU A OE2   1 
ATOM   6998  N  N     . ARG A 1 2332 ? 192.374 192.371 188.391 1.00 1.65  ? 2332 ARG A N     1 
ATOM   6999  C  CA    . ARG A 1 2332 ? 192.675 191.154 187.648 1.00 1.27  ? 2332 ARG A CA    1 
ATOM   7000  C  C     . ARG A 1 2332 ? 193.045 191.530 186.221 1.00 1.26  ? 2332 ARG A C     1 
ATOM   7001  O  O     . ARG A 1 2332 ? 192.234 192.121 185.503 1.00 2.37  ? 2332 ARG A O     1 
ATOM   7002  C  CB    . ARG A 1 2332 ? 191.486 190.189 187.672 1.00 1.63  ? 2332 ARG A CB    1 
ATOM   7003  C  CG    . ARG A 1 2332 ? 191.016 189.834 189.077 1.00 4.08  ? 2332 ARG A CG    1 
ATOM   7004  C  CD    . ARG A 1 2332 ? 189.592 189.314 189.091 1.00 3.00  ? 2332 ARG A CD    1 
ATOM   7005  N  NE    . ARG A 1 2332 ? 189.534 187.860 189.016 1.00 1.64  ? 2332 ARG A NE    1 
ATOM   7006  C  CZ    . ARG A 1 2332 ? 188.759 187.187 188.177 1.00 4.36  ? 2332 ARG A CZ    1 
ATOM   7007  N  NH1   . ARG A 1 2332 ? 187.954 187.807 187.331 1.00 2.79  ? 2332 ARG A NH1   1 
ATOM   7008  N  NH2   . ARG A 1 2332 ? 188.794 185.857 188.188 1.00 0.68  ? 2332 ARG A NH2   1 
ATOM   7009  N  N     . LEU A 1 2333 ? 194.262 191.183 185.813 1.00 1.07  ? 2333 LEU A N     1 
ATOM   7010  C  CA    . LEU A 1 2333 ? 194.776 191.520 184.491 1.00 0.67  ? 2333 LEU A CA    1 
ATOM   7011  C  C     . LEU A 1 2333 ? 194.751 190.277 183.611 1.00 0.53  ? 2333 LEU A C     1 
ATOM   7012  O  O     . LEU A 1 2333 ? 195.378 189.266 183.940 1.00 0.95  ? 2333 LEU A O     1 
ATOM   7013  C  CB    . LEU A 1 2333 ? 196.195 192.086 184.585 1.00 0.40  ? 2333 LEU A CB    1 
ATOM   7014  C  CG    . LEU A 1 2333 ? 196.389 193.490 185.172 1.00 0.72  ? 2333 LEU A CG    1 
ATOM   7015  C  CD1   . LEU A 1 2333 ? 196.311 193.487 186.691 1.00 1.30  ? 2333 LEU A CD1   1 
ATOM   7016  C  CD2   . LEU A 1 2333 ? 197.709 194.081 184.708 1.00 0.29  ? 2333 LEU A CD2   1 
ATOM   7017  N  N     . SER A 1 2334 ? 194.028 190.356 182.498 1.00 0.90  ? 2334 SER A N     1 
ATOM   7018  C  CA    . SER A 1 2334 ? 193.929 189.238 181.572 1.00 0.30  ? 2334 SER A CA    1 
ATOM   7019  C  C     . SER A 1 2334 ? 195.146 189.186 180.659 1.00 0.68  ? 2334 SER A C     1 
ATOM   7020  O  O     . SER A 1 2334 ? 195.612 190.213 180.162 1.00 2.38  ? 2334 SER A O     1 
ATOM   7021  C  CB    . SER A 1 2334 ? 192.658 189.350 180.730 1.00 0.69  ? 2334 SER A CB    1 
ATOM   7022  O  OG    . SER A 1 2334 ? 191.504 189.407 181.545 1.00 5.73  ? 2334 SER A OG    1 
ATOM   7023  N  N     . LEU A 1 2335 ? 195.657 187.983 180.440 1.00 0.63  ? 2335 LEU A N     1 
ATOM   7024  C  CA    . LEU A 1 2335 ? 196.780 187.802 179.532 1.00 0.47  ? 2335 LEU A CA    1 
ATOM   7025  C  C     . LEU A 1 2335 ? 196.291 187.871 178.090 1.00 1.52  ? 2335 LEU A C     1 
ATOM   7026  O  O     . LEU A 1 2335 ? 195.456 187.052 177.693 1.00 1.29  ? 2335 LEU A O     1 
ATOM   7027  C  CB    . LEU A 1 2335 ? 197.469 186.472 179.791 1.00 0.29  ? 2335 LEU A CB    1 
ATOM   7028  C  CG    . LEU A 1 2335 ? 198.919 186.371 179.318 1.00 0.43  ? 2335 LEU A CG    1 
ATOM   7029  C  CD1   . LEU A 1 2335 ? 199.800 187.338 180.093 1.00 0.16  ? 2335 LEU A CD1   1 
ATOM   7030  C  CD2   . LEU A 1 2335 ? 199.432 184.946 179.449 1.00 0.48  ? 2335 LEU A CD2   1 
ATOM   7031  N  N     . PRO A 1 2336 ? 196.773 188.818 177.285 1.00 0.59  ? 2336 PRO A N     1 
ATOM   7032  C  CA    . PRO A 1 2336 ? 196.324 188.887 175.896 1.00 0.40  ? 2336 PRO A CA    1 
ATOM   7033  C  C     . PRO A 1 2336 ? 196.874 187.724 175.092 1.00 0.74  ? 2336 PRO A C     1 
ATOM   7034  O  O     . PRO A 1 2336 ? 197.926 187.157 175.433 1.00 0.75  ? 2336 PRO A O     1 
ATOM   7035  C  CB    . PRO A 1 2336 ? 196.895 190.231 175.405 1.00 0.55  ? 2336 PRO A CB    1 
ATOM   7036  C  CG    . PRO A 1 2336 ? 197.356 190.951 176.633 1.00 0.34  ? 2336 PRO A CG    1 
ATOM   7037  C  CD    . PRO A 1 2336 ? 197.716 189.894 177.616 1.00 0.43  ? 2336 PRO A CD    1 
ATOM   7038  N  N     . PRO A 1 2337 ? 196.195 187.331 174.010 1.00 0.80  ? 2337 PRO A N     1 
ATOM   7039  C  CA    . PRO A 1 2337 ? 196.648 186.161 173.238 1.00 0.38  ? 2337 PRO A CA    1 
ATOM   7040  C  C     . PRO A 1 2337 ? 198.013 186.325 172.593 1.00 0.55  ? 2337 PRO A C     1 
ATOM   7041  O  O     . PRO A 1 2337 ? 198.650 185.314 172.272 1.00 1.04  ? 2337 PRO A O     1 
ATOM   7042  C  CB    . PRO A 1 2337 ? 195.547 185.999 172.181 1.00 0.59  ? 2337 PRO A CB    1 
ATOM   7043  C  CG    . PRO A 1 2337 ? 194.945 187.359 172.065 1.00 0.65  ? 2337 PRO A CG    1 
ATOM   7044  C  CD    . PRO A 1 2337 ? 194.954 187.898 173.460 1.00 1.03  ? 2337 PRO A CD    1 
ATOM   7045  N  N     . ASN A 1 2338 ? 198.487 187.551 172.390 1.00 0.53  ? 2338 ASN A N     1 
ATOM   7046  C  CA    . ASN A 1 2338 ? 199.774 187.776 171.746 1.00 0.26  ? 2338 ASN A CA    1 
ATOM   7047  C  C     . ASN A 1 2338 ? 200.945 187.705 172.717 1.00 0.23  ? 2338 ASN A C     1 
ATOM   7048  O  O     . ASN A 1 2338 ? 202.093 187.858 172.288 1.00 0.27  ? 2338 ASN A O     1 
ATOM   7049  C  CB    . ASN A 1 2338 ? 199.777 189.132 171.035 1.00 0.40  ? 2338 ASN A CB    1 
ATOM   7050  C  CG    . ASN A 1 2338 ? 199.798 190.299 172.003 1.00 0.86  ? 2338 ASN A CG    1 
ATOM   7051  O  OD1   . ASN A 1 2338 ? 198.960 190.393 172.898 1.00 1.00  ? 2338 ASN A OD1   1 
ATOM   7052  N  ND2   . ASN A 1 2338 ? 200.759 191.196 171.826 1.00 0.72  ? 2338 ASN A ND2   1 
ATOM   7053  N  N     . VAL A 1 2339 ? 200.690 187.473 174.000 1.00 0.21  ? 2339 VAL A N     1 
ATOM   7054  C  CA    . VAL A 1 2339 ? 201.723 187.469 175.027 1.00 0.17  ? 2339 VAL A CA    1 
ATOM   7055  C  C     . VAL A 1 2339 ? 202.096 186.030 175.350 1.00 0.07  ? 2339 VAL A C     1 
ATOM   7056  O  O     . VAL A 1 2339 ? 201.219 185.173 175.516 1.00 0.11  ? 2339 VAL A O     1 
ATOM   7057  C  CB    . VAL A 1 2339 ? 201.256 188.214 176.290 1.00 0.11  ? 2339 VAL A CB    1 
ATOM   7058  C  CG1   . VAL A 1 2339 ? 202.265 188.049 177.412 1.00 0.05  ? 2339 VAL A CG1   1 
ATOM   7059  C  CG2   . VAL A 1 2339 ? 201.037 189.683 175.984 1.00 0.09  ? 2339 VAL A CG2   1 
ATOM   7060  N  N     . ARG A 1 2340 ? 203.396 185.762 175.425 1.00 0.03  ? 2340 ARG A N     1 
ATOM   7061  C  CA    . ARG A 1 2340 ? 203.920 184.497 175.917 1.00 0.05  ? 2340 ARG A CA    1 
ATOM   7062  C  C     . ARG A 1 2340 ? 204.737 184.764 177.172 1.00 0.03  ? 2340 ARG A C     1 
ATOM   7063  O  O     . ARG A 1 2340 ? 205.564 185.679 177.194 1.00 0.04  ? 2340 ARG A O     1 
ATOM   7064  C  CB    . ARG A 1 2340 ? 204.791 183.806 174.863 1.00 0.07  ? 2340 ARG A CB    1 
ATOM   7065  C  CG    . ARG A 1 2340 ? 204.039 183.329 173.641 1.00 0.08  ? 2340 ARG A CG    1 
ATOM   7066  C  CD    . ARG A 1 2340 ? 202.958 182.326 173.996 1.00 0.13  ? 2340 ARG A CD    1 
ATOM   7067  N  NE    . ARG A 1 2340 ? 202.205 181.913 172.818 1.00 1.06  ? 2340 ARG A NE    1 
ATOM   7068  C  CZ    . ARG A 1 2340 ? 201.349 182.683 172.161 1.00 0.69  ? 2340 ARG A CZ    1 
ATOM   7069  N  NH1   . ARG A 1 2340 ? 201.064 183.909 172.572 1.00 0.19  ? 2340 ARG A NH1   1 
ATOM   7070  N  NH2   . ARG A 1 2340 ? 200.761 182.211 171.066 1.00 0.84  ? 2340 ARG A NH2   1 
ATOM   7071  N  N     . ILE A 1 2341 ? 204.500 183.977 178.213 1.00 0.03  ? 2341 ILE A N     1 
ATOM   7072  C  CA    . ILE A 1 2341 ? 205.304 184.025 179.427 1.00 0.03  ? 2341 ILE A CA    1 
ATOM   7073  C  C     . ILE A 1 2341 ? 206.342 182.918 179.336 1.00 0.04  ? 2341 ILE A C     1 
ATOM   7074  O  O     . ILE A 1 2341 ? 205.996 181.735 179.259 1.00 0.14  ? 2341 ILE A O     1 
ATOM   7075  C  CB    . ILE A 1 2341 ? 204.440 183.882 180.689 1.00 0.01  ? 2341 ILE A CB    1 
ATOM   7076  C  CG1   . ILE A 1 2341 ? 203.320 184.924 180.695 1.00 0.01  ? 2341 ILE A CG1   1 
ATOM   7077  C  CG2   . ILE A 1 2341 ? 205.296 184.024 181.935 1.00 0.02  ? 2341 ILE A CG2   1 
ATOM   7078  C  CD1   . ILE A 1 2341 ? 203.807 186.350 180.606 1.00 0.01  ? 2341 ILE A CD1   1 
ATOM   7079  N  N     . MET A 1 2342 ? 207.615 183.299 179.335 1.00 0.03  ? 2342 MET A N     1 
ATOM   7080  C  CA    . MET A 1 2342 ? 208.710 182.363 179.156 1.00 0.03  ? 2342 MET A CA    1 
ATOM   7081  C  C     . MET A 1 2342 ? 209.642 182.406 180.357 1.00 0.04  ? 2342 MET A C     1 
ATOM   7082  O  O     . MET A 1 2342 ? 209.823 183.449 180.989 1.00 0.03  ? 2342 MET A O     1 
ATOM   7083  C  CB    . MET A 1 2342 ? 209.497 182.666 177.880 1.00 0.02  ? 2342 MET A CB    1 
ATOM   7084  C  CG    . MET A 1 2342 ? 208.649 182.741 176.624 1.00 0.02  ? 2342 MET A CG    1 
ATOM   7085  S  SD    . MET A 1 2342 ? 209.645 182.660 175.127 1.00 7.99  ? 2342 MET A SD    1 
ATOM   7086  C  CE    . MET A 1 2342 ? 208.406 182.212 173.921 1.00 0.34  ? 2342 MET A CE    1 
ATOM   7087  N  N     . PHE A 1 2343 ? 210.231 181.253 180.666 1.00 0.04  ? 2343 PHE A N     1 
ATOM   7088  C  CA    . PHE A 1 2343 ? 211.171 181.145 181.810 1.00 0.03  ? 2343 PHE A CA    1 
ATOM   7089  C  C     . PHE A 1 2343 ? 212.441 180.483 181.319 1.00 0.03  ? 2343 PHE A C     1 
ATOM   7090  O  O     . PHE A 1 2343 ? 212.412 179.267 181.048 1.00 0.05  ? 2343 PHE A O     1 
ATOM   7091  C  CB    . PHE A 1 2343 ? 210.547 180.317 182.935 1.00 0.02  ? 2343 PHE A CB    1 
ATOM   7092  C  CG    . PHE A 1 2343 ? 209.267 180.867 183.548 1.00 0.04  ? 2343 PHE A CG    1 
ATOM   7093  C  CD1   . PHE A 1 2343 ? 208.029 180.597 182.976 1.00 0.06  ? 2343 PHE A CD1   1 
ATOM   7094  C  CD2   . PHE A 1 2343 ? 209.304 181.627 184.711 1.00 0.02  ? 2343 PHE A CD2   1 
ATOM   7095  C  CE1   . PHE A 1 2343 ? 206.866 181.092 183.542 1.00 0.03  ? 2343 PHE A CE1   1 
ATOM   7096  C  CE2   . PHE A 1 2343 ? 208.137 182.119 185.272 1.00 0.03  ? 2343 PHE A CE2   1 
ATOM   7097  C  CZ    . PHE A 1 2343 ? 206.922 181.850 184.687 1.00 0.03  ? 2343 PHE A CZ    1 
ATOM   7098  N  N     . GLU A 1 2344 ? 213.523 181.250 181.180 1.00 0.03  ? 2344 GLU A N     1 
ATOM   7099  C  CA    . GLU A 1 2344 ? 214.831 180.656 180.797 1.00 0.03  ? 2344 GLU A CA    1 
ATOM   7100  C  C     . GLU A 1 2344 ? 215.593 180.357 182.090 1.00 0.03  ? 2344 GLU A C     1 
ATOM   7101  O  O     . GLU A 1 2344 ? 215.980 181.316 182.785 1.00 0.06  ? 2344 GLU A O     1 
ATOM   7102  C  CB    . GLU A 1 2344 ? 215.622 181.578 179.875 1.00 0.04  ? 2344 GLU A CB    1 
ATOM   7103  C  CG    . GLU A 1 2344 ? 216.859 180.917 179.279 1.00 0.03  ? 2344 GLU A CG    1 
ATOM   7104  C  CD    . GLU A 1 2344 ? 217.828 181.953 178.753 1.00 0.03  ? 2344 GLU A CD    1 
ATOM   7105  O  OE1   . GLU A 1 2344 ? 217.419 182.766 177.900 1.00 0.05  ? 2344 GLU A OE1   1 
ATOM   7106  O  OE2   . GLU A 1 2344 ? 218.992 181.943 179.195 1.00 0.04  ? 2344 GLU A OE2   1 
ATOM   7107  N  N     . VAL A 1 2345 ? 215.786 179.078 182.402 1.00 0.07  ? 2345 VAL A N     1 
ATOM   7108  C  CA    . VAL A 1 2345 ? 216.411 178.709 183.702 1.00 0.13  ? 2345 VAL A CA    1 
ATOM   7109  C  C     . VAL A 1 2345 ? 217.460 177.610 183.494 1.00 0.11  ? 2345 VAL A C     1 
ATOM   7110  O  O     . VAL A 1 2345 ? 217.388 176.914 182.466 1.00 0.06  ? 2345 VAL A O     1 
ATOM   7111  C  CB    . VAL A 1 2345 ? 215.302 178.247 184.669 1.00 0.18  ? 2345 VAL A CB    1 
ATOM   7112  C  CG1   . VAL A 1 2345 ? 214.200 179.288 184.816 1.00 0.06  ? 2345 VAL A CG1   1 
ATOM   7113  C  CG2   . VAL A 1 2345 ? 214.715 176.903 184.257 1.00 0.08  ? 2345 VAL A CG2   1 
ATOM   7114  N  N     . GLN A 1 2346 ? 218.385 177.463 184.442 1.00 1.29  ? 2346 GLN A N     1 
ATOM   7115  C  CA    . GLN A 1 2346 ? 219.383 176.405 184.372 1.00 0.98  ? 2346 GLN A CA    1 
ATOM   7116  C  C     . GLN A 1 2346 ? 218.952 175.138 185.094 1.00 0.70  ? 2346 GLN A C     1 
ATOM   7117  O  O     . GLN A 1 2346 ? 219.498 174.066 184.811 1.00 0.77  ? 2346 GLN A O     1 
ATOM   7118  C  CB    . GLN A 1 2346 ? 220.722 176.883 184.944 1.00 0.67  ? 2346 GLN A CB    1 
ATOM   7119  C  CG    . GLN A 1 2346 ? 220.636 177.523 186.315 1.00 3.42  ? 2346 GLN A CG    1 
ATOM   7120  C  CD    . GLN A 1 2346 ? 222.000 177.742 186.940 1.00 7.18  ? 2346 GLN A CD    1 
ATOM   7121  O  OE1   . GLN A 1 2346 ? 223.008 177.233 186.451 1.00 5.72  ? 2346 GLN A OE1   1 
ATOM   7122  N  NE2   . GLN A 1 2346 ? 222.040 178.515 188.017 1.00 8.64  ? 2346 GLN A NE2   1 
ATOM   7123  N  N     . ASP A 1 2347 ? 217.989 175.234 186.003 1.00 1.30  ? 2347 ASP A N     1 
ATOM   7124  C  CA    . ASP A 1 2347 ? 217.510 174.082 186.754 1.00 2.16  ? 2347 ASP A CA    1 
ATOM   7125  C  C     . ASP A 1 2347 ? 216.143 174.424 187.325 1.00 2.49  ? 2347 ASP A C     1 
ATOM   7126  O  O     . ASP A 1 2347 ? 215.718 175.580 187.319 1.00 2.51  ? 2347 ASP A O     1 
ATOM   7127  C  CB    . ASP A 1 2347 ? 218.499 173.686 187.859 1.00 2.78  ? 2347 ASP A CB    1 
ATOM   7128  C  CG    . ASP A 1 2347 ? 218.715 174.792 188.876 1.00 6.99  ? 2347 ASP A CG    1 
ATOM   7129  O  OD1   . ASP A 1 2347 ? 217.809 175.041 189.699 1.00 8.71  ? 2347 ASP A OD1   1 
ATOM   7130  O  OD2   . ASP A 1 2347 ? 219.790 175.422 188.847 1.00 5.99  ? 2347 ASP A OD2   1 
ATOM   7131  N  N     . LEU A 1 2348 ? 215.454 173.399 187.815 1.00 4.89  ? 2348 LEU A N     1 
ATOM   7132  C  CA    . LEU A 1 2348 ? 214.151 173.553 188.449 1.00 2.66  ? 2348 LEU A CA    1 
ATOM   7133  C  C     . LEU A 1 2348 ? 214.099 172.788 189.759 1.00 4.78  ? 2348 LEU A C     1 
ATOM   7134  O  O     . LEU A 1 2348 ? 213.057 172.251 190.147 1.00 14.58 ? 2348 LEU A O     1 
ATOM   7135  C  CB    . LEU A 1 2348 ? 213.031 173.102 187.517 1.00 2.65  ? 2348 LEU A CB    1 
ATOM   7136  C  CG    . LEU A 1 2348 ? 212.640 174.066 186.395 1.00 3.45  ? 2348 LEU A CG    1 
ATOM   7137  C  CD1   . LEU A 1 2348 ? 211.519 173.480 185.562 1.00 1.96  ? 2348 LEU A CD1   1 
ATOM   7138  C  CD2   . LEU A 1 2348 ? 212.240 175.419 186.964 1.00 1.16  ? 2348 LEU A CD2   1 
ATOM   7139  N  N     . LYS A 1 2349 ? 215.222 172.737 190.476 1.00 6.06  ? 2349 LYS A N     1 
ATOM   7140  C  CA    . LYS A 1 2349 ? 215.304 171.947 191.697 1.00 6.11  ? 2349 LYS A CA    1 
ATOM   7141  C  C     . LYS A 1 2349 ? 214.533 172.554 192.863 1.00 5.57  ? 2349 LYS A C     1 
ATOM   7142  O  O     . LYS A 1 2349 ? 214.388 171.891 193.895 1.00 12.08 ? 2349 LYS A O     1 
ATOM   7143  C  CB    . LYS A 1 2349 ? 216.767 171.740 192.097 1.00 6.74  ? 2349 LYS A CB    1 
ATOM   7144  C  CG    . LYS A 1 2349 ? 217.577 173.011 192.214 1.00 5.93  ? 2349 LYS A CG    1 
ATOM   7145  C  CD    . LYS A 1 2349 ? 218.890 172.756 192.933 1.00 10.17 ? 2349 LYS A CD    1 
ATOM   7146  C  CE    . LYS A 1 2349 ? 218.659 172.151 194.308 1.00 10.50 ? 2349 LYS A CE    1 
ATOM   7147  N  NZ    . LYS A 1 2349 ? 219.910 172.098 195.109 1.00 17.34 ? 2349 LYS A NZ    1 
ATOM   7148  N  N     . TYR A 1 2350 ? 214.041 173.783 192.734 1.00 2.82  ? 2350 TYR A N     1 
ATOM   7149  C  CA    . TYR A 1 2350 ? 213.200 174.384 193.758 1.00 1.61  ? 2350 TYR A CA    1 
ATOM   7150  C  C     . TYR A 1 2350 ? 211.780 174.662 193.290 1.00 3.97  ? 2350 TYR A C     1 
ATOM   7151  O  O     . TYR A 1 2350 ? 210.946 175.055 194.112 1.00 9.17  ? 2350 TYR A O     1 
ATOM   7152  C  CB    . TYR A 1 2350 ? 213.830 175.685 194.279 1.00 2.73  ? 2350 TYR A CB    1 
ATOM   7153  C  CG    . TYR A 1 2350 ? 215.189 175.472 194.896 1.00 3.22  ? 2350 TYR A CG    1 
ATOM   7154  C  CD1   . TYR A 1 2350 ? 215.318 174.976 196.186 1.00 2.26  ? 2350 TYR A CD1   1 
ATOM   7155  C  CD2   . TYR A 1 2350 ? 216.347 175.749 194.182 1.00 3.94  ? 2350 TYR A CD2   1 
ATOM   7156  C  CE1   . TYR A 1 2350 ? 216.558 174.769 196.749 1.00 2.90  ? 2350 TYR A CE1   1 
ATOM   7157  C  CE2   . TYR A 1 2350 ? 217.592 175.547 194.739 1.00 2.81  ? 2350 TYR A CE2   1 
ATOM   7158  C  CZ    . TYR A 1 2350 ? 217.692 175.058 196.022 1.00 3.25  ? 2350 TYR A CZ    1 
ATOM   7159  O  OH    . TYR A 1 2350 ? 218.930 174.854 196.581 1.00 8.87  ? 2350 TYR A OH    1 
ATOM   7160  N  N     . ALA A 1 2351 ? 211.480 174.469 192.010 1.00 5.98  ? 2351 ALA A N     1 
ATOM   7161  C  CA    . ALA A 1 2351 ? 210.120 174.651 191.523 1.00 3.51  ? 2351 ALA A CA    1 
ATOM   7162  C  C     . ALA A 1 2351 ? 209.231 173.503 191.983 1.00 3.59  ? 2351 ALA A C     1 
ATOM   7163  O  O     . ALA A 1 2351 ? 209.660 172.347 192.040 1.00 4.62  ? 2351 ALA A O     1 
ATOM   7164  C  CB    . ALA A 1 2351 ? 210.110 174.745 189.999 1.00 2.22  ? 2351 ALA A CB    1 
ATOM   7165  N  N     . THR A 1 2352 ? 207.989 173.826 192.314 1.00 5.69  ? 2352 THR A N     1 
ATOM   7166  C  CA    . THR A 1 2352 ? 207.030 172.819 192.738 1.00 2.99  ? 2352 THR A CA    1 
ATOM   7167  C  C     . THR A 1 2352 ? 206.276 172.253 191.537 1.00 2.95  ? 2352 THR A C     1 
ATOM   7168  O  O     . THR A 1 2352 ? 206.375 172.749 190.412 1.00 2.50  ? 2352 THR A O     1 
ATOM   7169  C  CB    . THR A 1 2352 ? 206.049 173.401 193.757 1.00 3.86  ? 2352 THR A CB    1 
ATOM   7170  O  OG1   . THR A 1 2352 ? 205.317 174.478 193.160 1.00 9.17  ? 2352 THR A OG1   1 
ATOM   7171  C  CG2   . THR A 1 2352 ? 206.793 173.910 194.981 1.00 2.72  ? 2352 THR A CG2   1 
ATOM   7172  N  N     . LEU A 1 2353 ? 205.482 171.209 191.780 1.00 4.34  ? 2353 LEU A N     1 
ATOM   7173  C  CA    . LEU A 1 2353 ? 204.693 170.583 190.686 1.00 2.64  ? 2353 LEU A CA    1 
ATOM   7174  C  C     . LEU A 1 2353 ? 203.687 171.603 190.132 1.00 3.15  ? 2353 LEU A C     1 
ATOM   7175  O  O     . LEU A 1 2353 ? 203.468 171.617 188.902 1.00 2.05  ? 2353 LEU A O     1 
ATOM   7176  C  CB    . LEU A 1 2353 ? 203.997 169.335 191.228 1.00 3.08  ? 2353 LEU A CB    1 
ATOM   7177  C  CG    . LEU A 1 2353 ? 203.293 168.443 190.199 1.00 5.88  ? 2353 LEU A CG    1 
ATOM   7178  C  CD1   . LEU A 1 2353 ? 203.116 167.047 190.770 1.00 13.06 ? 2353 LEU A CD1   1 
ATOM   7179  C  CD2   . LEU A 1 2353 ? 201.945 169.013 189.797 1.00 10.79 ? 2353 LEU A CD2   1 
ATOM   7180  N  N     . ALA A 1 2354 ? 203.113 172.433 191.006 1.00 3.10  ? 2354 ALA A N     1 
ATOM   7181  C  CA    . ALA A 1 2354 ? 202.095 173.415 190.570 1.00 3.80  ? 2354 ALA A CA    1 
ATOM   7182  C  C     . ALA A 1 2354 ? 202.635 174.232 189.393 1.00 5.94  ? 2354 ALA A C     1 
ATOM   7183  O  O     . ALA A 1 2354 ? 201.885 174.450 188.420 1.00 4.58  ? 2354 ALA A O     1 
ATOM   7184  C  CB    . ALA A 1 2354 ? 201.717 174.300 191.729 1.00 3.71  ? 2354 ALA A CB    1 
ATOM   7185  N  N     . THR A 1 2355 ? 203.897 174.654 189.475 1.00 4.41  ? 2355 THR A N     1 
ATOM   7186  C  CA    . THR A 1 2355 ? 204.494 175.483 188.410 1.00 1.68  ? 2355 THR A CA    1 
ATOM   7187  C  C     . THR A 1 2355 ? 204.889 174.604 187.246 1.00 1.58  ? 2355 THR A C     1 
ATOM   7188  O  O     . THR A 1 2355 ? 204.578 174.980 186.096 1.00 2.09  ? 2355 THR A O     1 
ATOM   7189  C  CB    . THR A 1 2355 ? 205.691 176.247 188.976 1.00 1.10  ? 2355 THR A CB    1 
ATOM   7190  O  OG1   . THR A 1 2355 ? 205.168 177.045 190.032 1.00 3.26  ? 2355 THR A OG1   1 
ATOM   7191  C  CG2   . THR A 1 2355 ? 206.359 177.131 187.939 1.00 0.53  ? 2355 THR A CG2   1 
ATOM   7192  N  N     . VAL A 1 2356 ? 205.529 173.465 187.516 1.00 1.87  ? 2356 VAL A N     1 
ATOM   7193  C  CA    . VAL A 1 2356 ? 206.030 172.642 186.417 1.00 1.68  ? 2356 VAL A CA    1 
ATOM   7194  C  C     . VAL A 1 2356 ? 204.884 172.153 185.541 1.00 2.84  ? 2356 VAL A C     1 
ATOM   7195  O  O     . VAL A 1 2356 ? 204.986 172.143 184.309 1.00 3.71  ? 2356 VAL A O     1 
ATOM   7196  C  CB    . VAL A 1 2356 ? 206.871 171.473 186.965 1.00 3.25  ? 2356 VAL A CB    1 
ATOM   7197  C  CG1   . VAL A 1 2356 ? 207.305 170.548 185.841 1.00 2.67  ? 2356 VAL A CG1   1 
ATOM   7198  C  CG2   . VAL A 1 2356 ? 208.082 172.002 187.714 1.00 2.12  ? 2356 VAL A CG2   1 
ATOM   7199  N  N     . SER A 1 2357 ? 203.779 171.753 186.175 1.00 2.80  ? 2357 SER A N     1 
ATOM   7200  C  CA    . SER A 1 2357 ? 202.614 171.200 185.431 1.00 2.03  ? 2357 SER A CA    1 
ATOM   7201  C  C     . SER A 1 2357 ? 201.926 172.270 184.574 1.00 1.64  ? 2357 SER A C     1 
ATOM   7202  O  O     . SER A 1 2357 ? 201.246 171.888 183.601 1.00 2.09  ? 2357 SER A O     1 
ATOM   7203  C  CB    . SER A 1 2357 ? 201.630 170.578 186.387 1.00 2.55  ? 2357 SER A CB    1 
ATOM   7204  O  OG    . SER A 1 2357 ? 201.082 171.553 187.261 1.00 8.55  ? 2357 SER A OG    1 
ATOM   7205  N  N     . ARG A 1 2358 ? 202.094 173.548 184.910 1.00 1.60  ? 2358 ARG A N     1 
ATOM   7206  C  CA    . ARG A 1 2358 ? 201.356 174.618 184.187 1.00 1.92  ? 2358 ARG A CA    1 
ATOM   7207  C  C     . ARG A 1 2358 ? 202.170 175.177 183.011 1.00 1.66  ? 2358 ARG A C     1 
ATOM   7208  O  O     . ARG A 1 2358 ? 201.687 176.135 182.382 1.00 5.28  ? 2358 ARG A O     1 
ATOM   7209  C  CB    . ARG A 1 2358 ? 201.030 175.781 185.129 1.00 1.36  ? 2358 ARG A CB    1 
ATOM   7210  C  CG    . ARG A 1 2358 ? 199.893 175.596 186.121 1.00 1.22  ? 2358 ARG A CG    1 
ATOM   7211  C  CD    . ARG A 1 2358 ? 199.699 176.900 186.879 1.00 1.20  ? 2358 ARG A CD    1 
ATOM   7212  N  NE    . ARG A 1 2358 ? 198.495 176.937 187.716 1.00 1.86  ? 2358 ARG A NE    1 
ATOM   7213  C  CZ    . ARG A 1 2358 ? 198.265 176.163 188.766 1.00 0.98  ? 2358 ARG A CZ    1 
ATOM   7214  N  NH1   . ARG A 1 2358 ? 199.212 175.364 189.228 1.00 1.17  ? 2358 ARG A NH1   1 
ATOM   7215  N  NH2   . ARG A 1 2358 ? 197.087 176.200 189.360 1.00 1.33  ? 2358 ARG A NH2   1 
ATOM   7216  N  N     . CYS A 1 2359 ? 203.344 174.620 182.716 1.00 1.83  ? 2359 CYS A N     1 
ATOM   7217  C  CA    . CYS A 1 2359 ? 204.180 175.248 181.658 1.00 1.38  ? 2359 CYS A CA    1 
ATOM   7218  C  C     . CYS A 1 2359 ? 204.745 174.238 180.660 1.00 1.60  ? 2359 CYS A C     1 
ATOM   7219  O  O     . CYS A 1 2359 ? 205.209 173.168 181.104 1.00 9.11  ? 2359 CYS A O     1 
ATOM   7220  C  CB    . CYS A 1 2359 ? 205.385 175.968 182.255 1.00 1.22  ? 2359 CYS A CB    1 
ATOM   7221  S  SG    . CYS A 1 2359 ? 204.970 177.472 183.173 1.00 6.37  ? 2359 CYS A SG    1 
ATOM   7222  N  N     . GLY A 1 2360 ? 204.692 174.558 179.365 1.00 0.55  ? 2360 GLY A N     1 
ATOM   7223  C  CA    . GLY A 1 2360 ? 205.359 173.739 178.371 1.00 0.49  ? 2360 GLY A CA    1 
ATOM   7224  C  C     . GLY A 1 2360 ? 206.860 173.733 178.606 1.00 0.69  ? 2360 GLY A C     1 
ATOM   7225  O  O     . GLY A 1 2360 ? 207.459 174.753 178.948 1.00 0.45  ? 2360 GLY A O     1 
ATOM   7226  N  N     . MET A 1 2361 ? 207.468 172.567 178.436 1.00 1.40  ? 2361 MET A N     1 
ATOM   7227  C  CA    . MET A 1 2361 ? 208.876 172.377 178.747 1.00 0.57  ? 2361 MET A CA    1 
ATOM   7228  C  C     . MET A 1 2361 ? 209.655 172.083 177.477 1.00 0.22  ? 2361 MET A C     1 
ATOM   7229  O  O     . MET A 1 2361 ? 209.280 171.198 176.703 1.00 1.03  ? 2361 MET A O     1 
ATOM   7230  C  CB    . MET A 1 2361 ? 209.070 171.246 179.756 1.00 1.00  ? 2361 MET A CB    1 
ATOM   7231  C  CG    . MET A 1 2361 ? 208.480 171.521 181.120 1.00 2.25  ? 2361 MET A CG    1 
ATOM   7232  S  SD    . MET A 1 2361 ? 209.267 172.910 181.946 1.00 11.60 ? 2361 MET A SD    1 
ATOM   7233  C  CE    . MET A 1 2361 ? 208.199 173.096 183.365 1.00 5.50  ? 2361 MET A CE    1 
ATOM   7234  N  N     . VAL A 1 2362 ? 210.725 172.838 177.261 1.00 0.23  ? 2362 VAL A N     1 
ATOM   7235  C  CA    . VAL A 1 2362 ? 211.736 172.524 176.260 1.00 0.29  ? 2362 VAL A CA    1 
ATOM   7236  C  C     . VAL A 1 2362 ? 213.052 172.348 176.998 1.00 0.12  ? 2362 VAL A C     1 
ATOM   7237  O  O     . VAL A 1 2362 ? 213.562 173.300 177.601 1.00 0.09  ? 2362 VAL A O     1 
ATOM   7238  C  CB    . VAL A 1 2362 ? 211.850 173.612 175.181 1.00 0.13  ? 2362 VAL A CB    1 
ATOM   7239  C  CG1   . VAL A 1 2362 ? 212.815 173.168 174.096 1.00 0.20  ? 2362 VAL A CG1   1 
ATOM   7240  C  CG2   . VAL A 1 2362 ? 210.492 173.926 174.592 1.00 0.14  ? 2362 VAL A CG2   1 
ATOM   7241  N  N     . TRP A 1 2363 ? 213.595 171.138 176.961 1.00 0.19  ? 2363 TRP A N     1 
ATOM   7242  C  CA    . TRP A 1 2363 ? 214.823 170.810 177.668 1.00 0.12  ? 2363 TRP A CA    1 
ATOM   7243  C  C     . TRP A 1 2363 ? 216.015 171.006 176.747 1.00 0.05  ? 2363 TRP A C     1 
ATOM   7244  O  O     . TRP A 1 2363 ? 216.031 170.495 175.626 1.00 0.12  ? 2363 TRP A O     1 
ATOM   7245  C  CB    . TRP A 1 2363 ? 214.797 169.373 178.189 1.00 0.24  ? 2363 TRP A CB    1 
ATOM   7246  C  CG    . TRP A 1 2363 ? 216.156 168.855 178.548 1.00 0.08  ? 2363 TRP A CG    1 
ATOM   7247  C  CD1   . TRP A 1 2363 ? 216.943 168.033 177.799 1.00 0.12  ? 2363 TRP A CD1   1 
ATOM   7248  C  CD2   . TRP A 1 2363 ? 216.894 169.138 179.742 1.00 0.07  ? 2363 TRP A CD2   1 
ATOM   7249  N  NE1   . TRP A 1 2363 ? 218.121 167.780 178.452 1.00 0.18  ? 2363 TRP A NE1   1 
ATOM   7250  C  CE2   . TRP A 1 2363 ? 218.117 168.447 179.648 1.00 0.10  ? 2363 TRP A CE2   1 
ATOM   7251  C  CE3   . TRP A 1 2363 ? 216.636 169.903 180.883 1.00 0.08  ? 2363 TRP A CE3   1 
ATOM   7252  C  CZ2   . TRP A 1 2363 ? 219.080 168.497 180.652 1.00 0.11  ? 2363 TRP A CZ2   1 
ATOM   7253  C  CZ3   . TRP A 1 2363 ? 217.594 169.952 181.876 1.00 0.06  ? 2363 TRP A CZ3   1 
ATOM   7254  C  CH2   . TRP A 1 2363 ? 218.801 169.254 181.754 1.00 0.10  ? 2363 TRP A CH2   1 
ATOM   7255  N  N     . PHE A 1 2364 ? 217.006 171.744 177.224 1.00 0.05  ? 2364 PHE A N     1 
ATOM   7256  C  CA    . PHE A 1 2364 ? 218.270 171.908 176.529 1.00 0.06  ? 2364 PHE A CA    1 
ATOM   7257  C  C     . PHE A 1 2364 ? 219.332 171.126 177.285 1.00 0.11  ? 2364 PHE A C     1 
ATOM   7258  O  O     . PHE A 1 2364 ? 219.416 171.214 178.512 1.00 0.17  ? 2364 PHE A O     1 
ATOM   7259  C  CB    . PHE A 1 2364 ? 218.665 173.384 176.431 1.00 0.12  ? 2364 PHE A CB    1 
ATOM   7260  C  CG    . PHE A 1 2364 ? 217.817 174.187 175.483 1.00 0.01  ? 2364 PHE A CG    1 
ATOM   7261  C  CD1   . PHE A 1 2364 ? 216.478 174.422 175.756 1.00 0.02  ? 2364 PHE A CD1   1 
ATOM   7262  C  CD2   . PHE A 1 2364 ? 218.362 174.731 174.336 1.00 0.03  ? 2364 PHE A CD2   1 
ATOM   7263  C  CE1   . PHE A 1 2364 ? 215.705 175.163 174.899 1.00 0.02  ? 2364 PHE A CE1   1 
ATOM   7264  C  CE2   . PHE A 1 2364 ? 217.592 175.477 173.476 1.00 0.09  ? 2364 PHE A CE2   1 
ATOM   7265  C  CZ    . PHE A 1 2364 ? 216.260 175.692 173.756 1.00 0.02  ? 2364 PHE A CZ    1 
ATOM   7266  N  N     . SER A 1 2365 ? 220.116 170.343 176.560 1.00 0.86  ? 2365 SER A N     1 
ATOM   7267  C  CA    . SER A 1 2365 ? 221.278 169.687 177.130 1.00 1.38  ? 2365 SER A CA    1 
ATOM   7268  C  C     . SER A 1 2365 ? 222.539 170.407 176.678 1.00 2.98  ? 2365 SER A C     1 
ATOM   7269  O  O     . SER A 1 2365 ? 222.537 171.148 175.693 1.00 3.58  ? 2365 SER A O     1 
ATOM   7270  C  CB    . SER A 1 2365 ? 221.331 168.212 176.726 1.00 1.12  ? 2365 SER A CB    1 
ATOM   7271  O  OG    . SER A 1 2365 ? 221.549 168.067 175.336 1.00 3.92  ? 2365 SER A OG    1 
ATOM   7272  N  N     . GLU A 1 2366 ? 223.624 170.193 177.421 1.00 2.83  ? 2366 GLU A N     1 
ATOM   7273  C  CA    . GLU A 1 2366 ? 224.901 170.765 177.016 1.00 3.81  ? 2366 GLU A CA    1 
ATOM   7274  C  C     . GLU A 1 2366 ? 225.393 170.197 175.694 1.00 6.07  ? 2366 GLU A C     1 
ATOM   7275  O  O     . GLU A 1 2366 ? 226.262 170.807 175.062 1.00 15.46 ? 2366 GLU A O     1 
ATOM   7276  C  CB    . GLU A 1 2366 ? 225.945 170.545 178.110 1.00 6.47  ? 2366 GLU A CB    1 
ATOM   7277  C  CG    . GLU A 1 2366 ? 225.953 171.629 179.173 1.00 12.66 ? 2366 GLU A CG    1 
ATOM   7278  C  CD    . GLU A 1 2366 ? 227.106 171.491 180.150 1.00 22.53 ? 2366 GLU A CD    1 
ATOM   7279  O  OE1   . GLU A 1 2366 ? 227.210 170.436 180.808 1.00 21.73 ? 2366 GLU A OE1   1 
ATOM   7280  O  OE2   . GLU A 1 2366 ? 227.908 172.441 180.262 1.00 20.91 ? 2366 GLU A OE2   1 
ATOM   7281  N  N     . ASP A 1 2367 ? 224.859 169.056 175.262 1.00 5.17  ? 2367 ASP A N     1 
ATOM   7282  C  CA    . ASP A 1 2367 ? 225.205 168.505 173.958 1.00 3.90  ? 2367 ASP A CA    1 
ATOM   7283  C  C     . ASP A 1 2367 ? 224.502 169.238 172.823 1.00 3.51  ? 2367 ASP A C     1 
ATOM   7284  O  O     . ASP A 1 2367 ? 224.931 169.136 171.669 1.00 9.11  ? 2367 ASP A O     1 
ATOM   7285  C  CB    . ASP A 1 2367 ? 224.865 167.016 173.916 1.00 7.70  ? 2367 ASP A CB    1 
ATOM   7286  C  CG    . ASP A 1 2367 ? 225.763 166.191 174.816 1.00 19.06 ? 2367 ASP A CG    1 
ATOM   7287  O  OD1   . ASP A 1 2367 ? 226.925 166.595 175.029 1.00 20.58 ? 2367 ASP A OD1   1 
ATOM   7288  O  OD2   . ASP A 1 2367 ? 225.307 165.137 175.308 1.00 25.60 ? 2367 ASP A OD2   1 
ATOM   7289  N  N     . VAL A 1 2368 ? 223.430 169.969 173.127 1.00 4.01  ? 2368 VAL A N     1 
ATOM   7290  C  CA    . VAL A 1 2368 ? 222.724 170.732 172.099 1.00 2.30  ? 2368 VAL A CA    1 
ATOM   7291  C  C     . VAL A 1 2368 ? 223.639 171.796 171.507 1.00 2.66  ? 2368 VAL A C     1 
ATOM   7292  O  O     . VAL A 1 2368 ? 223.672 172.004 170.289 1.00 1.63  ? 2368 VAL A O     1 
ATOM   7293  C  CB    . VAL A 1 2368 ? 221.438 171.344 172.685 1.00 2.03  ? 2368 VAL A CB    1 
ATOM   7294  C  CG1   . VAL A 1 2368 ? 220.808 172.306 171.705 1.00 1.33  ? 2368 VAL A CG1   1 
ATOM   7295  C  CG2   . VAL A 1 2368 ? 220.458 170.246 173.054 1.00 4.57  ? 2368 VAL A CG2   1 
ATOM   7296  N  N     . LEU A 1 2369 ? 224.393 172.481 172.358 1.00 5.45  ? 2369 LEU A N     1 
ATOM   7297  C  CA    . LEU A 1 2369 ? 225.387 173.462 171.929 1.00 1.72  ? 2369 LEU A CA    1 
ATOM   7298  C  C     . LEU A 1 2369 ? 226.749 172.780 171.955 1.00 1.66  ? 2369 LEU A C     1 
ATOM   7299  O  O     . LEU A 1 2369 ? 227.328 172.570 173.022 1.00 6.43  ? 2369 LEU A O     1 
ATOM   7300  C  CB    . LEU A 1 2369 ? 225.351 174.689 172.832 1.00 1.47  ? 2369 LEU A CB    1 
ATOM   7301  C  CG    . LEU A 1 2369 ? 226.352 175.803 172.528 1.00 0.69  ? 2369 LEU A CG    1 
ATOM   7302  C  CD1   . LEU A 1 2369 ? 226.220 176.287 171.096 1.00 0.42  ? 2369 LEU A CD1   1 
ATOM   7303  C  CD2   . LEU A 1 2369 ? 226.163 176.938 173.504 1.00 0.32  ? 2369 LEU A CD2   1 
ATOM   7304  N  N     . SER A 1 2370 ? 227.257 172.429 170.779 1.00 1.61  ? 2370 SER A N     1 
ATOM   7305  C  CA    . SER A 1 2370 ? 228.547 171.769 170.683 1.00 2.57  ? 2370 SER A CA    1 
ATOM   7306  C  C     . SER A 1 2370 ? 229.683 172.788 170.755 1.00 3.25  ? 2370 SER A C     1 
ATOM   7307  O  O     . SER A 1 2370 ? 229.522 173.967 170.431 1.00 2.60  ? 2370 SER A O     1 
ATOM   7308  C  CB    . SER A 1 2370 ? 228.644 170.961 169.388 1.00 3.02  ? 2370 SER A CB    1 
ATOM   7309  O  OG    . SER A 1 2370 ? 228.776 171.809 168.264 1.00 2.00  ? 2370 SER A OG    1 
ATOM   7310  N  N     . THR A 1 2371 ? 230.849 172.311 171.196 1.00 2.95  ? 2371 THR A N     1 
ATOM   7311  C  CA    . THR A 1 2371 ? 232.015 173.183 171.298 1.00 2.35  ? 2371 THR A CA    1 
ATOM   7312  C  C     . THR A 1 2371 ? 232.466 173.671 169.927 1.00 3.52  ? 2371 THR A C     1 
ATOM   7313  O  O     . THR A 1 2371 ? 233.021 174.768 169.809 1.00 2.73  ? 2371 THR A O     1 
ATOM   7314  C  CB    . THR A 1 2371 ? 233.154 172.454 172.013 1.00 2.73  ? 2371 THR A CB    1 
ATOM   7315  O  OG1   . THR A 1 2371 ? 232.648 171.822 173.195 1.00 7.50  ? 2371 THR A OG1   1 
ATOM   7316  C  CG2   . THR A 1 2371 ? 234.245 173.425 172.408 1.00 2.65  ? 2371 THR A CG2   1 
ATOM   7317  N  N     . ASP A 1 2372 ? 232.223 172.878 168.882 1.00 6.62  ? 2372 ASP A N     1 
ATOM   7318  C  CA    . ASP A 1 2372 ? 232.504 173.328 167.523 1.00 3.75  ? 2372 ASP A CA    1 
ATOM   7319  C  C     . ASP A 1 2372 ? 231.654 174.540 167.159 1.00 3.29  ? 2372 ASP A C     1 
ATOM   7320  O  O     . ASP A 1 2372 ? 232.125 175.458 166.480 1.00 5.75  ? 2372 ASP A O     1 
ATOM   7321  C  CB    . ASP A 1 2372 ? 232.265 172.182 166.540 1.00 5.56  ? 2372 ASP A CB    1 
ATOM   7322  C  CG    . ASP A 1 2372 ? 232.593 172.559 165.110 1.00 16.89 ? 2372 ASP A CG    1 
ATOM   7323  O  OD1   . ASP A 1 2372 ? 233.534 173.353 164.902 1.00 25.17 ? 2372 ASP A OD1   1 
ATOM   7324  O  OD2   . ASP A 1 2372 ? 231.909 172.055 164.195 1.00 15.87 ? 2372 ASP A OD2   1 
ATOM   7325  N  N     . MET A 1 2373 ? 230.393 174.552 167.597 1.00 3.19  ? 2373 MET A N     1 
ATOM   7326  C  CA    . MET A 1 2373 ? 229.522 175.690 167.325 1.00 1.90  ? 2373 MET A CA    1 
ATOM   7327  C  C     . MET A 1 2373 ? 230.040 176.957 167.994 1.00 2.00  ? 2373 MET A C     1 
ATOM   7328  O  O     . MET A 1 2373 ? 230.038 178.034 167.386 1.00 2.13  ? 2373 MET A O     1 
ATOM   7329  C  CB    . MET A 1 2373 ? 228.104 175.378 167.799 1.00 3.05  ? 2373 MET A CB    1 
ATOM   7330  C  CG    . MET A 1 2373 ? 227.339 174.434 166.897 1.00 2.70  ? 2373 MET A CG    1 
ATOM   7331  S  SD    . MET A 1 2373 ? 225.991 173.611 167.763 1.00 4.45  ? 2373 MET A SD    1 
ATOM   7332  C  CE    . MET A 1 2373 ? 224.859 174.972 168.002 1.00 0.71  ? 2373 MET A CE    1 
ATOM   7333  N  N     . ILE A 1 2374 ? 230.488 176.845 169.246 1.00 2.90  ? 2374 ILE A N     1 
ATOM   7334  C  CA    . ILE A 1 2374 ? 231.029 177.998 169.959 1.00 1.57  ? 2374 ILE A CA    1 
ATOM   7335  C  C     . ILE A 1 2374 ? 232.296 178.499 169.281 1.00 2.56  ? 2374 ILE A C     1 
ATOM   7336  O  O     . ILE A 1 2374 ? 232.519 179.709 169.161 1.00 4.59  ? 2374 ILE A O     1 
ATOM   7337  C  CB    . ILE A 1 2374 ? 231.274 177.643 171.437 1.00 1.67  ? 2374 ILE A CB    1 
ATOM   7338  C  CG1   . ILE A 1 2374 ? 229.970 177.181 172.091 1.00 0.93  ? 2374 ILE A CG1   1 
ATOM   7339  C  CG2   . ILE A 1 2374 ? 231.871 178.829 172.184 1.00 1.26  ? 2374 ILE A CG2   1 
ATOM   7340  C  CD1   . ILE A 1 2374 ? 230.154 176.513 173.430 1.00 0.83  ? 2374 ILE A CD1   1 
ATOM   7341  N  N     . PHE A 1 2375 ? 233.147 177.576 168.827 1.00 1.82  ? 2375 PHE A N     1 
ATOM   7342  C  CA    . PHE A 1 2375 ? 234.362 177.972 168.121 1.00 1.77  ? 2375 PHE A CA    1 
ATOM   7343  C  C     . PHE A 1 2375 ? 234.035 178.696 166.822 1.00 3.24  ? 2375 PHE A C     1 
ATOM   7344  O  O     . PHE A 1 2375 ? 234.686 179.688 166.478 1.00 8.30  ? 2375 PHE A O     1 
ATOM   7345  C  CB    . PHE A 1 2375 ? 235.234 176.747 167.849 1.00 3.04  ? 2375 PHE A CB    1 
ATOM   7346  C  CG    . PHE A 1 2375 ? 235.871 176.174 169.079 1.00 2.55  ? 2375 PHE A CG    1 
ATOM   7347  C  CD1   . PHE A 1 2375 ? 235.919 176.903 170.255 1.00 2.13  ? 2375 PHE A CD1   1 
ATOM   7348  C  CD2   . PHE A 1 2375 ? 236.420 174.905 169.062 1.00 2.33  ? 2375 PHE A CD2   1 
ATOM   7349  C  CE1   . PHE A 1 2375 ? 236.501 176.378 171.384 1.00 3.11  ? 2375 PHE A CE1   1 
ATOM   7350  C  CE2   . PHE A 1 2375 ? 237.004 174.376 170.191 1.00 4.26  ? 2375 PHE A CE2   1 
ATOM   7351  C  CZ    . PHE A 1 2375 ? 237.048 175.112 171.352 1.00 3.31  ? 2375 PHE A CZ    1 
ATOM   7352  N  N     . ASN A 1 2376 ? 233.030 178.212 166.087 1.00 2.78  ? 2376 ASN A N     1 
ATOM   7353  C  CA    . ASN A 1 2376 ? 232.622 178.884 164.857 1.00 2.42  ? 2376 ASN A CA    1 
ATOM   7354  C  C     . ASN A 1 2376 ? 232.131 180.295 165.139 1.00 3.10  ? 2376 ASN A C     1 
ATOM   7355  O  O     . ASN A 1 2376 ? 232.445 181.231 164.395 1.00 4.14  ? 2376 ASN A O     1 
ATOM   7356  C  CB    . ASN A 1 2376 ? 231.527 178.082 164.153 1.00 3.10  ? 2376 ASN A CB    1 
ATOM   7357  C  CG    . ASN A 1 2376 ? 232.018 176.749 163.640 1.00 6.74  ? 2376 ASN A CG    1 
ATOM   7358  O  OD1   . ASN A 1 2376 ? 233.219 176.485 163.603 1.00 9.96  ? 2376 ASN A OD1   1 
ATOM   7359  N  ND2   . ASN A 1 2376 ? 231.084 175.892 163.246 1.00 6.55  ? 2376 ASN A ND2   1 
ATOM   7360  N  N     . ASN A 1 2377 ? 231.349 180.464 166.208 1.00 2.13  ? 2377 ASN A N     1 
ATOM   7361  C  CA    . ASN A 1 2377 ? 230.820 181.781 166.542 1.00 2.08  ? 2377 ASN A CA    1 
ATOM   7362  C  C     . ASN A 1 2377 ? 231.940 182.761 166.855 1.00 3.31  ? 2377 ASN A C     1 
ATOM   7363  O  O     . ASN A 1 2377 ? 231.911 183.912 166.408 1.00 4.66  ? 2377 ASN A O     1 
ATOM   7364  C  CB    . ASN A 1 2377 ? 229.855 181.666 167.722 1.00 2.03  ? 2377 ASN A CB    1 
ATOM   7365  C  CG    . ASN A 1 2377 ? 229.316 183.007 168.168 1.00 1.77  ? 2377 ASN A CG    1 
ATOM   7366  O  OD1   . ASN A 1 2377 ? 229.529 183.424 169.304 1.00 6.99  ? 2377 ASN A OD1   1 
ATOM   7367  N  ND2   . ASN A 1 2377 ? 228.610 183.691 167.278 1.00 1.65  ? 2377 ASN A ND2   1 
ATOM   7368  N  N     . PHE A 1 2378 ? 232.942 182.319 167.620 1.00 4.01  ? 2378 PHE A N     1 
ATOM   7369  C  CA    . PHE A 1 2378 ? 234.065 183.190 167.945 1.00 2.05  ? 2378 PHE A CA    1 
ATOM   7370  C  C     . PHE A 1 2378 ? 234.864 183.550 166.698 1.00 2.80  ? 2378 PHE A C     1 
ATOM   7371  O  O     . PHE A 1 2378 ? 235.289 184.698 166.534 1.00 3.38  ? 2378 PHE A O     1 
ATOM   7372  C  CB    . PHE A 1 2378 ? 234.953 182.520 168.993 1.00 2.16  ? 2378 PHE A CB    1 
ATOM   7373  C  CG    . PHE A 1 2378 ? 236.372 182.999 168.982 1.00 1.89  ? 2378 PHE A CG    1 
ATOM   7374  C  CD1   . PHE A 1 2378 ? 236.702 184.238 169.506 1.00 0.83  ? 2378 PHE A CD1   1 
ATOM   7375  C  CD2   . PHE A 1 2378 ? 237.380 182.212 168.451 1.00 2.50  ? 2378 PHE A CD2   1 
ATOM   7376  C  CE1   . PHE A 1 2378 ? 238.006 184.681 169.497 1.00 1.33  ? 2378 PHE A CE1   1 
ATOM   7377  C  CE2   . PHE A 1 2378 ? 238.686 182.653 168.439 1.00 2.97  ? 2378 PHE A CE2   1 
ATOM   7378  C  CZ    . PHE A 1 2378 ? 238.999 183.888 168.964 1.00 3.29  ? 2378 PHE A CZ    1 
ATOM   7379  N  N     . LEU A 1 2379 ? 235.080 182.580 165.808 1.00 2.83  ? 2379 LEU A N     1 
ATOM   7380  C  CA    . LEU A 1 2379 ? 235.838 182.854 164.591 1.00 4.35  ? 2379 LEU A CA    1 
ATOM   7381  C  C     . LEU A 1 2379 ? 235.046 183.721 163.620 1.00 6.14  ? 2379 LEU A C     1 
ATOM   7382  O  O     . LEU A 1 2379 ? 235.616 184.599 162.962 1.00 9.69  ? 2379 LEU A O     1 
ATOM   7383  C  CB    . LEU A 1 2379 ? 236.256 181.543 163.928 1.00 4.30  ? 2379 LEU A CB    1 
ATOM   7384  C  CG    . LEU A 1 2379 ? 237.423 180.827 164.607 1.00 4.04  ? 2379 LEU A CG    1 
ATOM   7385  C  CD1   . LEU A 1 2379 ? 237.751 179.535 163.893 1.00 7.12  ? 2379 LEU A CD1   1 
ATOM   7386  C  CD2   . LEU A 1 2379 ? 238.644 181.732 164.665 1.00 4.32  ? 2379 LEU A CD2   1 
ATOM   7387  N  N     . ALA A 1 2380 ? 233.737 183.488 163.508 1.00 4.83  ? 2380 ALA A N     1 
ATOM   7388  C  CA    . ALA A 1 2380 ? 232.919 184.303 162.615 1.00 2.50  ? 2380 ALA A CA    1 
ATOM   7389  C  C     . ALA A 1 2380 ? 232.899 185.758 163.063 1.00 3.98  ? 2380 ALA A C     1 
ATOM   7390  O  O     . ALA A 1 2380 ? 233.006 186.672 162.237 1.00 7.73  ? 2380 ALA A O     1 
ATOM   7391  C  CB    . ALA A 1 2380 ? 231.500 183.743 162.541 1.00 3.12  ? 2380 ALA A CB    1 
ATOM   7392  N  N     . ARG A 1 2381 ? 232.760 185.992 164.371 1.00 3.83  ? 2381 ARG A N     1 
ATOM   7393  C  CA    . ARG A 1 2381 ? 232.809 187.354 164.887 1.00 3.17  ? 2381 ARG A CA    1 
ATOM   7394  C  C     . ARG A 1 2381 ? 234.191 187.968 164.696 1.00 4.97  ? 2381 ARG A C     1 
ATOM   7395  O  O     . ARG A 1 2381 ? 234.310 189.156 164.376 1.00 5.84  ? 2381 ARG A O     1 
ATOM   7396  C  CB    . ARG A 1 2381 ? 232.411 187.375 166.362 1.00 2.41  ? 2381 ARG A CB    1 
ATOM   7397  C  CG    . ARG A 1 2381 ? 230.991 186.915 166.629 1.00 4.00  ? 2381 ARG A CG    1 
ATOM   7398  C  CD    . ARG A 1 2381 ? 230.747 186.705 168.113 1.00 2.74  ? 2381 ARG A CD    1 
ATOM   7399  N  NE    . ARG A 1 2381 ? 230.918 187.937 168.872 1.00 6.37  ? 2381 ARG A NE    1 
ATOM   7400  C  CZ    . ARG A 1 2381 ? 230.090 188.972 168.829 1.00 7.46  ? 2381 ARG A CZ    1 
ATOM   7401  N  NH1   . ARG A 1 2381 ? 228.986 188.948 168.099 1.00 7.45  ? 2381 ARG A NH1   1 
ATOM   7402  N  NH2   . ARG A 1 2381 ? 230.375 190.058 169.538 1.00 16.86 ? 2381 ARG A NH2   1 
ATOM   7403  N  N     . LEU A 1 2382 ? 235.245 187.172 164.892 1.00 3.44  ? 2382 LEU A N     1 
ATOM   7404  C  CA    . LEU A 1 2382 ? 236.601 187.681 164.720 1.00 4.91  ? 2382 LEU A CA    1 
ATOM   7405  C  C     . LEU A 1 2382 ? 236.866 188.103 163.282 1.00 8.42  ? 2382 LEU A C     1 
ATOM   7406  O  O     . LEU A 1 2382 ? 237.648 189.028 163.041 1.00 9.09  ? 2382 LEU A O     1 
ATOM   7407  C  CB    . LEU A 1 2382 ? 237.618 186.625 165.158 1.00 6.32  ? 2382 LEU A CB    1 
ATOM   7408  C  CG    . LEU A 1 2382 ? 239.080 187.072 165.212 1.00 8.86  ? 2382 LEU A CG    1 
ATOM   7409  C  CD1   . LEU A 1 2382 ? 239.266 188.192 166.221 1.00 6.13  ? 2382 LEU A CD1   1 
ATOM   7410  C  CD2   . LEU A 1 2382 ? 239.994 185.901 165.532 1.00 6.07  ? 2382 LEU A CD2   1 
ATOM   7411  N  N     . ARG A 1 2383 ? 236.222 187.447 162.318 1.00 4.91  ? 2383 ARG A N     1 
ATOM   7412  C  CA    . ARG A 1 2383 ? 236.421 187.753 160.909 1.00 4.95  ? 2383 ARG A CA    1 
ATOM   7413  C  C     . ARG A 1 2383 ? 235.504 188.854 160.393 1.00 5.75  ? 2383 ARG A C     1 
ATOM   7414  O  O     . ARG A 1 2383 ? 235.667 189.281 159.246 1.00 8.43  ? 2383 ARG A O     1 
ATOM   7415  C  CB    . ARG A 1 2383 ? 236.218 186.490 160.065 1.00 4.66  ? 2383 ARG A CB    1 
ATOM   7416  C  CG    . ARG A 1 2383 ? 237.346 185.486 160.186 1.00 7.28  ? 2383 ARG A CG    1 
ATOM   7417  C  CD    . ARG A 1 2383 ? 237.056 184.216 159.412 1.00 6.24  ? 2383 ARG A CD    1 
ATOM   7418  N  NE    . ARG A 1 2383 ? 238.277 183.474 159.124 1.00 7.70  ? 2383 ARG A NE    1 
ATOM   7419  C  CZ    . ARG A 1 2383 ? 238.534 182.251 159.569 1.00 7.43  ? 2383 ARG A CZ    1 
ATOM   7420  N  NH1   . ARG A 1 2383 ? 237.671 181.595 160.326 1.00 5.48  ? 2383 ARG A NH1   1 
ATOM   7421  N  NH2   . ARG A 1 2383 ? 239.689 181.675 159.249 1.00 8.07  ? 2383 ARG A NH2   1 
ATOM   7422  N  N     . SER A 1 2384 ? 234.557 189.317 161.193 1.00 5.99  ? 2384 SER A N     1 
ATOM   7423  C  CA    . SER A 1 2384 ? 233.597 190.297 160.701 1.00 5.75  ? 2384 SER A CA    1 
ATOM   7424  C  C     . SER A 1 2384 ? 233.514 191.555 161.553 1.00 9.48  ? 2384 SER A C     1 
ATOM   7425  O  O     . SER A 1 2384 ? 233.385 192.650 161.006 1.00 12.85 ? 2384 SER A O     1 
ATOM   7426  C  CB    . SER A 1 2384 ? 232.207 189.655 160.597 1.00 7.49  ? 2384 SER A CB    1 
ATOM   7427  O  OG    . SER A 1 2384 ? 232.252 188.456 159.844 1.00 16.79 ? 2384 SER A OG    1 
ATOM   7428  N  N     . ILE A 1 2385 ? 233.583 191.429 162.872 1.00 8.59  ? 2385 ILE A N     1 
ATOM   7429  C  CA    . ILE A 1 2385 ? 233.421 192.558 163.784 1.00 8.33  ? 2385 ILE A CA    1 
ATOM   7430  C  C     . ILE A 1 2385 ? 234.806 193.084 164.138 1.00 11.46 ? 2385 ILE A C     1 
ATOM   7431  O  O     . ILE A 1 2385 ? 235.596 192.350 164.749 1.00 10.44 ? 2385 ILE A O     1 
ATOM   7432  C  CB    . ILE A 1 2385 ? 232.644 192.160 165.047 1.00 8.76  ? 2385 ILE A CB    1 
ATOM   7433  C  CG1   . ILE A 1 2385 ? 231.350 191.438 164.667 1.00 5.35  ? 2385 ILE A CG1   1 
ATOM   7434  C  CG2   . ILE A 1 2385 ? 232.358 193.386 165.899 1.00 5.12  ? 2385 ILE A CG2   1 
ATOM   7435  C  CD1   . ILE A 1 2385 ? 230.572 190.920 165.851 1.00 5.26  ? 2385 ILE A CD1   1 
ATOM   7436  N  N     . PRO A 1 2386 ? 235.141 194.322 163.782 1.00 14.20 ? 2386 PRO A N     1 
ATOM   7437  C  CA    . PRO A 1 2386 ? 236.451 194.864 164.161 1.00 12.21 ? 2386 PRO A CA    1 
ATOM   7438  C  C     . PRO A 1 2386 ? 236.503 195.173 165.648 1.00 13.75 ? 2386 PRO A C     1 
ATOM   7439  O  O     . PRO A 1 2386 ? 235.530 195.647 166.239 1.00 25.14 ? 2386 PRO A O     1 
ATOM   7440  C  CB    . PRO A 1 2386 ? 236.569 196.139 163.317 1.00 16.66 ? 2386 PRO A CB    1 
ATOM   7441  C  CG    . PRO A 1 2386 ? 235.433 196.082 162.326 1.00 11.80 ? 2386 PRO A CG    1 
ATOM   7442  C  CD    . PRO A 1 2386 ? 234.366 195.273 162.976 1.00 8.28  ? 2386 PRO A CD    1 
ATOM   7443  N  N     . LEU A 1 2387 ? 237.655 194.888 166.254 1.00 12.43 ? 2387 LEU A N     1 
ATOM   7444  C  CA    . LEU A 1 2387 ? 237.834 195.139 167.677 1.00 9.63  ? 2387 LEU A CA    1 
ATOM   7445  C  C     . LEU A 1 2387 ? 238.115 196.602 167.991 1.00 15.20 ? 2387 LEU A C     1 
ATOM   7446  O  O     . LEU A 1 2387 ? 237.856 197.036 169.119 1.00 17.12 ? 2387 LEU A O     1 
ATOM   7447  C  CB    . LEU A 1 2387 ? 238.968 194.271 168.226 1.00 13.94 ? 2387 LEU A CB    1 
ATOM   7448  C  CG    . LEU A 1 2387 ? 238.778 192.755 168.152 1.00 12.04 ? 2387 LEU A CG    1 
ATOM   7449  C  CD1   . LEU A 1 2387 ? 240.113 192.049 168.306 1.00 9.29  ? 2387 LEU A CD1   1 
ATOM   7450  C  CD2   . LEU A 1 2387 ? 237.790 192.278 169.202 1.00 5.23  ? 2387 LEU A CD2   1 
ATOM   7451  N  N     . ASP A 1 2388 ? 238.640 197.366 167.029 1.00 21.61 ? 2388 ASP A N     1 
ATOM   7452  C  CA    . ASP A 1 2388 ? 238.987 198.760 167.297 1.00 18.04 ? 2388 ASP A CA    1 
ATOM   7453  C  C     . ASP A 1 2388 ? 237.749 199.596 167.595 1.00 25.47 ? 2388 ASP A C     1 
ATOM   7454  O  O     . ASP A 1 2388 ? 237.772 200.447 168.493 1.00 30.18 ? 2388 ASP A O     1 
ATOM   7455  C  CB    . ASP A 1 2388 ? 239.770 199.346 166.122 1.00 16.23 ? 2388 ASP A CB    1 
ATOM   7456  C  CG    . ASP A 1 2388 ? 239.017 199.254 164.810 1.00 30.47 ? 2388 ASP A CG    1 
ATOM   7457  O  OD1   . ASP A 1 2388 ? 238.733 198.124 164.366 1.00 32.82 ? 2388 ASP A OD1   1 
ATOM   7458  O  OD2   . ASP A 1 2388 ? 238.710 200.312 164.222 1.00 41.17 ? 2388 ASP A OD2   1 
ATOM   7459  N  N     . SER A 1 2410 ? 239.596 196.985 156.752 1.00 20.88 ? 2410 SER A N     1 
ATOM   7460  C  CA    . SER A 1 2410 ? 240.099 197.663 157.940 1.00 19.98 ? 2410 SER A CA    1 
ATOM   7461  C  C     . SER A 1 2410 ? 241.426 197.067 158.379 1.00 22.24 ? 2410 SER A C     1 
ATOM   7462  O  O     . SER A 1 2410 ? 241.587 195.847 158.395 1.00 20.14 ? 2410 SER A O     1 
ATOM   7463  C  CB    . SER A 1 2410 ? 239.083 197.578 159.079 1.00 19.54 ? 2410 SER A CB    1 
ATOM   7464  O  OG    . SER A 1 2410 ? 239.605 198.142 160.271 1.00 19.95 ? 2410 SER A OG    1 
ATOM   7465  N  N     . PRO A 1 2411 ? 242.386 197.928 158.727 1.00 21.35 ? 2411 PRO A N     1 
ATOM   7466  C  CA    . PRO A 1 2411 ? 243.679 197.418 159.206 1.00 20.40 ? 2411 PRO A CA    1 
ATOM   7467  C  C     . PRO A 1 2411 ? 243.554 196.558 160.449 1.00 16.34 ? 2411 PRO A C     1 
ATOM   7468  O  O     . PRO A 1 2411 ? 244.311 195.590 160.602 1.00 20.64 ? 2411 PRO A O     1 
ATOM   7469  C  CB    . PRO A 1 2411 ? 244.482 198.698 159.473 1.00 14.98 ? 2411 PRO A CB    1 
ATOM   7470  C  CG    . PRO A 1 2411 ? 243.449 199.748 159.702 1.00 17.23 ? 2411 PRO A CG    1 
ATOM   7471  C  CD    . PRO A 1 2411 ? 242.309 199.396 158.796 1.00 15.68 ? 2411 PRO A CD    1 
ATOM   7472  N  N     . MET A 1 2412 ? 242.618 196.878 161.342 1.00 14.07 ? 2412 MET A N     1 
ATOM   7473  C  CA    . MET A 1 2412 ? 242.393 196.035 162.511 1.00 15.88 ? 2412 MET A CA    1 
ATOM   7474  C  C     . MET A 1 2412 ? 241.689 194.739 162.126 1.00 13.98 ? 2412 MET A C     1 
ATOM   7475  O  O     . MET A 1 2412 ? 242.062 193.659 162.598 1.00 12.70 ? 2412 MET A O     1 
ATOM   7476  C  CB    . MET A 1 2412 ? 241.583 196.799 163.557 1.00 16.45 ? 2412 MET A CB    1 
ATOM   7477  C  CG    . MET A 1 2412 ? 241.424 196.069 164.875 1.00 17.95 ? 2412 MET A CG    1 
ATOM   7478  S  SD    . MET A 1 2412 ? 243.008 195.621 165.606 1.00 26.27 ? 2412 MET A SD    1 
ATOM   7479  C  CE    . MET A 1 2412 ? 242.649 193.981 166.214 1.00 12.56 ? 2412 MET A CE    1 
ATOM   7480  N  N     . LEU A 1 2413 ? 240.670 194.826 161.266 1.00 14.74 ? 2413 LEU A N     1 
ATOM   7481  C  CA    . LEU A 1 2413 ? 239.985 193.629 160.790 1.00 12.58 ? 2413 LEU A CA    1 
ATOM   7482  C  C     . LEU A 1 2413 ? 240.920 192.732 159.989 1.00 12.66 ? 2413 LEU A C     1 
ATOM   7483  O  O     . LEU A 1 2413 ? 240.818 191.502 160.061 1.00 15.41 ? 2413 LEU A O     1 
ATOM   7484  C  CB    . LEU A 1 2413 ? 238.766 194.017 159.956 1.00 13.64 ? 2413 LEU A CB    1 
ATOM   7485  C  CG    . LEU A 1 2413 ? 237.637 192.989 159.883 1.00 11.53 ? 2413 LEU A CG    1 
ATOM   7486  C  CD1   . LEU A 1 2413 ? 236.813 192.973 161.153 1.00 10.99 ? 2413 LEU A CD1   1 
ATOM   7487  C  CD2   . LEU A 1 2413 ? 236.755 193.287 158.688 1.00 13.81 ? 2413 LEU A CD2   1 
ATOM   7488  N  N     . GLN A 1 2414 ? 241.827 193.327 159.213 1.00 15.28 ? 2414 GLN A N     1 
ATOM   7489  C  CA    . GLN A 1 2414 ? 242.778 192.529 158.448 1.00 14.69 ? 2414 GLN A CA    1 
ATOM   7490  C  C     . GLN A 1 2414 ? 243.680 191.716 159.366 1.00 15.75 ? 2414 GLN A C     1 
ATOM   7491  O  O     . GLN A 1 2414 ? 244.040 190.578 159.044 1.00 21.62 ? 2414 GLN A O     1 
ATOM   7492  C  CB    . GLN A 1 2414 ? 243.609 193.433 157.535 1.00 19.06 ? 2414 GLN A CB    1 
ATOM   7493  C  CG    . GLN A 1 2414 ? 244.334 192.726 156.380 1.00 19.65 ? 2414 GLN A CG    1 
ATOM   7494  C  CD    . GLN A 1 2414 ? 243.562 191.568 155.756 1.00 19.74 ? 2414 GLN A CD    1 
ATOM   7495  O  OE1   . GLN A 1 2414 ? 242.332 191.577 155.680 1.00 20.08 ? 2414 GLN A OE1   1 
ATOM   7496  N  NE2   . GLN A 1 2414 ? 244.294 190.557 155.306 1.00 23.19 ? 2414 GLN A NE2   1 
ATOM   7497  N  N     . ILE A 1 2415 ? 244.072 192.289 160.505 1.00 14.11 ? 2415 ILE A N     1 
ATOM   7498  C  CA    . ILE A 1 2415 ? 244.855 191.536 161.479 1.00 13.16 ? 2415 ILE A CA    1 
ATOM   7499  C  C     . ILE A 1 2415 ? 244.032 190.394 162.058 1.00 12.62 ? 2415 ILE A C     1 
ATOM   7500  O  O     . ILE A 1 2415 ? 244.516 189.264 162.188 1.00 16.96 ? 2415 ILE A O     1 
ATOM   7501  C  CB    . ILE A 1 2415 ? 245.385 192.469 162.582 1.00 17.19 ? 2415 ILE A CB    1 
ATOM   7502  C  CG1   . ILE A 1 2415 ? 246.485 193.371 162.027 1.00 11.93 ? 2415 ILE A CG1   1 
ATOM   7503  C  CG2   . ILE A 1 2415 ? 245.898 191.665 163.769 1.00 11.53 ? 2415 ILE A CG2   1 
ATOM   7504  C  CD1   . ILE A 1 2415 ? 247.050 194.326 163.043 1.00 10.34 ? 2415 ILE A CD1   1 
ATOM   7505  N  N     . GLN A 1 2416 ? 242.774 190.668 162.412 1.00 11.77 ? 2416 GLN A N     1 
ATOM   7506  C  CA    . GLN A 1 2416 ? 241.912 189.627 162.960 1.00 5.98  ? 2416 GLN A CA    1 
ATOM   7507  C  C     . GLN A 1 2416 ? 241.675 188.515 161.945 1.00 10.48 ? 2416 GLN A C     1 
ATOM   7508  O  O     . GLN A 1 2416 ? 241.687 187.331 162.299 1.00 10.42 ? 2416 GLN A O     1 
ATOM   7509  C  CB    . GLN A 1 2416 ? 240.583 190.227 163.413 1.00 7.63  ? 2416 GLN A CB    1 
ATOM   7510  C  CG    . GLN A 1 2416 ? 240.709 191.343 164.436 1.00 8.20  ? 2416 GLN A CG    1 
ATOM   7511  C  CD    . GLN A 1 2416 ? 239.425 192.134 164.599 1.00 7.88  ? 2416 GLN A CD    1 
ATOM   7512  O  OE1   . GLN A 1 2416 ? 239.450 193.333 164.862 1.00 13.46 ? 2416 GLN A OE1   1 
ATOM   7513  N  NE2   . GLN A 1 2416 ? 238.293 191.459 164.445 1.00 10.16 ? 2416 GLN A NE2   1 
ATOM   7514  N  N     . ARG A 1 2417 ? 241.458 188.877 160.678 1.00 13.61 ? 2417 ARG A N     1 
ATOM   7515  C  CA    . ARG A 1 2417 ? 241.195 187.872 159.655 1.00 11.88 ? 2417 ARG A CA    1 
ATOM   7516  C  C     . ARG A 1 2417 ? 242.401 186.968 159.439 1.00 10.82 ? 2417 ARG A C     1 
ATOM   7517  O  O     . ARG A 1 2417 ? 242.258 185.745 159.340 1.00 12.30 ? 2417 ARG A O     1 
ATOM   7518  C  CB    . ARG A 1 2417 ? 240.787 188.551 158.347 1.00 10.93 ? 2417 ARG A CB    1 
ATOM   7519  C  CG    . ARG A 1 2417 ? 239.400 189.158 158.389 1.00 11.31 ? 2417 ARG A CG    1 
ATOM   7520  C  CD    . ARG A 1 2417 ? 238.800 189.281 157.004 1.00 12.05 ? 2417 ARG A CD    1 
ATOM   7521  N  NE    . ARG A 1 2417 ? 237.403 189.692 157.061 1.00 11.31 ? 2417 ARG A NE    1 
ATOM   7522  C  CZ    . ARG A 1 2417 ? 236.894 190.715 156.389 1.00 9.78  ? 2417 ARG A CZ    1 
ATOM   7523  N  NH1   . ARG A 1 2417 ? 237.639 191.452 155.582 1.00 11.87 ? 2417 ARG A NH1   1 
ATOM   7524  N  NH2   . ARG A 1 2417 ? 235.604 191.005 156.530 1.00 9.46  ? 2417 ARG A NH2   1 
ATOM   7525  N  N     . ASP A 1 2418 ? 243.600 187.553 159.360 1.00 15.30 ? 2418 ASP A N     1 
ATOM   7526  C  CA    . ASP A 1 2418 ? 244.806 186.739 159.244 1.00 12.81 ? 2418 ASP A CA    1 
ATOM   7527  C  C     . ASP A 1 2418 ? 245.027 185.905 160.499 1.00 11.37 ? 2418 ASP A C     1 
ATOM   7528  O  O     . ASP A 1 2418 ? 245.448 184.746 160.412 1.00 10.20 ? 2418 ASP A O     1 
ATOM   7529  C  CB    . ASP A 1 2418 ? 246.019 187.625 158.967 1.00 16.11 ? 2418 ASP A CB    1 
ATOM   7530  C  CG    . ASP A 1 2418 ? 245.982 188.250 157.587 1.00 29.21 ? 2418 ASP A CG    1 
ATOM   7531  O  OD1   . ASP A 1 2418 ? 245.396 187.639 156.670 1.00 32.15 ? 2418 ASP A OD1   1 
ATOM   7532  O  OD2   . ASP A 1 2418 ? 246.546 189.351 157.417 1.00 31.99 ? 2418 ASP A OD2   1 
ATOM   7533  N  N     . ALA A 1 2419 ? 244.753 186.478 161.671 1.00 11.21 ? 2419 ALA A N     1 
ATOM   7534  C  CA    . ALA A 1 2419 ? 244.878 185.724 162.914 1.00 10.42 ? 2419 ALA A CA    1 
ATOM   7535  C  C     . ALA A 1 2419 ? 243.845 184.607 162.990 1.00 10.15 ? 2419 ALA A C     1 
ATOM   7536  O  O     . ALA A 1 2419 ? 244.121 183.535 163.541 1.00 13.37 ? 2419 ALA A O     1 
ATOM   7537  C  CB    . ALA A 1 2419 ? 244.746 186.664 164.111 1.00 9.32  ? 2419 ALA A CB    1 
ATOM   7538  N  N     . ALA A 1 2420 ? 242.646 184.843 162.449 1.00 10.64 ? 2420 ALA A N     1 
ATOM   7539  C  CA    . ALA A 1 2420 ? 241.621 183.804 162.432 1.00 9.78  ? 2420 ALA A CA    1 
ATOM   7540  C  C     . ALA A 1 2420 ? 242.066 182.605 161.608 1.00 9.25  ? 2420 ALA A C     1 
ATOM   7541  O  O     . ALA A 1 2420 ? 241.803 181.455 161.979 1.00 9.70  ? 2420 ALA A O     1 
ATOM   7542  C  CB    . ALA A 1 2420 ? 240.310 184.369 161.893 1.00 7.08  ? 2420 ALA A CB    1 
ATOM   7543  N  N     . THR A 1 2421 ? 242.739 182.854 160.481 1.00 7.75  ? 2421 THR A N     1 
ATOM   7544  C  CA    . THR A 1 2421 ? 243.251 181.760 159.665 1.00 8.73  ? 2421 THR A CA    1 
ATOM   7545  C  C     . THR A 1 2421 ? 244.285 180.945 160.426 1.00 11.25 ? 2421 THR A C     1 
ATOM   7546  O  O     . THR A 1 2421 ? 244.329 179.715 160.308 1.00 17.53 ? 2421 THR A O     1 
ATOM   7547  C  CB    . THR A 1 2421 ? 243.848 182.308 158.367 1.00 12.11 ? 2421 THR A CB    1 
ATOM   7548  O  OG1   . THR A 1 2421 ? 242.905 183.184 157.736 1.00 12.55 ? 2421 THR A OG1   1 
ATOM   7549  C  CG2   . THR A 1 2421 ? 244.192 181.174 157.418 1.00 14.44 ? 2421 THR A CG2   1 
ATOM   7550  N  N     . ILE A 1 2422 ? 245.130 181.615 161.211 1.00 8.28  ? 2422 ILE A N     1 
ATOM   7551  C  CA    . ILE A 1 2422 ? 246.141 180.916 161.998 1.00 9.65  ? 2422 ILE A CA    1 
ATOM   7552  C  C     . ILE A 1 2422 ? 245.493 180.093 163.106 1.00 9.47  ? 2422 ILE A C     1 
ATOM   7553  O  O     . ILE A 1 2422 ? 245.905 178.958 163.373 1.00 10.94 ? 2422 ILE A O     1 
ATOM   7554  C  CB    . ILE A 1 2422 ? 247.158 181.926 162.560 1.00 13.73 ? 2422 ILE A CB    1 
ATOM   7555  C  CG1   . ILE A 1 2422 ? 247.741 182.771 161.428 1.00 10.89 ? 2422 ILE A CG1   1 
ATOM   7556  C  CG2   . ILE A 1 2422 ? 248.265 181.209 163.316 1.00 13.46 ? 2422 ILE A CG2   1 
ATOM   7557  C  CD1   . ILE A 1 2422 ? 248.469 184.002 161.900 1.00 10.33 ? 2422 ILE A CD1   1 
ATOM   7558  N  N     . MET A 1 2423 ? 244.476 180.648 163.773 1.00 8.11  ? 2423 MET A N     1 
ATOM   7559  C  CA    . MET A 1 2423 ? 243.844 179.933 164.878 1.00 8.30  ? 2423 MET A CA    1 
ATOM   7560  C  C     . MET A 1 2423 ? 242.955 178.797 164.395 1.00 12.35 ? 2423 MET A C     1 
ATOM   7561  O  O     . MET A 1 2423 ? 242.674 177.867 165.159 1.00 18.46 ? 2423 MET A O     1 
ATOM   7562  C  CB    . MET A 1 2423 ? 243.011 180.885 165.739 1.00 9.33  ? 2423 MET A CB    1 
ATOM   7563  C  CG    . MET A 1 2423 ? 243.791 181.922 166.511 1.00 11.90 ? 2423 MET A CG    1 
ATOM   7564  S  SD    . MET A 1 2423 ? 242.677 183.113 167.280 1.00 20.84 ? 2423 MET A SD    1 
ATOM   7565  C  CE    . MET A 1 2423 ? 243.448 184.659 166.829 1.00 14.98 ? 2423 MET A CE    1 
ATOM   7566  N  N     . GLN A 1 2424 ? 242.501 178.855 163.144 1.00 11.68 ? 2424 GLN A N     1 
ATOM   7567  C  CA    . GLN A 1 2424 ? 241.493 177.919 162.643 1.00 11.73 ? 2424 GLN A CA    1 
ATOM   7568  C  C     . GLN A 1 2424 ? 241.865 176.451 162.818 1.00 10.95 ? 2424 GLN A C     1 
ATOM   7569  O  O     . GLN A 1 2424 ? 241.001 175.676 163.260 1.00 12.12 ? 2424 GLN A O     1 
ATOM   7570  C  CB    . GLN A 1 2424 ? 241.204 178.246 161.170 1.00 12.02 ? 2424 GLN A CB    1 
ATOM   7571  C  CG    . GLN A 1 2424 ? 240.091 177.425 160.549 1.00 11.02 ? 2424 GLN A CG    1 
ATOM   7572  C  CD    . GLN A 1 2424 ? 238.723 178.037 160.776 1.00 13.42 ? 2424 GLN A CD    1 
ATOM   7573  O  OE1   . GLN A 1 2424 ? 238.446 179.142 160.314 1.00 19.54 ? 2424 GLN A OE1   1 
ATOM   7574  N  NE2   . GLN A 1 2424 ? 237.860 177.320 161.483 1.00 9.28  ? 2424 GLN A NE2   1 
ATOM   7575  N  N     . PRO A 1 2425 ? 243.087 175.997 162.500 1.00 12.40 ? 2425 PRO A N     1 
ATOM   7576  C  CA    . PRO A 1 2425 ? 243.392 174.566 162.691 1.00 8.05  ? 2425 PRO A CA    1 
ATOM   7577  C  C     . PRO A 1 2425 ? 243.231 174.083 164.122 1.00 10.47 ? 2425 PRO A C     1 
ATOM   7578  O  O     . PRO A 1 2425 ? 242.808 172.942 164.340 1.00 18.30 ? 2425 PRO A O     1 
ATOM   7579  C  CB    . PRO A 1 2425 ? 244.850 174.459 162.221 1.00 7.72  ? 2425 PRO A CB    1 
ATOM   7580  C  CG    . PRO A 1 2425 ? 245.018 175.573 161.275 1.00 6.42  ? 2425 PRO A CG    1 
ATOM   7581  C  CD    . PRO A 1 2425 ? 244.201 176.694 161.831 1.00 8.41  ? 2425 PRO A CD    1 
ATOM   7582  N  N     . TYR A 1 2426 ? 243.558 174.917 165.107 1.00 11.76 ? 2426 TYR A N     1 
ATOM   7583  C  CA    . TYR A 1 2426 ? 243.477 174.510 166.504 1.00 7.97  ? 2426 TYR A CA    1 
ATOM   7584  C  C     . TYR A 1 2426 ? 242.067 174.574 167.070 1.00 9.49  ? 2426 TYR A C     1 
ATOM   7585  O  O     . TYR A 1 2426 ? 241.827 174.011 168.143 1.00 12.99 ? 2426 TYR A O     1 
ATOM   7586  C  CB    . TYR A 1 2426 ? 244.410 175.373 167.354 1.00 12.27 ? 2426 TYR A CB    1 
ATOM   7587  C  CG    . TYR A 1 2426 ? 245.811 175.462 166.805 1.00 9.20  ? 2426 TYR A CG    1 
ATOM   7588  C  CD1   . TYR A 1 2426 ? 246.210 176.540 166.027 1.00 10.01 ? 2426 TYR A CD1   1 
ATOM   7589  C  CD2   . TYR A 1 2426 ? 246.734 174.461 167.061 1.00 7.30  ? 2426 TYR A CD2   1 
ATOM   7590  C  CE1   . TYR A 1 2426 ? 247.490 176.614 165.522 1.00 10.19 ? 2426 TYR A CE1   1 
ATOM   7591  C  CE2   . TYR A 1 2426 ? 248.013 174.528 166.563 1.00 8.30  ? 2426 TYR A CE2   1 
ATOM   7592  C  CZ    . TYR A 1 2426 ? 248.387 175.604 165.794 1.00 13.22 ? 2426 TYR A CZ    1 
ATOM   7593  O  OH    . TYR A 1 2426 ? 249.667 175.664 165.301 1.00 21.45 ? 2426 TYR A OH    1 
ATOM   7594  N  N     . PHE A 1 2427 ? 241.137 175.230 166.385 1.00 11.10 ? 2427 PHE A N     1 
ATOM   7595  C  CA    . PHE A 1 2427 ? 239.766 175.358 166.855 1.00 10.00 ? 2427 PHE A CA    1 
ATOM   7596  C  C     . PHE A 1 2427 ? 238.816 174.390 166.165 1.00 9.53  ? 2427 PHE A C     1 
ATOM   7597  O  O     . PHE A 1 2427 ? 237.597 174.559 166.261 1.00 20.91 ? 2427 PHE A O     1 
ATOM   7598  C  CB    . PHE A 1 2427 ? 239.279 176.795 166.674 1.00 8.88  ? 2427 PHE A CB    1 
ATOM   7599  C  CG    . PHE A 1 2427 ? 239.703 177.712 167.777 1.00 7.51  ? 2427 PHE A CG    1 
ATOM   7600  C  CD1   . PHE A 1 2427 ? 239.078 177.665 169.010 1.00 4.89  ? 2427 PHE A CD1   1 
ATOM   7601  C  CD2   . PHE A 1 2427 ? 240.737 178.612 167.590 1.00 9.00  ? 2427 PHE A CD2   1 
ATOM   7602  C  CE1   . PHE A 1 2427 ? 239.468 178.503 170.029 1.00 6.49  ? 2427 PHE A CE1   1 
ATOM   7603  C  CE2   . PHE A 1 2427 ? 241.133 179.454 168.608 1.00 5.54  ? 2427 PHE A CE2   1 
ATOM   7604  C  CZ    . PHE A 1 2427 ? 240.496 179.400 169.828 1.00 2.99  ? 2427 PHE A CZ    1 
ATOM   7605  N  N     . THR A 1 2428 ? 239.344 173.397 165.461 1.00 13.66 ? 2428 THR A N     1 
ATOM   7606  C  CA    . THR A 1 2428 ? 238.513 172.342 164.907 1.00 16.24 ? 2428 THR A CA    1 
ATOM   7607  C  C     . THR A 1 2428 ? 238.147 171.338 165.995 1.00 17.10 ? 2428 THR A C     1 
ATOM   7608  O  O     . THR A 1 2428 ? 238.757 171.294 167.067 1.00 21.27 ? 2428 THR A O     1 
ATOM   7609  C  CB    . THR A 1 2428 ? 239.234 171.625 163.766 1.00 15.37 ? 2428 THR A CB    1 
ATOM   7610  O  OG1   . THR A 1 2428 ? 240.293 170.823 164.302 1.00 15.11 ? 2428 THR A OG1   1 
ATOM   7611  C  CG2   . THR A 1 2428 ? 239.813 172.633 162.784 1.00 11.20 ? 2428 THR A CG2   1 
ATOM   7612  N  N     . SER A 1 2429 ? 237.129 170.530 165.708 1.00 21.28 ? 2429 SER A N     1 
ATOM   7613  C  CA    . SER A 1 2429 ? 236.761 169.456 166.620 1.00 15.94 ? 2429 SER A CA    1 
ATOM   7614  C  C     . SER A 1 2429 ? 237.909 168.461 166.742 1.00 20.14 ? 2429 SER A C     1 
ATOM   7615  O  O     . SER A 1 2429 ? 238.568 168.126 165.754 1.00 24.58 ? 2429 SER A O     1 
ATOM   7616  C  CB    . SER A 1 2429 ? 235.494 168.753 166.128 1.00 24.19 ? 2429 SER A CB    1 
ATOM   7617  O  OG    . SER A 1 2429 ? 235.667 168.254 164.814 1.00 30.48 ? 2429 SER A OG    1 
ATOM   7618  N  N     . ASN A 1 2430 ? 238.145 167.991 167.969 1.00 18.30 ? 2430 ASN A N     1 
ATOM   7619  C  CA    . ASN A 1 2430 ? 239.307 167.160 168.296 1.00 15.04 ? 2430 ASN A CA    1 
ATOM   7620  C  C     . ASN A 1 2430 ? 240.615 167.891 168.014 1.00 16.80 ? 2430 ASN A C     1 
ATOM   7621  O  O     . ASN A 1 2430 ? 241.622 167.273 167.656 1.00 20.22 ? 2430 ASN A O     1 
ATOM   7622  C  CB    . ASN A 1 2430 ? 239.272 165.818 167.557 1.00 17.57 ? 2430 ASN A CB    1 
ATOM   7623  C  CG    . ASN A 1 2430 ? 238.112 164.948 167.986 1.00 25.11 ? 2430 ASN A CG    1 
ATOM   7624  O  OD1   . ASN A 1 2430 ? 237.328 165.325 168.854 1.00 21.56 ? 2430 ASN A OD1   1 
ATOM   7625  N  ND2   . ASN A 1 2430 ? 237.995 163.773 167.377 1.00 24.73 ? 2430 ASN A ND2   1 
ATOM   7626  N  N     . GLY A 1 2431 ? 240.607 169.212 168.165 1.00 13.97 ? 2431 GLY A N     1 
ATOM   7627  C  CA    . GLY A 1 2431 ? 241.802 170.015 168.031 1.00 9.44  ? 2431 GLY A CA    1 
ATOM   7628  C  C     . GLY A 1 2431 ? 242.504 170.213 169.361 1.00 11.35 ? 2431 GLY A C     1 
ATOM   7629  O  O     . GLY A 1 2431 ? 242.226 169.542 170.356 1.00 12.20 ? 2431 GLY A O     1 
ATOM   7630  N  N     . LEU A 1 2432 ? 243.444 171.158 169.363 1.00 10.82 ? 2432 LEU A N     1 
ATOM   7631  C  CA    . LEU A 1 2432 ? 244.211 171.439 170.571 1.00 5.70  ? 2432 LEU A CA    1 
ATOM   7632  C  C     . LEU A 1 2432 ? 243.316 171.962 171.689 1.00 6.14  ? 2432 LEU A C     1 
ATOM   7633  O  O     . LEU A 1 2432 ? 243.405 171.509 172.834 1.00 11.13 ? 2432 LEU A O     1 
ATOM   7634  C  CB    . LEU A 1 2432 ? 245.323 172.440 170.258 1.00 4.78  ? 2432 LEU A CB    1 
ATOM   7635  C  CG    . LEU A 1 2432 ? 246.122 172.967 171.449 1.00 5.37  ? 2432 LEU A CG    1 
ATOM   7636  C  CD1   . LEU A 1 2432 ? 246.964 171.860 172.062 1.00 11.70 ? 2432 LEU A CD1   1 
ATOM   7637  C  CD2   . LEU A 1 2432 ? 246.994 174.132 171.027 1.00 8.82  ? 2432 LEU A CD2   1 
ATOM   7638  N  N     . VAL A 1 2433 ? 242.437 172.913 171.369 1.00 6.96  ? 2433 VAL A N     1 
ATOM   7639  C  CA    . VAL A 1 2433 ? 241.615 173.537 172.400 1.00 3.68  ? 2433 VAL A CA    1 
ATOM   7640  C  C     . VAL A 1 2433 ? 240.594 172.547 172.946 1.00 5.49  ? 2433 VAL A C     1 
ATOM   7641  O  O     . VAL A 1 2433 ? 240.300 172.539 174.148 1.00 6.68  ? 2433 VAL A O     1 
ATOM   7642  C  CB    . VAL A 1 2433 ? 240.940 174.806 171.846 1.00 4.37  ? 2433 VAL A CB    1 
ATOM   7643  C  CG1   . VAL A 1 2433 ? 240.154 175.503 172.935 1.00 3.11  ? 2433 VAL A CG1   1 
ATOM   7644  C  CG2   . VAL A 1 2433 ? 241.977 175.738 171.249 1.00 6.14  ? 2433 VAL A CG2   1 
ATOM   7645  N  N     . THR A 1 2434 ? 240.030 171.704 172.079 1.00 10.88 ? 2434 THR A N     1 
ATOM   7646  C  CA    . THR A 1 2434 ? 239.064 170.709 172.532 1.00 6.25  ? 2434 THR A CA    1 
ATOM   7647  C  C     . THR A 1 2434 ? 239.712 169.704 173.477 1.00 6.40  ? 2434 THR A C     1 
ATOM   7648  O  O     . THR A 1 2434 ? 239.157 169.382 174.533 1.00 7.04  ? 2434 THR A O     1 
ATOM   7649  C  CB    . THR A 1 2434 ? 238.439 170.001 171.329 1.00 10.42 ? 2434 THR A CB    1 
ATOM   7650  O  OG1   . THR A 1 2434 ? 237.770 170.961 170.502 1.00 15.33 ? 2434 THR A OG1   1 
ATOM   7651  C  CG2   . THR A 1 2434 ? 237.434 168.956 171.783 1.00 8.20  ? 2434 THR A CG2   1 
ATOM   7652  N  N     . LYS A 1 2435 ? 240.894 169.198 173.113 1.00 6.67  ? 2435 LYS A N     1 
ATOM   7653  C  CA    . LYS A 1 2435 ? 241.581 168.243 173.976 1.00 5.67  ? 2435 LYS A CA    1 
ATOM   7654  C  C     . LYS A 1 2435 ? 242.024 168.890 175.280 1.00 6.46  ? 2435 LYS A C     1 
ATOM   7655  O  O     . LYS A 1 2435 ? 241.952 168.267 176.347 1.00 7.44  ? 2435 LYS A O     1 
ATOM   7656  C  CB    . LYS A 1 2435 ? 242.781 167.634 173.250 1.00 8.15  ? 2435 LYS A CB    1 
ATOM   7657  C  CG    . LYS A 1 2435 ? 242.417 166.752 172.073 1.00 10.54 ? 2435 LYS A CG    1 
ATOM   7658  C  CD    . LYS A 1 2435 ? 243.644 166.055 171.510 1.00 11.38 ? 2435 LYS A CD    1 
ATOM   7659  C  CE    . LYS A 1 2435 ? 244.523 167.014 170.735 1.00 19.74 ? 2435 LYS A CE    1 
ATOM   7660  N  NZ    . LYS A 1 2435 ? 245.668 166.310 170.092 1.00 26.56 ? 2435 LYS A NZ    1 
ATOM   7661  N  N     . ALA A 1 2436 ? 242.495 170.136 175.214 1.00 8.76  ? 2436 ALA A N     1 
ATOM   7662  C  CA    . ALA A 1 2436 ? 242.879 170.848 176.428 1.00 3.07  ? 2436 ALA A CA    1 
ATOM   7663  C  C     . ALA A 1 2436 ? 241.679 171.054 177.344 1.00 2.83  ? 2436 ALA A C     1 
ATOM   7664  O  O     . ALA A 1 2436 ? 241.794 170.921 178.568 1.00 6.07  ? 2436 ALA A O     1 
ATOM   7665  C  CB    . ALA A 1 2436 ? 243.517 172.188 176.069 1.00 3.67  ? 2436 ALA A CB    1 
ATOM   7666  N  N     . LEU A 1 2437 ? 240.522 171.383 176.768 1.00 2.81  ? 2437 LEU A N     1 
ATOM   7667  C  CA    . LEU A 1 2437 ? 239.323 171.607 177.569 1.00 3.47  ? 2437 LEU A CA    1 
ATOM   7668  C  C     . LEU A 1 2437 ? 238.895 170.337 178.293 1.00 5.34  ? 2437 LEU A C     1 
ATOM   7669  O  O     . LEU A 1 2437 ? 238.541 170.373 179.477 1.00 5.17  ? 2437 LEU A O     1 
ATOM   7670  C  CB    . LEU A 1 2437 ? 238.195 172.129 176.678 1.00 3.91  ? 2437 LEU A CB    1 
ATOM   7671  C  CG    . LEU A 1 2437 ? 236.934 172.629 177.381 1.00 6.61  ? 2437 LEU A CG    1 
ATOM   7672  C  CD1   . LEU A 1 2437 ? 237.266 173.777 178.319 1.00 8.67  ? 2437 LEU A CD1   1 
ATOM   7673  C  CD2   . LEU A 1 2437 ? 235.897 173.050 176.357 1.00 6.87  ? 2437 LEU A CD2   1 
ATOM   7674  N  N     . GLU A 1 2438 ? 238.931 169.197 177.598 1.00 5.68  ? 2438 GLU A N     1 
ATOM   7675  C  CA    . GLU A 1 2438 ? 238.541 167.934 178.218 1.00 10.37 ? 2438 GLU A CA    1 
ATOM   7676  C  C     . GLU A 1 2438 ? 239.470 167.575 179.371 1.00 7.60  ? 2438 GLU A C     1 
ATOM   7677  O  O     . GLU A 1 2438 ? 239.024 167.081 180.414 1.00 6.30  ? 2438 GLU A O     1 
ATOM   7678  C  CB    . GLU A 1 2438 ? 238.525 166.820 177.170 1.00 7.95  ? 2438 GLU A CB    1 
ATOM   7679  C  CG    . GLU A 1 2438 ? 237.461 166.990 176.100 1.00 18.79 ? 2438 GLU A CG    1 
ATOM   7680  C  CD    . GLU A 1 2438 ? 236.050 166.863 176.647 1.00 29.60 ? 2438 GLU A CD    1 
ATOM   7681  O  OE1   . GLU A 1 2438 ? 235.850 166.100 177.616 1.00 31.60 ? 2438 GLU A OE1   1 
ATOM   7682  O  OE2   . GLU A 1 2438 ? 235.142 167.530 176.111 1.00 34.40 ? 2438 GLU A OE2   1 
ATOM   7683  N  N     . HIS A 1 2439 ? 240.771 167.811 179.197 1.00 4.65  ? 2439 HIS A N     1 
ATOM   7684  C  CA    . HIS A 1 2439 ? 241.726 167.510 180.258 1.00 6.72  ? 2439 HIS A CA    1 
ATOM   7685  C  C     . HIS A 1 2439 ? 241.555 168.451 181.443 1.00 6.63  ? 2439 HIS A C     1 
ATOM   7686  O  O     . HIS A 1 2439 ? 241.741 168.050 182.597 1.00 6.03  ? 2439 HIS A O     1 
ATOM   7687  C  CB    . HIS A 1 2439 ? 243.150 167.590 179.714 1.00 9.28  ? 2439 HIS A CB    1 
ATOM   7688  C  CG    . HIS A 1 2439 ? 244.188 167.083 180.661 1.00 10.56 ? 2439 HIS A CG    1 
ATOM   7689  N  ND1   . HIS A 1 2439 ? 244.288 165.755 181.016 1.00 8.70  ? 2439 HIS A ND1   1 
ATOM   7690  C  CD2   . HIS A 1 2439 ? 245.177 167.725 181.329 1.00 14.87 ? 2439 HIS A CD2   1 
ATOM   7691  C  CE1   . HIS A 1 2439 ? 245.290 165.601 181.864 1.00 13.49 ? 2439 HIS A CE1   1 
ATOM   7692  N  NE2   . HIS A 1 2439 ? 245.847 166.781 182.068 1.00 11.13 ? 2439 HIS A NE2   1 
ATOM   7693  N  N     . ALA A 1 2440 ? 241.204 169.712 181.176 1.00 6.89  ? 2440 ALA A N     1 
ATOM   7694  C  CA    . ALA A 1 2440 ? 241.057 170.688 182.251 1.00 3.70  ? 2440 ALA A CA    1 
ATOM   7695  C  C     . ALA A 1 2440 ? 239.926 170.308 183.198 1.00 3.13  ? 2440 ALA A C     1 
ATOM   7696  O  O     . ALA A 1 2440 ? 240.022 170.534 184.410 1.00 4.59  ? 2440 ALA A O     1 
ATOM   7697  C  CB    . ALA A 1 2440 ? 240.827 172.080 181.664 1.00 3.87  ? 2440 ALA A CB    1 
ATOM   7698  N  N     . PHE A 1 2441 ? 238.842 169.738 182.665 1.00 3.98  ? 2441 PHE A N     1 
ATOM   7699  C  CA    . PHE A 1 2441 ? 237.729 169.329 183.517 1.00 5.14  ? 2441 PHE A CA    1 
ATOM   7700  C  C     . PHE A 1 2441 ? 238.135 168.227 184.486 1.00 5.08  ? 2441 PHE A C     1 
ATOM   7701  O  O     . PHE A 1 2441 ? 237.489 168.046 185.524 1.00 7.85  ? 2441 PHE A O     1 
ATOM   7702  C  CB    . PHE A 1 2441 ? 236.545 168.875 182.662 1.00 2.35  ? 2441 PHE A CB    1 
ATOM   7703  C  CG    . PHE A 1 2441 ? 235.659 169.999 182.208 1.00 2.89  ? 2441 PHE A CG    1 
ATOM   7704  C  CD1   . PHE A 1 2441 ? 234.608 170.432 182.999 1.00 3.09  ? 2441 PHE A CD1   1 
ATOM   7705  C  CD2   . PHE A 1 2441 ? 235.876 170.622 180.992 1.00 2.95  ? 2441 PHE A CD2   1 
ATOM   7706  C  CE1   . PHE A 1 2441 ? 233.793 171.467 182.586 1.00 2.05  ? 2441 PHE A CE1   1 
ATOM   7707  C  CE2   . PHE A 1 2441 ? 235.063 171.659 180.573 1.00 3.34  ? 2441 PHE A CE2   1 
ATOM   7708  C  CZ    . PHE A 1 2441 ? 234.018 172.080 181.372 1.00 5.70  ? 2441 PHE A CZ    1 
ATOM   7709  N  N     . GLN A 1 2442 ? 239.194 167.482 184.171 1.00 5.97  ? 2442 GLN A N     1 
ATOM   7710  C  CA    . GLN A 1 2442 ? 239.666 166.444 185.075 1.00 7.14  ? 2442 GLN A CA    1 
ATOM   7711  C  C     . GLN A 1 2442 ? 240.461 167.013 186.242 1.00 8.47  ? 2442 GLN A C     1 
ATOM   7712  O  O     . GLN A 1 2442 ? 240.654 166.318 187.242 1.00 15.12 ? 2442 GLN A O     1 
ATOM   7713  C  CB    . GLN A 1 2442 ? 240.511 165.429 184.308 1.00 8.46  ? 2442 GLN A CB    1 
ATOM   7714  C  CG    . GLN A 1 2442 ? 239.718 164.660 183.272 1.00 9.44  ? 2442 GLN A CG    1 
ATOM   7715  C  CD    . GLN A 1 2442 ? 238.612 163.835 183.890 1.00 22.94 ? 2442 GLN A CD    1 
ATOM   7716  O  OE1   . GLN A 1 2442 ? 237.431 164.151 183.740 1.00 28.40 ? 2442 GLN A OE1   1 
ATOM   7717  N  NE2   . GLN A 1 2442 ? 238.986 162.769 184.589 1.00 17.08 ? 2442 GLN A NE2   1 
ATOM   7718  N  N     . LEU A 1 2443 ? 240.917 168.256 186.139 1.00 8.29  ? 2443 LEU A N     1 
ATOM   7719  C  CA    . LEU A 1 2443 ? 241.743 168.859 187.169 1.00 6.22  ? 2443 LEU A CA    1 
ATOM   7720  C  C     . LEU A 1 2443 ? 240.883 169.512 188.245 1.00 6.10  ? 2443 LEU A C     1 
ATOM   7721  O  O     . LEU A 1 2443 ? 239.667 169.665 188.105 1.00 10.89 ? 2443 LEU A O     1 
ATOM   7722  C  CB    . LEU A 1 2443 ? 242.689 169.887 186.555 1.00 5.39  ? 2443 LEU A CB    1 
ATOM   7723  C  CG    . LEU A 1 2443 ? 243.609 169.291 185.497 1.00 8.81  ? 2443 LEU A CG    1 
ATOM   7724  C  CD1   . LEU A 1 2443 ? 244.439 170.360 184.806 1.00 10.33 ? 2443 LEU A CD1   1 
ATOM   7725  C  CD2   . LEU A 1 2443 ? 244.492 168.251 186.147 1.00 5.54  ? 2443 LEU A CD2   1 
ATOM   7726  N  N     . GLU A 1 2444 ? 241.536 169.894 189.337 1.00 5.80  ? 2444 GLU A N     1 
ATOM   7727  C  CA    . GLU A 1 2444 ? 240.866 170.581 190.430 1.00 7.62  ? 2444 GLU A CA    1 
ATOM   7728  C  C     . GLU A 1 2444 ? 241.029 172.086 190.274 1.00 6.20  ? 2444 GLU A C     1 
ATOM   7729  O  O     . GLU A 1 2444 ? 242.121 172.581 189.982 1.00 6.20  ? 2444 GLU A O     1 
ATOM   7730  C  CB    . GLU A 1 2444 ? 241.413 170.126 191.783 1.00 8.67  ? 2444 GLU A CB    1 
ATOM   7731  C  CG    . GLU A 1 2444 ? 241.119 168.674 192.107 1.00 16.93 ? 2444 GLU A CG    1 
ATOM   7732  C  CD    . GLU A 1 2444 ? 239.639 168.407 192.305 1.00 23.97 ? 2444 GLU A CD    1 
ATOM   7733  O  OE1   . GLU A 1 2444 ? 238.923 169.315 192.780 1.00 23.85 ? 2444 GLU A OE1   1 
ATOM   7734  O  OE2   . GLU A 1 2444 ? 239.187 167.287 191.985 1.00 26.58 ? 2444 GLU A OE2   1 
ATOM   7735  N  N     . HIS A 1 2445 ? 239.932 172.806 190.462 1.00 5.50  ? 2445 HIS A N     1 
ATOM   7736  C  CA    . HIS A 1 2445 ? 239.903 174.251 190.313 1.00 2.85  ? 2445 HIS A CA    1 
ATOM   7737  C  C     . HIS A 1 2445 ? 239.307 174.873 191.565 1.00 2.85  ? 2445 HIS A C     1 
ATOM   7738  O  O     . HIS A 1 2445 ? 238.489 174.259 192.252 1.00 3.44  ? 2445 HIS A O     1 
ATOM   7739  C  CB    . HIS A 1 2445 ? 239.098 174.659 189.076 1.00 2.56  ? 2445 HIS A CB    1 
ATOM   7740  C  CG    . HIS A 1 2445 ? 239.461 173.895 187.843 1.00 4.94  ? 2445 HIS A CG    1 
ATOM   7741  N  ND1   . HIS A 1 2445 ? 240.431 174.323 186.961 1.00 5.27  ? 2445 HIS A ND1   1 
ATOM   7742  C  CD2   . HIS A 1 2445 ? 238.999 172.723 187.351 1.00 4.30  ? 2445 HIS A CD2   1 
ATOM   7743  C  CE1   . HIS A 1 2445 ? 240.542 173.452 185.976 1.00 2.38  ? 2445 HIS A CE1   1 
ATOM   7744  N  NE2   . HIS A 1 2445 ? 239.687 172.470 186.190 1.00 4.27  ? 2445 HIS A NE2   1 
ATOM   7745  N  N     . ILE A 1 2446 ? 239.731 176.105 191.859 1.00 1.59  ? 2446 ILE A N     1 
ATOM   7746  C  CA    . ILE A 1 2446 ? 239.257 176.779 193.065 1.00 2.09  ? 2446 ILE A CA    1 
ATOM   7747  C  C     . ILE A 1 2446 ? 237.758 177.034 192.984 1.00 2.21  ? 2446 ILE A C     1 
ATOM   7748  O  O     . ILE A 1 2446 ? 237.074 177.099 194.012 1.00 3.28  ? 2446 ILE A O     1 
ATOM   7749  C  CB    . ILE A 1 2446 ? 240.058 178.078 193.303 1.00 2.79  ? 2446 ILE A CB    1 
ATOM   7750  C  CG1   . ILE A 1 2446 ? 240.096 178.417 194.794 1.00 3.24  ? 2446 ILE A CG1   1 
ATOM   7751  C  CG2   . ILE A 1 2446 ? 239.491 179.240 192.505 1.00 2.17  ? 2446 ILE A CG2   1 
ATOM   7752  C  CD1   . ILE A 1 2446 ? 240.712 177.336 195.647 1.00 2.31  ? 2446 ILE A CD1   1 
ATOM   7753  N  N     . MET A 1 2447 ? 237.220 177.165 191.775 1.00 2.97  ? 2447 MET A N     1 
ATOM   7754  C  CA    . MET A 1 2447 ? 235.789 177.281 191.555 1.00 2.09  ? 2447 MET A CA    1 
ATOM   7755  C  C     . MET A 1 2447 ? 235.351 176.195 190.585 1.00 2.09  ? 2447 MET A C     1 
ATOM   7756  O  O     . MET A 1 2447 ? 236.167 175.608 189.874 1.00 2.12  ? 2447 MET A O     1 
ATOM   7757  C  CB    . MET A 1 2447 ? 235.408 178.662 191.009 1.00 4.33  ? 2447 MET A CB    1 
ATOM   7758  C  CG    . MET A 1 2447 ? 235.496 179.769 192.035 1.00 4.30  ? 2447 MET A CG    1 
ATOM   7759  S  SD    . MET A 1 2447 ? 234.643 181.262 191.511 1.00 12.05 ? 2447 MET A SD    1 
ATOM   7760  C  CE    . MET A 1 2447 ? 234.971 182.314 192.914 1.00 0.94  ? 2447 MET A CE    1 
ATOM   7761  N  N     . ASP A 1 2448 ? 234.046 175.923 190.576 1.00 2.66  ? 2448 ASP A N     1 
ATOM   7762  C  CA    . ASP A 1 2448 ? 233.498 174.946 189.643 1.00 1.74  ? 2448 ASP A CA    1 
ATOM   7763  C  C     . ASP A 1 2448 ? 233.807 175.356 188.211 1.00 2.38  ? 2448 ASP A C     1 
ATOM   7764  O  O     . ASP A 1 2448 ? 233.689 176.529 187.847 1.00 5.06  ? 2448 ASP A O     1 
ATOM   7765  C  CB    . ASP A 1 2448 ? 231.992 174.807 189.846 1.00 3.07  ? 2448 ASP A CB    1 
ATOM   7766  C  CG    . ASP A 1 2448 ? 231.641 174.022 191.092 1.00 12.52 ? 2448 ASP A CG    1 
ATOM   7767  O  OD1   . ASP A 1 2448 ? 232.559 173.449 191.716 1.00 15.40 ? 2448 ASP A OD1   1 
ATOM   7768  O  OD2   . ASP A 1 2448 ? 230.447 173.982 191.451 1.00 13.85 ? 2448 ASP A OD2   1 
ATOM   7769  N  N     . LEU A 1 2449 ? 234.209 174.388 187.397 1.00 2.69  ? 2449 LEU A N     1 
ATOM   7770  C  CA    . LEU A 1 2449 ? 234.674 174.671 186.050 1.00 1.55  ? 2449 LEU A CA    1 
ATOM   7771  C  C     . LEU A 1 2449 ? 233.533 174.466 185.064 1.00 3.01  ? 2449 LEU A C     1 
ATOM   7772  O  O     . LEU A 1 2449 ? 232.867 173.427 185.084 1.00 4.68  ? 2449 LEU A O     1 
ATOM   7773  C  CB    . LEU A 1 2449 ? 235.849 173.764 185.687 1.00 2.24  ? 2449 LEU A CB    1 
ATOM   7774  C  CG    . LEU A 1 2449 ? 236.470 174.105 184.335 1.00 4.76  ? 2449 LEU A CG    1 
ATOM   7775  C  CD1   . LEU A 1 2449 ? 237.049 175.497 184.455 1.00 1.92  ? 2449 LEU A CD1   1 
ATOM   7776  C  CD2   . LEU A 1 2449 ? 237.515 173.104 183.889 1.00 3.89  ? 2449 LEU A CD2   1 
ATOM   7777  N  N     . THR A 1 2450 ? 233.302 175.461 184.212 1.00 2.06  ? 2450 THR A N     1 
ATOM   7778  C  CA    . THR A 1 2450 ? 232.327 175.352 183.139 1.00 1.24  ? 2450 THR A CA    1 
ATOM   7779  C  C     . THR A 1 2450 ? 232.997 175.669 181.809 1.00 1.37  ? 2450 THR A C     1 
ATOM   7780  O  O     . THR A 1 2450 ? 234.010 176.370 181.749 1.00 4.17  ? 2450 THR A O     1 
ATOM   7781  C  CB    . THR A 1 2450 ? 231.120 176.283 183.358 1.00 2.53  ? 2450 THR A CB    1 
ATOM   7782  O  OG1   . THR A 1 2450 ? 231.530 177.652 183.253 1.00 9.05  ? 2450 THR A OG1   1 
ATOM   7783  C  CG2   . THR A 1 2450 ? 230.487 176.036 184.719 1.00 1.72  ? 2450 THR A CG2   1 
ATOM   7784  N  N     . ARG A 1 2451 ? 232.415 175.127 180.737 1.00 1.77  ? 2451 ARG A N     1 
ATOM   7785  C  CA    . ARG A 1 2451 ? 233.021 175.251 179.416 1.00 2.02  ? 2451 ARG A CA    1 
ATOM   7786  C  C     . ARG A 1 2451 ? 233.110 176.705 178.972 1.00 0.88  ? 2451 ARG A C     1 
ATOM   7787  O  O     . ARG A 1 2451 ? 234.127 177.131 178.414 1.00 1.31  ? 2451 ARG A O     1 
ATOM   7788  C  CB    . ARG A 1 2451 ? 232.226 174.428 178.401 1.00 2.60  ? 2451 ARG A CB    1 
ATOM   7789  C  CG    . ARG A 1 2451 ? 232.570 174.733 176.953 1.00 1.74  ? 2451 ARG A CG    1 
ATOM   7790  C  CD    . ARG A 1 2451 ? 231.767 173.883 175.989 1.00 3.75  ? 2451 ARG A CD    1 
ATOM   7791  N  NE    . ARG A 1 2451 ? 230.328 174.034 176.173 1.00 2.64  ? 2451 ARG A NE    1 
ATOM   7792  C  CZ    . ARG A 1 2451 ? 229.415 173.503 175.372 1.00 2.26  ? 2451 ARG A CZ    1 
ATOM   7793  N  NH1   . ARG A 1 2451 ? 229.755 172.783 174.317 1.00 2.06  ? 2451 ARG A NH1   1 
ATOM   7794  N  NH2   . ARG A 1 2451 ? 228.128 173.706 175.633 1.00 3.05  ? 2451 ARG A NH2   1 
ATOM   7795  N  N     . LEU A 1 2452 ? 232.059 177.486 179.216 1.00 1.11  ? 2452 LEU A N     1 
ATOM   7796  C  CA    . LEU A 1 2452 ? 232.014 178.846 178.696 1.00 0.65  ? 2452 LEU A CA    1 
ATOM   7797  C  C     . LEU A 1 2452 ? 232.875 179.813 179.498 1.00 0.95  ? 2452 LEU A C     1 
ATOM   7798  O  O     . LEU A 1 2452 ? 233.297 180.841 178.958 1.00 0.99  ? 2452 LEU A O     1 
ATOM   7799  C  CB    . LEU A 1 2452 ? 230.568 179.329 178.634 1.00 0.82  ? 2452 LEU A CB    1 
ATOM   7800  C  CG    . LEU A 1 2452 ? 229.815 178.740 177.439 1.00 0.70  ? 2452 LEU A CG    1 
ATOM   7801  C  CD1   . LEU A 1 2452 ? 228.510 179.452 177.221 1.00 0.65  ? 2452 LEU A CD1   1 
ATOM   7802  C  CD2   . LEU A 1 2452 ? 230.672 178.812 176.186 1.00 0.62  ? 2452 LEU A CD2   1 
ATOM   7803  N  N     . ARG A 1 2453 ? 233.147 179.521 180.773 1.00 1.38  ? 2453 ARG A N     1 
ATOM   7804  C  CA    . ARG A 1 2453 ? 234.087 180.358 181.512 1.00 1.00  ? 2453 ARG A CA    1 
ATOM   7805  C  C     . ARG A 1 2453 ? 235.487 180.255 180.920 1.00 1.02  ? 2453 ARG A C     1 
ATOM   7806  O  O     . ARG A 1 2453 ? 236.191 181.263 180.791 1.00 2.52  ? 2453 ARG A O     1 
ATOM   7807  C  CB    . ARG A 1 2453 ? 234.100 179.989 182.996 1.00 0.91  ? 2453 ARG A CB    1 
ATOM   7808  C  CG    . ARG A 1 2453 ? 235.044 180.871 183.809 1.00 0.77  ? 2453 ARG A CG    1 
ATOM   7809  C  CD    . ARG A 1 2453 ? 234.872 180.736 185.315 1.00 0.72  ? 2453 ARG A CD    1 
ATOM   7810  N  NE    . ARG A 1 2453 ? 235.101 179.385 185.807 1.00 3.74  ? 2453 ARG A NE    1 
ATOM   7811  C  CZ    . ARG A 1 2453 ? 236.229 178.976 186.372 1.00 2.50  ? 2453 ARG A CZ    1 
ATOM   7812  N  NH1   . ARG A 1 2453 ? 237.286 179.763 186.454 1.00 1.49  ? 2453 ARG A NH1   1 
ATOM   7813  N  NH2   . ARG A 1 2453 ? 236.300 177.740 186.855 1.00 5.48  ? 2453 ARG A NH2   1 
ATOM   7814  N  N     . CYS A 1 2454 ? 235.901 179.044 180.542 1.00 1.50  ? 2454 CYS A N     1 
ATOM   7815  C  CA    . CYS A 1 2454 ? 237.201 178.866 179.901 1.00 1.41  ? 2454 CYS A CA    1 
ATOM   7816  C  C     . CYS A 1 2454 ? 237.234 179.531 178.536 1.00 0.91  ? 2454 CYS A C     1 
ATOM   7817  O  O     . CYS A 1 2454 ? 238.164 180.281 178.219 1.00 1.48  ? 2454 CYS A O     1 
ATOM   7818  C  CB    . CYS A 1 2454 ? 237.517 177.380 179.760 1.00 3.58  ? 2454 CYS A CB    1 
ATOM   7819  S  SG    . CYS A 1 2454 ? 237.329 176.436 181.255 1.00 12.23 ? 2454 CYS A SG    1 
ATOM   7820  N  N     . LEU A 1 2455 ? 236.228 179.251 177.704 1.00 1.09  ? 2455 LEU A N     1 
ATOM   7821  C  CA    . LEU A 1 2455 ? 236.218 179.781 176.347 1.00 0.82  ? 2455 LEU A CA    1 
ATOM   7822  C  C     . LEU A 1 2455 ? 236.025 181.290 176.347 1.00 0.54  ? 2455 LEU A C     1 
ATOM   7823  O  O     . LEU A 1 2455 ? 236.645 181.999 175.546 1.00 1.24  ? 2455 LEU A O     1 
ATOM   7824  C  CB    . LEU A 1 2455 ? 235.132 179.085 175.529 1.00 0.90  ? 2455 LEU A CB    1 
ATOM   7825  C  CG    . LEU A 1 2455 ? 235.388 177.595 175.279 1.00 0.99  ? 2455 LEU A CG    1 
ATOM   7826  C  CD1   . LEU A 1 2455 ? 234.365 177.020 174.316 1.00 1.32  ? 2455 LEU A CD1   1 
ATOM   7827  C  CD2   . LEU A 1 2455 ? 236.801 177.367 174.767 1.00 0.76  ? 2455 LEU A CD2   1 
ATOM   7828  N  N     . GLY A 1 2456 ? 235.176 181.801 177.239 1.00 0.79  ? 2456 GLY A N     1 
ATOM   7829  C  CA    . GLY A 1 2456 ? 235.041 183.242 177.372 1.00 0.99  ? 2456 GLY A CA    1 
ATOM   7830  C  C     . GLY A 1 2456 ? 236.354 183.908 177.734 1.00 1.26  ? 2456 GLY A C     1 
ATOM   7831  O  O     . GLY A 1 2456 ? 236.700 184.958 177.188 1.00 1.16  ? 2456 GLY A O     1 
ATOM   7832  N  N     . SER A 1 2457 ? 237.100 183.305 178.661 1.00 1.13  ? 2457 SER A N     1 
ATOM   7833  C  CA    . SER A 1 2457 ? 238.437 183.797 178.973 1.00 0.84  ? 2457 SER A CA    1 
ATOM   7834  C  C     . SER A 1 2457 ? 239.377 183.632 177.786 1.00 1.21  ? 2457 SER A C     1 
ATOM   7835  O  O     . SER A 1 2457 ? 240.156 184.538 177.473 1.00 1.87  ? 2457 SER A O     1 
ATOM   7836  C  CB    . SER A 1 2457 ? 238.988 183.072 180.199 1.00 0.53  ? 2457 SER A CB    1 
ATOM   7837  O  OG    . SER A 1 2457 ? 240.336 183.432 180.438 1.00 1.50  ? 2457 SER A OG    1 
ATOM   7838  N  N     . LEU A 1 2458 ? 239.317 182.480 177.112 1.00 1.10  ? 2458 LEU A N     1 
ATOM   7839  C  CA    . LEU A 1 2458 ? 240.221 182.222 175.997 1.00 0.99  ? 2458 LEU A CA    1 
ATOM   7840  C  C     . LEU A 1 2458 ? 239.989 183.196 174.852 1.00 1.53  ? 2458 LEU A C     1 
ATOM   7841  O  O     . LEU A 1 2458 ? 240.945 183.683 174.237 1.00 1.45  ? 2458 LEU A O     1 
ATOM   7842  C  CB    . LEU A 1 2458 ? 240.057 180.780 175.515 1.00 1.39  ? 2458 LEU A CB    1 
ATOM   7843  C  CG    . LEU A 1 2458 ? 240.846 180.407 174.258 1.00 1.85  ? 2458 LEU A CG    1 
ATOM   7844  C  CD1   . LEU A 1 2458 ? 242.340 180.414 174.543 1.00 1.27  ? 2458 LEU A CD1   1 
ATOM   7845  C  CD2   . LEU A 1 2458 ? 240.404 179.064 173.716 1.00 0.55  ? 2458 LEU A CD2   1 
ATOM   7846  N  N     . PHE A 1 2459 ? 238.726 183.491 174.546 1.00 4.10  ? 2459 PHE A N     1 
ATOM   7847  C  CA    . PHE A 1 2459 ? 238.427 184.392 173.438 1.00 1.67  ? 2459 PHE A CA    1 
ATOM   7848  C  C     . PHE A 1 2459 ? 238.796 185.832 173.769 1.00 1.93  ? 2459 PHE A C     1 
ATOM   7849  O  O     . PHE A 1 2459 ? 239.219 186.580 172.878 1.00 3.06  ? 2459 PHE A O     1 
ATOM   7850  C  CB    . PHE A 1 2459 ? 236.949 184.289 173.064 1.00 1.32  ? 2459 PHE A CB    1 
ATOM   7851  C  CG    . PHE A 1 2459 ? 236.523 182.908 172.648 1.00 0.92  ? 2459 PHE A CG    1 
ATOM   7852  C  CD1   . PHE A 1 2459 ? 237.429 182.028 172.084 1.00 1.38  ? 2459 PHE A CD1   1 
ATOM   7853  C  CD2   . PHE A 1 2459 ? 235.214 182.492 172.827 1.00 0.88  ? 2459 PHE A CD2   1 
ATOM   7854  C  CE1   . PHE A 1 2459 ? 237.039 180.759 171.706 1.00 1.59  ? 2459 PHE A CE1   1 
ATOM   7855  C  CE2   . PHE A 1 2459 ? 234.821 181.224 172.452 1.00 1.09  ? 2459 PHE A CE2   1 
ATOM   7856  C  CZ    . PHE A 1 2459 ? 235.733 180.357 171.891 1.00 1.48  ? 2459 PHE A CZ    1 
ATOM   7857  N  N     . SER A 1 2460 ? 238.642 186.242 175.029 1.00 3.15  ? 2460 SER A N     1 
ATOM   7858  C  CA    . SER A 1 2460 ? 239.063 187.581 175.428 1.00 1.31  ? 2460 SER A CA    1 
ATOM   7859  C  C     . SER A 1 2460 ? 240.568 187.750 175.279 1.00 1.82  ? 2460 SER A C     1 
ATOM   7860  O  O     . SER A 1 2460 ? 241.040 188.795 174.819 1.00 4.22  ? 2460 SER A O     1 
ATOM   7861  C  CB    . SER A 1 2460 ? 238.635 187.863 176.867 1.00 1.36  ? 2460 SER A CB    1 
ATOM   7862  O  OG    . SER A 1 2460 ? 237.227 187.829 176.999 1.00 3.45  ? 2460 SER A OG    1 
ATOM   7863  N  N     . MET A 1 2461 ? 241.339 186.734 175.669 1.00 2.39  ? 2461 MET A N     1 
ATOM   7864  C  CA    . MET A 1 2461 ? 242.790 186.816 175.563 1.00 1.30  ? 2461 MET A CA    1 
ATOM   7865  C  C     . MET A 1 2461 ? 243.241 186.873 174.110 1.00 2.53  ? 2461 MET A C     1 
ATOM   7866  O  O     . MET A 1 2461 ? 244.157 187.630 173.769 1.00 9.94  ? 2461 MET A O     1 
ATOM   7867  C  CB    . MET A 1 2461 ? 243.433 185.633 176.287 1.00 2.13  ? 2461 MET A CB    1 
ATOM   7868  C  CG    . MET A 1 2461 ? 243.090 185.568 177.767 1.00 1.18  ? 2461 MET A CG    1 
ATOM   7869  S  SD    . MET A 1 2461 ? 244.135 184.458 178.722 1.00 1.65  ? 2461 MET A SD    1 
ATOM   7870  C  CE    . MET A 1 2461 ? 245.757 185.019 178.234 1.00 1.27  ? 2461 MET A CE    1 
ATOM   7871  N  N     . LEU A 1 2462 ? 242.608 186.086 173.237 1.00 2.59  ? 2462 LEU A N     1 
ATOM   7872  C  CA    . LEU A 1 2462 ? 242.977 186.103 171.826 1.00 2.23  ? 2462 LEU A CA    1 
ATOM   7873  C  C     . LEU A 1 2462 ? 242.644 187.438 171.174 1.00 2.75  ? 2462 LEU A C     1 
ATOM   7874  O  O     . LEU A 1 2462 ? 243.369 187.887 170.280 1.00 4.08  ? 2462 LEU A O     1 
ATOM   7875  C  CB    . LEU A 1 2462 ? 242.290 184.958 171.087 1.00 1.56  ? 2462 LEU A CB    1 
ATOM   7876  C  CG    . LEU A 1 2462 ? 242.752 183.554 171.480 1.00 2.17  ? 2462 LEU A CG    1 
ATOM   7877  C  CD1   . LEU A 1 2462 ? 241.914 182.498 170.784 1.00 3.31  ? 2462 LEU A CD1   1 
ATOM   7878  C  CD2   . LEU A 1 2462 ? 244.228 183.361 171.173 1.00 3.16  ? 2462 LEU A CD2   1 
ATOM   7879  N  N     . HIS A 1 2463 ? 241.555 188.083 171.599 1.00 3.64  ? 2463 HIS A N     1 
ATOM   7880  C  CA    . HIS A 1 2463 ? 241.251 189.422 171.106 1.00 4.88  ? 2463 HIS A CA    1 
ATOM   7881  C  C     . HIS A 1 2463 ? 242.342 190.408 171.500 1.00 7.38  ? 2463 HIS A C     1 
ATOM   7882  O  O     . HIS A 1 2463 ? 242.697 191.299 170.721 1.00 10.33 ? 2463 HIS A O     1 
ATOM   7883  C  CB    . HIS A 1 2463 ? 239.895 189.885 171.638 1.00 5.04  ? 2463 HIS A CB    1 
ATOM   7884  C  CG    . HIS A 1 2463 ? 238.727 189.237 170.966 1.00 4.25  ? 2463 HIS A CG    1 
ATOM   7885  N  ND1   . HIS A 1 2463 ? 237.481 189.159 171.551 1.00 5.79  ? 2463 HIS A ND1   1 
ATOM   7886  C  CD2   . HIS A 1 2463 ? 238.614 188.631 169.760 1.00 4.38  ? 2463 HIS A CD2   1 
ATOM   7887  C  CE1   . HIS A 1 2463 ? 236.651 188.538 170.733 1.00 4.73  ? 2463 HIS A CE1   1 
ATOM   7888  N  NE2   . HIS A 1 2463 ? 237.313 188.206 169.640 1.00 6.94  ? 2463 HIS A NE2   1 
ATOM   7889  N  N     . GLN A 1 2464 ? 242.880 190.265 172.713 1.00 9.34  ? 2464 GLN A N     1 
ATOM   7890  C  CA    . GLN A 1 2464 ? 243.984 191.114 173.148 1.00 6.79  ? 2464 GLN A CA    1 
ATOM   7891  C  C     . GLN A 1 2464 ? 245.228 190.875 172.304 1.00 7.28  ? 2464 GLN A C     1 
ATOM   7892  O  O     . GLN A 1 2464 ? 245.979 191.812 172.012 1.00 8.05  ? 2464 GLN A O     1 
ATOM   7893  C  CB    . GLN A 1 2464 ? 244.278 190.864 174.629 1.00 7.62  ? 2464 GLN A CB    1 
ATOM   7894  C  CG    . GLN A 1 2464 ? 245.363 191.744 175.225 1.00 9.28  ? 2464 GLN A CG    1 
ATOM   7895  C  CD    . GLN A 1 2464 ? 245.118 193.220 174.997 1.00 7.78  ? 2464 GLN A CD    1 
ATOM   7896  O  OE1   . GLN A 1 2464 ? 244.042 193.735 175.297 1.00 10.67 ? 2464 GLN A OE1   1 
ATOM   7897  N  NE2   . GLN A 1 2464 ? 246.120 193.909 174.469 1.00 10.54 ? 2464 GLN A NE2   1 
ATOM   7898  N  N     . ALA A 1 2465 ? 245.468 189.622 171.907 1.00 7.24  ? 2465 ALA A N     1 
ATOM   7899  C  CA    . ALA A 1 2465 ? 246.607 189.321 171.051 1.00 4.49  ? 2465 ALA A CA    1 
ATOM   7900  C  C     . ALA A 1 2465 ? 246.486 190.029 169.708 1.00 8.49  ? 2465 ALA A C     1 
ATOM   7901  O  O     . ALA A 1 2465 ? 247.484 190.504 169.156 1.00 9.55  ? 2465 ALA A O     1 
ATOM   7902  C  CB    . ALA A 1 2465 ? 246.731 187.813 170.849 1.00 5.20  ? 2465 ALA A CB    1 
ATOM   7903  N  N     . CYS A 1 2466 ? 245.269 190.098 169.163 1.00 11.55 ? 2466 CYS A N     1 
ATOM   7904  C  CA    . CYS A 1 2466 ? 245.054 190.856 167.935 1.00 6.77  ? 2466 CYS A CA    1 
ATOM   7905  C  C     . CYS A 1 2466 ? 245.338 192.335 168.154 1.00 7.80  ? 2466 CYS A C     1 
ATOM   7906  O  O     . CYS A 1 2466 ? 245.915 192.998 167.285 1.00 11.12 ? 2466 CYS A O     1 
ATOM   7907  C  CB    . CYS A 1 2466 ? 243.628 190.642 167.432 1.00 7.56  ? 2466 CYS A CB    1 
ATOM   7908  S  SG    . CYS A 1 2466 ? 243.275 188.953 166.901 1.00 21.05 ? 2466 CYS A SG    1 
ATOM   7909  N  N     . ARG A 1 2467 ? 244.941 192.868 169.311 1.00 10.39 ? 2467 ARG A N     1 
ATOM   7910  C  CA    . ARG A 1 2467 ? 245.263 194.252 169.641 1.00 7.11  ? 2467 ARG A CA    1 
ATOM   7911  C  C     . ARG A 1 2467 ? 246.762 194.458 169.814 1.00 6.30  ? 2467 ARG A C     1 
ATOM   7912  O  O     . ARG A 1 2467 ? 247.273 195.542 169.515 1.00 10.69 ? 2467 ARG A O     1 
ATOM   7913  C  CB    . ARG A 1 2467 ? 244.519 194.675 170.906 1.00 6.49  ? 2467 ARG A CB    1 
ATOM   7914  C  CG    . ARG A 1 2467 ? 243.020 194.789 170.734 1.00 10.23 ? 2467 ARG A CG    1 
ATOM   7915  C  CD    . ARG A 1 2467 ? 242.333 195.035 172.061 1.00 11.85 ? 2467 ARG A CD    1 
ATOM   7916  N  NE    . ARG A 1 2467 ? 240.921 194.681 172.016 1.00 14.34 ? 2467 ARG A NE    1 
ATOM   7917  C  CZ    . ARG A 1 2467 ? 239.964 195.468 171.545 1.00 16.54 ? 2467 ARG A CZ    1 
ATOM   7918  N  NH1   . ARG A 1 2467 ? 240.229 196.679 171.083 1.00 9.11  ? 2467 ARG A NH1   1 
ATOM   7919  N  NH2   . ARG A 1 2467 ? 238.708 195.032 171.541 1.00 13.91 ? 2467 ARG A NH2   1 
ATOM   7920  N  N     . ASN A 1 2468 ? 247.478 193.439 170.295 1.00 6.67  ? 2468 ASN A N     1 
ATOM   7921  C  CA    . ASN A 1 2468 ? 248.927 193.554 170.438 1.00 7.90  ? 2468 ASN A CA    1 
ATOM   7922  C  C     . ASN A 1 2468 ? 249.600 193.754 169.087 1.00 8.59  ? 2468 ASN A C     1 
ATOM   7923  O  O     . ASN A 1 2468 ? 250.513 194.578 168.954 1.00 15.52 ? 2468 ASN A O     1 
ATOM   7924  C  CB    . ASN A 1 2468 ? 249.492 192.313 171.129 1.00 5.57  ? 2468 ASN A CB    1 
ATOM   7925  C  CG    . ASN A 1 2468 ? 249.114 192.235 172.591 1.00 7.08  ? 2468 ASN A CG    1 
ATOM   7926  O  OD1   . ASN A 1 2468 ? 248.581 193.186 173.159 1.00 10.01 ? 2468 ASN A OD1   1 
ATOM   7927  N  ND2   . ASN A 1 2468 ? 249.380 191.089 173.208 1.00 6.11  ? 2468 ASN A ND2   1 
ATOM   7928  N  N     . VAL A 1 2469 ? 249.163 193.007 168.072 1.00 9.98  ? 2469 VAL A N     1 
ATOM   7929  C  CA    . VAL A 1 2469 ? 249.758 193.123 166.744 1.00 9.07  ? 2469 VAL A CA    1 
ATOM   7930  C  C     . VAL A 1 2469 ? 249.486 194.501 166.156 1.00 10.12 ? 2469 VAL A C     1 
ATOM   7931  O  O     . VAL A 1 2469 ? 250.364 195.113 165.536 1.00 13.65 ? 2469 VAL A O     1 
ATOM   7932  C  CB    . VAL A 1 2469 ? 249.240 191.997 165.831 1.00 8.53  ? 2469 VAL A CB    1 
ATOM   7933  C  CG1   . VAL A 1 2469 ? 249.814 192.135 164.432 1.00 11.02 ? 2469 VAL A CG1   1 
ATOM   7934  C  CG2   . VAL A 1 2469 ? 249.585 190.643 166.426 1.00 8.42  ? 2469 VAL A CG2   1 
ATOM   7935  N  N     . ALA A 1 2470 ? 248.266 195.012 166.338 1.00 9.18  ? 2470 ALA A N     1 
ATOM   7936  C  CA    . ALA A 1 2470 ? 247.957 196.362 165.879 1.00 11.05 ? 2470 ALA A CA    1 
ATOM   7937  C  C     . ALA A 1 2470 ? 248.797 197.400 166.608 1.00 15.49 ? 2470 ALA A C     1 
ATOM   7938  O  O     . ALA A 1 2470 ? 249.298 198.350 165.994 1.00 20.63 ? 2470 ALA A O     1 
ATOM   7939  C  CB    . ALA A 1 2470 ? 246.469 196.651 166.066 1.00 10.57 ? 2470 ALA A CB    1 
ATOM   7940  N  N     . GLN A 1 2471 ? 248.962 197.235 167.922 1.00 15.49 ? 2471 GLN A N     1 
ATOM   7941  C  CA    . GLN A 1 2471 ? 249.772 198.171 168.690 1.00 17.55 ? 2471 GLN A CA    1 
ATOM   7942  C  C     . GLN A 1 2471 ? 251.231 198.108 168.256 1.00 18.80 ? 2471 GLN A C     1 
ATOM   7943  O  O     . GLN A 1 2471 ? 251.937 199.123 168.263 1.00 21.32 ? 2471 GLN A O     1 
ATOM   7944  C  CB    . GLN A 1 2471 ? 249.623 197.877 170.184 1.00 17.51 ? 2471 GLN A CB    1 
ATOM   7945  C  CG    . GLN A 1 2471 ? 250.255 198.896 171.123 1.00 13.21 ? 2471 GLN A CG    1 
ATOM   7946  C  CD    . GLN A 1 2471 ? 251.721 198.636 171.390 1.00 22.92 ? 2471 GLN A CD    1 
ATOM   7947  O  OE1   . GLN A 1 2471 ? 252.493 199.560 171.645 1.00 32.94 ? 2471 GLN A OE1   1 
ATOM   7948  N  NE2   . GLN A 1 2471 ? 252.120 197.373 171.305 1.00 22.74 ? 2471 GLN A NE2   1 
ATOM   7949  N  N     . TYR A 1 2472 ? 251.699 196.918 167.869 1.00 15.31 ? 2472 TYR A N     1 
ATOM   7950  C  CA    . TYR A 1 2472 ? 253.040 196.799 167.308 1.00 14.68 ? 2472 TYR A CA    1 
ATOM   7951  C  C     . TYR A 1 2472 ? 253.155 197.561 165.994 1.00 17.22 ? 2472 TYR A C     1 
ATOM   7952  O  O     . TYR A 1 2472 ? 254.172 198.216 165.734 1.00 21.21 ? 2472 TYR A O     1 
ATOM   7953  C  CB    . TYR A 1 2472 ? 253.400 195.320 167.130 1.00 11.44 ? 2472 TYR A CB    1 
ATOM   7954  C  CG    . TYR A 1 2472 ? 254.672 195.042 166.353 1.00 14.90 ? 2472 TYR A CG    1 
ATOM   7955  C  CD1   . TYR A 1 2472 ? 255.829 194.640 167.006 1.00 13.39 ? 2472 TYR A CD1   1 
ATOM   7956  C  CD2   . TYR A 1 2472 ? 254.700 195.114 164.965 1.00 15.76 ? 2472 TYR A CD2   1 
ATOM   7957  C  CE1   . TYR A 1 2472 ? 256.986 194.369 166.307 1.00 18.02 ? 2472 TYR A CE1   1 
ATOM   7958  C  CE2   . TYR A 1 2472 ? 255.852 194.846 164.259 1.00 21.18 ? 2472 TYR A CE2   1 
ATOM   7959  C  CZ    . TYR A 1 2472 ? 256.992 194.472 164.933 1.00 21.79 ? 2472 TYR A CZ    1 
ATOM   7960  O  OH    . TYR A 1 2472 ? 258.141 194.199 164.229 1.00 25.86 ? 2472 TYR A OH    1 
ATOM   7961  N  N     . ASN A 1 2473 ? 252.126 197.483 165.146 1.00 22.58 ? 2473 ASN A N     1 
ATOM   7962  C  CA    . ASN A 1 2473 ? 252.162 198.201 163.876 1.00 20.66 ? 2473 ASN A CA    1 
ATOM   7963  C  C     . ASN A 1 2473 ? 252.189 199.709 164.095 1.00 19.95 ? 2473 ASN A C     1 
ATOM   7964  O  O     . ASN A 1 2473 ? 252.783 200.447 163.302 1.00 21.84 ? 2473 ASN A O     1 
ATOM   7965  C  CB    . ASN A 1 2473 ? 250.972 197.799 163.005 1.00 14.72 ? 2473 ASN A CB    1 
ATOM   7966  C  CG    . ASN A 1 2473 ? 251.091 196.385 162.472 1.00 20.22 ? 2473 ASN A CG    1 
ATOM   7967  O  OD1   . ASN A 1 2473 ? 252.053 195.677 162.769 1.00 19.98 ? 2473 ASN A OD1   1 
ATOM   7968  N  ND2   . ASN A 1 2473 ? 250.115 195.966 161.677 1.00 19.23 ? 2473 ASN A ND2   1 
ATOM   7969  N  N     . ALA A 1 2474 ? 251.543 200.184 165.162 1.00 18.71 ? 2474 ALA A N     1 
ATOM   7970  C  CA    . ALA A 1 2474 ? 251.648 201.595 165.517 1.00 19.43 ? 2474 ALA A CA    1 
ATOM   7971  C  C     . ALA A 1 2474 ? 253.076 201.958 165.902 1.00 25.87 ? 2474 ALA A C     1 
ATOM   7972  O  O     . ALA A 1 2474 ? 253.583 203.016 165.511 1.00 26.75 ? 2474 ALA A O     1 
ATOM   7973  C  CB    . ALA A 1 2474 ? 250.681 201.921 166.654 1.00 14.78 ? 2474 ALA A CB    1 
ATOM   7974  N  N     . ASN A 1 2475 ? 253.744 201.091 166.669 1.00 22.11 ? 2475 ASN A N     1 
ATOM   7975  C  CA    . ASN A 1 2475 ? 255.137 201.320 167.027 1.00 21.64 ? 2475 ASN A CA    1 
ATOM   7976  C  C     . ASN A 1 2475 ? 256.070 201.200 165.832 1.00 22.45 ? 2475 ASN A C     1 
ATOM   7977  O  O     . ASN A 1 2475 ? 257.159 201.782 165.851 1.00 30.36 ? 2475 ASN A O     1 
ATOM   7978  C  CB    . ASN A 1 2475 ? 255.581 200.333 168.107 1.00 23.68 ? 2475 ASN A CB    1 
ATOM   7979  C  CG    . ASN A 1 2475 ? 254.720 200.394 169.346 1.00 27.00 ? 2475 ASN A CG    1 
ATOM   7980  O  OD1   . ASN A 1 2475 ? 253.870 201.273 169.487 1.00 20.26 ? 2475 ASN A OD1   1 
ATOM   7981  N  ND2   . ASN A 1 2475 ? 254.936 199.454 170.257 1.00 24.66 ? 2475 ASN A ND2   1 
ATOM   7982  N  N     . HIS A 1 2476 ? 255.671 200.464 164.800 1.00 17.01 ? 2476 HIS A N     1 
ATOM   7983  C  CA    . HIS A 1 2476 ? 256.489 200.244 163.607 1.00 21.33 ? 2476 HIS A CA    1 
ATOM   7984  C  C     . HIS A 1 2476 ? 255.673 200.616 162.377 1.00 26.68 ? 2476 HIS A C     1 
ATOM   7985  O  O     . HIS A 1 2476 ? 255.232 199.741 161.622 1.00 32.55 ? 2476 HIS A O     1 
ATOM   7986  C  CB    . HIS A 1 2476 ? 256.960 198.792 163.518 1.00 18.81 ? 2476 HIS A CB    1 
ATOM   7987  C  CG    . HIS A 1 2476 ? 257.694 198.311 164.730 1.00 17.74 ? 2476 HIS A CG    1 
ATOM   7988  N  ND1   . HIS A 1 2476 ? 257.066 198.068 165.932 1.00 20.85 ? 2476 HIS A ND1   1 
ATOM   7989  C  CD2   . HIS A 1 2476 ? 258.998 197.997 164.916 1.00 17.40 ? 2476 HIS A CD2   1 
ATOM   7990  C  CE1   . HIS A 1 2476 ? 257.954 197.644 166.813 1.00 24.90 ? 2476 HIS A CE1   1 
ATOM   7991  N  NE2   . HIS A 1 2476 ? 259.132 197.588 166.221 1.00 22.17 ? 2476 HIS A NE2   1 
ATOM   7992  N  N     . PRO A 1 2477 ? 255.441 201.911 162.149 1.00 24.90 ? 2477 PRO A N     1 
ATOM   7993  C  CA    . PRO A 1 2477 ? 254.695 202.313 160.947 1.00 21.95 ? 2477 PRO A CA    1 
ATOM   7994  C  C     . PRO A 1 2477 ? 255.406 201.943 159.661 1.00 29.36 ? 2477 PRO A C     1 
ATOM   7995  O  O     . PRO A 1 2477 ? 254.753 201.836 158.615 1.00 33.41 ? 2477 PRO A O     1 
ATOM   7996  C  CB    . PRO A 1 2477 ? 254.567 203.835 161.100 1.00 27.59 ? 2477 PRO A CB    1 
ATOM   7997  C  CG    . PRO A 1 2477 ? 254.862 204.115 162.538 1.00 21.20 ? 2477 PRO A CG    1 
ATOM   7998  C  CD    . PRO A 1 2477 ? 255.847 203.074 162.954 1.00 24.74 ? 2477 PRO A CD    1 
ATOM   7999  N  N     . ASP A 1 2478 ? 256.722 201.741 159.708 1.00 29.26 ? 2478 ASP A N     1 
ATOM   8000  C  CA    . ASP A 1 2478 ? 257.477 201.387 158.513 1.00 33.18 ? 2478 ASP A CA    1 
ATOM   8001  C  C     . ASP A 1 2478 ? 257.251 199.931 158.122 1.00 31.17 ? 2478 ASP A C     1 
ATOM   8002  O  O     . ASP A 1 2478 ? 256.866 199.635 156.986 1.00 39.99 ? 2478 ASP A O     1 
ATOM   8003  C  CB    . ASP A 1 2478 ? 258.965 201.667 158.739 1.00 31.25 ? 2478 ASP A CB    1 
ATOM   8004  C  CG    . ASP A 1 2478 ? 259.846 201.044 157.678 1.00 41.67 ? 2478 ASP A CG    1 
ATOM   8005  O  OD1   . ASP A 1 2478 ? 259.579 201.263 156.477 1.00 42.43 ? 2478 ASP A OD1   1 
ATOM   8006  O  OD2   . ASP A 1 2478 ? 260.812 200.344 158.045 1.00 43.84 ? 2478 ASP A OD2   1 
ATOM   8007  N  N     . PHE A 1 2479 ? 257.476 199.008 159.054 1.00 33.32 ? 2479 PHE A N     1 
ATOM   8008  C  CA    . PHE A 1 2479 ? 257.387 197.576 158.772 1.00 37.16 ? 2479 PHE A CA    1 
ATOM   8009  C  C     . PHE A 1 2479 ? 256.321 196.927 159.641 1.00 32.83 ? 2479 PHE A C     1 
ATOM   8010  O  O     . PHE A 1 2479 ? 256.605 196.526 160.784 1.00 32.99 ? 2479 PHE A O     1 
ATOM   8011  C  CB    . PHE A 1 2479 ? 258.738 196.898 158.996 1.00 29.88 ? 2479 PHE A CB    1 
ATOM   8012  C  CG    . PHE A 1 2479 ? 259.785 197.288 157.994 1.00 33.93 ? 2479 PHE A CG    1 
ATOM   8013  C  CD1   . PHE A 1 2479 ? 259.425 197.738 156.735 1.00 37.05 ? 2479 PHE A CD1   1 
ATOM   8014  C  CD2   . PHE A 1 2479 ? 261.130 197.205 158.312 1.00 36.45 ? 2479 PHE A CD2   1 
ATOM   8015  C  CE1   . PHE A 1 2479 ? 260.388 198.095 155.809 1.00 38.72 ? 2479 PHE A CE1   1 
ATOM   8016  C  CE2   . PHE A 1 2479 ? 262.098 197.562 157.391 1.00 33.04 ? 2479 PHE A CE2   1 
ATOM   8017  C  CZ    . PHE A 1 2479 ? 261.727 198.008 156.138 1.00 35.92 ? 2479 PHE A CZ    1 
ATOM   8018  N  N     . PRO A 1 2480 ? 255.089 196.798 159.154 1.00 29.98 ? 2480 PRO A N     1 
ATOM   8019  C  CA    . PRO A 1 2480 ? 254.077 196.049 159.902 1.00 26.07 ? 2480 PRO A CA    1 
ATOM   8020  C  C     . PRO A 1 2480 ? 254.415 194.566 159.941 1.00 25.95 ? 2480 PRO A C     1 
ATOM   8021  O  O     . PRO A 1 2480 ? 255.116 194.033 159.075 1.00 27.47 ? 2480 PRO A O     1 
ATOM   8022  C  CB    . PRO A 1 2480 ? 252.786 196.309 159.121 1.00 26.18 ? 2480 PRO A CB    1 
ATOM   8023  C  CG    . PRO A 1 2480 ? 253.246 196.629 157.739 1.00 28.65 ? 2480 PRO A CG    1 
ATOM   8024  C  CD    . PRO A 1 2480 ? 254.556 197.349 157.898 1.00 31.58 ? 2480 PRO A CD    1 
ATOM   8025  N  N     . MET A 1 2481 ? 253.905 193.904 160.976 1.00 20.33 ? 2481 MET A N     1 
ATOM   8026  C  CA    . MET A 1 2481 ? 254.204 192.496 161.194 1.00 21.36 ? 2481 MET A CA    1 
ATOM   8027  C  C     . MET A 1 2481 ? 253.787 191.662 159.989 1.00 23.18 ? 2481 MET A C     1 
ATOM   8028  O  O     . MET A 1 2481 ? 252.683 191.819 159.460 1.00 26.18 ? 2481 MET A O     1 
ATOM   8029  C  CB    . MET A 1 2481 ? 253.489 192.000 162.449 1.00 19.00 ? 2481 MET A CB    1 
ATOM   8030  C  CG    . MET A 1 2481 ? 253.826 190.574 162.835 1.00 18.55 ? 2481 MET A CG    1 
ATOM   8031  S  SD    . MET A 1 2481 ? 252.963 190.048 164.326 1.00 37.20 ? 2481 MET A SD    1 
ATOM   8032  C  CE    . MET A 1 2481 ? 253.832 190.993 165.570 1.00 20.06 ? 2481 MET A CE    1 
ATOM   8033  N  N     . GLN A 1 2482 ? 254.679 190.781 159.553 1.00 22.42 ? 2482 GLN A N     1 
ATOM   8034  C  CA    . GLN A 1 2482 ? 254.410 189.895 158.435 1.00 17.77 ? 2482 GLN A CA    1 
ATOM   8035  C  C     . GLN A 1 2482 ? 253.726 188.621 158.918 1.00 18.42 ? 2482 GLN A C     1 
ATOM   8036  O  O     . GLN A 1 2482 ? 253.699 188.311 160.111 1.00 24.56 ? 2482 GLN A O     1 
ATOM   8037  C  CB    . GLN A 1 2482 ? 255.702 189.564 157.689 1.00 18.07 ? 2482 GLN A CB    1 
ATOM   8038  C  CG    . GLN A 1 2482 ? 256.339 190.766 157.022 1.00 20.19 ? 2482 GLN A CG    1 
ATOM   8039  C  CD    . GLN A 1 2482 ? 255.330 191.607 156.267 1.00 21.00 ? 2482 GLN A CD    1 
ATOM   8040  O  OE1   . GLN A 1 2482 ? 254.675 191.130 155.341 1.00 26.11 ? 2482 GLN A OE1   1 
ATOM   8041  N  NE2   . GLN A 1 2482 ? 255.194 192.864 156.665 1.00 23.40 ? 2482 GLN A NE2   1 
ATOM   8042  N  N     . ILE A 1 2483 ? 253.172 187.873 157.961 1.00 18.04 ? 2483 ILE A N     1 
ATOM   8043  C  CA    . ILE A 1 2483 ? 252.419 186.667 158.296 1.00 16.25 ? 2483 ILE A CA    1 
ATOM   8044  C  C     . ILE A 1 2483 ? 253.307 185.653 159.001 1.00 21.48 ? 2483 ILE A C     1 
ATOM   8045  O  O     . ILE A 1 2483 ? 252.855 184.953 159.916 1.00 27.85 ? 2483 ILE A O     1 
ATOM   8046  C  CB    . ILE A 1 2483 ? 251.774 186.067 157.031 1.00 22.77 ? 2483 ILE A CB    1 
ATOM   8047  C  CG1   . ILE A 1 2483 ? 251.097 187.159 156.205 1.00 24.19 ? 2483 ILE A CG1   1 
ATOM   8048  C  CG2   . ILE A 1 2483 ? 250.766 184.996 157.407 1.00 19.04 ? 2483 ILE A CG2   1 
ATOM   8049  C  CD1   . ILE A 1 2483 ? 250.026 187.921 156.955 1.00 19.02 ? 2483 ILE A CD1   1 
ATOM   8050  N  N     . GLU A 1 2484 ? 254.573 185.553 158.596 1.00 18.52 ? 2484 GLU A N     1 
ATOM   8051  C  CA    . GLU A 1 2484 ? 255.490 184.622 159.246 1.00 15.32 ? 2484 GLU A CA    1 
ATOM   8052  C  C     . GLU A 1 2484 ? 255.674 184.977 160.718 1.00 20.04 ? 2484 GLU A C     1 
ATOM   8053  O  O     . GLU A 1 2484 ? 255.671 184.096 161.586 1.00 16.08 ? 2484 GLU A O     1 
ATOM   8054  C  CB    . GLU A 1 2484 ? 256.827 184.610 158.497 1.00 15.63 ? 2484 GLU A CB    1 
ATOM   8055  C  CG    . GLU A 1 2484 ? 257.883 183.657 159.036 1.00 22.74 ? 2484 GLU A CG    1 
ATOM   8056  C  CD    . GLU A 1 2484 ? 258.660 184.230 160.204 1.00 26.39 ? 2484 GLU A CD    1 
ATOM   8057  O  OE1   . GLU A 1 2484 ? 259.229 183.441 160.986 1.00 22.47 ? 2484 GLU A OE1   1 
ATOM   8058  O  OE2   . GLU A 1 2484 ? 258.706 185.470 160.339 1.00 28.84 ? 2484 GLU A OE2   1 
ATOM   8059  N  N     . GLN A 1 2485 ? 255.832 186.267 161.021 1.00 20.84 ? 2485 GLN A N     1 
ATOM   8060  C  CA    . GLN A 1 2485 ? 255.880 186.684 162.419 1.00 16.76 ? 2485 GLN A CA    1 
ATOM   8061  C  C     . GLN A 1 2485 ? 254.496 186.624 163.052 1.00 18.08 ? 2485 GLN A C     1 
ATOM   8062  O  O     . GLN A 1 2485 ? 254.361 186.244 164.220 1.00 18.27 ? 2485 GLN A O     1 
ATOM   8063  C  CB    . GLN A 1 2485 ? 256.461 188.092 162.539 1.00 20.54 ? 2485 GLN A CB    1 
ATOM   8064  C  CG    . GLN A 1 2485 ? 256.628 188.561 163.979 1.00 16.94 ? 2485 GLN A CG    1 
ATOM   8065  C  CD    . GLN A 1 2485 ? 257.256 189.935 164.084 1.00 22.00 ? 2485 GLN A CD    1 
ATOM   8066  O  OE1   . GLN A 1 2485 ? 257.488 190.439 165.181 1.00 25.94 ? 2485 GLN A OE1   1 
ATOM   8067  N  NE2   . GLN A 1 2485 ? 257.529 190.551 162.941 1.00 26.78 ? 2485 GLN A NE2   1 
ATOM   8068  N  N     . LEU A 1 2486 ? 253.458 186.995 162.295 1.00 17.85 ? 2486 LEU A N     1 
ATOM   8069  C  CA    . LEU A 1 2486 ? 252.096 186.904 162.810 1.00 14.46 ? 2486 LEU A CA    1 
ATOM   8070  C  C     . LEU A 1 2486 ? 251.725 185.466 163.135 1.00 14.59 ? 2486 LEU A C     1 
ATOM   8071  O  O     . LEU A 1 2486 ? 251.143 185.192 164.189 1.00 15.50 ? 2486 LEU A O     1 
ATOM   8072  C  CB    . LEU A 1 2486 ? 251.109 187.493 161.805 1.00 16.03 ? 2486 LEU A CB    1 
ATOM   8073  C  CG    . LEU A 1 2486 ? 249.654 187.569 162.276 1.00 17.09 ? 2486 LEU A CG    1 
ATOM   8074  C  CD1   . LEU A 1 2486 ? 249.547 188.345 163.578 1.00 11.24 ? 2486 LEU A CD1   1 
ATOM   8075  C  CD2   . LEU A 1 2486 ? 248.776 188.190 161.207 1.00 14.52 ? 2486 LEU A CD2   1 
ATOM   8076  N  N     . GLU A 1 2487 ? 252.059 184.532 162.242 1.00 13.77 ? 2487 GLU A N     1 
ATOM   8077  C  CA    . GLU A 1 2487 ? 251.827 183.123 162.534 1.00 15.54 ? 2487 GLU A CA    1 
ATOM   8078  C  C     . GLU A 1 2487 ? 252.628 182.692 163.750 1.00 13.49 ? 2487 GLU A C     1 
ATOM   8079  O  O     . GLU A 1 2487 ? 252.131 181.958 164.609 1.00 13.28 ? 2487 GLU A O     1 
ATOM   8080  C  CB    . GLU A 1 2487 ? 252.191 182.262 161.324 1.00 12.90 ? 2487 GLU A CB    1 
ATOM   8081  C  CG    . GLU A 1 2487 ? 251.757 180.815 161.443 1.00 17.59 ? 2487 GLU A CG    1 
ATOM   8082  C  CD    . GLU A 1 2487 ? 251.698 180.113 160.102 1.00 30.85 ? 2487 GLU A CD    1 
ATOM   8083  O  OE1   . GLU A 1 2487 ? 252.723 180.106 159.391 1.00 28.88 ? 2487 GLU A OE1   1 
ATOM   8084  O  OE2   . GLU A 1 2487 ? 250.627 179.568 159.760 1.00 35.59 ? 2487 GLU A OE2   1 
ATOM   8085  N  N     . ARG A 1 2488 ? 253.872 183.158 163.846 1.00 17.89 ? 2488 ARG A N     1 
ATOM   8086  C  CA    . ARG A 1 2488 ? 254.755 182.703 164.910 1.00 14.92 ? 2488 ARG A CA    1 
ATOM   8087  C  C     . ARG A 1 2488 ? 254.268 183.199 166.270 1.00 13.24 ? 2488 ARG A C     1 
ATOM   8088  O  O     . ARG A 1 2488 ? 254.437 182.516 167.288 1.00 15.77 ? 2488 ARG A O     1 
ATOM   8089  C  CB    . ARG A 1 2488 ? 256.180 183.175 164.609 1.00 17.31 ? 2488 ARG A CB    1 
ATOM   8090  C  CG    . ARG A 1 2488 ? 257.221 182.615 165.530 1.00 21.49 ? 2488 ARG A CG    1 
ATOM   8091  C  CD    . ARG A 1 2488 ? 258.643 183.015 165.187 1.00 20.26 ? 2488 ARG A CD    1 
ATOM   8092  N  NE    . ARG A 1 2488 ? 258.882 184.442 165.350 1.00 19.52 ? 2488 ARG A NE    1 
ATOM   8093  C  CZ    . ARG A 1 2488 ? 259.143 185.276 164.355 1.00 21.34 ? 2488 ARG A CZ    1 
ATOM   8094  N  NH1   . ARG A 1 2488 ? 259.175 184.865 163.101 1.00 20.48 ? 2488 ARG A NH1   1 
ATOM   8095  N  NH2   . ARG A 1 2488 ? 259.386 186.554 164.629 1.00 27.66 ? 2488 ARG A NH2   1 
ATOM   8096  N  N     . TYR A 1 2489 ? 253.651 184.383 166.300 1.00 13.33 ? 2489 TYR A N     1 
ATOM   8097  C  CA    . TYR A 1 2489 ? 253.131 184.944 167.545 1.00 6.35  ? 2489 TYR A CA    1 
ATOM   8098  C  C     . TYR A 1 2489 ? 251.835 184.269 167.985 1.00 9.42  ? 2489 TYR A C     1 
ATOM   8099  O  O     . TYR A 1 2489 ? 251.659 183.974 169.172 1.00 11.22 ? 2489 TYR A O     1 
ATOM   8100  C  CB    . TYR A 1 2489 ? 252.912 186.449 167.376 1.00 7.30  ? 2489 TYR A CB    1 
ATOM   8101  C  CG    . TYR A 1 2489 ? 252.403 187.152 168.614 1.00 6.23  ? 2489 TYR A CG    1 
ATOM   8102  C  CD1   . TYR A 1 2489 ? 253.089 187.076 169.817 1.00 7.17  ? 2489 TYR A CD1   1 
ATOM   8103  C  CD2   . TYR A 1 2489 ? 251.224 187.886 168.578 1.00 6.94  ? 2489 TYR A CD2   1 
ATOM   8104  C  CE1   . TYR A 1 2489 ? 252.618 187.718 170.947 1.00 7.75  ? 2489 TYR A CE1   1 
ATOM   8105  C  CE2   . TYR A 1 2489 ? 250.746 188.530 169.704 1.00 5.34  ? 2489 TYR A CE2   1 
ATOM   8106  C  CZ    . TYR A 1 2489 ? 251.447 188.442 170.884 1.00 6.94  ? 2489 TYR A CZ    1 
ATOM   8107  O  OH    . TYR A 1 2489 ? 250.973 189.081 172.005 1.00 9.79  ? 2489 TYR A OH    1 
ATOM   8108  N  N     . ILE A 1 2490 ? 250.912 184.030 167.050 1.00 11.02 ? 2490 ILE A N     1 
ATOM   8109  C  CA    . ILE A 1 2490 ? 249.562 183.606 167.420 1.00 5.85  ? 2490 ILE A CA    1 
ATOM   8110  C  C     . ILE A 1 2490 ? 249.577 182.209 168.030 1.00 4.93  ? 2490 ILE A C     1 
ATOM   8111  O  O     . ILE A 1 2490 ? 248.886 181.943 169.021 1.00 6.66  ? 2490 ILE A O     1 
ATOM   8112  C  CB    . ILE A 1 2490 ? 248.621 183.686 166.203 1.00 6.75  ? 2490 ILE A CB    1 
ATOM   8113  C  CG1   . ILE A 1 2490 ? 248.424 185.138 165.765 1.00 5.74  ? 2490 ILE A CG1   1 
ATOM   8114  C  CG2   . ILE A 1 2490 ? 247.273 183.065 166.524 1.00 8.93  ? 2490 ILE A CG2   1 
ATOM   8115  C  CD1   . ILE A 1 2490 ? 247.859 186.036 166.840 1.00 5.42  ? 2490 ILE A CD1   1 
ATOM   8116  N  N     . GLN A 1 2491 ? 250.357 181.294 167.449 1.00 4.26  ? 2491 GLN A N     1 
ATOM   8117  C  CA    . GLN A 1 2491 ? 250.363 179.915 167.931 1.00 5.10  ? 2491 GLN A CA    1 
ATOM   8118  C  C     . GLN A 1 2491 ? 250.851 179.829 169.370 1.00 9.26  ? 2491 GLN A C     1 
ATOM   8119  O  O     . GLN A 1 2491 ? 250.266 179.111 170.190 1.00 8.21  ? 2491 GLN A O     1 
ATOM   8120  C  CB    . GLN A 1 2491 ? 251.226 179.040 167.022 1.00 7.80  ? 2491 GLN A CB    1 
ATOM   8121  C  CG    . GLN A 1 2491 ? 251.041 179.309 165.548 1.00 11.21 ? 2491 GLN A CG    1 
ATOM   8122  C  CD    . GLN A 1 2491 ? 251.264 178.085 164.693 1.00 19.13 ? 2491 GLN A CD    1 
ATOM   8123  O  OE1   . GLN A 1 2491 ? 252.168 177.291 164.944 1.00 17.25 ? 2491 GLN A OE1   1 
ATOM   8124  N  NE2   . GLN A 1 2491 ? 250.433 177.924 163.670 1.00 25.67 ? 2491 GLN A NE2   1 
ATOM   8125  N  N     . ARG A 1 2492 ? 251.922 180.552 169.697 1.00 10.64 ? 2492 ARG A N     1 
ATOM   8126  C  CA    . ARG A 1 2492 ? 252.417 180.554 171.070 1.00 5.02  ? 2492 ARG A CA    1 
ATOM   8127  C  C     . ARG A 1 2492 ? 251.479 181.298 172.008 1.00 3.58  ? 2492 ARG A C     1 
ATOM   8128  O  O     . ARG A 1 2492 ? 251.272 180.867 173.148 1.00 4.53  ? 2492 ARG A O     1 
ATOM   8129  C  CB    . ARG A 1 2492 ? 253.821 181.145 171.116 1.00 6.18  ? 2492 ARG A CB    1 
ATOM   8130  C  CG    . ARG A 1 2492 ? 254.833 180.262 170.450 1.00 9.47  ? 2492 ARG A CG    1 
ATOM   8131  C  CD    . ARG A 1 2492 ? 256.214 180.861 170.493 1.00 12.80 ? 2492 ARG A CD    1 
ATOM   8132  N  NE    . ARG A 1 2492 ? 257.181 179.965 169.875 1.00 15.28 ? 2492 ARG A NE    1 
ATOM   8133  C  CZ    . ARG A 1 2492 ? 257.497 179.989 168.591 1.00 13.14 ? 2492 ARG A CZ    1 
ATOM   8134  N  NH1   . ARG A 1 2492 ? 256.842 180.752 167.742 1.00 9.97  ? 2492 ARG A NH1   1 
ATOM   8135  N  NH2   . ARG A 1 2492 ? 258.472 179.202 168.144 1.00 14.24 ? 2492 ARG A NH2   1 
ATOM   8136  N  N     . TYR A 1 2493 ? 250.897 182.409 171.556 1.00 2.29  ? 2493 TYR A N     1 
ATOM   8137  C  CA    . TYR A 1 2493 ? 249.948 183.112 172.411 1.00 2.49  ? 2493 TYR A CA    1 
ATOM   8138  C  C     . TYR A 1 2493 ? 248.715 182.259 172.673 1.00 5.22  ? 2493 TYR A C     1 
ATOM   8139  O  O     . TYR A 1 2493 ? 248.157 182.289 173.775 1.00 6.56  ? 2493 TYR A O     1 
ATOM   8140  C  CB    . TYR A 1 2493 ? 249.555 184.451 171.793 1.00 3.67  ? 2493 TYR A CB    1 
ATOM   8141  C  CG    . TYR A 1 2493 ? 248.845 185.365 172.767 1.00 5.18  ? 2493 TYR A CG    1 
ATOM   8142  C  CD1   . TYR A 1 2493 ? 247.489 185.214 173.031 1.00 5.04  ? 2493 TYR A CD1   1 
ATOM   8143  C  CD2   . TYR A 1 2493 ? 249.532 186.370 173.431 1.00 3.44  ? 2493 TYR A CD2   1 
ATOM   8144  C  CE1   . TYR A 1 2493 ? 246.841 186.038 173.922 1.00 4.41  ? 2493 TYR A CE1   1 
ATOM   8145  C  CE2   . TYR A 1 2493 ? 248.890 187.201 174.322 1.00 4.05  ? 2493 TYR A CE2   1 
ATOM   8146  C  CZ    . TYR A 1 2493 ? 247.544 187.031 174.564 1.00 6.44  ? 2493 TYR A CZ    1 
ATOM   8147  O  OH    . TYR A 1 2493 ? 246.896 187.856 175.453 1.00 11.33 ? 2493 TYR A OH    1 
ATOM   8148  N  N     . LEU A 1 2494 ? 248.278 181.495 171.670 1.00 6.87  ? 2494 LEU A N     1 
ATOM   8149  C  CA    . LEU A 1 2494 ? 247.144 180.600 171.867 1.00 3.54  ? 2494 LEU A CA    1 
ATOM   8150  C  C     . LEU A 1 2494 ? 247.434 179.572 172.950 1.00 2.93  ? 2494 LEU A C     1 
ATOM   8151  O  O     . LEU A 1 2494 ? 246.592 179.318 173.818 1.00 3.33  ? 2494 LEU A O     1 
ATOM   8152  C  CB    . LEU A 1 2494 ? 246.789 179.912 170.551 1.00 5.19  ? 2494 LEU A CB    1 
ATOM   8153  C  CG    . LEU A 1 2494 ? 245.755 178.790 170.615 1.00 2.62  ? 2494 LEU A CG    1 
ATOM   8154  C  CD1   . LEU A 1 2494 ? 244.394 179.322 171.035 1.00 2.08  ? 2494 LEU A CD1   1 
ATOM   8155  C  CD2   . LEU A 1 2494 ? 245.669 178.106 169.272 1.00 7.39  ? 2494 LEU A CD2   1 
ATOM   8156  N  N     . VAL A 1 2495 ? 248.629 178.977 172.923 1.00 4.90  ? 2495 VAL A N     1 
ATOM   8157  C  CA    . VAL A 1 2495 ? 249.028 178.056 173.984 1.00 3.59  ? 2495 VAL A CA    1 
ATOM   8158  C  C     . VAL A 1 2495 ? 249.088 178.785 175.320 1.00 3.36  ? 2495 VAL A C     1 
ATOM   8159  O  O     . VAL A 1 2495 ? 248.617 178.280 176.345 1.00 2.96  ? 2495 VAL A O     1 
ATOM   8160  C  CB    . VAL A 1 2495 ? 250.377 177.400 173.637 1.00 3.00  ? 2495 VAL A CB    1 
ATOM   8161  C  CG1   . VAL A 1 2495 ? 250.904 176.601 174.821 1.00 3.72  ? 2495 VAL A CG1   1 
ATOM   8162  C  CG2   . VAL A 1 2495 ? 250.236 176.520 172.410 1.00 3.96  ? 2495 VAL A CG2   1 
ATOM   8163  N  N     . TYR A 1 2496 ? 249.660 179.991 175.322 1.00 4.15  ? 2496 TYR A N     1 
ATOM   8164  C  CA    . TYR A 1 2496 ? 249.704 180.800 176.533 1.00 2.37  ? 2496 TYR A CA    1 
ATOM   8165  C  C     . TYR A 1 2496 ? 248.301 181.119 177.035 1.00 3.70  ? 2496 TYR A C     1 
ATOM   8166  O  O     . TYR A 1 2496 ? 248.027 181.023 178.236 1.00 3.44  ? 2496 TYR A O     1 
ATOM   8167  C  CB    . TYR A 1 2496 ? 250.494 182.081 176.253 1.00 2.70  ? 2496 TYR A CB    1 
ATOM   8168  C  CG    . TYR A 1 2496 ? 250.317 183.191 177.263 1.00 2.69  ? 2496 TYR A CG    1 
ATOM   8169  C  CD1   . TYR A 1 2496 ? 251.081 183.232 178.421 1.00 1.93  ? 2496 TYR A CD1   1 
ATOM   8170  C  CD2   . TYR A 1 2496 ? 249.406 184.215 177.044 1.00 3.12  ? 2496 TYR A CD2   1 
ATOM   8171  C  CE1   . TYR A 1 2496 ? 250.929 184.248 179.338 1.00 3.83  ? 2496 TYR A CE1   1 
ATOM   8172  C  CE2   . TYR A 1 2496 ? 249.247 185.233 177.956 1.00 2.60  ? 2496 TYR A CE2   1 
ATOM   8173  C  CZ    . TYR A 1 2496 ? 250.009 185.248 179.101 1.00 3.19  ? 2496 TYR A CZ    1 
ATOM   8174  O  OH    . TYR A 1 2496 ? 249.851 186.265 180.009 1.00 6.92  ? 2496 TYR A OH    1 
ATOM   8175  N  N     . ALA A 1 2497 ? 247.394 181.480 176.127 1.00 2.61  ? 2497 ALA A N     1 
ATOM   8176  C  CA    . ALA A 1 2497 ? 246.033 181.817 176.528 1.00 1.52  ? 2497 ALA A CA    1 
ATOM   8177  C  C     . ALA A 1 2497 ? 245.278 180.590 177.028 1.00 1.28  ? 2497 ALA A C     1 
ATOM   8178  O  O     . ALA A 1 2497 ? 244.460 180.695 177.948 1.00 1.15  ? 2497 ALA A O     1 
ATOM   8179  C  CB    . ALA A 1 2497 ? 245.289 182.474 175.367 1.00 3.45  ? 2497 ALA A CB    1 
ATOM   8180  N  N     . ILE A 1 2498 ? 245.539 179.424 176.433 1.00 2.00  ? 2498 ILE A N     1 
ATOM   8181  C  CA    . ILE A 1 2498 ? 244.861 178.198 176.851 1.00 1.56  ? 2498 ILE A CA    1 
ATOM   8182  C  C     . ILE A 1 2498 ? 245.219 177.851 178.290 1.00 1.34  ? 2498 ILE A C     1 
ATOM   8183  O  O     . ILE A 1 2498 ? 244.352 177.469 179.086 1.00 1.14  ? 2498 ILE A O     1 
ATOM   8184  C  CB    . ILE A 1 2498 ? 245.201 177.047 175.884 1.00 2.01  ? 2498 ILE A CB    1 
ATOM   8185  C  CG1   . ILE A 1 2498 ? 244.407 177.189 174.585 1.00 1.64  ? 2498 ILE A CG1   1 
ATOM   8186  C  CG2   . ILE A 1 2498 ? 244.940 175.695 176.529 1.00 1.48  ? 2498 ILE A CG2   1 
ATOM   8187  C  CD1   . ILE A 1 2498 ? 244.813 176.203 173.516 1.00 2.32  ? 2498 ILE A CD1   1 
ATOM   8188  N  N     . LEU A 1 2499 ? 246.499 177.974 178.647 1.00 1.78  ? 2499 LEU A N     1 
ATOM   8189  C  CA    . LEU A 1 2499 ? 246.933 177.617 179.995 1.00 1.81  ? 2499 LEU A CA    1 
ATOM   8190  C  C     . LEU A 1 2499 ? 246.271 178.495 181.050 1.00 1.41  ? 2499 LEU A C     1 
ATOM   8191  O  O     . LEU A 1 2499 ? 245.804 177.994 182.079 1.00 1.54  ? 2499 LEU A O     1 
ATOM   8192  C  CB    . LEU A 1 2499 ? 248.451 177.721 180.097 1.00 2.23  ? 2499 LEU A CB    1 
ATOM   8193  C  CG    . LEU A 1 2499 ? 249.259 176.550 179.549 1.00 3.16  ? 2499 LEU A CG    1 
ATOM   8194  C  CD1   . LEU A 1 2499 ? 250.715 176.938 179.468 1.00 3.50  ? 2499 LEU A CD1   1 
ATOM   8195  C  CD2   . LEU A 1 2499 ? 249.081 175.326 180.426 1.00 4.65  ? 2499 LEU A CD2   1 
ATOM   8196  N  N     . TRP A 1 2500 ? 246.218 179.805 180.811 1.00 0.88  ? 2500 TRP A N     1 
ATOM   8197  C  CA    . TRP A 1 2500 ? 245.653 180.710 181.804 1.00 0.78  ? 2500 TRP A CA    1 
ATOM   8198  C  C     . TRP A 1 2500 ? 244.133 180.676 181.827 1.00 0.91  ? 2500 TRP A C     1 
ATOM   8199  O  O     . TRP A 1 2500 ? 243.530 180.888 182.883 1.00 1.23  ? 2500 TRP A O     1 
ATOM   8200  C  CB    . TRP A 1 2500 ? 246.156 182.131 181.561 1.00 1.06  ? 2500 TRP A CB    1 
ATOM   8201  C  CG    . TRP A 1 2500 ? 247.566 182.309 182.007 1.00 0.75  ? 2500 TRP A CG    1 
ATOM   8202  C  CD1   . TRP A 1 2500 ? 248.670 182.413 181.216 1.00 0.70  ? 2500 TRP A CD1   1 
ATOM   8203  C  CD2   . TRP A 1 2500 ? 248.030 182.374 183.357 1.00 0.73  ? 2500 TRP A CD2   1 
ATOM   8204  N  NE1   . TRP A 1 2500 ? 249.793 182.553 181.990 1.00 1.68  ? 2500 TRP A NE1   1 
ATOM   8205  C  CE2   . TRP A 1 2500 ? 249.427 182.531 183.309 1.00 2.45  ? 2500 TRP A CE2   1 
ATOM   8206  C  CE3   . TRP A 1 2500 ? 247.400 182.318 184.603 1.00 0.86  ? 2500 TRP A CE3   1 
ATOM   8207  C  CZ2   . TRP A 1 2500 ? 250.205 182.635 184.459 1.00 2.12  ? 2500 TRP A CZ2   1 
ATOM   8208  C  CZ3   . TRP A 1 2500 ? 248.172 182.419 185.742 1.00 1.23  ? 2500 TRP A CZ3   1 
ATOM   8209  C  CH2   . TRP A 1 2500 ? 249.559 182.577 185.662 1.00 1.70  ? 2500 TRP A CH2   1 
ATOM   8210  N  N     . SER A 1 2501 ? 243.496 180.416 180.687 1.00 1.48  ? 2501 SER A N     1 
ATOM   8211  C  CA    . SER A 1 2501 ? 242.043 180.344 180.644 1.00 0.63  ? 2501 SER A CA    1 
ATOM   8212  C  C     . SER A 1 2501 ? 241.501 179.060 181.251 1.00 1.13  ? 2501 SER A C     1 
ATOM   8213  O  O     . SER A 1 2501 ? 240.356 179.043 181.711 1.00 3.99  ? 2501 SER A O     1 
ATOM   8214  C  CB    . SER A 1 2501 ? 241.556 180.480 179.203 1.00 0.72  ? 2501 SER A CB    1 
ATOM   8215  O  OG    . SER A 1 2501 ? 242.025 181.686 178.629 1.00 0.61  ? 2501 SER A OG    1 
ATOM   8216  N  N     . LEU A 1 2502 ? 242.293 177.988 181.265 1.00 0.75  ? 2502 LEU A N     1 
ATOM   8217  C  CA    . LEU A 1 2502 ? 241.834 176.691 181.732 1.00 1.19  ? 2502 LEU A CA    1 
ATOM   8218  C  C     . LEU A 1 2502 ? 242.432 176.273 183.065 1.00 2.66  ? 2502 LEU A C     1 
ATOM   8219  O  O     . LEU A 1 2502 ? 241.891 175.365 183.705 1.00 6.38  ? 2502 LEU A O     1 
ATOM   8220  C  CB    . LEU A 1 2502 ? 242.148 175.607 180.691 1.00 2.10  ? 2502 LEU A CB    1 
ATOM   8221  C  CG    . LEU A 1 2502 ? 241.172 175.372 179.534 1.00 2.79  ? 2502 LEU A CG    1 
ATOM   8222  C  CD1   . LEU A 1 2502 ? 240.892 176.642 178.741 1.00 1.36  ? 2502 LEU A CD1   1 
ATOM   8223  C  CD2   . LEU A 1 2502 ? 241.715 174.293 178.618 1.00 0.77  ? 2502 LEU A CD2   1 
ATOM   8224  N  N     . SER A 1 2503 ? 243.520 176.905 183.499 1.00 3.89  ? 2503 SER A N     1 
ATOM   8225  C  CA    . SER A 1 2503 ? 244.169 176.550 184.750 1.00 2.21  ? 2503 SER A CA    1 
ATOM   8226  C  C     . SER A 1 2503 ? 244.515 177.755 185.612 1.00 1.80  ? 2503 SER A C     1 
ATOM   8227  O  O     . SER A 1 2503 ? 245.058 177.571 186.707 1.00 4.32  ? 2503 SER A O     1 
ATOM   8228  C  CB    . SER A 1 2503 ? 245.444 175.736 184.480 1.00 2.68  ? 2503 SER A CB    1 
ATOM   8229  O  OG    . SER A 1 2503 ? 246.440 176.534 183.869 1.00 3.60  ? 2503 SER A OG    1 
ATOM   8230  N  N     . GLY A 1 2504 ? 244.213 178.974 185.162 1.00 1.49  ? 2504 GLY A N     1 
ATOM   8231  C  CA    . GLY A 1 2504 ? 244.477 180.156 185.965 1.00 2.13  ? 2504 GLY A CA    1 
ATOM   8232  C  C     . GLY A 1 2504 ? 243.720 180.186 187.275 1.00 0.68  ? 2504 GLY A C     1 
ATOM   8233  O  O     . GLY A 1 2504 ? 244.097 180.935 188.182 1.00 2.90  ? 2504 GLY A O     1 
ATOM   8234  N  N     . ASP A 1 2505 ? 242.661 179.394 187.397 1.00 0.56  ? 2505 ASP A N     1 
ATOM   8235  C  CA    . ASP A 1 2505 ? 241.898 179.274 188.630 1.00 0.97  ? 2505 ASP A CA    1 
ATOM   8236  C  C     . ASP A 1 2505 ? 242.292 178.042 189.436 1.00 2.21  ? 2505 ASP A C     1 
ATOM   8237  O  O     . ASP A 1 2505 ? 241.565 177.652 190.355 1.00 2.46  ? 2505 ASP A O     1 
ATOM   8238  C  CB    . ASP A 1 2505 ? 240.402 179.258 188.316 1.00 1.19  ? 2505 ASP A CB    1 
ATOM   8239  C  CG    . ASP A 1 2505 ? 239.935 177.935 187.751 1.00 6.00  ? 2505 ASP A CG    1 
ATOM   8240  O  OD1   . ASP A 1 2505 ? 240.690 177.308 186.976 1.00 2.81  ? 2505 ASP A OD1   1 
ATOM   8241  O  OD2   . ASP A 1 2505 ? 238.798 177.532 188.067 1.00 11.64 ? 2505 ASP A OD2   1 
ATOM   8242  N  N     . SER A 1 2506 ? 243.423 177.428 189.115 1.00 1.89  ? 2506 SER A N     1 
ATOM   8243  C  CA    . SER A 1 2506 ? 243.914 176.247 189.801 1.00 3.21  ? 2506 SER A CA    1 
ATOM   8244  C  C     . SER A 1 2506 ? 245.282 176.537 190.406 1.00 3.57  ? 2506 SER A C     1 
ATOM   8245  O  O     . SER A 1 2506 ? 245.930 177.534 190.085 1.00 6.28  ? 2506 SER A O     1 
ATOM   8246  C  CB    . SER A 1 2506 ? 243.985 175.049 188.843 1.00 4.48  ? 2506 SER A CB    1 
ATOM   8247  O  OG    . SER A 1 2506 ? 245.085 175.162 187.959 1.00 7.11  ? 2506 SER A OG    1 
ATOM   8248  N  N     . ARG A 1 2507 ? 245.716 175.649 191.296 1.00 4.64  ? 2507 ARG A N     1 
ATOM   8249  C  CA    . ARG A 1 2507 ? 247.002 175.817 191.953 1.00 3.98  ? 2507 ARG A CA    1 
ATOM   8250  C  C     . ARG A 1 2507 ? 248.147 175.542 190.981 1.00 5.12  ? 2507 ARG A C     1 
ATOM   8251  O  O     . ARG A 1 2507 ? 247.952 175.084 189.851 1.00 12.42 ? 2507 ARG A O     1 
ATOM   8252  C  CB    . ARG A 1 2507 ? 247.115 174.898 193.168 1.00 5.04  ? 2507 ARG A CB    1 
ATOM   8253  C  CG    . ARG A 1 2507 ? 245.820 174.694 193.923 1.00 8.13  ? 2507 ARG A CG    1 
ATOM   8254  C  CD    . ARG A 1 2507 ? 245.957 173.583 194.949 1.00 13.43 ? 2507 ARG A CD    1 
ATOM   8255  N  NE    . ARG A 1 2507 ? 246.242 172.292 194.335 1.00 12.14 ? 2507 ARG A NE    1 
ATOM   8256  C  CZ    . ARG A 1 2507 ? 245.385 171.282 194.291 1.00 17.97 ? 2507 ARG A CZ    1 
ATOM   8257  N  NH1   . ARG A 1 2507 ? 244.174 171.378 194.815 1.00 20.82 ? 2507 ARG A NH1   1 
ATOM   8258  N  NH2   . ARG A 1 2507 ? 245.750 170.145 193.705 1.00 17.81 ? 2507 ARG A NH2   1 
ATOM   8259  N  N     . LEU A 1 2508 ? 249.364 175.824 191.449 1.00 8.78  ? 2508 LEU A N     1 
ATOM   8260  C  CA    . LEU A 1 2508 ? 250.547 175.706 190.603 1.00 10.98 ? 2508 LEU A CA    1 
ATOM   8261  C  C     . LEU A 1 2508 ? 250.735 174.282 190.096 1.00 10.36 ? 2508 LEU A C     1 
ATOM   8262  O  O     . LEU A 1 2508 ? 251.102 174.074 188.933 1.00 7.81  ? 2508 LEU A O     1 
ATOM   8263  C  CB    . LEU A 1 2508 ? 251.785 176.171 191.370 1.00 8.50  ? 2508 LEU A CB    1 
ATOM   8264  C  CG    . LEU A 1 2508 ? 253.144 175.820 190.765 1.00 13.31 ? 2508 LEU A CG    1 
ATOM   8265  C  CD1   . LEU A 1 2508 ? 253.507 176.769 189.629 1.00 17.37 ? 2508 LEU A CD1   1 
ATOM   8266  C  CD2   . LEU A 1 2508 ? 254.218 175.823 191.835 1.00 13.71 ? 2508 LEU A CD2   1 
ATOM   8267  N  N     . LYS A 1 2509 ? 250.494 173.289 190.954 1.00 7.99  ? 2509 LYS A N     1 
ATOM   8268  C  CA    . LYS A 1 2509 ? 250.662 171.901 190.539 1.00 9.92  ? 2509 LYS A CA    1 
ATOM   8269  C  C     . LYS A 1 2509 ? 249.690 171.545 189.420 1.00 13.76 ? 2509 LYS A C     1 
ATOM   8270  O  O     . LYS A 1 2509 ? 250.047 170.827 188.480 1.00 12.83 ? 2509 LYS A O     1 
ATOM   8271  C  CB    . LYS A 1 2509 ? 250.492 170.974 191.744 1.00 14.17 ? 2509 LYS A CB    1 
ATOM   8272  C  CG    . LYS A 1 2509 ? 250.669 169.486 191.454 1.00 15.89 ? 2509 LYS A CG    1 
ATOM   8273  C  CD    . LYS A 1 2509 ? 249.353 168.786 191.154 1.00 17.80 ? 2509 LYS A CD    1 
ATOM   8274  C  CE    . LYS A 1 2509 ? 248.493 168.673 192.401 1.00 24.44 ? 2509 LYS A CE    1 
ATOM   8275  N  NZ    . LYS A 1 2509 ? 247.206 167.978 192.125 1.00 22.41 ? 2509 LYS A NZ    1 
ATOM   8276  N  N     . MET A 1 2510 ? 248.453 172.040 189.502 1.00 14.20 ? 2510 MET A N     1 
ATOM   8277  C  CA    . MET A 1 2510 ? 247.493 171.804 188.427 1.00 8.02  ? 2510 MET A CA    1 
ATOM   8278  C  C     . MET A 1 2510 ? 247.831 172.631 187.192 1.00 9.01  ? 2510 MET A C     1 
ATOM   8279  O  O     . MET A 1 2510 ? 247.645 172.168 186.061 1.00 12.06 ? 2510 MET A O     1 
ATOM   8280  C  CB    . MET A 1 2510 ? 246.078 172.103 188.913 1.00 6.41  ? 2510 MET A CB    1 
ATOM   8281  C  CG    . MET A 1 2510 ? 245.562 171.103 189.928 1.00 11.53 ? 2510 MET A CG    1 
ATOM   8282  S  SD    . MET A 1 2510 ? 245.605 169.413 189.306 1.00 18.75 ? 2510 MET A SD    1 
ATOM   8283  C  CE    . MET A 1 2510 ? 244.421 168.617 190.383 1.00 14.80 ? 2510 MET A CE    1 
ATOM   8284  N  N     . ARG A 1 2511 ? 248.323 173.858 187.385 1.00 7.43  ? 2511 ARG A N     1 
ATOM   8285  C  CA    . ARG A 1 2511 ? 248.790 174.649 186.251 1.00 5.90  ? 2511 ARG A CA    1 
ATOM   8286  C  C     . ARG A 1 2511 ? 249.950 173.962 185.552 1.00 10.93 ? 2511 ARG A C     1 
ATOM   8287  O  O     . ARG A 1 2511 ? 250.048 173.988 184.319 1.00 10.36 ? 2511 ARG A O     1 
ATOM   8288  C  CB    . ARG A 1 2511 ? 249.206 176.047 186.705 1.00 5.21  ? 2511 ARG A CB    1 
ATOM   8289  C  CG    . ARG A 1 2511 ? 248.087 176.911 187.217 1.00 5.23  ? 2511 ARG A CG    1 
ATOM   8290  C  CD    . ARG A 1 2511 ? 248.629 178.240 187.698 1.00 5.12  ? 2511 ARG A CD    1 
ATOM   8291  N  NE    . ARG A 1 2511 ? 247.572 179.151 188.116 1.00 2.02  ? 2511 ARG A NE    1 
ATOM   8292  C  CZ    . ARG A 1 2511 ? 247.787 180.336 188.669 1.00 3.26  ? 2511 ARG A CZ    1 
ATOM   8293  N  NH1   . ARG A 1 2511 ? 249.012 180.778 188.897 1.00 2.82  ? 2511 ARG A NH1   1 
ATOM   8294  N  NH2   . ARG A 1 2511 ? 246.747 181.094 189.002 1.00 3.29  ? 2511 ARG A NH2   1 
ATOM   8295  N  N     . ALA A 1 2512 ? 250.851 173.356 186.326 1.00 14.59 ? 2512 ALA A N     1 
ATOM   8296  C  CA    . ALA A 1 2512 ? 251.950 172.614 185.726 1.00 9.12  ? 2512 ALA A CA    1 
ATOM   8297  C  C     . ALA A 1 2512 ? 251.440 171.418 184.934 1.00 6.76  ? 2512 ALA A C     1 
ATOM   8298  O  O     . ALA A 1 2512 ? 251.824 171.234 183.776 1.00 5.60  ? 2512 ALA A O     1 
ATOM   8299  C  CB    . ALA A 1 2512 ? 252.934 172.166 186.805 1.00 9.20  ? 2512 ALA A CB    1 
ATOM   8300  N  N     . GLU A 1 2513 ? 250.537 170.626 185.523 1.00 10.01 ? 2513 GLU A N     1 
ATOM   8301  C  CA    . GLU A 1 2513 ? 250.154 169.355 184.913 1.00 10.15 ? 2513 GLU A CA    1 
ATOM   8302  C  C     . GLU A 1 2513 ? 249.482 169.569 183.563 1.00 10.83 ? 2513 GLU A C     1 
ATOM   8303  O  O     . GLU A 1 2513 ? 249.700 168.796 182.623 1.00 14.97 ? 2513 GLU A O     1 
ATOM   8304  C  CB    . GLU A 1 2513 ? 249.233 168.566 185.843 1.00 9.04  ? 2513 GLU A CB    1 
ATOM   8305  C  CG    . GLU A 1 2513 ? 249.194 167.078 185.519 1.00 18.06 ? 2513 GLU A CG    1 
ATOM   8306  C  CD    . GLU A 1 2513 ? 248.101 166.699 184.540 1.00 20.65 ? 2513 GLU A CD    1 
ATOM   8307  O  OE1   . GLU A 1 2513 ? 246.926 167.008 184.805 1.00 26.62 ? 2513 GLU A OE1   1 
ATOM   8308  O  OE2   . GLU A 1 2513 ? 248.420 166.081 183.504 1.00 23.16 ? 2513 GLU A OE2   1 
ATOM   8309  N  N     . LEU A 1 2514 ? 248.648 170.607 183.453 1.00 9.43  ? 2514 LEU A N     1 
ATOM   8310  C  CA    . LEU A 1 2514 ? 248.086 170.963 182.154 1.00 7.12  ? 2514 LEU A CA    1 
ATOM   8311  C  C     . LEU A 1 2514 ? 249.190 171.327 181.168 1.00 6.51  ? 2514 LEU A C     1 
ATOM   8312  O  O     . LEU A 1 2514 ? 249.027 171.162 179.955 1.00 8.28  ? 2514 LEU A O     1 
ATOM   8313  C  CB    . LEU A 1 2514 ? 247.098 172.121 182.314 1.00 8.72  ? 2514 LEU A CB    1 
ATOM   8314  C  CG    . LEU A 1 2514 ? 246.344 172.600 181.070 1.00 6.81  ? 2514 LEU A CG    1 
ATOM   8315  C  CD1   . LEU A 1 2514 ? 245.530 171.471 180.458 1.00 7.08  ? 2514 LEU A CD1   1 
ATOM   8316  C  CD2   . LEU A 1 2514 ? 245.454 173.785 181.400 1.00 2.89  ? 2514 LEU A CD2   1 
ATOM   8317  N  N     . GLY A 1 2515 ? 250.320 171.823 181.677 1.00 6.97  ? 2515 GLY A N     1 
ATOM   8318  C  CA    . GLY A 1 2515 ? 251.434 172.158 180.805 1.00 6.26  ? 2515 GLY A CA    1 
ATOM   8319  C  C     . GLY A 1 2515 ? 252.047 170.953 180.117 1.00 10.15 ? 2515 GLY A C     1 
ATOM   8320  O  O     . GLY A 1 2515 ? 252.293 170.980 178.909 1.00 9.71  ? 2515 GLY A O     1 
ATOM   8321  N  N     . GLU A 1 2516 ? 252.315 169.878 180.870 1.00 8.25  ? 2516 GLU A N     1 
ATOM   8322  C  CA    . GLU A 1 2516 ? 252.879 168.689 180.235 1.00 10.15 ? 2516 GLU A CA    1 
ATOM   8323  C  C     . GLU A 1 2516 ? 251.890 168.061 179.263 1.00 12.48 ? 2516 GLU A C     1 
ATOM   8324  O  O     . GLU A 1 2516 ? 252.283 167.593 178.190 1.00 15.88 ? 2516 GLU A O     1 
ATOM   8325  C  CB    . GLU A 1 2516 ? 253.340 167.644 181.259 1.00 18.30 ? 2516 GLU A CB    1 
ATOM   8326  C  CG    . GLU A 1 2516 ? 254.548 168.026 182.104 1.00 13.93 ? 2516 GLU A CG    1 
ATOM   8327  C  CD    . GLU A 1 2516 ? 254.181 168.824 183.323 1.00 19.27 ? 2516 GLU A CD    1 
ATOM   8328  O  OE1   . GLU A 1 2516 ? 252.975 168.998 183.549 1.00 25.80 ? 2516 GLU A OE1   1 
ATOM   8329  O  OE2   . GLU A 1 2516 ? 255.091 169.273 184.050 1.00 22.87 ? 2516 GLU A OE2   1 
ATOM   8330  N  N     . TYR A 1 2517 ? 250.604 168.038 179.621 1.00 9.59  ? 2517 TYR A N     1 
ATOM   8331  C  CA    . TYR A 1 2517 ? 249.614 167.454 178.722 1.00 12.79 ? 2517 TYR A CA    1 
ATOM   8332  C  C     . TYR A 1 2517 ? 249.560 168.208 177.403 1.00 13.39 ? 2517 TYR A C     1 
ATOM   8333  O  O     . TYR A 1 2517 ? 249.471 167.597 176.331 1.00 15.80 ? 2517 TYR A O     1 
ATOM   8334  C  CB    . TYR A 1 2517 ? 248.234 167.436 179.373 1.00 11.97 ? 2517 TYR A CB    1 
ATOM   8335  C  CG    . TYR A 1 2517 ? 247.166 166.956 178.423 1.00 12.07 ? 2517 TYR A CG    1 
ATOM   8336  C  CD1   . TYR A 1 2517 ? 247.148 165.641 177.979 1.00 12.95 ? 2517 TYR A CD1   1 
ATOM   8337  C  CD2   . TYR A 1 2517 ? 246.191 167.819 177.947 1.00 13.01 ? 2517 TYR A CD2   1 
ATOM   8338  C  CE1   . TYR A 1 2517 ? 246.185 165.196 177.106 1.00 11.63 ? 2517 TYR A CE1   1 
ATOM   8339  C  CE2   . TYR A 1 2517 ? 245.220 167.380 177.071 1.00 14.09 ? 2517 TYR A CE2   1 
ATOM   8340  C  CZ    . TYR A 1 2517 ? 245.221 166.068 176.653 1.00 12.38 ? 2517 TYR A CZ    1 
ATOM   8341  O  OH    . TYR A 1 2517 ? 244.257 165.624 175.781 1.00 12.75 ? 2517 TYR A OH    1 
ATOM   8342  N  N     . ILE A 1 2518 ? 249.601 169.541 177.459 1.00 10.71 ? 2518 ILE A N     1 
ATOM   8343  C  CA    . ILE A 1 2518 ? 249.675 170.329 176.233 1.00 10.28 ? 2518 ILE A CA    1 
ATOM   8344  C  C     . ILE A 1 2518 ? 250.961 170.011 175.486 1.00 12.34 ? 2518 ILE A C     1 
ATOM   8345  O  O     . ILE A 1 2518 ? 250.955 169.824 174.265 1.00 17.58 ? 2518 ILE A O     1 
ATOM   8346  C  CB    . ILE A 1 2518 ? 249.554 171.831 176.551 1.00 6.34  ? 2518 ILE A CB    1 
ATOM   8347  C  CG1   . ILE A 1 2518 ? 248.136 172.165 177.014 1.00 6.54  ? 2518 ILE A CG1   1 
ATOM   8348  C  CG2   . ILE A 1 2518 ? 249.927 172.671 175.340 1.00 7.34  ? 2518 ILE A CG2   1 
ATOM   8349  C  CD1   . ILE A 1 2518 ? 247.939 173.621 177.363 1.00 5.53  ? 2518 ILE A CD1   1 
ATOM   8350  N  N     . ARG A 1 2519 ? 252.077 169.912 176.213 1.00 11.19 ? 2519 ARG A N     1 
ATOM   8351  C  CA    . ARG A 1 2519 ? 253.364 169.635 175.583 1.00 11.30 ? 2519 ARG A CA    1 
ATOM   8352  C  C     . ARG A 1 2519 ? 253.348 168.321 174.816 1.00 16.17 ? 2519 ARG A C     1 
ATOM   8353  O  O     . ARG A 1 2519 ? 254.001 168.206 173.772 1.00 19.75 ? 2519 ARG A O     1 
ATOM   8354  C  CB    . ARG A 1 2519 ? 254.465 169.629 176.643 1.00 12.25 ? 2519 ARG A CB    1 
ATOM   8355  C  CG    . ARG A 1 2519 ? 255.844 169.273 176.122 1.00 14.57 ? 2519 ARG A CG    1 
ATOM   8356  C  CD    . ARG A 1 2519 ? 256.844 169.177 177.261 1.00 10.16 ? 2519 ARG A CD    1 
ATOM   8357  N  NE    . ARG A 1 2519 ? 257.114 170.481 177.853 1.00 8.96  ? 2519 ARG A NE    1 
ATOM   8358  C  CZ    . ARG A 1 2519 ? 257.769 171.464 177.250 1.00 13.36 ? 2519 ARG A CZ    1 
ATOM   8359  N  NH1   . ARG A 1 2519 ? 258.287 171.313 176.042 1.00 13.41 ? 2519 ARG A NH1   1 
ATOM   8360  N  NH2   . ARG A 1 2519 ? 257.912 172.628 177.877 1.00 10.33 ? 2519 ARG A NH2   1 
ATOM   8361  N  N     . ARG A 1 2520 ? 252.602 167.327 175.302 1.00 13.21 ? 2520 ARG A N     1 
ATOM   8362  C  CA    . ARG A 1 2520 ? 252.509 166.058 174.589 1.00 11.79 ? 2520 ARG A CA    1 
ATOM   8363  C  C     . ARG A 1 2520 ? 251.713 166.198 173.295 1.00 17.68 ? 2520 ARG A C     1 
ATOM   8364  O  O     . ARG A 1 2520 ? 252.145 165.717 172.241 1.00 20.08 ? 2520 ARG A O     1 
ATOM   8365  C  CB    . ARG A 1 2520 ? 251.879 164.995 175.491 1.00 11.88 ? 2520 ARG A CB    1 
ATOM   8366  C  CG    . ARG A 1 2520 ? 252.600 164.799 176.812 1.00 14.79 ? 2520 ARG A CG    1 
ATOM   8367  C  CD    . ARG A 1 2520 ? 252.324 163.435 177.417 1.00 13.27 ? 2520 ARG A CD    1 
ATOM   8368  N  NE    . ARG A 1 2520 ? 250.916 163.251 177.749 1.00 17.26 ? 2520 ARG A NE    1 
ATOM   8369  C  CZ    . ARG A 1 2520 ? 250.376 163.561 178.920 1.00 18.53 ? 2520 ARG A CZ    1 
ATOM   8370  N  NH1   . ARG A 1 2520 ? 251.095 164.095 179.894 1.00 18.10 ? 2520 ARG A NH1   1 
ATOM   8371  N  NH2   . ARG A 1 2520 ? 249.081 163.331 179.120 1.00 21.43 ? 2520 ARG A NH2   1 
ATOM   8372  N  N     . ILE A 1 2521 ? 250.564 166.866 173.346 1.00 16.30 ? 2521 ILE A N     1 
ATOM   8373  C  CA    . ILE A 1 2521 ? 249.630 166.810 172.225 1.00 13.14 ? 2521 ILE A CA    1 
ATOM   8374  C  C     . ILE A 1 2521 ? 249.801 167.960 171.234 1.00 12.04 ? 2521 ILE A C     1 
ATOM   8375  O  O     . ILE A 1 2521 ? 249.342 167.854 170.093 1.00 16.64 ? 2521 ILE A O     1 
ATOM   8376  C  CB    . ILE A 1 2521 ? 248.185 166.754 172.746 1.00 12.14 ? 2521 ILE A CB    1 
ATOM   8377  C  CG1   . ILE A 1 2521 ? 247.800 168.084 173.395 1.00 15.41 ? 2521 ILE A CG1   1 
ATOM   8378  C  CG2   . ILE A 1 2521 ? 248.018 165.607 173.724 1.00 12.55 ? 2521 ILE A CG2   1 
ATOM   8379  C  CD1   . ILE A 1 2521 ? 246.406 168.100 173.947 1.00 13.44 ? 2521 ILE A CD1   1 
ATOM   8380  N  N     . THR A 1 2522 ? 250.436 169.058 171.629 1.00 14.88 ? 2522 THR A N     1 
ATOM   8381  C  CA    . THR A 1 2522 ? 250.518 170.178 170.705 1.00 15.98 ? 2522 THR A CA    1 
ATOM   8382  C  C     . THR A 1 2522 ? 251.666 169.986 169.719 1.00 14.60 ? 2522 THR A C     1 
ATOM   8383  O  O     . THR A 1 2522 ? 252.602 169.214 169.949 1.00 14.02 ? 2522 THR A O     1 
ATOM   8384  C  CB    . THR A 1 2522 ? 250.710 171.505 171.440 1.00 15.88 ? 2522 THR A CB    1 
ATOM   8385  O  OG1   . THR A 1 2522 ? 250.602 172.580 170.499 1.00 14.19 ? 2522 THR A OG1   1 
ATOM   8386  C  CG2   . THR A 1 2522 ? 252.097 171.574 172.060 1.00 18.02 ? 2522 THR A CG2   1 
ATOM   8387  N  N     . THR A 1 2523 ? 251.574 170.703 168.604 1.00 16.02 ? 2523 THR A N     1 
ATOM   8388  C  CA    . THR A 1 2523 ? 252.671 170.824 167.658 1.00 13.17 ? 2523 THR A CA    1 
ATOM   8389  C  C     . THR A 1 2523 ? 253.254 172.229 167.637 1.00 13.39 ? 2523 THR A C     1 
ATOM   8390  O  O     . THR A 1 2523 ? 254.189 172.488 166.873 1.00 16.89 ? 2523 THR A O     1 
ATOM   8391  C  CB    . THR A 1 2523 ? 252.215 170.425 166.251 1.00 16.99 ? 2523 THR A CB    1 
ATOM   8392  O  OG1   . THR A 1 2523 ? 251.168 171.301 165.817 1.00 29.08 ? 2523 THR A OG1   1 
ATOM   8393  C  CG2   . THR A 1 2523 ? 251.705 168.997 166.247 1.00 14.91 ? 2523 THR A CG2   1 
ATOM   8394  N  N     . VAL A 1 2524 ? 252.717 173.135 168.442 1.00 13.75 ? 2524 VAL A N     1 
ATOM   8395  C  CA    . VAL A 1 2524 ? 253.288 174.481 168.566 1.00 11.28 ? 2524 VAL A CA    1 
ATOM   8396  C  C     . VAL A 1 2524 ? 254.641 174.384 169.258 1.00 13.40 ? 2524 VAL A C     1 
ATOM   8397  O  O     . VAL A 1 2524 ? 254.771 173.652 170.256 1.00 13.28 ? 2524 VAL A O     1 
ATOM   8398  C  CB    . VAL A 1 2524 ? 252.333 175.388 169.343 1.00 11.56 ? 2524 VAL A CB    1 
ATOM   8399  C  CG1   . VAL A 1 2524 ? 252.893 176.795 169.453 1.00 13.03 ? 2524 VAL A CG1   1 
ATOM   8400  C  CG2   . VAL A 1 2524 ? 250.967 175.405 168.683 1.00 12.17 ? 2524 VAL A CG2   1 
ATOM   8401  N  N     . PRO A 1 2525 ? 255.674 175.068 168.768 1.00 14.23 ? 2525 PRO A N     1 
ATOM   8402  C  CA    . PRO A 1 2525 ? 256.962 175.053 169.470 1.00 12.06 ? 2525 PRO A CA    1 
ATOM   8403  C  C     . PRO A 1 2525 ? 256.820 175.594 170.886 1.00 14.57 ? 2525 PRO A C     1 
ATOM   8404  O  O     . PRO A 1 2525 ? 256.081 176.545 171.139 1.00 21.87 ? 2525 PRO A O     1 
ATOM   8405  C  CB    . PRO A 1 2525 ? 257.847 175.957 168.605 1.00 8.35  ? 2525 PRO A CB    1 
ATOM   8406  C  CG    . PRO A 1 2525 ? 257.231 175.901 167.254 1.00 13.57 ? 2525 PRO A CG    1 
ATOM   8407  C  CD    . PRO A 1 2525 ? 255.754 175.765 167.474 1.00 11.84 ? 2525 PRO A CD    1 
ATOM   8408  N  N     . LEU A 1 2526 ? 257.545 174.976 171.805 1.00 11.99 ? 2526 LEU A N     1 
ATOM   8409  C  CA    . LEU A 1 2526 ? 257.444 175.245 173.229 1.00 12.16 ? 2526 LEU A CA    1 
ATOM   8410  C  C     . LEU A 1 2526 ? 258.833 175.463 173.808 1.00 17.73 ? 2526 LEU A C     1 
ATOM   8411  O  O     . LEU A 1 2526 ? 259.833 175.070 173.199 1.00 22.93 ? 2526 LEU A O     1 
ATOM   8412  C  CB    . LEU A 1 2526 ? 256.748 174.079 173.948 1.00 9.34  ? 2526 LEU A CB    1 
ATOM   8413  C  CG    . LEU A 1 2526 ? 255.282 173.855 173.578 1.00 6.99  ? 2526 LEU A CG    1 
ATOM   8414  C  CD1   . LEU A 1 2526 ? 254.679 172.805 174.477 1.00 8.46  ? 2526 LEU A CD1   1 
ATOM   8415  C  CD2   . LEU A 1 2526 ? 254.490 175.149 173.674 1.00 12.43 ? 2526 LEU A CD2   1 
ATOM   8416  N  N     . PRO A 1 2527 ? 258.930 176.117 174.965 1.00 15.81 ? 2527 PRO A N     1 
ATOM   8417  C  CA    . PRO A 1 2527 ? 260.240 176.278 175.603 1.00 13.83 ? 2527 PRO A CA    1 
ATOM   8418  C  C     . PRO A 1 2527 ? 260.879 174.927 175.898 1.00 18.75 ? 2527 PRO A C     1 
ATOM   8419  O  O     . PRO A 1 2527 ? 260.210 173.978 176.310 1.00 19.49 ? 2527 PRO A O     1 
ATOM   8420  C  CB    . PRO A 1 2527 ? 259.916 177.043 176.890 1.00 13.43 ? 2527 PRO A CB    1 
ATOM   8421  C  CG    . PRO A 1 2527 ? 258.648 177.755 176.588 1.00 9.16  ? 2527 PRO A CG    1 
ATOM   8422  C  CD    . PRO A 1 2527 ? 257.873 176.832 175.702 1.00 11.29 ? 2527 PRO A CD    1 
ATOM   8423  N  N     . THR A 1 2528 ? 262.191 174.856 175.689 1.00 18.05 ? 2528 THR A N     1 
ATOM   8424  C  CA    . THR A 1 2528 ? 262.939 173.613 175.788 1.00 19.64 ? 2528 THR A CA    1 
ATOM   8425  C  C     . THR A 1 2528 ? 263.614 173.432 177.141 1.00 25.18 ? 2528 THR A C     1 
ATOM   8426  O  O     . THR A 1 2528 ? 264.475 172.557 177.278 1.00 27.80 ? 2528 THR A O     1 
ATOM   8427  C  CB    . THR A 1 2528 ? 263.984 173.539 174.673 1.00 21.56 ? 2528 THR A CB    1 
ATOM   8428  O  OG1   . THR A 1 2528 ? 264.903 174.629 174.808 1.00 21.66 ? 2528 THR A OG1   1 
ATOM   8429  C  CG2   . THR A 1 2528 ? 263.315 173.610 173.310 1.00 16.88 ? 2528 THR A CG2   1 
ATOM   8430  N  N     . ALA A 1 2529 ? 263.252 174.239 178.134 1.00 29.55 ? 2529 ALA A N     1 
ATOM   8431  C  CA    . ALA A 1 2529 ? 263.843 174.098 179.453 1.00 18.30 ? 2529 ALA A CA    1 
ATOM   8432  C  C     . ALA A 1 2529 ? 263.476 172.738 180.043 1.00 25.48 ? 2529 ALA A C     1 
ATOM   8433  O  O     . ALA A 1 2529 ? 262.378 172.228 179.794 1.00 29.63 ? 2529 ALA A O     1 
ATOM   8434  C  CB    . ALA A 1 2529 ? 263.369 175.220 180.377 1.00 24.44 ? 2529 ALA A CB    1 
ATOM   8435  N  N     . PRO A 1 2530 ? 264.370 172.119 180.820 1.00 26.62 ? 2530 PRO A N     1 
ATOM   8436  C  CA    . PRO A 1 2530 ? 264.083 170.756 181.295 1.00 25.09 ? 2530 PRO A CA    1 
ATOM   8437  C  C     . PRO A 1 2530 ? 262.974 170.685 182.329 1.00 24.85 ? 2530 PRO A C     1 
ATOM   8438  O  O     . PRO A 1 2530 ? 262.104 169.811 182.227 1.00 27.72 ? 2530 PRO A O     1 
ATOM   8439  C  CB    . PRO A 1 2530 ? 265.433 170.307 181.870 1.00 23.95 ? 2530 PRO A CB    1 
ATOM   8440  C  CG    . PRO A 1 2530 ? 266.084 171.577 182.302 1.00 24.00 ? 2530 PRO A CG    1 
ATOM   8441  C  CD    . PRO A 1 2530 ? 265.689 172.597 181.272 1.00 26.84 ? 2530 PRO A CD    1 
ATOM   8442  N  N     . ASN A 1 2531 ? 262.969 171.579 183.321 1.00 20.80 ? 2531 ASN A N     1 
ATOM   8443  C  CA    . ASN A 1 2531 ? 262.053 171.455 184.450 1.00 24.14 ? 2531 ASN A CA    1 
ATOM   8444  C  C     . ASN A 1 2531 ? 261.298 172.749 184.743 1.00 20.43 ? 2531 ASN A C     1 
ATOM   8445  O  O     . ASN A 1 2531 ? 260.823 172.940 185.867 1.00 23.79 ? 2531 ASN A O     1 
ATOM   8446  C  CB    . ASN A 1 2531 ? 262.807 170.998 185.701 1.00 21.65 ? 2531 ASN A CB    1 
ATOM   8447  C  CG    . ASN A 1 2531 ? 263.727 169.823 185.430 1.00 31.91 ? 2531 ASN A CG    1 
ATOM   8448  O  OD1   . ASN A 1 2531 ? 264.944 169.925 185.579 1.00 31.19 ? 2531 ASN A OD1   1 
ATOM   8449  N  ND2   . ASN A 1 2531 ? 263.147 168.699 185.027 1.00 25.94 ? 2531 ASN A ND2   1 
ATOM   8450  N  N     . ILE A 1 2532 ? 261.170 173.636 183.766 1.00 17.71 ? 2532 ILE A N     1 
ATOM   8451  C  CA    . ILE A 1 2532 ? 260.479 174.911 183.940 1.00 11.19 ? 2532 ILE A CA    1 
ATOM   8452  C  C     . ILE A 1 2532 ? 259.083 174.780 183.342 1.00 11.93 ? 2532 ILE A C     1 
ATOM   8453  O  O     . ILE A 1 2532 ? 258.964 174.483 182.143 1.00 12.46 ? 2532 ILE A O     1 
ATOM   8454  C  CB    . ILE A 1 2532 ? 261.253 176.067 183.292 1.00 12.85 ? 2532 ILE A CB    1 
ATOM   8455  C  CG1   . ILE A 1 2532 ? 262.648 176.175 183.905 1.00 14.55 ? 2532 ILE A CG1   1 
ATOM   8456  C  CG2   . ILE A 1 2532 ? 260.500 177.375 183.471 1.00 11.57 ? 2532 ILE A CG2   1 
ATOM   8457  C  CD1   . ILE A 1 2532 ? 262.637 176.454 185.391 1.00 16.02 ? 2532 ILE A CD1   1 
ATOM   8458  N  N     . PRO A 1 2533 ? 258.021 174.981 184.119 1.00 8.96  ? 2533 PRO A N     1 
ATOM   8459  C  CA    . PRO A 1 2533 ? 256.667 174.871 183.562 1.00 8.63  ? 2533 PRO A CA    1 
ATOM   8460  C  C     . PRO A 1 2533 ? 256.418 175.917 182.487 1.00 8.40  ? 2533 PRO A C     1 
ATOM   8461  O  O     . PRO A 1 2533 ? 257.009 176.998 182.490 1.00 17.53 ? 2533 PRO A O     1 
ATOM   8462  C  CB    . PRO A 1 2533 ? 255.758 175.091 184.777 1.00 9.79  ? 2533 PRO A CB    1 
ATOM   8463  C  CG    . PRO A 1 2533 ? 256.611 175.738 185.803 1.00 6.26  ? 2533 PRO A CG    1 
ATOM   8464  C  CD    . PRO A 1 2533 ? 258.014 175.288 185.557 1.00 7.33  ? 2533 PRO A CD    1 
ATOM   8465  N  N     . ILE A 1 2534 ? 255.534 175.571 181.549 1.00 8.51  ? 2534 ILE A N     1 
ATOM   8466  C  CA    . ILE A 1 2534 ? 255.232 176.471 180.441 1.00 7.16  ? 2534 ILE A CA    1 
ATOM   8467  C  C     . ILE A 1 2534 ? 254.553 177.734 180.950 1.00 5.28  ? 2534 ILE A C     1 
ATOM   8468  O  O     . ILE A 1 2534 ? 254.738 178.823 180.393 1.00 5.73  ? 2534 ILE A O     1 
ATOM   8469  C  CB    . ILE A 1 2534 ? 254.367 175.745 179.392 1.00 6.36  ? 2534 ILE A CB    1 
ATOM   8470  C  CG1   . ILE A 1 2534 ? 255.134 174.566 178.803 1.00 8.36  ? 2534 ILE A CG1   1 
ATOM   8471  C  CG2   . ILE A 1 2534 ? 254.002 176.686 178.258 1.00 4.20  ? 2534 ILE A CG2   1 
ATOM   8472  C  CD1   . ILE A 1 2534 ? 254.278 173.648 177.964 1.00 12.46 ? 2534 ILE A CD1   1 
ATOM   8473  N  N     . ILE A 1 2535 ? 253.773 177.617 182.027 1.00 4.84  ? 2535 ILE A N     1 
ATOM   8474  C  CA    . ILE A 1 2535 ? 253.105 178.756 182.636 1.00 4.57  ? 2535 ILE A CA    1 
ATOM   8475  C  C     . ILE A 1 2535 ? 254.088 179.815 183.125 1.00 6.11  ? 2535 ILE A C     1 
ATOM   8476  O  O     . ILE A 1 2535 ? 253.676 180.930 183.451 1.00 6.97  ? 2535 ILE A O     1 
ATOM   8477  C  CB    . ILE A 1 2535 ? 252.201 178.265 183.791 1.00 7.68  ? 2535 ILE A CB    1 
ATOM   8478  C  CG1   . ILE A 1 2535 ? 251.071 179.257 184.063 1.00 6.74  ? 2535 ILE A CG1   1 
ATOM   8479  C  CG2   . ILE A 1 2535 ? 253.016 178.025 185.052 1.00 6.61  ? 2535 ILE A CG2   1 
ATOM   8480  C  CD1   . ILE A 1 2535 ? 249.936 179.165 183.078 1.00 2.24  ? 2535 ILE A CD1   1 
ATOM   8481  N  N     . ASP A 1 2536 ? 255.377 179.491 183.173 1.00 5.95  ? 2536 ASP A N     1 
ATOM   8482  C  CA    . ASP A 1 2536 ? 256.421 180.422 183.579 1.00 5.12  ? 2536 ASP A CA    1 
ATOM   8483  C  C     . ASP A 1 2536 ? 256.972 181.235 182.414 1.00 4.81  ? 2536 ASP A C     1 
ATOM   8484  O  O     . ASP A 1 2536 ? 257.954 181.961 182.590 1.00 6.00  ? 2536 ASP A O     1 
ATOM   8485  C  CB    . ASP A 1 2536 ? 257.565 179.663 184.261 1.00 6.09  ? 2536 ASP A CB    1 
ATOM   8486  C  CG    . ASP A 1 2536 ? 257.229 179.251 185.680 1.00 12.60 ? 2536 ASP A CG    1 
ATOM   8487  O  OD1   . ASP A 1 2536 ? 256.114 179.563 186.144 1.00 14.10 ? 2536 ASP A OD1   1 
ATOM   8488  O  OD2   . ASP A 1 2536 ? 258.079 178.610 186.329 1.00 17.31 ? 2536 ASP A OD2   1 
ATOM   8489  N  N     . TYR A 1 2537 ? 256.371 181.124 181.234 1.00 5.81  ? 2537 TYR A N     1 
ATOM   8490  C  CA    . TYR A 1 2537 ? 256.840 181.802 180.037 1.00 3.82  ? 2537 TYR A CA    1 
ATOM   8491  C  C     . TYR A 1 2537 ? 255.734 182.681 179.472 1.00 4.62  ? 2537 TYR A C     1 
ATOM   8492  O  O     . TYR A 1 2537 ? 254.561 182.293 179.471 1.00 7.71  ? 2537 TYR A O     1 
ATOM   8493  C  CB    . TYR A 1 2537 ? 257.282 180.795 178.969 1.00 4.45  ? 2537 TYR A CB    1 
ATOM   8494  C  CG    . TYR A 1 2537 ? 258.641 180.180 179.193 1.00 5.05  ? 2537 TYR A CG    1 
ATOM   8495  C  CD1   . TYR A 1 2537 ? 258.784 179.021 179.942 1.00 5.48  ? 2537 TYR A CD1   1 
ATOM   8496  C  CD2   . TYR A 1 2537 ? 259.780 180.744 178.636 1.00 6.88  ? 2537 TYR A CD2   1 
ATOM   8497  C  CE1   . TYR A 1 2537 ? 260.021 178.449 180.141 1.00 6.13  ? 2537 TYR A CE1   1 
ATOM   8498  C  CE2   . TYR A 1 2537 ? 261.024 180.178 178.832 1.00 5.10  ? 2537 TYR A CE2   1 
ATOM   8499  C  CZ    . TYR A 1 2537 ? 261.138 179.031 179.584 1.00 8.75  ? 2537 TYR A CZ    1 
ATOM   8500  O  OH    . TYR A 1 2537 ? 262.374 178.460 179.786 1.00 17.76 ? 2537 TYR A OH    1 
ATOM   8501  N  N     . GLU A 1 2538 ? 256.107 183.860 178.995 1.00 6.20  ? 2538 GLU A N     1 
ATOM   8502  C  CA    . GLU A 1 2538 ? 255.217 184.705 178.214 1.00 8.86  ? 2538 GLU A CA    1 
ATOM   8503  C  C     . GLU A 1 2538 ? 255.575 184.585 176.737 1.00 7.01  ? 2538 GLU A C     1 
ATOM   8504  O  O     . GLU A 1 2538 ? 256.509 183.878 176.353 1.00 8.63  ? 2538 GLU A O     1 
ATOM   8505  C  CB    . GLU A 1 2538 ? 255.296 186.162 178.670 1.00 6.49  ? 2538 GLU A CB    1 
ATOM   8506  C  CG    . GLU A 1 2538 ? 256.668 186.770 178.510 1.00 7.12  ? 2538 GLU A CG    1 
ATOM   8507  C  CD    . GLU A 1 2538 ? 256.621 188.270 178.356 1.00 13.71 ? 2538 GLU A CD    1 
ATOM   8508  O  OE1   . GLU A 1 2538 ? 257.344 188.798 177.483 1.00 14.87 ? 2538 GLU A OE1   1 
ATOM   8509  O  OE2   . GLU A 1 2538 ? 255.859 188.920 179.097 1.00 16.39 ? 2538 GLU A OE2   1 
ATOM   8510  N  N     . VAL A 1 2539 ? 254.822 185.295 175.905 1.00 5.23  ? 2539 VAL A N     1 
ATOM   8511  C  CA    . VAL A 1 2539 ? 255.048 185.318 174.465 1.00 5.33  ? 2539 VAL A CA    1 
ATOM   8512  C  C     . VAL A 1 2539 ? 255.361 186.751 174.067 1.00 6.30  ? 2539 VAL A C     1 
ATOM   8513  O  O     . VAL A 1 2539 ? 254.505 187.636 174.187 1.00 8.81  ? 2539 VAL A O     1 
ATOM   8514  C  CB    . VAL A 1 2539 ? 253.838 184.781 173.683 1.00 5.78  ? 2539 VAL A CB    1 
ATOM   8515  C  CG1   . VAL A 1 2539 ? 254.180 184.646 172.211 1.00 4.87  ? 2539 VAL A CG1   1 
ATOM   8516  C  CG2   . VAL A 1 2539 ? 253.383 183.446 174.254 1.00 2.78  ? 2539 VAL A CG2   1 
ATOM   8517  N  N     . SER A 1 2540 ? 256.584 186.982 173.601 1.00 8.62  ? 2540 SER A N     1 
ATOM   8518  C  CA    . SER A 1 2540 ? 256.962 188.297 173.112 1.00 9.64  ? 2540 SER A CA    1 
ATOM   8519  C  C     . SER A 1 2540 ? 256.340 188.543 171.740 1.00 11.38 ? 2540 SER A C     1 
ATOM   8520  O  O     . SER A 1 2540 ? 256.002 187.612 171.004 1.00 13.19 ? 2540 SER A O     1 
ATOM   8521  C  CB    . SER A 1 2540 ? 258.482 188.430 173.038 1.00 10.23 ? 2540 SER A CB    1 
ATOM   8522  O  OG    . SER A 1 2540 ? 259.040 187.466 172.162 1.00 20.57 ? 2540 SER A OG    1 
ATOM   8523  N  N     . ILE A 1 2541 ? 256.200 189.824 171.396 1.00 10.35 ? 2541 ILE A N     1 
ATOM   8524  C  CA    . ILE A 1 2541 ? 255.547 190.213 170.156 1.00 10.55 ? 2541 ILE A CA    1 
ATOM   8525  C  C     . ILE A 1 2541 ? 256.297 189.708 168.930 1.00 13.87 ? 2541 ILE A C     1 
ATOM   8526  O  O     . ILE A 1 2541 ? 255.731 189.667 167.834 1.00 15.79 ? 2541 ILE A O     1 
ATOM   8527  C  CB    . ILE A 1 2541 ? 255.373 191.749 170.115 1.00 12.86 ? 2541 ILE A CB    1 
ATOM   8528  C  CG1   . ILE A 1 2541 ? 254.415 192.164 168.998 1.00 17.22 ? 2541 ILE A CG1   1 
ATOM   8529  C  CG2   . ILE A 1 2541 ? 256.712 192.435 169.933 1.00 9.28  ? 2541 ILE A CG2   1 
ATOM   8530  C  CD1   . ILE A 1 2541 ? 252.995 191.697 169.206 1.00 10.40 ? 2541 ILE A CD1   1 
ATOM   8531  N  N     . SER A 1 2542 ? 257.553 189.300 169.091 1.00 15.24 ? 2542 SER A N     1 
ATOM   8532  C  CA    . SER A 1 2542 ? 258.337 188.709 168.016 1.00 11.48 ? 2542 SER A CA    1 
ATOM   8533  C  C     . SER A 1 2542 ? 258.072 187.216 167.844 1.00 15.93 ? 2542 SER A C     1 
ATOM   8534  O  O     . SER A 1 2542 ? 258.817 186.547 167.123 1.00 18.61 ? 2542 SER A O     1 
ATOM   8535  C  CB    . SER A 1 2542 ? 259.828 188.939 168.262 1.00 14.45 ? 2542 SER A CB    1 
ATOM   8536  O  OG    . SER A 1 2542 ? 260.290 188.154 169.347 1.00 16.24 ? 2542 SER A OG    1 
ATOM   8537  N  N     . GLY A 1 2543 ? 257.039 186.684 168.489 1.00 14.82 ? 2543 GLY A N     1 
ATOM   8538  C  CA    . GLY A 1 2543 ? 256.725 185.271 168.380 1.00 11.70 ? 2543 GLY A CA    1 
ATOM   8539  C  C     . GLY A 1 2543 ? 257.759 184.356 168.994 1.00 14.20 ? 2543 GLY A C     1 
ATOM   8540  O  O     . GLY A 1 2543 ? 257.994 183.257 168.477 1.00 17.15 ? 2543 GLY A O     1 
ATOM   8541  N  N     . GLU A 1 2544 ? 258.385 184.779 170.084 1.00 13.53 ? 2544 GLU A N     1 
ATOM   8542  C  CA    . GLU A 1 2544 ? 259.354 183.964 170.796 1.00 11.31 ? 2544 GLU A CA    1 
ATOM   8543  C  C     . GLU A 1 2544 ? 258.887 183.787 172.230 1.00 14.47 ? 2544 GLU A C     1 
ATOM   8544  O  O     . GLU A 1 2544 ? 258.360 184.725 172.837 1.00 17.32 ? 2544 GLU A O     1 
ATOM   8545  C  CB    . GLU A 1 2544 ? 260.752 184.598 170.780 1.00 9.82  ? 2544 GLU A CB    1 
ATOM   8546  C  CG    . GLU A 1 2544 ? 261.323 184.845 169.393 1.00 13.29 ? 2544 GLU A CG    1 
ATOM   8547  C  CD    . GLU A 1 2544 ? 261.337 183.604 168.522 1.00 21.38 ? 2544 GLU A CD    1 
ATOM   8548  O  OE1   . GLU A 1 2544 ? 261.711 182.521 169.017 1.00 23.93 ? 2544 GLU A OE1   1 
ATOM   8549  O  OE2   . GLU A 1 2544 ? 260.977 183.715 167.331 1.00 23.07 ? 2544 GLU A OE2   1 
ATOM   8550  N  N     . TRP A 1 2545 ? 259.062 182.586 172.764 1.00 10.57 ? 2545 TRP A N     1 
ATOM   8551  C  CA    . TRP A 1 2545 ? 258.874 182.386 174.191 1.00 9.48  ? 2545 TRP A CA    1 
ATOM   8552  C  C     . TRP A 1 2545 ? 259.944 183.160 174.948 1.00 12.51 ? 2545 TRP A C     1 
ATOM   8553  O  O     . TRP A 1 2545 ? 261.131 183.078 174.621 1.00 20.57 ? 2545 TRP A O     1 
ATOM   8554  C  CB    . TRP A 1 2545 ? 258.947 180.902 174.546 1.00 11.45 ? 2545 TRP A CB    1 
ATOM   8555  C  CG    . TRP A 1 2545 ? 257.770 180.106 174.083 1.00 9.81  ? 2545 TRP A CG    1 
ATOM   8556  C  CD1   . TRP A 1 2545 ? 257.730 179.256 173.019 1.00 9.11  ? 2545 TRP A CD1   1 
ATOM   8557  C  CD2   . TRP A 1 2545 ? 256.458 180.091 174.658 1.00 8.80  ? 2545 TRP A CD2   1 
ATOM   8558  N  NE1   . TRP A 1 2545 ? 256.481 178.703 172.902 1.00 8.28  ? 2545 TRP A NE1   1 
ATOM   8559  C  CE2   . TRP A 1 2545 ? 255.679 179.202 173.893 1.00 8.02  ? 2545 TRP A CE2   1 
ATOM   8560  C  CE3   . TRP A 1 2545 ? 255.868 180.737 175.749 1.00 9.10  ? 2545 TRP A CE3   1 
ATOM   8561  C  CZ2   . TRP A 1 2545 ? 254.340 178.945 174.182 1.00 7.51  ? 2545 TRP A CZ2   1 
ATOM   8562  C  CZ3   . TRP A 1 2545 ? 254.539 180.479 176.032 1.00 6.72  ? 2545 TRP A CZ3   1 
ATOM   8563  C  CH2   . TRP A 1 2545 ? 253.790 179.593 175.252 1.00 6.15  ? 2545 TRP A CH2   1 
ATOM   8564  N  N     . SER A 1 2546 ? 259.524 183.926 175.950 1.00 9.60  ? 2546 SER A N     1 
ATOM   8565  C  CA    . SER A 1 2546 ? 260.453 184.650 176.801 1.00 6.70  ? 2546 SER A CA    1 
ATOM   8566  C  C     . SER A 1 2546 ? 260.115 184.329 178.251 1.00 9.23  ? 2546 SER A C     1 
ATOM   8567  O  O     . SER A 1 2546 ? 258.939 184.399 178.643 1.00 10.76 ? 2546 SER A O     1 
ATOM   8568  C  CB    . SER A 1 2546 ? 260.393 186.162 176.552 1.00 10.67 ? 2546 SER A CB    1 
ATOM   8569  O  OG    . SER A 1 2546 ? 259.055 186.619 176.486 1.00 13.32 ? 2546 SER A OG    1 
ATOM   8570  N  N     . PRO A 1 2547 ? 261.100 183.958 179.066 1.00 8.25  ? 2547 PRO A N     1 
ATOM   8571  C  CA    . PRO A 1 2547 ? 260.807 183.622 180.463 1.00 6.18  ? 2547 PRO A CA    1 
ATOM   8572  C  C     . PRO A 1 2547 ? 260.259 184.821 181.222 1.00 5.94  ? 2547 PRO A C     1 
ATOM   8573  O  O     . PRO A 1 2547 ? 260.681 185.959 181.014 1.00 7.98  ? 2547 PRO A O     1 
ATOM   8574  C  CB    . PRO A 1 2547 ? 262.166 183.175 181.011 1.00 5.35  ? 2547 PRO A CB    1 
ATOM   8575  C  CG    . PRO A 1 2547 ? 263.163 183.834 180.125 1.00 6.21  ? 2547 PRO A CG    1 
ATOM   8576  C  CD    . PRO A 1 2547 ? 262.538 183.878 178.765 1.00 5.43  ? 2547 PRO A CD    1 
ATOM   8577  N  N     . TRP A 1 2548 ? 259.302 184.549 182.110 1.00 4.60  ? 2548 TRP A N     1 
ATOM   8578  C  CA    . TRP A 1 2548 ? 258.742 185.600 182.946 1.00 4.28  ? 2548 TRP A CA    1 
ATOM   8579  C  C     . TRP A 1 2548 ? 259.768 186.164 183.921 1.00 6.03  ? 2548 TRP A C     1 
ATOM   8580  O  O     . TRP A 1 2548 ? 259.595 187.286 184.405 1.00 6.86  ? 2548 TRP A O     1 
ATOM   8581  C  CB    . TRP A 1 2548 ? 257.538 185.067 183.720 1.00 3.91  ? 2548 TRP A CB    1 
ATOM   8582  C  CG    . TRP A 1 2548 ? 256.225 185.204 183.011 1.00 3.93  ? 2548 TRP A CG    1 
ATOM   8583  C  CD1   . TRP A 1 2548 ? 255.383 184.195 182.649 1.00 3.90  ? 2548 TRP A CD1   1 
ATOM   8584  C  CD2   . TRP A 1 2548 ? 255.592 186.422 182.596 1.00 3.66  ? 2548 TRP A CD2   1 
ATOM   8585  N  NE1   . TRP A 1 2548 ? 254.268 184.704 182.032 1.00 3.30  ? 2548 TRP A NE1   1 
ATOM   8586  C  CE2   . TRP A 1 2548 ? 254.372 186.069 181.986 1.00 3.74  ? 2548 TRP A CE2   1 
ATOM   8587  C  CE3   . TRP A 1 2548 ? 255.939 187.771 182.676 1.00 2.21  ? 2548 TRP A CE3   1 
ATOM   8588  C  CZ2   . TRP A 1 2548 ? 253.499 187.018 181.460 1.00 4.95  ? 2548 TRP A CZ2   1 
ATOM   8589  C  CZ3   . TRP A 1 2548 ? 255.073 188.709 182.154 1.00 2.96  ? 2548 TRP A CZ3   1 
ATOM   8590  C  CH2   . TRP A 1 2548 ? 253.869 188.329 181.552 1.00 4.48  ? 2548 TRP A CH2   1 
ATOM   8591  N  N     . GLN A 1 2549 ? 260.831 185.408 184.216 1.00 6.58  ? 2549 GLN A N     1 
ATOM   8592  C  CA    . GLN A 1 2549 ? 261.854 185.866 185.145 1.00 8.36  ? 2549 GLN A CA    1 
ATOM   8593  C  C     . GLN A 1 2549 ? 262.628 187.065 184.611 1.00 12.06 ? 2549 GLN A C     1 
ATOM   8594  O  O     . GLN A 1 2549 ? 263.227 187.801 185.402 1.00 15.96 ? 2549 GLN A O     1 
ATOM   8595  C  CB    . GLN A 1 2549 ? 262.817 184.723 185.461 1.00 8.62  ? 2549 GLN A CB    1 
ATOM   8596  C  CG    . GLN A 1 2549 ? 263.598 184.894 186.753 1.00 12.38 ? 2549 GLN A CG    1 
ATOM   8597  C  CD    . GLN A 1 2549 ? 262.717 184.791 187.981 1.00 14.88 ? 2549 GLN A CD    1 
ATOM   8598  O  OE1   . GLN A 1 2549 ? 262.078 183.765 188.215 1.00 19.96 ? 2549 GLN A OE1   1 
ATOM   8599  N  NE2   . GLN A 1 2549 ? 262.684 185.851 188.776 1.00 15.65 ? 2549 GLN A NE2   1 
ATOM   8600  N  N     . ALA A 1 2550 ? 262.629 187.279 183.294 1.00 10.36 ? 2550 ALA A N     1 
ATOM   8601  C  CA    . ALA A 1 2550 ? 263.296 188.444 182.728 1.00 6.69  ? 2550 ALA A CA    1 
ATOM   8602  C  C     . ALA A 1 2550 ? 262.617 189.747 183.123 1.00 10.65 ? 2550 ALA A C     1 
ATOM   8603  O  O     . ALA A 1 2550 ? 263.245 190.807 183.047 1.00 14.85 ? 2550 ALA A O     1 
ATOM   8604  C  CB    . ALA A 1 2550 ? 263.357 188.327 181.205 1.00 8.77  ? 2550 ALA A CB    1 
ATOM   8605  N  N     . LYS A 1 2551 ? 261.351 189.693 183.537 1.00 11.25 ? 2551 LYS A N     1 
ATOM   8606  C  CA    . LYS A 1 2551 ? 260.612 190.865 183.981 1.00 9.29  ? 2551 LYS A CA    1 
ATOM   8607  C  C     . LYS A 1 2551 ? 260.478 190.923 185.497 1.00 9.62  ? 2551 LYS A C     1 
ATOM   8608  O  O     . LYS A 1 2551 ? 259.588 191.609 186.011 1.00 15.33 ? 2551 LYS A O     1 
ATOM   8609  C  CB    . LYS A 1 2551 ? 259.233 190.896 183.322 1.00 7.76  ? 2551 LYS A CB    1 
ATOM   8610  C  CG    . LYS A 1 2551 ? 259.272 191.144 181.826 1.00 9.89  ? 2551 LYS A CG    1 
ATOM   8611  C  CD    . LYS A 1 2551 ? 257.880 191.352 181.262 1.00 12.64 ? 2551 LYS A CD    1 
ATOM   8612  C  CE    . LYS A 1 2551 ? 257.914 191.511 179.755 1.00 9.40  ? 2551 LYS A CE    1 
ATOM   8613  N  NZ    . LYS A 1 2551 ? 256.562 191.366 179.156 1.00 10.76 ? 2551 LYS A NZ    1 
ATOM   8614  N  N     . VAL A 1 2552 ? 261.340 190.218 186.221 1.00 12.40 ? 2552 VAL A N     1 
ATOM   8615  C  CA    . VAL A 1 2552 ? 261.313 190.216 187.681 1.00 10.15 ? 2552 VAL A CA    1 
ATOM   8616  C  C     . VAL A 1 2552 ? 262.696 190.637 188.163 1.00 16.28 ? 2552 VAL A C     1 
ATOM   8617  O  O     . VAL A 1 2552 ? 263.534 189.781 188.486 1.00 12.15 ? 2552 VAL A O     1 
ATOM   8618  C  CB    . VAL A 1 2552 ? 260.906 188.842 188.238 1.00 10.41 ? 2552 VAL A CB    1 
ATOM   8619  C  CG1   . VAL A 1 2552 ? 260.940 188.835 189.764 1.00 8.11  ? 2552 VAL A CG1   1 
ATOM   8620  C  CG2   . VAL A 1 2552 ? 259.534 188.445 187.734 1.00 9.88  ? 2552 VAL A CG2   1 
ATOM   8621  N  N     . PRO A 1 2553 ? 262.996 191.930 188.188 1.00 17.20 ? 2553 PRO A N     1 
ATOM   8622  C  CA    . PRO A 1 2553 ? 264.291 192.380 188.701 1.00 16.43 ? 2553 PRO A CA    1 
ATOM   8623  C  C     . PRO A 1 2553 ? 264.325 192.395 190.220 1.00 20.30 ? 2553 PRO A C     1 
ATOM   8624  O  O     . PRO A 1 2553 ? 263.304 192.541 190.894 1.00 22.26 ? 2553 PRO A O     1 
ATOM   8625  C  CB    . PRO A 1 2553 ? 264.410 193.800 188.137 1.00 16.11 ? 2553 PRO A CB    1 
ATOM   8626  C  CG    . PRO A 1 2553 ? 262.997 194.264 188.072 1.00 18.25 ? 2553 PRO A CG    1 
ATOM   8627  C  CD    . PRO A 1 2553 ? 262.185 193.054 187.688 1.00 9.06  ? 2553 PRO A CD    1 
ATOM   8628  N  N     . GLN A 1 2554 ? 265.531 192.232 190.756 1.00 22.40 ? 2554 GLN A N     1 
ATOM   8629  C  CA    . GLN A 1 2554 ? 265.759 192.374 192.194 1.00 16.68 ? 2554 GLN A CA    1 
ATOM   8630  C  C     . GLN A 1 2554 ? 265.898 193.861 192.489 1.00 21.24 ? 2554 GLN A C     1 
ATOM   8631  O  O     . GLN A 1 2554 ? 266.987 194.432 192.427 1.00 25.21 ? 2554 GLN A O     1 
ATOM   8632  C  CB    . GLN A 1 2554 ? 266.993 191.596 192.630 1.00 15.28 ? 2554 GLN A CB    1 
ATOM   8633  C  CG    . GLN A 1 2554 ? 267.235 191.631 194.128 1.00 23.91 ? 2554 GLN A CG    1 
ATOM   8634  C  CD    . GLN A 1 2554 ? 268.638 191.203 194.504 1.00 29.92 ? 2554 GLN A CD    1 
ATOM   8635  O  OE1   . GLN A 1 2554 ? 269.016 191.237 195.675 1.00 29.13 ? 2554 GLN A OE1   1 
ATOM   8636  N  NE2   . GLN A 1 2554 ? 269.420 190.798 193.511 1.00 27.74 ? 2554 GLN A NE2   1 
ATOM   8637  N  N     . ILE A 1 2555 ? 264.773 194.497 192.809 1.00 19.42 ? 2555 ILE A N     1 
ATOM   8638  C  CA    . ILE A 1 2555 ? 264.765 195.937 193.022 1.00 13.86 ? 2555 ILE A CA    1 
ATOM   8639  C  C     . ILE A 1 2555 ? 265.342 196.263 194.397 1.00 17.05 ? 2555 ILE A C     1 
ATOM   8640  O  O     . ILE A 1 2555 ? 265.422 195.416 195.291 1.00 15.80 ? 2555 ILE A O     1 
ATOM   8641  C  CB    . ILE A 1 2555 ? 263.348 196.514 192.878 1.00 15.51 ? 2555 ILE A CB    1 
ATOM   8642  C  CG1   . ILE A 1 2555 ? 262.427 195.917 193.941 1.00 14.23 ? 2555 ILE A CG1   1 
ATOM   8643  C  CG2   . ILE A 1 2555 ? 262.798 196.227 191.493 1.00 19.55 ? 2555 ILE A CG2   1 
ATOM   8644  C  CD1   . ILE A 1 2555 ? 261.087 196.592 194.029 1.00 11.53 ? 2555 ILE A CD1   1 
ATOM   8645  N  N     . GLU A 1 2556 ? 265.751 197.516 194.558 1.00 18.28 ? 2556 GLU A N     1 
ATOM   8646  C  CA    . GLU A 1 2556 ? 266.039 198.097 195.861 1.00 12.89 ? 2556 GLU A CA    1 
ATOM   8647  C  C     . GLU A 1 2556 ? 265.014 199.196 196.105 1.00 17.21 ? 2556 GLU A C     1 
ATOM   8648  O  O     . GLU A 1 2556 ? 264.879 200.114 195.289 1.00 23.19 ? 2556 GLU A O     1 
ATOM   8649  C  CB    . GLU A 1 2556 ? 267.463 198.649 195.930 1.00 9.03  ? 2556 GLU A CB    1 
ATOM   8650  C  CG    . GLU A 1 2556 ? 268.556 197.622 195.669 1.00 12.09 ? 2556 GLU A CG    1 
ATOM   8651  C  CD    . GLU A 1 2556 ? 268.504 196.439 196.618 1.00 20.61 ? 2556 GLU A CD    1 
ATOM   8652  O  OE1   . GLU A 1 2556 ? 268.521 196.652 197.848 1.00 30.70 ? 2556 GLU A OE1   1 
ATOM   8653  O  OE2   . GLU A 1 2556 ? 268.457 195.290 196.131 1.00 22.78 ? 2556 GLU A OE2   1 
ATOM   8654  N  N     . VAL A 1 2557 ? 264.292 199.095 197.209 1.00 13.11 ? 2557 VAL A N     1 
ATOM   8655  C  CA    . VAL A 1 2557 ? 263.177 199.986 197.505 1.00 4.64  ? 2557 VAL A CA    1 
ATOM   8656  C  C     . VAL A 1 2557 ? 263.694 201.193 198.277 1.00 11.70 ? 2557 VAL A C     1 
ATOM   8657  O  O     . VAL A 1 2557 ? 264.569 201.069 199.140 1.00 14.42 ? 2557 VAL A O     1 
ATOM   8658  C  CB    . VAL A 1 2557 ? 262.083 199.233 198.288 1.00 7.81  ? 2557 VAL A CB    1 
ATOM   8659  C  CG1   . VAL A 1 2557 ? 261.146 200.192 198.999 1.00 7.60  ? 2557 VAL A CG1   1 
ATOM   8660  C  CG2   . VAL A 1 2557 ? 261.305 198.320 197.355 1.00 11.09 ? 2557 VAL A CG2   1 
ATOM   8661  N  N     . GLU A 1 2558 ? 263.168 202.374 197.946 1.00 16.66 ? 2558 GLU A N     1 
ATOM   8662  C  CA    . GLU A 1 2558 ? 263.517 203.582 198.681 1.00 17.18 ? 2558 GLU A CA    1 
ATOM   8663  C  C     . GLU A 1 2558 ? 263.159 203.420 200.154 1.00 16.37 ? 2558 GLU A C     1 
ATOM   8664  O  O     . GLU A 1 2558 ? 262.108 202.872 200.495 1.00 13.40 ? 2558 GLU A O     1 
ATOM   8665  C  CB    . GLU A 1 2558 ? 262.793 204.789 198.088 1.00 16.30 ? 2558 GLU A CB    1 
ATOM   8666  C  CG    . GLU A 1 2558 ? 263.220 205.153 196.675 1.00 20.39 ? 2558 GLU A CG    1 
ATOM   8667  C  CD    . GLU A 1 2558 ? 264.652 205.646 196.601 1.00 26.48 ? 2558 GLU A CD    1 
ATOM   8668  O  OE1   . GLU A 1 2558 ? 265.125 206.269 197.576 1.00 28.45 ? 2558 GLU A OE1   1 
ATOM   8669  O  OE2   . GLU A 1 2558 ? 265.304 205.420 195.560 1.00 30.23 ? 2558 GLU A OE2   1 
ATOM   8670  N  N     . THR A 1 2559 ? 264.043 203.905 201.028 1.00 18.15 ? 2559 THR A N     1 
ATOM   8671  C  CA    . THR A 1 2559 ? 263.937 203.594 202.450 1.00 13.21 ? 2559 THR A CA    1 
ATOM   8672  C  C     . THR A 1 2559 ? 262.668 204.144 203.086 1.00 17.91 ? 2559 THR A C     1 
ATOM   8673  O  O     . THR A 1 2559 ? 262.252 203.641 204.133 1.00 17.89 ? 2559 THR A O     1 
ATOM   8674  C  CB    . THR A 1 2559 ? 265.165 204.118 203.201 1.00 13.56 ? 2559 THR A CB    1 
ATOM   8675  O  OG1   . THR A 1 2559 ? 265.129 203.657 204.557 1.00 20.25 ? 2559 THR A OG1   1 
ATOM   8676  C  CG2   . THR A 1 2559 ? 265.195 205.634 203.192 1.00 16.15 ? 2559 THR A CG2   1 
ATOM   8677  N  N     . HIS A 1 2560 ? 262.041 205.157 202.490 1.00 17.28 ? 2560 HIS A N     1 
ATOM   8678  C  CA    . HIS A 1 2560 ? 260.815 205.708 203.053 1.00 13.33 ? 2560 HIS A CA    1 
ATOM   8679  C  C     . HIS A 1 2560 ? 259.559 205.014 202.544 1.00 18.20 ? 2560 HIS A C     1 
ATOM   8680  O  O     . HIS A 1 2560 ? 258.464 205.313 203.033 1.00 22.69 ? 2560 HIS A O     1 
ATOM   8681  C  CB    . HIS A 1 2560 ? 260.723 207.210 202.763 1.00 18.43 ? 2560 HIS A CB    1 
ATOM   8682  C  CG    . HIS A 1 2560 ? 260.362 207.536 201.348 1.00 17.00 ? 2560 HIS A CG    1 
ATOM   8683  N  ND1   . HIS A 1 2560 ? 261.294 207.600 200.336 1.00 24.19 ? 2560 HIS A ND1   1 
ATOM   8684  C  CD2   . HIS A 1 2560 ? 259.169 207.830 200.778 1.00 17.07 ? 2560 HIS A CD2   1 
ATOM   8685  C  CE1   . HIS A 1 2560 ? 260.692 207.912 199.204 1.00 21.94 ? 2560 HIS A CE1   1 
ATOM   8686  N  NE2   . HIS A 1 2560 ? 259.401 208.058 199.444 1.00 18.97 ? 2560 HIS A NE2   1 
ATOM   8687  N  N     . LYS A 1 2561 ? 259.683 204.094 201.587 1.00 15.58 ? 2561 LYS A N     1 
ATOM   8688  C  CA    . LYS A 1 2561 ? 258.549 203.348 201.062 1.00 10.15 ? 2561 LYS A CA    1 
ATOM   8689  C  C     . LYS A 1 2561 ? 258.544 201.898 201.527 1.00 12.61 ? 2561 LYS A C     1 
ATOM   8690  O  O     . LYS A 1 2561 ? 257.925 201.047 200.879 1.00 17.22 ? 2561 LYS A O     1 
ATOM   8691  C  CB    . LYS A 1 2561 ? 258.535 203.404 199.534 1.00 15.51 ? 2561 LYS A CB    1 
ATOM   8692  C  CG    . LYS A 1 2561 ? 258.802 204.774 198.945 1.00 19.20 ? 2561 LYS A CG    1 
ATOM   8693  C  CD    . LYS A 1 2561 ? 258.874 204.699 197.427 1.00 18.67 ? 2561 LYS A CD    1 
ATOM   8694  C  CE    . LYS A 1 2561 ? 258.968 206.079 196.801 1.00 26.07 ? 2561 LYS A CE    1 
ATOM   8695  N  NZ    . LYS A 1 2561 ? 257.781 206.917 197.123 1.00 22.94 ? 2561 LYS A NZ    1 
ATOM   8696  N  N     . VAL A 1 2562 ? 259.222 201.599 202.633 1.00 13.99 ? 2562 VAL A N     1 
ATOM   8697  C  CA    . VAL A 1 2562 ? 259.370 200.223 203.092 1.00 11.82 ? 2562 VAL A CA    1 
ATOM   8698  C  C     . VAL A 1 2562 ? 258.010 199.688 203.523 1.00 14.59 ? 2562 VAL A C     1 
ATOM   8699  O  O     . VAL A 1 2562 ? 257.382 200.223 204.443 1.00 21.61 ? 2562 VAL A O     1 
ATOM   8700  C  CB    . VAL A 1 2562 ? 260.387 200.136 204.235 1.00 11.12 ? 2562 VAL A CB    1 
ATOM   8701  C  CG1   . VAL A 1 2562 ? 260.371 198.757 204.842 1.00 13.65 ? 2562 VAL A CG1   1 
ATOM   8702  C  CG2   . VAL A 1 2562 ? 261.773 200.480 203.739 1.00 13.29 ? 2562 VAL A CG2   1 
ATOM   8703  N  N     . ALA A 1 2563 ? 257.558 198.624 202.860 1.00 11.78 ? 2563 ALA A N     1 
ATOM   8704  C  CA    . ALA A 1 2563 ? 256.273 197.981 203.147 1.00 6.59  ? 2563 ALA A CA    1 
ATOM   8705  C  C     . ALA A 1 2563 ? 255.111 198.968 203.077 1.00 9.72  ? 2563 ALA A C     1 
ATOM   8706  O  O     . ALA A 1 2563 ? 254.147 198.863 203.840 1.00 11.81 ? 2563 ALA A O     1 
ATOM   8707  C  CB    . ALA A 1 2563 ? 256.296 197.273 204.503 1.00 6.34  ? 2563 ALA A CB    1 
ATOM   8708  N  N     . ALA A 1 2564 ? 255.194 199.936 202.169 1.00 13.36 ? 2564 ALA A N     1 
ATOM   8709  C  CA    . ALA A 1 2564 ? 254.096 200.864 201.972 1.00 11.22 ? 2564 ALA A CA    1 
ATOM   8710  C  C     . ALA A 1 2564 ? 252.965 200.180 201.201 1.00 18.47 ? 2564 ALA A C     1 
ATOM   8711  O  O     . ALA A 1 2564 ? 253.204 199.237 200.441 1.00 17.91 ? 2564 ALA A O     1 
ATOM   8712  C  CB    . ALA A 1 2564 ? 254.572 202.107 201.224 1.00 9.16  ? 2564 ALA A CB    1 
ATOM   8713  N  N     . PRO A 1 2565 ? 251.721 200.630 201.388 1.00 18.79 ? 2565 PRO A N     1 
ATOM   8714  C  CA    . PRO A 1 2565 ? 250.588 199.933 200.751 1.00 17.64 ? 2565 PRO A CA    1 
ATOM   8715  C  C     . PRO A 1 2565 ? 250.631 199.917 199.233 1.00 18.42 ? 2565 PRO A C     1 
ATOM   8716  O  O     . PRO A 1 2565 ? 250.047 199.017 198.619 1.00 27.05 ? 2565 PRO A O     1 
ATOM   8717  C  CB    . PRO A 1 2565 ? 249.371 200.712 201.272 1.00 15.79 ? 2565 PRO A CB    1 
ATOM   8718  C  CG    . PRO A 1 2565 ? 249.921 202.044 201.667 1.00 18.90 ? 2565 PRO A CG    1 
ATOM   8719  C  CD    . PRO A 1 2565 ? 251.258 201.731 202.246 1.00 14.47 ? 2565 PRO A CD    1 
ATOM   8720  N  N     . ASP A 1 2566 ? 251.294 200.884 198.604 1.00 13.72 ? 2566 ASP A N     1 
ATOM   8721  C  CA    . ASP A 1 2566 ? 251.307 200.996 197.152 1.00 15.70 ? 2566 ASP A CA    1 
ATOM   8722  C  C     . ASP A 1 2566 ? 252.497 200.284 196.516 1.00 13.95 ? 2566 ASP A C     1 
ATOM   8723  O  O     . ASP A 1 2566 ? 252.549 200.159 195.288 1.00 12.74 ? 2566 ASP A O     1 
ATOM   8724  C  CB    . ASP A 1 2566 ? 251.296 202.475 196.752 1.00 17.82 ? 2566 ASP A CB    1 
ATOM   8725  C  CG    . ASP A 1 2566 ? 251.152 202.682 195.259 1.00 23.17 ? 2566 ASP A CG    1 
ATOM   8726  O  OD1   . ASP A 1 2566 ? 250.033 202.490 194.742 1.00 26.89 ? 2566 ASP A OD1   1 
ATOM   8727  O  OD2   . ASP A 1 2566 ? 252.153 203.034 194.603 1.00 23.59 ? 2566 ASP A OD2   1 
ATOM   8728  N  N     . VAL A 1 2567 ? 253.440 199.791 197.315 1.00 11.92 ? 2567 VAL A N     1 
ATOM   8729  C  CA    . VAL A 1 2567 ? 254.684 199.222 196.809 1.00 5.08  ? 2567 VAL A CA    1 
ATOM   8730  C  C     . VAL A 1 2567 ? 254.518 197.721 196.638 1.00 4.06  ? 2567 VAL A C     1 
ATOM   8731  O  O     . VAL A 1 2567 ? 254.084 197.024 197.565 1.00 10.69 ? 2567 VAL A O     1 
ATOM   8732  C  CB    . VAL A 1 2567 ? 255.864 199.542 197.743 1.00 7.30  ? 2567 VAL A CB    1 
ATOM   8733  C  CG1   . VAL A 1 2567 ? 257.172 199.132 197.097 1.00 6.12  ? 2567 VAL A CG1   1 
ATOM   8734  C  CG2   . VAL A 1 2567 ? 255.885 201.018 198.070 1.00 10.05 ? 2567 VAL A CG2   1 
ATOM   8735  N  N     . VAL A 1 2568 ? 254.859 197.224 195.454 1.00 3.59  ? 2568 VAL A N     1 
ATOM   8736  C  CA    . VAL A 1 2568 ? 254.794 195.806 195.129 1.00 1.91  ? 2568 VAL A CA    1 
ATOM   8737  C  C     . VAL A 1 2568 ? 256.187 195.357 194.726 1.00 1.22  ? 2568 VAL A C     1 
ATOM   8738  O  O     . VAL A 1 2568 ? 256.777 195.911 193.790 1.00 3.08  ? 2568 VAL A O     1 
ATOM   8739  C  CB    . VAL A 1 2568 ? 253.786 195.522 194.003 1.00 2.39  ? 2568 VAL A CB    1 
ATOM   8740  C  CG1   . VAL A 1 2568 ? 253.677 194.027 193.744 1.00 0.58  ? 2568 VAL A CG1   1 
ATOM   8741  C  CG2   . VAL A 1 2568 ? 252.433 196.122 194.335 1.00 2.08  ? 2568 VAL A CG2   1 
ATOM   8742  N  N     . VAL A 1 2569 ? 256.717 194.362 195.430 1.00 1.25  ? 2569 VAL A N     1 
ATOM   8743  C  CA    . VAL A 1 2569 ? 258.001 193.776 195.061 1.00 1.38  ? 2569 VAL A CA    1 
ATOM   8744  C  C     . VAL A 1 2569 ? 257.751 192.772 193.945 1.00 1.64  ? 2569 VAL A C     1 
ATOM   8745  O  O     . VAL A 1 2569 ? 256.957 191.836 194.119 1.00 2.59  ? 2569 VAL A O     1 
ATOM   8746  C  CB    . VAL A 1 2569 ? 258.693 193.125 196.270 1.00 2.03  ? 2569 VAL A CB    1 
ATOM   8747  C  CG1   . VAL A 1 2569 ? 259.999 192.473 195.845 1.00 1.51  ? 2569 VAL A CG1   1 
ATOM   8748  C  CG2   . VAL A 1 2569 ? 258.935 194.159 197.355 1.00 1.33  ? 2569 VAL A CG2   1 
ATOM   8749  N  N     . PRO A 1 2570 ? 258.382 192.935 192.784 1.00 3.55  ? 2570 PRO A N     1 
ATOM   8750  C  CA    . PRO A 1 2570 ? 258.129 192.022 191.661 1.00 2.42  ? 2570 PRO A CA    1 
ATOM   8751  C  C     . PRO A 1 2570 ? 258.545 190.597 191.983 1.00 3.94  ? 2570 PRO A C     1 
ATOM   8752  O  O     . PRO A 1 2570 ? 259.684 190.334 192.372 1.00 4.79  ? 2570 PRO A O     1 
ATOM   8753  C  CB    . PRO A 1 2570 ? 258.976 192.617 190.531 1.00 2.53  ? 2570 PRO A CB    1 
ATOM   8754  C  CG    . PRO A 1 2570 ? 259.135 194.047 190.896 1.00 5.23  ? 2570 PRO A CG    1 
ATOM   8755  C  CD    . PRO A 1 2570 ? 259.226 194.071 192.388 1.00 5.08  ? 2570 PRO A CD    1 
ATOM   8756  N  N     . THR A 1 2571 ? 257.602 189.675 191.822 1.00 4.42  ? 2571 THR A N     1 
ATOM   8757  C  CA    . THR A 1 2571 ? 257.855 188.247 191.934 1.00 3.42  ? 2571 THR A CA    1 
ATOM   8758  C  C     . THR A 1 2571 ? 257.345 187.563 190.676 1.00 3.72  ? 2571 THR A C     1 
ATOM   8759  O  O     . THR A 1 2571 ? 256.731 188.188 189.807 1.00 6.14  ? 2571 THR A O     1 
ATOM   8760  C  CB    . THR A 1 2571 ? 257.194 187.640 193.182 1.00 5.19  ? 2571 THR A CB    1 
ATOM   8761  O  OG1   . THR A 1 2571 ? 255.768 187.667 193.038 1.00 5.62  ? 2571 THR A OG1   1 
ATOM   8762  C  CG2   . THR A 1 2571 ? 257.592 188.409 194.433 1.00 2.93  ? 2571 THR A CG2   1 
ATOM   8763  N  N     . LEU A 1 2572 ? 257.611 186.260 190.583 1.00 6.34  ? 2572 LEU A N     1 
ATOM   8764  C  CA    . LEU A 1 2572 ? 257.167 185.494 189.425 1.00 3.14  ? 2572 LEU A CA    1 
ATOM   8765  C  C     . LEU A 1 2572 ? 255.648 185.512 189.301 1.00 5.25  ? 2572 LEU A C     1 
ATOM   8766  O  O     . LEU A 1 2572 ? 255.110 185.628 188.195 1.00 9.67  ? 2572 LEU A O     1 
ATOM   8767  C  CB    . LEU A 1 2572 ? 257.679 184.057 189.521 1.00 7.07  ? 2572 LEU A CB    1 
ATOM   8768  C  CG    . LEU A 1 2572 ? 257.352 183.138 188.341 1.00 7.35  ? 2572 LEU A CG    1 
ATOM   8769  C  CD1   . LEU A 1 2572 ? 258.006 183.649 187.070 1.00 6.75  ? 2572 LEU A CD1   1 
ATOM   8770  C  CD2   . LEU A 1 2572 ? 257.769 181.706 188.630 1.00 10.90 ? 2572 LEU A CD2   1 
ATOM   8771  N  N     . ASP A 1 2573 ? 254.942 185.405 190.427 1.00 5.60  ? 2573 ASP A N     1 
ATOM   8772  C  CA    . ASP A 1 2573 ? 253.484 185.370 190.383 1.00 4.40  ? 2573 ASP A CA    1 
ATOM   8773  C  C     . ASP A 1 2573 ? 252.895 186.741 190.075 1.00 4.63  ? 2573 ASP A C     1 
ATOM   8774  O  O     . ASP A 1 2573 ? 251.902 186.843 189.346 1.00 7.75  ? 2573 ASP A O     1 
ATOM   8775  C  CB    . ASP A 1 2573 ? 252.935 184.832 191.704 1.00 5.24  ? 2573 ASP A CB    1 
ATOM   8776  C  CG    . ASP A 1 2573 ? 253.240 183.363 191.906 1.00 14.99 ? 2573 ASP A CG    1 
ATOM   8777  O  OD1   . ASP A 1 2573 ? 253.354 182.635 190.899 1.00 18.04 ? 2573 ASP A OD1   1 
ATOM   8778  O  OD2   . ASP A 1 2573 ? 253.366 182.930 193.069 1.00 17.62 ? 2573 ASP A OD2   1 
ATOM   8779  N  N     . THR A 1 2574 ? 253.484 187.806 190.625 1.00 3.39  ? 2574 THR A N     1 
ATOM   8780  C  CA    . THR A 1 2574 ? 252.903 189.136 190.454 1.00 2.69  ? 2574 THR A CA    1 
ATOM   8781  C  C     . THR A 1 2574 ? 252.946 189.589 188.999 1.00 2.06  ? 2574 THR A C     1 
ATOM   8782  O  O     . THR A 1 2574 ? 251.965 190.141 188.492 1.00 1.66  ? 2574 THR A O     1 
ATOM   8783  C  CB    . THR A 1 2574 ? 253.617 190.148 191.353 1.00 2.11  ? 2574 THR A CB    1 
ATOM   8784  O  OG1   . THR A 1 2574 ? 255.034 190.035 191.183 1.00 5.40  ? 2574 THR A OG1   1 
ATOM   8785  C  CG2   . THR A 1 2574 ? 253.261 189.911 192.811 1.00 1.00  ? 2574 THR A CG2   1 
ATOM   8786  N  N     . VAL A 1 2575 ? 254.069 189.370 188.314 1.00 2.89  ? 2575 VAL A N     1 
ATOM   8787  C  CA    . VAL A 1 2575 ? 254.185 189.818 186.929 1.00 2.96  ? 2575 VAL A CA    1 
ATOM   8788  C  C     . VAL A 1 2575 ? 253.266 189.009 186.017 1.00 2.86  ? 2575 VAL A C     1 
ATOM   8789  O  O     . VAL A 1 2575 ? 252.724 189.536 185.041 1.00 4.99  ? 2575 VAL A O     1 
ATOM   8790  C  CB    . VAL A 1 2575 ? 255.653 189.768 186.463 1.00 4.79  ? 2575 VAL A CB    1 
ATOM   8791  C  CG1   . VAL A 1 2575 ? 256.525 190.595 187.388 1.00 4.59  ? 2575 VAL A CG1   1 
ATOM   8792  C  CG2   . VAL A 1 2575 ? 256.159 188.335 186.389 1.00 6.88  ? 2575 VAL A CG2   1 
ATOM   8793  N  N     . ARG A 1 2576 ? 253.082 187.720 186.311 1.00 3.01  ? 2576 ARG A N     1 
ATOM   8794  C  CA    . ARG A 1 2576 ? 252.173 186.903 185.512 1.00 2.34  ? 2576 ARG A CA    1 
ATOM   8795  C  C     . ARG A 1 2576 ? 250.725 187.294 185.763 1.00 1.90  ? 2576 ARG A C     1 
ATOM   8796  O  O     . ARG A 1 2576 ? 249.940 187.453 184.820 1.00 1.69  ? 2576 ARG A O     1 
ATOM   8797  C  CB    . ARG A 1 2576 ? 252.384 185.419 185.818 1.00 3.05  ? 2576 ARG A CB    1 
ATOM   8798  C  CG    . ARG A 1 2576 ? 253.745 184.906 185.432 1.00 4.68  ? 2576 ARG A CG    1 
ATOM   8799  C  CD    . ARG A 1 2576 ? 253.898 183.416 185.687 1.00 4.48  ? 2576 ARG A CD    1 
ATOM   8800  N  NE    . ARG A 1 2576 ? 253.416 183.009 186.999 1.00 4.68  ? 2576 ARG A NE    1 
ATOM   8801  C  CZ    . ARG A 1 2576 ? 253.686 181.837 187.557 1.00 10.79 ? 2576 ARG A CZ    1 
ATOM   8802  N  NH1   . ARG A 1 2576 ? 254.434 180.935 186.943 1.00 8.04  ? 2576 ARG A NH1   1 
ATOM   8803  N  NH2   . ARG A 1 2576 ? 253.196 181.564 188.763 1.00 8.95  ? 2576 ARG A NH2   1 
ATOM   8804  N  N     . HIS A 1 2577 ? 250.350 187.447 187.034 1.00 2.04  ? 2577 HIS A N     1 
ATOM   8805  C  CA    . HIS A 1 2577 ? 248.977 187.807 187.363 1.00 1.48  ? 2577 HIS A CA    1 
ATOM   8806  C  C     . HIS A 1 2577 ? 248.632 189.199 186.853 1.00 1.57  ? 2577 HIS A C     1 
ATOM   8807  O  O     . HIS A 1 2577 ? 247.511 189.433 186.389 1.00 3.53  ? 2577 HIS A O     1 
ATOM   8808  C  CB    . HIS A 1 2577 ? 248.762 187.713 188.874 1.00 1.85  ? 2577 HIS A CB    1 
ATOM   8809  C  CG    . HIS A 1 2577 ? 248.733 186.311 189.394 1.00 1.79  ? 2577 HIS A CG    1 
ATOM   8810  N  ND1   . HIS A 1 2577 ? 248.840 186.012 190.735 1.00 3.79  ? 2577 HIS A ND1   1 
ATOM   8811  C  CD2   . HIS A 1 2577 ? 248.616 185.124 188.753 1.00 1.58  ? 2577 HIS A CD2   1 
ATOM   8812  C  CE1   . HIS A 1 2577 ? 248.783 184.703 190.899 1.00 1.89  ? 2577 HIS A CE1   1 
ATOM   8813  N  NE2   . HIS A 1 2577 ? 248.650 184.141 189.711 1.00 1.36  ? 2577 HIS A NE2   1 
ATOM   8814  N  N     . GLU A 1 2578 ? 249.580 190.134 186.935 1.00 1.53  ? 2578 GLU A N     1 
ATOM   8815  C  CA    . GLU A 1 2578 ? 249.334 191.490 186.452 1.00 1.58  ? 2578 GLU A CA    1 
ATOM   8816  C  C     . GLU A 1 2578 ? 249.099 191.502 184.947 1.00 1.94  ? 2578 GLU A C     1 
ATOM   8817  O  O     . GLU A 1 2578 ? 248.208 192.206 184.456 1.00 2.60  ? 2578 GLU A O     1 
ATOM   8818  C  CB    . GLU A 1 2578 ? 250.505 192.399 186.833 1.00 4.12  ? 2578 GLU A CB    1 
ATOM   8819  C  CG    . GLU A 1 2578 ? 250.282 193.887 186.599 1.00 7.63  ? 2578 GLU A CG    1 
ATOM   8820  C  CD    . GLU A 1 2578 ? 250.564 194.317 185.170 1.00 18.21 ? 2578 GLU A CD    1 
ATOM   8821  O  OE1   . GLU A 1 2578 ? 251.408 193.677 184.509 1.00 20.09 ? 2578 GLU A OE1   1 
ATOM   8822  O  OE2   . GLU A 1 2578 ? 249.941 195.297 184.708 1.00 18.08 ? 2578 GLU A OE2   1 
ATOM   8823  N  N     . ALA A 1 2579 ? 249.889 190.731 184.199 1.00 2.47  ? 2579 ALA A N     1 
ATOM   8824  C  CA    . ALA A 1 2579 ? 249.696 190.650 182.755 1.00 1.03  ? 2579 ALA A CA    1 
ATOM   8825  C  C     . ALA A 1 2579 ? 248.349 190.028 182.408 1.00 1.12  ? 2579 ALA A C     1 
ATOM   8826  O  O     . ALA A 1 2579 ? 247.658 190.499 181.499 1.00 1.33  ? 2579 ALA A O     1 
ATOM   8827  C  CB    . ALA A 1 2579 ? 250.834 189.854 182.119 1.00 0.76  ? 2579 ALA A CB    1 
ATOM   8828  N  N     . LEU A 1 2580 ? 247.965 188.963 183.117 1.00 1.05  ? 2580 LEU A N     1 
ATOM   8829  C  CA    . LEU A 1 2580 ? 246.666 188.343 182.878 1.00 0.76  ? 2580 LEU A CA    1 
ATOM   8830  C  C     . LEU A 1 2580 ? 245.528 189.286 183.242 1.00 0.92  ? 2580 LEU A C     1 
ATOM   8831  O  O     . LEU A 1 2580 ? 244.533 189.380 182.514 1.00 1.08  ? 2580 LEU A O     1 
ATOM   8832  C  CB    . LEU A 1 2580 ? 246.554 187.039 183.666 1.00 0.63  ? 2580 LEU A CB    1 
ATOM   8833  C  CG    . LEU A 1 2580 ? 245.255 186.255 183.471 1.00 1.24  ? 2580 LEU A CG    1 
ATOM   8834  C  CD1   . LEU A 1 2580 ? 245.175 185.700 182.057 1.00 1.38  ? 2580 LEU A CD1   1 
ATOM   8835  C  CD2   . LEU A 1 2580 ? 245.132 185.145 184.494 1.00 1.16  ? 2580 LEU A CD2   1 
ATOM   8836  N  N     . LEU A 1 2581 ? 245.655 189.991 184.368 1.00 1.40  ? 2581 LEU A N     1 
ATOM   8837  C  CA    . LEU A 1 2581 ? 244.640 190.967 184.750 1.00 1.07  ? 2581 LEU A CA    1 
ATOM   8838  C  C     . LEU A 1 2581 ? 244.555 192.093 183.732 1.00 1.11  ? 2581 LEU A C     1 
ATOM   8839  O  O     . LEU A 1 2581 ? 243.464 192.593 183.437 1.00 1.61  ? 2581 LEU A O     1 
ATOM   8840  C  CB    . LEU A 1 2581 ? 244.942 191.525 186.138 1.00 1.10  ? 2581 LEU A CB    1 
ATOM   8841  C  CG    . LEU A 1 2581 ? 244.573 190.652 187.333 1.00 1.35  ? 2581 LEU A CG    1 
ATOM   8842  C  CD1   . LEU A 1 2581 ? 244.690 191.450 188.613 1.00 0.66  ? 2581 LEU A CD1   1 
ATOM   8843  C  CD2   . LEU A 1 2581 ? 243.172 190.096 187.175 1.00 0.83  ? 2581 LEU A CD2   1 
ATOM   8844  N  N     . TYR A 1 2582 ? 245.701 192.508 183.186 1.00 0.87  ? 2582 TYR A N     1 
ATOM   8845  C  CA    . TYR A 1 2582 ? 245.714 193.562 182.180 1.00 1.56  ? 2582 TYR A CA    1 
ATOM   8846  C  C     . TYR A 1 2582 ? 244.875 193.180 180.969 1.00 3.50  ? 2582 TYR A C     1 
ATOM   8847  O  O     . TYR A 1 2582 ? 244.102 193.997 180.458 1.00 8.97  ? 2582 TYR A O     1 
ATOM   8848  C  CB    . TYR A 1 2582 ? 247.155 193.858 181.762 1.00 2.28  ? 2582 TYR A CB    1 
ATOM   8849  C  CG    . TYR A 1 2582 ? 247.325 195.080 180.895 1.00 5.11  ? 2582 TYR A CG    1 
ATOM   8850  C  CD1   . TYR A 1 2582 ? 247.112 195.023 179.523 1.00 6.00  ? 2582 TYR A CD1   1 
ATOM   8851  C  CD2   . TYR A 1 2582 ? 247.716 196.292 181.445 1.00 11.03 ? 2582 TYR A CD2   1 
ATOM   8852  C  CE1   . TYR A 1 2582 ? 247.272 196.138 178.730 1.00 6.08  ? 2582 TYR A CE1   1 
ATOM   8853  C  CE2   . TYR A 1 2582 ? 247.884 197.411 180.660 1.00 6.87  ? 2582 TYR A CE2   1 
ATOM   8854  C  CZ    . TYR A 1 2582 ? 247.659 197.329 179.303 1.00 11.74 ? 2582 TYR A CZ    1 
ATOM   8855  O  OH    . TYR A 1 2582 ? 247.823 198.447 178.516 1.00 25.69 ? 2582 TYR A OH    1 
ATOM   8856  N  N     . THR A 1 2583 ? 245.008 191.939 180.501 1.00 2.57  ? 2583 THR A N     1 
ATOM   8857  C  CA    . THR A 1 2583 ? 244.278 191.504 179.316 1.00 1.99  ? 2583 THR A CA    1 
ATOM   8858  C  C     . THR A 1 2583 ? 242.772 191.554 179.546 1.00 2.45  ? 2583 THR A C     1 
ATOM   8859  O  O     . THR A 1 2583 ? 242.029 192.132 178.745 1.00 8.27  ? 2583 THR A O     1 
ATOM   8860  C  CB    . THR A 1 2583 ? 244.722 190.095 178.923 1.00 3.78  ? 2583 THR A CB    1 
ATOM   8861  O  OG1   . THR A 1 2583 ? 246.029 190.150 178.340 1.00 3.93  ? 2583 THR A OG1   1 
ATOM   8862  C  CG2   . THR A 1 2583 ? 243.750 189.479 177.929 1.00 3.40  ? 2583 THR A CG2   1 
ATOM   8863  N  N     . TRP A 1 2584 ? 242.304 190.955 180.643 1.00 1.25  ? 2584 TRP A N     1 
ATOM   8864  C  CA    . TRP A 1 2584 ? 240.873 190.947 180.927 1.00 1.01  ? 2584 TRP A CA    1 
ATOM   8865  C  C     . TRP A 1 2584 ? 240.348 192.355 181.185 1.00 1.91  ? 2584 TRP A C     1 
ATOM   8866  O  O     . TRP A 1 2584 ? 239.269 192.717 180.704 1.00 1.99  ? 2584 TRP A O     1 
ATOM   8867  C  CB    . TRP A 1 2584 ? 240.582 190.038 182.119 1.00 0.77  ? 2584 TRP A CB    1 
ATOM   8868  C  CG    . TRP A 1 2584 ? 240.922 188.594 181.899 1.00 1.23  ? 2584 TRP A CG    1 
ATOM   8869  C  CD1   . TRP A 1 2584 ? 241.109 187.966 180.703 1.00 1.49  ? 2584 TRP A CD1   1 
ATOM   8870  C  CD2   . TRP A 1 2584 ? 241.111 187.597 182.908 1.00 0.92  ? 2584 TRP A CD2   1 
ATOM   8871  N  NE1   . TRP A 1 2584 ? 241.405 186.642 180.905 1.00 0.67  ? 2584 TRP A NE1   1 
ATOM   8872  C  CE2   . TRP A 1 2584 ? 241.413 186.389 182.250 1.00 0.90  ? 2584 TRP A CE2   1 
ATOM   8873  C  CE3   . TRP A 1 2584 ? 241.056 187.608 184.306 1.00 0.61  ? 2584 TRP A CE3   1 
ATOM   8874  C  CZ2   . TRP A 1 2584 ? 241.655 185.202 182.941 1.00 2.45  ? 2584 TRP A CZ2   1 
ATOM   8875  C  CZ3   . TRP A 1 2584 ? 241.297 186.429 184.990 1.00 0.66  ? 2584 TRP A CZ3   1 
ATOM   8876  C  CH2   . TRP A 1 2584 ? 241.591 185.244 184.305 1.00 0.78  ? 2584 TRP A CH2   1 
ATOM   8877  N  N     . LEU A 1 2585 ? 241.095 193.161 181.944 1.00 2.34  ? 2585 LEU A N     1 
ATOM   8878  C  CA    . LEU A 1 2585 ? 240.641 194.510 182.267 1.00 1.28  ? 2585 LEU A CA    1 
ATOM   8879  C  C     . LEU A 1 2585 ? 240.593 195.397 181.030 1.00 3.65  ? 2585 LEU A C     1 
ATOM   8880  O  O     . LEU A 1 2585 ? 239.654 196.183 180.862 1.00 2.85  ? 2585 LEU A O     1 
ATOM   8881  C  CB    . LEU A 1 2585 ? 241.548 195.129 183.328 1.00 0.96  ? 2585 LEU A CB    1 
ATOM   8882  C  CG    . LEU A 1 2585 ? 241.335 194.666 184.769 1.00 0.65  ? 2585 LEU A CG    1 
ATOM   8883  C  CD1   . LEU A 1 2585 ? 242.599 194.884 185.581 1.00 0.73  ? 2585 LEU A CD1   1 
ATOM   8884  C  CD2   . LEU A 1 2585 ? 240.166 195.398 185.387 1.00 0.38  ? 2585 LEU A CD2   1 
ATOM   8885  N  N     . ALA A 1 2586 ? 241.598 195.289 180.155 1.00 3.68  ? 2586 ALA A N     1 
ATOM   8886  C  CA    . ALA A 1 2586 ? 241.636 196.131 178.964 1.00 2.70  ? 2586 ALA A CA    1 
ATOM   8887  C  C     . ALA A 1 2586 ? 240.480 195.826 178.023 1.00 2.87  ? 2586 ALA A C     1 
ATOM   8888  O  O     . ALA A 1 2586 ? 240.070 196.691 177.242 1.00 3.64  ? 2586 ALA A O     1 
ATOM   8889  C  CB    . ALA A 1 2586 ? 242.972 195.962 178.240 1.00 2.94  ? 2586 ALA A CB    1 
ATOM   8890  N  N     . GLU A 1 2587 ? 239.946 194.612 178.081 1.00 3.69  ? 2587 GLU A N     1 
ATOM   8891  C  CA    . GLU A 1 2587 ? 238.792 194.227 177.284 1.00 3.49  ? 2587 GLU A CA    1 
ATOM   8892  C  C     . GLU A 1 2587 ? 237.472 194.492 177.993 1.00 2.37  ? 2587 GLU A C     1 
ATOM   8893  O  O     . GLU A 1 2587 ? 236.417 194.154 177.448 1.00 6.64  ? 2587 GLU A O     1 
ATOM   8894  C  CB    . GLU A 1 2587 ? 238.888 192.744 176.904 1.00 4.01  ? 2587 GLU A CB    1 
ATOM   8895  C  CG    . GLU A 1 2587 ? 240.094 192.364 176.038 1.00 6.49  ? 2587 GLU A CG    1 
ATOM   8896  C  CD    . GLU A 1 2587 ? 240.095 192.981 174.641 1.00 16.40 ? 2587 GLU A CD    1 
ATOM   8897  O  OE1   . GLU A 1 2587 ? 239.304 193.906 174.365 1.00 14.39 ? 2587 GLU A OE1   1 
ATOM   8898  O  OE2   . GLU A 1 2587 ? 240.909 192.533 173.807 1.00 16.33 ? 2587 GLU A OE2   1 
ATOM   8899  N  N     . HIS A 1 2588 ? 237.511 195.077 179.191 1.00 1.12  ? 2588 HIS A N     1 
ATOM   8900  C  CA    . HIS A 1 2588 ? 236.330 195.359 180.007 1.00 0.87  ? 2588 HIS A CA    1 
ATOM   8901  C  C     . HIS A 1 2588 ? 235.578 194.089 180.388 1.00 0.86  ? 2588 HIS A C     1 
ATOM   8902  O  O     . HIS A 1 2588 ? 234.382 194.131 180.681 1.00 1.54  ? 2588 HIS A O     1 
ATOM   8903  C  CB    . HIS A 1 2588 ? 235.397 196.350 179.304 1.00 0.39  ? 2588 HIS A CB    1 
ATOM   8904  C  CG    . HIS A 1 2588 ? 236.107 197.546 178.754 1.00 0.51  ? 2588 HIS A CG    1 
ATOM   8905  N  ND1   . HIS A 1 2588 ? 236.958 198.319 179.511 1.00 1.05  ? 2588 HIS A ND1   1 
ATOM   8906  C  CD2   . HIS A 1 2588 ? 236.119 198.083 177.511 1.00 0.30  ? 2588 HIS A CD2   1 
ATOM   8907  C  CE1   . HIS A 1 2588 ? 237.452 199.290 178.766 1.00 0.47  ? 2588 HIS A CE1   1 
ATOM   8908  N  NE2   . HIS A 1 2588 ? 236.958 199.170 177.548 1.00 0.42  ? 2588 HIS A NE2   1 
ATOM   8909  N  N     . LYS A 1 2589 ? 236.274 192.963 180.387 1.00 1.35  ? 2589 LYS A N     1 
ATOM   8910  C  CA    . LYS A 1 2589 ? 235.700 191.679 180.760 1.00 1.15  ? 2589 LYS A CA    1 
ATOM   8911  C  C     . LYS A 1 2589 ? 235.628 191.567 182.279 1.00 0.47  ? 2589 LYS A C     1 
ATOM   8912  O  O     . LYS A 1 2589 ? 236.644 191.755 182.955 1.00 1.05  ? 2589 LYS A O     1 
ATOM   8913  C  CB    . LYS A 1 2589 ? 236.546 190.542 180.186 1.00 1.62  ? 2589 LYS A CB    1 
ATOM   8914  C  CG    . LYS A 1 2589 ? 236.033 189.142 180.474 1.00 2.18  ? 2589 LYS A CG    1 
ATOM   8915  C  CD    . LYS A 1 2589 ? 235.034 188.691 179.420 1.00 4.10  ? 2589 LYS A CD    1 
ATOM   8916  C  CE    . LYS A 1 2589 ? 234.839 187.182 179.453 1.00 3.16  ? 2589 LYS A CE    1 
ATOM   8917  N  NZ    . LYS A 1 2589 ? 233.808 186.732 178.481 1.00 5.47  ? 2589 LYS A NZ    1 
ATOM   8918  N  N     . PRO A 1 2590 ? 234.457 191.287 182.849 1.00 0.34  ? 2590 PRO A N     1 
ATOM   8919  C  CA    . PRO A 1 2590 ? 234.380 191.084 184.300 1.00 0.19  ? 2590 PRO A CA    1 
ATOM   8920  C  C     . PRO A 1 2590 ? 235.236 189.902 184.731 1.00 0.20  ? 2590 PRO A C     1 
ATOM   8921  O  O     . PRO A 1 2590 ? 235.318 188.888 184.037 1.00 0.50  ? 2590 PRO A O     1 
ATOM   8922  C  CB    . PRO A 1 2590 ? 232.890 190.822 184.544 1.00 0.12  ? 2590 PRO A CB    1 
ATOM   8923  C  CG    . PRO A 1 2590 ? 232.377 190.341 183.234 1.00 0.17  ? 2590 PRO A CG    1 
ATOM   8924  C  CD    . PRO A 1 2590 ? 233.157 191.083 182.196 1.00 0.22  ? 2590 PRO A CD    1 
ATOM   8925  N  N     . LEU A 1 2591 ? 235.876 190.037 185.888 1.00 0.16  ? 2591 LEU A N     1 
ATOM   8926  C  CA    . LEU A 1 2591 ? 236.790 189.007 186.355 1.00 0.08  ? 2591 LEU A CA    1 
ATOM   8927  C  C     . LEU A 1 2591 ? 236.674 188.893 187.867 1.00 0.07  ? 2591 LEU A C     1 
ATOM   8928  O  O     . LEU A 1 2591 ? 236.214 189.815 188.545 1.00 0.03  ? 2591 LEU A O     1 
ATOM   8929  C  CB    . LEU A 1 2591 ? 238.233 189.308 185.922 1.00 0.22  ? 2591 LEU A CB    1 
ATOM   8930  C  CG    . LEU A 1 2591 ? 238.924 190.577 186.434 1.00 0.08  ? 2591 LEU A CG    1 
ATOM   8931  C  CD1   . LEU A 1 2591 ? 239.567 190.350 187.802 1.00 0.06  ? 2591 LEU A CD1   1 
ATOM   8932  C  CD2   . LEU A 1 2591 ? 239.935 191.115 185.437 1.00 0.31  ? 2591 LEU A CD2   1 
ATOM   8933  N  N     . VAL A 1 2592 ? 237.094 187.746 188.388 1.00 0.05  ? 2592 VAL A N     1 
ATOM   8934  C  CA    . VAL A 1 2592 ? 237.135 187.500 189.821 1.00 0.03  ? 2592 VAL A CA    1 
ATOM   8935  C  C     . VAL A 1 2592 ? 238.513 186.971 190.187 1.00 0.03  ? 2592 VAL A C     1 
ATOM   8936  O  O     . VAL A 1 2592 ? 239.004 186.023 189.566 1.00 0.04  ? 2592 VAL A O     1 
ATOM   8937  C  CB    . VAL A 1 2592 ? 236.032 186.518 190.270 1.00 0.04  ? 2592 VAL A CB    1 
ATOM   8938  C  CG1   . VAL A 1 2592 ? 236.393 185.873 191.594 1.00 0.06  ? 2592 VAL A CG1   1 
ATOM   8939  C  CG2   . VAL A 1 2592 ? 234.710 187.244 190.397 1.00 0.02  ? 2592 VAL A CG2   1 
ATOM   8940  N  N     . LEU A 1 2593 ? 239.136 187.592 191.182 1.00 0.04  ? 2593 LEU A N     1 
ATOM   8941  C  CA    . LEU A 1 2593 ? 240.342 187.068 191.807 1.00 0.04  ? 2593 LEU A CA    1 
ATOM   8942  C  C     . LEU A 1 2593 ? 239.938 186.266 193.036 1.00 0.04  ? 2593 LEU A C     1 
ATOM   8943  O  O     . LEU A 1 2593 ? 239.220 186.773 193.902 1.00 0.09  ? 2593 LEU A O     1 
ATOM   8944  C  CB    . LEU A 1 2593 ? 241.301 188.192 192.201 1.00 0.05  ? 2593 LEU A CB    1 
ATOM   8945  C  CG    . LEU A 1 2593 ? 241.752 189.176 191.123 1.00 0.07  ? 2593 LEU A CG    1 
ATOM   8946  C  CD1   . LEU A 1 2593 ? 240.949 190.458 191.205 1.00 0.07  ? 2593 LEU A CD1   1 
ATOM   8947  C  CD2   . LEU A 1 2593 ? 243.234 189.466 191.258 1.00 0.21  ? 2593 LEU A CD2   1 
ATOM   8948  N  N     . CYS A 1 2594 ? 240.386 185.020 193.104 1.00 0.07  ? 2594 CYS A N     1 
ATOM   8949  C  CA    . CYS A 1 2594 ? 240.067 184.140 194.216 1.00 0.13  ? 2594 CYS A CA    1 
ATOM   8950  C  C     . CYS A 1 2594 ? 241.352 183.687 194.892 1.00 0.14  ? 2594 CYS A C     1 
ATOM   8951  O  O     . CYS A 1 2594 ? 242.332 183.351 194.222 1.00 0.31  ? 2594 CYS A O     1 
ATOM   8952  C  CB    . CYS A 1 2594 ? 239.257 182.925 193.756 1.00 0.16  ? 2594 CYS A CB    1 
ATOM   8953  S  SG    . CYS A 1 2594 ? 238.562 181.947 195.103 1.00 0.80  ? 2594 CYS A SG    1 
ATOM   8954  N  N     . GLY A 1 2595 ? 241.341 183.683 196.220 1.00 0.15  ? 2595 GLY A N     1 
ATOM   8955  C  CA    . GLY A 1 2595 ? 242.487 183.266 196.986 1.00 0.09  ? 2595 GLY A CA    1 
ATOM   8956  C  C     . GLY A 1 2595 ? 242.281 183.444 198.472 1.00 0.10  ? 2595 GLY A C     1 
ATOM   8957  O  O     . GLY A 1 2595 ? 241.296 184.035 198.921 1.00 0.37  ? 2595 GLY A O     1 
ATOM   8958  N  N     . PRO A 1 2596 ? 243.216 182.928 199.270 1.00 0.47  ? 2596 PRO A N     1 
ATOM   8959  C  CA    . PRO A 1 2596 ? 243.100 183.081 200.717 1.00 0.17  ? 2596 PRO A CA    1 
ATOM   8960  C  C     . PRO A 1 2596 ? 243.230 184.540 201.112 1.00 0.16  ? 2596 PRO A C     1 
ATOM   8961  O  O     . PRO A 1 2596 ? 243.910 185.326 200.430 1.00 0.16  ? 2596 PRO A O     1 
ATOM   8962  C  CB    . PRO A 1 2596 ? 244.276 182.246 201.257 1.00 0.22  ? 2596 PRO A CB    1 
ATOM   8963  C  CG    . PRO A 1 2596 ? 244.714 181.396 200.118 1.00 0.41  ? 2596 PRO A CG    1 
ATOM   8964  C  CD    . PRO A 1 2596 ? 244.428 182.186 198.893 1.00 0.60  ? 2596 PRO A CD    1 
ATOM   8965  N  N     . PRO A 1 2597 ? 242.591 184.952 202.208 1.00 0.18  ? 2597 PRO A N     1 
ATOM   8966  C  CA    . PRO A 1 2597 ? 242.640 186.367 202.614 1.00 0.23  ? 2597 PRO A CA    1 
ATOM   8967  C  C     . PRO A 1 2597 ? 244.067 186.828 202.860 1.00 0.28  ? 2597 PRO A C     1 
ATOM   8968  O  O     . PRO A 1 2597 ? 244.794 186.253 203.674 1.00 1.62  ? 2597 PRO A O     1 
ATOM   8969  C  CB    . PRO A 1 2597 ? 241.801 186.395 203.898 1.00 0.16  ? 2597 PRO A CB    1 
ATOM   8970  C  CG    . PRO A 1 2597 ? 241.713 184.966 204.342 1.00 0.15  ? 2597 PRO A CG    1 
ATOM   8971  C  CD    . PRO A 1 2597 ? 241.744 184.149 203.103 1.00 0.22  ? 2597 PRO A CD    1 
ATOM   8972  N  N     . GLY A 1 2598 ? 244.467 187.873 202.145 1.00 0.14  ? 2598 GLY A N     1 
ATOM   8973  C  CA    . GLY A 1 2598 ? 245.810 188.401 202.232 1.00 0.19  ? 2598 GLY A CA    1 
ATOM   8974  C  C     . GLY A 1 2598 ? 246.790 187.868 201.213 1.00 0.18  ? 2598 GLY A C     1 
ATOM   8975  O  O     . GLY A 1 2598 ? 247.996 188.088 201.369 1.00 0.20  ? 2598 GLY A O     1 
ATOM   8976  N  N     . SER A 1 2599 ? 246.320 187.181 200.172 1.00 0.18  ? 2599 SER A N     1 
ATOM   8977  C  CA    . SER A 1 2599 ? 247.216 186.579 199.193 1.00 0.34  ? 2599 SER A CA    1 
ATOM   8978  C  C     . SER A 1 2599 ? 247.691 187.562 198.132 1.00 0.28  ? 2599 SER A C     1 
ATOM   8979  O  O     . SER A 1 2599 ? 248.549 187.201 197.321 1.00 0.30  ? 2599 SER A O     1 
ATOM   8980  C  CB    . SER A 1 2599 ? 246.538 185.384 198.516 1.00 0.20  ? 2599 SER A CB    1 
ATOM   8981  O  OG    . SER A 1 2599 ? 245.369 185.778 197.820 1.00 0.16  ? 2599 SER A OG    1 
ATOM   8982  N  N     . GLY A 1 2600 ? 247.169 188.778 198.120 1.00 0.13  ? 2600 GLY A N     1 
ATOM   8983  C  CA    . GLY A 1 2600 ? 247.575 189.784 197.173 1.00 0.17  ? 2600 GLY A CA    1 
ATOM   8984  C  C     . GLY A 1 2600 ? 246.588 190.097 196.067 1.00 0.27  ? 2600 GLY A C     1 
ATOM   8985  O  O     . GLY A 1 2600 ? 247.005 190.611 195.026 1.00 1.66  ? 2600 GLY A O     1 
ATOM   8986  N  N     . LYS A 1 2601 ? 245.301 189.802 196.259 1.00 0.22  ? 2601 LYS A N     1 
ATOM   8987  C  CA    . LYS A 1 2601 ? 244.318 190.037 195.206 1.00 0.21  ? 2601 LYS A CA    1 
ATOM   8988  C  C     . LYS A 1 2601 ? 244.099 191.526 194.973 1.00 0.70  ? 2601 LYS A C     1 
ATOM   8989  O  O     . LYS A 1 2601 ? 244.123 191.994 193.829 1.00 0.71  ? 2601 LYS A O     1 
ATOM   8990  C  CB    . LYS A 1 2601 ? 243.005 189.340 195.560 1.00 0.14  ? 2601 LYS A CB    1 
ATOM   8991  C  CG    . LYS A 1 2601 ? 243.126 187.826 195.639 1.00 0.10  ? 2601 LYS A CG    1 
ATOM   8992  C  CD    . LYS A 1 2601 ? 241.817 187.176 196.045 1.00 0.06  ? 2601 LYS A CD    1 
ATOM   8993  C  CE    . LYS A 1 2601 ? 241.383 187.624 197.429 1.00 0.08  ? 2601 LYS A CE    1 
ATOM   8994  N  NZ    . LYS A 1 2601 ? 242.355 187.225 198.481 1.00 0.05  ? 2601 LYS A NZ    1 
ATOM   8995  N  N     . THR A 1 2602 ? 243.884 192.290 196.047 1.00 1.18  ? 2602 THR A N     1 
ATOM   8996  C  CA    . THR A 1 2602 ? 243.753 193.736 195.903 1.00 0.99  ? 2602 THR A CA    1 
ATOM   8997  C  C     . THR A 1 2602 ? 245.055 194.354 195.413 1.00 1.06  ? 2602 THR A C     1 
ATOM   8998  O  O     . THR A 1 2602 ? 245.042 195.276 194.590 1.00 1.26  ? 2602 THR A O     1 
ATOM   8999  C  CB    . THR A 1 2602 ? 243.329 194.366 197.231 1.00 1.24  ? 2602 THR A CB    1 
ATOM   9000  O  OG1   . THR A 1 2602 ? 242.196 193.667 197.756 1.00 9.14  ? 2602 THR A OG1   1 
ATOM   9001  C  CG2   . THR A 1 2602 ? 242.973 195.828 197.036 1.00 0.98  ? 2602 THR A CG2   1 
ATOM   9002  N  N     . MET A 1 2603 ? 246.187 193.855 195.908 1.00 0.58  ? 2603 MET A N     1 
ATOM   9003  C  CA    . MET A 1 2603 ? 247.483 194.378 195.493 1.00 0.47  ? 2603 MET A CA    1 
ATOM   9004  C  C     . MET A 1 2603 ? 247.718 194.155 194.005 1.00 0.81  ? 2603 MET A C     1 
ATOM   9005  O  O     . MET A 1 2603 ? 248.173 195.058 193.295 1.00 0.94  ? 2603 MET A O     1 
ATOM   9006  C  CB    . MET A 1 2603 ? 248.588 193.722 196.321 1.00 0.40  ? 2603 MET A CB    1 
ATOM   9007  C  CG    . MET A 1 2603 ? 249.965 194.277 196.062 1.00 0.40  ? 2603 MET A CG    1 
ATOM   9008  S  SD    . MET A 1 2603 ? 251.277 193.121 196.484 1.00 0.22  ? 2603 MET A SD    1 
ATOM   9009  C  CE    . MET A 1 2603 ? 250.941 191.781 195.347 1.00 0.30  ? 2603 MET A CE    1 
ATOM   9010  N  N     . THR A 1 2604 ? 247.406 192.955 193.511 1.00 0.55  ? 2604 THR A N     1 
ATOM   9011  C  CA    . THR A 1 2604 ? 247.608 192.667 192.096 1.00 0.80  ? 2604 THR A CA    1 
ATOM   9012  C  C     . THR A 1 2604 ? 246.653 193.473 191.222 1.00 0.80  ? 2604 THR A C     1 
ATOM   9013  O  O     . THR A 1 2604 ? 247.058 194.005 190.183 1.00 1.29  ? 2604 THR A O     1 
ATOM   9014  C  CB    . THR A 1 2604 ? 247.443 191.171 191.835 1.00 1.22  ? 2604 THR A CB    1 
ATOM   9015  O  OG1   . THR A 1 2604 ? 248.287 190.435 192.728 1.00 2.05  ? 2604 THR A OG1   1 
ATOM   9016  C  CG2   . THR A 1 2604 ? 247.826 190.839 190.407 1.00 0.86  ? 2604 THR A CG2   1 
ATOM   9017  N  N     . LEU A 1 2605 ? 245.386 193.576 191.627 1.00 0.67  ? 2605 LEU A N     1 
ATOM   9018  C  CA    . LEU A 1 2605 ? 244.410 194.314 190.833 1.00 0.61  ? 2605 LEU A CA    1 
ATOM   9019  C  C     . LEU A 1 2605 ? 244.782 195.788 190.728 1.00 0.97  ? 2605 LEU A C     1 
ATOM   9020  O  O     . LEU A 1 2605 ? 244.743 196.373 189.641 1.00 1.53  ? 2605 LEU A O     1 
ATOM   9021  C  CB    . LEU A 1 2605 ? 243.015 194.158 191.433 1.00 1.80  ? 2605 LEU A CB    1 
ATOM   9022  C  CG    . LEU A 1 2605 ? 241.963 195.103 190.849 1.00 1.06  ? 2605 LEU A CG    1 
ATOM   9023  C  CD1   . LEU A 1 2605 ? 241.655 194.750 189.401 1.00 0.37  ? 2605 LEU A CD1   1 
ATOM   9024  C  CD2   . LEU A 1 2605 ? 240.709 195.095 191.691 1.00 0.62  ? 2605 LEU A CD2   1 
ATOM   9025  N  N     . PHE A 1 2606 ? 245.151 196.404 191.852 1.00 1.19  ? 2606 PHE A N     1 
ATOM   9026  C  CA    . PHE A 1 2606 ? 245.515 197.817 191.828 1.00 1.25  ? 2606 PHE A CA    1 
ATOM   9027  C  C     . PHE A 1 2606 ? 246.843 198.042 191.120 1.00 1.50  ? 2606 PHE A C     1 
ATOM   9028  O  O     . PHE A 1 2606 ? 247.044 199.096 190.509 1.00 3.15  ? 2606 PHE A O     1 
ATOM   9029  C  CB    . PHE A 1 2606 ? 245.559 198.386 193.249 1.00 1.17  ? 2606 PHE A CB    1 
ATOM   9030  C  CG    . PHE A 1 2606 ? 244.208 198.508 193.910 1.00 1.70  ? 2606 PHE A CG    1 
ATOM   9031  C  CD1   . PHE A 1 2606 ? 243.074 197.957 193.334 1.00 2.01  ? 2606 PHE A CD1   1 
ATOM   9032  C  CD2   . PHE A 1 2606 ? 244.076 199.174 195.114 1.00 3.23  ? 2606 PHE A CD2   1 
ATOM   9033  C  CE1   . PHE A 1 2606 ? 241.840 198.069 193.945 1.00 1.54  ? 2606 PHE A CE1   1 
ATOM   9034  C  CE2   . PHE A 1 2606 ? 242.844 199.291 195.729 1.00 6.42  ? 2606 PHE A CE2   1 
ATOM   9035  C  CZ    . PHE A 1 2606 ? 241.726 198.738 195.143 1.00 1.84  ? 2606 PHE A CZ    1 
ATOM   9036  N  N     . SER A 1 2607 ? 247.758 197.075 191.193 1.00 1.84  ? 2607 SER A N     1 
ATOM   9037  C  CA    . SER A 1 2607 ? 249.001 197.180 190.439 1.00 1.68  ? 2607 SER A CA    1 
ATOM   9038  C  C     . SER A 1 2607 ? 248.739 197.150 188.939 1.00 3.41  ? 2607 SER A C     1 
ATOM   9039  O  O     . SER A 1 2607 ? 249.355 197.906 188.180 1.00 9.76  ? 2607 SER A O     1 
ATOM   9040  C  CB    . SER A 1 2607 ? 249.955 196.057 190.845 1.00 1.98  ? 2607 SER A CB    1 
ATOM   9041  O  OG    . SER A 1 2607 ? 251.162 196.114 190.108 1.00 12.41 ? 2607 SER A OG    1 
ATOM   9042  N  N     . ALA A 1 2608 ? 247.826 196.285 188.494 1.00 2.52  ? 2608 ALA A N     1 
ATOM   9043  C  CA    . ALA A 1 2608 ? 247.492 196.217 187.077 1.00 2.18  ? 2608 ALA A CA    1 
ATOM   9044  C  C     . ALA A 1 2608 ? 246.737 197.457 186.614 1.00 2.65  ? 2608 ALA A C     1 
ATOM   9045  O  O     . ALA A 1 2608 ? 246.890 197.879 185.463 1.00 3.18  ? 2608 ALA A O     1 
ATOM   9046  C  CB    . ALA A 1 2608 ? 246.675 194.958 186.790 1.00 1.71  ? 2608 ALA A CB    1 
ATOM   9047  N  N     . LEU A 1 2609 ? 245.924 198.050 187.491 1.00 2.31  ? 2609 LEU A N     1 
ATOM   9048  C  CA    . LEU A 1 2609 ? 245.174 199.243 187.114 1.00 3.35  ? 2609 LEU A CA    1 
ATOM   9049  C  C     . LEU A 1 2609 ? 246.085 200.446 186.910 1.00 6.28  ? 2609 LEU A C     1 
ATOM   9050  O  O     . LEU A 1 2609 ? 245.733 201.363 186.159 1.00 5.71  ? 2609 LEU A O     1 
ATOM   9051  C  CB    . LEU A 1 2609 ? 244.118 199.551 188.175 1.00 2.45  ? 2609 LEU A CB    1 
ATOM   9052  C  CG    . LEU A 1 2609 ? 242.912 198.614 188.192 1.00 1.52  ? 2609 LEU A CG    1 
ATOM   9053  C  CD1   . LEU A 1 2609 ? 242.057 198.865 189.417 1.00 1.03  ? 2609 LEU A CD1   1 
ATOM   9054  C  CD2   . LEU A 1 2609 ? 242.098 198.779 186.922 1.00 1.90  ? 2609 LEU A CD2   1 
ATOM   9055  N  N     . ARG A 1 2610 ? 247.245 200.470 187.569 1.00 8.09  ? 2610 ARG A N     1 
ATOM   9056  C  CA    . ARG A 1 2610 ? 248.175 201.582 187.390 1.00 5.48  ? 2610 ARG A CA    1 
ATOM   9057  C  C     . ARG A 1 2610 ? 248.722 201.620 185.970 1.00 9.36  ? 2610 ARG A C     1 
ATOM   9058  O  O     . ARG A 1 2610 ? 248.929 202.701 185.408 1.00 17.13 ? 2610 ARG A O     1 
ATOM   9059  C  CB    . ARG A 1 2610 ? 249.309 201.488 188.410 1.00 7.83  ? 2610 ARG A CB    1 
ATOM   9060  C  CG    . ARG A 1 2610 ? 248.833 201.637 189.843 1.00 5.62  ? 2610 ARG A CG    1 
ATOM   9061  C  CD    . ARG A 1 2610 ? 249.937 201.404 190.855 1.00 8.41  ? 2610 ARG A CD    1 
ATOM   9062  N  NE    . ARG A 1 2610 ? 249.376 201.156 192.179 1.00 9.98  ? 2610 ARG A NE    1 
ATOM   9063  C  CZ    . ARG A 1 2610 ? 249.673 200.111 192.938 1.00 8.19  ? 2610 ARG A CZ    1 
ATOM   9064  N  NH1   . ARG A 1 2610 ? 250.563 199.210 192.559 1.00 10.40 ? 2610 ARG A NH1   1 
ATOM   9065  N  NH2   . ARG A 1 2610 ? 249.061 199.968 194.110 1.00 9.07  ? 2610 ARG A NH2   1 
ATOM   9066  N  N     . ALA A 1 2611 ? 248.957 200.454 185.374 1.00 5.62  ? 2611 ALA A N     1 
ATOM   9067  C  CA    . ALA A 1 2611 ? 249.386 200.373 183.985 1.00 8.70  ? 2611 ALA A CA    1 
ATOM   9068  C  C     . ALA A 1 2611 ? 248.237 200.540 183.003 1.00 8.33  ? 2611 ALA A C     1 
ATOM   9069  O  O     . ALA A 1 2611 ? 248.459 200.453 181.791 1.00 16.28 ? 2611 ALA A O     1 
ATOM   9070  C  CB    . ALA A 1 2611 ? 250.089 199.037 183.727 1.00 7.83  ? 2611 ALA A CB    1 
ATOM   9071  N  N     . LEU A 1 2612 ? 247.023 200.776 183.492 1.00 5.77  ? 2612 LEU A N     1 
ATOM   9072  C  CA    . LEU A 1 2612 ? 245.832 200.894 182.655 1.00 8.32  ? 2612 LEU A CA    1 
ATOM   9073  C  C     . LEU A 1 2612 ? 245.125 202.193 183.015 1.00 6.23  ? 2612 LEU A C     1 
ATOM   9074  O  O     . LEU A 1 2612 ? 244.128 202.192 183.750 1.00 9.54  ? 2612 LEU A O     1 
ATOM   9075  C  CB    . LEU A 1 2612 ? 244.924 199.677 182.824 1.00 6.02  ? 2612 LEU A CB    1 
ATOM   9076  C  CG    . LEU A 1 2612 ? 244.042 199.282 181.642 1.00 7.05  ? 2612 LEU A CG    1 
ATOM   9077  C  CD1   . LEU A 1 2612 ? 244.872 199.130 180.389 1.00 6.15  ? 2612 LEU A CD1   1 
ATOM   9078  C  CD2   . LEU A 1 2612 ? 243.349 197.972 181.955 1.00 10.84 ? 2612 LEU A CD2   1 
ATOM   9079  N  N     . PRO A 1 2613 ? 245.617 203.328 182.512 1.00 8.96  ? 2613 PRO A N     1 
ATOM   9080  C  CA    . PRO A 1 2613 ? 244.951 204.604 182.792 1.00 9.24  ? 2613 PRO A CA    1 
ATOM   9081  C  C     . PRO A 1 2613 ? 243.581 204.674 182.139 1.00 22.98 ? 2613 PRO A C     1 
ATOM   9082  O  O     . PRO A 1 2613 ? 243.169 203.735 181.450 1.00 24.68 ? 2613 PRO A O     1 
ATOM   9083  C  CB    . PRO A 1 2613 ? 245.914 205.642 182.203 1.00 6.40  ? 2613 PRO A CB    1 
ATOM   9084  C  CG    . PRO A 1 2613 ? 246.629 204.909 181.128 1.00 10.43 ? 2613 PRO A CG    1 
ATOM   9085  C  CD    . PRO A 1 2613 ? 246.771 203.493 181.610 1.00 11.97 ? 2613 PRO A CD    1 
ATOM   9086  N  N     . ASP A 1 2614 ? 242.876 205.783 182.346 1.00 16.71 ? 2614 ASP A N     1 
ATOM   9087  C  CA    . ASP A 1 2614 ? 241.500 205.959 181.895 1.00 12.70 ? 2614 ASP A CA    1 
ATOM   9088  C  C     . ASP A 1 2614 ? 240.553 204.951 182.537 1.00 9.31  ? 2614 ASP A C     1 
ATOM   9089  O  O     . ASP A 1 2614 ? 239.533 204.586 181.944 1.00 13.10 ? 2614 ASP A O     1 
ATOM   9090  C  CB    . ASP A 1 2614 ? 241.397 205.884 180.364 1.00 14.68 ? 2614 ASP A CB    1 
ATOM   9091  C  CG    . ASP A 1 2614 ? 242.049 207.067 179.681 1.00 28.55 ? 2614 ASP A CG    1 
ATOM   9092  O  OD1   . ASP A 1 2614 ? 242.079 208.161 180.284 1.00 31.08 ? 2614 ASP A OD1   1 
ATOM   9093  O  OD2   . ASP A 1 2614 ? 242.533 206.904 178.541 1.00 28.22 ? 2614 ASP A OD2   1 
ATOM   9094  N  N     . MET A 1 2615 ? 240.875 204.493 183.745 1.00 7.93  ? 2615 MET A N     1 
ATOM   9095  C  CA    . MET A 1 2615 ? 240.032 203.565 184.489 1.00 6.35  ? 2615 MET A CA    1 
ATOM   9096  C  C     . MET A 1 2615 ? 240.080 203.925 185.966 1.00 6.21  ? 2615 MET A C     1 
ATOM   9097  O  O     . MET A 1 2615 ? 241.156 203.927 186.572 1.00 10.03 ? 2615 MET A O     1 
ATOM   9098  C  CB    . MET A 1 2615 ? 240.468 202.114 184.261 1.00 5.76  ? 2615 MET A CB    1 
ATOM   9099  C  CG    . MET A 1 2615 ? 239.805 201.476 183.051 1.00 10.48 ? 2615 MET A CG    1 
ATOM   9100  S  SD    . MET A 1 2615 ? 240.521 199.913 182.519 1.00 22.84 ? 2615 MET A SD    1 
ATOM   9101  C  CE    . MET A 1 2615 ? 240.069 198.830 183.866 1.00 2.27  ? 2615 MET A CE    1 
ATOM   9102  N  N     . GLU A 1 2616 ? 238.919 204.233 186.534 1.00 5.54  ? 2616 GLU A N     1 
ATOM   9103  C  CA    . GLU A 1 2616 ? 238.782 204.579 187.943 1.00 4.55  ? 2616 GLU A CA    1 
ATOM   9104  C  C     . GLU A 1 2616 ? 238.189 203.398 188.698 1.00 2.11  ? 2616 GLU A C     1 
ATOM   9105  O  O     . GLU A 1 2616 ? 237.176 202.833 188.277 1.00 5.42  ? 2616 GLU A O     1 
ATOM   9106  C  CB    . GLU A 1 2616 ? 237.894 205.811 188.121 1.00 9.87  ? 2616 GLU A CB    1 
ATOM   9107  C  CG    . GLU A 1 2616 ? 237.772 206.271 189.566 1.00 15.97 ? 2616 GLU A CG    1 
ATOM   9108  C  CD    . GLU A 1 2616 ? 236.927 207.521 189.728 1.00 23.01 ? 2616 GLU A CD    1 
ATOM   9109  O  OE1   . GLU A 1 2616 ? 236.408 208.031 188.716 1.00 24.34 ? 2616 GLU A OE1   1 
ATOM   9110  O  OE2   . GLU A 1 2616 ? 236.781 207.991 190.876 1.00 29.09 ? 2616 GLU A OE2   1 
ATOM   9111  N  N     . VAL A 1 2617 ? 238.811 203.039 189.816 1.00 1.12  ? 2617 VAL A N     1 
ATOM   9112  C  CA    . VAL A 1 2617 ? 238.370 201.917 190.636 1.00 0.83  ? 2617 VAL A CA    1 
ATOM   9113  C  C     . VAL A 1 2617 ? 237.594 202.455 191.831 1.00 0.35  ? 2617 VAL A C     1 
ATOM   9114  O  O     . VAL A 1 2617 ? 237.998 203.442 192.458 1.00 0.79  ? 2617 VAL A O     1 
ATOM   9115  C  CB    . VAL A 1 2617 ? 239.560 201.044 191.079 1.00 0.73  ? 2617 VAL A CB    1 
ATOM   9116  C  CG1   . VAL A 1 2617 ? 240.554 201.842 191.909 1.00 1.35  ? 2617 VAL A CG1   1 
ATOM   9117  C  CG2   . VAL A 1 2617 ? 239.072 199.822 191.848 1.00 0.63  ? 2617 VAL A CG2   1 
ATOM   9118  N  N     . VAL A 1 2618 ? 236.457 201.832 192.120 1.00 0.49  ? 2618 VAL A N     1 
ATOM   9119  C  CA    . VAL A 1 2618 ? 235.642 202.159 193.282 1.00 0.51  ? 2618 VAL A CA    1 
ATOM   9120  C  C     . VAL A 1 2618 ? 235.436 200.878 194.072 1.00 0.26  ? 2618 VAL A C     1 
ATOM   9121  O  O     . VAL A 1 2618 ? 234.821 199.927 193.573 1.00 0.52  ? 2618 VAL A O     1 
ATOM   9122  C  CB    . VAL A 1 2618 ? 234.298 202.788 192.884 1.00 0.41  ? 2618 VAL A CB    1 
ATOM   9123  C  CG1   . VAL A 1 2618 ? 233.354 202.818 194.070 1.00 0.45  ? 2618 VAL A CG1   1 
ATOM   9124  C  CG2   . VAL A 1 2618 ? 234.512 204.183 192.332 1.00 0.42  ? 2618 VAL A CG2   1 
ATOM   9125  N  N     . GLY A 1 2619 ? 235.942 200.853 195.299 1.00 0.21  ? 2619 GLY A N     1 
ATOM   9126  C  CA    . GLY A 1 2619 ? 235.894 199.651 196.109 1.00 0.45  ? 2619 GLY A CA    1 
ATOM   9127  C  C     . GLY A 1 2619 ? 234.602 199.461 196.875 1.00 0.34  ? 2619 GLY A C     1 
ATOM   9128  O  O     . GLY A 1 2619 ? 234.218 200.309 197.683 1.00 0.50  ? 2619 GLY A O     1 
ATOM   9129  N  N     . LEU A 1 2620 ? 233.924 198.347 196.625 1.00 0.74  ? 2620 LEU A N     1 
ATOM   9130  C  CA    . LEU A 1 2620 ? 232.736 197.952 197.367 1.00 0.68  ? 2620 LEU A CA    1 
ATOM   9131  C  C     . LEU A 1 2620 ? 233.071 196.729 198.206 1.00 0.66  ? 2620 LEU A C     1 
ATOM   9132  O  O     . LEU A 1 2620 ? 233.735 195.806 197.723 1.00 1.81  ? 2620 LEU A O     1 
ATOM   9133  C  CB    . LEU A 1 2620 ? 231.565 197.647 196.430 1.00 0.32  ? 2620 LEU A CB    1 
ATOM   9134  C  CG    . LEU A 1 2620 ? 230.970 198.814 195.643 1.00 0.51  ? 2620 LEU A CG    1 
ATOM   9135  C  CD1   . LEU A 1 2620 ? 231.667 198.978 194.300 1.00 0.98  ? 2620 LEU A CD1   1 
ATOM   9136  C  CD2   . LEU A 1 2620 ? 229.477 198.620 195.457 1.00 0.40  ? 2620 LEU A CD2   1 
ATOM   9137  N  N     . ASN A 1 2621 ? 232.622 196.727 199.452 1.00 0.75  ? 2621 ASN A N     1 
ATOM   9138  C  CA    . ASN A 1 2621 ? 232.931 195.661 200.399 1.00 1.05  ? 2621 ASN A CA    1 
ATOM   9139  C  C     . ASN A 1 2621 ? 231.643 194.911 200.714 1.00 0.79  ? 2621 ASN A C     1 
ATOM   9140  O  O     . ASN A 1 2621 ? 230.799 195.390 201.473 1.00 5.81  ? 2621 ASN A O     1 
ATOM   9141  C  CB    . ASN A 1 2621 ? 233.579 196.231 201.653 1.00 2.12  ? 2621 ASN A CB    1 
ATOM   9142  C  CG    . ASN A 1 2621 ? 234.913 196.873 201.364 1.00 5.56  ? 2621 ASN A CG    1 
ATOM   9143  O  OD1   . ASN A 1 2621 ? 235.000 198.084 201.177 1.00 2.97  ? 2621 ASN A OD1   1 
ATOM   9144  N  ND2   . ASN A 1 2621 ? 235.964 196.063 201.318 1.00 5.16  ? 2621 ASN A ND2   1 
ATOM   9145  N  N     . PHE A 1 2622 ? 231.498 193.732 200.121 1.00 0.63  ? 2622 PHE A N     1 
ATOM   9146  C  CA    . PHE A 1 2622 ? 230.297 192.936 200.310 1.00 0.46  ? 2622 PHE A CA    1 
ATOM   9147  C  C     . PHE A 1 2622 ? 230.309 192.275 201.682 1.00 0.88  ? 2622 PHE A C     1 
ATOM   9148  O  O     . PHE A 1 2622 ? 231.361 191.897 202.201 1.00 1.29  ? 2622 PHE A O     1 
ATOM   9149  C  CB    . PHE A 1 2622 ? 230.179 191.872 199.219 1.00 0.36  ? 2622 PHE A CB    1 
ATOM   9150  C  CG    . PHE A 1 2622 ? 229.687 192.398 197.897 1.00 0.57  ? 2622 PHE A CG    1 
ATOM   9151  C  CD1   . PHE A 1 2622 ? 229.719 193.753 197.611 1.00 0.36  ? 2622 PHE A CD1   1 
ATOM   9152  C  CD2   . PHE A 1 2622 ? 229.202 191.530 196.933 1.00 0.25  ? 2622 PHE A CD2   1 
ATOM   9153  C  CE1   . PHE A 1 2622 ? 229.273 194.229 196.397 1.00 0.27  ? 2622 PHE A CE1   1 
ATOM   9154  C  CE2   . PHE A 1 2622 ? 228.754 192.003 195.717 1.00 0.12  ? 2622 PHE A CE2   1 
ATOM   9155  C  CZ    . PHE A 1 2622 ? 228.789 193.354 195.450 1.00 0.13  ? 2622 PHE A CZ    1 
ATOM   9156  N  N     . SER A 1 2623 ? 229.130 192.151 202.268 1.00 0.71  ? 2623 SER A N     1 
ATOM   9157  C  CA    . SER A 1 2623 ? 228.927 191.397 203.493 1.00 0.75  ? 2623 SER A CA    1 
ATOM   9158  C  C     . SER A 1 2623 ? 227.875 190.327 203.224 1.00 0.56  ? 2623 SER A C     1 
ATOM   9159  O  O     . SER A 1 2623 ? 227.431 190.137 202.091 1.00 0.67  ? 2623 SER A O     1 
ATOM   9160  C  CB    . SER A 1 2623 ? 228.527 192.328 204.639 1.00 1.17  ? 2623 SER A CB    1 
ATOM   9161  O  OG    . SER A 1 2623 ? 227.238 192.876 204.426 1.00 1.54  ? 2623 SER A OG    1 
ATOM   9162  N  N     . SER A 1 2624 ? 227.477 189.618 204.280 1.00 0.81  ? 2624 SER A N     1 
ATOM   9163  C  CA    . SER A 1 2624 ? 226.382 188.664 204.137 1.00 1.04  ? 2624 SER A CA    1 
ATOM   9164  C  C     . SER A 1 2624 ? 225.067 189.370 203.837 1.00 0.82  ? 2624 SER A C     1 
ATOM   9165  O  O     . SER A 1 2624 ? 224.190 188.795 203.187 1.00 1.86  ? 2624 SER A O     1 
ATOM   9166  C  CB    . SER A 1 2624 ? 226.259 187.809 205.398 1.00 2.14  ? 2624 SER A CB    1 
ATOM   9167  O  OG    . SER A 1 2624 ? 226.052 188.612 206.545 1.00 5.90  ? 2624 SER A OG    1 
ATOM   9168  N  N     . ALA A 1 2625 ? 224.923 190.616 204.279 1.00 0.73  ? 2625 ALA A N     1 
ATOM   9169  C  CA    . ALA A 1 2625 ? 223.698 191.381 204.108 1.00 0.62  ? 2625 ALA A CA    1 
ATOM   9170  C  C     . ALA A 1 2625 ? 223.735 192.303 202.895 1.00 1.23  ? 2625 ALA A C     1 
ATOM   9171  O  O     . ALA A 1 2625 ? 222.847 193.148 202.748 1.00 2.34  ? 2625 ALA A O     1 
ATOM   9172  C  CB    . ALA A 1 2625 ? 223.406 192.196 205.369 1.00 1.62  ? 2625 ALA A CB    1 
ATOM   9173  N  N     . THR A 1 2626 ? 224.739 192.171 202.033 1.00 1.27  ? 2626 THR A N     1 
ATOM   9174  C  CA    . THR A 1 2626 ? 224.841 193.042 200.871 1.00 0.95  ? 2626 THR A CA    1 
ATOM   9175  C  C     . THR A 1 2626 ? 223.735 192.727 199.868 1.00 0.93  ? 2626 THR A C     1 
ATOM   9176  O  O     . THR A 1 2626 ? 223.535 191.570 199.488 1.00 1.18  ? 2626 THR A O     1 
ATOM   9177  C  CB    . THR A 1 2626 ? 226.214 192.895 200.215 1.00 0.66  ? 2626 THR A CB    1 
ATOM   9178  O  OG1   . THR A 1 2626 ? 227.202 193.530 201.032 1.00 1.07  ? 2626 THR A OG1   1 
ATOM   9179  C  CG2   . THR A 1 2626 ? 226.228 193.538 198.835 1.00 0.49  ? 2626 THR A CG2   1 
ATOM   9180  N  N     . THR A 1 2627 ? 223.020 193.761 199.445 1.00 1.65  ? 2627 THR A N     1 
ATOM   9181  C  CA    . THR A 1 2627 ? 221.953 193.656 198.460 1.00 1.10  ? 2627 THR A CA    1 
ATOM   9182  C  C     . THR A 1 2627 ? 222.352 194.464 197.230 1.00 1.15  ? 2627 THR A C     1 
ATOM   9183  O  O     . THR A 1 2627 ? 223.369 195.167 197.265 1.00 1.68  ? 2627 THR A O     1 
ATOM   9184  C  CB    . THR A 1 2627 ? 220.627 194.155 199.044 1.00 2.90  ? 2627 THR A CB    1 
ATOM   9185  O  OG1   . THR A 1 2627 ? 220.687 195.572 199.235 1.00 6.72  ? 2627 THR A OG1   1 
ATOM   9186  C  CG2   . THR A 1 2627 ? 220.340 193.479 200.374 1.00 2.18  ? 2627 THR A CG2   1 
ATOM   9187  N  N     . PRO A 1 2628 ? 221.605 194.388 196.124 1.00 2.12  ? 2628 PRO A N     1 
ATOM   9188  C  CA    . PRO A 1 2628 ? 221.926 195.250 194.976 1.00 1.36  ? 2628 PRO A CA    1 
ATOM   9189  C  C     . PRO A 1 2628 ? 221.888 196.730 195.304 1.00 1.41  ? 2628 PRO A C     1 
ATOM   9190  O  O     . PRO A 1 2628 ? 222.481 197.527 194.570 1.00 1.13  ? 2628 PRO A O     1 
ATOM   9191  C  CB    . PRO A 1 2628 ? 220.844 194.875 193.957 1.00 0.67  ? 2628 PRO A CB    1 
ATOM   9192  C  CG    . PRO A 1 2628 ? 220.549 193.464 194.261 1.00 0.45  ? 2628 PRO A CG    1 
ATOM   9193  C  CD    . PRO A 1 2628 ? 220.616 193.358 195.758 1.00 0.72  ? 2628 PRO A CD    1 
ATOM   9194  N  N     . GLU A 1 2629 ? 221.219 197.116 196.390 1.00 2.13  ? 2629 GLU A N     1 
ATOM   9195  C  CA    . GLU A 1 2629 ? 221.087 198.526 196.728 1.00 2.04  ? 2629 GLU A CA    1 
ATOM   9196  C  C     . GLU A 1 2629 ? 222.442 199.148 197.058 1.00 3.52  ? 2629 GLU A C     1 
ATOM   9197  O  O     . GLU A 1 2629 ? 222.633 200.354 196.868 1.00 4.24  ? 2629 GLU A O     1 
ATOM   9198  C  CB    . GLU A 1 2629 ? 220.115 198.677 197.896 1.00 3.31  ? 2629 GLU A CB    1 
ATOM   9199  C  CG    . GLU A 1 2629 ? 219.843 200.101 198.309 1.00 11.98 ? 2629 GLU A CG    1 
ATOM   9200  C  CD    . GLU A 1 2629 ? 219.123 200.877 197.220 1.00 17.79 ? 2629 GLU A CD    1 
ATOM   9201  O  OE1   . GLU A 1 2629 ? 218.424 200.250 196.399 1.00 16.67 ? 2629 GLU A OE1   1 
ATOM   9202  O  OE2   . GLU A 1 2629 ? 219.247 202.115 197.179 1.00 27.46 ? 2629 GLU A OE2   1 
ATOM   9203  N  N     . LEU A 1 2630 ? 223.391 198.344 197.547 1.00 1.41  ? 2630 LEU A N     1 
ATOM   9204  C  CA    . LEU A 1 2630 ? 224.752 198.834 197.745 1.00 0.95  ? 2630 LEU A CA    1 
ATOM   9205  C  C     . LEU A 1 2630 ? 225.388 199.250 196.426 1.00 1.80  ? 2630 LEU A C     1 
ATOM   9206  O  O     . LEU A 1 2630 ? 226.088 200.267 196.360 1.00 3.32  ? 2630 LEU A O     1 
ATOM   9207  C  CB    . LEU A 1 2630 ? 225.606 197.766 198.427 1.00 2.75  ? 2630 LEU A CB    1 
ATOM   9208  C  CG    . LEU A 1 2630 ? 227.031 198.191 198.791 1.00 0.84  ? 2630 LEU A CG    1 
ATOM   9209  C  CD1   . LEU A 1 2630 ? 227.037 199.061 200.033 1.00 3.56  ? 2630 LEU A CD1   1 
ATOM   9210  C  CD2   . LEU A 1 2630 ? 227.936 196.982 198.967 1.00 0.39  ? 2630 LEU A CD2   1 
ATOM   9211  N  N     . LEU A 1 2631 ? 225.170 198.466 195.371 1.00 1.37  ? 2631 LEU A N     1 
ATOM   9212  C  CA    . LEU A 1 2631 ? 225.652 198.853 194.051 1.00 0.76  ? 2631 LEU A CA    1 
ATOM   9213  C  C     . LEU A 1 2631 ? 224.955 200.116 193.561 1.00 1.12  ? 2631 LEU A C     1 
ATOM   9214  O  O     . LEU A 1 2631 ? 225.579 200.965 192.914 1.00 1.12  ? 2631 LEU A O     1 
ATOM   9215  C  CB    . LEU A 1 2631 ? 225.443 197.709 193.059 1.00 1.09  ? 2631 LEU A CB    1 
ATOM   9216  C  CG    . LEU A 1 2631 ? 226.281 196.439 193.232 1.00 0.50  ? 2631 LEU A CG    1 
ATOM   9217  C  CD1   . LEU A 1 2631 ? 225.775 195.340 192.323 1.00 0.20  ? 2631 LEU A CD1   1 
ATOM   9218  C  CD2   . LEU A 1 2631 ? 227.744 196.702 192.966 1.00 1.24  ? 2631 LEU A CD2   1 
ATOM   9219  N  N     . LEU A 1 2632 ? 223.663 200.257 193.866 1.00 1.52  ? 2632 LEU A N     1 
ATOM   9220  C  CA    . LEU A 1 2632 ? 222.893 201.388 193.362 1.00 0.98  ? 2632 LEU A CA    1 
ATOM   9221  C  C     . LEU A 1 2632 ? 223.341 202.700 193.995 1.00 1.94  ? 2632 LEU A C     1 
ATOM   9222  O  O     . LEU A 1 2632 ? 223.354 203.741 193.327 1.00 2.45  ? 2632 LEU A O     1 
ATOM   9223  C  CB    . LEU A 1 2632 ? 221.403 201.150 193.600 1.00 1.48  ? 2632 LEU A CB    1 
ATOM   9224  C  CG    . LEU A 1 2632 ? 220.828 199.960 192.830 1.00 1.13  ? 2632 LEU A CG    1 
ATOM   9225  C  CD1   . LEU A 1 2632 ? 219.424 199.630 193.301 1.00 2.24  ? 2632 LEU A CD1   1 
ATOM   9226  C  CD2   . LEU A 1 2632 ? 220.847 200.231 191.337 1.00 0.31  ? 2632 LEU A CD2   1 
ATOM   9227  N  N     . LYS A 1 2633 ? 223.697 202.677 195.281 1.00 3.13  ? 2633 LYS A N     1 
ATOM   9228  C  CA    . LYS A 1 2633 ? 224.242 203.875 195.914 1.00 1.89  ? 2633 LYS A CA    1 
ATOM   9229  C  C     . LYS A 1 2633 ? 225.558 204.289 195.271 1.00 2.07  ? 2633 LYS A C     1 
ATOM   9230  O  O     . LYS A 1 2633 ? 225.814 205.482 195.079 1.00 4.10  ? 2633 LYS A O     1 
ATOM   9231  C  CB    . LYS A 1 2633 ? 224.433 203.653 197.412 1.00 2.31  ? 2633 LYS A CB    1 
ATOM   9232  C  CG    . LYS A 1 2633 ? 223.173 203.362 198.191 1.00 3.22  ? 2633 LYS A CG    1 
ATOM   9233  C  CD    . LYS A 1 2633 ? 222.256 204.567 198.187 1.00 9.43  ? 2633 LYS A CD    1 
ATOM   9234  C  CE    . LYS A 1 2633 ? 221.082 204.370 199.116 1.00 14.12 ? 2633 LYS A CE    1 
ATOM   9235  N  NZ    . LYS A 1 2633 ? 220.135 203.345 198.654 1.00 18.10 ? 2633 LYS A NZ    1 
ATOM   9236  N  N     . THR A 1 2634 ? 226.406 203.315 194.936 1.00 1.71  ? 2634 THR A N     1 
ATOM   9237  C  CA    . THR A 1 2634 ? 227.644 203.618 194.228 1.00 1.33  ? 2634 THR A CA    1 
ATOM   9238  C  C     . THR A 1 2634 ? 227.359 204.238 192.865 1.00 1.25  ? 2634 THR A C     1 
ATOM   9239  O  O     . THR A 1 2634 ? 228.064 205.154 192.429 1.00 2.93  ? 2634 THR A O     1 
ATOM   9240  C  CB    . THR A 1 2634 ? 228.485 202.349 194.087 1.00 1.13  ? 2634 THR A CB    1 
ATOM   9241  O  OG1   . THR A 1 2634 ? 228.835 201.867 195.388 1.00 1.29  ? 2634 THR A OG1   1 
ATOM   9242  C  CG2   . THR A 1 2634 ? 229.752 202.622 193.306 1.00 0.88  ? 2634 THR A CG2   1 
ATOM   9243  N  N     . PHE A 1 2635 ? 226.320 203.755 192.180 1.00 0.80  ? 2635 PHE A N     1 
ATOM   9244  C  CA    . PHE A 1 2635 ? 225.923 204.361 190.914 1.00 1.00  ? 2635 PHE A CA    1 
ATOM   9245  C  C     . PHE A 1 2635 ? 225.440 205.792 191.117 1.00 2.23  ? 2635 PHE A C     1 
ATOM   9246  O  O     . PHE A 1 2635 ? 225.726 206.673 190.300 1.00 5.52  ? 2635 PHE A O     1 
ATOM   9247  C  CB    . PHE A 1 2635 ? 224.837 203.519 190.246 1.00 1.14  ? 2635 PHE A CB    1 
ATOM   9248  C  CG    . PHE A 1 2635 ? 225.319 202.189 189.744 1.00 0.80  ? 2635 PHE A CG    1 
ATOM   9249  C  CD1   . PHE A 1 2635 ? 226.646 202.004 189.398 1.00 0.49  ? 2635 PHE A CD1   1 
ATOM   9250  C  CD2   . PHE A 1 2635 ? 224.443 201.124 189.611 1.00 0.58  ? 2635 PHE A CD2   1 
ATOM   9251  C  CE1   . PHE A 1 2635 ? 227.089 200.784 188.934 1.00 0.51  ? 2635 PHE A CE1   1 
ATOM   9252  C  CE2   . PHE A 1 2635 ? 224.882 199.901 189.148 1.00 0.41  ? 2635 PHE A CE2   1 
ATOM   9253  C  CZ    . PHE A 1 2635 ? 226.208 199.731 188.808 1.00 0.43  ? 2635 PHE A CZ    1 
ATOM   9254  N  N     . ASP A 1 2636 ? 224.704 206.044 192.204 1.00 2.75  ? 2636 ASP A N     1 
ATOM   9255  C  CA    . ASP A 1 2636 ? 224.175 207.382 192.446 1.00 2.32  ? 2636 ASP A CA    1 
ATOM   9256  C  C     . ASP A 1 2636 ? 225.282 208.401 192.672 1.00 5.50  ? 2636 ASP A C     1 
ATOM   9257  O  O     . ASP A 1 2636 ? 225.130 209.571 192.305 1.00 9.14  ? 2636 ASP A O     1 
ATOM   9258  C  CB    . ASP A 1 2636 ? 223.232 207.364 193.648 1.00 2.65  ? 2636 ASP A CB    1 
ATOM   9259  C  CG    . ASP A 1 2636 ? 221.869 206.812 193.308 1.00 12.85 ? 2636 ASP A CG    1 
ATOM   9260  O  OD1   . ASP A 1 2636 ? 221.386 207.064 192.184 1.00 16.69 ? 2636 ASP A OD1   1 
ATOM   9261  O  OD2   . ASP A 1 2636 ? 221.278 206.125 194.168 1.00 21.01 ? 2636 ASP A OD2   1 
ATOM   9262  N  N     . HIS A 1 2637 ? 226.395 207.982 193.269 1.00 2.48  ? 2637 HIS A N     1 
ATOM   9263  C  CA    . HIS A 1 2637 ? 227.468 208.905 193.608 1.00 1.95  ? 2637 HIS A CA    1 
ATOM   9264  C  C     . HIS A 1 2637 ? 228.448 209.120 192.459 1.00 3.34  ? 2637 HIS A C     1 
ATOM   9265  O  O     . HIS A 1 2637 ? 228.908 210.245 192.242 1.00 2.92  ? 2637 HIS A O     1 
ATOM   9266  C  CB    . HIS A 1 2637 ? 228.218 208.398 194.842 1.00 1.91  ? 2637 HIS A CB    1 
ATOM   9267  C  CG    . HIS A 1 2637 ? 229.332 209.294 195.280 1.00 5.52  ? 2637 HIS A CG    1 
ATOM   9268  N  ND1   . HIS A 1 2637 ? 230.625 209.153 194.819 1.00 5.67  ? 2637 HIS A ND1   1 
ATOM   9269  C  CD2   . HIS A 1 2637 ? 229.350 210.344 196.133 1.00 5.70  ? 2637 HIS A CD2   1 
ATOM   9270  C  CE1   . HIS A 1 2637 ? 231.390 210.076 195.372 1.00 7.64  ? 2637 HIS A CE1   1 
ATOM   9271  N  NE2   . HIS A 1 2637 ? 230.641 210.813 196.174 1.00 6.21  ? 2637 HIS A NE2   1 
ATOM   9272  N  N     . TYR A 1 2638 ? 228.773 208.065 191.714 1.00 3.37  ? 2638 TYR A N     1 
ATOM   9273  C  CA    . TYR A 1 2638 ? 229.791 208.137 190.679 1.00 2.10  ? 2638 TYR A CA    1 
ATOM   9274  C  C     . TYR A 1 2638 ? 229.236 208.213 189.264 1.00 3.03  ? 2638 TYR A C     1 
ATOM   9275  O  O     . TYR A 1 2638 ? 230.006 208.474 188.334 1.00 4.12  ? 2638 TYR A O     1 
ATOM   9276  C  CB    . TYR A 1 2638 ? 230.728 206.925 190.774 1.00 1.94  ? 2638 TYR A CB    1 
ATOM   9277  C  CG    . TYR A 1 2638 ? 231.540 206.862 192.040 1.00 2.51  ? 2638 TYR A CG    1 
ATOM   9278  C  CD1   . TYR A 1 2638 ? 232.761 207.518 192.136 1.00 3.71  ? 2638 TYR A CD1   1 
ATOM   9279  C  CD2   . TYR A 1 2638 ? 231.095 206.142 193.139 1.00 1.60  ? 2638 TYR A CD2   1 
ATOM   9280  C  CE1   . TYR A 1 2638 ? 233.511 207.463 193.293 1.00 3.15  ? 2638 TYR A CE1   1 
ATOM   9281  C  CE2   . TYR A 1 2638 ? 231.838 206.081 194.299 1.00 2.24  ? 2638 TYR A CE2   1 
ATOM   9282  C  CZ    . TYR A 1 2638 ? 233.044 206.742 194.370 1.00 3.12  ? 2638 TYR A CZ    1 
ATOM   9283  O  OH    . TYR A 1 2638 ? 233.787 206.683 195.526 1.00 12.05 ? 2638 TYR A OH    1 
ATOM   9284  N  N     . CYS A 1 2639 ? 227.941 208.000 189.074 1.00 2.78  ? 2639 CYS A N     1 
ATOM   9285  C  CA    . CYS A 1 2639 ? 227.369 207.890 187.743 1.00 1.47  ? 2639 CYS A CA    1 
ATOM   9286  C  C     . CYS A 1 2639 ? 226.116 208.748 187.645 1.00 1.17  ? 2639 CYS A C     1 
ATOM   9287  O  O     . CYS A 1 2639 ? 225.519 209.134 188.652 1.00 1.63  ? 2639 CYS A O     1 
ATOM   9288  C  CB    . CYS A 1 2639 ? 227.039 206.430 187.401 1.00 1.39  ? 2639 CYS A CB    1 
ATOM   9289  S  SG    . CYS A 1 2639 ? 228.469 205.325 187.364 1.00 5.27  ? 2639 CYS A SG    1 
ATOM   9290  N  N     . GLU A 1 2640 ? 225.729 209.052 186.412 1.00 1.97  ? 2640 GLU A N     1 
ATOM   9291  C  CA    . GLU A 1 2640 ? 224.514 209.804 186.139 1.00 2.81  ? 2640 GLU A CA    1 
ATOM   9292  C  C     . GLU A 1 2640 ? 223.604 209.006 185.215 1.00 1.80  ? 2640 GLU A C     1 
ATOM   9293  O  O     . GLU A 1 2640 ? 224.066 208.265 184.345 1.00 1.16  ? 2640 GLU A O     1 
ATOM   9294  C  CB    . GLU A 1 2640 ? 224.826 211.173 185.514 1.00 2.54  ? 2640 GLU A CB    1 
ATOM   9295  C  CG    . GLU A 1 2640 ? 225.458 211.109 184.134 1.00 9.39  ? 2640 GLU A CG    1 
ATOM   9296  C  CD    . GLU A 1 2640 ? 225.805 212.481 183.586 1.00 25.04 ? 2640 GLU A CD    1 
ATOM   9297  O  OE1   . GLU A 1 2640 ? 225.572 213.483 184.293 1.00 21.27 ? 2640 GLU A OE1   1 
ATOM   9298  O  OE2   . GLU A 1 2640 ? 226.305 212.556 182.443 1.00 27.26 ? 2640 GLU A OE2   1 
ATOM   9299  N  N     . TYR A 1 2641 ? 222.302 209.155 185.431 1.00 3.56  ? 2641 TYR A N     1 
ATOM   9300  C  CA    . TYR A 1 2641 ? 221.290 208.629 184.523 1.00 1.71  ? 2641 TYR A CA    1 
ATOM   9301  C  C     . TYR A 1 2641 ? 220.924 209.722 183.530 1.00 1.61  ? 2641 TYR A C     1 
ATOM   9302  O  O     . TYR A 1 2641 ? 220.547 210.826 183.933 1.00 5.80  ? 2641 TYR A O     1 
ATOM   9303  C  CB    . TYR A 1 2641 ? 220.048 208.171 185.287 1.00 1.56  ? 2641 TYR A CB    1 
ATOM   9304  C  CG    . TYR A 1 2641 ? 220.270 207.021 186.240 1.00 1.53  ? 2641 TYR A CG    1 
ATOM   9305  C  CD1   . TYR A 1 2641 ? 220.725 207.242 187.532 1.00 2.33  ? 2641 TYR A CD1   1 
ATOM   9306  C  CD2   . TYR A 1 2641 ? 220.002 205.715 185.854 1.00 0.83  ? 2641 TYR A CD2   1 
ATOM   9307  C  CE1   . TYR A 1 2641 ? 220.921 206.195 188.409 1.00 1.87  ? 2641 TYR A CE1   1 
ATOM   9308  C  CE2   . TYR A 1 2641 ? 220.195 204.659 186.725 1.00 1.15  ? 2641 TYR A CE2   1 
ATOM   9309  C  CZ    . TYR A 1 2641 ? 220.655 204.905 188.001 1.00 1.80  ? 2641 TYR A CZ    1 
ATOM   9310  O  OH    . TYR A 1 2641 ? 220.848 203.861 188.870 1.00 2.93  ? 2641 TYR A OH    1 
ATOM   9311  N  N     . ARG A 1 2642 ? 221.045 209.426 182.239 1.00 1.75  ? 2642 ARG A N     1 
ATOM   9312  C  CA    . ARG A 1 2642 ? 220.699 210.382 181.199 1.00 3.36  ? 2642 ARG A CA    1 
ATOM   9313  C  C     . ARG A 1 2642 ? 219.705 209.763 180.224 1.00 5.43  ? 2642 ARG A C     1 
ATOM   9314  O  O     . ARG A 1 2642 ? 219.820 208.589 179.860 1.00 4.19  ? 2642 ARG A O     1 
ATOM   9315  C  CB    . ARG A 1 2642 ? 221.956 210.886 180.464 1.00 3.66  ? 2642 ARG A CB    1 
ATOM   9316  C  CG    . ARG A 1 2642 ? 222.597 209.923 179.477 1.00 3.62  ? 2642 ARG A CG    1 
ATOM   9317  C  CD    . ARG A 1 2642 ? 223.606 210.656 178.596 1.00 3.72  ? 2642 ARG A CD    1 
ATOM   9318  N  NE    . ARG A 1 2642 ? 224.165 209.813 177.544 1.00 5.87  ? 2642 ARG A NE    1 
ATOM   9319  C  CZ    . ARG A 1 2642 ? 225.081 208.875 177.740 1.00 6.56  ? 2642 ARG A CZ    1 
ATOM   9320  N  NH1   . ARG A 1 2642 ? 225.591 208.643 178.938 1.00 9.62  ? 2642 ARG A NH1   1 
ATOM   9321  N  NH2   . ARG A 1 2642 ? 225.502 208.154 176.704 1.00 4.16  ? 2642 ARG A NH2   1 
ATOM   9322  N  N     . ARG A 1 2643 ? 218.712 210.557 179.832 1.00 12.44 ? 2643 ARG A N     1 
ATOM   9323  C  CA    . ARG A 1 2643 ? 217.727 210.160 178.837 1.00 7.61  ? 2643 ARG A CA    1 
ATOM   9324  C  C     . ARG A 1 2643 ? 218.337 210.295 177.447 1.00 6.71  ? 2643 ARG A C     1 
ATOM   9325  O  O     . ARG A 1 2643 ? 218.800 211.374 177.066 1.00 8.24  ? 2643 ARG A O     1 
ATOM   9326  C  CB    . ARG A 1 2643 ? 216.466 211.016 178.962 1.00 7.82  ? 2643 ARG A CB    1 
ATOM   9327  C  CG    . ARG A 1 2643 ? 215.363 210.719 177.945 1.00 16.91 ? 2643 ARG A CG    1 
ATOM   9328  C  CD    . ARG A 1 2643 ? 214.729 209.340 178.078 1.00 19.64 ? 2643 ARG A CD    1 
ATOM   9329  N  NE    . ARG A 1 2643 ? 214.000 209.171 179.331 1.00 21.45 ? 2643 ARG A NE    1 
ATOM   9330  C  CZ    . ARG A 1 2643 ? 213.558 208.006 179.786 1.00 23.04 ? 2643 ARG A CZ    1 
ATOM   9331  N  NH1   . ARG A 1 2643 ? 213.712 206.890 179.092 1.00 17.83 ? 2643 ARG A NH1   1 
ATOM   9332  N  NH2   . ARG A 1 2643 ? 212.934 207.962 180.959 1.00 16.85 ? 2643 ARG A NH2   1 
ATOM   9333  N  N     . THR A 1 2644 ? 218.343 209.198 176.702 1.00 6.91  ? 2644 THR A N     1 
ATOM   9334  C  CA    . THR A 1 2644 ? 218.810 209.137 175.329 1.00 6.76  ? 2644 THR A CA    1 
ATOM   9335  C  C     . THR A 1 2644 ? 217.676 208.645 174.440 1.00 9.43  ? 2644 THR A C     1 
ATOM   9336  O  O     . THR A 1 2644 ? 216.702 208.064 174.933 1.00 12.73 ? 2644 THR A O     1 
ATOM   9337  C  CB    . THR A 1 2644 ? 220.025 208.205 175.191 1.00 8.84  ? 2644 THR A CB    1 
ATOM   9338  O  OG1   . THR A 1 2644 ? 219.597 206.839 175.263 1.00 11.77 ? 2644 THR A OG1   1 
ATOM   9339  C  CG2   . THR A 1 2644 ? 221.049 208.478 176.284 1.00 6.78  ? 2644 THR A CG2   1 
ATOM   9340  N  N     . PRO A 1 2645 ? 217.755 208.875 173.126 1.00 10.74 ? 2645 PRO A N     1 
ATOM   9341  C  CA    . PRO A 1 2645 ? 216.685 208.387 172.241 1.00 11.09 ? 2645 PRO A CA    1 
ATOM   9342  C  C     . PRO A 1 2645 ? 216.484 206.884 172.301 1.00 8.87  ? 2645 PRO A C     1 
ATOM   9343  O  O     . PRO A 1 2645 ? 215.383 206.405 172.000 1.00 10.29 ? 2645 PRO A O     1 
ATOM   9344  C  CB    . PRO A 1 2645 ? 217.154 208.835 170.850 1.00 8.99  ? 2645 PRO A CB    1 
ATOM   9345  C  CG    . PRO A 1 2645 ? 218.016 210.012 171.114 1.00 8.66  ? 2645 PRO A CG    1 
ATOM   9346  C  CD    . PRO A 1 2645 ? 218.729 209.705 172.395 1.00 6.08  ? 2645 PRO A CD    1 
ATOM   9347  N  N     . ASN A 1 2646 ? 217.509 206.124 172.677 1.00 8.58  ? 2646 ASN A N     1 
ATOM   9348  C  CA    . ASN A 1 2646 ? 217.416 204.674 172.758 1.00 8.53  ? 2646 ASN A CA    1 
ATOM   9349  C  C     . ASN A 1 2646 ? 217.117 204.167 174.163 1.00 9.33  ? 2646 ASN A C     1 
ATOM   9350  O  O     . ASN A 1 2646 ? 217.041 202.951 174.361 1.00 14.19 ? 2646 ASN A O     1 
ATOM   9351  C  CB    . ASN A 1 2646 ? 218.707 204.035 172.242 1.00 7.01  ? 2646 ASN A CB    1 
ATOM   9352  C  CG    . ASN A 1 2646 ? 218.739 203.932 170.735 1.00 15.81 ? 2646 ASN A CG    1 
ATOM   9353  O  OD1   . ASN A 1 2646 ? 219.038 204.903 170.040 1.00 15.50 ? 2646 ASN A OD1   1 
ATOM   9354  N  ND2   . ASN A 1 2646 ? 218.419 202.754 170.217 1.00 15.63 ? 2646 ASN A ND2   1 
ATOM   9355  N  N     . GLY A 1 2647 ? 216.948 205.055 175.134 1.00 6.72  ? 2647 GLY A N     1 
ATOM   9356  C  CA    . GLY A 1 2647 ? 216.638 204.678 176.496 1.00 2.71  ? 2647 GLY A CA    1 
ATOM   9357  C  C     . GLY A 1 2647 ? 217.562 205.345 177.488 1.00 3.51  ? 2647 GLY A C     1 
ATOM   9358  O  O     . GLY A 1 2647 ? 218.403 206.175 177.145 1.00 3.58  ? 2647 GLY A O     1 
ATOM   9359  N  N     . VAL A 1 2648 ? 217.396 204.962 178.748 1.00 1.88  ? 2648 VAL A N     1 
ATOM   9360  C  CA    . VAL A 1 2648 ? 218.201 205.513 179.831 1.00 1.26  ? 2648 VAL A CA    1 
ATOM   9361  C  C     . VAL A 1 2648 ? 219.565 204.837 179.835 1.00 1.04  ? 2648 VAL A C     1 
ATOM   9362  O  O     . VAL A 1 2648 ? 219.664 203.607 179.774 1.00 1.10  ? 2648 VAL A O     1 
ATOM   9363  C  CB    . VAL A 1 2648 ? 217.490 205.341 181.182 1.00 2.33  ? 2648 VAL A CB    1 
ATOM   9364  C  CG1   . VAL A 1 2648 ? 218.343 205.892 182.310 1.00 0.93  ? 2648 VAL A CG1   1 
ATOM   9365  C  CG2   . VAL A 1 2648 ? 216.136 206.024 181.153 1.00 1.27  ? 2648 VAL A CG2   1 
ATOM   9366  N  N     . VAL A 1 2649 ? 220.621 205.642 179.902 1.00 1.26  ? 2649 VAL A N     1 
ATOM   9367  C  CA    . VAL A 1 2649 ? 221.994 205.157 179.935 1.00 0.73  ? 2649 VAL A CA    1 
ATOM   9368  C  C     . VAL A 1 2649 ? 222.633 205.616 181.237 1.00 1.29  ? 2649 VAL A C     1 
ATOM   9369  O  O     . VAL A 1 2649 ? 222.544 206.796 181.594 1.00 2.62  ? 2649 VAL A O     1 
ATOM   9370  C  CB    . VAL A 1 2649 ? 222.802 205.650 178.721 1.00 1.72  ? 2649 VAL A CB    1 
ATOM   9371  C  CG1   . VAL A 1 2649 ? 224.288 205.443 178.948 1.00 2.43  ? 2649 VAL A CG1   1 
ATOM   9372  C  CG2   . VAL A 1 2649 ? 222.352 204.934 177.465 1.00 2.06  ? 2649 VAL A CG2   1 
ATOM   9373  N  N     . LEU A 1 2650 ? 223.254 204.683 181.953 1.00 1.21  ? 2650 LEU A N     1 
ATOM   9374  C  CA    . LEU A 1 2650 ? 224.004 204.987 183.165 1.00 0.39  ? 2650 LEU A CA    1 
ATOM   9375  C  C     . LEU A 1 2650 ? 225.491 204.959 182.836 1.00 0.32  ? 2650 LEU A C     1 
ATOM   9376  O  O     . LEU A 1 2650 ? 226.023 203.917 182.441 1.00 0.60  ? 2650 LEU A O     1 
ATOM   9377  C  CB    . LEU A 1 2650 ? 223.676 203.990 184.274 1.00 0.45  ? 2650 LEU A CB    1 
ATOM   9378  C  CG    . LEU A 1 2650 ? 224.311 204.235 185.644 1.00 0.25  ? 2650 LEU A CG    1 
ATOM   9379  C  CD1   . LEU A 1 2650 ? 223.744 205.492 186.276 1.00 0.45  ? 2650 LEU A CD1   1 
ATOM   9380  C  CD2   . LEU A 1 2650 ? 224.099 203.034 186.547 1.00 0.24  ? 2650 LEU A CD2   1 
ATOM   9381  N  N     . ALA A 1 2651 ? 226.152 206.099 182.995 1.00 0.47  ? 2651 ALA A N     1 
ATOM   9382  C  CA    . ALA A 1 2651 ? 227.560 206.249 182.669 1.00 0.66  ? 2651 ALA A CA    1 
ATOM   9383  C  C     . ALA A 1 2651 ? 228.261 207.006 183.786 1.00 1.05  ? 2651 ALA A C     1 
ATOM   9384  O  O     . ALA A 1 2651 ? 227.623 207.785 184.503 1.00 1.37  ? 2651 ALA A O     1 
ATOM   9385  C  CB    . ALA A 1 2651 ? 227.754 206.991 181.337 1.00 0.45  ? 2651 ALA A CB    1 
ATOM   9386  N  N     . PRO A 1 2652 ? 229.566 206.796 183.958 1.00 1.47  ? 2652 PRO A N     1 
ATOM   9387  C  CA    . PRO A 1 2652 ? 230.297 207.527 184.999 1.00 1.93  ? 2652 PRO A CA    1 
ATOM   9388  C  C     . PRO A 1 2652 ? 230.252 209.028 184.764 1.00 2.68  ? 2652 PRO A C     1 
ATOM   9389  O  O     . PRO A 1 2652 ? 230.222 209.503 183.627 1.00 2.20  ? 2652 PRO A O     1 
ATOM   9390  C  CB    . PRO A 1 2652 ? 231.728 206.988 184.877 1.00 2.14  ? 2652 PRO A CB    1 
ATOM   9391  C  CG    . PRO A 1 2652 ? 231.586 205.686 184.189 1.00 1.46  ? 2652 PRO A CG    1 
ATOM   9392  C  CD    . PRO A 1 2652 ? 230.429 205.828 183.262 1.00 0.99  ? 2652 PRO A CD    1 
ATOM   9393  N  N     . VAL A 1 2653 ? 230.246 209.776 185.869 1.00 5.81  ? 2653 VAL A N     1 
ATOM   9394  C  CA    . VAL A 1 2653 ? 230.191 211.234 185.795 1.00 3.40  ? 2653 VAL A CA    1 
ATOM   9395  C  C     . VAL A 1 2653 ? 231.404 211.770 185.047 1.00 4.55  ? 2653 VAL A C     1 
ATOM   9396  O  O     . VAL A 1 2653 ? 231.286 212.643 184.178 1.00 8.96  ? 2653 VAL A O     1 
ATOM   9397  C  CB    . VAL A 1 2653 ? 230.079 211.836 187.206 1.00 5.65  ? 2653 VAL A CB    1 
ATOM   9398  C  CG1   . VAL A 1 2653 ? 230.401 213.321 187.185 1.00 5.21  ? 2653 VAL A CG1   1 
ATOM   9399  C  CG2   . VAL A 1 2653 ? 228.689 211.596 187.770 1.00 3.61  ? 2653 VAL A CG2   1 
ATOM   9400  N  N     . GLN A 1 2654 ? 232.583 211.244 185.362 1.00 7.40  ? 2654 GLN A N     1 
ATOM   9401  C  CA    . GLN A 1 2654 ? 233.792 211.645 184.659 1.00 8.00  ? 2654 GLN A CA    1 
ATOM   9402  C  C     . GLN A 1 2654 ? 233.797 211.064 183.249 1.00 4.50  ? 2654 GLN A C     1 
ATOM   9403  O  O     . GLN A 1 2654 ? 233.597 209.860 183.060 1.00 5.66  ? 2654 GLN A O     1 
ATOM   9404  C  CB    . GLN A 1 2654 ? 235.022 211.184 185.437 1.00 9.15  ? 2654 GLN A CB    1 
ATOM   9405  C  CG    . GLN A 1 2654 ? 236.307 211.896 185.064 1.00 17.75 ? 2654 GLN A CG    1 
ATOM   9406  C  CD    . GLN A 1 2654 ? 237.513 211.312 185.771 1.00 25.21 ? 2654 GLN A CD    1 
ATOM   9407  O  OE1   . GLN A 1 2654 ? 238.641 211.767 185.578 1.00 28.95 ? 2654 GLN A OE1   1 
ATOM   9408  N  NE2   . GLN A 1 2654 ? 237.280 210.296 186.593 1.00 16.11 ? 2654 GLN A NE2   1 
ATOM   9409  N  N     . LEU A 1 2655 ? 234.026 211.922 182.261 1.00 10.75 ? 2655 LEU A N     1 
ATOM   9410  C  CA    . LEU A 1 2655 ? 233.988 211.524 180.862 1.00 10.09 ? 2655 LEU A CA    1 
ATOM   9411  C  C     . LEU A 1 2655 ? 235.306 210.890 180.438 1.00 10.44 ? 2655 LEU A C     1 
ATOM   9412  O  O     . LEU A 1 2655 ? 236.377 211.229 180.952 1.00 8.01  ? 2655 LEU A O     1 
ATOM   9413  C  CB    . LEU A 1 2655 ? 233.682 212.721 179.963 1.00 9.12  ? 2655 LEU A CB    1 
ATOM   9414  C  CG    . LEU A 1 2655 ? 232.427 213.552 180.238 1.00 13.10 ? 2655 LEU A CG    1 
ATOM   9415  C  CD1   . LEU A 1 2655 ? 232.066 214.356 179.005 1.00 10.67 ? 2655 LEU A CD1   1 
ATOM   9416  C  CD2   . LEU A 1 2655 ? 231.256 212.674 180.664 1.00 9.63  ? 2655 LEU A CD2   1 
ATOM   9417  N  N     . GLY A 1 2656 ? 235.216 209.960 179.491 1.00 10.44 ? 2656 GLY A N     1 
ATOM   9418  C  CA    . GLY A 1 2656 ? 236.395 209.299 178.974 1.00 6.20  ? 2656 GLY A CA    1 
ATOM   9419  C  C     . GLY A 1 2656 ? 237.003 208.273 179.895 1.00 7.88  ? 2656 GLY A C     1 
ATOM   9420  O  O     . GLY A 1 2656 ? 238.075 207.745 179.588 1.00 16.52 ? 2656 GLY A O     1 
ATOM   9421  N  N     . LYS A 1 2657 ? 236.352 207.967 181.010 1.00 8.93  ? 2657 LYS A N     1 
ATOM   9422  C  CA    . LYS A 1 2657 ? 236.864 207.034 182.000 1.00 5.71  ? 2657 LYS A CA    1 
ATOM   9423  C  C     . LYS A 1 2657 ? 235.949 205.824 182.097 1.00 3.80  ? 2657 LYS A C     1 
ATOM   9424  O  O     . LYS A 1 2657 ? 234.721 205.955 182.065 1.00 4.75  ? 2657 LYS A O     1 
ATOM   9425  C  CB    . LYS A 1 2657 ? 236.982 207.698 183.374 1.00 7.10  ? 2657 LYS A CB    1 
ATOM   9426  C  CG    . LYS A 1 2657 ? 237.932 208.872 183.425 1.00 7.67  ? 2657 LYS A CG    1 
ATOM   9427  C  CD    . LYS A 1 2657 ? 239.363 208.411 183.251 1.00 14.71 ? 2657 LYS A CD    1 
ATOM   9428  C  CE    . LYS A 1 2657 ? 240.336 209.571 183.294 1.00 20.76 ? 2657 LYS A CE    1 
ATOM   9429  N  NZ    . LYS A 1 2657 ? 240.398 210.175 184.650 1.00 23.83 ? 2657 LYS A NZ    1 
ATOM   9430  N  N     . TRP A 1 2658 ? 236.553 204.649 182.210 1.00 5.58  ? 2658 TRP A N     1 
ATOM   9431  C  CA    . TRP A 1 2658 ? 235.832 203.421 182.502 1.00 1.18  ? 2658 TRP A CA    1 
ATOM   9432  C  C     . TRP A 1 2658 ? 235.870 203.211 184.010 1.00 1.98  ? 2658 TRP A C     1 
ATOM   9433  O  O     . TRP A 1 2658 ? 236.950 203.176 184.605 1.00 6.59  ? 2658 TRP A O     1 
ATOM   9434  C  CB    . TRP A 1 2658 ? 236.447 202.232 181.770 1.00 1.52  ? 2658 TRP A CB    1 
ATOM   9435  C  CG    . TRP A 1 2658 ? 235.848 201.994 180.423 1.00 0.32  ? 2658 TRP A CG    1 
ATOM   9436  C  CD1   . TRP A 1 2658 ? 236.100 202.691 179.282 1.00 0.22  ? 2658 TRP A CD1   1 
ATOM   9437  C  CD2   . TRP A 1 2658 ? 234.880 200.996 180.080 1.00 0.29  ? 2658 TRP A CD2   1 
ATOM   9438  N  NE1   . TRP A 1 2658 ? 235.359 202.185 178.245 1.00 0.50  ? 2658 TRP A NE1   1 
ATOM   9439  C  CE2   . TRP A 1 2658 ? 234.599 201.146 178.709 1.00 0.26  ? 2658 TRP A CE2   1 
ATOM   9440  C  CE3   . TRP A 1 2658 ? 234.227 199.990 180.796 1.00 0.25  ? 2658 TRP A CE3   1 
ATOM   9441  C  CZ2   . TRP A 1 2658 ? 233.695 200.328 178.040 1.00 0.18  ? 2658 TRP A CZ2   1 
ATOM   9442  C  CZ3   . TRP A 1 2658 ? 233.329 199.182 180.133 1.00 0.23  ? 2658 TRP A CZ3   1 
ATOM   9443  C  CH2   . TRP A 1 2658 ? 233.070 199.354 178.768 1.00 0.18  ? 2658 TRP A CH2   1 
ATOM   9444  N  N     . LEU A 1 2659 ? 234.703 203.083 184.623 1.00 1.95  ? 2659 LEU A N     1 
ATOM   9445  C  CA    . LEU A 1 2659 ? 234.604 202.998 186.071 1.00 0.93  ? 2659 LEU A CA    1 
ATOM   9446  C  C     . LEU A 1 2659 ? 234.539 201.531 186.473 1.00 0.55  ? 2659 LEU A C     1 
ATOM   9447  O  O     . LEU A 1 2659 ? 233.697 200.779 185.970 1.00 0.73  ? 2659 LEU A O     1 
ATOM   9448  C  CB    . LEU A 1 2659 ? 233.380 203.769 186.562 1.00 0.55  ? 2659 LEU A CB    1 
ATOM   9449  C  CG    . LEU A 1 2659 ? 233.138 204.000 188.052 1.00 2.72  ? 2659 LEU A CG    1 
ATOM   9450  C  CD1   . LEU A 1 2659 ? 232.322 205.258 188.196 1.00 9.10  ? 2659 LEU A CD1   1 
ATOM   9451  C  CD2   . LEU A 1 2659 ? 232.431 202.859 188.710 1.00 2.40  ? 2659 LEU A CD2   1 
ATOM   9452  N  N     . VAL A 1 2660 ? 235.429 201.126 187.374 1.00 0.68  ? 2660 VAL A N     1 
ATOM   9453  C  CA    . VAL A 1 2660 ? 235.584 199.732 187.772 1.00 0.36  ? 2660 VAL A CA    1 
ATOM   9454  C  C     . VAL A 1 2660 ? 234.991 199.562 189.162 1.00 0.36  ? 2660 VAL A C     1 
ATOM   9455  O  O     . VAL A 1 2660 ? 235.465 200.177 190.124 1.00 0.56  ? 2660 VAL A O     1 
ATOM   9456  C  CB    . VAL A 1 2660 ? 237.059 199.299 187.751 1.00 0.47  ? 2660 VAL A CB    1 
ATOM   9457  C  CG1   . VAL A 1 2660 ? 237.184 197.805 187.992 1.00 0.31  ? 2660 VAL A CG1   1 
ATOM   9458  C  CG2   . VAL A 1 2660 ? 237.710 199.691 186.438 1.00 0.36  ? 2660 VAL A CG2   1 
ATOM   9459  N  N     . LEU A 1 2661 ? 233.959 198.728 189.272 1.00 0.54  ? 2661 LEU A N     1 
ATOM   9460  C  CA    . LEU A 1 2661 ? 233.388 198.373 190.567 1.00 0.33  ? 2661 LEU A CA    1 
ATOM   9461  C  C     . LEU A 1 2661 ? 234.151 197.172 191.107 1.00 0.30  ? 2661 LEU A C     1 
ATOM   9462  O  O     . LEU A 1 2661 ? 234.034 196.064 190.576 1.00 0.26  ? 2661 LEU A O     1 
ATOM   9463  C  CB    . LEU A 1 2661 ? 231.898 198.053 190.468 1.00 0.72  ? 2661 LEU A CB    1 
ATOM   9464  C  CG    . LEU A 1 2661 ? 230.875 199.184 190.351 1.00 0.79  ? 2661 LEU A CG    1 
ATOM   9465  C  CD1   . LEU A 1 2661 ? 230.942 199.819 188.994 1.00 2.69  ? 2661 LEU A CD1   1 
ATOM   9466  C  CD2   . LEU A 1 2661 ? 229.473 198.687 190.631 1.00 1.65  ? 2661 LEU A CD2   1 
ATOM   9467  N  N     . PHE A 1 2662 ? 234.925 197.389 192.163 1.00 0.49  ? 2662 PHE A N     1 
ATOM   9468  C  CA    . PHE A 1 2662 ? 235.690 196.329 192.801 1.00 0.34  ? 2662 PHE A CA    1 
ATOM   9469  C  C     . PHE A 1 2662 ? 234.916 195.814 194.008 1.00 0.47  ? 2662 PHE A C     1 
ATOM   9470  O  O     . PHE A 1 2662 ? 234.692 196.556 194.970 1.00 0.91  ? 2662 PHE A O     1 
ATOM   9471  C  CB    . PHE A 1 2662 ? 237.072 196.831 193.213 1.00 0.44  ? 2662 PHE A CB    1 
ATOM   9472  C  CG    . PHE A 1 2662 ? 237.907 195.796 193.906 1.00 1.06  ? 2662 PHE A CG    1 
ATOM   9473  C  CD1   . PHE A 1 2662 ? 237.847 194.468 193.524 1.00 1.09  ? 2662 PHE A CD1   1 
ATOM   9474  C  CD2   . PHE A 1 2662 ? 238.749 196.153 194.944 1.00 1.03  ? 2662 PHE A CD2   1 
ATOM   9475  C  CE1   . PHE A 1 2662 ? 238.610 193.519 194.160 1.00 0.94  ? 2662 PHE A CE1   1 
ATOM   9476  C  CE2   . PHE A 1 2662 ? 239.517 195.207 195.584 1.00 1.66  ? 2662 PHE A CE2   1 
ATOM   9477  C  CZ    . PHE A 1 2662 ? 239.449 193.889 195.193 1.00 1.73  ? 2662 PHE A CZ    1 
ATOM   9478  N  N     . CYS A 1 2663 ? 234.510 194.549 193.953 1.00 0.52  ? 2663 CYS A N     1 
ATOM   9479  C  CA    . CYS A 1 2663 ? 233.787 193.892 195.035 1.00 0.68  ? 2663 CYS A CA    1 
ATOM   9480  C  C     . CYS A 1 2663 ? 234.721 192.895 195.708 1.00 1.10  ? 2663 CYS A C     1 
ATOM   9481  O  O     . CYS A 1 2663 ? 235.151 191.922 195.081 1.00 0.86  ? 2663 CYS A O     1 
ATOM   9482  C  CB    . CYS A 1 2663 ? 232.530 193.203 194.503 1.00 0.96  ? 2663 CYS A CB    1 
ATOM   9483  S  SG    . CYS A 1 2663 ? 231.527 194.246 193.413 1.00 1.45  ? 2663 CYS A SG    1 
ATOM   9484  N  N     . ASP A 1 2664 ? 235.023 193.135 196.985 1.00 1.35  ? 2664 ASP A N     1 
ATOM   9485  C  CA    . ASP A 1 2664 ? 236.085 192.422 197.687 1.00 1.93  ? 2664 ASP A CA    1 
ATOM   9486  C  C     . ASP A 1 2664 ? 235.650 191.082 198.268 1.00 4.89  ? 2664 ASP A C     1 
ATOM   9487  O  O     . ASP A 1 2664 ? 236.505 190.221 198.503 1.00 5.61  ? 2664 ASP A O     1 
ATOM   9488  C  CB    . ASP A 1 2664 ? 236.638 193.294 198.818 1.00 3.05  ? 2664 ASP A CB    1 
ATOM   9489  C  CG    . ASP A 1 2664 ? 238.001 192.837 199.299 1.00 12.28 ? 2664 ASP A CG    1 
ATOM   9490  O  OD1   . ASP A 1 2664 ? 238.599 191.949 198.657 1.00 13.81 ? 2664 ASP A OD1   1 
ATOM   9491  O  OD2   . ASP A 1 2664 ? 238.475 193.365 200.326 1.00 16.96 ? 2664 ASP A OD2   1 
ATOM   9492  N  N     . GLU A 1 2665 ? 234.363 190.888 198.522 1.00 1.16  ? 2665 GLU A N     1 
ATOM   9493  C  CA    . GLU A 1 2665 ? 233.853 189.671 199.148 1.00 0.85  ? 2665 GLU A CA    1 
ATOM   9494  C  C     . GLU A 1 2665 ? 232.625 189.170 198.402 1.00 1.24  ? 2665 GLU A C     1 
ATOM   9495  O  O     . GLU A 1 2665 ? 231.578 188.884 198.987 1.00 1.39  ? 2665 GLU A O     1 
ATOM   9496  C  CB    . GLU A 1 2665 ? 233.541 189.915 200.620 1.00 1.32  ? 2665 GLU A CB    1 
ATOM   9497  C  CG    . GLU A 1 2665 ? 234.703 190.458 201.440 1.00 1.77  ? 2665 GLU A CG    1 
ATOM   9498  C  CD    . GLU A 1 2665 ? 235.754 189.405 201.752 1.00 3.67  ? 2665 GLU A CD    1 
ATOM   9499  O  OE1   . GLU A 1 2665 ? 235.528 188.218 201.443 1.00 5.49  ? 2665 GLU A OE1   1 
ATOM   9500  O  OE2   . GLU A 1 2665 ? 236.811 189.767 202.309 1.00 7.07  ? 2665 GLU A OE2   1 
ATOM   9501  N  N     . ILE A 1 2666 ? 232.755 189.057 197.078 1.00 0.72  ? 2666 ILE A N     1 
ATOM   9502  C  CA    . ILE A 1 2666 ? 231.610 188.876 196.192 1.00 0.35  ? 2666 ILE A CA    1 
ATOM   9503  C  C     . ILE A 1 2666 ? 230.810 187.609 196.484 1.00 0.32  ? 2666 ILE A C     1 
ATOM   9504  O  O     . ILE A 1 2666 ? 229.666 187.494 196.036 1.00 0.33  ? 2666 ILE A O     1 
ATOM   9505  C  CB    . ILE A 1 2666 ? 232.092 188.908 194.724 1.00 0.31  ? 2666 ILE A CB    1 
ATOM   9506  C  CG1   . ILE A 1 2666 ? 230.943 189.275 193.781 1.00 0.16  ? 2666 ILE A CG1   1 
ATOM   9507  C  CG2   . ILE A 1 2666 ? 232.742 187.588 194.336 1.00 0.17  ? 2666 ILE A CG2   1 
ATOM   9508  C  CD1   . ILE A 1 2666 ? 231.397 189.746 192.421 1.00 0.19  ? 2666 ILE A CD1   1 
ATOM   9509  N  N     . ASN A 1 2667 ? 231.364 186.657 197.232 1.00 0.68  ? 2667 ASN A N     1 
ATOM   9510  C  CA    . ASN A 1 2667 ? 230.665 185.407 197.499 1.00 0.41  ? 2667 ASN A CA    1 
ATOM   9511  C  C     . ASN A 1 2667 ? 230.190 185.275 198.946 1.00 0.51  ? 2667 ASN A C     1 
ATOM   9512  O  O     . ASN A 1 2667 ? 229.721 184.202 199.332 1.00 0.75  ? 2667 ASN A O     1 
ATOM   9513  C  CB    . ASN A 1 2667 ? 231.548 184.218 197.107 1.00 0.22  ? 2667 ASN A CB    1 
ATOM   9514  C  CG    . ASN A 1 2667 ? 232.807 184.125 197.933 1.00 0.63  ? 2667 ASN A CG    1 
ATOM   9515  O  OD1   . ASN A 1 2667 ? 233.316 185.127 198.428 1.00 4.61  ? 2667 ASN A OD1   1 
ATOM   9516  N  ND2   . ASN A 1 2667 ? 233.347 182.922 198.042 1.00 0.36  ? 2667 ASN A ND2   1 
ATOM   9517  N  N     . LEU A 1 2668 ? 230.315 186.329 199.755 1.00 0.58  ? 2668 LEU A N     1 
ATOM   9518  C  CA    . LEU A 1 2668 ? 229.673 186.390 201.070 1.00 0.77  ? 2668 LEU A CA    1 
ATOM   9519  C  C     . LEU A 1 2668 ? 228.168 186.652 201.110 1.00 0.46  ? 2668 LEU A C     1 
ATOM   9520  O  O     . LEU A 1 2668 ? 227.528 186.198 202.066 1.00 0.64  ? 2668 LEU A O     1 
ATOM   9521  C  CB    . LEU A 1 2668 ? 230.346 187.421 201.980 1.00 1.09  ? 2668 LEU A CB    1 
ATOM   9522  C  CG    . LEU A 1 2668 ? 231.749 187.049 202.445 1.00 2.36  ? 2668 LEU A CG    1 
ATOM   9523  C  CD1   . LEU A 1 2668 ? 232.357 188.168 203.261 1.00 3.81  ? 2668 LEU A CD1   1 
ATOM   9524  C  CD2   . LEU A 1 2668 ? 231.651 185.780 203.261 1.00 4.10  ? 2668 LEU A CD2   1 
ATOM   9525  N  N     . PRO A 1 2669 ? 227.562 187.397 200.175 1.00 0.71  ? 2669 PRO A N     1 
ATOM   9526  C  CA    . PRO A 1 2669 ? 226.143 187.740 200.339 1.00 0.73  ? 2669 PRO A CA    1 
ATOM   9527  C  C     . PRO A 1 2669 ? 225.275 186.510 200.566 1.00 0.61  ? 2669 PRO A C     1 
ATOM   9528  O  O     . PRO A 1 2669 ? 225.501 185.451 199.978 1.00 0.88  ? 2669 PRO A O     1 
ATOM   9529  C  CB    . PRO A 1 2669 ? 225.795 188.439 199.024 1.00 0.34  ? 2669 PRO A CB    1 
ATOM   9530  C  CG    . PRO A 1 2669 ? 227.063 189.041 198.603 1.00 0.38  ? 2669 PRO A CG    1 
ATOM   9531  C  CD    . PRO A 1 2669 ? 228.121 188.061 198.982 1.00 0.44  ? 2669 PRO A CD    1 
ATOM   9532  N  N     . ASP A 1 2670 ? 224.292 186.663 201.452 1.00 1.01  ? 2670 ASP A N     1 
ATOM   9533  C  CA    . ASP A 1 2670 ? 223.484 185.537 201.901 1.00 1.61  ? 2670 ASP A CA    1 
ATOM   9534  C  C     . ASP A 1 2670 ? 222.808 184.834 200.734 1.00 2.53  ? 2670 ASP A C     1 
ATOM   9535  O  O     . ASP A 1 2670 ? 222.205 185.469 199.866 1.00 1.75  ? 2670 ASP A O     1 
ATOM   9536  C  CB    . ASP A 1 2670 ? 222.424 186.004 202.900 1.00 1.28  ? 2670 ASP A CB    1 
ATOM   9537  C  CG    . ASP A 1 2670 ? 222.992 186.267 204.280 1.00 7.82  ? 2670 ASP A CG    1 
ATOM   9538  O  OD1   . ASP A 1 2670 ? 222.447 187.139 204.989 1.00 6.86  ? 2670 ASP A OD1   1 
ATOM   9539  O  OD2   . ASP A 1 2670 ? 223.974 185.599 204.661 1.00 11.92 ? 2670 ASP A OD2   1 
ATOM   9540  N  N     . MET A 1 2671 ? 222.916 183.512 200.724 1.00 1.69  ? 2671 MET A N     1 
ATOM   9541  C  CA    . MET A 1 2671 ? 222.161 182.673 199.812 1.00 1.03  ? 2671 MET A CA    1 
ATOM   9542  C  C     . MET A 1 2671 ? 220.833 182.321 200.466 1.00 2.23  ? 2671 MET A C     1 
ATOM   9543  O  O     . MET A 1 2671 ? 220.808 181.821 201.595 1.00 6.83  ? 2671 MET A O     1 
ATOM   9544  C  CB    . MET A 1 2671 ? 222.948 181.405 199.480 1.00 1.81  ? 2671 MET A CB    1 
ATOM   9545  C  CG    . MET A 1 2671 ? 222.301 180.521 198.439 1.00 1.79  ? 2671 MET A CG    1 
ATOM   9546  S  SD    . MET A 1 2671 ? 223.494 179.579 197.474 1.00 20.88 ? 2671 MET A SD    1 
ATOM   9547  C  CE    . MET A 1 2671 ? 224.268 180.875 196.516 1.00 0.98  ? 2671 MET A CE    1 
ATOM   9548  N  N     . ASP A 1 2672 ? 219.733 182.595 199.770 1.00 1.12  ? 2672 ASP A N     1 
ATOM   9549  C  CA    . ASP A 1 2672 ? 218.422 182.281 200.313 1.00 1.26  ? 2672 ASP A CA    1 
ATOM   9550  C  C     . ASP A 1 2672 ? 218.207 180.766 200.323 1.00 1.83  ? 2672 ASP A C     1 
ATOM   9551  O  O     . ASP A 1 2672 ? 219.058 179.982 199.891 1.00 1.38  ? 2672 ASP A O     1 
ATOM   9552  C  CB    . ASP A 1 2672 ? 217.330 183.010 199.530 1.00 1.73  ? 2672 ASP A CB    1 
ATOM   9553  C  CG    . ASP A 1 2672 ? 217.231 182.565 198.075 1.00 1.52  ? 2672 ASP A CG    1 
ATOM   9554  O  OD1   . ASP A 1 2672 ? 218.006 181.692 197.634 1.00 1.77  ? 2672 ASP A OD1   1 
ATOM   9555  O  OD2   . ASP A 1 2672 ? 216.358 183.099 197.365 1.00 3.18  ? 2672 ASP A OD2   1 
ATOM   9556  N  N     . LYS A 1 2673 ? 217.044 180.345 200.823 1.00 2.05  ? 2673 LYS A N     1 
ATOM   9557  C  CA    . LYS A 1 2673 ? 216.755 178.919 200.922 1.00 2.98  ? 2673 LYS A CA    1 
ATOM   9558  C  C     . LYS A 1 2673 ? 216.596 178.256 199.561 1.00 1.78  ? 2673 LYS A C     1 
ATOM   9559  O  O     . LYS A 1 2673 ? 216.560 177.024 199.492 1.00 3.93  ? 2673 LYS A O     1 
ATOM   9560  C  CB    . LYS A 1 2673 ? 215.500 178.689 201.768 1.00 2.26  ? 2673 LYS A CB    1 
ATOM   9561  C  CG    . LYS A 1 2673 ? 214.262 179.386 201.247 1.00 3.16  ? 2673 LYS A CG    1 
ATOM   9562  C  CD    . LYS A 1 2673 ? 213.020 178.970 202.014 1.00 5.38  ? 2673 LYS A CD    1 
ATOM   9563  C  CE    . LYS A 1 2673 ? 213.031 179.500 203.433 1.00 12.42 ? 2673 LYS A CE    1 
ATOM   9564  N  NZ    . LYS A 1 2673 ? 211.731 179.259 204.114 1.00 15.90 ? 2673 LYS A NZ    1 
ATOM   9565  N  N     . TYR A 1 2674 ? 216.506 179.035 198.484 1.00 1.99  ? 2674 TYR A N     1 
ATOM   9566  C  CA    . TYR A 1 2674 ? 216.379 178.503 197.135 1.00 1.19  ? 2674 TYR A CA    1 
ATOM   9567  C  C     . TYR A 1 2674 ? 217.655 178.675 196.317 1.00 1.85  ? 2674 TYR A C     1 
ATOM   9568  O  O     . TYR A 1 2674 ? 217.601 178.683 195.084 1.00 2.17  ? 2674 TYR A O     1 
ATOM   9569  C  CB    . TYR A 1 2674 ? 215.192 179.154 196.430 1.00 1.21  ? 2674 TYR A CB    1 
ATOM   9570  C  CG    . TYR A 1 2674 ? 213.951 179.203 197.288 1.00 1.95  ? 2674 TYR A CG    1 
ATOM   9571  C  CD1   . TYR A 1 2674 ? 213.260 178.042 197.610 1.00 1.88  ? 2674 TYR A CD1   1 
ATOM   9572  C  CD2   . TYR A 1 2674 ? 213.471 180.407 197.782 1.00 1.41  ? 2674 TYR A CD2   1 
ATOM   9573  C  CE1   . TYR A 1 2674 ? 212.128 178.080 198.394 1.00 1.28  ? 2674 TYR A CE1   1 
ATOM   9574  C  CE2   . TYR A 1 2674 ? 212.336 180.455 198.565 1.00 1.87  ? 2674 TYR A CE2   1 
ATOM   9575  C  CZ    . TYR A 1 2674 ? 211.669 179.288 198.869 1.00 1.59  ? 2674 TYR A CZ    1 
ATOM   9576  O  OH    . TYR A 1 2674 ? 210.541 179.331 199.650 1.00 5.23  ? 2674 TYR A OH    1 
ATOM   9577  N  N     . GLY A 1 2675 ? 218.799 178.822 196.981 1.00 2.97  ? 2675 GLY A N     1 
ATOM   9578  C  CA    . GLY A 1 2675 ? 220.083 178.809 196.303 1.00 1.99  ? 2675 GLY A CA    1 
ATOM   9579  C  C     . GLY A 1 2675 ? 220.401 180.025 195.462 1.00 1.45  ? 2675 GLY A C     1 
ATOM   9580  O  O     . GLY A 1 2675 ? 221.168 179.916 194.503 1.00 1.28  ? 2675 GLY A O     1 
ATOM   9581  N  N     . THR A 1 2676 ? 219.852 181.188 195.803 1.00 1.38  ? 2676 THR A N     1 
ATOM   9582  C  CA    . THR A 1 2676 ? 220.037 182.398 195.013 1.00 1.03  ? 2676 THR A CA    1 
ATOM   9583  C  C     . THR A 1 2676 ? 220.608 183.514 195.875 1.00 0.53  ? 2676 THR A C     1 
ATOM   9584  O  O     . THR A 1 2676 ? 220.129 183.755 196.986 1.00 0.53  ? 2676 THR A O     1 
ATOM   9585  C  CB    . THR A 1 2676 ? 218.714 182.851 194.386 1.00 1.10  ? 2676 THR A CB    1 
ATOM   9586  O  OG1   . THR A 1 2676 ? 218.193 181.806 193.557 1.00 1.52  ? 2676 THR A OG1   1 
ATOM   9587  C  CG2   . THR A 1 2676 ? 218.920 184.103 193.544 1.00 0.84  ? 2676 THR A CG2   1 
ATOM   9588  N  N     . GLN A 1 2677 ? 221.633 184.187 195.358 1.00 0.91  ? 2677 GLN A N     1 
ATOM   9589  C  CA    . GLN A 1 2677 ? 222.125 185.438 195.921 1.00 0.43  ? 2677 GLN A CA    1 
ATOM   9590  C  C     . GLN A 1 2677 ? 221.618 186.579 195.047 1.00 0.32  ? 2677 GLN A C     1 
ATOM   9591  O  O     . GLN A 1 2677 ? 221.903 186.614 193.845 1.00 0.91  ? 2677 GLN A O     1 
ATOM   9592  C  CB    . GLN A 1 2677 ? 223.651 185.448 195.993 1.00 0.20  ? 2677 GLN A CB    1 
ATOM   9593  C  CG    . GLN A 1 2677 ? 224.241 184.485 197.008 1.00 0.22  ? 2677 GLN A CG    1 
ATOM   9594  C  CD    . GLN A 1 2677 ? 225.720 184.237 196.781 1.00 0.42  ? 2677 GLN A CD    1 
ATOM   9595  O  OE1   . GLN A 1 2677 ? 226.113 183.639 195.782 1.00 0.59  ? 2677 GLN A OE1   1 
ATOM   9596  N  NE2   . GLN A 1 2677 ? 226.548 184.701 197.709 1.00 0.35  ? 2677 GLN A NE2   1 
ATOM   9597  N  N     . ARG A 1 2678 ? 220.863 187.500 195.648 1.00 0.09  ? 2678 ARG A N     1 
ATOM   9598  C  CA    . ARG A 1 2678 ? 220.197 188.537 194.865 1.00 0.09  ? 2678 ARG A CA    1 
ATOM   9599  C  C     . ARG A 1 2678 ? 221.202 189.443 194.161 1.00 0.12  ? 2678 ARG A C     1 
ATOM   9600  O  O     . ARG A 1 2678 ? 221.025 189.777 192.984 1.00 0.11  ? 2678 ARG A O     1 
ATOM   9601  C  CB    . ARG A 1 2678 ? 219.269 189.361 195.757 1.00 0.19  ? 2678 ARG A CB    1 
ATOM   9602  C  CG    . ARG A 1 2678 ? 218.536 190.466 195.014 1.00 0.28  ? 2678 ARG A CG    1 
ATOM   9603  C  CD    . ARG A 1 2678 ? 217.614 191.252 195.927 1.00 0.60  ? 2678 ARG A CD    1 
ATOM   9604  N  NE    . ARG A 1 2678 ? 216.557 190.426 196.497 1.00 2.15  ? 2678 ARG A NE    1 
ATOM   9605  C  CZ    . ARG A 1 2678 ? 215.672 190.855 197.385 1.00 2.06  ? 2678 ARG A CZ    1 
ATOM   9606  N  NH1   . ARG A 1 2678 ? 215.687 192.099 197.832 1.00 1.71  ? 2678 ARG A NH1   1 
ATOM   9607  N  NH2   . ARG A 1 2678 ? 214.748 190.012 197.838 1.00 3.34  ? 2678 ARG A NH2   1 
ATOM   9608  N  N     . VAL A 1 2679 ? 222.262 189.849 194.860 1.00 0.12  ? 2679 VAL A N     1 
ATOM   9609  C  CA    . VAL A 1 2679 ? 223.237 190.754 194.260 1.00 0.14  ? 2679 VAL A CA    1 
ATOM   9610  C  C     . VAL A 1 2679 ? 223.986 190.061 193.124 1.00 0.05  ? 2679 VAL A C     1 
ATOM   9611  O  O     . VAL A 1 2679 ? 224.325 190.690 192.118 1.00 0.01  ? 2679 VAL A O     1 
ATOM   9612  C  CB    . VAL A 1 2679 ? 224.189 191.315 195.335 1.00 0.16  ? 2679 VAL A CB    1 
ATOM   9613  C  CG1   . VAL A 1 2679 ? 225.125 190.242 195.862 1.00 0.07  ? 2679 VAL A CG1   1 
ATOM   9614  C  CG2   . VAL A 1 2679 ? 224.979 192.495 194.788 1.00 0.04  ? 2679 VAL A CG2   1 
ATOM   9615  N  N     . ILE A 1 2680 ? 224.244 188.758 193.260 1.00 0.03  ? 2680 ILE A N     1 
ATOM   9616  C  CA    . ILE A 1 2680 ? 224.915 188.023 192.193 1.00 0.04  ? 2680 ILE A CA    1 
ATOM   9617  C  C     . ILE A 1 2680 ? 224.040 187.967 190.947 1.00 0.03  ? 2680 ILE A C     1 
ATOM   9618  O  O     . ILE A 1 2680 ? 224.522 188.159 189.826 1.00 0.05  ? 2680 ILE A O     1 
ATOM   9619  C  CB    . ILE A 1 2680 ? 225.314 186.617 192.679 1.00 0.08  ? 2680 ILE A CB    1 
ATOM   9620  C  CG1   . ILE A 1 2680 ? 226.229 186.719 193.900 1.00 0.05  ? 2680 ILE A CG1   1 
ATOM   9621  C  CG2   . ILE A 1 2680 ? 225.998 185.838 191.566 1.00 0.02  ? 2680 ILE A CG2   1 
ATOM   9622  C  CD1   . ILE A 1 2680 ? 227.473 187.527 193.659 1.00 0.07  ? 2680 ILE A CD1   1 
ATOM   9623  N  N     . SER A 1 2681 ? 222.742 187.711 191.122 1.00 0.04  ? 2681 SER A N     1 
ATOM   9624  C  CA    . SER A 1 2681 ? 221.822 187.772 189.992 1.00 0.07  ? 2681 SER A CA    1 
ATOM   9625  C  C     . SER A 1 2681 ? 221.798 189.169 189.388 1.00 0.03  ? 2681 SER A C     1 
ATOM   9626  O  O     . SER A 1 2681 ? 221.705 189.326 188.166 1.00 0.10  ? 2681 SER A O     1 
ATOM   9627  C  CB    . SER A 1 2681 ? 220.417 187.355 190.428 1.00 0.11  ? 2681 SER A CB    1 
ATOM   9628  O  OG    . SER A 1 2681 ? 220.390 186.013 190.869 1.00 0.41  ? 2681 SER A OG    1 
ATOM   9629  N  N     . PHE A 1 2682 ? 221.880 190.195 190.235 1.00 0.04  ? 2682 PHE A N     1 
ATOM   9630  C  CA    . PHE A 1 2682 ? 221.913 191.567 189.747 1.00 0.02  ? 2682 PHE A CA    1 
ATOM   9631  C  C     . PHE A 1 2682 ? 223.173 191.839 188.934 1.00 0.05  ? 2682 PHE A C     1 
ATOM   9632  O  O     . PHE A 1 2682 ? 223.114 192.497 187.888 1.00 0.03  ? 2682 PHE A O     1 
ATOM   9633  C  CB    . PHE A 1 2682 ? 221.802 192.533 190.928 1.00 0.04  ? 2682 PHE A CB    1 
ATOM   9634  C  CG    . PHE A 1 2682 ? 221.640 193.965 190.529 1.00 0.05  ? 2682 PHE A CG    1 
ATOM   9635  C  CD1   . PHE A 1 2682 ? 220.415 194.448 190.110 1.00 0.06  ? 2682 PHE A CD1   1 
ATOM   9636  C  CD2   . PHE A 1 2682 ? 222.709 194.839 190.595 1.00 0.09  ? 2682 PHE A CD2   1 
ATOM   9637  C  CE1   . PHE A 1 2682 ? 220.264 195.769 189.750 1.00 0.08  ? 2682 PHE A CE1   1 
ATOM   9638  C  CE2   . PHE A 1 2682 ? 222.560 196.163 190.235 1.00 0.05  ? 2682 PHE A CE2   1 
ATOM   9639  C  CZ    . PHE A 1 2682 ? 221.338 196.627 189.813 1.00 0.03  ? 2682 PHE A CZ    1 
ATOM   9640  N  N     . ILE A 1 2683 ? 224.309 191.318 189.382 1.00 0.02  ? 2683 ILE A N     1 
ATOM   9641  C  CA    . ILE A 1 2683 ? 225.582 191.535 188.634 1.00 0.03  ? 2683 ILE A CA    1 
ATOM   9642  C  C     . ILE A 1 2683 ? 225.523 190.732 187.324 1.00 0.05  ? 2683 ILE A C     1 
ATOM   9643  O  O     . ILE A 1 2683 ? 225.981 191.259 186.290 1.00 0.01  ? 2683 ILE A O     1 
ATOM   9644  C  CB    . ILE A 1 2683 ? 226.816 191.197 189.490 1.00 0.02  ? 2683 ILE A CB    1 
ATOM   9645  C  CG1   . ILE A 1 2683 ? 226.851 192.033 190.771 1.00 0.02  ? 2683 ILE A CG1   1 
ATOM   9646  C  CG2   . ILE A 1 2683 ? 228.104 191.350 188.681 1.00 0.01  ? 2683 ILE A CG2   1 
ATOM   9647  C  CD1   . ILE A 1 2683 ? 227.965 191.660 191.731 1.00 0.02  ? 2683 ILE A CD1   1 
ATOM   9648  N  N     . ARG A 1 2684 ? 224.962 189.523 187.369 1.00 0.01  ? 2684 ARG A N     1 
ATOM   9649  C  CA    . ARG A 1 2684 ? 224.866 188.671 186.156 1.00 0.03  ? 2684 ARG A CA    1 
ATOM   9650  C  C     . ARG A 1 2684 ? 224.015 189.416 185.120 1.00 0.06  ? 2684 ARG A C     1 
ATOM   9651  O  O     . ARG A 1 2684 ? 224.397 189.423 183.932 1.00 0.06  ? 2684 ARG A O     1 
ATOM   9652  C  CB    . ARG A 1 2684 ? 224.280 187.294 186.490 1.00 0.07  ? 2684 ARG A CB    1 
ATOM   9653  C  CG    . ARG A 1 2684 ? 224.200 186.349 185.299 1.00 0.08  ? 2684 ARG A CG    1 
ATOM   9654  C  CD    . ARG A 1 2684 ? 222.803 185.777 185.133 1.00 0.10  ? 2684 ARG A CD    1 
ATOM   9655  N  NE    . ARG A 1 2684 ? 222.638 185.029 183.882 1.00 2.79  ? 2684 ARG A NE    1 
ATOM   9656  C  CZ    . ARG A 1 2684 ? 221.505 184.469 183.476 1.00 0.38  ? 2684 ARG A CZ    1 
ATOM   9657  N  NH1   . ARG A 1 2684 ? 220.407 184.599 184.196 1.00 0.19  ? 2684 ARG A NH1   1 
ATOM   9658  N  NH2   . ARG A 1 2684 ? 221.477 183.782 182.349 1.00 0.13  ? 2684 ARG A NH2   1 
ATOM   9659  N  N     . GLN A 1 2685 ? 222.924 190.033 185.568 1.00 0.04  ? 2685 GLN A N     1 
ATOM   9660  C  CA    . GLN A 1 2685 ? 222.051 190.811 184.655 1.00 0.05  ? 2685 GLN A CA    1 
ATOM   9661  C  C     . GLN A 1 2685 ? 222.868 191.951 184.027 1.00 0.10  ? 2685 GLN A C     1 
ATOM   9662  O  O     . GLN A 1 2685 ? 222.793 192.112 182.793 1.00 0.25  ? 2685 GLN A O     1 
ATOM   9663  C  CB    . GLN A 1 2685 ? 220.825 191.300 185.426 1.00 0.06  ? 2685 GLN A CB    1 
ATOM   9664  C  CG    . GLN A 1 2685 ? 219.876 192.183 184.623 1.00 0.05  ? 2685 GLN A CG    1 
ATOM   9665  C  CD    . GLN A 1 2685 ? 218.718 192.695 185.451 1.00 0.07  ? 2685 GLN A CD    1 
ATOM   9666  O  OE1   . GLN A 1 2685 ? 218.904 193.371 186.468 1.00 0.19  ? 2685 GLN A OE1   1 
ATOM   9667  N  NE2   . GLN A 1 2685 ? 217.507 192.368 185.027 1.00 0.07  ? 2685 GLN A NE2   1 
ATOM   9668  N  N     . MET A 1 2686 ? 223.634 192.695 184.830 1.00 0.10  ? 2686 MET A N     1 
ATOM   9669  C  CA    . MET A 1 2686 ? 224.356 193.839 184.280 1.00 0.23  ? 2686 MET A CA    1 
ATOM   9670  C  C     . MET A 1 2686 ? 225.463 193.416 183.323 1.00 0.37  ? 2686 MET A C     1 
ATOM   9671  O  O     . MET A 1 2686 ? 225.851 194.197 182.447 1.00 4.68  ? 2686 MET A O     1 
ATOM   9672  C  CB    . MET A 1 2686 ? 224.949 194.709 185.388 1.00 0.31  ? 2686 MET A CB    1 
ATOM   9673  C  CG    . MET A 1 2686 ? 223.935 195.470 186.207 1.00 0.24  ? 2686 MET A CG    1 
ATOM   9674  S  SD    . MET A 1 2686 ? 224.746 196.410 187.508 1.00 11.49 ? 2686 MET A SD    1 
ATOM   9675  C  CE    . MET A 1 2686 ? 225.399 195.099 188.526 1.00 0.07  ? 2686 MET A CE    1 
ATOM   9676  N  N     . VAL A 1 2687 ? 225.992 192.206 183.471 1.00 0.41  ? 2687 VAL A N     1 
ATOM   9677  C  CA    . VAL A 1 2687 ? 227.073 191.777 182.592 1.00 0.79  ? 2687 VAL A CA    1 
ATOM   9678  C  C     . VAL A 1 2687 ? 226.521 191.188 181.301 1.00 0.94  ? 2687 VAL A C     1 
ATOM   9679  O  O     . VAL A 1 2687 ? 226.920 191.594 180.204 1.00 6.75  ? 2687 VAL A O     1 
ATOM   9680  C  CB    . VAL A 1 2687 ? 227.988 190.785 183.329 1.00 2.02  ? 2687 VAL A CB    1 
ATOM   9681  C  CG1   . VAL A 1 2687 ? 228.929 190.119 182.346 1.00 1.68  ? 2687 VAL A CG1   1 
ATOM   9682  C  CG2   . VAL A 1 2687 ? 228.768 191.508 184.418 1.00 0.26  ? 2687 VAL A CG2   1 
ATOM   9683  N  N     . GLU A 1 2688 ? 225.585 190.239 181.423 1.00 0.88  ? 2688 GLU A N     1 
ATOM   9684  C  CA    . GLU A 1 2688 ? 225.050 189.492 180.289 1.00 0.94  ? 2688 GLU A CA    1 
ATOM   9685  C  C     . GLU A 1 2688 ? 224.030 190.303 179.490 1.00 1.00  ? 2688 GLU A C     1 
ATOM   9686  O  O     . GLU A 1 2688 ? 224.024 190.243 178.256 1.00 1.51  ? 2688 GLU A O     1 
ATOM   9687  C  CB    . GLU A 1 2688 ? 224.479 188.160 180.800 1.00 0.97  ? 2688 GLU A CB    1 
ATOM   9688  C  CG    . GLU A 1 2688 ? 224.092 187.134 179.728 1.00 2.66  ? 2688 GLU A CG    1 
ATOM   9689  C  CD    . GLU A 1 2688 ? 222.739 187.355 179.187 1.00 7.23  ? 2688 GLU A CD    1 
ATOM   9690  O  OE1   . GLU A 1 2688 ? 221.930 187.885 179.966 1.00 15.47 ? 2688 GLU A OE1   1 
ATOM   9691  O  OE2   . GLU A 1 2688 ? 222.477 187.000 178.016 1.00 10.50 ? 2688 GLU A OE2   1 
ATOM   9692  N  N     . HIS A 1 2689 ? 223.160 191.061 180.166 1.00 0.40  ? 2689 HIS A N     1 
ATOM   9693  C  CA    . HIS A 1 2689 ? 222.221 191.975 179.516 1.00 0.33  ? 2689 HIS A CA    1 
ATOM   9694  C  C     . HIS A 1 2689 ? 222.731 193.410 179.405 1.00 0.32  ? 2689 HIS A C     1 
ATOM   9695  O  O     . HIS A 1 2689 ? 222.077 194.232 178.755 1.00 0.40  ? 2689 HIS A O     1 
ATOM   9696  C  CB    . HIS A 1 2689 ? 220.871 191.988 180.254 1.00 0.43  ? 2689 HIS A CB    1 
ATOM   9697  C  CG    . HIS A 1 2689 ? 220.156 190.673 180.237 1.00 0.42  ? 2689 HIS A CG    1 
ATOM   9698  N  ND1   . HIS A 1 2689 ? 220.140 189.857 179.128 1.00 0.47  ? 2689 HIS A ND1   1 
ATOM   9699  C  CD2   . HIS A 1 2689 ? 219.469 190.014 181.197 1.00 1.31  ? 2689 HIS A CD2   1 
ATOM   9700  C  CE1   . HIS A 1 2689 ? 219.449 188.767 179.394 1.00 0.85  ? 2689 HIS A CE1   1 
ATOM   9701  N  NE2   . HIS A 1 2689 ? 219.043 188.831 180.648 1.00 2.15  ? 2689 HIS A NE2   1 
ATOM   9702  N  N     . GLY A 1 2690 ? 223.873 193.738 180.001 1.00 0.44  ? 2690 GLY A N     1 
ATOM   9703  C  CA    . GLY A 1 2690 ? 224.381 195.092 179.866 1.00 0.23  ? 2690 GLY A CA    1 
ATOM   9704  C  C     . GLY A 1 2690 ? 223.585 196.162 180.580 1.00 0.12  ? 2690 GLY A C     1 
ATOM   9705  O  O     . GLY A 1 2690 ? 223.682 197.337 180.216 1.00 0.16  ? 2690 GLY A O     1 
ATOM   9706  N  N     . GLY A 1 2691 ? 222.811 195.800 181.595 1.00 0.22  ? 2691 GLY A N     1 
ATOM   9707  C  CA    . GLY A 1 2691 ? 222.031 196.793 182.304 1.00 0.15  ? 2691 GLY A CA    1 
ATOM   9708  C  C     . GLY A 1 2691 ? 221.169 196.174 183.378 1.00 0.06  ? 2691 GLY A C     1 
ATOM   9709  O  O     . GLY A 1 2691 ? 221.384 195.033 183.791 1.00 0.10  ? 2691 GLY A O     1 
ATOM   9710  N  N     . PHE A 1 2692 ? 220.188 196.949 183.832 1.00 0.04  ? 2692 PHE A N     1 
ATOM   9711  C  CA    . PHE A 1 2692 ? 219.269 196.530 184.878 1.00 0.04  ? 2692 PHE A CA    1 
ATOM   9712  C  C     . PHE A 1 2692 ? 218.007 197.371 184.763 1.00 0.03  ? 2692 PHE A C     1 
ATOM   9713  O  O     . PHE A 1 2692 ? 217.915 198.276 183.929 1.00 0.04  ? 2692 PHE A O     1 
ATOM   9714  C  CB    . PHE A 1 2692 ? 219.905 196.664 186.264 1.00 0.06  ? 2692 PHE A CB    1 
ATOM   9715  C  CG    . PHE A 1 2692 ? 220.208 198.079 186.653 1.00 0.06  ? 2692 PHE A CG    1 
ATOM   9716  C  CD1   . PHE A 1 2692 ? 221.372 198.696 186.230 1.00 0.08  ? 2692 PHE A CD1   1 
ATOM   9717  C  CD2   . PHE A 1 2692 ? 219.326 198.793 187.444 1.00 0.06  ? 2692 PHE A CD2   1 
ATOM   9718  C  CE1   . PHE A 1 2692 ? 221.651 199.997 186.591 1.00 0.15  ? 2692 PHE A CE1   1 
ATOM   9719  C  CE2   . PHE A 1 2692 ? 219.597 200.093 187.805 1.00 0.13  ? 2692 PHE A CE2   1 
ATOM   9720  C  CZ    . PHE A 1 2692 ? 220.761 200.695 187.379 1.00 0.09  ? 2692 PHE A CZ    1 
ATOM   9721  N  N     . TYR A 1 2693 ? 217.034 197.071 185.614 1.00 0.05  ? 2693 TYR A N     1 
ATOM   9722  C  CA    . TYR A 1 2693 ? 215.781 197.810 185.664 1.00 0.09  ? 2693 TYR A CA    1 
ATOM   9723  C  C     . TYR A 1 2693 ? 215.799 198.789 186.830 1.00 0.27  ? 2693 TYR A C     1 
ATOM   9724  O  O     . TYR A 1 2693 ? 216.120 198.412 187.960 1.00 0.25  ? 2693 TYR A O     1 
ATOM   9725  C  CB    . TYR A 1 2693 ? 214.585 196.869 185.798 1.00 0.04  ? 2693 TYR A CB    1 
ATOM   9726  C  CG    . TYR A 1 2693 ? 214.125 196.263 184.496 1.00 0.03  ? 2693 TYR A CG    1 
ATOM   9727  C  CD1   . TYR A 1 2693 ? 213.360 196.996 183.599 1.00 0.03  ? 2693 TYR A CD1   1 
ATOM   9728  C  CD2   . TYR A 1 2693 ? 214.446 194.956 184.167 1.00 0.03  ? 2693 TYR A CD2   1 
ATOM   9729  C  CE1   . TYR A 1 2693 ? 212.936 196.445 182.409 1.00 0.07  ? 2693 TYR A CE1   1 
ATOM   9730  C  CE2   . TYR A 1 2693 ? 214.026 194.395 182.980 1.00 0.04  ? 2693 TYR A CE2   1 
ATOM   9731  C  CZ    . TYR A 1 2693 ? 213.272 195.142 182.105 1.00 0.07  ? 2693 TYR A CZ    1 
ATOM   9732  O  OH    . TYR A 1 2693 ? 212.855 194.579 180.922 1.00 0.05  ? 2693 TYR A OH    1 
ATOM   9733  N  N     . ARG A 1 2694 ? 215.449 200.040 186.549 1.00 0.92  ? 2694 ARG A N     1 
ATOM   9734  C  CA    . ARG A 1 2694 ? 215.254 201.045 187.587 1.00 0.88  ? 2694 ARG A CA    1 
ATOM   9735  C  C     . ARG A 1 2694 ? 213.863 200.848 188.174 1.00 1.35  ? 2694 ARG A C     1 
ATOM   9736  O  O     . ARG A 1 2694 ? 212.857 201.056 187.488 1.00 1.85  ? 2694 ARG A O     1 
ATOM   9737  C  CB    . ARG A 1 2694 ? 215.426 202.447 187.008 1.00 1.10  ? 2694 ARG A CB    1 
ATOM   9738  C  CG    . ARG A 1 2694 ? 215.594 203.542 188.050 1.00 2.23  ? 2694 ARG A CG    1 
ATOM   9739  C  CD    . ARG A 1 2694 ? 215.063 204.879 187.550 1.00 2.14  ? 2694 ARG A CD    1 
ATOM   9740  N  NE    . ARG A 1 2694 ? 216.045 205.640 186.790 1.00 2.52  ? 2694 ARG A NE    1 
ATOM   9741  C  CZ    . ARG A 1 2694 ? 215.779 206.299 185.670 1.00 3.14  ? 2694 ARG A CZ    1 
ATOM   9742  N  NH1   . ARG A 1 2694 ? 214.576 206.275 185.122 1.00 1.74  ? 2694 ARG A NH1   1 
ATOM   9743  N  NH2   . ARG A 1 2694 ? 216.745 207.000 185.086 1.00 4.65  ? 2694 ARG A NH2   1 
ATOM   9744  N  N     . THR A 1 2695 ? 213.798 200.439 189.443 1.00 1.62  ? 2695 THR A N     1 
ATOM   9745  C  CA    . THR A 1 2695 ? 212.528 200.024 190.029 1.00 1.62  ? 2695 THR A CA    1 
ATOM   9746  C  C     . THR A 1 2695 ? 211.581 201.186 190.291 1.00 2.58  ? 2695 THR A C     1 
ATOM   9747  O  O     . THR A 1 2695 ? 210.379 200.957 190.462 1.00 4.22  ? 2695 THR A O     1 
ATOM   9748  C  CB    . THR A 1 2695 ? 212.768 199.252 191.330 1.00 2.11  ? 2695 THR A CB    1 
ATOM   9749  O  OG1   . THR A 1 2695 ? 213.470 200.080 192.265 1.00 10.31 ? 2695 THR A OG1   1 
ATOM   9750  C  CG2   . THR A 1 2695 ? 213.581 197.998 191.060 1.00 1.83  ? 2695 THR A CG2   1 
ATOM   9751  N  N     . SER A 1 2696 ? 212.085 202.420 190.336 1.00 3.44  ? 2696 SER A N     1 
ATOM   9752  C  CA    . SER A 1 2696 ? 211.210 203.559 190.601 1.00 3.29  ? 2696 SER A CA    1 
ATOM   9753  C  C     . SER A 1 2696 ? 210.224 203.788 189.460 1.00 3.61  ? 2696 SER A C     1 
ATOM   9754  O  O     . SER A 1 2696 ? 209.053 204.097 189.701 1.00 9.24  ? 2696 SER A O     1 
ATOM   9755  C  CB    . SER A 1 2696 ? 212.042 204.817 190.853 1.00 7.25  ? 2696 SER A CB    1 
ATOM   9756  O  OG    . SER A 1 2696 ? 212.669 205.263 189.666 1.00 9.77  ? 2696 SER A OG    1 
ATOM   9757  N  N     . ASP A 1 2697 ? 210.677 203.648 188.215 1.00 2.21  ? 2697 ASP A N     1 
ATOM   9758  C  CA    . ASP A 1 2697 ? 209.825 203.882 187.055 1.00 2.10  ? 2697 ASP A CA    1 
ATOM   9759  C  C     . ASP A 1 2697 ? 209.710 202.665 186.146 1.00 1.97  ? 2697 ASP A C     1 
ATOM   9760  O  O     . ASP A 1 2697 ? 209.137 202.776 185.057 1.00 2.94  ? 2697 ASP A O     1 
ATOM   9761  C  CB    . ASP A 1 2697 ? 210.334 205.084 186.252 1.00 4.10  ? 2697 ASP A CB    1 
ATOM   9762  C  CG    . ASP A 1 2697 ? 211.754 204.901 185.762 1.00 6.25  ? 2697 ASP A CG    1 
ATOM   9763  O  OD1   . ASP A 1 2697 ? 212.395 203.900 186.142 1.00 4.07  ? 2697 ASP A OD1   1 
ATOM   9764  O  OD2   . ASP A 1 2697 ? 212.232 205.757 184.990 1.00 12.75 ? 2697 ASP A OD2   1 
ATOM   9765  N  N     . GLN A 1 2698 ? 210.244 201.514 186.561 1.00 2.02  ? 2698 GLN A N     1 
ATOM   9766  C  CA    . GLN A 1 2698 ? 210.153 200.273 185.786 1.00 1.39  ? 2698 GLN A CA    1 
ATOM   9767  C  C     . GLN A 1 2698 ? 210.777 200.432 184.402 1.00 1.43  ? 2698 GLN A C     1 
ATOM   9768  O  O     . GLN A 1 2698 ? 210.250 199.939 183.403 1.00 5.75  ? 2698 GLN A O     1 
ATOM   9769  C  CB    . GLN A 1 2698 ? 208.702 199.803 185.674 1.00 1.20  ? 2698 GLN A CB    1 
ATOM   9770  C  CG    . GLN A 1 2698 ? 208.270 198.824 186.738 1.00 0.33  ? 2698 GLN A CG    1 
ATOM   9771  C  CD    . GLN A 1 2698 ? 208.417 199.369 188.138 1.00 0.74  ? 2698 GLN A CD    1 
ATOM   9772  O  OE1   . GLN A 1 2698 ? 207.847 200.405 188.477 1.00 2.24  ? 2698 GLN A OE1   1 
ATOM   9773  N  NE2   . GLN A 1 2698 ? 209.180 198.669 188.966 1.00 2.37  ? 2698 GLN A NE2   1 
ATOM   9774  N  N     . THR A 1 2699 ? 211.908 201.123 184.342 1.00 1.85  ? 2699 THR A N     1 
ATOM   9775  C  CA    . THR A 1 2699 ? 212.554 201.474 183.084 1.00 0.98  ? 2699 THR A CA    1 
ATOM   9776  C  C     . THR A 1 2699 ? 213.896 200.767 182.987 1.00 0.32  ? 2699 THR A C     1 
ATOM   9777  O  O     . THR A 1 2699 ? 214.658 200.736 183.959 1.00 0.19  ? 2699 THR A O     1 
ATOM   9778  C  CB    . THR A 1 2699 ? 212.741 202.992 182.971 1.00 2.16  ? 2699 THR A CB    1 
ATOM   9779  O  OG1   . THR A 1 2699 ? 211.463 203.619 182.808 1.00 6.33  ? 2699 THR A OG1   1 
ATOM   9780  C  CG2   . THR A 1 2699 ? 213.625 203.347 181.787 1.00 1.71  ? 2699 THR A CG2   1 
ATOM   9781  N  N     . TRP A 1 2700 ? 214.176 200.194 181.821 1.00 0.18  ? 2700 TRP A N     1 
ATOM   9782  C  CA    . TRP A 1 2700 ? 215.466 199.561 181.591 1.00 0.11  ? 2700 TRP A CA    1 
ATOM   9783  C  C     . TRP A 1 2700 ? 216.564 200.612 181.507 1.00 0.13  ? 2700 TRP A C     1 
ATOM   9784  O  O     . TRP A 1 2700 ? 216.424 201.623 180.812 1.00 0.33  ? 2700 TRP A O     1 
ATOM   9785  C  CB    . TRP A 1 2700 ? 215.433 198.724 180.315 1.00 0.07  ? 2700 TRP A CB    1 
ATOM   9786  C  CG    . TRP A 1 2700 ? 216.750 198.097 179.990 1.00 0.06  ? 2700 TRP A CG    1 
ATOM   9787  C  CD1   . TRP A 1 2700 ? 217.651 198.520 179.060 1.00 0.04  ? 2700 TRP A CD1   1 
ATOM   9788  C  CD2   . TRP A 1 2700 ? 217.323 196.938 180.605 1.00 0.04  ? 2700 TRP A CD2   1 
ATOM   9789  N  NE1   . TRP A 1 2700 ? 218.745 197.694 179.052 1.00 0.04  ? 2700 TRP A NE1   1 
ATOM   9790  C  CE2   . TRP A 1 2700 ? 218.568 196.714 179.991 1.00 0.04  ? 2700 TRP A CE2   1 
ATOM   9791  C  CE3   . TRP A 1 2700 ? 216.901 196.066 181.612 1.00 0.02  ? 2700 TRP A CE3   1 
ATOM   9792  C  CZ2   . TRP A 1 2700 ? 219.396 195.652 180.349 1.00 0.08  ? 2700 TRP A CZ2   1 
ATOM   9793  C  CZ3   . TRP A 1 2700 ? 217.722 195.017 181.964 1.00 0.02  ? 2700 TRP A CZ3   1 
ATOM   9794  C  CH2   . TRP A 1 2700 ? 218.955 194.819 181.336 1.00 0.06  ? 2700 TRP A CH2   1 
ATOM   9795  N  N     . VAL A 1 2701 ? 217.662 200.369 182.215 1.00 0.08  ? 2701 VAL A N     1 
ATOM   9796  C  CA    . VAL A 1 2701 ? 218.820 201.251 182.223 1.00 0.21  ? 2701 VAL A CA    1 
ATOM   9797  C  C     . VAL A 1 2701 ? 219.985 200.493 181.606 1.00 0.07  ? 2701 VAL A C     1 
ATOM   9798  O  O     . VAL A 1 2701 ? 220.262 199.354 181.994 1.00 0.08  ? 2701 VAL A O     1 
ATOM   9799  C  CB    . VAL A 1 2701 ? 219.169 201.723 183.647 1.00 0.16  ? 2701 VAL A CB    1 
ATOM   9800  C  CG1   . VAL A 1 2701 ? 220.465 202.515 183.641 1.00 0.13  ? 2701 VAL A CG1   1 
ATOM   9801  C  CG2   . VAL A 1 2701 ? 218.035 202.552 184.225 1.00 0.28  ? 2701 VAL A CG2   1 
ATOM   9802  N  N     . LYS A 1 2702 ? 220.652 201.115 180.644 1.00 0.18  ? 2702 LYS A N     1 
ATOM   9803  C  CA    . LYS A 1 2702 ? 221.801 200.521 179.981 1.00 0.21  ? 2702 LYS A CA    1 
ATOM   9804  C  C     . LYS A 1 2702 ? 223.092 201.086 180.560 1.00 0.29  ? 2702 LYS A C     1 
ATOM   9805  O  O     . LYS A 1 2702 ? 223.237 202.300 180.714 1.00 0.21  ? 2702 LYS A O     1 
ATOM   9806  C  CB    . LYS A 1 2702 ? 221.755 200.771 178.474 1.00 0.36  ? 2702 LYS A CB    1 
ATOM   9807  C  CG    . LYS A 1 2702 ? 222.866 200.087 177.705 1.00 1.67  ? 2702 LYS A CG    1 
ATOM   9808  C  CD    . LYS A 1 2702 ? 222.720 200.303 176.210 1.00 3.22  ? 2702 LYS A CD    1 
ATOM   9809  C  CE    . LYS A 1 2702 ? 223.839 199.622 175.445 1.00 8.16  ? 2702 LYS A CE    1 
ATOM   9810  N  NZ    . LYS A 1 2702 ? 223.712 199.825 173.977 1.00 19.38 ? 2702 LYS A NZ    1 
ATOM   9811  N  N     . LEU A 1 2703 ? 224.023 200.194 180.878 1.00 0.63  ? 2703 LEU A N     1 
ATOM   9812  C  CA    . LEU A 1 2703 ? 225.320 200.599 181.395 1.00 0.28  ? 2703 LEU A CA    1 
ATOM   9813  C  C     . LEU A 1 2703 ? 226.246 201.022 180.264 1.00 0.23  ? 2703 LEU A C     1 
ATOM   9814  O  O     . LEU A 1 2703 ? 226.213 200.470 179.162 1.00 0.94  ? 2703 LEU A O     1 
ATOM   9815  C  CB    . LEU A 1 2703 ? 225.965 199.459 182.183 1.00 0.50  ? 2703 LEU A CB    1 
ATOM   9816  C  CG    . LEU A 1 2703 ? 225.301 199.011 183.483 1.00 0.47  ? 2703 LEU A CG    1 
ATOM   9817  C  CD1   . LEU A 1 2703 ? 226.095 197.876 184.099 1.00 1.86  ? 2703 LEU A CD1   1 
ATOM   9818  C  CD2   . LEU A 1 2703 ? 225.176 200.171 184.457 1.00 0.44  ? 2703 LEU A CD2   1 
ATOM   9819  N  N     . GLU A 1 2704 ? 227.077 202.020 180.549 1.00 0.20  ? 2704 GLU A N     1 
ATOM   9820  C  CA    . GLU A 1 2704 ? 228.109 202.459 179.621 1.00 0.34  ? 2704 GLU A CA    1 
ATOM   9821  C  C     . GLU A 1 2704 ? 229.364 202.787 180.413 1.00 0.39  ? 2704 GLU A C     1 
ATOM   9822  O  O     . GLU A 1 2704 ? 229.294 203.498 181.419 1.00 0.45  ? 2704 GLU A O     1 
ATOM   9823  C  CB    . GLU A 1 2704 ? 227.650 203.673 178.803 1.00 0.97  ? 2704 GLU A CB    1 
ATOM   9824  C  CG    . GLU A 1 2704 ? 228.778 204.427 178.118 1.00 4.59  ? 2704 GLU A CG    1 
ATOM   9825  C  CD    . GLU A 1 2704 ? 228.362 205.805 177.644 1.00 13.76 ? 2704 GLU A CD    1 
ATOM   9826  O  OE1   . GLU A 1 2704 ? 227.454 205.893 176.792 1.00 18.01 ? 2704 GLU A OE1   1 
ATOM   9827  O  OE2   . GLU A 1 2704 ? 228.943 206.802 178.120 1.00 13.85 ? 2704 GLU A OE2   1 
ATOM   9828  N  N     . ARG A 1 2705 ? 230.503 202.258 179.958 1.00 0.36  ? 2705 ARG A N     1 
ATOM   9829  C  CA    . ARG A 1 2705 ? 231.805 202.492 180.588 1.00 0.22  ? 2705 ARG A CA    1 
ATOM   9830  C  C     . ARG A 1 2705 ? 231.812 202.084 182.060 1.00 0.25  ? 2705 ARG A C     1 
ATOM   9831  O  O     . ARG A 1 2705 ? 232.382 202.768 182.910 1.00 0.51  ? 2705 ARG A O     1 
ATOM   9832  C  CB    . ARG A 1 2705 ? 232.249 203.947 180.427 1.00 0.39  ? 2705 ARG A CB    1 
ATOM   9833  C  CG    . ARG A 1 2705 ? 232.527 204.360 178.993 1.00 0.32  ? 2705 ARG A CG    1 
ATOM   9834  C  CD    . ARG A 1 2705 ? 232.906 205.829 178.894 1.00 1.74  ? 2705 ARG A CD    1 
ATOM   9835  N  NE    . ARG A 1 2705 ? 231.828 206.716 179.317 1.00 1.50  ? 2705 ARG A NE    1 
ATOM   9836  C  CZ    . ARG A 1 2705 ? 231.907 207.561 180.334 1.00 2.48  ? 2705 ARG A CZ    1 
ATOM   9837  N  NH1   . ARG A 1 2705 ? 232.997 207.645 181.081 1.00 2.77  ? 2705 ARG A NH1   1 
ATOM   9838  N  NH2   . ARG A 1 2705 ? 230.866 208.338 180.615 1.00 3.85  ? 2705 ARG A NH2   1 
ATOM   9839  N  N     . ILE A 1 2706 ? 231.178 200.955 182.364 1.00 0.18  ? 2706 ILE A N     1 
ATOM   9840  C  CA    . ILE A 1 2706 ? 231.158 200.398 183.712 1.00 0.17  ? 2706 ILE A CA    1 
ATOM   9841  C  C     . ILE A 1 2706 ? 231.517 198.921 183.625 1.00 0.15  ? 2706 ILE A C     1 
ATOM   9842  O  O     . ILE A 1 2706 ? 230.838 198.156 182.931 1.00 0.60  ? 2706 ILE A O     1 
ATOM   9843  C  CB    . ILE A 1 2706 ? 229.792 200.592 184.394 1.00 0.31  ? 2706 ILE A CB    1 
ATOM   9844  C  CG1   . ILE A 1 2706 ? 229.518 202.080 184.629 1.00 0.28  ? 2706 ILE A CG1   1 
ATOM   9845  C  CG2   . ILE A 1 2706 ? 229.719 199.803 185.686 1.00 0.19  ? 2706 ILE A CG2   1 
ATOM   9846  C  CD1   . ILE A 1 2706 ? 228.103 202.389 185.050 1.00 0.43  ? 2706 ILE A CD1   1 
ATOM   9847  N  N     . GLN A 1 2707 ? 232.579 198.523 184.318 1.00 0.26  ? 2707 GLN A N     1 
ATOM   9848  C  CA    . GLN A 1 2707 ? 232.998 197.132 184.387 1.00 0.13  ? 2707 GLN A CA    1 
ATOM   9849  C  C     . GLN A 1 2707 ? 233.113 196.702 185.843 1.00 0.19  ? 2707 GLN A C     1 
ATOM   9850  O  O     . GLN A 1 2707 ? 233.179 197.528 186.756 1.00 0.33  ? 2707 GLN A O     1 
ATOM   9851  C  CB    . GLN A 1 2707 ? 234.333 196.898 183.667 1.00 0.19  ? 2707 GLN A CB    1 
ATOM   9852  C  CG    . GLN A 1 2707 ? 235.436 197.871 184.032 1.00 0.26  ? 2707 GLN A CG    1 
ATOM   9853  C  CD    . GLN A 1 2707 ? 236.649 197.728 183.137 1.00 0.74  ? 2707 GLN A CD    1 
ATOM   9854  O  OE1   . GLN A 1 2707 ? 237.008 198.651 182.409 1.00 6.84  ? 2707 GLN A OE1   1 
ATOM   9855  N  NE2   . GLN A 1 2707 ? 237.287 196.568 183.185 1.00 0.41  ? 2707 GLN A NE2   1 
ATOM   9856  N  N     . PHE A 1 2708 ? 233.142 195.388 186.050 1.00 0.49  ? 2708 PHE A N     1 
ATOM   9857  C  CA    . PHE A 1 2708 ? 233.114 194.801 187.381 1.00 0.10  ? 2708 PHE A CA    1 
ATOM   9858  C  C     . PHE A 1 2708 ? 234.328 193.907 187.594 1.00 0.09  ? 2708 PHE A C     1 
ATOM   9859  O  O     . PHE A 1 2708 ? 234.717 193.146 186.705 1.00 0.14  ? 2708 PHE A O     1 
ATOM   9860  C  CB    . PHE A 1 2708 ? 231.829 193.995 187.593 1.00 0.12  ? 2708 PHE A CB    1 
ATOM   9861  C  CG    . PHE A 1 2708 ? 230.577 194.782 187.344 1.00 0.50  ? 2708 PHE A CG    1 
ATOM   9862  C  CD1   . PHE A 1 2708 ? 230.017 194.836 186.079 1.00 0.50  ? 2708 PHE A CD1   1 
ATOM   9863  C  CD2   . PHE A 1 2708 ? 229.965 195.476 188.372 1.00 0.93  ? 2708 PHE A CD2   1 
ATOM   9864  C  CE1   . PHE A 1 2708 ? 228.870 195.564 185.844 1.00 0.50  ? 2708 PHE A CE1   1 
ATOM   9865  C  CE2   . PHE A 1 2708 ? 228.814 196.204 188.142 1.00 1.02  ? 2708 PHE A CE2   1 
ATOM   9866  C  CZ    . PHE A 1 2708 ? 228.269 196.247 186.878 1.00 0.48  ? 2708 PHE A CZ    1 
ATOM   9867  N  N     . VAL A 1 2709 ? 234.925 194.016 188.775 1.00 0.16  ? 2709 VAL A N     1 
ATOM   9868  C  CA    . VAL A 1 2709 ? 235.983 193.119 189.220 1.00 0.03  ? 2709 VAL A CA    1 
ATOM   9869  C  C     . VAL A 1 2709 ? 235.589 192.581 190.585 1.00 0.08  ? 2709 VAL A C     1 
ATOM   9870  O  O     . VAL A 1 2709 ? 235.195 193.347 191.470 1.00 0.21  ? 2709 VAL A O     1 
ATOM   9871  C  CB    . VAL A 1 2709 ? 237.353 193.822 189.286 1.00 0.07  ? 2709 VAL A CB    1 
ATOM   9872  C  CG1   . VAL A 1 2709 ? 238.374 192.934 189.976 1.00 0.06  ? 2709 VAL A CG1   1 
ATOM   9873  C  CG2   . VAL A 1 2709 ? 237.830 194.185 187.894 1.00 0.08  ? 2709 VAL A CG2   1 
ATOM   9874  N  N     . GLY A 1 2710 ? 235.685 191.268 190.753 1.00 0.11  ? 2710 GLY A N     1 
ATOM   9875  C  CA    . GLY A 1 2710 ? 235.361 190.618 192.007 1.00 0.06  ? 2710 GLY A CA    1 
ATOM   9876  C  C     . GLY A 1 2710 ? 236.601 190.076 192.688 1.00 0.05  ? 2710 GLY A C     1 
ATOM   9877  O  O     . GLY A 1 2710 ? 237.561 189.672 192.031 1.00 0.04  ? 2710 GLY A O     1 
ATOM   9878  N  N     . ALA A 1 2711 ? 236.585 190.098 194.013 1.00 0.27  ? 2711 ALA A N     1 
ATOM   9879  C  CA    . ALA A 1 2711 ? 237.561 189.391 194.825 1.00 0.16  ? 2711 ALA A CA    1 
ATOM   9880  C  C     . ALA A 1 2711 ? 236.802 188.560 195.844 1.00 0.20  ? 2711 ALA A C     1 
ATOM   9881  O  O     . ALA A 1 2711 ? 235.692 188.913 196.244 1.00 0.38  ? 2711 ALA A O     1 
ATOM   9882  C  CB    . ALA A 1 2711 ? 238.533 190.343 195.529 1.00 0.14  ? 2711 ALA A CB    1 
ATOM   9883  N  N     . CYS A 1 2712 ? 237.394 187.443 196.243 1.00 0.27  ? 2712 CYS A N     1 
ATOM   9884  C  CA    . CYS A 1 2712 ? 236.709 186.539 197.153 1.00 0.38  ? 2712 CYS A CA    1 
ATOM   9885  C  C     . CYS A 1 2712 ? 237.704 185.518 197.681 1.00 0.34  ? 2712 CYS A C     1 
ATOM   9886  O  O     . CYS A 1 2712 ? 238.792 185.332 197.132 1.00 0.23  ? 2712 CYS A O     1 
ATOM   9887  C  CB    . CYS A 1 2712 ? 235.537 185.834 196.466 1.00 0.23  ? 2712 CYS A CB    1 
ATOM   9888  S  SG    . CYS A 1 2712 ? 236.010 184.800 195.079 1.00 0.58  ? 2712 CYS A SG    1 
ATOM   9889  N  N     . ASN A 1 2713 ? 237.315 184.875 198.750 1.00 0.90  ? 2713 ASN A N     1 
ATOM   9890  C  CA    . ASN A 1 2713 ? 237.975 183.701 199.284 1.00 0.79  ? 2713 ASN A CA    1 
ATOM   9891  C  C     . ASN A 1 2713 ? 237.387 182.452 198.644 1.00 1.10  ? 2713 ASN A C     1 
ATOM   9892  O  O     . ASN A 1 2713 ? 236.292 182.497 198.076 1.00 1.54  ? 2713 ASN A O     1 
ATOM   9893  C  CB    . ASN A 1 2713 ? 237.818 183.667 200.801 1.00 2.55  ? 2713 ASN A CB    1 
ATOM   9894  C  CG    . ASN A 1 2713 ? 238.589 184.779 201.490 1.00 0.71  ? 2713 ASN A CG    1 
ATOM   9895  O  OD1   . ASN A 1 2713 ? 238.361 185.072 202.662 1.00 1.59  ? 2713 ASN A OD1   1 
ATOM   9896  N  ND2   . ASN A 1 2713 ? 239.509 185.400 200.763 1.00 0.11  ? 2713 ASN A ND2   1 
ATOM   9897  N  N     . PRO A 1 2714 ? 238.096 181.326 198.690 1.00 2.29  ? 2714 PRO A N     1 
ATOM   9898  C  CA    . PRO A 1 2714 ? 237.577 180.094 198.083 1.00 1.34  ? 2714 PRO A CA    1 
ATOM   9899  C  C     . PRO A 1 2714 ? 236.221 179.723 198.656 1.00 1.16  ? 2714 PRO A C     1 
ATOM   9900  O  O     . PRO A 1 2714 ? 235.972 179.908 199.857 1.00 4.89  ? 2714 PRO A O     1 
ATOM   9901  C  CB    . PRO A 1 2714 ? 238.642 179.053 198.447 1.00 2.68  ? 2714 PRO A CB    1 
ATOM   9902  C  CG    . PRO A 1 2714 ? 239.895 179.846 198.519 1.00 2.18  ? 2714 PRO A CG    1 
ATOM   9903  C  CD    . PRO A 1 2714 ? 239.506 181.180 199.096 1.00 1.31  ? 2714 PRO A CD    1 
ATOM   9904  N  N     . PRO A 1 2715 ? 235.315 179.205 197.823 1.00 1.83  ? 2715 PRO A N     1 
ATOM   9905  C  CA    . PRO A 1 2715 ? 233.949 178.930 198.298 1.00 1.46  ? 2715 PRO A CA    1 
ATOM   9906  C  C     . PRO A 1 2715 ? 233.882 177.898 199.407 1.00 2.29  ? 2715 PRO A C     1 
ATOM   9907  O  O     . PRO A 1 2715 ? 232.868 177.838 200.114 1.00 3.69  ? 2715 PRO A O     1 
ATOM   9908  C  CB    . PRO A 1 2715 ? 233.228 178.445 197.032 1.00 1.25  ? 2715 PRO A CB    1 
ATOM   9909  C  CG    . PRO A 1 2715 ? 234.319 177.976 196.130 1.00 0.78  ? 2715 PRO A CG    1 
ATOM   9910  C  CD    . PRO A 1 2715 ? 235.479 178.878 196.397 1.00 1.46  ? 2715 PRO A CD    1 
ATOM   9911  N  N     . THR A 1 2716 ? 234.921 177.083 199.580 1.00 2.84  ? 2716 THR A N     1 
ATOM   9912  C  CA    . THR A 1 2716 ? 234.953 176.115 200.668 1.00 4.62  ? 2716 THR A CA    1 
ATOM   9913  C  C     . THR A 1 2716 ? 235.182 176.757 202.030 1.00 5.42  ? 2716 THR A C     1 
ATOM   9914  O  O     . THR A 1 2716 ? 234.967 176.093 203.049 1.00 10.99 ? 2716 THR A O     1 
ATOM   9915  C  CB    . THR A 1 2716 ? 236.037 175.069 200.400 1.00 6.42  ? 2716 THR A CB    1 
ATOM   9916  O  OG1   . THR A 1 2716 ? 237.303 175.719 200.237 1.00 10.56 ? 2716 THR A OG1   1 
ATOM   9917  C  CG2   . THR A 1 2716 ? 235.712 174.284 199.139 1.00 4.74  ? 2716 THR A CG2   1 
ATOM   9918  N  N     . ASP A 1 2717 ? 235.606 178.017 202.076 1.00 3.42  ? 2717 ASP A N     1 
ATOM   9919  C  CA    . ASP A 1 2717 ? 235.830 178.686 203.347 1.00 4.45  ? 2717 ASP A CA    1 
ATOM   9920  C  C     . ASP A 1 2717 ? 234.501 178.979 204.043 1.00 4.55  ? 2717 ASP A C     1 
ATOM   9921  O  O     . ASP A 1 2717 ? 233.472 179.149 203.384 1.00 3.18  ? 2717 ASP A O     1 
ATOM   9922  C  CB    . ASP A 1 2717 ? 236.607 179.983 203.137 1.00 6.04  ? 2717 ASP A CB    1 
ATOM   9923  C  CG    . ASP A 1 2717 ? 237.985 179.746 202.557 1.00 9.87  ? 2717 ASP A CG    1 
ATOM   9924  O  OD1   . ASP A 1 2717 ? 238.331 178.574 202.303 1.00 7.12  ? 2717 ASP A OD1   1 
ATOM   9925  O  OD2   . ASP A 1 2717 ? 238.725 180.732 202.357 1.00 14.86 ? 2717 ASP A OD2   1 
ATOM   9926  N  N     . PRO A 1 2718 ? 234.493 179.028 205.375 1.00 6.32  ? 2718 PRO A N     1 
ATOM   9927  C  CA    . PRO A 1 2718 ? 233.238 179.276 206.100 1.00 4.62  ? 2718 PRO A CA    1 
ATOM   9928  C  C     . PRO A 1 2718 ? 232.642 180.633 205.753 1.00 2.61  ? 2718 PRO A C     1 
ATOM   9929  O  O     . PRO A 1 2718 ? 233.352 181.632 205.622 1.00 4.55  ? 2718 PRO A O     1 
ATOM   9930  C  CB    . PRO A 1 2718 ? 233.659 179.193 207.571 1.00 4.03  ? 2718 PRO A CB    1 
ATOM   9931  C  CG    . PRO A 1 2718 ? 235.121 179.485 207.559 1.00 4.15  ? 2718 PRO A CG    1 
ATOM   9932  C  CD    . PRO A 1 2718 ? 235.627 178.857 206.300 1.00 3.84  ? 2718 PRO A CD    1 
ATOM   9933  N  N     . GLY A 1 2719 ? 231.317 180.658 205.609 1.00 1.70  ? 2719 GLY A N     1 
ATOM   9934  C  CA    . GLY A 1 2719 ? 230.602 181.846 205.204 1.00 0.78  ? 2719 GLY A CA    1 
ATOM   9935  C  C     . GLY A 1 2719 ? 230.582 182.100 203.712 1.00 1.22  ? 2719 GLY A C     1 
ATOM   9936  O  O     . GLY A 1 2719 ? 229.838 182.977 203.259 1.00 1.40  ? 2719 GLY A O     1 
ATOM   9937  N  N     . ARG A 1 2720 ? 231.364 181.357 202.936 1.00 1.09  ? 2720 ARG A N     1 
ATOM   9938  C  CA    . ARG A 1 2720 ? 231.466 181.566 201.500 1.00 0.94  ? 2720 ARG A CA    1 
ATOM   9939  C  C     . ARG A 1 2720 ? 230.556 180.595 200.762 1.00 1.00  ? 2720 ARG A C     1 
ATOM   9940  O  O     . ARG A 1 2720 ? 230.485 179.410 201.099 1.00 3.84  ? 2720 ARG A O     1 
ATOM   9941  C  CB    . ARG A 1 2720 ? 232.910 181.396 201.023 1.00 1.49  ? 2720 ARG A CB    1 
ATOM   9942  C  CG    . ARG A 1 2720 ? 233.821 182.611 201.201 1.00 0.94  ? 2720 ARG A CG    1 
ATOM   9943  C  CD    . ARG A 1 2720 ? 233.904 183.101 202.630 1.00 2.05  ? 2720 ARG A CD    1 
ATOM   9944  N  NE    . ARG A 1 2720 ? 234.731 184.296 202.746 1.00 5.07  ? 2720 ARG A NE    1 
ATOM   9945  C  CZ    . ARG A 1 2720 ? 234.922 184.967 203.873 1.00 3.75  ? 2720 ARG A CZ    1 
ATOM   9946  N  NH1   . ARG A 1 2720 ? 234.347 184.596 205.003 1.00 4.01  ? 2720 ARG A NH1   1 
ATOM   9947  N  NH2   . ARG A 1 2720 ? 235.702 186.044 203.862 1.00 3.07  ? 2720 ARG A NH2   1 
ATOM   9948  N  N     . LYS A 1 2721 ? 229.854 181.104 199.765 1.00 1.23  ? 2721 LYS A N     1 
ATOM   9949  C  CA    . LYS A 1 2721 ? 228.982 180.280 198.948 1.00 1.74  ? 2721 LYS A CA    1 
ATOM   9950  C  C     . LYS A 1 2721 ? 229.538 180.149 197.535 1.00 0.76  ? 2721 LYS A C     1 
ATOM   9951  O  O     . LYS A 1 2721 ? 230.181 181.071 197.028 1.00 0.41  ? 2721 LYS A O     1 
ATOM   9952  C  CB    . LYS A 1 2721 ? 227.563 180.859 198.880 1.00 1.60  ? 2721 LYS A CB    1 
ATOM   9953  C  CG    . LYS A 1 2721 ? 226.667 180.488 200.052 1.00 2.69  ? 2721 LYS A CG    1 
ATOM   9954  C  CD    . LYS A 1 2721 ? 227.030 181.228 201.326 1.00 2.83  ? 2721 LYS A CD    1 
ATOM   9955  C  CE    . LYS A 1 2721 ? 226.703 182.704 201.230 1.00 1.32  ? 2721 LYS A CE    1 
ATOM   9956  N  NZ    . LYS A 1 2721 ? 226.997 183.411 202.505 1.00 1.09  ? 2721 LYS A NZ    1 
ATOM   9957  N  N     . PRO A 1 2722 ? 229.324 179.008 196.882 1.00 2.49  ? 2722 PRO A N     1 
ATOM   9958  C  CA    . PRO A 1 2722 ? 229.723 178.883 195.476 1.00 0.46  ? 2722 PRO A CA    1 
ATOM   9959  C  C     . PRO A 1 2722 ? 228.956 179.860 194.599 1.00 0.33  ? 2722 PRO A C     1 
ATOM   9960  O  O     . PRO A 1 2722 ? 227.762 180.096 194.792 1.00 0.44  ? 2722 PRO A O     1 
ATOM   9961  C  CB    . PRO A 1 2722 ? 229.382 177.429 195.135 1.00 0.31  ? 2722 PRO A CB    1 
ATOM   9962  C  CG    . PRO A 1 2722 ? 228.358 177.033 196.140 1.00 0.68  ? 2722 PRO A CG    1 
ATOM   9963  C  CD    . PRO A 1 2722 ? 228.711 177.770 197.392 1.00 1.18  ? 2722 PRO A CD    1 
ATOM   9964  N  N     . LEU A 1 2723 ? 229.658 180.430 193.627 1.00 0.35  ? 2723 LEU A N     1 
ATOM   9965  C  CA    . LEU A 1 2723 ? 229.027 181.345 192.693 1.00 0.18  ? 2723 LEU A CA    1 
ATOM   9966  C  C     . LEU A 1 2723 ? 228.181 180.576 191.686 1.00 0.24  ? 2723 LEU A C     1 
ATOM   9967  O  O     . LEU A 1 2723 ? 228.497 179.445 191.308 1.00 0.24  ? 2723 LEU A O     1 
ATOM   9968  C  CB    . LEU A 1 2723 ? 230.085 182.182 191.975 1.00 0.15  ? 2723 LEU A CB    1 
ATOM   9969  C  CG    . LEU A 1 2723 ? 230.729 183.285 192.821 1.00 0.14  ? 2723 LEU A CG    1 
ATOM   9970  C  CD1   . LEU A 1 2723 ? 231.812 184.012 192.042 1.00 0.08  ? 2723 LEU A CD1   1 
ATOM   9971  C  CD2   . LEU A 1 2723 ? 229.676 184.263 193.318 1.00 0.08  ? 2723 LEU A CD2   1 
ATOM   9972  N  N     . SER A 1 2724 ? 227.084 181.199 191.262 1.00 0.41  ? 2724 SER A N     1 
ATOM   9973  C  CA    . SER A 1 2724 ? 226.201 180.587 190.279 1.00 0.40  ? 2724 SER A CA    1 
ATOM   9974  C  C     . SER A 1 2724 ? 226.942 180.341 188.970 1.00 0.35  ? 2724 SER A C     1 
ATOM   9975  O  O     . SER A 1 2724 ? 227.712 181.186 188.504 1.00 0.31  ? 2724 SER A O     1 
ATOM   9976  C  CB    . SER A 1 2724 ? 224.983 181.479 190.039 1.00 0.37  ? 2724 SER A CB    1 
ATOM   9977  O  OG    . SER A 1 2724 ? 224.190 180.998 188.971 1.00 3.17  ? 2724 SER A OG    1 
ATOM   9978  N  N     . HIS A 1 2725 ? 226.678 179.189 188.347 1.00 0.81  ? 2725 HIS A N     1 
ATOM   9979  C  CA    . HIS A 1 2725 ? 227.359 178.835 187.069 1.00 0.46  ? 2725 HIS A CA    1 
ATOM   9980  C  C     . HIS A 1 2725 ? 226.924 179.803 185.960 1.00 0.19  ? 2725 HIS A C     1 
ATOM   9981  O  O     . HIS A 1 2725 ? 227.695 180.003 185.001 1.00 0.12  ? 2725 HIS A O     1 
ATOM   9982  C  CB    . HIS A 1 2725 ? 227.103 177.365 186.716 1.00 1.83  ? 2725 HIS A CB    1 
ATOM   9983  C  CG    . HIS A 1 2725 ? 227.796 176.397 187.611 1.00 2.21  ? 2725 HIS A CG    1 
ATOM   9984  N  ND1   . HIS A 1 2725 ? 228.136 175.123 187.211 1.00 3.69  ? 2725 HIS A ND1   1 
ATOM   9985  C  CD2   . HIS A 1 2725 ? 228.200 176.505 188.882 1.00 3.13  ? 2725 HIS A CD2   1 
ATOM   9986  C  CE1   . HIS A 1 2725 ? 228.733 174.495 188.213 1.00 3.42  ? 2725 HIS A CE1   1 
ATOM   9987  N  NE2   . HIS A 1 2725 ? 228.784 175.319 189.237 1.00 3.89  ? 2725 HIS A NE2   1 
ATOM   9988  N  N     . ARG A 1 2726 ? 225.731 180.390 186.090 1.00 0.16  ? 2726 ARG A N     1 
ATOM   9989  C  CA    . ARG A 1 2726 ? 225.229 181.359 185.080 1.00 0.34  ? 2726 ARG A CA    1 
ATOM   9990  C  C     . ARG A 1 2726 ? 225.994 182.687 185.216 1.00 0.20  ? 2726 ARG A C     1 
ATOM   9991  O  O     . ARG A 1 2726 ? 226.016 183.456 184.236 1.00 0.59  ? 2726 ARG A O     1 
ATOM   9992  C  CB    . ARG A 1 2726 ? 223.714 181.537 185.214 1.00 0.54  ? 2726 ARG A CB    1 
ATOM   9993  C  CG    . ARG A 1 2726 ? 222.877 180.771 184.203 1.00 0.15  ? 2726 ARG A CG    1 
ATOM   9994  C  CD    . ARG A 1 2726 ? 221.404 181.079 184.400 1.00 0.25  ? 2726 ARG A CD    1 
ATOM   9995  N  NE    . ARG A 1 2726 ? 220.606 180.811 183.197 1.00 0.12  ? 2726 ARG A NE    1 
ATOM   9996  C  CZ    . ARG A 1 2726 ? 219.303 181.023 183.107 1.00 0.09  ? 2726 ARG A CZ    1 
ATOM   9997  N  NH1   . ARG A 1 2726 ? 218.628 181.439 184.163 1.00 0.82  ? 2726 ARG A NH1   1 
ATOM   9998  N  NH2   . ARG A 1 2726 ? 218.682 180.822 181.961 1.00 0.07  ? 2726 ARG A NH2   1 
ATOM   9999  N  N     . PHE A 1 2727 ? 226.595 182.940 186.379 1.00 0.13  ? 2727 PHE A N     1 
ATOM   10000 C  CA    . PHE A 1 2727 ? 227.412 184.167 186.575 1.00 0.09  ? 2727 PHE A CA    1 
ATOM   10001 C  C     . PHE A 1 2727 ? 228.859 183.875 186.198 1.00 0.12  ? 2727 PHE A C     1 
ATOM   10002 O  O     . PHE A 1 2727 ? 229.549 184.799 185.728 1.00 0.13  ? 2727 PHE A O     1 
ATOM   10003 C  CB    . PHE A 1 2727 ? 227.297 184.627 188.032 1.00 0.04  ? 2727 PHE A CB    1 
ATOM   10004 C  CG    . PHE A 1 2727 ? 228.313 185.670 188.478 1.00 0.07  ? 2727 PHE A CG    1 
ATOM   10005 C  CD1   . PHE A 1 2727 ? 229.538 185.287 189.012 1.00 0.04  ? 2727 PHE A CD1   1 
ATOM   10006 C  CD2   . PHE A 1 2727 ? 228.034 187.029 188.374 1.00 0.03  ? 2727 PHE A CD2   1 
ATOM   10007 C  CE1   . PHE A 1 2727 ? 230.460 186.238 189.420 1.00 0.04  ? 2727 PHE A CE1   1 
ATOM   10008 C  CE2   . PHE A 1 2727 ? 228.961 187.973 188.786 1.00 0.03  ? 2727 PHE A CE2   1 
ATOM   10009 C  CZ    . PHE A 1 2727 ? 230.169 187.576 189.308 1.00 0.02  ? 2727 PHE A CZ    1 
ATOM   10010 N  N     . LEU A 1 2728 ? 229.304 182.628 186.377 1.00 0.05  ? 2728 LEU A N     1 
ATOM   10011 C  CA    . LEU A 1 2728 ? 230.711 182.322 186.144 1.00 0.08  ? 2728 LEU A CA    1 
ATOM   10012 C  C     . LEU A 1 2728 ? 231.055 182.237 184.661 1.00 0.31  ? 2728 LEU A C     1 
ATOM   10013 O  O     . LEU A 1 2728 ? 232.221 182.413 184.298 1.00 0.43  ? 2728 LEU A O     1 
ATOM   10014 C  CB    . LEU A 1 2728 ? 231.088 181.019 186.851 1.00 0.30  ? 2728 LEU A CB    1 
ATOM   10015 C  CG    . LEU A 1 2728 ? 231.134 181.053 188.381 1.00 0.20  ? 2728 LEU A CG    1 
ATOM   10016 C  CD1   . LEU A 1 2728 ? 231.579 179.718 188.942 1.00 0.37  ? 2728 LEU A CD1   1 
ATOM   10017 C  CD2   . LEU A 1 2728 ? 232.053 182.162 188.862 1.00 0.10  ? 2728 LEU A CD2   1 
ATOM   10018 N  N     . ARG A 1 2729 ? 230.074 181.964 183.792 1.00 0.88  ? 2729 ARG A N     1 
ATOM   10019 C  CA    . ARG A 1 2729 ? 230.378 181.857 182.366 1.00 0.32  ? 2729 ARG A CA    1 
ATOM   10020 C  C     . ARG A 1 2729 ? 230.880 183.176 181.797 1.00 0.45  ? 2729 ARG A C     1 
ATOM   10021 O  O     . ARG A 1 2729 ? 231.574 183.185 180.776 1.00 1.03  ? 2729 ARG A O     1 
ATOM   10022 C  CB    . ARG A 1 2729 ? 229.156 181.381 181.580 1.00 0.64  ? 2729 ARG A CB    1 
ATOM   10023 C  CG    . ARG A 1 2729 ? 227.983 182.346 181.571 1.00 1.34  ? 2729 ARG A CG    1 
ATOM   10024 C  CD    . ARG A 1 2729 ? 226.817 181.763 180.796 1.00 2.24  ? 2729 ARG A CD    1 
ATOM   10025 N  NE    . ARG A 1 2729 ? 227.083 181.609 179.369 1.00 4.86  ? 2729 ARG A NE    1 
ATOM   10026 C  CZ    . ARG A 1 2729 ? 226.922 182.571 178.472 1.00 3.67  ? 2729 ARG A CZ    1 
ATOM   10027 N  NH1   . ARG A 1 2729 ? 226.418 183.745 178.800 1.00 9.72  ? 2729 ARG A NH1   1 
ATOM   10028 N  NH2   . ARG A 1 2729 ? 227.248 182.342 177.204 1.00 6.81  ? 2729 ARG A NH2   1 
ATOM   10029 N  N     . HIS A 1 2730 ? 230.544 184.292 182.436 1.00 0.34  ? 2730 HIS A N     1 
ATOM   10030 C  CA    . HIS A 1 2730 ? 230.990 185.604 182.000 1.00 0.35  ? 2730 HIS A CA    1 
ATOM   10031 C  C     . HIS A 1 2730 ? 232.272 186.056 182.674 1.00 0.38  ? 2730 HIS A C     1 
ATOM   10032 O  O     . HIS A 1 2730 ? 232.903 187.005 182.196 1.00 0.78  ? 2730 HIS A O     1 
ATOM   10033 C  CB    . HIS A 1 2730 ? 229.901 186.644 182.269 1.00 0.26  ? 2730 HIS A CB    1 
ATOM   10034 C  CG    . HIS A 1 2730 ? 228.597 186.319 181.623 1.00 0.80  ? 2730 HIS A CG    1 
ATOM   10035 N  ND1   . HIS A 1 2730 ? 227.573 185.689 182.294 1.00 0.63  ? 2730 HIS A ND1   1 
ATOM   10036 C  CD2   . HIS A 1 2730 ? 228.156 186.521 180.362 1.00 0.75  ? 2730 HIS A CD2   1 
ATOM   10037 C  CE1   . HIS A 1 2730 ? 226.553 185.523 181.474 1.00 0.94  ? 2730 HIS A CE1   1 
ATOM   10038 N  NE2   . HIS A 1 2730 ? 226.882 186.020 180.295 1.00 1.06  ? 2730 HIS A NE2   1 
ATOM   10039 N  N     . VAL A 1 2731 ? 232.673 185.409 183.758 1.00 0.34  ? 2731 VAL A N     1 
ATOM   10040 C  CA    . VAL A 1 2731 ? 233.672 185.936 184.673 1.00 0.27  ? 2731 VAL A CA    1 
ATOM   10041 C  C     . VAL A 1 2731 ? 234.827 184.947 184.761 1.00 0.19  ? 2731 VAL A C     1 
ATOM   10042 O  O     . VAL A 1 2731 ? 234.755 183.952 185.481 1.00 0.78  ? 2731 VAL A O     1 
ATOM   10043 C  CB    . VAL A 1 2731 ? 233.065 186.203 186.062 1.00 0.21  ? 2731 VAL A CB    1 
ATOM   10044 C  CG1   . VAL A 1 2731 ? 234.106 186.767 186.985 1.00 0.14  ? 2731 VAL A CG1   1 
ATOM   10045 C  CG2   . VAL A 1 2731 ? 231.875 187.146 185.950 1.00 0.13  ? 2731 VAL A CG2   1 
ATOM   10046 N  N     . PRO A 1 2732 ? 235.917 185.187 184.032 1.00 0.13  ? 2732 PRO A N     1 
ATOM   10047 C  CA    . PRO A 1 2732 ? 237.129 184.387 184.241 1.00 0.18  ? 2732 PRO A CA    1 
ATOM   10048 C  C     . PRO A 1 2732 ? 237.667 184.557 185.653 1.00 0.13  ? 2732 PRO A C     1 
ATOM   10049 O  O     . PRO A 1 2732 ? 237.585 185.632 186.251 1.00 0.27  ? 2732 PRO A O     1 
ATOM   10050 C  CB    . PRO A 1 2732 ? 238.108 184.941 183.196 1.00 0.18  ? 2732 PRO A CB    1 
ATOM   10051 C  CG    . PRO A 1 2732 ? 237.561 186.271 182.824 1.00 0.25  ? 2732 PRO A CG    1 
ATOM   10052 C  CD    . PRO A 1 2732 ? 236.078 186.130 182.917 1.00 0.28  ? 2732 PRO A CD    1 
ATOM   10053 N  N     . VAL A 1 2733 ? 238.222 183.474 186.186 1.00 0.11  ? 2733 VAL A N     1 
ATOM   10054 C  CA    . VAL A 1 2733 ? 238.711 183.427 187.557 1.00 0.11  ? 2733 VAL A CA    1 
ATOM   10055 C  C     . VAL A 1 2733 ? 240.202 183.130 187.532 1.00 0.12  ? 2733 VAL A C     1 
ATOM   10056 O  O     . VAL A 1 2733 ? 240.641 182.181 186.874 1.00 0.19  ? 2733 VAL A O     1 
ATOM   10057 C  CB    . VAL A 1 2733 ? 237.956 182.377 188.394 1.00 0.10  ? 2733 VAL A CB    1 
ATOM   10058 C  CG1   . VAL A 1 2733 ? 238.586 182.237 189.769 1.00 0.11  ? 2733 VAL A CG1   1 
ATOM   10059 C  CG2   . VAL A 1 2733 ? 236.491 182.745 188.509 1.00 0.10  ? 2733 VAL A CG2   1 
ATOM   10060 N  N     . VAL A 1 2734 ? 240.974 183.949 188.235 1.00 0.16  ? 2734 VAL A N     1 
ATOM   10061 C  CA    . VAL A 1 2734 ? 242.394 183.717 188.456 1.00 0.27  ? 2734 VAL A CA    1 
ATOM   10062 C  C     . VAL A 1 2734 ? 242.592 183.383 189.928 1.00 0.19  ? 2734 VAL A C     1 
ATOM   10063 O  O     . VAL A 1 2734 ? 241.993 184.021 190.801 1.00 0.13  ? 2734 VAL A O     1 
ATOM   10064 C  CB    . VAL A 1 2734 ? 243.250 184.928 188.025 1.00 0.40  ? 2734 VAL A CB    1 
ATOM   10065 C  CG1   . VAL A 1 2734 ? 242.936 186.156 188.866 1.00 2.04  ? 2734 VAL A CG1   1 
ATOM   10066 C  CG2   . VAL A 1 2734 ? 244.728 184.589 188.116 1.00 0.37  ? 2734 VAL A CG2   1 
ATOM   10067 N  N     . TYR A 1 2735 ? 243.395 182.360 190.199 1.00 0.41  ? 2735 TYR A N     1 
ATOM   10068 C  CA    . TYR A 1 2735 ? 243.669 181.928 191.562 1.00 0.36  ? 2735 TYR A CA    1 
ATOM   10069 C  C     . TYR A 1 2735 ? 244.964 182.569 192.045 1.00 0.41  ? 2735 TYR A C     1 
ATOM   10070 O  O     . TYR A 1 2735 ? 246.030 182.350 191.457 1.00 0.89  ? 2735 TYR A O     1 
ATOM   10071 C  CB    . TYR A 1 2735 ? 243.766 180.407 191.645 1.00 0.64  ? 2735 TYR A CB    1 
ATOM   10072 C  CG    . TYR A 1 2735 ? 244.030 179.893 193.041 1.00 1.13  ? 2735 TYR A CG    1 
ATOM   10073 C  CD1   . TYR A 1 2735 ? 243.219 180.265 194.105 1.00 1.22  ? 2735 TYR A CD1   1 
ATOM   10074 C  CD2   . TYR A 1 2735 ? 245.101 179.050 193.298 1.00 0.82  ? 2735 TYR A CD2   1 
ATOM   10075 C  CE1   . TYR A 1 2735 ? 243.458 179.800 195.380 1.00 1.93  ? 2735 TYR A CE1   1 
ATOM   10076 C  CE2   . TYR A 1 2735 ? 245.349 178.580 194.572 1.00 1.86  ? 2735 TYR A CE2   1 
ATOM   10077 C  CZ    . TYR A 1 2735 ? 244.525 178.959 195.608 1.00 5.10  ? 2735 TYR A CZ    1 
ATOM   10078 O  OH    . TYR A 1 2735 ? 244.769 178.493 196.878 1.00 12.45 ? 2735 TYR A OH    1 
ATOM   10079 N  N     . VAL A 1 2736 ? 244.872 183.351 193.111 1.00 0.19  ? 2736 VAL A N     1 
ATOM   10080 C  CA    . VAL A 1 2736 ? 246.029 183.989 193.721 1.00 0.46  ? 2736 VAL A CA    1 
ATOM   10081 C  C     . VAL A 1 2736 ? 246.278 183.287 195.046 1.00 0.37  ? 2736 VAL A C     1 
ATOM   10082 O  O     . VAL A 1 2736 ? 245.513 183.453 196.004 1.00 0.32  ? 2736 VAL A O     1 
ATOM   10083 C  CB    . VAL A 1 2736 ? 245.823 185.497 193.908 1.00 0.59  ? 2736 VAL A CB    1 
ATOM   10084 C  CG1   . VAL A 1 2736 ? 247.043 186.121 194.561 1.00 0.25  ? 2736 VAL A CG1   1 
ATOM   10085 C  CG2   . VAL A 1 2736 ? 245.527 186.160 192.570 1.00 0.47  ? 2736 VAL A CG2   1 
ATOM   10086 N  N     . ASP A 1 2737 ? 247.338 182.494 195.101 1.00 0.49  ? 2737 ASP A N     1 
ATOM   10087 C  CA    . ASP A 1 2737 ? 247.698 181.765 196.304 1.00 1.13  ? 2737 ASP A CA    1 
ATOM   10088 C  C     . ASP A 1 2737 ? 248.643 182.596 197.168 1.00 0.55  ? 2737 ASP A C     1 
ATOM   10089 O  O     . ASP A 1 2737 ? 249.137 183.650 196.765 1.00 0.68  ? 2737 ASP A O     1 
ATOM   10090 C  CB    . ASP A 1 2737 ? 248.340 180.428 195.942 1.00 1.28  ? 2737 ASP A CB    1 
ATOM   10091 C  CG    . ASP A 1 2737 ? 248.236 179.410 197.057 1.00 4.81  ? 2737 ASP A CG    1 
ATOM   10092 O  OD1   . ASP A 1 2737 ? 247.595 179.712 198.085 1.00 3.14  ? 2737 ASP A OD1   1 
ATOM   10093 O  OD2   . ASP A 1 2737 ? 248.799 178.306 196.907 1.00 14.41 ? 2737 ASP A OD2   1 
ATOM   10094 N  N     . TYR A 1 2738 ? 248.884 182.107 198.376 1.00 0.94  ? 2738 TYR A N     1 
ATOM   10095 C  CA    . TYR A 1 2738 ? 249.877 182.727 199.234 1.00 0.77  ? 2738 TYR A CA    1 
ATOM   10096 C  C     . TYR A 1 2738 ? 251.258 182.580 198.602 1.00 1.23  ? 2738 TYR A C     1 
ATOM   10097 O  O     . TYR A 1 2738 ? 251.566 181.531 198.023 1.00 1.46  ? 2738 TYR A O     1 
ATOM   10098 C  CB    . TYR A 1 2738 ? 249.866 182.088 200.623 1.00 0.47  ? 2738 TYR A CB    1 
ATOM   10099 C  CG    . TYR A 1 2738 ? 248.758 182.598 201.510 1.00 0.36  ? 2738 TYR A CG    1 
ATOM   10100 C  CD1   . TYR A 1 2738 ? 248.345 183.919 201.438 1.00 0.41  ? 2738 TYR A CD1   1 
ATOM   10101 C  CD2   . TYR A 1 2738 ? 248.120 181.757 202.410 1.00 0.25  ? 2738 TYR A CD2   1 
ATOM   10102 C  CE1   . TYR A 1 2738 ? 247.330 184.393 202.242 1.00 0.30  ? 2738 TYR A CE1   1 
ATOM   10103 C  CE2   . TYR A 1 2738 ? 247.105 182.221 203.217 1.00 0.32  ? 2738 TYR A CE2   1 
ATOM   10104 C  CZ    . TYR A 1 2738 ? 246.715 183.541 203.130 1.00 0.35  ? 2738 TYR A CZ    1 
ATOM   10105 O  OH    . TYR A 1 2738 ? 245.700 184.012 203.929 1.00 0.30  ? 2738 TYR A OH    1 
ATOM   10106 N  N     . PRO A 1 2739 ? 252.099 183.611 198.665 1.00 1.78  ? 2739 PRO A N     1 
ATOM   10107 C  CA    . PRO A 1 2739 ? 253.481 183.455 198.206 1.00 1.26  ? 2739 PRO A CA    1 
ATOM   10108 C  C     . PRO A 1 2739 ? 254.191 182.368 198.998 1.00 1.91  ? 2739 PRO A C     1 
ATOM   10109 O  O     . PRO A 1 2739 ? 253.976 182.205 200.200 1.00 2.62  ? 2739 PRO A O     1 
ATOM   10110 C  CB    . PRO A 1 2739 ? 254.096 184.835 198.458 1.00 0.72  ? 2739 PRO A CB    1 
ATOM   10111 C  CG    . PRO A 1 2739 ? 252.938 185.769 198.451 1.00 0.67  ? 2739 PRO A CG    1 
ATOM   10112 C  CD    . PRO A 1 2739 ? 251.786 185.002 199.029 1.00 1.26  ? 2739 PRO A CD    1 
ATOM   10113 N  N     . GLY A 1 2740 ? 255.046 181.615 198.306 1.00 1.95  ? 2740 GLY A N     1 
ATOM   10114 C  CA    . GLY A 1 2740 ? 255.775 180.552 198.931 1.00 3.37  ? 2740 GLY A CA    1 
ATOM   10115 C  C     . GLY A 1 2740 ? 256.905 181.075 199.794 1.00 4.68  ? 2740 GLY A C     1 
ATOM   10116 O  O     . GLY A 1 2740 ? 257.154 182.284 199.875 1.00 4.13  ? 2740 GLY A O     1 
ATOM   10117 N  N     . PRO A 1 2741 ? 257.603 180.153 200.464 1.00 4.84  ? 2741 PRO A N     1 
ATOM   10118 C  CA    . PRO A 1 2741 ? 258.714 180.572 201.335 1.00 4.72  ? 2741 PRO A CA    1 
ATOM   10119 C  C     . PRO A 1 2741 ? 259.799 181.343 200.603 1.00 4.97  ? 2741 PRO A C     1 
ATOM   10120 O  O     . PRO A 1 2741 ? 260.371 182.283 201.168 1.00 5.23  ? 2741 PRO A O     1 
ATOM   10121 C  CB    . PRO A 1 2741 ? 259.236 179.239 201.890 1.00 7.78  ? 2741 PRO A CB    1 
ATOM   10122 C  CG    . PRO A 1 2741 ? 258.073 178.306 201.779 1.00 10.02 ? 2741 PRO A CG    1 
ATOM   10123 C  CD    . PRO A 1 2741 ? 257.384 178.699 200.512 1.00 8.66  ? 2741 PRO A CD    1 
ATOM   10124 N  N     . ALA A 1 2742 ? 260.099 180.973 199.356 1.00 4.19  ? 2742 ALA A N     1 
ATOM   10125 C  CA    . ALA A 1 2742 ? 261.116 181.693 198.598 1.00 3.07  ? 2742 ALA A CA    1 
ATOM   10126 C  C     . ALA A 1 2742 ? 260.590 183.035 198.109 1.00 2.35  ? 2742 ALA A C     1 
ATOM   10127 O  O     . ALA A 1 2742 ? 261.334 184.021 198.067 1.00 2.07  ? 2742 ALA A O     1 
ATOM   10128 C  CB    . ALA A 1 2742 ? 261.601 180.843 197.424 1.00 3.19  ? 2742 ALA A CB    1 
ATOM   10129 N  N     . SER A 1 2743 ? 259.315 183.088 197.722 1.00 5.18  ? 2743 SER A N     1 
ATOM   10130 C  CA    . SER A 1 2743 ? 258.718 184.356 197.316 1.00 1.37  ? 2743 SER A CA    1 
ATOM   10131 C  C     . SER A 1 2743 ? 258.646 185.328 198.489 1.00 2.45  ? 2743 SER A C     1 
ATOM   10132 O  O     . SER A 1 2743 ? 258.906 186.525 198.326 1.00 3.20  ? 2743 SER A O     1 
ATOM   10133 C  CB    . SER A 1 2743 ? 257.333 184.111 196.721 1.00 1.91  ? 2743 SER A CB    1 
ATOM   10134 O  OG    . SER A 1 2743 ? 256.753 185.313 196.250 1.00 8.15  ? 2743 SER A OG    1 
ATOM   10135 N  N     . LEU A 1 2744 ? 258.296 184.828 199.676 1.00 2.67  ? 2744 LEU A N     1 
ATOM   10136 C  CA    . LEU A 1 2744 ? 258.272 185.678 200.863 1.00 0.98  ? 2744 LEU A CA    1 
ATOM   10137 C  C     . LEU A 1 2744 ? 259.660 186.205 201.190 1.00 1.51  ? 2744 LEU A C     1 
ATOM   10138 O  O     . LEU A 1 2744 ? 259.816 187.371 201.572 1.00 1.46  ? 2744 LEU A O     1 
ATOM   10139 C  CB    . LEU A 1 2744 ? 257.700 184.905 202.048 1.00 1.28  ? 2744 LEU A CB    1 
ATOM   10140 C  CG    . LEU A 1 2744 ? 256.206 184.589 201.989 1.00 1.37  ? 2744 LEU A CG    1 
ATOM   10141 C  CD1   . LEU A 1 2744 ? 255.786 183.784 203.205 1.00 1.25  ? 2744 LEU A CD1   1 
ATOM   10142 C  CD2   . LEU A 1 2744 ? 255.391 185.864 201.872 1.00 0.90  ? 2744 LEU A CD2   1 
ATOM   10143 N  N     . THR A 1 2745 ? 260.683 185.360 201.045 1.00 1.99  ? 2745 THR A N     1 
ATOM   10144 C  CA    . THR A 1 2745 ? 262.051 185.801 201.287 1.00 1.51  ? 2745 THR A CA    1 
ATOM   10145 C  C     . THR A 1 2745 ? 262.453 186.898 200.312 1.00 3.12  ? 2745 THR A C     1 
ATOM   10146 O  O     . THR A 1 2745 ? 263.149 187.848 200.685 1.00 4.83  ? 2745 THR A O     1 
ATOM   10147 C  CB    . THR A 1 2745 ? 263.007 184.612 201.187 1.00 1.26  ? 2745 THR A CB    1 
ATOM   10148 O  OG1   . THR A 1 2745 ? 262.655 183.634 202.174 1.00 1.84  ? 2745 THR A OG1   1 
ATOM   10149 C  CG2   . THR A 1 2745 ? 264.443 185.050 201.409 1.00 1.07  ? 2745 THR A CG2   1 
ATOM   10150 N  N     . GLN A 1 2746 ? 262.024 186.784 199.055 1.00 4.71  ? 2746 GLN A N     1 
ATOM   10151 C  CA    . GLN A 1 2746 ? 262.338 187.814 198.071 1.00 2.96  ? 2746 GLN A CA    1 
ATOM   10152 C  C     . GLN A 1 2746 ? 261.594 189.113 198.365 1.00 3.12  ? 2746 GLN A C     1 
ATOM   10153 O  O     . GLN A 1 2746 ? 262.167 190.200 198.247 1.00 3.40  ? 2746 GLN A O     1 
ATOM   10154 C  CB    . GLN A 1 2746 ? 262.009 187.306 196.667 1.00 4.09  ? 2746 GLN A CB    1 
ATOM   10155 C  CG    . GLN A 1 2746 ? 262.230 188.324 195.563 1.00 5.67  ? 2746 GLN A CG    1 
ATOM   10156 C  CD    . GLN A 1 2746 ? 263.674 188.372 195.093 1.00 20.27 ? 2746 GLN A CD    1 
ATOM   10157 O  OE1   . GLN A 1 2746 ? 264.537 187.681 195.633 1.00 14.60 ? 2746 GLN A OE1   1 
ATOM   10158 N  NE2   . GLN A 1 2746 ? 263.939 189.190 194.080 1.00 15.29 ? 2746 GLN A NE2   1 
ATOM   10159 N  N     . ILE A 1 2747 ? 260.318 189.021 198.752 1.00 1.60  ? 2747 ILE A N     1 
ATOM   10160 C  CA    . ILE A 1 2747 ? 259.525 190.221 199.006 1.00 1.06  ? 2747 ILE A CA    1 
ATOM   10161 C  C     . ILE A 1 2747 ? 260.069 190.980 200.210 1.00 1.56  ? 2747 ILE A C     1 
ATOM   10162 O  O     . ILE A 1 2747 ? 260.496 192.133 200.102 1.00 1.66  ? 2747 ILE A O     1 
ATOM   10163 C  CB    . ILE A 1 2747 ? 258.042 189.862 199.206 1.00 1.34  ? 2747 ILE A CB    1 
ATOM   10164 C  CG1   . ILE A 1 2747 ? 257.432 189.323 197.911 1.00 2.32  ? 2747 ILE A CG1   1 
ATOM   10165 C  CG2   . ILE A 1 2747 ? 257.262 191.061 199.716 1.00 0.30  ? 2747 ILE A CG2   1 
ATOM   10166 C  CD1   . ILE A 1 2747 ? 256.222 188.455 198.129 1.00 0.72  ? 2747 ILE A CD1   1 
ATOM   10167 N  N     . TYR A 1 2748 ? 260.061 190.337 201.373 1.00 1.16  ? 2748 TYR A N     1 
ATOM   10168 C  CA    . TYR A 1 2748 ? 260.400 191.008 202.617 1.00 0.82  ? 2748 TYR A CA    1 
ATOM   10169 C  C     . TYR A 1 2748 ? 261.895 191.042 202.893 1.00 1.05  ? 2748 TYR A C     1 
ATOM   10170 O  O     . TYR A 1 2748 ? 262.329 191.804 203.762 1.00 3.00  ? 2748 TYR A O     1 
ATOM   10171 C  CB    . TYR A 1 2748 ? 259.642 190.350 203.767 1.00 0.46  ? 2748 TYR A CB    1 
ATOM   10172 C  CG    . TYR A 1 2748 ? 258.152 190.466 203.568 1.00 0.23  ? 2748 TYR A CG    1 
ATOM   10173 C  CD1   . TYR A 1 2748 ? 257.500 191.667 203.800 1.00 0.39  ? 2748 TYR A CD1   1 
ATOM   10174 C  CD2   . TYR A 1 2748 ? 257.406 189.393 203.105 1.00 0.22  ? 2748 TYR A CD2   1 
ATOM   10175 C  CE1   . TYR A 1 2748 ? 256.143 191.791 203.604 1.00 0.26  ? 2748 TYR A CE1   1 
ATOM   10176 C  CE2   . TYR A 1 2748 ? 256.046 189.508 202.903 1.00 0.34  ? 2748 TYR A CE2   1 
ATOM   10177 C  CZ    . TYR A 1 2748 ? 255.420 190.713 203.154 1.00 0.28  ? 2748 TYR A CZ    1 
ATOM   10178 O  OH    . TYR A 1 2748 ? 254.067 190.840 202.961 1.00 0.20  ? 2748 TYR A OH    1 
ATOM   10179 N  N     . GLY A 1 2749 ? 262.691 190.251 202.173 1.00 1.26  ? 2749 GLY A N     1 
ATOM   10180 C  CA    . GLY A 1 2749 ? 264.122 190.493 202.152 1.00 1.27  ? 2749 GLY A CA    1 
ATOM   10181 C  C     . GLY A 1 2749 ? 264.468 191.798 201.468 1.00 2.36  ? 2749 GLY A C     1 
ATOM   10182 O  O     . GLY A 1 2749 ? 265.407 192.488 201.877 1.00 5.51  ? 2749 GLY A O     1 
ATOM   10183 N  N     . THR A 1 2750 ? 263.727 192.152 200.417 1.00 4.53  ? 2750 THR A N     1 
ATOM   10184 C  CA    . THR A 1 2750 ? 263.887 193.459 199.789 1.00 4.30  ? 2750 THR A CA    1 
ATOM   10185 C  C     . THR A 1 2750 ? 263.497 194.574 200.749 1.00 2.86  ? 2750 THR A C     1 
ATOM   10186 O  O     . THR A 1 2750 ? 264.190 195.592 200.852 1.00 6.42  ? 2750 THR A O     1 
ATOM   10187 C  CB    . THR A 1 2750 ? 263.049 193.527 198.510 1.00 2.61  ? 2750 THR A CB    1 
ATOM   10188 O  OG1   . THR A 1 2750 ? 263.526 192.556 197.572 1.00 7.69  ? 2750 THR A OG1   1 
ATOM   10189 C  CG2   . THR A 1 2750 ? 263.125 194.910 197.884 1.00 3.92  ? 2750 THR A CG2   1 
ATOM   10190 N  N     . PHE A 1 2751 ? 262.384 194.396 201.468 1.00 2.23  ? 2751 PHE A N     1 
ATOM   10191 C  CA    . PHE A 1 2751 ? 261.952 195.401 202.433 1.00 3.35  ? 2751 PHE A CA    1 
ATOM   10192 C  C     . PHE A 1 2751 ? 262.942 195.532 203.583 1.00 7.13  ? 2751 PHE A C     1 
ATOM   10193 O  O     . PHE A 1 2751 ? 263.265 196.648 204.008 1.00 7.43  ? 2751 PHE A O     1 
ATOM   10194 C  CB    . PHE A 1 2751 ? 260.562 195.049 202.964 1.00 1.96  ? 2751 PHE A CB    1 
ATOM   10195 C  CG    . PHE A 1 2751 ? 259.451 195.398 202.023 1.00 2.41  ? 2751 PHE A CG    1 
ATOM   10196 C  CD1   . PHE A 1 2751 ? 259.554 196.491 201.182 1.00 3.62  ? 2751 PHE A CD1   1 
ATOM   10197 C  CD2   . PHE A 1 2751 ? 258.302 194.630 201.976 1.00 1.54  ? 2751 PHE A CD2   1 
ATOM   10198 C  CE1   . PHE A 1 2751 ? 258.534 196.813 200.317 1.00 3.50  ? 2751 PHE A CE1   1 
ATOM   10199 C  CE2   . PHE A 1 2751 ? 257.276 194.949 201.111 1.00 1.73  ? 2751 PHE A CE2   1 
ATOM   10200 C  CZ    . PHE A 1 2751 ? 257.393 196.042 200.282 1.00 2.24  ? 2751 PHE A CZ    1 
ATOM   10201 N  N     . ASN A 1 2752 ? 263.433 194.404 204.103 1.00 2.52  ? 2752 ASN A N     1 
ATOM   10202 C  CA    . ASN A 1 2752 ? 264.357 194.449 205.232 1.00 3.41  ? 2752 ASN A CA    1 
ATOM   10203 C  C     . ASN A 1 2752 ? 265.674 195.111 204.846 1.00 6.92  ? 2752 ASN A C     1 
ATOM   10204 O  O     . ASN A 1 2752 ? 266.260 195.849 205.645 1.00 8.66  ? 2752 ASN A O     1 
ATOM   10205 C  CB    . ASN A 1 2752 ? 264.593 193.040 205.776 1.00 3.23  ? 2752 ASN A CB    1 
ATOM   10206 C  CG    . ASN A 1 2752 ? 263.443 192.544 206.629 1.00 1.08  ? 2752 ASN A CG    1 
ATOM   10207 O  OD1   . ASN A 1 2752 ? 262.466 193.256 206.854 1.00 1.71  ? 2752 ASN A OD1   1 
ATOM   10208 N  ND2   . ASN A 1 2752 ? 263.546 191.311 207.098 1.00 2.57  ? 2752 ASN A ND2   1 
ATOM   10209 N  N     . ARG A 1 2753 ? 266.157 194.857 203.627 1.00 7.52  ? 2753 ARG A N     1 
ATOM   10210 C  CA    . ARG A 1 2753 ? 267.374 195.519 203.167 1.00 9.15  ? 2753 ARG A CA    1 
ATOM   10211 C  C     . ARG A 1 2753 ? 267.193 197.031 203.123 1.00 8.92  ? 2753 ARG A C     1 
ATOM   10212 O  O     . ARG A 1 2753 ? 268.099 197.785 203.498 1.00 11.88 ? 2753 ARG A O     1 
ATOM   10213 C  CB    . ARG A 1 2753 ? 267.771 194.990 201.790 1.00 5.61  ? 2753 ARG A CB    1 
ATOM   10214 C  CG    . ARG A 1 2753 ? 268.555 193.691 201.821 1.00 11.94 ? 2753 ARG A CG    1 
ATOM   10215 C  CD    . ARG A 1 2753 ? 269.187 193.396 200.472 1.00 10.73 ? 2753 ARG A CD    1 
ATOM   10216 N  NE    . ARG A 1 2753 ? 268.268 193.653 199.369 1.00 10.98 ? 2753 ARG A NE    1 
ATOM   10217 C  CZ    . ARG A 1 2753 ? 267.427 192.758 198.867 1.00 10.65 ? 2753 ARG A CZ    1 
ATOM   10218 N  NH1   . ARG A 1 2753 ? 267.364 191.527 199.343 1.00 6.72  ? 2753 ARG A NH1   1 
ATOM   10219 N  NH2   . ARG A 1 2753 ? 266.631 193.110 197.863 1.00 7.66  ? 2753 ARG A NH2   1 
ATOM   10220 N  N     . ALA A 1 2754 ? 266.031 197.495 202.662 1.00 4.99  ? 2754 ALA A N     1 
ATOM   10221 C  CA    . ALA A 1 2754 ? 265.773 198.930 202.615 1.00 7.90  ? 2754 ALA A CA    1 
ATOM   10222 C  C     . ALA A 1 2754 ? 265.623 199.517 204.014 1.00 11.07 ? 2754 ALA A C     1 
ATOM   10223 O  O     . ALA A 1 2754 ? 266.156 200.595 204.302 1.00 13.64 ? 2754 ALA A O     1 
ATOM   10224 C  CB    . ALA A 1 2754 ? 264.527 199.206 201.778 1.00 7.03  ? 2754 ALA A CB    1 
ATOM   10225 N  N     . MET A 1 2755 ? 264.900 198.823 204.895 1.00 14.94 ? 2755 MET A N     1 
ATOM   10226 C  CA    . MET A 1 2755 ? 264.637 199.357 206.229 1.00 8.36  ? 2755 MET A CA    1 
ATOM   10227 C  C     . MET A 1 2755 ? 265.875 199.284 207.118 1.00 8.81  ? 2755 MET A C     1 
ATOM   10228 O  O     . MET A 1 2755 ? 266.042 200.108 208.023 1.00 16.92 ? 2755 MET A O     1 
ATOM   10229 C  CB    . MET A 1 2755 ? 263.443 198.623 206.843 1.00 5.82  ? 2755 MET A CB    1 
ATOM   10230 C  CG    . MET A 1 2755 ? 263.298 198.718 208.349 1.00 8.74  ? 2755 MET A CG    1 
ATOM   10231 S  SD    . MET A 1 2755 ? 262.503 197.244 209.015 1.00 14.00 ? 2755 MET A SD    1 
ATOM   10232 C  CE    . MET A 1 2755 ? 263.910 196.195 209.335 1.00 6.15  ? 2755 MET A CE    1 
ATOM   10233 N  N     . LEU A 1 2756 ? 266.763 198.325 206.866 1.00 8.29  ? 2756 LEU A N     1 
ATOM   10234 C  CA    . LEU A 1 2756 ? 268.012 198.266 207.618 1.00 6.53  ? 2756 LEU A CA    1 
ATOM   10235 C  C     . LEU A 1 2756 ? 269.101 199.162 207.040 1.00 11.80 ? 2756 LEU A C     1 
ATOM   10236 O  O     . LEU A 1 2756 ? 270.255 199.048 207.467 1.00 13.50 ? 2756 LEU A O     1 
ATOM   10237 C  CB    . LEU A 1 2756 ? 268.506 196.822 207.711 1.00 6.84  ? 2756 LEU A CB    1 
ATOM   10238 C  CG    . LEU A 1 2756 ? 267.709 195.912 208.651 1.00 9.57  ? 2756 LEU A CG    1 
ATOM   10239 C  CD1   . LEU A 1 2756 ? 268.498 194.672 208.996 1.00 9.10  ? 2756 LEU A CD1   1 
ATOM   10240 C  CD2   . LEU A 1 2756 ? 267.366 196.664 209.923 1.00 9.22  ? 2756 LEU A CD2   1 
ATOM   10241 N  N     . ARG A 1 2757 ? 268.781 200.029 206.077 1.00 15.99 ? 2757 ARG A N     1 
ATOM   10242 C  CA    . ARG A 1 2757 ? 269.712 201.087 205.701 1.00 12.75 ? 2757 ARG A CA    1 
ATOM   10243 C  C     . ARG A 1 2757 ? 269.604 202.295 206.621 1.00 13.07 ? 2757 ARG A C     1 
ATOM   10244 O  O     . ARG A 1 2757 ? 270.453 203.188 206.550 1.00 14.08 ? 2757 ARG A O     1 
ATOM   10245 C  CB    . ARG A 1 2757 ? 269.496 201.522 204.249 1.00 15.33 ? 2757 ARG A CB    1 
ATOM   10246 C  CG    . ARG A 1 2757 ? 269.902 200.486 203.217 1.00 16.27 ? 2757 ARG A CG    1 
ATOM   10247 C  CD    . ARG A 1 2757 ? 269.982 201.089 201.823 1.00 15.47 ? 2757 ARG A CD    1 
ATOM   10248 N  NE    . ARG A 1 2757 ? 268.678 201.236 201.188 1.00 17.47 ? 2757 ARG A NE    1 
ATOM   10249 C  CZ    . ARG A 1 2757 ? 268.101 200.308 200.438 1.00 16.87 ? 2757 ARG A CZ    1 
ATOM   10250 N  NH1   . ARG A 1 2757 ? 268.675 199.136 200.222 1.00 18.66 ? 2757 ARG A NH1   1 
ATOM   10251 N  NH2   . ARG A 1 2757 ? 266.919 200.565 199.886 1.00 16.35 ? 2757 ARG A NH2   1 
ATOM   10252 N  N     . LEU A 1 2758 ? 268.577 202.348 207.473 1.00 13.94 ? 2758 LEU A N     1 
ATOM   10253 C  CA    . LEU A 1 2758 ? 268.503 203.395 208.486 1.00 12.38 ? 2758 LEU A CA    1 
ATOM   10254 C  C     . LEU A 1 2758 ? 269.668 203.291 209.460 1.00 17.81 ? 2758 LEU A C     1 
ATOM   10255 O  O     . LEU A 1 2758 ? 270.281 204.300 209.827 1.00 23.47 ? 2758 LEU A O     1 
ATOM   10256 C  CB    . LEU A 1 2758 ? 267.171 203.317 209.232 1.00 12.05 ? 2758 LEU A CB    1 
ATOM   10257 C  CG    . LEU A 1 2758 ? 265.889 203.563 208.437 1.00 14.46 ? 2758 LEU A CG    1 
ATOM   10258 C  CD1   . LEU A 1 2758 ? 264.669 203.408 209.325 1.00 10.93 ? 2758 LEU A CD1   1 
ATOM   10259 C  CD2   . LEU A 1 2758 ? 265.916 204.947 207.810 1.00 9.94  ? 2758 LEU A CD2   1 
ATOM   10260 N  N     . ILE A 1 2759 ? 269.994 202.073 209.881 1.00 13.68 ? 2759 ILE A N     1 
ATOM   10261 C  CA    . ILE A 1 2759 ? 271.124 201.840 210.774 1.00 13.67 ? 2759 ILE A CA    1 
ATOM   10262 C  C     . ILE A 1 2759 ? 272.197 201.101 209.982 1.00 16.80 ? 2759 ILE A C     1 
ATOM   10263 O  O     . ILE A 1 2759 ? 272.100 199.878 209.807 1.00 22.81 ? 2759 ILE A O     1 
ATOM   10264 C  CB    . ILE A 1 2759 ? 270.706 201.044 212.018 1.00 17.08 ? 2759 ILE A CB    1 
ATOM   10265 C  CG1   . ILE A 1 2759 ? 269.436 201.634 212.638 1.00 16.61 ? 2759 ILE A CG1   1 
ATOM   10266 C  CG2   . ILE A 1 2759 ? 271.828 201.033 213.037 1.00 17.91 ? 2759 ILE A CG2   1 
ATOM   10267 C  CD1   . ILE A 1 2759 ? 269.596 203.043 213.149 1.00 15.71 ? 2759 ILE A CD1   1 
ATOM   10268 N  N     . PRO A 1 2760 ? 273.222 201.795 209.484 1.00 21.10 ? 2760 PRO A N     1 
ATOM   10269 C  CA    . PRO A 1 2760 ? 274.248 201.116 208.675 1.00 16.87 ? 2760 PRO A CA    1 
ATOM   10270 C  C     . PRO A 1 2760 ? 274.966 199.990 209.399 1.00 21.74 ? 2760 PRO A C     1 
ATOM   10271 O  O     . PRO A 1 2760 ? 275.445 199.050 208.751 1.00 24.92 ? 2760 PRO A O     1 
ATOM   10272 C  CB    . PRO A 1 2760 ? 275.204 202.262 208.318 1.00 20.30 ? 2760 PRO A CB    1 
ATOM   10273 C  CG    . PRO A 1 2760 ? 274.325 203.460 208.285 1.00 19.26 ? 2760 PRO A CG    1 
ATOM   10274 C  CD    . PRO A 1 2760 ? 273.348 203.261 209.411 1.00 18.45 ? 2760 PRO A CD    1 
ATOM   10275 N  N     . SER A 1 2761 ? 275.064 200.058 210.725 1.00 16.12 ? 2761 SER A N     1 
ATOM   10276 C  CA    . SER A 1 2761 ? 275.705 198.993 211.486 1.00 16.84 ? 2761 SER A CA    1 
ATOM   10277 C  C     . SER A 1 2761 ? 274.880 197.713 211.533 1.00 16.56 ? 2761 SER A C     1 
ATOM   10278 O  O     . SER A 1 2761 ? 275.390 196.692 212.004 1.00 17.50 ? 2761 SER A O     1 
ATOM   10279 C  CB    . SER A 1 2761 ? 275.999 199.470 212.909 1.00 24.17 ? 2761 SER A CB    1 
ATOM   10280 O  OG    . SER A 1 2761 ? 274.803 199.696 213.632 1.00 26.87 ? 2761 SER A OG    1 
ATOM   10281 N  N     . LEU A 1 2762 ? 273.628 197.739 211.075 1.00 19.10 ? 2762 LEU A N     1 
ATOM   10282 C  CA    . LEU A 1 2762 ? 272.768 196.564 211.102 1.00 14.40 ? 2762 LEU A CA    1 
ATOM   10283 C  C     . LEU A 1 2762 ? 272.487 196.004 209.712 1.00 15.10 ? 2762 LEU A C     1 
ATOM   10284 O  O     . LEU A 1 2762 ? 271.575 195.184 209.561 1.00 16.07 ? 2762 LEU A O     1 
ATOM   10285 C  CB    . LEU A 1 2762 ? 271.450 196.892 211.810 1.00 17.22 ? 2762 LEU A CB    1 
ATOM   10286 C  CG    . LEU A 1 2762 ? 271.541 197.110 213.323 1.00 15.73 ? 2762 LEU A CG    1 
ATOM   10287 C  CD1   . LEU A 1 2762 ? 270.162 197.358 213.911 1.00 13.40 ? 2762 LEU A CD1   1 
ATOM   10288 C  CD2   . LEU A 1 2762 ? 272.217 195.931 214.001 1.00 14.48 ? 2762 LEU A CD2   1 
ATOM   10289 N  N     . ARG A 1 2763 ? 273.249 196.419 208.698 1.00 20.15 ? 2763 ARG A N     1 
ATOM   10290 C  CA    . ARG A 1 2763 ? 273.011 195.941 207.335 1.00 16.82 ? 2763 ARG A CA    1 
ATOM   10291 C  C     . ARG A 1 2763 ? 273.229 194.436 207.223 1.00 14.01 ? 2763 ARG A C     1 
ATOM   10292 O  O     . ARG A 1 2763 ? 272.508 193.751 206.489 1.00 14.55 ? 2763 ARG A O     1 
ATOM   10293 C  CB    . ARG A 1 2763 ? 273.921 196.687 206.359 1.00 18.27 ? 2763 ARG A CB    1 
ATOM   10294 C  CG    . ARG A 1 2763 ? 273.669 196.375 204.891 1.00 25.44 ? 2763 ARG A CG    1 
ATOM   10295 C  CD    . ARG A 1 2763 ? 274.607 197.172 203.992 1.00 26.29 ? 2763 ARG A CD    1 
ATOM   10296 N  NE    . ARG A 1 2763 ? 274.371 198.609 204.075 1.00 26.71 ? 2763 ARG A NE    1 
ATOM   10297 C  CZ    . ARG A 1 2763 ? 273.456 199.256 203.367 1.00 31.13 ? 2763 ARG A CZ    1 
ATOM   10298 N  NH1   . ARG A 1 2763 ? 272.693 198.630 202.487 1.00 32.78 ? 2763 ARG A NH1   1 
ATOM   10299 N  NH2   . ARG A 1 2763 ? 273.313 200.568 203.537 1.00 31.64 ? 2763 ARG A NH2   1 
ATOM   10300 N  N     . THR A 1 2764 ? 274.220 193.908 207.942 1.00 14.07 ? 2764 THR A N     1 
ATOM   10301 C  CA    . THR A 1 2764 ? 274.568 192.495 207.822 1.00 12.63 ? 2764 THR A CA    1 
ATOM   10302 C  C     . THR A 1 2764 ? 273.426 191.586 208.262 1.00 10.52 ? 2764 THR A C     1 
ATOM   10303 O  O     . THR A 1 2764 ? 273.275 190.477 207.736 1.00 17.60 ? 2764 THR A O     1 
ATOM   10304 C  CB    . THR A 1 2764 ? 275.833 192.204 208.634 1.00 19.33 ? 2764 THR A CB    1 
ATOM   10305 O  OG1   . THR A 1 2764 ? 276.913 193.002 208.137 1.00 26.28 ? 2764 THR A OG1   1 
ATOM   10306 C  CG2   . THR A 1 2764 ? 276.224 190.740 208.538 1.00 15.79 ? 2764 THR A CG2   1 
ATOM   10307 N  N     . TYR A 1 2765 ? 272.602 192.035 209.207 1.00 11.45 ? 2765 TYR A N     1 
ATOM   10308 C  CA    . TYR A 1 2765 ? 271.549 191.197 209.764 1.00 10.33 ? 2765 TYR A CA    1 
ATOM   10309 C  C     . TYR A 1 2765 ? 270.262 191.212 208.940 1.00 6.62  ? 2765 TYR A C     1 
ATOM   10310 O  O     . TYR A 1 2765 ? 269.213 190.816 209.461 1.00 6.02  ? 2765 TYR A O     1 
ATOM   10311 C  CB    . TYR A 1 2765 ? 271.253 191.617 211.206 1.00 6.89  ? 2765 TYR A CB    1 
ATOM   10312 C  CG    . TYR A 1 2765 ? 272.457 191.572 212.115 1.00 7.37  ? 2765 TYR A CG    1 
ATOM   10313 C  CD1   . TYR A 1 2765 ? 272.950 190.364 212.583 1.00 8.83  ? 2765 TYR A CD1   1 
ATOM   10314 C  CD2   . TYR A 1 2765 ? 273.099 192.738 212.510 1.00 8.38  ? 2765 TYR A CD2   1 
ATOM   10315 C  CE1   . TYR A 1 2765 ? 274.050 190.314 213.414 1.00 9.18  ? 2765 TYR A CE1   1 
ATOM   10316 C  CE2   . TYR A 1 2765 ? 274.198 192.700 213.342 1.00 8.39  ? 2765 TYR A CE2   1 
ATOM   10317 C  CZ    . TYR A 1 2765 ? 274.669 191.484 213.792 1.00 9.98  ? 2765 TYR A CZ    1 
ATOM   10318 O  OH    . TYR A 1 2765 ? 275.764 191.437 214.621 1.00 19.83 ? 2765 TYR A OH    1 
ATOM   10319 N  N     . ALA A 1 2766 ? 270.310 191.645 207.680 1.00 7.99  ? 2766 ALA A N     1 
ATOM   10320 C  CA    . ALA A 1 2766 ? 269.096 191.692 206.868 1.00 6.13  ? 2766 ALA A CA    1 
ATOM   10321 C  C     . ALA A 1 2766 ? 268.590 190.291 206.542 1.00 5.47  ? 2766 ALA A C     1 
ATOM   10322 O  O     . ALA A 1 2766 ? 267.398 190.002 206.694 1.00 5.77  ? 2766 ALA A O     1 
ATOM   10323 C  CB    . ALA A 1 2766 ? 269.349 192.484 205.587 1.00 5.44  ? 2766 ALA A CB    1 
ATOM   10324 N  N     . GLU A 1 2767 ? 269.480 189.412 206.079 1.00 6.96  ? 2767 GLU A N     1 
ATOM   10325 C  CA    . GLU A 1 2767 ? 269.062 188.055 205.735 1.00 3.66  ? 2767 GLU A CA    1 
ATOM   10326 C  C     . GLU A 1 2767 ? 268.570 187.259 206.938 1.00 3.11  ? 2767 GLU A C     1 
ATOM   10327 O  O     . GLU A 1 2767 ? 267.488 186.653 206.844 1.00 3.53  ? 2767 GLU A O     1 
ATOM   10328 C  CB    . GLU A 1 2767 ? 270.201 187.333 205.006 1.00 8.17  ? 2767 GLU A CB    1 
ATOM   10329 C  CG    . GLU A 1 2767 ? 270.292 187.651 203.527 1.00 12.78 ? 2767 GLU A CG    1 
ATOM   10330 C  CD    . GLU A 1 2767 ? 271.626 187.255 202.928 1.00 28.46 ? 2767 GLU A CD    1 
ATOM   10331 O  OE1   . GLU A 1 2767 ? 271.772 187.343 201.690 1.00 31.81 ? 2767 GLU A OE1   1 
ATOM   10332 O  OE2   . GLU A 1 2767 ? 272.529 186.857 203.692 1.00 23.90 ? 2767 GLU A OE2   1 
ATOM   10333 N  N     . PRO A 1 2768 ? 269.285 187.193 208.071 1.00 6.68  ? 2768 PRO A N     1 
ATOM   10334 C  CA    . PRO A 1 2768 ? 268.727 186.472 209.229 1.00 2.82  ? 2768 PRO A CA    1 
ATOM   10335 C  C     . PRO A 1 2768 ? 267.431 187.067 209.752 1.00 1.84  ? 2768 PRO A C     1 
ATOM   10336 O  O     . PRO A 1 2768 ? 266.576 186.320 210.244 1.00 2.17  ? 2768 PRO A O     1 
ATOM   10337 C  CB    . PRO A 1 2768 ? 269.848 186.555 210.274 1.00 2.41  ? 2768 PRO A CB    1 
ATOM   10338 C  CG    . PRO A 1 2768 ? 270.707 187.675 209.838 1.00 4.35  ? 2768 PRO A CG    1 
ATOM   10339 C  CD    . PRO A 1 2768 ? 270.650 187.675 208.348 1.00 5.04  ? 2768 PRO A CD    1 
ATOM   10340 N  N     . LEU A 1 2769 ? 267.260 188.387 209.670 1.00 2.10  ? 2769 LEU A N     1 
ATOM   10341 C  CA    . LEU A 1 2769 ? 266.009 188.995 210.107 1.00 2.30  ? 2769 LEU A CA    1 
ATOM   10342 C  C     . LEU A 1 2769 ? 264.843 188.537 209.242 1.00 2.67  ? 2769 LEU A C     1 
ATOM   10343 O  O     . LEU A 1 2769 ? 263.762 188.227 209.757 1.00 3.98  ? 2769 LEU A O     1 
ATOM   10344 C  CB    . LEU A 1 2769 ? 266.126 190.519 210.084 1.00 2.87  ? 2769 LEU A CB    1 
ATOM   10345 C  CG    . LEU A 1 2769 ? 264.900 191.294 210.571 1.00 1.65  ? 2769 LEU A CG    1 
ATOM   10346 C  CD1   . LEU A 1 2769 ? 264.756 191.169 212.079 1.00 0.72  ? 2769 LEU A CD1   1 
ATOM   10347 C  CD2   . LEU A 1 2769 ? 264.981 192.748 210.150 1.00 1.71  ? 2769 LEU A CD2   1 
ATOM   10348 N  N     . THR A 1 2770 ? 265.044 188.489 207.922 1.00 2.01  ? 2770 THR A N     1 
ATOM   10349 C  CA    . THR A 1 2770 ? 264.005 187.985 207.031 1.00 1.33  ? 2770 THR A CA    1 
ATOM   10350 C  C     . THR A 1 2770 ? 263.733 186.507 207.282 1.00 1.51  ? 2770 THR A C     1 
ATOM   10351 O  O     . THR A 1 2770 ? 262.573 186.080 207.312 1.00 0.98  ? 2770 THR A O     1 
ATOM   10352 C  CB    . THR A 1 2770 ? 264.405 188.214 205.573 1.00 1.88  ? 2770 THR A CB    1 
ATOM   10353 O  OG1   . THR A 1 2770 ? 264.662 189.606 205.357 1.00 1.76  ? 2770 THR A OG1   1 
ATOM   10354 C  CG2   . THR A 1 2770 ? 263.298 187.758 204.634 1.00 0.71  ? 2770 THR A CG2   1 
ATOM   10355 N  N     . ALA A 1 2771 ? 264.792 185.715 207.467 1.00 1.48  ? 2771 ALA A N     1 
ATOM   10356 C  CA    . ALA A 1 2771 ? 264.621 184.282 207.682 1.00 1.83  ? 2771 ALA A CA    1 
ATOM   10357 C  C     . ALA A 1 2771 ? 263.849 184.003 208.963 1.00 2.31  ? 2771 ALA A C     1 
ATOM   10358 O  O     . ALA A 1 2771 ? 262.970 183.133 208.990 1.00 2.70  ? 2771 ALA A O     1 
ATOM   10359 C  CB    . ALA A 1 2771 ? 265.984 183.592 207.714 1.00 2.56  ? 2771 ALA A CB    1 
ATOM   10360 N  N     . ALA A 1 2772 ? 264.159 184.734 210.035 1.00 1.49  ? 2772 ALA A N     1 
ATOM   10361 C  CA    . ALA A 1 2772 ? 263.401 184.592 211.273 1.00 1.23  ? 2772 ALA A CA    1 
ATOM   10362 C  C     . ALA A 1 2772 ? 261.947 185.001 211.075 1.00 0.56  ? 2772 ALA A C     1 
ATOM   10363 O  O     . ALA A 1 2772 ? 261.035 184.359 211.608 1.00 0.66  ? 2772 ALA A O     1 
ATOM   10364 C  CB    . ALA A 1 2772 ? 264.052 185.416 212.384 1.00 1.02  ? 2772 ALA A CB    1 
ATOM   10365 N  N     . MET A 1 2773 ? 261.716 186.071 210.314 1.00 1.06  ? 2773 MET A N     1 
ATOM   10366 C  CA    . MET A 1 2773 ? 260.353 186.511 210.034 1.00 0.57  ? 2773 MET A CA    1 
ATOM   10367 C  C     . MET A 1 2773 ? 259.564 185.432 209.305 1.00 0.79  ? 2773 MET A C     1 
ATOM   10368 O  O     . MET A 1 2773 ? 258.431 185.113 209.679 1.00 0.66  ? 2773 MET A O     1 
ATOM   10369 C  CB    . MET A 1 2773 ? 260.386 187.794 209.207 1.00 0.58  ? 2773 MET A CB    1 
ATOM   10370 C  CG    . MET A 1 2773 ? 260.439 189.066 210.015 1.00 0.52  ? 2773 MET A CG    1 
ATOM   10371 S  SD    . MET A 1 2773 ? 260.384 190.519 208.956 1.00 7.16  ? 2773 MET A SD    1 
ATOM   10372 C  CE    . MET A 1 2773 ? 259.968 191.783 210.140 1.00 0.64  ? 2773 MET A CE    1 
ATOM   10373 N  N     . VAL A 1 2774 ? 260.157 184.853 208.259 1.00 2.17  ? 2774 VAL A N     1 
ATOM   10374 C  CA    . VAL A 1 2774 ? 259.459 183.843 207.469 1.00 1.02  ? 2774 VAL A CA    1 
ATOM   10375 C  C     . VAL A 1 2774 ? 259.230 182.582 208.293 1.00 0.98  ? 2774 VAL A C     1 
ATOM   10376 O  O     . VAL A 1 2774 ? 258.157 181.971 208.228 1.00 2.20  ? 2774 VAL A O     1 
ATOM   10377 C  CB    . VAL A 1 2774 ? 260.238 183.549 206.174 1.00 1.28  ? 2774 VAL A CB    1 
ATOM   10378 C  CG1   . VAL A 1 2774 ? 259.617 182.381 205.425 1.00 1.91  ? 2774 VAL A CG1   1 
ATOM   10379 C  CG2   . VAL A 1 2774 ? 260.280 184.783 205.289 1.00 0.66  ? 2774 VAL A CG2   1 
ATOM   10380 N  N     . GLU A 1 2775 ? 260.225 182.173 209.082 1.00 0.74  ? 2775 GLU A N     1 
ATOM   10381 C  CA    . GLU A 1 2775 ? 260.090 180.941 209.854 1.00 1.42  ? 2775 GLU A CA    1 
ATOM   10382 C  C     . GLU A 1 2775 ? 258.980 181.054 210.891 1.00 1.82  ? 2775 GLU A C     1 
ATOM   10383 O  O     . GLU A 1 2775 ? 258.121 180.171 210.993 1.00 2.40  ? 2775 GLU A O     1 
ATOM   10384 C  CB    . GLU A 1 2775 ? 261.416 180.587 210.525 1.00 4.37  ? 2775 GLU A CB    1 
ATOM   10385 C  CG    . GLU A 1 2775 ? 261.359 179.271 211.279 1.00 3.60  ? 2775 GLU A CG    1 
ATOM   10386 C  CD    . GLU A 1 2775 ? 262.680 178.891 211.900 1.00 11.78 ? 2775 GLU A CD    1 
ATOM   10387 O  OE1   . GLU A 1 2775 ? 263.648 179.663 211.759 1.00 14.99 ? 2775 GLU A OE1   1 
ATOM   10388 O  OE2   . GLU A 1 2775 ? 262.755 177.812 212.525 1.00 18.48 ? 2775 GLU A OE2   1 
ATOM   10389 N  N     . PHE A 1 2776 ? 258.978 182.135 211.675 1.00 0.71  ? 2776 PHE A N     1 
ATOM   10390 C  CA    . PHE A 1 2776 ? 257.956 182.275 212.705 1.00 0.67  ? 2776 PHE A CA    1 
ATOM   10391 C  C     . PHE A 1 2776 ? 256.573 182.469 212.094 1.00 0.88  ? 2776 PHE A C     1 
ATOM   10392 O  O     . PHE A 1 2776 ? 255.582 181.941 212.614 1.00 1.21  ? 2776 PHE A O     1 
ATOM   10393 C  CB    . PHE A 1 2776 ? 258.287 183.430 213.649 1.00 0.78  ? 2776 PHE A CB    1 
ATOM   10394 C  CG    . PHE A 1 2776 ? 257.327 183.548 214.791 1.00 1.03  ? 2776 PHE A CG    1 
ATOM   10395 C  CD1   . PHE A 1 2776 ? 257.418 182.694 215.877 1.00 2.23  ? 2776 PHE A CD1   1 
ATOM   10396 C  CD2   . PHE A 1 2776 ? 256.306 184.482 214.763 1.00 0.47  ? 2776 PHE A CD2   1 
ATOM   10397 C  CE1   . PHE A 1 2776 ? 256.521 182.784 216.920 1.00 2.64  ? 2776 PHE A CE1   1 
ATOM   10398 C  CE2   . PHE A 1 2776 ? 255.411 184.576 215.804 1.00 0.91  ? 2776 PHE A CE2   1 
ATOM   10399 C  CZ    . PHE A 1 2776 ? 255.517 183.724 216.883 1.00 2.02  ? 2776 PHE A CZ    1 
ATOM   10400 N  N     . TYR A 1 2777 ? 256.482 183.232 211.003 1.00 1.01  ? 2777 TYR A N     1 
ATOM   10401 C  CA    . TYR A 1 2777 ? 255.192 183.431 210.350 1.00 0.78  ? 2777 TYR A CA    1 
ATOM   10402 C  C     . TYR A 1 2777 ? 254.638 182.117 209.816 1.00 0.96  ? 2777 TYR A C     1 
ATOM   10403 O  O     . TYR A 1 2777 ? 253.440 181.839 209.950 1.00 1.17  ? 2777 TYR A O     1 
ATOM   10404 C  CB    . TYR A 1 2777 ? 255.323 184.451 209.222 1.00 0.59  ? 2777 TYR A CB    1 
ATOM   10405 C  CG    . TYR A 1 2777 ? 254.241 184.337 208.177 1.00 0.65  ? 2777 TYR A CG    1 
ATOM   10406 C  CD1   . TYR A 1 2777 ? 252.951 184.776 208.438 1.00 0.71  ? 2777 TYR A CD1   1 
ATOM   10407 C  CD2   . TYR A 1 2777 ? 254.504 183.782 206.932 1.00 0.78  ? 2777 TYR A CD2   1 
ATOM   10408 C  CE1   . TYR A 1 2777 ? 251.957 184.668 207.493 1.00 0.82  ? 2777 TYR A CE1   1 
ATOM   10409 C  CE2   . TYR A 1 2777 ? 253.514 183.674 205.978 1.00 0.64  ? 2777 TYR A CE2   1 
ATOM   10410 C  CZ    . TYR A 1 2777 ? 252.243 184.119 206.265 1.00 0.60  ? 2777 TYR A CZ    1 
ATOM   10411 O  OH    . TYR A 1 2777 ? 251.250 184.013 205.321 1.00 3.45  ? 2777 TYR A OH    1 
ATOM   10412 N  N     . THR A 1 2778 ? 255.491 181.300 209.193 1.00 1.00  ? 2778 THR A N     1 
ATOM   10413 C  CA    . THR A 1 2778 ? 255.045 180.007 208.686 1.00 1.14  ? 2778 THR A CA    1 
ATOM   10414 C  C     . THR A 1 2778 ? 254.624 179.086 209.824 1.00 1.18  ? 2778 THR A C     1 
ATOM   10415 O  O     . THR A 1 2778 ? 253.603 178.394 209.730 1.00 1.51  ? 2778 THR A O     1 
ATOM   10416 C  CB    . THR A 1 2778 ? 256.150 179.356 207.853 1.00 1.00  ? 2778 THR A CB    1 
ATOM   10417 O  OG1   . THR A 1 2778 ? 256.551 180.250 206.809 1.00 1.18  ? 2778 THR A OG1   1 
ATOM   10418 C  CG2   . THR A 1 2778 ? 255.658 178.059 207.234 1.00 4.63  ? 2778 THR A CG2   1 
ATOM   10419 N  N     . MET A 1 2779 ? 255.400 179.067 210.911 1.00 1.58  ? 2779 MET A N     1 
ATOM   10420 C  CA    . MET A 1 2779 ? 255.058 178.229 212.054 1.00 0.97  ? 2779 MET A CA    1 
ATOM   10421 C  C     . MET A 1 2779 ? 253.736 178.655 212.678 1.00 1.68  ? 2779 MET A C     1 
ATOM   10422 O  O     . MET A 1 2779 ? 252.908 177.807 213.031 1.00 3.57  ? 2779 MET A O     1 
ATOM   10423 C  CB    . MET A 1 2779 ? 256.181 178.278 213.090 1.00 0.92  ? 2779 MET A CB    1 
ATOM   10424 C  CG    . MET A 1 2779 ? 257.398 177.455 212.713 1.00 1.84  ? 2779 MET A CG    1 
ATOM   10425 S  SD    . MET A 1 2779 ? 258.890 177.975 213.580 1.00 16.87 ? 2779 MET A SD    1 
ATOM   10426 C  CE    . MET A 1 2779 ? 258.263 178.176 215.241 1.00 5.57  ? 2779 MET A CE    1 
ATOM   10427 N  N     . SER A 1 2780 ? 253.521 179.963 212.824 1.00 1.27  ? 2780 SER A N     1 
ATOM   10428 C  CA    . SER A 1 2780 ? 252.271 180.450 213.397 1.00 1.34  ? 2780 SER A CA    1 
ATOM   10429 C  C     . SER A 1 2780 ? 251.087 180.137 212.492 1.00 1.78  ? 2780 SER A C     1 
ATOM   10430 O  O     . SER A 1 2780 ? 250.008 179.774 212.974 1.00 3.69  ? 2780 SER A O     1 
ATOM   10431 C  CB    . SER A 1 2780 ? 252.363 181.952 213.660 1.00 2.45  ? 2780 SER A CB    1 
ATOM   10432 O  OG    . SER A 1 2780 ? 253.472 182.261 214.483 1.00 3.03  ? 2780 SER A OG    1 
ATOM   10433 N  N     . GLN A 1 2781 ? 251.272 180.274 211.178 1.00 1.89  ? 2781 GLN A N     1 
ATOM   10434 C  CA    . GLN A 1 2781 ? 250.189 180.001 210.243 1.00 1.39  ? 2781 GLN A CA    1 
ATOM   10435 C  C     . GLN A 1 2781 ? 249.799 178.527 210.272 1.00 2.31  ? 2781 GLN A C     1 
ATOM   10436 O  O     . GLN A 1 2781 ? 248.621 178.185 210.122 1.00 3.16  ? 2781 GLN A O     1 
ATOM   10437 C  CB    . GLN A 1 2781 ? 250.599 180.437 208.837 1.00 1.60  ? 2781 GLN A CB    1 
ATOM   10438 C  CG    . GLN A 1 2781 ? 249.508 180.321 207.794 1.00 1.82  ? 2781 GLN A CG    1 
ATOM   10439 C  CD    . GLN A 1 2781 ? 249.963 180.803 206.434 1.00 4.95  ? 2781 GLN A CD    1 
ATOM   10440 O  OE1   . GLN A 1 2781 ? 250.985 180.353 205.916 1.00 10.03 ? 2781 GLN A OE1   1 
ATOM   10441 N  NE2   . GLN A 1 2781 ? 249.208 181.723 205.847 1.00 2.63  ? 2781 GLN A NE2   1 
ATOM   10442 N  N     . GLU A 1 2782 ? 250.778 177.641 210.458 1.00 2.90  ? 2782 GLU A N     1 
ATOM   10443 C  CA    . GLU A 1 2782 ? 250.485 176.222 210.605 1.00 2.51  ? 2782 GLU A CA    1 
ATOM   10444 C  C     . GLU A 1 2782 ? 249.892 175.914 211.973 1.00 4.09  ? 2782 GLU A C     1 
ATOM   10445 O  O     . GLU A 1 2782 ? 248.931 175.144 212.078 1.00 4.75  ? 2782 GLU A O     1 
ATOM   10446 C  CB    . GLU A 1 2782 ? 251.761 175.407 210.360 1.00 2.13  ? 2782 GLU A CB    1 
ATOM   10447 C  CG    . GLU A 1 2782 ? 251.636 173.889 210.512 1.00 9.10  ? 2782 GLU A CG    1 
ATOM   10448 C  CD    . GLU A 1 2782 ? 251.665 173.415 211.953 1.00 17.80 ? 2782 GLU A CD    1 
ATOM   10449 O  OE1   . GLU A 1 2782 ? 252.575 173.832 212.702 1.00 19.20 ? 2782 GLU A OE1   1 
ATOM   10450 O  OE2   . GLU A 1 2782 ? 250.780 172.622 212.336 1.00 21.23 ? 2782 GLU A OE2   1 
ATOM   10451 N  N     . ARG A 1 2783 ? 250.452 176.505 213.031 1.00 3.13  ? 2783 ARG A N     1 
ATOM   10452 C  CA    . ARG A 1 2783 ? 250.027 176.186 214.390 1.00 2.83  ? 2783 ARG A CA    1 
ATOM   10453 C  C     . ARG A 1 2783 ? 248.583 176.604 214.644 1.00 2.92  ? 2783 ARG A C     1 
ATOM   10454 O  O     . ARG A 1 2783 ? 247.818 175.861 215.269 1.00 8.44  ? 2783 ARG A O     1 
ATOM   10455 C  CB    . ARG A 1 2783 ? 250.967 176.853 215.394 1.00 4.03  ? 2783 ARG A CB    1 
ATOM   10456 C  CG    . ARG A 1 2783 ? 250.546 176.736 216.848 1.00 3.38  ? 2783 ARG A CG    1 
ATOM   10457 C  CD    . ARG A 1 2783 ? 250.790 175.352 217.417 1.00 3.05  ? 2783 ARG A CD    1 
ATOM   10458 N  NE    . ARG A 1 2783 ? 250.553 175.305 218.857 1.00 6.69  ? 2783 ARG A NE    1 
ATOM   10459 C  CZ    . ARG A 1 2783 ? 249.362 175.404 219.435 1.00 9.55  ? 2783 ARG A CZ    1 
ATOM   10460 N  NH1   . ARG A 1 2783 ? 248.252 175.526 218.724 1.00 7.95  ? 2783 ARG A NH1   1 
ATOM   10461 N  NH2   . ARG A 1 2783 ? 249.283 175.375 220.762 1.00 8.37  ? 2783 ARG A NH2   1 
ATOM   10462 N  N     . PHE A 1 2784 ? 248.190 177.785 214.177 1.00 2.27  ? 2784 PHE A N     1 
ATOM   10463 C  CA    . PHE A 1 2784 ? 246.859 178.327 214.424 1.00 1.95  ? 2784 PHE A CA    1 
ATOM   10464 C  C     . PHE A 1 2784 ? 246.123 178.474 213.104 1.00 3.06  ? 2784 PHE A C     1 
ATOM   10465 O  O     . PHE A 1 2784 ? 246.615 179.134 212.183 1.00 9.15  ? 2784 PHE A O     1 
ATOM   10466 C  CB    . PHE A 1 2784 ? 246.943 179.668 215.155 1.00 2.12  ? 2784 PHE A CB    1 
ATOM   10467 C  CG    . PHE A 1 2784 ? 247.846 179.645 216.350 1.00 1.70  ? 2784 PHE A CG    1 
ATOM   10468 C  CD1   . PHE A 1 2784 ? 247.497 178.930 217.480 1.00 1.74  ? 2784 PHE A CD1   1 
ATOM   10469 C  CD2   . PHE A 1 2784 ? 249.047 180.330 216.344 1.00 2.60  ? 2784 PHE A CD2   1 
ATOM   10470 C  CE1   . PHE A 1 2784 ? 248.324 178.901 218.582 1.00 2.30  ? 2784 PHE A CE1   1 
ATOM   10471 C  CE2   . PHE A 1 2784 ? 249.878 180.304 217.445 1.00 2.92  ? 2784 PHE A CE2   1 
ATOM   10472 C  CZ    . PHE A 1 2784 ? 249.516 179.593 218.565 1.00 1.90  ? 2784 PHE A CZ    1 
ATOM   10473 N  N     . THR A 1 2785 ? 244.945 177.863 213.015 1.00 2.57  ? 2785 THR A N     1 
ATOM   10474 C  CA    . THR A 1 2785 ? 244.152 177.835 211.796 1.00 2.81  ? 2785 THR A CA    1 
ATOM   10475 C  C     . THR A 1 2785 ? 242.707 178.185 212.124 1.00 3.35  ? 2785 THR A C     1 
ATOM   10476 O  O     . THR A 1 2785 ? 242.321 178.294 213.291 1.00 3.46  ? 2785 THR A O     1 
ATOM   10477 C  CB    . THR A 1 2785 ? 244.223 176.460 211.109 1.00 4.47  ? 2785 THR A CB    1 
ATOM   10478 O  OG1   . THR A 1 2785 ? 243.643 175.466 211.962 1.00 4.49  ? 2785 THR A OG1   1 
ATOM   10479 C  CG2   . THR A 1 2785 ? 245.664 176.081 210.807 1.00 1.83  ? 2785 THR A CG2   1 
ATOM   10480 N  N     . GLN A 1 2786 ? 241.903 178.355 211.072 1.00 4.90  ? 2786 GLN A N     1 
ATOM   10481 C  CA    . GLN A 1 2786 ? 240.495 178.688 211.254 1.00 3.99  ? 2786 GLN A CA    1 
ATOM   10482 C  C     . GLN A 1 2786 ? 239.718 177.575 211.942 1.00 6.05  ? 2786 GLN A C     1 
ATOM   10483 O  O     . GLN A 1 2786 ? 238.611 177.822 212.432 1.00 9.43  ? 2786 GLN A O     1 
ATOM   10484 C  CB    . GLN A 1 2786 ? 239.840 179.009 209.910 1.00 6.59  ? 2786 GLN A CB    1 
ATOM   10485 C  CG    . GLN A 1 2786 ? 240.183 180.376 209.354 1.00 11.57 ? 2786 GLN A CG    1 
ATOM   10486 C  CD    . GLN A 1 2786 ? 239.240 180.803 208.245 1.00 14.26 ? 2786 GLN A CD    1 
ATOM   10487 O  OE1   . GLN A 1 2786 ? 239.637 180.910 207.087 1.00 21.52 ? 2786 GLN A OE1   1 
ATOM   10488 N  NE2   . GLN A 1 2786 ? 237.985 181.056 208.599 1.00 10.89 ? 2786 GLN A NE2   1 
ATOM   10489 N  N     . ASP A 1 2787 ? 240.263 176.357 211.980 1.00 6.27  ? 2787 ASP A N     1 
ATOM   10490 C  CA    . ASP A 1 2787 ? 239.585 175.266 212.670 1.00 5.00  ? 2787 ASP A CA    1 
ATOM   10491 C  C     . ASP A 1 2787 ? 239.484 175.537 214.165 1.00 8.57  ? 2787 ASP A C     1 
ATOM   10492 O  O     . ASP A 1 2787 ? 238.447 175.267 214.782 1.00 7.65  ? 2787 ASP A O     1 
ATOM   10493 C  CB    . ASP A 1 2787 ? 240.314 173.947 212.410 1.00 6.04  ? 2787 ASP A CB    1 
ATOM   10494 C  CG    . ASP A 1 2787 ? 240.463 173.645 210.933 1.00 23.05 ? 2787 ASP A CG    1 
ATOM   10495 O  OD1   . ASP A 1 2787 ? 239.465 173.231 210.305 1.00 21.23 ? 2787 ASP A OD1   1 
ATOM   10496 O  OD2   . ASP A 1 2787 ? 241.578 173.820 210.399 1.00 27.17 ? 2787 ASP A OD2   1 
ATOM   10497 N  N     . THR A 1 2788 ? 240.549 176.070 214.766 1.00 5.74  ? 2788 THR A N     1 
ATOM   10498 C  CA    . THR A 1 2788 ? 240.527 176.365 216.194 1.00 4.40  ? 2788 THR A CA    1 
ATOM   10499 C  C     . THR A 1 2788 ? 239.648 177.576 216.485 1.00 5.41  ? 2788 THR A C     1 
ATOM   10500 O  O     . THR A 1 2788 ? 238.675 177.483 217.243 1.00 5.92  ? 2788 THR A O     1 
ATOM   10501 C  CB    . THR A 1 2788 ? 241.953 176.590 216.706 1.00 6.57  ? 2788 THR A CB    1 
ATOM   10502 O  OG1   . THR A 1 2788 ? 242.641 175.338 216.776 1.00 17.88 ? 2788 THR A OG1   1 
ATOM   10503 C  CG2   . THR A 1 2788 ? 241.927 177.210 218.092 1.00 4.56  ? 2788 THR A CG2   1 
ATOM   10504 N  N     . GLN A 1 2789 ? 239.973 178.719 215.892 1.00 5.59  ? 2789 GLN A N     1 
ATOM   10505 C  CA    . GLN A 1 2789 ? 239.207 179.939 216.077 1.00 5.69  ? 2789 GLN A CA    1 
ATOM   10506 C  C     . GLN A 1 2789 ? 238.950 180.601 214.733 1.00 5.67  ? 2789 GLN A C     1 
ATOM   10507 O  O     . GLN A 1 2789 ? 239.789 180.532 213.831 1.00 6.72  ? 2789 GLN A O     1 
ATOM   10508 C  CB    . GLN A 1 2789 ? 239.937 180.920 217.007 1.00 2.62  ? 2789 GLN A CB    1 
ATOM   10509 C  CG    . GLN A 1 2789 ? 240.178 180.376 218.402 1.00 2.26  ? 2789 GLN A CG    1 
ATOM   10510 C  CD    . GLN A 1 2789 ? 238.927 180.380 219.259 1.00 5.08  ? 2789 GLN A CD    1 
ATOM   10511 O  OE1   . GLN A 1 2789 ? 237.918 180.989 218.909 1.00 5.06  ? 2789 GLN A OE1   1 
ATOM   10512 N  NE2   . GLN A 1 2789 ? 238.987 179.689 220.390 1.00 3.22  ? 2789 GLN A NE2   1 
ATOM   10513 N  N     . PRO A 1 2790 ? 237.796 181.258 214.574 1.00 7.72  ? 2790 PRO A N     1 
ATOM   10514 C  CA    . PRO A 1 2790 ? 237.451 181.844 213.270 1.00 4.22  ? 2790 PRO A CA    1 
ATOM   10515 C  C     . PRO A 1 2790 ? 238.344 182.993 212.845 1.00 3.19  ? 2790 PRO A C     1 
ATOM   10516 O  O     . PRO A 1 2790 ? 238.330 183.345 211.661 1.00 8.61  ? 2790 PRO A O     1 
ATOM   10517 C  CB    . PRO A 1 2790 ? 236.008 182.318 213.478 1.00 4.69  ? 2790 PRO A CB    1 
ATOM   10518 C  CG    . PRO A 1 2790 ? 235.934 182.599 214.934 1.00 8.24  ? 2790 PRO A CG    1 
ATOM   10519 C  CD    . PRO A 1 2790 ? 236.752 181.517 215.579 1.00 4.74  ? 2790 PRO A CD    1 
ATOM   10520 N  N     . HIS A 1 2791 ? 239.095 183.600 213.760 1.00 2.86  ? 2791 HIS A N     1 
ATOM   10521 C  CA    . HIS A 1 2791 ? 239.945 184.738 213.442 1.00 1.66  ? 2791 HIS A CA    1 
ATOM   10522 C  C     . HIS A 1 2791 ? 241.421 184.370 213.383 1.00 1.74  ? 2791 HIS A C     1 
ATOM   10523 O  O     . HIS A 1 2791 ? 242.274 185.262 213.374 1.00 5.42  ? 2791 HIS A O     1 
ATOM   10524 C  CB    . HIS A 1 2791 ? 239.716 185.866 214.452 1.00 1.50  ? 2791 HIS A CB    1 
ATOM   10525 C  CG    . HIS A 1 2791 ? 240.117 185.521 215.850 1.00 1.24  ? 2791 HIS A CG    1 
ATOM   10526 N  ND1   . HIS A 1 2791 ? 239.358 184.708 216.664 1.00 1.74  ? 2791 HIS A ND1   1 
ATOM   10527 C  CD2   . HIS A 1 2791 ? 241.194 185.885 216.583 1.00 0.98  ? 2791 HIS A CD2   1 
ATOM   10528 C  CE1   . HIS A 1 2791 ? 239.953 184.583 217.837 1.00 1.14  ? 2791 HIS A CE1   1 
ATOM   10529 N  NE2   . HIS A 1 2791 ? 241.070 185.288 217.813 1.00 0.53  ? 2791 HIS A NE2   1 
ATOM   10530 N  N     . TYR A 1 2792 ? 241.745 183.078 213.344 1.00 2.23  ? 2792 TYR A N     1 
ATOM   10531 C  CA    . TYR A 1 2792 ? 243.133 182.629 213.241 1.00 2.53  ? 2792 TYR A CA    1 
ATOM   10532 C  C     . TYR A 1 2792 ? 243.529 182.536 211.767 1.00 3.28  ? 2792 TYR A C     1 
ATOM   10533 O  O     . TYR A 1 2792 ? 243.745 181.462 211.205 1.00 5.93  ? 2792 TYR A O     1 
ATOM   10534 C  CB    . TYR A 1 2792 ? 243.317 181.294 213.953 1.00 2.30  ? 2792 TYR A CB    1 
ATOM   10535 C  CG    . TYR A 1 2792 ? 243.367 181.373 215.463 1.00 2.24  ? 2792 TYR A CG    1 
ATOM   10536 C  CD1   . TYR A 1 2792 ? 243.122 182.567 216.132 1.00 1.74  ? 2792 TYR A CD1   1 
ATOM   10537 C  CD2   . TYR A 1 2792 ? 243.654 180.247 216.221 1.00 1.79  ? 2792 TYR A CD2   1 
ATOM   10538 C  CE1   . TYR A 1 2792 ? 243.168 182.634 217.511 1.00 1.03  ? 2792 TYR A CE1   1 
ATOM   10539 C  CE2   . TYR A 1 2792 ? 243.702 180.304 217.597 1.00 2.01  ? 2792 TYR A CE2   1 
ATOM   10540 C  CZ    . TYR A 1 2792 ? 243.459 181.497 218.240 1.00 2.55  ? 2792 TYR A CZ    1 
ATOM   10541 O  OH    . TYR A 1 2792 ? 243.507 181.548 219.611 1.00 2.66  ? 2792 TYR A OH    1 
ATOM   10542 N  N     . ILE A 1 2793 ? 243.612 183.703 211.135 1.00 3.26  ? 2793 ILE A N     1 
ATOM   10543 C  CA    . ILE A 1 2793 ? 244.053 183.825 209.751 1.00 2.38  ? 2793 ILE A CA    1 
ATOM   10544 C  C     . ILE A 1 2793 ? 245.350 184.614 209.757 1.00 2.18  ? 2793 ILE A C     1 
ATOM   10545 O  O     . ILE A 1 2793 ? 245.376 185.782 210.163 1.00 4.14  ? 2793 ILE A O     1 
ATOM   10546 C  CB    . ILE A 1 2793 ? 243.005 184.503 208.855 1.00 4.89  ? 2793 ILE A CB    1 
ATOM   10547 C  CG1   . ILE A 1 2793 ? 241.720 183.680 208.780 1.00 3.34  ? 2793 ILE A CG1   1 
ATOM   10548 C  CG2   . ILE A 1 2793 ? 243.570 184.740 207.463 1.00 5.00  ? 2793 ILE A CG2   1 
ATOM   10549 C  CD1   . ILE A 1 2793 ? 240.727 184.007 209.852 1.00 8.29  ? 2793 ILE A CD1   1 
ATOM   10550 N  N     . TYR A 1 2794 ? 246.423 183.985 209.299 1.00 1.81  ? 2794 TYR A N     1 
ATOM   10551 C  CA    . TYR A 1 2794 ? 247.714 184.636 209.163 1.00 1.05  ? 2794 TYR A CA    1 
ATOM   10552 C  C     . TYR A 1 2794 ? 248.084 184.684 207.690 1.00 1.06  ? 2794 TYR A C     1 
ATOM   10553 O  O     . TYR A 1 2794 ? 248.008 183.669 206.991 1.00 3.28  ? 2794 TYR A O     1 
ATOM   10554 C  CB    . TYR A 1 2794 ? 248.782 183.912 209.982 1.00 1.22  ? 2794 TYR A CB    1 
ATOM   10555 C  CG    . TYR A 1 2794 ? 248.507 183.952 211.468 1.00 2.82  ? 2794 TYR A CG    1 
ATOM   10556 C  CD1   . TYR A 1 2794 ? 248.817 185.078 212.219 1.00 2.51  ? 2794 TYR A CD1   1 
ATOM   10557 C  CD2   . TYR A 1 2794 ? 247.920 182.875 212.114 1.00 1.83  ? 2794 TYR A CD2   1 
ATOM   10558 C  CE1   . TYR A 1 2794 ? 248.561 185.125 213.574 1.00 2.40  ? 2794 TYR A CE1   1 
ATOM   10559 C  CE2   . TYR A 1 2794 ? 247.661 182.912 213.468 1.00 1.46  ? 2794 TYR A CE2   1 
ATOM   10560 C  CZ    . TYR A 1 2794 ? 247.984 184.039 214.193 1.00 4.13  ? 2794 TYR A CZ    1 
ATOM   10561 O  OH    . TYR A 1 2794 ? 247.728 184.079 215.543 1.00 9.18  ? 2794 TYR A OH    1 
ATOM   10562 N  N     . SER A 1 2795 ? 248.468 185.862 207.226 1.00 0.90  ? 2795 SER A N     1 
ATOM   10563 C  CA    . SER A 1 2795 ? 248.714 186.111 205.815 1.00 0.58  ? 2795 SER A CA    1 
ATOM   10564 C  C     . SER A 1 2795 ? 249.941 187.002 205.676 1.00 0.63  ? 2795 SER A C     1 
ATOM   10565 O  O     . SER A 1 2795 ? 250.478 187.467 206.687 1.00 0.79  ? 2795 SER A O     1 
ATOM   10566 C  CB    . SER A 1 2795 ? 247.484 186.758 205.174 1.00 0.51  ? 2795 SER A CB    1 
ATOM   10567 O  OG    . SER A 1 2795 ? 247.205 188.020 205.748 1.00 0.66  ? 2795 SER A OG    1 
ATOM   10568 N  N     . PRO A 1 2796 ? 250.423 187.260 204.454 1.00 0.73  ? 2796 PRO A N     1 
ATOM   10569 C  CA    . PRO A 1 2796 ? 251.498 188.250 204.285 1.00 0.68  ? 2796 PRO A CA    1 
ATOM   10570 C  C     . PRO A 1 2796 ? 251.134 189.645 204.764 1.00 0.28  ? 2796 PRO A C     1 
ATOM   10571 O  O     . PRO A 1 2796 ? 252.020 190.506 204.823 1.00 0.37  ? 2796 PRO A O     1 
ATOM   10572 C  CB    . PRO A 1 2796 ? 251.754 188.228 202.774 1.00 0.29  ? 2796 PRO A CB    1 
ATOM   10573 C  CG    . PRO A 1 2796 ? 251.397 186.850 202.380 1.00 0.37  ? 2796 PRO A CG    1 
ATOM   10574 C  CD    . PRO A 1 2796 ? 250.203 186.492 203.214 1.00 0.25  ? 2796 PRO A CD    1 
ATOM   10575 N  N     . ARG A 1 2797 ? 249.869 189.896 205.105 1.00 0.39  ? 2797 ARG A N     1 
ATOM   10576 C  CA    . ARG A 1 2797 ? 249.505 191.166 205.724 1.00 1.22  ? 2797 ARG A CA    1 
ATOM   10577 C  C     . ARG A 1 2797 ? 250.212 191.341 207.062 1.00 1.60  ? 2797 ARG A C     1 
ATOM   10578 O  O     . ARG A 1 2797 ? 250.653 192.446 207.398 1.00 2.51  ? 2797 ARG A O     1 
ATOM   10579 C  CB    . ARG A 1 2797 ? 247.989 191.246 205.898 1.00 0.68  ? 2797 ARG A CB    1 
ATOM   10580 C  CG    . ARG A 1 2797 ? 247.288 191.948 204.756 1.00 0.83  ? 2797 ARG A CG    1 
ATOM   10581 C  CD    . ARG A 1 2797 ? 245.866 192.321 205.115 1.00 2.20  ? 2797 ARG A CD    1 
ATOM   10582 N  NE    . ARG A 1 2797 ? 245.027 191.152 205.343 1.00 5.06  ? 2797 ARG A NE    1 
ATOM   10583 C  CZ    . ARG A 1 2797 ? 243.999 190.812 204.577 1.00 3.21  ? 2797 ARG A CZ    1 
ATOM   10584 N  NH1   . ARG A 1 2797 ? 243.680 191.510 203.500 1.00 2.92  ? 2797 ARG A NH1   1 
ATOM   10585 N  NH2   . ARG A 1 2797 ? 243.277 189.743 204.898 1.00 0.91  ? 2797 ARG A NH2   1 
ATOM   10586 N  N     . GLU A 1 2798 ? 250.326 190.262 207.838 1.00 1.27  ? 2798 GLU A N     1 
ATOM   10587 C  CA    . GLU A 1 2798 ? 251.102 190.312 209.074 1.00 1.13  ? 2798 GLU A CA    1 
ATOM   10588 C  C     . GLU A 1 2798 ? 252.576 190.565 208.792 1.00 0.72  ? 2798 GLU A C     1 
ATOM   10589 O  O     . GLU A 1 2798 ? 253.242 191.283 209.546 1.00 1.11  ? 2798 GLU A O     1 
ATOM   10590 C  CB    . GLU A 1 2798 ? 250.919 189.012 209.860 1.00 0.98  ? 2798 GLU A CB    1 
ATOM   10591 C  CG    . GLU A 1 2798 ? 249.699 189.008 210.767 1.00 1.42  ? 2798 GLU A CG    1 
ATOM   10592 C  CD    . GLU A 1 2798 ? 248.401 189.169 210.005 1.00 8.90  ? 2798 GLU A CD    1 
ATOM   10593 O  OE1   . GLU A 1 2798 ? 248.031 188.247 209.251 1.00 4.50  ? 2798 GLU A OE1   1 
ATOM   10594 O  OE2   . GLU A 1 2798 ? 247.755 190.228 210.155 1.00 17.30 ? 2798 GLU A OE2   1 
ATOM   10595 N  N     . MET A 1 2799 ? 253.105 189.982 207.714 1.00 1.07  ? 2799 MET A N     1 
ATOM   10596 C  CA    . MET A 1 2799 ? 254.487 190.252 207.330 1.00 0.52  ? 2799 MET A CA    1 
ATOM   10597 C  C     . MET A 1 2799 ? 254.682 191.720 206.965 1.00 0.66  ? 2799 MET A C     1 
ATOM   10598 O  O     . MET A 1 2799 ? 255.696 192.326 207.325 1.00 0.87  ? 2799 MET A O     1 
ATOM   10599 C  CB    . MET A 1 2799 ? 254.892 189.350 206.167 1.00 0.41  ? 2799 MET A CB    1 
ATOM   10600 C  CG    . MET A 1 2799 ? 254.927 187.867 206.498 1.00 1.07  ? 2799 MET A CG    1 
ATOM   10601 S  SD    . MET A 1 2799 ? 256.304 187.410 207.565 1.00 11.93 ? 2799 MET A SD    1 
ATOM   10602 C  CE    . MET A 1 2799 ? 257.698 187.897 206.555 1.00 0.28  ? 2799 MET A CE    1 
ATOM   10603 N  N     . THR A 1 2800 ? 253.722 192.305 206.248 1.00 0.71  ? 2800 THR A N     1 
ATOM   10604 C  CA    . THR A 1 2800 ? 253.807 193.720 205.903 1.00 0.56  ? 2800 THR A CA    1 
ATOM   10605 C  C     . THR A 1 2800 ? 253.745 194.593 207.151 1.00 0.72  ? 2800 THR A C     1 
ATOM   10606 O  O     . THR A 1 2800 ? 254.505 195.559 207.286 1.00 1.15  ? 2800 THR A O     1 
ATOM   10607 C  CB    . THR A 1 2800 ? 252.691 194.087 204.924 1.00 0.84  ? 2800 THR A CB    1 
ATOM   10608 O  OG1   . THR A 1 2800 ? 252.772 193.244 203.771 1.00 0.80  ? 2800 THR A OG1   1 
ATOM   10609 C  CG2   . THR A 1 2800 ? 252.808 195.539 204.491 1.00 1.23  ? 2800 THR A CG2   1 
ATOM   10610 N  N     . ARG A 1 2801 ? 252.844 194.263 208.079 1.00 0.64  ? 2801 ARG A N     1 
ATOM   10611 C  CA    . ARG A 1 2801 ? 252.773 194.999 209.338 1.00 0.58  ? 2801 ARG A CA    1 
ATOM   10612 C  C     . ARG A 1 2801 ? 254.023 194.775 210.179 1.00 0.92  ? 2801 ARG A C     1 
ATOM   10613 O  O     . ARG A 1 2801 ? 254.466 195.676 210.898 1.00 0.98  ? 2801 ARG A O     1 
ATOM   10614 C  CB    . ARG A 1 2801 ? 251.521 194.587 210.112 1.00 0.78  ? 2801 ARG A CB    1 
ATOM   10615 C  CG    . ARG A 1 2801 ? 250.237 195.184 209.571 1.00 6.97  ? 2801 ARG A CG    1 
ATOM   10616 C  CD    . ARG A 1 2801 ? 249.042 194.302 209.877 1.00 9.72  ? 2801 ARG A CD    1 
ATOM   10617 N  NE    . ARG A 1 2801 ? 247.851 194.728 209.150 1.00 19.73 ? 2801 ARG A NE    1 
ATOM   10618 C  CZ    . ARG A 1 2801 ? 246.792 193.961 208.932 1.00 13.53 ? 2801 ARG A CZ    1 
ATOM   10619 N  NH1   . ARG A 1 2801 ? 246.740 192.714 209.371 1.00 11.60 ? 2801 ARG A NH1   1 
ATOM   10620 N  NH2   . ARG A 1 2801 ? 245.759 194.456 208.258 1.00 9.37  ? 2801 ARG A NH2   1 
ATOM   10621 N  N     . TRP A 1 2802 ? 254.601 193.575 210.099 1.00 0.55  ? 2802 TRP A N     1 
ATOM   10622 C  CA    . TRP A 1 2802 ? 255.810 193.265 210.855 1.00 0.44  ? 2802 TRP A CA    1 
ATOM   10623 C  C     . TRP A 1 2802 ? 256.963 194.160 210.427 1.00 0.59  ? 2802 TRP A C     1 
ATOM   10624 O  O     . TRP A 1 2802 ? 257.679 194.720 211.265 1.00 1.08  ? 2802 TRP A O     1 
ATOM   10625 C  CB    . TRP A 1 2802 ? 256.173 191.795 210.653 1.00 0.73  ? 2802 TRP A CB    1 
ATOM   10626 C  CG    . TRP A 1 2802 ? 256.982 191.188 211.748 1.00 0.44  ? 2802 TRP A CG    1 
ATOM   10627 C  CD1   . TRP A 1 2802 ? 257.712 191.842 212.695 1.00 0.29  ? 2802 TRP A CD1   1 
ATOM   10628 C  CD2   . TRP A 1 2802 ? 257.173 189.792 211.988 1.00 0.49  ? 2802 TRP A CD2   1 
ATOM   10629 N  NE1   . TRP A 1 2802 ? 258.330 190.940 213.521 1.00 0.23  ? 2802 TRP A NE1   1 
ATOM   10630 C  CE2   . TRP A 1 2802 ? 258.016 189.673 213.107 1.00 0.35  ? 2802 TRP A CE2   1 
ATOM   10631 C  CE3   . TRP A 1 2802 ? 256.703 188.630 211.369 1.00 0.67  ? 2802 TRP A CE3   1 
ATOM   10632 C  CZ2   . TRP A 1 2802 ? 258.398 188.439 213.620 1.00 0.60  ? 2802 TRP A CZ2   1 
ATOM   10633 C  CZ3   . TRP A 1 2802 ? 257.086 187.408 211.880 1.00 0.42  ? 2802 TRP A CZ3   1 
ATOM   10634 C  CH2   . TRP A 1 2802 ? 257.926 187.321 212.993 1.00 0.39  ? 2802 TRP A CH2   1 
ATOM   10635 N  N     . VAL A 1 2803 ? 257.157 194.305 209.117 1.00 1.25  ? 2803 VAL A N     1 
ATOM   10636 C  CA    . VAL A 1 2803 ? 258.247 195.129 208.607 1.00 1.09  ? 2803 VAL A CA    1 
ATOM   10637 C  C     . VAL A 1 2803 ? 257.966 196.603 208.869 1.00 1.08  ? 2803 VAL A C     1 
ATOM   10638 O  O     . VAL A 1 2803 ? 258.861 197.363 209.255 1.00 2.08  ? 2803 VAL A O     1 
ATOM   10639 C  CB    . VAL A 1 2803 ? 258.466 194.842 207.110 1.00 1.01  ? 2803 VAL A CB    1 
ATOM   10640 C  CG1   . VAL A 1 2803 ? 259.478 195.802 206.524 1.00 1.69  ? 2803 VAL A CG1   1 
ATOM   10641 C  CG2   . VAL A 1 2803 ? 258.910 193.405 206.912 1.00 1.02  ? 2803 VAL A CG2   1 
ATOM   10642 N  N     . ARG A 1 2804 ? 256.716 197.028 208.666 1.00 1.11  ? 2804 ARG A N     1 
ATOM   10643 C  CA    . ARG A 1 2804 ? 256.336 198.406 208.961 1.00 2.61  ? 2804 ARG A CA    1 
ATOM   10644 C  C     . ARG A 1 2804 ? 256.517 198.735 210.438 1.00 3.42  ? 2804 ARG A C     1 
ATOM   10645 O  O     . ARG A 1 2804 ? 257.006 199.816 210.781 1.00 4.62  ? 2804 ARG A O     1 
ATOM   10646 C  CB    . ARG A 1 2804 ? 254.892 198.657 208.525 1.00 3.84  ? 2804 ARG A CB    1 
ATOM   10647 C  CG    . ARG A 1 2804 ? 254.587 200.107 208.185 1.00 10.28 ? 2804 ARG A CG    1 
ATOM   10648 C  CD    . ARG A 1 2804 ? 255.352 200.612 206.975 1.00 10.00 ? 2804 ARG A CD    1 
ATOM   10649 N  NE    . ARG A 1 2804 ? 255.582 202.048 207.065 1.00 17.40 ? 2804 ARG A NE    1 
ATOM   10650 C  CZ    . ARG A 1 2804 ? 256.214 202.772 206.150 1.00 22.76 ? 2804 ARG A CZ    1 
ATOM   10651 N  NH1   . ARG A 1 2804 ? 256.676 202.228 205.037 1.00 14.36 ? 2804 ARG A NH1   1 
ATOM   10652 N  NH2   . ARG A 1 2804 ? 256.382 204.075 206.357 1.00 23.90 ? 2804 ARG A NH2   1 
ATOM   10653 N  N     . GLY A 1 2805 ? 256.129 197.816 211.324 1.00 3.02  ? 2805 GLY A N     1 
ATOM   10654 C  CA    . GLY A 1 2805 ? 256.264 198.075 212.748 1.00 2.22  ? 2805 GLY A CA    1 
ATOM   10655 C  C     . GLY A 1 2805 ? 257.708 198.270 213.170 1.00 2.26  ? 2805 GLY A C     1 
ATOM   10656 O  O     . GLY A 1 2805 ? 258.026 199.183 213.936 1.00 6.16  ? 2805 GLY A O     1 
ATOM   10657 N  N     . ILE A 1 2806 ? 258.601 197.412 212.677 1.00 1.75  ? 2806 ILE A N     1 
ATOM   10658 C  CA    . ILE A 1 2806 ? 260.024 197.573 212.965 1.00 3.46  ? 2806 ILE A CA    1 
ATOM   10659 C  C     . ILE A 1 2806 ? 260.545 198.867 212.358 1.00 4.13  ? 2806 ILE A C     1 
ATOM   10660 O  O     . ILE A 1 2806 ? 261.336 199.589 212.977 1.00 4.01  ? 2806 ILE A O     1 
ATOM   10661 C  CB    . ILE A 1 2806 ? 260.814 196.350 212.464 1.00 0.99  ? 2806 ILE A CB    1 
ATOM   10662 C  CG1   . ILE A 1 2806 ? 260.331 195.079 213.161 1.00 1.07  ? 2806 ILE A CG1   1 
ATOM   10663 C  CG2   . ILE A 1 2806 ? 262.306 196.555 212.668 1.00 0.54  ? 2806 ILE A CG2   1 
ATOM   10664 C  CD1   . ILE A 1 2806 ? 261.154 193.860 212.842 1.00 0.91  ? 2806 ILE A CD1   1 
ATOM   10665 N  N     . PHE A 1 2807 ? 260.111 199.179 211.137 1.00 3.57  ? 2807 PHE A N     1 
ATOM   10666 C  CA    . PHE A 1 2807 ? 260.576 200.381 210.458 1.00 3.64  ? 2807 PHE A CA    1 
ATOM   10667 C  C     . PHE A 1 2807 ? 260.167 201.644 211.207 1.00 5.73  ? 2807 PHE A C     1 
ATOM   10668 O  O     . PHE A 1 2807 ? 260.958 202.587 211.324 1.00 10.08 ? 2807 PHE A O     1 
ATOM   10669 C  CB    . PHE A 1 2807 ? 260.046 200.398 209.024 1.00 3.33  ? 2807 PHE A CB    1 
ATOM   10670 C  CG    . PHE A 1 2807 ? 260.306 201.676 208.299 1.00 10.34 ? 2807 PHE A CG    1 
ATOM   10671 C  CD1   . PHE A 1 2807 ? 261.554 201.941 207.768 1.00 7.46  ? 2807 PHE A CD1   1 
ATOM   10672 C  CD2   . PHE A 1 2807 ? 259.294 202.601 208.118 1.00 12.85 ? 2807 PHE A CD2   1 
ATOM   10673 C  CE1   . PHE A 1 2807 ? 261.796 203.116 207.098 1.00 9.48  ? 2807 PHE A CE1   1 
ATOM   10674 C  CE2   . PHE A 1 2807 ? 259.530 203.773 207.440 1.00 10.92 ? 2807 PHE A CE2   1 
ATOM   10675 C  CZ    . PHE A 1 2807 ? 260.782 204.034 206.930 1.00 9.52  ? 2807 PHE A CZ    1 
ATOM   10676 N  N     . GLU A 1 2808 ? 258.937 201.682 211.723 1.00 5.38  ? 2808 GLU A N     1 
ATOM   10677 C  CA    . GLU A 1 2808 ? 258.489 202.846 212.479 1.00 5.94  ? 2808 GLU A CA    1 
ATOM   10678 C  C     . GLU A 1 2808 ? 259.285 203.026 213.765 1.00 7.65  ? 2808 GLU A C     1 
ATOM   10679 O  O     . GLU A 1 2808 ? 259.519 204.160 214.194 1.00 10.75 ? 2808 GLU A O     1 
ATOM   10680 C  CB    . GLU A 1 2808 ? 256.997 202.728 212.786 1.00 6.04  ? 2808 GLU A CB    1 
ATOM   10681 C  CG    . GLU A 1 2808 ? 256.123 202.721 211.546 1.00 13.32 ? 2808 GLU A CG    1 
ATOM   10682 C  CD    . GLU A 1 2808 ? 254.752 202.132 211.798 1.00 20.36 ? 2808 GLU A CD    1 
ATOM   10683 O  OE1   . GLU A 1 2808 ? 254.465 201.760 212.956 1.00 16.41 ? 2808 GLU A OE1   1 
ATOM   10684 O  OE2   . GLU A 1 2808 ? 253.963 202.035 210.835 1.00 18.38 ? 2808 GLU A OE2   1 
ATOM   10685 N  N     . ALA A 1 2809 ? 259.710 201.928 214.387 1.00 5.47  ? 2809 ALA A N     1 
ATOM   10686 C  CA    . ALA A 1 2809 ? 260.512 201.991 215.598 1.00 3.03  ? 2809 ALA A CA    1 
ATOM   10687 C  C     . ALA A 1 2809 ? 261.988 202.246 215.322 1.00 6.53  ? 2809 ALA A C     1 
ATOM   10688 O  O     . ALA A 1 2809 ? 262.761 202.392 216.276 1.00 16.15 ? 2809 ALA A O     1 
ATOM   10689 C  CB    . ALA A 1 2809 ? 260.358 200.696 216.398 1.00 3.07  ? 2809 ALA A CB    1 
ATOM   10690 N  N     . LEU A 1 2810 ? 262.399 202.294 214.054 1.00 5.89  ? 2810 LEU A N     1 
ATOM   10691 C  CA    . LEU A 1 2810 ? 263.795 202.499 213.701 1.00 4.32  ? 2810 LEU A CA    1 
ATOM   10692 C  C     . LEU A 1 2810 ? 264.080 203.849 213.058 1.00 11.93 ? 2810 LEU A C     1 
ATOM   10693 O  O     . LEU A 1 2810 ? 265.243 204.263 213.035 1.00 17.14 ? 2810 LEU A O     1 
ATOM   10694 C  CB    . LEU A 1 2810 ? 264.271 201.391 212.750 1.00 5.62  ? 2810 LEU A CB    1 
ATOM   10695 C  CG    . LEU A 1 2810 ? 264.673 200.042 213.349 1.00 3.43  ? 2810 LEU A CG    1 
ATOM   10696 C  CD1   . LEU A 1 2810 ? 265.017 199.057 212.249 1.00 4.44  ? 2810 LEU A CD1   1 
ATOM   10697 C  CD2   . LEU A 1 2810 ? 265.840 200.197 214.301 1.00 10.03 ? 2810 LEU A CD2   1 
ATOM   10698 N  N     . ARG A 1 2811 ? 263.063 204.541 212.538 1.00 7.69  ? 2811 ARG A N     1 
ATOM   10699 C  CA    . ARG A 1 2811 ? 263.295 205.822 211.869 1.00 11.54 ? 2811 ARG A CA    1 
ATOM   10700 C  C     . ARG A 1 2811 ? 263.952 206.871 212.757 1.00 13.15 ? 2811 ARG A C     1 
ATOM   10701 O  O     . ARG A 1 2811 ? 264.947 207.476 212.320 1.00 19.48 ? 2811 ARG A O     1 
ATOM   10702 C  CB    . ARG A 1 2811 ? 261.982 206.362 211.296 1.00 12.89 ? 2811 ARG A CB    1 
ATOM   10703 C  CG    . ARG A 1 2811 ? 261.413 205.570 210.155 1.00 15.21 ? 2811 ARG A CG    1 
ATOM   10704 C  CD    . ARG A 1 2811 ? 260.101 206.170 209.699 1.00 19.53 ? 2811 ARG A CD    1 
ATOM   10705 N  NE    . ARG A 1 2811 ? 259.050 206.018 210.695 1.00 19.97 ? 2811 ARG A NE    1 
ATOM   10706 C  CZ    . ARG A 1 2811 ? 257.843 206.558 210.596 1.00 23.44 ? 2811 ARG A CZ    1 
ATOM   10707 N  NH1   . ARG A 1 2811 ? 257.501 207.291 209.550 1.00 20.75 ? 2811 ARG A NH1   1 
ATOM   10708 N  NH2   . ARG A 1 2811 ? 256.958 206.353 211.566 1.00 22.76 ? 2811 ARG A NH2   1 
ATOM   10709 N  N     . PRO A 1 2812 ? 263.473 207.153 213.979 1.00 14.42 ? 2812 PRO A N     1 
ATOM   10710 C  CA    . PRO A 1 2812 ? 264.074 208.249 214.747 1.00 13.78 ? 2812 PRO A CA    1 
ATOM   10711 C  C     . PRO A 1 2812 ? 265.328 207.836 215.502 1.00 11.76 ? 2812 PRO A C     1 
ATOM   10712 O  O     . PRO A 1 2812 ? 265.784 208.559 216.393 1.00 24.61 ? 2812 PRO A O     1 
ATOM   10713 C  CB    . PRO A 1 2812 ? 262.950 208.641 215.708 1.00 15.53 ? 2812 PRO A CB    1 
ATOM   10714 C  CG    . PRO A 1 2812 ? 262.299 207.342 216.003 1.00 14.45 ? 2812 PRO A CG    1 
ATOM   10715 C  CD    . PRO A 1 2812 ? 262.335 206.559 214.710 1.00 8.53  ? 2812 PRO A CD    1 
ATOM   10716 N  N     . LEU A 1 2813 ? 265.893 206.683 215.159 1.00 14.56 ? 2813 LEU A N     1 
ATOM   10717 C  CA    . LEU A 1 2813 ? 267.035 206.129 215.874 1.00 15.89 ? 2813 LEU A CA    1 
ATOM   10718 C  C     . LEU A 1 2813 ? 268.309 206.332 215.068 1.00 22.12 ? 2813 LEU A C     1 
ATOM   10719 O  O     . LEU A 1 2813 ? 268.379 205.947 213.896 1.00 25.20 ? 2813 LEU A O     1 
ATOM   10720 C  CB    . LEU A 1 2813 ? 266.828 204.642 216.161 1.00 15.75 ? 2813 LEU A CB    1 
ATOM   10721 C  CG    . LEU A 1 2813 ? 265.697 204.295 217.130 1.00 12.47 ? 2813 LEU A CG    1 
ATOM   10722 C  CD1   . LEU A 1 2813 ? 265.835 202.862 217.617 1.00 9.15  ? 2813 LEU A CD1   1 
ATOM   10723 C  CD2   . LEU A 1 2813 ? 265.679 205.264 218.297 1.00 14.33 ? 2813 LEU A CD2   1 
ATOM   10724 N  N     . GLU A 1 2814 ? 269.314 206.940 215.699 1.00 21.35 ? 2814 GLU A N     1 
ATOM   10725 C  CA    . GLU A 1 2814 ? 270.603 207.119 215.043 1.00 23.19 ? 2814 GLU A CA    1 
ATOM   10726 C  C     . GLU A 1 2814 ? 271.415 205.831 215.018 1.00 23.40 ? 2814 GLU A C     1 
ATOM   10727 O  O     . GLU A 1 2814 ? 272.167 205.600 214.065 1.00 22.91 ? 2814 GLU A O     1 
ATOM   10728 C  CB    . GLU A 1 2814 ? 271.392 208.242 215.728 1.00 26.39 ? 2814 GLU A CB    1 
ATOM   10729 C  CG    . GLU A 1 2814 ? 272.085 207.860 217.033 1.00 31.73 ? 2814 GLU A CG    1 
ATOM   10730 C  CD    . GLU A 1 2814 ? 271.122 207.383 218.108 1.00 34.28 ? 2814 GLU A CD    1 
ATOM   10731 O  OE1   . GLU A 1 2814 ? 269.938 207.783 218.075 1.00 31.54 ? 2814 GLU A OE1   1 
ATOM   10732 O  OE2   . GLU A 1 2814 ? 271.549 206.605 218.987 1.00 36.80 ? 2814 GLU A OE2   1 
ATOM   10733 N  N     . THR A 1 2815 ? 271.276 204.984 216.037 1.00 20.16 ? 2815 THR A N     1 
ATOM   10734 C  CA    . THR A 1 2815 ? 271.998 203.722 216.082 1.00 20.55 ? 2815 THR A CA    1 
ATOM   10735 C  C     . THR A 1 2815 ? 271.276 202.778 217.030 1.00 16.84 ? 2815 THR A C     1 
ATOM   10736 O  O     . THR A 1 2815 ? 270.481 203.200 217.874 1.00 19.40 ? 2815 THR A O     1 
ATOM   10737 C  CB    . THR A 1 2815 ? 273.455 203.912 216.520 1.00 20.98 ? 2815 THR A CB    1 
ATOM   10738 O  OG1   . THR A 1 2815 ? 274.209 202.740 216.189 1.00 24.35 ? 2815 THR A OG1   1 
ATOM   10739 C  CG2   . THR A 1 2815 ? 273.537 204.153 218.019 1.00 18.47 ? 2815 THR A CG2   1 
ATOM   10740 N  N     . LEU A 1 2816 ? 271.572 201.484 216.879 1.00 14.27 ? 2816 LEU A N     1 
ATOM   10741 C  CA    . LEU A 1 2816 ? 270.937 200.448 217.676 1.00 9.22  ? 2816 LEU A CA    1 
ATOM   10742 C  C     . LEU A 1 2816 ? 271.792 199.197 217.624 1.00 7.64  ? 2816 LEU A C     1 
ATOM   10743 O  O     . LEU A 1 2816 ? 272.244 198.821 216.533 1.00 23.87 ? 2816 LEU A O     1 
ATOM   10744 C  CB    . LEU A 1 2816 ? 269.528 200.141 217.164 1.00 9.64  ? 2816 LEU A CB    1 
ATOM   10745 C  CG    . LEU A 1 2816 ? 268.592 199.355 218.084 1.00 9.29  ? 2816 LEU A CG    1 
ATOM   10746 C  CD1   . LEU A 1 2816 ? 268.125 200.211 219.249 1.00 3.42  ? 2816 LEU A CD1   1 
ATOM   10747 C  CD2   . LEU A 1 2816 ? 267.407 198.828 217.297 1.00 7.77  ? 2816 LEU A CD2   1 
ATOM   10748 N  N     . PRO A 1 2817 ? 272.043 198.538 218.750 1.00 13.47 ? 2817 PRO A N     1 
ATOM   10749 C  CA    . PRO A 1 2817 ? 272.716 197.235 218.709 1.00 10.56 ? 2817 PRO A CA    1 
ATOM   10750 C  C     . PRO A 1 2817 ? 271.785 196.166 218.158 1.00 11.40 ? 2817 PRO A C     1 
ATOM   10751 O  O     . PRO A 1 2817 ? 270.573 196.349 218.046 1.00 17.14 ? 2817 PRO A O     1 
ATOM   10752 C  CB    . PRO A 1 2817 ? 273.084 196.971 220.170 1.00 8.52  ? 2817 PRO A CB    1 
ATOM   10753 C  CG    . PRO A 1 2817 ? 272.115 197.783 220.956 1.00 12.56 ? 2817 PRO A CG    1 
ATOM   10754 C  CD    . PRO A 1 2817 ? 271.782 198.990 220.127 1.00 11.79 ? 2817 PRO A CD    1 
ATOM   10755 N  N     . VAL A 1 2818 ? 272.380 195.027 217.802 1.00 11.28 ? 2818 VAL A N     1 
ATOM   10756 C  CA    . VAL A 1 2818 ? 271.601 193.945 217.209 1.00 10.00 ? 2818 VAL A CA    1 
ATOM   10757 C  C     . VAL A 1 2818 ? 270.598 193.393 218.217 1.00 8.00  ? 2818 VAL A C     1 
ATOM   10758 O  O     . VAL A 1 2818 ? 269.487 192.992 217.849 1.00 8.75  ? 2818 VAL A O     1 
ATOM   10759 C  CB    . VAL A 1 2818 ? 272.533 192.850 216.656 1.00 9.72  ? 2818 VAL A CB    1 
ATOM   10760 C  CG1   . VAL A 1 2818 ? 273.318 192.175 217.774 1.00 9.76  ? 2818 VAL A CG1   1 
ATOM   10761 C  CG2   . VAL A 1 2818 ? 271.738 191.834 215.848 1.00 6.46  ? 2818 VAL A CG2   1 
ATOM   10762 N  N     . GLU A 1 2819 ? 270.965 193.369 219.500 1.00 9.08  ? 2819 GLU A N     1 
ATOM   10763 C  CA    . GLU A 1 2819 ? 270.020 192.954 220.530 1.00 8.46  ? 2819 GLU A CA    1 
ATOM   10764 C  C     . GLU A 1 2819 ? 268.820 193.891 220.597 1.00 9.98  ? 2819 GLU A C     1 
ATOM   10765 O  O     . GLU A 1 2819 ? 267.704 193.448 220.882 1.00 7.85  ? 2819 GLU A O     1 
ATOM   10766 C  CB    . GLU A 1 2819 ? 270.717 192.875 221.887 1.00 10.65 ? 2819 GLU A CB    1 
ATOM   10767 C  CG    . GLU A 1 2819 ? 271.767 191.776 221.995 1.00 15.92 ? 2819 GLU A CG    1 
ATOM   10768 C  CD    . GLU A 1 2819 ? 273.111 192.182 221.420 1.00 20.29 ? 2819 GLU A CD    1 
ATOM   10769 O  OE1   . GLU A 1 2819 ? 273.255 193.345 220.989 1.00 16.26 ? 2819 GLU A OE1   1 
ATOM   10770 O  OE2   . GLU A 1 2819 ? 274.024 191.330 221.391 1.00 29.54 ? 2819 GLU A OE2   1 
ATOM   10771 N  N     . GLY A 1 2820 ? 269.033 195.184 220.342 1.00 8.19  ? 2820 GLY A N     1 
ATOM   10772 C  CA    . GLY A 1 2820 ? 267.915 196.103 220.244 1.00 4.56  ? 2820 GLY A CA    1 
ATOM   10773 C  C     . GLY A 1 2820 ? 267.018 195.815 219.058 1.00 4.97  ? 2820 GLY A C     1 
ATOM   10774 O  O     . GLY A 1 2820 ? 265.802 196.009 219.133 1.00 5.28  ? 2820 GLY A O     1 
ATOM   10775 N  N     . LEU A 1 2821 ? 267.603 195.366 217.945 1.00 7.61  ? 2821 LEU A N     1 
ATOM   10776 C  CA    . LEU A 1 2821 ? 266.805 194.979 216.786 1.00 3.59  ? 2821 LEU A CA    1 
ATOM   10777 C  C     . LEU A 1 2821 ? 265.928 193.773 217.094 1.00 2.40  ? 2821 LEU A C     1 
ATOM   10778 O  O     . LEU A 1 2821 ? 264.760 193.728 216.695 1.00 2.67  ? 2821 LEU A O     1 
ATOM   10779 C  CB    . LEU A 1 2821 ? 267.717 194.687 215.596 1.00 4.55  ? 2821 LEU A CB    1 
ATOM   10780 C  CG    . LEU A 1 2821 ? 267.023 194.239 214.309 1.00 3.71  ? 2821 LEU A CG    1 
ATOM   10781 C  CD1   . LEU A 1 2821 ? 266.100 195.330 213.788 1.00 1.76  ? 2821 LEU A CD1   1 
ATOM   10782 C  CD2   . LEU A 1 2821 ? 268.043 193.842 213.258 1.00 3.49  ? 2821 LEU A CD2   1 
ATOM   10783 N  N     . ILE A 1 2822 ? 266.475 192.786 217.806 1.00 1.63  ? 2822 ILE A N     1 
ATOM   10784 C  CA    . ILE A 1 2822 ? 265.708 191.584 218.122 1.00 1.64  ? 2822 ILE A CA    1 
ATOM   10785 C  C     . ILE A 1 2822 ? 264.539 191.918 219.038 1.00 2.92  ? 2822 ILE A C     1 
ATOM   10786 O  O     . ILE A 1 2822 ? 263.453 191.341 218.913 1.00 1.85  ? 2822 ILE A O     1 
ATOM   10787 C  CB    . ILE A 1 2822 ? 266.622 190.510 218.739 1.00 3.17  ? 2822 ILE A CB    1 
ATOM   10788 C  CG1   . ILE A 1 2822 ? 267.819 190.239 217.830 1.00 3.54  ? 2822 ILE A CG1   1 
ATOM   10789 C  CG2   . ILE A 1 2822 ? 265.847 189.228 218.989 1.00 5.41  ? 2822 ILE A CG2   1 
ATOM   10790 C  CD1   . ILE A 1 2822 ? 267.443 189.943 216.400 1.00 4.18  ? 2822 ILE A CD1   1 
ATOM   10791 N  N     . ARG A 1 2823 ? 264.742 192.848 219.975 1.00 4.69  ? 2823 ARG A N     1 
ATOM   10792 C  CA    . ARG A 1 2823 ? 263.661 193.223 220.881 1.00 2.23  ? 2823 ARG A CA    1 
ATOM   10793 C  C     . ARG A 1 2823 ? 262.497 193.846 220.122 1.00 1.68  ? 2823 ARG A C     1 
ATOM   10794 O  O     . ARG A 1 2823 ? 261.332 193.537 220.399 1.00 1.75  ? 2823 ARG A O     1 
ATOM   10795 C  CB    . ARG A 1 2823 ? 264.181 194.174 221.957 1.00 4.47  ? 2823 ARG A CB    1 
ATOM   10796 C  CG    . ARG A 1 2823 ? 263.274 194.258 223.168 1.00 3.27  ? 2823 ARG A CG    1 
ATOM   10797 C  CD    . ARG A 1 2823 ? 263.912 195.017 224.314 1.00 3.40  ? 2823 ARG A CD    1 
ATOM   10798 N  NE    . ARG A 1 2823 ? 263.124 194.891 225.535 1.00 11.46 ? 2823 ARG A NE    1 
ATOM   10799 C  CZ    . ARG A 1 2823 ? 263.017 193.783 226.255 1.00 8.59  ? 2823 ARG A CZ    1 
ATOM   10800 N  NH1   . ARG A 1 2823 ? 263.701 192.692 225.951 1.00 6.43  ? 2823 ARG A NH1   1 
ATOM   10801 N  NH2   . ARG A 1 2823 ? 262.209 193.769 227.309 1.00 5.11  ? 2823 ARG A NH2   1 
ATOM   10802 N  N     . ILE A 1 2824 ? 262.790 194.727 219.163 1.00 1.58  ? 2824 ILE A N     1 
ATOM   10803 C  CA    . ILE A 1 2824 ? 261.737 195.270 218.309 1.00 1.43  ? 2824 ILE A CA    1 
ATOM   10804 C  C     . ILE A 1 2824 ? 261.093 194.156 217.495 1.00 1.59  ? 2824 ILE A C     1 
ATOM   10805 O  O     . ILE A 1 2824 ? 259.866 194.098 217.354 1.00 1.58  ? 2824 ILE A O     1 
ATOM   10806 C  CB    . ILE A 1 2824 ? 262.301 196.377 217.397 1.00 1.46  ? 2824 ILE A CB    1 
ATOM   10807 C  CG1   . ILE A 1 2824 ? 263.010 197.447 218.227 1.00 1.50  ? 2824 ILE A CG1   1 
ATOM   10808 C  CG2   . ILE A 1 2824 ? 261.194 196.995 216.558 1.00 1.61  ? 2824 ILE A CG2   1 
ATOM   10809 C  CD1   . ILE A 1 2824 ? 263.706 198.501 217.393 1.00 5.03  ? 2824 ILE A CD1   1 
ATOM   10810 N  N     . TRP A 1 2825 ? 261.913 193.255 216.953 1.00 2.00  ? 2825 TRP A N     1 
ATOM   10811 C  CA    . TRP A 1 2825 ? 261.391 192.130 216.187 1.00 0.67  ? 2825 TRP A CA    1 
ATOM   10812 C  C     . TRP A 1 2825 ? 260.518 191.230 217.054 1.00 1.17  ? 2825 TRP A C     1 
ATOM   10813 O  O     . TRP A 1 2825 ? 259.457 190.770 216.615 1.00 1.50  ? 2825 TRP A O     1 
ATOM   10814 C  CB    . TRP A 1 2825 ? 262.554 191.345 215.581 1.00 0.87  ? 2825 TRP A CB    1 
ATOM   10815 C  CG    . TRP A 1 2825 ? 262.145 190.118 214.846 1.00 0.97  ? 2825 TRP A CG    1 
ATOM   10816 C  CD1   . TRP A 1 2825 ? 261.794 190.030 213.533 1.00 0.41  ? 2825 TRP A CD1   1 
ATOM   10817 C  CD2   . TRP A 1 2825 ? 262.054 188.794 215.377 1.00 1.05  ? 2825 TRP A CD2   1 
ATOM   10818 N  NE1   . TRP A 1 2825 ? 261.485 188.734 213.214 1.00 0.44  ? 2825 TRP A NE1   1 
ATOM   10819 C  CE2   . TRP A 1 2825 ? 261.637 187.955 214.329 1.00 0.41  ? 2825 TRP A CE2   1 
ATOM   10820 C  CE3   . TRP A 1 2825 ? 262.283 188.237 216.639 1.00 1.09  ? 2825 TRP A CE3   1 
ATOM   10821 C  CZ2   . TRP A 1 2825 ? 261.440 186.588 214.502 1.00 0.70  ? 2825 TRP A CZ2   1 
ATOM   10822 C  CZ3   . TRP A 1 2825 ? 262.087 186.883 216.809 1.00 1.41  ? 2825 TRP A CZ3   1 
ATOM   10823 C  CH2   . TRP A 1 2825 ? 261.671 186.073 215.746 1.00 1.87  ? 2825 TRP A CH2   1 
ATOM   10824 N  N     . ALA A 1 2826 ? 260.950 190.960 218.287 1.00 2.50  ? 2826 ALA A N     1 
ATOM   10825 C  CA    . ALA A 1 2826 ? 260.143 190.150 219.192 1.00 1.03  ? 2826 ALA A CA    1 
ATOM   10826 C  C     . ALA A 1 2826 ? 258.883 190.889 219.626 1.00 0.47  ? 2826 ALA A C     1 
ATOM   10827 O  O     . ALA A 1 2826 ? 257.813 190.284 219.748 1.00 0.54  ? 2826 ALA A O     1 
ATOM   10828 C  CB    . ALA A 1 2826 ? 260.970 189.744 220.409 1.00 0.61  ? 2826 ALA A CB    1 
ATOM   10829 N  N     . HIS A 1 2827 ? 258.995 192.195 219.870 1.00 0.59  ? 2827 HIS A N     1 
ATOM   10830 C  CA    . HIS A 1 2827 ? 257.837 192.968 220.302 1.00 0.40  ? 2827 HIS A CA    1 
ATOM   10831 C  C     . HIS A 1 2827 ? 256.750 192.987 219.238 1.00 0.34  ? 2827 HIS A C     1 
ATOM   10832 O  O     . HIS A 1 2827 ? 255.569 192.786 219.542 1.00 0.24  ? 2827 HIS A O     1 
ATOM   10833 C  CB    . HIS A 1 2827 ? 258.260 194.391 220.658 1.00 0.42  ? 2827 HIS A CB    1 
ATOM   10834 C  CG    . HIS A 1 2827 ? 257.112 195.314 220.914 1.00 0.45  ? 2827 HIS A CG    1 
ATOM   10835 N  ND1   . HIS A 1 2827 ? 256.381 195.285 222.080 1.00 0.36  ? 2827 HIS A ND1   1 
ATOM   10836 C  CD2   . HIS A 1 2827 ? 256.570 196.292 220.154 1.00 0.63  ? 2827 HIS A CD2   1 
ATOM   10837 C  CE1   . HIS A 1 2827 ? 255.433 196.203 222.026 1.00 0.40  ? 2827 HIS A CE1   1 
ATOM   10838 N  NE2   . HIS A 1 2827 ? 255.527 196.829 220.867 1.00 0.48  ? 2827 HIS A NE2   1 
ATOM   10839 N  N     . GLU A 1 2828 ? 257.131 193.218 217.980 1.00 0.55  ? 2828 GLU A N     1 
ATOM   10840 C  CA    . GLU A 1 2828 ? 256.145 193.264 216.909 1.00 0.29  ? 2828 GLU A CA    1 
ATOM   10841 C  C     . GLU A 1 2828 ? 255.524 191.897 216.657 1.00 0.24  ? 2828 GLU A C     1 
ATOM   10842 O  O     . GLU A 1 2828 ? 254.348 191.813 216.289 1.00 0.55  ? 2828 GLU A O     1 
ATOM   10843 C  CB    . GLU A 1 2828 ? 256.784 193.816 215.635 1.00 1.48  ? 2828 GLU A CB    1 
ATOM   10844 C  CG    . GLU A 1 2828 ? 257.225 195.265 215.758 1.00 1.56  ? 2828 GLU A CG    1 
ATOM   10845 C  CD    . GLU A 1 2828 ? 256.054 196.224 215.886 1.00 8.45  ? 2828 GLU A CD    1 
ATOM   10846 O  OE1   . GLU A 1 2828 ? 254.919 195.835 215.544 1.00 9.93  ? 2828 GLU A OE1   1 
ATOM   10847 O  OE2   . GLU A 1 2828 ? 256.267 197.365 216.342 1.00 8.28  ? 2828 GLU A OE2   1 
ATOM   10848 N  N     . ALA A 1 2829 ? 256.291 190.823 216.852 1.00 0.31  ? 2829 ALA A N     1 
ATOM   10849 C  CA    . ALA A 1 2829 ? 255.730 189.483 216.725 1.00 0.46  ? 2829 ALA A CA    1 
ATOM   10850 C  C     . ALA A 1 2829 ? 254.638 189.241 217.761 1.00 0.32  ? 2829 ALA A C     1 
ATOM   10851 O  O     . ALA A 1 2829 ? 253.596 188.656 217.449 1.00 0.41  ? 2829 ALA A O     1 
ATOM   10852 C  CB    . ALA A 1 2829 ? 256.837 188.438 216.851 1.00 0.52  ? 2829 ALA A CB    1 
ATOM   10853 N  N     . LEU A 1 2830 ? 254.858 189.689 218.999 1.00 0.34  ? 2830 LEU A N     1 
ATOM   10854 C  CA    . LEU A 1 2830 ? 253.842 189.526 220.036 1.00 0.51  ? 2830 LEU A CA    1 
ATOM   10855 C  C     . LEU A 1 2830 ? 252.582 190.316 219.705 1.00 0.29  ? 2830 LEU A C     1 
ATOM   10856 O  O     . LEU A 1 2830 ? 251.464 189.835 219.912 1.00 0.74  ? 2830 LEU A O     1 
ATOM   10857 C  CB    . LEU A 1 2830 ? 254.403 189.955 221.390 1.00 0.84  ? 2830 LEU A CB    1 
ATOM   10858 C  CG    . LEU A 1 2830 ? 255.507 189.077 221.978 1.00 0.82  ? 2830 LEU A CG    1 
ATOM   10859 C  CD1   . LEU A 1 2830 ? 256.308 189.855 223.006 1.00 0.30  ? 2830 LEU A CD1   1 
ATOM   10860 C  CD2   . LEU A 1 2830 ? 254.925 187.816 222.587 1.00 2.00  ? 2830 LEU A CD2   1 
ATOM   10861 N  N     . ARG A 1 2831 ? 252.746 191.531 219.181 1.00 0.25  ? 2831 ARG A N     1 
ATOM   10862 C  CA    . ARG A 1 2831 ? 251.592 192.359 218.856 1.00 0.34  ? 2831 ARG A CA    1 
ATOM   10863 C  C     . ARG A 1 2831 ? 250.797 191.795 217.686 1.00 0.70  ? 2831 ARG A C     1 
ATOM   10864 O  O     . ARG A 1 2831 ? 249.574 191.961 217.634 1.00 1.75  ? 2831 ARG A O     1 
ATOM   10865 C  CB    . ARG A 1 2831 ? 252.045 193.787 218.558 1.00 0.50  ? 2831 ARG A CB    1 
ATOM   10866 C  CG    . ARG A 1 2831 ? 252.724 194.484 219.728 1.00 0.32  ? 2831 ARG A CG    1 
ATOM   10867 C  CD    . ARG A 1 2831 ? 251.725 194.905 220.804 1.00 0.60  ? 2831 ARG A CD    1 
ATOM   10868 N  NE    . ARG A 1 2831 ? 251.319 193.791 221.654 1.00 0.53  ? 2831 ARG A NE    1 
ATOM   10869 C  CZ    . ARG A 1 2831 ? 252.107 193.179 222.526 1.00 0.39  ? 2831 ARG A CZ    1 
ATOM   10870 N  NH1   . ARG A 1 2831 ? 253.346 193.587 222.747 1.00 0.18  ? 2831 ARG A NH1   1 
ATOM   10871 N  NH2   . ARG A 1 2831 ? 251.644 192.126 223.191 1.00 0.69  ? 2831 ARG A NH2   1 
ATOM   10872 N  N     . LEU A 1 2832 ? 251.462 191.125 216.747 1.00 0.65  ? 2832 LEU A N     1 
ATOM   10873 C  CA    . LEU A 1 2832 ? 250.810 190.632 215.543 1.00 0.61  ? 2832 LEU A CA    1 
ATOM   10874 C  C     . LEU A 1 2832 ? 250.301 189.206 215.664 1.00 0.50  ? 2832 LEU A C     1 
ATOM   10875 O  O     . LEU A 1 2832 ? 249.325 188.854 214.996 1.00 1.68  ? 2832 LEU A O     1 
ATOM   10876 C  CB    . LEU A 1 2832 ? 251.767 190.709 214.352 1.00 1.23  ? 2832 LEU A CB    1 
ATOM   10877 C  CG    . LEU A 1 2832 ? 252.065 192.108 213.818 1.00 0.59  ? 2832 LEU A CG    1 
ATOM   10878 C  CD1   . LEU A 1 2832 ? 253.112 192.020 212.742 1.00 0.45  ? 2832 LEU A CD1   1 
ATOM   10879 C  CD2   . LEU A 1 2832 ? 250.804 192.762 213.288 1.00 1.08  ? 2832 LEU A CD2   1 
ATOM   10880 N  N     . PHE A 1 2833 ? 250.934 188.376 216.487 1.00 0.46  ? 2833 PHE A N     1 
ATOM   10881 C  CA    . PHE A 1 2833 ? 250.585 186.967 216.563 1.00 0.46  ? 2833 PHE A CA    1 
ATOM   10882 C  C     . PHE A 1 2833 ? 249.967 186.554 217.886 1.00 0.55  ? 2833 PHE A C     1 
ATOM   10883 O  O     . PHE A 1 2833 ? 249.126 185.654 217.899 1.00 1.43  ? 2833 PHE A O     1 
ATOM   10884 C  CB    . PHE A 1 2833 ? 251.824 186.100 216.301 1.00 0.46  ? 2833 PHE A CB    1 
ATOM   10885 C  CG    . PHE A 1 2833 ? 252.413 186.283 214.934 1.00 0.27  ? 2833 PHE A CG    1 
ATOM   10886 C  CD1   . PHE A 1 2833 ? 251.933 185.558 213.859 1.00 0.45  ? 2833 PHE A CD1   1 
ATOM   10887 C  CD2   . PHE A 1 2833 ? 253.441 187.181 214.724 1.00 0.29  ? 2833 PHE A CD2   1 
ATOM   10888 C  CE1   . PHE A 1 2833 ? 252.471 185.722 212.602 1.00 0.44  ? 2833 PHE A CE1   1 
ATOM   10889 C  CE2   . PHE A 1 2833 ? 253.982 187.352 213.467 1.00 0.57  ? 2833 PHE A CE2   1 
ATOM   10890 C  CZ    . PHE A 1 2833 ? 253.496 186.620 212.404 1.00 0.53  ? 2833 PHE A CZ    1 
ATOM   10891 N  N     . GLN A 1 2834 ? 250.346 187.191 218.990 1.00 0.61  ? 2834 GLN A N     1 
ATOM   10892 C  CA    . GLN A 1 2834 ? 249.866 186.774 220.300 1.00 0.47  ? 2834 GLN A CA    1 
ATOM   10893 C  C     . GLN A 1 2834 ? 248.608 187.510 220.745 1.00 0.62  ? 2834 GLN A C     1 
ATOM   10894 O  O     . GLN A 1 2834 ? 247.827 186.959 221.526 1.00 1.47  ? 2834 GLN A O     1 
ATOM   10895 C  CB    . GLN A 1 2834 ? 250.969 186.968 221.343 1.00 0.46  ? 2834 GLN A CB    1 
ATOM   10896 C  CG    . GLN A 1 2834 ? 250.812 186.112 222.583 1.00 1.15  ? 2834 GLN A CG    1 
ATOM   10897 C  CD    . GLN A 1 2834 ? 251.781 186.502 223.677 1.00 2.84  ? 2834 GLN A CD    1 
ATOM   10898 O  OE1   . GLN A 1 2834 ? 251.776 187.637 224.146 1.00 5.60  ? 2834 GLN A OE1   1 
ATOM   10899 N  NE2   . GLN A 1 2834 ? 252.620 185.562 224.088 1.00 3.07  ? 2834 GLN A NE2   1 
ATOM   10900 N  N     . ASP A 1 2835 ? 248.383 188.734 220.260 1.00 0.57  ? 2835 ASP A N     1 
ATOM   10901 C  CA    . ASP A 1 2835 ? 247.290 189.554 220.771 1.00 0.63  ? 2835 ASP A CA    1 
ATOM   10902 C  C     . ASP A 1 2835 ? 245.915 189.028 220.379 1.00 0.36  ? 2835 ASP A C     1 
ATOM   10903 O  O     . ASP A 1 2835 ? 244.927 189.385 221.026 1.00 0.43  ? 2835 ASP A O     1 
ATOM   10904 C  CB    . ASP A 1 2835 ? 247.447 190.997 220.295 1.00 0.82  ? 2835 ASP A CB    1 
ATOM   10905 C  CG    . ASP A 1 2835 ? 248.545 191.739 221.030 1.00 1.77  ? 2835 ASP A CG    1 
ATOM   10906 O  OD1   . ASP A 1 2835 ? 249.190 191.135 221.911 1.00 0.72  ? 2835 ASP A OD1   1 
ATOM   10907 O  OD2   . ASP A 1 2835 ? 248.765 192.930 220.728 1.00 3.41  ? 2835 ASP A OD2   1 
ATOM   10908 N  N     . ARG A 1 2836 ? 245.827 188.203 219.341 1.00 0.46  ? 2836 ARG A N     1 
ATOM   10909 C  CA    . ARG A 1 2836 ? 244.556 187.633 218.919 1.00 0.58  ? 2836 ARG A CA    1 
ATOM   10910 C  C     . ARG A 1 2836 ? 244.273 186.274 219.539 1.00 0.65  ? 2836 ARG A C     1 
ATOM   10911 O  O     . ARG A 1 2836 ? 243.167 185.751 219.367 1.00 1.04  ? 2836 ARG A O     1 
ATOM   10912 C  CB    . ARG A 1 2836 ? 244.519 187.501 217.395 1.00 0.62  ? 2836 ARG A CB    1 
ATOM   10913 C  CG    . ARG A 1 2836 ? 245.395 186.379 216.865 1.00 0.59  ? 2836 ARG A CG    1 
ATOM   10914 C  CD    . ARG A 1 2836 ? 245.337 186.313 215.362 1.00 1.65  ? 2836 ARG A CD    1 
ATOM   10915 N  NE    . ARG A 1 2836 ? 245.952 187.485 214.752 1.00 5.70  ? 2836 ARG A NE    1 
ATOM   10916 C  CZ    . ARG A 1 2836 ? 245.863 187.790 213.467 1.00 2.56  ? 2836 ARG A CZ    1 
ATOM   10917 N  NH1   . ARG A 1 2836 ? 245.177 187.036 212.623 1.00 2.28  ? 2836 ARG A NH1   1 
ATOM   10918 N  NH2   . ARG A 1 2836 ? 246.473 188.881 213.014 1.00 4.56  ? 2836 ARG A NH2   1 
ATOM   10919 N  N     . LEU A 1 2837 ? 245.235 185.692 220.249 1.00 0.59  ? 2837 LEU A N     1 
ATOM   10920 C  CA    . LEU A 1 2837 ? 245.075 184.339 220.761 1.00 0.81  ? 2837 LEU A CA    1 
ATOM   10921 C  C     . LEU A 1 2837 ? 244.107 184.313 221.938 1.00 1.86  ? 2837 LEU A C     1 
ATOM   10922 O  O     . LEU A 1 2837 ? 244.039 185.254 222.731 1.00 2.97  ? 2837 LEU A O     1 
ATOM   10923 C  CB    . LEU A 1 2837 ? 246.431 183.769 221.163 1.00 1.33  ? 2837 LEU A CB    1 
ATOM   10924 C  CG    . LEU A 1 2837 ? 247.418 183.630 220.000 1.00 1.31  ? 2837 LEU A CG    1 
ATOM   10925 C  CD1   . LEU A 1 2837 ? 248.746 183.093 220.483 1.00 1.15  ? 2837 LEU A CD1   1 
ATOM   10926 C  CD2   . LEU A 1 2837 ? 246.843 182.744 218.901 1.00 0.92  ? 2837 LEU A CD2   1 
ATOM   10927 N  N     . VAL A 1 2838 ? 243.355 183.222 222.041 1.00 2.64  ? 2838 VAL A N     1 
ATOM   10928 C  CA    . VAL A 1 2838 ? 242.287 183.100 223.028 1.00 2.41  ? 2838 VAL A CA    1 
ATOM   10929 C  C     . VAL A 1 2838 ? 242.786 182.362 224.263 1.00 5.29  ? 2838 VAL A C     1 
ATOM   10930 O  O     . VAL A 1 2838 ? 242.490 182.758 225.395 1.00 10.09 ? 2838 VAL A O     1 
ATOM   10931 C  CB    . VAL A 1 2838 ? 241.065 182.390 222.420 1.00 3.30  ? 2838 VAL A CB    1 
ATOM   10932 C  CG1   . VAL A 1 2838 ? 239.960 182.249 223.452 1.00 3.84  ? 2838 VAL A CG1   1 
ATOM   10933 C  CG2   . VAL A 1 2838 ? 240.572 183.139 221.192 1.00 1.16  ? 2838 VAL A CG2   1 
ATOM   10934 N  N     . GLU A 1 2839 ? 243.539 181.289 224.060 1.00 6.93  ? 2839 GLU A N     1 
ATOM   10935 C  CA    . GLU A 1 2839 ? 243.927 180.392 225.136 1.00 7.66  ? 2839 GLU A CA    1 
ATOM   10936 C  C     . GLU A 1 2839 ? 245.336 180.691 225.633 1.00 6.85  ? 2839 GLU A C     1 
ATOM   10937 O  O     . GLU A 1 2839 ? 246.200 181.149 224.881 1.00 8.03  ? 2839 GLU A O     1 
ATOM   10938 C  CB    . GLU A 1 2839 ? 243.830 178.932 224.683 1.00 7.69  ? 2839 GLU A CB    1 
ATOM   10939 C  CG    . GLU A 1 2839 ? 242.406 178.368 224.547 1.00 9.80  ? 2839 GLU A CG    1 
ATOM   10940 C  CD    . GLU A 1 2839 ? 241.434 178.770 225.661 1.00 20.91 ? 2839 GLU A CD    1 
ATOM   10941 O  OE1   . GLU A 1 2839 ? 241.864 179.121 226.782 1.00 26.12 ? 2839 GLU A OE1   1 
ATOM   10942 O  OE2   . GLU A 1 2839 ? 240.214 178.735 225.406 1.00 25.35 ? 2839 GLU A OE2   1 
ATOM   10943 N  N     . ASP A 1 2840 ? 245.555 180.418 226.922 1.00 13.94 ? 2840 ASP A N     1 
ATOM   10944 C  CA    . ASP A 1 2840 ? 246.866 180.638 227.528 1.00 8.18  ? 2840 ASP A CA    1 
ATOM   10945 C  C     . ASP A 1 2840 ? 247.915 179.687 226.970 1.00 9.13  ? 2840 ASP A C     1 
ATOM   10946 O  O     . ASP A 1 2840 ? 249.095 180.045 226.893 1.00 12.07 ? 2840 ASP A O     1 
ATOM   10947 C  CB    . ASP A 1 2840 ? 246.771 180.487 229.045 1.00 11.47 ? 2840 ASP A CB    1 
ATOM   10948 C  CG    . ASP A 1 2840 ? 246.507 181.806 229.744 1.00 20.09 ? 2840 ASP A CG    1 
ATOM   10949 O  OD1   . ASP A 1 2840 ? 246.659 182.865 229.102 1.00 17.27 ? 2840 ASP A OD1   1 
ATOM   10950 O  OD2   . ASP A 1 2840 ? 246.146 181.783 230.939 1.00 23.24 ? 2840 ASP A OD2   1 
ATOM   10951 N  N     . GLU A 1 2841 ? 247.514 178.470 226.598 1.00 9.19  ? 2841 GLU A N     1 
ATOM   10952 C  CA    . GLU A 1 2841 ? 248.445 177.556 225.946 1.00 9.79  ? 2841 GLU A CA    1 
ATOM   10953 C  C     . GLU A 1 2841 ? 248.919 178.117 224.614 1.00 8.97  ? 2841 GLU A C     1 
ATOM   10954 O  O     . GLU A 1 2841 ? 250.108 178.032 224.281 1.00 9.57  ? 2841 GLU A O     1 
ATOM   10955 C  CB    . GLU A 1 2841 ? 247.783 176.193 225.745 1.00 7.90  ? 2841 GLU A CB    1 
ATOM   10956 C  CG    . GLU A 1 2841 ? 248.683 175.152 225.106 1.00 13.91 ? 2841 GLU A CG    1 
ATOM   10957 C  CD    . GLU A 1 2841 ? 249.865 174.775 225.975 1.00 27.24 ? 2841 GLU A CD    1 
ATOM   10958 O  OE1   . GLU A 1 2841 ? 249.769 174.909 227.214 1.00 22.46 ? 2841 GLU A OE1   1 
ATOM   10959 O  OE2   . GLU A 1 2841 ? 250.895 174.341 225.418 1.00 37.32 ? 2841 GLU A OE2   1 
ATOM   10960 N  N     . GLU A 1 2842 ? 248.001 178.697 223.837 1.00 4.32  ? 2842 GLU A N     1 
ATOM   10961 C  CA    . GLU A 1 2842 ? 248.371 179.279 222.552 1.00 4.32  ? 2842 GLU A CA    1 
ATOM   10962 C  C     . GLU A 1 2842 ? 249.323 180.453 222.735 1.00 3.22  ? 2842 GLU A C     1 
ATOM   10963 O  O     . GLU A 1 2842 ? 250.308 180.583 222.002 1.00 2.69  ? 2842 GLU A O     1 
ATOM   10964 C  CB    . GLU A 1 2842 ? 247.113 179.713 221.804 1.00 3.99  ? 2842 GLU A CB    1 
ATOM   10965 C  CG    . GLU A 1 2842 ? 246.189 178.569 221.445 1.00 3.98  ? 2842 GLU A CG    1 
ATOM   10966 C  CD    . GLU A 1 2842 ? 244.774 179.028 221.165 1.00 9.74  ? 2842 GLU A CD    1 
ATOM   10967 O  OE1   . GLU A 1 2842 ? 244.492 180.231 221.340 1.00 7.12  ? 2842 GLU A OE1   1 
ATOM   10968 O  OE2   . GLU A 1 2842 ? 243.940 178.184 220.775 1.00 12.90 ? 2842 GLU A OE2   1 
ATOM   10969 N  N     . ARG A 1 2843 ? 249.046 181.314 223.718 1.00 5.06  ? 2843 ARG A N     1 
ATOM   10970 C  CA    . ARG A 1 2843 ? 249.931 182.437 223.998 1.00 5.98  ? 2843 ARG A CA    1 
ATOM   10971 C  C     . ARG A 1 2843 ? 251.278 181.968 224.532 1.00 4.00  ? 2843 ARG A C     1 
ATOM   10972 O  O     . ARG A 1 2843 ? 252.309 182.583 224.236 1.00 2.17  ? 2843 ARG A O     1 
ATOM   10973 C  CB    . ARG A 1 2843 ? 249.260 183.397 224.982 1.00 2.69  ? 2843 ARG A CB    1 
ATOM   10974 C  CG    . ARG A 1 2843 ? 247.907 183.901 224.509 1.00 3.32  ? 2843 ARG A CG    1 
ATOM   10975 C  CD    . ARG A 1 2843 ? 247.383 185.039 225.365 1.00 6.01  ? 2843 ARG A CD    1 
ATOM   10976 N  NE    . ARG A 1 2843 ? 246.597 184.553 226.492 1.00 9.23  ? 2843 ARG A NE    1 
ATOM   10977 C  CZ    . ARG A 1 2843 ? 245.275 184.600 226.564 1.00 9.97  ? 2843 ARG A CZ    1 
ATOM   10978 N  NH1   . ARG A 1 2843 ? 244.547 185.121 225.590 1.00 6.63  ? 2843 ARG A NH1   1 
ATOM   10979 N  NH2   . ARG A 1 2843 ? 244.664 184.107 227.639 1.00 12.90 ? 2843 ARG A NH2   1 
ATOM   10980 N  N     . ARG A 1 2844 ? 251.288 180.892 225.320 1.00 5.33  ? 2844 ARG A N     1 
ATOM   10981 C  CA    . ARG A 1 2844 ? 252.548 180.338 225.804 1.00 3.98  ? 2844 ARG A CA    1 
ATOM   10982 C  C     . ARG A 1 2844 ? 253.394 179.805 224.655 1.00 3.14  ? 2844 ARG A C     1 
ATOM   10983 O  O     . ARG A 1 2844 ? 254.611 180.018 224.622 1.00 2.21  ? 2844 ARG A O     1 
ATOM   10984 C  CB    . ARG A 1 2844 ? 252.275 179.240 226.832 1.00 8.32  ? 2844 ARG A CB    1 
ATOM   10985 C  CG    . ARG A 1 2844 ? 253.305 179.157 227.942 1.00 8.96  ? 2844 ARG A CG    1 
ATOM   10986 C  CD    . ARG A 1 2844 ? 252.931 178.098 228.967 1.00 17.66 ? 2844 ARG A CD    1 
ATOM   10987 N  NE    . ARG A 1 2844 ? 251.662 178.389 229.622 1.00 21.25 ? 2844 ARG A NE    1 
ATOM   10988 C  CZ    . ARG A 1 2844 ? 250.549 177.689 229.447 1.00 22.01 ? 2844 ARG A CZ    1 
ATOM   10989 N  NH1   . ARG A 1 2844 ? 250.509 176.642 228.639 1.00 19.64 ? 2844 ARG A NH1   1 
ATOM   10990 N  NH2   . ARG A 1 2844 ? 249.447 178.052 230.096 1.00 16.64 ? 2844 ARG A NH2   1 
ATOM   10991 N  N     . TRP A 1 2845 ? 252.765 179.109 223.705 1.00 4.09  ? 2845 TRP A N     1 
ATOM   10992 C  CA    . TRP A 1 2845 ? 253.501 178.589 222.556 1.00 2.18  ? 2845 TRP A CA    1 
ATOM   10993 C  C     . TRP A 1 2845 ? 254.111 179.717 221.735 1.00 2.96  ? 2845 TRP A C     1 
ATOM   10994 O  O     . TRP A 1 2845 ? 255.274 179.640 221.325 1.00 4.85  ? 2845 TRP A O     1 
ATOM   10995 C  CB    . TRP A 1 2845 ? 252.581 177.734 221.686 1.00 2.06  ? 2845 TRP A CB    1 
ATOM   10996 C  CG    . TRP A 1 2845 ? 253.256 177.150 220.481 1.00 2.62  ? 2845 TRP A CG    1 
ATOM   10997 C  CD1   . TRP A 1 2845 ? 253.813 175.909 220.379 1.00 4.26  ? 2845 TRP A CD1   1 
ATOM   10998 C  CD2   . TRP A 1 2845 ? 253.445 177.779 219.208 1.00 3.19  ? 2845 TRP A CD2   1 
ATOM   10999 N  NE1   . TRP A 1 2845 ? 254.338 175.728 219.125 1.00 3.49  ? 2845 TRP A NE1   1 
ATOM   11000 C  CE2   . TRP A 1 2845 ? 254.124 176.860 218.385 1.00 3.53  ? 2845 TRP A CE2   1 
ATOM   11001 C  CE3   . TRP A 1 2845 ? 253.107 179.029 218.684 1.00 2.48  ? 2845 TRP A CE3   1 
ATOM   11002 C  CZ2   . TRP A 1 2845 ? 254.473 177.152 217.068 1.00 2.80  ? 2845 TRP A CZ2   1 
ATOM   11003 C  CZ3   . TRP A 1 2845 ? 253.455 179.319 217.379 1.00 4.58  ? 2845 TRP A CZ3   1 
ATOM   11004 C  CH2   . TRP A 1 2845 ? 254.129 178.383 216.586 1.00 4.01  ? 2845 TRP A CH2   1 
ATOM   11005 N  N     . THR A 1 2846 ? 253.334 180.774 221.480 1.00 3.33  ? 2846 THR A N     1 
ATOM   11006 C  CA    . THR A 1 2846 ? 253.840 181.900 220.706 1.00 2.44  ? 2846 THR A CA    1 
ATOM   11007 C  C     . THR A 1 2846 ? 255.002 182.577 221.420 1.00 2.69  ? 2846 THR A C     1 
ATOM   11008 O  O     . THR A 1 2846 ? 256.004 182.934 220.794 1.00 3.18  ? 2846 THR A O     1 
ATOM   11009 C  CB    . THR A 1 2846 ? 252.710 182.897 220.442 1.00 3.85  ? 2846 THR A CB    1 
ATOM   11010 O  OG1   . THR A 1 2846 ? 251.714 182.277 219.622 1.00 7.01  ? 2846 THR A OG1   1 
ATOM   11011 C  CG2   . THR A 1 2846 ? 253.232 184.140 219.738 1.00 1.30  ? 2846 THR A CG2   1 
ATOM   11012 N  N     . ASP A 1 2847 ? 254.886 182.749 222.737 1.00 4.00  ? 2847 ASP A N     1 
ATOM   11013 C  CA    . ASP A 1 2847 ? 255.952 183.377 223.506 1.00 4.43  ? 2847 ASP A CA    1 
ATOM   11014 C  C     . ASP A 1 2847 ? 257.233 182.551 223.460 1.00 5.93  ? 2847 ASP A C     1 
ATOM   11015 O  O     . ASP A 1 2847 ? 258.333 183.102 223.344 1.00 6.37  ? 2847 ASP A O     1 
ATOM   11016 C  CB    . ASP A 1 2847 ? 255.491 183.581 224.948 1.00 6.59  ? 2847 ASP A CB    1 
ATOM   11017 C  CG    . ASP A 1 2847 ? 256.274 184.658 225.663 1.00 18.52 ? 2847 ASP A CG    1 
ATOM   11018 O  OD1   . ASP A 1 2847 ? 256.290 185.808 225.178 1.00 16.56 ? 2847 ASP A OD1   1 
ATOM   11019 O  OD2   . ASP A 1 2847 ? 256.876 184.352 226.714 1.00 22.98 ? 2847 ASP A OD2   1 
ATOM   11020 N  N     . GLU A 1 2848 ? 257.107 181.225 223.548 1.00 8.07  ? 2848 GLU A N     1 
ATOM   11021 C  CA    . GLU A 1 2848 ? 258.290 180.369 223.551 1.00 4.66  ? 2848 GLU A CA    1 
ATOM   11022 C  C     . GLU A 1 2848 ? 258.967 180.340 222.185 1.00 6.96  ? 2848 GLU A C     1 
ATOM   11023 O  O     . GLU A 1 2848 ? 260.193 180.464 222.091 1.00 10.45 ? 2848 GLU A O     1 
ATOM   11024 C  CB    . GLU A 1 2848 ? 257.909 178.957 223.989 1.00 5.84  ? 2848 GLU A CB    1 
ATOM   11025 C  CG    . GLU A 1 2848 ? 258.947 177.901 223.658 1.00 17.36 ? 2848 GLU A CG    1 
ATOM   11026 C  CD    . GLU A 1 2848 ? 260.227 178.073 224.454 1.00 23.35 ? 2848 GLU A CD    1 
ATOM   11027 O  OE1   . GLU A 1 2848 ? 261.266 178.405 223.846 1.00 18.97 ? 2848 GLU A OE1   1 
ATOM   11028 O  OE2   . GLU A 1 2848 ? 260.192 177.876 225.686 1.00 21.86 ? 2848 GLU A OE2   1 
ATOM   11029 N  N     . ASN A 1 2849 ? 258.186 180.189 221.115 1.00 7.95  ? 2849 ASN A N     1 
ATOM   11030 C  CA    . ASN A 1 2849 ? 258.767 180.014 219.791 1.00 4.56  ? 2849 ASN A CA    1 
ATOM   11031 C  C     . ASN A 1 2849 ? 259.334 181.307 219.220 1.00 5.60  ? 2849 ASN A C     1 
ATOM   11032 O  O     . ASN A 1 2849 ? 260.147 181.253 218.294 1.00 7.14  ? 2849 ASN A O     1 
ATOM   11033 C  CB    . ASN A 1 2849 ? 257.729 179.417 218.845 1.00 4.52  ? 2849 ASN A CB    1 
ATOM   11034 C  CG    . ASN A 1 2849 ? 257.559 177.924 219.047 1.00 8.87  ? 2849 ASN A CG    1 
ATOM   11035 O  OD1   . ASN A 1 2849 ? 256.680 177.482 219.784 1.00 6.03  ? 2849 ASN A OD1   1 
ATOM   11036 N  ND2   . ASN A 1 2849 ? 258.411 177.138 218.400 1.00 10.33 ? 2849 ASN A ND2   1 
ATOM   11037 N  N     . ILE A 1 2850 ? 258.924 182.463 219.747 1.00 5.01  ? 2850 ILE A N     1 
ATOM   11038 C  CA    . ILE A 1 2850 ? 259.590 183.710 219.386 1.00 3.85  ? 2850 ILE A CA    1 
ATOM   11039 C  C     . ILE A 1 2850 ? 261.044 183.673 219.837 1.00 7.93  ? 2850 ILE A C     1 
ATOM   11040 O  O     . ILE A 1 2850 ? 261.953 184.073 219.100 1.00 9.79  ? 2850 ILE A O     1 
ATOM   11041 C  CB    . ILE A 1 2850 ? 258.833 184.912 219.983 1.00 4.53  ? 2850 ILE A CB    1 
ATOM   11042 C  CG1   . ILE A 1 2850 ? 257.568 185.198 219.177 1.00 3.60  ? 2850 ILE A CG1   1 
ATOM   11043 C  CG2   . ILE A 1 2850 ? 259.707 186.149 220.013 1.00 2.87  ? 2850 ILE A CG2   1 
ATOM   11044 C  CD1   . ILE A 1 2850 ? 256.684 186.256 219.779 1.00 2.17  ? 2850 ILE A CD1   1 
ATOM   11045 N  N     . ASP A 1 2851 ? 261.286 183.180 221.054 1.00 10.15 ? 2851 ASP A N     1 
ATOM   11046 C  CA    . ASP A 1 2851 ? 262.652 183.024 221.540 1.00 9.22  ? 2851 ASP A CA    1 
ATOM   11047 C  C     . ASP A 1 2851 ? 263.416 181.979 220.738 1.00 11.14 ? 2851 ASP A C     1 
ATOM   11048 O  O     . ASP A 1 2851 ? 264.601 182.161 220.438 1.00 15.64 ? 2851 ASP A O     1 
ATOM   11049 C  CB    . ASP A 1 2851 ? 262.635 182.659 223.024 1.00 10.76 ? 2851 ASP A CB    1 
ATOM   11050 C  CG    . ASP A 1 2851 ? 261.980 183.726 223.879 1.00 15.28 ? 2851 ASP A CG    1 
ATOM   11051 O  OD1   . ASP A 1 2851 ? 262.473 184.872 223.887 1.00 19.77 ? 2851 ASP A OD1   1 
ATOM   11052 O  OD2   . ASP A 1 2851 ? 260.966 183.420 224.536 1.00 19.26 ? 2851 ASP A OD2   1 
ATOM   11053 N  N     . THR A 1 2852 ? 262.756 180.872 220.389 1.00 5.86  ? 2852 THR A N     1 
ATOM   11054 C  CA    . THR A 1 2852 ? 263.426 179.807 219.648 1.00 6.66  ? 2852 THR A CA    1 
ATOM   11055 C  C     . THR A 1 2852 ? 263.870 180.282 218.270 1.00 9.92  ? 2852 THR A C     1 
ATOM   11056 O  O     . THR A 1 2852 ? 265.015 180.057 217.861 1.00 11.47 ? 2852 THR A O     1 
ATOM   11057 C  CB    . THR A 1 2852 ? 262.498 178.597 219.521 1.00 7.93  ? 2852 THR A CB    1 
ATOM   11058 O  OG1   . THR A 1 2852 ? 262.152 178.114 220.824 1.00 13.95 ? 2852 THR A OG1   1 
ATOM   11059 C  CG2   . THR A 1 2852 ? 263.175 177.488 218.734 1.00 10.79 ? 2852 THR A CG2   1 
ATOM   11060 N  N     . VAL A 1 2853 ? 262.972 180.946 217.538 1.00 7.29  ? 2853 VAL A N     1 
ATOM   11061 C  CA    . VAL A 1 2853 ? 263.293 181.393 216.187 1.00 5.71  ? 2853 VAL A CA    1 
ATOM   11062 C  C     . VAL A 1 2853 ? 264.402 182.439 216.212 1.00 6.45  ? 2853 VAL A C     1 
ATOM   11063 O  O     . VAL A 1 2853 ? 265.322 182.405 215.388 1.00 12.02 ? 2853 VAL A O     1 
ATOM   11064 C  CB    . VAL A 1 2853 ? 262.026 181.920 215.486 1.00 6.98  ? 2853 VAL A CB    1 
ATOM   11065 C  CG1   . VAL A 1 2853 ? 262.383 182.632 214.196 1.00 3.43  ? 2853 VAL A CG1   1 
ATOM   11066 C  CG2   . VAL A 1 2853 ? 261.059 180.779 215.212 1.00 1.93  ? 2853 VAL A CG2   1 
ATOM   11067 N  N     . ALA A 1 2854 ? 264.338 183.376 217.160 1.00 6.40  ? 2854 ALA A N     1 
ATOM   11068 C  CA    . ALA A 1 2854 ? 265.301 184.474 217.190 1.00 5.62  ? 2854 ALA A CA    1 
ATOM   11069 C  C     . ALA A 1 2854 ? 266.722 183.974 217.418 1.00 10.06 ? 2854 ALA A C     1 
ATOM   11070 O  O     . ALA A 1 2854 ? 267.660 184.431 216.756 1.00 16.97 ? 2854 ALA A O     1 
ATOM   11071 C  CB    . ALA A 1 2854 ? 264.913 185.481 218.270 1.00 4.11  ? 2854 ALA A CB    1 
ATOM   11072 N  N     . LEU A 1 2855 ? 266.906 183.047 218.358 1.00 11.76 ? 2855 LEU A N     1 
ATOM   11073 C  CA    . LEU A 1 2855 ? 268.253 182.561 218.647 1.00 13.78 ? 2855 LEU A CA    1 
ATOM   11074 C  C     . LEU A 1 2855 ? 268.759 181.616 217.567 1.00 14.02 ? 2855 LEU A C     1 
ATOM   11075 O  O     . LEU A 1 2855 ? 269.974 181.482 217.386 1.00 22.49 ? 2855 LEU A O     1 
ATOM   11076 C  CB    . LEU A 1 2855 ? 268.295 181.886 220.019 1.00 16.01 ? 2855 LEU A CB    1 
ATOM   11077 C  CG    . LEU A 1 2855 ? 268.493 182.791 221.242 1.00 19.30 ? 2855 LEU A CG    1 
ATOM   11078 C  CD1   . LEU A 1 2855 ? 269.857 183.461 221.179 1.00 22.86 ? 2855 LEU A CD1   1 
ATOM   11079 C  CD2   . LEU A 1 2855 ? 267.397 183.839 221.375 1.00 13.03 ? 2855 LEU A CD2   1 
ATOM   11080 N  N     . LYS A 1 2856 ? 267.855 180.953 216.848 1.00 7.19  ? 2856 LYS A N     1 
ATOM   11081 C  CA    . LYS A 1 2856 ? 268.281 180.104 215.741 1.00 8.51  ? 2856 LYS A CA    1 
ATOM   11082 C  C     . LYS A 1 2856 ? 268.919 180.929 214.631 1.00 8.44  ? 2856 LYS A C     1 
ATOM   11083 O  O     . LYS A 1 2856 ? 269.926 180.518 214.042 1.00 11.88 ? 2856 LYS A O     1 
ATOM   11084 C  CB    . LYS A 1 2856 ? 267.095 179.299 215.211 1.00 7.08  ? 2856 LYS A CB    1 
ATOM   11085 C  CG    . LYS A 1 2856 ? 267.347 178.630 213.873 1.00 7.57  ? 2856 LYS A CG    1 
ATOM   11086 C  CD    . LYS A 1 2856 ? 266.077 178.018 213.320 1.00 12.06 ? 2856 LYS A CD    1 
ATOM   11087 C  CE    . LYS A 1 2856 ? 266.282 177.514 211.903 1.00 11.30 ? 2856 LYS A CE    1 
ATOM   11088 N  NZ    . LYS A 1 2856 ? 265.055 176.855 211.374 1.00 13.10 ? 2856 LYS A NZ    1 
ATOM   11089 N  N     . HIS A 1 2857 ? 268.354 182.100 214.337 1.00 6.32  ? 2857 HIS A N     1 
ATOM   11090 C  CA    . HIS A 1 2857 ? 268.881 182.962 213.288 1.00 6.34  ? 2857 HIS A CA    1 
ATOM   11091 C  C     . HIS A 1 2857 ? 269.829 184.035 213.802 1.00 8.07  ? 2857 HIS A C     1 
ATOM   11092 O  O     . HIS A 1 2857 ? 270.566 184.620 213.003 1.00 9.73  ? 2857 HIS A O     1 
ATOM   11093 C  CB    . HIS A 1 2857 ? 267.736 183.632 212.521 1.00 4.87  ? 2857 HIS A CB    1 
ATOM   11094 C  CG    . HIS A 1 2857 ? 266.775 182.665 211.909 1.00 6.17  ? 2857 HIS A CG    1 
ATOM   11095 N  ND1   . HIS A 1 2857 ? 266.973 182.107 210.666 1.00 5.93  ? 2857 HIS A ND1   1 
ATOM   11096 C  CD2   . HIS A 1 2857 ? 265.610 182.153 212.369 1.00 7.29  ? 2857 HIS A CD2   1 
ATOM   11097 C  CE1   . HIS A 1 2857 ? 265.973 181.292 210.386 1.00 7.74  ? 2857 HIS A CE1   1 
ATOM   11098 N  NE2   . HIS A 1 2857 ? 265.130 181.304 211.402 1.00 6.52  ? 2857 HIS A NE2   1 
ATOM   11099 N  N     . PHE A 1 2858 ? 269.836 184.308 215.105 1.00 10.23 ? 2858 PHE A N     1 
ATOM   11100 C  CA    . PHE A 1 2858 ? 270.718 185.314 215.695 1.00 9.82  ? 2858 PHE A CA    1 
ATOM   11101 C  C     . PHE A 1 2858 ? 271.475 184.706 216.868 1.00 17.01 ? 2858 PHE A C     1 
ATOM   11102 O  O     . PHE A 1 2858 ? 271.126 184.939 218.032 1.00 23.00 ? 2858 PHE A O     1 
ATOM   11103 C  CB    . PHE A 1 2858 ? 269.931 186.549 216.134 1.00 5.07  ? 2858 PHE A CB    1 
ATOM   11104 C  CG    . PHE A 1 2858 ? 269.403 187.366 214.994 1.00 4.76  ? 2858 PHE A CG    1 
ATOM   11105 C  CD1   . PHE A 1 2858 ? 270.176 188.363 214.423 1.00 3.87  ? 2858 PHE A CD1   1 
ATOM   11106 C  CD2   . PHE A 1 2858 ? 268.136 187.134 214.485 1.00 3.76  ? 2858 PHE A CD2   1 
ATOM   11107 C  CE1   . PHE A 1 2858 ? 269.694 189.113 213.373 1.00 2.98  ? 2858 PHE A CE1   1 
ATOM   11108 C  CE2   . PHE A 1 2858 ? 267.650 187.882 213.436 1.00 1.88  ? 2858 PHE A CE2   1 
ATOM   11109 C  CZ    . PHE A 1 2858 ? 268.428 188.873 212.879 1.00 1.46  ? 2858 PHE A CZ    1 
ATOM   11110 N  N     . PRO A 1 2859 ? 272.505 183.912 216.603 1.00 19.92 ? 2859 PRO A N     1 
ATOM   11111 C  CA    . PRO A 1 2859 ? 273.396 183.463 217.674 1.00 19.71 ? 2859 PRO A CA    1 
ATOM   11112 C  C     . PRO A 1 2859 ? 274.267 184.622 218.145 1.00 20.92 ? 2859 PRO A C     1 
ATOM   11113 O  O     . PRO A 1 2859 ? 274.239 185.719 217.590 1.00 28.90 ? 2859 PRO A O     1 
ATOM   11114 C  CB    . PRO A 1 2859 ? 274.237 182.375 217.003 1.00 18.65 ? 2859 PRO A CB    1 
ATOM   11115 C  CG    . PRO A 1 2859 ? 273.424 181.909 215.863 1.00 14.30 ? 2859 PRO A CG    1 
ATOM   11116 C  CD    . PRO A 1 2859 ? 272.703 183.125 215.373 1.00 18.88 ? 2859 PRO A CD    1 
ATOM   11117 N  N     . ASN A 1 2860 ? 275.055 184.353 219.186 1.00 15.44 ? 2860 ASN A N     1 
ATOM   11118 C  CA    . ASN A 1 2860 ? 276.059 185.295 219.679 1.00 21.10 ? 2860 ASN A CA    1 
ATOM   11119 C  C     . ASN A 1 2860 ? 275.433 186.634 220.062 1.00 22.64 ? 2860 ASN A C     1 
ATOM   11120 O  O     . ASN A 1 2860 ? 276.008 187.698 219.831 1.00 29.23 ? 2860 ASN A O     1 
ATOM   11121 C  CB    . ASN A 1 2860 ? 277.174 185.491 218.652 1.00 19.31 ? 2860 ASN A CB    1 
ATOM   11122 C  CG    . ASN A 1 2860 ? 277.581 184.194 217.983 1.00 25.09 ? 2860 ASN A CG    1 
ATOM   11123 O  OD1   . ASN A 1 2860 ? 277.460 184.045 216.768 1.00 26.61 ? 2860 ASN A OD1   1 
ATOM   11124 N  ND2   . ASN A 1 2860 ? 278.055 183.242 218.778 1.00 22.11 ? 2860 ASN A ND2   1 
ATOM   11125 N  N     . ILE A 1 2861 ? 274.242 186.579 220.653 1.00 19.70 ? 2861 ILE A N     1 
ATOM   11126 C  CA    . ILE A 1 2861 ? 273.556 187.761 221.153 1.00 17.14 ? 2861 ILE A CA    1 
ATOM   11127 C  C     . ILE A 1 2861 ? 273.238 187.533 222.621 1.00 19.63 ? 2861 ILE A C     1 
ATOM   11128 O  O     . ILE A 1 2861 ? 273.119 186.392 223.080 1.00 26.07 ? 2861 ILE A O     1 
ATOM   11129 C  CB    . ILE A 1 2861 ? 272.265 188.073 220.367 1.00 19.49 ? 2861 ILE A CB    1 
ATOM   11130 C  CG1   . ILE A 1 2861 ? 271.266 186.923 220.510 1.00 20.29 ? 2861 ILE A CG1   1 
ATOM   11131 C  CG2   . ILE A 1 2861 ? 272.580 188.334 218.905 1.00 21.44 ? 2861 ILE A CG2   1 
ATOM   11132 C  CD1   . ILE A 1 2861 ? 269.892 187.243 219.971 1.00 24.77 ? 2861 ILE A CD1   1 
ATOM   11133 N  N     . ASP A 1 2862 ? 273.099 188.627 223.362 1.00 20.35 ? 2862 ASP A N     1 
ATOM   11134 C  CA    . ASP A 1 2862 ? 272.793 188.545 224.788 1.00 21.40 ? 2862 ASP A CA    1 
ATOM   11135 C  C     . ASP A 1 2862 ? 271.288 188.328 224.913 1.00 21.09 ? 2862 ASP A C     1 
ATOM   11136 O  O     . ASP A 1 2862 ? 270.495 189.245 224.690 1.00 22.01 ? 2862 ASP A O     1 
ATOM   11137 C  CB    . ASP A 1 2862 ? 273.267 189.802 225.512 1.00 14.26 ? 2862 ASP A CB    1 
ATOM   11138 C  CG    . ASP A 1 2862 ? 272.699 189.936 226.921 1.00 26.37 ? 2862 ASP A CG    1 
ATOM   11139 O  OD1   . ASP A 1 2862 ? 272.199 188.940 227.487 1.00 22.58 ? 2862 ASP A OD1   1 
ATOM   11140 O  OD2   . ASP A 1 2862 ? 272.770 191.052 227.476 1.00 36.54 ? 2862 ASP A OD2   1 
ATOM   11141 N  N     . ARG A 1 2863 ? 270.903 187.105 225.283 1.00 21.47 ? 2863 ARG A N     1 
ATOM   11142 C  CA    . ARG A 1 2863 ? 269.493 186.724 225.313 1.00 20.92 ? 2863 ARG A CA    1 
ATOM   11143 C  C     . ARG A 1 2863 ? 268.685 187.619 226.244 1.00 24.77 ? 2863 ARG A C     1 
ATOM   11144 O  O     . ARG A 1 2863 ? 267.589 188.070 225.893 1.00 23.74 ? 2863 ARG A O     1 
ATOM   11145 C  CB    . ARG A 1 2863 ? 269.366 185.261 225.741 1.00 15.56 ? 2863 ARG A CB    1 
ATOM   11146 C  CG    . ARG A 1 2863 ? 267.953 184.701 225.734 1.00 26.07 ? 2863 ARG A CG    1 
ATOM   11147 C  CD    . ARG A 1 2863 ? 267.971 183.219 226.092 1.00 28.60 ? 2863 ARG A CD    1 
ATOM   11148 N  NE    . ARG A 1 2863 ? 266.638 182.637 226.191 1.00 24.59 ? 2863 ARG A NE    1 
ATOM   11149 C  CZ    . ARG A 1 2863 ? 265.952 182.131 225.175 1.00 26.91 ? 2863 ARG A CZ    1 
ATOM   11150 N  NH1   . ARG A 1 2863 ? 266.448 182.106 223.950 1.00 28.42 ? 2863 ARG A NH1   1 
ATOM   11151 N  NH2   . ARG A 1 2863 ? 264.741 181.627 225.396 1.00 26.67 ? 2863 ARG A NH2   1 
ATOM   11152 N  N     . GLU A 1 2864 ? 269.212 187.888 227.442 1.00 25.23 ? 2864 GLU A N     1 
ATOM   11153 C  CA    . GLU A 1 2864 ? 268.433 188.599 228.451 1.00 20.07 ? 2864 GLU A CA    1 
ATOM   11154 C  C     . GLU A 1 2864 ? 268.118 190.025 228.015 1.00 23.25 ? 2864 GLU A C     1 
ATOM   11155 O  O     . GLU A 1 2864 ? 266.975 190.482 228.145 1.00 26.27 ? 2864 GLU A O     1 
ATOM   11156 C  CB    . GLU A 1 2864 ? 269.178 188.576 229.788 1.00 24.66 ? 2864 GLU A CB    1 
ATOM   11157 C  CG    . GLU A 1 2864 ? 268.572 189.435 230.897 1.00 27.43 ? 2864 GLU A CG    1 
ATOM   11158 C  CD    . GLU A 1 2864 ? 269.109 190.854 230.913 1.00 32.41 ? 2864 GLU A CD    1 
ATOM   11159 O  OE1   . GLU A 1 2864 ? 270.010 191.161 230.104 1.00 30.05 ? 2864 GLU A OE1   1 
ATOM   11160 O  OE2   . GLU A 1 2864 ? 268.635 191.660 231.740 1.00 33.93 ? 2864 GLU A OE2   1 
ATOM   11161 N  N     . LYS A 1 2865 ? 269.109 190.744 227.484 1.00 20.80 ? 2865 LYS A N     1 
ATOM   11162 C  CA    . LYS A 1 2865 ? 268.893 192.133 227.098 1.00 19.49 ? 2865 LYS A CA    1 
ATOM   11163 C  C     . LYS A 1 2865 ? 267.998 192.261 225.874 1.00 21.55 ? 2865 LYS A C     1 
ATOM   11164 O  O     . LYS A 1 2865 ? 267.375 193.314 225.687 1.00 31.54 ? 2865 LYS A O     1 
ATOM   11165 C  CB    . LYS A 1 2865 ? 270.244 192.819 226.859 1.00 18.87 ? 2865 LYS A CB    1 
ATOM   11166 C  CG    . LYS A 1 2865 ? 270.197 194.339 226.662 1.00 26.23 ? 2865 LYS A CG    1 
ATOM   11167 C  CD    . LYS A 1 2865 ? 270.088 194.755 225.200 1.00 20.05 ? 2865 LYS A CD    1 
ATOM   11168 C  CE    . LYS A 1 2865 ? 270.107 196.273 225.067 1.00 25.75 ? 2865 LYS A CE    1 
ATOM   11169 N  NZ    . LYS A 1 2865 ? 269.968 196.723 223.654 1.00 15.30 ? 2865 LYS A NZ    1 
ATOM   11170 N  N     . ALA A 1 2866 ? 267.896 191.221 225.062 1.00 19.24 ? 2866 ALA A N     1 
ATOM   11171 C  CA    . ALA A 1 2866 ? 267.071 191.246 223.865 1.00 15.28 ? 2866 ALA A CA    1 
ATOM   11172 C  C     . ALA A 1 2866 ? 265.713 190.588 224.037 1.00 15.11 ? 2866 ALA A C     1 
ATOM   11173 O  O     . ALA A 1 2866 ? 264.766 190.983 223.355 1.00 17.44 ? 2866 ALA A O     1 
ATOM   11174 C  CB    . ALA A 1 2866 ? 267.803 190.563 222.699 1.00 15.93 ? 2866 ALA A CB    1 
ATOM   11175 N  N     . MET A 1 2867 ? 265.580 189.608 224.932 1.00 19.24 ? 2867 MET A N     1 
ATOM   11176 C  CA    . MET A 1 2867 ? 264.362 188.813 224.998 1.00 11.95 ? 2867 MET A CA    1 
ATOM   11177 C  C     . MET A 1 2867 ? 263.762 188.766 226.401 1.00 14.57 ? 2867 MET A C     1 
ATOM   11178 O  O     . MET A 1 2867 ? 263.048 187.815 226.727 1.00 20.21 ? 2867 MET A O     1 
ATOM   11179 C  CB    . MET A 1 2867 ? 264.628 187.399 224.486 1.00 17.37 ? 2867 MET A CB    1 
ATOM   11180 C  CG    . MET A 1 2867 ? 264.923 187.358 222.996 1.00 19.86 ? 2867 MET A CG    1 
ATOM   11181 S  SD    . MET A 1 2867 ? 263.545 187.966 222.015 1.00 34.54 ? 2867 MET A SD    1 
ATOM   11182 C  CE    . MET A 1 2867 ? 263.063 186.494 221.138 1.00 15.18 ? 2867 MET A CE    1 
ATOM   11183 N  N     . SER A 1 2868 ? 264.034 189.769 227.233 1.00 14.03 ? 2868 SER A N     1 
ATOM   11184 C  CA    . SER A 1 2868 ? 263.396 189.874 228.541 1.00 9.70  ? 2868 SER A CA    1 
ATOM   11185 C  C     . SER A 1 2868 ? 261.884 189.884 228.388 1.00 13.41 ? 2868 SER A C     1 
ATOM   11186 O  O     . SER A 1 2868 ? 261.326 190.749 227.707 1.00 19.18 ? 2868 SER A O     1 
ATOM   11187 C  CB    . SER A 1 2868 ? 263.861 191.146 229.254 1.00 12.26 ? 2868 SER A CB    1 
ATOM   11188 O  OG    . SER A 1 2868 ? 265.250 191.109 229.524 1.00 21.04 ? 2868 SER A OG    1 
ATOM   11189 N  N     . ARG A 1 2869 ? 261.222 188.922 229.033 1.00 15.92 ? 2869 ARG A N     1 
ATOM   11190 C  CA    . ARG A 1 2869 ? 259.819 188.625 228.738 1.00 15.98 ? 2869 ARG A CA    1 
ATOM   11191 C  C     . ARG A 1 2869 ? 258.880 189.821 228.832 1.00 22.65 ? 2869 ARG A C     1 
ATOM   11192 O  O     . ARG A 1 2869 ? 258.008 189.954 227.960 1.00 33.44 ? 2869 ARG A O     1 
ATOM   11193 C  CB    . ARG A 1 2869 ? 259.356 187.463 229.627 1.00 20.51 ? 2869 ARG A CB    1 
ATOM   11194 C  CG    . ARG A 1 2869 ? 259.882 186.081 229.199 1.00 20.09 ? 2869 ARG A CG    1 
ATOM   11195 C  CD    . ARG A 1 2869 ? 259.516 185.728 227.746 1.00 24.96 ? 2869 ARG A CD    1 
ATOM   11196 N  NE    . ARG A 1 2869 ? 260.308 186.425 226.736 1.00 23.05 ? 2869 ARG A NE    1 
ATOM   11197 C  CZ    . ARG A 1 2869 ? 260.098 186.349 225.428 1.00 16.05 ? 2869 ARG A CZ    1 
ATOM   11198 N  NH1   . ARG A 1 2869 ? 259.103 185.638 224.929 1.00 13.66 ? 2869 ARG A NH1   1 
ATOM   11199 N  NH2   . ARG A 1 2869 ? 260.903 187.010 224.604 1.00 14.18 ? 2869 ARG A NH2   1 
ATOM   11200 N  N     . PRO A 1 2870 ? 258.980 190.713 229.824 1.00 18.85 ? 2870 PRO A N     1 
ATOM   11201 C  CA    . PRO A 1 2870 ? 258.152 191.926 229.762 1.00 11.33 ? 2870 PRO A CA    1 
ATOM   11202 C  C     . PRO A 1 2870 ? 258.646 192.887 228.689 1.00 6.55  ? 2870 PRO A C     1 
ATOM   11203 O  O     . PRO A 1 2870 ? 259.361 193.847 228.986 1.00 9.11  ? 2870 PRO A O     1 
ATOM   11204 C  CB    . PRO A 1 2870 ? 258.289 192.519 231.169 1.00 8.10  ? 2870 PRO A CB    1 
ATOM   11205 C  CG    . PRO A 1 2870 ? 259.595 192.011 231.659 1.00 11.67 ? 2870 PRO A CG    1 
ATOM   11206 C  CD    . PRO A 1 2870 ? 259.743 190.637 231.084 1.00 10.93 ? 2870 PRO A CD    1 
ATOM   11207 N  N     . ILE A 1 2871 ? 258.280 192.630 227.435 1.00 4.05  ? 2871 ILE A N     1 
ATOM   11208 C  CA    . ILE A 1 2871 ? 258.670 193.485 226.317 1.00 4.84  ? 2871 ILE A CA    1 
ATOM   11209 C  C     . ILE A 1 2871 ? 257.621 194.580 226.171 1.00 2.22  ? 2871 ILE A C     1 
ATOM   11210 O  O     . ILE A 1 2871 ? 256.499 194.323 225.729 1.00 4.27  ? 2871 ILE A O     1 
ATOM   11211 C  CB    . ILE A 1 2871 ? 258.816 192.691 225.014 1.00 5.10  ? 2871 ILE A CB    1 
ATOM   11212 C  CG1   . ILE A 1 2871 ? 259.574 191.387 225.250 1.00 5.27  ? 2871 ILE A CG1   1 
ATOM   11213 C  CG2   . ILE A 1 2871 ? 259.526 193.534 223.969 1.00 3.67  ? 2871 ILE A CG2   1 
ATOM   11214 C  CD1   . ILE A 1 2871 ? 259.887 190.629 223.987 1.00 5.49  ? 2871 ILE A CD1   1 
ATOM   11215 N  N     . LEU A 1 2872 ? 257.989 195.807 226.527 1.00 2.36  ? 2872 LEU A N     1 
ATOM   11216 C  CA    . LEU A 1 2872 ? 257.079 196.940 226.463 1.00 2.01  ? 2872 LEU A CA    1 
ATOM   11217 C  C     . LEU A 1 2872 ? 257.741 198.076 225.703 1.00 1.27  ? 2872 LEU A C     1 
ATOM   11218 O  O     . LEU A 1 2872 ? 258.904 198.405 225.957 1.00 1.51  ? 2872 LEU A O     1 
ATOM   11219 C  CB    . LEU A 1 2872 ? 256.667 197.406 227.862 1.00 5.09  ? 2872 LEU A CB    1 
ATOM   11220 C  CG    . LEU A 1 2872 ? 256.096 196.324 228.779 1.00 2.90  ? 2872 LEU A CG    1 
ATOM   11221 C  CD1   . LEU A 1 2872 ? 256.014 196.826 230.208 1.00 4.04  ? 2872 LEU A CD1   1 
ATOM   11222 C  CD2   . LEU A 1 2872 ? 254.735 195.869 228.282 1.00 1.44  ? 2872 LEU A CD2   1 
ATOM   11223 N  N     . TYR A 1 2873 ? 257.000 198.668 224.774 1.00 1.68  ? 2873 TYR A N     1 
ATOM   11224 C  CA    . TYR A 1 2873 ? 257.466 199.804 223.997 1.00 1.03  ? 2873 TYR A CA    1 
ATOM   11225 C  C     . TYR A 1 2873 ? 256.453 200.930 224.116 1.00 0.67  ? 2873 TYR A C     1 
ATOM   11226 O  O     . TYR A 1 2873 ? 255.244 200.690 224.114 1.00 0.77  ? 2873 TYR A O     1 
ATOM   11227 C  CB    . TYR A 1 2873 ? 257.669 199.427 222.527 1.00 0.45  ? 2873 TYR A CB    1 
ATOM   11228 C  CG    . TYR A 1 2873 ? 259.007 198.790 222.245 1.00 0.38  ? 2873 TYR A CG    1 
ATOM   11229 C  CD1   . TYR A 1 2873 ? 259.245 197.461 222.563 1.00 0.73  ? 2873 TYR A CD1   1 
ATOM   11230 C  CD2   . TYR A 1 2873 ? 260.032 199.516 221.662 1.00 0.54  ? 2873 TYR A CD2   1 
ATOM   11231 C  CE1   . TYR A 1 2873 ? 260.466 196.875 222.308 1.00 0.48  ? 2873 TYR A CE1   1 
ATOM   11232 C  CE2   . TYR A 1 2873 ? 261.253 198.938 221.402 1.00 0.69  ? 2873 TYR A CE2   1 
ATOM   11233 C  CZ    . TYR A 1 2873 ? 261.467 197.620 221.728 1.00 0.55  ? 2873 TYR A CZ    1 
ATOM   11234 O  OH    . TYR A 1 2873 ? 262.686 197.046 221.469 1.00 2.50  ? 2873 TYR A OH    1 
ATOM   11235 N  N     . SER A 1 2874 ? 256.953 202.156 224.232 1.00 0.65  ? 2874 SER A N     1 
ATOM   11236 C  CA    . SER A 1 2874 ? 256.072 203.302 224.392 1.00 1.33  ? 2874 SER A CA    1 
ATOM   11237 C  C     . SER A 1 2874 ? 256.793 204.560 223.941 1.00 1.80  ? 2874 SER A C     1 
ATOM   11238 O  O     . SER A 1 2874 ? 258.023 204.642 223.989 1.00 2.12  ? 2874 SER A O     1 
ATOM   11239 C  CB    . SER A 1 2874 ? 255.609 203.450 225.848 1.00 0.72  ? 2874 SER A CB    1 
ATOM   11240 O  OG    . SER A 1 2874 ? 254.613 204.447 225.967 1.00 0.81  ? 2874 SER A OG    1 
ATOM   11241 N  N     . ASN A 1 2875 ? 256.006 205.541 223.501 1.00 2.04  ? 2875 ASN A N     1 
ATOM   11242 C  CA    . ASN A 1 2875 ? 256.489 206.893 223.261 1.00 3.24  ? 2875 ASN A CA    1 
ATOM   11243 C  C     . ASN A 1 2875 ? 255.954 207.870 224.302 1.00 7.61  ? 2875 ASN A C     1 
ATOM   11244 O  O     . ASN A 1 2875 ? 255.890 209.074 224.048 1.00 11.21 ? 2875 ASN A O     1 
ATOM   11245 C  CB    . ASN A 1 2875 ? 256.120 207.352 221.849 1.00 2.51  ? 2875 ASN A CB    1 
ATOM   11246 C  CG    . ASN A 1 2875 ? 254.654 207.148 221.533 1.00 4.36  ? 2875 ASN A CG    1 
ATOM   11247 O  OD1   . ASN A 1 2875 ? 253.875 206.731 222.386 1.00 7.37  ? 2875 ASN A OD1   1 
ATOM   11248 N  ND2   . ASN A 1 2875 ? 254.272 207.437 220.296 1.00 6.14  ? 2875 ASN A ND2   1 
ATOM   11249 N  N     . TRP A 1 2876 ? 255.558 207.362 225.470 1.00 2.37  ? 2876 TRP A N     1 
ATOM   11250 C  CA    . TRP A 1 2876 ? 254.981 208.208 226.507 1.00 3.09  ? 2876 TRP A CA    1 
ATOM   11251 C  C     . TRP A 1 2876 ? 256.039 208.841 227.402 1.00 9.05  ? 2876 TRP A C     1 
ATOM   11252 O  O     . TRP A 1 2876 ? 255.814 209.931 227.935 1.00 10.94 ? 2876 TRP A O     1 
ATOM   11253 C  CB    . TRP A 1 2876 ? 254.004 207.397 227.355 1.00 1.85  ? 2876 TRP A CB    1 
ATOM   11254 C  CG    . TRP A 1 2876 ? 252.702 207.126 226.679 1.00 1.78  ? 2876 TRP A CG    1 
ATOM   11255 C  CD1   . TRP A 1 2876 ? 252.220 207.734 225.559 1.00 2.10  ? 2876 TRP A CD1   1 
ATOM   11256 C  CD2   . TRP A 1 2876 ? 251.706 206.184 227.085 1.00 1.03  ? 2876 TRP A CD2   1 
ATOM   11257 N  NE1   . TRP A 1 2876 ? 250.987 207.224 225.238 1.00 0.96  ? 2876 TRP A NE1   1 
ATOM   11258 C  CE2   . TRP A 1 2876 ? 250.647 206.271 226.161 1.00 0.86  ? 2876 TRP A CE2   1 
ATOM   11259 C  CE3   . TRP A 1 2876 ? 251.606 205.272 228.139 1.00 0.85  ? 2876 TRP A CE3   1 
ATOM   11260 C  CZ2   . TRP A 1 2876 ? 249.506 205.484 226.259 1.00 0.95  ? 2876 TRP A CZ2   1 
ATOM   11261 C  CZ3   . TRP A 1 2876 ? 250.472 204.492 228.234 1.00 1.12  ? 2876 TRP A CZ3   1 
ATOM   11262 C  CH2   . TRP A 1 2876 ? 249.435 204.603 227.299 1.00 0.90  ? 2876 TRP A CH2   1 
ATOM   11263 N  N     . LEU A 1 2877 ? 257.181 208.181 227.584 1.00 6.52  ? 2877 LEU A N     1 
ATOM   11264 C  CA    . LEU A 1 2877 ? 258.234 208.681 228.457 1.00 6.01  ? 2877 LEU A CA    1 
ATOM   11265 C  C     . LEU A 1 2877 ? 259.340 209.391 227.693 1.00 13.04 ? 2877 LEU A C     1 
ATOM   11266 O  O     . LEU A 1 2877 ? 260.343 209.787 228.297 1.00 20.47 ? 2877 LEU A O     1 
ATOM   11267 C  CB    . LEU A 1 2877 ? 258.827 207.541 229.287 1.00 6.35  ? 2877 LEU A CB    1 
ATOM   11268 C  CG    . LEU A 1 2877 ? 257.862 206.709 230.136 1.00 8.68  ? 2877 LEU A CG    1 
ATOM   11269 C  CD1   . LEU A 1 2877 ? 258.614 206.024 231.261 1.00 6.16  ? 2877 LEU A CD1   1 
ATOM   11270 C  CD2   . LEU A 1 2877 ? 256.734 207.561 230.688 1.00 4.34  ? 2877 LEU A CD2   1 
ATOM   11271 N  N     . SER A 1 2878 ? 259.184 209.564 226.386 1.00 13.84 ? 2878 SER A N     1 
ATOM   11272 C  CA    . SER A 1 2878 ? 260.187 210.222 225.563 1.00 12.26 ? 2878 SER A CA    1 
ATOM   11273 C  C     . SER A 1 2878 ? 259.524 210.668 224.268 1.00 14.55 ? 2878 SER A C     1 
ATOM   11274 O  O     . SER A 1 2878 ? 258.320 210.491 224.070 1.00 20.09 ? 2878 SER A O     1 
ATOM   11275 C  CB    . SER A 1 2878 ? 261.376 209.296 225.297 1.00 16.80 ? 2878 SER A CB    1 
ATOM   11276 O  OG    . SER A 1 2878 ? 260.946 208.067 224.736 1.00 17.64 ? 2878 SER A OG    1 
ATOM   11277 N  N     . LYS A 1 2879 ? 260.327 211.257 223.383 1.00 13.90 ? 2879 LYS A N     1 
ATOM   11278 C  CA    . LYS A 1 2879 ? 259.830 211.638 222.066 1.00 15.76 ? 2879 LYS A CA    1 
ATOM   11279 C  C     . LYS A 1 2879 ? 259.684 210.434 221.148 1.00 13.48 ? 2879 LYS A C     1 
ATOM   11280 O  O     . LYS A 1 2879 ? 258.838 210.445 220.248 1.00 12.32 ? 2879 LYS A O     1 
ATOM   11281 C  CB    . LYS A 1 2879 ? 260.764 212.664 221.427 1.00 16.12 ? 2879 LYS A CB    1 
ATOM   11282 C  CG    . LYS A 1 2879 ? 262.212 212.213 221.356 1.00 19.66 ? 2879 LYS A CG    1 
ATOM   11283 C  CD    . LYS A 1 2879 ? 263.087 213.245 220.665 1.00 25.77 ? 2879 LYS A CD    1 
ATOM   11284 C  CE    . LYS A 1 2879 ? 264.532 212.780 220.591 1.00 26.28 ? 2879 LYS A CE    1 
ATOM   11285 N  NZ    . LYS A 1 2879 ? 265.076 212.433 221.932 1.00 24.84 ? 2879 LYS A NZ    1 
ATOM   11286 N  N     . ASP A 1 2880 ? 260.484 209.396 221.363 1.00 13.74 ? 2880 ASP A N     1 
ATOM   11287 C  CA    . ASP A 1 2880 ? 260.589 208.269 220.451 1.00 9.21  ? 2880 ASP A CA    1 
ATOM   11288 C  C     . ASP A 1 2880 ? 259.885 207.046 221.019 1.00 6.17  ? 2880 ASP A C     1 
ATOM   11289 O  O     . ASP A 1 2880 ? 259.620 206.945 222.220 1.00 11.37 ? 2880 ASP A O     1 
ATOM   11290 C  CB    . ASP A 1 2880 ? 262.060 207.948 220.168 1.00 9.22  ? 2880 ASP A CB    1 
ATOM   11291 C  CG    . ASP A 1 2880 ? 262.681 208.903 219.178 1.00 16.52 ? 2880 ASP A CG    1 
ATOM   11292 O  OD1   . ASP A 1 2880 ? 261.975 209.830 218.729 1.00 22.54 ? 2880 ASP A OD1   1 
ATOM   11293 O  OD2   . ASP A 1 2880 ? 263.874 208.734 218.855 1.00 18.60 ? 2880 ASP A OD2   1 
ATOM   11294 N  N     . TYR A 1 2881 ? 259.587 206.107 220.125 1.00 3.83  ? 2881 TYR A N     1 
ATOM   11295 C  CA    . TYR A 1 2881 ? 258.965 204.835 220.483 1.00 1.50  ? 2881 TYR A CA    1 
ATOM   11296 C  C     . TYR A 1 2881 ? 260.085 203.868 220.844 1.00 2.41  ? 2881 TYR A C     1 
ATOM   11297 O  O     . TYR A 1 2881 ? 260.602 203.132 220.004 1.00 4.38  ? 2881 TYR A O     1 
ATOM   11298 C  CB    . TYR A 1 2881 ? 258.105 204.327 219.333 1.00 3.10  ? 2881 TYR A CB    1 
ATOM   11299 C  CG    . TYR A 1 2881 ? 257.263 203.115 219.645 1.00 2.19  ? 2881 TYR A CG    1 
ATOM   11300 C  CD1   . TYR A 1 2881 ? 256.149 203.212 220.467 1.00 1.38  ? 2881 TYR A CD1   1 
ATOM   11301 C  CD2   . TYR A 1 2881 ? 257.556 201.878 219.084 1.00 1.00  ? 2881 TYR A CD2   1 
ATOM   11302 C  CE1   . TYR A 1 2881 ? 255.368 202.111 220.744 1.00 0.97  ? 2881 TYR A CE1   1 
ATOM   11303 C  CE2   . TYR A 1 2881 ? 256.778 200.771 219.352 1.00 1.01  ? 2881 TYR A CE2   1 
ATOM   11304 C  CZ    . TYR A 1 2881 ? 255.684 200.894 220.181 1.00 1.10  ? 2881 TYR A CZ    1 
ATOM   11305 O  OH    . TYR A 1 2881 ? 254.905 199.794 220.454 1.00 1.75  ? 2881 TYR A OH    1 
ATOM   11306 N  N     . ILE A 1 2882 ? 260.461 203.877 222.115 1.00 5.18  ? 2882 ILE A N     1 
ATOM   11307 C  CA    . ILE A 1 2882 ? 261.606 203.118 222.613 1.00 3.72  ? 2882 ILE A CA    1 
ATOM   11308 C  C     . ILE A 1 2882 ? 261.108 202.218 223.734 1.00 1.63  ? 2882 ILE A C     1 
ATOM   11309 O  O     . ILE A 1 2882 ? 260.011 202.434 224.277 1.00 2.20  ? 2882 ILE A O     1 
ATOM   11310 C  CB    . ILE A 1 2882 ? 262.748 204.047 223.083 1.00 3.08  ? 2882 ILE A CB    1 
ATOM   11311 C  CG1   . ILE A 1 2882 ? 262.308 204.858 224.303 1.00 3.27  ? 2882 ILE A CG1   1 
ATOM   11312 C  CG2   . ILE A 1 2882 ? 263.204 204.946 221.944 1.00 3.93  ? 2882 ILE A CG2   1 
ATOM   11313 C  CD1   . ILE A 1 2882 ? 263.413 205.682 224.916 1.00 4.70  ? 2882 ILE A CD1   1 
ATOM   11314 N  N     . PRO A 1 2883 ? 261.869 201.180 224.092 1.00 1.71  ? 2883 PRO A N     1 
ATOM   11315 C  CA    . PRO A 1 2883 ? 261.429 200.296 225.178 1.00 1.52  ? 2883 PRO A CA    1 
ATOM   11316 C  C     . PRO A 1 2883 ? 261.288 201.042 226.498 1.00 2.22  ? 2883 PRO A C     1 
ATOM   11317 O  O     . PRO A 1 2883 ? 262.055 201.957 226.810 1.00 3.49  ? 2883 PRO A O     1 
ATOM   11318 C  CB    . PRO A 1 2883 ? 262.540 199.240 225.244 1.00 1.76  ? 2883 PRO A CB    1 
ATOM   11319 C  CG    . PRO A 1 2883 ? 263.723 199.909 224.652 1.00 0.76  ? 2883 PRO A CG    1 
ATOM   11320 C  CD    . PRO A 1 2883 ? 263.171 200.753 223.552 1.00 1.18  ? 2883 PRO A CD    1 
ATOM   11321 N  N     . VAL A 1 2884 ? 260.292 200.632 227.279 1.00 1.84  ? 2884 VAL A N     1 
ATOM   11322 C  CA    . VAL A 1 2884 ? 259.934 201.290 228.531 1.00 2.31  ? 2884 VAL A CA    1 
ATOM   11323 C  C     . VAL A 1 2884 ? 259.914 200.252 229.645 1.00 3.58  ? 2884 VAL A C     1 
ATOM   11324 O  O     . VAL A 1 2884 ? 259.465 199.118 229.443 1.00 1.73  ? 2884 VAL A O     1 
ATOM   11325 C  CB    . VAL A 1 2884 ? 258.572 202.014 228.421 1.00 1.64  ? 2884 VAL A CB    1 
ATOM   11326 C  CG1   . VAL A 1 2884 ? 257.463 201.043 228.041 1.00 0.93  ? 2884 VAL A CG1   1 
ATOM   11327 C  CG2   . VAL A 1 2884 ? 258.233 202.736 229.715 1.00 2.10  ? 2884 VAL A CG2   1 
ATOM   11328 N  N     . ASP A 1 2885 ? 260.426 200.633 230.813 1.00 4.55  ? 2885 ASP A N     1 
ATOM   11329 C  CA    . ASP A 1 2885 ? 260.361 199.761 231.977 1.00 5.75  ? 2885 ASP A CA    1 
ATOM   11330 C  C     . ASP A 1 2885 ? 258.932 199.668 232.496 1.00 5.05  ? 2885 ASP A C     1 
ATOM   11331 O  O     . ASP A 1 2885 ? 258.174 200.643 232.452 1.00 4.48  ? 2885 ASP A O     1 
ATOM   11332 C  CB    . ASP A 1 2885 ? 261.285 200.269 233.081 1.00 5.35  ? 2885 ASP A CB    1 
ATOM   11333 C  CG    . ASP A 1 2885 ? 261.557 199.220 234.139 1.00 16.96 ? 2885 ASP A CG    1 
ATOM   11334 O  OD1   . ASP A 1 2885 ? 260.710 199.047 235.041 1.00 14.32 ? 2885 ASP A OD1   1 
ATOM   11335 O  OD2   . ASP A 1 2885 ? 262.615 198.563 234.065 1.00 22.78 ? 2885 ASP A OD2   1 
ATOM   11336 N  N     . GLN A 1 2886 ? 258.567 198.485 232.994 1.00 3.58  ? 2886 GLN A N     1 
ATOM   11337 C  CA    . GLN A 1 2886 ? 257.203 198.264 233.465 1.00 5.03  ? 2886 GLN A CA    1 
ATOM   11338 C  C     . GLN A 1 2886 ? 256.874 199.154 234.658 1.00 7.46  ? 2886 GLN A C     1 
ATOM   11339 O  O     . GLN A 1 2886 ? 255.790 199.743 234.726 1.00 5.49  ? 2886 GLN A O     1 
ATOM   11340 C  CB    . GLN A 1 2886 ? 257.002 196.791 233.821 1.00 5.43  ? 2886 GLN A CB    1 
ATOM   11341 C  CG    . GLN A 1 2886 ? 255.567 196.437 234.155 1.00 4.69  ? 2886 GLN A CG    1 
ATOM   11342 C  CD    . GLN A 1 2886 ? 255.367 194.956 234.373 1.00 6.65  ? 2886 GLN A CD    1 
ATOM   11343 O  OE1   . GLN A 1 2886 ? 255.972 194.361 235.263 1.00 15.19 ? 2886 GLN A OE1   1 
ATOM   11344 N  NE2   . GLN A 1 2886 ? 254.509 194.349 233.563 1.00 8.56  ? 2886 GLN A NE2   1 
ATOM   11345 N  N     . GLU A 1 2887 ? 257.800 199.262 235.614 1.00 9.46  ? 2887 GLU A N     1 
ATOM   11346 C  CA    . GLU A 1 2887 ? 257.546 200.088 236.790 1.00 7.07  ? 2887 GLU A CA    1 
ATOM   11347 C  C     . GLU A 1 2887 ? 257.524 201.570 236.436 1.00 7.84  ? 2887 GLU A C     1 
ATOM   11348 O  O     . GLU A 1 2887 ? 256.713 202.329 236.977 1.00 7.05  ? 2887 GLU A O     1 
ATOM   11349 C  CB    . GLU A 1 2887 ? 258.587 199.801 237.870 1.00 6.84  ? 2887 GLU A CB    1 
ATOM   11350 C  CG    . GLU A 1 2887 ? 258.511 198.390 238.427 1.00 12.16 ? 2887 GLU A CG    1 
ATOM   11351 C  CD    . GLU A 1 2887 ? 257.084 197.945 238.688 1.00 15.95 ? 2887 GLU A CD    1 
ATOM   11352 O  OE1   . GLU A 1 2887 ? 256.375 198.631 239.456 1.00 19.72 ? 2887 GLU A OE1   1 
ATOM   11353 O  OE2   . GLU A 1 2887 ? 256.672 196.910 238.128 1.00 14.17 ? 2887 GLU A OE2   1 
ATOM   11354 N  N     . GLU A 1 2888 ? 258.408 202.000 235.534 1.00 8.39  ? 2888 GLU A N     1 
ATOM   11355 C  CA    . GLU A 1 2888 ? 258.368 203.385 235.071 1.00 5.62  ? 2888 GLU A CA    1 
ATOM   11356 C  C     . GLU A 1 2888 ? 257.057 203.683 234.357 1.00 5.78  ? 2888 GLU A C     1 
ATOM   11357 O  O     . GLU A 1 2888 ? 256.471 204.756 234.539 1.00 9.21  ? 2888 GLU A O     1 
ATOM   11358 C  CB    . GLU A 1 2888 ? 259.556 203.669 234.150 1.00 5.43  ? 2888 GLU A CB    1 
ATOM   11359 C  CG    . GLU A 1 2888 ? 260.914 203.610 234.834 1.00 12.40 ? 2888 GLU A CG    1 
ATOM   11360 C  CD    . GLU A 1 2888 ? 261.109 204.711 235.858 1.00 25.24 ? 2888 GLU A CD    1 
ATOM   11361 O  OE1   . GLU A 1 2888 ? 260.554 205.813 235.662 1.00 28.15 ? 2888 GLU A OE1   1 
ATOM   11362 O  OE2   . GLU A 1 2888 ? 261.816 204.474 236.860 1.00 28.25 ? 2888 GLU A OE2   1 
ATOM   11363 N  N     . LEU A 1 2889 ? 256.581 202.742 233.539 1.00 5.19  ? 2889 LEU A N     1 
ATOM   11364 C  CA    . LEU A 1 2889 ? 255.305 202.920 232.855 1.00 4.38  ? 2889 LEU A CA    1 
ATOM   11365 C  C     . LEU A 1 2889 ? 254.147 202.965 233.846 1.00 3.89  ? 2889 LEU A C     1 
ATOM   11366 O  O     . LEU A 1 2889 ? 253.199 203.736 233.663 1.00 4.50  ? 2889 LEU A O     1 
ATOM   11367 C  CB    . LEU A 1 2889 ? 255.098 201.798 231.837 1.00 1.90  ? 2889 LEU A CB    1 
ATOM   11368 C  CG    . LEU A 1 2889 ? 253.821 201.849 230.999 1.00 1.12  ? 2889 LEU A CG    1 
ATOM   11369 C  CD1   . LEU A 1 2889 ? 253.929 202.897 229.904 1.00 0.87  ? 2889 LEU A CD1   1 
ATOM   11370 C  CD2   . LEU A 1 2889 ? 253.510 200.484 230.414 1.00 0.78  ? 2889 LEU A CD2   1 
ATOM   11371 N  N     . ARG A 1 2890 ? 254.203 202.139 234.893 1.00 5.94  ? 2890 ARG A N     1 
ATOM   11372 C  CA    . ARG A 1 2890 ? 253.116 202.101 235.867 1.00 4.46  ? 2890 ARG A CA    1 
ATOM   11373 C  C     . ARG A 1 2890 ? 252.966 203.437 236.580 1.00 5.42  ? 2890 ARG A C     1 
ATOM   11374 O  O     . ARG A 1 2890 ? 251.844 203.907 236.802 1.00 8.96  ? 2890 ARG A O     1 
ATOM   11375 C  CB    . ARG A 1 2890 ? 253.358 200.979 236.876 1.00 6.18  ? 2890 ARG A CB    1 
ATOM   11376 C  CG    . ARG A 1 2890 ? 252.107 200.533 237.613 1.00 4.87  ? 2890 ARG A CG    1 
ATOM   11377 C  CD    . ARG A 1 2890 ? 252.449 199.664 238.806 1.00 5.95  ? 2890 ARG A CD    1 
ATOM   11378 N  NE    . ARG A 1 2890 ? 253.326 198.560 238.439 1.00 9.32  ? 2890 ARG A NE    1 
ATOM   11379 C  CZ    . ARG A 1 2890 ? 252.903 197.371 238.030 1.00 11.09 ? 2890 ARG A CZ    1 
ATOM   11380 N  NH1   . ARG A 1 2890 ? 251.615 197.094 237.920 1.00 8.50  ? 2890 ARG A NH1   1 
ATOM   11381 N  NH2   . ARG A 1 2890 ? 253.798 196.438 237.717 1.00 7.02  ? 2890 ARG A NH2   1 
ATOM   11382 N  N     . ASP A 1 2891 ? 254.085 204.064 236.950 1.00 6.73  ? 2891 ASP A N     1 
ATOM   11383 C  CA    . ASP A 1 2891 ? 254.021 205.373 237.594 1.00 4.20  ? 2891 ASP A CA    1 
ATOM   11384 C  C     . ASP A 1 2891 ? 253.427 206.418 236.661 1.00 6.41  ? 2891 ASP A C     1 
ATOM   11385 O  O     . ASP A 1 2891 ? 252.614 207.248 237.086 1.00 12.65 ? 2891 ASP A O     1 
ATOM   11386 C  CB    . ASP A 1 2891 ? 255.413 205.800 238.053 1.00 8.01  ? 2891 ASP A CB    1 
ATOM   11387 C  CG    . ASP A 1 2891 ? 256.001 204.863 239.084 1.00 16.52 ? 2891 ASP A CG    1 
ATOM   11388 O  OD1   . ASP A 1 2891 ? 257.242 204.786 239.177 1.00 23.94 ? 2891 ASP A OD1   1 
ATOM   11389 O  OD2   . ASP A 1 2891 ? 255.222 204.206 239.800 1.00 16.55 ? 2891 ASP A OD2   1 
ATOM   11390 N  N     . TYR A 1 2892 ? 253.824 206.395 235.386 1.00 8.46  ? 2892 TYR A N     1 
ATOM   11391 C  CA    . TYR A 1 2892 ? 253.314 207.375 234.432 1.00 3.53  ? 2892 TYR A CA    1 
ATOM   11392 C  C     . TYR A 1 2892 ? 251.814 207.219 234.221 1.00 2.80  ? 2892 TYR A C     1 
ATOM   11393 O  O     . TYR A 1 2892 ? 251.088 208.215 234.138 1.00 5.23  ? 2892 TYR A O     1 
ATOM   11394 C  CB    . TYR A 1 2892 ? 254.063 207.250 233.107 1.00 5.25  ? 2892 TYR A CB    1 
ATOM   11395 C  CG    . TYR A 1 2892 ? 253.583 208.207 232.042 1.00 3.24  ? 2892 TYR A CG    1 
ATOM   11396 C  CD1   . TYR A 1 2892 ? 254.004 209.528 232.032 1.00 2.29  ? 2892 TYR A CD1   1 
ATOM   11397 C  CD2   . TYR A 1 2892 ? 252.708 207.789 231.048 1.00 1.82  ? 2892 TYR A CD2   1 
ATOM   11398 C  CE1   . TYR A 1 2892 ? 253.565 210.408 231.065 1.00 3.58  ? 2892 TYR A CE1   1 
ATOM   11399 C  CE2   . TYR A 1 2892 ? 252.266 208.659 230.082 1.00 1.53  ? 2892 TYR A CE2   1 
ATOM   11400 C  CZ    . TYR A 1 2892 ? 252.698 209.967 230.091 1.00 4.74  ? 2892 TYR A CZ    1 
ATOM   11401 O  OH    . TYR A 1 2892 ? 252.255 210.836 229.120 1.00 8.49  ? 2892 TYR A OH    1 
ATOM   11402 N  N     . VAL A 1 2893 ? 251.330 205.978 234.129 1.00 2.70  ? 2893 VAL A N     1 
ATOM   11403 C  CA    . VAL A 1 2893 ? 249.907 205.755 233.899 1.00 3.72  ? 2893 VAL A CA    1 
ATOM   11404 C  C     . VAL A 1 2893 ? 249.098 206.177 235.121 1.00 3.51  ? 2893 VAL A C     1 
ATOM   11405 O  O     . VAL A 1 2893 ? 248.001 206.735 234.993 1.00 3.92  ? 2893 VAL A O     1 
ATOM   11406 C  CB    . VAL A 1 2893 ? 249.647 204.287 233.510 1.00 4.08  ? 2893 VAL A CB    1 
ATOM   11407 C  CG1   . VAL A 1 2893 ? 248.152 204.006 233.429 1.00 2.54  ? 2893 VAL A CG1   1 
ATOM   11408 C  CG2   . VAL A 1 2893 ? 250.309 203.970 232.184 1.00 2.21  ? 2893 VAL A CG2   1 
ATOM   11409 N  N     . LYS A 1 2894 ? 249.626 205.934 236.325 1.00 5.68  ? 2894 LYS A N     1 
ATOM   11410 C  CA    . LYS A 1 2894 ? 248.960 206.419 237.531 1.00 3.92  ? 2894 LYS A CA    1 
ATOM   11411 C  C     . LYS A 1 2894 ? 248.898 207.940 237.552 1.00 4.19  ? 2894 LYS A C     1 
ATOM   11412 O  O     . LYS A 1 2894 ? 247.871 208.520 237.922 1.00 6.16  ? 2894 LYS A O     1 
ATOM   11413 C  CB    . LYS A 1 2894 ? 249.667 205.903 238.786 1.00 8.34  ? 2894 LYS A CB    1 
ATOM   11414 C  CG    . LYS A 1 2894 ? 249.548 204.413 239.005 1.00 11.13 ? 2894 LYS A CG    1 
ATOM   11415 C  CD    . LYS A 1 2894 ? 250.241 203.978 240.280 1.00 20.64 ? 2894 LYS A CD    1 
ATOM   11416 C  CE    . LYS A 1 2894 ? 250.133 202.474 240.479 1.00 18.30 ? 2894 LYS A CE    1 
ATOM   11417 N  NZ    . LYS A 1 2894 ? 250.818 202.026 241.720 1.00 23.26 ? 2894 LYS A NZ    1 
ATOM   11418 N  N     . ALA A 1 2895 ? 249.986 208.603 237.160 1.00 5.07  ? 2895 ALA A N     1 
ATOM   11419 C  CA    . ALA A 1 2895 ? 249.985 210.060 237.111 1.00 3.35  ? 2895 ALA A CA    1 
ATOM   11420 C  C     . ALA A 1 2895 ? 248.971 210.578 236.099 1.00 4.47  ? 2895 ALA A C     1 
ATOM   11421 O  O     . ALA A 1 2895 ? 248.268 211.562 236.361 1.00 5.21  ? 2895 ALA A O     1 
ATOM   11422 C  CB    . ALA A 1 2895 ? 251.386 210.574 236.779 1.00 2.22  ? 2895 ALA A CB    1 
ATOM   11423 N  N     . ARG A 1 2896 ? 248.877 209.929 234.936 1.00 4.73  ? 2896 ARG A N     1 
ATOM   11424 C  CA    . ARG A 1 2896 ? 247.930 210.375 233.921 1.00 3.61  ? 2896 ARG A CA    1 
ATOM   11425 C  C     . ARG A 1 2896 ? 246.501 209.988 234.277 1.00 2.97  ? 2896 ARG A C     1 
ATOM   11426 O  O     . ARG A 1 2896 ? 245.563 210.711 233.925 1.00 5.62  ? 2896 ARG A O     1 
ATOM   11427 C  CB    . ARG A 1 2896 ? 248.313 209.808 232.552 1.00 2.94  ? 2896 ARG A CB    1 
ATOM   11428 C  CG    . ARG A 1 2896 ? 249.664 210.284 232.038 1.00 1.87  ? 2896 ARG A CG    1 
ATOM   11429 C  CD    . ARG A 1 2896 ? 249.831 211.787 232.202 1.00 4.82  ? 2896 ARG A CD    1 
ATOM   11430 N  NE    . ARG A 1 2896 ? 248.889 212.548 231.392 1.00 4.41  ? 2896 ARG A NE    1 
ATOM   11431 C  CZ    . ARG A 1 2896 ? 248.583 213.822 231.604 1.00 4.12  ? 2896 ARG A CZ    1 
ATOM   11432 N  NH1   . ARG A 1 2896 ? 249.098 214.498 232.617 1.00 3.49  ? 2896 ARG A NH1   1 
ATOM   11433 N  NH2   . ARG A 1 2896 ? 247.732 214.431 230.781 1.00 4.01  ? 2896 ARG A NH2   1 
ATOM   11434 N  N     . LEU A 1 2897 ? 246.314 208.861 234.967 1.00 2.15  ? 2897 LEU A N     1 
ATOM   11435 C  CA    . LEU A 1 2897 ? 244.974 208.476 235.399 1.00 3.03  ? 2897 LEU A CA    1 
ATOM   11436 C  C     . LEU A 1 2897 ? 244.410 209.464 236.408 1.00 3.24  ? 2897 LEU A C     1 
ATOM   11437 O  O     . LEU A 1 2897 ? 243.196 209.701 236.434 1.00 3.90  ? 2897 LEU A O     1 
ATOM   11438 C  CB    . LEU A 1 2897 ? 244.992 207.065 235.992 1.00 1.87  ? 2897 LEU A CB    1 
ATOM   11439 C  CG    . LEU A 1 2897 ? 244.788 205.907 235.014 1.00 2.03  ? 2897 LEU A CG    1 
ATOM   11440 C  CD1   . LEU A 1 2897 ? 244.947 204.577 235.726 1.00 2.11  ? 2897 LEU A CD1   1 
ATOM   11441 C  CD2   . LEU A 1 2897 ? 243.431 205.997 234.332 1.00 0.84  ? 2897 LEU A CD2   1 
ATOM   11442 N  N     . LYS A 1 2898 ? 245.270 210.049 237.244 1.00 4.10  ? 2898 LYS A N     1 
ATOM   11443 C  CA    . LYS A 1 2898 ? 244.829 211.071 238.186 1.00 4.57  ? 2898 LYS A CA    1 
ATOM   11444 C  C     . LYS A 1 2898 ? 244.223 212.263 237.454 1.00 8.33  ? 2898 LYS A C     1 
ATOM   11445 O  O     . LYS A 1 2898 ? 243.161 212.768 237.835 1.00 14.08 ? 2898 LYS A O     1 
ATOM   11446 C  CB    . LYS A 1 2898 ? 246.006 211.510 239.055 1.00 6.09  ? 2898 LYS A CB    1 
ATOM   11447 C  CG    . LYS A 1 2898 ? 245.650 212.496 240.148 1.00 10.37 ? 2898 LYS A CG    1 
ATOM   11448 C  CD    . LYS A 1 2898 ? 246.861 212.811 241.009 1.00 17.10 ? 2898 LYS A CD    1 
ATOM   11449 C  CE    . LYS A 1 2898 ? 246.519 213.804 242.105 1.00 24.01 ? 2898 LYS A CE    1 
ATOM   11450 N  NZ    . LYS A 1 2898 ? 247.700 214.118 242.949 1.00 24.87 ? 2898 LYS A NZ    1 
ATOM   11451 N  N     . VAL A 1 2899 ? 244.888 212.723 236.394 1.00 4.20  ? 2899 VAL A N     1 
ATOM   11452 C  CA    . VAL A 1 2899 ? 244.351 213.819 235.595 1.00 3.07  ? 2899 VAL A CA    1 
ATOM   11453 C  C     . VAL A 1 2899 ? 243.092 213.377 234.859 1.00 4.37  ? 2899 VAL A C     1 
ATOM   11454 O  O     . VAL A 1 2899 ? 242.141 214.152 234.705 1.00 7.35  ? 2899 VAL A O     1 
ATOM   11455 C  CB    . VAL A 1 2899 ? 245.428 214.340 234.628 1.00 1.47  ? 2899 VAL A CB    1 
ATOM   11456 C  CG1   . VAL A 1 2899 ? 244.912 215.523 233.842 1.00 1.41  ? 2899 VAL A CG1   1 
ATOM   11457 C  CG2   . VAL A 1 2899 ? 246.687 214.714 235.391 1.00 1.33  ? 2899 VAL A CG2   1 
ATOM   11458 N  N     . PHE A 1 2900 ? 243.066 212.123 234.399 1.00 3.79  ? 2900 PHE A N     1 
ATOM   11459 C  CA    . PHE A 1 2900 ? 241.908 211.612 233.670 1.00 3.10  ? 2900 PHE A CA    1 
ATOM   11460 C  C     . PHE A 1 2900 ? 240.662 211.589 234.548 1.00 4.77  ? 2900 PHE A C     1 
ATOM   11461 O  O     . PHE A 1 2900 ? 239.549 211.827 234.065 1.00 2.74  ? 2900 PHE A O     1 
ATOM   11462 C  CB    . PHE A 1 2900 ? 242.221 210.216 233.128 1.00 1.27  ? 2900 PHE A CB    1 
ATOM   11463 C  CG    . PHE A 1 2900 ? 241.115 209.612 232.314 1.00 0.67  ? 2900 PHE A CG    1 
ATOM   11464 C  CD1   . PHE A 1 2900 ? 240.825 210.091 231.046 1.00 0.52  ? 2900 PHE A CD1   1 
ATOM   11465 C  CD2   . PHE A 1 2900 ? 240.384 208.544 232.801 1.00 0.55  ? 2900 PHE A CD2   1 
ATOM   11466 C  CE1   . PHE A 1 2900 ? 239.816 209.525 230.289 1.00 0.46  ? 2900 PHE A CE1   1 
ATOM   11467 C  CE2   . PHE A 1 2900 ? 239.373 207.975 232.050 1.00 0.46  ? 2900 PHE A CE2   1 
ATOM   11468 C  CZ    . PHE A 1 2900 ? 239.088 208.468 230.792 1.00 0.31  ? 2900 PHE A CZ    1 
ATOM   11469 N  N     . TYR A 1 2901 ? 240.825 211.297 235.841 1.00 4.82  ? 2901 TYR A N     1 
ATOM   11470 C  CA    . TYR A 1 2901 ? 239.683 211.283 236.750 1.00 6.00  ? 2901 TYR A CA    1 
ATOM   11471 C  C     . TYR A 1 2901 ? 239.065 212.669 236.888 1.00 7.68  ? 2901 TYR A C     1 
ATOM   11472 O  O     . TYR A 1 2901 ? 237.839 212.805 236.957 1.00 9.84  ? 2901 TYR A O     1 
ATOM   11473 C  CB    . TYR A 1 2901 ? 240.104 210.753 238.120 1.00 6.18  ? 2901 TYR A CB    1 
ATOM   11474 C  CG    . TYR A 1 2901 ? 240.638 209.341 238.105 1.00 6.46  ? 2901 TYR A CG    1 
ATOM   11475 C  CD1   . TYR A 1 2901 ? 240.194 208.416 237.169 1.00 5.01  ? 2901 TYR A CD1   1 
ATOM   11476 C  CD2   . TYR A 1 2901 ? 241.589 208.932 239.030 1.00 4.07  ? 2901 TYR A CD2   1 
ATOM   11477 C  CE1   . TYR A 1 2901 ? 240.682 207.127 237.155 1.00 3.96  ? 2901 TYR A CE1   1 
ATOM   11478 C  CE2   . TYR A 1 2901 ? 242.084 207.646 239.023 1.00 2.32  ? 2901 TYR A CE2   1 
ATOM   11479 C  CZ    . TYR A 1 2901 ? 241.627 206.746 238.085 1.00 3.36  ? 2901 TYR A CZ    1 
ATOM   11480 O  OH    . TYR A 1 2901 ? 242.121 205.462 238.078 1.00 6.57  ? 2901 TYR A OH    1 
ATOM   11481 N  N     . GLU A 1 2902 ? 239.898 213.708 236.929 1.00 8.23  ? 2902 GLU A N     1 
ATOM   11482 C  CA    . GLU A 1 2902 ? 239.434 215.071 237.160 1.00 7.77  ? 2902 GLU A CA    1 
ATOM   11483 C  C     . GLU A 1 2902 ? 238.926 215.766 235.903 1.00 8.41  ? 2902 GLU A C     1 
ATOM   11484 O  O     . GLU A 1 2902 ? 238.317 216.834 236.016 1.00 19.54 ? 2902 GLU A O     1 
ATOM   11485 C  CB    . GLU A 1 2902 ? 240.564 215.900 237.774 1.00 8.90  ? 2902 GLU A CB    1 
ATOM   11486 C  CG    . GLU A 1 2902 ? 240.949 215.467 239.178 1.00 15.35 ? 2902 GLU A CG    1 
ATOM   11487 C  CD    . GLU A 1 2902 ? 242.080 216.293 239.754 1.00 26.23 ? 2902 GLU A CD    1 
ATOM   11488 O  OE1   . GLU A 1 2902 ? 242.651 217.122 239.014 1.00 26.80 ? 2902 GLU A OE1   1 
ATOM   11489 O  OE2   . GLU A 1 2902 ? 242.397 216.118 240.949 1.00 32.32 ? 2902 GLU A OE2   1 
ATOM   11490 N  N     . GLU A 1 2903 ? 239.150 215.203 234.720 1.00 7.57  ? 2903 GLU A N     1 
ATOM   11491 C  CA    . GLU A 1 2903 ? 238.755 215.858 233.479 1.00 7.10  ? 2903 GLU A CA    1 
ATOM   11492 C  C     . GLU A 1 2903 ? 237.693 215.109 232.688 1.00 11.52 ? 2903 GLU A C     1 
ATOM   11493 O  O     . GLU A 1 2903 ? 236.793 215.741 232.133 1.00 19.72 ? 2903 GLU A O     1 
ATOM   11494 C  CB    . GLU A 1 2903 ? 239.977 216.079 232.580 1.00 6.96  ? 2903 GLU A CB    1 
ATOM   11495 C  CG    . GLU A 1 2903 ? 240.947 217.127 233.091 1.00 11.03 ? 2903 GLU A CG    1 
ATOM   11496 C  CD    . GLU A 1 2903 ? 242.140 217.314 232.178 1.00 21.10 ? 2903 GLU A CD    1 
ATOM   11497 O  OE1   . GLU A 1 2903 ? 242.061 216.907 230.998 1.00 27.01 ? 2903 GLU A OE1   1 
ATOM   11498 O  OE2   . GLU A 1 2903 ? 243.157 217.880 232.631 1.00 22.54 ? 2903 GLU A OE2   1 
ATOM   11499 N  N     . GLU A 1 2904 ? 237.770 213.782 232.609 1.00 10.81 ? 2904 GLU A N     1 
ATOM   11500 C  CA    . GLU A 1 2904 ? 236.894 213.017 231.731 1.00 7.79  ? 2904 GLU A CA    1 
ATOM   11501 C  C     . GLU A 1 2904 ? 235.953 212.090 232.490 1.00 10.76 ? 2904 GLU A C     1 
ATOM   11502 O  O     . GLU A 1 2904 ? 234.733 212.193 232.346 1.00 17.36 ? 2904 GLU A O     1 
ATOM   11503 C  CB    . GLU A 1 2904 ? 237.737 212.209 230.738 1.00 4.71  ? 2904 GLU A CB    1 
ATOM   11504 C  CG    . GLU A 1 2904 ? 238.495 213.054 229.738 1.00 9.11  ? 2904 GLU A CG    1 
ATOM   11505 C  CD    . GLU A 1 2904 ? 237.577 213.791 228.786 1.00 17.62 ? 2904 GLU A CD    1 
ATOM   11506 O  OE1   . GLU A 1 2904 ? 236.741 213.130 228.134 1.00 14.58 ? 2904 GLU A OE1   1 
ATOM   11507 O  OE2   . GLU A 1 2904 ? 237.692 215.029 228.689 1.00 17.80 ? 2904 GLU A OE2   1 
ATOM   11508 N  N     . LEU A 1 2905 ? 236.490 211.183 233.304 1.00 8.19  ? 2905 LEU A N     1 
ATOM   11509 C  CA    . LEU A 1 2905 ? 235.678 210.136 233.913 1.00 7.34  ? 2905 LEU A CA    1 
ATOM   11510 C  C     . LEU A 1 2905 ? 236.219 209.856 235.306 1.00 6.14  ? 2905 LEU A C     1 
ATOM   11511 O  O     . LEU A 1 2905 ? 237.325 209.327 235.447 1.00 10.61 ? 2905 LEU A O     1 
ATOM   11512 C  CB    . LEU A 1 2905 ? 235.691 208.871 233.060 1.00 7.53  ? 2905 LEU A CB    1 
ATOM   11513 C  CG    . LEU A 1 2905 ? 234.431 208.009 233.073 1.00 5.81  ? 2905 LEU A CG    1 
ATOM   11514 C  CD1   . LEU A 1 2905 ? 233.202 208.853 232.793 1.00 5.55  ? 2905 LEU A CD1   1 
ATOM   11515 C  CD2   . LEU A 1 2905 ? 234.559 206.877 232.068 1.00 7.26  ? 2905 LEU A CD2   1 
ATOM   11516 N  N     . ASP A 1 2906 ? 235.438 210.193 236.327 1.00 8.45  ? 2906 ASP A N     1 
ATOM   11517 C  CA    . ASP A 1 2906 ? 235.844 209.939 237.710 1.00 9.37  ? 2906 ASP A CA    1 
ATOM   11518 C  C     . ASP A 1 2906 ? 235.403 208.539 238.143 1.00 8.99  ? 2906 ASP A C     1 
ATOM   11519 O  O     . ASP A 1 2906 ? 234.577 208.349 239.032 1.00 12.10 ? 2906 ASP A O     1 
ATOM   11520 C  CB    . ASP A 1 2906 ? 235.289 211.017 238.633 1.00 11.40 ? 2906 ASP A CB    1 
ATOM   11521 C  CG    . ASP A 1 2906 ? 235.799 210.878 240.052 1.00 18.42 ? 2906 ASP A CG    1 
ATOM   11522 O  OD1   . ASP A 1 2906 ? 236.979 211.206 240.295 1.00 21.28 ? 2906 ASP A OD1   1 
ATOM   11523 O  OD2   . ASP A 1 2906 ? 235.023 210.445 240.928 1.00 29.58 ? 2906 ASP A OD2   1 
ATOM   11524 N  N     . VAL A 1 2907 ? 235.973 207.550 237.471 1.00 7.72  ? 2907 VAL A N     1 
ATOM   11525 C  CA    . VAL A 1 2907 ? 235.806 206.146 237.819 1.00 6.53  ? 2907 VAL A CA    1 
ATOM   11526 C  C     . VAL A 1 2907 ? 237.181 205.575 238.140 1.00 6.75  ? 2907 VAL A C     1 
ATOM   11527 O  O     . VAL A 1 2907 ? 237.964 205.271 237.241 1.00 12.62 ? 2907 VAL A O     1 
ATOM   11528 C  CB    . VAL A 1 2907 ? 235.127 205.356 236.684 1.00 6.93  ? 2907 VAL A CB    1 
ATOM   11529 C  CG1   . VAL A 1 2907 ? 234.842 203.936 237.129 1.00 5.05  ? 2907 VAL A CG1   1 
ATOM   11530 C  CG2   . VAL A 1 2907 ? 233.846 206.048 236.238 1.00 7.86  ? 2907 VAL A CG2   1 
ATOM   11531 N  N     . PRO A 1 2908 ? 237.516 205.430 239.421 1.00 5.73  ? 2908 PRO A N     1 
ATOM   11532 C  CA    . PRO A 1 2908 ? 238.848 204.925 239.781 1.00 6.26  ? 2908 PRO A CA    1 
ATOM   11533 C  C     . PRO A 1 2908 ? 239.083 203.521 239.244 1.00 7.59  ? 2908 PRO A C     1 
ATOM   11534 O  O     . PRO A 1 2908 ? 238.181 202.682 239.223 1.00 13.71 ? 2908 PRO A O     1 
ATOM   11535 C  CB    . PRO A 1 2908 ? 238.833 204.946 241.315 1.00 8.70  ? 2908 PRO A CB    1 
ATOM   11536 C  CG    . PRO A 1 2908 ? 237.765 205.929 241.671 1.00 5.91  ? 2908 PRO A CG    1 
ATOM   11537 C  CD    . PRO A 1 2908 ? 236.722 205.783 240.607 1.00 5.95  ? 2908 PRO A CD    1 
ATOM   11538 N  N     . LEU A 1 2909 ? 240.316 203.271 238.814 1.00 5.71  ? 2909 LEU A N     1 
ATOM   11539 C  CA    . LEU A 1 2909 ? 240.706 201.992 238.242 1.00 2.59  ? 2909 LEU A CA    1 
ATOM   11540 C  C     . LEU A 1 2909 ? 241.903 201.435 238.996 1.00 2.82  ? 2909 LEU A C     1 
ATOM   11541 O  O     . LEU A 1 2909 ? 242.826 202.175 239.346 1.00 4.60  ? 2909 LEU A O     1 
ATOM   11542 C  CB    . LEU A 1 2909 ? 241.055 202.124 236.755 1.00 2.95  ? 2909 LEU A CB    1 
ATOM   11543 C  CG    . LEU A 1 2909 ? 239.999 202.732 235.833 1.00 4.26  ? 2909 LEU A CG    1 
ATOM   11544 C  CD1   . LEU A 1 2909 ? 240.627 203.132 234.512 1.00 3.12  ? 2909 LEU A CD1   1 
ATOM   11545 C  CD2   . LEU A 1 2909 ? 238.859 201.754 235.616 1.00 2.59  ? 2909 LEU A CD2   1 
ATOM   11546 N  N     . VAL A 1 2910 ? 241.879 200.132 239.240 1.00 2.97  ? 2910 VAL A N     1 
ATOM   11547 C  CA    . VAL A 1 2910 ? 243.017 199.429 239.819 1.00 3.76  ? 2910 VAL A CA    1 
ATOM   11548 C  C     . VAL A 1 2910 ? 243.944 199.018 238.687 1.00 3.14  ? 2910 VAL A C     1 
ATOM   11549 O  O     . VAL A 1 2910 ? 243.511 198.396 237.711 1.00 7.32  ? 2910 VAL A O     1 
ATOM   11550 C  CB    . VAL A 1 2910 ? 242.556 198.206 240.630 1.00 4.82  ? 2910 VAL A CB    1 
ATOM   11551 C  CG1   . VAL A 1 2910 ? 243.757 197.425 241.140 1.00 3.32  ? 2910 VAL A CG1   1 
ATOM   11552 C  CG2   . VAL A 1 2910 ? 241.662 198.636 241.780 1.00 3.04  ? 2910 VAL A CG2   1 
ATOM   11553 N  N     . LEU A 1 2911 ? 245.219 199.375 238.806 1.00 2.11  ? 2911 LEU A N     1 
ATOM   11554 C  CA    . LEU A 1 2911 ? 246.189 199.143 237.743 1.00 2.68  ? 2911 LEU A CA    1 
ATOM   11555 C  C     . LEU A 1 2911 ? 246.908 197.823 237.994 1.00 4.73  ? 2911 LEU A C     1 
ATOM   11556 O  O     . LEU A 1 2911 ? 247.678 197.701 238.951 1.00 18.36 ? 2911 LEU A O     1 
ATOM   11557 C  CB    . LEU A 1 2911 ? 247.189 200.291 237.662 1.00 5.07  ? 2911 LEU A CB    1 
ATOM   11558 C  CG    . LEU A 1 2911 ? 246.768 201.502 236.834 1.00 5.58  ? 2911 LEU A CG    1 
ATOM   11559 C  CD1   . LEU A 1 2911 ? 247.947 202.425 236.630 1.00 6.88  ? 2911 LEU A CD1   1 
ATOM   11560 C  CD2   . LEU A 1 2911 ? 246.183 201.078 235.509 1.00 4.77  ? 2911 LEU A CD2   1 
ATOM   11561 N  N     . PHE A 1 2912 ? 246.659 196.840 237.140 1.00 1.49  ? 2912 PHE A N     1 
ATOM   11562 C  CA    . PHE A 1 2912 ? 247.422 195.604 237.132 1.00 2.14  ? 2912 PHE A CA    1 
ATOM   11563 C  C     . PHE A 1 2912 ? 248.188 195.482 235.820 1.00 3.23  ? 2912 PHE A C     1 
ATOM   11564 O  O     . PHE A 1 2912 ? 248.047 196.302 234.910 1.00 3.01  ? 2912 PHE A O     1 
ATOM   11565 C  CB    . PHE A 1 2912 ? 246.516 194.387 237.377 1.00 1.87  ? 2912 PHE A CB    1 
ATOM   11566 C  CG    . PHE A 1 2912 ? 245.348 194.279 236.440 1.00 1.74  ? 2912 PHE A CG    1 
ATOM   11567 C  CD1   . PHE A 1 2912 ? 244.166 194.944 236.709 1.00 1.42  ? 2912 PHE A CD1   1 
ATOM   11568 C  CD2   . PHE A 1 2912 ? 245.415 193.476 235.316 1.00 2.20  ? 2912 PHE A CD2   1 
ATOM   11569 C  CE1   . PHE A 1 2912 ? 243.082 194.831 235.863 1.00 0.76  ? 2912 PHE A CE1   1 
ATOM   11570 C  CE2   . PHE A 1 2912 ? 244.332 193.361 234.467 1.00 1.62  ? 2912 PHE A CE2   1 
ATOM   11571 C  CZ    . PHE A 1 2912 ? 243.167 194.038 234.742 1.00 1.24  ? 2912 PHE A CZ    1 
ATOM   11572 N  N     . ASN A 1 2913 ? 249.018 194.439 235.742 1.00 3.24  ? 2913 ASN A N     1 
ATOM   11573 C  CA    . ASN A 1 2913 ? 250.002 194.343 234.667 1.00 1.33  ? 2913 ASN A CA    1 
ATOM   11574 C  C     . ASN A 1 2913 ? 249.344 194.245 233.296 1.00 3.80  ? 2913 ASN A C     1 
ATOM   11575 O  O     . ASN A 1 2913 ? 249.824 194.846 232.328 1.00 2.94  ? 2913 ASN A O     1 
ATOM   11576 C  CB    . ASN A 1 2913 ? 250.923 193.149 234.908 1.00 1.80  ? 2913 ASN A CB    1 
ATOM   11577 C  CG    . ASN A 1 2913 ? 251.995 193.441 235.937 1.00 2.43  ? 2913 ASN A CG    1 
ATOM   11578 O  OD1   . ASN A 1 2913 ? 252.129 194.569 236.407 1.00 3.95  ? 2913 ASN A OD1   1 
ATOM   11579 N  ND2   . ASN A 1 2913 ? 252.765 192.423 236.295 1.00 1.82  ? 2913 ASN A ND2   1 
ATOM   11580 N  N     . GLU A 1 2914 ? 248.251 193.488 233.186 1.00 4.32  ? 2914 GLU A N     1 
ATOM   11581 C  CA    . GLU A 1 2914 ? 247.593 193.334 231.891 1.00 2.79  ? 2914 GLU A CA    1 
ATOM   11582 C  C     . GLU A 1 2914 ? 247.025 194.652 231.381 1.00 2.81  ? 2914 GLU A C     1 
ATOM   11583 O  O     . GLU A 1 2914 ? 246.962 194.863 230.165 1.00 5.94  ? 2914 GLU A O     1 
ATOM   11584 C  CB    . GLU A 1 2914 ? 246.493 192.279 231.977 1.00 4.14  ? 2914 GLU A CB    1 
ATOM   11585 C  CG    . GLU A 1 2914 ? 246.999 190.855 232.053 1.00 10.22 ? 2914 GLU A CG    1 
ATOM   11586 C  CD    . GLU A 1 2914 ? 246.048 189.937 232.796 1.00 19.05 ? 2914 GLU A CD    1 
ATOM   11587 O  OE1   . GLU A 1 2914 ? 244.839 189.940 232.478 1.00 9.62  ? 2914 GLU A OE1   1 
ATOM   11588 O  OE2   . GLU A 1 2914 ? 246.510 189.210 233.701 1.00 15.51 ? 2914 GLU A OE2   1 
ATOM   11589 N  N     . VAL A 1 2915 ? 246.607 195.544 232.282 1.00 2.31  ? 2915 VAL A N     1 
ATOM   11590 C  CA    . VAL A 1 2915 ? 246.099 196.846 231.855 1.00 1.41  ? 2915 VAL A CA    1 
ATOM   11591 C  C     . VAL A 1 2915 ? 247.201 197.652 231.180 1.00 0.93  ? 2915 VAL A C     1 
ATOM   11592 O  O     . VAL A 1 2915 ? 246.978 198.291 230.145 1.00 2.16  ? 2915 VAL A O     1 
ATOM   11593 C  CB    . VAL A 1 2915 ? 245.490 197.608 233.049 1.00 1.80  ? 2915 VAL A CB    1 
ATOM   11594 C  CG1   . VAL A 1 2915 ? 245.372 199.086 232.731 1.00 2.46  ? 2915 VAL A CG1   1 
ATOM   11595 C  CG2   . VAL A 1 2915 ? 244.134 197.046 233.396 1.00 1.05  ? 2915 VAL A CG2   1 
ATOM   11596 N  N     . LEU A 1 2916 ? 248.408 197.629 231.751 1.00 1.00  ? 2916 LEU A N     1 
ATOM   11597 C  CA    . LEU A 1 2916 ? 249.521 198.377 231.174 1.00 0.86  ? 2916 LEU A CA    1 
ATOM   11598 C  C     . LEU A 1 2916 ? 249.850 197.886 229.770 1.00 0.98  ? 2916 LEU A C     1 
ATOM   11599 O  O     . LEU A 1 2916 ? 250.137 198.687 228.874 1.00 0.81  ? 2916 LEU A O     1 
ATOM   11600 C  CB    . LEU A 1 2916 ? 250.748 198.271 232.078 1.00 0.88  ? 2916 LEU A CB    1 
ATOM   11601 C  CG    . LEU A 1 2916 ? 250.615 198.829 233.492 1.00 1.60  ? 2916 LEU A CG    1 
ATOM   11602 C  CD1   . LEU A 1 2916 ? 251.894 198.596 234.275 1.00 4.21  ? 2916 LEU A CD1   1 
ATOM   11603 C  CD2   . LEU A 1 2916 ? 250.267 200.308 233.457 1.00 1.97  ? 2916 LEU A CD2   1 
ATOM   11604 N  N     . ASP A 1 2917 ? 249.829 196.569 229.565 1.00 1.22  ? 2917 ASP A N     1 
ATOM   11605 C  CA    . ASP A 1 2917 ? 250.037 196.035 228.224 1.00 1.18  ? 2917 ASP A CA    1 
ATOM   11606 C  C     . ASP A 1 2917 ? 248.876 196.415 227.308 1.00 0.74  ? 2917 ASP A C     1 
ATOM   11607 O  O     . ASP A 1 2917 ? 249.085 196.768 226.143 1.00 0.26  ? 2917 ASP A O     1 
ATOM   11608 C  CB    . ASP A 1 2917 ? 250.220 194.516 228.295 1.00 1.73  ? 2917 ASP A CB    1 
ATOM   11609 C  CG    . ASP A 1 2917 ? 250.660 193.901 226.968 1.00 9.27  ? 2917 ASP A CG    1 
ATOM   11610 O  OD1   . ASP A 1 2917 ? 250.804 194.629 225.965 1.00 8.27  ? 2917 ASP A OD1   1 
ATOM   11611 O  OD2   . ASP A 1 2917 ? 250.876 192.672 226.933 1.00 12.56 ? 2917 ASP A OD2   1 
ATOM   11612 N  N     . HIS A 1 2918 ? 247.646 196.376 227.832 1.00 0.61  ? 2918 HIS A N     1 
ATOM   11613 C  CA    . HIS A 1 2918 ? 246.478 196.682 227.011 1.00 1.08  ? 2918 HIS A CA    1 
ATOM   11614 C  C     . HIS A 1 2918 ? 246.463 198.138 226.559 1.00 0.41  ? 2918 HIS A C     1 
ATOM   11615 O  O     . HIS A 1 2918 ? 246.164 198.424 225.394 1.00 0.23  ? 2918 HIS A O     1 
ATOM   11616 C  CB    . HIS A 1 2918 ? 245.194 196.350 227.771 1.00 0.67  ? 2918 HIS A CB    1 
ATOM   11617 C  CG    . HIS A 1 2918 ? 244.942 194.883 227.915 1.00 1.32  ? 2918 HIS A CG    1 
ATOM   11618 N  ND1   . HIS A 1 2918 ? 243.970 194.375 228.750 1.00 3.03  ? 2918 HIS A ND1   1 
ATOM   11619 C  CD2   . HIS A 1 2918 ? 245.538 193.816 227.337 1.00 2.50  ? 2918 HIS A CD2   1 
ATOM   11620 C  CE1   . HIS A 1 2918 ? 243.975 193.057 228.674 1.00 1.78  ? 2918 HIS A CE1   1 
ATOM   11621 N  NE2   . HIS A 1 2918 ? 244.918 192.692 227.824 1.00 3.07  ? 2918 HIS A NE2   1 
ATOM   11622 N  N     . VAL A 1 2919 ? 246.773 199.072 227.460 1.00 0.43  ? 2919 VAL A N     1 
ATOM   11623 C  CA    . VAL A 1 2919 ? 246.745 200.480 227.077 1.00 0.66  ? 2919 VAL A CA    1 
ATOM   11624 C  C     . VAL A 1 2919 ? 247.816 200.775 226.038 1.00 0.26  ? 2919 VAL A C     1 
ATOM   11625 O  O     . VAL A 1 2919 ? 247.614 201.612 225.152 1.00 0.22  ? 2919 VAL A O     1 
ATOM   11626 C  CB    . VAL A 1 2919 ? 246.868 201.396 228.313 1.00 0.43  ? 2919 VAL A CB    1 
ATOM   11627 C  CG1   . VAL A 1 2919 ? 245.718 201.149 229.271 1.00 0.38  ? 2919 VAL A CG1   1 
ATOM   11628 C  CG2   . VAL A 1 2919 ? 248.201 201.206 229.015 1.00 0.70  ? 2919 VAL A CG2   1 
ATOM   11629 N  N     . LEU A 1 2920 ? 248.964 200.098 226.118 1.00 0.26  ? 2920 LEU A N     1 
ATOM   11630 C  CA    . LEU A 1 2920 ? 249.991 200.260 225.094 1.00 0.21  ? 2920 LEU A CA    1 
ATOM   11631 C  C     . LEU A 1 2920 ? 249.515 199.735 223.743 1.00 0.28  ? 2920 LEU A C     1 
ATOM   11632 O  O     . LEU A 1 2920 ? 249.800 200.338 222.704 1.00 0.43  ? 2920 LEU A O     1 
ATOM   11633 C  CB    . LEU A 1 2920 ? 251.276 199.557 225.528 1.00 0.18  ? 2920 LEU A CB    1 
ATOM   11634 C  CG    . LEU A 1 2920 ? 252.083 200.243 226.634 1.00 0.35  ? 2920 LEU A CG    1 
ATOM   11635 C  CD1   . LEU A 1 2920 ? 253.391 199.515 226.875 1.00 0.37  ? 2920 LEU A CD1   1 
ATOM   11636 C  CD2   . LEU A 1 2920 ? 252.334 201.706 226.307 1.00 0.33  ? 2920 LEU A CD2   1 
ATOM   11637 N  N     . ARG A 1 2921 ? 248.792 198.611 223.739 1.00 0.19  ? 2921 ARG A N     1 
ATOM   11638 C  CA    . ARG A 1 2921 ? 248.264 198.070 222.490 1.00 0.21  ? 2921 ARG A CA    1 
ATOM   11639 C  C     . ARG A 1 2921 ? 247.223 198.995 221.875 1.00 0.28  ? 2921 ARG A C     1 
ATOM   11640 O  O     . ARG A 1 2921 ? 247.196 199.176 220.652 1.00 0.50  ? 2921 ARG A O     1 
ATOM   11641 C  CB    . ARG A 1 2921 ? 247.667 196.681 222.725 1.00 0.64  ? 2921 ARG A CB    1 
ATOM   11642 C  CG    . ARG A 1 2921 ? 248.654 195.648 223.229 1.00 0.58  ? 2921 ARG A CG    1 
ATOM   11643 C  CD    . ARG A 1 2921 ? 247.934 194.389 223.669 1.00 1.63  ? 2921 ARG A CD    1 
ATOM   11644 N  NE    . ARG A 1 2921 ? 248.821 193.465 224.364 1.00 2.53  ? 2921 ARG A NE    1 
ATOM   11645 C  CZ    . ARG A 1 2921 ? 248.463 192.261 224.787 1.00 1.94  ? 2921 ARG A CZ    1 
ATOM   11646 N  NH1   . ARG A 1 2921 ? 247.239 191.798 224.597 1.00 1.66  ? 2921 ARG A NH1   1 
ATOM   11647 N  NH2   . ARG A 1 2921 ? 249.358 191.498 225.409 1.00 2.44  ? 2921 ARG A NH2   1 
ATOM   11648 N  N     . ILE A 1 2922 ? 246.351 199.578 222.698 1.00 0.28  ? 2922 ILE A N     1 
ATOM   11649 C  CA    . ILE A 1 2922 ? 245.361 200.520 222.186 1.00 0.22  ? 2922 ILE A CA    1 
ATOM   11650 C  C     . ILE A 1 2922 ? 246.044 201.785 221.678 1.00 0.35  ? 2922 ILE A C     1 
ATOM   11651 O  O     . ILE A 1 2922 ? 245.627 202.368 220.671 1.00 0.58  ? 2922 ILE A O     1 
ATOM   11652 C  CB    . ILE A 1 2922 ? 244.312 200.828 223.270 1.00 0.17  ? 2922 ILE A CB    1 
ATOM   11653 C  CG1   . ILE A 1 2922 ? 243.568 199.552 223.671 1.00 0.15  ? 2922 ILE A CG1   1 
ATOM   11654 C  CG2   . ILE A 1 2922 ? 243.332 201.890 222.794 1.00 0.10  ? 2922 ILE A CG2   1 
ATOM   11655 C  CD1   . ILE A 1 2922 ? 242.661 199.722 224.865 1.00 0.30  ? 2922 ILE A CD1   1 
ATOM   11656 N  N     . ASP A 1 2923 ? 247.107 202.220 222.356 1.00 0.29  ? 2923 ASP A N     1 
ATOM   11657 C  CA    . ASP A 1 2923 ? 247.817 203.425 221.942 1.00 0.57  ? 2923 ASP A CA    1 
ATOM   11658 C  C     . ASP A 1 2923 ? 248.445 203.254 220.565 1.00 0.89  ? 2923 ASP A C     1 
ATOM   11659 O  O     . ASP A 1 2923 ? 248.511 204.207 219.782 1.00 2.29  ? 2923 ASP A O     1 
ATOM   11660 C  CB    . ASP A 1 2923 ? 248.880 203.782 222.982 1.00 0.57  ? 2923 ASP A CB    1 
ATOM   11661 C  CG    . ASP A 1 2923 ? 249.627 205.052 222.638 1.00 2.02  ? 2923 ASP A CG    1 
ATOM   11662 O  OD1   . ASP A 1 2923 ? 249.013 206.133 222.688 1.00 2.55  ? 2923 ASP A OD1   1 
ATOM   11663 O  OD2   . ASP A 1 2923 ? 250.828 204.970 222.314 1.00 7.67  ? 2923 ASP A OD2   1 
ATOM   11664 N  N     . ARG A 1 2924 ? 248.917 202.044 220.255 1.00 0.95  ? 2924 ARG A N     1 
ATOM   11665 C  CA    . ARG A 1 2924 ? 249.519 201.786 218.950 1.00 0.98  ? 2924 ARG A CA    1 
ATOM   11666 C  C     . ARG A 1 2924 ? 248.513 201.976 217.821 1.00 0.80  ? 2924 ARG A C     1 
ATOM   11667 O  O     . ARG A 1 2924 ? 248.826 202.580 216.790 1.00 3.18  ? 2924 ARG A O     1 
ATOM   11668 C  CB    . ARG A 1 2924 ? 250.099 200.374 218.923 1.00 0.70  ? 2924 ARG A CB    1 
ATOM   11669 C  CG    . ARG A 1 2924 ? 251.396 200.229 219.681 1.00 1.16  ? 2924 ARG A CG    1 
ATOM   11670 C  CD    . ARG A 1 2924 ? 251.880 198.795 219.680 1.00 1.72  ? 2924 ARG A CD    1 
ATOM   11671 N  NE    . ARG A 1 2924 ? 251.744 198.163 218.374 1.00 3.85  ? 2924 ARG A NE    1 
ATOM   11672 C  CZ    . ARG A 1 2924 ? 252.759 197.724 217.644 1.00 2.76  ? 2924 ARG A CZ    1 
ATOM   11673 N  NH1   . ARG A 1 2924 ? 254.012 197.896 218.031 1.00 2.37  ? 2924 ARG A NH1   1 
ATOM   11674 N  NH2   . ARG A 1 2924 ? 252.512 197.105 216.495 1.00 4.01  ? 2924 ARG A NH2   1 
ATOM   11675 N  N     . ILE A 1 2925 ? 247.295 201.466 218.003 1.00 0.90  ? 2925 ILE A N     1 
ATOM   11676 C  CA    . ILE A 1 2925 ? 246.301 201.505 216.934 1.00 1.27  ? 2925 ILE A CA    1 
ATOM   11677 C  C     . ILE A 1 2925 ? 245.802 202.928 216.700 1.00 0.87  ? 2925 ILE A C     1 
ATOM   11678 O  O     . ILE A 1 2925 ? 245.572 203.334 215.557 1.00 1.29  ? 2925 ILE A O     1 
ATOM   11679 C  CB    . ILE A 1 2925 ? 245.150 200.532 217.247 1.00 1.55  ? 2925 ILE A CB    1 
ATOM   11680 C  CG1   . ILE A 1 2925 ? 245.715 199.163 217.629 1.00 1.24  ? 2925 ILE A CG1   1 
ATOM   11681 C  CG2   . ILE A 1 2925 ? 244.215 200.404 216.063 1.00 0.29  ? 2925 ILE A CG2   1 
ATOM   11682 C  CD1   . ILE A 1 2925 ? 246.685 198.596 216.620 1.00 0.81  ? 2925 ILE A CD1   1 
ATOM   11683 N  N     . PHE A 1 2926 ? 245.625 203.706 217.770 1.00 1.69  ? 2926 PHE A N     1 
ATOM   11684 C  CA    . PHE A 1 2926 ? 245.215 205.099 217.620 1.00 1.22  ? 2926 PHE A CA    1 
ATOM   11685 C  C     . PHE A 1 2926 ? 246.253 205.962 216.917 1.00 2.33  ? 2926 PHE A C     1 
ATOM   11686 O  O     . PHE A 1 2926 ? 245.915 207.067 216.486 1.00 6.50  ? 2926 PHE A O     1 
ATOM   11687 C  CB    . PHE A 1 2926 ? 244.888 205.720 218.981 1.00 0.85  ? 2926 PHE A CB    1 
ATOM   11688 C  CG    . PHE A 1 2926 ? 243.623 205.208 219.598 1.00 0.57  ? 2926 PHE A CG    1 
ATOM   11689 C  CD1   . PHE A 1 2926 ? 242.703 204.499 218.846 1.00 0.38  ? 2926 PHE A CD1   1 
ATOM   11690 C  CD2   . PHE A 1 2926 ? 243.335 205.464 220.928 1.00 0.10  ? 2926 PHE A CD2   1 
ATOM   11691 C  CE1   . PHE A 1 2926 ? 241.533 204.042 219.412 1.00 0.33  ? 2926 PHE A CE1   1 
ATOM   11692 C  CE2   . PHE A 1 2926 ? 242.168 205.010 221.497 1.00 0.08  ? 2926 PHE A CE2   1 
ATOM   11693 C  CZ    . PHE A 1 2926 ? 241.265 204.300 220.739 1.00 0.13  ? 2926 PHE A CZ    1 
ATOM   11694 N  N     . ARG A 1 2927 ? 247.496 205.499 216.795 1.00 2.66  ? 2927 ARG A N     1 
ATOM   11695 C  CA    . ARG A 1 2927 ? 248.543 206.252 216.122 1.00 2.84  ? 2927 ARG A CA    1 
ATOM   11696 C  C     . ARG A 1 2927 ? 248.787 205.771 214.697 1.00 3.01  ? 2927 ARG A C     1 
ATOM   11697 O  O     . ARG A 1 2927 ? 249.752 206.208 214.062 1.00 6.76  ? 2927 ARG A O     1 
ATOM   11698 C  CB    . ARG A 1 2927 ? 249.839 206.191 216.935 1.00 3.53  ? 2927 ARG A CB    1 
ATOM   11699 C  CG    . ARG A 1 2927 ? 249.719 206.809 218.316 1.00 3.69  ? 2927 ARG A CG    1 
ATOM   11700 C  CD    . ARG A 1 2927 ? 251.053 206.837 219.041 1.00 4.17  ? 2927 ARG A CD    1 
ATOM   11701 N  NE    . ARG A 1 2927 ? 251.393 205.543 219.623 1.00 5.50  ? 2927 ARG A NE    1 
ATOM   11702 C  CZ    . ARG A 1 2927 ? 252.372 204.762 219.190 1.00 10.36 ? 2927 ARG A CZ    1 
ATOM   11703 N  NH1   . ARG A 1 2927 ? 253.134 205.113 218.166 1.00 8.89  ? 2927 ARG A NH1   1 
ATOM   11704 N  NH2   . ARG A 1 2927 ? 252.594 203.602 219.799 1.00 4.80  ? 2927 ARG A NH2   1 
ATOM   11705 N  N     . GLN A 1 2928 ? 247.935 204.886 214.178 1.00 3.77  ? 2928 GLN A N     1 
ATOM   11706 C  CA    . GLN A 1 2928 ? 248.016 204.393 212.815 1.00 3.28  ? 2928 GLN A CA    1 
ATOM   11707 C  C     . GLN A 1 2928 ? 246.835 204.902 211.995 1.00 1.99  ? 2928 GLN A C     1 
ATOM   11708 O  O     . GLN A 1 2928 ? 245.728 205.046 212.520 1.00 2.13  ? 2928 GLN A O     1 
ATOM   11709 C  CB    . GLN A 1 2928 ? 248.023 202.859 212.772 1.00 3.21  ? 2928 GLN A CB    1 
ATOM   11710 C  CG    . GLN A 1 2928 ? 249.331 202.211 213.200 1.00 4.56  ? 2928 GLN A CG    1 
ATOM   11711 C  CD    . GLN A 1 2928 ? 250.536 202.784 212.480 1.00 12.72 ? 2928 GLN A CD    1 
ATOM   11712 O  OE1   . GLN A 1 2928 ? 250.741 202.533 211.294 1.00 15.37 ? 2928 GLN A OE1   1 
ATOM   11713 N  NE2   . GLN A 1 2928 ? 251.344 203.551 213.199 1.00 11.04 ? 2928 GLN A NE2   1 
ATOM   11714 N  N     . PRO A 1 2929 ? 247.041 205.197 210.711 1.00 4.13  ? 2929 PRO A N     1 
ATOM   11715 C  CA    . PRO A 1 2929 ? 245.907 205.568 209.855 1.00 2.05  ? 2929 PRO A CA    1 
ATOM   11716 C  C     . PRO A 1 2929 ? 244.936 204.410 209.688 1.00 1.87  ? 2929 PRO A C     1 
ATOM   11717 O  O     . PRO A 1 2929 ? 245.332 203.248 209.586 1.00 3.28  ? 2929 PRO A O     1 
ATOM   11718 C  CB    . PRO A 1 2929 ? 246.575 205.941 208.526 1.00 3.38  ? 2929 PRO A CB    1 
ATOM   11719 C  CG    . PRO A 1 2929 ? 247.870 205.199 208.541 1.00 3.57  ? 2929 PRO A CG    1 
ATOM   11720 C  CD    . PRO A 1 2929 ? 248.316 205.214 209.975 1.00 4.51  ? 2929 PRO A CD    1 
ATOM   11721 N  N     . GLN A 1 2930 ? 243.645 204.749 209.644 1.00 2.74  ? 2930 GLN A N     1 
ATOM   11722 C  CA    . GLN A 1 2930 ? 242.563 203.761 209.659 1.00 2.29  ? 2930 GLN A CA    1 
ATOM   11723 C  C     . GLN A 1 2930 ? 242.757 202.756 210.790 1.00 1.64  ? 2930 GLN A C     1 
ATOM   11724 O  O     . GLN A 1 2930 ? 242.576 201.549 210.619 1.00 2.52  ? 2930 GLN A O     1 
ATOM   11725 C  CB    . GLN A 1 2930 ? 242.432 203.050 208.311 1.00 1.77  ? 2930 GLN A CB    1 
ATOM   11726 C  CG    . GLN A 1 2930 ? 241.457 203.717 207.362 1.00 4.30  ? 2930 GLN A CG    1 
ATOM   11727 C  CD    . GLN A 1 2930 ? 241.276 202.946 206.070 1.00 5.68  ? 2930 GLN A CD    1 
ATOM   11728 O  OE1   . GLN A 1 2930 ? 240.171 202.523 205.735 1.00 4.57  ? 2930 GLN A OE1   1 
ATOM   11729 N  NE2   . GLN A 1 2930 ? 242.365 202.763 205.335 1.00 3.84  ? 2930 GLN A NE2   1 
ATOM   11730 N  N     . GLY A 1 2931 ? 243.123 203.263 211.962 1.00 1.10  ? 2931 GLY A N     1 
ATOM   11731 C  CA    . GLY A 1 2931 ? 243.409 202.395 213.081 1.00 0.60  ? 2931 GLY A CA    1 
ATOM   11732 C  C     . GLY A 1 2931 ? 242.144 201.985 213.797 1.00 0.25  ? 2931 GLY A C     1 
ATOM   11733 O  O     . GLY A 1 2931 ? 241.600 202.738 214.607 1.00 0.14  ? 2931 GLY A O     1 
ATOM   11734 N  N     . HIS A 1 2932 ? 241.676 200.779 213.506 1.00 0.30  ? 2932 HIS A N     1 
ATOM   11735 C  CA    . HIS A 1 2932 ? 240.436 200.255 214.051 1.00 0.09  ? 2932 HIS A CA    1 
ATOM   11736 C  C     . HIS A 1 2932 ? 240.725 199.107 215.006 1.00 0.06  ? 2932 HIS A C     1 
ATOM   11737 O  O     . HIS A 1 2932 ? 241.638 198.307 214.794 1.00 0.19  ? 2932 HIS A O     1 
ATOM   11738 C  CB    . HIS A 1 2932 ? 239.508 199.796 212.928 1.00 0.22  ? 2932 HIS A CB    1 
ATOM   11739 C  CG    . HIS A 1 2932 ? 239.188 200.865 211.934 1.00 0.34  ? 2932 HIS A CG    1 
ATOM   11740 N  ND1   . HIS A 1 2932 ? 238.969 202.177 212.297 1.00 0.17  ? 2932 HIS A ND1   1 
ATOM   11741 C  CD2   . HIS A 1 2932 ? 239.071 200.824 210.587 1.00 0.49  ? 2932 HIS A CD2   1 
ATOM   11742 C  CE1   . HIS A 1 2932 ? 238.717 202.894 211.219 1.00 0.15  ? 2932 HIS A CE1   1 
ATOM   11743 N  NE2   . HIS A 1 2932 ? 238.773 202.098 210.168 1.00 0.33  ? 2932 HIS A NE2   1 
ATOM   11744 N  N     . LEU A 1 2933 ? 239.933 199.036 216.066 1.00 0.14  ? 2933 LEU A N     1 
ATOM   11745 C  CA    . LEU A 1 2933 ? 240.154 198.099 217.154 1.00 0.13  ? 2933 LEU A CA    1 
ATOM   11746 C  C     . LEU A 1 2933 ? 238.949 197.187 217.312 1.00 0.09  ? 2933 LEU A C     1 
ATOM   11747 O  O     . LEU A 1 2933 ? 237.804 197.642 217.264 1.00 0.14  ? 2933 LEU A O     1 
ATOM   11748 C  CB    . LEU A 1 2933 ? 240.415 198.840 218.464 1.00 0.12  ? 2933 LEU A CB    1 
ATOM   11749 C  CG    . LEU A 1 2933 ? 241.872 199.159 218.774 1.00 1.59  ? 2933 LEU A CG    1 
ATOM   11750 C  CD1   . LEU A 1 2933 ? 241.968 200.012 220.019 1.00 1.94  ? 2933 LEU A CD1   1 
ATOM   11751 C  CD2   . LEU A 1 2933 ? 242.653 197.875 218.943 1.00 1.92  ? 2933 LEU A CD2   1 
ATOM   11752 N  N     . LEU A 1 2934 ? 239.218 195.902 217.500 1.00 0.15  ? 2934 LEU A N     1 
ATOM   11753 C  CA    . LEU A 1 2934 ? 238.203 194.912 217.848 1.00 0.12  ? 2934 LEU A CA    1 
ATOM   11754 C  C     . LEU A 1 2934 ? 238.604 194.340 219.206 1.00 0.09  ? 2934 LEU A C     1 
ATOM   11755 O  O     . LEU A 1 2934 ? 239.397 193.400 219.289 1.00 0.08  ? 2934 LEU A O     1 
ATOM   11756 C  CB    . LEU A 1 2934 ? 238.083 193.827 216.776 1.00 0.18  ? 2934 LEU A CB    1 
ATOM   11757 C  CG    . LEU A 1 2934 ? 237.091 192.700 217.068 1.00 0.26  ? 2934 LEU A CG    1 
ATOM   11758 C  CD1   . LEU A 1 2934 ? 235.720 193.262 217.403 1.00 0.35  ? 2934 LEU A CD1   1 
ATOM   11759 C  CD2   . LEU A 1 2934 ? 237.008 191.733 215.899 1.00 0.72  ? 2934 LEU A CD2   1 
ATOM   11760 N  N     . LEU A 1 2935 ? 238.061 194.921 220.268 1.00 0.19  ? 2935 LEU A N     1 
ATOM   11761 C  CA    . LEU A 1 2935 ? 238.347 194.491 221.630 1.00 0.16  ? 2935 LEU A CA    1 
ATOM   11762 C  C     . LEU A 1 2935 ? 237.333 193.433 222.042 1.00 0.14  ? 2935 LEU A C     1 
ATOM   11763 O  O     . LEU A 1 2935 ? 236.134 193.713 222.119 1.00 0.41  ? 2935 LEU A O     1 
ATOM   11764 C  CB    . LEU A 1 2935 ? 238.303 195.680 222.588 1.00 0.34  ? 2935 LEU A CB    1 
ATOM   11765 C  CG    . LEU A 1 2935 ? 239.311 196.806 222.357 1.00 0.24  ? 2935 LEU A CG    1 
ATOM   11766 C  CD1   . LEU A 1 2935 ? 239.417 197.678 223.594 1.00 0.13  ? 2935 LEU A CD1   1 
ATOM   11767 C  CD2   . LEU A 1 2935 ? 240.672 196.255 221.966 1.00 0.30  ? 2935 LEU A CD2   1 
ATOM   11768 N  N     . ILE A 1 2936 ? 237.809 192.222 222.311 1.00 0.21  ? 2936 ILE A N     1 
ATOM   11769 C  CA    . ILE A 1 2936 ? 236.946 191.102 222.665 1.00 0.40  ? 2936 ILE A CA    1 
ATOM   11770 C  C     . ILE A 1 2936 ? 237.254 190.699 224.099 1.00 0.58  ? 2936 ILE A C     1 
ATOM   11771 O  O     . ILE A 1 2936 ? 238.408 190.416 224.441 1.00 0.74  ? 2936 ILE A O     1 
ATOM   11772 C  CB    . ILE A 1 2936 ? 237.123 189.918 221.704 1.00 0.80  ? 2936 ILE A CB    1 
ATOM   11773 C  CG1   . ILE A 1 2936 ? 236.896 190.377 220.261 1.00 0.55  ? 2936 ILE A CG1   1 
ATOM   11774 C  CG2   . ILE A 1 2936 ? 236.170 188.790 222.067 1.00 0.77  ? 2936 ILE A CG2   1 
ATOM   11775 C  CD1   . ILE A 1 2936 ? 237.058 189.283 219.241 1.00 0.84  ? 2936 ILE A CD1   1 
ATOM   11776 N  N     . GLY A 1 2937 ? 236.225 190.674 224.933 1.00 0.80  ? 2937 GLY A N     1 
ATOM   11777 C  CA    . GLY A 1 2937 ? 236.396 190.295 226.322 1.00 0.91  ? 2937 GLY A CA    1 
ATOM   11778 C  C     . GLY A 1 2937 ? 235.074 190.361 227.051 1.00 1.71  ? 2937 GLY A C     1 
ATOM   11779 O  O     . GLY A 1 2937 ? 234.067 190.846 226.523 1.00 5.37  ? 2937 GLY A O     1 
ATOM   11780 N  N     . VAL A 1 2938 ? 235.098 189.860 228.285 1.00 1.77  ? 2938 VAL A N     1 
ATOM   11781 C  CA    . VAL A 1 2938 ? 233.900 189.851 229.112 1.00 1.54  ? 2938 VAL A CA    1 
ATOM   11782 C  C     . VAL A 1 2938 ? 233.512 191.285 229.470 1.00 0.98  ? 2938 VAL A C     1 
ATOM   11783 O  O     . VAL A 1 2938 ? 234.361 192.178 229.578 1.00 1.86  ? 2938 VAL A O     1 
ATOM   11784 C  CB    . VAL A 1 2938 ? 234.141 188.999 230.371 1.00 1.66  ? 2938 VAL A CB    1 
ATOM   11785 C  CG1   . VAL A 1 2938 ? 232.873 188.871 231.205 1.00 1.88  ? 2938 VAL A CG1   1 
ATOM   11786 C  CG2   . VAL A 1 2938 ? 234.670 187.628 229.985 1.00 2.53  ? 2938 VAL A CG2   1 
ATOM   11787 N  N     . SER A 1 2939 ? 232.211 191.510 229.636 1.00 0.92  ? 2939 SER A N     1 
ATOM   11788 C  CA    . SER A 1 2939 ? 231.723 192.819 230.044 1.00 0.80  ? 2939 SER A CA    1 
ATOM   11789 C  C     . SER A 1 2939 ? 232.244 193.173 231.429 1.00 0.83  ? 2939 SER A C     1 
ATOM   11790 O  O     . SER A 1 2939 ? 232.405 192.306 232.292 1.00 1.95  ? 2939 SER A O     1 
ATOM   11791 C  CB    . SER A 1 2939 ? 230.196 192.845 230.035 1.00 2.39  ? 2939 SER A CB    1 
ATOM   11792 O  OG    . SER A 1 2939 ? 229.690 192.658 228.728 1.00 10.30 ? 2939 SER A OG    1 
ATOM   11793 N  N     . GLY A 1 2940 ? 232.518 194.456 231.638 1.00 0.76  ? 2940 GLY A N     1 
ATOM   11794 C  CA    . GLY A 1 2940 ? 233.034 194.909 232.911 1.00 0.73  ? 2940 GLY A CA    1 
ATOM   11795 C  C     . GLY A 1 2940 ? 234.515 194.705 233.106 1.00 0.96  ? 2940 GLY A C     1 
ATOM   11796 O  O     . GLY A 1 2940 ? 235.004 194.838 234.233 1.00 3.28  ? 2940 GLY A O     1 
ATOM   11797 N  N     . ALA A 1 2941 ? 235.249 194.382 232.046 1.00 0.80  ? 2941 ALA A N     1 
ATOM   11798 C  CA    . ALA A 1 2941 ? 236.688 194.195 232.120 1.00 0.59  ? 2941 ALA A CA    1 
ATOM   11799 C  C     . ALA A 1 2941 ? 237.464 195.467 231.813 1.00 1.06  ? 2941 ALA A C     1 
ATOM   11800 O  O     . ALA A 1 2941 ? 238.699 195.445 231.838 1.00 2.03  ? 2941 ALA A O     1 
ATOM   11801 C  CB    . ALA A 1 2941 ? 237.123 193.079 231.166 1.00 0.58  ? 2941 ALA A CB    1 
ATOM   11802 N  N     . GLY A 1 2942 ? 236.777 196.569 231.530 1.00 0.60  ? 2942 GLY A N     1 
ATOM   11803 C  CA    . GLY A 1 2942 ? 237.440 197.829 231.275 1.00 0.80  ? 2942 GLY A CA    1 
ATOM   11804 C  C     . GLY A 1 2942 ? 237.753 198.133 229.829 1.00 0.26  ? 2942 GLY A C     1 
ATOM   11805 O  O     . GLY A 1 2942 ? 238.556 199.033 229.569 1.00 0.40  ? 2942 GLY A O     1 
ATOM   11806 N  N     . LYS A 1 2943 ? 237.149 197.414 228.880 1.00 0.36  ? 2943 LYS A N     1 
ATOM   11807 C  CA    . LYS A 1 2943 ? 237.454 197.645 227.471 1.00 0.42  ? 2943 LYS A CA    1 
ATOM   11808 C  C     . LYS A 1 2943 ? 237.081 199.062 227.049 1.00 0.39  ? 2943 LYS A C     1 
ATOM   11809 O  O     . LYS A 1 2943 ? 237.863 199.751 226.389 1.00 0.27  ? 2943 LYS A O     1 
ATOM   11810 C  CB    . LYS A 1 2943 ? 236.729 196.618 226.600 1.00 0.26  ? 2943 LYS A CB    1 
ATOM   11811 C  CG    . LYS A 1 2943 ? 237.240 195.198 226.753 1.00 0.36  ? 2943 LYS A CG    1 
ATOM   11812 C  CD    . LYS A 1 2943 ? 236.564 194.251 225.771 1.00 0.32  ? 2943 LYS A CD    1 
ATOM   11813 C  CE    . LYS A 1 2943 ? 235.053 194.285 225.914 1.00 0.49  ? 2943 LYS A CE    1 
ATOM   11814 N  NZ    . LYS A 1 2943 ? 234.610 193.965 227.297 1.00 0.51  ? 2943 LYS A NZ    1 
ATOM   11815 N  N     . THR A 1 2944 ? 235.887 199.518 227.434 1.00 0.26  ? 2944 THR A N     1 
ATOM   11816 C  CA    . THR A 1 2944 ? 235.470 200.867 227.071 1.00 0.24  ? 2944 THR A CA    1 
ATOM   11817 C  C     . THR A 1 2944 ? 236.265 201.916 227.837 1.00 0.39  ? 2944 THR A C     1 
ATOM   11818 O  O     . THR A 1 2944 ? 236.695 202.920 227.259 1.00 0.35  ? 2944 THR A O     1 
ATOM   11819 C  CB    . THR A 1 2944 ? 233.974 201.045 227.322 1.00 0.45  ? 2944 THR A CB    1 
ATOM   11820 O  OG1   . THR A 1 2944 ? 233.257 199.952 226.739 1.00 0.65  ? 2944 THR A OG1   1 
ATOM   11821 C  CG2   . THR A 1 2944 ? 233.484 202.344 226.712 1.00 0.54  ? 2944 THR A CG2   1 
ATOM   11822 N  N     . THR A 1 2945 ? 236.469 201.701 229.138 1.00 0.42  ? 2945 THR A N     1 
ATOM   11823 C  CA    . THR A 1 2945 ? 237.149 202.697 229.959 1.00 0.21  ? 2945 THR A CA    1 
ATOM   11824 C  C     . THR A 1 2945 ? 238.593 202.886 229.517 1.00 0.19  ? 2945 THR A C     1 
ATOM   11825 O  O     . THR A 1 2945 ? 239.074 204.020 229.419 1.00 1.10  ? 2945 THR A O     1 
ATOM   11826 C  CB    . THR A 1 2945 ? 237.087 202.292 231.433 1.00 0.24  ? 2945 THR A CB    1 
ATOM   11827 O  OG1   . THR A 1 2945 ? 235.723 202.083 231.814 1.00 0.48  ? 2945 THR A OG1   1 
ATOM   11828 C  CG2   . THR A 1 2945 ? 237.688 203.376 232.307 1.00 0.12  ? 2945 THR A CG2   1 
ATOM   11829 N  N     . LEU A 1 2946 ? 239.300 201.789 229.243 1.00 0.14  ? 2946 LEU A N     1 
ATOM   11830 C  CA    . LEU A 1 2946 ? 240.675 201.904 228.777 1.00 0.12  ? 2946 LEU A CA    1 
ATOM   11831 C  C     . LEU A 1 2946 ? 240.738 202.585 227.417 1.00 0.09  ? 2946 LEU A C     1 
ATOM   11832 O  O     . LEU A 1 2946 ? 241.646 203.383 227.159 1.00 0.10  ? 2946 LEU A O     1 
ATOM   11833 C  CB    . LEU A 1 2946 ? 241.331 200.526 228.726 1.00 0.17  ? 2946 LEU A CB    1 
ATOM   11834 C  CG    . LEU A 1 2946 ? 241.669 199.899 230.079 1.00 0.16  ? 2946 LEU A CG    1 
ATOM   11835 C  CD1   . LEU A 1 2946 ? 242.541 198.672 229.893 1.00 0.23  ? 2946 LEU A CD1   1 
ATOM   11836 C  CD2   . LEU A 1 2946 ? 242.341 200.908 230.996 1.00 0.14  ? 2946 LEU A CD2   1 
ATOM   11837 N  N     . SER A 1 2947 ? 239.781 202.287 226.537 1.00 0.10  ? 2947 SER A N     1 
ATOM   11838 C  CA    . SER A 1 2947 ? 239.749 202.934 225.231 1.00 0.09  ? 2947 SER A CA    1 
ATOM   11839 C  C     . SER A 1 2947 ? 239.557 204.439 225.364 1.00 0.08  ? 2947 SER A C     1 
ATOM   11840 O  O     . SER A 1 2947 ? 240.223 205.218 224.674 1.00 0.07  ? 2947 SER A O     1 
ATOM   11841 C  CB    . SER A 1 2947 ? 238.645 202.323 224.369 1.00 0.10  ? 2947 SER A CB    1 
ATOM   11842 O  OG    . SER A 1 2947 ? 238.866 200.943 224.162 1.00 1.07  ? 2947 SER A OG    1 
ATOM   11843 N  N     . ARG A 1 2948 ? 238.652 204.867 226.247 1.00 0.09  ? 2948 ARG A N     1 
ATOM   11844 C  CA    . ARG A 1 2948 ? 238.463 206.297 226.470 1.00 0.12  ? 2948 ARG A CA    1 
ATOM   11845 C  C     . ARG A 1 2948 ? 239.703 206.929 227.086 1.00 0.10  ? 2948 ARG A C     1 
ATOM   11846 O  O     . ARG A 1 2948 ? 240.072 208.056 226.738 1.00 0.16  ? 2948 ARG A O     1 
ATOM   11847 C  CB    . ARG A 1 2948 ? 237.237 206.535 227.352 1.00 0.13  ? 2948 ARG A CB    1 
ATOM   11848 C  CG    . ARG A 1 2948 ? 235.937 206.079 226.723 1.00 0.78  ? 2948 ARG A CG    1 
ATOM   11849 C  CD    . ARG A 1 2948 ? 234.788 206.092 227.713 1.00 2.35  ? 2948 ARG A CD    1 
ATOM   11850 N  NE    . ARG A 1 2948 ? 234.406 207.444 228.100 1.00 4.41  ? 2948 ARG A NE    1 
ATOM   11851 C  CZ    . ARG A 1 2948 ? 233.314 207.743 228.790 1.00 6.08  ? 2948 ARG A CZ    1 
ATOM   11852 N  NH1   . ARG A 1 2948 ? 232.468 206.806 229.183 1.00 5.63  ? 2948 ARG A NH1   1 
ATOM   11853 N  NH2   . ARG A 1 2948 ? 233.062 209.013 229.090 1.00 5.53  ? 2948 ARG A NH2   1 
ATOM   11854 N  N     . PHE A 1 2949 ? 240.355 206.222 228.009 1.00 0.09  ? 2949 PHE A N     1 
ATOM   11855 C  CA    . PHE A 1 2949 ? 241.547 206.758 228.656 1.00 0.10  ? 2949 PHE A CA    1 
ATOM   11856 C  C     . PHE A 1 2949 ? 242.693 206.920 227.665 1.00 0.11  ? 2949 PHE A C     1 
ATOM   11857 O  O     . PHE A 1 2949 ? 243.400 207.933 227.685 1.00 0.19  ? 2949 PHE A O     1 
ATOM   11858 C  CB    . PHE A 1 2949 ? 241.949 205.854 229.820 1.00 0.08  ? 2949 PHE A CB    1 
ATOM   11859 C  CG    . PHE A 1 2949 ? 243.331 206.107 230.341 1.00 0.06  ? 2949 PHE A CG    1 
ATOM   11860 C  CD1   . PHE A 1 2949 ? 243.644 207.308 230.954 1.00 0.10  ? 2949 PHE A CD1   1 
ATOM   11861 C  CD2   . PHE A 1 2949 ? 244.314 205.142 230.231 1.00 0.07  ? 2949 PHE A CD2   1 
ATOM   11862 C  CE1   . PHE A 1 2949 ? 244.909 207.544 231.439 1.00 0.12  ? 2949 PHE A CE1   1 
ATOM   11863 C  CE2   . PHE A 1 2949 ? 245.586 205.371 230.715 1.00 0.16  ? 2949 PHE A CE2   1 
ATOM   11864 C  CZ    . PHE A 1 2949 ? 245.882 206.573 231.325 1.00 0.25  ? 2949 PHE A CZ    1 
ATOM   11865 N  N     . VAL A 1 2950 ? 242.904 205.927 226.800 1.00 0.12  ? 2950 VAL A N     1 
ATOM   11866 C  CA    . VAL A 1 2950 ? 243.945 206.040 225.784 1.00 0.13  ? 2950 VAL A CA    1 
ATOM   11867 C  C     . VAL A 1 2950 ? 243.559 207.082 224.739 1.00 0.08  ? 2950 VAL A C     1 
ATOM   11868 O  O     . VAL A 1 2950 ? 244.413 207.816 224.230 1.00 0.24  ? 2950 VAL A O     1 
ATOM   11869 C  CB    . VAL A 1 2950 ? 244.226 204.663 225.154 1.00 0.14  ? 2950 VAL A CB    1 
ATOM   11870 C  CG1   . VAL A 1 2950 ? 245.220 204.788 224.016 1.00 0.19  ? 2950 VAL A CG1   1 
ATOM   11871 C  CG2   . VAL A 1 2950 ? 244.754 203.706 226.205 1.00 0.09  ? 2950 VAL A CG2   1 
ATOM   11872 N  N     . ALA A 1 2951 ? 242.269 207.167 224.408 1.00 0.05  ? 2951 ALA A N     1 
ATOM   11873 C  CA    . ALA A 1 2951 ? 241.809 208.186 223.470 1.00 0.16  ? 2951 ALA A CA    1 
ATOM   11874 C  C     . ALA A 1 2951 ? 242.055 209.586 224.015 1.00 0.66  ? 2951 ALA A C     1 
ATOM   11875 O  O     . ALA A 1 2951 ? 242.388 210.506 223.258 1.00 1.10  ? 2951 ALA A O     1 
ATOM   11876 C  CB    . ALA A 1 2951 ? 240.328 207.986 223.156 1.00 0.15  ? 2951 ALA A CB    1 
ATOM   11877 N  N     . TRP A 1 2952 ? 241.886 209.770 225.325 1.00 0.51  ? 2952 TRP A N     1 
ATOM   11878 C  CA    . TRP A 1 2952 ? 242.161 211.065 225.935 1.00 0.39  ? 2952 TRP A CA    1 
ATOM   11879 C  C     . TRP A 1 2952 ? 243.657 211.354 225.982 1.00 0.68  ? 2952 TRP A C     1 
ATOM   11880 O  O     . TRP A 1 2952 ? 244.063 212.521 225.941 1.00 1.37  ? 2952 TRP A O     1 
ATOM   11881 C  CB    . TRP A 1 2952 ? 241.546 211.114 227.336 1.00 0.46  ? 2952 TRP A CB    1 
ATOM   11882 C  CG    . TRP A 1 2952 ? 242.057 212.212 228.217 1.00 1.07  ? 2952 TRP A CG    1 
ATOM   11883 C  CD1   . TRP A 1 2952 ? 241.582 213.486 228.293 1.00 1.04  ? 2952 TRP A CD1   1 
ATOM   11884 C  CD2   . TRP A 1 2952 ? 243.127 212.127 229.163 1.00 0.70  ? 2952 TRP A CD2   1 
ATOM   11885 N  NE1   . TRP A 1 2952 ? 242.294 214.202 229.221 1.00 0.95  ? 2952 TRP A NE1   1 
ATOM   11886 C  CE2   . TRP A 1 2952 ? 243.249 213.391 229.769 1.00 0.76  ? 2952 TRP A CE2   1 
ATOM   11887 C  CE3   . TRP A 1 2952 ? 243.999 211.104 229.552 1.00 0.70  ? 2952 TRP A CE3   1 
ATOM   11888 C  CZ2   . TRP A 1 2952 ? 244.206 213.662 230.744 1.00 1.67  ? 2952 TRP A CZ2   1 
ATOM   11889 C  CZ3   . TRP A 1 2952 ? 244.948 211.376 230.518 1.00 1.17  ? 2952 TRP A CZ3   1 
ATOM   11890 C  CH2   . TRP A 1 2952 ? 245.044 212.643 231.103 1.00 1.71  ? 2952 TRP A CH2   1 
ATOM   11891 N  N     . MET A 1 2953 ? 244.487 210.311 226.055 1.00 0.65  ? 2953 MET A N     1 
ATOM   11892 C  CA    . MET A 1 2953 ? 245.933 210.507 226.060 1.00 0.73  ? 2953 MET A CA    1 
ATOM   11893 C  C     . MET A 1 2953 ? 246.464 210.872 224.681 1.00 1.70  ? 2953 MET A C     1 
ATOM   11894 O  O     . MET A 1 2953 ? 247.504 211.530 224.571 1.00 6.84  ? 2953 MET A O     1 
ATOM   11895 C  CB    . MET A 1 2953 ? 246.635 209.250 226.569 1.00 1.83  ? 2953 MET A CB    1 
ATOM   11896 C  CG    . MET A 1 2953 ? 246.536 209.031 228.067 1.00 2.13  ? 2953 MET A CG    1 
ATOM   11897 S  SD    . MET A 1 2953 ? 247.469 207.583 228.575 1.00 24.58 ? 2953 MET A SD    1 
ATOM   11898 C  CE    . MET A 1 2953 ? 249.129 208.254 228.611 1.00 2.47  ? 2953 MET A CE    1 
ATOM   11899 N  N     . ASN A 1 2954 ? 245.784 210.445 223.621 1.00 2.17  ? 2954 ASN A N     1 
ATOM   11900 C  CA    . ASN A 1 2954 ? 246.220 210.700 222.256 1.00 1.86  ? 2954 ASN A CA    1 
ATOM   11901 C  C     . ASN A 1 2954 ? 245.493 211.876 221.617 1.00 3.38  ? 2954 ASN A C     1 
ATOM   11902 O  O     . ASN A 1 2954 ? 245.661 212.114 220.418 1.00 9.62  ? 2954 ASN A O     1 
ATOM   11903 C  CB    . ASN A 1 2954 ? 246.039 209.444 221.406 1.00 1.39  ? 2954 ASN A CB    1 
ATOM   11904 C  CG    . ASN A 1 2954 ? 247.067 208.381 221.717 1.00 2.82  ? 2954 ASN A CG    1 
ATOM   11905 O  OD1   . ASN A 1 2954 ? 248.256 208.559 221.462 1.00 6.79  ? 2954 ASN A OD1   1 
ATOM   11906 N  ND2   . ASN A 1 2954 ? 246.618 207.270 222.282 1.00 3.26  ? 2954 ASN A ND2   1 
ATOM   11907 N  N     . GLY A 1 2955 ? 244.693 212.613 222.385 1.00 1.98  ? 2955 GLY A N     1 
ATOM   11908 C  CA    . GLY A 1 2955 ? 243.965 213.743 221.853 1.00 0.64  ? 2955 GLY A CA    1 
ATOM   11909 C  C     . GLY A 1 2955 ? 242.750 213.395 221.030 1.00 0.90  ? 2955 GLY A C     1 
ATOM   11910 O  O     . GLY A 1 2955 ? 242.230 214.266 220.322 1.00 2.26  ? 2955 GLY A O     1 
ATOM   11911 N  N     . LEU A 1 2956 ? 242.278 212.155 221.096 1.00 2.17  ? 2956 LEU A N     1 
ATOM   11912 C  CA    . LEU A 1 2956 ? 241.125 211.719 220.322 1.00 0.60  ? 2956 LEU A CA    1 
ATOM   11913 C  C     . LEU A 1 2956 ? 239.849 211.979 221.108 1.00 1.12  ? 2956 LEU A C     1 
ATOM   11914 O  O     . LEU A 1 2956 ? 239.760 211.640 222.292 1.00 4.07  ? 2956 LEU A O     1 
ATOM   11915 C  CB    . LEU A 1 2956 ? 241.230 210.232 219.976 1.00 0.84  ? 2956 LEU A CB    1 
ATOM   11916 C  CG    . LEU A 1 2956 ? 242.024 209.789 218.742 1.00 0.72  ? 2956 LEU A CG    1 
ATOM   11917 C  CD1   . LEU A 1 2956 ? 243.459 210.279 218.780 1.00 1.39  ? 2956 LEU A CD1   1 
ATOM   11918 C  CD2   . LEU A 1 2956 ? 241.978 208.272 218.599 1.00 0.22  ? 2956 LEU A CD2   1 
ATOM   11919 N  N     . SER A 1 2957 ? 238.868 212.585 220.451 1.00 1.00  ? 2957 SER A N     1 
ATOM   11920 C  CA    . SER A 1 2957 ? 237.551 212.735 221.043 1.00 0.68  ? 2957 SER A CA    1 
ATOM   11921 C  C     . SER A 1 2957 ? 236.824 211.398 221.024 1.00 0.78  ? 2957 SER A C     1 
ATOM   11922 O  O     . SER A 1 2957 ? 236.934 210.628 220.068 1.00 0.97  ? 2957 SER A O     1 
ATOM   11923 C  CB    . SER A 1 2957 ? 236.741 213.789 220.292 1.00 2.06  ? 2957 SER A CB    1 
ATOM   11924 O  OG    . SER A 1 2957 ? 237.398 215.043 220.320 1.00 13.59 ? 2957 SER A OG    1 
ATOM   11925 N  N     . VAL A 1 2958 ? 236.088 211.120 222.090 1.00 2.21  ? 2958 VAL A N     1 
ATOM   11926 C  CA    . VAL A 1 2958 ? 235.343 209.876 222.217 1.00 1.22  ? 2958 VAL A CA    1 
ATOM   11927 C  C     . VAL A 1 2958 ? 233.911 210.138 221.778 1.00 1.15  ? 2958 VAL A C     1 
ATOM   11928 O  O     . VAL A 1 2958 ? 233.236 211.018 222.322 1.00 1.62  ? 2958 VAL A O     1 
ATOM   11929 C  CB    . VAL A 1 2958 ? 235.388 209.331 223.653 1.00 0.74  ? 2958 VAL A CB    1 
ATOM   11930 C  CG1   . VAL A 1 2958 ? 234.338 208.251 223.836 1.00 0.73  ? 2958 VAL A CG1   1 
ATOM   11931 C  CG2   . VAL A 1 2958 ? 236.768 208.794 223.971 1.00 0.64  ? 2958 VAL A CG2   1 
ATOM   11932 N  N     . TYR A 1 2959 ? 233.450 209.384 220.786 1.00 1.51  ? 2959 TYR A N     1 
ATOM   11933 C  CA    . TYR A 1 2959 ? 232.060 209.411 220.361 1.00 0.87  ? 2959 TYR A CA    1 
ATOM   11934 C  C     . TYR A 1 2959 ? 231.430 208.056 220.638 1.00 0.81  ? 2959 TYR A C     1 
ATOM   11935 O  O     . TYR A 1 2959 ? 231.948 207.023 220.203 1.00 1.00  ? 2959 TYR A O     1 
ATOM   11936 C  CB    . TYR A 1 2959 ? 231.927 209.758 218.876 1.00 0.80  ? 2959 TYR A CB    1 
ATOM   11937 C  CG    . TYR A 1 2959 ? 230.504 210.058 218.464 1.00 2.04  ? 2959 TYR A CG    1 
ATOM   11938 C  CD1   . TYR A 1 2959 ? 229.611 209.032 218.177 1.00 2.10  ? 2959 TYR A CD1   1 
ATOM   11939 C  CD2   . TYR A 1 2959 ? 230.048 211.366 218.372 1.00 2.06  ? 2959 TYR A CD2   1 
ATOM   11940 C  CE1   . TYR A 1 2959 ? 228.312 209.299 217.810 1.00 2.67  ? 2959 TYR A CE1   1 
ATOM   11941 C  CE2   . TYR A 1 2959 ? 228.750 211.641 218.002 1.00 3.13  ? 2959 TYR A CE2   1 
ATOM   11942 C  CZ    . TYR A 1 2959 ? 227.885 210.604 217.721 1.00 5.14  ? 2959 TYR A CZ    1 
ATOM   11943 O  OH    . TYR A 1 2959 ? 226.589 210.871 217.352 1.00 7.36  ? 2959 TYR A OH    1 
ATOM   11944 N  N     . GLN A 1 2960 ? 230.317 208.068 221.359 1.00 0.65  ? 2960 GLN A N     1 
ATOM   11945 C  CA    . GLN A 1 2960 ? 229.505 206.883 221.580 1.00 1.59  ? 2960 GLN A CA    1 
ATOM   11946 C  C     . GLN A 1 2960 ? 228.072 207.199 221.193 1.00 2.67  ? 2960 GLN A C     1 
ATOM   11947 O  O     . GLN A 1 2960 ? 227.536 208.246 221.571 1.00 7.48  ? 2960 GLN A O     1 
ATOM   11948 C  CB    . GLN A 1 2960 ? 229.570 206.418 223.044 1.00 1.23  ? 2960 GLN A CB    1 
ATOM   11949 C  CG    . GLN A 1 2960 ? 230.963 206.043 223.515 1.00 1.60  ? 2960 GLN A CG    1 
ATOM   11950 C  CD    . GLN A 1 2960 ? 230.994 205.611 224.967 1.00 4.05  ? 2960 GLN A CD    1 
ATOM   11951 O  OE1   . GLN A 1 2960 ? 230.386 204.609 225.343 1.00 4.46  ? 2960 GLN A OE1   1 
ATOM   11952 N  NE2   . GLN A 1 2960 ? 231.705 206.366 225.794 1.00 7.36  ? 2960 GLN A NE2   1 
ATOM   11953 N  N     . ILE A 1 2961 ? 227.456 206.306 220.420 1.00 1.82  ? 2961 ILE A N     1 
ATOM   11954 C  CA    . ILE A 1 2961 ? 226.061 206.496 220.049 1.00 3.17  ? 2961 ILE A CA    1 
ATOM   11955 C  C     . ILE A 1 2961 ? 225.184 206.273 221.271 1.00 6.95  ? 2961 ILE A C     1 
ATOM   11956 O  O     . ILE A 1 2961 ? 225.442 205.384 222.095 1.00 8.20  ? 2961 ILE A O     1 
ATOM   11957 C  CB    . ILE A 1 2961 ? 225.679 205.586 218.871 1.00 2.31  ? 2961 ILE A CB    1 
ATOM   11958 C  CG1   . ILE A 1 2961 ? 225.500 204.132 219.312 1.00 3.30  ? 2961 ILE A CG1   1 
ATOM   11959 C  CG2   . ILE A 1 2961 ? 226.698 205.701 217.753 1.00 5.17  ? 2961 ILE A CG2   1 
ATOM   11960 C  CD1   . ILE A 1 2961 ? 224.982 203.235 218.216 1.00 6.55  ? 2961 ILE A CD1   1 
ATOM   11961 N  N     . LYS A 1 2962 ? 224.163 207.115 221.420 1.00 9.74  ? 2962 LYS A N     1 
ATOM   11962 C  CA    . LYS A 1 2962 ? 223.354 207.149 222.634 1.00 6.00  ? 2962 LYS A CA    1 
ATOM   11963 C  C     . LYS A 1 2962 ? 222.065 206.366 222.385 1.00 7.85  ? 2962 LYS A C     1 
ATOM   11964 O  O     . LYS A 1 2962 ? 220.984 206.917 222.165 1.00 7.96  ? 2962 LYS A O     1 
ATOM   11965 C  CB    . LYS A 1 2962 ? 223.080 208.590 223.035 1.00 8.61  ? 2962 LYS A CB    1 
ATOM   11966 C  CG    . LYS A 1 2962 ? 224.351 209.367 223.330 1.00 12.72 ? 2962 LYS A CG    1 
ATOM   11967 C  CD    . LYS A 1 2962 ? 225.048 208.886 224.587 1.00 20.05 ? 2962 LYS A CD    1 
ATOM   11968 C  CE    . LYS A 1 2962 ? 226.321 209.680 224.835 1.00 13.94 ? 2962 LYS A CE    1 
ATOM   11969 N  NZ    . LYS A 1 2962 ? 226.047 211.097 225.188 1.00 18.64 ? 2962 LYS A NZ    1 
ATOM   11970 N  N     . VAL A 1 2963 ? 222.204 205.040 222.417 1.00 6.45  ? 2963 VAL A N     1 
ATOM   11971 C  CA    . VAL A 1 2963 ? 221.079 204.179 222.076 1.00 7.88  ? 2963 VAL A CA    1 
ATOM   11972 C  C     . VAL A 1 2963 ? 220.019 204.227 223.169 1.00 10.38 ? 2963 VAL A C     1 
ATOM   11973 O  O     . VAL A 1 2963 ? 220.274 204.571 224.330 1.00 6.99  ? 2963 VAL A O     1 
ATOM   11974 C  CB    . VAL A 1 2963 ? 221.534 202.734 221.819 1.00 7.60  ? 2963 VAL A CB    1 
ATOM   11975 C  CG1   . VAL A 1 2963 ? 222.479 202.677 220.645 1.00 8.34  ? 2963 VAL A CG1   1 
ATOM   11976 C  CG2   . VAL A 1 2963 ? 222.194 202.161 223.061 1.00 12.73 ? 2963 VAL A CG2   1 
ATOM   11977 N  N     . HIS A 1 2964 ? 218.802 203.872 222.774 1.00 10.48 ? 2964 HIS A N     1 
ATOM   11978 C  CA    . HIS A 1 2964 ? 217.674 203.739 223.674 1.00 9.07  ? 2964 HIS A CA    1 
ATOM   11979 C  C     . HIS A 1 2964 ? 216.704 202.750 223.041 1.00 11.30 ? 2964 HIS A C     1 
ATOM   11980 O  O     . HIS A 1 2964 ? 216.985 202.167 221.991 1.00 13.95 ? 2964 HIS A O     1 
ATOM   11981 C  CB    . HIS A 1 2964 ? 217.035 205.102 223.965 1.00 9.12  ? 2964 HIS A CB    1 
ATOM   11982 C  CG    . HIS A 1 2964 ? 216.747 205.913 222.740 1.00 9.95  ? 2964 HIS A CG    1 
ATOM   11983 N  ND1   . HIS A 1 2964 ? 215.543 205.855 222.074 1.00 11.45 ? 2964 HIS A ND1   1 
ATOM   11984 C  CD2   . HIS A 1 2964 ? 217.506 206.812 222.071 1.00 8.34  ? 2964 HIS A CD2   1 
ATOM   11985 C  CE1   . HIS A 1 2964 ? 215.576 206.678 221.040 1.00 8.64  ? 2964 HIS A CE1   1 
ATOM   11986 N  NE2   . HIS A 1 2964 ? 216.754 207.271 221.017 1.00 8.94  ? 2964 HIS A NE2   1 
ATOM   11987 N  N     . ARG A 1 2965 ? 215.558 202.551 223.693 1.00 14.19 ? 2965 ARG A N     1 
ATOM   11988 C  CA    . ARG A 1 2965 ? 214.602 201.570 223.194 1.00 16.14 ? 2965 ARG A CA    1 
ATOM   11989 C  C     . ARG A 1 2965 ? 214.032 201.952 221.834 1.00 11.40 ? 2965 ARG A C     1 
ATOM   11990 O  O     . ARG A 1 2965 ? 213.610 201.071 221.080 1.00 12.28 ? 2965 ARG A O     1 
ATOM   11991 C  CB    . ARG A 1 2965 ? 213.461 201.385 224.193 1.00 15.84 ? 2965 ARG A CB    1 
ATOM   11992 C  CG    . ARG A 1 2965 ? 212.777 202.677 224.601 1.00 19.25 ? 2965 ARG A CG    1 
ATOM   11993 C  CD    . ARG A 1 2965 ? 211.657 202.388 225.576 1.00 25.91 ? 2965 ARG A CD    1 
ATOM   11994 N  NE    . ARG A 1 2965 ? 210.723 201.419 225.018 1.00 21.13 ? 2965 ARG A NE    1 
ATOM   11995 C  CZ    . ARG A 1 2965 ? 210.496 200.219 225.534 1.00 25.01 ? 2965 ARG A CZ    1 
ATOM   11996 N  NH1   . ARG A 1 2965 ? 211.122 199.807 226.625 1.00 24.37 ? 2965 ARG A NH1   1 
ATOM   11997 N  NH2   . ARG A 1 2965 ? 209.628 199.409 224.936 1.00 22.57 ? 2965 ARG A NH2   1 
ATOM   11998 N  N     . LYS A 1 2966 ? 214.015 203.242 221.502 1.00 11.96 ? 2966 LYS A N     1 
ATOM   11999 C  CA    . LYS A 1 2966 ? 213.465 203.721 220.241 1.00 13.29 ? 2966 LYS A CA    1 
ATOM   12000 C  C     . LYS A 1 2966 ? 214.543 204.125 219.241 1.00 13.92 ? 2966 LYS A C     1 
ATOM   12001 O  O     . LYS A 1 2966 ? 214.236 204.800 218.253 1.00 15.53 ? 2966 LYS A O     1 
ATOM   12002 C  CB    . LYS A 1 2966 ? 212.516 204.895 220.492 1.00 11.67 ? 2966 LYS A CB    1 
ATOM   12003 C  CG    . LYS A 1 2966 ? 211.303 204.597 221.382 1.00 14.13 ? 2966 LYS A CG    1 
ATOM   12004 C  CD    . LYS A 1 2966 ? 210.250 203.705 220.716 1.00 14.24 ? 2966 LYS A CD    1 
ATOM   12005 C  CE    . LYS A 1 2966 ? 210.433 202.226 221.038 1.00 22.43 ? 2966 LYS A CE    1 
ATOM   12006 N  NZ    . LYS A 1 2966 ? 209.333 201.398 220.467 1.00 26.74 ? 2966 LYS A NZ    1 
ATOM   12007 N  N     . TYR A 1 2967 ? 215.795 203.742 219.477 1.00 14.54 ? 2967 TYR A N     1 
ATOM   12008 C  CA    . TYR A 1 2967 ? 216.877 204.083 218.562 1.00 7.91  ? 2967 TYR A CA    1 
ATOM   12009 C  C     . TYR A 1 2967 ? 216.819 203.182 217.333 1.00 9.41  ? 2967 TYR A C     1 
ATOM   12010 O  O     . TYR A 1 2967 ? 216.858 201.955 217.449 1.00 9.78  ? 2967 TYR A O     1 
ATOM   12011 C  CB    . TYR A 1 2967 ? 218.219 203.938 219.277 1.00 6.96  ? 2967 TYR A CB    1 
ATOM   12012 C  CG    . TYR A 1 2967 ? 219.406 204.518 218.547 1.00 6.30  ? 2967 TYR A CG    1 
ATOM   12013 C  CD1   . TYR A 1 2967 ? 220.115 203.765 217.620 1.00 3.67  ? 2967 TYR A CD1   1 
ATOM   12014 C  CD2   . TYR A 1 2967 ? 219.836 205.813 218.807 1.00 4.79  ? 2967 TYR A CD2   1 
ATOM   12015 C  CE1   . TYR A 1 2967 ? 221.208 204.290 216.963 1.00 4.12  ? 2967 TYR A CE1   1 
ATOM   12016 C  CE2   . TYR A 1 2967 ? 220.927 206.346 218.156 1.00 4.61  ? 2967 TYR A CE2   1 
ATOM   12017 C  CZ    . TYR A 1 2967 ? 221.610 205.582 217.234 1.00 3.05  ? 2967 TYR A CZ    1 
ATOM   12018 O  OH    . TYR A 1 2967 ? 222.695 206.115 216.588 1.00 2.28  ? 2967 TYR A OH    1 
ATOM   12019 N  N     . THR A 1 2968 ? 216.722 203.791 216.153 1.00 11.71 ? 2968 THR A N     1 
ATOM   12020 C  CA    . THR A 1 2968 ? 216.480 203.062 214.915 1.00 12.46 ? 2968 THR A CA    1 
ATOM   12021 C  C     . THR A 1 2968 ? 217.619 203.289 213.927 1.00 7.81  ? 2968 THR A C     1 
ATOM   12022 O  O     . THR A 1 2968 ? 218.642 203.903 214.246 1.00 5.40  ? 2968 THR A O     1 
ATOM   12023 C  CB    . THR A 1 2968 ? 215.139 203.466 214.291 1.00 12.70 ? 2968 THR A CB    1 
ATOM   12024 O  OG1   . THR A 1 2968 ? 215.251 204.782 213.739 1.00 15.79 ? 2968 THR A OG1   1 
ATOM   12025 C  CG2   . THR A 1 2968 ? 214.030 203.439 215.327 1.00 9.53  ? 2968 THR A CG2   1 
ATOM   12026 N  N     . GLY A 1 2969 ? 217.426 202.773 212.711 1.00 10.22 ? 2969 GLY A N     1 
ATOM   12027 C  CA    . GLY A 1 2969 ? 218.484 202.809 211.714 1.00 5.06  ? 2969 GLY A CA    1 
ATOM   12028 C  C     . GLY A 1 2969 ? 218.815 204.210 211.236 1.00 8.75  ? 2969 GLY A C     1 
ATOM   12029 O  O     . GLY A 1 2969 ? 219.984 204.542 211.029 1.00 14.85 ? 2969 GLY A O     1 
ATOM   12030 N  N     . GLU A 1 2970 ? 217.795 205.048 211.037 1.00 9.14  ? 2970 GLU A N     1 
ATOM   12031 C  CA    . GLU A 1 2970 ? 218.061 206.411 210.591 1.00 7.41  ? 2970 GLU A CA    1 
ATOM   12032 C  C     . GLU A 1 2970 ? 218.612 207.269 211.724 1.00 8.50  ? 2970 GLU A C     1 
ATOM   12033 O  O     . GLU A 1 2970 ? 219.233 208.310 211.478 1.00 9.51  ? 2970 GLU A O     1 
ATOM   12034 C  CB    . GLU A 1 2970 ? 216.808 207.035 209.968 1.00 8.53  ? 2970 GLU A CB    1 
ATOM   12035 C  CG    . GLU A 1 2970 ? 215.661 207.333 210.911 1.00 14.23 ? 2970 GLU A CG    1 
ATOM   12036 C  CD    . GLU A 1 2970 ? 214.758 206.132 211.138 1.00 24.13 ? 2970 GLU A CD    1 
ATOM   12037 O  OE1   . GLU A 1 2970 ? 215.169 204.997 210.817 1.00 18.74 ? 2970 GLU A OE1   1 
ATOM   12038 O  OE2   . GLU A 1 2970 ? 213.627 206.328 211.633 1.00 26.04 ? 2970 GLU A OE2   1 
ATOM   12039 N  N     . ASP A 1 2971 ? 218.393 206.856 212.976 1.00 10.01 ? 2971 ASP A N     1 
ATOM   12040 C  CA    . ASP A 1 2971 ? 219.127 207.465 214.081 1.00 8.49  ? 2971 ASP A CA    1 
ATOM   12041 C  C     . ASP A 1 2971 ? 220.612 207.138 213.996 1.00 4.90  ? 2971 ASP A C     1 
ATOM   12042 O  O     . ASP A 1 2971 ? 221.463 207.994 214.265 1.00 5.63  ? 2971 ASP A O     1 
ATOM   12043 C  CB    . ASP A 1 2971 ? 218.556 207.005 215.422 1.00 7.13  ? 2971 ASP A CB    1 
ATOM   12044 C  CG    . ASP A 1 2971 ? 217.094 207.351 215.580 1.00 14.11 ? 2971 ASP A CG    1 
ATOM   12045 O  OD1   . ASP A 1 2971 ? 216.281 206.898 214.749 1.00 20.29 ? 2971 ASP A OD1   1 
ATOM   12046 O  OD2   . ASP A 1 2971 ? 216.760 208.079 216.538 1.00 19.08 ? 2971 ASP A OD2   1 
ATOM   12047 N  N     . PHE A 1 2972 ? 220.939 205.897 213.634 1.00 3.81  ? 2972 PHE A N     1 
ATOM   12048 C  CA    . PHE A 1 2972 ? 222.337 205.517 213.463 1.00 2.66  ? 2972 PHE A CA    1 
ATOM   12049 C  C     . PHE A 1 2972 ? 222.957 206.229 212.268 1.00 2.95  ? 2972 PHE A C     1 
ATOM   12050 O  O     . PHE A 1 2972 ? 224.131 206.612 212.309 1.00 1.97  ? 2972 PHE A O     1 
ATOM   12051 C  CB    . PHE A 1 2972 ? 222.448 204.000 213.315 1.00 3.15  ? 2972 PHE A CB    1 
ATOM   12052 C  CG    . PHE A 1 2972 ? 223.859 203.489 213.326 1.00 3.16  ? 2972 PHE A CG    1 
ATOM   12053 C  CD1   . PHE A 1 2972 ? 224.647 203.617 214.456 1.00 2.89  ? 2972 PHE A CD1   1 
ATOM   12054 C  CD2   . PHE A 1 2972 ? 224.396 202.870 212.210 1.00 2.47  ? 2972 PHE A CD2   1 
ATOM   12055 C  CE1   . PHE A 1 2972 ? 225.945 203.145 214.470 1.00 2.33  ? 2972 PHE A CE1   1 
ATOM   12056 C  CE2   . PHE A 1 2972 ? 225.690 202.398 212.220 1.00 1.98  ? 2972 PHE A CE2   1 
ATOM   12057 C  CZ    . PHE A 1 2972 ? 226.466 202.536 213.351 1.00 1.83  ? 2972 PHE A CZ    1 
ATOM   12058 N  N     . ASP A 1 2973 ? 222.183 206.412 211.194 1.00 4.80  ? 2973 ASP A N     1 
ATOM   12059 C  CA    . ASP A 1 2973 ? 222.691 207.119 210.024 1.00 3.06  ? 2973 ASP A CA    1 
ATOM   12060 C  C     . ASP A 1 2973 ? 222.987 208.579 210.341 1.00 2.19  ? 2973 ASP A C     1 
ATOM   12061 O  O     . ASP A 1 2973 ? 224.014 209.119 209.913 1.00 1.86  ? 2973 ASP A O     1 
ATOM   12062 C  CB    . ASP A 1 2973 ? 221.693 207.010 208.872 1.00 4.72  ? 2973 ASP A CB    1 
ATOM   12063 C  CG    . ASP A 1 2973 ? 221.830 205.713 208.103 1.00 11.09 ? 2973 ASP A CG    1 
ATOM   12064 O  OD1   . ASP A 1 2973 ? 222.686 204.887 208.478 1.00 16.70 ? 2973 ASP A OD1   1 
ATOM   12065 O  OD2   . ASP A 1 2973 ? 221.083 205.519 207.123 1.00 12.80 ? 2973 ASP A OD2   1 
ATOM   12066 N  N     . GLU A 1 2974 ? 222.096 209.238 211.085 1.00 2.57  ? 2974 GLU A N     1 
ATOM   12067 C  CA    . GLU A 1 2974 ? 222.355 210.613 211.494 1.00 4.55  ? 2974 GLU A CA    1 
ATOM   12068 C  C     . GLU A 1 2974 ? 223.551 210.693 212.430 1.00 5.37  ? 2974 GLU A C     1 
ATOM   12069 O  O     . GLU A 1 2974 ? 224.352 211.632 212.349 1.00 3.23  ? 2974 GLU A O     1 
ATOM   12070 C  CB    . GLU A 1 2974 ? 221.108 211.213 212.144 1.00 4.00  ? 2974 GLU A CB    1 
ATOM   12071 C  CG    . GLU A 1 2974 ? 221.265 212.665 212.569 1.00 10.34 ? 2974 GLU A CG    1 
ATOM   12072 C  CD    . GLU A 1 2974 ? 221.473 213.609 211.396 1.00 20.29 ? 2974 GLU A CD    1 
ATOM   12073 O  OE1   . GLU A 1 2974 ? 221.031 213.286 210.273 1.00 18.86 ? 2974 GLU A OE1   1 
ATOM   12074 O  OE2   . GLU A 1 2974 ? 222.089 214.676 211.599 1.00 22.19 ? 2974 GLU A OE2   1 
ATOM   12075 N  N     . ASP A 1 2975 ? 223.692 209.714 213.328 1.00 3.29  ? 2975 ASP A N     1 
ATOM   12076 C  CA    . ASP A 1 2975 ? 224.868 209.665 214.188 1.00 2.52  ? 2975 ASP A CA    1 
ATOM   12077 C  C     . ASP A 1 2975 ? 226.136 209.442 213.372 1.00 1.89  ? 2975 ASP A C     1 
ATOM   12078 O  O     . ASP A 1 2975 ? 227.182 210.028 213.666 1.00 2.80  ? 2975 ASP A O     1 
ATOM   12079 C  CB    . ASP A 1 2975 ? 224.703 208.572 215.243 1.00 2.75  ? 2975 ASP A CB    1 
ATOM   12080 C  CG    . ASP A 1 2975 ? 223.942 209.052 216.460 1.00 8.35  ? 2975 ASP A CG    1 
ATOM   12081 O  OD1   . ASP A 1 2975 ? 223.776 210.278 216.614 1.00 15.00 ? 2975 ASP A OD1   1 
ATOM   12082 O  OD2   . ASP A 1 2975 ? 223.501 208.203 217.263 1.00 8.17  ? 2975 ASP A OD2   1 
ATOM   12083 N  N     . LEU A 1 2976 ? 226.058 208.597 212.340 1.00 1.69  ? 2976 LEU A N     1 
ATOM   12084 C  CA    . LEU A 1 2976 ? 227.204 208.400 211.456 1.00 1.05  ? 2976 LEU A CA    1 
ATOM   12085 C  C     . LEU A 1 2976 ? 227.574 209.690 210.738 1.00 1.17  ? 2976 LEU A C     1 
ATOM   12086 O  O     . LEU A 1 2976 ? 228.758 210.001 210.577 1.00 1.52  ? 2976 LEU A O     1 
ATOM   12087 C  CB    . LEU A 1 2976 ? 226.909 207.296 210.443 1.00 1.22  ? 2976 LEU A CB    1 
ATOM   12088 C  CG    . LEU A 1 2976 ? 227.046 205.849 210.911 1.00 1.10  ? 2976 LEU A CG    1 
ATOM   12089 C  CD1   . LEU A 1 2976 ? 226.718 204.904 209.768 1.00 2.23  ? 2976 LEU A CD1   1 
ATOM   12090 C  CD2   . LEU A 1 2976 ? 228.438 205.585 211.452 1.00 1.12  ? 2976 LEU A CD2   1 
ATOM   12091 N  N     . ARG A 1 2977 ? 226.572 210.450 210.292 1.00 1.69  ? 2977 ARG A N     1 
ATOM   12092 C  CA    . ARG A 1 2977 ? 226.845 211.716 209.619 1.00 0.85  ? 2977 ARG A CA    1 
ATOM   12093 C  C     . ARG A 1 2977 ? 227.546 212.693 210.551 1.00 1.03  ? 2977 ARG A C     1 
ATOM   12094 O  O     . ARG A 1 2977 ? 228.445 213.427 210.126 1.00 2.03  ? 2977 ARG A O     1 
ATOM   12095 C  CB    . ARG A 1 2977 ? 225.547 212.324 209.088 1.00 1.62  ? 2977 ARG A CB    1 
ATOM   12096 C  CG    . ARG A 1 2977 ? 225.011 211.662 207.836 1.00 1.15  ? 2977 ARG A CG    1 
ATOM   12097 C  CD    . ARG A 1 2977 ? 223.629 212.185 207.482 1.00 2.50  ? 2977 ARG A CD    1 
ATOM   12098 N  NE    . ARG A 1 2977 ? 222.836 211.174 206.796 1.00 4.86  ? 2977 ARG A NE    1 
ATOM   12099 C  CZ    . ARG A 1 2977 ? 221.709 210.660 207.264 1.00 2.25  ? 2977 ARG A CZ    1 
ATOM   12100 N  NH1   . ARG A 1 2977 ? 221.185 211.069 208.407 1.00 1.33  ? 2977 ARG A NH1   1 
ATOM   12101 N  NH2   . ARG A 1 2977 ? 221.090 209.712 206.567 1.00 3.86  ? 2977 ARG A NH2   1 
ATOM   12102 N  N     . THR A 1 2978 ? 227.146 212.720 211.822 1.00 1.23  ? 2978 THR A N     1 
ATOM   12103 C  CA    . THR A 1 2978 ? 227.766 213.631 212.778 1.00 1.54  ? 2978 THR A CA    1 
ATOM   12104 C  C     . THR A 1 2978 ? 229.246 213.316 212.968 1.00 1.39  ? 2978 THR A C     1 
ATOM   12105 O  O     . THR A 1 2978 ? 230.085 214.223 212.971 1.00 1.51  ? 2978 THR A O     1 
ATOM   12106 C  CB    . THR A 1 2978 ? 227.024 213.570 214.113 1.00 1.99  ? 2978 THR A CB    1 
ATOM   12107 O  OG1   . THR A 1 2978 ? 225.702 214.096 213.950 1.00 6.14  ? 2978 THR A OG1   1 
ATOM   12108 C  CG2   . THR A 1 2978 ? 227.754 214.375 215.177 1.00 1.72  ? 2978 THR A CG2   1 
ATOM   12109 N  N     . VAL A 1 2979 ? 229.586 212.034 213.112 1.00 1.00  ? 2979 VAL A N     1 
ATOM   12110 C  CA    . VAL A 1 2979 ? 230.979 211.654 213.324 1.00 0.92  ? 2979 VAL A CA    1 
ATOM   12111 C  C     . VAL A 1 2979 ? 231.803 211.903 212.068 1.00 1.18  ? 2979 VAL A C     1 
ATOM   12112 O  O     . VAL A 1 2979 ? 232.951 212.355 212.142 1.00 2.28  ? 2979 VAL A O     1 
ATOM   12113 C  CB    . VAL A 1 2979 ? 231.073 210.185 213.776 1.00 1.34  ? 2979 VAL A CB    1 
ATOM   12114 C  CG1   . VAL A 1 2979 ? 232.475 209.864 214.257 1.00 1.51  ? 2979 VAL A CG1   1 
ATOM   12115 C  CG2   . VAL A 1 2979 ? 230.074 209.913 214.868 1.00 2.40  ? 2979 VAL A CG2   1 
ATOM   12116 N  N     . LEU A 1 2980 ? 231.238 211.605 210.897 1.00 1.41  ? 2980 LEU A N     1 
ATOM   12117 C  CA    . LEU A 1 2980 ? 231.980 211.787 209.654 1.00 0.77  ? 2980 LEU A CA    1 
ATOM   12118 C  C     . LEU A 1 2980 ? 232.233 213.261 209.365 1.00 0.71  ? 2980 LEU A C     1 
ATOM   12119 O  O     . LEU A 1 2980 ? 233.310 213.623 208.881 1.00 1.55  ? 2980 LEU A O     1 
ATOM   12120 C  CB    . LEU A 1 2980 ? 231.235 211.122 208.498 1.00 1.29  ? 2980 LEU A CB    1 
ATOM   12121 C  CG    . LEU A 1 2980 ? 231.223 209.592 208.530 1.00 0.48  ? 2980 LEU A CG    1 
ATOM   12122 C  CD1   . LEU A 1 2980 ? 230.587 209.032 207.275 1.00 2.31  ? 2980 LEU A CD1   1 
ATOM   12123 C  CD2   . LEU A 1 2980 ? 232.624 209.043 208.709 1.00 0.36  ? 2980 LEU A CD2   1 
ATOM   12124 N  N     . ARG A 1 2981 ? 231.257 214.127 209.648 1.00 1.55  ? 2981 ARG A N     1 
ATOM   12125 C  CA    . ARG A 1 2981 ? 231.468 215.559 209.455 1.00 1.46  ? 2981 ARG A CA    1 
ATOM   12126 C  C     . ARG A 1 2981 ? 232.588 216.075 210.347 1.00 1.56  ? 2981 ARG A C     1 
ATOM   12127 O  O     . ARG A 1 2981 ? 233.424 216.871 209.909 1.00 2.09  ? 2981 ARG A O     1 
ATOM   12128 C  CB    . ARG A 1 2981 ? 230.180 216.334 209.731 1.00 2.02  ? 2981 ARG A CB    1 
ATOM   12129 C  CG    . ARG A 1 2981 ? 229.078 216.141 208.715 1.00 2.35  ? 2981 ARG A CG    1 
ATOM   12130 C  CD    . ARG A 1 2981 ? 227.774 216.736 209.229 1.00 2.83  ? 2981 ARG A CD    1 
ATOM   12131 N  NE    . ARG A 1 2981 ? 226.648 216.532 208.324 1.00 3.16  ? 2981 ARG A NE    1 
ATOM   12132 C  CZ    . ARG A 1 2981 ? 226.521 217.100 207.133 1.00 5.86  ? 2981 ARG A CZ    1 
ATOM   12133 N  NH1   . ARG A 1 2981 ? 227.440 217.923 206.654 1.00 6.48  ? 2981 ARG A NH1   1 
ATOM   12134 N  NH2   . ARG A 1 2981 ? 225.439 216.840 206.403 1.00 4.80  ? 2981 ARG A NH2   1 
ATOM   12135 N  N     . ARG A 1 2982 ? 232.619 215.635 211.605 1.00 1.16  ? 2982 ARG A N     1 
ATOM   12136 C  CA    . ARG A 1 2982 ? 233.643 216.115 212.526 1.00 1.33  ? 2982 ARG A CA    1 
ATOM   12137 C  C     . ARG A 1 2982 ? 235.031 215.632 212.121 1.00 1.66  ? 2982 ARG A C     1 
ATOM   12138 O  O     . ARG A 1 2982 ? 235.995 216.405 212.156 1.00 4.54  ? 2982 ARG A O     1 
ATOM   12139 C  CB    . ARG A 1 2982 ? 233.308 215.678 213.950 1.00 1.76  ? 2982 ARG A CB    1 
ATOM   12140 C  CG    . ARG A 1 2982 ? 232.072 216.340 214.528 1.00 1.43  ? 2982 ARG A CG    1 
ATOM   12141 C  CD    . ARG A 1 2982 ? 231.656 215.683 215.827 1.00 1.65  ? 2982 ARG A CD    1 
ATOM   12142 N  NE    . ARG A 1 2982 ? 232.720 215.726 216.821 1.00 3.40  ? 2982 ARG A NE    1 
ATOM   12143 C  CZ    . ARG A 1 2982 ? 232.661 215.141 218.009 1.00 3.23  ? 2982 ARG A CZ    1 
ATOM   12144 N  NH1   . ARG A 1 2982 ? 231.601 214.448 218.386 1.00 2.15  ? 2982 ARG A NH1   1 
ATOM   12145 N  NH2   . ARG A 1 2982 ? 233.692 215.253 218.839 1.00 3.15  ? 2982 ARG A NH2   1 
ATOM   12146 N  N     . SER A 1 2983 ? 235.155 214.368 211.726 1.00 1.19  ? 2983 SER A N     1 
ATOM   12147 C  CA    . SER A 1 2983 ? 236.453 213.816 211.362 1.00 1.04  ? 2983 SER A CA    1 
ATOM   12148 C  C     . SER A 1 2983 ? 236.817 214.055 209.903 1.00 1.85  ? 2983 SER A C     1 
ATOM   12149 O  O     . SER A 1 2983 ? 238.007 214.044 209.569 1.00 1.63  ? 2983 SER A O     1 
ATOM   12150 C  CB    . SER A 1 2983 ? 236.494 212.313 211.658 1.00 0.77  ? 2983 SER A CB    1 
ATOM   12151 O  OG    . SER A 1 2983 ? 235.830 211.569 210.655 1.00 2.42  ? 2983 SER A OG    1 
ATOM   12152 N  N     . GLY A 1 2984 ? 235.837 214.274 209.033 1.00 1.24  ? 2984 GLY A N     1 
ATOM   12153 C  CA    . GLY A 1 2984 ? 236.120 214.485 207.630 1.00 0.78  ? 2984 GLY A CA    1 
ATOM   12154 C  C     . GLY A 1 2984 ? 236.230 215.941 207.231 1.00 2.04  ? 2984 GLY A C     1 
ATOM   12155 O  O     . GLY A 1 2984 ? 236.965 216.278 206.299 1.00 2.82  ? 2984 GLY A O     1 
ATOM   12156 N  N     . CYS A 1 2985 ? 235.510 216.820 207.925 1.00 2.01  ? 2985 CYS A N     1 
ATOM   12157 C  CA    . CYS A 1 2985 ? 235.489 218.240 207.596 1.00 3.51  ? 2985 CYS A CA    1 
ATOM   12158 C  C     . CYS A 1 2985 ? 236.228 219.108 208.599 1.00 3.62  ? 2985 CYS A C     1 
ATOM   12159 O  O     . CYS A 1 2985 ? 236.899 220.062 208.202 1.00 5.24  ? 2985 CYS A O     1 
ATOM   12160 C  CB    . CYS A 1 2985 ? 234.044 218.735 207.476 1.00 2.14  ? 2985 CYS A CB    1 
ATOM   12161 S  SG    . CYS A 1 2985 ? 233.032 217.823 206.295 1.00 12.57 ? 2985 CYS A SG    1 
ATOM   12162 N  N     . LYS A 1 2986 ? 236.125 218.805 209.891 1.00 2.93  ? 2986 LYS A N     1 
ATOM   12163 C  CA    . LYS A 1 2986 ? 236.734 219.613 210.939 1.00 2.53  ? 2986 LYS A CA    1 
ATOM   12164 C  C     . LYS A 1 2986 ? 238.100 219.097 211.373 1.00 2.60  ? 2986 LYS A C     1 
ATOM   12165 O  O     . LYS A 1 2986 ? 238.696 219.665 212.294 1.00 7.21  ? 2986 LYS A O     1 
ATOM   12166 C  CB    . LYS A 1 2986 ? 235.799 219.697 212.146 1.00 2.16  ? 2986 LYS A CB    1 
ATOM   12167 C  CG    . LYS A 1 2986 ? 234.469 220.360 211.848 1.00 4.39  ? 2986 LYS A CG    1 
ATOM   12168 C  CD    . LYS A 1 2986 ? 234.672 221.834 211.536 1.00 9.22  ? 2986 LYS A CD    1 
ATOM   12169 C  CE    . LYS A 1 2986 ? 233.355 222.548 211.311 1.00 10.89 ? 2986 LYS A CE    1 
ATOM   12170 N  NZ    . LYS A 1 2986 ? 233.576 223.979 210.966 1.00 15.28 ? 2986 LYS A NZ    1 
ATOM   12171 N  N     . ASN A 1 2987 ? 238.605 218.039 210.736 1.00 2.29  ? 2987 ASN A N     1 
ATOM   12172 C  CA    . ASN A 1 2987 ? 239.928 217.487 211.031 1.00 1.55  ? 2987 ASN A CA    1 
ATOM   12173 C  C     . ASN A 1 2987 ? 240.057 217.079 212.499 1.00 1.87  ? 2987 ASN A C     1 
ATOM   12174 O  O     . ASN A 1 2987 ? 241.108 217.248 213.120 1.00 1.95  ? 2987 ASN A O     1 
ATOM   12175 C  CB    . ASN A 1 2987 ? 241.030 218.477 210.642 1.00 1.58  ? 2987 ASN A CB    1 
ATOM   12176 C  CG    . ASN A 1 2987 ? 242.364 217.805 210.421 1.00 2.85  ? 2987 ASN A CG    1 
ATOM   12177 O  OD1   . ASN A 1 2987 ? 242.467 216.832 209.677 1.00 5.37  ? 2987 ASN A OD1   1 
ATOM   12178 N  ND2   . ASN A 1 2987 ? 243.399 218.324 211.066 1.00 1.57  ? 2987 ASN A ND2   1 
ATOM   12179 N  N     . GLU A 1 2988 ? 238.986 216.525 213.054 1.00 1.46  ? 2988 GLU A N     1 
ATOM   12180 C  CA    . GLU A 1 2988 ? 238.939 216.147 214.460 1.00 1.57  ? 2988 GLU A CA    1 
ATOM   12181 C  C     . GLU A 1 2988 ? 239.207 214.654 214.597 1.00 2.26  ? 2988 GLU A C     1 
ATOM   12182 O  O     . GLU A 1 2988 ? 238.474 213.834 214.033 1.00 2.94  ? 2988 GLU A O     1 
ATOM   12183 C  CB    . GLU A 1 2988 ? 237.587 216.509 215.071 1.00 2.11  ? 2988 GLU A CB    1 
ATOM   12184 C  CG    . GLU A 1 2988 ? 237.442 216.107 216.526 1.00 3.39  ? 2988 GLU A CG    1 
ATOM   12185 C  CD    . GLU A 1 2988 ? 236.066 216.407 217.079 1.00 7.99  ? 2988 GLU A CD    1 
ATOM   12186 O  OE1   . GLU A 1 2988 ? 235.209 216.899 216.316 1.00 10.74 ? 2988 GLU A OE1   1 
ATOM   12187 O  OE2   . GLU A 1 2988 ? 235.842 216.150 218.278 1.00 10.20 ? 2988 GLU A OE2   1 
ATOM   12188 N  N     . LYS A 1 2989 ? 240.250 214.305 215.346 1.00 1.95  ? 2989 LYS A N     1 
ATOM   12189 C  CA    . LYS A 1 2989 ? 240.548 212.907 215.627 1.00 1.05  ? 2989 LYS A CA    1 
ATOM   12190 C  C     . LYS A 1 2989 ? 239.517 212.356 216.605 1.00 0.72  ? 2989 LYS A C     1 
ATOM   12191 O  O     . LYS A 1 2989 ? 239.345 212.891 217.704 1.00 1.04  ? 2989 LYS A O     1 
ATOM   12192 C  CB    . LYS A 1 2989 ? 241.960 212.769 216.190 1.00 2.46  ? 2989 LYS A CB    1 
ATOM   12193 C  CG    . LYS A 1 2989 ? 243.054 213.117 215.193 1.00 3.18  ? 2989 LYS A CG    1 
ATOM   12194 C  CD    . LYS A 1 2989 ? 244.438 212.809 215.739 1.00 3.90  ? 2989 LYS A CD    1 
ATOM   12195 C  CE    . LYS A 1 2989 ? 244.861 213.812 216.793 1.00 12.56 ? 2989 LYS A CE    1 
ATOM   12196 N  NZ    . LYS A 1 2989 ? 246.258 213.577 217.247 1.00 24.52 ? 2989 LYS A NZ    1 
ATOM   12197 N  N     . ILE A 1 2990 ? 238.828 211.290 216.206 1.00 1.75  ? 2990 ILE A N     1 
ATOM   12198 C  CA    . ILE A 1 2990 ? 237.683 210.771 216.943 1.00 0.49  ? 2990 ILE A CA    1 
ATOM   12199 C  C     . ILE A 1 2990 ? 237.863 209.276 217.160 1.00 0.47  ? 2990 ILE A C     1 
ATOM   12200 O  O     . ILE A 1 2990 ? 238.177 208.538 216.219 1.00 0.41  ? 2990 ILE A O     1 
ATOM   12201 C  CB    . ILE A 1 2990 ? 236.361 211.051 216.203 1.00 0.62  ? 2990 ILE A CB    1 
ATOM   12202 C  CG1   . ILE A 1 2990 ? 236.040 212.546 216.240 1.00 1.35  ? 2990 ILE A CG1   1 
ATOM   12203 C  CG2   . ILE A 1 2990 ? 235.221 210.239 216.804 1.00 0.57  ? 2990 ILE A CG2   1 
ATOM   12204 C  CD1   . ILE A 1 2990 ? 234.708 212.896 215.641 1.00 1.18  ? 2990 ILE A CD1   1 
ATOM   12205 N  N     . ALA A 1 2991 ? 237.666 208.833 218.399 1.00 0.66  ? 2991 ALA A N     1 
ATOM   12206 C  CA    . ALA A 1 2991 ? 237.582 207.413 218.731 1.00 0.46  ? 2991 ALA A CA    1 
ATOM   12207 C  C     . ALA A 1 2991 ? 236.103 207.055 218.820 1.00 0.71  ? 2991 ALA A C     1 
ATOM   12208 O  O     . ALA A 1 2991 ? 235.438 207.351 219.815 1.00 0.75  ? 2991 ALA A O     1 
ATOM   12209 C  CB    . ALA A 1 2991 ? 238.316 207.103 220.030 1.00 0.26  ? 2991 ALA A CB    1 
ATOM   12210 N  N     . PHE A 1 2992 ? 235.588 206.425 217.769 1.00 0.47  ? 2992 PHE A N     1 
ATOM   12211 C  CA    . PHE A 1 2992 ? 234.187 206.020 217.701 1.00 0.56  ? 2992 PHE A CA    1 
ATOM   12212 C  C     . PHE A 1 2992 ? 234.069 204.659 218.376 1.00 0.98  ? 2992 PHE A C     1 
ATOM   12213 O  O     . PHE A 1 2992 ? 234.280 203.619 217.749 1.00 2.31  ? 2992 PHE A O     1 
ATOM   12214 C  CB    . PHE A 1 2992 ? 233.712 205.997 216.251 1.00 0.87  ? 2992 PHE A CB    1 
ATOM   12215 C  CG    . PHE A 1 2992 ? 232.278 205.583 216.081 1.00 1.14  ? 2992 PHE A CG    1 
ATOM   12216 C  CD1   . PHE A 1 2992 ? 231.355 205.781 217.092 1.00 1.79  ? 2992 PHE A CD1   1 
ATOM   12217 C  CD2   . PHE A 1 2992 ? 231.853 204.999 214.900 1.00 2.15  ? 2992 PHE A CD2   1 
ATOM   12218 C  CE1   . PHE A 1 2992 ? 230.044 205.395 216.934 1.00 6.02  ? 2992 PHE A CE1   1 
ATOM   12219 C  CE2   . PHE A 1 2992 ? 230.539 204.615 214.733 1.00 2.83  ? 2992 PHE A CE2   1 
ATOM   12220 C  CZ    . PHE A 1 2992 ? 229.632 204.813 215.750 1.00 5.61  ? 2992 PHE A CZ    1 
ATOM   12221 N  N     . ILE A 1 2993 ? 233.725 204.668 219.658 1.00 1.21  ? 2993 ILE A N     1 
ATOM   12222 C  CA    . ILE A 1 2993 ? 233.655 203.453 220.460 1.00 0.79  ? 2993 ILE A CA    1 
ATOM   12223 C  C     . ILE A 1 2993 ? 232.219 202.949 220.446 1.00 1.08  ? 2993 ILE A C     1 
ATOM   12224 O  O     . ILE A 1 2993 ? 231.300 203.651 220.878 1.00 2.78  ? 2993 ILE A O     1 
ATOM   12225 C  CB    . ILE A 1 2993 ? 234.139 203.705 221.895 1.00 0.63  ? 2993 ILE A CB    1 
ATOM   12226 C  CG1   . ILE A 1 2993 ? 235.512 204.380 221.873 1.00 0.20  ? 2993 ILE A CG1   1 
ATOM   12227 C  CG2   . ILE A 1 2993 ? 234.181 202.399 222.679 1.00 0.46  ? 2993 ILE A CG2   1 
ATOM   12228 C  CD1   . ILE A 1 2993 ? 236.065 204.691 223.240 1.00 0.23  ? 2993 ILE A CD1   1 
ATOM   12229 N  N     . MET A 1 2994 ? 232.026 201.732 219.949 1.00 1.62  ? 2994 MET A N     1 
ATOM   12230 C  CA    . MET A 1 2994 ? 230.702 201.154 219.795 1.00 3.06  ? 2994 MET A CA    1 
ATOM   12231 C  C     . MET A 1 2994 ? 230.731 199.685 220.191 1.00 1.95  ? 2994 MET A C     1 
ATOM   12232 O  O     . MET A 1 2994 ? 231.601 198.930 219.752 1.00 3.00  ? 2994 MET A O     1 
ATOM   12233 C  CB    . MET A 1 2994 ? 230.202 201.336 218.354 1.00 5.53  ? 2994 MET A CB    1 
ATOM   12234 C  CG    . MET A 1 2994 ? 228.804 200.815 218.090 1.00 15.46 ? 2994 MET A CG    1 
ATOM   12235 S  SD    . MET A 1 2994 ? 228.283 201.104 216.386 1.00 38.27 ? 2994 MET A SD    1 
ATOM   12236 C  CE    . MET A 1 2994 ? 229.289 199.933 215.492 1.00 18.23 ? 2994 MET A CE    1 
ATOM   12237 N  N     . ASP A 1 2995 ? 229.783 199.294 221.035 1.00 3.10  ? 2995 ASP A N     1 
ATOM   12238 C  CA    . ASP A 1 2995 ? 229.689 197.937 221.546 1.00 7.54  ? 2995 ASP A CA    1 
ATOM   12239 C  C     . ASP A 1 2995 ? 228.775 197.086 220.670 1.00 4.79  ? 2995 ASP A C     1 
ATOM   12240 O  O     . ASP A 1 2995 ? 228.021 197.595 219.837 1.00 5.59  ? 2995 ASP A O     1 
ATOM   12241 C  CB    . ASP A 1 2995 ? 229.175 197.939 222.988 1.00 4.47  ? 2995 ASP A CB    1 
ATOM   12242 C  CG    . ASP A 1 2995 ? 229.580 196.697 223.755 1.00 6.70  ? 2995 ASP A CG    1 
ATOM   12243 O  OD1   . ASP A 1 2995 ? 230.714 196.657 224.271 1.00 10.19 ? 2995 ASP A OD1   1 
ATOM   12244 O  OD2   . ASP A 1 2995 ? 228.764 195.755 223.838 1.00 14.33 ? 2995 ASP A OD2   1 
ATOM   12245 N  N     . GLU A 1 2996 ? 228.856 195.770 220.874 1.00 9.20  ? 2996 GLU A N     1 
ATOM   12246 C  CA    . GLU A 1 2996 ? 227.953 194.855 220.182 1.00 10.14 ? 2996 GLU A CA    1 
ATOM   12247 C  C     . GLU A 1 2996 ? 226.503 195.106 220.578 1.00 6.65  ? 2996 GLU A C     1 
ATOM   12248 O  O     . GLU A 1 2996 ? 225.590 194.930 219.765 1.00 5.40  ? 2996 GLU A O     1 
ATOM   12249 C  CB    . GLU A 1 2996 ? 228.348 193.403 220.467 1.00 8.82  ? 2996 GLU A CB    1 
ATOM   12250 C  CG    . GLU A 1 2996 ? 228.190 192.985 221.922 1.00 9.39  ? 2996 GLU A CG    1 
ATOM   12251 C  CD    . GLU A 1 2996 ? 228.642 191.561 222.193 1.00 14.11 ? 2996 GLU A CD    1 
ATOM   12252 O  OE1   . GLU A 1 2996 ? 229.102 190.884 221.251 1.00 14.69 ? 2996 GLU A OE1   1 
ATOM   12253 O  OE2   . GLU A 1 2996 ? 228.546 191.123 223.354 1.00 9.34  ? 2996 GLU A OE2   1 
ATOM   12254 N  N     . SER A 1 2997 ? 226.273 195.521 221.826 1.00 7.48  ? 2997 SER A N     1 
ATOM   12255 C  CA    . SER A 1 2997 ? 224.917 195.817 222.272 1.00 9.61  ? 2997 SER A CA    1 
ATOM   12256 C  C     . SER A 1 2997 ? 224.343 197.024 221.542 1.00 8.91  ? 2997 SER A C     1 
ATOM   12257 O  O     . SER A 1 2997 ? 223.121 197.154 221.405 1.00 13.56 ? 2997 SER A O     1 
ATOM   12258 C  CB    . SER A 1 2997 ? 224.900 196.039 223.784 1.00 10.12 ? 2997 SER A CB    1 
ATOM   12259 O  OG    . SER A 1 2997 ? 225.910 196.951 224.172 1.00 12.39 ? 2997 SER A OG    1 
ATOM   12260 N  N     . ASN A 1 2998 ? 225.208 197.924 221.070 1.00 10.43 ? 2998 ASN A N     1 
ATOM   12261 C  CA    . ASN A 1 2998 ? 224.749 199.062 220.283 1.00 10.80 ? 2998 ASN A CA    1 
ATOM   12262 C  C     . ASN A 1 2998 ? 224.155 198.635 218.947 1.00 10.04 ? 2998 ASN A C     1 
ATOM   12263 O  O     . ASN A 1 2998 ? 223.406 199.406 218.340 1.00 15.54 ? 2998 ASN A O     1 
ATOM   12264 C  CB    . ASN A 1 2998 ? 225.900 200.040 220.042 1.00 7.15  ? 2998 ASN A CB    1 
ATOM   12265 C  CG    . ASN A 1 2998 ? 226.321 200.768 221.296 1.00 8.54  ? 2998 ASN A CG    1 
ATOM   12266 O  OD1   . ASN A 1 2998 ? 225.745 200.575 222.364 1.00 13.14 ? 2998 ASN A OD1   1 
ATOM   12267 N  ND2   . ASN A 1 2998 ? 227.338 201.608 221.175 1.00 10.16 ? 2998 ASN A ND2   1 
ATOM   12268 N  N     . VAL A 1 2999 ? 224.470 197.429 218.481 1.00 7.34  ? 2999 VAL A N     1 
ATOM   12269 C  CA    . VAL A 1 2999 ? 223.953 196.936 217.212 1.00 8.87  ? 2999 VAL A CA    1 
ATOM   12270 C  C     . VAL A 1 2999 ? 222.527 196.447 217.430 1.00 12.87 ? 2999 VAL A C     1 
ATOM   12271 O  O     . VAL A 1 2999 ? 222.300 195.285 217.787 1.00 13.95 ? 2999 VAL A O     1 
ATOM   12272 C  CB    . VAL A 1 2999 ? 224.848 195.819 216.641 1.00 8.10  ? 2999 VAL A CB    1 
ATOM   12273 C  CG1   . VAL A 1 2999 ? 224.253 195.251 215.360 1.00 9.88  ? 2999 VAL A CG1   1 
ATOM   12274 C  CG2   . VAL A 1 2999 ? 226.258 196.337 216.405 1.00 4.93  ? 2999 VAL A CG2   1 
ATOM   12275 N  N     . LEU A 1 3000 ? 221.556 197.339 217.231 1.00 14.90 ? 3000 LEU A N     1 
ATOM   12276 C  CA    . LEU A 1 3000 ? 220.156 196.978 217.399 1.00 13.87 ? 3000 LEU A CA    1 
ATOM   12277 C  C     . LEU A 1 3000 ? 219.555 196.384 216.136 1.00 15.62 ? 3000 LEU A C     1 
ATOM   12278 O  O     . LEU A 1 3000 ? 218.426 195.882 216.177 1.00 18.59 ? 3000 LEU A O     1 
ATOM   12279 C  CB    . LEU A 1 3000 ? 219.345 198.199 217.834 1.00 12.73 ? 3000 LEU A CB    1 
ATOM   12280 C  CG    . LEU A 1 3000 ? 219.938 199.029 218.972 1.00 12.94 ? 3000 LEU A CG    1 
ATOM   12281 C  CD1   . LEU A 1 3000 ? 218.976 200.122 219.399 1.00 10.96 ? 3000 LEU A CD1   1 
ATOM   12282 C  CD2   . LEU A 1 3000 ? 220.284 198.136 220.153 1.00 15.79 ? 3000 LEU A CD2   1 
ATOM   12283 N  N     . ASP A 1 3001 ? 220.283 196.423 215.024 1.00 11.81 ? 3001 ASP A N     1 
ATOM   12284 C  CA    . ASP A 1 3001 ? 219.807 195.899 213.757 1.00 12.60 ? 3001 ASP A CA    1 
ATOM   12285 C  C     . ASP A 1 3001 ? 221.010 195.532 212.901 1.00 15.10 ? 3001 ASP A C     1 
ATOM   12286 O  O     . ASP A 1 3001 ? 222.081 196.131 213.021 1.00 21.20 ? 3001 ASP A O     1 
ATOM   12287 C  CB    . ASP A 1 3001 ? 218.907 196.922 213.038 1.00 15.64 ? 3001 ASP A CB    1 
ATOM   12288 C  CG    . ASP A 1 3001 ? 218.684 196.588 211.576 1.00 21.96 ? 3001 ASP A CG    1 
ATOM   12289 O  OD1   . ASP A 1 3001 ? 218.567 195.390 211.242 1.00 25.55 ? 3001 ASP A OD1   1 
ATOM   12290 O  OD2   . ASP A 1 3001 ? 218.623 197.531 210.759 1.00 24.87 ? 3001 ASP A OD2   1 
ATOM   12291 N  N     . SER A 1 3002 ? 220.819 194.534 212.034 1.00 18.10 ? 3002 SER A N     1 
ATOM   12292 C  CA    . SER A 1 3002 ? 221.890 194.110 211.140 1.00 16.16 ? 3002 SER A CA    1 
ATOM   12293 C  C     . SER A 1 3002 ? 222.311 195.211 210.177 1.00 17.13 ? 3002 SER A C     1 
ATOM   12294 O  O     . SER A 1 3002 ? 223.442 195.187 209.680 1.00 20.17 ? 3002 SER A O     1 
ATOM   12295 C  CB    . SER A 1 3002 ? 221.459 192.872 210.353 1.00 19.14 ? 3002 SER A CB    1 
ATOM   12296 O  OG    . SER A 1 3002 ? 220.375 193.172 209.493 1.00 29.47 ? 3002 SER A OG    1 
ATOM   12297 N  N     . GLY A 1 3003 ? 221.428 196.172 209.898 1.00 11.81 ? 3003 GLY A N     1 
ATOM   12298 C  CA    . GLY A 1 3003 ? 221.782 197.267 209.015 1.00 7.77  ? 3003 GLY A CA    1 
ATOM   12299 C  C     . GLY A 1 3003 ? 222.819 198.204 209.589 1.00 10.48 ? 3003 GLY A C     1 
ATOM   12300 O  O     . GLY A 1 3003 ? 223.456 198.946 208.834 1.00 11.12 ? 3003 GLY A O     1 
ATOM   12301 N  N     . PHE A 1 3004 ? 223.000 198.192 210.912 1.00 10.84 ? 3004 PHE A N     1 
ATOM   12302 C  CA    . PHE A 1 3004 ? 224.037 199.013 211.526 1.00 7.47  ? 3004 PHE A CA    1 
ATOM   12303 C  C     . PHE A 1 3004 ? 225.417 198.606 211.031 1.00 4.35  ? 3004 PHE A C     1 
ATOM   12304 O  O     . PHE A 1 3004 ? 226.238 199.459 210.675 1.00 4.45  ? 3004 PHE A O     1 
ATOM   12305 C  CB    . PHE A 1 3004 ? 223.977 198.893 213.051 1.00 7.34  ? 3004 PHE A CB    1 
ATOM   12306 C  CG    . PHE A 1 3004 ? 222.859 199.670 213.695 1.00 6.24  ? 3004 PHE A CG    1 
ATOM   12307 C  CD1   . PHE A 1 3004 ? 221.643 199.841 213.056 1.00 6.20  ? 3004 PHE A CD1   1 
ATOM   12308 C  CD2   . PHE A 1 3004 ? 223.024 200.210 214.957 1.00 7.09  ? 3004 PHE A CD2   1 
ATOM   12309 C  CE1   . PHE A 1 3004 ? 220.621 200.542 213.656 1.00 5.07  ? 3004 PHE A CE1   1 
ATOM   12310 C  CE2   . PHE A 1 3004 ? 222.004 200.913 215.563 1.00 7.75  ? 3004 PHE A CE2   1 
ATOM   12311 C  CZ    . PHE A 1 3004 ? 220.801 201.079 214.911 1.00 6.76  ? 3004 PHE A CZ    1 
ATOM   12312 N  N     . LEU A 1 3005 ? 225.685 197.301 210.990 1.00 6.70  ? 3005 LEU A N     1 
ATOM   12313 C  CA    . LEU A 1 3005 ? 227.004 196.801 210.630 1.00 5.94  ? 3005 LEU A CA    1 
ATOM   12314 C  C     . LEU A 1 3005 ? 227.273 196.844 209.134 1.00 5.24  ? 3005 LEU A C     1 
ATOM   12315 O  O     . LEU A 1 3005 ? 228.441 196.883 208.733 1.00 8.10  ? 3005 LEU A O     1 
ATOM   12316 C  CB    . LEU A 1 3005 ? 227.179 195.374 211.141 1.00 5.88  ? 3005 LEU A CB    1 
ATOM   12317 C  CG    . LEU A 1 3005 ? 227.264 195.281 212.661 1.00 12.60 ? 3005 LEU A CG    1 
ATOM   12318 C  CD1   . LEU A 1 3005 ? 227.532 193.859 213.068 1.00 12.15 ? 3005 LEU A CD1   1 
ATOM   12319 C  CD2   . LEU A 1 3005 ? 228.344 196.210 213.194 1.00 5.80  ? 3005 LEU A CD2   1 
ATOM   12320 N  N     . GLU A 1 3006 ? 226.231 196.825 208.304 1.00 4.73  ? 3006 GLU A N     1 
ATOM   12321 C  CA    . GLU A 1 3006 ? 226.437 196.998 206.871 1.00 6.72  ? 3006 GLU A CA    1 
ATOM   12322 C  C     . GLU A 1 3006 ? 227.003 198.381 206.574 1.00 5.91  ? 3006 GLU A C     1 
ATOM   12323 O  O     . GLU A 1 3006 ? 227.799 198.548 205.644 1.00 8.03  ? 3006 GLU A O     1 
ATOM   12324 C  CB    . GLU A 1 3006 ? 225.122 196.757 206.127 1.00 8.24  ? 3006 GLU A CB    1 
ATOM   12325 C  CG    . GLU A 1 3006 ? 225.228 196.673 204.611 1.00 6.07  ? 3006 GLU A CG    1 
ATOM   12326 C  CD    . GLU A 1 3006 ? 225.221 198.033 203.938 1.00 24.78 ? 3006 GLU A CD    1 
ATOM   12327 O  OE1   . GLU A 1 3006 ? 224.618 198.972 204.498 1.00 18.48 ? 3006 GLU A OE1   1 
ATOM   12328 O  OE2   . GLU A 1 3006 ? 225.812 198.158 202.846 1.00 26.61 ? 3006 GLU A OE2   1 
ATOM   12329 N  N     . ARG A 1 3007 ? 226.616 199.379 207.370 1.00 4.00  ? 3007 ARG A N     1 
ATOM   12330 C  CA    . ARG A 1 3007 ? 227.210 200.704 207.247 1.00 3.46  ? 3007 ARG A CA    1 
ATOM   12331 C  C     . ARG A 1 3007 ? 228.639 200.722 207.777 1.00 3.59  ? 3007 ARG A C     1 
ATOM   12332 O  O     . ARG A 1 3007 ? 229.529 201.315 207.157 1.00 5.27  ? 3007 ARG A O     1 
ATOM   12333 C  CB    . ARG A 1 3007 ? 226.357 201.733 207.988 1.00 2.81  ? 3007 ARG A CB    1 
ATOM   12334 C  CG    . ARG A 1 3007 ? 224.931 201.860 207.489 1.00 1.85  ? 3007 ARG A CG    1 
ATOM   12335 C  CD    . ARG A 1 3007 ? 224.861 202.733 206.252 1.00 7.31  ? 3007 ARG A CD    1 
ATOM   12336 N  NE    . ARG A 1 3007 ? 223.547 203.341 206.094 1.00 14.00 ? 3007 ARG A NE    1 
ATOM   12337 C  CZ    . ARG A 1 3007 ? 223.192 204.108 205.071 1.00 11.31 ? 3007 ARG A CZ    1 
ATOM   12338 N  NH1   . ARG A 1 3007 ? 224.029 204.372 204.083 1.00 7.42  ? 3007 ARG A NH1   1 
ATOM   12339 N  NH2   . ARG A 1 3007 ? 221.966 204.620 205.040 1.00 16.18 ? 3007 ARG A NH2   1 
ATOM   12340 N  N     . MET A 1 3008 ? 228.876 200.081 208.925 1.00 1.87  ? 3008 MET A N     1 
ATOM   12341 C  CA    . MET A 1 3008 ? 230.218 200.057 209.496 1.00 2.38  ? 3008 MET A CA    1 
ATOM   12342 C  C     . MET A 1 3008 ? 231.177 199.226 208.660 1.00 2.33  ? 3008 MET A C     1 
ATOM   12343 O  O     . MET A 1 3008 ? 232.367 199.547 208.585 1.00 4.47  ? 3008 MET A O     1 
ATOM   12344 C  CB    . MET A 1 3008 ? 230.177 199.534 210.932 1.00 2.68  ? 3008 MET A CB    1 
ATOM   12345 C  CG    . MET A 1 3008 ? 229.179 200.247 211.818 1.00 5.01  ? 3008 MET A CG    1 
ATOM   12346 S  SD    . MET A 1 3008 ? 229.762 201.887 212.288 1.00 22.10 ? 3008 MET A SD    1 
ATOM   12347 C  CE    . MET A 1 3008 ? 231.459 201.531 212.736 1.00 6.55  ? 3008 MET A CE    1 
ATOM   12348 N  N     . ASN A 1 3009 ? 230.683 198.163 208.022 1.00 2.86  ? 3009 ASN A N     1 
ATOM   12349 C  CA    . ASN A 1 3009 ? 231.542 197.348 207.171 1.00 2.15  ? 3009 ASN A CA    1 
ATOM   12350 C  C     . ASN A 1 3009 ? 232.122 198.174 206.030 1.00 1.92  ? 3009 ASN A C     1 
ATOM   12351 O  O     . ASN A 1 3009 ? 233.290 198.007 205.661 1.00 1.97  ? 3009 ASN A O     1 
ATOM   12352 C  CB    . ASN A 1 3009 ? 230.759 196.154 206.627 1.00 2.13  ? 3009 ASN A CB    1 
ATOM   12353 C  CG    . ASN A 1 3009 ? 231.653 195.102 206.015 1.00 3.11  ? 3009 ASN A CG    1 
ATOM   12354 O  OD1   . ASN A 1 3009 ? 232.433 194.454 206.711 1.00 4.27  ? 3009 ASN A OD1   1 
ATOM   12355 N  ND2   . ASN A 1 3009 ? 231.547 194.926 204.705 1.00 1.15  ? 3009 ASN A ND2   1 
ATOM   12356 N  N     . THR A 1 3010 ? 231.318 199.069 205.457 1.00 2.77  ? 3010 THR A N     1 
ATOM   12357 C  CA    . THR A 1 3010 ? 231.826 199.967 204.425 1.00 3.22  ? 3010 THR A CA    1 
ATOM   12358 C  C     . THR A 1 3010 ? 232.741 201.029 205.022 1.00 2.34  ? 3010 THR A C     1 
ATOM   12359 O  O     . THR A 1 3010 ? 233.786 201.352 204.445 1.00 1.68  ? 3010 THR A O     1 
ATOM   12360 C  CB    . THR A 1 3010 ? 230.663 200.619 203.680 1.00 3.99  ? 3010 THR A CB    1 
ATOM   12361 O  OG1   . THR A 1 3010 ? 229.660 199.635 203.407 1.00 11.29 ? 3010 THR A OG1   1 
ATOM   12362 C  CG2   . THR A 1 3010 ? 231.139 201.225 202.373 1.00 2.67  ? 3010 THR A CG2   1 
ATOM   12363 N  N     . LEU A 1 3011 ? 232.364 201.577 206.178 1.00 2.78  ? 3011 LEU A N     1 
ATOM   12364 C  CA    . LEU A 1 3011 ? 233.141 202.650 206.792 1.00 1.54  ? 3011 LEU A CA    1 
ATOM   12365 C  C     . LEU A 1 3011 ? 234.524 202.169 207.215 1.00 1.90  ? 3011 LEU A C     1 
ATOM   12366 O  O     . LEU A 1 3011 ? 235.515 202.887 207.044 1.00 2.03  ? 3011 LEU A O     1 
ATOM   12367 C  CB    . LEU A 1 3011 ? 232.381 203.222 207.987 1.00 1.57  ? 3011 LEU A CB    1 
ATOM   12368 C  CG    . LEU A 1 3011 ? 233.064 204.350 208.763 1.00 1.25  ? 3011 LEU A CG    1 
ATOM   12369 C  CD1   . LEU A 1 3011 ? 233.457 205.484 207.828 1.00 0.98  ? 3011 LEU A CD1   1 
ATOM   12370 C  CD2   . LEU A 1 3011 ? 232.160 204.853 209.871 1.00 0.88  ? 3011 LEU A CD2   1 
ATOM   12371 N  N     . LEU A 1 3012 ? 234.609 200.959 207.775 1.00 1.33  ? 3012 LEU A N     1 
ATOM   12372 C  CA    . LEU A 1 3012 ? 235.892 200.445 208.243 1.00 0.91  ? 3012 LEU A CA    1 
ATOM   12373 C  C     . LEU A 1 3012 ? 236.860 200.231 207.088 1.00 1.37  ? 3012 LEU A C     1 
ATOM   12374 O  O     . LEU A 1 3012 ? 238.065 200.463 207.231 1.00 1.39  ? 3012 LEU A O     1 
ATOM   12375 C  CB    . LEU A 1 3012 ? 235.686 199.140 209.008 1.00 2.15  ? 3012 LEU A CB    1 
ATOM   12376 C  CG    . LEU A 1 3012 ? 234.984 199.207 210.364 1.00 0.94  ? 3012 LEU A CG    1 
ATOM   12377 C  CD1   . LEU A 1 3012 ? 234.537 197.820 210.785 1.00 2.24  ? 3012 LEU A CD1   1 
ATOM   12378 C  CD2   . LEU A 1 3012 ? 235.887 199.827 211.410 1.00 0.25  ? 3012 LEU A CD2   1 
ATOM   12379 N  N     . ALA A 1 3013 ? 236.357 199.783 205.941 1.00 3.23  ? 3013 ALA A N     1 
ATOM   12380 C  CA    . ALA A 1 3013 ? 237.219 199.429 204.821 1.00 2.44  ? 3013 ALA A CA    1 
ATOM   12381 C  C     . ALA A 1 3013 ? 237.554 200.619 203.927 1.00 2.85  ? 3013 ALA A C     1 
ATOM   12382 O  O     . ALA A 1 3013 ? 238.711 200.780 203.528 1.00 6.24  ? 3013 ALA A O     1 
ATOM   12383 C  CB    . ALA A 1 3013 ? 236.564 198.325 203.992 1.00 2.27  ? 3013 ALA A CB    1 
ATOM   12384 N  N     . ASN A 1 3014 ? 236.570 201.457 203.603 1.00 3.71  ? 3014 ASN A N     1 
ATOM   12385 C  CA    . ASN A 1 3014 ? 236.761 202.520 202.629 1.00 5.15  ? 3014 ASN A CA    1 
ATOM   12386 C  C     . ASN A 1 3014 ? 236.772 203.917 203.229 1.00 4.98  ? 3014 ASN A C     1 
ATOM   12387 O  O     . ASN A 1 3014 ? 237.094 204.871 202.513 1.00 6.75  ? 3014 ASN A O     1 
ATOM   12388 C  CB    . ASN A 1 3014 ? 235.672 202.451 201.547 1.00 2.85  ? 3014 ASN A CB    1 
ATOM   12389 C  CG    . ASN A 1 3014 ? 235.582 201.085 200.901 1.00 7.45  ? 3014 ASN A CG    1 
ATOM   12390 O  OD1   . ASN A 1 3014 ? 236.538 200.613 200.287 1.00 8.24  ? 3014 ASN A OD1   1 
ATOM   12391 N  ND2   . ASN A 1 3014 ? 234.429 200.438 201.040 1.00 4.76  ? 3014 ASN A ND2   1 
ATOM   12392 N  N     . GLY A 1 3015 ? 236.432 204.070 204.505 1.00 4.10  ? 3015 GLY A N     1 
ATOM   12393 C  CA    . GLY A 1 3015 ? 236.347 205.396 205.082 1.00 2.08  ? 3015 GLY A CA    1 
ATOM   12394 C  C     . GLY A 1 3015 ? 235.217 206.234 204.540 1.00 2.55  ? 3015 GLY A C     1 
ATOM   12395 O  O     . GLY A 1 3015 ? 235.247 207.459 204.668 1.00 4.85  ? 3015 GLY A O     1 
ATOM   12396 N  N     . GLU A 1 3016 ? 234.217 205.605 203.930 1.00 2.91  ? 3016 GLU A N     1 
ATOM   12397 C  CA    . GLU A 1 3016 ? 233.118 206.320 203.303 1.00 2.78  ? 3016 GLU A CA    1 
ATOM   12398 C  C     . GLU A 1 3016 ? 231.931 205.379 203.191 1.00 3.31  ? 3016 GLU A C     1 
ATOM   12399 O  O     . GLU A 1 3016 ? 232.095 204.159 203.132 1.00 5.45  ? 3016 GLU A O     1 
ATOM   12400 C  CB    . GLU A 1 3016 ? 233.517 206.847 201.919 1.00 5.24  ? 3016 GLU A CB    1 
ATOM   12401 C  CG    . GLU A 1 3016 ? 233.800 205.749 200.912 1.00 8.44  ? 3016 GLU A CG    1 
ATOM   12402 C  CD    . GLU A 1 3016 ? 234.260 206.280 199.572 1.00 15.96 ? 3016 GLU A CD    1 
ATOM   12403 O  OE1   . GLU A 1 3016 ? 234.381 207.514 199.426 1.00 29.21 ? 3016 GLU A OE1   1 
ATOM   12404 O  OE2   . GLU A 1 3016 ? 234.503 205.461 198.663 1.00 19.54 ? 3016 GLU A OE2   1 
ATOM   12405 N  N     . VAL A 1 3017 ? 230.736 205.957 203.179 1.00 3.11  ? 3017 VAL A N     1 
ATOM   12406 C  CA    . VAL A 1 3017 ? 229.495 205.227 202.975 1.00 3.09  ? 3017 VAL A CA    1 
ATOM   12407 C  C     . VAL A 1 3017 ? 228.810 205.837 201.759 1.00 6.82  ? 3017 VAL A C     1 
ATOM   12408 O  O     . VAL A 1 3017 ? 228.383 206.993 201.809 1.00 12.45 ? 3017 VAL A O     1 
ATOM   12409 C  CB    . VAL A 1 3017 ? 228.574 205.280 204.207 1.00 4.87  ? 3017 VAL A CB    1 
ATOM   12410 C  CG1   . VAL A 1 3017 ? 227.354 204.404 203.994 1.00 8.51  ? 3017 VAL A CG1   1 
ATOM   12411 C  CG2   . VAL A 1 3017 ? 229.334 204.858 205.454 1.00 1.22  ? 3017 VAL A CG2   1 
ATOM   12412 N  N     . PRO A 1 3018 ? 228.690 205.106 200.643 1.00 9.88  ? 3018 PRO A N     1 
ATOM   12413 C  CA    . PRO A 1 3018 ? 228.233 205.742 199.393 1.00 8.56  ? 3018 PRO A CA    1 
ATOM   12414 C  C     . PRO A 1 3018 ? 226.879 206.426 199.488 1.00 6.45  ? 3018 PRO A C     1 
ATOM   12415 O  O     . PRO A 1 3018 ? 226.693 207.491 198.890 1.00 8.96  ? 3018 PRO A O     1 
ATOM   12416 C  CB    . PRO A 1 3018 ? 228.205 204.573 198.392 1.00 8.29  ? 3018 PRO A CB    1 
ATOM   12417 C  CG    . PRO A 1 3018 ? 228.356 203.319 199.215 1.00 9.59  ? 3018 PRO A CG    1 
ATOM   12418 C  CD    . PRO A 1 3018 ? 229.104 203.709 200.441 1.00 8.40  ? 3018 PRO A CD    1 
ATOM   12419 N  N     . GLY A 1 3019 ? 225.925 205.854 200.221 1.00 3.39  ? 3019 GLY A N     1 
ATOM   12420 C  CA    . GLY A 1 3019 ? 224.597 206.425 200.312 1.00 6.63  ? 3019 GLY A CA    1 
ATOM   12421 C  C     . GLY A 1 3019 ? 224.257 207.159 201.588 1.00 8.29  ? 3019 GLY A C     1 
ATOM   12422 O  O     . GLY A 1 3019 ? 223.082 207.486 201.798 1.00 11.85 ? 3019 GLY A O     1 
ATOM   12423 N  N     . LEU A 1 3020 ? 225.232 207.438 202.455 1.00 3.44  ? 3020 LEU A N     1 
ATOM   12424 C  CA    . LEU A 1 3020 ? 224.922 208.049 203.744 1.00 3.15  ? 3020 LEU A CA    1 
ATOM   12425 C  C     . LEU A 1 3020 ? 224.510 209.508 203.581 1.00 2.70  ? 3020 LEU A C     1 
ATOM   12426 O  O     . LEU A 1 3020 ? 223.545 209.964 204.205 1.00 3.29  ? 3020 LEU A O     1 
ATOM   12427 C  CB    . LEU A 1 3020 ? 226.121 207.927 204.682 1.00 4.66  ? 3020 LEU A CB    1 
ATOM   12428 C  CG    . LEU A 1 3020 ? 225.859 208.294 206.142 1.00 1.94  ? 3020 LEU A CG    1 
ATOM   12429 C  CD1   . LEU A 1 3020 ? 224.816 207.375 206.753 1.00 2.39  ? 3020 LEU A CD1   1 
ATOM   12430 C  CD2   . LEU A 1 3020 ? 227.142 208.244 206.934 1.00 1.15  ? 3020 LEU A CD2   1 
ATOM   12431 N  N     . PHE A 1 3021 ? 225.226 210.256 202.749 1.00 4.14  ? 3021 PHE A N     1 
ATOM   12432 C  CA    . PHE A 1 3021 ? 224.933 211.663 202.500 1.00 2.37  ? 3021 PHE A CA    1 
ATOM   12433 C  C     . PHE A 1 3021 ? 224.135 211.770 201.206 1.00 3.63  ? 3021 PHE A C     1 
ATOM   12434 O  O     . PHE A 1 3021 ? 224.663 211.507 200.120 1.00 4.33  ? 3021 PHE A O     1 
ATOM   12435 C  CB    . PHE A 1 3021 ? 226.221 212.480 202.420 1.00 1.12  ? 3021 PHE A CB    1 
ATOM   12436 C  CG    . PHE A 1 3021 ? 226.965 212.571 203.721 1.00 1.56  ? 3021 PHE A CG    1 
ATOM   12437 C  CD1   . PHE A 1 3021 ? 226.691 213.589 204.618 1.00 1.24  ? 3021 PHE A CD1   1 
ATOM   12438 C  CD2   . PHE A 1 3021 ? 227.946 211.647 204.040 1.00 1.01  ? 3021 PHE A CD2   1 
ATOM   12439 C  CE1   . PHE A 1 3021 ? 227.376 213.679 205.814 1.00 0.81  ? 3021 PHE A CE1   1 
ATOM   12440 C  CE2   . PHE A 1 3021 ? 228.635 211.732 205.232 1.00 1.04  ? 3021 PHE A CE2   1 
ATOM   12441 C  CZ    . PHE A 1 3021 ? 228.350 212.749 206.120 1.00 0.90  ? 3021 PHE A CZ    1 
ATOM   12442 N  N     . GLU A 1 3022 ? 222.867 212.158 201.318 1.00 4.21  ? 3022 GLU A N     1 
ATOM   12443 C  CA    . GLU A 1 3022 ? 221.994 212.280 200.161 1.00 5.48  ? 3022 GLU A CA    1 
ATOM   12444 C  C     . GLU A 1 3022 ? 221.147 213.537 200.280 1.00 5.43  ? 3022 GLU A C     1 
ATOM   12445 O  O     . GLU A 1 3022 ? 220.829 213.977 201.388 1.00 7.94  ? 3022 GLU A O     1 
ATOM   12446 C  CB    . GLU A 1 3022 ? 221.083 211.056 200.008 1.00 4.39  ? 3022 GLU A CB    1 
ATOM   12447 C  CG    . GLU A 1 3022 ? 221.753 209.857 199.369 1.00 7.22  ? 3022 GLU A CG    1 
ATOM   12448 C  CD    . GLU A 1 3022 ? 220.829 208.662 199.263 1.00 19.34 ? 3022 GLU A CD    1 
ATOM   12449 O  OE1   . GLU A 1 3022 ? 221.313 207.520 199.403 1.00 19.78 ? 3022 GLU A OE1   1 
ATOM   12450 O  OE2   . GLU A 1 3022 ? 219.617 208.863 199.040 1.00 21.30 ? 3022 GLU A OE2   1 
ATOM   12451 N  N     . GLY A 1 3023 ? 220.783 214.101 199.135 1.00 4.63  ? 3023 GLY A N     1 
ATOM   12452 C  CA    . GLY A 1 3023 ? 219.908 215.264 199.134 1.00 2.80  ? 3023 GLY A CA    1 
ATOM   12453 C  C     . GLY A 1 3023 ? 220.580 216.471 199.753 1.00 3.61  ? 3023 GLY A C     1 
ATOM   12454 O  O     . GLY A 1 3023 ? 221.700 216.844 199.389 1.00 6.17  ? 3023 GLY A O     1 
ATOM   12455 N  N     . ASP A 1 3024 ? 219.882 217.101 200.701 1.00 8.16  ? 3024 ASP A N     1 
ATOM   12456 C  CA    . ASP A 1 3024 ? 220.417 218.289 201.356 1.00 4.39  ? 3024 ASP A CA    1 
ATOM   12457 C  C     . ASP A 1 3024 ? 221.629 217.962 202.217 1.00 3.64  ? 3024 ASP A C     1 
ATOM   12458 O  O     . ASP A 1 3024 ? 222.495 218.822 202.412 1.00 5.05  ? 3024 ASP A O     1 
ATOM   12459 C  CB    . ASP A 1 3024 ? 219.333 218.956 202.200 1.00 6.04  ? 3024 ASP A CB    1 
ATOM   12460 C  CG    . ASP A 1 3024 ? 218.297 219.672 201.357 1.00 11.17 ? 3024 ASP A CG    1 
ATOM   12461 O  OD1   . ASP A 1 3024 ? 218.578 219.942 200.172 1.00 20.87 ? 3024 ASP A OD1   1 
ATOM   12462 O  OD2   . ASP A 1 3024 ? 217.200 219.960 201.877 1.00 15.40 ? 3024 ASP A OD2   1 
ATOM   12463 N  N     . GLU A 1 3025 ? 221.706 216.736 202.738 1.00 3.67  ? 3025 GLU A N     1 
ATOM   12464 C  CA    . GLU A 1 3025 ? 222.863 216.344 203.536 1.00 3.97  ? 3025 GLU A CA    1 
ATOM   12465 C  C     . GLU A 1 3025 ? 224.139 216.370 202.705 1.00 4.84  ? 3025 GLU A C     1 
ATOM   12466 O  O     . GLU A 1 3025 ? 225.192 216.806 203.186 1.00 7.58  ? 3025 GLU A O     1 
ATOM   12467 C  CB    . GLU A 1 3025 ? 222.641 214.956 204.137 1.00 3.60  ? 3025 GLU A CB    1 
ATOM   12468 C  CG    . GLU A 1 3025 ? 221.517 214.887 205.160 1.00 4.93  ? 3025 GLU A CG    1 
ATOM   12469 C  CD    . GLU A 1 3025 ? 221.821 215.672 206.420 1.00 15.70 ? 3025 GLU A CD    1 
ATOM   12470 O  OE1   . GLU A 1 3025 ? 223.007 215.765 206.797 1.00 16.10 ? 3025 GLU A OE1   1 
ATOM   12471 O  OE2   . GLU A 1 3025 ? 220.870 216.197 207.036 1.00 22.29 ? 3025 GLU A OE2   1 
ATOM   12472 N  N     . TYR A 1 3026 ? 224.068 215.904 201.456 1.00 2.96  ? 3026 TYR A N     1 
ATOM   12473 C  CA    . TYR A 1 3026 ? 225.237 215.957 200.586 1.00 2.85  ? 3026 TYR A CA    1 
ATOM   12474 C  C     . TYR A 1 3026 ? 225.608 217.393 200.243 1.00 2.96  ? 3026 TYR A C     1 
ATOM   12475 O  O     . TYR A 1 3026 ? 226.794 217.738 200.191 1.00 3.07  ? 3026 TYR A O     1 
ATOM   12476 C  CB    . TYR A 1 3026 ? 224.994 215.147 199.313 1.00 2.99  ? 3026 TYR A CB    1 
ATOM   12477 C  CG    . TYR A 1 3026 ? 226.250 214.914 198.506 1.00 2.66  ? 3026 TYR A CG    1 
ATOM   12478 C  CD1   . TYR A 1 3026 ? 227.127 213.888 198.831 1.00 1.69  ? 3026 TYR A CD1   1 
ATOM   12479 C  CD2   . TYR A 1 3026 ? 226.564 215.724 197.423 1.00 1.36  ? 3026 TYR A CD2   1 
ATOM   12480 C  CE1   . TYR A 1 3026 ? 228.276 213.672 198.100 1.00 3.09  ? 3026 TYR A CE1   1 
ATOM   12481 C  CE2   . TYR A 1 3026 ? 227.710 215.517 196.685 1.00 1.57  ? 3026 TYR A CE2   1 
ATOM   12482 C  CZ    . TYR A 1 3026 ? 228.564 214.489 197.028 1.00 4.42  ? 3026 TYR A CZ    1 
ATOM   12483 O  OH    . TYR A 1 3026 ? 229.707 214.275 196.296 1.00 5.81  ? 3026 TYR A OH    1 
ATOM   12484 N  N     . ALA A 1 3027 ? 224.608 218.241 199.991 1.00 3.29  ? 3027 ALA A N     1 
ATOM   12485 C  CA    . ALA A 1 3027 ? 224.883 219.636 199.670 1.00 3.70  ? 3027 ALA A CA    1 
ATOM   12486 C  C     . ALA A 1 3027 ? 225.545 220.352 200.841 1.00 2.75  ? 3027 ALA A C     1 
ATOM   12487 O  O     . ALA A 1 3027 ? 226.486 221.130 200.651 1.00 2.16  ? 3027 ALA A O     1 
ATOM   12488 C  CB    . ALA A 1 3027 ? 223.593 220.345 199.262 1.00 2.40  ? 3027 ALA A CB    1 
ATOM   12489 N  N     . THR A 1 3028 ? 225.058 220.108 202.060 1.00 3.25  ? 3028 THR A N     1 
ATOM   12490 C  CA    . THR A 1 3028 ? 225.690 220.688 203.240 1.00 4.12  ? 3028 THR A CA    1 
ATOM   12491 C  C     . THR A 1 3028 ? 227.097 220.137 203.432 1.00 5.04  ? 3028 THR A C     1 
ATOM   12492 O  O     . THR A 1 3028 ? 228.017 220.876 203.805 1.00 4.77  ? 3028 THR A O     1 
ATOM   12493 C  CB    . THR A 1 3028 ? 224.828 220.427 204.476 1.00 5.72  ? 3028 THR A CB    1 
ATOM   12494 O  OG1   . THR A 1 3028 ? 223.539 221.022 204.293 1.00 9.59  ? 3028 THR A OG1   1 
ATOM   12495 C  CG2   . THR A 1 3028 ? 225.471 221.015 205.717 1.00 6.72  ? 3028 THR A CG2   1 
ATOM   12496 N  N     . LEU A 1 3029 ? 227.286 218.842 203.172 1.00 2.70  ? 3029 LEU A N     1 
ATOM   12497 C  CA    . LEU A 1 3029 ? 228.610 218.242 203.287 1.00 2.32  ? 3029 LEU A CA    1 
ATOM   12498 C  C     . LEU A 1 3029 ? 229.598 218.889 202.325 1.00 2.93  ? 3029 LEU A C     1 
ATOM   12499 O  O     . LEU A 1 3029 ? 230.751 219.147 202.691 1.00 6.79  ? 3029 LEU A O     1 
ATOM   12500 C  CB    . LEU A 1 3029 ? 228.529 216.737 203.035 1.00 3.57  ? 3029 LEU A CB    1 
ATOM   12501 C  CG    . LEU A 1 3029 ? 229.853 215.971 203.077 1.00 1.93  ? 3029 LEU A CG    1 
ATOM   12502 C  CD1   . LEU A 1 3029 ? 230.445 216.009 204.470 1.00 1.43  ? 3029 LEU A CD1   1 
ATOM   12503 C  CD2   . LEU A 1 3029 ? 229.668 214.537 202.609 1.00 1.12  ? 3029 LEU A CD2   1 
ATOM   12504 N  N     . MET A 1 3030 ? 229.166 219.162 201.093 1.00 3.38  ? 3030 MET A N     1 
ATOM   12505 C  CA    . MET A 1 3030 ? 230.050 219.794 200.122 1.00 2.92  ? 3030 MET A CA    1 
ATOM   12506 C  C     . MET A 1 3030 ? 230.452 221.197 200.555 1.00 3.62  ? 3030 MET A C     1 
ATOM   12507 O  O     . MET A 1 3030 ? 231.601 221.604 200.350 1.00 7.34  ? 3030 MET A O     1 
ATOM   12508 C  CB    . MET A 1 3030 ? 229.386 219.830 198.746 1.00 2.81  ? 3030 MET A CB    1 
ATOM   12509 C  CG    . MET A 1 3030 ? 229.197 218.469 198.075 1.00 3.98  ? 3030 MET A CG    1 
ATOM   12510 S  SD    . MET A 1 3030 ? 230.706 217.613 197.558 1.00 15.31 ? 3030 MET A SD    1 
ATOM   12511 C  CE    . MET A 1 3030 ? 231.220 216.749 199.042 1.00 2.16  ? 3030 MET A CE    1 
ATOM   12512 N  N     . THR A 1 3031 ? 229.524 221.952 201.143 1.00 2.94  ? 3031 THR A N     1 
ATOM   12513 C  CA    . THR A 1 3031 ? 229.861 223.271 201.668 1.00 3.51  ? 3031 THR A CA    1 
ATOM   12514 C  C     . THR A 1 3031 ? 230.889 223.171 202.787 1.00 6.20  ? 3031 THR A C     1 
ATOM   12515 O  O     . THR A 1 3031 ? 231.835 223.963 202.844 1.00 7.51  ? 3031 THR A O     1 
ATOM   12516 C  CB    . THR A 1 3031 ? 228.598 223.975 202.165 1.00 5.53  ? 3031 THR A CB    1 
ATOM   12517 O  OG1   . THR A 1 3031 ? 227.642 224.051 201.102 1.00 5.82  ? 3031 THR A OG1   1 
ATOM   12518 C  CG2   . THR A 1 3031 ? 228.923 225.377 202.653 1.00 4.00  ? 3031 THR A CG2   1 
ATOM   12519 N  N     . GLN A 1 3032 ? 230.719 222.200 203.685 1.00 5.03  ? 3032 GLN A N     1 
ATOM   12520 C  CA    . GLN A 1 3032 ? 231.641 222.055 204.806 1.00 3.62  ? 3032 GLN A CA    1 
ATOM   12521 C  C     . GLN A 1 3032 ? 232.996 221.531 204.346 1.00 5.48  ? 3032 GLN A C     1 
ATOM   12522 O  O     . GLN A 1 3032 ? 234.036 221.931 204.882 1.00 6.07  ? 3032 GLN A O     1 
ATOM   12523 C  CB    . GLN A 1 3032 ? 231.024 221.135 205.858 1.00 5.29  ? 3032 GLN A CB    1 
ATOM   12524 C  CG    . GLN A 1 3032 ? 229.794 221.729 206.514 1.00 4.70  ? 3032 GLN A CG    1 
ATOM   12525 C  CD    . GLN A 1 3032 ? 229.163 220.805 207.535 1.00 7.48  ? 3032 GLN A CD    1 
ATOM   12526 O  OE1   . GLN A 1 3032 ? 229.599 219.671 207.720 1.00 11.01 ? 3032 GLN A OE1   1 
ATOM   12527 N  NE2   . GLN A 1 3032 ? 228.124 221.289 208.200 1.00 12.81 ? 3032 GLN A NE2   1 
ATOM   12528 N  N     . CYS A 1 3033 ? 233.005 220.633 203.359 1.00 6.16  ? 3033 CYS A N     1 
ATOM   12529 C  CA    . CYS A 1 3033 ? 234.269 220.128 202.831 1.00 4.22  ? 3033 CYS A CA    1 
ATOM   12530 C  C     . CYS A 1 3033 ? 235.060 221.230 202.142 1.00 5.17  ? 3033 CYS A C     1 
ATOM   12531 O  O     . CYS A 1 3033 ? 236.288 221.291 202.263 1.00 6.13  ? 3033 CYS A O     1 
ATOM   12532 C  CB    . CYS A 1 3033 ? 234.012 218.966 201.870 1.00 4.37  ? 3033 CYS A CB    1 
ATOM   12533 S  SG    . CYS A 1 3033 ? 233.404 217.469 202.663 1.00 17.02 ? 3033 CYS A SG    1 
ATOM   12534 N  N     . LYS A 1 3034 ? 234.375 222.104 201.400 1.00 5.74  ? 3034 LYS A N     1 
ATOM   12535 C  CA    . LYS A 1 3034 ? 235.057 223.227 200.767 1.00 5.93  ? 3034 LYS A CA    1 
ATOM   12536 C  C     . LYS A 1 3034 ? 235.651 224.162 201.812 1.00 7.33  ? 3034 LYS A C     1 
ATOM   12537 O  O     . LYS A 1 3034 ? 236.783 224.638 201.659 1.00 7.27  ? 3034 LYS A O     1 
ATOM   12538 C  CB    . LYS A 1 3034 ? 234.093 223.978 199.851 1.00 9.36  ? 3034 LYS A CB    1 
ATOM   12539 C  CG    . LYS A 1 3034 ? 234.728 225.130 199.099 1.00 8.39  ? 3034 LYS A CG    1 
ATOM   12540 C  CD    . LYS A 1 3034 ? 233.749 225.763 198.131 1.00 9.94  ? 3034 LYS A CD    1 
ATOM   12541 C  CE    . LYS A 1 3034 ? 234.340 227.006 197.488 1.00 19.05 ? 3034 LYS A CE    1 
ATOM   12542 N  NZ    . LYS A 1 3034 ? 235.497 226.673 196.612 1.00 21.67 ? 3034 LYS A NZ    1 
ATOM   12543 N  N     . GLU A 1 3035 ? 234.903 224.437 202.882 1.00 6.24  ? 3035 GLU A N     1 
ATOM   12544 C  CA    . GLU A 1 3035 ? 235.444 225.221 203.988 1.00 6.59  ? 3035 GLU A CA    1 
ATOM   12545 C  C     . GLU A 1 3035 ? 236.586 224.490 204.682 1.00 8.72  ? 3035 GLU A C     1 
ATOM   12546 O  O     . GLU A 1 3035 ? 237.601 225.103 205.033 1.00 11.20 ? 3035 GLU A O     1 
ATOM   12547 C  CB    . GLU A 1 3035 ? 234.335 225.549 204.989 1.00 5.76  ? 3035 GLU A CB    1 
ATOM   12548 C  CG    . GLU A 1 3035 ? 234.784 226.431 206.142 1.00 10.25 ? 3035 GLU A CG    1 
ATOM   12549 C  CD    . GLU A 1 3035 ? 233.654 226.782 207.088 1.00 24.45 ? 3035 GLU A CD    1 
ATOM   12550 O  OE1   . GLU A 1 3035 ? 232.518 226.319 206.856 1.00 28.48 ? 3035 GLU A OE1   1 
ATOM   12551 O  OE2   . GLU A 1 3035 ? 233.902 227.521 208.062 1.00 27.51 ? 3035 GLU A OE2   1 
ATOM   12552 N  N     . GLY A 1 3036 ? 236.435 223.183 204.898 1.00 7.47  ? 3036 GLY A N     1 
ATOM   12553 C  CA    . GLY A 1 3036 ? 237.471 222.432 205.588 1.00 5.94  ? 3036 GLY A CA    1 
ATOM   12554 C  C     . GLY A 1 3036 ? 238.759 222.331 204.796 1.00 7.19  ? 3036 GLY A C     1 
ATOM   12555 O  O     . GLY A 1 3036 ? 239.852 222.455 205.354 1.00 13.83 ? 3036 GLY A O     1 
ATOM   12556 N  N     . ALA A 1 3037 ? 238.651 222.097 203.488 1.00 5.92  ? 3037 ALA A N     1 
ATOM   12557 C  CA    . ALA A 1 3037 ? 239.845 221.996 202.657 1.00 5.74  ? 3037 ALA A CA    1 
ATOM   12558 C  C     . ALA A 1 3037 ? 240.545 223.342 202.511 1.00 13.48 ? 3037 ALA A C     1 
ATOM   12559 O  O     . ALA A 1 3037 ? 241.770 223.386 202.355 1.00 17.40 ? 3037 ALA A O     1 
ATOM   12560 C  CB    . ALA A 1 3037 ? 239.485 221.428 201.285 1.00 5.90  ? 3037 ALA A CB    1 
ATOM   12561 N  N     . GLN A 1 3038 ? 239.789 224.442 202.553 1.00 14.70 ? 3038 GLN A N     1 
ATOM   12562 C  CA    . GLN A 1 3038 ? 240.398 225.767 202.480 1.00 16.40 ? 3038 GLN A CA    1 
ATOM   12563 C  C     . GLN A 1 3038 ? 241.307 226.026 203.676 1.00 17.77 ? 3038 GLN A C     1 
ATOM   12564 O  O     . GLN A 1 3038 ? 242.398 226.587 203.523 1.00 18.09 ? 3038 GLN A O     1 
ATOM   12565 C  CB    . GLN A 1 3038 ? 239.312 226.839 202.390 1.00 15.46 ? 3038 GLN A CB    1 
ATOM   12566 C  CG    . GLN A 1 3038 ? 239.842 228.251 202.240 1.00 22.91 ? 3038 GLN A CG    1 
ATOM   12567 C  CD    . GLN A 1 3038 ? 240.640 228.444 200.969 1.00 28.61 ? 3038 GLN A CD    1 
ATOM   12568 O  OE1   . GLN A 1 3038 ? 241.868 228.514 200.999 1.00 27.50 ? 3038 GLN A OE1   1 
ATOM   12569 N  NE2   . GLN A 1 3038 ? 239.943 228.530 199.842 1.00 26.02 ? 3038 GLN A NE2   1 
ATOM   12570 N  N     . LYS A 1 3039 ? 240.877 225.618 204.871 1.00 15.60 ? 3039 LYS A N     1 
ATOM   12571 C  CA    . LYS A 1 3039 ? 241.700 225.786 206.062 1.00 14.70 ? 3039 LYS A CA    1 
ATOM   12572 C  C     . LYS A 1 3039 ? 242.985 224.972 205.996 1.00 21.81 ? 3039 LYS A C     1 
ATOM   12573 O  O     . LYS A 1 3039 ? 243.926 225.258 206.746 1.00 24.63 ? 3039 LYS A O     1 
ATOM   12574 C  CB    . LYS A 1 3039 ? 240.899 225.400 207.306 1.00 10.35 ? 3039 LYS A CB    1 
ATOM   12575 C  CG    . LYS A 1 3039 ? 239.901 226.458 207.746 1.00 17.12 ? 3039 LYS A CG    1 
ATOM   12576 C  CD    . LYS A 1 3039 ? 238.862 225.896 208.708 1.00 17.28 ? 3039 LYS A CD    1 
ATOM   12577 C  CE    . LYS A 1 3039 ? 239.485 224.978 209.748 1.00 18.39 ? 3039 LYS A CE    1 
ATOM   12578 N  NZ    . LYS A 1 3039 ? 240.487 225.682 210.595 1.00 20.14 ? 3039 LYS A NZ    1 
ATOM   12579 N  N     . GLU A 1 3040 ? 243.041 223.967 205.127 1.00 21.53 ? 3040 GLU A N     1 
ATOM   12580 C  CA    . GLU A 1 3040 ? 244.228 223.148 204.934 1.00 18.29 ? 3040 GLU A CA    1 
ATOM   12581 C  C     . GLU A 1 3040 ? 245.113 223.663 203.805 1.00 22.70 ? 3040 GLU A C     1 
ATOM   12582 O  O     . GLU A 1 3040 ? 246.205 223.124 203.592 1.00 28.77 ? 3040 GLU A O     1 
ATOM   12583 C  CB    . GLU A 1 3040 ? 243.811 221.697 204.663 1.00 17.58 ? 3040 GLU A CB    1 
ATOM   12584 C  CG    . GLU A 1 3040 ? 244.892 220.656 204.896 1.00 20.10 ? 3040 GLU A CG    1 
ATOM   12585 C  CD    . GLU A 1 3040 ? 244.326 219.251 205.002 1.00 21.45 ? 3040 GLU A CD    1 
ATOM   12586 O  OE1   . GLU A 1 3040 ? 244.548 218.445 204.073 1.00 12.20 ? 3040 GLU A OE1   1 
ATOM   12587 O  OE2   . GLU A 1 3040 ? 243.654 218.958 206.012 1.00 18.60 ? 3040 GLU A OE2   1 
ATOM   12588 N  N     . GLY A 1 3041 ? 244.676 224.695 203.087 1.00 19.72 ? 3041 GLY A N     1 
ATOM   12589 C  CA    . GLY A 1 3041 ? 245.453 225.255 202.003 1.00 18.53 ? 3041 GLY A CA    1 
ATOM   12590 C  C     . GLY A 1 3041 ? 245.327 224.545 200.674 1.00 21.98 ? 3041 GLY A C     1 
ATOM   12591 O  O     . GLY A 1 3041 ? 246.114 224.826 199.765 1.00 29.32 ? 3041 GLY A O     1 
ATOM   12592 N  N     . LEU A 1 3042 ? 244.368 223.636 200.528 1.00 21.94 ? 3042 LEU A N     1 
ATOM   12593 C  CA    . LEU A 1 3042 ? 244.185 222.908 199.281 1.00 23.17 ? 3042 LEU A CA    1 
ATOM   12594 C  C     . LEU A 1 3042 ? 243.221 223.650 198.368 1.00 27.34 ? 3042 LEU A C     1 
ATOM   12595 O  O     . LEU A 1 3042 ? 242.248 224.254 198.828 1.00 27.83 ? 3042 LEU A O     1 
ATOM   12596 C  CB    . LEU A 1 3042 ? 243.671 221.493 199.546 1.00 14.56 ? 3042 LEU A CB    1 
ATOM   12597 C  CG    . LEU A 1 3042 ? 244.417 220.691 200.611 1.00 17.17 ? 3042 LEU A CG    1 
ATOM   12598 C  CD1   . LEU A 1 3042 ? 243.911 219.260 200.641 1.00 23.93 ? 3042 LEU A CD1   1 
ATOM   12599 C  CD2   . LEU A 1 3042 ? 245.914 220.725 200.359 1.00 17.91 ? 3042 LEU A CD2   1 
ATOM   12600 N  N     . MET A 1 3043 ? 243.500 223.601 197.066 1.00 24.05 ? 3043 MET A N     1 
ATOM   12601 C  CA    . MET A 1 3043 ? 242.662 224.252 196.060 1.00 23.20 ? 3043 MET A CA    1 
ATOM   12602 C  C     . MET A 1 3043 ? 241.701 223.211 195.500 1.00 24.34 ? 3043 MET A C     1 
ATOM   12603 O  O     . MET A 1 3043 ? 242.013 222.491 194.553 1.00 28.59 ? 3043 MET A O     1 
ATOM   12604 C  CB    . MET A 1 3043 ? 243.523 224.874 194.970 1.00 25.87 ? 3043 MET A CB    1 
ATOM   12605 C  CG    . MET A 1 3043 ? 244.382 226.034 195.447 1.00 28.08 ? 3043 MET A CG    1 
ATOM   12606 S  SD    . MET A 1 3043 ? 245.338 226.789 194.119 1.00 57.69 ? 3043 MET A SD    1 
ATOM   12607 C  CE    . MET A 1 3043 ? 246.601 225.546 193.866 1.00 32.14 ? 3043 MET A CE    1 
ATOM   12608 N  N     . LEU A 1 3044 ? 240.513 223.131 196.095 1.00 18.45 ? 3044 LEU A N     1 
ATOM   12609 C  CA    . LEU A 1 3044 ? 239.502 222.161 195.694 1.00 14.78 ? 3044 LEU A CA    1 
ATOM   12610 C  C     . LEU A 1 3044 ? 238.165 222.864 195.507 1.00 15.77 ? 3044 LEU A C     1 
ATOM   12611 O  O     . LEU A 1 3044 ? 237.723 223.608 196.387 1.00 13.46 ? 3044 LEU A O     1 
ATOM   12612 C  CB    . LEU A 1 3044 ? 239.364 221.043 196.729 1.00 12.26 ? 3044 LEU A CB    1 
ATOM   12613 C  CG    . LEU A 1 3044 ? 240.584 220.149 196.946 1.00 13.32 ? 3044 LEU A CG    1 
ATOM   12614 C  CD1   . LEU A 1 3044 ? 240.311 219.141 198.048 1.00 11.04 ? 3044 LEU A CD1   1 
ATOM   12615 C  CD2   . LEU A 1 3044 ? 240.976 219.446 195.659 1.00 10.54 ? 3044 LEU A CD2   1 
ATOM   12616 N  N     . ASP A 1 3045 ? 237.529 222.626 194.362 1.00 19.20 ? 3045 ASP A N     1 
ATOM   12617 C  CA    . ASP A 1 3045 ? 236.217 223.197 194.088 1.00 20.49 ? 3045 ASP A CA    1 
ATOM   12618 C  C     . ASP A 1 3045 ? 235.258 222.134 193.567 1.00 17.37 ? 3045 ASP A C     1 
ATOM   12619 O  O     . ASP A 1 3045 ? 234.042 222.238 193.761 1.00 23.35 ? 3045 ASP A O     1 
ATOM   12620 C  CB    . ASP A 1 3045 ? 236.334 224.344 193.082 1.00 25.38 ? 3045 ASP A CB    1 
ATOM   12621 C  CG    . ASP A 1 3045 ? 235.002 225.009 192.801 1.00 33.09 ? 3045 ASP A CG    1 
ATOM   12622 O  OD1   . ASP A 1 3045 ? 234.399 225.555 193.747 1.00 23.80 ? 3045 ASP A OD1   1 
ATOM   12623 O  OD2   . ASP A 1 3045 ? 234.558 224.979 191.634 1.00 36.01 ? 3045 ASP A OD2   1 
ATOM   12624 N  N     . SER A 1 3046 ? 235.796 221.109 192.910 1.00 14.58 ? 3046 SER A N     1 
ATOM   12625 C  CA    . SER A 1 3046 ? 234.967 220.037 192.378 1.00 7.63  ? 3046 SER A CA    1 
ATOM   12626 C  C     . SER A 1 3046 ? 234.374 219.204 193.507 1.00 10.95 ? 3046 SER A C     1 
ATOM   12627 O  O     . SER A 1 3046 ? 235.036 218.926 194.508 1.00 13.78 ? 3046 SER A O     1 
ATOM   12628 C  CB    . SER A 1 3046 ? 235.789 219.150 191.444 1.00 8.85  ? 3046 SER A CB    1 
ATOM   12629 O  OG    . SER A 1 3046 ? 235.109 217.943 191.152 1.00 13.00 ? 3046 SER A OG    1 
ATOM   12630 N  N     . HIS A 1 3047 ? 233.111 218.806 193.339 1.00 11.77 ? 3047 HIS A N     1 
ATOM   12631 C  CA    . HIS A 1 3047 ? 232.461 217.970 194.344 1.00 7.48  ? 3047 HIS A CA    1 
ATOM   12632 C  C     . HIS A 1 3047 ? 233.159 216.622 194.477 1.00 8.45  ? 3047 HIS A C     1 
ATOM   12633 O  O     . HIS A 1 3047 ? 233.332 216.112 195.589 1.00 13.17 ? 3047 HIS A O     1 
ATOM   12634 C  CB    . HIS A 1 3047 ? 230.986 217.777 194.001 1.00 4.57  ? 3047 HIS A CB    1 
ATOM   12635 C  CG    . HIS A 1 3047 ? 230.115 218.920 194.418 1.00 10.36 ? 3047 HIS A CG    1 
ATOM   12636 N  ND1   . HIS A 1 3047 ? 228.739 218.856 194.383 1.00 10.48 ? 3047 HIS A ND1   1 
ATOM   12637 C  CD2   . HIS A 1 3047 ? 230.423 220.157 194.874 1.00 10.91 ? 3047 HIS A CD2   1 
ATOM   12638 C  CE1   . HIS A 1 3047 ? 228.237 220.004 194.803 1.00 9.99  ? 3047 HIS A CE1   1 
ATOM   12639 N  NE2   . HIS A 1 3047 ? 229.238 220.811 195.107 1.00 10.21 ? 3047 HIS A NE2   1 
ATOM   12640 N  N     . GLU A 1 3048 ? 233.555 216.026 193.350 1.00 10.08 ? 3048 GLU A N     1 
ATOM   12641 C  CA    . GLU A 1 3048 ? 234.283 214.763 193.397 1.00 5.58  ? 3048 GLU A CA    1 
ATOM   12642 C  C     . GLU A 1 3048 ? 235.619 214.928 194.108 1.00 6.52  ? 3048 GLU A C     1 
ATOM   12643 O  O     . GLU A 1 3048 ? 236.008 214.081 194.921 1.00 7.01  ? 3048 GLU A O     1 
ATOM   12644 C  CB    . GLU A 1 3048 ? 234.490 214.219 191.982 1.00 6.41  ? 3048 GLU A CB    1 
ATOM   12645 C  CG    . GLU A 1 3048 ? 233.248 213.633 191.318 1.00 14.98 ? 3048 GLU A CG    1 
ATOM   12646 C  CD    . GLU A 1 3048 ? 232.126 214.641 191.130 1.00 19.88 ? 3048 GLU A CD    1 
ATOM   12647 O  OE1   . GLU A 1 3048 ? 232.266 215.545 190.281 1.00 19.68 ? 3048 GLU A OE1   1 
ATOM   12648 O  OE2   . GLU A 1 3048 ? 231.098 214.519 191.831 1.00 15.38 ? 3048 GLU A OE2   1 
ATOM   12649 N  N     . GLU A 1 3049 ? 236.336 216.014 193.812 1.00 7.57  ? 3049 GLU A N     1 
ATOM   12650 C  CA    . GLU A 1 3049 ? 237.595 216.281 194.498 1.00 5.57  ? 3049 GLU A CA    1 
ATOM   12651 C  C     . GLU A 1 3049 ? 237.374 216.533 195.983 1.00 6.09  ? 3049 GLU A C     1 
ATOM   12652 O  O     . GLU A 1 3049 ? 238.176 216.101 196.819 1.00 7.23  ? 3049 GLU A O     1 
ATOM   12653 C  CB    . GLU A 1 3049 ? 238.300 217.472 193.853 1.00 7.38  ? 3049 GLU A CB    1 
ATOM   12654 C  CG    . GLU A 1 3049 ? 239.216 217.101 192.708 1.00 10.88 ? 3049 GLU A CG    1 
ATOM   12655 C  CD    . GLU A 1 3049 ? 239.581 218.295 191.852 1.00 21.87 ? 3049 GLU A CD    1 
ATOM   12656 O  OE1   . GLU A 1 3049 ? 239.400 218.223 190.618 1.00 22.15 ? 3049 GLU A OE1   1 
ATOM   12657 O  OE2   . GLU A 1 3049 ? 240.050 219.306 192.417 1.00 23.07 ? 3049 GLU A OE2   1 
ATOM   12658 N  N     . LEU A 1 3050 ? 236.296 217.240 196.328 1.00 7.10  ? 3050 LEU A N     1 
ATOM   12659 C  CA    . LEU A 1 3050 ? 235.981 217.476 197.732 1.00 4.02  ? 3050 LEU A CA    1 
ATOM   12660 C  C     . LEU A 1 3050 ? 235.660 216.176 198.456 1.00 2.64  ? 3050 LEU A C     1 
ATOM   12661 O  O     . LEU A 1 3050 ? 236.072 215.979 199.604 1.00 3.51  ? 3050 LEU A O     1 
ATOM   12662 C  CB    . LEU A 1 3050 ? 234.816 218.458 197.852 1.00 6.02  ? 3050 LEU A CB    1 
ATOM   12663 C  CG    . LEU A 1 3050 ? 235.124 219.929 197.577 1.00 9.19  ? 3050 LEU A CG    1 
ATOM   12664 C  CD1   . LEU A 1 3050 ? 233.854 220.756 197.651 1.00 8.33  ? 3050 LEU A CD1   1 
ATOM   12665 C  CD2   . LEU A 1 3050 ? 236.166 220.453 198.546 1.00 7.14  ? 3050 LEU A CD2   1 
ATOM   12666 N  N     . TYR A 1 3051 ? 234.923 215.277 197.801 1.00 2.77  ? 3051 TYR A N     1 
ATOM   12667 C  CA    . TYR A 1 3051 ? 234.535 214.028 198.449 1.00 1.46  ? 3051 TYR A CA    1 
ATOM   12668 C  C     . TYR A 1 3051 ? 235.738 213.116 198.668 1.00 2.46  ? 3051 TYR A C     1 
ATOM   12669 O  O     . TYR A 1 3051 ? 235.808 212.413 199.682 1.00 2.71  ? 3051 TYR A O     1 
ATOM   12670 C  CB    . TYR A 1 3051 ? 233.458 213.322 197.626 1.00 1.34  ? 3051 TYR A CB    1 
ATOM   12671 C  CG    . TYR A 1 3051 ? 232.747 212.224 198.383 1.00 3.02  ? 3051 TYR A CG    1 
ATOM   12672 C  CD1   . TYR A 1 3051 ? 231.695 212.515 199.239 1.00 3.33  ? 3051 TYR A CD1   1 
ATOM   12673 C  CD2   . TYR A 1 3051 ? 233.133 210.897 198.246 1.00 4.53  ? 3051 TYR A CD2   1 
ATOM   12674 C  CE1   . TYR A 1 3051 ? 231.046 211.517 199.940 1.00 3.53  ? 3051 TYR A CE1   1 
ATOM   12675 C  CE2   . TYR A 1 3051 ? 232.489 209.893 198.940 1.00 3.98  ? 3051 TYR A CE2   1 
ATOM   12676 C  CZ    . TYR A 1 3051 ? 231.448 210.208 199.784 1.00 5.03  ? 3051 TYR A CZ    1 
ATOM   12677 O  OH    . TYR A 1 3051 ? 230.805 209.208 200.475 1.00 11.76 ? 3051 TYR A OH    1 
ATOM   12678 N  N     . LYS A 1 3052 ? 236.685 213.102 197.727 1.00 2.85  ? 3052 LYS A N     1 
ATOM   12679 C  CA    . LYS A 1 3052 ? 237.901 212.315 197.921 1.00 1.60  ? 3052 LYS A CA    1 
ATOM   12680 C  C     . LYS A 1 3052 ? 238.721 212.841 199.093 1.00 1.85  ? 3052 LYS A C     1 
ATOM   12681 O  O     . LYS A 1 3052 ? 239.254 212.057 199.887 1.00 2.35  ? 3052 LYS A O     1 
ATOM   12682 C  CB    . LYS A 1 3052 ? 238.742 212.305 196.646 1.00 3.43  ? 3052 LYS A CB    1 
ATOM   12683 C  CG    . LYS A 1 3052 ? 238.104 211.586 195.474 1.00 3.81  ? 3052 LYS A CG    1 
ATOM   12684 C  CD    . LYS A 1 3052 ? 239.009 211.611 194.255 1.00 6.27  ? 3052 LYS A CD    1 
ATOM   12685 C  CE    . LYS A 1 3052 ? 238.417 210.814 193.105 1.00 15.88 ? 3052 LYS A CE    1 
ATOM   12686 N  NZ    . LYS A 1 3052 ? 237.175 211.434 192.569 1.00 19.39 ? 3052 LYS A NZ    1 
ATOM   12687 N  N     . TRP A 1 3053 ? 238.844 214.164 199.210 1.00 1.97  ? 3053 TRP A N     1 
ATOM   12688 C  CA    . TRP A 1 3053 ? 239.552 214.741 200.349 1.00 0.93  ? 3053 TRP A CA    1 
ATOM   12689 C  C     . TRP A 1 3053 ? 238.829 214.432 201.651 1.00 1.28  ? 3053 TRP A C     1 
ATOM   12690 O  O     . TRP A 1 3053 ? 239.465 214.152 202.673 1.00 1.13  ? 3053 TRP A O     1 
ATOM   12691 C  CB    . TRP A 1 3053 ? 239.703 216.250 200.161 1.00 0.94  ? 3053 TRP A CB    1 
ATOM   12692 C  CG    . TRP A 1 3053 ? 240.184 216.964 201.385 1.00 1.43  ? 3053 TRP A CG    1 
ATOM   12693 C  CD1   . TRP A 1 3053 ? 241.476 217.149 201.767 1.00 1.27  ? 3053 TRP A CD1   1 
ATOM   12694 C  CD2   . TRP A 1 3053 ? 239.375 217.585 202.392 1.00 1.37  ? 3053 TRP A CD2   1 
ATOM   12695 N  NE1   . TRP A 1 3053 ? 241.527 217.848 202.945 1.00 2.93  ? 3053 TRP A NE1   1 
ATOM   12696 C  CE2   . TRP A 1 3053 ? 240.249 218.128 203.352 1.00 1.74  ? 3053 TRP A CE2   1 
ATOM   12697 C  CE3   . TRP A 1 3053 ? 237.998 217.733 202.574 1.00 1.34  ? 3053 TRP A CE3   1 
ATOM   12698 C  CZ2   . TRP A 1 3053 ? 239.793 218.808 204.476 1.00 1.70  ? 3053 TRP A CZ2   1 
ATOM   12699 C  CZ3   . TRP A 1 3053 ? 237.547 218.407 203.690 1.00 2.37  ? 3053 TRP A CZ3   1 
ATOM   12700 C  CH2   . TRP A 1 3053 ? 238.441 218.936 204.627 1.00 2.62  ? 3053 TRP A CH2   1 
ATOM   12701 N  N     . PHE A 1 3054 ? 237.497 214.480 201.628 1.00 0.90  ? 3054 PHE A N     1 
ATOM   12702 C  CA    . PHE A 1 3054 ? 236.704 214.137 202.805 1.00 0.88  ? 3054 PHE A CA    1 
ATOM   12703 C  C     . PHE A 1 3054 ? 236.913 212.682 203.208 1.00 0.79  ? 3054 PHE A C     1 
ATOM   12704 O  O     . PHE A 1 3054 ? 237.004 212.368 204.401 1.00 0.85  ? 3054 PHE A O     1 
ATOM   12705 C  CB    . PHE A 1 3054 ? 235.231 214.434 202.520 1.00 0.57  ? 3054 PHE A CB    1 
ATOM   12706 C  CG    . PHE A 1 3054 ? 234.277 213.868 203.528 1.00 0.38  ? 3054 PHE A CG    1 
ATOM   12707 C  CD1   . PHE A 1 3054 ? 234.060 214.509 204.734 1.00 0.75  ? 3054 PHE A CD1   1 
ATOM   12708 C  CD2   . PHE A 1 3054 ? 233.552 212.723 203.244 1.00 0.65  ? 3054 PHE A CD2   1 
ATOM   12709 C  CE1   . PHE A 1 3054 ? 233.169 213.998 205.653 1.00 0.40  ? 3054 PHE A CE1   1 
ATOM   12710 C  CE2   . PHE A 1 3054 ? 232.655 212.210 204.160 1.00 0.54  ? 3054 PHE A CE2   1 
ATOM   12711 C  CZ    . PHE A 1 3054 ? 232.464 212.849 205.366 1.00 0.39  ? 3054 PHE A CZ    1 
ATOM   12712 N  N     . THR A 1 3055 ? 236.991 211.781 202.231 1.00 0.69  ? 3055 THR A N     1 
ATOM   12713 C  CA    . THR A 1 3055 ? 237.281 210.382 202.529 1.00 0.96  ? 3055 THR A CA    1 
ATOM   12714 C  C     . THR A 1 3055 ? 238.676 210.223 203.120 1.00 0.79  ? 3055 THR A C     1 
ATOM   12715 O  O     . THR A 1 3055 ? 238.875 209.454 204.067 1.00 0.80  ? 3055 THR A O     1 
ATOM   12716 C  CB    . THR A 1 3055 ? 237.136 209.536 201.263 1.00 1.78  ? 3055 THR A CB    1 
ATOM   12717 O  OG1   . THR A 1 3055 ? 235.815 209.697 200.732 1.00 4.51  ? 3055 THR A OG1   1 
ATOM   12718 C  CG2   . THR A 1 3055 ? 237.378 208.068 201.566 1.00 1.59  ? 3055 THR A CG2   1 
ATOM   12719 N  N     . SER A 1 3056 ? 239.656 210.945 202.574 1.00 0.78  ? 3056 SER A N     1 
ATOM   12720 C  CA    . SER A 1 3056 ? 241.022 210.838 203.074 1.00 0.90  ? 3056 SER A CA    1 
ATOM   12721 C  C     . SER A 1 3056 ? 241.133 211.360 204.501 1.00 0.69  ? 3056 SER A C     1 
ATOM   12722 O  O     . SER A 1 3056 ? 241.955 210.873 205.286 1.00 0.62  ? 3056 SER A O     1 
ATOM   12723 C  CB    . SER A 1 3056 ? 241.979 211.586 202.143 1.00 0.93  ? 3056 SER A CB    1 
ATOM   12724 O  OG    . SER A 1 3056 ? 241.709 212.975 202.133 1.00 1.62  ? 3056 SER A OG    1 
ATOM   12725 N  N     . GLN A 1 3057 ? 240.322 212.360 204.852 1.00 0.75  ? 3057 GLN A N     1 
ATOM   12726 C  CA    . GLN A 1 3057 ? 240.317 212.859 206.225 1.00 0.68  ? 3057 GLN A CA    1 
ATOM   12727 C  C     . GLN A 1 3057 ? 239.695 211.850 207.180 1.00 0.62  ? 3057 GLN A C     1 
ATOM   12728 O  O     . GLN A 1 3057 ? 240.201 211.648 208.289 1.00 1.32  ? 3057 GLN A O     1 
ATOM   12729 C  CB    . GLN A 1 3057 ? 239.576 214.194 206.293 1.00 1.18  ? 3057 GLN A CB    1 
ATOM   12730 C  CG    . GLN A 1 3057 ? 240.262 215.323 205.542 1.00 0.82  ? 3057 GLN A CG    1 
ATOM   12731 C  CD    . GLN A 1 3057 ? 241.454 215.883 206.290 1.00 2.03  ? 3057 GLN A CD    1 
ATOM   12732 O  OE1   . GLN A 1 3057 ? 242.582 215.828 205.809 1.00 3.27  ? 3057 GLN A OE1   1 
ATOM   12733 N  NE2   . GLN A 1 3057 ? 241.206 216.436 207.468 1.00 3.18  ? 3057 GLN A NE2   1 
ATOM   12734 N  N     . VAL A 1 3058 ? 238.600 211.208 206.768 1.00 0.43  ? 3058 VAL A N     1 
ATOM   12735 C  CA    . VAL A 1 3058 ? 237.975 210.183 207.601 1.00 0.39  ? 3058 VAL A CA    1 
ATOM   12736 C  C     . VAL A 1 3058 ? 238.930 209.017 207.808 1.00 0.65  ? 3058 VAL A C     1 
ATOM   12737 O  O     . VAL A 1 3058 ? 238.993 208.428 208.895 1.00 0.81  ? 3058 VAL A O     1 
ATOM   12738 C  CB    . VAL A 1 3058 ? 236.643 209.726 206.974 1.00 0.41  ? 3058 VAL A CB    1 
ATOM   12739 C  CG1   . VAL A 1 3058 ? 236.113 208.484 207.679 1.00 0.31  ? 3058 VAL A CG1   1 
ATOM   12740 C  CG2   . VAL A 1 3058 ? 235.621 210.846 207.020 1.00 0.53  ? 3058 VAL A CG2   1 
ATOM   12741 N  N     . ILE A 1 3059 ? 239.700 208.677 206.773 1.00 0.59  ? 3059 ILE A N     1 
ATOM   12742 C  CA    . ILE A 1 3059 ? 240.646 207.569 206.866 1.00 0.77  ? 3059 ILE A CA    1 
ATOM   12743 C  C     . ILE A 1 3059 ? 241.697 207.845 207.934 1.00 0.84  ? 3059 ILE A C     1 
ATOM   12744 O  O     . ILE A 1 3059 ? 242.043 206.962 208.727 1.00 1.12  ? 3059 ILE A O     1 
ATOM   12745 C  CB    . ILE A 1 3059 ? 241.282 207.304 205.488 1.00 1.05  ? 3059 ILE A CB    1 
ATOM   12746 C  CG1   . ILE A 1 3059 ? 240.314 206.512 204.605 1.00 0.93  ? 3059 ILE A CG1   1 
ATOM   12747 C  CG2   . ILE A 1 3059 ? 242.619 206.595 205.623 1.00 1.45  ? 3059 ILE A CG2   1 
ATOM   12748 C  CD1   . ILE A 1 3059 ? 240.881 206.132 203.265 1.00 1.11  ? 3059 ILE A CD1   1 
ATOM   12749 N  N     . ARG A 1 3060 ? 242.207 209.073 207.988 1.00 0.86  ? 3060 ARG A N     1 
ATOM   12750 C  CA    . ARG A 1 3060 ? 243.284 209.399 208.912 1.00 1.23  ? 3060 ARG A CA    1 
ATOM   12751 C  C     . ARG A 1 3060 ? 242.803 209.804 210.301 1.00 1.00  ? 3060 ARG A C     1 
ATOM   12752 O  O     . ARG A 1 3060 ? 243.577 209.694 211.258 1.00 1.74  ? 3060 ARG A O     1 
ATOM   12753 C  CB    . ARG A 1 3060 ? 244.156 210.515 208.329 1.00 0.83  ? 3060 ARG A CB    1 
ATOM   12754 C  CG    . ARG A 1 3060 ? 243.437 211.834 208.139 1.00 2.13  ? 3060 ARG A CG    1 
ATOM   12755 C  CD    . ARG A 1 3060 ? 244.327 212.855 207.447 1.00 4.91  ? 3060 ARG A CD    1 
ATOM   12756 N  NE    . ARG A 1 3060 ? 245.522 213.155 208.224 1.00 3.97  ? 3060 ARG A NE    1 
ATOM   12757 C  CZ    . ARG A 1 3060 ? 245.597 214.113 209.138 1.00 4.70  ? 3060 ARG A CZ    1 
ATOM   12758 N  NH1   . ARG A 1 3060 ? 244.562 214.888 209.413 1.00 3.42  ? 3060 ARG A NH1   1 
ATOM   12759 N  NH2   . ARG A 1 3060 ? 246.740 214.296 209.793 1.00 8.50  ? 3060 ARG A NH2   1 
ATOM   12760 N  N     . ASN A 1 3061 ? 241.557 210.252 210.447 1.00 0.66  ? 3061 ASN A N     1 
ATOM   12761 C  CA    . ASN A 1 3061 ? 241.088 210.787 211.719 1.00 0.61  ? 3061 ASN A CA    1 
ATOM   12762 C  C     . ASN A 1 3061 ? 240.108 209.893 212.460 1.00 0.60  ? 3061 ASN A C     1 
ATOM   12763 O  O     . ASN A 1 3061 ? 240.124 209.879 213.692 1.00 1.08  ? 3061 ASN A O     1 
ATOM   12764 C  CB    . ASN A 1 3061 ? 240.434 212.159 211.517 1.00 0.93  ? 3061 ASN A CB    1 
ATOM   12765 C  CG    . ASN A 1 3061 ? 241.437 213.235 211.168 1.00 1.36  ? 3061 ASN A CG    1 
ATOM   12766 O  OD1   . ASN A 1 3061 ? 242.516 213.302 211.749 1.00 5.55  ? 3061 ASN A OD1   1 
ATOM   12767 N  ND2   . ASN A 1 3061 ? 241.076 214.098 210.230 1.00 1.18  ? 3061 ASN A ND2   1 
ATOM   12768 N  N     . LEU A 1 3062 ? 239.258 209.153 211.757 1.00 0.35  ? 3062 LEU A N     1 
ATOM   12769 C  CA    . LEU A 1 3062 ? 238.226 208.366 212.419 1.00 0.19  ? 3062 LEU A CA    1 
ATOM   12770 C  C     . LEU A 1 3062 ? 238.797 207.024 212.860 1.00 0.09  ? 3062 LEU A C     1 
ATOM   12771 O  O     . LEU A 1 3062 ? 239.329 206.266 212.044 1.00 0.43  ? 3062 LEU A O     1 
ATOM   12772 C  CB    . LEU A 1 3062 ? 237.029 208.167 211.494 1.00 0.22  ? 3062 LEU A CB    1 
ATOM   12773 C  CG    . LEU A 1 3062 ? 235.889 207.324 212.066 1.00 0.16  ? 3062 LEU A CG    1 
ATOM   12774 C  CD1   . LEU A 1 3062 ? 235.432 207.875 213.408 1.00 0.20  ? 3062 LEU A CD1   1 
ATOM   12775 C  CD2   . LEU A 1 3062 ? 234.732 207.255 211.093 1.00 0.23  ? 3062 LEU A CD2   1 
ATOM   12776 N  N     . HIS A 1 3063 ? 238.692 206.738 214.154 1.00 0.20  ? 3063 HIS A N     1 
ATOM   12777 C  CA    . HIS A 1 3063 ? 239.103 205.467 214.728 1.00 0.12  ? 3063 HIS A CA    1 
ATOM   12778 C  C     . HIS A 1 3063 ? 237.878 204.794 215.326 1.00 0.09  ? 3063 HIS A C     1 
ATOM   12779 O  O     . HIS A 1 3063 ? 237.163 205.403 216.128 1.00 0.35  ? 3063 HIS A O     1 
ATOM   12780 C  CB    . HIS A 1 3063 ? 240.176 205.661 215.802 1.00 0.10  ? 3063 HIS A CB    1 
ATOM   12781 C  CG    . HIS A 1 3063 ? 241.467 206.206 215.277 1.00 0.10  ? 3063 HIS A CG    1 
ATOM   12782 N  ND1   . HIS A 1 3063 ? 242.518 205.399 214.903 1.00 0.20  ? 3063 HIS A ND1   1 
ATOM   12783 C  CD2   . HIS A 1 3063 ? 241.877 207.479 215.067 1.00 0.17  ? 3063 HIS A CD2   1 
ATOM   12784 C  CE1   . HIS A 1 3063 ? 243.520 206.150 214.483 1.00 0.47  ? 3063 HIS A CE1   1 
ATOM   12785 N  NE2   . HIS A 1 3063 ? 243.155 207.416 214.572 1.00 0.22  ? 3063 HIS A NE2   1 
ATOM   12786 N  N     . VAL A 1 3064 ? 237.636 203.549 214.938 1.00 0.11  ? 3064 VAL A N     1 
ATOM   12787 C  CA    . VAL A 1 3064 ? 236.488 202.792 215.415 1.00 0.19  ? 3064 VAL A CA    1 
ATOM   12788 C  C     . VAL A 1 3064 ? 236.996 201.723 216.369 1.00 0.08  ? 3064 VAL A C     1 
ATOM   12789 O  O     . VAL A 1 3064 ? 237.889 200.942 216.022 1.00 0.07  ? 3064 VAL A O     1 
ATOM   12790 C  CB    . VAL A 1 3064 ? 235.693 202.172 214.257 1.00 0.27  ? 3064 VAL A CB    1 
ATOM   12791 C  CG1   . VAL A 1 3064 ? 234.689 201.158 214.784 1.00 0.05  ? 3064 VAL A CG1   1 
ATOM   12792 C  CG2   . VAL A 1 3064 ? 234.995 203.259 213.460 1.00 0.30  ? 3064 VAL A CG2   1 
ATOM   12793 N  N     . VAL A 1 3065 ? 236.440 201.702 217.574 1.00 0.14  ? 3065 VAL A N     1 
ATOM   12794 C  CA    . VAL A 1 3065 ? 236.725 200.667 218.558 1.00 0.11  ? 3065 VAL A CA    1 
ATOM   12795 C  C     . VAL A 1 3065 ? 235.464 199.835 218.726 1.00 0.08  ? 3065 VAL A C     1 
ATOM   12796 O  O     . VAL A 1 3065 ? 234.425 200.349 219.158 1.00 0.24  ? 3065 VAL A O     1 
ATOM   12797 C  CB    . VAL A 1 3065 ? 237.183 201.262 219.897 1.00 0.10  ? 3065 VAL A CB    1 
ATOM   12798 C  CG1   . VAL A 1 3065 ? 237.498 200.154 220.887 1.00 0.06  ? 3065 VAL A CG1   1 
ATOM   12799 C  CG2   . VAL A 1 3065 ? 238.388 202.164 219.693 1.00 0.05  ? 3065 VAL A CG2   1 
ATOM   12800 N  N     . PHE A 1 3066 ? 235.553 198.558 218.380 1.00 0.04  ? 3066 PHE A N     1 
ATOM   12801 C  CA    . PHE A 1 3066 ? 234.450 197.617 218.525 1.00 0.19  ? 3066 PHE A CA    1 
ATOM   12802 C  C     . PHE A 1 3066 ? 234.718 196.723 219.725 1.00 0.25  ? 3066 PHE A C     1 
ATOM   12803 O  O     . PHE A 1 3066 ? 235.765 196.074 219.798 1.00 0.19  ? 3066 PHE A O     1 
ATOM   12804 C  CB    . PHE A 1 3066 ? 234.270 196.781 217.258 1.00 0.79  ? 3066 PHE A CB    1 
ATOM   12805 C  CG    . PHE A 1 3066 ? 232.851 196.374 217.001 1.00 2.95  ? 3066 PHE A CG    1 
ATOM   12806 C  CD1   . PHE A 1 3066 ? 231.941 197.265 216.463 1.00 3.74  ? 3066 PHE A CD1   1 
ATOM   12807 C  CD2   . PHE A 1 3066 ? 232.423 195.095 217.318 1.00 4.28  ? 3066 PHE A CD2   1 
ATOM   12808 C  CE1   . PHE A 1 3066 ? 230.634 196.882 216.235 1.00 12.11 ? 3066 PHE A CE1   1 
ATOM   12809 C  CE2   . PHE A 1 3066 ? 231.118 194.709 217.093 1.00 8.72  ? 3066 PHE A CE2   1 
ATOM   12810 C  CZ    . PHE A 1 3066 ? 230.221 195.603 216.551 1.00 7.94  ? 3066 PHE A CZ    1 
ATOM   12811 N  N     . THR A 1 3067 ? 233.771 196.689 220.657 1.00 1.10  ? 3067 THR A N     1 
ATOM   12812 C  CA    . THR A 1 3067 ? 233.856 195.846 221.840 1.00 2.12  ? 3067 THR A CA    1 
ATOM   12813 C  C     . THR A 1 3067 ? 232.745 194.807 221.793 1.00 1.85  ? 3067 THR A C     1 
ATOM   12814 O  O     . THR A 1 3067 ? 231.589 195.141 221.523 1.00 4.16  ? 3067 THR A O     1 
ATOM   12815 C  CB    . THR A 1 3067 ? 233.758 196.676 223.122 1.00 1.60  ? 3067 THR A CB    1 
ATOM   12816 O  OG1   . THR A 1 3067 ? 232.570 197.474 223.090 1.00 5.25  ? 3067 THR A OG1   1 
ATOM   12817 C  CG2   . THR A 1 3067 ? 234.967 197.583 223.260 1.00 0.48  ? 3067 THR A CG2   1 
ATOM   12818 N  N     . MET A 1 3068 ? 233.102 193.548 222.042 1.00 2.67  ? 3068 MET A N     1 
ATOM   12819 C  CA    . MET A 1 3068 ? 232.137 192.461 222.022 1.00 4.60  ? 3068 MET A CA    1 
ATOM   12820 C  C     . MET A 1 3068 ? 232.585 191.367 222.981 1.00 2.59  ? 3068 MET A C     1 
ATOM   12821 O  O     . MET A 1 3068 ? 233.779 191.193 223.232 1.00 1.52  ? 3068 MET A O     1 
ATOM   12822 C  CB    . MET A 1 3068 ? 231.964 191.897 220.608 1.00 3.87  ? 3068 MET A CB    1 
ATOM   12823 C  CG    . MET A 1 3068 ? 233.247 191.417 219.962 1.00 3.94  ? 3068 MET A CG    1 
ATOM   12824 S  SD    . MET A 1 3068 ? 232.998 190.882 218.260 1.00 18.13 ? 3068 MET A SD    1 
ATOM   12825 C  CE    . MET A 1 3068 ? 231.538 189.868 218.437 1.00 17.25 ? 3068 MET A CE    1 
ATOM   12826 N  N     . ASN A 1 3069 ? 231.608 190.631 223.514 1.00 7.36  ? 3069 ASN A N     1 
ATOM   12827 C  CA    . ASN A 1 3069 ? 231.912 189.508 224.386 1.00 6.11  ? 3069 ASN A CA    1 
ATOM   12828 C  C     . ASN A 1 3069 ? 232.360 188.294 223.575 1.00 6.69  ? 3069 ASN A C     1 
ATOM   12829 O  O     . ASN A 1 3069 ? 231.966 188.130 222.419 1.00 7.42  ? 3069 ASN A O     1 
ATOM   12830 C  CB    . ASN A 1 3069 ? 230.699 189.134 225.231 1.00 5.86  ? 3069 ASN A CB    1 
ATOM   12831 C  CG    . ASN A 1 3069 ? 230.288 190.232 226.181 1.00 7.55  ? 3069 ASN A CG    1 
ATOM   12832 O  OD1   . ASN A 1 3069 ? 231.022 190.584 227.102 1.00 10.11 ? 3069 ASN A OD1   1 
ATOM   12833 N  ND2   . ASN A 1 3069 ? 229.110 190.788 225.957 1.00 14.76 ? 3069 ASN A ND2   1 
ATOM   12834 N  N     . PRO A 1 3070 ? 233.192 187.433 224.162 1.00 6.56  ? 3070 PRO A N     1 
ATOM   12835 C  CA    . PRO A 1 3070 ? 233.571 186.188 223.481 1.00 7.33  ? 3070 PRO A CA    1 
ATOM   12836 C  C     . PRO A 1 3070 ? 232.387 185.237 223.390 1.00 10.95 ? 3070 PRO A C     1 
ATOM   12837 O  O     . PRO A 1 3070 ? 231.872 184.758 224.402 1.00 16.42 ? 3070 PRO A O     1 
ATOM   12838 C  CB    . PRO A 1 3070 ? 234.684 185.620 224.371 1.00 5.41  ? 3070 PRO A CB    1 
ATOM   12839 C  CG    . PRO A 1 3070 ? 235.138 186.765 225.218 1.00 4.19  ? 3070 PRO A CG    1 
ATOM   12840 C  CD    . PRO A 1 3070 ? 233.930 187.616 225.421 1.00 3.49  ? 3070 PRO A CD    1 
ATOM   12841 N  N     . SER A 1 3071 ? 231.950 184.976 222.162 1.00 13.46 ? 3071 SER A N     1 
ATOM   12842 C  CA    . SER A 1 3071 ? 230.908 183.990 221.890 1.00 14.71 ? 3071 SER A CA    1 
ATOM   12843 C  C     . SER A 1 3071 ? 231.349 183.197 220.670 1.00 18.30 ? 3071 SER A C     1 
ATOM   12844 O  O     . SER A 1 3071 ? 231.504 183.767 219.588 1.00 18.02 ? 3071 SER A O     1 
ATOM   12845 C  CB    . SER A 1 3071 ? 229.553 184.656 221.655 1.00 15.19 ? 3071 SER A CB    1 
ATOM   12846 O  OG    . SER A 1 3071 ? 229.192 185.476 222.753 1.00 18.34 ? 3071 SER A OG    1 
ATOM   12847 N  N     . SER A 1 3072 ? 231.558 181.890 220.847 1.00 24.41 ? 3072 SER A N     1 
ATOM   12848 C  CA    . SER A 1 3072 ? 232.074 181.067 219.757 1.00 20.54 ? 3072 SER A CA    1 
ATOM   12849 C  C     . SER A 1 3072 ? 231.154 181.115 218.543 1.00 19.07 ? 3072 SER A C     1 
ATOM   12850 O  O     . SER A 1 3072 ? 231.606 181.343 217.417 1.00 20.99 ? 3072 SER A O     1 
ATOM   12851 C  CB    . SER A 1 3072 ? 232.264 179.628 220.236 1.00 17.92 ? 3072 SER A CB    1 
ATOM   12852 O  OG    . SER A 1 3072 ? 233.202 179.565 221.296 1.00 22.83 ? 3072 SER A OG    1 
ATOM   12853 N  N     . GLU A 1 3073 ? 229.855 180.910 218.757 1.00 20.80 ? 3073 GLU A N     1 
ATOM   12854 C  CA    . GLU A 1 3073 ? 228.902 181.028 217.658 1.00 22.85 ? 3073 GLU A CA    1 
ATOM   12855 C  C     . GLU A 1 3073 ? 228.812 182.468 217.168 1.00 18.75 ? 3073 GLU A C     1 
ATOM   12856 O  O     . GLU A 1 3073 ? 228.784 182.723 215.958 1.00 24.19 ? 3073 GLU A O     1 
ATOM   12857 C  CB    . GLU A 1 3073 ? 227.529 180.518 218.094 1.00 22.77 ? 3073 GLU A CB    1 
ATOM   12858 C  CG    . GLU A 1 3073 ? 226.449 180.680 217.038 1.00 25.47 ? 3073 GLU A CG    1 
ATOM   12859 C  CD    . GLU A 1 3073 ? 225.095 180.183 217.505 1.00 35.47 ? 3073 GLU A CD    1 
ATOM   12860 O  OE1   . GLU A 1 3073 ? 224.579 180.714 218.511 1.00 33.57 ? 3073 GLU A OE1   1 
ATOM   12861 O  OE2   . GLU A 1 3073 ? 224.546 179.262 216.865 1.00 37.00 ? 3073 GLU A OE2   1 
ATOM   12862 N  N     . GLY A 1 3074 ? 228.770 183.424 218.098 1.00 17.76 ? 3074 GLY A N     1 
ATOM   12863 C  CA    . GLY A 1 3074 ? 228.648 184.818 217.703 1.00 16.30 ? 3074 GLY A CA    1 
ATOM   12864 C  C     . GLY A 1 3074 ? 229.858 185.319 216.937 1.00 17.67 ? 3074 GLY A C     1 
ATOM   12865 O  O     . GLY A 1 3074 ? 229.726 186.062 215.961 1.00 15.23 ? 3074 GLY A O     1 
ATOM   12866 N  N     . LEU A 1 3075 ? 231.054 184.923 217.377 1.00 14.03 ? 3075 LEU A N     1 
ATOM   12867 C  CA    . LEU A 1 3075 ? 232.272 185.386 216.720 1.00 12.97 ? 3075 LEU A CA    1 
ATOM   12868 C  C     . LEU A 1 3075 ? 232.373 184.841 215.300 1.00 17.15 ? 3075 LEU A C     1 
ATOM   12869 O  O     . LEU A 1 3075 ? 232.722 185.574 214.366 1.00 12.77 ? 3075 LEU A O     1 
ATOM   12870 C  CB    . LEU A 1 3075 ? 233.494 184.983 217.544 1.00 15.91 ? 3075 LEU A CB    1 
ATOM   12871 C  CG    . LEU A 1 3075 ? 234.828 185.579 217.105 1.00 15.41 ? 3075 LEU A CG    1 
ATOM   12872 C  CD1   . LEU A 1 3075 ? 234.824 187.077 217.347 1.00 12.36 ? 3075 LEU A CD1   1 
ATOM   12873 C  CD2   . LEU A 1 3075 ? 235.983 184.912 217.828 1.00 12.30 ? 3075 LEU A CD2   1 
ATOM   12874 N  N     . LYS A 1 3076 ? 232.074 183.552 215.116 1.00 17.71 ? 3076 LYS A N     1 
ATOM   12875 C  CA    . LYS A 1 3076 ? 232.090 182.975 213.773 1.00 12.70 ? 3076 LYS A CA    1 
ATOM   12876 C  C     . LYS A 1 3076 ? 231.041 183.621 212.879 1.00 14.33 ? 3076 LYS A C     1 
ATOM   12877 O  O     . LYS A 1 3076 ? 231.310 183.918 211.710 1.00 22.65 ? 3076 LYS A O     1 
ATOM   12878 C  CB    . LYS A 1 3076 ? 231.873 181.462 213.837 1.00 13.57 ? 3076 LYS A CB    1 
ATOM   12879 C  CG    . LYS A 1 3076 ? 232.948 180.701 214.584 1.00 12.15 ? 3076 LYS A CG    1 
ATOM   12880 C  CD    . LYS A 1 3076 ? 232.725 179.203 214.495 1.00 14.01 ? 3076 LYS A CD    1 
ATOM   12881 C  CE    . LYS A 1 3076 ? 233.864 178.436 215.140 1.00 12.56 ? 3076 LYS A CE    1 
ATOM   12882 N  NZ    . LYS A 1 3076 ? 233.664 176.964 215.042 1.00 22.79 ? 3076 LYS A NZ    1 
ATOM   12883 N  N     . ASP A 1 3077 ? 229.837 183.842 213.410 1.00 14.33 ? 3077 ASP A N     1 
ATOM   12884 C  CA    . ASP A 1 3077 ? 228.800 184.503 212.627 1.00 16.16 ? 3077 ASP A CA    1 
ATOM   12885 C  C     . ASP A 1 3077 ? 229.160 185.957 212.352 1.00 13.49 ? 3077 ASP A C     1 
ATOM   12886 O  O     . ASP A 1 3077 ? 228.719 186.533 211.351 1.00 20.06 ? 3077 ASP A O     1 
ATOM   12887 C  CB    . ASP A 1 3077 ? 227.458 184.414 213.352 1.00 19.93 ? 3077 ASP A CB    1 
ATOM   12888 C  CG    . ASP A 1 3077 ? 226.910 183.002 213.392 1.00 27.53 ? 3077 ASP A CG    1 
ATOM   12889 O  OD1   . ASP A 1 3077 ? 227.205 182.221 212.465 1.00 28.62 ? 3077 ASP A OD1   1 
ATOM   12890 O  OD2   . ASP A 1 3077 ? 226.183 182.675 214.352 1.00 29.94 ? 3077 ASP A OD2   1 
ATOM   12891 N  N     . ARG A 1 3078 ? 229.962 186.563 213.229 1.00 15.83 ? 3078 ARG A N     1 
ATOM   12892 C  CA    . ARG A 1 3078 ? 230.252 187.987 213.103 1.00 14.75 ? 3078 ARG A CA    1 
ATOM   12893 C  C     . ARG A 1 3078 ? 231.093 188.263 211.864 1.00 12.27 ? 3078 ARG A C     1 
ATOM   12894 O  O     . ARG A 1 3078 ? 231.019 189.353 211.288 1.00 11.24 ? 3078 ARG A O     1 
ATOM   12895 C  CB    . ARG A 1 3078 ? 230.981 188.480 214.355 1.00 13.69 ? 3078 ARG A CB    1 
ATOM   12896 C  CG    . ARG A 1 3078 ? 231.334 189.947 214.328 1.00 17.44 ? 3078 ARG A CG    1 
ATOM   12897 C  CD    . ARG A 1 3078 ? 230.041 190.736 214.353 1.00 13.60 ? 3078 ARG A CD    1 
ATOM   12898 N  NE    . ARG A 1 3078 ? 229.366 190.514 215.627 1.00 21.12 ? 3078 ARG A NE    1 
ATOM   12899 C  CZ    . ARG A 1 3078 ? 228.115 190.853 215.898 1.00 23.55 ? 3078 ARG A CZ    1 
ATOM   12900 N  NH1   . ARG A 1 3078 ? 227.327 191.386 214.982 1.00 21.31 ? 3078 ARG A NH1   1 
ATOM   12901 N  NH2   . ARG A 1 3078 ? 227.634 190.635 217.120 1.00 24.75 ? 3078 ARG A NH2   1 
ATOM   12902 N  N     . ALA A 1 3079 ? 231.892 187.280 211.439 1.00 8.68  ? 3079 ALA A N     1 
ATOM   12903 C  CA    . ALA A 1 3079 ? 232.788 187.471 210.303 1.00 9.16  ? 3079 ALA A CA    1 
ATOM   12904 C  C     . ALA A 1 3079 ? 232.012 187.708 209.012 1.00 13.20 ? 3079 ALA A C     1 
ATOM   12905 O  O     . ALA A 1 3079 ? 232.397 188.545 208.190 1.00 11.04 ? 3079 ALA A O     1 
ATOM   12906 C  CB    . ALA A 1 3079 ? 233.714 186.263 210.164 1.00 6.27  ? 3079 ALA A CB    1 
ATOM   12907 N  N     . ALA A 1 3080 ? 230.923 186.965 208.804 1.00 10.44 ? 3080 ALA A N     1 
ATOM   12908 C  CA    . ALA A 1 3080 ? 230.144 187.145 207.584 1.00 7.25  ? 3080 ALA A CA    1 
ATOM   12909 C  C     . ALA A 1 3080 ? 229.416 188.483 207.583 1.00 5.58  ? 3080 ALA A C     1 
ATOM   12910 O  O     . ALA A 1 3080 ? 229.362 189.165 206.552 1.00 3.40  ? 3080 ALA A O     1 
ATOM   12911 C  CB    . ALA A 1 3080 ? 229.155 185.992 207.416 1.00 6.25  ? 3080 ALA A CB    1 
ATOM   12912 N  N     . THR A 1 3081 ? 228.843 188.872 208.724 1.00 8.47  ? 3081 THR A N     1 
ATOM   12913 C  CA    . THR A 1 3081 ? 228.094 190.123 208.795 1.00 7.87  ? 3081 THR A CA    1 
ATOM   12914 C  C     . THR A 1 3081 ? 229.003 191.331 208.590 1.00 9.24  ? 3081 THR A C     1 
ATOM   12915 O  O     . THR A 1 3081 ? 228.627 192.285 207.899 1.00 12.92 ? 3081 THR A O     1 
ATOM   12916 C  CB    . THR A 1 3081 ? 227.366 190.218 210.137 1.00 11.81 ? 3081 THR A CB    1 
ATOM   12917 O  OG1   . THR A 1 3081 ? 226.457 189.118 210.265 1.00 11.60 ? 3081 THR A OG1   1 
ATOM   12918 C  CG2   . THR A 1 3081 ? 226.589 191.519 210.240 1.00 9.76  ? 3081 THR A CG2   1 
ATOM   12919 N  N     . SER A 1 3082 ? 230.191 191.319 209.191 1.00 7.94  ? 3082 SER A N     1 
ATOM   12920 C  CA    . SER A 1 3082 ? 231.160 192.404 209.049 1.00 5.98  ? 3082 SER A CA    1 
ATOM   12921 C  C     . SER A 1 3082 ? 232.544 191.812 208.825 1.00 5.12  ? 3082 SER A C     1 
ATOM   12922 O  O     . SER A 1 3082 ? 233.348 191.712 209.760 1.00 8.14  ? 3082 SER A O     1 
ATOM   12923 C  CB    . SER A 1 3082 ? 231.140 193.324 210.271 1.00 7.42  ? 3082 SER A CB    1 
ATOM   12924 O  OG    . SER A 1 3082 ? 232.100 194.357 210.145 1.00 8.23  ? 3082 SER A OG    1 
ATOM   12925 N  N     . PRO A 1 3083 ? 232.855 191.403 207.591 1.00 6.49  ? 3083 PRO A N     1 
ATOM   12926 C  CA    . PRO A 1 3083 ? 234.212 190.904 207.313 1.00 5.67  ? 3083 PRO A CA    1 
ATOM   12927 C  C     . PRO A 1 3083 ? 235.295 191.939 207.547 1.00 2.22  ? 3083 PRO A C     1 
ATOM   12928 O  O     . PRO A 1 3083 ? 236.451 191.568 207.787 1.00 2.11  ? 3083 PRO A O     1 
ATOM   12929 C  CB    . PRO A 1 3083 ? 234.136 190.484 205.837 1.00 3.39  ? 3083 PRO A CB    1 
ATOM   12930 C  CG    . PRO A 1 3083 ? 232.930 191.176 205.296 1.00 2.29  ? 3083 PRO A CG    1 
ATOM   12931 C  CD    . PRO A 1 3083 ? 231.969 191.263 206.426 1.00 2.89  ? 3083 PRO A CD    1 
ATOM   12932 N  N     . ALA A 1 3084 ? 234.960 193.229 207.481 1.00 3.06  ? 3084 ALA A N     1 
ATOM   12933 C  CA    . ALA A 1 3084 ? 235.928 194.273 207.788 1.00 2.95  ? 3084 ALA A CA    1 
ATOM   12934 C  C     . ALA A 1 3084 ? 236.365 194.248 209.247 1.00 3.35  ? 3084 ALA A C     1 
ATOM   12935 O  O     . ALA A 1 3084 ? 237.469 194.705 209.556 1.00 3.45  ? 3084 ALA A O     1 
ATOM   12936 C  CB    . ALA A 1 3084 ? 235.353 195.644 207.437 1.00 2.70  ? 3084 ALA A CB    1 
ATOM   12937 N  N     . LEU A 1 3085 ? 235.529 193.721 210.146 1.00 2.71  ? 3085 LEU A N     1 
ATOM   12938 C  CA    . LEU A 1 3085 ? 235.911 193.635 211.552 1.00 3.26  ? 3085 LEU A CA    1 
ATOM   12939 C  C     . LEU A 1 3085 ? 237.126 192.740 211.756 1.00 4.47  ? 3085 LEU A C     1 
ATOM   12940 O  O     . LEU A 1 3085 ? 237.861 192.909 212.734 1.00 6.58  ? 3085 LEU A O     1 
ATOM   12941 C  CB    . LEU A 1 3085 ? 234.741 193.115 212.389 1.00 4.33  ? 3085 LEU A CB    1 
ATOM   12942 C  CG    . LEU A 1 3085 ? 233.727 194.116 212.941 1.00 3.68  ? 3085 LEU A CG    1 
ATOM   12943 C  CD1   . LEU A 1 3085 ? 232.856 193.446 213.987 1.00 8.32  ? 3085 LEU A CD1   1 
ATOM   12944 C  CD2   . LEU A 1 3085 ? 234.418 195.329 213.526 1.00 3.69  ? 3085 LEU A CD2   1 
ATOM   12945 N  N     . PHE A 1 3086 ? 237.358 191.794 210.850 1.00 3.00  ? 3086 PHE A N     1 
ATOM   12946 C  CA    . PHE A 1 3086 ? 238.410 190.805 211.024 1.00 1.89  ? 3086 PHE A CA    1 
ATOM   12947 C  C     . PHE A 1 3086 ? 239.563 190.961 210.043 1.00 2.91  ? 3086 PHE A C     1 
ATOM   12948 O  O     . PHE A 1 3086 ? 240.566 190.254 210.179 1.00 5.36  ? 3086 PHE A O     1 
ATOM   12949 C  CB    . PHE A 1 3086 ? 237.818 189.397 210.928 1.00 3.00  ? 3086 PHE A CB    1 
ATOM   12950 C  CG    . PHE A 1 3086 ? 236.859 189.079 212.038 1.00 5.98  ? 3086 PHE A CG    1 
ATOM   12951 C  CD1   . PHE A 1 3086 ? 235.521 189.415 211.932 1.00 4.69  ? 3086 PHE A CD1   1 
ATOM   12952 C  CD2   . PHE A 1 3086 ? 237.301 188.466 213.196 1.00 6.35  ? 3086 PHE A CD2   1 
ATOM   12953 C  CE1   . PHE A 1 3086 ? 234.642 189.135 212.953 1.00 6.62  ? 3086 PHE A CE1   1 
ATOM   12954 C  CE2   . PHE A 1 3086 ? 236.423 188.183 214.220 1.00 7.84  ? 3086 PHE A CE2   1 
ATOM   12955 C  CZ    . PHE A 1 3086 ? 235.094 188.517 214.097 1.00 8.60  ? 3086 PHE A CZ    1 
ATOM   12956 N  N     . ASN A 1 3087 ? 239.460 191.863 209.065 1.00 3.96  ? 3087 ASN A N     1 
ATOM   12957 C  CA    . ASN A 1 3087 ? 240.582 192.156 208.188 1.00 3.65  ? 3087 ASN A CA    1 
ATOM   12958 C  C     . ASN A 1 3087 ? 240.949 193.632 208.111 1.00 4.47  ? 3087 ASN A C     1 
ATOM   12959 O  O     . ASN A 1 3087 ? 242.013 193.952 207.572 1.00 6.96  ? 3087 ASN A O     1 
ATOM   12960 C  CB    . ASN A 1 3087 ? 240.321 191.615 206.769 1.00 4.22  ? 3087 ASN A CB    1 
ATOM   12961 C  CG    . ASN A 1 3087 ? 239.105 192.237 206.107 1.00 7.73  ? 3087 ASN A CG    1 
ATOM   12962 O  OD1   . ASN A 1 3087 ? 239.006 193.453 205.968 1.00 12.46 ? 3087 ASN A OD1   1 
ATOM   12963 N  ND2   . ASN A 1 3087 ? 238.177 191.394 205.675 1.00 9.95  ? 3087 ASN A ND2   1 
ATOM   12964 N  N     . ARG A 1 3088 ? 240.113 194.533 208.632 1.00 3.98  ? 3088 ARG A N     1 
ATOM   12965 C  CA    . ARG A 1 3088 ? 240.455 195.945 208.729 1.00 4.45  ? 3088 ARG A CA    1 
ATOM   12966 C  C     . ARG A 1 3088 ? 240.657 196.426 210.158 1.00 4.74  ? 3088 ARG A C     1 
ATOM   12967 O  O     . ARG A 1 3088 ? 241.149 197.544 210.347 1.00 3.53  ? 3088 ARG A O     1 
ATOM   12968 C  CB    . ARG A 1 3088 ? 239.377 196.819 208.065 1.00 5.98  ? 3088 ARG A CB    1 
ATOM   12969 C  CG    . ARG A 1 3088 ? 239.065 196.475 206.620 1.00 3.85  ? 3088 ARG A CG    1 
ATOM   12970 C  CD    . ARG A 1 3088 ? 240.308 196.493 205.750 1.00 6.05  ? 3088 ARG A CD    1 
ATOM   12971 N  NE    . ARG A 1 3088 ? 240.084 197.212 204.501 1.00 12.61 ? 3088 ARG A NE    1 
ATOM   12972 C  CZ    . ARG A 1 3088 ? 239.639 196.651 203.384 1.00 12.50 ? 3088 ARG A CZ    1 
ATOM   12973 N  NH1   . ARG A 1 3088 ? 239.367 195.359 203.318 1.00 9.93  ? 3088 ARG A NH1   1 
ATOM   12974 N  NH2   . ARG A 1 3088 ? 239.462 197.410 202.304 1.00 9.28  ? 3088 ARG A NH2   1 
ATOM   12975 N  N     . CYS A 1 3089 ? 240.298 195.632 211.160 1.00 6.54  ? 3089 CYS A N     1 
ATOM   12976 C  CA    . CYS A 1 3089 ? 240.467 196.001 212.558 1.00 2.10  ? 3089 CYS A CA    1 
ATOM   12977 C  C     . CYS A 1 3089 ? 241.502 195.096 213.207 1.00 1.63  ? 3089 CYS A C     1 
ATOM   12978 O  O     . CYS A 1 3089 ? 241.550 193.895 212.934 1.00 2.61  ? 3089 CYS A O     1 
ATOM   12979 C  CB    . CYS A 1 3089 ? 239.144 195.902 213.323 1.00 0.43  ? 3089 CYS A CB    1 
ATOM   12980 S  SG    . CYS A 1 3089 ? 237.742 196.712 212.531 1.00 7.73  ? 3089 CYS A SG    1 
ATOM   12981 N  N     . VAL A 1 3090 ? 242.330 195.680 214.066 1.00 1.38  ? 3090 VAL A N     1 
ATOM   12982 C  CA    . VAL A 1 3090 ? 243.291 194.908 214.846 1.00 1.58  ? 3090 VAL A CA    1 
ATOM   12983 C  C     . VAL A 1 3090 ? 242.552 194.271 216.013 1.00 0.67  ? 3090 VAL A C     1 
ATOM   12984 O  O     . VAL A 1 3090 ? 241.880 194.960 216.787 1.00 0.90  ? 3090 VAL A O     1 
ATOM   12985 C  CB    . VAL A 1 3090 ? 244.448 195.792 215.334 1.00 1.18  ? 3090 VAL A CB    1 
ATOM   12986 C  CG1   . VAL A 1 3090 ? 245.284 195.053 216.361 1.00 0.67  ? 3090 VAL A CG1   1 
ATOM   12987 C  CG2   . VAL A 1 3090 ? 245.299 196.236 214.161 1.00 0.76  ? 3090 VAL A CG2   1 
ATOM   12988 N  N     . LEU A 1 3091 ? 242.662 192.953 216.136 1.00 0.82  ? 3091 LEU A N     1 
ATOM   12989 C  CA    . LEU A 1 3091 ? 241.926 192.217 217.151 1.00 0.41  ? 3091 LEU A CA    1 
ATOM   12990 C  C     . LEU A 1 3091 ? 242.818 191.996 218.366 1.00 0.50  ? 3091 LEU A C     1 
ATOM   12991 O  O     . LEU A 1 3091 ? 243.943 191.507 218.241 1.00 0.38  ? 3091 LEU A O     1 
ATOM   12992 C  CB    . LEU A 1 3091 ? 241.427 190.883 216.587 1.00 0.50  ? 3091 LEU A CB    1 
ATOM   12993 C  CG    . LEU A 1 3091 ? 240.391 190.054 217.360 1.00 0.63  ? 3091 LEU A CG    1 
ATOM   12994 C  CD1   . LEU A 1 3091 ? 239.748 189.050 216.423 1.00 0.54  ? 3091 LEU A CD1   1 
ATOM   12995 C  CD2   . LEU A 1 3091 ? 240.974 189.331 218.570 1.00 0.32  ? 3091 LEU A CD2   1 
ATOM   12996 N  N     . ASN A 1 3092 ? 242.311 192.372 219.535 1.00 0.58  ? 3092 ASN A N     1 
ATOM   12997 C  CA    . ASN A 1 3092 ? 242.987 192.149 220.807 1.00 0.50  ? 3092 ASN A CA    1 
ATOM   12998 C  C     . ASN A 1 3092 ? 242.047 191.359 221.704 1.00 0.34  ? 3092 ASN A C     1 
ATOM   12999 O  O     . ASN A 1 3092 ? 240.991 191.862 222.103 1.00 0.23  ? 3092 ASN A O     1 
ATOM   13000 C  CB    . ASN A 1 3092 ? 243.392 193.471 221.457 1.00 0.72  ? 3092 ASN A CB    1 
ATOM   13001 C  CG    . ASN A 1 3092 ? 244.403 194.237 220.634 1.00 1.91  ? 3092 ASN A CG    1 
ATOM   13002 O  OD1   . ASN A 1 3092 ? 244.117 195.319 220.129 1.00 13.57 ? 3092 ASN A OD1   1 
ATOM   13003 N  ND2   . ASN A 1 3092 ? 245.598 193.683 220.500 1.00 4.52  ? 3092 ASN A ND2   1 
ATOM   13004 N  N     . TRP A 1 3093 ? 242.423 190.120 222.010 1.00 0.27  ? 3093 TRP A N     1 
ATOM   13005 C  CA    . TRP A 1 3093 ? 241.617 189.255 222.868 1.00 0.45  ? 3093 TRP A CA    1 
ATOM   13006 C  C     . TRP A 1 3093 ? 241.935 189.578 224.319 1.00 0.41  ? 3093 TRP A C     1 
ATOM   13007 O  O     . TRP A 1 3093 ? 242.834 188.997 224.929 1.00 2.46  ? 3093 TRP A O     1 
ATOM   13008 C  CB    . TRP A 1 3093 ? 241.880 187.788 222.562 1.00 0.79  ? 3093 TRP A CB    1 
ATOM   13009 C  CG    . TRP A 1 3093 ? 240.775 186.891 223.011 1.00 1.02  ? 3093 TRP A CG    1 
ATOM   13010 C  CD1   . TRP A 1 3093 ? 240.609 186.355 224.254 1.00 0.62  ? 3093 TRP A CD1   1 
ATOM   13011 C  CD2   . TRP A 1 3093 ? 239.681 186.413 222.220 1.00 1.17  ? 3093 TRP A CD2   1 
ATOM   13012 N  NE1   . TRP A 1 3093 ? 239.479 185.582 224.289 1.00 1.16  ? 3093 TRP A NE1   1 
ATOM   13013 C  CE2   . TRP A 1 3093 ? 238.889 185.599 223.053 1.00 1.43  ? 3093 TRP A CE2   1 
ATOM   13014 C  CE3   . TRP A 1 3093 ? 239.293 186.597 220.891 1.00 1.04  ? 3093 TRP A CE3   1 
ATOM   13015 C  CZ2   . TRP A 1 3093 ? 237.735 184.970 222.600 1.00 1.36  ? 3093 TRP A CZ2   1 
ATOM   13016 C  CZ3   . TRP A 1 3093 ? 238.146 185.973 220.444 1.00 2.18  ? 3093 TRP A CZ3   1 
ATOM   13017 C  CH2   . TRP A 1 3093 ? 237.380 185.169 221.294 1.00 1.89  ? 3093 TRP A CH2   1 
ATOM   13018 N  N     . PHE A 1 3094 ? 241.191 190.528 224.881 1.00 0.37  ? 3094 PHE A N     1 
ATOM   13019 C  CA    . PHE A 1 3094 ? 241.328 190.809 226.304 1.00 0.44  ? 3094 PHE A CA    1 
ATOM   13020 C  C     . PHE A 1 3094 ? 240.732 189.692 227.151 1.00 0.84  ? 3094 PHE A C     1 
ATOM   13021 O  O     . PHE A 1 3094 ? 241.269 189.377 228.219 1.00 2.38  ? 3094 PHE A O     1 
ATOM   13022 C  CB    . PHE A 1 3094 ? 240.680 192.152 226.645 1.00 0.46  ? 3094 PHE A CB    1 
ATOM   13023 C  CG    . PHE A 1 3094 ? 241.415 193.343 226.087 1.00 1.70  ? 3094 PHE A CG    1 
ATOM   13024 C  CD1   . PHE A 1 3094 ? 242.633 193.189 225.439 1.00 1.44  ? 3094 PHE A CD1   1 
ATOM   13025 C  CD2   . PHE A 1 3094 ? 240.893 194.618 226.220 1.00 1.15  ? 3094 PHE A CD2   1 
ATOM   13026 C  CE1   . PHE A 1 3094 ? 243.310 194.282 224.928 1.00 1.02  ? 3094 PHE A CE1   1 
ATOM   13027 C  CE2   . PHE A 1 3094 ? 241.565 195.714 225.716 1.00 1.35  ? 3094 PHE A CE2   1 
ATOM   13028 C  CZ    . PHE A 1 3094 ? 242.773 195.546 225.069 1.00 2.28  ? 3094 PHE A CZ    1 
ATOM   13029 N  N     . GLY A 1 3095 ? 239.644 189.081 226.688 1.00 0.57  ? 3095 GLY A N     1 
ATOM   13030 C  CA    . GLY A 1 3095 ? 239.048 187.960 227.391 1.00 0.68  ? 3095 GLY A CA    1 
ATOM   13031 C  C     . GLY A 1 3095 ? 238.568 188.343 228.774 1.00 1.72  ? 3095 GLY A C     1 
ATOM   13032 O  O     . GLY A 1 3095 ? 238.060 189.446 229.007 1.00 4.03  ? 3095 GLY A O     1 
ATOM   13033 N  N     . ASP A 1 3096 ? 238.727 187.416 229.708 1.00 2.08  ? 3096 ASP A N     1 
ATOM   13034 C  CA    . ASP A 1 3096 ? 238.412 187.633 231.110 1.00 2.05  ? 3096 ASP A CA    1 
ATOM   13035 C  C     . ASP A 1 3096 ? 239.695 187.912 231.883 1.00 1.64  ? 3096 ASP A C     1 
ATOM   13036 O  O     . ASP A 1 3096 ? 240.800 187.626 231.419 1.00 2.68  ? 3096 ASP A O     1 
ATOM   13037 C  CB    . ASP A 1 3096 ? 237.690 186.415 231.693 1.00 2.70  ? 3096 ASP A CB    1 
ATOM   13038 C  CG    . ASP A 1 3096 ? 236.926 186.736 232.962 1.00 6.78  ? 3096 ASP A CG    1 
ATOM   13039 O  OD1   . ASP A 1 3096 ? 237.187 187.793 233.573 1.00 4.09  ? 3096 ASP A OD1   1 
ATOM   13040 O  OD2   . ASP A 1 3096 ? 236.062 185.927 233.352 1.00 10.58 ? 3096 ASP A OD2   1 
ATOM   13041 N  N     . TRP A 1 3097 ? 239.536 188.496 233.070 1.00 1.52  ? 3097 TRP A N     1 
ATOM   13042 C  CA    . TRP A 1 3097 ? 240.682 188.721 233.939 1.00 1.08  ? 3097 TRP A CA    1 
ATOM   13043 C  C     . TRP A 1 3097 ? 241.275 187.386 234.374 1.00 2.29  ? 3097 TRP A C     1 
ATOM   13044 O  O     . TRP A 1 3097 ? 240.552 186.472 234.778 1.00 4.99  ? 3097 TRP A O     1 
ATOM   13045 C  CB    . TRP A 1 3097 ? 240.278 189.541 235.164 1.00 0.74  ? 3097 TRP A CB    1 
ATOM   13046 C  CG    . TRP A 1 3097 ? 240.038 190.990 234.879 1.00 0.53  ? 3097 TRP A CG    1 
ATOM   13047 C  CD1   . TRP A 1 3097 ? 239.993 191.587 233.655 1.00 0.56  ? 3097 TRP A CD1   1 
ATOM   13048 C  CD2   . TRP A 1 3097 ? 239.816 192.029 235.839 1.00 0.58  ? 3097 TRP A CD2   1 
ATOM   13049 N  NE1   . TRP A 1 3097 ? 239.751 192.930 233.792 1.00 0.47  ? 3097 TRP A NE1   1 
ATOM   13050 C  CE2   . TRP A 1 3097 ? 239.638 193.228 235.123 1.00 0.55  ? 3097 TRP A CE2   1 
ATOM   13051 C  CE3   . TRP A 1 3097 ? 239.744 192.060 237.235 1.00 0.48  ? 3097 TRP A CE3   1 
ATOM   13052 C  CZ2   . TRP A 1 3097 ? 239.398 194.447 235.754 1.00 0.87  ? 3097 TRP A CZ2   1 
ATOM   13053 C  CZ3   . TRP A 1 3097 ? 239.506 193.271 237.859 1.00 1.13  ? 3097 TRP A CZ3   1 
ATOM   13054 C  CH2   . TRP A 1 3097 ? 239.337 194.448 237.120 1.00 0.55  ? 3097 TRP A CH2   1 
ATOM   13055 N  N     . SER A 1 3098 ? 242.595 187.279 234.289 1.00 2.09  ? 3098 SER A N     1 
ATOM   13056 C  CA    . SER A 1 3098 ? 243.269 186.045 234.648 1.00 2.47  ? 3098 SER A CA    1 
ATOM   13057 C  C     . SER A 1 3098 ? 243.404 185.927 236.165 1.00 2.63  ? 3098 SER A C     1 
ATOM   13058 O  O     . SER A 1 3098 ? 243.042 186.830 236.924 1.00 2.25  ? 3098 SER A O     1 
ATOM   13059 C  CB    . SER A 1 3098 ? 244.641 185.977 233.982 1.00 2.07  ? 3098 SER A CB    1 
ATOM   13060 O  OG    . SER A 1 3098 ? 245.475 187.031 234.427 1.00 4.16  ? 3098 SER A OG    1 
ATOM   13061 N  N     . THR A 1 3099 ? 243.934 184.784 236.601 1.00 3.04  ? 3099 THR A N     1 
ATOM   13062 C  CA    . THR A 1 3099 ? 244.222 184.600 238.020 1.00 1.63  ? 3099 THR A CA    1 
ATOM   13063 C  C     . THR A 1 3099 ? 245.275 185.595 238.491 1.00 3.04  ? 3099 THR A C     1 
ATOM   13064 O  O     . THR A 1 3099 ? 245.198 186.113 239.611 1.00 4.40  ? 3099 THR A O     1 
ATOM   13065 C  CB    . THR A 1 3099 ? 244.679 183.163 238.278 1.00 2.06  ? 3099 THR A CB    1 
ATOM   13066 O  OG1   . THR A 1 3099 ? 243.620 182.260 237.939 1.00 4.70  ? 3099 THR A OG1   1 
ATOM   13067 C  CG2   . THR A 1 3099 ? 245.049 182.965 239.738 1.00 4.15  ? 3099 THR A CG2   1 
ATOM   13068 N  N     . GLU A 1 3100 ? 246.264 185.879 237.641 1.00 3.75  ? 3100 GLU A N     1 
ATOM   13069 C  CA    . GLU A 1 3100 ? 247.262 186.891 237.970 1.00 5.20  ? 3100 GLU A CA    1 
ATOM   13070 C  C     . GLU A 1 3100 ? 246.625 188.264 238.116 1.00 4.92  ? 3100 GLU A C     1 
ATOM   13071 O  O     . GLU A 1 3100 ? 246.963 189.019 239.035 1.00 5.31  ? 3100 GLU A O     1 
ATOM   13072 C  CB    . GLU A 1 3100 ? 248.347 186.920 236.893 1.00 9.13  ? 3100 GLU A CB    1 
ATOM   13073 C  CG    . GLU A 1 3100 ? 249.481 187.883 237.171 1.00 12.46 ? 3100 GLU A CG    1 
ATOM   13074 C  CD    . GLU A 1 3100 ? 250.545 187.835 236.096 1.00 26.10 ? 3100 GLU A CD    1 
ATOM   13075 O  OE1   . GLU A 1 3100 ? 250.375 187.063 235.129 1.00 26.93 ? 3100 GLU A OE1   1 
ATOM   13076 O  OE2   . GLU A 1 3100 ? 251.550 188.566 236.213 1.00 25.85 ? 3100 GLU A OE2   1 
ATOM   13077 N  N     . ALA A 1 3101 ? 245.706 188.611 237.210 1.00 3.12  ? 3101 ALA A N     1 
ATOM   13078 C  CA    . ALA A 1 3101 ? 245.032 189.901 237.296 1.00 3.44  ? 3101 ALA A CA    1 
ATOM   13079 C  C     . ALA A 1 3101 ? 244.191 190.000 238.561 1.00 3.41  ? 3101 ALA A C     1 
ATOM   13080 O  O     . ALA A 1 3101 ? 244.208 191.029 239.244 1.00 2.50  ? 3101 ALA A O     1 
ATOM   13081 C  CB    . ALA A 1 3101 ? 244.168 190.125 236.057 1.00 2.27  ? 3101 ALA A CB    1 
ATOM   13082 N  N     . LEU A 1 3102 ? 243.459 188.933 238.895 1.00 2.50  ? 3102 LEU A N     1 
ATOM   13083 C  CA    . LEU A 1 3102 ? 242.637 188.935 240.101 1.00 0.70  ? 3102 LEU A CA    1 
ATOM   13084 C  C     . LEU A 1 3102 ? 243.490 189.124 241.348 1.00 1.82  ? 3102 LEU A C     1 
ATOM   13085 O  O     . LEU A 1 3102 ? 243.128 189.883 242.254 1.00 2.80  ? 3102 LEU A O     1 
ATOM   13086 C  CB    . LEU A 1 3102 ? 241.836 187.635 240.189 1.00 0.73  ? 3102 LEU A CB    1 
ATOM   13087 C  CG    . LEU A 1 3102 ? 240.703 187.421 239.186 1.00 0.83  ? 3102 LEU A CG    1 
ATOM   13088 C  CD1   . LEU A 1 3102 ? 240.149 186.015 239.305 1.00 0.59  ? 3102 LEU A CD1   1 
ATOM   13089 C  CD2   . LEU A 1 3102 ? 239.601 188.443 239.397 1.00 0.13  ? 3102 LEU A CD2   1 
ATOM   13090 N  N     . TYR A 1 3103 ? 244.632 188.437 241.413 1.00 1.48  ? 3103 TYR A N     1 
ATOM   13091 C  CA    . TYR A 1 3103 ? 245.507 188.555 242.572 1.00 1.46  ? 3103 TYR A CA    1 
ATOM   13092 C  C     . TYR A 1 3103 ? 246.076 189.962 242.699 1.00 1.85  ? 3103 TYR A C     1 
ATOM   13093 O  O     . TYR A 1 3103 ? 246.143 190.520 243.799 1.00 2.49  ? 3103 TYR A O     1 
ATOM   13094 C  CB    . TYR A 1 3103 ? 246.633 187.522 242.488 1.00 2.27  ? 3103 TYR A CB    1 
ATOM   13095 C  CG    . TYR A 1 3103 ? 247.516 187.493 243.712 1.00 2.66  ? 3103 TYR A CG    1 
ATOM   13096 C  CD1   . TYR A 1 3103 ? 247.211 186.681 244.794 1.00 3.16  ? 3103 TYR A CD1   1 
ATOM   13097 C  CD2   . TYR A 1 3103 ? 248.659 188.277 243.782 1.00 2.41  ? 3103 TYR A CD2   1 
ATOM   13098 C  CE1   . TYR A 1 3103 ? 248.016 186.656 245.913 1.00 5.30  ? 3103 TYR A CE1   1 
ATOM   13099 C  CE2   . TYR A 1 3103 ? 249.468 188.258 244.896 1.00 3.82  ? 3103 TYR A CE2   1 
ATOM   13100 C  CZ    . TYR A 1 3103 ? 249.144 187.446 245.958 1.00 7.88  ? 3103 TYR A CZ    1 
ATOM   13101 O  OH    . TYR A 1 3103 ? 249.952 187.426 247.069 1.00 16.23 ? 3103 TYR A OH    1 
ATOM   13102 N  N     . GLN A 1 3104 ? 246.504 190.548 241.580 1.00 3.86  ? 3104 GLN A N     1 
ATOM   13103 C  CA    . GLN A 1 3104 ? 247.082 191.887 241.626 1.00 2.61  ? 3104 GLN A CA    1 
ATOM   13104 C  C     . GLN A 1 3104 ? 246.033 192.922 242.007 1.00 1.55  ? 3104 GLN A C     1 
ATOM   13105 O  O     . GLN A 1 3104 ? 246.312 193.846 242.779 1.00 2.66  ? 3104 GLN A O     1 
ATOM   13106 C  CB    . GLN A 1 3104 ? 247.730 192.222 240.282 1.00 2.82  ? 3104 GLN A CB    1 
ATOM   13107 C  CG    . GLN A 1 3104 ? 248.947 191.368 239.974 1.00 3.42  ? 3104 GLN A CG    1 
ATOM   13108 C  CD    . GLN A 1 3104 ? 249.573 191.689 238.632 1.00 10.19 ? 3104 GLN A CD    1 
ATOM   13109 O  OE1   . GLN A 1 3104 ? 249.066 192.519 237.879 1.00 11.50 ? 3104 GLN A OE1   1 
ATOM   13110 N  NE2   . GLN A 1 3104 ? 250.680 191.027 238.324 1.00 6.58  ? 3104 GLN A NE2   1 
ATOM   13111 N  N     . VAL A 1 3105 ? 244.817 192.780 241.480 1.00 1.28  ? 3105 VAL A N     1 
ATOM   13112 C  CA    . VAL A 1 3105 ? 243.732 193.677 241.871 1.00 1.37  ? 3105 VAL A CA    1 
ATOM   13113 C  C     . VAL A 1 3105 ? 243.429 193.520 243.354 1.00 2.05  ? 3105 VAL A C     1 
ATOM   13114 O  O     . VAL A 1 3105 ? 243.278 194.504 244.084 1.00 6.58  ? 3105 VAL A O     1 
ATOM   13115 C  CB    . VAL A 1 3105 ? 242.482 193.420 241.010 1.00 1.47  ? 3105 VAL A CB    1 
ATOM   13116 C  CG1   . VAL A 1 3105 ? 241.295 194.192 241.558 1.00 1.13  ? 3105 VAL A CG1   1 
ATOM   13117 C  CG2   . VAL A 1 3105 ? 242.741 193.811 239.577 1.00 1.29  ? 3105 VAL A CG2   1 
ATOM   13118 N  N     . GLY A 1 3106 ? 243.347 192.274 243.820 1.00 1.64  ? 3106 GLY A N     1 
ATOM   13119 C  CA    . GLY A 1 3106 ? 243.060 192.039 245.225 1.00 2.08  ? 3106 GLY A CA    1 
ATOM   13120 C  C     . GLY A 1 3106 ? 244.145 192.570 246.143 1.00 1.98  ? 3106 GLY A C     1 
ATOM   13121 O  O     . GLY A 1 3106 ? 243.858 193.225 247.147 1.00 5.64  ? 3106 GLY A O     1 
ATOM   13122 N  N     . LYS A 1 3107 ? 245.407 192.293 245.813 1.00 1.64  ? 3107 LYS A N     1 
ATOM   13123 C  CA    . LYS A 1 3107 ? 246.501 192.755 246.661 1.00 3.09  ? 3107 LYS A CA    1 
ATOM   13124 C  C     . LYS A 1 3107 ? 246.601 194.274 246.652 1.00 5.26  ? 3107 LYS A C     1 
ATOM   13125 O  O     . LYS A 1 3107 ? 246.842 194.896 247.694 1.00 11.53 ? 3107 LYS A O     1 
ATOM   13126 C  CB    . LYS A 1 3107 ? 247.822 192.123 246.219 1.00 3.23  ? 3107 LYS A CB    1 
ATOM   13127 C  CG    . LYS A 1 3107 ? 249.011 192.519 247.081 1.00 8.74  ? 3107 LYS A CG    1 
ATOM   13128 C  CD    . LYS A 1 3107 ? 250.277 191.766 246.689 1.00 14.98 ? 3107 LYS A CD    1 
ATOM   13129 C  CE    . LYS A 1 3107 ? 250.842 192.273 245.371 1.00 17.04 ? 3107 LYS A CE    1 
ATOM   13130 N  NZ    . LYS A 1 3107 ? 252.139 191.630 245.033 1.00 23.24 ? 3107 LYS A NZ    1 
ATOM   13131 N  N     . GLU A 1 3108 ? 246.420 194.891 245.483 1.00 7.40  ? 3108 GLU A N     1 
ATOM   13132 C  CA    . GLU A 1 3108 ? 246.489 196.344 245.398 1.00 10.33 ? 3108 GLU A CA    1 
ATOM   13133 C  C     . GLU A 1 3108 ? 245.321 197.000 246.128 1.00 8.53  ? 3108 GLU A C     1 
ATOM   13134 O  O     . GLU A 1 3108 ? 245.501 198.012 246.812 1.00 12.19 ? 3108 GLU A O     1 
ATOM   13135 C  CB    . GLU A 1 3108 ? 246.522 196.779 243.932 1.00 10.86 ? 3108 GLU A CB    1 
ATOM   13136 C  CG    . GLU A 1 3108 ? 246.596 198.284 243.719 1.00 14.71 ? 3108 GLU A CG    1 
ATOM   13137 C  CD    . GLU A 1 3108 ? 247.923 198.886 244.149 1.00 23.13 ? 3108 GLU A CD    1 
ATOM   13138 O  OE1   . GLU A 1 3108 ? 248.821 198.134 244.584 1.00 22.23 ? 3108 GLU A OE1   1 
ATOM   13139 O  OE2   . GLU A 1 3108 ? 248.063 200.123 244.059 1.00 25.35 ? 3108 GLU A OE2   1 
ATOM   13140 N  N     . PHE A 1 3109 ? 244.120 196.432 245.996 1.00 6.20  ? 3109 PHE A N     1 
ATOM   13141 C  CA    . PHE A 1 3109 ? 242.937 197.058 246.576 1.00 6.04  ? 3109 PHE A CA    1 
ATOM   13142 C  C     . PHE A 1 3109 ? 242.879 196.867 248.088 1.00 5.79  ? 3109 PHE A C     1 
ATOM   13143 O  O     . PHE A 1 3109 ? 242.257 197.676 248.787 1.00 9.91  ? 3109 PHE A O     1 
ATOM   13144 C  CB    . PHE A 1 3109 ? 241.679 196.501 245.907 1.00 4.43  ? 3109 PHE A CB    1 
ATOM   13145 C  CG    . PHE A 1 3109 ? 240.423 197.256 246.236 1.00 5.25  ? 3109 PHE A CG    1 
ATOM   13146 C  CD1   . PHE A 1 3109 ? 239.661 196.925 247.342 1.00 3.33  ? 3109 PHE A CD1   1 
ATOM   13147 C  CD2   . PHE A 1 3109 ? 240.002 198.303 245.428 1.00 2.86  ? 3109 PHE A CD2   1 
ATOM   13148 C  CE1   . PHE A 1 3109 ? 238.508 197.620 247.641 1.00 1.29  ? 3109 PHE A CE1   1 
ATOM   13149 C  CE2   . PHE A 1 3109 ? 238.849 199.003 245.723 1.00 1.63  ? 3109 PHE A CE2   1 
ATOM   13150 C  CZ    . PHE A 1 3109 ? 238.100 198.659 246.830 1.00 3.41  ? 3109 PHE A CZ    1 
ATOM   13151 N  N     . THR A 1 3110 ? 243.517 195.823 248.612 1.00 6.94  ? 3110 THR A N     1 
ATOM   13152 C  CA    . THR A 1 3110 ? 243.509 195.540 250.041 1.00 7.77  ? 3110 THR A CA    1 
ATOM   13153 C  C     . THR A 1 3110 ? 244.738 196.083 250.761 1.00 9.36  ? 3110 THR A C     1 
ATOM   13154 O  O     . THR A 1 3110 ? 245.036 195.640 251.874 1.00 11.55 ? 3110 THR A O     1 
ATOM   13155 C  CB    . THR A 1 3110 ? 243.391 194.034 250.287 1.00 6.05  ? 3110 THR A CB    1 
ATOM   13156 O  OG1   . THR A 1 3110 ? 244.468 193.352 249.632 1.00 9.26  ? 3110 THR A OG1   1 
ATOM   13157 C  CG2   . THR A 1 3110 ? 242.070 193.511 249.747 1.00 3.79  ? 3110 THR A CG2   1 
ATOM   13158 N  N     . SER A 1 3111 ? 245.469 197.015 250.148 1.00 12.13 ? 3111 SER A N     1 
ATOM   13159 C  CA    . SER A 1 3111 ? 246.619 197.610 250.821 1.00 9.04  ? 3111 SER A CA    1 
ATOM   13160 C  C     . SER A 1 3111 ? 246.186 198.408 252.045 1.00 10.50 ? 3111 SER A C     1 
ATOM   13161 O  O     . SER A 1 3111 ? 246.840 198.365 253.093 1.00 12.30 ? 3111 SER A O     1 
ATOM   13162 C  CB    . SER A 1 3111 ? 247.399 198.488 249.844 1.00 14.08 ? 3111 SER A CB    1 
ATOM   13163 O  OG    . SER A 1 3111 ? 247.811 197.744 248.711 1.00 21.74 ? 3111 SER A OG    1 
ATOM   13164 N  N     . LYS A 1 3112 ? 245.080 199.147 251.926 1.00 12.82 ? 3112 LYS A N     1 
ATOM   13165 C  CA    . LYS A 1 3112 ? 244.543 199.884 253.067 1.00 10.95 ? 3112 LYS A CA    1 
ATOM   13166 C  C     . LYS A 1 3112 ? 244.105 198.947 254.184 1.00 10.93 ? 3112 LYS A C     1 
ATOM   13167 O  O     . LYS A 1 3112 ? 244.083 199.340 255.354 1.00 10.79 ? 3112 LYS A O     1 
ATOM   13168 C  CB    . LYS A 1 3112 ? 243.367 200.750 252.618 1.00 18.44 ? 3112 LYS A CB    1 
ATOM   13169 C  CG    . LYS A 1 3112 ? 242.318 199.978 251.833 1.00 17.53 ? 3112 LYS A CG    1 
ATOM   13170 C  CD    . LYS A 1 3112 ? 241.251 200.891 251.249 1.00 23.25 ? 3112 LYS A CD    1 
ATOM   13171 C  CE    . LYS A 1 3112 ? 240.274 200.102 250.387 1.00 20.63 ? 3112 LYS A CE    1 
ATOM   13172 N  NZ    . LYS A 1 3112 ? 239.232 200.966 249.773 1.00 16.50 ? 3112 LYS A NZ    1 
ATOM   13173 N  N     . MET A 1 3113 ? 243.742 197.718 253.833 1.00 16.55 ? 3113 MET A N     1 
ATOM   13174 C  CA    . MET A 1 3113 ? 243.297 196.731 254.805 1.00 10.00 ? 3113 MET A CA    1 
ATOM   13175 C  C     . MET A 1 3113 ? 244.423 196.393 255.776 1.00 12.93 ? 3113 MET A C     1 
ATOM   13176 O  O     . MET A 1 3113 ? 245.601 196.360 255.409 1.00 15.33 ? 3113 MET A O     1 
ATOM   13177 C  CB    . MET A 1 3113 ? 242.844 195.473 254.066 1.00 10.42 ? 3113 MET A CB    1 
ATOM   13178 C  CG    . MET A 1 3113 ? 241.497 195.590 253.374 1.00 8.02  ? 3113 MET A CG    1 
ATOM   13179 S  SD    . MET A 1 3113 ? 240.823 193.974 252.960 1.00 26.88 ? 3113 MET A SD    1 
ATOM   13180 C  CE    . MET A 1 3113 ? 239.447 193.861 254.071 1.00 2.51  ? 3113 MET A CE    1 
ATOM   13181 N  N     . ASP A 1 3114 ? 244.052 196.143 257.032 1.00 16.03 ? 3114 ASP A N     1 
ATOM   13182 C  CA    . ASP A 1 3114 ? 245.008 195.728 258.055 1.00 13.07 ? 3114 ASP A CA    1 
ATOM   13183 C  C     . ASP A 1 3114 ? 244.926 194.210 258.188 1.00 14.48 ? 3114 ASP A C     1 
ATOM   13184 O  O     . ASP A 1 3114 ? 244.324 193.664 259.113 1.00 21.37 ? 3114 ASP A O     1 
ATOM   13185 C  CB    . ASP A 1 3114 ? 244.735 196.438 259.378 1.00 16.90 ? 3114 ASP A CB    1 
ATOM   13186 C  CG    . ASP A 1 3114 ? 245.673 195.993 260.481 1.00 27.93 ? 3114 ASP A CG    1 
ATOM   13187 O  OD1   . ASP A 1 3114 ? 246.903 196.028 260.267 1.00 34.89 ? 3114 ASP A OD1   1 
ATOM   13188 O  OD2   . ASP A 1 3114 ? 245.182 195.609 261.565 1.00 35.12 ? 3114 ASP A OD2   1 
ATOM   13189 N  N     . LEU A 1 3115 ? 245.548 193.520 257.231 1.00 16.47 ? 3115 LEU A N     1 
ATOM   13190 C  CA    . LEU A 1 3115 ? 245.508 192.069 257.150 1.00 10.54 ? 3115 LEU A CA    1 
ATOM   13191 C  C     . LEU A 1 3115 ? 246.788 191.418 257.657 1.00 13.60 ? 3115 LEU A C     1 
ATOM   13192 O  O     . LEU A 1 3115 ? 247.090 190.280 257.279 1.00 19.51 ? 3115 LEU A O     1 
ATOM   13193 C  CB    . LEU A 1 3115 ? 245.234 191.631 255.711 1.00 9.19  ? 3115 LEU A CB    1 
ATOM   13194 C  CG    . LEU A 1 3115 ? 243.960 192.193 255.081 1.00 12.35 ? 3115 LEU A CG    1 
ATOM   13195 C  CD1   . LEU A 1 3115 ? 243.804 191.697 253.652 1.00 8.49  ? 3115 LEU A CD1   1 
ATOM   13196 C  CD2   . LEU A 1 3115 ? 242.743 191.834 255.918 1.00 10.25 ? 3115 LEU A CD2   1 
ATOM   13197 N  N     . GLU A 1 3116 ? 247.542 192.107 258.504 1.00 16.88 ? 3116 GLU A N     1 
ATOM   13198 C  CA    . GLU A 1 3116 ? 248.816 191.598 258.994 1.00 17.74 ? 3116 GLU A CA    1 
ATOM   13199 C  C     . GLU A 1 3116 ? 248.585 190.763 260.248 1.00 19.30 ? 3116 GLU A C     1 
ATOM   13200 O  O     . GLU A 1 3116 ? 248.115 191.277 261.268 1.00 25.53 ? 3116 GLU A O     1 
ATOM   13201 C  CB    . GLU A 1 3116 ? 249.783 192.747 259.278 1.00 16.44 ? 3116 GLU A CB    1 
ATOM   13202 C  CG    . GLU A 1 3116 ? 250.255 193.505 258.036 1.00 22.28 ? 3116 GLU A CG    1 
ATOM   13203 C  CD    . GLU A 1 3116 ? 251.090 192.665 257.075 1.00 27.94 ? 3116 GLU A CD    1 
ATOM   13204 O  OE1   . GLU A 1 3116 ? 251.491 193.205 256.023 1.00 26.68 ? 3116 GLU A OE1   1 
ATOM   13205 O  OE2   . GLU A 1 3116 ? 251.373 191.485 257.371 1.00 26.06 ? 3116 GLU A OE2   1 
ATOM   13206 N  N     . LYS A 1 3117 ? 248.902 189.472 260.163 1.00 20.71 ? 3117 LYS A N     1 
ATOM   13207 C  CA    . LYS A 1 3117 ? 248.826 188.555 261.299 1.00 19.46 ? 3117 LYS A CA    1 
ATOM   13208 C  C     . LYS A 1 3117 ? 250.174 187.860 261.414 1.00 21.75 ? 3117 LYS A C     1 
ATOM   13209 O  O     . LYS A 1 3117 ? 250.405 186.819 260.784 1.00 20.14 ? 3117 LYS A O     1 
ATOM   13210 C  CB    . LYS A 1 3117 ? 247.685 187.550 261.135 1.00 17.46 ? 3117 LYS A CB    1 
ATOM   13211 C  CG    . LYS A 1 3117 ? 247.480 186.661 262.350 1.00 18.18 ? 3117 LYS A CG    1 
ATOM   13212 C  CD    . LYS A 1 3117 ? 246.133 185.953 262.325 1.00 15.71 ? 3117 LYS A CD    1 
ATOM   13213 C  CE    . LYS A 1 3117 ? 246.035 184.978 261.170 1.00 18.64 ? 3117 LYS A CE    1 
ATOM   13214 N  NZ    . LYS A 1 3117 ? 244.728 184.270 261.142 1.00 20.88 ? 3117 LYS A NZ    1 
ATOM   13215 N  N     . PRO A 1 3118 ? 251.098 188.416 262.204 1.00 22.86 ? 3118 PRO A N     1 
ATOM   13216 C  CA    . PRO A 1 3118 ? 252.431 187.801 262.317 1.00 21.71 ? 3118 PRO A CA    1 
ATOM   13217 C  C     . PRO A 1 3118 ? 252.408 186.388 262.870 1.00 24.46 ? 3118 PRO A C     1 
ATOM   13218 O  O     . PRO A 1 3118 ? 253.332 185.612 262.598 1.00 26.25 ? 3118 PRO A O     1 
ATOM   13219 C  CB    . PRO A 1 3118 ? 253.177 188.762 263.255 1.00 18.17 ? 3118 PRO A CB    1 
ATOM   13220 C  CG    . PRO A 1 3118 ? 252.096 189.471 264.007 1.00 20.35 ? 3118 PRO A CG    1 
ATOM   13221 C  CD    . PRO A 1 3118 ? 250.978 189.628 263.027 1.00 21.76 ? 3118 PRO A CD    1 
ATOM   13222 N  N     . ASN A 1 3119 ? 251.381 186.030 263.636 1.00 22.53 ? 3119 ASN A N     1 
ATOM   13223 C  CA    . ASN A 1 3119 ? 251.279 184.702 264.228 1.00 17.70 ? 3119 ASN A CA    1 
ATOM   13224 C  C     . ASN A 1 3119 ? 250.629 183.682 263.302 1.00 23.34 ? 3119 ASN A C     1 
ATOM   13225 O  O     . ASN A 1 3119 ? 250.413 182.542 263.727 1.00 28.02 ? 3119 ASN A O     1 
ATOM   13226 C  CB    . ASN A 1 3119 ? 250.499 184.776 265.543 1.00 20.75 ? 3119 ASN A CB    1 
ATOM   13227 C  CG    . ASN A 1 3119 ? 249.099 185.330 265.364 1.00 24.98 ? 3119 ASN A CG    1 
ATOM   13228 O  OD1   . ASN A 1 3119 ? 248.231 184.684 264.777 1.00 24.39 ? 3119 ASN A OD1   1 
ATOM   13229 N  ND2   . ASN A 1 3119 ? 248.873 186.535 265.872 1.00 27.87 ? 3119 ASN A ND2   1 
ATOM   13230 N  N     . TYR A 1 3120 ? 250.302 184.061 262.068 1.00 23.23 ? 3120 TYR A N     1 
ATOM   13231 C  CA    . TYR A 1 3120 ? 249.674 183.136 261.133 1.00 16.54 ? 3120 TYR A CA    1 
ATOM   13232 C  C     . TYR A 1 3120 ? 250.597 181.960 260.836 1.00 16.24 ? 3120 TYR A C     1 
ATOM   13233 O  O     . TYR A 1 3120 ? 251.806 182.126 260.660 1.00 19.84 ? 3120 TYR A O     1 
ATOM   13234 C  CB    . TYR A 1 3120 ? 249.313 183.876 259.843 1.00 16.95 ? 3120 TYR A CB    1 
ATOM   13235 C  CG    . TYR A 1 3120 ? 248.902 182.993 258.684 1.00 13.70 ? 3120 TYR A CG    1 
ATOM   13236 C  CD1   . TYR A 1 3120 ? 247.625 182.458 258.617 1.00 11.16 ? 3120 TYR A CD1   1 
ATOM   13237 C  CD2   . TYR A 1 3120 ? 249.782 182.717 257.648 1.00 12.07 ? 3120 TYR A CD2   1 
ATOM   13238 C  CE1   . TYR A 1 3120 ? 247.238 181.662 257.558 1.00 12.19 ? 3120 TYR A CE1   1 
ATOM   13239 C  CE2   . TYR A 1 3120 ? 249.406 181.919 256.585 1.00 10.68 ? 3120 TYR A CE2   1 
ATOM   13240 C  CZ    . TYR A 1 3120 ? 248.133 181.395 256.544 1.00 13.96 ? 3120 TYR A CZ    1 
ATOM   13241 O  OH    . TYR A 1 3120 ? 247.751 180.600 255.489 1.00 14.77 ? 3120 TYR A OH    1 
ATOM   13242 N  N     . ILE A 1 3121 ? 250.019 180.761 260.790 1.00 14.53 ? 3121 ILE A N     1 
ATOM   13243 C  CA    . ILE A 1 3121 ? 250.757 179.539 260.485 1.00 15.15 ? 3121 ILE A CA    1 
ATOM   13244 C  C     . ILE A 1 3121 ? 250.397 179.098 259.076 1.00 14.57 ? 3121 ILE A C     1 
ATOM   13245 O  O     . ILE A 1 3121 ? 249.214 178.950 258.746 1.00 18.57 ? 3121 ILE A O     1 
ATOM   13246 C  CB    . ILE A 1 3121 ? 250.454 178.415 261.494 1.00 18.07 ? 3121 ILE A CB    1 
ATOM   13247 C  CG1   . ILE A 1 3121 ? 250.886 178.791 262.913 1.00 17.67 ? 3121 ILE A CG1   1 
ATOM   13248 C  CG2   . ILE A 1 3121 ? 251.130 177.121 261.068 1.00 17.61 ? 3121 ILE A CG2   1 
ATOM   13249 C  CD1   . ILE A 1 3121 ? 249.823 179.509 263.711 1.00 16.02 ? 3121 ILE A CD1   1 
ATOM   13250 N  N     . VAL A 1 3122 ? 251.412 178.881 258.245 1.00 15.33 ? 3122 VAL A N     1 
ATOM   13251 C  CA    . VAL A 1 3122 ? 251.195 178.383 256.890 1.00 12.86 ? 3122 VAL A CA    1 
ATOM   13252 C  C     . VAL A 1 3122 ? 250.870 176.898 256.963 1.00 17.35 ? 3122 VAL A C     1 
ATOM   13253 O  O     . VAL A 1 3122 ? 251.661 176.119 257.515 1.00 24.16 ? 3122 VAL A O     1 
ATOM   13254 C  CB    . VAL A 1 3122 ? 252.414 178.640 255.994 1.00 15.55 ? 3122 VAL A CB    1 
ATOM   13255 C  CG1   . VAL A 1 3122 ? 252.198 178.025 254.623 1.00 18.60 ? 3122 VAL A CG1   1 
ATOM   13256 C  CG2   . VAL A 1 3122 ? 252.677 180.126 255.878 1.00 11.59 ? 3122 VAL A CG2   1 
ATOM   13257 N  N     . PRO A 1 3123 ? 249.731 176.463 256.430 1.00 15.22 ? 3123 PRO A N     1 
ATOM   13258 C  CA    . PRO A 1 3123 ? 249.406 175.035 256.456 1.00 16.28 ? 3123 PRO A CA    1 
ATOM   13259 C  C     . PRO A 1 3123 ? 250.341 174.234 255.563 1.00 22.45 ? 3123 PRO A C     1 
ATOM   13260 O  O     . PRO A 1 3123 ? 250.929 174.756 254.613 1.00 28.63 ? 3123 PRO A O     1 
ATOM   13261 C  CB    . PRO A 1 3123 ? 247.967 174.991 255.930 1.00 19.11 ? 3123 PRO A CB    1 
ATOM   13262 C  CG    . PRO A 1 3123 ? 247.845 176.220 255.095 1.00 15.17 ? 3123 PRO A CG    1 
ATOM   13263 C  CD    . PRO A 1 3123 ? 248.674 177.259 255.788 1.00 16.16 ? 3123 PRO A CD    1 
ATOM   13264 N  N     . ASP A 1 3124 ? 250.479 172.948 255.888 1.00 24.03 ? 3124 ASP A N     1 
ATOM   13265 C  CA    . ASP A 1 3124 ? 251.288 172.055 255.065 1.00 26.05 ? 3124 ASP A CA    1 
ATOM   13266 C  C     . ASP A 1 3124 ? 250.728 171.962 253.652 1.00 30.85 ? 3124 ASP A C     1 
ATOM   13267 O  O     . ASP A 1 3124 ? 251.470 172.021 252.667 1.00 34.66 ? 3124 ASP A O     1 
ATOM   13268 C  CB    . ASP A 1 3124 ? 251.365 170.673 255.713 1.00 24.93 ? 3124 ASP A CB    1 
ATOM   13269 C  CG    . ASP A 1 3124 ? 251.933 170.719 257.117 1.00 33.43 ? 3124 ASP A CG    1 
ATOM   13270 O  OD1   . ASP A 1 3124 ? 253.090 171.164 257.277 1.00 32.17 ? 3124 ASP A OD1   1 
ATOM   13271 O  OD2   . ASP A 1 3124 ? 251.224 170.310 258.062 1.00 34.30 ? 3124 ASP A OD2   1 
ATOM   13272 N  N     . TYR A 1 3125 ? 249.410 171.814 253.534 1.00 28.01 ? 3125 TYR A N     1 
ATOM   13273 C  CA    . TYR A 1 3125 ? 248.737 171.825 252.238 1.00 27.39 ? 3125 TYR A CA    1 
ATOM   13274 C  C     . TYR A 1 3125 ? 248.035 173.169 252.095 1.00 31.86 ? 3125 TYR A C     1 
ATOM   13275 O  O     . TYR A 1 3125 ? 246.974 173.396 252.683 1.00 27.84 ? 3125 TYR A O     1 
ATOM   13276 C  CB    . TYR A 1 3125 ? 247.765 170.655 252.116 1.00 27.23 ? 3125 TYR A CB    1 
ATOM   13277 C  CG    . TYR A 1 3125 ? 246.849 170.728 250.911 1.00 31.00 ? 3125 TYR A CG    1 
ATOM   13278 C  CD1   . TYR A 1 3125 ? 247.248 170.224 249.680 1.00 27.78 ? 3125 TYR A CD1   1 
ATOM   13279 C  CD2   . TYR A 1 3125 ? 245.574 171.277 251.010 1.00 37.24 ? 3125 TYR A CD2   1 
ATOM   13280 C  CE1   . TYR A 1 3125 ? 246.414 170.282 248.578 1.00 30.49 ? 3125 TYR A CE1   1 
ATOM   13281 C  CE2   . TYR A 1 3125 ? 244.735 171.342 249.914 1.00 30.85 ? 3125 TYR A CE2   1 
ATOM   13282 C  CZ    . TYR A 1 3125 ? 245.160 170.841 248.702 1.00 35.26 ? 3125 TYR A CZ    1 
ATOM   13283 O  OH    . TYR A 1 3125 ? 244.327 170.899 247.609 1.00 39.89 ? 3125 TYR A OH    1 
ATOM   13284 N  N     . MET A 1 3126 ? 248.637 174.066 251.329 1.00 35.18 ? 3126 MET A N     1 
ATOM   13285 C  CA    . MET A 1 3126 ? 248.100 175.401 251.084 1.00 22.21 ? 3126 MET A CA    1 
ATOM   13286 C  C     . MET A 1 3126 ? 247.216 175.376 249.844 1.00 22.09 ? 3126 MET A C     1 
ATOM   13287 O  O     . MET A 1 3126 ? 247.686 174.991 248.766 1.00 19.50 ? 3126 MET A O     1 
ATOM   13288 C  CB    . MET A 1 3126 ? 249.231 176.403 250.895 1.00 19.20 ? 3126 MET A CB    1 
ATOM   13289 C  CG    . MET A 1 3126 ? 248.798 177.858 250.788 1.00 19.54 ? 3126 MET A CG    1 
ATOM   13290 S  SD    . MET A 1 3126 ? 248.068 178.526 252.293 1.00 42.38 ? 3126 MET A SD    1 
ATOM   13291 C  CE    . MET A 1 3126 ? 247.088 179.861 251.618 1.00 11.72 ? 3126 MET A CE    1 
ATOM   13292 N  N     . PRO A 1 3127 ? 245.945 175.767 249.949 1.00 22.31 ? 3127 PRO A N     1 
ATOM   13293 C  CA    . PRO A 1 3127 ? 245.047 175.751 248.782 1.00 14.59 ? 3127 PRO A CA    1 
ATOM   13294 C  C     . PRO A 1 3127 ? 245.371 176.867 247.792 1.00 19.05 ? 3127 PRO A C     1 
ATOM   13295 O  O     . PRO A 1 3127 ? 244.633 177.843 247.642 1.00 18.54 ? 3127 PRO A O     1 
ATOM   13296 C  CB    . PRO A 1 3127 ? 243.666 175.911 249.432 1.00 13.73 ? 3127 PRO A CB    1 
ATOM   13297 C  CG    . PRO A 1 3127 ? 243.930 176.720 250.651 1.00 13.63 ? 3127 PRO A CG    1 
ATOM   13298 C  CD    . PRO A 1 3127 ? 245.281 176.295 251.155 1.00 14.96 ? 3127 PRO A CD    1 
ATOM   13299 N  N     . VAL A 1 3128 ? 246.498 176.713 247.099 1.00 18.68 ? 3128 VAL A N     1 
ATOM   13300 C  CA    . VAL A 1 3128 ? 247.017 177.776 246.247 1.00 18.76 ? 3128 VAL A CA    1 
ATOM   13301 C  C     . VAL A 1 3128 ? 246.243 177.813 244.936 1.00 19.53 ? 3128 VAL A C     1 
ATOM   13302 O  O     . VAL A 1 3128 ? 246.074 176.787 244.262 1.00 17.89 ? 3128 VAL A O     1 
ATOM   13303 C  CB    . VAL A 1 3128 ? 248.518 177.570 245.996 1.00 21.65 ? 3128 VAL A CB    1 
ATOM   13304 C  CG1   . VAL A 1 3128 ? 249.041 178.612 245.032 1.00 16.14 ? 3128 VAL A CG1   1 
ATOM   13305 C  CG2   . VAL A 1 3128 ? 249.286 177.613 247.305 1.00 23.30 ? 3128 VAL A CG2   1 
ATOM   13306 N  N     . VAL A 1 3129 ? 245.768 179.001 244.567 1.00 16.84 ? 3129 VAL A N     1 
ATOM   13307 C  CA    . VAL A 1 3129 ? 245.117 179.200 243.280 1.00 9.45  ? 3129 VAL A CA    1 
ATOM   13308 C  C     . VAL A 1 3129 ? 245.910 180.113 242.355 1.00 10.52 ? 3129 VAL A C     1 
ATOM   13309 O  O     . VAL A 1 3129 ? 245.676 180.085 241.136 1.00 10.75 ? 3129 VAL A O     1 
ATOM   13310 C  CB    . VAL A 1 3129 ? 243.682 179.741 243.458 1.00 13.45 ? 3129 VAL A CB    1 
ATOM   13311 C  CG1   . VAL A 1 3129 ? 242.835 178.746 244.232 1.00 10.12 ? 3129 VAL A CG1   1 
ATOM   13312 C  CG2   . VAL A 1 3129 ? 243.698 181.090 244.147 1.00 6.56  ? 3129 VAL A CG2   1 
ATOM   13313 N  N     . TYR A 1 3130 ? 246.833 180.914 242.878 1.00 14.27 ? 3130 TYR A N     1 
ATOM   13314 C  CA    . TYR A 1 3130 ? 247.713 181.758 242.079 1.00 7.86  ? 3130 TYR A CA    1 
ATOM   13315 C  C     . TYR A 1 3130 ? 249.063 181.062 241.961 1.00 15.58 ? 3130 TYR A C     1 
ATOM   13316 O  O     . TYR A 1 3130 ? 249.747 180.847 242.967 1.00 17.60 ? 3130 TYR A O     1 
ATOM   13317 C  CB    . TYR A 1 3130 ? 247.850 183.137 242.720 1.00 7.83  ? 3130 TYR A CB    1 
ATOM   13318 C  CG    . TYR A 1 3130 ? 248.782 184.084 242.001 1.00 8.02  ? 3130 TYR A CG    1 
ATOM   13319 C  CD1   . TYR A 1 3130 ? 248.822 184.143 240.614 1.00 6.55  ? 3130 TYR A CD1   1 
ATOM   13320 C  CD2   . TYR A 1 3130 ? 249.625 184.921 242.717 1.00 5.96  ? 3130 TYR A CD2   1 
ATOM   13321 C  CE1   . TYR A 1 3130 ? 249.679 185.011 239.964 1.00 8.43  ? 3130 TYR A CE1   1 
ATOM   13322 C  CE2   . TYR A 1 3130 ? 250.481 185.789 242.077 1.00 9.53  ? 3130 TYR A CE2   1 
ATOM   13323 C  CZ    . TYR A 1 3130 ? 250.507 185.831 240.703 1.00 11.58 ? 3130 TYR A CZ    1 
ATOM   13324 O  OH    . TYR A 1 3130 ? 251.365 186.701 240.071 1.00 17.42 ? 3130 TYR A OH    1 
ATOM   13325 N  N     . ASP A 1 3131 ? 249.452 180.722 240.727 1.00 18.82 ? 3131 ASP A N     1 
ATOM   13326 C  CA    . ASP A 1 3131 ? 250.648 179.912 240.518 1.00 17.14 ? 3131 ASP A CA    1 
ATOM   13327 C  C     . ASP A 1 3131 ? 251.904 180.587 241.055 1.00 17.84 ? 3131 ASP A C     1 
ATOM   13328 O  O     . ASP A 1 3131 ? 252.822 179.902 241.521 1.00 25.06 ? 3131 ASP A O     1 
ATOM   13329 C  CB    . ASP A 1 3131 ? 250.817 179.596 239.033 1.00 17.34 ? 3131 ASP A CB    1 
ATOM   13330 C  CG    . ASP A 1 3131 ? 249.757 178.646 238.512 1.00 29.35 ? 3131 ASP A CG    1 
ATOM   13331 O  OD1   . ASP A 1 3131 ? 249.258 177.817 239.301 1.00 29.04 ? 3131 ASP A OD1   1 
ATOM   13332 O  OD2   . ASP A 1 3131 ? 249.427 178.725 237.310 1.00 30.56 ? 3131 ASP A OD2   1 
ATOM   13333 N  N     . LYS A 1 3132 ? 251.970 181.915 241.010 1.00 11.57 ? 3132 LYS A N     1 
ATOM   13334 C  CA    . LYS A 1 3132 ? 253.141 182.638 241.485 1.00 15.48 ? 3132 LYS A CA    1 
ATOM   13335 C  C     . LYS A 1 3132 ? 252.965 183.192 242.892 1.00 15.22 ? 3132 LYS A C     1 
ATOM   13336 O  O     . LYS A 1 3132 ? 253.662 184.142 243.262 1.00 17.53 ? 3132 LYS A O     1 
ATOM   13337 C  CB    . LYS A 1 3132 ? 253.504 183.766 240.519 1.00 14.46 ? 3132 LYS A CB    1 
ATOM   13338 C  CG    . LYS A 1 3132 ? 253.985 183.284 239.164 1.00 16.00 ? 3132 LYS A CG    1 
ATOM   13339 C  CD    . LYS A 1 3132 ? 254.487 184.442 238.318 1.00 19.22 ? 3132 LYS A CD    1 
ATOM   13340 C  CE    . LYS A 1 3132 ? 253.347 185.297 237.794 1.00 23.98 ? 3132 LYS A CE    1 
ATOM   13341 N  NZ    . LYS A 1 3132 ? 253.842 186.361 236.878 1.00 28.86 ? 3132 LYS A NZ    1 
ATOM   13342 N  N     . LEU A 1 3133 ? 252.053 182.635 243.677 1.00 16.63 ? 3133 LEU A N     1 
ATOM   13343 C  CA    . LEU A 1 3133 ? 251.957 182.984 245.086 1.00 13.94 ? 3133 LEU A CA    1 
ATOM   13344 C  C     . LEU A 1 3133 ? 253.231 182.541 245.798 1.00 15.53 ? 3133 LEU A C     1 
ATOM   13345 O  O     . LEU A 1 3133 ? 253.654 181.387 245.627 1.00 24.70 ? 3133 LEU A O     1 
ATOM   13346 C  CB    . LEU A 1 3133 ? 250.731 182.330 245.718 1.00 12.74 ? 3133 LEU A CB    1 
ATOM   13347 C  CG    . LEU A 1 3133 ? 250.433 182.650 247.186 1.00 14.68 ? 3133 LEU A CG    1 
ATOM   13348 C  CD1   . LEU A 1 3133 ? 250.097 184.122 247.358 1.00 8.00  ? 3133 LEU A CD1   1 
ATOM   13349 C  CD2   . LEU A 1 3133 ? 249.308 181.778 247.710 1.00 14.93 ? 3133 LEU A CD2   1 
ATOM   13350 N  N     . PRO A 1 3134 ? 253.877 183.410 246.583 1.00 14.50 ? 3134 PRO A N     1 
ATOM   13351 C  CA    . PRO A 1 3134 ? 255.161 183.047 247.199 1.00 17.62 ? 3134 PRO A CA    1 
ATOM   13352 C  C     . PRO A 1 3134 ? 255.103 181.800 248.069 1.00 24.94 ? 3134 PRO A C     1 
ATOM   13353 O  O     . PRO A 1 3134 ? 254.108 181.553 248.757 1.00 28.76 ? 3134 PRO A O     1 
ATOM   13354 C  CB    . PRO A 1 3134 ? 255.494 184.295 248.021 1.00 16.35 ? 3134 PRO A CB    1 
ATOM   13355 C  CG    . PRO A 1 3134 ? 254.961 185.396 247.167 1.00 11.93 ? 3134 PRO A CG    1 
ATOM   13356 C  CD    . PRO A 1 3134 ? 253.628 184.860 246.676 1.00 12.32 ? 3134 PRO A CD    1 
ATOM   13357 N  N     . GLN A 1 3135 ? 256.180 181.008 248.030 1.00 24.15 ? 3135 GLN A N     1 
ATOM   13358 C  CA    . GLN A 1 3135 ? 256.184 179.698 248.679 1.00 20.90 ? 3135 GLN A CA    1 
ATOM   13359 C  C     . GLN A 1 3135 ? 255.910 179.764 250.177 1.00 24.98 ? 3135 GLN A C     1 
ATOM   13360 O  O     . GLN A 1 3135 ? 255.172 178.899 250.679 1.00 34.41 ? 3135 GLN A O     1 
ATOM   13361 C  CB    . GLN A 1 3135 ? 257.506 178.980 248.384 1.00 28.82 ? 3135 GLN A CB    1 
ATOM   13362 C  CG    . GLN A 1 3135 ? 257.772 178.721 246.908 1.00 30.92 ? 3135 GLN A CG    1 
ATOM   13363 C  CD    . GLN A 1 3135 ? 256.684 177.893 246.257 1.00 36.49 ? 3135 GLN A CD    1 
ATOM   13364 O  OE1   . GLN A 1 3135 ? 256.379 176.786 246.701 1.00 31.66 ? 3135 GLN A OE1   1 
ATOM   13365 N  NE2   . GLN A 1 3135 ? 256.095 178.424 245.190 1.00 36.83 ? 3135 GLN A NE2   1 
ATOM   13366 N  N     . PRO A 1 3136 ? 256.510 180.668 250.952 1.00 23.02 ? 3136 PRO A N     1 
ATOM   13367 C  CA    . PRO A 1 3136 ? 256.012 180.928 252.309 1.00 17.82 ? 3136 PRO A CA    1 
ATOM   13368 C  C     . PRO A 1 3136 ? 255.013 182.071 252.317 1.00 23.86 ? 3136 PRO A C     1 
ATOM   13369 O  O     . PRO A 1 3136 ? 255.384 183.215 252.619 1.00 26.08 ? 3136 PRO A O     1 
ATOM   13370 C  CB    . PRO A 1 3136 ? 257.285 181.288 253.084 1.00 17.89 ? 3136 PRO A CB    1 
ATOM   13371 C  CG    . PRO A 1 3136 ? 258.202 181.878 252.054 1.00 22.41 ? 3136 PRO A CG    1 
ATOM   13372 C  CD    . PRO A 1 3136 ? 257.729 181.452 250.678 1.00 22.13 ? 3136 PRO A CD    1 
ATOM   13373 N  N     . PRO A 1 3137 ? 253.747 181.822 251.976 1.00 20.54 ? 3137 PRO A N     1 
ATOM   13374 C  CA    . PRO A 1 3137 ? 252.793 182.932 251.884 1.00 18.78 ? 3137 PRO A CA    1 
ATOM   13375 C  C     . PRO A 1 3137 ? 252.575 183.583 253.241 1.00 16.63 ? 3137 PRO A C     1 
ATOM   13376 O  O     . PRO A 1 3137 ? 252.616 182.924 254.281 1.00 21.88 ? 3137 PRO A O     1 
ATOM   13377 C  CB    . PRO A 1 3137 ? 251.516 182.258 251.375 1.00 17.21 ? 3137 PRO A CB    1 
ATOM   13378 C  CG    . PRO A 1 3137 ? 251.600 180.883 251.916 1.00 20.42 ? 3137 PRO A CG    1 
ATOM   13379 C  CD    . PRO A 1 3137 ? 253.062 180.518 251.945 1.00 20.73 ? 3137 PRO A CD    1 
ATOM   13380 N  N     . SER A 1 3138 ? 252.353 184.893 253.222 1.00 16.22 ? 3138 SER A N     1 
ATOM   13381 C  CA    . SER A 1 3138 ? 251.984 185.613 254.427 1.00 12.00 ? 3138 SER A CA    1 
ATOM   13382 C  C     . SER A 1 3138 ? 250.468 185.563 254.603 1.00 11.70 ? 3138 SER A C     1 
ATOM   13383 O  O     . SER A 1 3138 ? 249.736 185.053 253.752 1.00 12.77 ? 3138 SER A O     1 
ATOM   13384 C  CB    . SER A 1 3138 ? 252.493 187.052 254.370 1.00 13.81 ? 3138 SER A CB    1 
ATOM   13385 O  OG    . SER A 1 3138 ? 251.801 187.797 253.386 1.00 16.35 ? 3138 SER A OG    1 
ATOM   13386 N  N     . HIS A 1 3139 ? 249.988 186.094 255.730 1.00 15.81 ? 3139 HIS A N     1 
ATOM   13387 C  CA    . HIS A 1 3139 ? 248.551 186.091 255.986 1.00 8.51  ? 3139 HIS A CA    1 
ATOM   13388 C  C     . HIS A 1 3139 ? 247.805 186.934 254.958 1.00 8.22  ? 3139 HIS A C     1 
ATOM   13389 O  O     . HIS A 1 3139 ? 246.732 186.542 254.486 1.00 9.81  ? 3139 HIS A O     1 
ATOM   13390 C  CB    . HIS A 1 3139 ? 248.265 186.588 257.401 1.00 10.10 ? 3139 HIS A CB    1 
ATOM   13391 C  CG    . HIS A 1 3139 ? 246.806 186.694 257.718 1.00 14.43 ? 3139 HIS A CG    1 
ATOM   13392 N  ND1   . HIS A 1 3139 ? 246.169 187.900 257.906 1.00 10.29 ? 3139 HIS A ND1   1 
ATOM   13393 C  CD2   . HIS A 1 3139 ? 245.856 185.739 257.859 1.00 7.89  ? 3139 HIS A CD2   1 
ATOM   13394 C  CE1   . HIS A 1 3139 ? 244.891 187.685 258.163 1.00 10.97 ? 3139 HIS A CE1   1 
ATOM   13395 N  NE2   . HIS A 1 3139 ? 244.675 186.383 258.139 1.00 10.84 ? 3139 HIS A NE2   1 
ATOM   13396 N  N     . ARG A 1 3140 ? 248.357 188.097 254.605 1.00 10.43 ? 3140 ARG A N     1 
ATOM   13397 C  CA    . ARG A 1 3140 ? 247.757 188.913 253.553 1.00 6.38  ? 3140 ARG A CA    1 
ATOM   13398 C  C     . ARG A 1 3140 ? 247.785 188.190 252.213 1.00 5.06  ? 3140 ARG A C     1 
ATOM   13399 O  O     . ARG A 1 3140 ? 246.816 188.244 251.449 1.00 6.83  ? 3140 ARG A O     1 
ATOM   13400 C  CB    . ARG A 1 3140 ? 248.483 190.255 253.461 1.00 7.13  ? 3140 ARG A CB    1 
ATOM   13401 C  CG    . ARG A 1 3140 ? 247.850 191.245 252.504 1.00 6.84  ? 3140 ARG A CG    1 
ATOM   13402 C  CD    . ARG A 1 3140 ? 248.740 192.458 252.319 1.00 3.91  ? 3140 ARG A CD    1 
ATOM   13403 N  NE    . ARG A 1 3140 ? 248.761 193.307 253.505 1.00 7.09  ? 3140 ARG A NE    1 
ATOM   13404 C  CZ    . ARG A 1 3140 ? 247.782 194.130 253.856 1.00 10.20 ? 3140 ARG A CZ    1 
ATOM   13405 N  NH1   . ARG A 1 3140 ? 246.689 194.258 253.122 1.00 9.52  ? 3140 ARG A NH1   1 
ATOM   13406 N  NH2   . ARG A 1 3140 ? 247.903 194.841 254.972 1.00 12.95 ? 3140 ARG A NH2   1 
ATOM   13407 N  N     . GLU A 1 3141 ? 248.892 187.510 251.916 1.00 10.99 ? 3141 GLU A N     1 
ATOM   13408 C  CA    . GLU A 1 3141 ? 248.987 186.736 250.683 1.00 9.43  ? 3141 GLU A CA    1 
ATOM   13409 C  C     . GLU A 1 3141 ? 247.954 185.618 250.653 1.00 7.17  ? 3141 GLU A C     1 
ATOM   13410 O  O     . GLU A 1 3141 ? 247.379 185.321 249.601 1.00 6.59  ? 3141 GLU A O     1 
ATOM   13411 C  CB    . GLU A 1 3141 ? 250.399 186.174 250.544 1.00 8.42  ? 3141 GLU A CB    1 
ATOM   13412 C  CG    . GLU A 1 3141 ? 251.422 187.194 250.094 1.00 11.07 ? 3141 GLU A CG    1 
ATOM   13413 C  CD    . GLU A 1 3141 ? 252.838 186.768 250.417 1.00 24.11 ? 3141 GLU A CD    1 
ATOM   13414 O  OE1   . GLU A 1 3141 ? 253.372 185.901 249.704 1.00 22.37 ? 3141 GLU A OE1   1 
ATOM   13415 O  OE2   . GLU A 1 3141 ? 253.426 187.313 251.373 1.00 25.16 ? 3141 GLU A OE2   1 
ATOM   13416 N  N     . ALA A 1 3142 ? 247.714 184.979 251.800 1.00 7.60  ? 3142 ALA A N     1 
ATOM   13417 C  CA    . ALA A 1 3142 ? 246.687 183.947 251.874 1.00 6.16  ? 3142 ALA A CA    1 
ATOM   13418 C  C     . ALA A 1 3142 ? 245.293 184.538 251.697 1.00 5.58  ? 3142 ALA A C     1 
ATOM   13419 O  O     . ALA A 1 3142 ? 244.435 183.927 251.050 1.00 7.38  ? 3142 ALA A O     1 
ATOM   13420 C  CB    . ALA A 1 3142 ? 246.792 183.199 253.202 1.00 5.29  ? 3142 ALA A CB    1 
ATOM   13421 N  N     . ILE A 1 3143 ? 245.048 185.721 252.266 1.00 3.28  ? 3143 ILE A N     1 
ATOM   13422 C  CA    . ILE A 1 3143 ? 243.731 186.347 252.161 1.00 2.69  ? 3143 ILE A CA    1 
ATOM   13423 C  C     . ILE A 1 3143 ? 243.409 186.676 250.710 1.00 4.17  ? 3143 ILE A C     1 
ATOM   13424 O  O     . ILE A 1 3143 ? 242.327 186.353 250.206 1.00 6.59  ? 3143 ILE A O     1 
ATOM   13425 C  CB    . ILE A 1 3143 ? 243.658 187.602 253.049 1.00 3.18  ? 3143 ILE A CB    1 
ATOM   13426 C  CG1   . ILE A 1 3143 ? 243.548 187.217 254.524 1.00 2.97  ? 3143 ILE A CG1   1 
ATOM   13427 C  CG2   . ILE A 1 3143 ? 242.480 188.475 252.640 1.00 3.18  ? 3143 ILE A CG2   1 
ATOM   13428 C  CD1   . ILE A 1 3143 ? 242.182 186.720 254.920 1.00 2.15  ? 3143 ILE A CD1   1 
ATOM   13429 N  N     . VAL A 1 3144 ? 244.345 187.324 250.015 1.00 5.58  ? 3144 VAL A N     1 
ATOM   13430 C  CA    . VAL A 1 3144 ? 244.124 187.671 248.615 1.00 2.55  ? 3144 VAL A CA    1 
ATOM   13431 C  C     . VAL A 1 3144 ? 244.002 186.410 247.772 1.00 2.32  ? 3144 VAL A C     1 
ATOM   13432 O  O     . VAL A 1 3144 ? 243.190 186.344 246.842 1.00 3.32  ? 3144 VAL A O     1 
ATOM   13433 C  CB    . VAL A 1 3144 ? 245.248 188.594 248.109 1.00 3.30  ? 3144 VAL A CB    1 
ATOM   13434 C  CG1   . VAL A 1 3144 ? 245.067 188.896 246.633 1.00 1.67  ? 3144 VAL A CG1   1 
ATOM   13435 C  CG2   . VAL A 1 3144 ? 245.278 189.881 248.916 1.00 2.52  ? 3144 VAL A CG2   1 
ATOM   13436 N  N     . ASN A 1 3145 ? 244.792 185.384 248.096 1.00 3.49  ? 3145 ASN A N     1 
ATOM   13437 C  CA    . ASN A 1 3145 ? 244.664 184.103 247.411 1.00 3.08  ? 3145 ASN A CA    1 
ATOM   13438 C  C     . ASN A 1 3145 ? 243.274 183.515 247.609 1.00 2.42  ? 3145 ASN A C     1 
ATOM   13439 O  O     . ASN A 1 3145 ? 242.687 182.956 246.676 1.00 2.60  ? 3145 ASN A O     1 
ATOM   13440 C  CB    . ASN A 1 3145 ? 245.735 183.135 247.916 1.00 3.09  ? 3145 ASN A CB    1 
ATOM   13441 C  CG    . ASN A 1 3145 ? 245.855 181.896 247.058 1.00 7.59  ? 3145 ASN A CG    1 
ATOM   13442 O  OD1   . ASN A 1 3145 ? 246.208 181.973 245.884 1.00 14.25 ? 3145 ASN A OD1   1 
ATOM   13443 N  ND2   . ASN A 1 3145 ? 245.559 180.743 247.642 1.00 9.44  ? 3145 ASN A ND2   1 
ATOM   13444 N  N     . SER A 1 3146 ? 242.730 183.631 248.823 1.00 2.60  ? 3146 SER A N     1 
ATOM   13445 C  CA    . SER A 1 3146 ? 241.370 183.168 249.078 1.00 1.88  ? 3146 SER A CA    1 
ATOM   13446 C  C     . SER A 1 3146 ? 240.348 184.013 248.327 1.00 1.27  ? 3146 SER A C     1 
ATOM   13447 O  O     . SER A 1 3146 ? 239.327 183.494 247.864 1.00 0.60  ? 3146 SER A O     1 
ATOM   13448 C  CB    . SER A 1 3146 ? 241.083 183.185 250.579 1.00 3.24  ? 3146 SER A CB    1 
ATOM   13449 O  OG    . SER A 1 3146 ? 241.999 182.366 251.281 1.00 7.96  ? 3146 SER A OG    1 
ATOM   13450 N  N     . CYS A 1 3147 ? 240.601 185.319 248.206 1.00 2.91  ? 3147 CYS A N     1 
ATOM   13451 C  CA    . CYS A 1 3147 ? 239.708 186.178 247.439 1.00 0.74  ? 3147 CYS A CA    1 
ATOM   13452 C  C     . CYS A 1 3147 ? 239.673 185.765 245.974 1.00 0.51  ? 3147 CYS A C     1 
ATOM   13453 O  O     . CYS A 1 3147 ? 238.615 185.797 245.337 1.00 0.45  ? 3147 CYS A O     1 
ATOM   13454 C  CB    . CYS A 1 3147 ? 240.132 187.640 247.576 1.00 0.71  ? 3147 CYS A CB    1 
ATOM   13455 S  SG    . CYS A 1 3147 ? 239.901 188.353 249.218 1.00 4.88  ? 3147 CYS A SG    1 
ATOM   13456 N  N     . VAL A 1 3148 ? 240.825 185.384 245.419 1.00 0.53  ? 3148 VAL A N     1 
ATOM   13457 C  CA    . VAL A 1 3148 ? 240.858 184.890 244.046 1.00 0.44  ? 3148 VAL A CA    1 
ATOM   13458 C  C     . VAL A 1 3148 ? 240.077 183.589 243.933 1.00 0.35  ? 3148 VAL A C     1 
ATOM   13459 O  O     . VAL A 1 3148 ? 239.335 183.376 242.967 1.00 0.37  ? 3148 VAL A O     1 
ATOM   13460 C  CB    . VAL A 1 3148 ? 242.315 184.721 243.569 1.00 0.67  ? 3148 VAL A CB    1 
ATOM   13461 C  CG1   . VAL A 1 3148 ? 242.353 184.142 242.165 1.00 0.96  ? 3148 VAL A CG1   1 
ATOM   13462 C  CG2   . VAL A 1 3148 ? 243.044 186.047 243.617 1.00 0.46  ? 3148 VAL A CG2   1 
ATOM   13463 N  N     . PHE A 1 3149 ? 240.220 182.705 244.924 1.00 0.45  ? 3149 PHE A N     1 
ATOM   13464 C  CA    . PHE A 1 3149 ? 239.536 181.418 244.883 1.00 0.34  ? 3149 PHE A CA    1 
ATOM   13465 C  C     . PHE A 1 3149 ? 238.022 181.592 244.863 1.00 0.43  ? 3149 PHE A C     1 
ATOM   13466 O  O     . PHE A 1 3149 ? 237.317 180.863 244.156 1.00 0.49  ? 3149 PHE A O     1 
ATOM   13467 C  CB    . PHE A 1 3149 ? 239.952 180.559 246.077 1.00 0.57  ? 3149 PHE A CB    1 
ATOM   13468 C  CG    . PHE A 1 3149 ? 239.120 179.318 246.246 1.00 0.80  ? 3149 PHE A CG    1 
ATOM   13469 C  CD1   . PHE A 1 3149 ? 239.410 178.175 245.523 1.00 0.49  ? 3149 PHE A CD1   1 
ATOM   13470 C  CD2   . PHE A 1 3149 ? 238.045 179.297 247.120 1.00 0.77  ? 3149 PHE A CD2   1 
ATOM   13471 C  CE1   . PHE A 1 3149 ? 238.648 177.034 245.670 1.00 0.71  ? 3149 PHE A CE1   1 
ATOM   13472 C  CE2   . PHE A 1 3149 ? 237.278 178.158 247.266 1.00 0.55  ? 3149 PHE A CE2   1 
ATOM   13473 C  CZ    . PHE A 1 3149 ? 237.580 177.026 246.543 1.00 0.72  ? 3149 PHE A CZ    1 
ATOM   13474 N  N     . VAL A 1 3150 ? 237.505 182.544 245.643 1.00 0.38  ? 3150 VAL A N     1 
ATOM   13475 C  CA    . VAL A 1 3150 ? 236.058 182.730 245.737 1.00 0.27  ? 3150 VAL A CA    1 
ATOM   13476 C  C     . VAL A 1 3150 ? 235.479 183.114 244.383 1.00 0.45  ? 3150 VAL A C     1 
ATOM   13477 O  O     . VAL A 1 3150 ? 234.433 182.598 243.969 1.00 1.31  ? 3150 VAL A O     1 
ATOM   13478 C  CB    . VAL A 1 3150 ? 235.725 183.777 246.816 1.00 0.24  ? 3150 VAL A CB    1 
ATOM   13479 C  CG1   . VAL A 1 3150 ? 234.263 184.161 246.749 1.00 0.14  ? 3150 VAL A CG1   1 
ATOM   13480 C  CG2   . VAL A 1 3150 ? 236.075 183.248 248.196 1.00 0.19  ? 3150 VAL A CG2   1 
ATOM   13481 N  N     . HIS A 1 3151 ? 236.151 184.020 243.669 1.00 0.51  ? 3151 HIS A N     1 
ATOM   13482 C  CA    . HIS A 1 3151 ? 235.676 184.432 242.353 1.00 0.19  ? 3151 HIS A CA    1 
ATOM   13483 C  C     . HIS A 1 3151 ? 235.651 183.264 241.377 1.00 0.72  ? 3151 HIS A C     1 
ATOM   13484 O  O     . HIS A 1 3151 ? 234.694 183.104 240.613 1.00 0.87  ? 3151 HIS A O     1 
ATOM   13485 C  CB    . HIS A 1 3151 ? 236.555 185.562 241.813 1.00 0.21  ? 3151 HIS A CB    1 
ATOM   13486 C  CG    . HIS A 1 3151 ? 236.101 186.098 240.492 1.00 0.09  ? 3151 HIS A CG    1 
ATOM   13487 N  ND1   . HIS A 1 3151 ? 235.058 186.988 240.367 1.00 0.06  ? 3151 HIS A ND1   1 
ATOM   13488 C  CD2   . HIS A 1 3151 ? 236.552 185.870 239.237 1.00 0.08  ? 3151 HIS A CD2   1 
ATOM   13489 C  CE1   . HIS A 1 3151 ? 234.883 187.283 239.093 1.00 0.10  ? 3151 HIS A CE1   1 
ATOM   13490 N  NE2   . HIS A 1 3151 ? 235.778 186.617 238.386 1.00 0.24  ? 3151 HIS A NE2   1 
ATOM   13491 N  N     . GLN A 1 3152 ? 236.695 182.434 241.391 1.00 0.80  ? 3152 GLN A N     1 
ATOM   13492 C  CA    . GLN A 1 3152 ? 236.753 181.289 240.491 1.00 1.08  ? 3152 GLN A CA    1 
ATOM   13493 C  C     . GLN A 1 3152 ? 235.719 180.226 240.837 1.00 1.54  ? 3152 GLN A C     1 
ATOM   13494 O  O     . GLN A 1 3152 ? 235.363 179.422 239.969 1.00 2.85  ? 3152 GLN A O     1 
ATOM   13495 C  CB    . GLN A 1 3152 ? 238.158 180.687 240.508 1.00 1.38  ? 3152 GLN A CB    1 
ATOM   13496 C  CG    . GLN A 1 3152 ? 239.258 181.717 240.341 1.00 3.76  ? 3152 GLN A CG    1 
ATOM   13497 C  CD    . GLN A 1 3152 ? 240.502 181.154 239.691 1.00 5.55  ? 3152 GLN A CD    1 
ATOM   13498 O  OE1   . GLN A 1 3152 ? 241.043 181.735 238.751 1.00 7.24  ? 3152 GLN A OE1   1 
ATOM   13499 N  NE2   . GLN A 1 3152 ? 240.970 180.019 240.193 1.00 6.54  ? 3152 GLN A NE2   1 
ATOM   13500 N  N     . THR A 1 3153 ? 235.236 180.204 242.079 1.00 1.16  ? 3153 THR A N     1 
ATOM   13501 C  CA    . THR A 1 3153 ? 234.202 179.248 242.458 1.00 1.34  ? 3153 THR A CA    1 
ATOM   13502 C  C     . THR A 1 3153 ? 232.884 179.537 241.747 1.00 1.56  ? 3153 THR A C     1 
ATOM   13503 O  O     . THR A 1 3153 ? 232.157 178.603 241.389 1.00 2.67  ? 3153 THR A O     1 
ATOM   13504 C  CB    . THR A 1 3153 ? 234.020 179.262 243.979 1.00 1.01  ? 3153 THR A CB    1 
ATOM   13505 O  OG1   . THR A 1 3153 ? 235.177 178.694 244.602 1.00 1.35  ? 3153 THR A OG1   1 
ATOM   13506 C  CG2   . THR A 1 3153 ? 232.805 178.458 244.392 1.00 4.69  ? 3153 THR A CG2   1 
ATOM   13507 N  N     . LEU A 1 3154 ? 232.572 180.814 241.512 1.00 1.05  ? 3154 LEU A N     1 
ATOM   13508 C  CA    . LEU A 1 3154 ? 231.337 181.155 240.815 1.00 1.37  ? 3154 LEU A CA    1 
ATOM   13509 C  C     . LEU A 1 3154 ? 231.340 180.650 239.380 1.00 2.31  ? 3154 LEU A C     1 
ATOM   13510 O  O     . LEU A 1 3154 ? 230.283 180.288 238.849 1.00 4.71  ? 3154 LEU A O     1 
ATOM   13511 C  CB    . LEU A 1 3154 ? 231.101 182.665 240.849 1.00 0.88  ? 3154 LEU A CB    1 
ATOM   13512 C  CG    . LEU A 1 3154 ? 230.423 183.234 242.098 1.00 0.32  ? 3154 LEU A CG    1 
ATOM   13513 C  CD1   . LEU A 1 3154 ? 229.014 182.675 242.238 1.00 0.51  ? 3154 LEU A CD1   1 
ATOM   13514 C  CD2   . LEU A 1 3154 ? 231.225 183.000 243.365 1.00 0.19  ? 3154 LEU A CD2   1 
ATOM   13515 N  N     . HIS A 1 3155 ? 232.506 180.629 238.730 1.00 2.10  ? 3155 HIS A N     1 
ATOM   13516 C  CA    . HIS A 1 3155 ? 232.593 180.029 237.404 1.00 2.51  ? 3155 HIS A CA    1 
ATOM   13517 C  C     . HIS A 1 3155 ? 232.301 178.537 237.457 1.00 3.85  ? 3155 HIS A C     1 
ATOM   13518 O  O     . HIS A 1 3155 ? 231.585 178.004 236.603 1.00 9.38  ? 3155 HIS A O     1 
ATOM   13519 C  CB    . HIS A 1 3155 ? 233.969 180.291 236.797 1.00 2.34  ? 3155 HIS A CB    1 
ATOM   13520 C  CG    . HIS A 1 3155 ? 234.184 181.712 236.385 1.00 2.41  ? 3155 HIS A CG    1 
ATOM   13521 N  ND1   . HIS A 1 3155 ? 235.134 182.521 236.968 1.00 3.06  ? 3155 HIS A ND1   1 
ATOM   13522 C  CD2   . HIS A 1 3155 ? 233.569 182.470 235.448 1.00 2.78  ? 3155 HIS A CD2   1 
ATOM   13523 C  CE1   . HIS A 1 3155 ? 235.097 183.716 236.407 1.00 4.16  ? 3155 HIS A CE1   1 
ATOM   13524 N  NE2   . HIS A 1 3155 ? 234.155 183.712 235.482 1.00 5.66  ? 3155 HIS A NE2   1 
ATOM   13525 N  N     . GLN A 1 3156 ? 232.847 177.845 238.460 1.00 4.89  ? 3156 GLN A N     1 
ATOM   13526 C  CA    . GLN A 1 3156 ? 232.498 176.444 238.666 1.00 6.76  ? 3156 GLN A CA    1 
ATOM   13527 C  C     . GLN A 1 3156 ? 231.021 176.297 239.002 1.00 7.89  ? 3156 GLN A C     1 
ATOM   13528 O  O     . GLN A 1 3156 ? 230.357 175.370 238.525 1.00 12.57 ? 3156 GLN A O     1 
ATOM   13529 C  CB    . GLN A 1 3156 ? 233.363 175.843 239.777 1.00 6.61  ? 3156 GLN A CB    1 
ATOM   13530 C  CG    . GLN A 1 3156 ? 234.880 176.046 239.651 1.00 6.76  ? 3156 GLN A CG    1 
ATOM   13531 C  CD    . GLN A 1 3156 ? 235.515 175.441 238.396 1.00 20.87 ? 3156 GLN A CD    1 
ATOM   13532 O  OE1   . GLN A 1 3156 ? 234.913 175.379 237.324 1.00 15.97 ? 3156 GLN A OE1   1 
ATOM   13533 N  NE2   . GLN A 1 3156 ? 236.756 174.992 238.542 1.00 23.60 ? 3156 GLN A NE2   1 
ATOM   13534 N  N     . ALA A 1 3157 ? 230.493 177.206 239.823 1.00 8.49  ? 3157 ALA A N     1 
ATOM   13535 C  CA    . ALA A 1 3157 ? 229.088 177.143 240.207 1.00 7.96  ? 3157 ALA A CA    1 
ATOM   13536 C  C     . ALA A 1 3157 ? 228.172 177.336 239.007 1.00 8.77  ? 3157 ALA A C     1 
ATOM   13537 O  O     . ALA A 1 3157 ? 227.170 176.628 238.864 1.00 9.76  ? 3157 ALA A O     1 
ATOM   13538 C  CB    . ALA A 1 3157 ? 228.795 178.190 241.284 1.00 3.53  ? 3157 ALA A CB    1 
ATOM   13539 N  N     . ASN A 1 3158 ? 228.493 178.293 238.131 1.00 8.74  ? 3158 ASN A N     1 
ATOM   13540 C  CA    . ASN A 1 3158 ? 227.683 178.487 236.933 1.00 6.76  ? 3158 ASN A CA    1 
ATOM   13541 C  C     . ASN A 1 3158 ? 227.732 177.263 236.030 1.00 10.20 ? 3158 ASN A C     1 
ATOM   13542 O  O     . ASN A 1 3158 ? 226.720 176.884 235.431 1.00 13.59 ? 3158 ASN A O     1 
ATOM   13543 C  CB    . ASN A 1 3158 ? 228.140 179.730 236.172 1.00 5.30  ? 3158 ASN A CB    1 
ATOM   13544 C  CG    . ASN A 1 3158 ? 227.516 181.004 236.704 1.00 4.90  ? 3158 ASN A CG    1 
ATOM   13545 O  OD1   . ASN A 1 3158 ? 226.827 180.993 237.720 1.00 5.80  ? 3158 ASN A OD1   1 
ATOM   13546 N  ND2   . ASN A 1 3158 ? 227.741 182.108 236.003 1.00 4.01  ? 3158 ASN A ND2   1 
ATOM   13547 N  N     . ALA A 1 3159 ? 228.905 176.633 235.920 1.00 14.92 ? 3159 ALA A N     1 
ATOM   13548 C  CA    . ALA A 1 3159 ? 229.044 175.458 235.068 1.00 10.26 ? 3159 ALA A CA    1 
ATOM   13549 C  C     . ALA A 1 3159 ? 228.159 174.314 235.548 1.00 11.93 ? 3159 ALA A C     1 
ATOM   13550 O  O     . ALA A 1 3159 ? 227.557 173.604 234.736 1.00 20.24 ? 3159 ALA A O     1 
ATOM   13551 C  CB    . ALA A 1 3159 ? 230.508 175.023 235.015 1.00 9.65  ? 3159 ALA A CB    1 
ATOM   13552 N  N     . ARG A 1 3160 ? 228.073 174.116 236.866 1.00 13.16 ? 3160 ARG A N     1 
ATOM   13553 C  CA    . ARG A 1 3160 ? 227.243 173.040 237.400 1.00 13.82 ? 3160 ARG A CA    1 
ATOM   13554 C  C     . ARG A 1 3160 ? 225.766 173.269 237.101 1.00 18.41 ? 3160 ARG A C     1 
ATOM   13555 O  O     . ARG A 1 3160 ? 225.052 172.335 236.721 1.00 29.79 ? 3160 ARG A O     1 
ATOM   13556 C  CB    . ARG A 1 3160 ? 227.474 172.893 238.903 1.00 16.52 ? 3160 ARG A CB    1 
ATOM   13557 C  CG    . ARG A 1 3160 ? 228.690 172.050 239.251 1.00 22.74 ? 3160 ARG A CG    1 
ATOM   13558 C  CD    . ARG A 1 3160 ? 228.807 171.806 240.748 1.00 26.00 ? 3160 ARG A CD    1 
ATOM   13559 N  NE    . ARG A 1 3160 ? 227.547 171.390 241.351 1.00 22.17 ? 3160 ARG A NE    1 
ATOM   13560 C  CZ    . ARG A 1 3160 ? 226.967 172.006 242.371 1.00 29.63 ? 3160 ARG A CZ    1 
ATOM   13561 N  NH1   . ARG A 1 3160 ? 227.505 173.079 242.927 1.00 28.48 ? 3160 ARG A NH1   1 
ATOM   13562 N  NH2   . ARG A 1 3160 ? 225.821 171.530 242.853 1.00 29.11 ? 3160 ARG A NH2   1 
ATOM   13563 N  N     . LEU A 1 3161 ? 225.280 174.500 237.272 1.00 11.73 ? 3161 LEU A N     1 
ATOM   13564 C  CA    . LEU A 1 3161 ? 223.881 174.772 236.955 1.00 13.32 ? 3161 LEU A CA    1 
ATOM   13565 C  C     . LEU A 1 3161 ? 223.634 174.741 235.452 1.00 16.01 ? 3161 LEU A C     1 
ATOM   13566 O  O     . LEU A 1 3161 ? 222.572 174.297 235.003 1.00 18.29 ? 3161 LEU A O     1 
ATOM   13567 C  CB    . LEU A 1 3161 ? 223.442 176.111 237.546 1.00 9.56  ? 3161 LEU A CB    1 
ATOM   13568 C  CG    . LEU A 1 3161 ? 223.082 176.153 239.035 1.00 12.87 ? 3161 LEU A CG    1 
ATOM   13569 C  CD1   . LEU A 1 3161 ? 224.299 176.019 239.933 1.00 14.14 ? 3161 LEU A CD1   1 
ATOM   13570 C  CD2   . LEU A 1 3161 ? 222.313 177.426 239.355 1.00 10.13 ? 3161 LEU A CD2   1 
ATOM   13571 N  N     . ALA A 1 3162 ? 224.600 175.212 234.658 1.00 14.73 ? 3162 ALA A N     1 
ATOM   13572 C  CA    . ALA A 1 3162 ? 224.443 175.166 233.210 1.00 14.62 ? 3162 ALA A CA    1 
ATOM   13573 C  C     . ALA A 1 3162 ? 224.379 173.730 232.706 1.00 23.17 ? 3162 ALA A C     1 
ATOM   13574 O  O     . ALA A 1 3162 ? 223.560 173.407 231.837 1.00 26.41 ? 3162 ALA A O     1 
ATOM   13575 C  CB    . ALA A 1 3162 ? 225.584 175.925 232.533 1.00 13.75 ? 3162 ALA A CB    1 
ATOM   13576 N  N     . LYS A 1 3163 ? 225.226 172.850 233.246 1.00 22.29 ? 3163 LYS A N     1 
ATOM   13577 C  CA    . LYS A 1 3163 ? 225.221 171.453 232.826 1.00 20.36 ? 3163 LYS A CA    1 
ATOM   13578 C  C     . LYS A 1 3163 ? 223.943 170.728 233.229 1.00 20.32 ? 3163 LYS A C     1 
ATOM   13579 O  O     . LYS A 1 3163 ? 223.611 169.706 232.621 1.00 33.45 ? 3163 LYS A O     1 
ATOM   13580 C  CB    . LYS A 1 3163 ? 226.444 170.728 233.394 1.00 22.27 ? 3163 LYS A CB    1 
ATOM   13581 C  CG    . LYS A 1 3163 ? 226.248 170.163 234.790 1.00 23.28 ? 3163 LYS A CG    1 
ATOM   13582 C  CD    . LYS A 1 3163 ? 227.563 169.696 235.390 1.00 24.66 ? 3163 LYS A CD    1 
ATOM   13583 C  CE    . LYS A 1 3163 ? 227.382 169.246 236.831 1.00 26.49 ? 3163 LYS A CE    1 
ATOM   13584 N  NZ    . LYS A 1 3163 ? 226.345 168.182 236.954 1.00 27.22 ? 3163 LYS A NZ    1 
ATOM   13585 N  N     . ARG A 1 3164 ? 223.222 171.230 234.231 1.00 17.17 ? 3164 ARG A N     1 
ATOM   13586 C  CA    . ARG A 1 3164 ? 221.934 170.676 234.626 1.00 19.08 ? 3164 ARG A CA    1 
ATOM   13587 C  C     . ARG A 1 3164 ? 220.762 171.398 233.978 1.00 19.53 ? 3164 ARG A C     1 
ATOM   13588 O  O     . ARG A 1 3164 ? 219.611 171.137 234.337 1.00 17.95 ? 3164 ARG A O     1 
ATOM   13589 C  CB    . ARG A 1 3164 ? 221.780 170.715 236.150 1.00 16.31 ? 3164 ARG A CB    1 
ATOM   13590 C  CG    . ARG A 1 3164 ? 222.896 170.038 236.920 1.00 24.93 ? 3164 ARG A CG    1 
ATOM   13591 C  CD    . ARG A 1 3164 ? 222.501 169.834 238.376 1.00 28.02 ? 3164 ARG A CD    1 
ATOM   13592 N  NE    . ARG A 1 3164 ? 222.932 170.938 239.225 1.00 34.36 ? 3164 ARG A NE    1 
ATOM   13593 C  CZ    . ARG A 1 3164 ? 224.191 171.186 239.561 1.00 32.44 ? 3164 ARG A CZ    1 
ATOM   13594 N  NH1   . ARG A 1 3164 ? 225.182 170.406 239.162 1.00 28.65 ? 3164 ARG A NH1   1 
ATOM   13595 N  NH2   . ARG A 1 3164 ? 224.463 172.243 240.321 1.00 28.55 ? 3164 ARG A NH2   1 
ATOM   13596 N  N     . GLY A 1 3165 ? 221.027 172.307 233.043 1.00 22.72 ? 3165 GLY A N     1 
ATOM   13597 C  CA    . GLY A 1 3165 ? 219.970 173.069 232.415 1.00 18.89 ? 3165 GLY A CA    1 
ATOM   13598 C  C     . GLY A 1 3165 ? 219.477 174.253 233.211 1.00 21.51 ? 3165 GLY A C     1 
ATOM   13599 O  O     . GLY A 1 3165 ? 218.517 174.907 232.788 1.00 20.86 ? 3165 GLY A O     1 
ATOM   13600 N  N     . GLY A 1 3166 ? 220.096 174.550 234.350 1.00 23.67 ? 3166 GLY A N     1 
ATOM   13601 C  CA    . GLY A 1 3166 ? 219.687 175.693 235.136 1.00 16.23 ? 3166 GLY A CA    1 
ATOM   13602 C  C     . GLY A 1 3166 ? 220.100 177.004 234.493 1.00 16.63 ? 3166 GLY A C     1 
ATOM   13603 O  O     . GLY A 1 3166 ? 220.995 177.065 233.652 1.00 12.52 ? 3166 GLY A O     1 
ATOM   13604 N  N     . ARG A 1 3167 ? 219.425 178.070 234.907 1.00 17.29 ? 3167 ARG A N     1 
ATOM   13605 C  CA    . ARG A 1 3167 ? 219.690 179.399 234.375 1.00 14.43 ? 3167 ARG A CA    1 
ATOM   13606 C  C     . ARG A 1 3167 ? 220.832 180.032 235.158 1.00 12.62 ? 3167 ARG A C     1 
ATOM   13607 O  O     . ARG A 1 3167 ? 220.809 180.058 236.392 1.00 12.34 ? 3167 ARG A O     1 
ATOM   13608 C  CB    . ARG A 1 3167 ? 218.434 180.265 234.463 1.00 17.76 ? 3167 ARG A CB    1 
ATOM   13609 C  CG    . ARG A 1 3167 ? 217.403 179.998 233.376 1.00 22.17 ? 3167 ARG A CG    1 
ATOM   13610 C  CD    . ARG A 1 3167 ? 216.655 178.690 233.628 1.00 27.57 ? 3167 ARG A CD    1 
ATOM   13611 N  NE    . ARG A 1 3167 ? 215.623 178.437 232.632 1.00 30.45 ? 3167 ARG A NE    1 
ATOM   13612 C  CZ    . ARG A 1 3167 ? 214.377 178.878 232.722 1.00 26.46 ? 3167 ARG A CZ    1 
ATOM   13613 N  NH1   . ARG A 1 3167 ? 213.967 179.573 233.771 1.00 23.22 ? 3167 ARG A NH1   1 
ATOM   13614 N  NH2   . ARG A 1 3167 ? 213.520 178.608 231.742 1.00 24.11 ? 3167 ARG A NH2   1 
ATOM   13615 N  N     . THR A 1 3168 ? 221.835 180.532 234.443 1.00 7.96  ? 3168 THR A N     1 
ATOM   13616 C  CA    . THR A 1 3168 ? 223.006 181.131 235.066 1.00 8.86  ? 3168 THR A CA    1 
ATOM   13617 C  C     . THR A 1 3168 ? 223.203 182.544 234.540 1.00 7.26  ? 3168 THR A C     1 
ATOM   13618 O  O     . THR A 1 3168 ? 222.808 182.868 233.417 1.00 8.22  ? 3168 THR A O     1 
ATOM   13619 C  CB    . THR A 1 3168 ? 224.283 180.308 234.809 1.00 6.86  ? 3168 THR A CB    1 
ATOM   13620 O  OG1   . THR A 1 3168 ? 224.584 180.306 233.408 1.00 10.53 ? 3168 THR A OG1   1 
ATOM   13621 C  CG2   . THR A 1 3168 ? 224.100 178.881 235.283 1.00 10.96 ? 3168 THR A CG2   1 
ATOM   13622 N  N     . MET A 1 3169 ? 223.816 183.383 235.369 1.00 6.64  ? 3169 MET A N     1 
ATOM   13623 C  CA    . MET A 1 3169 ? 224.129 184.754 235.005 1.00 4.45  ? 3169 MET A CA    1 
ATOM   13624 C  C     . MET A 1 3169 ? 225.638 184.929 234.940 1.00 3.81  ? 3169 MET A C     1 
ATOM   13625 O  O     . MET A 1 3169 ? 226.387 184.290 235.684 1.00 4.17  ? 3169 MET A O     1 
ATOM   13626 C  CB    . MET A 1 3169 ? 223.515 185.743 235.997 1.00 3.89  ? 3169 MET A CB    1 
ATOM   13627 C  CG    . MET A 1 3169 ? 222.000 185.691 236.001 1.00 4.90  ? 3169 MET A CG    1 
ATOM   13628 S  SD    . MET A 1 3169 ? 221.268 186.391 234.514 1.00 22.67 ? 3169 MET A SD    1 
ATOM   13629 C  CE    . MET A 1 3169 ? 219.531 186.229 234.900 1.00 12.39 ? 3169 MET A CE    1 
ATOM   13630 N  N     . ALA A 1 3170 ? 226.077 185.796 234.030 1.00 3.39  ? 3170 ALA A N     1 
ATOM   13631 C  CA    . ALA A 1 3170 ? 227.500 185.938 233.749 1.00 2.43  ? 3170 ALA A CA    1 
ATOM   13632 C  C     . ALA A 1 3170 ? 228.259 186.429 234.974 1.00 1.35  ? 3170 ALA A C     1 
ATOM   13633 O  O     . ALA A 1 3170 ? 227.800 187.312 235.703 1.00 1.97  ? 3170 ALA A O     1 
ATOM   13634 C  CB    . ALA A 1 3170 ? 227.708 186.905 232.583 1.00 2.36  ? 3170 ALA A CB    1 
ATOM   13635 N  N     . ILE A 1 3171 ? 229.430 185.845 235.198 1.00 0.93  ? 3171 ILE A N     1 
ATOM   13636 C  CA    . ILE A 1 3171 ? 230.345 186.281 236.243 1.00 0.72  ? 3171 ILE A CA    1 
ATOM   13637 C  C     . ILE A 1 3171 ? 231.404 187.157 235.590 1.00 1.09  ? 3171 ILE A C     1 
ATOM   13638 O  O     . ILE A 1 3171 ? 232.098 186.722 234.663 1.00 2.75  ? 3171 ILE A O     1 
ATOM   13639 C  CB    . ILE A 1 3171 ? 230.978 185.087 236.973 1.00 2.12  ? 3171 ILE A CB    1 
ATOM   13640 C  CG1   . ILE A 1 3171 ? 229.889 184.201 237.583 1.00 1.57  ? 3171 ILE A CG1   1 
ATOM   13641 C  CG2   . ILE A 1 3171 ? 231.938 185.570 238.048 1.00 0.77  ? 3171 ILE A CG2   1 
ATOM   13642 C  CD1   . ILE A 1 3171 ? 228.944 184.940 238.500 1.00 0.84  ? 3171 ILE A CD1   1 
ATOM   13643 N  N     . THR A 1 3172 ? 231.523 188.386 236.067 1.00 0.71  ? 3172 THR A N     1 
ATOM   13644 C  CA    . THR A 1 3172 ? 232.343 189.415 235.453 1.00 0.78  ? 3172 THR A CA    1 
ATOM   13645 C  C     . THR A 1 3172 ? 233.351 189.958 236.457 1.00 0.18  ? 3172 THR A C     1 
ATOM   13646 O  O     . THR A 1 3172 ? 233.201 189.759 237.668 1.00 0.15  ? 3172 THR A O     1 
ATOM   13647 C  CB    . THR A 1 3172 ? 231.467 190.562 234.923 1.00 0.53  ? 3172 THR A CB    1 
ATOM   13648 O  OG1   . THR A 1 3172 ? 230.973 191.342 236.018 1.00 0.88  ? 3172 THR A OG1   1 
ATOM   13649 C  CG2   . THR A 1 3172 ? 230.294 190.017 234.126 1.00 1.21  ? 3172 THR A CG2   1 
ATOM   13650 N  N     . PRO A 1 3173 ? 234.405 190.630 235.988 1.00 0.39  ? 3173 PRO A N     1 
ATOM   13651 C  CA    . PRO A 1 3173 ? 235.330 191.282 236.928 1.00 0.27  ? 3173 PRO A CA    1 
ATOM   13652 C  C     . PRO A 1 3173 ? 234.662 192.307 237.826 1.00 0.07  ? 3173 PRO A C     1 
ATOM   13653 O  O     . PRO A 1 3173 ? 235.182 192.587 238.912 1.00 0.05  ? 3173 PRO A O     1 
ATOM   13654 C  CB    . PRO A 1 3173 ? 236.364 191.935 236.001 1.00 0.19  ? 3173 PRO A CB    1 
ATOM   13655 C  CG    . PRO A 1 3173 ? 236.339 191.092 234.782 1.00 0.12  ? 3173 PRO A CG    1 
ATOM   13656 C  CD    . PRO A 1 3173 ? 234.907 190.689 234.604 1.00 0.17  ? 3173 PRO A CD    1 
ATOM   13657 N  N     . ARG A 1 3174 ? 233.532 192.879 237.411 1.00 0.12  ? 3174 ARG A N     1 
ATOM   13658 C  CA    . ARG A 1 3174 ? 232.817 193.805 238.279 1.00 0.20  ? 3174 ARG A CA    1 
ATOM   13659 C  C     . ARG A 1 3174 ? 232.256 193.105 239.510 1.00 0.11  ? 3174 ARG A C     1 
ATOM   13660 O  O     . ARG A 1 3174 ? 232.066 193.744 240.550 1.00 0.09  ? 3174 ARG A O     1 
ATOM   13661 C  CB    . ARG A 1 3174 ? 231.710 194.507 237.498 1.00 0.34  ? 3174 ARG A CB    1 
ATOM   13662 C  CG    . ARG A 1 3174 ? 232.239 195.465 236.452 1.00 0.60  ? 3174 ARG A CG    1 
ATOM   13663 C  CD    . ARG A 1 3174 ? 231.192 196.464 236.020 1.00 0.71  ? 3174 ARG A CD    1 
ATOM   13664 N  NE    . ARG A 1 3174 ? 230.834 197.383 237.090 1.00 0.84  ? 3174 ARG A NE    1 
ATOM   13665 C  CZ    . ARG A 1 3174 ? 229.874 198.292 237.002 1.00 2.53  ? 3174 ARG A CZ    1 
ATOM   13666 N  NH1   . ARG A 1 3174 ? 229.160 198.436 235.899 1.00 1.64  ? 3174 ARG A NH1   1 
ATOM   13667 N  NH2   . ARG A 1 3174 ? 229.626 199.079 238.046 1.00 3.35  ? 3174 ARG A NH2   1 
ATOM   13668 N  N     . HIS A 1 3175 ? 231.981 191.804 239.414 1.00 0.13  ? 3175 HIS A N     1 
ATOM   13669 C  CA    . HIS A 1 3175 ? 231.654 191.030 240.607 1.00 0.06  ? 3175 HIS A CA    1 
ATOM   13670 C  C     . HIS A 1 3175 ? 232.836 190.983 241.568 1.00 0.06  ? 3175 HIS A C     1 
ATOM   13671 O  O     . HIS A 1 3175 ? 232.662 191.112 242.784 1.00 0.10  ? 3175 HIS A O     1 
ATOM   13672 C  CB    . HIS A 1 3175 ? 231.233 189.615 240.220 1.00 0.17  ? 3175 HIS A CB    1 
ATOM   13673 C  CG    . HIS A 1 3175 ? 229.941 189.545 239.470 1.00 0.22  ? 3175 HIS A CG    1 
ATOM   13674 N  ND1   . HIS A 1 3175 ? 229.835 189.875 238.136 1.00 0.34  ? 3175 HIS A ND1   1 
ATOM   13675 C  CD2   . HIS A 1 3175 ? 228.702 189.162 239.862 1.00 0.23  ? 3175 HIS A CD2   1 
ATOM   13676 C  CE1   . HIS A 1 3175 ? 228.587 189.709 237.742 1.00 0.76  ? 3175 HIS A CE1   1 
ATOM   13677 N  NE2   . HIS A 1 3175 ? 227.879 189.277 238.770 1.00 0.64  ? 3175 HIS A NE2   1 
ATOM   13678 N  N     . TYR A 1 3176 ? 234.045 190.784 241.038 1.00 0.05  ? 3176 TYR A N     1 
ATOM   13679 C  CA    . TYR A 1 3176 ? 235.238 190.762 241.878 1.00 0.04  ? 3176 TYR A CA    1 
ATOM   13680 C  C     . TYR A 1 3176 ? 235.494 192.124 242.510 1.00 0.05  ? 3176 TYR A C     1 
ATOM   13681 O  O     . TYR A 1 3176 ? 235.826 192.213 243.696 1.00 0.04  ? 3176 TYR A O     1 
ATOM   13682 C  CB    . TYR A 1 3176 ? 236.445 190.309 241.053 1.00 0.06  ? 3176 TYR A CB    1 
ATOM   13683 C  CG    . TYR A 1 3176 ? 237.700 190.073 241.858 1.00 0.05  ? 3176 TYR A CG    1 
ATOM   13684 C  CD1   . TYR A 1 3176 ? 237.859 188.916 242.604 1.00 0.08  ? 3176 TYR A CD1   1 
ATOM   13685 C  CD2   . TYR A 1 3176 ? 238.735 191.000 241.860 1.00 0.07  ? 3176 TYR A CD2   1 
ATOM   13686 C  CE1   . TYR A 1 3176 ? 239.003 188.690 243.336 1.00 0.14  ? 3176 TYR A CE1   1 
ATOM   13687 C  CE2   . TYR A 1 3176 ? 239.885 190.782 242.591 1.00 0.09  ? 3176 TYR A CE2   1 
ATOM   13688 C  CZ    . TYR A 1 3176 ? 240.012 189.624 243.328 1.00 0.13  ? 3176 TYR A CZ    1 
ATOM   13689 O  OH    . TYR A 1 3176 ? 241.150 189.394 244.060 1.00 0.51  ? 3176 TYR A OH    1 
ATOM   13690 N  N     . LEU A 1 3177 ? 235.353 193.196 241.728 1.00 0.12  ? 3177 LEU A N     1 
ATOM   13691 C  CA    . LEU A 1 3177 ? 235.491 194.538 242.283 1.00 0.09  ? 3177 LEU A CA    1 
ATOM   13692 C  C     . LEU A 1 3177 ? 234.414 194.807 243.321 1.00 0.09  ? 3177 LEU A C     1 
ATOM   13693 O  O     . LEU A 1 3177 ? 234.673 195.445 244.348 1.00 0.13  ? 3177 LEU A O     1 
ATOM   13694 C  CB    . LEU A 1 3177 ? 235.443 195.573 241.162 1.00 0.08  ? 3177 LEU A CB    1 
ATOM   13695 C  CG    . LEU A 1 3177 ? 236.669 195.574 240.252 1.00 0.16  ? 3177 LEU A CG    1 
ATOM   13696 C  CD1   . LEU A 1 3177 ? 236.336 196.181 238.902 1.00 0.29  ? 3177 LEU A CD1   1 
ATOM   13697 C  CD2   . LEU A 1 3177 ? 237.823 196.313 240.910 1.00 0.10  ? 3177 LEU A CD2   1 
ATOM   13698 N  N     . ASP A 1 3178 ? 233.197 194.324 243.070 1.00 0.07  ? 3178 ASP A N     1 
ATOM   13699 C  CA    . ASP A 1 3178 ? 232.150 194.374 244.081 1.00 0.08  ? 3178 ASP A CA    1 
ATOM   13700 C  C     . ASP A 1 3178 ? 232.564 193.613 245.333 1.00 0.12  ? 3178 ASP A C     1 
ATOM   13701 O  O     . ASP A 1 3178 ? 232.340 194.077 246.455 1.00 0.22  ? 3178 ASP A O     1 
ATOM   13702 C  CB    . ASP A 1 3178 ? 230.856 193.803 243.505 1.00 0.23  ? 3178 ASP A CB    1 
ATOM   13703 C  CG    . ASP A 1 3178 ? 229.631 194.528 243.990 1.00 3.95  ? 3178 ASP A CG    1 
ATOM   13704 O  OD1   . ASP A 1 3178 ? 229.699 195.136 245.077 1.00 9.80  ? 3178 ASP A OD1   1 
ATOM   13705 O  OD2   . ASP A 1 3178 ? 228.600 194.496 243.287 1.00 11.55 ? 3178 ASP A OD2   1 
ATOM   13706 N  N     . PHE A 1 3179 ? 233.182 192.445 245.154 1.00 0.09  ? 3179 PHE A N     1 
ATOM   13707 C  CA    . PHE A 1 3179 ? 233.576 191.609 246.283 1.00 0.03  ? 3179 PHE A CA    1 
ATOM   13708 C  C     . PHE A 1 3179 ? 234.609 192.310 247.161 1.00 0.05  ? 3179 PHE A C     1 
ATOM   13709 O  O     . PHE A 1 3179 ? 234.420 192.439 248.374 1.00 0.12  ? 3179 PHE A O     1 
ATOM   13710 C  CB    . PHE A 1 3179 ? 234.110 190.273 245.754 1.00 0.04  ? 3179 PHE A CB    1 
ATOM   13711 C  CG    . PHE A 1 3179 ? 234.776 189.408 246.792 1.00 0.04  ? 3179 PHE A CG    1 
ATOM   13712 C  CD1   . PHE A 1 3179 ? 234.280 189.317 248.079 1.00 0.03  ? 3179 PHE A CD1   1 
ATOM   13713 C  CD2   . PHE A 1 3179 ? 235.898 188.672 246.466 1.00 0.11  ? 3179 PHE A CD2   1 
ATOM   13714 C  CE1   . PHE A 1 3179 ? 234.897 188.520 249.017 1.00 0.13  ? 3179 PHE A CE1   1 
ATOM   13715 C  CE2   . PHE A 1 3179 ? 236.515 187.870 247.403 1.00 0.21  ? 3179 PHE A CE2   1 
ATOM   13716 C  CZ    . PHE A 1 3179 ? 236.013 187.794 248.680 1.00 0.12  ? 3179 PHE A CZ    1 
ATOM   13717 N  N     . ILE A 1 3180 ? 235.704 192.784 246.563 1.00 0.07  ? 3180 ILE A N     1 
ATOM   13718 C  CA    . ILE A 1 3180 ? 236.769 193.374 247.369 1.00 0.13  ? 3180 ILE A CA    1 
ATOM   13719 C  C     . ILE A 1 3180 ? 236.332 194.706 247.958 1.00 0.12  ? 3180 ILE A C     1 
ATOM   13720 O  O     . ILE A 1 3180 ? 236.783 195.089 249.044 1.00 0.16  ? 3180 ILE A O     1 
ATOM   13721 C  CB    . ILE A 1 3180 ? 238.061 193.514 246.542 1.00 0.27  ? 3180 ILE A CB    1 
ATOM   13722 C  CG1   . ILE A 1 3180 ? 237.814 194.365 245.297 1.00 0.28  ? 3180 ILE A CG1   1 
ATOM   13723 C  CG2   . ILE A 1 3180 ? 238.603 192.142 246.172 1.00 0.06  ? 3180 ILE A CG2   1 
ATOM   13724 C  CD1   . ILE A 1 3180 ? 238.990 194.440 244.368 1.00 0.55  ? 3180 ILE A CD1   1 
ATOM   13725 N  N     . ASN A 1 3181 ? 235.457 195.434 247.265 1.00 0.24  ? 3181 ASN A N     1 
ATOM   13726 C  CA    . ASN A 1 3181 ? 234.916 196.670 247.816 1.00 0.61  ? 3181 ASN A CA    1 
ATOM   13727 C  C     . ASN A 1 3181 ? 234.135 196.391 249.096 1.00 0.42  ? 3181 ASN A C     1 
ATOM   13728 O  O     . ASN A 1 3181 ? 234.340 197.051 250.119 1.00 0.89  ? 3181 ASN A O     1 
ATOM   13729 C  CB    . ASN A 1 3181 ? 234.030 197.361 246.776 1.00 1.50  ? 3181 ASN A CB    1 
ATOM   13730 C  CG    . ASN A 1 3181 ? 233.596 198.750 247.197 1.00 6.20  ? 3181 ASN A CG    1 
ATOM   13731 O  OD1   . ASN A 1 3181 ? 233.926 199.219 248.284 1.00 13.03 ? 3181 ASN A OD1   1 
ATOM   13732 N  ND2   . ASN A 1 3181 ? 232.835 199.413 246.334 1.00 11.22 ? 3181 ASN A ND2   1 
ATOM   13733 N  N     . HIS A 1 3182 ? 233.250 195.393 249.058 1.00 0.20  ? 3182 HIS A N     1 
ATOM   13734 C  CA    . HIS A 1 3182 ? 232.506 195.014 250.253 1.00 0.26  ? 3182 HIS A CA    1 
ATOM   13735 C  C     . HIS A 1 3182 ? 233.438 194.503 251.343 1.00 0.51  ? 3182 HIS A C     1 
ATOM   13736 O  O     . HIS A 1 3182 ? 233.197 194.735 252.533 1.00 2.11  ? 3182 HIS A O     1 
ATOM   13737 C  CB    . HIS A 1 3182 ? 231.458 193.955 249.905 1.00 0.24  ? 3182 HIS A CB    1 
ATOM   13738 C  CG    . HIS A 1 3182 ? 230.228 194.510 249.259 1.00 0.47  ? 3182 HIS A CG    1 
ATOM   13739 N  ND1   . HIS A 1 3182 ? 229.565 193.858 248.245 1.00 0.28  ? 3182 HIS A ND1   1 
ATOM   13740 C  CD2   . HIS A 1 3182 ? 229.529 195.645 249.499 1.00 0.73  ? 3182 HIS A CD2   1 
ATOM   13741 C  CE1   . HIS A 1 3182 ? 228.520 194.575 247.873 1.00 0.43  ? 3182 HIS A CE1   1 
ATOM   13742 N  NE2   . HIS A 1 3182 ? 228.474 195.662 248.620 1.00 0.69  ? 3182 HIS A NE2   1 
ATOM   13743 N  N     . TYR A 1 3183 ? 234.504 193.802 250.958 1.00 0.18  ? 3183 TYR A N     1 
ATOM   13744 C  CA    . TYR A 1 3183 ? 235.444 193.277 251.943 1.00 0.42  ? 3183 TYR A CA    1 
ATOM   13745 C  C     . TYR A 1 3183 ? 236.127 194.407 252.703 1.00 0.88  ? 3183 TYR A C     1 
ATOM   13746 O  O     . TYR A 1 3183 ? 236.265 194.351 253.929 1.00 1.89  ? 3183 TYR A O     1 
ATOM   13747 C  CB    . TYR A 1 3183 ? 236.467 192.375 251.254 1.00 0.67  ? 3183 TYR A CB    1 
ATOM   13748 C  CG    . TYR A 1 3183 ? 237.389 191.625 252.192 1.00 0.81  ? 3183 TYR A CG    1 
ATOM   13749 C  CD1   . TYR A 1 3183 ? 237.000 191.316 253.485 1.00 0.96  ? 3183 TYR A CD1   1 
ATOM   13750 C  CD2   . TYR A 1 3183 ? 238.644 191.213 251.769 1.00 1.08  ? 3183 TYR A CD2   1 
ATOM   13751 C  CE1   . TYR A 1 3183 ? 237.843 190.629 254.338 1.00 0.92  ? 3183 TYR A CE1   1 
ATOM   13752 C  CE2   . TYR A 1 3183 ? 239.489 190.524 252.609 1.00 2.33  ? 3183 TYR A CE2   1 
ATOM   13753 C  CZ    . TYR A 1 3183 ? 239.084 190.234 253.892 1.00 1.59  ? 3183 TYR A CZ    1 
ATOM   13754 O  OH    . TYR A 1 3183 ? 239.928 189.548 254.731 1.00 1.92  ? 3183 TYR A OH    1 
ATOM   13755 N  N     . ALA A 1 3184 ? 236.552 195.451 251.991 1.00 1.26  ? 3184 ALA A N     1 
ATOM   13756 C  CA    . ALA A 1 3184 ? 237.191 196.586 252.648 1.00 1.49  ? 3184 ALA A CA    1 
ATOM   13757 C  C     . ALA A 1 3184 ? 236.214 197.320 253.562 1.00 2.00  ? 3184 ALA A C     1 
ATOM   13758 O  O     . ALA A 1 3184 ? 236.563 197.701 254.685 1.00 3.30  ? 3184 ALA A O     1 
ATOM   13759 C  CB    . ALA A 1 3184 ? 237.769 197.539 251.601 1.00 1.85  ? 3184 ALA A CB    1 
ATOM   13760 N  N     . ASN A 1 3185 ? 234.981 197.527 253.093 1.00 1.92  ? 3185 ASN A N     1 
ATOM   13761 C  CA    . ASN A 1 3185 ? 234.000 198.272 253.875 1.00 1.74  ? 3185 ASN A CA    1 
ATOM   13762 C  C     . ASN A 1 3185 ? 233.594 197.509 255.131 1.00 4.64  ? 3185 ASN A C     1 
ATOM   13763 O  O     . ASN A 1 3185 ? 233.575 198.070 256.233 1.00 7.65  ? 3185 ASN A O     1 
ATOM   13764 C  CB    . ASN A 1 3185 ? 232.774 198.584 253.019 1.00 1.88  ? 3185 ASN A CB    1 
ATOM   13765 C  CG    . ASN A 1 3185 ? 233.121 199.366 251.771 1.00 3.20  ? 3185 ASN A CG    1 
ATOM   13766 O  OD1   . ASN A 1 3185 ? 234.265 199.773 251.577 1.00 5.44  ? 3185 ASN A OD1   1 
ATOM   13767 N  ND2   . ASN A 1 3185 ? 232.131 199.577 250.914 1.00 5.55  ? 3185 ASN A ND2   1 
ATOM   13768 N  N     . LEU A 1 3186 ? 233.258 196.226 254.981 1.00 4.45  ? 3186 LEU A N     1 
ATOM   13769 C  CA    . LEU A 1 3186 ? 232.838 195.428 256.128 1.00 3.00  ? 3186 LEU A CA    1 
ATOM   13770 C  C     . LEU A 1 3186 ? 233.961 195.281 257.145 1.00 4.55  ? 3186 LEU A C     1 
ATOM   13771 O  O     . LEU A 1 3186 ? 233.723 195.348 258.356 1.00 9.63  ? 3186 LEU A O     1 
ATOM   13772 C  CB    . LEU A 1 3186 ? 232.351 194.058 255.660 1.00 1.84  ? 3186 LEU A CB    1 
ATOM   13773 C  CG    . LEU A 1 3186 ? 231.016 194.058 254.916 1.00 2.75  ? 3186 LEU A CG    1 
ATOM   13774 C  CD1   . LEU A 1 3186 ? 230.666 192.668 254.421 1.00 1.97  ? 3186 LEU A CD1   1 
ATOM   13775 C  CD2   . LEU A 1 3186 ? 229.916 194.605 255.814 1.00 5.58  ? 3186 LEU A CD2   1 
ATOM   13776 N  N     . PHE A 1 3187 ? 235.190 195.077 256.671 1.00 4.20  ? 3187 PHE A N     1 
ATOM   13777 C  CA    . PHE A 1 3187 ? 236.332 194.936 257.570 1.00 3.66  ? 3187 PHE A CA    1 
ATOM   13778 C  C     . PHE A 1 3187 ? 236.534 196.194 258.402 1.00 5.08  ? 3187 PHE A C     1 
ATOM   13779 O  O     . PHE A 1 3187 ? 236.739 196.121 259.617 1.00 6.03  ? 3187 PHE A O     1 
ATOM   13780 C  CB    . PHE A 1 3187 ? 237.580 194.623 256.752 1.00 3.87  ? 3187 PHE A CB    1 
ATOM   13781 C  CG    . PHE A 1 3187 ? 238.779 194.241 257.568 1.00 4.96  ? 3187 PHE A CG    1 
ATOM   13782 C  CD1   . PHE A 1 3187 ? 238.911 192.961 258.074 1.00 5.75  ? 3187 PHE A CD1   1 
ATOM   13783 C  CD2   . PHE A 1 3187 ? 239.796 195.154 257.794 1.00 6.52  ? 3187 PHE A CD2   1 
ATOM   13784 C  CE1   . PHE A 1 3187 ? 240.021 192.603 258.813 1.00 11.37 ? 3187 PHE A CE1   1 
ATOM   13785 C  CE2   . PHE A 1 3187 ? 240.909 194.802 258.529 1.00 9.18  ? 3187 PHE A CE2   1 
ATOM   13786 C  CZ    . PHE A 1 3187 ? 241.023 193.526 259.038 1.00 8.95  ? 3187 PHE A CZ    1 
ATOM   13787 N  N     . HIS A 1 3188 ? 236.484 197.361 257.759 1.00 7.67  ? 3188 HIS A N     1 
ATOM   13788 C  CA    . HIS A 1 3188 ? 236.591 198.610 258.501 1.00 7.41  ? 3188 HIS A CA    1 
ATOM   13789 C  C     . HIS A 1 3188 ? 235.401 198.801 259.430 1.00 9.63  ? 3188 HIS A C     1 
ATOM   13790 O  O     . HIS A 1 3188 ? 235.564 199.224 260.578 1.00 11.78 ? 3188 HIS A O     1 
ATOM   13791 C  CB    . HIS A 1 3188 ? 236.714 199.786 257.535 1.00 5.43  ? 3188 HIS A CB    1 
ATOM   13792 C  CG    . HIS A 1 3188 ? 236.534 201.121 258.186 1.00 14.51 ? 3188 HIS A CG    1 
ATOM   13793 N  ND1   . HIS A 1 3188 ? 237.451 201.651 259.065 1.00 19.40 ? 3188 HIS A ND1   1 
ATOM   13794 C  CD2   . HIS A 1 3188 ? 235.533 202.028 258.092 1.00 14.72 ? 3188 HIS A CD2   1 
ATOM   13795 C  CE1   . HIS A 1 3188 ? 237.028 202.830 259.483 1.00 20.17 ? 3188 HIS A CE1   1 
ATOM   13796 N  NE2   . HIS A 1 3188 ? 235.866 203.083 258.907 1.00 20.89 ? 3188 HIS A NE2   1 
ATOM   13797 N  N     . GLU A 1 3189 ? 234.195 198.486 258.948 1.00 6.63  ? 3189 GLU A N     1 
ATOM   13798 C  CA    . GLU A 1 3189 ? 232.993 198.645 259.760 1.00 7.17  ? 3189 GLU A CA    1 
ATOM   13799 C  C     . GLU A 1 3189 ? 233.023 197.731 260.979 1.00 11.20 ? 3189 GLU A C     1 
ATOM   13800 O  O     . GLU A 1 3189 ? 232.705 198.154 262.096 1.00 13.74 ? 3189 GLU A O     1 
ATOM   13801 C  CB    . GLU A 1 3189 ? 231.757 198.369 258.906 1.00 9.05  ? 3189 GLU A CB    1 
ATOM   13802 C  CG    . GLU A 1 3189 ? 230.431 198.604 259.603 1.00 13.29 ? 3189 GLU A CG    1 
ATOM   13803 C  CD    . GLU A 1 3189 ? 229.283 197.899 258.907 1.00 16.31 ? 3189 GLU A CD    1 
ATOM   13804 O  OE1   . GLU A 1 3189 ? 229.140 198.065 257.678 1.00 17.40 ? 3189 GLU A OE1   1 
ATOM   13805 O  OE2   . GLU A 1 3189 ? 228.523 197.181 259.589 1.00 15.73 ? 3189 GLU A OE2   1 
ATOM   13806 N  N     . LYS A 1 3190 ? 233.410 196.468 260.785 1.00 9.38  ? 3190 LYS A N     1 
ATOM   13807 C  CA    . LYS A 1 3190 ? 233.418 195.522 261.897 1.00 6.61  ? 3190 LYS A CA    1 
ATOM   13808 C  C     . LYS A 1 3190 ? 234.549 195.818 262.870 1.00 6.84  ? 3190 LYS A C     1 
ATOM   13809 O  O     . LYS A 1 3190 ? 234.379 195.684 264.087 1.00 13.55 ? 3190 LYS A O     1 
ATOM   13810 C  CB    . LYS A 1 3190 ? 233.521 194.094 261.369 1.00 6.40  ? 3190 LYS A CB    1 
ATOM   13811 C  CG    . LYS A 1 3190 ? 232.244 193.591 260.745 1.00 5.63  ? 3190 LYS A CG    1 
ATOM   13812 C  CD    . LYS A 1 3190 ? 231.109 193.588 261.748 1.00 4.72  ? 3190 LYS A CD    1 
ATOM   13813 C  CE    . LYS A 1 3190 ? 229.853 193.008 261.139 1.00 6.68  ? 3190 LYS A CE    1 
ATOM   13814 N  NZ    . LYS A 1 3190 ? 228.862 192.607 262.172 1.00 7.09  ? 3190 LYS A NZ    1 
ATOM   13815 N  N     . ARG A 1 3191 ? 235.717 196.205 262.353 1.00 13.28 ? 3191 ARG A N     1 
ATOM   13816 C  CA    . ARG A 1 3191 ? 236.825 196.578 263.225 1.00 10.43 ? 3191 ARG A CA    1 
ATOM   13817 C  C     . ARG A 1 3191 ? 236.485 197.820 264.038 1.00 9.03  ? 3191 ARG A C     1 
ATOM   13818 O  O     . ARG A 1 3191 ? 236.763 197.878 265.242 1.00 11.23 ? 3191 ARG A O     1 
ATOM   13819 C  CB    . ARG A 1 3191 ? 238.083 196.808 262.388 1.00 10.22 ? 3191 ARG A CB    1 
ATOM   13820 C  CG    . ARG A 1 3191 ? 239.343 197.110 263.175 1.00 16.41 ? 3191 ARG A CG    1 
ATOM   13821 C  CD    . ARG A 1 3191 ? 240.530 197.230 262.231 1.00 23.53 ? 3191 ARG A CD    1 
ATOM   13822 N  NE    . ARG A 1 3191 ? 241.762 197.597 262.917 1.00 34.59 ? 3191 ARG A NE    1 
ATOM   13823 C  CZ    . ARG A 1 3191 ? 242.594 196.727 263.473 1.00 35.19 ? 3191 ARG A CZ    1 
ATOM   13824 N  NH1   . ARG A 1 3191 ? 242.378 195.424 263.402 1.00 27.88 ? 3191 ARG A NH1   1 
ATOM   13825 N  NH2   . ARG A 1 3191 ? 243.675 197.176 264.105 1.00 31.76 ? 3191 ARG A NH2   1 
ATOM   13826 N  N     . SER A 1 3192 ? 235.874 198.818 263.397 1.00 9.39  ? 3192 SER A N     1 
ATOM   13827 C  CA    . SER A 1 3192 ? 235.506 200.046 264.097 1.00 12.50 ? 3192 SER A CA    1 
ATOM   13828 C  C     . SER A 1 3192 ? 234.444 199.787 265.159 1.00 14.80 ? 3192 SER A C     1 
ATOM   13829 O  O     . SER A 1 3192 ? 234.527 200.327 266.268 1.00 15.23 ? 3192 SER A O     1 
ATOM   13830 C  CB    . SER A 1 3192 ? 235.020 201.091 263.094 1.00 11.85 ? 3192 SER A CB    1 
ATOM   13831 O  OG    . SER A 1 3192 ? 234.624 202.285 263.743 1.00 20.87 ? 3192 SER A OG    1 
ATOM   13832 N  N     . GLU A 1 3193 ? 233.436 198.971 264.838 1.00 13.67 ? 3193 GLU A N     1 
ATOM   13833 C  CA    . GLU A 1 3193 ? 232.395 198.663 265.814 1.00 10.33 ? 3193 GLU A CA    1 
ATOM   13834 C  C     . GLU A 1 3193 ? 232.965 197.926 267.018 1.00 13.06 ? 3193 GLU A C     1 
ATOM   13835 O  O     . GLU A 1 3193 ? 232.618 198.231 268.164 1.00 17.88 ? 3193 GLU A O     1 
ATOM   13836 C  CB    . GLU A 1 3193 ? 231.284 197.837 265.163 1.00 8.93  ? 3193 GLU A CB    1 
ATOM   13837 C  CG    . GLU A 1 3193 ? 230.381 198.622 264.233 1.00 15.33 ? 3193 GLU A CG    1 
ATOM   13838 C  CD    . GLU A 1 3193 ? 229.190 197.813 263.754 1.00 29.34 ? 3193 GLU A CD    1 
ATOM   13839 O  OE1   . GLU A 1 3193 ? 229.279 197.210 262.664 1.00 23.88 ? 3193 GLU A OE1   1 
ATOM   13840 O  OE2   . GLU A 1 3193 ? 228.166 197.781 264.468 1.00 34.90 ? 3193 GLU A OE2   1 
ATOM   13841 N  N     . LEU A 1 3194 ? 233.843 196.951 266.775 1.00 12.42 ? 3194 LEU A N     1 
ATOM   13842 C  CA    . LEU A 1 3194 ? 234.396 196.161 267.870 1.00 11.17 ? 3194 LEU A CA    1 
ATOM   13843 C  C     . LEU A 1 3194 ? 235.285 197.007 268.771 1.00 17.03 ? 3194 LEU A C     1 
ATOM   13844 O  O     . LEU A 1 3194 ? 235.195 196.924 270.002 1.00 26.33 ? 3194 LEU A O     1 
ATOM   13845 C  CB    . LEU A 1 3194 ? 235.173 194.971 267.312 1.00 12.21 ? 3194 LEU A CB    1 
ATOM   13846 C  CG    . LEU A 1 3194 ? 235.493 193.855 268.303 1.00 17.77 ? 3194 LEU A CG    1 
ATOM   13847 C  CD1   . LEU A 1 3194 ? 234.223 193.320 268.946 1.00 21.07 ? 3194 LEU A CD1   1 
ATOM   13848 C  CD2   . LEU A 1 3194 ? 236.241 192.751 267.602 1.00 20.73 ? 3194 LEU A CD2   1 
ATOM   13849 N  N     . GLU A 1 3195 ? 236.156 197.823 268.176 1.00 18.65 ? 3195 GLU A N     1 
ATOM   13850 C  CA    . GLU A 1 3195 ? 237.024 198.680 268.979 1.00 16.52 ? 3195 GLU A CA    1 
ATOM   13851 C  C     . GLU A 1 3195 ? 236.212 199.714 269.745 1.00 13.99 ? 3195 GLU A C     1 
ATOM   13852 O  O     . GLU A 1 3195 ? 236.522 200.026 270.900 1.00 16.86 ? 3195 GLU A O     1 
ATOM   13853 C  CB    . GLU A 1 3195 ? 238.063 199.361 268.088 1.00 17.25 ? 3195 GLU A CB    1 
ATOM   13854 C  CG    . GLU A 1 3195 ? 239.073 198.404 267.479 1.00 19.17 ? 3195 GLU A CG    1 
ATOM   13855 C  CD    . GLU A 1 3195 ? 240.077 199.105 266.588 1.00 31.87 ? 3195 GLU A CD    1 
ATOM   13856 O  OE1   . GLU A 1 3195 ? 239.912 200.318 266.345 1.00 31.26 ? 3195 GLU A OE1   1 
ATOM   13857 O  OE2   . GLU A 1 3195 ? 241.029 198.442 266.129 1.00 35.95 ? 3195 GLU A OE2   1 
ATOM   13858 N  N     . GLU A 1 3196 ? 235.174 200.264 269.113 1.00 19.47 ? 3196 GLU A N     1 
ATOM   13859 C  CA    . GLU A 1 3196 ? 234.308 201.215 269.800 1.00 20.05 ? 3196 GLU A CA    1 
ATOM   13860 C  C     . GLU A 1 3196 ? 233.576 200.543 270.955 1.00 18.86 ? 3196 GLU A C     1 
ATOM   13861 O  O     . GLU A 1 3196 ? 233.436 201.126 272.036 1.00 21.00 ? 3196 GLU A O     1 
ATOM   13862 C  CB    . GLU A 1 3196 ? 233.311 201.820 268.810 1.00 16.62 ? 3196 GLU A CB    1 
ATOM   13863 C  CG    . GLU A 1 3196 ? 232.379 202.870 269.389 1.00 18.97 ? 3196 GLU A CG    1 
ATOM   13864 C  CD    . GLU A 1 3196 ? 233.120 204.118 269.841 1.00 34.47 ? 3196 GLU A CD    1 
ATOM   13865 O  OE1   . GLU A 1 3196 ? 234.211 204.395 269.298 1.00 38.53 ? 3196 GLU A OE1   1 
ATOM   13866 O  OE2   . GLU A 1 3196 ? 232.609 204.832 270.726 1.00 34.36 ? 3196 GLU A OE2   1 
ATOM   13867 N  N     . GLN A 1 3197 ? 233.102 199.313 270.741 1.00 17.86 ? 3197 GLN A N     1 
ATOM   13868 C  CA    . GLN A 1 3197 ? 232.460 198.561 271.815 1.00 18.47 ? 3197 GLN A CA    1 
ATOM   13869 C  C     . GLN A 1 3197 ? 233.435 198.270 272.947 1.00 18.95 ? 3197 GLN A C     1 
ATOM   13870 O  O     . GLN A 1 3197 ? 233.089 198.411 274.127 1.00 22.21 ? 3197 GLN A O     1 
ATOM   13871 C  CB    . GLN A 1 3197 ? 231.878 197.258 271.270 1.00 18.90 ? 3197 GLN A CB    1 
ATOM   13872 C  CG    . GLN A 1 3197 ? 231.114 196.449 272.305 1.00 22.53 ? 3197 GLN A CG    1 
ATOM   13873 C  CD    . GLN A 1 3197 ? 230.498 195.193 271.727 1.00 25.43 ? 3197 GLN A CD    1 
ATOM   13874 O  OE1   . GLN A 1 3197 ? 230.664 194.891 270.546 1.00 30.11 ? 3197 GLN A OE1   1 
ATOM   13875 N  NE2   . GLN A 1 3197 ? 229.785 194.446 272.563 1.00 25.35 ? 3197 GLN A NE2   1 
ATOM   13876 N  N     . GLN A 1 3198 ? 234.659 197.860 272.609 1.00 16.16 ? 3198 GLN A N     1 
ATOM   13877 C  CA    . GLN A 1 3198 ? 235.656 197.584 273.637 1.00 16.43 ? 3198 GLN A CA    1 
ATOM   13878 C  C     . GLN A 1 3198 ? 236.020 198.841 274.416 1.00 20.28 ? 3198 GLN A C     1 
ATOM   13879 O  O     . GLN A 1 3198 ? 236.415 198.752 275.585 1.00 23.73 ? 3198 GLN A O     1 
ATOM   13880 C  CB    . GLN A 1 3198 ? 236.903 196.968 273.004 1.00 20.56 ? 3198 GLN A CB    1 
ATOM   13881 C  CG    . GLN A 1 3198 ? 237.796 196.218 273.977 1.00 20.93 ? 3198 GLN A CG    1 
ATOM   13882 C  CD    . GLN A 1 3198 ? 237.018 195.286 274.886 1.00 25.26 ? 3198 GLN A CD    1 
ATOM   13883 O  OE1   . GLN A 1 3198 ? 236.292 194.408 274.422 1.00 28.37 ? 3198 GLN A OE1   1 
ATOM   13884 N  NE2   . GLN A 1 3198 ? 237.167 195.473 276.191 1.00 27.08 ? 3198 GLN A NE2   1 
ATOM   13885 N  N     . MET A 1 3199 ? 235.895 200.012 273.792 1.00 19.78 ? 3199 MET A N     1 
ATOM   13886 C  CA    . MET A 1 3199 ? 236.164 201.262 274.495 1.00 19.97 ? 3199 MET A CA    1 
ATOM   13887 C  C     . MET A 1 3199 ? 235.123 201.507 275.581 1.00 23.90 ? 3199 MET A C     1 
ATOM   13888 O  O     . MET A 1 3199 ? 235.465 201.873 276.711 1.00 31.68 ? 3199 MET A O     1 
ATOM   13889 C  CB    . MET A 1 3199 ? 236.214 202.418 273.490 1.00 21.15 ? 3199 MET A CB    1 
ATOM   13890 C  CG    . MET A 1 3199 ? 236.547 203.805 274.056 1.00 29.19 ? 3199 MET A CG    1 
ATOM   13891 S  SD    . MET A 1 3199 ? 235.273 204.618 275.047 1.00 50.51 ? 3199 MET A SD    1 
ATOM   13892 C  CE    . MET A 1 3199 ? 234.133 205.149 273.772 1.00 27.12 ? 3199 MET A CE    1 
ATOM   13893 N  N     . HIS A 1 3200 ? 233.842 201.309 275.255 1.00 24.53 ? 3200 HIS A N     1 
ATOM   13894 C  CA    . HIS A 1 3200 ? 232.790 201.512 276.243 1.00 24.37 ? 3200 HIS A CA    1 
ATOM   13895 C  C     . HIS A 1 3200 ? 232.899 200.508 277.385 1.00 23.84 ? 3200 HIS A C     1 
ATOM   13896 O  O     . HIS A 1 3200 ? 232.727 200.868 278.556 1.00 27.26 ? 3200 HIS A O     1 
ATOM   13897 C  CB    . HIS A 1 3200 ? 231.415 201.410 275.584 1.00 21.44 ? 3200 HIS A CB    1 
ATOM   13898 C  CG    . HIS A 1 3200 ? 231.094 202.551 274.670 1.00 21.99 ? 3200 HIS A CG    1 
ATOM   13899 N  ND1   . HIS A 1 3200 ? 231.268 202.483 273.306 1.00 28.25 ? 3200 HIS A ND1   1 
ATOM   13900 C  CD2   . HIS A 1 3200 ? 230.618 203.792 274.927 1.00 25.88 ? 3200 HIS A CD2   1 
ATOM   13901 C  CE1   . HIS A 1 3200 ? 230.904 203.629 272.760 1.00 30.19 ? 3200 HIS A CE1   1 
ATOM   13902 N  NE2   . HIS A 1 3200 ? 230.509 204.443 273.722 1.00 26.52 ? 3200 HIS A NE2   1 
ATOM   13903 N  N     . LEU A 1 3201 ? 233.184 199.243 277.064 1.00 15.35 ? 3201 LEU A N     1 
ATOM   13904 C  CA    . LEU A 1 3201 ? 233.272 198.219 278.098 1.00 17.65 ? 3201 LEU A CA    1 
ATOM   13905 C  C     . LEU A 1 3201 ? 234.393 198.525 279.083 1.00 22.59 ? 3201 LEU A C     1 
ATOM   13906 O  O     . LEU A 1 3201 ? 234.230 198.348 280.294 1.00 23.00 ? 3201 LEU A O     1 
ATOM   13907 C  CB    . LEU A 1 3201 ? 233.479 196.844 277.464 1.00 18.86 ? 3201 LEU A CB    1 
ATOM   13908 C  CG    . LEU A 1 3201 ? 232.324 196.269 276.640 1.00 23.30 ? 3201 LEU A CG    1 
ATOM   13909 C  CD1   . LEU A 1 3201 ? 232.605 194.822 276.273 1.00 28.55 ? 3201 LEU A CD1   1 
ATOM   13910 C  CD2   . LEU A 1 3201 ? 231.005 196.388 277.384 1.00 16.24 ? 3201 LEU A CD2   1 
ATOM   13911 N  N     . ASN A 1 3202 ? 235.541 198.981 278.580 1.00 25.64 ? 3202 ASN A N     1 
ATOM   13912 C  CA    . ASN A 1 3202 ? 236.650 199.325 279.464 1.00 21.52 ? 3202 ASN A CA    1 
ATOM   13913 C  C     . ASN A 1 3202 ? 236.306 200.515 280.349 1.00 24.39 ? 3202 ASN A C     1 
ATOM   13914 O  O     . ASN A 1 3202 ? 236.648 200.531 281.536 1.00 25.73 ? 3202 ASN A O     1 
ATOM   13915 C  CB    . ASN A 1 3202 ? 237.904 199.602 278.640 1.00 26.54 ? 3202 ASN A CB    1 
ATOM   13916 C  CG    . ASN A 1 3202 ? 238.599 198.331 278.204 1.00 32.26 ? 3202 ASN A CG    1 
ATOM   13917 O  OD1   . ASN A 1 3202 ? 238.154 197.229 278.528 1.00 24.44 ? 3202 ASN A OD1   1 
ATOM   13918 N  ND2   . ASN A 1 3202 ? 239.691 198.475 277.465 1.00 35.43 ? 3202 ASN A ND2   1 
ATOM   13919 N  N     . VAL A 1 3203 ? 235.641 201.527 279.788 1.00 25.68 ? 3203 VAL A N     1 
ATOM   13920 C  CA    . VAL A 1 3203 ? 235.201 202.657 280.598 1.00 23.21 ? 3203 VAL A CA    1 
ATOM   13921 C  C     . VAL A 1 3203 ? 234.130 202.220 281.588 1.00 27.69 ? 3203 VAL A C     1 
ATOM   13922 O  O     . VAL A 1 3203 ? 234.169 202.588 282.768 1.00 26.84 ? 3203 VAL A O     1 
ATOM   13923 C  CB    . VAL A 1 3203 ? 234.709 203.804 279.697 1.00 17.60 ? 3203 VAL A CB    1 
ATOM   13924 C  CG1   . VAL A 1 3203 ? 233.998 204.862 280.526 1.00 20.96 ? 3203 VAL A CG1   1 
ATOM   13925 C  CG2   . VAL A 1 3203 ? 235.873 204.411 278.936 1.00 23.46 ? 3203 VAL A CG2   1 
ATOM   13926 N  N     . GLY A 1 3204 ? 233.161 201.426 281.130 1.00 25.44 ? 3204 GLY A N     1 
ATOM   13927 C  CA    . GLY A 1 3204 ? 232.112 200.969 282.026 1.00 23.18 ? 3204 GLY A CA    1 
ATOM   13928 C  C     . GLY A 1 3204 ? 232.644 200.118 283.162 1.00 25.55 ? 3204 GLY A C     1 
ATOM   13929 O  O     . GLY A 1 3204 ? 232.199 200.240 284.304 1.00 32.38 ? 3204 GLY A O     1 
ATOM   13930 N  N     . LEU A 1 3205 ? 233.603 199.239 282.861 1.00 22.09 ? 3205 LEU A N     1 
ATOM   13931 C  CA    . LEU A 1 3205 ? 234.200 198.414 283.903 1.00 22.42 ? 3205 LEU A CA    1 
ATOM   13932 C  C     . LEU A 1 3205 ? 234.978 199.256 284.906 1.00 25.80 ? 3205 LEU A C     1 
ATOM   13933 O  O     . LEU A 1 3205 ? 234.920 198.999 286.114 1.00 29.68 ? 3205 LEU A O     1 
ATOM   13934 C  CB    . LEU A 1 3205 ? 235.104 197.351 283.278 1.00 23.26 ? 3205 LEU A CB    1 
ATOM   13935 C  CG    . LEU A 1 3205 ? 234.379 196.151 282.668 1.00 22.66 ? 3205 LEU A CG    1 
ATOM   13936 C  CD1   . LEU A 1 3205 ? 235.371 195.107 282.200 1.00 27.69 ? 3205 LEU A CD1   1 
ATOM   13937 C  CD2   . LEU A 1 3205 ? 233.410 195.561 283.677 1.00 24.30 ? 3205 LEU A CD2   1 
ATOM   13938 N  N     . ARG A 1 3206 ? 235.715 200.264 284.428 1.00 22.18 ? 3206 ARG A N     1 
ATOM   13939 C  CA    . ARG A 1 3206 ? 236.552 201.045 285.332 1.00 23.94 ? 3206 ARG A CA    1 
ATOM   13940 C  C     . ARG A 1 3206 ? 235.717 201.937 286.242 1.00 25.74 ? 3206 ARG A C     1 
ATOM   13941 O  O     . ARG A 1 3206 ? 236.123 202.209 287.378 1.00 31.86 ? 3206 ARG A O     1 
ATOM   13942 C  CB    . ARG A 1 3206 ? 237.571 201.874 284.541 1.00 24.45 ? 3206 ARG A CB    1 
ATOM   13943 C  CG    . ARG A 1 3206 ? 237.025 203.140 283.905 1.00 27.58 ? 3206 ARG A CG    1 
ATOM   13944 C  CD    . ARG A 1 3206 ? 238.110 203.921 283.176 1.00 28.23 ? 3206 ARG A CD    1 
ATOM   13945 N  NE    . ARG A 1 3206 ? 238.562 203.248 281.965 1.00 32.45 ? 3206 ARG A NE    1 
ATOM   13946 C  CZ    . ARG A 1 3206 ? 239.755 202.686 281.818 1.00 33.60 ? 3206 ARG A CZ    1 
ATOM   13947 N  NH1   . ARG A 1 3206 ? 240.647 202.691 282.794 1.00 31.48 ? 3206 ARG A NH1   1 
ATOM   13948 N  NH2   . ARG A 1 3206 ? 240.060 202.105 280.661 1.00 30.85 ? 3206 ARG A NH2   1 
ATOM   13949 N  N     . LYS A 1 3207 ? 234.558 202.405 285.770 1.00 25.75 ? 3207 LYS A N     1 
ATOM   13950 C  CA    . LYS A 1 3207 ? 233.673 203.178 286.636 1.00 27.52 ? 3207 LYS A CA    1 
ATOM   13951 C  C     . LYS A 1 3207 ? 233.108 202.316 287.757 1.00 26.86 ? 3207 LYS A C     1 
ATOM   13952 O  O     . LYS A 1 3207 ? 232.988 202.775 288.899 1.00 27.53 ? 3207 LYS A O     1 
ATOM   13953 C  CB    . LYS A 1 3207 ? 232.546 203.809 285.817 1.00 22.22 ? 3207 LYS A CB    1 
ATOM   13954 C  CG    . LYS A 1 3207 ? 233.020 204.763 284.736 1.00 20.48 ? 3207 LYS A CG    1 
ATOM   13955 C  CD    . LYS A 1 3207 ? 233.687 205.986 285.343 1.00 27.62 ? 3207 LYS A CD    1 
ATOM   13956 C  CE    . LYS A 1 3207 ? 234.015 207.025 284.282 1.00 32.70 ? 3207 LYS A CE    1 
ATOM   13957 N  NZ    . LYS A 1 3207 ? 235.097 206.565 283.369 1.00 33.20 ? 3207 LYS A NZ    1 
ATOM   13958 N  N     . ILE A 1 3208 ? 232.749 201.068 287.451 1.00 24.99 ? 3208 ILE A N     1 
ATOM   13959 C  CA    . ILE A 1 3208 ? 232.262 200.163 288.485 1.00 24.93 ? 3208 ILE A CA    1 
ATOM   13960 C  C     . ILE A 1 3208 ? 233.362 199.869 289.500 1.00 26.58 ? 3208 ILE A C     1 
ATOM   13961 O  O     . ILE A 1 3208 ? 233.123 199.883 290.713 1.00 33.07 ? 3208 ILE A O     1 
ATOM   13962 C  CB    . ILE A 1 3208 ? 231.719 198.870 287.853 1.00 26.35 ? 3208 ILE A CB    1 
ATOM   13963 C  CG1   . ILE A 1 3208 ? 230.534 199.180 286.936 1.00 26.74 ? 3208 ILE A CG1   1 
ATOM   13964 C  CG2   . ILE A 1 3208 ? 231.307 197.883 288.929 1.00 25.21 ? 3208 ILE A CG2   1 
ATOM   13965 C  CD1   . ILE A 1 3208 ? 229.960 197.957 286.266 1.00 22.11 ? 3208 ILE A CD1   1 
ATOM   13966 N  N     . LYS A 1 3209 ? 234.579 199.603 289.022 1.00 25.25 ? 3209 LYS A N     1 
ATOM   13967 C  CA    . LYS A 1 3209 ? 235.687 199.329 289.931 1.00 26.05 ? 3209 LYS A CA    1 
ATOM   13968 C  C     . LYS A 1 3209 ? 235.986 200.533 290.815 1.00 30.20 ? 3209 LYS A C     1 
ATOM   13969 O  O     . LYS A 1 3209 ? 236.252 200.383 292.013 1.00 31.43 ? 3209 LYS A O     1 
ATOM   13970 C  CB    . LYS A 1 3209 ? 236.930 198.923 289.142 1.00 28.52 ? 3209 LYS A CB    1 
ATOM   13971 C  CG    . LYS A 1 3209 ? 238.101 198.496 290.011 1.00 26.05 ? 3209 LYS A CG    1 
ATOM   13972 C  CD    . LYS A 1 3209 ? 239.040 197.570 289.259 1.00 22.40 ? 3209 LYS A CD    1 
ATOM   13973 C  CE    . LYS A 1 3209 ? 238.285 196.395 288.663 1.00 26.52 ? 3209 LYS A CE    1 
ATOM   13974 N  NZ    . LYS A 1 3209 ? 237.701 195.525 289.720 1.00 24.91 ? 3209 LYS A NZ    1 
ATOM   13975 N  N     . GLU A 1 3210 ? 235.951 201.737 290.240 1.00 27.75 ? 3210 GLU A N     1 
ATOM   13976 C  CA    . GLU A 1 3210 ? 236.126 202.942 291.044 1.00 30.59 ? 3210 GLU A CA    1 
ATOM   13977 C  C     . GLU A 1 3210 ? 235.010 203.079 292.071 1.00 32.14 ? 3210 GLU A C     1 
ATOM   13978 O  O     . GLU A 1 3210 ? 235.254 203.489 293.213 1.00 33.57 ? 3210 GLU A O     1 
ATOM   13979 C  CB    . GLU A 1 3210 ? 236.181 204.174 290.140 1.00 24.95 ? 3210 GLU A CB    1 
ATOM   13980 C  CG    . GLU A 1 3210 ? 237.503 204.354 289.415 1.00 32.07 ? 3210 GLU A CG    1 
ATOM   13981 C  CD    . GLU A 1 3210 ? 237.441 205.432 288.351 1.00 38.54 ? 3210 GLU A CD    1 
ATOM   13982 O  OE1   . GLU A 1 3210 ? 236.357 206.023 288.164 1.00 37.14 ? 3210 GLU A OE1   1 
ATOM   13983 O  OE2   . GLU A 1 3210 ? 238.476 205.689 287.703 1.00 34.60 ? 3210 GLU A OE2   1 
ATOM   13984 N  N     . THR A 1 3211 ? 233.780 202.733 291.685 1.00 27.72 ? 3211 THR A N     1 
ATOM   13985 C  CA    . THR A 1 3211 ? 232.649 202.823 292.603 1.00 28.19 ? 3211 THR A CA    1 
ATOM   13986 C  C     . THR A 1 3211 ? 232.841 201.913 293.811 1.00 29.78 ? 3211 THR A C     1 
ATOM   13987 O  O     . THR A 1 3211 ? 232.534 202.299 294.944 1.00 31.89 ? 3211 THR A O     1 
ATOM   13988 C  CB    . THR A 1 3211 ? 231.357 202.479 291.864 1.00 30.59 ? 3211 THR A CB    1 
ATOM   13989 O  OG1   . THR A 1 3211 ? 231.047 203.519 290.925 1.00 33.18 ? 3211 THR A OG1   1 
ATOM   13990 C  CG2   . THR A 1 3211 ? 230.199 202.321 292.837 1.00 25.24 ? 3211 THR A CG2   1 
ATOM   13991 N  N     . VAL A 1 3212 ? 233.355 200.701 293.588 1.00 29.24 ? 3212 VAL A N     1 
ATOM   13992 C  CA    . VAL A 1 3212 ? 233.625 199.789 294.697 1.00 27.50 ? 3212 VAL A CA    1 
ATOM   13993 C  C     . VAL A 1 3212 ? 234.656 200.396 295.642 1.00 33.69 ? 3212 VAL A C     1 
ATOM   13994 O  O     . VAL A 1 3212 ? 234.581 200.221 296.864 1.00 35.42 ? 3212 VAL A O     1 
ATOM   13995 C  CB    . VAL A 1 3212 ? 234.080 198.419 294.161 1.00 25.95 ? 3212 VAL A CB    1 
ATOM   13996 C  CG1   . VAL A 1 3212 ? 234.383 197.467 295.309 1.00 30.02 ? 3212 VAL A CG1   1 
ATOM   13997 C  CG2   . VAL A 1 3212 ? 233.025 197.834 293.244 1.00 28.08 ? 3212 VAL A CG2   1 
ATOM   13998 N  N     . ASP A 1 3213 ? 235.641 201.108 295.090 1.00 31.63 ? 3213 ASP A N     1 
ATOM   13999 C  CA    . ASP A 1 3213 ? 236.618 201.797 295.927 1.00 29.89 ? 3213 ASP A CA    1 
ATOM   14000 C  C     . ASP A 1 3213 ? 235.977 202.939 296.705 1.00 32.26 ? 3213 ASP A C     1 
ATOM   14001 O  O     . ASP A 1 3213 ? 236.315 203.166 297.874 1.00 37.37 ? 3213 ASP A O     1 
ATOM   14002 C  CB    . ASP A 1 3213 ? 237.772 202.316 295.070 1.00 32.50 ? 3213 ASP A CB    1 
ATOM   14003 C  CG    . ASP A 1 3213 ? 238.444 201.219 294.269 1.00 34.19 ? 3213 ASP A CG    1 
ATOM   14004 O  OD1   . ASP A 1 3213 ? 238.688 200.134 294.835 1.00 37.07 ? 3213 ASP A OD1   1 
ATOM   14005 O  OD2   . ASP A 1 3213 ? 238.727 201.443 293.074 1.00 34.32 ? 3213 ASP A OD2   1 
ATOM   14006 N  N     . GLN A 1 3214 ? 235.057 203.677 296.075 1.00 33.33 ? 3214 GLN A N     1 
ATOM   14007 C  CA    . GLN A 1 3214 ? 234.462 204.841 296.726 1.00 30.93 ? 3214 GLN A CA    1 
ATOM   14008 C  C     . GLN A 1 3214 ? 233.678 204.450 297.974 1.00 37.72 ? 3214 GLN A C     1 
ATOM   14009 O  O     . GLN A 1 3214 ? 233.759 205.130 299.003 1.00 37.87 ? 3214 GLN A O     1 
ATOM   14010 C  CB    . GLN A 1 3214 ? 233.558 205.593 295.746 1.00 25.93 ? 3214 GLN A CB    1 
ATOM   14011 C  CG    . GLN A 1 3214 ? 234.269 206.177 294.534 1.00 33.32 ? 3214 GLN A CG    1 
ATOM   14012 C  CD    . GLN A 1 3214 ? 235.714 206.543 294.812 1.00 38.37 ? 3214 GLN A CD    1 
ATOM   14013 O  OE1   . GLN A 1 3214 ? 235.998 207.456 295.587 1.00 36.01 ? 3214 GLN A OE1   1 
ATOM   14014 N  NE2   . GLN A 1 3214 ? 236.637 205.829 294.177 1.00 34.09 ? 3214 GLN A NE2   1 
ATOM   14015 N  N     . VAL A 1 3215 ? 232.902 203.368 297.900 1.00 32.35 ? 3215 VAL A N     1 
ATOM   14016 C  CA    . VAL A 1 3215 ? 232.123 202.957 299.061 1.00 30.46 ? 3215 VAL A CA    1 
ATOM   14017 C  C     . VAL A 1 3215 ? 233.034 202.442 300.169 1.00 35.95 ? 3215 VAL A C     1 
ATOM   14018 O  O     . VAL A 1 3215 ? 232.708 202.568 301.356 1.00 32.66 ? 3215 VAL A O     1 
ATOM   14019 C  CB    . VAL A 1 3215 ? 231.061 201.912 298.664 1.00 32.97 ? 3215 VAL A CB    1 
ATOM   14020 C  CG1   . VAL A 1 3215 ? 230.148 202.477 297.590 1.00 32.50 ? 3215 VAL A CG1   1 
ATOM   14021 C  CG2   . VAL A 1 3215 ? 231.716 200.627 298.186 1.00 26.82 ? 3215 VAL A CG2   1 
ATOM   14022 N  N     . GLU A 1 3216 ? 234.177 201.853 299.811 1.00 32.85 ? 3216 GLU A N     1 
ATOM   14023 C  CA    . GLU A 1 3216 ? 235.108 201.364 300.821 1.00 35.41 ? 3216 GLU A CA    1 
ATOM   14024 C  C     . GLU A 1 3216 ? 235.636 202.510 301.675 1.00 35.93 ? 3216 GLU A C     1 
ATOM   14025 O  O     . GLU A 1 3216 ? 235.691 202.408 302.907 1.00 35.35 ? 3216 GLU A O     1 
ATOM   14026 C  CB    . GLU A 1 3216 ? 236.257 200.610 300.149 1.00 33.78 ? 3216 GLU A CB    1 
ATOM   14027 C  CG    . GLU A 1 3216 ? 237.080 199.746 301.093 1.00 32.57 ? 3216 GLU A CG    1 
ATOM   14028 C  CD    . GLU A 1 3216 ? 238.201 200.515 301.765 1.00 36.57 ? 3216 GLU A CD    1 
ATOM   14029 O  OE1   . GLU A 1 3216 ? 239.033 201.105 301.046 1.00 39.57 ? 3216 GLU A OE1   1 
ATOM   14030 O  OE2   . GLU A 1 3216 ? 238.247 200.528 303.014 1.00 36.63 ? 3216 GLU A OE2   1 
ATOM   14031 N  N     . GLU A 1 3217 ? 236.027 203.617 301.038 1.00 32.78 ? 3217 GLU A N     1 
ATOM   14032 C  CA    . GLU A 1 3217 ? 236.472 204.775 301.806 1.00 34.79 ? 3217 GLU A CA    1 
ATOM   14033 C  C     . GLU A 1 3217 ? 235.296 205.509 302.433 1.00 37.87 ? 3217 GLU A C     1 
ATOM   14034 O  O     . GLU A 1 3217 ? 235.452 206.142 303.483 1.00 39.40 ? 3217 GLU A O     1 
ATOM   14035 C  CB    . GLU A 1 3217 ? 237.290 205.720 300.924 1.00 34.17 ? 3217 GLU A CB    1 
ATOM   14036 C  CG    . GLU A 1 3217 ? 236.482 206.508 299.907 1.00 33.67 ? 3217 GLU A CG    1 
ATOM   14037 C  CD    . GLU A 1 3217 ? 237.344 207.419 299.058 1.00 38.73 ? 3217 GLU A CD    1 
ATOM   14038 O  OE1   . GLU A 1 3217 ? 238.584 207.359 299.188 1.00 40.88 ? 3217 GLU A OE1   1 
ATOM   14039 O  OE2   . GLU A 1 3217 ? 236.782 208.200 298.261 1.00 38.24 ? 3217 GLU A OE2   1 
ATOM   14040 N  N     . LEU A 1 3218 ? 234.119 205.440 301.808 1.00 34.30 ? 3218 LEU A N     1 
ATOM   14041 C  CA    . LEU A 1 3218 ? 232.939 206.066 302.391 1.00 33.27 ? 3218 LEU A CA    1 
ATOM   14042 C  C     . LEU A 1 3218 ? 232.495 205.322 303.644 1.00 36.27 ? 3218 LEU A C     1 
ATOM   14043 O  O     . LEU A 1 3218 ? 232.064 205.945 304.623 1.00 39.60 ? 3218 LEU A O     1 
ATOM   14044 C  CB    . LEU A 1 3218 ? 231.814 206.131 301.358 1.00 29.93 ? 3218 LEU A CB    1 
ATOM   14045 C  CG    . LEU A 1 3218 ? 230.525 206.836 301.772 1.00 32.36 ? 3218 LEU A CG    1 
ATOM   14046 C  CD1   . LEU A 1 3218 ? 230.800 208.296 302.083 1.00 28.59 ? 3218 LEU A CD1   1 
ATOM   14047 C  CD2   . LEU A 1 3218 ? 229.485 206.719 300.668 1.00 32.12 ? 3218 LEU A CD2   1 
ATOM   14048 N  N     . ARG A 1 3219 ? 232.593 203.991 303.636 1.00 34.89 ? 3219 ARG A N     1 
ATOM   14049 C  CA    . ARG A 1 3219 ? 232.392 203.231 304.866 1.00 34.81 ? 3219 ARG A CA    1 
ATOM   14050 C  C     . ARG A 1 3219 ? 233.450 203.589 305.901 1.00 37.68 ? 3219 ARG A C     1 
ATOM   14051 O  O     . ARG A 1 3219 ? 233.152 203.698 307.096 1.00 35.17 ? 3219 ARG A O     1 
ATOM   14052 C  CB    . ARG A 1 3219 ? 232.416 201.731 304.576 1.00 29.77 ? 3219 ARG A CB    1 
ATOM   14053 C  CG    . ARG A 1 3219 ? 231.197 201.211 303.829 1.00 33.07 ? 3219 ARG A CG    1 
ATOM   14054 C  CD    . ARG A 1 3219 ? 231.185 199.689 303.799 1.00 31.62 ? 3219 ARG A CD    1 
ATOM   14055 N  NE    . ARG A 1 3219 ? 232.356 199.147 303.119 1.00 36.45 ? 3219 ARG A NE    1 
ATOM   14056 C  CZ    . ARG A 1 3219 ? 232.308 198.369 302.047 1.00 39.36 ? 3219 ARG A CZ    1 
ATOM   14057 N  NH1   . ARG A 1 3219 ? 231.156 198.012 301.502 1.00 37.42 ? 3219 ARG A NH1   1 
ATOM   14058 N  NH2   . ARG A 1 3219 ? 233.444 197.937 301.506 1.00 36.38 ? 3219 ARG A NH2   1 
ATOM   14059 N  N     . ARG A 1 3220 ? 234.699 203.764 305.461 1.00 33.83 ? 3220 ARG A N     1 
ATOM   14060 C  CA    . ARG A 1 3220 ? 235.737 204.257 306.357 1.00 34.65 ? 3220 ARG A CA    1 
ATOM   14061 C  C     . ARG A 1 3220 ? 235.404 205.659 306.851 1.00 37.44 ? 3220 ARG A C     1 
ATOM   14062 O  O     . ARG A 1 3220 ? 235.597 205.973 308.031 1.00 39.88 ? 3220 ARG A O     1 
ATOM   14063 C  CB    . ARG A 1 3220 ? 237.093 204.237 305.650 1.00 38.82 ? 3220 ARG A CB    1 
ATOM   14064 C  CG    . ARG A 1 3220 ? 238.147 205.131 306.282 1.00 37.74 ? 3220 ARG A CG    1 
ATOM   14065 C  CD    . ARG A 1 3220 ? 239.146 205.635 305.250 1.00 35.03 ? 3220 ARG A CD    1 
ATOM   14066 N  NE    . ARG A 1 3220 ? 238.506 206.394 304.181 1.00 40.50 ? 3220 ARG A NE    1 
ATOM   14067 C  CZ    . ARG A 1 3220 ? 238.064 207.638 304.304 1.00 44.05 ? 3220 ARG A CZ    1 
ATOM   14068 N  NH1   . ARG A 1 3220 ? 238.184 208.307 305.440 1.00 40.96 ? 3220 ARG A NH1   1 
ATOM   14069 N  NH2   . ARG A 1 3220 ? 237.491 208.230 303.259 1.00 39.43 ? 3220 ARG A NH2   1 
ATOM   14070 N  N     . ASP A 1 3221 ? 234.901 206.513 305.959 1.00 38.23 ? 3221 ASP A N     1 
ATOM   14071 C  CA    . ASP A 1 3221 ? 234.428 207.829 306.378 1.00 38.86 ? 3221 ASP A CA    1 
ATOM   14072 C  C     . ASP A 1 3221 ? 233.236 207.704 307.318 1.00 34.83 ? 3221 ASP A C     1 
ATOM   14073 O  O     . ASP A 1 3221 ? 233.118 208.461 308.289 1.00 33.38 ? 3221 ASP A O     1 
ATOM   14074 C  CB    . ASP A 1 3221 ? 234.068 208.672 305.155 1.00 34.98 ? 3221 ASP A CB    1 
ATOM   14075 C  CG    . ASP A 1 3221 ? 233.653 210.084 305.521 1.00 39.15 ? 3221 ASP A CG    1 
ATOM   14076 O  OD1   . ASP A 1 3221 ? 232.482 210.282 305.910 1.00 39.19 ? 3221 ASP A OD1   1 
ATOM   14077 O  OD2   . ASP A 1 3221 ? 234.498 210.997 305.420 1.00 39.69 ? 3221 ASP A OD2   1 
ATOM   14078 N  N     . LEU A 1 3222 ? 232.341 206.752 307.044 1.00 34.15 ? 3222 LEU A N     1 
ATOM   14079 C  CA    . LEU A 1 3222 ? 231.198 206.529 307.926 1.00 37.88 ? 3222 LEU A CA    1 
ATOM   14080 C  C     . LEU A 1 3222 ? 231.652 206.147 309.329 1.00 38.86 ? 3222 LEU A C     1 
ATOM   14081 O  O     . LEU A 1 3222 ? 231.084 206.615 310.323 1.00 38.94 ? 3222 LEU A O     1 
ATOM   14082 C  CB    . LEU A 1 3222 ? 230.287 205.447 307.345 1.00 37.64 ? 3222 LEU A CB    1 
ATOM   14083 C  CG    . LEU A 1 3222 ? 229.096 205.030 308.210 1.00 37.32 ? 3222 LEU A CG    1 
ATOM   14084 C  CD1   . LEU A 1 3222 ? 227.992 206.072 308.151 1.00 34.77 ? 3222 LEU A CD1   1 
ATOM   14085 C  CD2   . LEU A 1 3222 ? 228.574 203.667 307.783 1.00 30.28 ? 3222 LEU A CD2   1 
ATOM   14086 N  N     . ARG A 1 3223 ? 232.669 205.287 309.431 1.00 36.00 ? 3223 ARG A N     1 
ATOM   14087 C  CA    . ARG A 1 3223 ? 233.225 204.961 310.738 1.00 36.01 ? 3223 ARG A CA    1 
ATOM   14088 C  C     . ARG A 1 3223 ? 233.887 206.178 311.372 1.00 36.31 ? 3223 ARG A C     1 
ATOM   14089 O  O     . ARG A 1 3223 ? 233.774 206.395 312.586 1.00 36.81 ? 3223 ARG A O     1 
ATOM   14090 C  CB    . ARG A 1 3223 ? 234.221 203.807 310.613 1.00 36.56 ? 3223 ARG A CB    1 
ATOM   14091 C  CG    . ARG A 1 3223 ? 234.907 203.429 311.917 1.00 34.92 ? 3223 ARG A CG    1 
ATOM   14092 C  CD    . ARG A 1 3223 ? 236.211 202.687 311.667 1.00 39.32 ? 3223 ARG A CD    1 
ATOM   14093 N  NE    . ARG A 1 3223 ? 236.981 203.275 310.578 1.00 39.92 ? 3223 ARG A NE    1 
ATOM   14094 C  CZ    . ARG A 1 3223 ? 237.714 204.376 310.685 1.00 42.35 ? 3223 ARG A CZ    1 
ATOM   14095 N  NH1   . ARG A 1 3223 ? 237.804 205.037 311.827 1.00 37.90 ? 3223 ARG A NH1   1 
ATOM   14096 N  NH2   . ARG A 1 3223 ? 238.374 204.823 309.620 1.00 42.60 ? 3223 ARG A NH2   1 
ATOM   14097 N  N     . ILE A 1 3224 ? 234.585 206.983 310.569 1.00 36.74 ? 3224 ILE A N     1 
ATOM   14098 C  CA    . ILE A 1 3224 ? 235.239 208.180 311.090 1.00 35.60 ? 3224 ILE A CA    1 
ATOM   14099 C  C     . ILE A 1 3224 ? 234.207 209.168 311.618 1.00 37.10 ? 3224 ILE A C     1 
ATOM   14100 O  O     . ILE A 1 3224 ? 234.375 209.747 312.699 1.00 36.97 ? 3224 ILE A O     1 
ATOM   14101 C  CB    . ILE A 1 3224 ? 236.135 208.814 310.009 1.00 37.02 ? 3224 ILE A CB    1 
ATOM   14102 C  CG1   . ILE A 1 3224 ? 237.480 208.086 309.938 1.00 38.08 ? 3224 ILE A CG1   1 
ATOM   14103 C  CG2   . ILE A 1 3224 ? 236.349 210.297 310.279 1.00 33.84 ? 3224 ILE A CG2   1 
ATOM   14104 C  CD1   . ILE A 1 3224 ? 238.423 208.646 308.897 1.00 33.24 ? 3224 ILE A CD1   1 
ATOM   14105 N  N     . LYS A 1 3225 ? 233.119 209.375 310.867 1.00 34.70 ? 3225 LYS A N     1 
ATOM   14106 C  CA    . LYS A 1 3225 ? 232.065 210.273 311.329 1.00 35.38 ? 3225 LYS A CA    1 
ATOM   14107 C  C     . LYS A 1 3225 ? 231.414 209.760 312.605 1.00 38.82 ? 3225 LYS A C     1 
ATOM   14108 O  O     . LYS A 1 3225 ? 231.015 210.557 313.462 1.00 39.53 ? 3225 LYS A O     1 
ATOM   14109 C  CB    . LYS A 1 3225 ? 231.015 210.463 310.233 1.00 36.84 ? 3225 LYS A CB    1 
ATOM   14110 C  CG    . LYS A 1 3225 ? 231.547 211.105 308.962 1.00 36.15 ? 3225 LYS A CG    1 
ATOM   14111 C  CD    . LYS A 1 3225 ? 232.122 212.488 309.229 1.00 35.25 ? 3225 LYS A CD    1 
ATOM   14112 C  CE    . LYS A 1 3225 ? 231.047 213.450 309.705 1.00 34.22 ? 3225 LYS A CE    1 
ATOM   14113 N  NZ    . LYS A 1 3225 ? 229.783 213.298 308.935 1.00 37.89 ? 3225 LYS A NZ    1 
ATOM   14114 N  N     . SER A 1 3226 ? 231.289 208.438 312.746 1.00 37.36 ? 3226 SER A N     1 
ATOM   14115 C  CA    . SER A 1 3226 ? 230.776 207.875 313.991 1.00 35.69 ? 3226 SER A CA    1 
ATOM   14116 C  C     . SER A 1 3226 ? 231.704 208.190 315.157 1.00 38.85 ? 3226 SER A C     1 
ATOM   14117 O  O     . SER A 1 3226 ? 231.242 208.507 316.260 1.00 41.03 ? 3226 SER A O     1 
ATOM   14118 C  CB    . SER A 1 3226 ? 230.586 206.365 313.845 1.00 36.28 ? 3226 SER A CB    1 
ATOM   14119 O  OG    . SER A 1 3226 ? 231.835 205.700 313.771 1.00 39.51 ? 3226 SER A OG    1 
ATOM   14120 N  N     . GLN A 1 3227 ? 233.016 208.103 314.932 1.00 39.53 ? 3227 GLN A N     1 
ATOM   14121 C  CA    . GLN A 1 3227 ? 233.976 208.449 315.976 1.00 38.91 ? 3227 GLN A CA    1 
ATOM   14122 C  C     . GLN A 1 3227 ? 233.872 209.920 316.353 1.00 38.33 ? 3227 GLN A C     1 
ATOM   14123 O  O     . GLN A 1 3227 ? 233.999 210.279 317.529 1.00 39.38 ? 3227 GLN A O     1 
ATOM   14124 C  CB    . GLN A 1 3227 ? 235.394 208.108 315.520 1.00 35.93 ? 3227 GLN A CB    1 
ATOM   14125 C  CG    . GLN A 1 3227 ? 236.383 207.906 316.656 1.00 35.94 ? 3227 GLN A CG    1 
ATOM   14126 C  CD    . GLN A 1 3227 ? 237.092 209.187 317.047 1.00 38.30 ? 3227 GLN A CD    1 
ATOM   14127 O  OE1   . GLN A 1 3227 ? 237.004 210.197 316.350 1.00 39.53 ? 3227 GLN A OE1   1 
ATOM   14128 N  NE2   . GLN A 1 3227 ? 237.803 209.150 318.169 1.00 37.05 ? 3227 GLN A NE2   1 
ATOM   14129 N  N     . GLU A 1 3228 ? 233.650 210.790 315.364 1.00 36.51 ? 3228 GLU A N     1 
ATOM   14130 C  CA    . GLU A 1 3228 ? 233.475 212.210 315.649 1.00 35.92 ? 3228 GLU A CA    1 
ATOM   14131 C  C     . GLU A 1 3228 ? 232.244 212.450 316.514 1.00 37.83 ? 3228 GLU A C     1 
ATOM   14132 O  O     . GLU A 1 3228 ? 232.273 213.279 317.432 1.00 35.03 ? 3228 GLU A O     1 
ATOM   14133 C  CB    . GLU A 1 3228 ? 233.377 212.998 314.343 1.00 33.64 ? 3228 GLU A CB    1 
ATOM   14134 C  CG    . GLU A 1 3228 ? 233.298 214.504 314.526 1.00 36.29 ? 3228 GLU A CG    1 
ATOM   14135 C  CD    . GLU A 1 3228 ? 233.294 215.250 313.206 1.00 38.95 ? 3228 GLU A CD    1 
ATOM   14136 O  OE1   . GLU A 1 3228 ? 233.338 214.590 312.148 1.00 38.12 ? 3228 GLU A OE1   1 
ATOM   14137 O  OE2   . GLU A 1 3228 ? 233.245 216.498 313.228 1.00 39.54 ? 3228 GLU A OE2   1 
ATOM   14138 N  N     . LEU A 1 3229 ? 231.152 211.734 316.234 1.00 39.21 ? 3229 LEU A N     1 
ATOM   14139 C  CA    . LEU A 1 3229 ? 229.950 211.867 317.052 1.00 35.83 ? 3229 LEU A CA    1 
ATOM   14140 C  C     . LEU A 1 3229 ? 230.203 211.425 318.487 1.00 38.90 ? 3229 LEU A C     1 
ATOM   14141 O  O     . LEU A 1 3229 ? 229.730 212.065 319.434 1.00 38.07 ? 3229 LEU A O     1 
ATOM   14142 C  CB    . LEU A 1 3229 ? 228.806 211.062 316.439 1.00 35.68 ? 3229 LEU A CB    1 
ATOM   14143 C  CG    . LEU A 1 3229 ? 228.147 211.684 315.209 1.00 38.17 ? 3229 LEU A CG    1 
ATOM   14144 C  CD1   . LEU A 1 3229 ? 227.075 210.766 314.649 1.00 35.60 ? 3229 LEU A CD1   1 
ATOM   14145 C  CD2   . LEU A 1 3229 ? 227.566 213.037 315.570 1.00 33.67 ? 3229 LEU A CD2   1 
ATOM   14146 N  N     . GLU A 1 3230 ? 230.941 210.327 318.669 1.00 38.22 ? 3230 GLU A N     1 
ATOM   14147 C  CA    . GLU A 1 3230 ? 231.243 209.855 320.016 1.00 36.44 ? 3230 GLU A CA    1 
ATOM   14148 C  C     . GLU A 1 3230 ? 232.078 210.873 320.784 1.00 38.56 ? 3230 GLU A C     1 
ATOM   14149 O  O     . GLU A 1 3230 ? 231.844 211.106 321.975 1.00 38.72 ? 3230 GLU A O     1 
ATOM   14150 C  CB    . GLU A 1 3230 ? 231.965 208.510 319.951 1.00 34.97 ? 3230 GLU A CB    1 
ATOM   14151 C  CG    . GLU A 1 3230 ? 231.137 207.387 319.348 1.00 36.87 ? 3230 GLU A CG    1 
ATOM   14152 C  CD    . GLU A 1 3230 ? 231.991 206.298 318.731 1.00 43.93 ? 3230 GLU A CD    1 
ATOM   14153 O  OE1   . GLU A 1 3230 ? 233.234 206.412 318.786 1.00 42.69 ? 3230 GLU A OE1   1 
ATOM   14154 O  OE2   . GLU A 1 3230 ? 231.421 205.327 318.190 1.00 45.62 ? 3230 GLU A OE2   1 
ATOM   14155 N  N     . VAL A 1 3231 ? 233.059 211.486 320.120 1.00 35.72 ? 3231 VAL A N     1 
ATOM   14156 C  CA    . VAL A 1 3231 ? 233.906 212.474 320.784 1.00 33.47 ? 3231 VAL A CA    1 
ATOM   14157 C  C     . VAL A 1 3231 ? 233.106 213.730 321.109 1.00 38.89 ? 3231 VAL A C     1 
ATOM   14158 O  O     . VAL A 1 3231 ? 233.171 214.256 322.226 1.00 38.94 ? 3231 VAL A O     1 
ATOM   14159 C  CB    . VAL A 1 3231 ? 235.135 212.793 319.915 1.00 36.42 ? 3231 VAL A CB    1 
ATOM   14160 C  CG1   . VAL A 1 3231 ? 235.772 214.105 320.349 1.00 30.61 ? 3231 VAL A CG1   1 
ATOM   14161 C  CG2   . VAL A 1 3231 ? 236.143 211.655 319.982 1.00 33.48 ? 3231 VAL A CG2   1 
ATOM   14162 N  N     . LYS A 1 3232 ? 232.337 214.230 320.137 1.00 36.97 ? 3232 LYS A N     1 
ATOM   14163 C  CA    . LYS A 1 3232 ? 231.565 215.451 320.355 1.00 35.26 ? 3232 LYS A CA    1 
ATOM   14164 C  C     . LYS A 1 3232 ? 230.492 215.252 321.420 1.00 37.70 ? 3232 LYS A C     1 
ATOM   14165 O  O     . LYS A 1 3232 ? 230.288 216.125 322.271 1.00 39.07 ? 3232 LYS A O     1 
ATOM   14166 C  CB    . LYS A 1 3232 ? 230.938 215.919 319.042 1.00 36.72 ? 3232 LYS A CB    1 
ATOM   14167 C  CG    . LYS A 1 3232 ? 231.938 216.452 318.028 1.00 37.19 ? 3232 LYS A CG    1 
ATOM   14168 C  CD    . LYS A 1 3232 ? 232.959 217.370 318.682 1.00 31.53 ? 3232 LYS A CD    1 
ATOM   14169 C  CE    . LYS A 1 3232 ? 234.209 217.503 317.827 1.00 36.71 ? 3232 LYS A CE    1 
ATOM   14170 N  NZ    . LYS A 1 3232 ? 235.294 218.231 318.540 1.00 30.94 ? 3232 LYS A NZ    1 
ATOM   14171 N  N     . ASN A 1 3233 ? 229.789 214.117 321.382 1.00 34.86 ? 3233 ASN A N     1 
ATOM   14172 C  CA    . ASN A 1 3233 ? 228.749 213.862 322.375 1.00 35.56 ? 3233 ASN A CA    1 
ATOM   14173 C  C     . ASN A 1 3233 ? 229.339 213.729 323.774 1.00 38.93 ? 3233 ASN A C     1 
ATOM   14174 O  O     . ASN A 1 3233 ? 228.783 214.261 324.741 1.00 36.89 ? 3233 ASN A O     1 
ATOM   14175 C  CB    . ASN A 1 3233 ? 227.961 212.607 322.001 1.00 34.17 ? 3233 ASN A CB    1 
ATOM   14176 C  CG    . ASN A 1 3233 ? 226.567 212.593 322.597 1.00 37.48 ? 3233 ASN A CG    1 
ATOM   14177 O  OD1   . ASN A 1 3233 ? 226.377 212.918 323.770 1.00 40.13 ? 3233 ASN A OD1   1 
ATOM   14178 N  ND2   . ASN A 1 3233 ? 225.582 212.218 321.789 1.00 35.94 ? 3233 ASN A ND2   1 
ATOM   14179 N  N     . ALA A 1 3234 ? 230.463 213.018 323.901 1.00 38.96 ? 3234 ALA A N     1 
ATOM   14180 C  CA    . ALA A 1 3234 ? 231.098 212.870 325.206 1.00 37.22 ? 3234 ALA A CA    1 
ATOM   14181 C  C     . ALA A 1 3234 ? 231.601 214.208 325.731 1.00 38.81 ? 3234 ALA A C     1 
ATOM   14182 O  O     . ALA A 1 3234 ? 231.446 214.516 326.919 1.00 38.28 ? 3234 ALA A O     1 
ATOM   14183 C  CB    . ALA A 1 3234 ? 232.243 211.860 325.123 1.00 32.01 ? 3234 ALA A CB    1 
ATOM   14184 N  N     . ALA A 1 3235 ? 232.211 215.017 324.861 1.00 37.10 ? 3235 ALA A N     1 
ATOM   14185 C  CA    . ALA A 1 3235 ? 232.702 216.325 325.285 1.00 35.49 ? 3235 ALA A CA    1 
ATOM   14186 C  C     . ALA A 1 3235 ? 231.553 217.235 325.700 1.00 39.47 ? 3235 ALA A C     1 
ATOM   14187 O  O     . ALA A 1 3235 ? 231.656 217.963 326.696 1.00 39.03 ? 3235 ALA A O     1 
ATOM   14188 C  CB    . ALA A 1 3235 ? 233.520 216.968 324.166 1.00 31.49 ? 3235 ALA A CB    1 
ATOM   14189 N  N     . ALA A 1 3236 ? 230.453 217.214 324.947 1.00 38.46 ? 3236 ALA A N     1 
ATOM   14190 C  CA    . ALA A 1 3236 ? 229.298 218.032 325.299 1.00 34.63 ? 3236 ALA A CA    1 
ATOM   14191 C  C     . ALA A 1 3236 ? 228.681 217.583 326.619 1.00 38.19 ? 3236 ALA A C     1 
ATOM   14192 O  O     . ALA A 1 3236 ? 228.288 218.416 327.443 1.00 36.47 ? 3236 ALA A O     1 
ATOM   14193 C  CB    . ALA A 1 3236 ? 228.260 217.988 324.178 1.00 32.78 ? 3236 ALA A CB    1 
ATOM   14194 N  N     . ASN A 1 3237 ? 228.581 216.267 326.832 1.00 35.38 ? 3237 ASN A N     1 
ATOM   14195 C  CA    . ASN A 1 3237 ? 228.016 215.762 328.081 1.00 34.16 ? 3237 ASN A CA    1 
ATOM   14196 C  C     . ASN A 1 3237 ? 228.888 216.134 329.274 1.00 37.49 ? 3237 ASN A C     1 
ATOM   14197 O  O     . ASN A 1 3237 ? 228.375 216.533 330.326 1.00 39.46 ? 3237 ASN A O     1 
ATOM   14198 C  CB    . ASN A 1 3237 ? 227.835 214.247 327.999 1.00 35.34 ? 3237 ASN A CB    1 
ATOM   14199 C  CG    . ASN A 1 3237 ? 226.707 213.845 327.068 1.00 39.86 ? 3237 ASN A CG    1 
ATOM   14200 O  OD1   . ASN A 1 3237 ? 225.988 214.694 326.542 1.00 37.63 ? 3237 ASN A OD1   1 
ATOM   14201 N  ND2   . ASN A 1 3237 ? 226.547 212.542 326.861 1.00 34.19 ? 3237 ASN A ND2   1 
ATOM   14202 N  N     . ASP A 1 3238 ? 230.210 216.004 329.132 1.00 36.20 ? 3238 ASP A N     1 
ATOM   14203 C  CA    . ASP A 1 3238 ? 231.110 216.361 330.224 1.00 36.40 ? 3238 ASP A CA    1 
ATOM   14204 C  C     . ASP A 1 3238 ? 231.046 217.852 330.528 1.00 37.06 ? 3238 ASP A C     1 
ATOM   14205 O  O     . ASP A 1 3238 ? 231.048 218.255 331.696 1.00 37.04 ? 3238 ASP A O     1 
ATOM   14206 C  CB    . ASP A 1 3238 ? 232.542 215.942 329.883 1.00 35.55 ? 3238 ASP A CB    1 
ATOM   14207 C  CG    . ASP A 1 3238 ? 232.691 214.441 329.742 1.00 40.65 ? 3238 ASP A CG    1 
ATOM   14208 O  OD1   . ASP A 1 3238 ? 231.692 213.720 329.945 1.00 40.52 ? 3238 ASP A OD1   1 
ATOM   14209 O  OD2   . ASP A 1 3238 ? 233.809 213.981 329.427 1.00 36.82 ? 3238 ASP A OD2   1 
ATOM   14210 N  N     . LYS A 1 3239 ? 230.991 218.687 329.487 1.00 34.61 ? 3239 LYS A N     1 
ATOM   14211 C  CA    . LYS A 1 3239 ? 230.888 220.127 329.701 1.00 36.31 ? 3239 LYS A CA    1 
ATOM   14212 C  C     . LYS A 1 3239 ? 229.557 220.497 330.343 1.00 38.56 ? 3239 LYS A C     1 
ATOM   14213 O  O     . LYS A 1 3239 ? 229.506 221.380 331.208 1.00 40.17 ? 3239 LYS A O     1 
ATOM   14214 C  CB    . LYS A 1 3239 ? 231.071 220.866 328.374 1.00 36.88 ? 3239 LYS A CB    1 
ATOM   14215 C  CG    . LYS A 1 3239 ? 232.517 220.970 327.921 1.00 36.45 ? 3239 LYS A CG    1 
ATOM   14216 C  CD    . LYS A 1 3239 ? 232.620 221.561 326.524 1.00 35.89 ? 3239 LYS A CD    1 
ATOM   14217 C  CE    . LYS A 1 3239 ? 234.022 221.401 325.959 1.00 34.80 ? 3239 LYS A CE    1 
ATOM   14218 N  NZ    . LYS A 1 3239 ? 234.098 221.816 324.531 1.00 31.91 ? 3239 LYS A NZ    1 
ATOM   14219 N  N     . LEU A 1 3240 ? 228.471 219.840 329.931 1.00 38.25 ? 3240 LEU A N     1 
ATOM   14220 C  CA    . LEU A 1 3240 ? 227.169 220.112 330.530 1.00 35.58 ? 3240 LEU A CA    1 
ATOM   14221 C  C     . LEU A 1 3240 ? 227.123 219.685 331.992 1.00 39.22 ? 3240 LEU A C     1 
ATOM   14222 O  O     . LEU A 1 3240 ? 226.500 220.365 332.814 1.00 39.92 ? 3240 LEU A O     1 
ATOM   14223 C  CB    . LEU A 1 3240 ? 226.068 219.410 329.736 1.00 36.86 ? 3240 LEU A CB    1 
ATOM   14224 C  CG    . LEU A 1 3240 ? 225.349 220.262 328.688 1.00 39.77 ? 3240 LEU A CG    1 
ATOM   14225 C  CD1   . LEU A 1 3240 ? 224.208 219.484 328.052 1.00 32.39 ? 3240 LEU A CD1   1 
ATOM   14226 C  CD2   . LEU A 1 3240 ? 224.843 221.557 329.305 1.00 33.59 ? 3240 LEU A CD2   1 
ATOM   14227 N  N     . LYS A 1 3241 ? 227.771 218.570 332.334 1.00 36.74 ? 3241 LYS A N     1 
ATOM   14228 C  CA    . LYS A 1 3241 ? 227.795 218.095 333.712 1.00 34.93 ? 3241 LYS A CA    1 
ATOM   14229 C  C     . LYS A 1 3241 ? 228.599 218.999 334.638 1.00 35.77 ? 3241 LYS A C     1 
ATOM   14230 O  O     . LYS A 1 3241 ? 228.478 218.865 335.860 1.00 36.38 ? 3241 LYS A O     1 
ATOM   14231 C  CB    . LYS A 1 3241 ? 228.358 216.673 333.767 1.00 33.29 ? 3241 LYS A CB    1 
ATOM   14232 C  CG    . LYS A 1 3241 ? 227.392 215.602 333.291 1.00 32.27 ? 3241 LYS A CG    1 
ATOM   14233 C  CD    . LYS A 1 3241 ? 228.126 214.330 332.904 1.00 35.55 ? 3241 LYS A CD    1 
ATOM   14234 C  CE    . LYS A 1 3241 ? 227.239 213.407 332.082 1.00 32.84 ? 3241 LYS A CE    1 
ATOM   14235 N  NZ    . LYS A 1 3241 ? 228.008 212.270 331.504 1.00 34.41 ? 3241 LYS A NZ    1 
ATOM   14236 N  N     . GLU A 1 3449 ? 225.056 227.926 327.306 1.00 35.51 ? 3449 GLU A N     1 
ATOM   14237 C  CA    . GLU A 1 3449 ? 224.636 228.506 326.035 1.00 38.41 ? 3449 GLU A CA    1 
ATOM   14238 C  C     . GLU A 1 3449 ? 225.504 227.997 324.888 1.00 41.25 ? 3449 GLU A C     1 
ATOM   14239 O  O     . GLU A 1 3449 ? 224.993 227.597 323.843 1.00 41.70 ? 3449 GLU A O     1 
ATOM   14240 C  CB    . GLU A 1 3449 ? 224.687 230.033 326.100 1.00 36.95 ? 3449 GLU A CB    1 
ATOM   14241 C  CG    . GLU A 1 3449 ? 223.848 230.629 327.217 1.00 35.67 ? 3449 GLU A CG    1 
ATOM   14242 C  CD    . GLU A 1 3449 ? 223.928 232.142 327.264 1.00 42.81 ? 3449 GLU A CD    1 
ATOM   14243 O  OE1   . GLU A 1 3449 ? 224.671 232.724 326.446 1.00 43.39 ? 3449 GLU A OE1   1 
ATOM   14244 O  OE2   . GLU A 1 3449 ? 223.248 232.749 328.117 1.00 39.68 ? 3449 GLU A OE2   1 
ATOM   14245 N  N     . GLU A 1 3450 ? 226.823 228.021 325.092 1.00 40.55 ? 3450 GLU A N     1 
ATOM   14246 C  CA    . GLU A 1 3450 ? 227.735 227.502 324.078 1.00 39.22 ? 3450 GLU A CA    1 
ATOM   14247 C  C     . GLU A 1 3450 ? 227.589 225.996 323.912 1.00 37.47 ? 3450 GLU A C     1 
ATOM   14248 O  O     . GLU A 1 3450 ? 227.759 225.476 322.802 1.00 40.12 ? 3450 GLU A O     1 
ATOM   14249 C  CB    . GLU A 1 3450 ? 229.177 227.864 324.431 1.00 37.29 ? 3450 GLU A CB    1 
ATOM   14250 C  CG    . GLU A 1 3450 ? 230.184 227.547 323.337 1.00 34.96 ? 3450 GLU A CG    1 
ATOM   14251 C  CD    . GLU A 1 3450 ? 231.504 228.266 323.532 1.00 40.69 ? 3450 GLU A CD    1 
ATOM   14252 O  OE1   . GLU A 1 3450 ? 231.714 228.841 324.620 1.00 40.03 ? 3450 GLU A OE1   1 
ATOM   14253 O  OE2   . GLU A 1 3450 ? 232.332 228.255 322.596 1.00 38.89 ? 3450 GLU A OE2   1 
ATOM   14254 N  N     . TYR A 1 3451 ? 227.277 225.281 324.996 1.00 36.10 ? 3451 TYR A N     1 
ATOM   14255 C  CA    . TYR A 1 3451 ? 227.067 223.840 324.901 1.00 36.43 ? 3451 TYR A CA    1 
ATOM   14256 C  C     . TYR A 1 3451 ? 225.857 223.505 324.040 1.00 37.71 ? 3451 TYR A C     1 
ATOM   14257 O  O     . TYR A 1 3451 ? 225.815 222.435 323.422 1.00 35.77 ? 3451 TYR A O     1 
ATOM   14258 C  CB    . TYR A 1 3451 ? 226.913 223.238 326.298 1.00 37.82 ? 3451 TYR A CB    1 
ATOM   14259 C  CG    . TYR A 1 3451 ? 227.933 223.737 327.298 1.00 39.02 ? 3451 TYR A CG    1 
ATOM   14260 C  CD1   . TYR A 1 3451 ? 229.282 223.807 326.968 1.00 38.15 ? 3451 TYR A CD1   1 
ATOM   14261 C  CD2   . TYR A 1 3451 ? 227.549 224.143 328.568 1.00 37.99 ? 3451 TYR A CD2   1 
ATOM   14262 C  CE1   . TYR A 1 3451 ? 230.216 224.265 327.877 1.00 38.49 ? 3451 TYR A CE1   1 
ATOM   14263 C  CE2   . TYR A 1 3451 ? 228.476 224.601 329.483 1.00 38.48 ? 3451 TYR A CE2   1 
ATOM   14264 C  CZ    . TYR A 1 3451 ? 229.809 224.660 329.133 1.00 42.95 ? 3451 TYR A CZ    1 
ATOM   14265 O  OH    . TYR A 1 3451 ? 230.735 225.116 330.042 1.00 45.01 ? 3451 TYR A OH    1 
ATOM   14266 N  N     . ALA A 1 3452 ? 224.866 224.399 323.991 1.00 40.27 ? 3452 ALA A N     1 
ATOM   14267 C  CA    . ALA A 1 3452 ? 223.728 224.194 323.101 1.00 38.88 ? 3452 ALA A CA    1 
ATOM   14268 C  C     . ALA A 1 3452 ? 224.164 224.223 321.642 1.00 39.33 ? 3452 ALA A C     1 
ATOM   14269 O  O     . ALA A 1 3452 ? 223.633 223.478 320.811 1.00 38.27 ? 3452 ALA A O     1 
ATOM   14270 C  CB    . ALA A 1 3452 ? 222.656 225.250 323.364 1.00 33.51 ? 3452 ALA A CB    1 
ATOM   14271 N  N     . VAL A 1 3453 ? 225.123 225.089 321.309 1.00 35.52 ? 3453 VAL A N     1 
ATOM   14272 C  CA    . VAL A 1 3453 ? 225.681 225.092 319.962 1.00 34.84 ? 3453 VAL A CA    1 
ATOM   14273 C  C     . VAL A 1 3453 ? 226.471 223.813 319.709 1.00 36.93 ? 3453 VAL A C     1 
ATOM   14274 O  O     . VAL A 1 3453 ? 226.434 223.251 318.608 1.00 35.86 ? 3453 VAL A O     1 
ATOM   14275 C  CB    . VAL A 1 3453 ? 226.547 226.347 319.744 1.00 34.12 ? 3453 VAL A CB    1 
ATOM   14276 C  CG1   . VAL A 1 3453 ? 227.077 226.392 318.318 1.00 32.51 ? 3453 VAL A CG1   1 
ATOM   14277 C  CG2   . VAL A 1 3453 ? 225.748 227.602 320.063 1.00 30.75 ? 3453 VAL A CG2   1 
ATOM   14278 N  N     . LEU A 1 3454 ? 227.195 223.333 320.724 1.00 35.34 ? 3454 LEU A N     1 
ATOM   14279 C  CA    . LEU A 1 3454 ? 227.995 222.123 320.560 1.00 36.04 ? 3454 LEU A CA    1 
ATOM   14280 C  C     . LEU A 1 3454 ? 227.118 220.907 320.292 1.00 37.88 ? 3454 LEU A C     1 
ATOM   14281 O  O     . LEU A 1 3454 ? 227.433 220.089 319.419 1.00 37.52 ? 3454 LEU A O     1 
ATOM   14282 C  CB    . LEU A 1 3454 ? 228.861 221.897 321.799 1.00 37.98 ? 3454 LEU A CB    1 
ATOM   14283 C  CG    . LEU A 1 3454 ? 230.037 220.932 321.636 1.00 38.92 ? 3454 LEU A CG    1 
ATOM   14284 C  CD1   . LEU A 1 3454 ? 231.039 221.471 320.626 1.00 32.67 ? 3454 LEU A CD1   1 
ATOM   14285 C  CD2   . LEU A 1 3454 ? 230.708 220.670 322.976 1.00 33.91 ? 3454 LEU A CD2   1 
ATOM   14286 N  N     . ILE A 1 3455 ? 226.016 220.763 321.033 1.00 35.87 ? 3455 ILE A N     1 
ATOM   14287 C  CA    . ILE A 1 3455 ? 225.119 219.639 320.788 1.00 37.04 ? 3455 ILE A CA    1 
ATOM   14288 C  C     . ILE A 1 3455 ? 224.385 219.819 319.464 1.00 36.73 ? 3455 ILE A C     1 
ATOM   14289 O  O     . ILE A 1 3455 ? 224.053 218.834 318.792 1.00 35.72 ? 3455 ILE A O     1 
ATOM   14290 C  CB    . ILE A 1 3455 ? 224.140 219.449 321.964 1.00 36.36 ? 3455 ILE A CB    1 
ATOM   14291 C  CG1   . ILE A 1 3455 ? 223.207 220.651 322.105 1.00 36.94 ? 3455 ILE A CG1   1 
ATOM   14292 C  CG2   . ILE A 1 3455 ? 224.903 219.213 323.257 1.00 28.33 ? 3455 ILE A CG2   1 
ATOM   14293 C  CD1   . ILE A 1 3455 ? 222.069 220.430 323.079 1.00 31.58 ? 3455 ILE A CD1   1 
ATOM   14294 N  N     . SER A 1 3456 ? 224.114 221.067 319.070 1.00 34.64 ? 3456 SER A N     1 
ATOM   14295 C  CA    . SER A 1 3456 ? 223.542 221.315 317.751 1.00 36.57 ? 3456 SER A CA    1 
ATOM   14296 C  C     . SER A 1 3456 ? 224.517 220.914 316.652 1.00 37.44 ? 3456 SER A C     1 
ATOM   14297 O  O     . SER A 1 3456 ? 224.112 220.368 315.619 1.00 36.99 ? 3456 SER A O     1 
ATOM   14298 C  CB    . SER A 1 3456 ? 223.150 222.785 317.615 1.00 32.94 ? 3456 SER A CB    1 
ATOM   14299 O  OG    . SER A 1 3456 ? 224.282 223.589 317.324 1.00 36.85 ? 3456 SER A OG    1 
ATOM   14300 N  N     . GLU A 1 3457 ? 225.808 221.186 316.856 1.00 34.30 ? 3457 GLU A N     1 
ATOM   14301 C  CA    . GLU A 1 3457 ? 226.818 220.747 315.898 1.00 35.11 ? 3457 GLU A CA    1 
ATOM   14302 C  C     . GLU A 1 3457 ? 226.871 219.227 315.816 1.00 37.23 ? 3457 GLU A C     1 
ATOM   14303 O  O     . GLU A 1 3457 ? 226.999 218.661 314.725 1.00 38.82 ? 3457 GLU A O     1 
ATOM   14304 C  CB    . GLU A 1 3457 ? 228.183 221.318 316.281 1.00 30.82 ? 3457 GLU A CB    1 
ATOM   14305 C  CG    . GLU A 1 3457 ? 229.255 221.159 315.212 1.00 31.64 ? 3457 GLU A CG    1 
ATOM   14306 C  CD    . GLU A 1 3457 ? 230.025 219.860 315.346 1.00 41.80 ? 3457 GLU A CD    1 
ATOM   14307 O  OE1   . GLU A 1 3457 ? 230.112 219.332 316.476 1.00 43.62 ? 3457 GLU A OE1   1 
ATOM   14308 O  OE2   . GLU A 1 3457 ? 230.546 219.367 314.324 1.00 41.20 ? 3457 GLU A OE2   1 
ATOM   14309 N  N     . ALA A 1 3458 ? 226.776 218.550 316.963 1.00 35.05 ? 3458 ALA A N     1 
ATOM   14310 C  CA    . ALA A 1 3458 ? 226.741 217.092 316.961 1.00 36.19 ? 3458 ALA A CA    1 
ATOM   14311 C  C     . ALA A 1 3458 ? 225.498 216.574 316.249 1.00 37.76 ? 3458 ALA A C     1 
ATOM   14312 O  O     . ALA A 1 3458 ? 225.568 215.590 315.500 1.00 38.95 ? 3458 ALA A O     1 
ATOM   14313 C  CB    . ALA A 1 3458 ? 226.800 216.562 318.394 1.00 31.95 ? 3458 ALA A CB    1 
ATOM   14314 N  N     . GLN A 1 3459 ? 224.350 217.219 316.472 1.00 37.77 ? 3459 GLN A N     1 
ATOM   14315 C  CA    . GLN A 1 3459 ? 223.126 216.810 315.789 1.00 37.96 ? 3459 GLN A CA    1 
ATOM   14316 C  C     . GLN A 1 3459 ? 223.242 217.013 314.284 1.00 38.14 ? 3459 GLN A C     1 
ATOM   14317 O  O     . GLN A 1 3459 ? 222.746 216.198 313.498 1.00 37.20 ? 3459 GLN A O     1 
ATOM   14318 C  CB    . GLN A 1 3459 ? 221.930 217.578 316.349 1.00 32.77 ? 3459 GLN A CB    1 
ATOM   14319 C  CG    . GLN A 1 3459 ? 220.589 217.130 315.790 1.00 34.91 ? 3459 GLN A CG    1 
ATOM   14320 C  CD    . GLN A 1 3459 ? 219.417 217.797 316.480 1.00 40.82 ? 3459 GLN A CD    1 
ATOM   14321 O  OE1   . GLN A 1 3459 ? 219.203 217.617 317.680 1.00 37.46 ? 3459 GLN A OE1   1 
ATOM   14322 N  NE2   . GLN A 1 3459 ? 218.648 218.572 315.724 1.00 34.15 ? 3459 GLN A NE2   1 
ATOM   14323 N  N     . ALA A 1 3460 ? 223.887 218.105 313.864 1.00 36.07 ? 3460 ALA A N     1 
ATOM   14324 C  CA    . ALA A 1 3460 ? 224.097 218.337 312.438 1.00 35.03 ? 3460 ALA A CA    1 
ATOM   14325 C  C     . ALA A 1 3460 ? 224.966 217.244 311.825 1.00 37.93 ? 3460 ALA A C     1 
ATOM   14326 O  O     . ALA A 1 3460 ? 224.707 216.791 310.704 1.00 38.85 ? 3460 ALA A O     1 
ATOM   14327 C  CB    . ALA A 1 3460 ? 224.726 219.712 312.216 1.00 27.91 ? 3460 ALA A CB    1 
ATOM   14328 N  N     . ILE A 1 3461 ? 226.003 216.814 312.546 1.00 35.07 ? 3461 ILE A N     1 
ATOM   14329 C  CA    . ILE A 1 3461 ? 226.839 215.717 312.067 1.00 34.96 ? 3461 ILE A CA    1 
ATOM   14330 C  C     . ILE A 1 3461 ? 226.040 214.421 312.004 1.00 35.17 ? 3461 ILE A C     1 
ATOM   14331 O  O     . ILE A 1 3461 ? 226.261 213.591 311.112 1.00 36.26 ? 3461 ILE A O     1 
ATOM   14332 C  CB    . ILE A 1 3461 ? 228.089 215.575 312.953 1.00 33.09 ? 3461 ILE A CB    1 
ATOM   14333 C  CG1   . ILE A 1 3461 ? 228.914 216.864 312.919 1.00 35.00 ? 3461 ILE A CG1   1 
ATOM   14334 C  CG2   . ILE A 1 3461 ? 228.944 214.404 312.499 1.00 34.30 ? 3461 ILE A CG2   1 
ATOM   14335 C  CD1   . ILE A 1 3461 ? 229.200 217.372 311.523 1.00 34.60 ? 3461 ILE A CD1   1 
ATOM   14336 N  N     . LYS A 1 3462 ? 225.102 214.224 312.935 1.00 33.51 ? 3462 LYS A N     1 
ATOM   14337 C  CA    . LYS A 1 3462 ? 224.249 213.037 312.890 1.00 34.82 ? 3462 LYS A CA    1 
ATOM   14338 C  C     . LYS A 1 3462 ? 223.466 212.977 311.586 1.00 32.99 ? 3462 LYS A C     1 
ATOM   14339 O  O     . LYS A 1 3462 ? 223.311 211.901 310.995 1.00 32.52 ? 3462 LYS A O     1 
ATOM   14340 C  CB    . LYS A 1 3462 ? 223.297 213.025 314.088 1.00 32.51 ? 3462 LYS A CB    1 
ATOM   14341 C  CG    . LYS A 1 3462 ? 223.964 212.726 315.419 1.00 34.64 ? 3462 LYS A CG    1 
ATOM   14342 C  CD    . LYS A 1 3462 ? 222.953 212.252 316.451 1.00 32.67 ? 3462 LYS A CD    1 
ATOM   14343 C  CE    . LYS A 1 3462 ? 222.423 210.869 316.112 1.00 31.00 ? 3462 LYS A CE    1 
ATOM   14344 N  NZ    . LYS A 1 3462 ? 223.520 209.872 315.983 1.00 30.22 ? 3462 LYS A NZ    1 
ATOM   14345 N  N     . ALA A 1 3463 ? 222.957 214.122 311.125 1.00 34.07 ? 3463 ALA A N     1 
ATOM   14346 C  CA    . ALA A 1 3463 ? 222.306 214.166 309.820 1.00 36.75 ? 3463 ALA A CA    1 
ATOM   14347 C  C     . ALA A 1 3463 ? 223.289 213.835 308.706 1.00 36.87 ? 3463 ALA A C     1 
ATOM   14348 O  O     . ALA A 1 3463 ? 222.936 213.149 307.738 1.00 38.31 ? 3463 ALA A O     1 
ATOM   14349 C  CB    . ALA A 1 3463 ? 221.676 215.540 309.593 1.00 28.57 ? 3463 ALA A CB    1 
ATOM   14350 N  N     . ASP A 1 3464 ? 224.529 214.320 308.820 1.00 32.95 ? 3464 ASP A N     1 
ATOM   14351 C  CA    . ASP A 1 3464 ? 225.548 213.992 307.829 1.00 33.86 ? 3464 ASP A CA    1 
ATOM   14352 C  C     . ASP A 1 3464 ? 225.840 212.496 307.813 1.00 36.45 ? 3464 ASP A C     1 
ATOM   14353 O  O     . ASP A 1 3464 ? 225.985 211.895 306.742 1.00 35.01 ? 3464 ASP A O     1 
ATOM   14354 C  CB    . ASP A 1 3464 ? 226.823 214.785 308.106 1.00 34.00 ? 3464 ASP A CB    1 
ATOM   14355 C  CG    . ASP A 1 3464 ? 227.761 214.818 306.915 1.00 38.62 ? 3464 ASP A CG    1 
ATOM   14356 O  OD1   . ASP A 1 3464 ? 227.339 214.409 305.812 1.00 40.12 ? 3464 ASP A OD1   1 
ATOM   14357 O  OD2   . ASP A 1 3464 ? 228.919 215.253 307.081 1.00 39.00 ? 3464 ASP A OD2   1 
ATOM   14358 N  N     . LEU A 1 3465 ? 225.936 211.878 308.994 1.00 34.46 ? 3465 LEU A N     1 
ATOM   14359 C  CA    . LEU A 1 3465 ? 226.153 210.437 309.059 1.00 31.51 ? 3465 LEU A CA    1 
ATOM   14360 C  C     . LEU A 1 3465 ? 224.966 209.678 308.479 1.00 36.17 ? 3465 LEU A C     1 
ATOM   14361 O  O     . LEU A 1 3465 ? 225.141 208.653 307.811 1.00 36.25 ? 3465 LEU A O     1 
ATOM   14362 C  CB    . LEU A 1 3465 ? 226.419 210.011 310.503 1.00 30.51 ? 3465 LEU A CB    1 
ATOM   14363 C  CG    . LEU A 1 3465 ? 226.823 208.556 310.751 1.00 33.76 ? 3465 LEU A CG    1 
ATOM   14364 C  CD1   . LEU A 1 3465 ? 227.882 208.484 311.837 1.00 33.90 ? 3465 LEU A CD1   1 
ATOM   14365 C  CD2   . LEU A 1 3465 ? 225.619 207.710 311.135 1.00 28.51 ? 3465 LEU A CD2   1 
ATOM   14366 N  N     . ALA A 1 3466 ? 223.748 210.163 308.733 1.00 35.53 ? 3466 ALA A N     1 
ATOM   14367 C  CA    . ALA A 1 3466 ? 222.566 209.540 308.145 1.00 34.57 ? 3466 ALA A CA    1 
ATOM   14368 C  C     . ALA A 1 3466 ? 222.598 209.632 306.625 1.00 35.98 ? 3466 ALA A C     1 
ATOM   14369 O  O     . ALA A 1 3466 ? 222.236 208.676 305.930 1.00 35.66 ? 3466 ALA A O     1 
ATOM   14370 C  CB    . ALA A 1 3466 ? 221.299 210.188 308.699 1.00 27.69 ? 3466 ALA A CB    1 
ATOM   14371 N  N     . ALA A 1 3467 ? 223.023 210.780 306.092 1.00 31.10 ? 3467 ALA A N     1 
ATOM   14372 C  CA    . ALA A 1 3467 ? 223.164 210.914 304.646 1.00 31.38 ? 3467 ALA A CA    1 
ATOM   14373 C  C     . ALA A 1 3467 ? 224.258 209.997 304.113 1.00 33.71 ? 3467 ALA A C     1 
ATOM   14374 O  O     . ALA A 1 3467 ? 224.137 209.455 303.007 1.00 34.50 ? 3467 ALA A O     1 
ATOM   14375 C  CB    . ALA A 1 3467 ? 223.455 212.368 304.279 1.00 28.44 ? 3467 ALA A CB    1 
ATOM   14376 N  N     . VAL A 1 3468 ? 225.338 209.823 304.877 1.00 31.64 ? 3468 VAL A N     1 
ATOM   14377 C  CA    . VAL A 1 3468 ? 226.433 208.964 304.438 1.00 29.36 ? 3468 VAL A CA    1 
ATOM   14378 C  C     . VAL A 1 3468 ? 226.002 207.500 304.440 1.00 30.04 ? 3468 VAL A C     1 
ATOM   14379 O  O     . VAL A 1 3468 ? 226.240 206.768 303.475 1.00 32.08 ? 3468 VAL A O     1 
ATOM   14380 C  CB    . VAL A 1 3468 ? 227.676 209.191 305.317 1.00 33.83 ? 3468 VAL A CB    1 
ATOM   14381 C  CG1   . VAL A 1 3468 ? 228.658 208.040 305.162 1.00 33.70 ? 3468 VAL A CG1   1 
ATOM   14382 C  CG2   . VAL A 1 3468 ? 228.343 210.509 304.957 1.00 32.66 ? 3468 VAL A CG2   1 
ATOM   14383 N  N     . GLU A 1 3469 ? 225.359 207.054 305.524 1.00 32.54 ? 3469 GLU A N     1 
ATOM   14384 C  CA    . GLU A 1 3469 ? 224.991 205.644 305.629 1.00 32.21 ? 3469 GLU A CA    1 
ATOM   14385 C  C     . GLU A 1 3469 ? 223.931 205.269 304.601 1.00 35.23 ? 3469 GLU A C     1 
ATOM   14386 O  O     . GLU A 1 3469 ? 223.955 204.160 304.054 1.00 38.26 ? 3469 GLU A O     1 
ATOM   14387 C  CB    . GLU A 1 3469 ? 224.517 205.316 307.046 1.00 30.24 ? 3469 GLU A CB    1 
ATOM   14388 C  CG    . GLU A 1 3469 ? 223.250 206.030 307.484 1.00 34.59 ? 3469 GLU A CG    1 
ATOM   14389 C  CD    . GLU A 1 3469 ? 222.827 205.650 308.889 1.00 37.95 ? 3469 GLU A CD    1 
ATOM   14390 O  OE1   . GLU A 1 3469 ? 222.495 204.467 309.111 1.00 35.43 ? 3469 GLU A OE1   1 
ATOM   14391 O  OE2   . GLU A 1 3469 ? 222.824 206.535 309.771 1.00 41.41 ? 3469 GLU A OE2   1 
ATOM   14392 N  N     . ALA A 1 3470 ? 222.994 206.179 304.322 1.00 33.04 ? 3470 ALA A N     1 
ATOM   14393 C  CA    . ALA A 1 3470 ? 222.015 205.929 303.270 1.00 34.07 ? 3470 ALA A CA    1 
ATOM   14394 C  C     . ALA A 1 3470 ? 222.690 205.838 301.910 1.00 35.82 ? 3470 ALA A C     1 
ATOM   14395 O  O     . ALA A 1 3470 ? 222.306 205.017 301.068 1.00 35.91 ? 3470 ALA A O     1 
ATOM   14396 C  CB    . ALA A 1 3470 ? 220.949 207.024 303.272 1.00 30.80 ? 3470 ALA A CB    1 
ATOM   14397 N  N     . LYS A 1 3471 ? 223.702 206.677 301.677 1.00 30.83 ? 3471 LYS A N     1 
ATOM   14398 C  CA    . LYS A 1 3471 ? 224.434 206.631 300.417 1.00 28.10 ? 3471 LYS A CA    1 
ATOM   14399 C  C     . LYS A 1 3471 ? 225.221 205.333 300.284 1.00 29.94 ? 3471 LYS A C     1 
ATOM   14400 O  O     . LYS A 1 3471 ? 225.380 204.808 299.175 1.00 30.76 ? 3471 LYS A O     1 
ATOM   14401 C  CB    . LYS A 1 3471 ? 225.360 207.843 300.315 1.00 28.88 ? 3471 LYS A CB    1 
ATOM   14402 C  CG    . LYS A 1 3471 ? 226.116 207.956 299.003 1.00 29.59 ? 3471 LYS A CG    1 
ATOM   14403 C  CD    . LYS A 1 3471 ? 227.103 209.109 299.048 1.00 29.89 ? 3471 LYS A CD    1 
ATOM   14404 C  CE    . LYS A 1 3471 ? 226.995 209.978 297.807 1.00 32.07 ? 3471 LYS A CE    1 
ATOM   14405 N  NZ    . LYS A 1 3471 ? 228.151 210.907 297.678 1.00 33.47 ? 3471 LYS A NZ    1 
ATOM   14406 N  N     . VAL A 1 3472 ? 225.723 204.805 301.401 1.00 33.43 ? 3472 VAL A N     1 
ATOM   14407 C  CA    . VAL A 1 3472 ? 226.447 203.536 301.365 1.00 31.08 ? 3472 VAL A CA    1 
ATOM   14408 C  C     . VAL A 1 3472 ? 225.510 202.404 300.963 1.00 32.88 ? 3472 VAL A C     1 
ATOM   14409 O  O     . VAL A 1 3472 ? 225.839 201.575 300.105 1.00 34.73 ? 3472 VAL A O     1 
ATOM   14410 C  CB    . VAL A 1 3472 ? 227.113 203.259 302.726 1.00 31.29 ? 3472 VAL A CB    1 
ATOM   14411 C  CG1   . VAL A 1 3472 ? 227.450 201.782 302.869 1.00 28.59 ? 3472 VAL A CG1   1 
ATOM   14412 C  CG2   . VAL A 1 3472 ? 228.357 204.106 302.891 1.00 31.88 ? 3472 VAL A CG2   1 
ATOM   14413 N  N     . ASN A 1 3473 ? 224.326 202.354 301.579 1.00 33.02 ? 3473 ASN A N     1 
ATOM   14414 C  CA    . ASN A 1 3473 ? 223.386 201.278 301.287 1.00 30.91 ? 3473 ASN A CA    1 
ATOM   14415 C  C     . ASN A 1 3473 ? 222.868 201.360 299.857 1.00 32.25 ? 3473 ASN A C     1 
ATOM   14416 O  O     . ASN A 1 3473 ? 222.748 200.336 299.174 1.00 34.98 ? 3473 ASN A O     1 
ATOM   14417 C  CB    . ASN A 1 3473 ? 222.225 201.314 302.281 1.00 28.38 ? 3473 ASN A CB    1 
ATOM   14418 C  CG    . ASN A 1 3473 ? 222.682 201.167 303.717 1.00 34.77 ? 3473 ASN A CG    1 
ATOM   14419 O  OD1   . ASN A 1 3473 ? 223.871 201.000 303.987 1.00 35.30 ? 3473 ASN A OD1   1 
ATOM   14420 N  ND2   . ASN A 1 3473 ? 221.739 201.230 304.649 1.00 33.37 ? 3473 ASN A ND2   1 
ATOM   14421 N  N     . ARG A 1 3474 ? 222.550 202.569 299.387 1.00 28.87 ? 3474 ARG A N     1 
ATOM   14422 C  CA    . ARG A 1 3474 ? 222.037 202.715 298.030 1.00 29.61 ? 3474 ARG A CA    1 
ATOM   14423 C  C     . ARG A 1 3474 ? 223.100 202.376 296.994 1.00 31.20 ? 3474 ARG A C     1 
ATOM   14424 O  O     . ARG A 1 3474 ? 222.806 201.725 295.986 1.00 31.62 ? 3474 ARG A O     1 
ATOM   14425 C  CB    . ARG A 1 3474 ? 221.508 204.134 297.817 1.00 29.01 ? 3474 ARG A CB    1 
ATOM   14426 C  CG    . ARG A 1 3474 ? 220.874 204.352 296.454 1.00 27.19 ? 3474 ARG A CG    1 
ATOM   14427 C  CD    . ARG A 1 3474 ? 220.335 205.761 296.302 1.00 28.20 ? 3474 ARG A CD    1 
ATOM   14428 N  NE    . ARG A 1 3474 ? 221.392 206.764 296.342 1.00 34.35 ? 3474 ARG A NE    1 
ATOM   14429 C  CZ    . ARG A 1 3474 ? 221.178 208.070 296.418 1.00 37.36 ? 3474 ARG A CZ    1 
ATOM   14430 N  NH1   . ARG A 1 3474 ? 219.954 208.569 296.459 1.00 35.49 ? 3474 ARG A NH1   1 
ATOM   14431 N  NH2   . ARG A 1 3474 ? 222.220 208.898 296.450 1.00 37.57 ? 3474 ARG A NH2   1 
ATOM   14432 N  N     . SER A 1 3475 ? 224.342 202.808 297.225 1.00 30.53 ? 3475 SER A N     1 
ATOM   14433 C  CA    . SER A 1 3475 ? 225.412 202.504 296.279 1.00 30.76 ? 3475 SER A CA    1 
ATOM   14434 C  C     . SER A 1 3475 ? 225.787 201.029 296.326 1.00 29.04 ? 3475 SER A C     1 
ATOM   14435 O  O     . SER A 1 3475 ? 226.147 200.443 295.300 1.00 33.31 ? 3475 SER A O     1 
ATOM   14436 C  CB    . SER A 1 3475 ? 226.631 203.380 296.566 1.00 32.55 ? 3475 SER A CB    1 
ATOM   14437 O  OG    . SER A 1 3475 ? 227.688 203.084 295.672 1.00 37.43 ? 3475 SER A OG    1 
ATOM   14438 N  N     . THR A 1 3476 ? 225.723 200.417 297.511 1.00 28.62 ? 3476 THR A N     1 
ATOM   14439 C  CA    . THR A 1 3476 ? 225.964 198.981 297.612 1.00 28.99 ? 3476 THR A CA    1 
ATOM   14440 C  C     . THR A 1 3476 ? 224.882 198.194 296.886 1.00 28.57 ? 3476 THR A C     1 
ATOM   14441 O  O     . THR A 1 3476 ? 225.176 197.207 296.201 1.00 34.35 ? 3476 THR A O     1 
ATOM   14442 C  CB    . THR A 1 3476 ? 226.043 198.563 299.080 1.00 28.01 ? 3476 THR A CB    1 
ATOM   14443 O  OG1   . THR A 1 3476 ? 227.046 199.343 299.745 1.00 32.04 ? 3476 THR A OG1   1 
ATOM   14444 C  CG2   . THR A 1 3476 ? 226.396 197.090 299.201 1.00 24.11 ? 3476 THR A CG2   1 
ATOM   14445 N  N     . ALA A 1 3477 ? 223.623 198.615 297.026 1.00 29.02 ? 3477 ALA A N     1 
ATOM   14446 C  CA    . ALA A 1 3477 ? 222.540 197.979 296.281 1.00 33.53 ? 3477 ALA A CA    1 
ATOM   14447 C  C     . ALA A 1 3477 ? 222.702 198.200 294.784 1.00 30.75 ? 3477 ALA A C     1 
ATOM   14448 O  O     . ALA A 1 3477 ? 222.422 197.302 293.980 1.00 28.94 ? 3477 ALA A O     1 
ATOM   14449 C  CB    . ALA A 1 3477 ? 221.189 198.507 296.763 1.00 29.54 ? 3477 ALA A CB    1 
ATOM   14450 N  N     . LEU A 1 3478 ? 223.144 199.398 294.389 1.00 29.50 ? 3478 LEU A N     1 
ATOM   14451 C  CA    . LEU A 1 3478 ? 223.452 199.647 292.985 1.00 26.09 ? 3478 LEU A CA    1 
ATOM   14452 C  C     . LEU A 1 3478 ? 224.563 198.730 292.497 1.00 28.22 ? 3478 LEU A C     1 
ATOM   14453 O  O     . LEU A 1 3478 ? 224.480 198.169 291.400 1.00 29.71 ? 3478 LEU A O     1 
ATOM   14454 C  CB    . LEU A 1 3478 ? 223.842 201.112 292.786 1.00 23.67 ? 3478 LEU A CB    1 
ATOM   14455 C  CG    . LEU A 1 3478 ? 224.257 201.525 291.372 1.00 31.25 ? 3478 LEU A CG    1 
ATOM   14456 C  CD1   . LEU A 1 3478 ? 223.061 201.532 290.438 1.00 26.62 ? 3478 LEU A CD1   1 
ATOM   14457 C  CD2   . LEU A 1 3478 ? 224.940 202.881 291.385 1.00 27.80 ? 3478 LEU A CD2   1 
ATOM   14458 N  N     . LEU A 1 3479 ? 225.612 198.561 293.306 1.00 24.19 ? 3479 LEU A N     1 
ATOM   14459 C  CA    . LEU A 1 3479 ? 226.702 197.667 292.933 1.00 24.98 ? 3479 LEU A CA    1 
ATOM   14460 C  C     . LEU A 1 3479 ? 226.222 196.227 292.822 1.00 27.51 ? 3479 LEU A C     1 
ATOM   14461 O  O     . LEU A 1 3479 ? 226.614 195.503 291.899 1.00 31.82 ? 3479 LEU A O     1 
ATOM   14462 C  CB    . LEU A 1 3479 ? 227.840 197.781 293.946 1.00 27.69 ? 3479 LEU A CB    1 
ATOM   14463 C  CG    . LEU A 1 3479 ? 228.838 198.907 293.684 1.00 26.15 ? 3479 LEU A CG    1 
ATOM   14464 C  CD1   . LEU A 1 3479 ? 229.877 198.976 294.787 1.00 26.01 ? 3479 LEU A CD1   1 
ATOM   14465 C  CD2   . LEU A 1 3479 ? 229.497 198.713 292.331 1.00 28.14 ? 3479 LEU A CD2   1 
ATOM   14466 N  N     . LYS A 1 3480 ? 225.380 195.789 293.759 1.00 28.86 ? 3480 LYS A N     1 
ATOM   14467 C  CA    . LYS A 1 3480 ? 224.808 194.451 293.666 1.00 28.65 ? 3480 LYS A CA    1 
ATOM   14468 C  C     . LYS A 1 3480 ? 223.903 194.329 292.446 1.00 28.42 ? 3480 LYS A C     1 
ATOM   14469 O  O     . LYS A 1 3480 ? 223.890 193.293 291.773 1.00 28.57 ? 3480 LYS A O     1 
ATOM   14470 C  CB    . LYS A 1 3480 ? 224.045 194.116 294.950 1.00 27.94 ? 3480 LYS A CB    1 
ATOM   14471 C  CG    . LYS A 1 3480 ? 223.521 192.688 295.024 1.00 28.66 ? 3480 LYS A CG    1 
ATOM   14472 C  CD    . LYS A 1 3480 ? 222.044 192.605 294.662 1.00 32.26 ? 3480 LYS A CD    1 
ATOM   14473 C  CE    . LYS A 1 3480 ? 221.177 193.258 295.726 1.00 33.17 ? 3480 LYS A CE    1 
ATOM   14474 N  NZ    . LYS A 1 3480 ? 219.729 193.178 295.388 1.00 33.36 ? 3480 LYS A NZ    1 
ATOM   14475 N  N     . SER A 1 3481 ? 223.136 195.382 292.148 1.00 28.06 ? 3481 SER A N     1 
ATOM   14476 C  CA    . SER A 1 3481 ? 222.298 195.375 290.953 1.00 25.71 ? 3481 SER A CA    1 
ATOM   14477 C  C     . SER A 1 3481 ? 223.134 195.434 289.681 1.00 28.74 ? 3481 SER A C     1 
ATOM   14478 O  O     . SER A 1 3481 ? 222.694 194.957 288.629 1.00 28.66 ? 3481 SER A O     1 
ATOM   14479 C  CB    . SER A 1 3481 ? 221.315 196.544 290.999 1.00 26.97 ? 3481 SER A CB    1 
ATOM   14480 O  OG    . SER A 1 3481 ? 220.459 196.537 289.872 1.00 37.75 ? 3481 SER A OG    1 
ATOM   14481 N  N     . LEU A 1 3482 ? 224.330 196.014 289.753 1.00 29.42 ? 3482 LEU A N     1 
ATOM   14482 C  CA    . LEU A 1 3482 ? 225.240 196.086 288.618 1.00 27.33 ? 3482 LEU A CA    1 
ATOM   14483 C  C     . LEU A 1 3482 ? 226.227 194.929 288.583 1.00 30.64 ? 3482 LEU A C     1 
ATOM   14484 O  O     . LEU A 1 3482 ? 227.146 194.942 287.758 1.00 37.28 ? 3482 LEU A O     1 
ATOM   14485 C  CB    . LEU A 1 3482 ? 225.999 197.417 288.633 1.00 23.09 ? 3482 LEU A CB    1 
ATOM   14486 C  CG    . LEU A 1 3482 ? 225.191 198.673 288.304 1.00 24.50 ? 3482 LEU A CG    1 
ATOM   14487 C  CD1   . LEU A 1 3482 ? 226.107 199.874 288.141 1.00 22.60 ? 3482 LEU A CD1   1 
ATOM   14488 C  CD2   . LEU A 1 3482 ? 224.363 198.460 287.050 1.00 25.53 ? 3482 LEU A CD2   1 
ATOM   14489 N  N     . SER A 1 3483 ? 226.070 193.942 289.469 1.00 30.49 ? 3483 SER A N     1 
ATOM   14490 C  CA    . SER A 1 3483 ? 226.969 192.793 289.465 1.00 27.93 ? 3483 SER A CA    1 
ATOM   14491 C  C     . SER A 1 3483 ? 226.849 192.000 288.169 1.00 28.27 ? 3483 SER A C     1 
ATOM   14492 O  O     . SER A 1 3483 ? 227.862 191.585 287.592 1.00 33.80 ? 3483 SER A O     1 
ATOM   14493 C  CB    . SER A 1 3483 ? 226.681 191.899 290.670 1.00 32.76 ? 3483 SER A CB    1 
ATOM   14494 O  OG    . SER A 1 3483 ? 227.483 190.730 290.648 1.00 40.17 ? 3483 SER A OG    1 
ATOM   14495 N  N     . ALA A 1 3484 ? 225.619 191.779 287.696 1.00 30.75 ? 3484 ALA A N     1 
ATOM   14496 C  CA    . ALA A 1 3484 ? 225.428 191.026 286.462 1.00 25.80 ? 3484 ALA A CA    1 
ATOM   14497 C  C     . ALA A 1 3484 ? 226.008 191.764 285.264 1.00 29.95 ? 3484 ALA A C     1 
ATOM   14498 O  O     . ALA A 1 3484 ? 226.675 191.162 284.415 1.00 28.35 ? 3484 ALA A O     1 
ATOM   14499 C  CB    . ALA A 1 3484 ? 223.943 190.737 286.249 1.00 22.60 ? 3484 ALA A CB    1 
ATOM   14500 N  N     . GLU A 1 3485 ? 225.766 193.074 285.178 1.00 32.35 ? 3485 GLU A N     1 
ATOM   14501 C  CA    . GLU A 1 3485 ? 226.311 193.854 284.073 1.00 28.68 ? 3485 GLU A CA    1 
ATOM   14502 C  C     . GLU A 1 3485 ? 227.833 193.897 284.128 1.00 28.89 ? 3485 GLU A C     1 
ATOM   14503 O  O     . GLU A 1 3485 ? 228.498 193.828 283.089 1.00 28.27 ? 3485 GLU A O     1 
ATOM   14504 C  CB    . GLU A 1 3485 ? 225.726 195.266 284.090 1.00 27.57 ? 3485 GLU A CB    1 
ATOM   14505 C  CG    . GLU A 1 3485 ? 224.299 195.344 283.570 1.00 30.69 ? 3485 GLU A CG    1 
ATOM   14506 C  CD    . GLU A 1 3485 ? 223.273 194.902 284.600 1.00 36.35 ? 3485 GLU A CD    1 
ATOM   14507 O  OE1   . GLU A 1 3485 ? 223.662 194.632 285.757 1.00 36.88 ? 3485 GLU A OE1   1 
ATOM   14508 O  OE2   . GLU A 1 3485 ? 222.078 194.815 284.251 1.00 35.18 ? 3485 GLU A OE2   1 
ATOM   14509 N  N     . ARG A 1 3486 ? 228.401 194.006 285.332 1.00 27.05 ? 3486 ARG A N     1 
ATOM   14510 C  CA    . ARG A 1 3486 ? 229.855 193.981 285.461 1.00 29.73 ? 3486 ARG A CA    1 
ATOM   14511 C  C     . ARG A 1 3486 ? 230.422 192.638 285.014 1.00 31.16 ? 3486 ARG A C     1 
ATOM   14512 O  O     . ARG A 1 3486 ? 231.465 192.585 284.355 1.00 32.01 ? 3486 ARG A O     1 
ATOM   14513 C  CB    . ARG A 1 3486 ? 230.260 194.287 286.902 1.00 24.75 ? 3486 ARG A CB    1 
ATOM   14514 C  CG    . ARG A 1 3486 ? 231.757 194.447 287.107 1.00 24.37 ? 3486 ARG A CG    1 
ATOM   14515 C  CD    . ARG A 1 3486 ? 232.136 194.362 288.580 1.00 27.64 ? 3486 ARG A CD    1 
ATOM   14516 N  NE    . ARG A 1 3486 ? 231.467 193.265 289.271 1.00 35.17 ? 3486 ARG A NE    1 
ATOM   14517 C  CZ    . ARG A 1 3486 ? 231.699 191.979 289.045 1.00 31.82 ? 3486 ARG A CZ    1 
ATOM   14518 N  NH1   . ARG A 1 3486 ? 232.604 191.581 288.166 1.00 24.63 ? 3486 ARG A NH1   1 
ATOM   14519 N  NH2   . ARG A 1 3486 ? 231.010 191.067 289.725 1.00 35.25 ? 3486 ARG A NH2   1 
ATOM   14520 N  N     . GLU A 1 3487 ? 229.744 191.540 285.365 1.00 29.51 ? 3487 GLU A N     1 
ATOM   14521 C  CA    . GLU A 1 3487 ? 230.197 190.220 284.938 1.00 28.56 ? 3487 GLU A CA    1 
ATOM   14522 C  C     . GLU A 1 3487 ? 230.099 190.052 283.427 1.00 28.16 ? 3487 GLU A C     1 
ATOM   14523 O  O     . GLU A 1 3487 ? 231.012 189.508 282.799 1.00 29.76 ? 3487 GLU A O     1 
ATOM   14524 C  CB    . GLU A 1 3487 ? 229.386 189.134 285.648 1.00 28.33 ? 3487 GLU A CB    1 
ATOM   14525 C  CG    . GLU A 1 3487 ? 229.703 188.970 287.127 1.00 29.77 ? 3487 GLU A CG    1 
ATOM   14526 C  CD    . GLU A 1 3487 ? 231.018 188.250 287.375 1.00 37.18 ? 3487 GLU A CD    1 
ATOM   14527 O  OE1   . GLU A 1 3487 ? 232.082 188.794 287.009 1.00 35.45 ? 3487 GLU A OE1   1 
ATOM   14528 O  OE2   . GLU A 1 3487 ? 230.986 187.135 287.934 1.00 34.55 ? 3487 GLU A OE2   1 
ATOM   14529 N  N     . ARG A 1 3488 ? 228.993 190.503 282.829 1.00 26.63 ? 3488 ARG A N     1 
ATOM   14530 C  CA    . ARG A 1 3488 ? 228.805 190.341 281.390 1.00 21.04 ? 3488 ARG A CA    1 
ATOM   14531 C  C     . ARG A 1 3488 ? 229.830 191.143 280.599 1.00 26.56 ? 3488 ARG A C     1 
ATOM   14532 O  O     . ARG A 1 3488 ? 230.385 190.649 279.609 1.00 32.49 ? 3488 ARG A O     1 
ATOM   14533 C  CB    . ARG A 1 3488 ? 227.385 190.748 281.001 1.00 22.94 ? 3488 ARG A CB    1 
ATOM   14534 C  CG    . ARG A 1 3488 ? 227.075 190.595 279.523 1.00 23.86 ? 3488 ARG A CG    1 
ATOM   14535 C  CD    . ARG A 1 3488 ? 225.983 191.557 279.084 1.00 24.65 ? 3488 ARG A CD    1 
ATOM   14536 N  NE    . ARG A 1 3488 ? 224.890 191.626 280.046 1.00 30.03 ? 3488 ARG A NE    1 
ATOM   14537 C  CZ    . ARG A 1 3488 ? 224.589 192.699 280.765 1.00 30.94 ? 3488 ARG A CZ    1 
ATOM   14538 N  NH1   . ARG A 1 3488 ? 225.286 193.819 280.660 1.00 30.97 ? 3488 ARG A NH1   1 
ATOM   14539 N  NH2   . ARG A 1 3488 ? 223.566 192.645 281.612 1.00 34.12 ? 3488 ARG A NH2   1 
ATOM   14540 N  N     . TRP A 1 3489 ? 230.095 192.381 281.019 1.00 24.23 ? 3489 TRP A N     1 
ATOM   14541 C  CA    . TRP A 1 3489 ? 231.067 193.207 280.313 1.00 24.49 ? 3489 TRP A CA    1 
ATOM   14542 C  C     . TRP A 1 3489 ? 232.478 192.648 280.435 1.00 31.24 ? 3489 TRP A C     1 
ATOM   14543 O  O     . TRP A 1 3489 ? 233.285 192.801 279.512 1.00 34.34 ? 3489 TRP A O     1 
ATOM   14544 C  CB    . TRP A 1 3489 ? 231.012 194.640 280.837 1.00 24.23 ? 3489 TRP A CB    1 
ATOM   14545 C  CG    . TRP A 1 3489 ? 229.675 195.289 280.653 1.00 23.77 ? 3489 TRP A CG    1 
ATOM   14546 C  CD1   . TRP A 1 3489 ? 228.711 194.941 279.753 1.00 22.72 ? 3489 TRP A CD1   1 
ATOM   14547 C  CD2   . TRP A 1 3489 ? 229.156 196.401 281.388 1.00 24.72 ? 3489 TRP A CD2   1 
ATOM   14548 N  NE1   . TRP A 1 3489 ? 227.622 195.767 279.883 1.00 25.11 ? 3489 TRP A NE1   1 
ATOM   14549 C  CE2   . TRP A 1 3489 ? 227.871 196.673 280.880 1.00 25.46 ? 3489 TRP A CE2   1 
ATOM   14550 C  CE3   . TRP A 1 3489 ? 229.652 197.193 282.428 1.00 22.02 ? 3489 TRP A CE3   1 
ATOM   14551 C  CZ2   . TRP A 1 3489 ? 227.075 197.702 281.377 1.00 22.95 ? 3489 TRP A CZ2   1 
ATOM   14552 C  CZ3   . TRP A 1 3489 ? 228.864 198.214 282.916 1.00 25.96 ? 3489 TRP A CZ3   1 
ATOM   14553 C  CH2   . TRP A 1 3489 ? 227.590 198.461 282.391 1.00 31.56 ? 3489 TRP A CH2   1 
ATOM   14554 N  N     . GLU A 1 3490 ? 232.796 192.009 281.563 1.00 27.80 ? 3490 GLU A N     1 
ATOM   14555 C  CA    . GLU A 1 3490 ? 234.115 191.405 281.724 1.00 28.05 ? 3490 GLU A CA    1 
ATOM   14556 C  C     . GLU A 1 3490 ? 234.308 190.232 280.771 1.00 29.33 ? 3490 GLU A C     1 
ATOM   14557 O  O     . GLU A 1 3490 ? 235.396 190.059 280.206 1.00 30.74 ? 3490 GLU A O     1 
ATOM   14558 C  CB    . GLU A 1 3490 ? 234.316 190.961 283.172 1.00 23.57 ? 3490 GLU A CB    1 
ATOM   14559 C  CG    . GLU A 1 3490 ? 234.621 192.100 284.126 1.00 28.75 ? 3490 GLU A CG    1 
ATOM   14560 C  CD    . GLU A 1 3490 ? 234.425 191.712 285.578 1.00 37.07 ? 3490 GLU A CD    1 
ATOM   14561 O  OE1   . GLU A 1 3490 ? 234.034 190.554 285.838 1.00 37.36 ? 3490 GLU A OE1   1 
ATOM   14562 O  OE2   . GLU A 1 3490 ? 234.655 192.565 286.460 1.00 32.44 ? 3490 GLU A OE2   1 
ATOM   14563 N  N     . LYS A 1 3491 ? 233.271 189.411 280.589 1.00 27.27 ? 3491 LYS A N     1 
ATOM   14564 C  CA    . LYS A 1 3491 ? 233.380 188.256 279.702 1.00 27.73 ? 3491 LYS A CA    1 
ATOM   14565 C  C     . LYS A 1 3491 ? 233.638 188.683 278.263 1.00 27.59 ? 3491 LYS A C     1 
ATOM   14566 O  O     . LYS A 1 3491 ? 234.500 188.120 277.582 1.00 32.90 ? 3491 LYS A O     1 
ATOM   14567 C  CB    . LYS A 1 3491 ? 232.113 187.405 279.791 1.00 30.51 ? 3491 LYS A CB    1 
ATOM   14568 C  CG    . LYS A 1 3491 ? 231.800 186.869 281.180 1.00 29.85 ? 3491 LYS A CG    1 
ATOM   14569 C  CD    . LYS A 1 3491 ? 232.993 186.140 281.776 1.00 30.69 ? 3491 LYS A CD    1 
ATOM   14570 C  CE    . LYS A 1 3491 ? 232.706 185.690 283.201 1.00 30.56 ? 3491 LYS A CE    1 
ATOM   14571 N  NZ    . LYS A 1 3491 ? 232.362 186.834 284.091 1.00 31.24 ? 3491 LYS A NZ    1 
ATOM   14572 N  N     . THR A 1 3492 ? 232.897 189.686 277.782 1.00 29.66 ? 3492 THR A N     1 
ATOM   14573 C  CA    . THR A 1 3492 ? 233.080 190.148 276.409 1.00 28.07 ? 3492 THR A CA    1 
ATOM   14574 C  C     . THR A 1 3492 ? 234.454 190.776 276.215 1.00 28.98 ? 3492 THR A C     1 
ATOM   14575 O  O     . THR A 1 3492 ? 235.079 190.602 275.162 1.00 32.25 ? 3492 THR A O     1 
ATOM   14576 C  CB    . THR A 1 3492 ? 231.975 191.137 276.035 1.00 26.20 ? 3492 THR A CB    1 
ATOM   14577 O  OG1   . THR A 1 3492 ? 230.699 190.504 276.180 1.00 32.22 ? 3492 THR A OG1   1 
ATOM   14578 C  CG2   . THR A 1 3492 ? 232.135 191.598 274.596 1.00 22.73 ? 3492 THR A CG2   1 
ATOM   14579 N  N     . SER A 1 3493 ? 234.942 191.507 277.221 1.00 28.13 ? 3493 SER A N     1 
ATOM   14580 C  CA    . SER A 1 3493 ? 236.260 192.126 277.117 1.00 28.03 ? 3493 SER A CA    1 
ATOM   14581 C  C     . SER A 1 3493 ? 237.348 191.077 276.925 1.00 34.05 ? 3493 SER A C     1 
ATOM   14582 O  O     . SER A 1 3493 ? 238.317 191.304 276.192 1.00 36.26 ? 3493 SER A O     1 
ATOM   14583 C  CB    . SER A 1 3493 ? 236.542 192.970 278.358 1.00 25.99 ? 3493 SER A CB    1 
ATOM   14584 O  OG    . SER A 1 3493 ? 237.852 193.505 278.323 1.00 29.50 ? 3493 SER A OG    1 
ATOM   14585 N  N     . GLU A 1 3494 ? 237.212 189.924 277.585 1.00 28.79 ? 3494 GLU A N     1 
ATOM   14586 C  CA    . GLU A 1 3494 ? 238.162 188.839 277.372 1.00 30.53 ? 3494 GLU A CA    1 
ATOM   14587 C  C     . GLU A 1 3494 ? 238.082 188.307 275.947 1.00 33.58 ? 3494 GLU A C     1 
ATOM   14588 O  O     . GLU A 1 3494 ? 239.112 188.040 275.319 1.00 34.47 ? 3494 GLU A O     1 
ATOM   14589 C  CB    . GLU A 1 3494 ? 237.914 187.718 278.381 1.00 29.47 ? 3494 GLU A CB    1 
ATOM   14590 C  CG    . GLU A 1 3494 ? 238.728 186.447 278.142 1.00 31.72 ? 3494 GLU A CG    1 
ATOM   14591 C  CD    . GLU A 1 3494 ? 240.217 186.635 278.376 1.00 38.78 ? 3494 GLU A CD    1 
ATOM   14592 O  OE1   . GLU A 1 3494 ? 240.874 187.341 277.581 1.00 40.53 ? 3494 GLU A OE1   1 
ATOM   14593 O  OE2   . GLU A 1 3494 ? 240.735 186.073 279.363 1.00 38.89 ? 3494 GLU A OE2   1 
ATOM   14594 N  N     . THR A 1 3495 ? 236.871 188.156 275.417 1.00 29.65 ? 3495 THR A N     1 
ATOM   14595 C  CA    . THR A 1 3495 ? 236.666 187.665 274.055 1.00 30.46 ? 3495 THR A CA    1 
ATOM   14596 C  C     . THR A 1 3495 ? 236.984 188.703 272.990 1.00 27.70 ? 3495 THR A C     1 
ATOM   14597 O  O     . THR A 1 3495 ? 236.696 188.450 271.815 1.00 28.72 ? 3495 THR A O     1 
ATOM   14598 C  CB    . THR A 1 3495 ? 235.227 187.178 273.878 1.00 29.03 ? 3495 THR A CB    1 
ATOM   14599 O  OG1   . THR A 1 3495 ? 234.342 188.305 273.832 1.00 26.50 ? 3495 THR A OG1   1 
ATOM   14600 C  CG2   . THR A 1 3495 ? 234.829 186.266 275.025 1.00 23.62 ? 3495 THR A CG2   1 
ATOM   14601 N  N     . PHE A 1 3496 ? 237.551 189.852 273.365 1.00 26.75 ? 3496 PHE A N     1 
ATOM   14602 C  CA    . PHE A 1 3496 ? 237.904 190.864 272.376 1.00 21.44 ? 3496 PHE A CA    1 
ATOM   14603 C  C     . PHE A 1 3496 ? 238.948 190.344 271.399 1.00 24.49 ? 3496 PHE A C     1 
ATOM   14604 O  O     . PHE A 1 3496 ? 238.848 190.578 270.189 1.00 29.80 ? 3496 PHE A O     1 
ATOM   14605 C  CB    . PHE A 1 3496 ? 238.414 192.122 273.075 1.00 21.65 ? 3496 PHE A CB    1 
ATOM   14606 C  CG    . PHE A 1 3496 ? 238.833 193.208 272.131 1.00 22.53 ? 3496 PHE A CG    1 
ATOM   14607 C  CD1   . PHE A 1 3496 ? 237.985 193.631 271.120 1.00 25.19 ? 3496 PHE A CD1   1 
ATOM   14608 C  CD2   . PHE A 1 3496 ? 240.083 193.792 272.238 1.00 23.14 ? 3496 PHE A CD2   1 
ATOM   14609 C  CE1   . PHE A 1 3496 ? 238.373 194.625 270.246 1.00 26.34 ? 3496 PHE A CE1   1 
ATOM   14610 C  CE2   . PHE A 1 3496 ? 240.473 194.784 271.366 1.00 21.22 ? 3496 PHE A CE2   1 
ATOM   14611 C  CZ    . PHE A 1 3496 ? 239.619 195.201 270.370 1.00 21.00 ? 3496 PHE A CZ    1 
ATOM   14612 N  N     . LYS A 1 3497 ? 239.966 189.642 271.905 1.00 24.90 ? 3497 LYS A N     1 
ATOM   14613 C  CA    . LYS A 1 3497 ? 241.044 189.168 271.041 1.00 25.50 ? 3497 LYS A CA    1 
ATOM   14614 C  C     . LYS A 1 3497 ? 240.540 188.151 270.026 1.00 21.05 ? 3497 LYS A C     1 
ATOM   14615 O  O     . LYS A 1 3497 ? 240.940 188.186 268.856 1.00 22.07 ? 3497 LYS A O     1 
ATOM   14616 C  CB    . LYS A 1 3497 ? 242.170 188.574 271.884 1.00 26.09 ? 3497 LYS A CB    1 
ATOM   14617 C  CG    . LYS A 1 3497 ? 242.677 189.496 272.979 1.00 31.26 ? 3497 LYS A CG    1 
ATOM   14618 C  CD    . LYS A 1 3497 ? 243.908 188.920 273.657 1.00 32.18 ? 3497 LYS A CD    1 
ATOM   14619 C  CE    . LYS A 1 3497 ? 245.021 188.670 272.654 1.00 35.32 ? 3497 LYS A CE    1 
ATOM   14620 N  NZ    . LYS A 1 3497 ? 245.364 189.901 271.891 1.00 35.53 ? 3497 LYS A NZ    1 
ATOM   14621 N  N     . ASN A 1 3498 ? 239.667 187.236 270.455 1.00 20.68 ? 3498 ASN A N     1 
ATOM   14622 C  CA    . ASN A 1 3498 ? 239.160 186.212 269.545 1.00 20.09 ? 3498 ASN A CA    1 
ATOM   14623 C  C     . ASN A 1 3498 ? 238.388 186.836 268.390 1.00 23.07 ? 3498 ASN A C     1 
ATOM   14624 O  O     . ASN A 1 3498 ? 238.560 186.440 267.232 1.00 19.93 ? 3498 ASN A O     1 
ATOM   14625 C  CB    . ASN A 1 3498 ? 238.283 185.224 270.314 1.00 20.30 ? 3498 ASN A CB    1 
ATOM   14626 C  CG    . ASN A 1 3498 ? 237.896 184.008 269.489 1.00 26.38 ? 3498 ASN A CG    1 
ATOM   14627 O  OD1   . ASN A 1 3498 ? 238.258 183.889 268.320 1.00 36.95 ? 3498 ASN A OD1   1 
ATOM   14628 N  ND2   . ASN A 1 3498 ? 237.153 183.096 270.102 1.00 27.08 ? 3498 ASN A ND2   1 
ATOM   14629 N  N     . GLN A 1 3499 ? 237.533 187.819 268.686 1.00 20.11 ? 3499 GLN A N     1 
ATOM   14630 C  CA    . GLN A 1 3499 ? 236.767 188.468 267.627 1.00 18.43 ? 3499 GLN A CA    1 
ATOM   14631 C  C     . GLN A 1 3499 ? 237.677 189.239 266.676 1.00 20.49 ? 3499 GLN A C     1 
ATOM   14632 O  O     . GLN A 1 3499 ? 237.466 189.224 265.457 1.00 23.21 ? 3499 GLN A O     1 
ATOM   14633 C  CB    . GLN A 1 3499 ? 235.707 189.384 268.231 1.00 18.55 ? 3499 GLN A CB    1 
ATOM   14634 C  CG    . GLN A 1 3499 ? 234.765 188.692 269.193 1.00 23.34 ? 3499 GLN A CG    1 
ATOM   14635 C  CD    . GLN A 1 3499 ? 233.696 189.621 269.727 1.00 24.81 ? 3499 GLN A CD    1 
ATOM   14636 O  OE1   . GLN A 1 3499 ? 233.654 189.915 270.921 1.00 29.63 ? 3499 GLN A OE1   1 
ATOM   14637 N  NE2   . GLN A 1 3499 ? 232.825 190.090 268.841 1.00 28.66 ? 3499 GLN A NE2   1 
ATOM   14638 N  N     . MET A 1 3500 ? 238.697 189.917 267.211 1.00 17.12 ? 3500 MET A N     1 
ATOM   14639 C  CA    . MET A 1 3500 ? 239.680 190.575 266.355 1.00 16.29 ? 3500 MET A CA    1 
ATOM   14640 C  C     . MET A 1 3500 ? 240.393 189.582 265.446 1.00 16.97 ? 3500 MET A C     1 
ATOM   14641 O  O     . MET A 1 3500 ? 240.818 189.947 264.345 1.00 21.36 ? 3500 MET A O     1 
ATOM   14642 C  CB    . MET A 1 3500 ? 240.704 191.332 267.202 1.00 18.27 ? 3500 MET A CB    1 
ATOM   14643 C  CG    . MET A 1 3500 ? 240.155 192.512 267.985 1.00 22.65 ? 3500 MET A CG    1 
ATOM   14644 S  SD    . MET A 1 3500 ? 239.460 193.785 266.919 1.00 31.34 ? 3500 MET A SD    1 
ATOM   14645 C  CE    . MET A 1 3500 ? 240.943 194.414 266.140 1.00 26.36 ? 3500 MET A CE    1 
ATOM   14646 N  N     . SER A 1 3501 ? 240.533 188.333 265.882 1.00 14.85 ? 3501 SER A N     1 
ATOM   14647 C  CA    . SER A 1 3501 ? 241.253 187.321 265.124 1.00 12.80 ? 3501 SER A CA    1 
ATOM   14648 C  C     . SER A 1 3501 ? 240.412 186.658 264.041 1.00 11.71 ? 3501 SER A C     1 
ATOM   14649 O  O     . SER A 1 3501 ? 240.966 185.912 263.226 1.00 23.94 ? 3501 SER A O     1 
ATOM   14650 C  CB    . SER A 1 3501 ? 241.801 186.245 266.067 1.00 17.13 ? 3501 SER A CB    1 
ATOM   14651 O  OG    . SER A 1 3501 ? 240.761 185.428 266.573 1.00 26.70 ? 3501 SER A OG    1 
ATOM   14652 N  N     . THR A 1 3502 ? 239.103 186.899 264.002 1.00 9.75  ? 3502 THR A N     1 
ATOM   14653 C  CA    . THR A 1 3502 ? 238.240 186.283 263.005 1.00 10.23 ? 3502 THR A CA    1 
ATOM   14654 C  C     . THR A 1 3502 ? 237.560 187.287 262.085 1.00 9.97  ? 3502 THR A C     1 
ATOM   14655 O  O     . THR A 1 3502 ? 236.856 186.870 261.161 1.00 11.49 ? 3502 THR A O     1 
ATOM   14656 C  CB    . THR A 1 3502 ? 237.164 185.416 263.677 1.00 11.86 ? 3502 THR A CB    1 
ATOM   14657 O  OG1   . THR A 1 3502 ? 236.515 186.164 264.711 1.00 12.07 ? 3502 THR A OG1   1 
ATOM   14658 C  CG2   . THR A 1 3502 ? 237.779 184.155 264.269 1.00 11.29 ? 3502 THR A CG2   1 
ATOM   14659 N  N     . ILE A 1 3503 ? 237.744 188.592 262.308 1.00 7.97  ? 3503 ILE A N     1 
ATOM   14660 C  CA    . ILE A 1 3503 ? 237.106 189.589 261.452 1.00 8.20  ? 3503 ILE A CA    1 
ATOM   14661 C  C     . ILE A 1 3503 ? 237.610 189.465 260.021 1.00 5.74  ? 3503 ILE A C     1 
ATOM   14662 O  O     . ILE A 1 3503 ? 236.838 189.590 259.063 1.00 8.52  ? 3503 ILE A O     1 
ATOM   14663 C  CB    . ILE A 1 3503 ? 237.331 191.004 262.020 1.00 11.20 ? 3503 ILE A CB    1 
ATOM   14664 C  CG1   . ILE A 1 3503 ? 236.407 191.256 263.210 1.00 9.74  ? 3503 ILE A CG1   1 
ATOM   14665 C  CG2   . ILE A 1 3503 ? 237.090 192.062 260.953 1.00 7.57  ? 3503 ILE A CG2   1 
ATOM   14666 C  CD1   . ILE A 1 3503 ? 236.604 192.606 263.858 1.00 16.09 ? 3503 ILE A CD1   1 
ATOM   14667 N  N     . ALA A 1 3504 ? 238.908 189.195 259.853 1.00 4.84  ? 3504 ALA A N     1 
ATOM   14668 C  CA    . ALA A 1 3504 ? 239.472 189.059 258.515 1.00 4.75  ? 3504 ALA A CA    1 
ATOM   14669 C  C     . ALA A 1 3504 ? 238.789 187.944 257.736 1.00 3.18  ? 3504 ALA A C     1 
ATOM   14670 O  O     . ALA A 1 3504 ? 238.493 188.099 256.546 1.00 2.73  ? 3504 ALA A O     1 
ATOM   14671 C  CB    . ALA A 1 3504 ? 240.976 188.811 258.605 1.00 3.31  ? 3504 ALA A CB    1 
ATOM   14672 N  N     . GLY A 1 3505 ? 238.531 186.812 258.387 1.00 4.17  ? 3505 GLY A N     1 
ATOM   14673 C  CA    . GLY A 1 3505 ? 237.827 185.717 257.750 1.00 3.66  ? 3505 GLY A CA    1 
ATOM   14674 C  C     . GLY A 1 3505 ? 236.324 185.897 257.686 1.00 2.55  ? 3505 GLY A C     1 
ATOM   14675 O  O     . GLY A 1 3505 ? 235.695 185.542 256.685 1.00 2.02  ? 3505 GLY A O     1 
ATOM   14676 N  N     . ASP A 1 3506 ? 235.734 186.441 258.754 1.00 2.36  ? 3506 ASP A N     1 
ATOM   14677 C  CA    . ASP A 1 3506 ? 234.284 186.622 258.786 1.00 2.70  ? 3506 ASP A CA    1 
ATOM   14678 C  C     . ASP A 1 3506 ? 233.823 187.617 257.730 1.00 1.95  ? 3506 ASP A C     1 
ATOM   14679 O  O     . ASP A 1 3506 ? 232.824 187.385 257.041 1.00 0.80  ? 3506 ASP A O     1 
ATOM   14680 C  CB    . ASP A 1 3506 ? 233.841 187.077 260.175 1.00 4.46  ? 3506 ASP A CB    1 
ATOM   14681 C  CG    . ASP A 1 3506 ? 233.765 185.934 261.166 1.00 11.51 ? 3506 ASP A CG    1 
ATOM   14682 O  OD1   . ASP A 1 3506 ? 233.763 184.766 260.730 1.00 13.23 ? 3506 ASP A OD1   1 
ATOM   14683 O  OD2   . ASP A 1 3506 ? 233.715 186.206 262.385 1.00 15.22 ? 3506 ASP A OD2   1 
ATOM   14684 N  N     . CYS A 1 3507 ? 234.540 188.735 257.589 1.00 3.24  ? 3507 CYS A N     1 
ATOM   14685 C  CA    . CYS A 1 3507 ? 234.160 189.736 256.601 1.00 1.52  ? 3507 CYS A CA    1 
ATOM   14686 C  C     . CYS A 1 3507 ? 234.388 189.239 255.179 1.00 1.85  ? 3507 CYS A C     1 
ATOM   14687 O  O     . CYS A 1 3507 ? 233.633 189.600 254.272 1.00 1.56  ? 3507 CYS A O     1 
ATOM   14688 C  CB    . CYS A 1 3507 ? 234.927 191.034 256.850 1.00 2.29  ? 3507 CYS A CB    1 
ATOM   14689 S  SG    . CYS A 1 3507 ? 234.439 191.896 258.356 1.00 6.53  ? 3507 CYS A SG    1 
ATOM   14690 N  N     . LEU A 1 3508 ? 235.417 188.415 254.969 1.00 1.10  ? 3508 LEU A N     1 
ATOM   14691 C  CA    . LEU A 1 3508 ? 235.660 187.847 253.648 1.00 0.59  ? 3508 LEU A CA    1 
ATOM   14692 C  C     . LEU A 1 3508 ? 234.486 186.988 253.196 1.00 0.54  ? 3508 LEU A C     1 
ATOM   14693 O  O     . LEU A 1 3508 ? 234.027 187.093 252.052 1.00 0.52  ? 3508 LEU A O     1 
ATOM   14694 C  CB    . LEU A 1 3508 ? 236.954 187.032 253.668 1.00 1.21  ? 3508 LEU A CB    1 
ATOM   14695 C  CG    . LEU A 1 3508 ? 237.694 186.753 252.358 1.00 0.78  ? 3508 LEU A CG    1 
ATOM   14696 C  CD1   . LEU A 1 3508 ? 239.150 186.460 252.657 1.00 1.11  ? 3508 LEU A CD1   1 
ATOM   14697 C  CD2   . LEU A 1 3508 ? 237.070 185.595 251.593 1.00 0.50  ? 3508 LEU A CD2   1 
ATOM   14698 N  N     . LEU A 1 3509 ? 233.985 186.129 254.085 1.00 0.54  ? 3509 LEU A N     1 
ATOM   14699 C  CA    . LEU A 1 3509 ? 232.827 185.304 253.752 1.00 0.34  ? 3509 LEU A CA    1 
ATOM   14700 C  C     . LEU A 1 3509 ? 231.579 186.155 253.560 1.00 0.34  ? 3509 LEU A C     1 
ATOM   14701 O  O     . LEU A 1 3509 ? 230.801 185.926 252.626 1.00 0.12  ? 3509 LEU A O     1 
ATOM   14702 C  CB    . LEU A 1 3509 ? 232.597 184.264 254.847 1.00 0.57  ? 3509 LEU A CB    1 
ATOM   14703 C  CG    . LEU A 1 3509 ? 233.683 183.212 255.054 1.00 1.28  ? 3509 LEU A CG    1 
ATOM   14704 C  CD1   . LEU A 1 3509 ? 233.385 182.382 256.293 1.00 1.03  ? 3509 LEU A CD1   1 
ATOM   14705 C  CD2   . LEU A 1 3509 ? 233.809 182.328 253.830 1.00 0.67  ? 3509 LEU A CD2   1 
ATOM   14706 N  N     . SER A 1 3510 ? 231.372 187.137 254.438 1.00 0.86  ? 3510 SER A N     1 
ATOM   14707 C  CA    . SER A 1 3510 ? 230.195 187.992 254.341 1.00 0.32  ? 3510 SER A CA    1 
ATOM   14708 C  C     . SER A 1 3510 ? 230.217 188.827 253.068 1.00 0.28  ? 3510 SER A C     1 
ATOM   14709 O  O     . SER A 1 3510 ? 229.193 188.961 252.389 1.00 0.25  ? 3510 SER A O     1 
ATOM   14710 C  CB    . SER A 1 3510 ? 230.105 188.890 255.573 1.00 0.57  ? 3510 SER A CB    1 
ATOM   14711 O  OG    . SER A 1 3510 ? 230.122 188.121 256.760 1.00 2.09  ? 3510 SER A OG    1 
ATOM   14712 N  N     . ALA A 1 3511 ? 231.377 189.391 252.730 1.00 0.67  ? 3511 ALA A N     1 
ATOM   14713 C  CA    . ALA A 1 3511 ? 231.483 190.204 251.522 1.00 0.21  ? 3511 ALA A CA    1 
ATOM   14714 C  C     . ALA A 1 3511 ? 231.236 189.373 250.273 1.00 0.15  ? 3511 ALA A C     1 
ATOM   14715 O  O     . ALA A 1 3511 ? 230.578 189.832 249.333 1.00 0.61  ? 3511 ALA A O     1 
ATOM   14716 C  CB    . ALA A 1 3511 ? 232.854 190.871 251.461 1.00 0.22  ? 3511 ALA A CB    1 
ATOM   14717 N  N     . ALA A 1 3512 ? 231.761 188.145 250.242 1.00 0.17  ? 3512 ALA A N     1 
ATOM   14718 C  CA    . ALA A 1 3512 ? 231.548 187.276 249.091 1.00 0.05  ? 3512 ALA A CA    1 
ATOM   14719 C  C     . ALA A 1 3512 ? 230.074 186.943 248.920 1.00 0.08  ? 3512 ALA A C     1 
ATOM   14720 O  O     . ALA A 1 3512 ? 229.573 186.868 247.792 1.00 0.10  ? 3512 ALA A O     1 
ATOM   14721 C  CB    . ALA A 1 3512 ? 232.376 186.001 249.236 1.00 0.06  ? 3512 ALA A CB    1 
ATOM   14722 N  N     . PHE A 1 3513 ? 229.362 186.735 250.029 1.00 0.10  ? 3513 PHE A N     1 
ATOM   14723 C  CA    . PHE A 1 3513 ? 227.941 186.426 249.953 1.00 0.12  ? 3513 PHE A CA    1 
ATOM   14724 C  C     . PHE A 1 3513 ? 227.148 187.591 249.372 1.00 0.11  ? 3513 PHE A C     1 
ATOM   14725 O  O     . PHE A 1 3513 ? 226.226 187.384 248.576 1.00 0.14  ? 3513 PHE A O     1 
ATOM   14726 C  CB    . PHE A 1 3513 ? 227.419 186.044 251.339 1.00 0.10  ? 3513 PHE A CB    1 
ATOM   14727 C  CG    . PHE A 1 3513 ? 226.112 185.317 251.312 1.00 0.19  ? 3513 PHE A CG    1 
ATOM   14728 C  CD1   . PHE A 1 3513 ? 226.076 183.938 251.212 1.00 0.37  ? 3513 PHE A CD1   1 
ATOM   14729 C  CD2   . PHE A 1 3513 ? 224.918 186.008 251.393 1.00 0.27  ? 3513 PHE A CD2   1 
ATOM   14730 C  CE1   . PHE A 1 3513 ? 224.875 183.265 251.182 1.00 0.48  ? 3513 PHE A CE1   1 
ATOM   14731 C  CE2   . PHE A 1 3513 ? 223.715 185.337 251.365 1.00 0.46  ? 3513 PHE A CE2   1 
ATOM   14732 C  CZ    . PHE A 1 3513 ? 223.696 183.965 251.262 1.00 0.59  ? 3513 PHE A CZ    1 
ATOM   14733 N  N     . ILE A 1 3514 ? 227.490 188.822 249.756 1.00 0.13  ? 3514 ILE A N     1 
ATOM   14734 C  CA    . ILE A 1 3514 ? 226.785 189.989 249.236 1.00 0.25  ? 3514 ILE A CA    1 
ATOM   14735 C  C     . ILE A 1 3514 ? 227.051 190.175 247.747 1.00 0.22  ? 3514 ILE A C     1 
ATOM   14736 O  O     . ILE A 1 3514 ? 226.159 190.589 246.997 1.00 0.46  ? 3514 ILE A O     1 
ATOM   14737 C  CB    . ILE A 1 3514 ? 227.173 191.245 250.038 1.00 0.52  ? 3514 ILE A CB    1 
ATOM   14738 C  CG1   . ILE A 1 3514 ? 226.882 191.037 251.523 1.00 0.45  ? 3514 ILE A CG1   1 
ATOM   14739 C  CG2   . ILE A 1 3514 ? 226.426 192.463 249.524 1.00 0.72  ? 3514 ILE A CG2   1 
ATOM   14740 C  CD1   . ILE A 1 3514 ? 225.439 190.717 251.809 1.00 0.89  ? 3514 ILE A CD1   1 
ATOM   14741 N  N     . ALA A 1 3515 ? 228.262 189.871 247.289 1.00 0.12  ? 3515 ALA A N     1 
ATOM   14742 C  CA    . ALA A 1 3515 ? 228.643 190.143 245.910 1.00 0.14  ? 3515 ALA A CA    1 
ATOM   14743 C  C     . ALA A 1 3515 ? 228.231 189.056 244.927 1.00 0.08  ? 3515 ALA A C     1 
ATOM   14744 O  O     . ALA A 1 3515 ? 228.056 189.352 243.741 1.00 0.07  ? 3515 ALA A O     1 
ATOM   14745 C  CB    . ALA A 1 3515 ? 230.156 190.355 245.814 1.00 0.14  ? 3515 ALA A CB    1 
ATOM   14746 N  N     . TYR A 1 3516 ? 228.066 187.823 245.374 1.00 0.15  ? 3516 TYR A N     1 
ATOM   14747 C  CA    . TYR A 1 3516 ? 227.864 186.735 244.421 1.00 0.11  ? 3516 TYR A CA    1 
ATOM   14748 C  C     . TYR A 1 3516 ? 226.576 185.956 244.628 1.00 0.09  ? 3516 TYR A C     1 
ATOM   14749 O  O     . TYR A 1 3516 ? 225.989 185.494 243.649 1.00 0.73  ? 3516 TYR A O     1 
ATOM   14750 C  CB    . TYR A 1 3516 ? 229.042 185.758 244.474 1.00 0.06  ? 3516 TYR A CB    1 
ATOM   14751 C  CG    . TYR A 1 3516 ? 230.375 186.332 244.071 1.00 0.03  ? 3516 TYR A CG    1 
ATOM   14752 C  CD1   . TYR A 1 3516 ? 230.662 186.596 242.741 1.00 0.05  ? 3516 TYR A CD1   1 
ATOM   14753 C  CD2   . TYR A 1 3516 ? 231.359 186.581 245.014 1.00 0.03  ? 3516 TYR A CD2   1 
ATOM   14754 C  CE1   . TYR A 1 3516 ? 231.886 187.100 242.366 1.00 0.04  ? 3516 TYR A CE1   1 
ATOM   14755 C  CE2   . TYR A 1 3516 ? 232.585 187.090 244.644 1.00 0.03  ? 3516 TYR A CE2   1 
ATOM   14756 C  CZ    . TYR A 1 3516 ? 232.842 187.349 243.320 1.00 0.03  ? 3516 TYR A CZ    1 
ATOM   14757 O  OH    . TYR A 1 3516 ? 234.057 187.857 242.943 1.00 0.04  ? 3516 TYR A OH    1 
ATOM   14758 N  N     . ALA A 1 3517 ? 226.124 185.793 245.869 1.00 0.11  ? 3517 ALA A N     1 
ATOM   14759 C  CA    . ALA A 1 3517 ? 225.093 184.811 246.180 1.00 0.25  ? 3517 ALA A CA    1 
ATOM   14760 C  C     . ALA A 1 3517 ? 223.682 185.262 245.829 1.00 0.15  ? 3517 ALA A C     1 
ATOM   14761 O  O     . ALA A 1 3517 ? 222.756 184.454 245.935 1.00 0.89  ? 3517 ALA A O     1 
ATOM   14762 C  CB    . ALA A 1 3517 ? 225.153 184.449 247.666 1.00 0.21  ? 3517 ALA A CB    1 
ATOM   14763 N  N     . GLY A 1 3518 ? 223.497 186.511 245.406 1.00 0.21  ? 3518 GLY A N     1 
ATOM   14764 C  CA    . GLY A 1 3518 ? 222.154 187.062 245.317 1.00 0.18  ? 3518 GLY A CA    1 
ATOM   14765 C  C     . GLY A 1 3518 ? 221.264 186.350 244.316 1.00 0.23  ? 3518 GLY A C     1 
ATOM   14766 O  O     . GLY A 1 3518 ? 220.078 186.133 244.574 1.00 0.29  ? 3518 GLY A O     1 
ATOM   14767 N  N     . TYR A 1 3519 ? 221.818 185.977 243.162 1.00 0.44  ? 3519 TYR A N     1 
ATOM   14768 C  CA    . TYR A 1 3519 ? 220.992 185.382 242.118 1.00 0.30  ? 3519 TYR A CA    1 
ATOM   14769 C  C     . TYR A 1 3519 ? 220.571 183.956 242.452 1.00 0.40  ? 3519 TYR A C     1 
ATOM   14770 O  O     . TYR A 1 3519 ? 219.543 183.485 241.958 1.00 1.11  ? 3519 TYR A O     1 
ATOM   14771 C  CB    . TYR A 1 3519 ? 221.726 185.409 240.778 1.00 0.63  ? 3519 TYR A CB    1 
ATOM   14772 C  CG    . TYR A 1 3519 ? 220.888 184.863 239.651 1.00 1.45  ? 3519 TYR A CG    1 
ATOM   14773 C  CD1   . TYR A 1 3519 ? 219.811 185.583 239.159 1.00 1.19  ? 3519 TYR A CD1   1 
ATOM   14774 C  CD2   . TYR A 1 3519 ? 221.156 183.620 239.096 1.00 1.96  ? 3519 TYR A CD2   1 
ATOM   14775 C  CE1   . TYR A 1 3519 ? 219.030 185.089 238.142 1.00 4.22  ? 3519 TYR A CE1   1 
ATOM   14776 C  CE2   . TYR A 1 3519 ? 220.381 183.117 238.074 1.00 2.82  ? 3519 TYR A CE2   1 
ATOM   14777 C  CZ    . TYR A 1 3519 ? 219.318 183.857 237.601 1.00 4.38  ? 3519 TYR A CZ    1 
ATOM   14778 O  OH    . TYR A 1 3519 ? 218.538 183.366 236.582 1.00 9.23  ? 3519 TYR A OH    1 
ATOM   14779 N  N     . PHE A 1 3520 ? 221.335 183.259 243.286 1.00 0.46  ? 3520 PHE A N     1 
ATOM   14780 C  CA    . PHE A 1 3520 ? 221.112 181.839 243.488 1.00 1.24  ? 3520 PHE A CA    1 
ATOM   14781 C  C     . PHE A 1 3520 ? 220.046 181.583 244.553 1.00 1.72  ? 3520 PHE A C     1 
ATOM   14782 O  O     . PHE A 1 3520 ? 219.688 182.461 245.341 1.00 1.33  ? 3520 PHE A O     1 
ATOM   14783 C  CB    . PHE A 1 3520 ? 222.423 181.154 243.867 1.00 1.12  ? 3520 PHE A CB    1 
ATOM   14784 C  CG    . PHE A 1 3520 ? 223.529 181.399 242.887 1.00 1.16  ? 3520 PHE A CG    1 
ATOM   14785 C  CD1   . PHE A 1 3520 ? 223.580 180.701 241.692 1.00 1.18  ? 3520 PHE A CD1   1 
ATOM   14786 C  CD2   . PHE A 1 3520 ? 224.507 182.344 243.147 1.00 0.57  ? 3520 PHE A CD2   1 
ATOM   14787 C  CE1   . PHE A 1 3520 ? 224.590 180.931 240.785 1.00 2.68  ? 3520 PHE A CE1   1 
ATOM   14788 C  CE2   . PHE A 1 3520 ? 225.516 182.579 242.242 1.00 1.56  ? 3520 PHE A CE2   1 
ATOM   14789 C  CZ    . PHE A 1 3520 ? 225.561 181.871 241.061 1.00 3.40  ? 3520 PHE A CZ    1 
ATOM   14790 N  N     . ASP A 1 3521 ? 219.533 180.355 244.558 1.00 2.65  ? 3521 ASP A N     1 
ATOM   14791 C  CA    . ASP A 1 3521 ? 218.523 179.947 245.522 1.00 1.85  ? 3521 ASP A CA    1 
ATOM   14792 C  C     . ASP A 1 3521 ? 219.187 179.492 246.821 1.00 1.44  ? 3521 ASP A C     1 
ATOM   14793 O  O     . ASP A 1 3521 ? 220.410 179.544 246.975 1.00 2.01  ? 3521 ASP A O     1 
ATOM   14794 C  CB    . ASP A 1 3521 ? 217.625 178.863 244.926 1.00 1.96  ? 3521 ASP A CB    1 
ATOM   14795 C  CG    . ASP A 1 3521 ? 218.394 177.622 244.493 1.00 7.00  ? 3521 ASP A CG    1 
ATOM   14796 O  OD1   . ASP A 1 3521 ? 219.618 177.551 244.716 1.00 10.23 ? 3521 ASP A OD1   1 
ATOM   14797 O  OD2   . ASP A 1 3521 ? 217.763 176.710 243.921 1.00 8.66  ? 3521 ASP A OD2   1 
ATOM   14798 N  N     . GLN A 1 3522 ? 218.367 179.026 247.766 1.00 2.02  ? 3522 GLN A N     1 
ATOM   14799 C  CA    . GLN A 1 3522 ? 218.863 178.724 249.105 1.00 1.95  ? 3522 GLN A CA    1 
ATOM   14800 C  C     . GLN A 1 3522 ? 219.933 177.637 249.083 1.00 3.15  ? 3522 GLN A C     1 
ATOM   14801 O  O     . GLN A 1 3522 ? 220.967 177.763 249.751 1.00 2.40  ? 3522 GLN A O     1 
ATOM   14802 C  CB    . GLN A 1 3522 ? 217.707 178.311 250.015 1.00 1.75  ? 3522 GLN A CB    1 
ATOM   14803 C  CG    . GLN A 1 3522 ? 218.155 177.675 251.322 1.00 3.08  ? 3522 GLN A CG    1 
ATOM   14804 C  CD    . GLN A 1 3522 ? 217.054 177.616 252.358 1.00 6.32  ? 3522 GLN A CD    1 
ATOM   14805 O  OE1   . GLN A 1 3522 ? 215.872 177.602 252.023 1.00 10.65 ? 3522 GLN A OE1   1 
ATOM   14806 N  NE2   . GLN A 1 3522 ? 217.438 177.580 253.627 1.00 11.54 ? 3522 GLN A NE2   1 
ATOM   14807 N  N     . GLN A 1 3523 ? 219.705 176.563 248.324 1.00 3.87  ? 3523 GLN A N     1 
ATOM   14808 C  CA    . GLN A 1 3523 ? 220.662 175.461 248.294 1.00 4.00  ? 3523 GLN A CA    1 
ATOM   14809 C  C     . GLN A 1 3523 ? 221.993 175.894 247.694 1.00 5.54  ? 3523 GLN A C     1 
ATOM   14810 O  O     . GLN A 1 3523 ? 223.060 175.539 248.209 1.00 6.71  ? 3523 GLN A O     1 
ATOM   14811 C  CB    . GLN A 1 3523 ? 220.081 174.283 247.515 1.00 6.14  ? 3523 GLN A CB    1 
ATOM   14812 C  CG    . GLN A 1 3523 ? 220.977 173.050 247.464 1.00 7.12  ? 3523 GLN A CG    1 
ATOM   14813 C  CD    . GLN A 1 3523 ? 221.209 172.432 248.833 1.00 18.38 ? 3523 GLN A CD    1 
ATOM   14814 O  OE1   . GLN A 1 3523 ? 222.095 172.853 249.577 1.00 20.83 ? 3523 GLN A OE1   1 
ATOM   14815 N  NE2   . GLN A 1 3523 ? 220.412 171.425 249.167 1.00 13.06 ? 3523 GLN A NE2   1 
ATOM   14816 N  N     . MET A 1 3524 ? 221.954 176.661 246.605 1.00 3.40  ? 3524 MET A N     1 
ATOM   14817 C  CA    . MET A 1 3524 ? 223.189 177.063 245.942 1.00 2.60  ? 3524 MET A CA    1 
ATOM   14818 C  C     . MET A 1 3524 ? 223.940 178.107 246.759 1.00 3.85  ? 3524 MET A C     1 
ATOM   14819 O  O     . MET A 1 3524 ? 225.177 178.124 246.769 1.00 5.02  ? 3524 MET A O     1 
ATOM   14820 C  CB    . MET A 1 3524 ? 222.887 177.584 244.540 1.00 3.49  ? 3524 MET A CB    1 
ATOM   14821 C  CG    . MET A 1 3524 ? 224.124 177.820 243.701 1.00 5.94  ? 3524 MET A CG    1 
ATOM   14822 S  SD    . MET A 1 3524 ? 225.010 176.280 243.404 1.00 27.38 ? 3524 MET A SD    1 
ATOM   14823 C  CE    . MET A 1 3524 ? 226.680 176.771 243.813 1.00 9.90  ? 3524 MET A CE    1 
ATOM   14824 N  N     . ARG A 1 3525 ? 223.213 178.990 247.449 1.00 2.31  ? 3525 ARG A N     1 
ATOM   14825 C  CA    . ARG A 1 3525 ? 223.860 179.953 248.336 1.00 1.79  ? 3525 ARG A CA    1 
ATOM   14826 C  C     . ARG A 1 3525 ? 224.620 179.241 249.446 1.00 3.02  ? 3525 ARG A C     1 
ATOM   14827 O  O     . ARG A 1 3525 ? 225.748 179.617 249.784 1.00 6.40  ? 3525 ARG A O     1 
ATOM   14828 C  CB    . ARG A 1 3525 ? 222.822 180.906 248.928 1.00 1.57  ? 3525 ARG A CB    1 
ATOM   14829 C  CG    . ARG A 1 3525 ? 222.225 181.896 247.945 1.00 0.93  ? 3525 ARG A CG    1 
ATOM   14830 C  CD    . ARG A 1 3525 ? 221.342 182.900 248.660 1.00 0.46  ? 3525 ARG A CD    1 
ATOM   14831 N  NE    . ARG A 1 3525 ? 220.754 183.873 247.747 1.00 0.38  ? 3525 ARG A NE    1 
ATOM   14832 C  CZ    . ARG A 1 3525 ? 219.979 184.879 248.126 1.00 0.32  ? 3525 ARG A CZ    1 
ATOM   14833 N  NH1   . ARG A 1 3525 ? 219.694 185.088 249.400 1.00 0.34  ? 3525 ARG A NH1   1 
ATOM   14834 N  NH2   . ARG A 1 3525 ? 219.480 185.697 247.207 1.00 0.25  ? 3525 ARG A NH2   1 
ATOM   14835 N  N     . GLN A 1 3526 ? 224.009 178.208 250.030 1.00 3.59  ? 3526 GLN A N     1 
ATOM   14836 C  CA    . GLN A 1 3526 ? 224.664 177.460 251.097 1.00 2.95  ? 3526 GLN A CA    1 
ATOM   14837 C  C     . GLN A 1 3526 ? 225.879 176.703 250.573 1.00 3.46  ? 3526 GLN A C     1 
ATOM   14838 O  O     . GLN A 1 3526 ? 226.905 176.611 251.258 1.00 2.84  ? 3526 GLN A O     1 
ATOM   14839 C  CB    . GLN A 1 3526 ? 223.665 176.505 251.749 1.00 3.87  ? 3526 GLN A CB    1 
ATOM   14840 C  CG    . GLN A 1 3526 ? 224.187 175.781 252.976 1.00 2.16  ? 3526 GLN A CG    1 
ATOM   14841 C  CD    . GLN A 1 3526 ? 224.829 176.720 253.974 1.00 3.08  ? 3526 GLN A CD    1 
ATOM   14842 O  OE1   . GLN A 1 3526 ? 224.209 177.676 254.432 1.00 8.04  ? 3526 GLN A OE1   1 
ATOM   14843 N  NE2   . GLN A 1 3526 ? 226.076 176.444 254.328 1.00 5.69  ? 3526 GLN A NE2   1 
ATOM   14844 N  N     . ASN A 1 3527 ? 225.779 176.151 249.360 1.00 2.95  ? 3527 ASN A N     1 
ATOM   14845 C  CA    . ASN A 1 3527 ? 226.911 175.445 248.768 1.00 1.71  ? 3527 ASN A CA    1 
ATOM   14846 C  C     . ASN A 1 3527 ? 228.093 176.377 248.546 1.00 2.24  ? 3527 ASN A C     1 
ATOM   14847 O  O     . ASN A 1 3527 ? 229.244 175.999 248.789 1.00 2.65  ? 3527 ASN A O     1 
ATOM   14848 C  CB    . ASN A 1 3527 ? 226.496 174.788 247.451 1.00 3.82  ? 3527 ASN A CB    1 
ATOM   14849 C  CG    . ASN A 1 3527 ? 225.484 173.675 247.644 1.00 9.33  ? 3527 ASN A CG    1 
ATOM   14850 O  OD1   . ASN A 1 3527 ? 225.400 173.074 248.715 1.00 14.91 ? 3527 ASN A OD1   1 
ATOM   14851 N  ND2   . ASN A 1 3527 ? 224.716 173.387 246.601 1.00 10.18 ? 3527 ASN A ND2   1 
ATOM   14852 N  N     . LEU A 1 3528 ? 227.833 177.596 248.065 1.00 1.78  ? 3528 LEU A N     1 
ATOM   14853 C  CA    . LEU A 1 3528 ? 228.912 178.558 247.862 1.00 0.90  ? 3528 LEU A CA    1 
ATOM   14854 C  C     . LEU A 1 3528 ? 229.575 178.934 249.179 1.00 0.54  ? 3528 LEU A C     1 
ATOM   14855 O  O     . LEU A 1 3528 ? 230.805 179.022 249.260 1.00 0.65  ? 3528 LEU A O     1 
ATOM   14856 C  CB    . LEU A 1 3528 ? 228.381 179.805 247.156 1.00 0.63  ? 3528 LEU A CB    1 
ATOM   14857 C  CG    . LEU A 1 3528 ? 228.052 179.665 245.670 1.00 0.76  ? 3528 LEU A CG    1 
ATOM   14858 C  CD1   . LEU A 1 3528 ? 227.235 180.847 245.191 1.00 0.96  ? 3528 LEU A CD1   1 
ATOM   14859 C  CD2   . LEU A 1 3528 ? 229.327 179.530 244.856 1.00 0.86  ? 3528 LEU A CD2   1 
ATOM   14860 N  N     . PHE A 1 3529 ? 228.774 179.163 250.220 1.00 1.28  ? 3529 PHE A N     1 
ATOM   14861 C  CA    . PHE A 1 3529 ? 229.329 179.558 251.510 1.00 1.13  ? 3529 PHE A CA    1 
ATOM   14862 C  C     . PHE A 1 3529 ? 230.138 178.428 252.136 1.00 1.82  ? 3529 PHE A C     1 
ATOM   14863 O  O     . PHE A 1 3529 ? 231.187 178.672 252.740 1.00 2.09  ? 3529 PHE A O     1 
ATOM   14864 C  CB    . PHE A 1 3529 ? 228.204 180.009 252.441 1.00 0.93  ? 3529 PHE A CB    1 
ATOM   14865 C  CG    . PHE A 1 3529 ? 228.657 180.910 253.552 1.00 1.76  ? 3529 PHE A CG    1 
ATOM   14866 C  CD1   . PHE A 1 3529 ? 229.089 180.386 254.757 1.00 0.84  ? 3529 PHE A CD1   1 
ATOM   14867 C  CD2   . PHE A 1 3529 ? 228.652 182.286 253.388 1.00 0.58  ? 3529 PHE A CD2   1 
ATOM   14868 C  CE1   . PHE A 1 3529 ? 229.506 181.216 255.775 1.00 0.38  ? 3529 PHE A CE1   1 
ATOM   14869 C  CE2   . PHE A 1 3529 ? 229.068 183.119 254.403 1.00 0.35  ? 3529 PHE A CE2   1 
ATOM   14870 C  CZ    . PHE A 1 3529 ? 229.496 182.584 255.597 1.00 0.46  ? 3529 PHE A CZ    1 
ATOM   14871 N  N     . THR A 1 3530 ? 229.664 177.188 252.004 1.00 2.13  ? 3530 THR A N     1 
ATOM   14872 C  CA    . THR A 1 3530 ? 230.415 176.048 252.524 1.00 2.59  ? 3530 THR A CA    1 
ATOM   14873 C  C     . THR A 1 3530 ? 231.726 175.859 251.769 1.00 2.03  ? 3530 THR A C     1 
ATOM   14874 O  O     . THR A 1 3530 ? 232.757 175.541 252.374 1.00 3.98  ? 3530 THR A O     1 
ATOM   14875 C  CB    . THR A 1 3530 ? 229.557 174.782 252.458 1.00 2.19  ? 3530 THR A CB    1 
ATOM   14876 O  OG1   . THR A 1 3530 ? 228.448 174.911 253.355 1.00 2.19  ? 3530 THR A OG1   1 
ATOM   14877 C  CG2   . THR A 1 3530 ? 230.367 173.555 252.849 1.00 2.73  ? 3530 THR A CG2   1 
ATOM   14878 N  N     . THR A 1 3531 ? 231.707 176.054 250.449 1.00 1.63  ? 3531 THR A N     1 
ATOM   14879 C  CA    . THR A 1 3531 ? 232.934 175.945 249.664 1.00 0.89  ? 3531 THR A CA    1 
ATOM   14880 C  C     . THR A 1 3531 ? 233.949 177.009 250.067 1.00 1.67  ? 3531 THR A C     1 
ATOM   14881 O  O     . THR A 1 3531 ? 235.142 176.713 250.207 1.00 2.72  ? 3531 THR A O     1 
ATOM   14882 C  CB    . THR A 1 3531 ? 232.612 176.049 248.173 1.00 1.70  ? 3531 THR A CB    1 
ATOM   14883 O  OG1   . THR A 1 3531 ? 231.605 175.091 247.832 1.00 3.12  ? 3531 THR A OG1   1 
ATOM   14884 C  CG2   . THR A 1 3531 ? 233.855 175.790 247.337 1.00 1.46  ? 3531 THR A CG2   1 
ATOM   14885 N  N     . TRP A 1 3532 ? 233.498 178.253 250.251 1.00 2.03  ? 3532 TRP A N     1 
ATOM   14886 C  CA    . TRP A 1 3532 ? 234.402 179.304 250.709 1.00 1.13  ? 3532 TRP A CA    1 
ATOM   14887 C  C     . TRP A 1 3532 ? 234.888 179.032 252.124 1.00 1.33  ? 3532 TRP A C     1 
ATOM   14888 O  O     . TRP A 1 3532 ? 236.074 179.207 252.425 1.00 2.95  ? 3532 TRP A O     1 
ATOM   14889 C  CB    . TRP A 1 3532 ? 233.711 180.667 250.649 1.00 0.35  ? 3532 TRP A CB    1 
ATOM   14890 C  CG    . TRP A 1 3532 ? 233.117 181.012 249.332 1.00 0.19  ? 3532 TRP A CG    1 
ATOM   14891 C  CD1   . TRP A 1 3532 ? 233.554 180.618 248.103 1.00 0.24  ? 3532 TRP A CD1   1 
ATOM   14892 C  CD2   . TRP A 1 3532 ? 231.967 181.830 249.106 1.00 0.20  ? 3532 TRP A CD2   1 
ATOM   14893 N  NE1   . TRP A 1 3532 ? 232.746 181.137 247.127 1.00 0.16  ? 3532 TRP A NE1   1 
ATOM   14894 C  CE2   . TRP A 1 3532 ? 231.762 181.886 247.715 1.00 0.11  ? 3532 TRP A CE2   1 
ATOM   14895 C  CE3   . TRP A 1 3532 ? 231.087 182.519 249.945 1.00 0.15  ? 3532 TRP A CE3   1 
ATOM   14896 C  CZ2   . TRP A 1 3532 ? 230.720 182.605 247.146 1.00 0.14  ? 3532 TRP A CZ2   1 
ATOM   14897 C  CZ3   . TRP A 1 3532 ? 230.053 183.231 249.378 1.00 0.08  ? 3532 TRP A CZ3   1 
ATOM   14898 C  CH2   . TRP A 1 3532 ? 229.878 183.271 247.992 1.00 0.11  ? 3532 TRP A CH2   1 
ATOM   14899 N  N     . SER A 1 3533 ? 233.980 178.607 253.007 1.00 1.98  ? 3533 SER A N     1 
ATOM   14900 C  CA    . SER A 1 3533 ? 234.358 178.327 254.389 1.00 2.31  ? 3533 SER A CA    1 
ATOM   14901 C  C     . SER A 1 3533 ? 235.364 177.189 254.462 1.00 3.53  ? 3533 SER A C     1 
ATOM   14902 O  O     . SER A 1 3533 ? 236.318 177.243 255.248 1.00 3.08  ? 3533 SER A O     1 
ATOM   14903 C  CB    . SER A 1 3533 ? 233.114 177.999 255.214 1.00 1.92  ? 3533 SER A CB    1 
ATOM   14904 O  OG    . SER A 1 3533 ? 232.231 179.106 255.261 1.00 3.30  ? 3533 SER A OG    1 
ATOM   14905 N  N     . HIS A 1 3534 ? 235.170 176.148 253.649 1.00 2.73  ? 3534 HIS A N     1 
ATOM   14906 C  CA    . HIS A 1 3534 ? 236.133 175.054 253.605 1.00 4.26  ? 3534 HIS A CA    1 
ATOM   14907 C  C     . HIS A 1 3534 ? 237.503 175.543 253.155 1.00 4.20  ? 3534 HIS A C     1 
ATOM   14908 O  O     . HIS A 1 3534 ? 238.525 175.163 253.736 1.00 4.84  ? 3534 HIS A O     1 
ATOM   14909 C  CB    . HIS A 1 3534 ? 235.635 173.949 252.675 1.00 4.33  ? 3534 HIS A CB    1 
ATOM   14910 C  CG    . HIS A 1 3534 ? 234.599 173.061 253.288 1.00 10.93 ? 3534 HIS A CG    1 
ATOM   14911 N  ND1   . HIS A 1 3534 ? 234.358 173.023 254.644 1.00 10.53 ? 3534 HIS A ND1   1 
ATOM   14912 C  CD2   . HIS A 1 3534 ? 233.745 172.171 252.729 1.00 9.94  ? 3534 HIS A CD2   1 
ATOM   14913 C  CE1   . HIS A 1 3534 ? 233.396 172.151 254.893 1.00 12.56 ? 3534 HIS A CE1   1 
ATOM   14914 N  NE2   . HIS A 1 3534 ? 233.008 171.620 253.748 1.00 11.20 ? 3534 HIS A NE2   1 
ATOM   14915 N  N     . HIS A 1 3535 ? 237.539 176.399 252.132 1.00 3.86  ? 3535 HIS A N     1 
ATOM   14916 C  CA    . HIS A 1 3535 ? 238.812 176.889 251.617 1.00 2.26  ? 3535 HIS A CA    1 
ATOM   14917 C  C     . HIS A 1 3535 ? 239.558 177.707 252.663 1.00 3.44  ? 3535 HIS A C     1 
ATOM   14918 O  O     . HIS A 1 3535 ? 240.786 177.611 252.775 1.00 9.11  ? 3535 HIS A O     1 
ATOM   14919 C  CB    . HIS A 1 3535 ? 238.582 177.718 250.357 1.00 1.13  ? 3535 HIS A CB    1 
ATOM   14920 C  CG    . HIS A 1 3535 ? 239.843 178.158 249.685 1.00 2.04  ? 3535 HIS A CG    1 
ATOM   14921 N  ND1   . HIS A 1 3535 ? 240.470 179.348 249.988 1.00 2.83  ? 3535 HIS A ND1   1 
ATOM   14922 C  CD2   . HIS A 1 3535 ? 240.597 177.568 248.729 1.00 1.88  ? 3535 HIS A CD2   1 
ATOM   14923 C  CE1   . HIS A 1 3535 ? 241.556 179.471 249.248 1.00 3.50  ? 3535 HIS A CE1   1 
ATOM   14924 N  NE2   . HIS A 1 3535 ? 241.655 178.404 248.476 1.00 3.71  ? 3535 HIS A NE2   1 
ATOM   14925 N  N     . LEU A 1 3536 ? 238.836 178.529 253.424 1.00 2.52  ? 3536 LEU A N     1 
ATOM   14926 C  CA    . LEU A 1 3536 ? 239.475 179.303 254.482 1.00 3.59  ? 3536 LEU A CA    1 
ATOM   14927 C  C     . LEU A 1 3536 ? 240.085 178.388 255.536 1.00 5.53  ? 3536 LEU A C     1 
ATOM   14928 O  O     . LEU A 1 3536 ? 241.148 178.691 256.091 1.00 8.45  ? 3536 LEU A O     1 
ATOM   14929 C  CB    . LEU A 1 3536 ? 238.466 180.259 255.117 1.00 5.53  ? 3536 LEU A CB    1 
ATOM   14930 C  CG    . LEU A 1 3536 ? 237.951 181.411 254.250 1.00 3.38  ? 3536 LEU A CG    1 
ATOM   14931 C  CD1   . LEU A 1 3536 ? 237.288 182.467 255.113 1.00 4.29  ? 3536 LEU A CD1   1 
ATOM   14932 C  CD2   . LEU A 1 3536 ? 239.070 182.019 253.424 1.00 3.74  ? 3536 LEU A CD2   1 
ATOM   14933 N  N     . GLN A 1 3537 ? 239.422 177.267 255.830 1.00 6.62  ? 3537 GLN A N     1 
ATOM   14934 C  CA    . GLN A 1 3537 ? 239.965 176.310 256.789 1.00 6.65  ? 3537 GLN A CA    1 
ATOM   14935 C  C     . GLN A 1 3537 ? 241.277 175.711 256.299 1.00 7.92  ? 3537 GLN A C     1 
ATOM   14936 O  O     . GLN A 1 3537 ? 242.238 175.591 257.067 1.00 10.58 ? 3537 GLN A O     1 
ATOM   14937 C  CB    . GLN A 1 3537 ? 238.940 175.211 257.072 1.00 8.35  ? 3537 GLN A CB    1 
ATOM   14938 C  CG    . GLN A 1 3537 ? 237.702 175.693 257.804 1.00 10.68 ? 3537 GLN A CG    1 
ATOM   14939 C  CD    . GLN A 1 3537 ? 236.693 174.586 258.049 1.00 20.10 ? 3537 GLN A CD    1 
ATOM   14940 O  OE1   . GLN A 1 3537 ? 236.880 173.453 257.611 1.00 18.54 ? 3537 GLN A OE1   1 
ATOM   14941 N  NE2   . GLN A 1 3537 ? 235.618 174.913 258.759 1.00 19.79 ? 3537 GLN A NE2   1 
ATOM   14942 N  N     . GLN A 1 3538 ? 241.343 175.331 255.021 1.00 5.14  ? 3538 GLN A N     1 
ATOM   14943 C  CA    . GLN A 1 3538 ? 242.587 174.790 254.483 1.00 5.70  ? 3538 GLN A CA    1 
ATOM   14944 C  C     . GLN A 1 3538 ? 243.682 175.839 254.387 1.00 10.73 ? 3538 GLN A C     1 
ATOM   14945 O  O     . GLN A 1 3538 ? 244.858 175.477 254.297 1.00 21.73 ? 3538 GLN A O     1 
ATOM   14946 C  CB    . GLN A 1 3538 ? 242.356 174.161 253.106 1.00 10.15 ? 3538 GLN A CB    1 
ATOM   14947 C  CG    . GLN A 1 3538 ? 241.001 173.517 252.924 1.00 5.22  ? 3538 GLN A CG    1 
ATOM   14948 C  CD    . GLN A 1 3538 ? 240.946 172.614 251.709 1.00 21.45 ? 3538 GLN A CD    1 
ATOM   14949 O  OE1   . GLN A 1 3538 ? 241.843 172.630 250.867 1.00 26.19 ? 3538 GLN A OE1   1 
ATOM   14950 N  NE2   . GLN A 1 3538 ? 239.888 171.817 251.613 1.00 23.05 ? 3538 GLN A NE2   1 
ATOM   14951 N  N     . ALA A 1 3539 ? 243.328 177.123 254.399 1.00 9.73  ? 3539 ALA A N     1 
ATOM   14952 C  CA    . ALA A 1 3539 ? 244.299 178.205 254.345 1.00 8.29  ? 3539 ALA A CA    1 
ATOM   14953 C  C     . ALA A 1 3539 ? 244.641 178.758 255.722 1.00 9.44  ? 3539 ALA A C     1 
ATOM   14954 O  O     . ALA A 1 3539 ? 245.390 179.736 255.814 1.00 19.13 ? 3539 ALA A O     1 
ATOM   14955 C  CB    . ALA A 1 3539 ? 243.787 179.327 253.444 1.00 5.39  ? 3539 ALA A CB    1 
ATOM   14956 N  N     . ASN A 1 3540 ? 244.106 178.159 256.788 1.00 6.53  ? 3540 ASN A N     1 
ATOM   14957 C  CA    . ASN A 1 3540 ? 244.315 178.618 258.164 1.00 8.42  ? 3540 ASN A CA    1 
ATOM   14958 C  C     . ASN A 1 3540 ? 243.834 180.052 258.368 1.00 8.75  ? 3540 ASN A C     1 
ATOM   14959 O  O     . ASN A 1 3540 ? 244.402 180.800 259.167 1.00 15.63 ? 3540 ASN A O     1 
ATOM   14960 C  CB    . ASN A 1 3540 ? 245.782 178.490 258.585 1.00 10.62 ? 3540 ASN A CB    1 
ATOM   14961 C  CG    . ASN A 1 3540 ? 246.181 177.059 258.879 1.00 14.34 ? 3540 ASN A CG    1 
ATOM   14962 O  OD1   . ASN A 1 3540 ? 245.552 176.116 258.403 1.00 15.66 ? 3540 ASN A OD1   1 
ATOM   14963 N  ND2   . ASN A 1 3540 ? 247.237 176.893 259.665 1.00 17.14 ? 3540 ASN A ND2   1 
ATOM   14964 N  N     . ILE A 1 3541 ? 242.783 180.448 257.655 1.00 8.56  ? 3541 ILE A N     1 
ATOM   14965 C  CA    . ILE A 1 3541 ? 242.158 181.751 257.850 1.00 7.92  ? 3541 ILE A CA    1 
ATOM   14966 C  C     . ILE A 1 3541 ? 241.078 181.597 258.912 1.00 8.90  ? 3541 ILE A C     1 
ATOM   14967 O  O     . ILE A 1 3541 ? 240.165 180.777 258.768 1.00 12.01 ? 3541 ILE A O     1 
ATOM   14968 C  CB    . ILE A 1 3541 ? 241.572 182.296 256.538 1.00 6.41  ? 3541 ILE A CB    1 
ATOM   14969 C  CG1   . ILE A 1 3541 ? 242.622 182.259 255.425 1.00 7.78  ? 3541 ILE A CG1   1 
ATOM   14970 C  CG2   . ILE A 1 3541 ? 241.035 183.706 256.744 1.00 4.81  ? 3541 ILE A CG2   1 
ATOM   14971 C  CD1   . ILE A 1 3541 ? 243.644 183.367 255.502 1.00 7.61  ? 3541 ILE A CD1   1 
ATOM   14972 N  N     . GLN A 1 3542 ? 241.176 182.386 259.975 1.00 9.88  ? 3542 GLN A N     1 
ATOM   14973 C  CA    . GLN A 1 3542 ? 240.291 182.227 261.119 1.00 10.19 ? 3542 GLN A CA    1 
ATOM   14974 C  C     . GLN A 1 3542 ? 238.943 182.885 260.853 1.00 8.50  ? 3542 GLN A C     1 
ATOM   14975 O  O     . GLN A 1 3542 ? 238.876 184.042 260.426 1.00 10.32 ? 3542 GLN A O     1 
ATOM   14976 C  CB    . GLN A 1 3542 ? 240.932 182.826 262.369 1.00 10.83 ? 3542 GLN A CB    1 
ATOM   14977 C  CG    . GLN A 1 3542 ? 242.191 182.108 262.813 1.00 13.19 ? 3542 GLN A CG    1 
ATOM   14978 C  CD    . GLN A 1 3542 ? 241.930 180.668 263.197 1.00 24.83 ? 3542 GLN A CD    1 
ATOM   14979 O  OE1   . GLN A 1 3542 ? 242.331 179.745 262.492 1.00 31.49 ? 3542 GLN A OE1   1 
ATOM   14980 N  NE2   . GLN A 1 3542 ? 241.251 180.469 264.321 1.00 22.40 ? 3542 GLN A NE2   1 
ATOM   14981 N  N     . PHE A 1 3543 ? 237.870 182.140 261.107 1.00 7.59  ? 3543 PHE A N     1 
ATOM   14982 C  CA    . PHE A 1 3543 ? 236.514 182.659 261.007 1.00 6.38  ? 3543 PHE A CA    1 
ATOM   14983 C  C     . PHE A 1 3543 ? 235.624 181.863 261.949 1.00 10.25 ? 3543 PHE A C     1 
ATOM   14984 O  O     . PHE A 1 3543 ? 235.831 180.664 262.152 1.00 12.79 ? 3543 PHE A O     1 
ATOM   14985 C  CB    . PHE A 1 3543 ? 235.975 182.583 259.574 1.00 4.66  ? 3543 PHE A CB    1 
ATOM   14986 C  CG    . PHE A 1 3543 ? 235.800 181.181 259.065 1.00 6.23  ? 3543 PHE A CG    1 
ATOM   14987 C  CD1   . PHE A 1 3543 ? 236.869 180.487 258.521 1.00 6.62  ? 3543 PHE A CD1   1 
ATOM   14988 C  CD2   . PHE A 1 3543 ? 234.567 180.560 259.120 1.00 5.92  ? 3543 PHE A CD2   1 
ATOM   14989 C  CE1   . PHE A 1 3543 ? 236.710 179.201 258.054 1.00 6.60  ? 3543 PHE A CE1   1 
ATOM   14990 C  CE2   . PHE A 1 3543 ? 234.402 179.274 258.650 1.00 6.25  ? 3543 PHE A CE2   1 
ATOM   14991 C  CZ    . PHE A 1 3543 ? 235.474 178.593 258.118 1.00 4.96  ? 3543 PHE A CZ    1 
ATOM   14992 N  N     . ARG A 1 3544 ? 234.634 182.538 262.521 1.00 10.63 ? 3544 ARG A N     1 
ATOM   14993 C  CA    . ARG A 1 3544 ? 233.691 181.879 263.414 1.00 11.14 ? 3544 ARG A CA    1 
ATOM   14994 C  C     . ARG A 1 3544 ? 232.632 181.129 262.616 1.00 12.44 ? 3544 ARG A C     1 
ATOM   14995 O  O     . ARG A 1 3544 ? 232.231 181.556 261.529 1.00 15.76 ? 3544 ARG A O     1 
ATOM   14996 C  CB    . ARG A 1 3544 ? 233.040 182.897 264.347 1.00 10.85 ? 3544 ARG A CB    1 
ATOM   14997 C  CG    . ARG A 1 3544 ? 234.037 183.596 265.255 1.00 13.05 ? 3544 ARG A CG    1 
ATOM   14998 C  CD    . ARG A 1 3544 ? 233.482 184.882 265.832 1.00 15.30 ? 3544 ARG A CD    1 
ATOM   14999 N  NE    . ARG A 1 3544 ? 232.597 185.568 264.902 1.00 17.04 ? 3544 ARG A NE    1 
ATOM   15000 C  CZ    . ARG A 1 3544 ? 231.992 186.718 265.162 1.00 18.71 ? 3544 ARG A CZ    1 
ATOM   15001 N  NH1   . ARG A 1 3544 ? 232.172 187.350 266.310 1.00 19.07 ? 3544 ARG A NH1   1 
ATOM   15002 N  NH2   . ARG A 1 3544 ? 231.184 187.246 264.247 1.00 16.05 ? 3544 ARG A NH2   1 
ATOM   15003 N  N     . THR A 1 3545 ? 232.189 179.992 263.160 1.00 18.20 ? 3545 THR A N     1 
ATOM   15004 C  CA    . THR A 1 3545 ? 231.211 179.134 262.499 1.00 18.51 ? 3545 THR A CA    1 
ATOM   15005 C  C     . THR A 1 3545 ? 229.897 179.058 263.267 1.00 21.39 ? 3545 THR A C     1 
ATOM   15006 O  O     . THR A 1 3545 ? 229.077 178.177 262.997 1.00 21.52 ? 3545 THR A O     1 
ATOM   15007 C  CB    . THR A 1 3545 ? 231.779 177.727 262.296 1.00 21.65 ? 3545 THR A CB    1 
ATOM   15008 O  OG1   . THR A 1 3545 ? 232.081 177.145 263.571 1.00 28.13 ? 3545 THR A OG1   1 
ATOM   15009 C  CG2   . THR A 1 3545 ? 233.043 177.778 261.463 1.00 14.83 ? 3545 THR A CG2   1 
ATOM   15010 N  N     . ASP A 1 3546 ? 229.675 179.964 264.218 1.00 22.68 ? 3546 ASP A N     1 
ATOM   15011 C  CA    . ASP A 1 3546 ? 228.476 179.945 265.049 1.00 24.85 ? 3546 ASP A CA    1 
ATOM   15012 C  C     . ASP A 1 3546 ? 227.463 180.979 264.575 1.00 28.31 ? 3546 ASP A C     1 
ATOM   15013 O  O     . ASP A 1 3546 ? 226.292 180.646 264.370 1.00 26.10 ? 3546 ASP A O     1 
ATOM   15014 C  CB    . ASP A 1 3546 ? 228.850 180.174 266.516 1.00 19.70 ? 3546 ASP A CB    1 
ATOM   15015 C  CG    . ASP A 1 3546 ? 229.789 181.348 266.698 1.00 27.83 ? 3546 ASP A CG    1 
ATOM   15016 O  OD1   . ASP A 1 3546 ? 230.144 181.982 265.683 1.00 30.61 ? 3546 ASP A OD1   1 
ATOM   15017 O  OD2   . ASP A 1 3546 ? 230.171 181.637 267.851 1.00 31.88 ? 3546 ASP A OD2   1 
ATOM   15018 N  N     . ILE A 1 3547 ? 227.880 182.234 264.395 1.00 23.04 ? 3547 ILE A N     1 
ATOM   15019 C  CA    . ILE A 1 3547 ? 226.940 183.286 264.038 1.00 21.38 ? 3547 ILE A CA    1 
ATOM   15020 C  C     . ILE A 1 3547 ? 226.482 183.112 262.598 1.00 23.16 ? 3547 ILE A C     1 
ATOM   15021 O  O     . ILE A 1 3547 ? 227.281 182.829 261.696 1.00 21.01 ? 3547 ILE A O     1 
ATOM   15022 C  CB    . ILE A 1 3547 ? 227.577 184.668 264.278 1.00 26.73 ? 3547 ILE A CB    1 
ATOM   15023 C  CG1   . ILE A 1 3547 ? 226.579 185.786 263.967 1.00 18.53 ? 3547 ILE A CG1   1 
ATOM   15024 C  CG2   . ILE A 1 3547 ? 228.865 184.826 263.474 1.00 19.57 ? 3547 ILE A CG2   1 
ATOM   15025 C  CD1   . ILE A 1 3547 ? 227.064 187.157 264.360 1.00 12.99 ? 3547 ILE A CD1   1 
ATOM   15026 N  N     . ALA A 1 3548 ? 225.180 183.256 262.384 1.00 20.50 ? 3548 ALA A N     1 
ATOM   15027 C  CA    . ALA A 1 3548 ? 224.611 183.189 261.050 1.00 13.80 ? 3548 ALA A CA    1 
ATOM   15028 C  C     . ALA A 1 3548 ? 224.978 184.436 260.252 1.00 12.65 ? 3548 ALA A C     1 
ATOM   15029 O  O     . ALA A 1 3548 ? 225.287 185.493 260.809 1.00 11.91 ? 3548 ALA A O     1 
ATOM   15030 C  CB    . ALA A 1 3548 ? 223.094 183.033 261.120 1.00 15.99 ? 3548 ALA A CB    1 
ATOM   15031 N  N     . ARG A 1 3549 ? 224.941 184.301 258.925 1.00 9.77  ? 3549 ARG A N     1 
ATOM   15032 C  CA    . ARG A 1 3549 ? 225.333 185.410 258.064 1.00 6.62  ? 3549 ARG A CA    1 
ATOM   15033 C  C     . ARG A 1 3549 ? 224.346 186.569 258.170 1.00 6.03  ? 3549 ARG A C     1 
ATOM   15034 O  O     . ARG A 1 3549 ? 224.738 187.737 258.070 1.00 12.27 ? 3549 ARG A O     1 
ATOM   15035 C  CB    . ARG A 1 3549 ? 225.465 184.938 256.615 1.00 6.60  ? 3549 ARG A CB    1 
ATOM   15036 C  CG    . ARG A 1 3549 ? 224.372 183.995 256.154 1.00 11.22 ? 3549 ARG A CG    1 
ATOM   15037 C  CD    . ARG A 1 3549 ? 224.858 183.069 255.051 1.00 2.62  ? 3549 ARG A CD    1 
ATOM   15038 N  NE    . ARG A 1 3549 ? 223.828 182.109 254.678 1.00 3.05  ? 3549 ARG A NE    1 
ATOM   15039 C  CZ    . ARG A 1 3549 ? 223.993 181.124 253.807 1.00 3.56  ? 3549 ARG A CZ    1 
ATOM   15040 N  NH1   . ARG A 1 3549 ? 225.165 180.893 253.241 1.00 13.03 ? 3549 ARG A NH1   1 
ATOM   15041 N  NH2   . ARG A 1 3549 ? 222.961 180.344 253.505 1.00 2.93  ? 3549 ARG A NH2   1 
ATOM   15042 N  N     . THR A 1 3550 ? 223.062 186.268 258.370 1.00 7.01  ? 3550 THR A N     1 
ATOM   15043 C  CA    . THR A 1 3550 ? 222.073 187.329 258.538 1.00 7.28  ? 3550 THR A CA    1 
ATOM   15044 C  C     . THR A 1 3550 ? 222.310 188.126 259.813 1.00 9.38  ? 3550 THR A C     1 
ATOM   15045 O  O     . THR A 1 3550 ? 222.131 189.349 259.821 1.00 7.93  ? 3550 THR A O     1 
ATOM   15046 C  CB    . THR A 1 3550 ? 220.657 186.749 258.538 1.00 6.34  ? 3550 THR A CB    1 
ATOM   15047 O  OG1   . THR A 1 3550 ? 220.543 185.748 259.556 1.00 16.31 ? 3550 THR A OG1   1 
ATOM   15048 C  CG2   . THR A 1 3550 ? 220.330 186.142 257.190 1.00 4.15  ? 3550 THR A CG2   1 
ATOM   15049 N  N     . GLU A 1 3551 ? 222.699 187.458 260.896 1.00 12.71 ? 3551 GLU A N     1 
ATOM   15050 C  CA    . GLU A 1 3551 ? 222.947 188.156 262.153 1.00 9.96  ? 3551 GLU A CA    1 
ATOM   15051 C  C     . GLU A 1 3551 ? 224.219 188.989 262.110 1.00 8.50  ? 3551 GLU A C     1 
ATOM   15052 O  O     . GLU A 1 3551 ? 224.296 190.031 262.769 1.00 10.91 ? 3551 GLU A O     1 
ATOM   15053 C  CB    . GLU A 1 3551 ? 223.019 187.154 263.305 1.00 11.15 ? 3551 GLU A CB    1 
ATOM   15054 C  CG    . GLU A 1 3551 ? 221.861 186.180 263.344 1.00 12.21 ? 3551 GLU A CG    1 
ATOM   15055 C  CD    . GLU A 1 3551 ? 220.530 186.875 263.531 1.00 21.62 ? 3551 GLU A CD    1 
ATOM   15056 O  OE1   . GLU A 1 3551 ? 220.209 187.249 264.678 1.00 19.38 ? 3551 GLU A OE1   1 
ATOM   15057 O  OE2   . GLU A 1 3551 ? 219.804 187.050 262.527 1.00 26.57 ? 3551 GLU A OE2   1 
ATOM   15058 N  N     . TYR A 1 3552 ? 225.223 188.551 261.353 1.00 8.49  ? 3552 TYR A N     1 
ATOM   15059 C  CA    . TYR A 1 3552 ? 226.493 189.259 261.285 1.00 6.92  ? 3552 TYR A CA    1 
ATOM   15060 C  C     . TYR A 1 3552 ? 226.460 190.455 260.340 1.00 5.14  ? 3552 TYR A C     1 
ATOM   15061 O  O     . TYR A 1 3552 ? 227.308 191.343 260.464 1.00 5.97  ? 3552 TYR A O     1 
ATOM   15062 C  CB    . TYR A 1 3552 ? 227.603 188.287 260.867 1.00 6.53  ? 3552 TYR A CB    1 
ATOM   15063 C  CG    . TYR A 1 3552 ? 228.996 188.872 260.849 1.00 7.11  ? 3552 TYR A CG    1 
ATOM   15064 C  CD1   . TYR A 1 3552 ? 229.741 188.966 262.016 1.00 5.80  ? 3552 TYR A CD1   1 
ATOM   15065 C  CD2   . TYR A 1 3552 ? 229.583 189.295 259.663 1.00 5.28  ? 3552 TYR A CD2   1 
ATOM   15066 C  CE1   . TYR A 1 3552 ? 231.014 189.487 262.009 1.00 6.56  ? 3552 TYR A CE1   1 
ATOM   15067 C  CE2   . TYR A 1 3552 ? 230.860 189.815 259.647 1.00 5.43  ? 3552 TYR A CE2   1 
ATOM   15068 C  CZ    . TYR A 1 3552 ? 231.572 189.908 260.825 1.00 8.84  ? 3552 TYR A CZ    1 
ATOM   15069 O  OH    . TYR A 1 3552 ? 232.845 190.425 260.823 1.00 6.54  ? 3552 TYR A OH    1 
ATOM   15070 N  N     . LEU A 1 3553 ? 225.500 190.510 259.421 1.00 5.84  ? 3553 LEU A N     1 
ATOM   15071 C  CA    . LEU A 1 3553 ? 225.419 191.589 258.447 1.00 4.80  ? 3553 LEU A CA    1 
ATOM   15072 C  C     . LEU A 1 3553 ? 224.240 192.521 258.672 1.00 4.07  ? 3553 LEU A C     1 
ATOM   15073 O  O     . LEU A 1 3553 ? 224.010 193.416 257.854 1.00 4.04  ? 3553 LEU A O     1 
ATOM   15074 C  CB    . LEU A 1 3553 ? 225.359 191.015 257.028 1.00 3.01  ? 3553 LEU A CB    1 
ATOM   15075 C  CG    . LEU A 1 3553 ? 226.649 190.355 256.552 1.00 4.39  ? 3553 LEU A CG    1 
ATOM   15076 C  CD1   . LEU A 1 3553 ? 226.461 189.723 255.185 1.00 2.44  ? 3553 LEU A CD1   1 
ATOM   15077 C  CD2   . LEU A 1 3553 ? 227.758 191.393 256.520 1.00 3.38  ? 3553 LEU A CD2   1 
ATOM   15078 N  N     . SER A 1 3554 ? 223.487 192.340 259.752 1.00 6.22  ? 3554 SER A N     1 
ATOM   15079 C  CA    . SER A 1 3554 ? 222.384 193.232 260.073 1.00 6.31  ? 3554 SER A CA    1 
ATOM   15080 C  C     . SER A 1 3554 ? 222.143 193.181 261.572 1.00 5.53  ? 3554 SER A C     1 
ATOM   15081 O  O     . SER A 1 3554 ? 222.434 192.178 262.227 1.00 9.24  ? 3554 SER A O     1 
ATOM   15082 C  CB    . SER A 1 3554 ? 221.110 192.859 259.307 1.00 3.54  ? 3554 SER A CB    1 
ATOM   15083 O  OG    . SER A 1 3554 ? 220.509 191.699 259.848 1.00 7.62  ? 3554 SER A OG    1 
ATOM   15084 N  N     . ASN A 1 3555 ? 221.620 194.276 262.110 1.00 7.33  ? 3555 ASN A N     1 
ATOM   15085 C  CA    . ASN A 1 3555 ? 221.280 194.357 263.522 1.00 7.11  ? 3555 ASN A CA    1 
ATOM   15086 C  C     . ASN A 1 3555 ? 219.806 194.028 263.731 1.00 6.73  ? 3555 ASN A C     1 
ATOM   15087 O  O     . ASN A 1 3555 ? 219.008 193.996 262.792 1.00 9.07  ? 3555 ASN A O     1 
ATOM   15088 C  CB    . ASN A 1 3555 ? 221.614 195.743 264.081 1.00 6.29  ? 3555 ASN A CB    1 
ATOM   15089 C  CG    . ASN A 1 3555 ? 221.051 196.867 263.237 1.00 9.46  ? 3555 ASN A CG    1 
ATOM   15090 O  OD1   . ASN A 1 3555 ? 219.848 197.118 263.243 1.00 13.45 ? 3555 ASN A OD1   1 
ATOM   15091 N  ND2   . ASN A 1 3555 ? 221.921 197.556 262.510 1.00 11.32 ? 3555 ASN A ND2   1 
ATOM   15092 N  N     . ALA A 1 3556 ? 219.453 193.771 264.992 1.00 7.96  ? 3556 ALA A N     1 
ATOM   15093 C  CA    . ALA A 1 3556 ? 218.066 193.464 265.323 1.00 7.39  ? 3556 ALA A CA    1 
ATOM   15094 C  C     . ALA A 1 3556 ? 217.150 194.656 265.078 1.00 8.32  ? 3556 ALA A C     1 
ATOM   15095 O  O     . ALA A 1 3556 ? 215.980 194.473 264.724 1.00 13.72 ? 3556 ALA A O     1 
ATOM   15096 C  CB    . ALA A 1 3556 ? 217.963 193.004 266.776 1.00 8.77  ? 3556 ALA A CB    1 
ATOM   15097 N  N     . ASP A 1 3557 ? 217.658 195.876 265.266 1.00 7.69  ? 3557 ASP A N     1 
ATOM   15098 C  CA    . ASP A 1 3557 ? 216.847 197.062 265.015 1.00 8.14  ? 3557 ASP A CA    1 
ATOM   15099 C  C     . ASP A 1 3557 ? 216.449 197.160 263.549 1.00 11.75 ? 3557 ASP A C     1 
ATOM   15100 O  O     . ASP A 1 3557 ? 215.302 197.493 263.229 1.00 10.99 ? 3557 ASP A O     1 
ATOM   15101 C  CB    . ASP A 1 3557 ? 217.606 198.315 265.448 1.00 8.71  ? 3557 ASP A CB    1 
ATOM   15102 C  CG    . ASP A 1 3557 ? 217.721 198.433 266.953 1.00 18.04 ? 3557 ASP A CG    1 
ATOM   15103 O  OD1   . ASP A 1 3557 ? 216.794 197.988 267.656 1.00 20.73 ? 3557 ASP A OD1   1 
ATOM   15104 O  OD2   . ASP A 1 3557 ? 218.742 198.970 267.432 1.00 24.65 ? 3557 ASP A OD2   1 
ATOM   15105 N  N     . GLU A 1 3558 ? 217.386 196.881 262.642 1.00 6.61  ? 3558 GLU A N     1 
ATOM   15106 C  CA    . GLU A 1 3558 ? 217.077 196.954 261.218 1.00 8.27  ? 3558 GLU A CA    1 
ATOM   15107 C  C     . GLU A 1 3558 ? 216.122 195.844 260.801 1.00 7.00  ? 3558 GLU A C     1 
ATOM   15108 O  O     . GLU A 1 3558 ? 215.239 196.059 259.964 1.00 5.82  ? 3558 GLU A O     1 
ATOM   15109 C  CB    . GLU A 1 3558 ? 218.364 196.894 260.400 1.00 9.08  ? 3558 GLU A CB    1 
ATOM   15110 C  CG    . GLU A 1 3558 ? 218.188 197.324 258.965 1.00 12.59 ? 3558 GLU A CG    1 
ATOM   15111 C  CD    . GLU A 1 3558 ? 219.508 197.546 258.256 1.00 23.28 ? 3558 GLU A CD    1 
ATOM   15112 O  OE1   . GLU A 1 3558 ? 220.533 197.001 258.719 1.00 19.86 ? 3558 GLU A OE1   1 
ATOM   15113 O  OE2   . GLU A 1 3558 ? 219.515 198.265 257.236 1.00 23.18 ? 3558 GLU A OE2   1 
ATOM   15114 N  N     . ARG A 1 3559 ? 216.286 194.648 261.369 1.00 7.36  ? 3559 ARG A N     1 
ATOM   15115 C  CA    . ARG A 1 3559 ? 215.379 193.550 261.054 1.00 5.65  ? 3559 ARG A CA    1 
ATOM   15116 C  C     . ARG A 1 3559 ? 213.967 193.838 261.547 1.00 6.32  ? 3559 ARG A C     1 
ATOM   15117 O  O     . ARG A 1 3559 ? 212.991 193.446 260.899 1.00 6.20  ? 3559 ARG A O     1 
ATOM   15118 C  CB    . ARG A 1 3559 ? 215.908 192.248 261.652 1.00 4.93  ? 3559 ARG A CB    1 
ATOM   15119 C  CG    . ARG A 1 3559 ? 217.170 191.741 260.981 1.00 4.91  ? 3559 ARG A CG    1 
ATOM   15120 C  CD    . ARG A 1 3559 ? 217.599 190.388 261.519 1.00 5.87  ? 3559 ARG A CD    1 
ATOM   15121 N  NE    . ARG A 1 3559 ? 217.865 190.425 262.951 1.00 8.35  ? 3559 ARG A NE    1 
ATOM   15122 C  CZ    . ARG A 1 3559 ? 219.069 190.292 263.493 1.00 9.09  ? 3559 ARG A CZ    1 
ATOM   15123 N  NH1   . ARG A 1 3559 ? 220.150 190.143 262.746 1.00 8.20  ? 3559 ARG A NH1   1 
ATOM   15124 N  NH2   . ARG A 1 3559 ? 219.190 190.315 264.816 1.00 10.16 ? 3559 ARG A NH2   1 
ATOM   15125 N  N     . LEU A 1 3560 ? 213.842 194.522 262.688 1.00 8.84  ? 3560 LEU A N     1 
ATOM   15126 C  CA    . LEU A 1 3560 ? 212.526 194.908 263.185 1.00 7.34  ? 3560 LEU A CA    1 
ATOM   15127 C  C     . LEU A 1 3560 ? 211.825 195.852 262.218 1.00 6.84  ? 3560 LEU A C     1 
ATOM   15128 O  O     . LEU A 1 3560 ? 210.624 195.714 261.963 1.00 10.63 ? 3560 LEU A O     1 
ATOM   15129 C  CB    . LEU A 1 3560 ? 212.661 195.553 264.564 1.00 11.81 ? 3560 LEU A CB    1 
ATOM   15130 C  CG    . LEU A 1 3560 ? 211.397 195.675 265.416 1.00 11.48 ? 3560 LEU A CG    1 
ATOM   15131 C  CD1   . LEU A 1 3560 ? 210.872 194.305 265.791 1.00 6.76  ? 3560 LEU A CD1   1 
ATOM   15132 C  CD2   . LEU A 1 3560 ? 211.673 196.505 266.656 1.00 16.65 ? 3560 LEU A CD2   1 
ATOM   15133 N  N     . ARG A 1 3561 ? 212.560 196.826 261.673 1.00 7.20  ? 3561 ARG A N     1 
ATOM   15134 C  CA    . ARG A 1 3561 ? 211.968 197.737 260.698 1.00 6.08  ? 3561 ARG A CA    1 
ATOM   15135 C  C     . ARG A 1 3561 ? 211.655 197.018 259.392 1.00 7.98  ? 3561 ARG A C     1 
ATOM   15136 O  O     . ARG A 1 3561 ? 210.644 197.311 258.744 1.00 10.14 ? 3561 ARG A O     1 
ATOM   15137 C  CB    . ARG A 1 3561 ? 212.900 198.924 260.453 1.00 8.03  ? 3561 ARG A CB    1 
ATOM   15138 C  CG    . ARG A 1 3561 ? 212.445 199.847 259.336 1.00 11.42 ? 3561 ARG A CG    1 
ATOM   15139 C  CD    . ARG A 1 3561 ? 213.387 201.025 259.161 1.00 15.34 ? 3561 ARG A CD    1 
ATOM   15140 N  NE    . ARG A 1 3561 ? 214.414 200.749 258.164 1.00 21.94 ? 3561 ARG A NE    1 
ATOM   15141 C  CZ    . ARG A 1 3561 ? 215.602 200.233 258.439 1.00 18.48 ? 3561 ARG A CZ    1 
ATOM   15142 N  NH1   . ARG A 1 3561 ? 215.962 199.947 259.679 1.00 18.53 ? 3561 ARG A NH1   1 
ATOM   15143 N  NH2   . ARG A 1 3561 ? 216.454 199.999 257.444 1.00 16.97 ? 3561 ARG A NH2   1 
ATOM   15144 N  N     . TRP A 1 3562 ? 212.508 196.070 258.993 1.00 7.73  ? 3562 TRP A N     1 
ATOM   15145 C  CA    . TRP A 1 3562 ? 212.260 195.318 257.767 1.00 5.92  ? 3562 TRP A CA    1 
ATOM   15146 C  C     . TRP A 1 3562 ? 210.944 194.557 257.847 1.00 6.99  ? 3562 TRP A C     1 
ATOM   15147 O  O     . TRP A 1 3562 ? 210.200 194.485 256.864 1.00 10.89 ? 3562 TRP A O     1 
ATOM   15148 C  CB    . TRP A 1 3562 ? 213.419 194.359 257.492 1.00 4.82  ? 3562 TRP A CB    1 
ATOM   15149 C  CG    . TRP A 1 3562 ? 214.658 195.031 256.997 1.00 3.37  ? 3562 TRP A CG    1 
ATOM   15150 C  CD1   . TRP A 1 3562 ? 214.762 196.297 256.502 1.00 3.72  ? 3562 TRP A CD1   1 
ATOM   15151 C  CD2   . TRP A 1 3562 ? 215.974 194.472 256.947 1.00 4.19  ? 3562 TRP A CD2   1 
ATOM   15152 N  NE1   . TRP A 1 3562 ? 216.061 196.562 256.149 1.00 4.59  ? 3562 TRP A NE1   1 
ATOM   15153 C  CE2   . TRP A 1 3562 ? 216.825 195.457 256.411 1.00 4.22  ? 3562 TRP A CE2   1 
ATOM   15154 C  CE3   . TRP A 1 3562 ? 216.517 193.235 257.306 1.00 3.11  ? 3562 TRP A CE3   1 
ATOM   15155 C  CZ2   . TRP A 1 3562 ? 218.188 195.242 256.221 1.00 2.30  ? 3562 TRP A CZ2   1 
ATOM   15156 C  CZ3   . TRP A 1 3562 ? 217.869 193.026 257.120 1.00 1.76  ? 3562 TRP A CZ3   1 
ATOM   15157 C  CH2   . TRP A 1 3562 ? 218.691 194.024 256.585 1.00 2.15  ? 3562 TRP A CH2   1 
ATOM   15158 N  N     . GLN A 1 3563 ? 210.640 193.988 259.014 1.00 8.43  ? 3563 GLN A N     1 
ATOM   15159 C  CA    . GLN A 1 3563 ? 209.355 193.323 259.199 1.00 6.83  ? 3563 GLN A CA    1 
ATOM   15160 C  C     . GLN A 1 3563 ? 208.200 194.305 259.048 1.00 6.47  ? 3563 GLN A C     1 
ATOM   15161 O  O     . GLN A 1 3563 ? 207.176 193.980 258.435 1.00 5.75  ? 3563 GLN A O     1 
ATOM   15162 C  CB    . GLN A 1 3563 ? 209.308 192.648 260.569 1.00 6.14  ? 3563 GLN A CB    1 
ATOM   15163 C  CG    . GLN A 1 3563 ? 209.647 191.173 260.542 1.00 12.68 ? 3563 GLN A CG    1 
ATOM   15164 C  CD    . GLN A 1 3563 ? 209.855 190.601 261.929 1.00 23.09 ? 3563 GLN A CD    1 
ATOM   15165 O  OE1   . GLN A 1 3563 ? 209.248 191.057 262.899 1.00 26.17 ? 3563 GLN A OE1   1 
ATOM   15166 N  NE2   . GLN A 1 3563 ? 210.720 189.598 262.031 1.00 25.82 ? 3563 GLN A NE2   1 
ATOM   15167 N  N     . ALA A 1 3564 ? 208.348 195.512 259.599 1.00 8.83  ? 3564 ALA A N     1 
ATOM   15168 C  CA    . ALA A 1 3564 ? 207.307 196.524 259.461 1.00 5.97  ? 3564 ALA A CA    1 
ATOM   15169 C  C     . ALA A 1 3564 ? 207.104 196.926 258.005 1.00 10.06 ? 3564 ALA A C     1 
ATOM   15170 O  O     . ALA A 1 3564 ? 206.007 197.348 257.624 1.00 13.24 ? 3564 ALA A O     1 
ATOM   15171 C  CB    . ALA A 1 3564 ? 207.649 197.747 260.308 1.00 4.41  ? 3564 ALA A CB    1 
ATOM   15172 N  N     . SER A 1 3565 ? 208.141 196.800 257.180 1.00 8.79  ? 3565 SER A N     1 
ATOM   15173 C  CA    . SER A 1 3565 ? 208.052 197.068 255.754 1.00 5.06  ? 3565 SER A CA    1 
ATOM   15174 C  C     . SER A 1 3565 ? 207.545 195.873 254.959 1.00 6.25  ? 3565 SER A C     1 
ATOM   15175 O  O     . SER A 1 3565 ? 207.720 195.843 253.735 1.00 9.36  ? 3565 SER A O     1 
ATOM   15176 C  CB    . SER A 1 3565 ? 209.411 197.518 255.215 1.00 8.86  ? 3565 SER A CB    1 
ATOM   15177 O  OG    . SER A 1 3565 ? 209.794 198.760 255.773 1.00 9.84  ? 3565 SER A OG    1 
ATOM   15178 N  N     . SER A 1 3566 ? 206.935 194.898 255.637 1.00 8.76  ? 3566 SER A N     1 
ATOM   15179 C  CA    . SER A 1 3566 ? 206.335 193.713 255.024 1.00 4.98  ? 3566 SER A CA    1 
ATOM   15180 C  C     . SER A 1 3566 ? 207.369 192.799 254.373 1.00 6.96  ? 3566 SER A C     1 
ATOM   15181 O  O     . SER A 1 3566 ? 207.068 192.115 253.394 1.00 12.94 ? 3566 SER A O     1 
ATOM   15182 C  CB    . SER A 1 3566 ? 205.249 194.090 254.008 1.00 7.34  ? 3566 SER A CB    1 
ATOM   15183 O  OG    . SER A 1 3566 ? 205.804 194.710 252.860 1.00 14.32 ? 3566 SER A OG    1 
ATOM   15184 N  N     . LEU A 1 3567 ? 208.587 192.771 254.901 1.00 5.84  ? 3567 LEU A N     1 
ATOM   15185 C  CA    . LEU A 1 3567 ? 209.559 191.785 254.443 1.00 5.35  ? 3567 LEU A CA    1 
ATOM   15186 C  C     . LEU A 1 3567 ? 209.254 190.431 255.077 1.00 8.28  ? 3567 LEU A C     1 
ATOM   15187 O  O     . LEU A 1 3567 ? 209.113 190.348 256.301 1.00 8.53  ? 3567 LEU A O     1 
ATOM   15188 C  CB    . LEU A 1 3567 ? 210.981 192.209 254.786 1.00 5.45  ? 3567 LEU A CB    1 
ATOM   15189 C  CG    . LEU A 1 3567 ? 212.080 191.281 254.260 1.00 3.99  ? 3567 LEU A CG    1 
ATOM   15190 C  CD1   . LEU A 1 3567 ? 212.351 191.545 252.787 1.00 3.37  ? 3567 LEU A CD1   1 
ATOM   15191 C  CD2   . LEU A 1 3567 ? 213.351 191.416 255.080 1.00 2.03  ? 3567 LEU A CD2   1 
ATOM   15192 N  N     . PRO A 1 3568 ? 209.138 189.364 254.287 1.00 5.04  ? 3568 PRO A N     1 
ATOM   15193 C  CA    . PRO A 1 3568 ? 208.817 188.052 254.859 1.00 4.15  ? 3568 PRO A CA    1 
ATOM   15194 C  C     . PRO A 1 3568 ? 209.854 187.606 255.879 1.00 7.98  ? 3568 PRO A C     1 
ATOM   15195 O  O     . PRO A 1 3568 ? 211.052 187.852 255.728 1.00 8.30  ? 3568 PRO A O     1 
ATOM   15196 C  CB    . PRO A 1 3568 ? 208.804 187.131 253.635 1.00 4.56  ? 3568 PRO A CB    1 
ATOM   15197 C  CG    . PRO A 1 3568 ? 208.505 188.034 252.493 1.00 4.72  ? 3568 PRO A CG    1 
ATOM   15198 C  CD    . PRO A 1 3568 ? 209.179 189.331 252.816 1.00 6.30  ? 3568 PRO A CD    1 
ATOM   15199 N  N     . ALA A 1 3569 ? 209.374 186.942 256.933 1.00 6.34  ? 3569 ALA A N     1 
ATOM   15200 C  CA    . ALA A 1 3569 ? 210.236 186.442 258.004 1.00 6.81  ? 3569 ALA A CA    1 
ATOM   15201 C  C     . ALA A 1 3569 ? 210.911 185.164 257.519 1.00 16.22 ? 3569 ALA A C     1 
ATOM   15202 O  O     . ALA A 1 3569 ? 210.518 184.043 257.847 1.00 23.37 ? 3569 ALA A O     1 
ATOM   15203 C  CB    . ALA A 1 3569 ? 209.437 186.215 259.280 1.00 9.26  ? 3569 ALA A CB    1 
ATOM   15204 N  N     . ASP A 1 3570 ? 211.955 185.352 256.714 1.00 10.40 ? 3570 ASP A N     1 
ATOM   15205 C  CA    . ASP A 1 3570 ? 212.667 184.253 256.084 1.00 6.54  ? 3570 ASP A CA    1 
ATOM   15206 C  C     . ASP A 1 3570 ? 214.138 184.628 255.983 1.00 5.75  ? 3570 ASP A C     1 
ATOM   15207 O  O     . ASP A 1 3570 ? 214.471 185.791 255.746 1.00 7.94  ? 3570 ASP A O     1 
ATOM   15208 C  CB    . ASP A 1 3570 ? 212.085 183.952 254.698 1.00 5.77  ? 3570 ASP A CB    1 
ATOM   15209 C  CG    . ASP A 1 3570 ? 212.824 182.849 253.980 1.00 8.40  ? 3570 ASP A CG    1 
ATOM   15210 O  OD1   . ASP A 1 3570 ? 213.078 181.798 254.604 1.00 14.26 ? 3570 ASP A OD1   1 
ATOM   15211 O  OD2   . ASP A 1 3570 ? 213.148 183.033 252.791 1.00 8.12  ? 3570 ASP A OD2   1 
ATOM   15212 N  N     . ASP A 1 3571 ? 215.015 183.638 256.170 1.00 3.97  ? 3571 ASP A N     1 
ATOM   15213 C  CA    . ASP A 1 3571 ? 216.449 183.910 256.157 1.00 5.34  ? 3571 ASP A CA    1 
ATOM   15214 C  C     . ASP A 1 3571 ? 216.914 184.398 254.792 1.00 3.73  ? 3571 ASP A C     1 
ATOM   15215 O  O     . ASP A 1 3571 ? 217.699 185.347 254.700 1.00 2.13  ? 3571 ASP A O     1 
ATOM   15216 C  CB    . ASP A 1 3571 ? 217.226 182.665 256.577 1.00 7.53  ? 3571 ASP A CB    1 
ATOM   15217 C  CG    . ASP A 1 3571 ? 217.391 182.565 258.077 1.00 14.52 ? 3571 ASP A CG    1 
ATOM   15218 O  OD1   . ASP A 1 3571 ? 216.887 183.455 258.792 1.00 10.68 ? 3571 ASP A OD1   1 
ATOM   15219 O  OD2   . ASP A 1 3571 ? 218.031 181.598 258.545 1.00 22.06 ? 3571 ASP A OD2   1 
ATOM   15220 N  N     . LEU A 1 3572 ? 216.443 183.763 253.717 1.00 3.63  ? 3572 LEU A N     1 
ATOM   15221 C  CA    . LEU A 1 3572 ? 216.817 184.209 252.379 1.00 2.53  ? 3572 LEU A CA    1 
ATOM   15222 C  C     . LEU A 1 3572 ? 216.274 185.606 252.095 1.00 1.91  ? 3572 LEU A C     1 
ATOM   15223 O  O     . LEU A 1 3572 ? 216.944 186.421 251.453 1.00 1.12  ? 3572 LEU A O     1 
ATOM   15224 C  CB    . LEU A 1 3572 ? 216.341 183.196 251.335 1.00 1.02  ? 3572 LEU A CB    1 
ATOM   15225 C  CG    . LEU A 1 3572 ? 216.783 183.374 249.877 1.00 1.27  ? 3572 LEU A CG    1 
ATOM   15226 C  CD1   . LEU A 1 3572 ? 216.842 182.033 249.182 1.00 1.25  ? 3572 LEU A CD1   1 
ATOM   15227 C  CD2   . LEU A 1 3572 ? 215.834 184.294 249.119 1.00 0.77  ? 3572 LEU A CD2   1 
ATOM   15228 N  N     . CYS A 1 3573 ? 215.059 185.899 252.562 1.00 1.82  ? 3573 CYS A N     1 
ATOM   15229 C  CA    . CYS A 1 3573 ? 214.523 187.249 252.422 1.00 1.94  ? 3573 CYS A CA    1 
ATOM   15230 C  C     . CYS A 1 3573 ? 215.339 188.253 253.229 1.00 1.20  ? 3573 CYS A C     1 
ATOM   15231 O  O     . CYS A 1 3573 ? 215.560 189.383 252.780 1.00 0.78  ? 3573 CYS A O     1 
ATOM   15232 C  CB    . CYS A 1 3573 ? 213.055 187.276 252.841 1.00 2.78  ? 3573 CYS A CB    1 
ATOM   15233 S  SG    . CYS A 1 3573 ? 211.940 186.498 251.651 1.00 14.26 ? 3573 CYS A SG    1 
ATOM   15234 N  N     . THR A 1 3574 ? 215.788 187.862 254.424 1.00 1.99  ? 3574 THR A N     1 
ATOM   15235 C  CA    . THR A 1 3574 ? 216.659 188.730 255.210 1.00 0.96  ? 3574 THR A CA    1 
ATOM   15236 C  C     . THR A 1 3574 ? 218.003 188.933 254.518 1.00 0.62  ? 3574 THR A C     1 
ATOM   15237 O  O     . THR A 1 3574 ? 218.556 190.038 254.536 1.00 1.00  ? 3574 THR A O     1 
ATOM   15238 C  CB    . THR A 1 3574 ? 216.853 188.146 256.610 1.00 0.77  ? 3574 THR A CB    1 
ATOM   15239 O  OG1   . THR A 1 3574 ? 215.574 187.952 257.224 1.00 7.14  ? 3574 THR A OG1   1 
ATOM   15240 C  CG2   . THR A 1 3574 ? 217.675 189.087 257.473 1.00 0.53  ? 3574 THR A CG2   1 
ATOM   15241 N  N     . GLU A 1 3575 ? 218.542 187.879 253.903 1.00 0.59  ? 3575 GLU A N     1 
ATOM   15242 C  CA    . GLU A 1 3575 ? 219.768 188.017 253.124 1.00 0.74  ? 3575 GLU A CA    1 
ATOM   15243 C  C     . GLU A 1 3575 ? 219.580 188.992 251.970 1.00 0.53  ? 3575 GLU A C     1 
ATOM   15244 O  O     . GLU A 1 3575 ? 220.476 189.787 251.664 1.00 0.54  ? 3575 GLU A O     1 
ATOM   15245 C  CB    . GLU A 1 3575 ? 220.215 186.653 252.599 1.00 0.77  ? 3575 GLU A CB    1 
ATOM   15246 C  CG    . GLU A 1 3575 ? 220.747 185.710 253.658 1.00 1.09  ? 3575 GLU A CG    1 
ATOM   15247 C  CD    . GLU A 1 3575 ? 220.923 184.291 253.147 1.00 3.16  ? 3575 GLU A CD    1 
ATOM   15248 O  OE1   . GLU A 1 3575 ? 220.549 184.017 251.989 1.00 3.90  ? 3575 GLU A OE1   1 
ATOM   15249 O  OE2   . GLU A 1 3575 ? 221.447 183.450 253.905 1.00 9.29  ? 3575 GLU A OE2   1 
ATOM   15250 N  N     . ASN A 1 3576 ? 218.424 188.934 251.309 1.00 0.43  ? 3576 ASN A N     1 
ATOM   15251 C  CA    . ASN A 1 3576 ? 218.136 189.859 250.220 1.00 0.33  ? 3576 ASN A CA    1 
ATOM   15252 C  C     . ASN A 1 3576 ? 218.064 191.298 250.714 1.00 0.36  ? 3576 ASN A C     1 
ATOM   15253 O  O     . ASN A 1 3576 ? 218.553 192.216 250.047 1.00 0.39  ? 3576 ASN A O     1 
ATOM   15254 C  CB    . ASN A 1 3576 ? 216.834 189.457 249.530 1.00 0.42  ? 3576 ASN A CB    1 
ATOM   15255 C  CG    . ASN A 1 3576 ? 216.969 188.173 248.743 1.00 0.26  ? 3576 ASN A CG    1 
ATOM   15256 O  OD1   . ASN A 1 3576 ? 218.027 187.554 248.732 1.00 0.67  ? 3576 ASN A OD1   1 
ATOM   15257 N  ND2   . ASN A 1 3576 ? 215.899 187.772 248.073 1.00 0.21  ? 3576 ASN A ND2   1 
ATOM   15258 N  N     . ALA A 1 3577 ? 217.456 191.514 251.884 1.00 0.37  ? 3577 ALA A N     1 
ATOM   15259 C  CA    . ALA A 1 3577 ? 217.376 192.857 252.444 1.00 0.29  ? 3577 ALA A CA    1 
ATOM   15260 C  C     . ALA A 1 3577 ? 218.762 193.426 252.724 1.00 0.46  ? 3577 ALA A C     1 
ATOM   15261 O  O     . ALA A 1 3577 ? 219.015 194.610 252.479 1.00 0.59  ? 3577 ALA A O     1 
ATOM   15262 C  CB    . ALA A 1 3577 ? 216.534 192.842 253.719 1.00 0.57  ? 3577 ALA A CB    1 
ATOM   15263 N  N     . ILE A 1 3578 ? 219.670 192.594 253.241 1.00 0.45  ? 3578 ILE A N     1 
ATOM   15264 C  CA    . ILE A 1 3578 ? 221.045 193.030 253.467 1.00 0.49  ? 3578 ILE A CA    1 
ATOM   15265 C  C     . ILE A 1 3578 ? 221.699 193.429 252.150 1.00 0.43  ? 3578 ILE A C     1 
ATOM   15266 O  O     . ILE A 1 3578 ? 222.415 194.436 252.074 1.00 0.50  ? 3578 ILE A O     1 
ATOM   15267 C  CB    . ILE A 1 3578 ? 221.839 191.924 254.185 1.00 0.79  ? 3578 ILE A CB    1 
ATOM   15268 C  CG1   . ILE A 1 3578 ? 221.198 191.604 255.535 1.00 0.56  ? 3578 ILE A CG1   1 
ATOM   15269 C  CG2   . ILE A 1 3578 ? 223.293 192.330 254.345 1.00 0.72  ? 3578 ILE A CG2   1 
ATOM   15270 C  CD1   . ILE A 1 3578 ? 221.840 190.453 256.261 1.00 1.22  ? 3578 ILE A CD1   1 
ATOM   15271 N  N     . MET A 1 3579 ? 221.465 192.647 251.096 1.00 0.31  ? 3579 MET A N     1 
ATOM   15272 C  CA    . MET A 1 3579 ? 221.979 192.992 249.777 1.00 0.24  ? 3579 MET A CA    1 
ATOM   15273 C  C     . MET A 1 3579 ? 221.387 194.299 249.268 1.00 0.24  ? 3579 MET A C     1 
ATOM   15274 O  O     . MET A 1 3579 ? 222.095 195.100 248.647 1.00 0.39  ? 3579 MET A O     1 
ATOM   15275 C  CB    . MET A 1 3579 ? 221.685 191.858 248.800 1.00 0.28  ? 3579 MET A CB    1 
ATOM   15276 C  CG    . MET A 1 3579 ? 222.419 190.580 249.122 1.00 0.25  ? 3579 MET A CG    1 
ATOM   15277 S  SD    . MET A 1 3579 ? 221.928 189.217 248.060 1.00 4.08  ? 3579 MET A SD    1 
ATOM   15278 C  CE    . MET A 1 3579 ? 222.783 187.855 248.845 1.00 0.36  ? 3579 MET A CE    1 
ATOM   15279 N  N     . LEU A 1 3580 ? 220.103 194.536 249.524 1.00 0.32  ? 3580 LEU A N     1 
ATOM   15280 C  CA    . LEU A 1 3580 ? 219.435 195.766 249.122 1.00 0.21  ? 3580 LEU A CA    1 
ATOM   15281 C  C     . LEU A 1 3580 ? 219.883 196.974 249.928 1.00 0.26  ? 3580 LEU A C     1 
ATOM   15282 O  O     . LEU A 1 3580 ? 219.506 198.100 249.587 1.00 1.01  ? 3580 LEU A O     1 
ATOM   15283 C  CB    . LEU A 1 3580 ? 217.918 195.600 249.236 1.00 0.31  ? 3580 LEU A CB    1 
ATOM   15284 C  CG    . LEU A 1 3580 ? 217.284 194.589 248.279 1.00 0.26  ? 3580 LEU A CG    1 
ATOM   15285 C  CD1   . LEU A 1 3580 ? 215.826 194.350 248.626 1.00 0.39  ? 3580 LEU A CD1   1 
ATOM   15286 C  CD2   . LEU A 1 3580 ? 217.425 195.057 246.843 1.00 0.20  ? 3580 LEU A CD2   1 
ATOM   15287 N  N     . LYS A 1 3581 ? 220.664 196.773 250.983 1.00 0.41  ? 3581 LYS A N     1 
ATOM   15288 C  CA    . LYS A 1 3581 ? 221.194 197.860 251.794 1.00 0.55  ? 3581 LYS A CA    1 
ATOM   15289 C  C     . LYS A 1 3581 ? 222.685 198.085 251.595 1.00 1.38  ? 3581 LYS A C     1 
ATOM   15290 O  O     . LYS A 1 3581 ? 223.129 199.234 251.575 1.00 5.00  ? 3581 LYS A O     1 
ATOM   15291 C  CB    . LYS A 1 3581 ? 220.908 197.582 253.279 1.00 0.85  ? 3581 LYS A CB    1 
ATOM   15292 C  CG    . LYS A 1 3581 ? 221.556 198.559 254.239 1.00 6.85  ? 3581 LYS A CG    1 
ATOM   15293 C  CD    . LYS A 1 3581 ? 222.079 197.847 255.474 1.00 13.46 ? 3581 LYS A CD    1 
ATOM   15294 C  CE    . LYS A 1 3581 ? 222.615 198.838 256.495 1.00 15.79 ? 3581 LYS A CE    1 
ATOM   15295 N  NZ    . LYS A 1 3581 ? 223.230 198.159 257.667 1.00 10.24 ? 3581 LYS A NZ    1 
ATOM   15296 N  N     . ARG A 1 3582 ? 223.468 197.019 251.426 1.00 1.84  ? 3582 ARG A N     1 
ATOM   15297 C  CA    . ARG A 1 3582 ? 224.920 197.114 251.317 1.00 2.32  ? 3582 ARG A CA    1 
ATOM   15298 C  C     . ARG A 1 3582 ? 225.416 197.004 249.880 1.00 1.10  ? 3582 ARG A C     1 
ATOM   15299 O  O     . ARG A 1 3582 ? 226.606 196.760 249.661 1.00 2.91  ? 3582 ARG A O     1 
ATOM   15300 C  CB    . ARG A 1 3582 ? 225.595 196.041 252.173 1.00 1.28  ? 3582 ARG A CB    1 
ATOM   15301 C  CG    . ARG A 1 3582 ? 225.288 196.103 253.651 1.00 1.41  ? 3582 ARG A CG    1 
ATOM   15302 C  CD    . ARG A 1 3582 ? 225.921 194.919 254.365 1.00 2.05  ? 3582 ARG A CD    1 
ATOM   15303 N  NE    . ARG A 1 3582 ? 225.745 194.957 255.812 1.00 7.44  ? 3582 ARG A NE    1 
ATOM   15304 C  CZ    . ARG A 1 3582 ? 226.260 195.880 256.614 1.00 5.77  ? 3582 ARG A CZ    1 
ATOM   15305 N  NH1   . ARG A 1 3582 ? 227.029 196.851 256.153 1.00 6.10  ? 3582 ARG A NH1   1 
ATOM   15306 N  NH2   . ARG A 1 3582 ? 226.003 195.819 257.918 1.00 4.92  ? 3582 ARG A NH2   1 
ATOM   15307 N  N     . PHE A 1 3583 ? 224.535 197.169 248.899 1.00 0.50  ? 3583 PHE A N     1 
ATOM   15308 C  CA    . PHE A 1 3583 ? 224.930 196.996 247.507 1.00 0.82  ? 3583 PHE A CA    1 
ATOM   15309 C  C     . PHE A 1 3583 ? 225.928 198.066 247.084 1.00 0.71  ? 3583 PHE A C     1 
ATOM   15310 O  O     . PHE A 1 3583 ? 225.884 199.205 247.558 1.00 1.00  ? 3583 PHE A O     1 
ATOM   15311 C  CB    . PHE A 1 3583 ? 223.704 197.048 246.594 1.00 0.31  ? 3583 PHE A CB    1 
ATOM   15312 C  CG    . PHE A 1 3583 ? 222.994 198.369 246.614 1.00 0.47  ? 3583 PHE A CG    1 
ATOM   15313 C  CD1   . PHE A 1 3583 ? 223.341 199.376 245.727 1.00 0.44  ? 3583 PHE A CD1   1 
ATOM   15314 C  CD2   . PHE A 1 3583 ? 221.983 198.612 247.529 1.00 0.41  ? 3583 PHE A CD2   1 
ATOM   15315 C  CE1   . PHE A 1 3583 ? 222.699 200.590 245.753 1.00 0.26  ? 3583 PHE A CE1   1 
ATOM   15316 C  CE2   . PHE A 1 3583 ? 221.333 199.822 247.555 1.00 0.41  ? 3583 PHE A CE2   1 
ATOM   15317 C  CZ    . PHE A 1 3583 ? 221.692 200.813 246.667 1.00 0.41  ? 3583 PHE A CZ    1 
ATOM   15318 N  N     . ASN A 1 3584 ? 226.835 197.690 246.187 1.00 1.16  ? 3584 ASN A N     1 
ATOM   15319 C  CA    . ASN A 1 3584 ? 227.674 198.656 245.487 1.00 2.34  ? 3584 ASN A CA    1 
ATOM   15320 C  C     . ASN A 1 3584 ? 227.121 198.935 244.094 1.00 1.67  ? 3584 ASN A C     1 
ATOM   15321 O  O     . ASN A 1 3584 ? 226.803 200.081 243.765 1.00 12.04 ? 3584 ASN A O     1 
ATOM   15322 C  CB    . ASN A 1 3584 ? 229.120 198.154 245.407 1.00 2.18  ? 3584 ASN A CB    1 
ATOM   15323 C  CG    . ASN A 1 3584 ? 229.771 198.042 246.766 1.00 4.13  ? 3584 ASN A CG    1 
ATOM   15324 O  OD1   . ASN A 1 3584 ? 229.518 198.851 247.659 1.00 11.52 ? 3584 ASN A OD1   1 
ATOM   15325 N  ND2   . ASN A 1 3584 ? 230.622 197.039 246.935 1.00 1.60  ? 3584 ASN A ND2   1 
ATOM   15326 N  N     . ARG A 1 3585 ? 226.993 197.900 243.274 1.00 0.67  ? 3585 ARG A N     1 
ATOM   15327 C  CA    . ARG A 1 3585 ? 226.234 198.012 242.041 1.00 0.56  ? 3585 ARG A CA    1 
ATOM   15328 C  C     . ARG A 1 3585 ? 224.747 198.055 242.364 1.00 0.33  ? 3585 ARG A C     1 
ATOM   15329 O  O     . ARG A 1 3585 ? 224.290 197.483 243.356 1.00 1.09  ? 3585 ARG A O     1 
ATOM   15330 C  CB    . ARG A 1 3585 ? 226.540 196.844 241.104 1.00 0.76  ? 3585 ARG A CB    1 
ATOM   15331 C  CG    . ARG A 1 3585 ? 227.938 196.866 240.513 1.00 0.92  ? 3585 ARG A CG    1 
ATOM   15332 C  CD    . ARG A 1 3585 ? 228.185 195.628 239.672 1.00 1.15  ? 3585 ARG A CD    1 
ATOM   15333 N  NE    . ARG A 1 3585 ? 228.105 194.409 240.463 1.00 0.36  ? 3585 ARG A NE    1 
ATOM   15334 C  CZ    . ARG A 1 3585 ? 228.220 193.185 239.970 1.00 0.22  ? 3585 ARG A CZ    1 
ATOM   15335 N  NH1   . ARG A 1 3585 ? 228.388 192.975 238.676 1.00 0.49  ? 3585 ARG A NH1   1 
ATOM   15336 N  NH2   . ARG A 1 3585 ? 228.155 192.144 240.794 1.00 0.36  ? 3585 ARG A NH2   1 
ATOM   15337 N  N     . TYR A 1 3586 ? 223.994 198.750 241.520 1.00 0.22  ? 3586 TYR A N     1 
ATOM   15338 C  CA    . TYR A 1 3586 ? 222.579 198.939 241.795 1.00 0.20  ? 3586 TYR A CA    1 
ATOM   15339 C  C     . TYR A 1 3586 ? 221.840 197.608 241.702 1.00 0.15  ? 3586 TYR A C     1 
ATOM   15340 O  O     . TYR A 1 3586 ? 222.143 196.785 240.832 1.00 0.16  ? 3586 TYR A O     1 
ATOM   15341 C  CB    . TYR A 1 3586 ? 221.975 199.958 240.828 1.00 0.14  ? 3586 TYR A CB    1 
ATOM   15342 C  CG    . TYR A 1 3586 ? 222.443 201.372 241.081 1.00 0.16  ? 3586 TYR A CG    1 
ATOM   15343 C  CD1   . TYR A 1 3586 ? 222.089 202.041 242.243 1.00 0.15  ? 3586 TYR A CD1   1 
ATOM   15344 C  CD2   . TYR A 1 3586 ? 223.236 202.040 240.155 1.00 0.34  ? 3586 TYR A CD2   1 
ATOM   15345 C  CE1   . TYR A 1 3586 ? 222.512 203.332 242.479 1.00 0.21  ? 3586 TYR A CE1   1 
ATOM   15346 C  CE2   . TYR A 1 3586 ? 223.662 203.332 240.383 1.00 0.28  ? 3586 TYR A CE2   1 
ATOM   15347 C  CZ    . TYR A 1 3586 ? 223.296 203.973 241.547 1.00 0.26  ? 3586 TYR A CZ    1 
ATOM   15348 O  OH    . TYR A 1 3586 ? 223.718 205.261 241.781 1.00 0.33  ? 3586 TYR A OH    1 
ATOM   15349 N  N     . PRO A 1 3587 ? 220.873 197.361 242.583 1.00 0.26  ? 3587 PRO A N     1 
ATOM   15350 C  CA    . PRO A 1 3587 ? 220.239 196.041 242.637 1.00 0.15  ? 3587 PRO A CA    1 
ATOM   15351 C  C     . PRO A 1 3587 ? 219.232 195.820 241.520 1.00 0.11  ? 3587 PRO A C     1 
ATOM   15352 O  O     . PRO A 1 3587 ? 218.428 196.695 241.191 1.00 0.10  ? 3587 PRO A O     1 
ATOM   15353 C  CB    . PRO A 1 3587 ? 219.539 196.044 244.005 1.00 0.12  ? 3587 PRO A CB    1 
ATOM   15354 C  CG    . PRO A 1 3587 ? 220.124 197.212 244.747 1.00 0.18  ? 3587 PRO A CG    1 
ATOM   15355 C  CD    . PRO A 1 3587 ? 220.438 198.214 243.696 1.00 0.09  ? 3587 PRO A CD    1 
ATOM   15356 N  N     . LEU A 1 3588 ? 219.289 194.629 240.935 1.00 0.17  ? 3588 LEU A N     1 
ATOM   15357 C  CA    . LEU A 1 3588 ? 218.231 194.122 240.072 1.00 0.16  ? 3588 LEU A CA    1 
ATOM   15358 C  C     . LEU A 1 3588 ? 217.445 193.089 240.869 1.00 0.11  ? 3588 LEU A C     1 
ATOM   15359 O  O     . LEU A 1 3588 ? 218.004 192.077 241.303 1.00 0.09  ? 3588 LEU A O     1 
ATOM   15360 C  CB    . LEU A 1 3588 ? 218.804 193.512 238.792 1.00 0.17  ? 3588 LEU A CB    1 
ATOM   15361 C  CG    . LEU A 1 3588 ? 217.874 193.368 237.582 1.00 0.21  ? 3588 LEU A CG    1 
ATOM   15362 C  CD1   . LEU A 1 3588 ? 218.687 193.230 236.307 1.00 0.26  ? 3588 LEU A CD1   1 
ATOM   15363 C  CD2   . LEU A 1 3588 ? 216.918 192.186 237.730 1.00 0.12  ? 3588 LEU A CD2   1 
ATOM   15364 N  N     . ILE A 1 3589 ? 216.155 193.345 241.060 1.00 0.21  ? 3589 ILE A N     1 
ATOM   15365 C  CA    . ILE A 1 3589 ? 215.312 192.534 241.931 1.00 0.30  ? 3589 ILE A CA    1 
ATOM   15366 C  C     . ILE A 1 3589 ? 214.487 191.579 241.083 1.00 0.27  ? 3589 ILE A C     1 
ATOM   15367 O  O     . ILE A 1 3589 ? 213.824 191.997 240.127 1.00 0.40  ? 3589 ILE A O     1 
ATOM   15368 C  CB    . ILE A 1 3589 ? 214.406 193.417 242.804 1.00 0.30  ? 3589 ILE A CB    1 
ATOM   15369 C  CG1   . ILE A 1 3589 ? 215.249 194.307 243.717 1.00 0.23  ? 3589 ILE A CG1   1 
ATOM   15370 C  CG2   . ILE A 1 3589 ? 213.448 192.562 243.611 1.00 0.37  ? 3589 ILE A CG2   1 
ATOM   15371 C  CD1   . ILE A 1 3589 ? 214.470 195.429 244.359 1.00 2.94  ? 3589 ILE A CD1   1 
ATOM   15372 N  N     . ILE A 1 3590 ? 214.531 190.300 241.430 1.00 0.38  ? 3590 ILE A N     1 
ATOM   15373 C  CA    . ILE A 1 3590 ? 213.703 189.275 240.806 1.00 0.77  ? 3590 ILE A CA    1 
ATOM   15374 C  C     . ILE A 1 3590 ? 212.732 188.784 241.872 1.00 1.48  ? 3590 ILE A C     1 
ATOM   15375 O  O     . ILE A 1 3590 ? 213.116 188.046 242.784 1.00 1.67  ? 3590 ILE A O     1 
ATOM   15376 C  CB    . ILE A 1 3590 ? 214.541 188.128 240.234 1.00 0.61  ? 3590 ILE A CB    1 
ATOM   15377 C  CG1   . ILE A 1 3590 ? 215.542 188.659 239.207 1.00 0.43  ? 3590 ILE A CG1   1 
ATOM   15378 C  CG2   . ILE A 1 3590 ? 213.642 187.070 239.619 1.00 1.80  ? 3590 ILE A CG2   1 
ATOM   15379 C  CD1   . ILE A 1 3590 ? 216.496 187.620 238.691 1.00 0.41  ? 3590 ILE A CD1   1 
ATOM   15380 N  N     . ASP A 1 3591 ? 211.470 189.197 241.769 1.00 1.68  ? 3591 ASP A N     1 
ATOM   15381 C  CA    . ASP A 1 3591 ? 210.434 188.768 242.706 1.00 3.20  ? 3591 ASP A CA    1 
ATOM   15382 C  C     . ASP A 1 3591 ? 209.145 188.487 241.952 1.00 3.31  ? 3591 ASP A C     1 
ATOM   15383 O  O     . ASP A 1 3591 ? 208.356 189.399 241.678 1.00 4.03  ? 3591 ASP A O     1 
ATOM   15384 C  CB    . ASP A 1 3591 ? 210.199 189.809 243.798 1.00 3.82  ? 3591 ASP A CB    1 
ATOM   15385 C  CG    . ASP A 1 3591 ? 209.341 189.277 244.928 1.00 8.52  ? 3591 ASP A CG    1 
ATOM   15386 O  OD1   . ASP A 1 3591 ? 209.153 188.043 244.999 1.00 10.22 ? 3591 ASP A OD1   1 
ATOM   15387 O  OD2   . ASP A 1 3591 ? 208.844 190.084 245.737 1.00 12.06 ? 3591 ASP A OD2   1 
ATOM   15388 N  N     . PRO A 1 3592 ? 208.899 187.225 241.597 1.00 3.19  ? 3592 PRO A N     1 
ATOM   15389 C  CA    . PRO A 1 3592 ? 207.617 186.887 240.956 1.00 4.75  ? 3592 PRO A CA    1 
ATOM   15390 C  C     . PRO A 1 3592 ? 206.407 187.177 241.829 1.00 6.01  ? 3592 PRO A C     1 
ATOM   15391 O  O     . PRO A 1 3592 ? 205.354 187.558 241.304 1.00 7.90  ? 3592 PRO A O     1 
ATOM   15392 C  CB    . PRO A 1 3592 ? 207.756 185.387 240.657 1.00 1.94  ? 3592 PRO A CB    1 
ATOM   15393 C  CG    . PRO A 1 3592 ? 208.865 184.908 241.527 1.00 3.70  ? 3592 PRO A CG    1 
ATOM   15394 C  CD    . PRO A 1 3592 ? 209.789 186.062 241.726 1.00 3.69  ? 3592 PRO A CD    1 
ATOM   15395 N  N     . SER A 1 3593 ? 206.526 187.011 243.147 1.00 6.03  ? 3593 SER A N     1 
ATOM   15396 C  CA    . SER A 1 3593 ? 205.376 187.217 244.023 1.00 9.42  ? 3593 SER A CA    1 
ATOM   15397 C  C     . SER A 1 3593 ? 205.073 188.700 244.212 1.00 10.19 ? 3593 SER A C     1 
ATOM   15398 O  O     . SER A 1 3593 ? 203.903 189.093 244.283 1.00 13.39 ? 3593 SER A O     1 
ATOM   15399 C  CB    . SER A 1 3593 ? 205.620 186.541 245.367 1.00 10.86 ? 3593 SER A CB    1 
ATOM   15400 O  OG    . SER A 1 3593 ? 206.491 187.321 246.167 1.00 10.22 ? 3593 SER A OG    1 
ATOM   15401 N  N     . GLY A 1 3594 ? 206.106 189.533 244.314 1.00 11.32 ? 3594 GLY A N     1 
ATOM   15402 C  CA    . GLY A 1 3594 ? 205.931 190.967 244.389 1.00 6.74  ? 3594 GLY A CA    1 
ATOM   15403 C  C     . GLY A 1 3594 ? 206.088 191.596 245.758 1.00 8.89  ? 3594 GLY A C     1 
ATOM   15404 O  O     . GLY A 1 3594 ? 205.867 192.807 245.884 1.00 11.12 ? 3594 GLY A O     1 
ATOM   15405 N  N     . GLN A 1 3595 ? 206.459 190.831 246.791 1.00 12.82 ? 3595 GLN A N     1 
ATOM   15406 C  CA    . GLN A 1 3595 ? 206.684 191.449 248.096 1.00 8.79  ? 3595 GLN A CA    1 
ATOM   15407 C  C     . GLN A 1 3595 ? 207.931 192.322 248.108 1.00 6.60  ? 3595 GLN A C     1 
ATOM   15408 O  O     . GLN A 1 3595 ? 207.982 193.308 248.851 1.00 8.68  ? 3595 GLN A O     1 
ATOM   15409 C  CB    . GLN A 1 3595 ? 206.782 190.397 249.208 1.00 11.35 ? 3595 GLN A CB    1 
ATOM   15410 C  CG    . GLN A 1 3595 ? 205.468 189.735 249.590 1.00 11.12 ? 3595 GLN A CG    1 
ATOM   15411 C  CD    . GLN A 1 3595 ? 204.928 188.819 248.525 1.00 20.16 ? 3595 GLN A CD    1 
ATOM   15412 O  OE1   . GLN A 1 3595 ? 205.567 187.840 248.143 1.00 27.60 ? 3595 GLN A OE1   1 
ATOM   15413 N  NE2   . GLN A 1 3595 ? 203.762 189.163 247.999 1.00 21.28 ? 3595 GLN A NE2   1 
ATOM   15414 N  N     . ALA A 1 3596 ? 208.946 191.972 247.317 1.00 7.64  ? 3596 ALA A N     1 
ATOM   15415 C  CA    . ALA A 1 3596 ? 210.154 192.791 247.267 1.00 4.09  ? 3596 ALA A CA    1 
ATOM   15416 C  C     . ALA A 1 3596 ? 209.851 194.187 246.742 1.00 4.17  ? 3596 ALA A C     1 
ATOM   15417 O  O     . ALA A 1 3596 ? 210.387 195.179 247.250 1.00 5.03  ? 3596 ALA A O     1 
ATOM   15418 C  CB    . ALA A 1 3596 ? 211.216 192.114 246.405 1.00 2.17  ? 3596 ALA A CB    1 
ATOM   15419 N  N     . THR A 1 3597 ? 208.996 194.282 245.723 1.00 5.65  ? 3597 THR A N     1 
ATOM   15420 C  CA    . THR A 1 3597 ? 208.573 195.587 245.227 1.00 6.72  ? 3597 THR A CA    1 
ATOM   15421 C  C     . THR A 1 3597 ? 207.883 196.385 246.323 1.00 7.31  ? 3597 THR A C     1 
ATOM   15422 O  O     . THR A 1 3597 ? 208.161 197.574 246.503 1.00 10.67 ? 3597 THR A O     1 
ATOM   15423 C  CB    . THR A 1 3597 ? 207.646 195.415 244.024 1.00 10.94 ? 3597 THR A CB    1 
ATOM   15424 O  OG1   . THR A 1 3597 ? 208.338 194.721 242.980 1.00 15.51 ? 3597 THR A OG1   1 
ATOM   15425 C  CG2   . THR A 1 3597 ? 207.179 196.765 243.505 1.00 11.43 ? 3597 THR A CG2   1 
ATOM   15426 N  N     . GLU A 1 3598 ? 206.988 195.741 247.073 1.00 8.07  ? 3598 GLU A N     1 
ATOM   15427 C  CA    . GLU A 1 3598 ? 206.338 196.415 248.190 1.00 6.12  ? 3598 GLU A CA    1 
ATOM   15428 C  C     . GLU A 1 3598 ? 207.342 196.793 249.271 1.00 7.43  ? 3598 GLU A C     1 
ATOM   15429 O  O     . GLU A 1 3598 ? 207.309 197.911 249.795 1.00 10.30 ? 3598 GLU A O     1 
ATOM   15430 C  CB    . GLU A 1 3598 ? 205.231 195.525 248.761 1.00 7.69  ? 3598 GLU A CB    1 
ATOM   15431 C  CG    . GLU A 1 3598 ? 204.229 196.238 249.661 1.00 14.84 ? 3598 GLU A CG    1 
ATOM   15432 C  CD    . GLU A 1 3598 ? 203.875 197.638 249.187 1.00 25.95 ? 3598 GLU A CD    1 
ATOM   15433 O  OE1   . GLU A 1 3598 ? 203.641 197.831 247.975 1.00 21.35 ? 3598 GLU A OE1   1 
ATOM   15434 O  OE2   . GLU A 1 3598 ? 203.828 198.552 250.036 1.00 22.59 ? 3598 GLU A OE2   1 
ATOM   15435 N  N     . PHE A 1 3599 ? 208.269 195.885 249.588 1.00 7.27  ? 3599 PHE A N     1 
ATOM   15436 C  CA    . PHE A 1 3599 ? 209.260 196.153 250.628 1.00 4.25  ? 3599 PHE A CA    1 
ATOM   15437 C  C     . PHE A 1 3599 ? 210.124 197.356 250.276 1.00 5.18  ? 3599 PHE A C     1 
ATOM   15438 O  O     . PHE A 1 3599 ? 210.433 198.182 251.144 1.00 5.79  ? 3599 PHE A O     1 
ATOM   15439 C  CB    . PHE A 1 3599 ? 210.124 194.909 250.849 1.00 4.26  ? 3599 PHE A CB    1 
ATOM   15440 C  CG    . PHE A 1 3599 ? 211.366 195.162 251.652 1.00 4.30  ? 3599 PHE A CG    1 
ATOM   15441 C  CD1   . PHE A 1 3599 ? 211.301 195.304 253.027 1.00 4.12  ? 3599 PHE A CD1   1 
ATOM   15442 C  CD2   . PHE A 1 3599 ? 212.602 195.248 251.029 1.00 2.21  ? 3599 PHE A CD2   1 
ATOM   15443 C  CE1   . PHE A 1 3599 ? 212.447 195.534 253.766 1.00 4.70  ? 3599 PHE A CE1   1 
ATOM   15444 C  CE2   . PHE A 1 3599 ? 213.747 195.477 251.762 1.00 1.12  ? 3599 PHE A CE2   1 
ATOM   15445 C  CZ    . PHE A 1 3599 ? 213.671 195.619 253.130 1.00 2.26  ? 3599 PHE A CZ    1 
ATOM   15446 N  N     . ILE A 1 3600 ? 210.531 197.469 249.011 1.00 4.40  ? 3600 ILE A N     1 
ATOM   15447 C  CA    . ILE A 1 3600 ? 211.332 198.610 248.586 1.00 4.31  ? 3600 ILE A CA    1 
ATOM   15448 C  C     . ILE A 1 3600 ? 210.537 199.903 248.721 1.00 6.18  ? 3600 ILE A C     1 
ATOM   15449 O  O     . ILE A 1 3600 ? 211.073 200.936 249.137 1.00 7.71  ? 3600 ILE A O     1 
ATOM   15450 C  CB    . ILE A 1 3600 ? 211.840 198.392 247.147 1.00 5.52  ? 3600 ILE A CB    1 
ATOM   15451 C  CG1   . ILE A 1 3600 ? 212.914 197.306 247.133 1.00 4.45  ? 3600 ILE A CG1   1 
ATOM   15452 C  CG2   . ILE A 1 3600 ? 212.393 199.680 246.567 1.00 2.21  ? 3600 ILE A CG2   1 
ATOM   15453 C  CD1   . ILE A 1 3600 ? 214.093 197.605 248.030 1.00 2.37  ? 3600 ILE A CD1   1 
ATOM   15454 N  N     . MET A 1 3601 ? 209.249 199.873 248.367 1.00 7.60  ? 3601 MET A N     1 
ATOM   15455 C  CA    . MET A 1 3601 ? 208.424 201.070 248.499 1.00 5.84  ? 3601 MET A CA    1 
ATOM   15456 C  C     . MET A 1 3601 ? 208.122 201.399 249.957 1.00 7.28  ? 3601 MET A C     1 
ATOM   15457 O  O     . MET A 1 3601 ? 208.051 202.578 250.321 1.00 14.88 ? 3601 MET A O     1 
ATOM   15458 C  CB    . MET A 1 3601 ? 207.138 200.918 247.691 1.00 5.98  ? 3601 MET A CB    1 
ATOM   15459 C  CG    . MET A 1 3601 ? 207.381 200.548 246.242 1.00 7.84  ? 3601 MET A CG    1 
ATOM   15460 S  SD    . MET A 1 3601 ? 208.060 201.927 245.294 1.00 21.30 ? 3601 MET A SD    1 
ATOM   15461 C  CE    . MET A 1 3601 ? 206.685 203.071 245.316 1.00 7.04  ? 3601 MET A CE    1 
ATOM   15462 N  N     . ASN A 1 3602 ? 207.933 200.385 250.810 1.00 9.78  ? 3602 ASN A N     1 
ATOM   15463 C  CA    . ASN A 1 3602 ? 207.763 200.668 252.232 1.00 6.64  ? 3602 ASN A CA    1 
ATOM   15464 C  C     . ASN A 1 3602 ? 209.025 201.288 252.821 1.00 7.14  ? 3602 ASN A C     1 
ATOM   15465 O  O     . ASN A 1 3602 ? 208.949 202.221 253.626 1.00 9.89  ? 3602 ASN A O     1 
ATOM   15466 C  CB    . ASN A 1 3602 ? 207.396 199.404 253.014 1.00 7.54  ? 3602 ASN A CB    1 
ATOM   15467 C  CG    . ASN A 1 3602 ? 206.060 198.815 252.607 1.00 12.53 ? 3602 ASN A CG    1 
ATOM   15468 O  OD1   . ASN A 1 3602 ? 205.991 197.708 252.074 1.00 19.00 ? 3602 ASN A OD1   1 
ATOM   15469 N  ND2   . ASN A 1 3602 ? 204.990 199.546 252.866 1.00 12.34 ? 3602 ASN A ND2   1 
ATOM   15470 N  N     . GLU A 1 3603 ? 210.195 200.785 252.422 1.00 7.68  ? 3603 GLU A N     1 
ATOM   15471 C  CA    . GLU A 1 3603 ? 211.443 201.222 253.036 1.00 7.25  ? 3603 GLU A CA    1 
ATOM   15472 C  C     . GLU A 1 3603 ? 211.818 202.641 252.625 1.00 7.55  ? 3603 GLU A C     1 
ATOM   15473 O  O     . GLU A 1 3603 ? 212.648 203.273 253.289 1.00 6.66  ? 3603 GLU A O     1 
ATOM   15474 C  CB    . GLU A 1 3603 ? 212.572 200.260 252.666 1.00 5.28  ? 3603 GLU A CB    1 
ATOM   15475 C  CG    . GLU A 1 3603 ? 212.726 199.088 253.612 1.00 3.68  ? 3603 GLU A CG    1 
ATOM   15476 C  CD    . GLU A 1 3603 ? 213.175 199.502 254.997 1.00 12.75 ? 3603 GLU A CD    1 
ATOM   15477 O  OE1   . GLU A 1 3603 ? 214.176 200.239 255.108 1.00 11.51 ? 3603 GLU A OE1   1 
ATOM   15478 O  OE2   . GLU A 1 3603 ? 212.519 199.094 255.978 1.00 15.42 ? 3603 GLU A OE2   1 
ATOM   15479 N  N     . TYR A 1 3604 ? 211.228 203.161 251.548 1.00 9.16  ? 3604 TYR A N     1 
ATOM   15480 C  CA    . TYR A 1 3604 ? 211.663 204.433 250.986 1.00 6.54  ? 3604 TYR A CA    1 
ATOM   15481 C  C     . TYR A 1 3604 ? 210.534 205.451 250.831 1.00 10.80 ? 3604 TYR A C     1 
ATOM   15482 O  O     . TYR A 1 3604 ? 210.651 206.363 250.007 1.00 13.95 ? 3604 TYR A O     1 
ATOM   15483 C  CB    . TYR A 1 3604 ? 212.353 204.203 249.639 1.00 6.79  ? 3604 TYR A CB    1 
ATOM   15484 C  CG    . TYR A 1 3604 ? 213.737 203.598 249.744 1.00 7.51  ? 3604 TYR A CG    1 
ATOM   15485 C  CD1   . TYR A 1 3604 ? 213.912 202.223 249.832 1.00 6.48  ? 3604 TYR A CD1   1 
ATOM   15486 C  CD2   . TYR A 1 3604 ? 214.867 204.401 249.760 1.00 6.05  ? 3604 TYR A CD2   1 
ATOM   15487 C  CE1   . TYR A 1 3604 ? 215.174 201.667 249.928 1.00 4.60  ? 3604 TYR A CE1   1 
ATOM   15488 C  CE2   . TYR A 1 3604 ? 216.130 203.857 249.854 1.00 6.12  ? 3604 TYR A CE2   1 
ATOM   15489 C  CZ    . TYR A 1 3604 ? 216.279 202.490 249.938 1.00 5.23  ? 3604 TYR A CZ    1 
ATOM   15490 O  OH    . TYR A 1 3604 ? 217.539 201.949 250.035 1.00 8.84  ? 3604 TYR A OH    1 
ATOM   15491 N  N     . LYS A 1 3605 ? 209.444 205.331 251.599 1.00 14.46 ? 3605 LYS A N     1 
ATOM   15492 C  CA    . LYS A 1 3605 ? 208.441 206.394 251.574 1.00 11.31 ? 3605 LYS A CA    1 
ATOM   15493 C  C     . LYS A 1 3605 ? 208.998 207.705 252.111 1.00 14.07 ? 3605 LYS A C     1 
ATOM   15494 O  O     . LYS A 1 3605 ? 208.740 208.773 251.542 1.00 22.45 ? 3605 LYS A O     1 
ATOM   15495 C  CB    . LYS A 1 3605 ? 207.183 206.017 252.356 1.00 10.48 ? 3605 LYS A CB    1 
ATOM   15496 C  CG    . LYS A 1 3605 ? 206.350 204.886 251.803 1.00 15.58 ? 3605 LYS A CG    1 
ATOM   15497 C  CD    . LYS A 1 3605 ? 205.134 204.674 252.698 1.00 21.10 ? 3605 LYS A CD    1 
ATOM   15498 C  CE    . LYS A 1 3605 ? 204.199 203.615 252.153 1.00 20.67 ? 3605 LYS A CE    1 
ATOM   15499 N  NZ    . LYS A 1 3605 ? 204.821 202.277 252.174 1.00 17.24 ? 3605 LYS A NZ    1 
ATOM   15500 N  N     . ASP A 1 3606 ? 209.756 207.653 253.211 1.00 10.48 ? 3606 ASP A N     1 
ATOM   15501 C  CA    . ASP A 1 3606 ? 210.261 208.884 253.806 1.00 14.66 ? 3606 ASP A CA    1 
ATOM   15502 C  C     . ASP A 1 3606 ? 211.190 209.637 252.867 1.00 15.64 ? 3606 ASP A C     1 
ATOM   15503 O  O     . ASP A 1 3606 ? 211.350 210.853 253.014 1.00 22.34 ? 3606 ASP A O     1 
ATOM   15504 C  CB    . ASP A 1 3606 ? 210.981 208.588 255.126 1.00 21.52 ? 3606 ASP A CB    1 
ATOM   15505 C  CG    . ASP A 1 3606 ? 212.139 207.620 254.963 1.00 25.50 ? 3606 ASP A CG    1 
ATOM   15506 O  OD1   . ASP A 1 3606 ? 212.368 207.136 253.835 1.00 17.37 ? 3606 ASP A OD1   1 
ATOM   15507 O  OD2   . ASP A 1 3606 ? 212.828 207.349 255.968 1.00 28.83 ? 3606 ASP A OD2   1 
ATOM   15508 N  N     . ARG A 1 3607 ? 211.794 208.944 251.906 1.00 17.84 ? 3607 ARG A N     1 
ATOM   15509 C  CA    . ARG A 1 3607 ? 212.656 209.560 250.910 1.00 9.91  ? 3607 ARG A CA    1 
ATOM   15510 C  C     . ARG A 1 3607 ? 211.947 209.773 249.577 1.00 13.24 ? 3607 ARG A C     1 
ATOM   15511 O  O     . ARG A 1 3607 ? 212.600 210.126 248.591 1.00 17.11 ? 3607 ARG A O     1 
ATOM   15512 C  CB    . ARG A 1 3607 ? 213.915 208.715 250.719 1.00 10.32 ? 3607 ARG A CB    1 
ATOM   15513 C  CG    . ARG A 1 3607 ? 214.964 208.946 251.795 1.00 9.95  ? 3607 ARG A CG    1 
ATOM   15514 C  CD    . ARG A 1 3607 ? 216.065 207.904 251.756 1.00 15.08 ? 3607 ARG A CD    1 
ATOM   15515 N  NE    . ARG A 1 3607 ? 215.692 206.657 252.412 1.00 21.26 ? 3607 ARG A NE    1 
ATOM   15516 C  CZ    . ARG A 1 3607 ? 216.529 205.655 252.644 1.00 20.02 ? 3607 ARG A CZ    1 
ATOM   15517 N  NH1   . ARG A 1 3607 ? 217.805 205.726 252.301 1.00 18.42 ? 3607 ARG A NH1   1 
ATOM   15518 N  NH2   . ARG A 1 3607 ? 216.075 204.553 253.233 1.00 11.78 ? 3607 ARG A NH2   1 
ATOM   15519 N  N     . LYS A 1 3608 ? 210.629 209.566 249.532 1.00 13.34 ? 3608 LYS A N     1 
ATOM   15520 C  CA    . LYS A 1 3608 ? 209.799 209.860 248.363 1.00 10.22 ? 3608 LYS A CA    1 
ATOM   15521 C  C     . LYS A 1 3608 ? 210.264 209.077 247.132 1.00 8.73  ? 3608 LYS A C     1 
ATOM   15522 O  O     . LYS A 1 3608 ? 210.711 209.642 246.133 1.00 18.00 ? 3608 LYS A O     1 
ATOM   15523 C  CB    . LYS A 1 3608 ? 209.763 211.367 248.080 1.00 17.19 ? 3608 LYS A CB    1 
ATOM   15524 C  CG    . LYS A 1 3608 ? 209.116 212.190 249.182 1.00 19.56 ? 3608 LYS A CG    1 
ATOM   15525 C  CD    . LYS A 1 3608 ? 209.049 213.667 248.813 1.00 21.36 ? 3608 LYS A CD    1 
ATOM   15526 C  CE    . LYS A 1 3608 ? 210.428 214.308 248.819 1.00 29.20 ? 3608 LYS A CE    1 
ATOM   15527 N  NZ    . LYS A 1 3608 ? 211.014 214.349 250.186 1.00 29.45 ? 3608 LYS A NZ    1 
ATOM   15528 N  N     . ILE A 1 3609 ? 210.145 207.756 247.222 1.00 8.26  ? 3609 ILE A N     1 
ATOM   15529 C  CA    . ILE A 1 3609 ? 210.488 206.882 246.108 1.00 5.65  ? 3609 ILE A CA    1 
ATOM   15530 C  C     . ILE A 1 3609 ? 209.348 206.877 245.100 1.00 5.85  ? 3609 ILE A C     1 
ATOM   15531 O  O     . ILE A 1 3609 ? 208.168 206.924 245.467 1.00 7.80  ? 3609 ILE A O     1 
ATOM   15532 C  CB    . ILE A 1 3609 ? 210.806 205.460 246.611 1.00 5.33  ? 3609 ILE A CB    1 
ATOM   15533 C  CG1   . ILE A 1 3609 ? 211.244 204.562 245.451 1.00 3.57  ? 3609 ILE A CG1   1 
ATOM   15534 C  CG2   . ILE A 1 3609 ? 209.609 204.858 247.337 1.00 5.13  ? 3609 ILE A CG2   1 
ATOM   15535 C  CD1   . ILE A 1 3609 ? 211.836 203.248 245.886 1.00 4.20  ? 3609 ILE A CD1   1 
ATOM   15536 N  N     . THR A 1 3610 ? 209.699 206.832 243.820 1.00 7.68  ? 3610 THR A N     1 
ATOM   15537 C  CA    . THR A 1 3610 ? 208.736 206.821 242.728 1.00 5.15  ? 3610 THR A CA    1 
ATOM   15538 C  C     . THR A 1 3610 ? 208.826 205.494 241.988 1.00 5.54  ? 3610 THR A C     1 
ATOM   15539 O  O     . THR A 1 3610 ? 209.923 205.046 241.639 1.00 9.14  ? 3610 THR A O     1 
ATOM   15540 C  CB    . THR A 1 3610 ? 208.990 207.981 241.762 1.00 4.31  ? 3610 THR A CB    1 
ATOM   15541 O  OG1   . THR A 1 3610 ? 208.869 209.225 242.463 1.00 7.50  ? 3610 THR A OG1   1 
ATOM   15542 C  CG2   . THR A 1 3610 ? 207.998 207.956 240.613 1.00 7.59  ? 3610 THR A CG2   1 
ATOM   15543 N  N     . ARG A 1 3611 ? 207.676 204.865 241.761 1.00 5.12  ? 3611 ARG A N     1 
ATOM   15544 C  CA    . ARG A 1 3611 ? 207.605 203.660 240.949 1.00 3.91  ? 3611 ARG A CA    1 
ATOM   15545 C  C     . ARG A 1 3611 ? 207.393 204.049 239.493 1.00 5.36  ? 3611 ARG A C     1 
ATOM   15546 O  O     . ARG A 1 3611 ? 206.543 204.892 239.186 1.00 15.64 ? 3611 ARG A O     1 
ATOM   15547 C  CB    . ARG A 1 3611 ? 206.471 202.744 241.411 1.00 4.69  ? 3611 ARG A CB    1 
ATOM   15548 C  CG    . ARG A 1 3611 ? 206.430 201.420 240.663 1.00 7.98  ? 3611 ARG A CG    1 
ATOM   15549 C  CD    . ARG A 1 3611 ? 205.293 200.515 241.110 1.00 14.10 ? 3611 ARG A CD    1 
ATOM   15550 N  NE    . ARG A 1 3611 ? 205.393 200.070 242.494 1.00 20.32 ? 3611 ARG A NE    1 
ATOM   15551 C  CZ    . ARG A 1 3611 ? 204.550 200.427 243.452 1.00 20.45 ? 3611 ARG A CZ    1 
ATOM   15552 N  NH1   . ARG A 1 3611 ? 203.558 201.269 243.220 1.00 23.34 ? 3611 ARG A NH1   1 
ATOM   15553 N  NH2   . ARG A 1 3611 ? 204.703 199.923 244.671 1.00 18.50 ? 3611 ARG A NH2   1 
ATOM   15554 N  N     . THR A 1 3612 ? 208.162 203.439 238.599 1.00 3.27  ? 3612 THR A N     1 
ATOM   15555 C  CA    . THR A 1 3612 ? 207.997 203.639 237.169 1.00 5.51  ? 3612 THR A CA    1 
ATOM   15556 C  C     . THR A 1 3612 ? 208.402 202.356 236.455 1.00 2.89  ? 3612 THR A C     1 
ATOM   15557 O  O     . THR A 1 3612 ? 208.742 201.353 237.086 1.00 3.10  ? 3612 THR A O     1 
ATOM   15558 C  CB    . THR A 1 3612 ? 208.807 204.847 236.673 1.00 7.11  ? 3612 THR A CB    1 
ATOM   15559 O  OG1   . THR A 1 3612 ? 208.499 205.100 235.296 1.00 9.32  ? 3612 THR A OG1   1 
ATOM   15560 C  CG2   . THR A 1 3612 ? 210.294 204.596 236.818 1.00 3.12  ? 3612 THR A CG2   1 
ATOM   15561 N  N     . SER A 1 3613 ? 208.358 202.391 235.129 1.00 3.14  ? 3613 SER A N     1 
ATOM   15562 C  CA    . SER A 1 3613 ? 208.679 201.226 234.321 1.00 3.47  ? 3613 SER A CA    1 
ATOM   15563 C  C     . SER A 1 3613 ? 209.430 201.666 233.075 1.00 4.65  ? 3613 SER A C     1 
ATOM   15564 O  O     . SER A 1 3613 ? 209.293 202.805 232.619 1.00 6.49  ? 3613 SER A O     1 
ATOM   15565 C  CB    . SER A 1 3613 ? 207.415 200.451 233.928 1.00 3.23  ? 3613 SER A CB    1 
ATOM   15566 O  OG    . SER A 1 3613 ? 207.666 199.581 232.841 1.00 6.20  ? 3613 SER A OG    1 
ATOM   15567 N  N     . PHE A 1 3614 ? 210.225 200.747 232.525 1.00 4.31  ? 3614 PHE A N     1 
ATOM   15568 C  CA    . PHE A 1 3614 ? 210.924 201.019 231.275 1.00 3.81  ? 3614 PHE A CA    1 
ATOM   15569 C  C     . PHE A 1 3614 ? 209.959 201.240 230.120 1.00 6.38  ? 3614 PHE A C     1 
ATOM   15570 O  O     . PHE A 1 3614 ? 210.334 201.866 229.123 1.00 11.38 ? 3614 PHE A O     1 
ATOM   15571 C  CB    . PHE A 1 3614 ? 211.873 199.872 230.933 1.00 3.77  ? 3614 PHE A CB    1 
ATOM   15572 C  CG    . PHE A 1 3614 ? 213.111 199.829 231.776 1.00 3.72  ? 3614 PHE A CG    1 
ATOM   15573 C  CD1   . PHE A 1 3614 ? 214.127 200.749 231.581 1.00 3.73  ? 3614 PHE A CD1   1 
ATOM   15574 C  CD2   . PHE A 1 3614 ? 213.273 198.852 232.744 1.00 2.08  ? 3614 PHE A CD2   1 
ATOM   15575 C  CE1   . PHE A 1 3614 ? 215.271 200.709 232.350 1.00 2.67  ? 3614 PHE A CE1   1 
ATOM   15576 C  CE2   . PHE A 1 3614 ? 214.419 198.805 233.515 1.00 1.98  ? 3614 PHE A CE2   1 
ATOM   15577 C  CZ    . PHE A 1 3614 ? 215.418 199.737 233.319 1.00 2.11  ? 3614 PHE A CZ    1 
ATOM   15578 N  N     . LEU A 1 3615 ? 208.733 200.732 230.229 1.00 8.68  ? 3615 LEU A N     1 
ATOM   15579 C  CA    . LEU A 1 3615 ? 207.737 200.853 229.176 1.00 8.26  ? 3615 LEU A CA    1 
ATOM   15580 C  C     . LEU A 1 3615 ? 206.888 202.110 229.298 1.00 9.07  ? 3615 LEU A C     1 
ATOM   15581 O  O     . LEU A 1 3615 ? 206.212 202.475 228.331 1.00 14.47 ? 3615 LEU A O     1 
ATOM   15582 C  CB    . LEU A 1 3615 ? 206.831 199.619 229.185 1.00 6.87  ? 3615 LEU A CB    1 
ATOM   15583 C  CG    . LEU A 1 3615 ? 207.584 198.293 229.066 1.00 9.46  ? 3615 LEU A CG    1 
ATOM   15584 C  CD1   . LEU A 1 3615 ? 206.702 197.131 229.475 1.00 6.64  ? 3615 LEU A CD1   1 
ATOM   15585 C  CD2   . LEU A 1 3615 ? 208.122 198.096 227.659 1.00 8.03  ? 3615 LEU A CD2   1 
ATOM   15586 N  N     . ASP A 1 3616 ? 206.902 202.772 230.450 1.00 7.58  ? 3616 ASP A N     1 
ATOM   15587 C  CA    . ASP A 1 3616 ? 206.121 203.986 230.628 1.00 8.73  ? 3616 ASP A CA    1 
ATOM   15588 C  C     . ASP A 1 3616 ? 206.686 205.118 229.777 1.00 16.33 ? 3616 ASP A C     1 
ATOM   15589 O  O     . ASP A 1 3616 ? 207.883 205.164 229.477 1.00 17.42 ? 3616 ASP A O     1 
ATOM   15590 C  CB    . ASP A 1 3616 ? 206.099 204.397 232.100 1.00 9.89  ? 3616 ASP A CB    1 
ATOM   15591 C  CG    . ASP A 1 3616 ? 205.264 203.466 232.955 1.00 17.71 ? 3616 ASP A CG    1 
ATOM   15592 O  OD1   . ASP A 1 3616 ? 204.867 202.391 232.454 1.00 21.75 ? 3616 ASP A OD1   1 
ATOM   15593 O  OD2   . ASP A 1 3616 ? 205.004 203.804 234.129 1.00 21.50 ? 3616 ASP A OD2   1 
ATOM   15594 N  N     . ASP A 1 3617 ? 205.803 206.032 229.371 1.00 19.37 ? 3617 ASP A N     1 
ATOM   15595 C  CA    . ASP A 1 3617 ? 206.234 207.169 228.568 1.00 16.10 ? 3617 ASP A CA    1 
ATOM   15596 C  C     . ASP A 1 3617 ? 206.997 208.199 229.386 1.00 13.80 ? 3617 ASP A C     1 
ATOM   15597 O  O     . ASP A 1 3617 ? 207.792 208.956 228.821 1.00 15.45 ? 3617 ASP A O     1 
ATOM   15598 C  CB    . ASP A 1 3617 ? 205.030 207.829 227.897 1.00 19.03 ? 3617 ASP A CB    1 
ATOM   15599 C  CG    . ASP A 1 3617 ? 205.433 208.882 226.882 1.00 30.97 ? 3617 ASP A CG    1 
ATOM   15600 O  OD1   . ASP A 1 3617 ? 205.743 208.513 225.730 1.00 35.45 ? 3617 ASP A OD1   1 
ATOM   15601 O  OD2   . ASP A 1 3617 ? 205.443 210.079 227.239 1.00 29.90 ? 3617 ASP A OD2   1 
ATOM   15602 N  N     . ALA A 1 3618 ? 206.783 208.239 230.698 1.00 18.20 ? 3618 ALA A N     1 
ATOM   15603 C  CA    . ALA A 1 3618 ? 207.411 209.224 231.567 1.00 15.18 ? 3618 ALA A CA    1 
ATOM   15604 C  C     . ALA A 1 3618 ? 208.704 208.723 232.190 1.00 15.11 ? 3618 ALA A C     1 
ATOM   15605 O  O     . ALA A 1 3618 ? 209.252 209.392 233.070 1.00 19.03 ? 3618 ALA A O     1 
ATOM   15606 C  CB    . ALA A 1 3618 ? 206.435 209.654 232.662 1.00 11.50 ? 3618 ALA A CB    1 
ATOM   15607 N  N     . PHE A 1 3619 ? 209.206 207.562 231.756 1.00 13.07 ? 3619 PHE A N     1 
ATOM   15608 C  CA    . PHE A 1 3619 ? 210.376 206.976 232.398 1.00 8.08  ? 3619 PHE A CA    1 
ATOM   15609 C  C     . PHE A 1 3619 ? 211.593 207.885 232.285 1.00 8.27  ? 3619 PHE A C     1 
ATOM   15610 O  O     . PHE A 1 3619 ? 212.336 208.058 233.258 1.00 11.84 ? 3619 PHE A O     1 
ATOM   15611 C  CB    . PHE A 1 3619 ? 210.684 205.605 231.795 1.00 8.08  ? 3619 PHE A CB    1 
ATOM   15612 C  CG    . PHE A 1 3619 ? 212.070 205.117 232.094 1.00 7.86  ? 3619 PHE A CG    1 
ATOM   15613 C  CD1   . PHE A 1 3619 ? 212.402 204.681 233.368 1.00 5.54  ? 3619 PHE A CD1   1 
ATOM   15614 C  CD2   . PHE A 1 3619 ? 213.043 205.105 231.112 1.00 5.18  ? 3619 PHE A CD2   1 
ATOM   15615 C  CE1   . PHE A 1 3619 ? 213.679 204.238 233.652 1.00 3.71  ? 3619 PHE A CE1   1 
ATOM   15616 C  CE2   . PHE A 1 3619 ? 214.321 204.663 231.393 1.00 7.24  ? 3619 PHE A CE2   1 
ATOM   15617 C  CZ    . PHE A 1 3619 ? 214.638 204.230 232.664 1.00 7.06  ? 3619 PHE A CZ    1 
ATOM   15618 N  N     . ARG A 1 3620 ? 211.820 208.469 231.106 1.00 7.68  ? 3620 ARG A N     1 
ATOM   15619 C  CA    . ARG A 1 3620 ? 212.960 209.365 230.939 1.00 7.02  ? 3620 ARG A CA    1 
ATOM   15620 C  C     . ARG A 1 3620 ? 212.821 210.598 231.822 1.00 8.06  ? 3620 ARG A C     1 
ATOM   15621 O  O     . ARG A 1 3620 ? 213.796 211.036 232.446 1.00 9.55  ? 3620 ARG A O     1 
ATOM   15622 C  CB    . ARG A 1 3620 ? 213.104 209.768 229.472 1.00 12.58 ? 3620 ARG A CB    1 
ATOM   15623 C  CG    . ARG A 1 3620 ? 213.474 208.623 228.550 1.00 14.27 ? 3620 ARG A CG    1 
ATOM   15624 C  CD    . ARG A 1 3620 ? 213.548 209.089 227.110 1.00 22.69 ? 3620 ARG A CD    1 
ATOM   15625 N  NE    . ARG A 1 3620 ? 214.622 210.053 226.917 1.00 30.30 ? 3620 ARG A NE    1 
ATOM   15626 C  CZ    . ARG A 1 3620 ? 215.876 209.728 226.632 1.00 25.05 ? 3620 ARG A CZ    1 
ATOM   15627 N  NH1   . ARG A 1 3620 ? 216.240 208.470 226.459 1.00 16.10 ? 3620 ARG A NH1   1 
ATOM   15628 N  NH2   . ARG A 1 3620 ? 216.784 210.691 226.509 1.00 21.82 ? 3620 ARG A NH2   1 
ATOM   15629 N  N     . LYS A 1 3621 ? 211.618 211.175 231.886 1.00 9.42  ? 3621 LYS A N     1 
ATOM   15630 C  CA    . LYS A 1 3621 ? 211.385 212.305 232.779 1.00 6.78  ? 3621 LYS A CA    1 
ATOM   15631 C  C     . LYS A 1 3621 ? 211.545 211.902 234.239 1.00 7.98  ? 3621 LYS A C     1 
ATOM   15632 O  O     . LYS A 1 3621 ? 212.150 212.637 235.027 1.00 11.77 ? 3621 LYS A O     1 
ATOM   15633 C  CB    . LYS A 1 3621 ? 209.992 212.884 232.537 1.00 10.94 ? 3621 LYS A CB    1 
ATOM   15634 C  CG    . LYS A 1 3621 ? 209.679 214.105 233.386 1.00 12.90 ? 3621 LYS A CG    1 
ATOM   15635 C  CD    . LYS A 1 3621 ? 208.329 214.704 233.026 1.00 24.77 ? 3621 LYS A CD    1 
ATOM   15636 C  CE    . LYS A 1 3621 ? 207.955 215.829 233.973 1.00 27.02 ? 3621 LYS A CE    1 
ATOM   15637 N  NZ    . LYS A 1 3621 ? 208.875 216.991 233.839 1.00 26.65 ? 3621 LYS A NZ    1 
ATOM   15638 N  N     . ASN A 1 3622 ? 211.002 210.742 234.617 1.00 6.52  ? 3622 ASN A N     1 
ATOM   15639 C  CA    . ASN A 1 3622 ? 211.130 210.278 235.995 1.00 6.96  ? 3622 ASN A CA    1 
ATOM   15640 C  C     . ASN A 1 3622 ? 212.586 210.007 236.351 1.00 4.90  ? 3622 ASN A C     1 
ATOM   15641 O  O     . ASN A 1 3622 ? 213.047 210.373 237.438 1.00 4.63  ? 3622 ASN A O     1 
ATOM   15642 C  CB    . ASN A 1 3622 ? 210.282 209.025 236.202 1.00 8.19  ? 3622 ASN A CB    1 
ATOM   15643 C  CG    . ASN A 1 3622 ? 208.797 209.306 236.101 1.00 12.36 ? 3622 ASN A CG    1 
ATOM   15644 O  OD1   . ASN A 1 3622 ? 208.370 210.458 236.124 1.00 15.64 ? 3622 ASN A OD1   1 
ATOM   15645 N  ND2   . ASN A 1 3622 ? 208.003 208.253 235.968 1.00 11.48 ? 3622 ASN A ND2   1 
ATOM   15646 N  N     . LEU A 1 3623 ? 213.325 209.369 235.441 1.00 4.07  ? 3623 LEU A N     1 
ATOM   15647 C  CA    . LEU A 1 3623 ? 214.742 209.109 235.678 1.00 2.71  ? 3623 LEU A CA    1 
ATOM   15648 C  C     . LEU A 1 3623 ? 215.530 210.406 235.805 1.00 4.78  ? 3623 LEU A C     1 
ATOM   15649 O  O     . LEU A 1 3623 ? 216.392 210.533 236.681 1.00 4.20  ? 3623 LEU A O     1 
ATOM   15650 C  CB    . LEU A 1 3623 ? 215.304 208.250 234.552 1.00 2.66  ? 3623 LEU A CB    1 
ATOM   15651 C  CG    . LEU A 1 3623 ? 216.821 208.060 234.554 1.00 3.49  ? 3623 LEU A CG    1 
ATOM   15652 C  CD1   . LEU A 1 3623 ? 217.288 207.326 235.808 1.00 3.34  ? 3623 LEU A CD1   1 
ATOM   15653 C  CD2   . LEU A 1 3623 ? 217.256 207.351 233.291 1.00 0.63  ? 3623 LEU A CD2   1 
ATOM   15654 N  N     . GLU A 1 3624 ? 215.250 211.379 234.934 1.00 7.05  ? 3624 GLU A N     1 
ATOM   15655 C  CA    . GLU A 1 3624 ? 215.930 212.667 235.017 1.00 6.87  ? 3624 GLU A CA    1 
ATOM   15656 C  C     . GLU A 1 3624 ? 215.617 213.373 236.330 1.00 5.91  ? 3624 GLU A C     1 
ATOM   15657 O  O     . GLU A 1 3624 ? 216.506 213.966 236.952 1.00 8.12  ? 3624 GLU A O     1 
ATOM   15658 C  CB    . GLU A 1 3624 ? 215.532 213.541 233.828 1.00 9.27  ? 3624 GLU A CB    1 
ATOM   15659 C  CG    . GLU A 1 3624 ? 216.202 214.900 233.801 1.00 14.99 ? 3624 GLU A CG    1 
ATOM   15660 C  CD    . GLU A 1 3624 ? 215.596 215.823 232.763 1.00 23.86 ? 3624 GLU A CD    1 
ATOM   15661 O  OE1   . GLU A 1 3624 ? 215.930 215.676 231.568 1.00 25.18 ? 3624 GLU A OE1   1 
ATOM   15662 O  OE2   . GLU A 1 3624 ? 214.785 216.693 233.142 1.00 18.92 ? 3624 GLU A OE2   1 
ATOM   15663 N  N     . SER A 1 3625 ? 214.356 213.324 236.763 1.00 7.18  ? 3625 SER A N     1 
ATOM   15664 C  CA    . SER A 1 3625 ? 213.971 213.965 238.016 1.00 5.72  ? 3625 SER A CA    1 
ATOM   15665 C  C     . SER A 1 3625 ? 214.636 213.296 239.213 1.00 6.05  ? 3625 SER A C     1 
ATOM   15666 O  O     . SER A 1 3625 ? 215.115 213.977 240.125 1.00 6.84  ? 3625 SER A O     1 
ATOM   15667 C  CB    . SER A 1 3625 ? 212.451 213.945 238.162 1.00 6.08  ? 3625 SER A CB    1 
ATOM   15668 O  OG    . SER A 1 3625 ? 212.047 214.529 239.385 1.00 14.65 ? 3625 SER A OG    1 
ATOM   15669 N  N     . ALA A 1 3626 ? 214.670 211.960 239.229 1.00 4.92  ? 3626 ALA A N     1 
ATOM   15670 C  CA    . ALA A 1 3626 ? 215.290 211.252 240.343 1.00 2.82  ? 3626 ALA A CA    1 
ATOM   15671 C  C     . ALA A 1 3626 ? 216.784 211.535 240.418 1.00 4.25  ? 3626 ALA A C     1 
ATOM   15672 O  O     . ALA A 1 3626 ? 217.335 211.718 241.509 1.00 3.55  ? 3626 ALA A O     1 
ATOM   15673 C  CB    . ALA A 1 3626 ? 215.030 209.751 240.217 1.00 1.82  ? 3626 ALA A CB    1 
ATOM   15674 N  N     . LEU A 1 3627 ? 217.459 211.568 239.266 1.00 3.24  ? 3627 LEU A N     1 
ATOM   15675 C  CA    . LEU A 1 3627 ? 218.884 211.882 239.249 1.00 1.91  ? 3627 LEU A CA    1 
ATOM   15676 C  C     . LEU A 1 3627 ? 219.141 213.314 239.706 1.00 5.45  ? 3627 LEU A C     1 
ATOM   15677 O  O     . LEU A 1 3627 ? 220.100 213.575 240.439 1.00 4.35  ? 3627 LEU A O     1 
ATOM   15678 C  CB    . LEU A 1 3627 ? 219.452 211.662 237.848 1.00 2.40  ? 3627 LEU A CB    1 
ATOM   15679 C  CG    . LEU A 1 3627 ? 219.547 210.227 237.328 1.00 1.79  ? 3627 LEU A CG    1 
ATOM   15680 C  CD1   . LEU A 1 3627 ? 219.599 210.231 235.807 1.00 2.81  ? 3627 LEU A CD1   1 
ATOM   15681 C  CD2   . LEU A 1 3627 ? 220.752 209.515 237.905 1.00 0.36  ? 3627 LEU A CD2   1 
ATOM   15682 N  N     . ARG A 1 3628 ? 218.291 214.252 239.282 1.00 4.92  ? 3628 ARG A N     1 
ATOM   15683 C  CA    . ARG A 1 3628 ? 218.522 215.660 239.588 1.00 4.58  ? 3628 ARG A CA    1 
ATOM   15684 C  C     . ARG A 1 3628 ? 218.260 215.964 241.057 1.00 4.36  ? 3628 ARG A C     1 
ATOM   15685 O  O     . ARG A 1 3628 ? 219.046 216.662 241.708 1.00 10.19 ? 3628 ARG A O     1 
ATOM   15686 C  CB    . ARG A 1 3628 ? 217.650 216.536 238.686 1.00 7.00  ? 3628 ARG A CB    1 
ATOM   15687 C  CG    . ARG A 1 3628 ? 217.736 218.021 238.982 1.00 6.56  ? 3628 ARG A CG    1 
ATOM   15688 C  CD    . ARG A 1 3628 ? 216.925 218.837 237.990 1.00 7.93  ? 3628 ARG A CD    1 
ATOM   15689 N  NE    . ARG A 1 3628 ? 217.598 218.928 236.701 1.00 15.20 ? 3628 ARG A NE    1 
ATOM   15690 C  CZ    . ARG A 1 3628 ? 217.173 218.344 235.590 1.00 9.34  ? 3628 ARG A CZ    1 
ATOM   15691 N  NH1   . ARG A 1 3628 ? 216.045 217.655 235.560 1.00 10.62 ? 3628 ARG A NH1   1 
ATOM   15692 N  NH2   . ARG A 1 3628 ? 217.896 218.455 234.479 1.00 10.21 ? 3628 ARG A NH2   1 
ATOM   15693 N  N     . PHE A 1 3629 ? 217.162 215.450 241.602 1.00 4.86  ? 3629 PHE A N     1 
ATOM   15694 C  CA    . PHE A 1 3629 ? 216.778 215.736 242.978 1.00 4.81  ? 3629 PHE A CA    1 
ATOM   15695 C  C     . PHE A 1 3629 ? 217.295 214.708 243.973 1.00 6.26  ? 3629 PHE A C     1 
ATOM   15696 O  O     . PHE A 1 3629 ? 217.123 214.898 245.181 1.00 10.45 ? 3629 PHE A O     1 
ATOM   15697 C  CB    . PHE A 1 3629 ? 215.254 215.840 243.085 1.00 5.62  ? 3629 PHE A CB    1 
ATOM   15698 C  CG    . PHE A 1 3629 ? 214.655 216.843 242.149 1.00 8.04  ? 3629 PHE A CG    1 
ATOM   15699 C  CD1   . PHE A 1 3629 ? 215.192 218.117 242.047 1.00 9.53  ? 3629 PHE A CD1   1 
ATOM   15700 C  CD2   . PHE A 1 3629 ? 213.569 216.513 241.360 1.00 5.85  ? 3629 PHE A CD2   1 
ATOM   15701 C  CE1   . PHE A 1 3629 ? 214.649 219.044 241.179 1.00 10.82 ? 3629 PHE A CE1   1 
ATOM   15702 C  CE2   . PHE A 1 3629 ? 213.023 217.438 240.491 1.00 12.50 ? 3629 PHE A CE2   1 
ATOM   15703 C  CZ    . PHE A 1 3629 ? 213.564 218.705 240.401 1.00 8.70  ? 3629 PHE A CZ    1 
ATOM   15704 N  N     . GLY A 1 3630 ? 217.929 213.638 243.506 1.00 5.80  ? 3630 GLY A N     1 
ATOM   15705 C  CA    . GLY A 1 3630 ? 218.421 212.603 244.396 1.00 5.29  ? 3630 GLY A CA    1 
ATOM   15706 C  C     . GLY A 1 3630 ? 217.343 211.814 245.104 1.00 6.50  ? 3630 GLY A C     1 
ATOM   15707 O  O     . GLY A 1 3630 ? 217.473 211.532 246.301 1.00 8.41  ? 3630 GLY A O     1 
ATOM   15708 N  N     . ASN A 1 3631 ? 216.292 211.456 244.405 1.00 4.32  ? 3631 ASN A N     1 
ATOM   15709 C  CA    . ASN A 1 3631 ? 215.260 210.646 245.021 1.00 4.82  ? 3631 ASN A CA    1 
ATOM   15710 C  C     . ASN A 1 3631 ? 215.396 209.189 244.596 1.00 4.45  ? 3631 ASN A C     1 
ATOM   15711 O  O     . ASN A 1 3631 ? 215.836 208.900 243.480 1.00 3.21  ? 3631 ASN A O     1 
ATOM   15712 C  CB    . ASN A 1 3631 ? 213.867 211.156 244.641 1.00 7.21  ? 3631 ASN A CB    1 
ATOM   15713 C  CG    . ASN A 1 3631 ? 213.686 212.630 244.936 1.00 8.46  ? 3631 ASN A CG    1 
ATOM   15714 O  OD1   . ASN A 1 3631 ? 213.293 213.404 244.065 1.00 9.83  ? 3631 ASN A OD1   1 
ATOM   15715 N  ND2   . ASN A 1 3631 ? 213.973 213.029 246.169 1.00 9.10  ? 3631 ASN A ND2   1 
ATOM   15716 N  N     . PRO A 1 3632 ? 215.044 208.251 245.473 1.00 6.10  ? 3632 PRO A N     1 
ATOM   15717 C  CA    . PRO A 1 3632 ? 215.040 206.840 245.076 1.00 2.57  ? 3632 PRO A CA    1 
ATOM   15718 C  C     . PRO A 1 3632 ? 214.030 206.581 243.970 1.00 2.11  ? 3632 PRO A C     1 
ATOM   15719 O  O     . PRO A 1 3632 ? 212.934 207.144 243.957 1.00 6.47  ? 3632 PRO A O     1 
ATOM   15720 C  CB    . PRO A 1 3632 ? 214.667 206.106 246.369 1.00 3.12  ? 3632 PRO A CB    1 
ATOM   15721 C  CG    . PRO A 1 3632 ? 214.040 207.138 247.236 1.00 3.81  ? 3632 PRO A CG    1 
ATOM   15722 C  CD    . PRO A 1 3632 ? 214.698 208.429 246.890 1.00 5.45  ? 3632 PRO A CD    1 
ATOM   15723 N  N     . LEU A 1 3633 ? 214.411 205.714 243.035 1.00 1.12  ? 3633 LEU A N     1 
ATOM   15724 C  CA    . LEU A 1 3633 ? 213.568 205.361 241.903 1.00 1.14  ? 3633 LEU A CA    1 
ATOM   15725 C  C     . LEU A 1 3633 ? 213.504 203.847 241.783 1.00 0.97  ? 3633 LEU A C     1 
ATOM   15726 O  O     . LEU A 1 3633 ? 214.539 203.176 241.814 1.00 1.24  ? 3633 LEU A O     1 
ATOM   15727 C  CB    . LEU A 1 3633 ? 214.096 205.979 240.605 1.00 1.55  ? 3633 LEU A CB    1 
ATOM   15728 C  CG    . LEU A 1 3633 ? 213.222 205.829 239.357 1.00 1.37  ? 3633 LEU A CG    1 
ATOM   15729 C  CD1   . LEU A 1 3633 ? 211.909 206.572 239.521 1.00 2.39  ? 3633 LEU A CD1   1 
ATOM   15730 C  CD2   . LEU A 1 3633 ? 213.964 206.313 238.127 1.00 1.24  ? 3633 LEU A CD2   1 
ATOM   15731 N  N     . LEU A 1 3634 ? 212.294 203.316 241.651 1.00 1.16  ? 3634 LEU A N     1 
ATOM   15732 C  CA    . LEU A 1 3634 ? 212.074 201.896 241.409 1.00 0.93  ? 3634 LEU A CA    1 
ATOM   15733 C  C     . LEU A 1 3634 ? 211.530 201.733 239.996 1.00 1.53  ? 3634 LEU A C     1 
ATOM   15734 O  O     . LEU A 1 3634 ? 210.461 202.263 239.674 1.00 3.05  ? 3634 LEU A O     1 
ATOM   15735 C  CB    . LEU A 1 3634 ? 211.106 201.304 242.432 1.00 1.41  ? 3634 LEU A CB    1 
ATOM   15736 C  CG    . LEU A 1 3634 ? 210.620 199.883 242.142 1.00 2.16  ? 3634 LEU A CG    1 
ATOM   15737 C  CD1   . LEU A 1 3634 ? 211.784 198.903 242.104 1.00 0.70  ? 3634 LEU A CD1   1 
ATOM   15738 C  CD2   . LEU A 1 3634 ? 209.584 199.452 243.159 1.00 4.36  ? 3634 LEU A CD2   1 
ATOM   15739 N  N     . VAL A 1 3635 ? 212.261 201.004 239.160 1.00 0.77  ? 3635 VAL A N     1 
ATOM   15740 C  CA    . VAL A 1 3635 ? 211.904 200.836 237.757 1.00 1.37  ? 3635 VAL A CA    1 
ATOM   15741 C  C     . VAL A 1 3635 ? 211.590 199.363 237.532 1.00 1.07  ? 3635 VAL A C     1 
ATOM   15742 O  O     . VAL A 1 3635 ? 212.436 198.495 237.782 1.00 1.17  ? 3635 VAL A O     1 
ATOM   15743 C  CB    . VAL A 1 3635 ? 213.030 201.311 236.827 1.00 2.11  ? 3635 VAL A CB    1 
ATOM   15744 C  CG1   . VAL A 1 3635 ? 212.654 201.069 235.381 1.00 1.57  ? 3635 VAL A CG1   1 
ATOM   15745 C  CG2   . VAL A 1 3635 ? 213.362 202.769 237.079 1.00 1.49  ? 3635 VAL A CG2   1 
ATOM   15746 N  N     . GLN A 1 3636 ? 210.385 199.082 237.056 1.00 1.52  ? 3636 GLN A N     1 
ATOM   15747 C  CA    . GLN A 1 3636 ? 209.932 197.720 236.824 1.00 2.01  ? 3636 GLN A CA    1 
ATOM   15748 C  C     . GLN A 1 3636 ? 210.114 197.332 235.361 1.00 2.53  ? 3636 GLN A C     1 
ATOM   15749 O  O     . GLN A 1 3636 ? 210.475 198.150 234.511 1.00 5.37  ? 3636 GLN A O     1 
ATOM   15750 C  CB    . GLN A 1 3636 ? 208.467 197.560 237.242 1.00 3.76  ? 3636 GLN A CB    1 
ATOM   15751 C  CG    . GLN A 1 3636 ? 208.199 197.908 238.695 1.00 6.47  ? 3636 GLN A CG    1 
ATOM   15752 C  CD    . GLN A 1 3636 ? 206.757 197.672 239.097 1.00 13.12 ? 3636 GLN A CD    1 
ATOM   15753 O  OE1   . GLN A 1 3636 ? 206.476 196.914 240.025 1.00 16.82 ? 3636 GLN A OE1   1 
ATOM   15754 N  NE2   . GLN A 1 3636 ? 205.833 198.316 238.396 1.00 15.98 ? 3636 GLN A NE2   1 
ATOM   15755 N  N     . ASP A 1 3637 ? 209.861 196.051 235.083 1.00 3.11  ? 3637 ASP A N     1 
ATOM   15756 C  CA    . ASP A 1 3637 ? 209.941 195.489 233.734 1.00 5.61  ? 3637 ASP A CA    1 
ATOM   15757 C  C     . ASP A 1 3637 ? 211.348 195.639 233.153 1.00 5.52  ? 3637 ASP A C     1 
ATOM   15758 O  O     . ASP A 1 3637 ? 211.541 196.139 232.044 1.00 9.80  ? 3637 ASP A O     1 
ATOM   15759 C  CB    . ASP A 1 3637 ? 208.891 196.119 232.813 1.00 5.78  ? 3637 ASP A CB    1 
ATOM   15760 C  CG    . ASP A 1 3637 ? 207.498 196.100 233.420 1.00 8.82  ? 3637 ASP A CG    1 
ATOM   15761 O  OD1   . ASP A 1 3637 ? 206.985 195.001 233.710 1.00 12.68 ? 3637 ASP A OD1   1 
ATOM   15762 O  OD2   . ASP A 1 3637 ? 206.915 197.186 233.613 1.00 11.12 ? 3637 ASP A OD2   1 
ATOM   15763 N  N     . VAL A 1 3638 ? 212.341 195.180 233.917 1.00 4.02  ? 3638 VAL A N     1 
ATOM   15764 C  CA    . VAL A 1 3638 ? 213.732 195.278 233.492 1.00 3.11  ? 3638 VAL A CA    1 
ATOM   15765 C  C     . VAL A 1 3638 ? 214.057 194.336 232.342 1.00 2.74  ? 3638 VAL A C     1 
ATOM   15766 O  O     . VAL A 1 3638 ? 215.136 194.439 231.752 1.00 4.92  ? 3638 VAL A O     1 
ATOM   15767 C  CB    . VAL A 1 3638 ? 214.662 195.038 234.703 1.00 1.79  ? 3638 VAL A CB    1 
ATOM   15768 C  CG1   . VAL A 1 3638 ? 214.688 193.570 235.085 1.00 2.15  ? 3638 VAL A CG1   1 
ATOM   15769 C  CG2   . VAL A 1 3638 ? 216.067 195.576 234.438 1.00 1.61  ? 3638 VAL A CG2   1 
ATOM   15770 N  N     . GLU A 1 3639 ? 213.142 193.425 232.000 1.00 3.62  ? 3639 GLU A N     1 
ATOM   15771 C  CA    . GLU A 1 3639 ? 213.292 192.639 230.781 1.00 6.21  ? 3639 GLU A CA    1 
ATOM   15772 C  C     . GLU A 1 3639 ? 213.268 193.518 229.538 1.00 5.77  ? 3639 GLU A C     1 
ATOM   15773 O  O     . GLU A 1 3639 ? 213.776 193.109 228.488 1.00 8.89  ? 3639 GLU A O     1 
ATOM   15774 C  CB    . GLU A 1 3639 ? 212.189 191.582 230.693 1.00 3.50  ? 3639 GLU A CB    1 
ATOM   15775 C  CG    . GLU A 1 3639 ? 210.778 192.115 230.914 1.00 6.24  ? 3639 GLU A CG    1 
ATOM   15776 C  CD    . GLU A 1 3639 ? 210.379 192.178 232.381 1.00 11.10 ? 3639 GLU A CD    1 
ATOM   15777 O  OE1   . GLU A 1 3639 ? 211.258 192.402 233.237 1.00 6.55  ? 3639 GLU A OE1   1 
ATOM   15778 O  OE2   . GLU A 1 3639 ? 209.180 192.005 232.674 1.00 17.44 ? 3639 GLU A OE2   1 
ATOM   15779 N  N     . SER A 1 3640 ? 212.685 194.710 229.635 1.00 3.31  ? 3640 SER A N     1 
ATOM   15780 C  CA    . SER A 1 3640 ? 212.693 195.713 228.574 1.00 4.92  ? 3640 SER A CA    1 
ATOM   15781 C  C     . SER A 1 3640 ? 213.694 196.820 228.870 1.00 5.38  ? 3640 SER A C     1 
ATOM   15782 O  O     . SER A 1 3640 ? 213.415 197.999 228.645 1.00 6.10  ? 3640 SER A O     1 
ATOM   15783 C  CB    . SER A 1 3640 ? 211.295 196.290 228.379 1.00 5.50  ? 3640 SER A CB    1 
ATOM   15784 O  OG    . SER A 1 3640 ? 210.384 195.284 227.974 1.00 12.01 ? 3640 SER A OG    1 
ATOM   15785 N  N     . TYR A 1 3641 ? 214.863 196.446 229.392 1.00 4.37  ? 3641 TYR A N     1 
ATOM   15786 C  CA    . TYR A 1 3641 ? 215.841 197.411 229.885 1.00 2.29  ? 3641 TYR A CA    1 
ATOM   15787 C  C     . TYR A 1 3641 ? 216.203 198.440 228.821 1.00 5.43  ? 3641 TYR A C     1 
ATOM   15788 O  O     . TYR A 1 3641 ? 216.497 198.096 227.673 1.00 8.00  ? 3641 TYR A O     1 
ATOM   15789 C  CB    . TYR A 1 3641 ? 217.095 196.675 230.355 1.00 2.27  ? 3641 TYR A CB    1 
ATOM   15790 C  CG    . TYR A 1 3641 ? 218.269 197.577 230.654 1.00 1.92  ? 3641 TYR A CG    1 
ATOM   15791 C  CD1   . TYR A 1 3641 ? 218.338 198.288 231.843 1.00 1.25  ? 3641 TYR A CD1   1 
ATOM   15792 C  CD2   . TYR A 1 3641 ? 219.311 197.715 229.746 1.00 0.80  ? 3641 TYR A CD2   1 
ATOM   15793 C  CE1   . TYR A 1 3641 ? 219.407 199.111 232.119 1.00 1.50  ? 3641 TYR A CE1   1 
ATOM   15794 C  CE2   . TYR A 1 3641 ? 220.382 198.534 230.015 1.00 1.37  ? 3641 TYR A CE2   1 
ATOM   15795 C  CZ    . TYR A 1 3641 ? 220.427 199.231 231.200 1.00 1.55  ? 3641 TYR A CZ    1 
ATOM   15796 O  OH    . TYR A 1 3641 ? 221.495 200.050 231.472 1.00 1.69  ? 3641 TYR A OH    1 
ATOM   15797 N  N     . ASP A 1 3642 ? 216.188 199.709 229.219 1.00 4.89  ? 3642 ASP A N     1 
ATOM   15798 C  CA    . ASP A 1 3642 ? 216.538 200.804 228.328 1.00 3.24  ? 3642 ASP A CA    1 
ATOM   15799 C  C     . ASP A 1 3642 ? 218.019 201.118 228.480 1.00 2.84  ? 3642 ASP A C     1 
ATOM   15800 O  O     . ASP A 1 3642 ? 218.455 201.458 229.588 1.00 1.48  ? 3642 ASP A O     1 
ATOM   15801 C  CB    . ASP A 1 3642 ? 215.701 202.034 228.650 1.00 6.12  ? 3642 ASP A CB    1 
ATOM   15802 C  CG    . ASP A 1 3642 ? 215.674 203.042 227.519 1.00 8.14  ? 3642 ASP A CG    1 
ATOM   15803 O  OD1   . ASP A 1 3642 ? 216.351 202.824 226.496 1.00 9.76  ? 3642 ASP A OD1   1 
ATOM   15804 O  OD2   . ASP A 1 3642 ? 214.959 204.056 227.651 1.00 12.16 ? 3642 ASP A OD2   1 
ATOM   15805 N  N     . PRO A 1 3643 ? 218.824 201.021 227.416 1.00 4.52  ? 3643 PRO A N     1 
ATOM   15806 C  CA    . PRO A 1 3643 ? 220.272 201.236 227.556 1.00 2.38  ? 3643 PRO A CA    1 
ATOM   15807 C  C     . PRO A 1 3643 ? 220.648 202.665 227.919 1.00 3.32  ? 3643 PRO A C     1 
ATOM   15808 O  O     . PRO A 1 3643 ? 221.834 202.988 228.022 1.00 6.83  ? 3643 PRO A O     1 
ATOM   15809 C  CB    . PRO A 1 3643 ? 220.816 200.855 226.171 1.00 3.56  ? 3643 PRO A CB    1 
ATOM   15810 C  CG    . PRO A 1 3643 ? 219.759 200.001 225.567 1.00 4.21  ? 3643 PRO A CG    1 
ATOM   15811 C  CD    . PRO A 1 3643 ? 218.469 200.551 226.068 1.00 2.73  ? 3643 PRO A CD    1 
ATOM   15812 N  N     . VAL A 1 3644 ? 219.649 203.528 228.111 1.00 4.27  ? 3644 VAL A N     1 
ATOM   15813 C  CA    . VAL A 1 3644 ? 219.907 204.892 228.550 1.00 3.02  ? 3644 VAL A CA    1 
ATOM   15814 C  C     . VAL A 1 3644 ? 220.473 204.923 229.966 1.00 4.40  ? 3644 VAL A C     1 
ATOM   15815 O  O     . VAL A 1 3644 ? 221.107 205.907 230.356 1.00 11.75 ? 3644 VAL A O     1 
ATOM   15816 C  CB    . VAL A 1 3644 ? 218.615 205.733 228.434 1.00 5.20  ? 3644 VAL A CB    1 
ATOM   15817 C  CG1   . VAL A 1 3644 ? 217.618 205.356 229.524 1.00 6.44  ? 3644 VAL A CG1   1 
ATOM   15818 C  CG2   . VAL A 1 3644 ? 218.929 207.219 228.460 1.00 6.46  ? 3644 VAL A CG2   1 
ATOM   15819 N  N     . LEU A 1 3645 ? 220.271 203.856 230.744 1.00 2.45  ? 3645 LEU A N     1 
ATOM   15820 C  CA    . LEU A 1 3645 ? 220.831 203.759 232.087 1.00 3.23  ? 3645 LEU A CA    1 
ATOM   15821 C  C     . LEU A 1 3645 ? 222.277 203.290 232.124 1.00 1.90  ? 3645 LEU A C     1 
ATOM   15822 O  O     . LEU A 1 3645 ? 222.843 203.211 233.218 1.00 3.07  ? 3645 LEU A O     1 
ATOM   15823 C  CB    . LEU A 1 3645 ? 220.010 202.808 232.962 1.00 4.10  ? 3645 LEU A CB    1 
ATOM   15824 C  CG    . LEU A 1 3645 ? 218.605 203.198 233.393 1.00 1.69  ? 3645 LEU A CG    1 
ATOM   15825 C  CD1   . LEU A 1 3645 ? 217.958 202.041 234.120 1.00 1.95  ? 3645 LEU A CD1   1 
ATOM   15826 C  CD2   . LEU A 1 3645 ? 218.738 204.373 234.323 1.00 0.79  ? 3645 LEU A CD2   1 
ATOM   15827 N  N     . ASN A 1 3646 ? 222.876 202.963 230.980 1.00 2.79  ? 3646 ASN A N     1 
ATOM   15828 C  CA    . ASN A 1 3646 ? 224.241 202.443 230.991 1.00 2.01  ? 3646 ASN A CA    1 
ATOM   15829 C  C     . ASN A 1 3646 ? 225.222 203.367 231.702 1.00 1.97  ? 3646 ASN A C     1 
ATOM   15830 O  O     . ASN A 1 3646 ? 225.986 202.876 232.552 1.00 2.50  ? 3646 ASN A O     1 
ATOM   15831 C  CB    . ASN A 1 3646 ? 224.688 202.137 229.557 1.00 1.30  ? 3646 ASN A CB    1 
ATOM   15832 C  CG    . ASN A 1 3646 ? 224.128 200.832 229.038 1.00 1.12  ? 3646 ASN A CG    1 
ATOM   15833 O  OD1   . ASN A 1 3646 ? 223.440 200.112 229.756 1.00 2.33  ? 3646 ASN A OD1   1 
ATOM   15834 N  ND2   . ASN A 1 3646 ? 224.424 200.517 227.785 1.00 2.58  ? 3646 ASN A ND2   1 
ATOM   15835 N  N     . PRO A 1 3647 ? 225.267 204.676 231.429 1.00 2.48  ? 3647 PRO A N     1 
ATOM   15836 C  CA    . PRO A 1 3647 ? 226.145 205.543 232.233 1.00 2.50  ? 3647 PRO A CA    1 
ATOM   15837 C  C     . PRO A 1 3647 ? 225.755 205.621 233.700 1.00 2.35  ? 3647 PRO A C     1 
ATOM   15838 O  O     . PRO A 1 3647 ? 226.633 205.781 234.554 1.00 2.30  ? 3647 PRO A O     1 
ATOM   15839 C  CB    . PRO A 1 3647 ? 226.019 206.906 231.537 1.00 2.42  ? 3647 PRO A CB    1 
ATOM   15840 C  CG    . PRO A 1 3647 ? 224.700 206.849 230.861 1.00 3.75  ? 3647 PRO A CG    1 
ATOM   15841 C  CD    . PRO A 1 3647 ? 224.580 205.446 230.377 1.00 2.52  ? 3647 PRO A CD    1 
ATOM   15842 N  N     . VAL A 1 3648 ? 224.463 205.524 234.019 1.00 2.90  ? 3648 VAL A N     1 
ATOM   15843 C  CA    . VAL A 1 3648 ? 224.034 205.606 235.413 1.00 1.98  ? 3648 VAL A CA    1 
ATOM   15844 C  C     . VAL A 1 3648 ? 224.495 204.376 236.187 1.00 1.54  ? 3648 VAL A C     1 
ATOM   15845 O  O     . VAL A 1 3648 ? 225.021 204.486 237.300 1.00 2.46  ? 3648 VAL A O     1 
ATOM   15846 C  CB    . VAL A 1 3648 ? 222.508 205.784 235.498 1.00 2.75  ? 3648 VAL A CB    1 
ATOM   15847 C  CG1   . VAL A 1 3648 ? 222.048 205.741 236.948 1.00 0.56  ? 3648 VAL A CG1   1 
ATOM   15848 C  CG2   . VAL A 1 3648 ? 222.087 207.092 234.846 1.00 1.35  ? 3648 VAL A CG2   1 
ATOM   15849 N  N     . LEU A 1 3649 ? 224.309 203.188 235.607 1.00 1.32  ? 3649 LEU A N     1 
ATOM   15850 C  CA    . LEU A 1 3649 ? 224.694 201.963 236.293 1.00 1.11  ? 3649 LEU A CA    1 
ATOM   15851 C  C     . LEU A 1 3649 ? 226.206 201.835 236.418 1.00 1.95  ? 3649 LEU A C     1 
ATOM   15852 O  O     . LEU A 1 3649 ? 226.699 201.314 237.424 1.00 4.82  ? 3649 LEU A O     1 
ATOM   15853 C  CB    . LEU A 1 3649 ? 224.114 200.747 235.569 1.00 1.24  ? 3649 LEU A CB    1 
ATOM   15854 C  CG    . LEU A 1 3649 ? 222.589 200.694 235.457 1.00 1.66  ? 3649 LEU A CG    1 
ATOM   15855 C  CD1   . LEU A 1 3649 ? 222.134 199.363 234.885 1.00 0.67  ? 3649 LEU A CD1   1 
ATOM   15856 C  CD2   . LEU A 1 3649 ? 221.933 200.959 236.803 1.00 1.28  ? 3649 LEU A CD2   1 
ATOM   15857 N  N     . ASN A 1 3650 ? 226.955 202.305 235.423 1.00 1.61  ? 3650 ASN A N     1 
ATOM   15858 C  CA    . ASN A 1 3650 ? 228.410 202.300 235.489 1.00 1.24  ? 3650 ASN A CA    1 
ATOM   15859 C  C     . ASN A 1 3650 ? 228.975 203.461 236.292 1.00 2.22  ? 3650 ASN A C     1 
ATOM   15860 O  O     . ASN A 1 3650 ? 230.193 203.509 236.494 1.00 8.54  ? 3650 ASN A O     1 
ATOM   15861 C  CB    . ASN A 1 3650 ? 229.012 202.318 234.083 1.00 1.86  ? 3650 ASN A CB    1 
ATOM   15862 C  CG    . ASN A 1 3650 ? 228.786 201.028 233.334 1.00 2.65  ? 3650 ASN A CG    1 
ATOM   15863 O  OD1   . ASN A 1 3650 ? 228.332 200.039 233.904 1.00 8.20  ? 3650 ASN A OD1   1 
ATOM   15864 N  ND2   . ASN A 1 3650 ? 229.112 201.026 232.051 1.00 3.65  ? 3650 ASN A ND2   1 
ATOM   15865 N  N     . ARG A 1 3651 ? 228.130 204.390 236.743 1.00 1.82  ? 3651 ARG A N     1 
ATOM   15866 C  CA    . ARG A 1 3651 ? 228.565 205.526 237.556 1.00 2.22  ? 3651 ARG A CA    1 
ATOM   15867 C  C     . ARG A 1 3651 ? 229.608 206.366 236.822 1.00 4.26  ? 3651 ARG A C     1 
ATOM   15868 O  O     . ARG A 1 3651 ? 230.617 206.785 237.392 1.00 5.05  ? 3651 ARG A O     1 
ATOM   15869 C  CB    . ARG A 1 3651 ? 229.088 205.052 238.913 1.00 4.20  ? 3651 ARG A CB    1 
ATOM   15870 C  CG    . ARG A 1 3651 ? 228.007 204.470 239.810 1.00 3.96  ? 3651 ARG A CG    1 
ATOM   15871 C  CD    . ARG A 1 3651 ? 228.575 203.928 241.107 1.00 5.55  ? 3651 ARG A CD    1 
ATOM   15872 N  NE    . ARG A 1 3651 ? 227.662 202.977 241.730 1.00 10.65 ? 3651 ARG A NE    1 
ATOM   15873 C  CZ    . ARG A 1 3651 ? 226.710 203.305 242.593 1.00 3.47  ? 3651 ARG A CZ    1 
ATOM   15874 N  NH1   . ARG A 1 3651 ? 226.528 204.556 242.980 1.00 3.59  ? 3651 ARG A NH1   1 
ATOM   15875 N  NH2   . ARG A 1 3651 ? 225.916 202.353 243.075 1.00 0.49  ? 3651 ARG A NH2   1 
ATOM   15876 N  N     . GLU A 1 3652 ? 229.360 206.607 235.534 1.00 3.95  ? 3652 GLU A N     1 
ATOM   15877 C  CA    . GLU A 1 3652 ? 230.254 207.399 234.687 1.00 3.01  ? 3652 GLU A CA    1 
ATOM   15878 C  C     . GLU A 1 3652 ? 229.956 208.879 234.902 1.00 5.16  ? 3652 GLU A C     1 
ATOM   15879 O  O     . GLU A 1 3652 ? 229.255 209.529 234.123 1.00 12.10 ? 3652 GLU A O     1 
ATOM   15880 C  CB    . GLU A 1 3652 ? 230.091 207.014 233.222 1.00 5.12  ? 3652 GLU A CB    1 
ATOM   15881 C  CG    . GLU A 1 3652 ? 230.082 205.526 232.941 1.00 2.96  ? 3652 GLU A CG    1 
ATOM   15882 C  CD    . GLU A 1 3652 ? 229.592 205.209 231.541 1.00 6.94  ? 3652 GLU A CD    1 
ATOM   15883 O  OE1   . GLU A 1 3652 ? 229.617 206.117 230.682 1.00 7.32  ? 3652 GLU A OE1   1 
ATOM   15884 O  OE2   . GLU A 1 3652 ? 229.174 204.059 231.295 1.00 6.34  ? 3652 GLU A OE2   1 
ATOM   15885 N  N     . VAL A 1 3653 ? 230.507 209.422 235.976 1.00 6.69  ? 3653 VAL A N     1 
ATOM   15886 C  CA    . VAL A 1 3653 ? 230.261 210.808 236.350 1.00 8.89  ? 3653 VAL A CA    1 
ATOM   15887 C  C     . VAL A 1 3653 ? 231.480 211.651 236.004 1.00 9.20  ? 3653 VAL A C     1 
ATOM   15888 O  O     . VAL A 1 3653 ? 232.626 211.192 236.067 1.00 10.84 ? 3653 VAL A O     1 
ATOM   15889 C  CB    . VAL A 1 3653 ? 229.898 210.936 237.843 1.00 8.85  ? 3653 VAL A CB    1 
ATOM   15890 C  CG1   . VAL A 1 3653 ? 228.620 210.177 238.129 1.00 10.30 ? 3653 VAL A CG1   1 
ATOM   15891 C  CG2   . VAL A 1 3653 ? 231.026 210.416 238.715 1.00 7.37  ? 3653 VAL A CG2   1 
ATOM   15892 N  N     . ARG A 1 3654 ? 231.223 212.898 235.619 1.00 10.15 ? 3654 ARG A N     1 
ATOM   15893 C  CA    . ARG A 1 3654 ? 232.266 213.851 235.257 1.00 10.13 ? 3654 ARG A CA    1 
ATOM   15894 C  C     . ARG A 1 3654 ? 232.202 215.004 236.251 1.00 13.24 ? 3654 ARG A C     1 
ATOM   15895 O  O     . ARG A 1 3654 ? 231.220 215.750 236.281 1.00 17.21 ? 3654 ARG A O     1 
ATOM   15896 C  CB    . ARG A 1 3654 ? 232.091 214.316 233.807 1.00 13.68 ? 3654 ARG A CB    1 
ATOM   15897 C  CG    . ARG A 1 3654 ? 233.195 215.214 233.251 1.00 18.06 ? 3654 ARG A CG    1 
ATOM   15898 C  CD    . ARG A 1 3654 ? 232.962 216.687 233.550 1.00 24.65 ? 3654 ARG A CD    1 
ATOM   15899 N  NE    . ARG A 1 3654 ? 231.675 217.149 233.045 1.00 29.87 ? 3654 ARG A NE    1 
ATOM   15900 C  CZ    . ARG A 1 3654 ? 231.453 217.515 231.789 1.00 30.49 ? 3654 ARG A CZ    1 
ATOM   15901 N  NH1   . ARG A 1 3654 ? 232.417 217.497 230.883 1.00 30.25 ? 3654 ARG A NH1   1 
ATOM   15902 N  NH2   . ARG A 1 3654 ? 230.235 217.913 231.435 1.00 24.19 ? 3654 ARG A NH2   1 
ATOM   15903 N  N     . ARG A 1 3655 ? 233.246 215.139 237.068 1.00 13.46 ? 3655 ARG A N     1 
ATOM   15904 C  CA    . ARG A 1 3655 ? 233.305 216.170 238.103 1.00 14.56 ? 3655 ARG A CA    1 
ATOM   15905 C  C     . ARG A 1 3655 ? 234.236 217.283 237.644 1.00 21.35 ? 3655 ARG A C     1 
ATOM   15906 O  O     . ARG A 1 3655 ? 235.457 217.193 237.788 1.00 27.20 ? 3655 ARG A O     1 
ATOM   15907 C  CB    . ARG A 1 3655 ? 233.745 215.572 239.437 1.00 10.95 ? 3655 ARG A CB    1 
ATOM   15908 C  CG    . ARG A 1 3655 ? 232.671 214.720 240.094 1.00 14.37 ? 3655 ARG A CG    1 
ATOM   15909 C  CD    . ARG A 1 3655 ? 233.188 213.900 241.266 1.00 14.99 ? 3655 ARG A CD    1 
ATOM   15910 N  NE    . ARG A 1 3655 ? 232.097 213.189 241.922 1.00 16.53 ? 3655 ARG A NE    1 
ATOM   15911 C  CZ    . ARG A 1 3655 ? 231.983 211.870 241.987 1.00 18.91 ? 3655 ARG A CZ    1 
ATOM   15912 N  NH1   . ARG A 1 3655 ? 232.881 211.069 241.438 1.00 24.71 ? 3655 ARG A NH1   1 
ATOM   15913 N  NH2   . ARG A 1 3655 ? 230.938 211.338 242.618 1.00 17.86 ? 3655 ARG A NH2   1 
ATOM   15914 N  N     . THR A 1 3656 ? 233.651 218.341 237.085 1.00 24.61 ? 3656 THR A N     1 
ATOM   15915 C  CA    . THR A 1 3656 ? 234.389 219.514 236.646 1.00 25.71 ? 3656 THR A CA    1 
ATOM   15916 C  C     . THR A 1 3656 ? 233.605 220.763 237.019 1.00 24.61 ? 3656 THR A C     1 
ATOM   15917 O  O     . THR A 1 3656 ? 232.377 220.801 236.905 1.00 22.38 ? 3656 THR A O     1 
ATOM   15918 C  CB    . THR A 1 3656 ? 234.655 219.483 235.132 1.00 28.57 ? 3656 THR A CB    1 
ATOM   15919 O  OG1   . THR A 1 3656 ? 235.372 218.290 234.797 1.00 31.20 ? 3656 THR A OG1   1 
ATOM   15920 C  CG2   . THR A 1 3656 ? 235.472 220.693 234.697 1.00 25.00 ? 3656 THR A CG2   1 
ATOM   15921 N  N     . GLY A 1 3657 ? 234.328 221.784 237.468 1.00 28.27 ? 3657 GLY A N     1 
ATOM   15922 C  CA    . GLY A 1 3657 ? 233.705 223.051 237.818 1.00 20.72 ? 3657 GLY A CA    1 
ATOM   15923 C  C     . GLY A 1 3657 ? 232.802 222.981 239.028 1.00 16.08 ? 3657 GLY A C     1 
ATOM   15924 O  O     . GLY A 1 3657 ? 231.753 223.637 239.054 1.00 23.89 ? 3657 GLY A O     1 
ATOM   15925 N  N     . GLY A 1 3658 ? 233.186 222.200 240.035 1.00 18.62 ? 3658 GLY A N     1 
ATOM   15926 C  CA    . GLY A 1 3658 ? 232.376 222.071 241.235 1.00 15.15 ? 3658 GLY A CA    1 
ATOM   15927 C  C     . GLY A 1 3658 ? 231.035 221.415 241.002 1.00 16.99 ? 3658 GLY A C     1 
ATOM   15928 O  O     . GLY A 1 3658 ? 230.143 221.522 241.849 1.00 21.69 ? 3658 GLY A O     1 
ATOM   15929 N  N     . ARG A 1 3659 ? 230.871 220.730 239.876 1.00 12.91 ? 3659 ARG A N     1 
ATOM   15930 C  CA    . ARG A 1 3659 ? 229.605 220.116 239.504 1.00 12.13 ? 3659 ARG A CA    1 
ATOM   15931 C  C     . ARG A 1 3659 ? 229.827 218.644 239.197 1.00 14.46 ? 3659 ARG A C     1 
ATOM   15932 O  O     . ARG A 1 3659 ? 230.806 218.286 238.535 1.00 16.99 ? 3659 ARG A O     1 
ATOM   15933 C  CB    . ARG A 1 3659 ? 228.990 220.817 238.290 1.00 14.65 ? 3659 ARG A CB    1 
ATOM   15934 C  CG    . ARG A 1 3659 ? 228.343 222.150 238.576 1.00 14.37 ? 3659 ARG A CG    1 
ATOM   15935 C  CD    . ARG A 1 3659 ? 228.012 222.864 237.278 1.00 14.98 ? 3659 ARG A CD    1 
ATOM   15936 N  NE    . ARG A 1 3659 ? 226.870 222.264 236.601 1.00 11.58 ? 3659 ARG A NE    1 
ATOM   15937 C  CZ    . ARG A 1 3659 ? 226.786 222.079 235.291 1.00 13.61 ? 3659 ARG A CZ    1 
ATOM   15938 N  NH1   . ARG A 1 3659 ? 227.768 222.436 234.479 1.00 13.94 ? 3659 ARG A NH1   1 
ATOM   15939 N  NH2   . ARG A 1 3659 ? 225.690 221.525 234.783 1.00 11.60 ? 3659 ARG A NH2   1 
ATOM   15940 N  N     . VAL A 1 3660 ? 228.919 217.800 239.671 1.00 14.95 ? 3660 VAL A N     1 
ATOM   15941 C  CA    . VAL A 1 3660 ? 228.950 216.371 239.380 1.00 11.27 ? 3660 VAL A CA    1 
ATOM   15942 C  C     . VAL A 1 3660 ? 227.919 216.091 238.296 1.00 8.34  ? 3660 VAL A C     1 
ATOM   15943 O  O     . VAL A 1 3660 ? 226.712 216.209 238.533 1.00 13.78 ? 3660 VAL A O     1 
ATOM   15944 C  CB    . VAL A 1 3660 ? 228.670 215.542 240.641 1.00 8.24  ? 3660 VAL A CB    1 
ATOM   15945 C  CG1   . VAL A 1 3660 ? 228.795 214.059 240.343 1.00 7.05  ? 3660 VAL A CG1   1 
ATOM   15946 C  CG2   . VAL A 1 3660 ? 229.610 215.953 241.762 1.00 9.42  ? 3660 VAL A CG2   1 
ATOM   15947 N  N     . LEU A 1 3661 ? 228.387 215.714 237.111 1.00 5.59  ? 3661 LEU A N     1 
ATOM   15948 C  CA    . LEU A 1 3661 ? 227.536 215.581 235.937 1.00 8.21  ? 3661 LEU A CA    1 
ATOM   15949 C  C     . LEU A 1 3661 ? 227.443 214.128 235.497 1.00 9.17  ? 3661 LEU A C     1 
ATOM   15950 O  O     . LEU A 1 3661 ? 228.440 213.401 235.501 1.00 12.89 ? 3661 LEU A O     1 
ATOM   15951 C  CB    . LEU A 1 3661 ? 228.051 216.430 234.771 1.00 13.12 ? 3661 LEU A CB    1 
ATOM   15952 C  CG    . LEU A 1 3661 ? 227.585 217.886 234.662 1.00 10.81 ? 3661 LEU A CG    1 
ATOM   15953 C  CD1   . LEU A 1 3661 ? 226.120 217.964 234.286 1.00 14.15 ? 3661 LEU A CD1   1 
ATOM   15954 C  CD2   . LEU A 1 3661 ? 227.836 218.639 235.938 1.00 9.36  ? 3661 LEU A CD2   1 
ATOM   15955 N  N     . ILE A 1 3662 ? 226.238 213.716 235.117 1.00 11.97 ? 3662 ILE A N     1 
ATOM   15956 C  CA    . ILE A 1 3662 ? 225.988 212.408 234.525 1.00 6.86  ? 3662 ILE A CA    1 
ATOM   15957 C  C     . ILE A 1 3662 ? 225.367 212.638 233.153 1.00 6.58  ? 3662 ILE A C     1 
ATOM   15958 O  O     . ILE A 1 3662 ? 224.426 213.427 233.016 1.00 11.44 ? 3662 ILE A O     1 
ATOM   15959 C  CB    . ILE A 1 3662 ? 225.083 211.540 235.423 1.00 7.47  ? 3662 ILE A CB    1 
ATOM   15960 C  CG1   . ILE A 1 3662 ? 224.807 210.182 234.775 1.00 7.09  ? 3662 ILE A CG1   1 
ATOM   15961 C  CG2   . ILE A 1 3662 ? 223.787 212.264 235.778 1.00 6.66  ? 3662 ILE A CG2   1 
ATOM   15962 C  CD1   . ILE A 1 3662 ? 225.994 209.252 234.793 1.00 7.55  ? 3662 ILE A CD1   1 
ATOM   15963 N  N     . THR A 1 3663 ? 225.915 211.979 232.137 1.00 9.07  ? 3663 THR A N     1 
ATOM   15964 C  CA    . THR A 1 3663 ? 225.482 212.195 230.758 1.00 12.13 ? 3663 THR A CA    1 
ATOM   15965 C  C     . THR A 1 3663 ? 224.365 211.207 230.445 1.00 12.04 ? 3663 THR A C     1 
ATOM   15966 O  O     . THR A 1 3663 ? 224.615 210.023 230.208 1.00 14.16 ? 3663 THR A O     1 
ATOM   15967 C  CB    . THR A 1 3663 ? 226.651 212.047 229.792 1.00 14.88 ? 3663 THR A CB    1 
ATOM   15968 O  OG1   . THR A 1 3663 ? 227.680 212.978 230.143 1.00 17.82 ? 3663 THR A OG1   1 
ATOM   15969 C  CG2   . THR A 1 3663 ? 226.196 212.324 228.367 1.00 15.35 ? 3663 THR A CG2   1 
ATOM   15970 N  N     . LEU A 1 3664 ? 223.128 211.696 230.445 1.00 9.34  ? 3664 LEU A N     1 
ATOM   15971 C  CA    . LEU A 1 3664 ? 221.953 210.882 230.151 1.00 9.08  ? 3664 LEU A CA    1 
ATOM   15972 C  C     . LEU A 1 3664 ? 221.517 211.199 228.727 1.00 12.01 ? 3664 LEU A C     1 
ATOM   15973 O  O     . LEU A 1 3664 ? 220.912 212.242 228.468 1.00 13.09 ? 3664 LEU A O     1 
ATOM   15974 C  CB    . LEU A 1 3664 ? 220.837 211.154 231.153 1.00 6.33  ? 3664 LEU A CB    1 
ATOM   15975 C  CG    . LEU A 1 3664 ? 219.627 210.234 231.017 1.00 5.33  ? 3664 LEU A CG    1 
ATOM   15976 C  CD1   . LEU A 1 3664 ? 220.000 208.844 231.486 1.00 4.86  ? 3664 LEU A CD1   1 
ATOM   15977 C  CD2   . LEU A 1 3664 ? 218.433 210.769 231.790 1.00 6.50  ? 3664 LEU A CD2   1 
ATOM   15978 N  N     . GLY A 1 3665 ? 221.810 210.288 227.805 1.00 12.69 ? 3665 GLY A N     1 
ATOM   15979 C  CA    . GLY A 1 3665 ? 221.617 210.569 226.398 1.00 11.19 ? 3665 GLY A CA    1 
ATOM   15980 C  C     . GLY A 1 3665 ? 222.545 211.668 225.926 1.00 14.91 ? 3665 GLY A C     1 
ATOM   15981 O  O     . GLY A 1 3665 ? 223.763 211.578 226.102 1.00 25.52 ? 3665 GLY A O     1 
ATOM   15982 N  N     . ASP A 1 3666 ? 221.984 212.714 225.324 1.00 18.53 ? 3666 ASP A N     1 
ATOM   15983 C  CA    . ASP A 1 3666 ? 222.755 213.862 224.871 1.00 18.71 ? 3666 ASP A CA    1 
ATOM   15984 C  C     . ASP A 1 3666 ? 222.660 215.051 225.820 1.00 20.95 ? 3666 ASP A C     1 
ATOM   15985 O  O     . ASP A 1 3666 ? 223.192 216.120 225.504 1.00 25.04 ? 3666 ASP A O     1 
ATOM   15986 C  CB    . ASP A 1 3666 ? 222.299 214.281 223.472 1.00 25.81 ? 3666 ASP A CB    1 
ATOM   15987 C  CG    . ASP A 1 3666 ? 220.856 214.737 223.448 1.00 32.05 ? 3666 ASP A CG    1 
ATOM   15988 O  OD1   . ASP A 1 3666 ? 219.982 213.960 223.886 1.00 28.14 ? 3666 ASP A OD1   1 
ATOM   15989 O  OD2   . ASP A 1 3666 ? 220.595 215.871 222.993 1.00 31.84 ? 3666 ASP A OD2   1 
ATOM   15990 N  N     . GLN A 1 3667 ? 222.004 214.894 226.963 1.00 16.28 ? 3667 GLN A N     1 
ATOM   15991 C  CA    . GLN A 1 3667 ? 221.819 215.966 227.929 1.00 15.92 ? 3667 GLN A CA    1 
ATOM   15992 C  C     . GLN A 1 3667 ? 222.590 215.645 229.200 1.00 17.54 ? 3667 GLN A C     1 
ATOM   15993 O  O     . GLN A 1 3667 ? 222.479 214.537 229.733 1.00 24.38 ? 3667 GLN A O     1 
ATOM   15994 C  CB    . GLN A 1 3667 ? 220.334 216.163 228.246 1.00 21.25 ? 3667 GLN A CB    1 
ATOM   15995 C  CG    . GLN A 1 3667 ? 220.041 217.324 229.182 1.00 24.39 ? 3667 GLN A CG    1 
ATOM   15996 C  CD    . GLN A 1 3667 ? 218.556 217.515 229.422 1.00 32.28 ? 3667 GLN A CD    1 
ATOM   15997 O  OE1   . GLN A 1 3667 ? 217.731 216.755 228.917 1.00 35.44 ? 3667 GLN A OE1   1 
ATOM   15998 N  NE2   . GLN A 1 3667 ? 218.207 218.536 230.197 1.00 36.59 ? 3667 GLN A NE2   1 
ATOM   15999 N  N     . ASP A 1 3668 ? 223.373 216.609 229.678 1.00 11.33 ? 3668 ASP A N     1 
ATOM   16000 C  CA    . ASP A 1 3668 ? 224.097 216.451 230.929 1.00 11.70 ? 3668 ASP A CA    1 
ATOM   16001 C  C     . ASP A 1 3668 ? 223.231 216.879 232.111 1.00 10.67 ? 3668 ASP A C     1 
ATOM   16002 O  O     . ASP A 1 3668 ? 222.521 217.886 232.050 1.00 16.48 ? 3668 ASP A O     1 
ATOM   16003 C  CB    . ASP A 1 3668 ? 225.423 217.224 230.896 1.00 18.96 ? 3668 ASP A CB    1 
ATOM   16004 C  CG    . ASP A 1 3668 ? 225.246 218.725 230.683 1.00 30.90 ? 3668 ASP A CG    1 
ATOM   16005 O  OD1   . ASP A 1 3668 ? 224.110 219.201 230.488 1.00 40.72 ? 3668 ASP A OD1   1 
ATOM   16006 O  OD2   . ASP A 1 3668 ? 226.268 219.442 230.713 1.00 28.09 ? 3668 ASP A OD2   1 
ATOM   16007 N  N     . ILE A 1 3669 ? 223.271 216.086 233.175 1.00 8.40  ? 3669 ILE A N     1 
ATOM   16008 C  CA    . ILE A 1 3669 ? 222.425 216.287 234.345 1.00 4.83  ? 3669 ILE A CA    1 
ATOM   16009 C  C     . ILE A 1 3669 ? 223.302 216.308 235.586 1.00 7.11  ? 3669 ILE A C     1 
ATOM   16010 O  O     . ILE A 1 3669 ? 224.216 215.489 235.723 1.00 9.90  ? 3669 ILE A O     1 
ATOM   16011 C  CB    . ILE A 1 3669 ? 221.344 215.190 234.465 1.00 7.07  ? 3669 ILE A CB    1 
ATOM   16012 C  CG1   . ILE A 1 3669 ? 220.572 215.050 233.154 1.00 8.59  ? 3669 ILE A CG1   1 
ATOM   16013 C  CG2   . ILE A 1 3669 ? 220.392 215.490 235.613 1.00 6.03  ? 3669 ILE A CG2   1 
ATOM   16014 C  CD1   . ILE A 1 3669 ? 219.574 213.932 233.161 1.00 7.93  ? 3669 ILE A CD1   1 
ATOM   16015 N  N     . ASP A 1 3670 ? 223.028 217.249 236.484 1.00 6.80  ? 3670 ASP A N     1 
ATOM   16016 C  CA    . ASP A 1 3670 ? 223.701 217.268 237.775 1.00 8.67  ? 3670 ASP A CA    1 
ATOM   16017 C  C     . ASP A 1 3670 ? 223.206 216.101 238.620 1.00 8.79  ? 3670 ASP A C     1 
ATOM   16018 O  O     . ASP A 1 3670 ? 222.000 215.948 238.837 1.00 10.06 ? 3670 ASP A O     1 
ATOM   16019 C  CB    . ASP A 1 3670 ? 223.445 218.596 238.482 1.00 10.60 ? 3670 ASP A CB    1 
ATOM   16020 C  CG    . ASP A 1 3670 ? 223.931 219.784 237.678 1.00 19.61 ? 3670 ASP A CG    1 
ATOM   16021 O  OD1   . ASP A 1 3670 ? 225.140 219.842 237.376 1.00 18.01 ? 3670 ASP A OD1   1 
ATOM   16022 O  OD2   . ASP A 1 3670 ? 223.103 220.659 237.347 1.00 29.54 ? 3670 ASP A OD2   1 
ATOM   16023 N  N     . LEU A 1 3671 ? 224.135 215.277 239.097 1.00 11.46 ? 3671 LEU A N     1 
ATOM   16024 C  CA    . LEU A 1 3671 ? 223.797 214.074 239.847 1.00 5.58  ? 3671 LEU A CA    1 
ATOM   16025 C  C     . LEU A 1 3671 ? 223.812 214.374 241.340 1.00 6.21  ? 3671 LEU A C     1 
ATOM   16026 O  O     . LEU A 1 3671 ? 224.852 214.739 241.896 1.00 7.62  ? 3671 LEU A O     1 
ATOM   16027 C  CB    . LEU A 1 3671 ? 224.773 212.945 239.523 1.00 6.97  ? 3671 LEU A CB    1 
ATOM   16028 C  CG    . LEU A 1 3671 ? 224.554 211.662 240.327 1.00 5.69  ? 3671 LEU A CG    1 
ATOM   16029 C  CD1   . LEU A 1 3671 ? 223.194 211.067 240.022 1.00 4.34  ? 3671 LEU A CD1   1 
ATOM   16030 C  CD2   . LEU A 1 3671 ? 225.654 210.657 240.063 1.00 6.90  ? 3671 LEU A CD2   1 
ATOM   16031 N  N     . SER A 1 3672 ? 222.661 214.227 241.982 1.00 6.61  ? 3672 SER A N     1 
ATOM   16032 C  CA    . SER A 1 3672 ? 222.602 214.370 243.429 1.00 5.21  ? 3672 SER A CA    1 
ATOM   16033 C  C     . SER A 1 3672 ? 223.117 213.097 244.101 1.00 6.95  ? 3672 SER A C     1 
ATOM   16034 O  O     . SER A 1 3672 ? 222.853 211.992 243.623 1.00 9.07  ? 3672 SER A O     1 
ATOM   16035 C  CB    . SER A 1 3672 ? 221.178 214.664 243.880 1.00 6.67  ? 3672 SER A CB    1 
ATOM   16036 O  OG    . SER A 1 3672 ? 221.033 214.479 245.277 1.00 12.48 ? 3672 SER A OG    1 
ATOM   16037 N  N     . PRO A 1 3673 ? 223.862 213.224 245.203 1.00 7.26  ? 3673 PRO A N     1 
ATOM   16038 C  CA    . PRO A 1 3673 ? 224.440 212.034 245.846 1.00 4.50  ? 3673 PRO A CA    1 
ATOM   16039 C  C     . PRO A 1 3673 ? 223.421 211.127 246.515 1.00 6.46  ? 3673 PRO A C     1 
ATOM   16040 O  O     . PRO A 1 3673 ? 223.763 209.982 246.837 1.00 12.29 ? 3673 PRO A O     1 
ATOM   16041 C  CB    . PRO A 1 3673 ? 225.408 212.632 246.872 1.00 7.37  ? 3673 PRO A CB    1 
ATOM   16042 C  CG    . PRO A 1 3673 ? 224.831 213.964 247.182 1.00 8.59  ? 3673 PRO A CG    1 
ATOM   16043 C  CD    . PRO A 1 3673 ? 224.252 214.465 245.892 1.00 6.20  ? 3673 PRO A CD    1 
ATOM   16044 N  N     . SER A 1 3674 ? 222.195 211.586 246.739 1.00 8.98  ? 3674 SER A N     1 
ATOM   16045 C  CA    . SER A 1 3674 ? 221.176 210.768 247.378 1.00 5.28  ? 3674 SER A CA    1 
ATOM   16046 C  C     . SER A 1 3674 ? 220.404 209.903 246.391 1.00 7.85  ? 3674 SER A C     1 
ATOM   16047 O  O     . SER A 1 3674 ? 219.505 209.168 246.810 1.00 9.02  ? 3674 SER A O     1 
ATOM   16048 C  CB    . SER A 1 3674 ? 220.201 211.653 248.161 1.00 6.26  ? 3674 SER A CB    1 
ATOM   16049 O  OG    . SER A 1 3674 ? 219.782 212.761 247.387 1.00 15.66 ? 3674 SER A OG    1 
ATOM   16050 N  N     . PHE A 1 3675 ? 220.731 209.968 245.105 1.00 6.64  ? 3675 PHE A N     1 
ATOM   16051 C  CA    . PHE A 1 3675 ? 220.024 209.174 244.112 1.00 1.56  ? 3675 PHE A CA    1 
ATOM   16052 C  C     . PHE A 1 3675 ? 220.327 207.690 244.285 1.00 0.74  ? 3675 PHE A C     1 
ATOM   16053 O  O     . PHE A 1 3675 ? 221.461 207.297 244.571 1.00 2.17  ? 3675 PHE A O     1 
ATOM   16054 C  CB    . PHE A 1 3675 ? 220.395 209.620 242.697 1.00 1.92  ? 3675 PHE A CB    1 
ATOM   16055 C  CG    . PHE A 1 3675 ? 220.051 208.611 241.635 1.00 0.56  ? 3675 PHE A CG    1 
ATOM   16056 C  CD1   . PHE A 1 3675 ? 218.782 208.573 241.088 1.00 0.44  ? 3675 PHE A CD1   1 
ATOM   16057 C  CD2   . PHE A 1 3675 ? 220.993 207.700 241.187 1.00 0.21  ? 3675 PHE A CD2   1 
ATOM   16058 C  CE1   . PHE A 1 3675 ? 218.459 207.651 240.122 1.00 0.30  ? 3675 PHE A CE1   1 
ATOM   16059 C  CE2   . PHE A 1 3675 ? 220.673 206.771 240.221 1.00 0.23  ? 3675 PHE A CE2   1 
ATOM   16060 C  CZ    . PHE A 1 3675 ? 219.406 206.749 239.686 1.00 0.15  ? 3675 PHE A CZ    1 
ATOM   16061 N  N     . VAL A 1 3676 ? 219.302 206.870 244.098 1.00 0.46  ? 3676 VAL A N     1 
ATOM   16062 C  CA    . VAL A 1 3676 ? 219.444 205.419 244.070 1.00 0.31  ? 3676 VAL A CA    1 
ATOM   16063 C  C     . VAL A 1 3676 ? 218.364 204.865 243.155 1.00 0.34  ? 3676 VAL A C     1 
ATOM   16064 O  O     . VAL A 1 3676 ? 217.269 205.423 243.061 1.00 0.57  ? 3676 VAL A O     1 
ATOM   16065 C  CB    . VAL A 1 3676 ? 219.382 204.813 245.492 1.00 0.40  ? 3676 VAL A CB    1 
ATOM   16066 C  CG1   . VAL A 1 3676 ? 218.027 205.042 246.122 1.00 0.66  ? 3676 VAL A CG1   1 
ATOM   16067 C  CG2   . VAL A 1 3676 ? 219.697 203.335 245.456 1.00 0.25  ? 3676 VAL A CG2   1 
ATOM   16068 N  N     . ILE A 1 3677 ? 218.687 203.784 242.451 1.00 0.28  ? 3677 ILE A N     1 
ATOM   16069 C  CA    . ILE A 1 3677 ? 217.779 203.171 241.492 1.00 0.18  ? 3677 ILE A CA    1 
ATOM   16070 C  C     . ILE A 1 3677 ? 217.697 201.678 241.777 1.00 0.20  ? 3677 ILE A C     1 
ATOM   16071 O  O     . ILE A 1 3677 ? 218.719 201.027 242.016 1.00 0.25  ? 3677 ILE A O     1 
ATOM   16072 C  CB    . ILE A 1 3677 ? 218.224 203.438 240.039 1.00 0.23  ? 3677 ILE A CB    1 
ATOM   16073 C  CG1   . ILE A 1 3677 ? 217.282 202.754 239.046 1.00 0.11  ? 3677 ILE A CG1   1 
ATOM   16074 C  CG2   . ILE A 1 3677 ? 219.675 203.025 239.820 1.00 0.10  ? 3677 ILE A CG2   1 
ATOM   16075 C  CD1   . ILE A 1 3677 ? 217.355 203.330 237.653 1.00 0.13  ? 3677 ILE A CD1   1 
ATOM   16076 N  N     . PHE A 1 3678 ? 216.479 201.144 241.772 1.00 0.26  ? 3678 PHE A N     1 
ATOM   16077 C  CA    . PHE A 1 3678 ? 216.235 199.714 241.898 1.00 0.13  ? 3678 PHE A CA    1 
ATOM   16078 C  C     . PHE A 1 3678 ? 215.532 199.226 240.641 1.00 0.25  ? 3678 PHE A C     1 
ATOM   16079 O  O     . PHE A 1 3678 ? 214.534 199.813 240.218 1.00 1.39  ? 3678 PHE A O     1 
ATOM   16080 C  CB    . PHE A 1 3678 ? 215.383 199.393 243.131 1.00 0.22  ? 3678 PHE A CB    1 
ATOM   16081 C  CG    . PHE A 1 3678 ? 216.010 199.807 244.430 1.00 0.16  ? 3678 PHE A CG    1 
ATOM   16082 C  CD1   . PHE A 1 3678 ? 215.789 201.071 244.950 1.00 0.12  ? 3678 PHE A CD1   1 
ATOM   16083 C  CD2   . PHE A 1 3678 ? 216.813 198.929 245.136 1.00 0.11  ? 3678 PHE A CD2   1 
ATOM   16084 C  CE1   . PHE A 1 3678 ? 216.362 201.453 246.144 1.00 0.27  ? 3678 PHE A CE1   1 
ATOM   16085 C  CE2   . PHE A 1 3678 ? 217.388 199.305 246.333 1.00 0.19  ? 3678 PHE A CE2   1 
ATOM   16086 C  CZ    . PHE A 1 3678 ? 217.162 200.568 246.838 1.00 0.21  ? 3678 PHE A CZ    1 
ATOM   16087 N  N     . LEU A 1 3679 ? 216.057 198.161 240.049 1.00 0.26  ? 3679 LEU A N     1 
ATOM   16088 C  CA    . LEU A 1 3679 ? 215.440 197.516 238.900 1.00 0.31  ? 3679 LEU A CA    1 
ATOM   16089 C  C     . LEU A 1 3679 ? 214.744 196.241 239.355 1.00 0.62  ? 3679 LEU A C     1 
ATOM   16090 O  O     . LEU A 1 3679 ? 215.270 195.505 240.192 1.00 2.23  ? 3679 LEU A O     1 
ATOM   16091 C  CB    . LEU A 1 3679 ? 216.478 197.197 237.822 1.00 0.20  ? 3679 LEU A CB    1 
ATOM   16092 C  CG    . LEU A 1 3679 ? 217.460 198.315 237.457 1.00 0.35  ? 3679 LEU A CG    1 
ATOM   16093 C  CD1   . LEU A 1 3679 ? 218.363 197.884 236.314 1.00 0.39  ? 3679 LEU A CD1   1 
ATOM   16094 C  CD2   . LEU A 1 3679 ? 216.726 199.603 237.109 1.00 0.21  ? 3679 LEU A CD2   1 
ATOM   16095 N  N     . SER A 1 3680 ? 213.559 195.987 238.809 1.00 0.90  ? 3680 SER A N     1 
ATOM   16096 C  CA    . SER A 1 3680 ? 212.766 194.845 239.236 1.00 0.85  ? 3680 SER A CA    1 
ATOM   16097 C  C     . SER A 1 3680 ? 212.149 194.146 238.036 1.00 1.40  ? 3680 SER A C     1 
ATOM   16098 O  O     . SER A 1 3680 ? 211.846 194.767 237.016 1.00 1.72  ? 3680 SER A O     1 
ATOM   16099 C  CB    . SER A 1 3680 ? 211.666 195.262 240.220 1.00 1.32  ? 3680 SER A CB    1 
ATOM   16100 O  OG    . SER A 1 3680 ? 210.911 196.346 239.714 1.00 3.68  ? 3680 SER A OG    1 
ATOM   16101 N  N     . THR A 1 3681 ? 211.973 192.836 238.178 1.00 1.70  ? 3681 THR A N     1 
ATOM   16102 C  CA    . THR A 1 3681 ? 211.231 192.024 237.227 1.00 1.65  ? 3681 THR A CA    1 
ATOM   16103 C  C     . THR A 1 3681 ? 210.414 191.000 237.998 1.00 1.21  ? 3681 THR A C     1 
ATOM   16104 O  O     . THR A 1 3681 ? 210.782 190.595 239.103 1.00 1.96  ? 3681 THR A O     1 
ATOM   16105 C  CB    . THR A 1 3681 ? 212.149 191.309 236.222 1.00 3.44  ? 3681 THR A CB    1 
ATOM   16106 O  OG1   . THR A 1 3681 ? 211.361 190.495 235.347 1.00 4.00  ? 3681 THR A OG1   1 
ATOM   16107 C  CG2   . THR A 1 3681 ? 213.163 190.433 236.941 1.00 1.58  ? 3681 THR A CG2   1 
ATOM   16108 N  N     . ARG A 1 3682 ? 209.293 190.593 237.411 1.00 3.78  ? 3682 ARG A N     1 
ATOM   16109 C  CA    . ARG A 1 3682 ? 208.462 189.544 237.979 1.00 3.90  ? 3682 ARG A CA    1 
ATOM   16110 C  C     . ARG A 1 3682 ? 208.669 188.197 237.302 1.00 3.89  ? 3682 ARG A C     1 
ATOM   16111 O  O     . ARG A 1 3682 ? 208.004 187.225 237.669 1.00 9.16  ? 3682 ARG A O     1 
ATOM   16112 C  CB    . ARG A 1 3682 ? 206.985 189.944 237.902 1.00 1.97  ? 3682 ARG A CB    1 
ATOM   16113 C  CG    . ARG A 1 3682 ? 206.603 191.077 238.835 1.00 2.19  ? 3682 ARG A CG    1 
ATOM   16114 C  CD    . ARG A 1 3682 ? 205.113 191.358 238.778 1.00 2.16  ? 3682 ARG A CD    1 
ATOM   16115 N  NE    . ARG A 1 3682 ? 204.716 191.905 237.485 1.00 4.32  ? 3682 ARG A NE    1 
ATOM   16116 C  CZ    . ARG A 1 3682 ? 204.031 191.235 236.569 1.00 6.17  ? 3682 ARG A CZ    1 
ATOM   16117 N  NH1   . ARG A 1 3682 ? 203.655 189.983 236.766 1.00 5.54  ? 3682 ARG A NH1   1 
ATOM   16118 N  NH2   . ARG A 1 3682 ? 203.723 191.835 235.424 1.00 8.52  ? 3682 ARG A NH2   1 
ATOM   16119 N  N     . ASP A 1 3683 ? 209.577 188.115 236.331 1.00 3.43  ? 3683 ASP A N     1 
ATOM   16120 C  CA    . ASP A 1 3683 ? 209.799 186.883 235.594 1.00 4.42  ? 3683 ASP A CA    1 
ATOM   16121 C  C     . ASP A 1 3683 ? 211.073 186.227 236.101 1.00 6.56  ? 3683 ASP A C     1 
ATOM   16122 O  O     . ASP A 1 3683 ? 212.168 186.741 235.833 1.00 8.49  ? 3683 ASP A O     1 
ATOM   16123 C  CB    . ASP A 1 3683 ? 209.904 187.173 234.097 1.00 4.56  ? 3683 ASP A CB    1 
ATOM   16124 C  CG    . ASP A 1 3683 ? 209.844 185.918 233.246 1.00 9.98  ? 3683 ASP A CG    1 
ATOM   16125 O  OD1   . ASP A 1 3683 ? 210.238 184.833 233.719 1.00 17.15 ? 3683 ASP A OD1   1 
ATOM   16126 O  OD2   . ASP A 1 3683 ? 209.396 186.020 232.085 1.00 12.26 ? 3683 ASP A OD2   1 
ATOM   16127 N  N     . PRO A 1 3684 ? 210.994 185.112 236.832 1.00 6.94  ? 3684 PRO A N     1 
ATOM   16128 C  CA    . PRO A 1 3684 ? 212.221 184.426 237.262 1.00 7.80  ? 3684 PRO A CA    1 
ATOM   16129 C  C     . PRO A 1 3684 ? 212.979 183.762 236.126 1.00 10.73 ? 3684 PRO A C     1 
ATOM   16130 O  O     . PRO A 1 3684 ? 214.158 183.434 236.305 1.00 15.82 ? 3684 PRO A O     1 
ATOM   16131 C  CB    . PRO A 1 3684 ? 211.705 183.389 238.265 1.00 11.13 ? 3684 PRO A CB    1 
ATOM   16132 C  CG    . PRO A 1 3684 ? 210.311 183.118 237.822 1.00 11.12 ? 3684 PRO A CG    1 
ATOM   16133 C  CD    . PRO A 1 3684 ? 209.782 184.428 237.311 1.00 6.59  ? 3684 PRO A CD    1 
ATOM   16134 N  N     . THR A 1 3685 ? 212.347 183.559 234.974 1.00 9.43  ? 3685 THR A N     1 
ATOM   16135 C  CA    . THR A 1 3685 ? 212.948 182.855 233.852 1.00 7.17  ? 3685 THR A CA    1 
ATOM   16136 C  C     . THR A 1 3685 ? 213.573 183.788 232.826 1.00 9.11  ? 3685 THR A C     1 
ATOM   16137 O  O     . THR A 1 3685 ? 214.054 183.313 231.791 1.00 19.79 ? 3685 THR A O     1 
ATOM   16138 C  CB    . THR A 1 3685 ? 211.898 181.971 233.163 1.00 10.39 ? 3685 THR A CB    1 
ATOM   16139 O  OG1   . THR A 1 3685 ? 211.109 182.769 232.274 1.00 14.50 ? 3685 THR A OG1   1 
ATOM   16140 C  CG2   . THR A 1 3685 ? 210.993 181.327 234.194 1.00 13.17 ? 3685 THR A CG2   1 
ATOM   16141 N  N     . VAL A 1 3686 ? 213.580 185.095 233.076 1.00 8.36  ? 3686 VAL A N     1 
ATOM   16142 C  CA    . VAL A 1 3686 ? 214.131 186.039 232.113 1.00 6.67  ? 3686 VAL A CA    1 
ATOM   16143 C  C     . VAL A 1 3686 ? 215.648 185.900 232.069 1.00 7.71  ? 3686 VAL A C     1 
ATOM   16144 O  O     . VAL A 1 3686 ? 216.299 185.655 233.093 1.00 8.79  ? 3686 VAL A O     1 
ATOM   16145 C  CB    . VAL A 1 3686 ? 213.696 187.473 232.458 1.00 8.64  ? 3686 VAL A CB    1 
ATOM   16146 C  CG1   . VAL A 1 3686 ? 214.277 187.910 233.788 1.00 6.63  ? 3686 VAL A CG1   1 
ATOM   16147 C  CG2   . VAL A 1 3686 ? 214.102 188.436 231.352 1.00 9.51  ? 3686 VAL A CG2   1 
ATOM   16148 N  N     . GLU A 1 3687 ? 216.213 186.027 230.872 1.00 10.49 ? 3687 GLU A N     1 
ATOM   16149 C  CA    . GLU A 1 3687 ? 217.652 185.923 230.680 1.00 6.93  ? 3687 GLU A CA    1 
ATOM   16150 C  C     . GLU A 1 3687 ? 218.235 187.317 230.486 1.00 4.73  ? 3687 GLU A C     1 
ATOM   16151 O  O     . GLU A 1 3687 ? 217.742 188.092 229.662 1.00 11.46 ? 3687 GLU A O     1 
ATOM   16152 C  CB    . GLU A 1 3687 ? 217.978 185.044 229.472 1.00 9.19  ? 3687 GLU A CB    1 
ATOM   16153 C  CG    . GLU A 1 3687 ? 217.154 183.774 229.386 1.00 16.00 ? 3687 GLU A CG    1 
ATOM   16154 C  CD    . GLU A 1 3687 ? 217.875 182.564 229.945 1.00 21.51 ? 3687 GLU A CD    1 
ATOM   16155 O  OE1   . GLU A 1 3687 ? 218.933 182.741 230.583 1.00 24.15 ? 3687 GLU A OE1   1 
ATOM   16156 O  OE2   . GLU A 1 3687 ? 217.384 181.436 229.745 1.00 27.88 ? 3687 GLU A OE2   1 
ATOM   16157 N  N     . PHE A 1 3688 ? 219.271 187.632 231.249 1.00 4.23  ? 3688 PHE A N     1 
ATOM   16158 C  CA    . PHE A 1 3688 ? 219.771 188.950 230.901 1.00 4.45  ? 3688 PHE A CA    1 
ATOM   16159 C  C     . PHE A 1 3688 ? 221.077 188.845 230.129 1.00 7.81  ? 3688 PHE A C     1 
ATOM   16160 O  O     . PHE A 1 3688 ? 221.847 187.900 230.335 1.00 8.67  ? 3688 PHE A O     1 
ATOM   16161 C  CB    . PHE A 1 3688 ? 219.984 189.807 232.151 1.00 4.01  ? 3688 PHE A CB    1 
ATOM   16162 C  CG    . PHE A 1 3688 ? 218.734 190.046 232.941 1.00 4.84  ? 3688 PHE A CG    1 
ATOM   16163 C  CD1   . PHE A 1 3688 ? 217.846 191.037 232.566 1.00 3.79  ? 3688 PHE A CD1   1 
ATOM   16164 C  CD2   . PHE A 1 3688 ? 218.452 189.295 234.065 1.00 3.32  ? 3688 PHE A CD2   1 
ATOM   16165 C  CE1   . PHE A 1 3688 ? 216.699 191.263 233.289 1.00 3.43  ? 3688 PHE A CE1   1 
ATOM   16166 C  CE2   . PHE A 1 3688 ? 217.307 189.518 234.795 1.00 2.26  ? 3688 PHE A CE2   1 
ATOM   16167 C  CZ    . PHE A 1 3688 ? 216.431 190.506 234.408 1.00 3.15  ? 3688 PHE A CZ    1 
ATOM   16168 N  N     . PRO A 1 3689 ? 221.336 189.794 229.227 1.00 6.84  ? 3689 PRO A N     1 
ATOM   16169 C  CA    . PRO A 1 3689 ? 222.603 189.780 228.503 1.00 6.14  ? 3689 PRO A CA    1 
ATOM   16170 C  C     . PRO A 1 3689 ? 223.764 190.042 229.443 1.00 4.26  ? 3689 PRO A C     1 
ATOM   16171 O  O     . PRO A 1 3689 ? 223.597 190.675 230.500 1.00 6.26  ? 3689 PRO A O     1 
ATOM   16172 C  CB    . PRO A 1 3689 ? 222.434 190.917 227.479 1.00 5.73  ? 3689 PRO A CB    1 
ATOM   16173 C  CG    . PRO A 1 3689 ? 221.458 191.834 228.122 1.00 5.56  ? 3689 PRO A CG    1 
ATOM   16174 C  CD    . PRO A 1 3689 ? 220.486 190.927 228.822 1.00 5.77  ? 3689 PRO A CD    1 
ATOM   16175 N  N     . PRO A 1 3690 ? 224.963 189.554 229.112 1.00 7.53  ? 3690 PRO A N     1 
ATOM   16176 C  CA    . PRO A 1 3690 ? 226.100 189.700 230.036 1.00 5.38  ? 3690 PRO A CA    1 
ATOM   16177 C  C     . PRO A 1 3690 ? 226.441 191.140 230.381 1.00 3.90  ? 3690 PRO A C     1 
ATOM   16178 O  O     . PRO A 1 3690 ? 226.954 191.396 231.478 1.00 3.32  ? 3690 PRO A O     1 
ATOM   16179 C  CB    . PRO A 1 3690 ? 227.248 189.015 229.282 1.00 5.15  ? 3690 PRO A CB    1 
ATOM   16180 C  CG    . PRO A 1 3690 ? 226.564 188.042 228.382 1.00 6.85  ? 3690 PRO A CG    1 
ATOM   16181 C  CD    . PRO A 1 3690 ? 225.312 188.738 227.938 1.00 6.71  ? 3690 PRO A CD    1 
ATOM   16182 N  N     . ASP A 1 3691 ? 226.186 192.086 229.475 1.00 4.14  ? 3691 ASP A N     1 
ATOM   16183 C  CA    . ASP A 1 3691 ? 226.492 193.485 229.763 1.00 5.85  ? 3691 ASP A CA    1 
ATOM   16184 C  C     . ASP A 1 3691 ? 225.633 194.020 230.905 1.00 5.19  ? 3691 ASP A C     1 
ATOM   16185 O  O     . ASP A 1 3691 ? 226.121 194.759 231.768 1.00 5.77  ? 3691 ASP A O     1 
ATOM   16186 C  CB    . ASP A 1 3691 ? 226.331 194.330 228.493 1.00 7.52  ? 3691 ASP A CB    1 
ATOM   16187 C  CG    . ASP A 1 3691 ? 224.912 194.333 227.957 1.00 16.88 ? 3691 ASP A CG    1 
ATOM   16188 O  OD1   . ASP A 1 3691 ? 224.039 193.650 228.533 1.00 17.34 ? 3691 ASP A OD1   1 
ATOM   16189 O  OD2   . ASP A 1 3691 ? 224.667 195.023 226.946 1.00 24.80 ? 3691 ASP A OD2   1 
ATOM   16190 N  N     . LEU A 1 3692 ? 224.349 193.656 230.929 1.00 5.18  ? 3692 LEU A N     1 
ATOM   16191 C  CA    . LEU A 1 3692 ? 223.487 194.070 232.032 1.00 2.20  ? 3692 LEU A CA    1 
ATOM   16192 C  C     . LEU A 1 3692 ? 223.864 193.361 233.328 1.00 1.86  ? 3692 LEU A C     1 
ATOM   16193 O  O     . LEU A 1 3692 ? 223.803 193.959 234.408 1.00 2.11  ? 3692 LEU A O     1 
ATOM   16194 C  CB    . LEU A 1 3692 ? 222.021 193.812 231.688 1.00 4.36  ? 3692 LEU A CB    1 
ATOM   16195 C  CG    . LEU A 1 3692 ? 220.982 194.412 232.642 1.00 3.42  ? 3692 LEU A CG    1 
ATOM   16196 C  CD1   . LEU A 1 3692 ? 221.169 195.914 232.797 1.00 0.68  ? 3692 LEU A CD1   1 
ATOM   16197 C  CD2   . LEU A 1 3692 ? 219.572 194.095 232.181 1.00 2.24  ? 3692 LEU A CD2   1 
ATOM   16198 N  N     . CYS A 1 3693 ? 224.255 192.086 233.238 1.00 3.29  ? 3693 CYS A N     1 
ATOM   16199 C  CA    . CYS A 1 3693 ? 224.616 191.334 234.433 1.00 2.12  ? 3693 CYS A CA    1 
ATOM   16200 C  C     . CYS A 1 3693 ? 225.824 191.935 235.135 1.00 2.02  ? 3693 CYS A C     1 
ATOM   16201 O  O     . CYS A 1 3693 ? 225.951 191.822 236.358 1.00 3.12  ? 3693 CYS A O     1 
ATOM   16202 C  CB    . CYS A 1 3693 ? 224.886 189.872 234.071 1.00 1.69  ? 3693 CYS A CB    1 
ATOM   16203 S  SG    . CYS A 1 3693 ? 223.469 188.998 233.381 1.00 6.74  ? 3693 CYS A SG    1 
ATOM   16204 N  N     . SER A 1 3694 ? 226.723 192.571 234.381 1.00 1.73  ? 3694 SER A N     1 
ATOM   16205 C  CA    . SER A 1 3694 ? 227.898 193.191 234.977 1.00 1.04  ? 3694 SER A CA    1 
ATOM   16206 C  C     . SER A 1 3694 ? 227.584 194.519 235.654 1.00 0.97  ? 3694 SER A C     1 
ATOM   16207 O  O     . SER A 1 3694 ? 228.383 194.985 236.471 1.00 1.14  ? 3694 SER A O     1 
ATOM   16208 C  CB    . SER A 1 3694 ? 228.977 193.395 233.910 1.00 1.33  ? 3694 SER A CB    1 
ATOM   16209 O  OG    . SER A 1 3694 ? 228.517 194.239 232.872 1.00 4.22  ? 3694 SER A OG    1 
ATOM   16210 N  N     . ARG A 1 3695 ? 226.448 195.136 235.342 1.00 1.30  ? 3695 ARG A N     1 
ATOM   16211 C  CA    . ARG A 1 3695 ? 226.122 196.463 235.849 1.00 0.99  ? 3695 ARG A CA    1 
ATOM   16212 C  C     . ARG A 1 3695 ? 225.196 196.444 237.055 1.00 0.80  ? 3695 ARG A C     1 
ATOM   16213 O  O     . ARG A 1 3695 ? 224.954 197.501 237.645 1.00 0.54  ? 3695 ARG A O     1 
ATOM   16214 C  CB    . ARG A 1 3695 ? 225.491 197.304 234.738 1.00 1.22  ? 3695 ARG A CB    1 
ATOM   16215 C  CG    . ARG A 1 3695 ? 226.393 197.535 233.550 1.00 1.41  ? 3695 ARG A CG    1 
ATOM   16216 C  CD    . ARG A 1 3695 ? 225.684 198.314 232.462 1.00 1.22  ? 3695 ARG A CD    1 
ATOM   16217 N  NE    . ARG A 1 3695 ? 226.051 197.842 231.133 1.00 2.53  ? 3695 ARG A NE    1 
ATOM   16218 C  CZ    . ARG A 1 3695 ? 226.638 198.590 230.211 1.00 2.65  ? 3695 ARG A CZ    1 
ATOM   16219 N  NH1   . ARG A 1 3695 ? 226.956 199.853 230.445 1.00 2.34  ? 3695 ARG A NH1   1 
ATOM   16220 N  NH2   . ARG A 1 3695 ? 226.921 198.057 229.027 1.00 2.69  ? 3695 ARG A NH2   1 
ATOM   16221 N  N     . VAL A 1 3696 ? 224.676 195.280 237.448 1.00 1.00  ? 3696 VAL A N     1 
ATOM   16222 C  CA    . VAL A 1 3696 ? 223.654 195.204 238.480 1.00 0.81  ? 3696 VAL A CA    1 
ATOM   16223 C  C     . VAL A 1 3696 ? 224.070 194.206 239.549 1.00 0.32  ? 3696 VAL A C     1 
ATOM   16224 O  O     . VAL A 1 3696 ? 224.978 193.393 239.362 1.00 5.18  ? 3696 VAL A O     1 
ATOM   16225 C  CB    . VAL A 1 3696 ? 222.270 194.817 237.911 1.00 0.63  ? 3696 VAL A CB    1 
ATOM   16226 C  CG1   . VAL A 1 3696 ? 221.797 195.847 236.897 1.00 0.27  ? 3696 VAL A CG1   1 
ATOM   16227 C  CG2   . VAL A 1 3696 ? 222.315 193.425 237.302 1.00 0.41  ? 3696 VAL A CG2   1 
ATOM   16228 N  N     . THR A 1 3697 ? 223.393 194.289 240.687 1.00 0.25  ? 3697 THR A N     1 
ATOM   16229 C  CA    . THR A 1 3697 ? 223.501 193.315 241.767 1.00 0.24  ? 3697 THR A CA    1 
ATOM   16230 C  C     . THR A 1 3697 ? 222.219 192.493 241.764 1.00 0.11  ? 3697 THR A C     1 
ATOM   16231 O  O     . THR A 1 3697 ? 221.138 193.022 242.036 1.00 0.14  ? 3697 THR A O     1 
ATOM   16232 C  CB    . THR A 1 3697 ? 223.708 194.004 243.116 1.00 0.42  ? 3697 THR A CB    1 
ATOM   16233 O  OG1   . THR A 1 3697 ? 224.953 194.710 243.113 1.00 1.23  ? 3697 THR A OG1   1 
ATOM   16234 C  CG2   . THR A 1 3697 ? 223.707 192.984 244.245 1.00 1.11  ? 3697 THR A CG2   1 
ATOM   16235 N  N     . PHE A 1 3698 ? 222.331 191.209 241.444 1.00 0.13  ? 3698 PHE A N     1 
ATOM   16236 C  CA    . PHE A 1 3698 ? 221.146 190.363 241.392 1.00 0.16  ? 3698 PHE A CA    1 
ATOM   16237 C  C     . PHE A 1 3698 ? 220.680 190.025 242.801 1.00 0.13  ? 3698 PHE A C     1 
ATOM   16238 O  O     . PHE A 1 3698 ? 221.466 189.576 243.638 1.00 0.55  ? 3698 PHE A O     1 
ATOM   16239 C  CB    . PHE A 1 3698 ? 221.431 189.089 240.600 1.00 0.12  ? 3698 PHE A CB    1 
ATOM   16240 C  CG    . PHE A 1 3698 ? 221.384 189.284 239.115 1.00 0.22  ? 3698 PHE A CG    1 
ATOM   16241 C  CD1   . PHE A 1 3698 ? 220.180 189.500 238.472 1.00 0.16  ? 3698 PHE A CD1   1 
ATOM   16242 C  CD2   . PHE A 1 3698 ? 222.545 189.257 238.364 1.00 0.54  ? 3698 PHE A CD2   1 
ATOM   16243 C  CE1   . PHE A 1 3698 ? 220.133 189.683 237.106 1.00 0.21  ? 3698 PHE A CE1   1 
ATOM   16244 C  CE2   . PHE A 1 3698 ? 222.504 189.441 236.997 1.00 0.82  ? 3698 PHE A CE2   1 
ATOM   16245 C  CZ    . PHE A 1 3698 ? 221.297 189.655 236.370 1.00 0.53  ? 3698 PHE A CZ    1 
ATOM   16246 N  N     . VAL A 1 3699 ? 219.398 190.260 243.063 1.00 0.10  ? 3699 VAL A N     1 
ATOM   16247 C  CA    . VAL A 1 3699 ? 218.771 189.960 244.347 1.00 0.17  ? 3699 VAL A CA    1 
ATOM   16248 C  C     . VAL A 1 3699 ? 217.520 189.153 244.024 1.00 0.14  ? 3699 VAL A C     1 
ATOM   16249 O  O     . VAL A 1 3699 ? 216.484 189.720 243.664 1.00 0.19  ? 3699 VAL A O     1 
ATOM   16250 C  CB    . VAL A 1 3699 ? 218.430 191.224 245.144 1.00 0.18  ? 3699 VAL A CB    1 
ATOM   16251 C  CG1   . VAL A 1 3699 ? 217.780 190.856 246.457 1.00 0.13  ? 3699 VAL A CG1   1 
ATOM   16252 C  CG2   . VAL A 1 3699 ? 219.675 192.063 245.381 1.00 0.14  ? 3699 VAL A CG2   1 
ATOM   16253 N  N     . ASN A 1 3700 ? 217.611 187.834 244.146 1.00 0.20  ? 3700 ASN A N     1 
ATOM   16254 C  CA    . ASN A 1 3700 ? 216.563 186.927 243.695 1.00 0.65  ? 3700 ASN A CA    1 
ATOM   16255 C  C     . ASN A 1 3700 ? 215.704 186.506 244.880 1.00 0.44  ? 3700 ASN A C     1 
ATOM   16256 O  O     . ASN A 1 3700 ? 216.215 185.966 245.864 1.00 0.31  ? 3700 ASN A O     1 
ATOM   16257 C  CB    . ASN A 1 3700 ? 217.171 185.709 243.001 1.00 0.75  ? 3700 ASN A CB    1 
ATOM   16258 C  CG    . ASN A 1 3700 ? 216.175 184.971 242.135 1.00 0.62  ? 3700 ASN A CG    1 
ATOM   16259 O  OD1   . ASN A 1 3700 ? 214.979 185.251 242.165 1.00 1.01  ? 3700 ASN A OD1   1 
ATOM   16260 N  ND2   . ASN A 1 3700 ? 216.667 184.027 241.347 1.00 0.94  ? 3700 ASN A ND2   1 
ATOM   16261 N  N     . PHE A 1 3701 ? 214.400 186.752 244.777 1.00 1.02  ? 3701 PHE A N     1 
ATOM   16262 C  CA    . PHE A 1 3701 ? 213.441 186.388 245.817 1.00 0.91  ? 3701 PHE A CA    1 
ATOM   16263 C  C     . PHE A 1 3701 ? 212.775 185.085 245.391 1.00 1.76  ? 3701 PHE A C     1 
ATOM   16264 O  O     . PHE A 1 3701 ? 211.752 185.081 244.706 1.00 5.53  ? 3701 PHE A O     1 
ATOM   16265 C  CB    . PHE A 1 3701 ? 212.424 187.500 246.035 1.00 0.87  ? 3701 PHE A CB    1 
ATOM   16266 C  CG    . PHE A 1 3701 ? 212.946 188.651 246.842 1.00 0.78  ? 3701 PHE A CG    1 
ATOM   16267 C  CD1   . PHE A 1 3701 ? 213.792 189.590 246.271 1.00 0.33  ? 3701 PHE A CD1   1 
ATOM   16268 C  CD2   . PHE A 1 3701 ? 212.592 188.799 248.172 1.00 0.46  ? 3701 PHE A CD2   1 
ATOM   16269 C  CE1   . PHE A 1 3701 ? 214.273 190.648 247.010 1.00 0.23  ? 3701 PHE A CE1   1 
ATOM   16270 C  CE2   . PHE A 1 3701 ? 213.071 189.859 248.917 1.00 0.26  ? 3701 PHE A CE2   1 
ATOM   16271 C  CZ    . PHE A 1 3701 ? 213.909 190.785 248.336 1.00 0.25  ? 3701 PHE A CZ    1 
ATOM   16272 N  N     . THR A 1 3702 ? 213.370 183.969 245.797 1.00 2.64  ? 3702 THR A N     1 
ATOM   16273 C  CA    . THR A 1 3702 ? 212.835 182.650 245.503 1.00 1.87  ? 3702 THR A CA    1 
ATOM   16274 C  C     . THR A 1 3702 ? 212.153 182.083 246.738 1.00 3.06  ? 3702 THR A C     1 
ATOM   16275 O  O     . THR A 1 3702 ? 212.605 182.303 247.866 1.00 4.80  ? 3702 THR A O     1 
ATOM   16276 C  CB    . THR A 1 3702 ? 213.934 181.695 245.030 1.00 3.67  ? 3702 THR A CB    1 
ATOM   16277 O  OG1   . THR A 1 3702 ? 214.766 181.331 246.137 1.00 2.60  ? 3702 THR A OG1   1 
ATOM   16278 C  CG2   . THR A 1 3702 ? 214.779 182.346 243.950 1.00 2.15  ? 3702 THR A CG2   1 
ATOM   16279 N  N     . VAL A 1 3703 ? 211.060 181.356 246.520 1.00 3.45  ? 3703 VAL A N     1 
ATOM   16280 C  CA    . VAL A 1 3703 ? 210.336 180.743 247.623 1.00 2.05  ? 3703 VAL A CA    1 
ATOM   16281 C  C     . VAL A 1 3703 ? 211.141 179.568 248.162 1.00 1.10  ? 3703 VAL A C     1 
ATOM   16282 O  O     . VAL A 1 3703 ? 211.545 178.672 247.409 1.00 1.58  ? 3703 VAL A O     1 
ATOM   16283 C  CB    . VAL A 1 3703 ? 208.937 180.301 247.169 1.00 1.64  ? 3703 VAL A CB    1 
ATOM   16284 C  CG1   . VAL A 1 3703 ? 208.244 179.504 248.263 1.00 1.68  ? 3703 VAL A CG1   1 
ATOM   16285 C  CG2   . VAL A 1 3703 ? 208.108 181.505 246.773 1.00 1.33  ? 3703 VAL A CG2   1 
ATOM   16286 N  N     . THR A 1 3704 ? 211.384 179.572 249.465 1.00 2.23  ? 3704 THR A N     1 
ATOM   16287 C  CA    . THR A 1 3704 ? 212.052 178.472 250.140 1.00 2.53  ? 3704 THR A CA    1 
ATOM   16288 C  C     . THR A 1 3704 ? 211.022 177.572 250.809 1.00 2.34  ? 3704 THR A C     1 
ATOM   16289 O  O     . THR A 1 3704 ? 209.902 177.988 251.114 1.00 3.22  ? 3704 THR A O     1 
ATOM   16290 C  CB    . THR A 1 3704 ? 213.056 178.987 251.176 1.00 4.95  ? 3704 THR A CB    1 
ATOM   16291 O  OG1   . THR A 1 3704 ? 212.357 179.463 252.332 1.00 5.10  ? 3704 THR A OG1   1 
ATOM   16292 C  CG2   . THR A 1 3704 ? 213.887 180.116 250.593 1.00 2.40  ? 3704 THR A CG2   1 
ATOM   16293 N  N     . ARG A 1 3705 ? 211.418 176.316 251.029 1.00 2.59  ? 3705 ARG A N     1 
ATOM   16294 C  CA    . ARG A 1 3705 ? 210.505 175.350 251.630 1.00 2.90  ? 3705 ARG A CA    1 
ATOM   16295 C  C     . ARG A 1 3705 ? 210.110 175.763 253.041 1.00 3.73  ? 3705 ARG A C     1 
ATOM   16296 O  O     . ARG A 1 3705 ? 208.944 175.626 253.431 1.00 5.71  ? 3705 ARG A O     1 
ATOM   16297 C  CB    . ARG A 1 3705 ? 211.139 173.960 251.633 1.00 3.62  ? 3705 ARG A CB    1 
ATOM   16298 C  CG    . ARG A 1 3705 ? 211.176 173.307 250.269 1.00 4.74  ? 3705 ARG A CG    1 
ATOM   16299 C  CD    . ARG A 1 3705 ? 211.971 172.017 250.284 1.00 6.93  ? 3705 ARG A CD    1 
ATOM   16300 N  NE    . ARG A 1 3705 ? 211.849 171.287 249.026 1.00 6.26  ? 3705 ARG A NE    1 
ATOM   16301 C  CZ    . ARG A 1 3705 ? 210.765 170.623 248.644 1.00 7.96  ? 3705 ARG A CZ    1 
ATOM   16302 N  NH1   . ARG A 1 3705 ? 209.689 170.556 249.410 1.00 4.14  ? 3705 ARG A NH1   1 
ATOM   16303 N  NH2   . ARG A 1 3705 ? 210.766 170.004 247.467 1.00 5.76  ? 3705 ARG A NH2   1 
ATOM   16304 N  N     . SER A 1 3706 ? 211.067 176.267 253.824 1.00 3.20  ? 3706 SER A N     1 
ATOM   16305 C  CA    . SER A 1 3706 ? 210.763 176.693 255.185 1.00 2.25  ? 3706 SER A CA    1 
ATOM   16306 C  C     . SER A 1 3706 ? 209.815 177.887 255.201 1.00 3.44  ? 3706 SER A C     1 
ATOM   16307 O  O     . SER A 1 3706 ? 208.884 177.934 256.014 1.00 4.50  ? 3706 SER A O     1 
ATOM   16308 C  CB    . SER A 1 3706 ? 212.054 177.024 255.931 1.00 4.37  ? 3706 SER A CB    1 
ATOM   16309 O  OG    . SER A 1 3706 ? 212.719 178.121 255.335 1.00 9.37  ? 3706 SER A OG    1 
ATOM   16310 N  N     . SER A 1 3707 ? 210.041 178.865 254.322 1.00 2.96  ? 3707 SER A N     1 
ATOM   16311 C  CA    . SER A 1 3707 ? 209.190 180.051 254.307 1.00 2.58  ? 3707 SER A CA    1 
ATOM   16312 C  C     . SER A 1 3707 ? 207.764 179.706 253.903 1.00 3.31  ? 3707 SER A C     1 
ATOM   16313 O  O     . SER A 1 3707 ? 206.804 180.228 254.481 1.00 5.91  ? 3707 SER A O     1 
ATOM   16314 C  CB    . SER A 1 3707 ? 209.774 181.111 253.373 1.00 3.56  ? 3707 SER A CB    1 
ATOM   16315 O  OG    . SER A 1 3707 ? 209.867 180.634 252.044 1.00 9.39  ? 3707 SER A OG    1 
ATOM   16316 N  N     . LEU A 1 3708 ? 207.604 178.832 252.908 1.00 4.16  ? 3708 LEU A N     1 
ATOM   16317 C  CA    . LEU A 1 3708 ? 206.266 178.414 252.503 1.00 1.85  ? 3708 LEU A CA    1 
ATOM   16318 C  C     . LEU A 1 3708 ? 205.586 177.601 253.598 1.00 1.88  ? 3708 LEU A C     1 
ATOM   16319 O  O     . LEU A 1 3708 ? 204.372 177.719 253.800 1.00 2.04  ? 3708 LEU A O     1 
ATOM   16320 C  CB    . LEU A 1 3708 ? 206.339 177.621 251.201 1.00 2.52  ? 3708 LEU A CB    1 
ATOM   16321 C  CG    . LEU A 1 3708 ? 204.997 177.255 250.570 1.00 1.75  ? 3708 LEU A CG    1 
ATOM   16322 C  CD1   . LEU A 1 3708 ? 204.098 178.474 250.460 1.00 2.41  ? 3708 LEU A CD1   1 
ATOM   16323 C  CD2   . LEU A 1 3708 ? 205.222 176.636 249.214 1.00 0.99  ? 3708 LEU A CD2   1 
ATOM   16324 N  N     . GLN A 1 3709 ? 206.349 176.770 254.312 1.00 2.17  ? 3709 GLN A N     1 
ATOM   16325 C  CA    . GLN A 1 3709 ? 205.781 176.032 255.436 1.00 2.21  ? 3709 GLN A CA    1 
ATOM   16326 C  C     . GLN A 1 3709 ? 205.268 176.978 256.512 1.00 2.75  ? 3709 GLN A C     1 
ATOM   16327 O  O     . GLN A 1 3709 ? 204.183 176.770 257.065 1.00 7.47  ? 3709 GLN A O     1 
ATOM   16328 C  CB    . GLN A 1 3709 ? 206.817 175.071 256.018 1.00 2.22  ? 3709 GLN A CB    1 
ATOM   16329 C  CG    . GLN A 1 3709 ? 206.909 173.741 255.302 1.00 2.40  ? 3709 GLN A CG    1 
ATOM   16330 C  CD    . GLN A 1 3709 ? 208.280 173.105 255.421 1.00 11.14 ? 3709 GLN A CD    1 
ATOM   16331 O  OE1   . GLN A 1 3709 ? 209.094 173.506 256.254 1.00 13.87 ? 3709 GLN A OE1   1 
ATOM   16332 N  NE2   . GLN A 1 3709 ? 208.540 172.104 254.588 1.00 9.68  ? 3709 GLN A NE2   1 
ATOM   16333 N  N     . SER A 1 3710 ? 206.038 178.025 256.827 1.00 2.88  ? 3710 SER A N     1 
ATOM   16334 C  CA    . SER A 1 3710 ? 205.579 179.014 257.797 1.00 3.07  ? 3710 SER A CA    1 
ATOM   16335 C  C     . SER A 1 3710 ? 204.335 179.736 257.301 1.00 3.78  ? 3710 SER A C     1 
ATOM   16336 O  O     . SER A 1 3710 ? 203.403 179.986 258.073 1.00 6.15  ? 3710 SER A O     1 
ATOM   16337 C  CB    . SER A 1 3710 ? 206.693 180.018 258.096 1.00 4.86  ? 3710 SER A CB    1 
ATOM   16338 O  OG    . SER A 1 3710 ? 207.801 179.394 258.714 1.00 12.56 ? 3710 SER A OG    1 
ATOM   16339 N  N     . GLN A 1 3711 ? 204.307 180.085 256.012 1.00 2.05  ? 3711 GLN A N     1 
ATOM   16340 C  CA    . GLN A 1 3711 ? 203.147 180.773 255.454 1.00 2.65  ? 3711 GLN A CA    1 
ATOM   16341 C  C     . GLN A 1 3711 ? 201.896 179.912 255.541 1.00 2.56  ? 3711 GLN A C     1 
ATOM   16342 O  O     . GLN A 1 3711 ? 200.822 180.399 255.909 1.00 4.07  ? 3711 GLN A O     1 
ATOM   16343 C  CB    . GLN A 1 3711 ? 203.415 181.162 254.000 1.00 3.51  ? 3711 GLN A CB    1 
ATOM   16344 C  CG    . GLN A 1 3711 ? 204.354 182.332 253.819 1.00 4.84  ? 3711 GLN A CG    1 
ATOM   16345 C  CD    . GLN A 1 3711 ? 204.671 182.593 252.361 1.00 10.11 ? 3711 GLN A CD    1 
ATOM   16346 O  OE1   . GLN A 1 3711 ? 205.835 182.685 251.973 1.00 12.56 ? 3711 GLN A OE1   1 
ATOM   16347 N  NE2   . GLN A 1 3711 ? 203.632 182.704 251.542 1.00 10.04 ? 3711 GLN A NE2   1 
ATOM   16348 N  N     . CYS A 1 3712 ? 202.014 178.628 255.203 1.00 3.19  ? 3712 CYS A N     1 
ATOM   16349 C  CA    . CYS A 1 3712 ? 200.854 177.748 255.212 1.00 2.49  ? 3712 CYS A CA    1 
ATOM   16350 C  C     . CYS A 1 3712 ? 200.454 177.342 256.622 1.00 2.63  ? 3712 CYS A C     1 
ATOM   16351 O  O     . CYS A 1 3712 ? 199.263 177.165 256.893 1.00 5.65  ? 3712 CYS A O     1 
ATOM   16352 C  CB    . CYS A 1 3712 ? 201.130 176.517 254.352 1.00 1.96  ? 3712 CYS A CB    1 
ATOM   16353 S  SG    . CYS A 1 3712 ? 201.490 176.913 252.627 1.00 2.49  ? 3712 CYS A SG    1 
ATOM   16354 N  N     . LEU A 1 3713 ? 201.425 177.191 257.527 1.00 2.18  ? 3713 LEU A N     1 
ATOM   16355 C  CA    . LEU A 1 3713 ? 201.088 176.930 258.922 1.00 3.10  ? 3713 LEU A CA    1 
ATOM   16356 C  C     . LEU A 1 3713 ? 200.334 178.104 259.530 1.00 3.26  ? 3713 LEU A C     1 
ATOM   16357 O  O     . LEU A 1 3713 ? 199.369 177.915 260.280 1.00 4.68  ? 3713 LEU A O     1 
ATOM   16358 C  CB    . LEU A 1 3713 ? 202.354 176.633 259.725 1.00 4.27  ? 3713 LEU A CB    1 
ATOM   16359 C  CG    . LEU A 1 3713 ? 202.161 176.496 261.236 1.00 3.12  ? 3713 LEU A CG    1 
ATOM   16360 C  CD1   . LEU A 1 3713 ? 201.385 175.232 261.557 1.00 3.80  ? 3713 LEU A CD1   1 
ATOM   16361 C  CD2   . LEU A 1 3713 ? 203.495 176.505 261.959 1.00 7.11  ? 3713 LEU A CD2   1 
ATOM   16362 N  N     . ASN A 1 3714 ? 200.759 179.331 259.216 1.00 3.29  ? 3714 ASN A N     1 
ATOM   16363 C  CA    . ASN A 1 3714 ? 200.066 180.505 259.734 1.00 5.69  ? 3714 ASN A CA    1 
ATOM   16364 C  C     . ASN A 1 3714 ? 198.668 180.628 259.147 1.00 5.50  ? 3714 ASN A C     1 
ATOM   16365 O  O     . ASN A 1 3714 ? 197.723 180.995 259.854 1.00 7.35  ? 3714 ASN A O     1 
ATOM   16366 C  CB    . ASN A 1 3714 ? 200.881 181.766 259.445 1.00 6.78  ? 3714 ASN A CB    1 
ATOM   16367 C  CG    . ASN A 1 3714 ? 202.117 181.875 260.314 1.00 10.38 ? 3714 ASN A CG    1 
ATOM   16368 O  OD1   . ASN A 1 3714 ? 202.313 181.089 261.241 1.00 10.34 ? 3714 ASN A OD1   1 
ATOM   16369 N  ND2   . ASN A 1 3714 ? 202.962 182.855 260.018 1.00 15.05 ? 3714 ASN A ND2   1 
ATOM   16370 N  N     . GLU A 1 3715 ? 198.516 180.334 257.854 1.00 5.45  ? 3715 GLU A N     1 
ATOM   16371 C  CA    . GLU A 1 3715 ? 197.219 180.513 257.207 1.00 6.76  ? 3715 GLU A CA    1 
ATOM   16372 C  C     . GLU A 1 3715 ? 196.180 179.535 257.749 1.00 6.55  ? 3715 GLU A C     1 
ATOM   16373 O  O     . GLU A 1 3715 ? 195.028 179.918 257.978 1.00 9.06  ? 3715 GLU A O     1 
ATOM   16374 C  CB    . GLU A 1 3715 ? 197.360 180.373 255.691 1.00 6.71  ? 3715 GLU A CB    1 
ATOM   16375 C  CG    . GLU A 1 3715 ? 196.062 180.590 254.936 1.00 12.65 ? 3715 GLU A CG    1 
ATOM   16376 C  CD    . GLU A 1 3715 ? 195.532 182.010 255.064 1.00 26.30 ? 3715 GLU A CD    1 
ATOM   16377 O  OE1   . GLU A 1 3715 ? 196.341 182.935 255.293 1.00 31.23 ? 3715 GLU A OE1   1 
ATOM   16378 O  OE2   . GLU A 1 3715 ? 194.303 182.201 254.943 1.00 29.16 ? 3715 GLU A OE2   1 
ATOM   16379 N  N     . VAL A 1 3716 ? 196.560 178.273 257.954 1.00 4.29  ? 3716 VAL A N     1 
ATOM   16380 C  CA    . VAL A 1 3716 ? 195.615 177.310 258.513 1.00 6.05  ? 3716 VAL A CA    1 
ATOM   16381 C  C     . VAL A 1 3716 ? 195.297 177.654 259.964 1.00 9.32  ? 3716 VAL A C     1 
ATOM   16382 O  O     . VAL A 1 3716 ? 194.165 177.471 260.425 1.00 10.30 ? 3716 VAL A O     1 
ATOM   16383 C  CB    . VAL A 1 3716 ? 196.143 175.868 258.364 1.00 3.53  ? 3716 VAL A CB    1 
ATOM   16384 C  CG1   . VAL A 1 3716 ? 197.432 175.660 259.136 1.00 3.88  ? 3716 VAL A CG1   1 
ATOM   16385 C  CG2   . VAL A 1 3716 ? 195.083 174.868 258.802 1.00 4.49  ? 3716 VAL A CG2   1 
ATOM   16386 N  N     . LEU A 1 3717 ? 196.286 178.168 260.702 1.00 6.09  ? 3717 LEU A N     1 
ATOM   16387 C  CA    . LEU A 1 3717 ? 196.033 178.621 262.064 1.00 5.21  ? 3717 LEU A CA    1 
ATOM   16388 C  C     . LEU A 1 3717 ? 195.023 179.761 262.083 1.00 7.74  ? 3717 LEU A C     1 
ATOM   16389 O  O     . LEU A 1 3717 ? 194.144 179.807 262.949 1.00 9.49  ? 3717 LEU A O     1 
ATOM   16390 C  CB    . LEU A 1 3717 ? 197.343 179.049 262.722 1.00 7.44  ? 3717 LEU A CB    1 
ATOM   16391 C  CG    . LEU A 1 3717 ? 197.461 178.865 264.235 1.00 13.63 ? 3717 LEU A CG    1 
ATOM   16392 C  CD1   . LEU A 1 3717 ? 197.570 177.395 264.597 1.00 7.91  ? 3717 LEU A CD1   1 
ATOM   16393 C  CD2   . LEU A 1 3717 ? 198.647 179.649 264.776 1.00 13.29 ? 3717 LEU A CD2   1 
ATOM   16394 N  N     . LYS A 1 3718 ? 195.137 180.689 261.132 1.00 8.34  ? 3718 LYS A N     1 
ATOM   16395 C  CA    . LYS A 1 3718 ? 194.177 181.781 261.040 1.00 9.12  ? 3718 LYS A CA    1 
ATOM   16396 C  C     . LYS A 1 3718 ? 192.776 181.265 260.728 1.00 12.42 ? 3718 LYS A C     1 
ATOM   16397 O  O     . LYS A 1 3718 ? 191.788 181.753 261.283 1.00 12.04 ? 3718 LYS A O     1 
ATOM   16398 C  CB    . LYS A 1 3718 ? 194.631 182.782 259.979 1.00 8.50  ? 3718 LYS A CB    1 
ATOM   16399 C  CG    . LYS A 1 3718 ? 193.731 183.990 259.831 1.00 12.40 ? 3718 LYS A CG    1 
ATOM   16400 C  CD    . LYS A 1 3718 ? 193.781 184.867 261.070 1.00 19.45 ? 3718 LYS A CD    1 
ATOM   16401 C  CE    . LYS A 1 3718 ? 192.868 186.072 260.927 1.00 24.73 ? 3718 LYS A CE    1 
ATOM   16402 N  NZ    . LYS A 1 3718 ? 193.342 186.995 259.859 1.00 25.35 ? 3718 LYS A NZ    1 
ATOM   16403 N  N     . ALA A 1 3719 ? 192.673 180.281 259.834 1.00 10.46 ? 3719 ALA A N     1 
ATOM   16404 C  CA    . ALA A 1 3719 ? 191.371 179.755 259.447 1.00 7.88  ? 3719 ALA A CA    1 
ATOM   16405 C  C     . ALA A 1 3719 ? 190.768 178.862 260.528 1.00 11.19 ? 3719 ALA A C     1 
ATOM   16406 O  O     . ALA A 1 3719 ? 189.565 178.939 260.796 1.00 14.60 ? 3719 ALA A O     1 
ATOM   16407 C  CB    . ALA A 1 3719 ? 191.487 178.983 258.133 1.00 8.42  ? 3719 ALA A CB    1 
ATOM   16408 N  N     . GLU A 1 3720 ? 191.580 178.016 261.155 1.00 15.44 ? 3720 GLU A N     1 
ATOM   16409 C  CA    . GLU A 1 3720 ? 191.079 176.974 262.044 1.00 10.05 ? 3720 GLU A CA    1 
ATOM   16410 C  C     . GLU A 1 3720 ? 191.068 177.373 263.513 1.00 11.07 ? 3720 GLU A C     1 
ATOM   16411 O  O     . GLU A 1 3720 ? 190.140 177.005 264.237 1.00 18.09 ? 3720 GLU A O     1 
ATOM   16412 C  CB    . GLU A 1 3720 ? 191.905 175.698 261.872 1.00 9.63  ? 3720 GLU A CB    1 
ATOM   16413 C  CG    . GLU A 1 3720 ? 191.610 174.971 260.582 1.00 10.37 ? 3720 GLU A CG    1 
ATOM   16414 C  CD    . GLU A 1 3720 ? 190.193 174.442 260.539 1.00 20.42 ? 3720 GLU A CD    1 
ATOM   16415 O  OE1   . GLU A 1 3720 ? 189.905 173.461 261.256 1.00 22.31 ? 3720 GLU A OE1   1 
ATOM   16416 O  OE2   . GLU A 1 3720 ? 189.364 175.017 259.802 1.00 18.54 ? 3720 GLU A OE2   1 
ATOM   16417 N  N     . ARG A 1 3721 ? 192.073 178.113 263.973 1.00 12.92 ? 3721 ARG A N     1 
ATOM   16418 C  CA    . ARG A 1 3721 ? 192.182 178.520 265.374 1.00 11.33 ? 3721 ARG A CA    1 
ATOM   16419 C  C     . ARG A 1 3721 ? 192.403 180.026 265.435 1.00 15.22 ? 3721 ARG A C     1 
ATOM   16420 O  O     . ARG A 1 3721 ? 193.494 180.493 265.779 1.00 17.07 ? 3721 ARG A O     1 
ATOM   16421 C  CB    . ARG A 1 3721 ? 193.314 177.767 266.076 1.00 12.76 ? 3721 ARG A CB    1 
ATOM   16422 C  CG    . ARG A 1 3721 ? 193.258 176.251 265.924 1.00 8.84  ? 3721 ARG A CG    1 
ATOM   16423 C  CD    . ARG A 1 3721 ? 191.987 175.679 266.526 1.00 11.96 ? 3721 ARG A CD    1 
ATOM   16424 N  NE    . ARG A 1 3721 ? 191.943 175.831 267.976 1.00 20.94 ? 3721 ARG A NE    1 
ATOM   16425 C  CZ    . ARG A 1 3721 ? 192.618 175.076 268.831 1.00 25.79 ? 3721 ARG A CZ    1 
ATOM   16426 N  NH1   . ARG A 1 3721 ? 193.384 174.079 268.419 1.00 18.84 ? 3721 ARG A NH1   1 
ATOM   16427 N  NH2   . ARG A 1 3721 ? 192.515 175.321 270.134 1.00 21.06 ? 3721 ARG A NH2   1 
ATOM   16428 N  N     . PRO A 1 3722 ? 191.379 180.817 265.098 1.00 17.52 ? 3722 PRO A N     1 
ATOM   16429 C  CA    . PRO A 1 3722 ? 191.564 182.277 265.076 1.00 13.88 ? 3722 PRO A CA    1 
ATOM   16430 C  C     . PRO A 1 3722 ? 191.958 182.860 266.422 1.00 15.65 ? 3722 PRO A C     1 
ATOM   16431 O  O     . PRO A 1 3722 ? 192.698 183.851 266.464 1.00 21.93 ? 3722 PRO A O     1 
ATOM   16432 C  CB    . PRO A 1 3722 ? 190.195 182.793 264.608 1.00 12.08 ? 3722 PRO A CB    1 
ATOM   16433 C  CG    . PRO A 1 3722 ? 189.241 181.705 264.964 1.00 13.66 ? 3722 PRO A CG    1 
ATOM   16434 C  CD    . PRO A 1 3722 ? 189.996 180.432 264.768 1.00 13.30 ? 3722 PRO A CD    1 
ATOM   16435 N  N     . ASP A 1 3723 ? 191.479 182.282 267.524 1.00 16.27 ? 3723 ASP A N     1 
ATOM   16436 C  CA    . ASP A 1 3723 ? 191.916 182.727 268.843 1.00 12.76 ? 3723 ASP A CA    1 
ATOM   16437 C  C     . ASP A 1 3723 ? 193.397 182.437 269.062 1.00 17.78 ? 3723 ASP A C     1 
ATOM   16438 O  O     . ASP A 1 3723 ? 194.122 183.267 269.624 1.00 20.71 ? 3723 ASP A O     1 
ATOM   16439 C  CB    . ASP A 1 3723 ? 191.064 182.068 269.926 1.00 17.72 ? 3723 ASP A CB    1 
ATOM   16440 C  CG    . ASP A 1 3723 ? 191.278 180.568 270.008 1.00 24.47 ? 3723 ASP A CG    1 
ATOM   16441 O  OD1   . ASP A 1 3723 ? 191.158 179.893 268.966 1.00 18.26 ? 3723 ASP A OD1   1 
ATOM   16442 O  OD2   . ASP A 1 3723 ? 191.567 180.065 271.115 1.00 28.87 ? 3723 ASP A OD2   1 
ATOM   16443 N  N     . VAL A 1 3724 ? 193.863 181.265 268.629 1.00 17.32 ? 3724 VAL A N     1 
ATOM   16444 C  CA    . VAL A 1 3724 ? 195.272 180.915 268.789 1.00 14.28 ? 3724 VAL A CA    1 
ATOM   16445 C  C     . VAL A 1 3724 ? 196.141 181.746 267.855 1.00 17.96 ? 3724 VAL A C     1 
ATOM   16446 O  O     . VAL A 1 3724 ? 197.227 182.201 268.237 1.00 19.22 ? 3724 VAL A O     1 
ATOM   16447 C  CB    . VAL A 1 3724 ? 195.474 179.406 268.563 1.00 12.96 ? 3724 VAL A CB    1 
ATOM   16448 C  CG1   . VAL A 1 3724 ? 196.946 179.034 268.686 1.00 15.38 ? 3724 VAL A CG1   1 
ATOM   16449 C  CG2   . VAL A 1 3724 ? 194.636 178.604 269.546 1.00 16.27 ? 3724 VAL A CG2   1 
ATOM   16450 N  N     . ASP A 1 3725 ? 195.687 181.951 266.616 1.00 18.20 ? 3725 ASP A N     1 
ATOM   16451 C  CA    . ASP A 1 3725 ? 196.478 182.716 265.657 1.00 15.04 ? 3725 ASP A CA    1 
ATOM   16452 C  C     . ASP A 1 3725 ? 196.632 184.164 266.100 1.00 20.02 ? 3725 ASP A C     1 
ATOM   16453 O  O     . ASP A 1 3725 ? 197.715 184.747 265.973 1.00 27.76 ? 3725 ASP A O     1 
ATOM   16454 C  CB    . ASP A 1 3725 ? 195.839 182.645 264.271 1.00 13.06 ? 3725 ASP A CB    1 
ATOM   16455 C  CG    . ASP A 1 3725 ? 196.805 183.025 263.167 1.00 16.88 ? 3725 ASP A CG    1 
ATOM   16456 O  OD1   . ASP A 1 3725 ? 197.799 182.298 262.968 1.00 16.18 ? 3725 ASP A OD1   1 
ATOM   16457 O  OD2   . ASP A 1 3725 ? 196.579 184.056 262.500 1.00 21.68 ? 3725 ASP A OD2   1 
ATOM   16458 N  N     . GLU A 1 3726 ? 195.558 184.761 266.621 1.00 18.89 ? 3726 GLU A N     1 
ATOM   16459 C  CA    . GLU A 1 3726 ? 195.644 186.128 267.122 1.00 18.40 ? 3726 GLU A CA    1 
ATOM   16460 C  C     . GLU A 1 3726 ? 196.601 186.221 268.303 1.00 21.50 ? 3726 GLU A C     1 
ATOM   16461 O  O     . GLU A 1 3726 ? 197.419 187.145 268.378 1.00 24.14 ? 3726 GLU A O     1 
ATOM   16462 C  CB    . GLU A 1 3726 ? 194.254 186.631 267.509 1.00 17.85 ? 3726 GLU A CB    1 
ATOM   16463 C  CG    . GLU A 1 3726 ? 194.218 188.075 267.971 1.00 23.61 ? 3726 GLU A CG    1 
ATOM   16464 C  CD    . GLU A 1 3726 ? 192.814 188.548 268.295 1.00 31.47 ? 3726 GLU A CD    1 
ATOM   16465 O  OE1   . GLU A 1 3726 ? 191.870 187.738 268.178 1.00 32.63 ? 3726 GLU A OE1   1 
ATOM   16466 O  OE2   . GLU A 1 3726 ? 192.653 189.729 268.666 1.00 35.40 ? 3726 GLU A OE2   1 
ATOM   16467 N  N     . LYS A 1 3727 ? 196.525 185.259 269.227 1.00 18.47 ? 3727 LYS A N     1 
ATOM   16468 C  CA    . LYS A 1 3727 ? 197.424 185.253 270.375 1.00 15.56 ? 3727 LYS A CA    1 
ATOM   16469 C  C     . LYS A 1 3727 ? 198.877 185.157 269.932 1.00 20.42 ? 3727 LYS A C     1 
ATOM   16470 O  O     . LYS A 1 3727 ? 199.754 185.813 270.506 1.00 27.89 ? 3727 LYS A O     1 
ATOM   16471 C  CB    . LYS A 1 3727 ? 197.063 184.098 271.311 1.00 16.94 ? 3727 LYS A CB    1 
ATOM   16472 C  CG    . LYS A 1 3727 ? 198.157 183.710 272.289 1.00 21.54 ? 3727 LYS A CG    1 
ATOM   16473 C  CD    . LYS A 1 3727 ? 197.792 182.453 273.067 1.00 21.17 ? 3727 LYS A CD    1 
ATOM   16474 C  CE    . LYS A 1 3727 ? 196.640 182.701 274.022 1.00 18.44 ? 3727 LYS A CE    1 
ATOM   16475 N  NZ    . LYS A 1 3727 ? 196.991 183.716 275.052 1.00 29.49 ? 3727 LYS A NZ    1 
ATOM   16476 N  N     . ARG A 1 3728 ? 199.150 184.344 268.910 1.00 15.40 ? 3728 ARG A N     1 
ATOM   16477 C  CA    . ARG A 1 3728 ? 200.502 184.248 268.374 1.00 17.19 ? 3728 ARG A CA    1 
ATOM   16478 C  C     . ARG A 1 3728 ? 200.965 185.579 267.792 1.00 19.44 ? 3728 ARG A C     1 
ATOM   16479 O  O     . ARG A 1 3728 ? 202.111 185.992 268.000 1.00 20.71 ? 3728 ARG A O     1 
ATOM   16480 C  CB    . ARG A 1 3728 ? 200.562 183.144 267.316 1.00 14.55 ? 3728 ARG A CB    1 
ATOM   16481 C  CG    . ARG A 1 3728 ? 201.857 183.083 266.532 1.00 12.95 ? 3728 ARG A CG    1 
ATOM   16482 C  CD    . ARG A 1 3728 ? 201.662 182.368 265.204 1.00 13.73 ? 3728 ARG A CD    1 
ATOM   16483 N  NE    . ARG A 1 3728 ? 200.915 183.180 264.252 1.00 19.43 ? 3728 ARG A NE    1 
ATOM   16484 C  CZ    . ARG A 1 3728 ? 201.466 184.004 263.372 1.00 21.08 ? 3728 ARG A CZ    1 
ATOM   16485 N  NH1   . ARG A 1 3728 ? 202.778 184.144 263.283 1.00 16.40 ? 3728 ARG A NH1   1 
ATOM   16486 N  NH2   . ARG A 1 3728 ? 200.681 184.707 262.560 1.00 18.20 ? 3728 ARG A NH2   1 
ATOM   16487 N  N     . SER A 1 3729 ? 200.085 186.266 267.057 1.00 21.30 ? 3729 SER A N     1 
ATOM   16488 C  CA    . SER A 1 3729 ? 200.459 187.543 266.455 1.00 17.65 ? 3729 SER A CA    1 
ATOM   16489 C  C     . SER A 1 3729 ? 200.737 188.604 267.516 1.00 20.90 ? 3729 SER A C     1 
ATOM   16490 O  O     . SER A 1 3729 ? 201.699 189.371 267.393 1.00 17.47 ? 3729 SER A O     1 
ATOM   16491 C  CB    . SER A 1 3729 ? 199.361 188.013 265.502 1.00 21.02 ? 3729 SER A CB    1 
ATOM   16492 O  OG    . SER A 1 3729 ? 199.464 189.404 265.254 1.00 29.66 ? 3729 SER A OG    1 
ATOM   16493 N  N     . ASP A 1 3730 ? 199.901 188.672 268.557 1.00 20.23 ? 3730 ASP A N     1 
ATOM   16494 C  CA    . ASP A 1 3730 ? 200.117 189.659 269.609 1.00 17.50 ? 3730 ASP A CA    1 
ATOM   16495 C  C     . ASP A 1 3730 ? 201.428 189.415 270.342 1.00 16.69 ? 3730 ASP A C     1 
ATOM   16496 O  O     . ASP A 1 3730 ? 202.158 190.361 270.654 1.00 17.97 ? 3730 ASP A O     1 
ATOM   16497 C  CB    . ASP A 1 3730 ? 198.947 189.654 270.594 1.00 19.37 ? 3730 ASP A CB    1 
ATOM   16498 C  CG    . ASP A 1 3730 ? 197.603 189.723 269.904 1.00 29.69 ? 3730 ASP A CG    1 
ATOM   16499 O  OD1   . ASP A 1 3730 ? 196.685 188.983 270.315 1.00 32.01 ? 3730 ASP A OD1   1 
ATOM   16500 O  OD2   . ASP A 1 3730 ? 197.465 190.515 268.948 1.00 30.89 ? 3730 ASP A OD2   1 
ATOM   16501 N  N     . LEU A 1 3731 ? 201.742 188.149 270.628 1.00 16.22 ? 3731 LEU A N     1 
ATOM   16502 C  CA    . LEU A 1 3731 ? 202.976 187.839 271.341 1.00 14.72 ? 3731 LEU A CA    1 
ATOM   16503 C  C     . LEU A 1 3731 ? 204.203 188.228 270.528 1.00 14.82 ? 3731 LEU A C     1 
ATOM   16504 O  O     . LEU A 1 3731 ? 205.164 188.781 271.074 1.00 20.55 ? 3731 LEU A O     1 
ATOM   16505 C  CB    . LEU A 1 3731 ? 203.018 186.354 271.691 1.00 14.30 ? 3731 LEU A CB    1 
ATOM   16506 C  CG    . LEU A 1 3731 ? 202.125 185.919 272.852 1.00 17.94 ? 3731 LEU A CG    1 
ATOM   16507 C  CD1   . LEU A 1 3731 ? 202.300 184.443 273.106 1.00 18.88 ? 3731 LEU A CD1   1 
ATOM   16508 C  CD2   . LEU A 1 3731 ? 202.424 186.723 274.108 1.00 18.02 ? 3731 LEU A CD2   1 
ATOM   16509 N  N     . LEU A 1 3732 ? 204.190 187.947 269.224 1.00 10.88 ? 3732 LEU A N     1 
ATOM   16510 C  CA    . LEU A 1 3732 ? 205.326 188.312 268.383 1.00 12.76 ? 3732 LEU A CA    1 
ATOM   16511 C  C     . LEU A 1 3732 ? 205.522 189.821 268.355 1.00 14.89 ? 3732 LEU A C     1 
ATOM   16512 O  O     . LEU A 1 3732 ? 206.659 190.308 268.351 1.00 14.48 ? 3732 LEU A O     1 
ATOM   16513 C  CB    . LEU A 1 3732 ? 205.130 187.762 266.971 1.00 10.24 ? 3732 LEU A CB    1 
ATOM   16514 C  CG    . LEU A 1 3732 ? 205.141 186.238 266.852 1.00 12.57 ? 3732 LEU A CG    1 
ATOM   16515 C  CD1   . LEU A 1 3732 ? 204.800 185.800 265.437 1.00 14.24 ? 3732 LEU A CD1   1 
ATOM   16516 C  CD2   . LEU A 1 3732 ? 206.487 185.677 267.281 1.00 13.58 ? 3732 LEU A CD2   1 
ATOM   16517 N  N     . LYS A 1 3733 ? 204.425 190.579 268.333 1.00 15.03 ? 3733 LYS A N     1 
ATOM   16518 C  CA    . LYS A 1 3733 ? 204.533 192.028 268.448 1.00 15.54 ? 3733 LYS A CA    1 
ATOM   16519 C  C     . LYS A 1 3733 ? 205.039 192.432 269.827 1.00 14.20 ? 3733 LYS A C     1 
ATOM   16520 O  O     . LYS A 1 3733 ? 205.900 193.310 269.944 1.00 14.50 ? 3733 LYS A O     1 
ATOM   16521 C  CB    . LYS A 1 3733 ? 203.181 192.678 268.154 1.00 14.28 ? 3733 LYS A CB    1 
ATOM   16522 C  CG    . LYS A 1 3733 ? 203.199 194.193 268.210 1.00 15.17 ? 3733 LYS A CG    1 
ATOM   16523 C  CD    . LYS A 1 3733 ? 201.869 194.779 267.770 1.00 23.30 ? 3733 LYS A CD    1 
ATOM   16524 C  CE    . LYS A 1 3733 ? 200.790 194.538 268.813 1.00 22.53 ? 3733 LYS A CE    1 
ATOM   16525 N  NZ    . LYS A 1 3733 ? 201.037 195.316 270.057 1.00 21.57 ? 3733 LYS A NZ    1 
ATOM   16526 N  N     . LEU A 1 3734 ? 204.521 191.796 270.881 1.00 11.67 ? 3734 LEU A N     1 
ATOM   16527 C  CA    . LEU A 1 3734 ? 204.976 192.098 272.234 1.00 13.97 ? 3734 LEU A CA    1 
ATOM   16528 C  C     . LEU A 1 3734 ? 206.444 191.731 272.421 1.00 14.10 ? 3734 LEU A C     1 
ATOM   16529 O  O     . LEU A 1 3734 ? 207.224 192.509 272.982 1.00 17.62 ? 3734 LEU A O     1 
ATOM   16530 C  CB    . LEU A 1 3734 ? 204.105 191.367 273.258 1.00 15.89 ? 3734 LEU A CB    1 
ATOM   16531 C  CG    . LEU A 1 3734 ? 202.946 192.126 273.912 1.00 17.52 ? 3734 LEU A CG    1 
ATOM   16532 C  CD1   . LEU A 1 3734 ? 201.962 192.660 272.886 1.00 17.57 ? 3734 LEU A CD1   1 
ATOM   16533 C  CD2   . LEU A 1 3734 ? 202.238 191.231 274.914 1.00 16.76 ? 3734 LEU A CD2   1 
ATOM   16534 N  N     . GLN A 1 3735 ? 206.841 190.543 271.955 1.00 10.73 ? 3735 GLN A N     1 
ATOM   16535 C  CA    . GLN A 1 3735 ? 208.229 190.117 272.118 1.00 14.18 ? 3735 GLN A CA    1 
ATOM   16536 C  C     . GLN A 1 3735 ? 209.174 190.970 271.281 1.00 12.41 ? 3735 GLN A C     1 
ATOM   16537 O  O     . GLN A 1 3735 ? 210.316 191.214 271.683 1.00 14.04 ? 3735 GLN A O     1 
ATOM   16538 C  CB    . GLN A 1 3735 ? 208.376 188.637 271.764 1.00 15.72 ? 3735 GLN A CB    1 
ATOM   16539 C  CG    . GLN A 1 3735 ? 207.655 187.712 272.728 1.00 19.06 ? 3735 GLN A CG    1 
ATOM   16540 C  CD    . GLN A 1 3735 ? 207.792 186.250 272.361 1.00 20.82 ? 3735 GLN A CD    1 
ATOM   16541 O  OE1   . GLN A 1 3735 ? 207.321 185.368 273.078 1.00 25.25 ? 3735 GLN A OE1   1 
ATOM   16542 N  NE2   . GLN A 1 3735 ? 208.443 185.985 271.237 1.00 23.60 ? 3735 GLN A NE2   1 
ATOM   16543 N  N     . GLY A 1 3736 ? 208.721 191.424 270.112 1.00 11.61 ? 3736 GLY A N     1 
ATOM   16544 C  CA    . GLY A 1 3736 ? 209.535 192.332 269.324 1.00 10.65 ? 3736 GLY A CA    1 
ATOM   16545 C  C     . GLY A 1 3736 ? 209.790 193.646 270.036 1.00 17.88 ? 3736 GLY A C     1 
ATOM   16546 O  O     . GLY A 1 3736 ? 210.914 194.154 270.040 1.00 17.66 ? 3736 GLY A O     1 
ATOM   16547 N  N     . GLU A 1 3737 ? 208.751 194.214 270.649 1.00 16.38 ? 3737 GLU A N     1 
ATOM   16548 C  CA    . GLU A 1 3737 ? 208.924 195.436 271.426 1.00 17.00 ? 3737 GLU A CA    1 
ATOM   16549 C  C     . GLU A 1 3737 ? 209.761 195.188 272.673 1.00 15.96 ? 3737 GLU A C     1 
ATOM   16550 O  O     . GLU A 1 3737 ? 210.573 196.033 273.062 1.00 18.21 ? 3737 GLU A O     1 
ATOM   16551 C  CB    . GLU A 1 3737 ? 207.565 196.018 271.805 1.00 17.40 ? 3737 GLU A CB    1 
ATOM   16552 C  CG    . GLU A 1 3737 ? 206.701 196.419 270.627 1.00 16.81 ? 3737 GLU A CG    1 
ATOM   16553 C  CD    . GLU A 1 3737 ? 205.237 196.122 270.865 1.00 24.90 ? 3737 GLU A CD    1 
ATOM   16554 O  OE1   . GLU A 1 3737 ? 204.923 195.480 271.889 1.00 24.07 ? 3737 GLU A OE1   1 
ATOM   16555 O  OE2   . GLU A 1 3737 ? 204.402 196.533 270.033 1.00 26.41 ? 3737 GLU A OE2   1 
ATOM   16556 N  N     . PHE A 1 3738 ? 209.566 194.037 273.322 1.00 15.91 ? 3738 PHE A N     1 
ATOM   16557 C  CA    . PHE A 1 3738 ? 210.291 193.745 274.554 1.00 13.30 ? 3738 PHE A CA    1 
ATOM   16558 C  C     . PHE A 1 3738 ? 211.786 193.606 274.296 1.00 16.56 ? 3738 PHE A C     1 
ATOM   16559 O  O     . PHE A 1 3738 ? 212.604 194.151 275.046 1.00 19.85 ? 3738 PHE A O     1 
ATOM   16560 C  CB    . PHE A 1 3738 ? 209.737 192.474 275.191 1.00 12.98 ? 3738 PHE A CB    1 
ATOM   16561 C  CG    . PHE A 1 3738 ? 208.446 192.679 275.929 1.00 18.03 ? 3738 PHE A CG    1 
ATOM   16562 C  CD1   . PHE A 1 3738 ? 207.667 191.596 276.296 1.00 17.86 ? 3738 PHE A CD1   1 
ATOM   16563 C  CD2   . PHE A 1 3738 ? 208.003 193.953 276.239 1.00 16.68 ? 3738 PHE A CD2   1 
ATOM   16564 C  CE1   . PHE A 1 3738 ? 206.475 191.779 276.965 1.00 18.54 ? 3738 PHE A CE1   1 
ATOM   16565 C  CE2   . PHE A 1 3738 ? 206.812 194.143 276.909 1.00 19.09 ? 3738 PHE A CE2   1 
ATOM   16566 C  CZ    . PHE A 1 3738 ? 206.048 193.054 277.273 1.00 17.27 ? 3738 PHE A CZ    1 
ATOM   16567 N  N     . GLN A 1 3739 ? 212.161 192.886 273.236 1.00 14.54 ? 3739 GLN A N     1 
ATOM   16568 C  CA    . GLN A 1 3739 ? 213.574 192.761 272.889 1.00 16.26 ? 3739 GLN A CA    1 
ATOM   16569 C  C     . GLN A 1 3739 ? 214.149 194.097 272.438 1.00 15.92 ? 3739 GLN A C     1 
ATOM   16570 O  O     . GLN A 1 3739 ? 215.329 194.381 272.668 1.00 14.87 ? 3739 GLN A O     1 
ATOM   16571 C  CB    . GLN A 1 3739 ? 213.761 191.700 271.804 1.00 13.40 ? 3739 GLN A CB    1 
ATOM   16572 C  CG    . GLN A 1 3739 ? 213.391 190.297 272.243 1.00 12.84 ? 3739 GLN A CG    1 
ATOM   16573 C  CD    . GLN A 1 3739 ? 214.340 189.750 273.291 1.00 19.44 ? 3739 GLN A CD    1 
ATOM   16574 O  OE1   . GLN A 1 3739 ? 215.479 190.201 273.410 1.00 21.57 ? 3739 GLN A OE1   1 
ATOM   16575 N  NE2   . GLN A 1 3739 ? 213.872 188.778 274.062 1.00 22.34 ? 3739 GLN A NE2   1 
ATOM   16576 N  N     . LEU A 1 3740 ? 213.331 194.923 271.781 1.00 15.47 ? 3740 LEU A N     1 
ATOM   16577 C  CA    . LEU A 1 3740 ? 213.767 196.267 271.419 1.00 12.36 ? 3740 LEU A CA    1 
ATOM   16578 C  C     . LEU A 1 3740 ? 214.088 197.089 272.661 1.00 17.01 ? 3740 LEU A C     1 
ATOM   16579 O  O     . LEU A 1 3740 ? 215.130 197.749 272.728 1.00 22.04 ? 3740 LEU A O     1 
ATOM   16580 C  CB    . LEU A 1 3740 ? 212.685 196.959 270.590 1.00 12.82 ? 3740 LEU A CB    1 
ATOM   16581 C  CG    . LEU A 1 3740 ? 212.893 198.443 270.277 1.00 14.88 ? 3740 LEU A CG    1 
ATOM   16582 C  CD1   . LEU A 1 3740 ? 214.001 198.660 269.259 1.00 16.79 ? 3740 LEU A CD1   1 
ATOM   16583 C  CD2   . LEU A 1 3740 ? 211.593 199.085 269.822 1.00 11.31 ? 3740 LEU A CD2   1 
ATOM   16584 N  N     . ARG A 1 3741 ? 213.210 197.038 273.663 1.00 14.92 ? 3741 ARG A N     1 
ATOM   16585 C  CA    . ARG A 1 3741 ? 213.398 197.842 274.865 1.00 14.41 ? 3741 ARG A CA    1 
ATOM   16586 C  C     . ARG A 1 3741 ? 214.649 197.426 275.627 1.00 15.85 ? 3741 ARG A C     1 
ATOM   16587 O  O     . ARG A 1 3741 ? 215.379 198.278 276.147 1.00 23.16 ? 3741 ARG A O     1 
ATOM   16588 C  CB    . ARG A 1 3741 ? 212.161 197.736 275.756 1.00 15.89 ? 3741 ARG A CB    1 
ATOM   16589 C  CG    . ARG A 1 3741 ? 212.088 198.778 276.853 1.00 18.49 ? 3741 ARG A CG    1 
ATOM   16590 C  CD    . ARG A 1 3741 ? 212.136 200.189 276.294 1.00 19.24 ? 3741 ARG A CD    1 
ATOM   16591 N  NE    . ARG A 1 3741 ? 212.298 201.174 277.357 1.00 24.46 ? 3741 ARG A NE    1 
ATOM   16592 C  CZ    . ARG A 1 3741 ? 213.361 201.953 277.502 1.00 26.23 ? 3741 ARG A CZ    1 
ATOM   16593 N  NH1   . ARG A 1 3741 ? 214.383 201.893 276.665 1.00 27.26 ? 3741 ARG A NH1   1 
ATOM   16594 N  NH2   . ARG A 1 3741 ? 213.402 202.810 278.518 1.00 23.03 ? 3741 ARG A NH2   1 
ATOM   16595 N  N     . LEU A 1 3742 ? 214.909 196.121 275.710 1.00 14.02 ? 3742 LEU A N     1 
ATOM   16596 C  CA    . LEU A 1 3742 ? 216.097 195.645 276.412 1.00 13.85 ? 3742 LEU A CA    1 
ATOM   16597 C  C     . LEU A 1 3742 ? 217.371 196.142 275.740 1.00 16.70 ? 3742 LEU A C     1 
ATOM   16598 O  O     . LEU A 1 3742 ? 218.356 196.462 276.418 1.00 19.57 ? 3742 LEU A O     1 
ATOM   16599 C  CB    . LEU A 1 3742 ? 216.084 194.120 276.487 1.00 11.59 ? 3742 LEU A CB    1 
ATOM   16600 C  CG    . LEU A 1 3742 ? 215.145 193.495 277.523 1.00 17.75 ? 3742 LEU A CG    1 
ATOM   16601 C  CD1   . LEU A 1 3742 ? 215.527 192.048 277.781 1.00 18.94 ? 3742 LEU A CD1   1 
ATOM   16602 C  CD2   . LEU A 1 3742 ? 215.161 194.293 278.820 1.00 15.40 ? 3742 LEU A CD2   1 
ATOM   16603 N  N     . ARG A 1 3743 ? 217.379 196.198 274.406 1.00 18.35 ? 3743 ARG A N     1 
ATOM   16604 C  CA    . ARG A 1 3743 ? 218.548 196.709 273.698 1.00 16.12 ? 3743 ARG A CA    1 
ATOM   16605 C  C     . ARG A 1 3743 ? 218.783 198.183 274.005 1.00 18.02 ? 3743 ARG A C     1 
ATOM   16606 O  O     . ARG A 1 3743 ? 219.930 198.604 274.199 1.00 20.35 ? 3743 ARG A O     1 
ATOM   16607 C  CB    . ARG A 1 3743 ? 218.395 196.477 272.198 1.00 14.80 ? 3743 ARG A CB    1 
ATOM   16608 C  CG    . ARG A 1 3743 ? 218.840 195.098 271.754 1.00 11.90 ? 3743 ARG A CG    1 
ATOM   16609 C  CD    . ARG A 1 3743 ? 218.663 194.905 270.258 1.00 15.23 ? 3743 ARG A CD    1 
ATOM   16610 N  NE    . ARG A 1 3743 ? 217.403 194.246 269.940 1.00 15.09 ? 3743 ARG A NE    1 
ATOM   16611 C  CZ    . ARG A 1 3743 ? 216.383 194.835 269.333 1.00 16.81 ? 3743 ARG A CZ    1 
ATOM   16612 N  NH1   . ARG A 1 3743 ? 216.442 196.099 268.954 1.00 12.67 ? 3743 ARG A NH1   1 
ATOM   16613 N  NH2   . ARG A 1 3743 ? 215.276 194.136 269.102 1.00 17.20 ? 3743 ARG A NH2   1 
ATOM   16614 N  N     . GLN A 1 3744 ? 217.717 198.986 274.053 1.00 15.05 ? 3744 GLN A N     1 
ATOM   16615 C  CA    . GLN A 1 3744 ? 217.873 200.375 274.471 1.00 17.31 ? 3744 GLN A CA    1 
ATOM   16616 C  C     . GLN A 1 3744 ? 218.320 200.465 275.924 1.00 17.78 ? 3744 GLN A C     1 
ATOM   16617 O  O     . GLN A 1 3744 ? 219.122 201.337 276.279 1.00 23.47 ? 3744 GLN A O     1 
ATOM   16618 C  CB    . GLN A 1 3744 ? 216.569 201.148 274.267 1.00 17.99 ? 3744 GLN A CB    1 
ATOM   16619 C  CG    . GLN A 1 3744 ? 215.750 200.703 273.079 1.00 15.25 ? 3744 GLN A CG    1 
ATOM   16620 C  CD    . GLN A 1 3744 ? 214.719 201.731 272.660 1.00 21.55 ? 3744 GLN A CD    1 
ATOM   16621 O  OE1   . GLN A 1 3744 ? 213.905 202.175 273.469 1.00 21.55 ? 3744 GLN A OE1   1 
ATOM   16622 N  NE2   . GLN A 1 3744 ? 214.746 202.114 271.390 1.00 24.53 ? 3744 GLN A NE2   1 
ATOM   16623 N  N     . LEU A 1 3745 ? 217.805 199.579 276.779 1.00 16.39 ? 3745 LEU A N     1 
ATOM   16624 C  CA    . LEU A 1 3745 ? 218.157 199.623 278.195 1.00 20.25 ? 3745 LEU A CA    1 
ATOM   16625 C  C     . LEU A 1 3745 ? 219.637 199.336 278.415 1.00 18.75 ? 3745 LEU A C     1 
ATOM   16626 O  O     . LEU A 1 3745 ? 220.289 200.007 279.223 1.00 25.03 ? 3745 LEU A O     1 
ATOM   16627 C  CB    . LEU A 1 3745 ? 217.291 198.639 278.980 1.00 22.08 ? 3745 LEU A CB    1 
ATOM   16628 C  CG    . LEU A 1 3745 ? 215.874 199.147 279.249 1.00 19.61 ? 3745 LEU A CG    1 
ATOM   16629 C  CD1   . LEU A 1 3745 ? 214.951 198.014 279.650 1.00 19.86 ? 3745 LEU A CD1   1 
ATOM   16630 C  CD2   . LEU A 1 3745 ? 215.898 200.226 280.315 1.00 20.62 ? 3745 LEU A CD2   1 
ATOM   16631 N  N     . GLU A 1 3746 ? 220.186 198.344 277.711 1.00 19.99 ? 3746 GLU A N     1 
ATOM   16632 C  CA    . GLU A 1 3746 ? 221.609 198.059 277.861 1.00 21.27 ? 3746 GLU A CA    1 
ATOM   16633 C  C     . GLU A 1 3746 ? 222.463 199.127 277.192 1.00 24.63 ? 3746 GLU A C     1 
ATOM   16634 O  O     . GLU A 1 3746 ? 223.574 199.411 277.655 1.00 28.98 ? 3746 GLU A O     1 
ATOM   16635 C  CB    . GLU A 1 3746 ? 221.942 196.676 277.301 1.00 17.59 ? 3746 GLU A CB    1 
ATOM   16636 C  CG    . GLU A 1 3746 ? 221.765 196.538 275.802 1.00 24.21 ? 3746 GLU A CG    1 
ATOM   16637 C  CD    . GLU A 1 3746 ? 222.117 195.155 275.296 1.00 33.23 ? 3746 GLU A CD    1 
ATOM   16638 O  OE1   . GLU A 1 3746 ? 222.489 194.293 276.121 1.00 30.71 ? 3746 GLU A OE1   1 
ATOM   16639 O  OE2   . GLU A 1 3746 ? 222.022 194.929 274.071 1.00 33.03 ? 3746 GLU A OE2   1 
ATOM   16640 N  N     . LYS A 1 3747 ? 221.969 199.727 276.107 1.00 20.21 ? 3747 LYS A N     1 
ATOM   16641 C  CA    . LYS A 1 3747 ? 222.693 200.820 275.470 1.00 20.81 ? 3747 LYS A CA    1 
ATOM   16642 C  C     . LYS A 1 3747 ? 222.688 202.066 276.349 1.00 25.63 ? 3747 LYS A C     1 
ATOM   16643 O  O     . LYS A 1 3747 ? 223.736 202.683 276.571 1.00 32.25 ? 3747 LYS A O     1 
ATOM   16644 C  CB    . LYS A 1 3747 ? 222.083 201.123 274.100 1.00 18.67 ? 3747 LYS A CB    1 
ATOM   16645 C  CG    . LYS A 1 3747 ? 222.533 202.441 273.500 1.00 21.44 ? 3747 LYS A CG    1 
ATOM   16646 C  CD    . LYS A 1 3747 ? 221.986 202.627 272.094 1.00 22.02 ? 3747 LYS A CD    1 
ATOM   16647 C  CE    . LYS A 1 3747 ? 222.492 201.547 271.155 1.00 24.64 ? 3747 LYS A CE    1 
ATOM   16648 N  NZ    . LYS A 1 3747 ? 222.030 201.769 269.757 1.00 24.55 ? 3747 LYS A NZ    1 
ATOM   16649 N  N     . SER A 1 3748 ? 221.514 202.446 276.863 1.00 24.46 ? 3748 SER A N     1 
ATOM   16650 C  CA    . SER A 1 3748 ? 221.422 203.638 277.701 1.00 23.73 ? 3748 SER A CA    1 
ATOM   16651 C  C     . SER A 1 3748 ? 222.232 203.481 278.980 1.00 21.25 ? 3748 SER A C     1 
ATOM   16652 O  O     . SER A 1 3748 ? 222.913 204.417 279.413 1.00 24.11 ? 3748 SER A O     1 
ATOM   16653 C  CB    . SER A 1 3748 ? 219.960 203.938 278.031 1.00 26.74 ? 3748 SER A CB    1 
ATOM   16654 O  OG    . SER A 1 3748 ? 219.192 204.118 276.855 1.00 30.40 ? 3748 SER A OG    1 
ATOM   16655 N  N     . LEU A 1 3749 ? 222.172 202.301 279.601 1.00 18.31 ? 3749 LEU A N     1 
ATOM   16656 C  CA    . LEU A 1 3749 ? 222.915 202.077 280.837 1.00 19.89 ? 3749 LEU A CA    1 
ATOM   16657 C  C     . LEU A 1 3749 ? 224.415 202.146 280.582 1.00 18.43 ? 3749 LEU A C     1 
ATOM   16658 O  O     . LEU A 1 3749 ? 225.172 202.666 281.410 1.00 23.20 ? 3749 LEU A O     1 
ATOM   16659 C  CB    . LEU A 1 3749 ? 222.510 200.735 281.450 1.00 22.59 ? 3749 LEU A CB    1 
ATOM   16660 C  CG    . LEU A 1 3749 ? 223.003 200.327 282.843 1.00 22.99 ? 3749 LEU A CG    1 
ATOM   16661 C  CD1   . LEU A 1 3749 ? 222.002 199.368 283.459 1.00 24.36 ? 3749 LEU A CD1   1 
ATOM   16662 C  CD2   . LEU A 1 3749 ? 224.374 199.685 282.805 1.00 23.72 ? 3749 LEU A CD2   1 
ATOM   16663 N  N     . LEU A 1 3750 ? 224.864 201.623 279.439 1.00 23.04 ? 3750 LEU A N     1 
ATOM   16664 C  CA    . LEU A 1 3750 ? 226.264 201.768 279.056 1.00 22.83 ? 3750 LEU A CA    1 
ATOM   16665 C  C     . LEU A 1 3750 ? 226.622 203.229 278.814 1.00 23.60 ? 3750 LEU A C     1 
ATOM   16666 O  O     . LEU A 1 3750 ? 227.698 203.687 279.220 1.00 25.27 ? 3750 LEU A O     1 
ATOM   16667 C  CB    . LEU A 1 3750 ? 226.556 200.929 277.814 1.00 19.64 ? 3750 LEU A CB    1 
ATOM   16668 C  CG    . LEU A 1 3750 ? 227.992 200.428 277.643 1.00 20.99 ? 3750 LEU A CG    1 
ATOM   16669 C  CD1   . LEU A 1 3750 ? 228.481 199.763 278.913 1.00 23.21 ? 3750 LEU A CD1   1 
ATOM   16670 C  CD2   . LEU A 1 3750 ? 228.093 199.478 276.462 1.00 17.16 ? 3750 LEU A CD2   1 
ATOM   16671 N  N     . GLN A 1 3751 ? 225.733 203.981 278.158 1.00 19.88 ? 3751 GLN A N     1 
ATOM   16672 C  CA    . GLN A 1 3751 ? 226.005 205.391 277.894 1.00 22.08 ? 3751 GLN A CA    1 
ATOM   16673 C  C     . GLN A 1 3751 ? 226.135 206.182 279.190 1.00 27.12 ? 3751 GLN A C     1 
ATOM   16674 O  O     . GLN A 1 3751 ? 226.957 207.101 279.284 1.00 30.51 ? 3751 GLN A O     1 
ATOM   16675 C  CB    . GLN A 1 3751 ? 224.903 205.992 277.020 1.00 18.01 ? 3751 GLN A CB    1 
ATOM   16676 C  CG    . GLN A 1 3751 ? 224.861 205.481 275.591 1.00 26.78 ? 3751 GLN A CG    1 
ATOM   16677 C  CD    . GLN A 1 3751 ? 226.238 205.208 275.019 1.00 33.41 ? 3751 GLN A CD    1 
ATOM   16678 O  OE1   . GLN A 1 3751 ? 227.059 206.116 274.886 1.00 33.36 ? 3751 GLN A OE1   1 
ATOM   16679 N  NE2   . GLN A 1 3751 ? 226.495 203.952 274.672 1.00 30.84 ? 3751 GLN A NE2   1 
ATOM   16680 N  N     . ALA A 1 3752 ? 225.321 205.848 280.195 1.00 22.15 ? 3752 ALA A N     1 
ATOM   16681 C  CA    . ALA A 1 3752 ? 225.358 206.584 281.455 1.00 22.56 ? 3752 ALA A CA    1 
ATOM   16682 C  C     . ALA A 1 3752 ? 226.714 206.455 282.134 1.00 22.13 ? 3752 ALA A C     1 
ATOM   16683 O  O     . ALA A 1 3752 ? 227.234 207.431 282.685 1.00 28.62 ? 3752 ALA A O     1 
ATOM   16684 C  CB    . ALA A 1 3752 ? 224.243 206.094 282.380 1.00 23.42 ? 3752 ALA A CB    1 
ATOM   16685 N  N     . LEU A 1 3753 ? 227.298 205.257 282.111 1.00 20.34 ? 3753 LEU A N     1 
ATOM   16686 C  CA    . LEU A 1 3753 ? 228.626 205.068 282.678 1.00 20.98 ? 3753 LEU A CA    1 
ATOM   16687 C  C     . LEU A 1 3753 ? 229.722 205.626 281.784 1.00 25.48 ? 3753 LEU A C     1 
ATOM   16688 O  O     . LEU A 1 3753 ? 230.829 205.881 282.269 1.00 30.08 ? 3753 LEU A O     1 
ATOM   16689 C  CB    . LEU A 1 3753 ? 228.884 203.584 282.939 1.00 21.66 ? 3753 LEU A CB    1 
ATOM   16690 C  CG    . LEU A 1 3753 ? 228.392 203.009 284.267 1.00 19.11 ? 3753 LEU A CG    1 
ATOM   16691 C  CD1   . LEU A 1 3753 ? 226.883 202.844 284.264 1.00 18.44 ? 3753 LEU A CD1   1 
ATOM   16692 C  CD2   . LEU A 1 3753 ? 229.078 201.683 284.548 1.00 24.37 ? 3753 LEU A CD2   1 
ATOM   16693 N  N     . ASN A 1 3754 ? 229.447 205.813 280.494 1.00 28.93 ? 3754 ASN A N     1 
ATOM   16694 C  CA    . ASN A 1 3754 ? 230.442 206.310 279.555 1.00 21.85 ? 3754 ASN A CA    1 
ATOM   16695 C  C     . ASN A 1 3754 ? 230.407 207.822 279.391 1.00 26.13 ? 3754 ASN A C     1 
ATOM   16696 O  O     . ASN A 1 3754 ? 231.288 208.375 278.724 1.00 34.48 ? 3754 ASN A O     1 
ATOM   16697 C  CB    . ASN A 1 3754 ? 230.250 205.646 278.190 1.00 24.70 ? 3754 ASN A CB    1 
ATOM   16698 C  CG    . ASN A 1 3754 ? 230.538 204.159 278.218 1.00 25.67 ? 3754 ASN A CG    1 
ATOM   16699 O  OD1   . ASN A 1 3754 ? 231.595 203.727 278.673 1.00 24.10 ? 3754 ASN A OD1   1 
ATOM   16700 N  ND2   . ASN A 1 3754 ? 229.586 203.365 277.744 1.00 32.06 ? 3754 ASN A ND2   1 
ATOM   16701 N  N     . GLU A 1 3755 ? 229.424 208.500 279.978 1.00 28.47 ? 3755 GLU A N     1 
ATOM   16702 C  CA    . GLU A 1 3755 ? 229.295 209.945 279.859 1.00 27.24 ? 3755 GLU A CA    1 
ATOM   16703 C  C     . GLU A 1 3755 ? 229.389 210.669 281.193 1.00 27.26 ? 3755 GLU A C     1 
ATOM   16704 O  O     . GLU A 1 3755 ? 229.306 211.901 281.220 1.00 30.13 ? 3755 GLU A O     1 
ATOM   16705 C  CB    . GLU A 1 3755 ? 227.969 210.301 279.174 1.00 24.43 ? 3755 GLU A CB    1 
ATOM   16706 C  CG    . GLU A 1 3755 ? 227.890 209.871 277.719 1.00 26.79 ? 3755 GLU A CG    1 
ATOM   16707 C  CD    . GLU A 1 3755 ? 228.857 210.630 276.832 1.00 33.76 ? 3755 GLU A CD    1 
ATOM   16708 O  OE1   . GLU A 1 3755 ? 229.118 211.818 277.115 1.00 35.42 ? 3755 GLU A OE1   1 
ATOM   16709 O  OE2   . GLU A 1 3755 ? 229.357 210.038 275.853 1.00 37.40 ? 3755 GLU A OE2   1 
ATOM   16710 N  N     . VAL A 1 3756 ? 229.560 209.949 282.292 1.00 25.45 ? 3756 VAL A N     1 
ATOM   16711 C  CA    . VAL A 1 3756 ? 229.609 210.556 283.618 1.00 26.91 ? 3756 VAL A CA    1 
ATOM   16712 C  C     . VAL A 1 3756 ? 231.055 210.887 283.968 1.00 29.49 ? 3756 VAL A C     1 
ATOM   16713 O  O     . VAL A 1 3756 ? 231.970 210.090 283.729 1.00 33.96 ? 3756 VAL A O     1 
ATOM   16714 C  CB    . VAL A 1 3756 ? 228.968 209.629 284.669 1.00 29.60 ? 3756 VAL A CB    1 
ATOM   16715 C  CG1   . VAL A 1 3756 ? 229.648 208.264 284.677 1.00 26.37 ? 3756 VAL A CG1   1 
ATOM   16716 C  CG2   . VAL A 1 3756 ? 229.011 210.270 286.047 1.00 24.41 ? 3756 VAL A CG2   1 
ATOM   16717 N  N     . LYS A 1 3757 ? 231.263 212.076 284.521 1.00 29.85 ? 3757 LYS A N     1 
ATOM   16718 C  CA    . LYS A 1 3757 ? 232.585 212.539 284.911 1.00 31.11 ? 3757 LYS A CA    1 
ATOM   16719 C  C     . LYS A 1 3757 ? 232.803 212.333 286.404 1.00 31.80 ? 3757 LYS A C     1 
ATOM   16720 O  O     . LYS A 1 3757 ? 231.856 212.239 287.190 1.00 30.61 ? 3757 LYS A O     1 
ATOM   16721 C  CB    . LYS A 1 3757 ? 232.771 214.015 284.550 1.00 24.55 ? 3757 LYS A CB    1 
ATOM   16722 C  CG    . LYS A 1 3757 ? 232.302 214.375 283.148 1.00 29.79 ? 3757 LYS A CG    1 
ATOM   16723 C  CD    . LYS A 1 3757 ? 233.028 213.563 282.087 1.00 29.90 ? 3757 LYS A CD    1 
ATOM   16724 C  CE    . LYS A 1 3757 ? 234.511 213.888 282.057 1.00 32.63 ? 3757 LYS A CE    1 
ATOM   16725 N  NZ    . LYS A 1 3757 ? 235.243 213.035 281.079 1.00 31.61 ? 3757 LYS A NZ    1 
ATOM   16726 N  N     . GLY A 1 3758 ? 234.070 212.267 286.788 1.00 33.34 ? 3758 GLY A N     1 
ATOM   16727 C  CA    . GLY A 1 3758 ? 234.404 212.044 288.186 1.00 28.49 ? 3758 GLY A CA    1 
ATOM   16728 C  C     . GLY A 1 3758 ? 233.936 210.677 288.641 1.00 34.08 ? 3758 GLY A C     1 
ATOM   16729 O  O     . GLY A 1 3758 ? 234.266 209.648 288.039 1.00 35.54 ? 3758 GLY A O     1 
ATOM   16730 N  N     . ARG A 1 3759 ? 233.150 210.652 289.715 1.00 32.20 ? 3759 ARG A N     1 
ATOM   16731 C  CA    . ARG A 1 3759 ? 232.644 209.418 290.291 1.00 30.24 ? 3759 ARG A CA    1 
ATOM   16732 C  C     . ARG A 1 3759 ? 231.125 209.365 290.170 1.00 30.90 ? 3759 ARG A C     1 
ATOM   16733 O  O     . ARG A 1 3759 ? 230.453 210.398 290.122 1.00 31.84 ? 3759 ARG A O     1 
ATOM   16734 C  CB    . ARG A 1 3759 ? 233.056 209.281 291.762 1.00 32.34 ? 3759 ARG A CB    1 
ATOM   16735 C  CG    . ARG A 1 3759 ? 234.530 209.556 292.018 1.00 31.12 ? 3759 ARG A CG    1 
ATOM   16736 C  CD    . ARG A 1 3759 ? 234.810 209.769 293.496 1.00 30.13 ? 3759 ARG A CD    1 
ATOM   16737 N  NE    . ARG A 1 3759 ? 234.429 211.110 293.931 1.00 32.77 ? 3759 ARG A NE    1 
ATOM   16738 C  CZ    . ARG A 1 3759 ? 234.532 211.550 295.177 1.00 34.47 ? 3759 ARG A CZ    1 
ATOM   16739 N  NH1   . ARG A 1 3759 ? 235.002 210.782 296.146 1.00 32.33 ? 3759 ARG A NH1   1 
ATOM   16740 N  NH2   . ARG A 1 3759 ? 234.152 212.793 295.459 1.00 29.68 ? 3759 ARG A NH2   1 
ATOM   16741 N  N     . ILE A 1 3760 ? 230.599 208.141 290.106 1.00 29.52 ? 3760 ILE A N     1 
ATOM   16742 C  CA    . ILE A 1 3760 ? 229.156 207.948 290.008 1.00 30.56 ? 3760 ILE A CA    1 
ATOM   16743 C  C     . ILE A 1 3760 ? 228.458 208.446 291.270 1.00 33.58 ? 3760 ILE A C     1 
ATOM   16744 O  O     . ILE A 1 3760 ? 227.413 209.104 291.199 1.00 35.88 ? 3760 ILE A O     1 
ATOM   16745 C  CB    . ILE A 1 3760 ? 228.839 206.469 289.729 1.00 28.28 ? 3760 ILE A CB    1 
ATOM   16746 C  CG1   . ILE A 1 3760 ? 229.394 206.051 288.366 1.00 26.03 ? 3760 ILE A CG1   1 
ATOM   16747 C  CG2   . ILE A 1 3760 ? 227.341 206.212 289.802 1.00 30.06 ? 3760 ILE A CG2   1 
ATOM   16748 C  CD1   . ILE A 1 3760 ? 229.155 204.599 288.030 1.00 25.11 ? 3760 ILE A CD1   1 
ATOM   16749 N  N     . LEU A 1 3761 ? 229.029 208.150 292.442 1.00 28.24 ? 3761 LEU A N     1 
ATOM   16750 C  CA    . LEU A 1 3761 ? 228.383 208.503 293.701 1.00 29.91 ? 3761 LEU A CA    1 
ATOM   16751 C  C     . LEU A 1 3761 ? 228.262 210.010 293.882 1.00 34.98 ? 3761 LEU A C     1 
ATOM   16752 O  O     . LEU A 1 3761 ? 227.383 210.476 294.618 1.00 37.33 ? 3761 LEU A O     1 
ATOM   16753 C  CB    . LEU A 1 3761 ? 229.155 207.901 294.876 1.00 26.37 ? 3761 LEU A CB    1 
ATOM   16754 C  CG    . LEU A 1 3761 ? 228.998 206.404 295.136 1.00 25.49 ? 3761 LEU A CG    1 
ATOM   16755 C  CD1   . LEU A 1 3761 ? 230.011 205.619 294.325 1.00 30.96 ? 3761 LEU A CD1   1 
ATOM   16756 C  CD2   . LEU A 1 3761 ? 229.144 206.103 296.619 1.00 27.54 ? 3761 LEU A CD2   1 
ATOM   16757 N  N     . ASP A 1 3762 ? 229.132 210.788 293.232 1.00 34.56 ? 3762 ASP A N     1 
ATOM   16758 C  CA    . ASP A 1 3762 ? 229.100 212.237 293.407 1.00 33.42 ? 3762 ASP A CA    1 
ATOM   16759 C  C     . ASP A 1 3762 ? 227.787 212.830 292.910 1.00 36.28 ? 3762 ASP A C     1 
ATOM   16760 O  O     . ASP A 1 3762 ? 227.223 213.727 293.547 1.00 39.33 ? 3762 ASP A O     1 
ATOM   16761 C  CB    . ASP A 1 3762 ? 230.285 212.879 292.687 1.00 33.23 ? 3762 ASP A CB    1 
ATOM   16762 C  CG    . ASP A 1 3762 ? 231.605 212.598 293.376 1.00 36.01 ? 3762 ASP A CG    1 
ATOM   16763 O  OD1   . ASP A 1 3762 ? 231.649 212.656 294.622 1.00 33.54 ? 3762 ASP A OD1   1 
ATOM   16764 O  OD2   . ASP A 1 3762 ? 232.600 212.325 292.672 1.00 35.30 ? 3762 ASP A OD2   1 
ATOM   16765 N  N     . ASP A 1 3763 ? 227.287 212.346 291.777 1.00 34.67 ? 3763 ASP A N     1 
ATOM   16766 C  CA    . ASP A 1 3763 ? 226.047 212.841 291.190 1.00 35.48 ? 3763 ASP A CA    1 
ATOM   16767 C  C     . ASP A 1 3763 ? 224.939 211.828 291.464 1.00 35.34 ? 3763 ASP A C     1 
ATOM   16768 O  O     . ASP A 1 3763 ? 224.933 210.735 290.890 1.00 34.87 ? 3763 ASP A O     1 
ATOM   16769 C  CB    . ASP A 1 3763 ? 226.213 213.082 289.691 1.00 33.33 ? 3763 ASP A CB    1 
ATOM   16770 C  CG    . ASP A 1 3763 ? 224.957 213.636 289.049 1.00 39.54 ? 3763 ASP A CG    1 
ATOM   16771 O  OD1   . ASP A 1 3763 ? 224.468 214.692 289.506 1.00 38.21 ? 3763 ASP A OD1   1 
ATOM   16772 O  OD2   . ASP A 1 3763 ? 224.458 213.018 288.084 1.00 38.17 ? 3763 ASP A OD2   1 
ATOM   16773 N  N     . ASP A 1 3764 ? 224.003 212.199 292.341 1.00 37.64 ? 3764 ASP A N     1 
ATOM   16774 C  CA    . ASP A 1 3764 ? 222.893 211.312 292.668 1.00 33.53 ? 3764 ASP A CA    1 
ATOM   16775 C  C     . ASP A 1 3764 ? 221.960 211.090 291.486 1.00 33.26 ? 3764 ASP A C     1 
ATOM   16776 O  O     . ASP A 1 3764 ? 221.233 210.091 291.467 1.00 35.71 ? 3764 ASP A O     1 
ATOM   16777 C  CB    . ASP A 1 3764 ? 222.104 211.871 293.853 1.00 34.27 ? 3764 ASP A CB    1 
ATOM   16778 C  CG    . ASP A 1 3764 ? 222.884 211.812 295.152 1.00 39.45 ? 3764 ASP A CG    1 
ATOM   16779 O  OD1   . ASP A 1 3764 ? 224.060 211.391 295.123 1.00 39.24 ? 3764 ASP A OD1   1 
ATOM   16780 O  OD2   . ASP A 1 3764 ? 222.321 212.186 296.203 1.00 38.74 ? 3764 ASP A OD2   1 
ATOM   16781 N  N     . THR A 1 3765 ? 221.961 211.997 290.506 1.00 28.75 ? 3765 THR A N     1 
ATOM   16782 C  CA    . THR A 1 3765 ? 221.129 211.811 289.322 1.00 30.21 ? 3765 THR A CA    1 
ATOM   16783 C  C     . THR A 1 3765 ? 221.546 210.568 288.547 1.00 30.07 ? 3765 THR A C     1 
ATOM   16784 O  O     . THR A 1 3765 ? 220.694 209.785 288.110 1.00 32.63 ? 3765 THR A O     1 
ATOM   16785 C  CB    . THR A 1 3765 ? 221.198 213.050 288.430 1.00 29.54 ? 3765 THR A CB    1 
ATOM   16786 O  OG1   . THR A 1 3765 ? 220.783 214.201 289.175 1.00 32.13 ? 3765 THR A OG1   1 
ATOM   16787 C  CG2   . THR A 1 3765 ? 220.296 212.887 287.218 1.00 24.81 ? 3765 THR A CG2   1 
ATOM   16788 N  N     . ILE A 1 3766 ? 222.854 210.362 288.379 1.00 27.96 ? 3766 ILE A N     1 
ATOM   16789 C  CA    . ILE A 1 3766 ? 223.344 209.176 287.678 1.00 28.52 ? 3766 ILE A CA    1 
ATOM   16790 C  C     . ILE A 1 3766 ? 222.919 207.912 288.411 1.00 30.34 ? 3766 ILE A C     1 
ATOM   16791 O  O     . ILE A 1 3766 ? 222.528 206.917 287.787 1.00 30.20 ? 3766 ILE A O     1 
ATOM   16792 C  CB    . ILE A 1 3766 ? 224.873 209.251 287.507 1.00 29.48 ? 3766 ILE A CB    1 
ATOM   16793 C  CG1   . ILE A 1 3766 ? 225.240 210.300 286.459 1.00 25.21 ? 3766 ILE A CG1   1 
ATOM   16794 C  CG2   . ILE A 1 3766 ? 225.442 207.895 287.115 1.00 26.89 ? 3766 ILE A CG2   1 
ATOM   16795 C  CD1   . ILE A 1 3766 ? 224.712 209.986 285.078 1.00 28.47 ? 3766 ILE A CD1   1 
ATOM   16796 N  N     . ILE A 1 3767 ? 222.981 207.930 289.746 1.00 28.63 ? 3767 ILE A N     1 
ATOM   16797 C  CA    . ILE A 1 3767 ? 222.574 206.765 290.527 1.00 27.92 ? 3767 ILE A CA    1 
ATOM   16798 C  C     . ILE A 1 3767 ? 221.096 206.466 290.310 1.00 29.17 ? 3767 ILE A C     1 
ATOM   16799 O  O     . ILE A 1 3767 ? 220.703 205.309 290.123 1.00 32.39 ? 3767 ILE A O     1 
ATOM   16800 C  CB    . ILE A 1 3767 ? 222.897 206.980 292.016 1.00 29.39 ? 3767 ILE A CB    1 
ATOM   16801 C  CG1   . ILE A 1 3767 ? 224.393 207.235 292.205 1.00 30.82 ? 3767 ILE A CG1   1 
ATOM   16802 C  CG2   . ILE A 1 3767 ? 222.438 205.788 292.842 1.00 24.98 ? 3767 ILE A CG2   1 
ATOM   16803 C  CD1   . ILE A 1 3767 ? 224.810 207.383 293.654 1.00 31.42 ? 3767 ILE A CD1   1 
ATOM   16804 N  N     . THR A 1 3768 ? 220.255 207.502 290.329 1.00 28.79 ? 3768 THR A N     1 
ATOM   16805 C  CA    . THR A 1 3768 ? 218.827 207.299 290.107 1.00 26.73 ? 3768 THR A CA    1 
ATOM   16806 C  C     . THR A 1 3768 ? 218.553 206.756 288.711 1.00 27.58 ? 3768 THR A C     1 
ATOM   16807 O  O     . THR A 1 3768 ? 217.711 205.868 288.537 1.00 31.65 ? 3768 THR A O     1 
ATOM   16808 C  CB    . THR A 1 3768 ? 218.070 208.606 290.330 1.00 26.93 ? 3768 THR A CB    1 
ATOM   16809 O  OG1   . THR A 1 3768 ? 218.636 209.631 289.506 1.00 32.06 ? 3768 THR A OG1   1 
ATOM   16810 C  CG2   . THR A 1 3768 ? 218.151 209.027 291.789 1.00 25.45 ? 3768 THR A CG2   1 
ATOM   16811 N  N     . THR A 1 3769 ? 219.253 207.278 287.701 1.00 28.08 ? 3769 THR A N     1 
ATOM   16812 C  CA    . THR A 1 3769 ? 219.037 206.814 286.334 1.00 29.74 ? 3769 THR A CA    1 
ATOM   16813 C  C     . THR A 1 3769 ? 219.412 205.348 286.177 1.00 24.98 ? 3769 THR A C     1 
ATOM   16814 O  O     . THR A 1 3769 ? 218.699 204.586 285.512 1.00 30.48 ? 3769 THR A O     1 
ATOM   16815 C  CB    . THR A 1 3769 ? 219.829 207.672 285.351 1.00 27.69 ? 3769 THR A CB    1 
ATOM   16816 O  OG1   . THR A 1 3769 ? 221.218 207.655 285.709 1.00 31.91 ? 3769 THR A OG1   1 
ATOM   16817 C  CG2   . THR A 1 3769 ? 219.316 209.106 285.362 1.00 26.10 ? 3769 THR A CG2   1 
ATOM   16818 N  N     . LEU A 1 3770 ? 220.526 204.930 286.781 1.00 24.18 ? 3770 LEU A N     1 
ATOM   16819 C  CA    . LEU A 1 3770 ? 220.925 203.528 286.701 1.00 25.29 ? 3770 LEU A CA    1 
ATOM   16820 C  C     . LEU A 1 3770 ? 219.889 202.625 287.354 1.00 28.13 ? 3770 LEU A C     1 
ATOM   16821 O  O     . LEU A 1 3770 ? 219.557 201.561 286.819 1.00 30.63 ? 3770 LEU A O     1 
ATOM   16822 C  CB    . LEU A 1 3770 ? 222.292 203.329 287.355 1.00 22.43 ? 3770 LEU A CB    1 
ATOM   16823 C  CG    . LEU A 1 3770 ? 223.482 204.020 286.692 1.00 19.55 ? 3770 LEU A CG    1 
ATOM   16824 C  CD1   . LEU A 1 3770 ? 224.787 203.506 287.277 1.00 20.82 ? 3770 LEU A CD1   1 
ATOM   16825 C  CD2   . LEU A 1 3770 ? 223.446 203.815 285.189 1.00 21.91 ? 3770 LEU A CD2   1 
ATOM   16826 N  N     . GLU A 1 3771 ? 219.367 203.033 288.512 1.00 27.48 ? 3771 GLU A N     1 
ATOM   16827 C  CA    . GLU A 1 3771 ? 218.342 202.238 289.180 1.00 24.20 ? 3771 GLU A CA    1 
ATOM   16828 C  C     . GLU A 1 3771 ? 217.086 202.130 288.325 1.00 28.12 ? 3771 GLU A C     1 
ATOM   16829 O  O     . GLU A 1 3771 ? 216.500 201.049 288.205 1.00 30.17 ? 3771 GLU A O     1 
ATOM   16830 C  CB    . GLU A 1 3771 ? 218.016 202.848 290.541 1.00 29.20 ? 3771 GLU A CB    1 
ATOM   16831 C  CG    . GLU A 1 3771 ? 219.183 202.865 291.510 1.00 27.39 ? 3771 GLU A CG    1 
ATOM   16832 C  CD    . GLU A 1 3771 ? 218.936 203.771 292.698 1.00 30.10 ? 3771 GLU A CD    1 
ATOM   16833 O  OE1   . GLU A 1 3771 ? 218.581 204.949 292.483 1.00 33.11 ? 3771 GLU A OE1   1 
ATOM   16834 O  OE2   . GLU A 1 3771 ? 219.100 203.309 293.848 1.00 33.72 ? 3771 GLU A OE2   1 
ATOM   16835 N  N     . ASN A 1 3772 ? 216.660 203.242 287.721 1.00 24.90 ? 3772 ASN A N     1 
ATOM   16836 C  CA    . ASN A 1 3772 ? 215.465 203.219 286.884 1.00 23.16 ? 3772 ASN A CA    1 
ATOM   16837 C  C     . ASN A 1 3772 ? 215.672 202.356 285.644 1.00 24.10 ? 3772 ASN A C     1 
ATOM   16838 O  O     . ASN A 1 3772 ? 214.773 201.603 285.252 1.00 22.26 ? 3772 ASN A O     1 
ATOM   16839 C  CB    . ASN A 1 3772 ? 215.071 204.643 286.492 1.00 22.74 ? 3772 ASN A CB    1 
ATOM   16840 C  CG    . ASN A 1 3772 ? 214.758 205.512 287.695 1.00 27.39 ? 3772 ASN A CG    1 
ATOM   16841 O  OD1   . ASN A 1 3772 ? 214.884 205.076 288.839 1.00 26.63 ? 3772 ASN A OD1   1 
ATOM   16842 N  ND2   . ASN A 1 3772 ? 214.344 206.747 287.440 1.00 30.93 ? 3772 ASN A ND2   1 
ATOM   16843 N  N     . LEU A 1 3773 ? 216.843 202.459 285.012 1.00 24.89 ? 3773 LEU A N     1 
ATOM   16844 C  CA    . LEU A 1 3773 ? 217.142 201.590 283.877 1.00 23.53 ? 3773 LEU A CA    1 
ATOM   16845 C  C     . LEU A 1 3773 ? 217.218 200.131 284.306 1.00 23.10 ? 3773 LEU A C     1 
ATOM   16846 O  O     . LEU A 1 3773 ? 216.713 199.245 283.609 1.00 28.95 ? 3773 LEU A O     1 
ATOM   16847 C  CB    . LEU A 1 3773 ? 218.448 202.024 283.213 1.00 24.10 ? 3773 LEU A CB    1 
ATOM   16848 C  CG    . LEU A 1 3773 ? 218.436 203.403 282.551 1.00 24.03 ? 3773 LEU A CG    1 
ATOM   16849 C  CD1   . LEU A 1 3773 ? 219.788 203.710 281.935 1.00 19.36 ? 3773 LEU A CD1   1 
ATOM   16850 C  CD2   . LEU A 1 3773 ? 217.333 203.489 281.507 1.00 23.80 ? 3773 LEU A CD2   1 
ATOM   16851 N  N     . LYS A 1 3774 ? 217.846 199.862 285.452 1.00 22.90 ? 3774 LYS A N     1 
ATOM   16852 C  CA    . LYS A 1 3774 ? 217.880 198.499 285.970 1.00 23.26 ? 3774 LYS A CA    1 
ATOM   16853 C  C     . LYS A 1 3774 ? 216.489 198.016 286.359 1.00 23.53 ? 3774 LYS A C     1 
ATOM   16854 O  O     . LYS A 1 3774 ? 216.139 196.856 286.113 1.00 28.20 ? 3774 LYS A O     1 
ATOM   16855 C  CB    . LYS A 1 3774 ? 218.832 198.410 287.162 1.00 20.82 ? 3774 LYS A CB    1 
ATOM   16856 C  CG    . LYS A 1 3774 ? 220.297 198.342 286.774 1.00 22.74 ? 3774 LYS A CG    1 
ATOM   16857 C  CD    . LYS A 1 3774 ? 220.604 197.064 286.012 1.00 26.31 ? 3774 LYS A CD    1 
ATOM   16858 C  CE    . LYS A 1 3774 ? 220.124 195.833 286.769 1.00 27.61 ? 3774 LYS A CE    1 
ATOM   16859 N  NZ    . LYS A 1 3774 ? 220.562 194.565 286.129 1.00 28.37 ? 3774 LYS A NZ    1 
ATOM   16860 N  N     . ARG A 1 3775 ? 215.686 198.886 286.977 1.00 25.31 ? 3775 ARG A N     1 
ATOM   16861 C  CA    . ARG A 1 3775 ? 214.335 198.496 287.367 1.00 24.28 ? 3775 ARG A CA    1 
ATOM   16862 C  C     . ARG A 1 3775 ? 213.480 198.171 286.150 1.00 22.12 ? 3775 ARG A C     1 
ATOM   16863 O  O     . ARG A 1 3775 ? 212.746 197.176 286.146 1.00 24.60 ? 3775 ARG A O     1 
ATOM   16864 C  CB    . ARG A 1 3775 ? 213.688 199.605 288.195 1.00 22.22 ? 3775 ARG A CB    1 
ATOM   16865 C  CG    . ARG A 1 3775 ? 212.276 199.301 288.658 1.00 27.54 ? 3775 ARG A CG    1 
ATOM   16866 C  CD    . ARG A 1 3775 ? 211.673 200.496 289.372 1.00 28.60 ? 3775 ARG A CD    1 
ATOM   16867 N  NE    . ARG A 1 3775 ? 212.590 201.052 290.358 1.00 31.52 ? 3775 ARG A NE    1 
ATOM   16868 C  CZ    . ARG A 1 3775 ? 213.153 202.250 290.268 1.00 33.02 ? 3775 ARG A CZ    1 
ATOM   16869 N  NH1   . ARG A 1 3775 ? 212.916 203.050 289.242 1.00 28.11 ? 3775 ARG A NH1   1 
ATOM   16870 N  NH2   . ARG A 1 3775 ? 213.976 202.654 291.232 1.00 32.14 ? 3775 ARG A NH2   1 
ATOM   16871 N  N     . GLU A 1 3776 ? 213.563 198.992 285.104 1.00 22.36 ? 3776 GLU A N     1 
ATOM   16872 C  CA    . GLU A 1 3776 ? 212.826 198.691 283.884 1.00 21.47 ? 3776 GLU A CA    1 
ATOM   16873 C  C     . GLU A 1 3776 ? 213.404 197.476 283.174 1.00 24.78 ? 3776 GLU A C     1 
ATOM   16874 O  O     . GLU A 1 3776 ? 212.661 196.721 282.538 1.00 24.66 ? 3776 GLU A O     1 
ATOM   16875 C  CB    . GLU A 1 3776 ? 212.815 199.907 282.957 1.00 16.26 ? 3776 GLU A CB    1 
ATOM   16876 C  CG    . GLU A 1 3776 ? 211.675 199.906 281.952 1.00 19.79 ? 3776 GLU A CG    1 
ATOM   16877 C  CD    . GLU A 1 3776 ? 211.788 201.025 280.934 1.00 31.46 ? 3776 GLU A CD    1 
ATOM   16878 O  OE1   . GLU A 1 3776 ? 212.922 201.374 280.548 1.00 26.44 ? 3776 GLU A OE1   1 
ATOM   16879 O  OE2   . GLU A 1 3776 ? 210.737 201.559 280.521 1.00 34.08 ? 3776 GLU A OE2   1 
ATOM   16880 N  N     . ALA A 1 3777 ? 214.719 197.265 283.274 1.00 20.72 ? 3777 ALA A N     1 
ATOM   16881 C  CA    . ALA A 1 3777 ? 215.328 196.084 282.671 1.00 18.97 ? 3777 ALA A CA    1 
ATOM   16882 C  C     . ALA A 1 3777 ? 214.819 194.805 283.321 1.00 20.97 ? 3777 ALA A C     1 
ATOM   16883 O  O     . ALA A 1 3777 ? 214.578 193.805 282.637 1.00 24.41 ? 3777 ALA A O     1 
ATOM   16884 C  CB    . ALA A 1 3777 ? 216.852 196.166 282.769 1.00 23.36 ? 3777 ALA A CB    1 
ATOM   16885 N  N     . ALA A 1 3778 ? 214.655 194.814 284.646 1.00 21.75 ? 3778 ALA A N     1 
ATOM   16886 C  CA    . ALA A 1 3778 ? 214.173 193.621 285.336 1.00 19.73 ? 3778 ALA A CA    1 
ATOM   16887 C  C     . ALA A 1 3778 ? 212.710 193.343 285.013 1.00 23.24 ? 3778 ALA A C     1 
ATOM   16888 O  O     . ALA A 1 3778 ? 212.321 192.186 284.816 1.00 22.09 ? 3778 ALA A O     1 
ATOM   16889 C  CB    . ALA A 1 3778 ? 214.375 193.766 286.843 1.00 19.23 ? 3778 ALA A CB    1 
ATOM   16890 N  N     . GLU A 1 3779 ? 211.881 194.389 284.955 1.00 22.82 ? 3779 GLU A N     1 
ATOM   16891 C  CA    . GLU A 1 3779 ? 210.460 194.190 284.684 1.00 19.84 ? 3779 GLU A CA    1 
ATOM   16892 C  C     . GLU A 1 3779 ? 210.224 193.698 283.262 1.00 23.24 ? 3779 GLU A C     1 
ATOM   16893 O  O     . GLU A 1 3779 ? 209.396 192.807 283.040 1.00 26.95 ? 3779 GLU A O     1 
ATOM   16894 C  CB    . GLU A 1 3779 ? 209.687 195.482 284.937 1.00 19.82 ? 3779 GLU A CB    1 
ATOM   16895 C  CG    . GLU A 1 3779 ? 209.677 195.911 286.389 1.00 23.85 ? 3779 GLU A CG    1 
ATOM   16896 C  CD    . GLU A 1 3779 ? 208.906 194.950 287.273 1.00 31.28 ? 3779 GLU A CD    1 
ATOM   16897 O  OE1   . GLU A 1 3779 ? 207.929 194.340 286.787 1.00 32.77 ? 3779 GLU A OE1   1 
ATOM   16898 O  OE2   . GLU A 1 3779 ? 209.278 194.804 288.456 1.00 30.97 ? 3779 GLU A OE2   1 
ATOM   16899 N  N     . VAL A 1 3780 ? 210.932 194.266 282.285 1.00 22.90 ? 3780 VAL A N     1 
ATOM   16900 C  CA    . VAL A 1 3780 ? 210.799 193.787 280.914 1.00 20.75 ? 3780 VAL A CA    1 
ATOM   16901 C  C     . VAL A 1 3780 ? 211.296 192.351 280.810 1.00 19.95 ? 3780 VAL A C     1 
ATOM   16902 O  O     . VAL A 1 3780 ? 210.676 191.512 280.146 1.00 24.05 ? 3780 VAL A O     1 
ATOM   16903 C  CB    . VAL A 1 3780 ? 211.534 194.725 279.941 1.00 19.17 ? 3780 VAL A CB    1 
ATOM   16904 C  CG1   . VAL A 1 3780 ? 211.476 194.174 278.529 1.00 16.79 ? 3780 VAL A CG1   1 
ATOM   16905 C  CG2   . VAL A 1 3780 ? 210.919 196.109 279.982 1.00 18.55 ? 3780 VAL A CG2   1 
ATOM   16906 N  N     . THR A 1 3781 ? 212.410 192.041 281.475 1.00 20.85 ? 3781 THR A N     1 
ATOM   16907 C  CA    . THR A 1 3781 ? 212.878 190.661 281.536 1.00 19.32 ? 3781 THR A CA    1 
ATOM   16908 C  C     . THR A 1 3781 ? 211.850 189.758 282.201 1.00 20.88 ? 3781 THR A C     1 
ATOM   16909 O  O     . THR A 1 3781 ? 211.728 188.582 281.839 1.00 22.33 ? 3781 THR A O     1 
ATOM   16910 C  CB    . THR A 1 3781 ? 214.214 190.598 282.276 1.00 21.51 ? 3781 THR A CB    1 
ATOM   16911 O  OG1   . THR A 1 3781 ? 215.113 191.562 281.715 1.00 22.05 ? 3781 THR A OG1   1 
ATOM   16912 C  CG2   . THR A 1 3781 ? 214.831 189.216 282.159 1.00 19.86 ? 3781 THR A CG2   1 
ATOM   16913 N  N     . ARG A 1 3782 ? 211.100 190.286 283.172 1.00 28.73 ? 3782 ARG A N     1 
ATOM   16914 C  CA    . ARG A 1 3782 ? 209.984 189.536 283.741 1.00 22.09 ? 3782 ARG A CA    1 
ATOM   16915 C  C     . ARG A 1 3782 ? 208.858 189.367 282.727 1.00 21.27 ? 3782 ARG A C     1 
ATOM   16916 O  O     . ARG A 1 3782 ? 208.198 188.323 282.694 1.00 26.26 ? 3782 ARG A O     1 
ATOM   16917 C  CB    . ARG A 1 3782 ? 209.481 190.232 285.005 1.00 20.54 ? 3782 ARG A CB    1 
ATOM   16918 C  CG    . ARG A 1 3782 ? 208.392 189.482 285.752 1.00 26.83 ? 3782 ARG A CG    1 
ATOM   16919 C  CD    . ARG A 1 3782 ? 207.336 190.438 286.279 1.00 23.39 ? 3782 ARG A CD    1 
ATOM   16920 N  NE    . ARG A 1 3782 ? 206.647 191.141 285.202 1.00 28.16 ? 3782 ARG A NE    1 
ATOM   16921 C  CZ    . ARG A 1 3782 ? 205.661 192.008 285.385 1.00 32.36 ? 3782 ARG A CZ    1 
ATOM   16922 N  NH1   . ARG A 1 3782 ? 205.220 192.308 286.596 1.00 28.66 ? 3782 ARG A NH1   1 
ATOM   16923 N  NH2   . ARG A 1 3782 ? 205.103 192.592 284.328 1.00 32.74 ? 3782 ARG A NH2   1 
ATOM   16924 N  N     . LYS A 1 3783 ? 208.622 190.384 281.894 1.00 22.61 ? 3783 LYS A N     1 
ATOM   16925 C  CA    . LYS A 1 3783 ? 207.576 190.284 280.879 1.00 20.21 ? 3783 LYS A CA    1 
ATOM   16926 C  C     . LYS A 1 3783 ? 207.980 189.364 279.734 1.00 23.62 ? 3783 LYS A C     1 
ATOM   16927 O  O     . LYS A 1 3783 ? 207.112 188.783 279.075 1.00 29.90 ? 3783 LYS A O     1 
ATOM   16928 C  CB    . LYS A 1 3783 ? 207.226 191.670 280.338 1.00 18.10 ? 3783 LYS A CB    1 
ATOM   16929 C  CG    . LYS A 1 3783 ? 206.640 192.618 281.365 1.00 21.82 ? 3783 LYS A CG    1 
ATOM   16930 C  CD    . LYS A 1 3783 ? 206.774 194.065 280.916 1.00 20.57 ? 3783 LYS A CD    1 
ATOM   16931 C  CE    . LYS A 1 3783 ? 206.919 194.997 282.106 1.00 25.96 ? 3783 LYS A CE    1 
ATOM   16932 N  NZ    . LYS A 1 3783 ? 207.329 196.370 281.698 1.00 25.44 ? 3783 LYS A NZ    1 
ATOM   16933 N  N     . VAL A 1 3784 ? 209.280 189.236 279.463 1.00 20.73 ? 3784 VAL A N     1 
ATOM   16934 C  CA    . VAL A 1 3784 ? 209.727 188.319 278.418 1.00 25.08 ? 3784 VAL A CA    1 
ATOM   16935 C  C     . VAL A 1 3784 ? 209.516 186.874 278.848 1.00 23.65 ? 3784 VAL A C     1 
ATOM   16936 O  O     . VAL A 1 3784 ? 209.121 186.023 278.042 1.00 25.36 ? 3784 VAL A O     1 
ATOM   16937 C  CB    . VAL A 1 3784 ? 211.196 188.594 278.050 1.00 22.66 ? 3784 VAL A CB    1 
ATOM   16938 C  CG1   . VAL A 1 3784 ? 211.693 187.561 277.050 1.00 24.33 ? 3784 VAL A CG1   1 
ATOM   16939 C  CG2   . VAL A 1 3784 ? 211.339 189.985 277.470 1.00 19.87 ? 3784 VAL A CG2   1 
ATOM   16940 N  N     . GLU A 1 3785 ? 209.776 186.571 280.122 1.00 23.21 ? 3785 GLU A N     1 
ATOM   16941 C  CA    . GLU A 1 3785 ? 209.592 185.208 280.612 1.00 25.60 ? 3785 GLU A CA    1 
ATOM   16942 C  C     . GLU A 1 3785 ? 208.134 184.778 280.520 1.00 27.49 ? 3785 GLU A C     1 
ATOM   16943 O  O     . GLU A 1 3785 ? 207.838 183.634 280.151 1.00 26.10 ? 3785 GLU A O     1 
ATOM   16944 C  CB    . GLU A 1 3785 ? 210.097 185.094 282.051 1.00 25.59 ? 3785 GLU A CB    1 
ATOM   16945 C  CG    . GLU A 1 3785 ? 211.594 185.318 282.219 1.00 27.97 ? 3785 GLU A CG    1 
ATOM   16946 C  CD    . GLU A 1 3785 ? 212.432 184.165 281.692 1.00 34.63 ? 3785 GLU A CD    1 
ATOM   16947 O  OE1   . GLU A 1 3785 ? 211.855 183.134 281.287 1.00 34.08 ? 3785 GLU A OE1   1 
ATOM   16948 O  OE2   . GLU A 1 3785 ? 213.674 184.292 281.687 1.00 36.15 ? 3785 GLU A OE2   1 
ATOM   16949 N  N     . GLU A 1 3786 ? 207.205 185.678 280.855 1.00 23.93 ? 3786 GLU A N     1 
ATOM   16950 C  CA    . GLU A 1 3786 ? 205.793 185.322 280.807 1.00 24.60 ? 3786 GLU A CA    1 
ATOM   16951 C  C     . GLU A 1 3786 ? 205.291 185.195 279.374 1.00 26.88 ? 3786 GLU A C     1 
ATOM   16952 O  O     . GLU A 1 3786 ? 204.332 184.460 279.121 1.00 30.33 ? 3786 GLU A O     1 
ATOM   16953 C  CB    . GLU A 1 3786 ? 204.962 186.344 281.586 1.00 21.44 ? 3786 GLU A CB    1 
ATOM   16954 C  CG    . GLU A 1 3786 ? 204.881 187.719 280.948 1.00 30.70 ? 3786 GLU A CG    1 
ATOM   16955 C  CD    . GLU A 1 3786 ? 204.195 188.737 281.839 1.00 37.05 ? 3786 GLU A CD    1 
ATOM   16956 O  OE1   . GLU A 1 3786 ? 203.761 188.362 282.949 1.00 34.83 ? 3786 GLU A OE1   1 
ATOM   16957 O  OE2   . GLU A 1 3786 ? 204.091 189.914 281.430 1.00 34.98 ? 3786 GLU A OE2   1 
ATOM   16958 N  N     . THR A 1 3787 ? 205.914 185.899 278.425 1.00 24.35 ? 3787 THR A N     1 
ATOM   16959 C  CA    . THR A 1 3787 ? 205.560 185.704 277.024 1.00 22.60 ? 3787 THR A CA    1 
ATOM   16960 C  C     . THR A 1 3787 ? 206.176 184.437 276.450 1.00 26.98 ? 3787 THR A C     1 
ATOM   16961 O  O     . THR A 1 3787 ? 205.717 183.955 275.410 1.00 31.95 ? 3787 THR A O     1 
ATOM   16962 C  CB    . THR A 1 3787 ? 205.987 186.907 276.183 1.00 21.55 ? 3787 THR A CB    1 
ATOM   16963 O  OG1   . THR A 1 3787 ? 207.335 187.271 276.508 1.00 30.91 ? 3787 THR A OG1   1 
ATOM   16964 C  CG2   . THR A 1 3787 ? 205.066 188.090 276.434 1.00 22.53 ? 3787 THR A CG2   1 
ATOM   16965 N  N     . ASP A 1 3788 ? 207.208 183.891 277.097 1.00 22.22 ? 3788 ASP A N     1 
ATOM   16966 C  CA    . ASP A 1 3788 ? 207.798 182.645 276.621 1.00 24.09 ? 3788 ASP A CA    1 
ATOM   16967 C  C     . ASP A 1 3788 ? 206.868 181.463 276.860 1.00 23.00 ? 3788 ASP A C     1 
ATOM   16968 O  O     . ASP A 1 3788 ? 206.733 180.587 275.998 1.00 29.36 ? 3788 ASP A O     1 
ATOM   16969 C  CB    . ASP A 1 3788 ? 209.150 182.409 277.294 1.00 24.87 ? 3788 ASP A CB    1 
ATOM   16970 C  CG    . ASP A 1 3788 ? 210.243 183.288 276.724 1.00 32.05 ? 3788 ASP A CG    1 
ATOM   16971 O  OD1   . ASP A 1 3788 ? 209.961 184.054 275.779 1.00 27.44 ? 3788 ASP A OD1   1 
ATOM   16972 O  OD2   . ASP A 1 3788 ? 211.388 183.208 277.217 1.00 37.90 ? 3788 ASP A OD2   1 
ATOM   16973 N  N     . ILE A 1 3789 ? 206.218 181.417 278.027 1.00 26.13 ? 3789 ILE A N     1 
ATOM   16974 C  CA    . ILE A 1 3789 ? 205.356 180.281 278.342 1.00 24.08 ? 3789 ILE A CA    1 
ATOM   16975 C  C     . ILE A 1 3789 ? 204.101 180.292 277.478 1.00 25.75 ? 3789 ILE A C     1 
ATOM   16976 O  O     . ILE A 1 3789 ? 203.600 179.229 277.093 1.00 29.69 ? 3789 ILE A O     1 
ATOM   16977 C  CB    . ILE A 1 3789 ? 205.014 180.259 279.845 1.00 23.51 ? 3789 ILE A CB    1 
ATOM   16978 C  CG1   . ILE A 1 3789 ? 204.240 181.510 280.256 1.00 27.06 ? 3789 ILE A CG1   1 
ATOM   16979 C  CG2   . ILE A 1 3789 ? 206.283 180.136 280.674 1.00 23.20 ? 3789 ILE A CG2   1 
ATOM   16980 C  CD1   . ILE A 1 3789 ? 203.676 181.445 281.656 1.00 28.73 ? 3789 ILE A CD1   1 
ATOM   16981 N  N     . VAL A 1 3790 ? 203.572 181.475 277.159 1.00 24.51 ? 3790 VAL A N     1 
ATOM   16982 C  CA    . VAL A 1 3790 ? 202.346 181.542 276.370 1.00 22.50 ? 3790 VAL A CA    1 
ATOM   16983 C  C     . VAL A 1 3790 ? 202.611 181.126 274.925 1.00 22.73 ? 3790 VAL A C     1 
ATOM   16984 O  O     . VAL A 1 3790 ? 201.739 180.539 274.272 1.00 21.50 ? 3790 VAL A O     1 
ATOM   16985 C  CB    . VAL A 1 3790 ? 201.730 182.951 276.468 1.00 23.90 ? 3790 VAL A CB    1 
ATOM   16986 C  CG1   . VAL A 1 3790 ? 200.432 183.033 275.677 1.00 18.96 ? 3790 VAL A CG1   1 
ATOM   16987 C  CG2   . VAL A 1 3790 ? 201.497 183.324 277.922 1.00 18.89 ? 3790 VAL A CG2   1 
ATOM   16988 N  N     . MET A 1 3791 ? 203.807 181.415 274.398 1.00 23.14 ? 3791 MET A N     1 
ATOM   16989 C  CA    . MET A 1 3791 ? 204.202 180.863 273.104 1.00 21.17 ? 3791 MET A CA    1 
ATOM   16990 C  C     . MET A 1 3791 ? 204.211 179.340 273.121 1.00 24.68 ? 3791 MET A C     1 
ATOM   16991 O  O     . MET A 1 3791 ? 203.863 178.700 272.122 1.00 21.79 ? 3791 MET A O     1 
ATOM   16992 C  CB    . MET A 1 3791 ? 205.574 181.399 272.690 1.00 23.05 ? 3791 MET A CB    1 
ATOM   16993 C  CG    . MET A 1 3791 ? 205.897 181.267 271.197 1.00 24.74 ? 3791 MET A CG    1 
ATOM   16994 S  SD    . MET A 1 3791 ? 204.576 181.567 270.002 1.00 50.92 ? 3791 MET A SD    1 
ATOM   16995 C  CE    . MET A 1 3791 ? 204.139 183.259 270.359 1.00 15.97 ? 3791 MET A CE    1 
ATOM   16996 N  N     . GLN A 1 3792 ? 204.616 178.740 274.243 1.00 21.87 ? 3792 GLN A N     1 
ATOM   16997 C  CA    . GLN A 1 3792 ? 204.573 177.286 274.347 1.00 20.96 ? 3792 GLN A CA    1 
ATOM   16998 C  C     . GLN A 1 3792 ? 203.151 176.761 274.197 1.00 22.56 ? 3792 GLN A C     1 
ATOM   16999 O  O     . GLN A 1 3792 ? 202.947 175.666 273.663 1.00 26.59 ? 3792 GLN A O     1 
ATOM   17000 C  CB    . GLN A 1 3792 ? 205.183 176.833 275.672 1.00 23.16 ? 3792 GLN A CB    1 
ATOM   17001 C  CG    . GLN A 1 3792 ? 206.670 177.128 275.788 1.00 26.33 ? 3792 GLN A CG    1 
ATOM   17002 C  CD    . GLN A 1 3792 ? 207.157 177.138 277.224 1.00 34.19 ? 3792 GLN A CD    1 
ATOM   17003 O  OE1   . GLN A 1 3792 ? 207.730 178.124 277.689 1.00 35.96 ? 3792 GLN A OE1   1 
ATOM   17004 N  NE2   . GLN A 1 3792 ? 206.937 176.037 277.933 1.00 30.76 ? 3792 GLN A NE2   1 
ATOM   17005 N  N     . GLU A 1 3793 ? 202.158 177.525 274.658 1.00 21.55 ? 3793 GLU A N     1 
ATOM   17006 C  CA    . GLU A 1 3793 ? 200.770 177.180 274.379 1.00 22.43 ? 3793 GLU A CA    1 
ATOM   17007 C  C     . GLU A 1 3793 ? 200.462 177.301 272.891 1.00 24.04 ? 3793 GLU A C     1 
ATOM   17008 O  O     . GLU A 1 3793 ? 199.754 176.458 272.326 1.00 24.20 ? 3793 GLU A O     1 
ATOM   17009 C  CB    . GLU A 1 3793 ? 199.836 178.069 275.198 1.00 21.76 ? 3793 GLU A CB    1 
ATOM   17010 C  CG    . GLU A 1 3793 ? 198.355 177.767 275.015 1.00 29.15 ? 3793 GLU A CG    1 
ATOM   17011 C  CD    . GLU A 1 3793 ? 197.964 176.390 275.523 1.00 34.64 ? 3793 GLU A CD    1 
ATOM   17012 O  OE1   . GLU A 1 3793 ? 198.653 175.865 276.422 1.00 34.86 ? 3793 GLU A OE1   1 
ATOM   17013 O  OE2   . GLU A 1 3793 ? 196.965 175.835 275.020 1.00 35.03 ? 3793 GLU A OE2   1 
ATOM   17014 N  N     . VAL A 1 3794 ? 200.975 178.346 272.240 1.00 24.44 ? 3794 VAL A N     1 
ATOM   17015 C  CA    . VAL A 1 3794 ? 200.772 178.505 270.803 1.00 19.30 ? 3794 VAL A CA    1 
ATOM   17016 C  C     . VAL A 1 3794 ? 201.509 177.414 270.034 1.00 20.68 ? 3794 VAL A C     1 
ATOM   17017 O  O     . VAL A 1 3794 ? 200.975 176.841 269.076 1.00 24.22 ? 3794 VAL A O     1 
ATOM   17018 C  CB    . VAL A 1 3794 ? 201.212 179.911 270.356 1.00 16.41 ? 3794 VAL A CB    1 
ATOM   17019 C  CG1   . VAL A 1 3794 ? 201.399 179.965 268.849 1.00 14.23 ? 3794 VAL A CG1   1 
ATOM   17020 C  CG2   . VAL A 1 3794 ? 200.190 180.945 270.799 1.00 14.46 ? 3794 VAL A CG2   1 
ATOM   17021 N  N     . GLU A 1 3795 ? 202.742 177.108 270.442 1.00 25.47 ? 3795 GLU A N     1 
ATOM   17022 C  CA    . GLU A 1 3795 ? 203.548 176.131 269.716 1.00 22.53 ? 3795 GLU A CA    1 
ATOM   17023 C  C     . GLU A 1 3795 ? 202.924 174.741 269.774 1.00 20.03 ? 3795 GLU A C     1 
ATOM   17024 O  O     . GLU A 1 3795 ? 202.910 174.019 268.769 1.00 22.27 ? 3795 GLU A O     1 
ATOM   17025 C  CB    . GLU A 1 3795 ? 204.966 176.105 270.282 1.00 17.44 ? 3795 GLU A CB    1 
ATOM   17026 C  CG    . GLU A 1 3795 ? 205.920 175.157 269.575 1.00 22.61 ? 3795 GLU A CG    1 
ATOM   17027 C  CD    . GLU A 1 3795 ? 206.205 175.562 268.140 1.00 35.47 ? 3795 GLU A CD    1 
ATOM   17028 O  OE1   . GLU A 1 3795 ? 206.097 176.767 267.825 1.00 34.94 ? 3795 GLU A OE1   1 
ATOM   17029 O  OE2   . GLU A 1 3795 ? 206.541 174.676 267.327 1.00 41.72 ? 3795 GLU A OE2   1 
ATOM   17030 N  N     . THR A 1 3796 ? 202.403 174.347 270.938 1.00 18.41 ? 3796 THR A N     1 
ATOM   17031 C  CA    . THR A 1 3796 ? 201.846 173.004 271.072 1.00 21.14 ? 3796 THR A CA    1 
ATOM   17032 C  C     . THR A 1 3796 ? 200.538 172.855 270.301 1.00 20.22 ? 3796 THR A C     1 
ATOM   17033 O  O     . THR A 1 3796 ? 200.214 171.753 269.844 1.00 18.38 ? 3796 THR A O     1 
ATOM   17034 C  CB    . THR A 1 3796 ? 201.649 172.651 272.551 1.00 19.42 ? 3796 THR A CB    1 
ATOM   17035 O  OG1   . THR A 1 3796 ? 201.267 171.277 272.672 1.00 31.99 ? 3796 THR A OG1   1 
ATOM   17036 C  CG2   . THR A 1 3796 ? 200.577 173.519 273.183 1.00 18.79 ? 3796 THR A CG2   1 
ATOM   17037 N  N     . VAL A 1 3797 ? 199.777 173.942 270.146 1.00 19.04 ? 3797 VAL A N     1 
ATOM   17038 C  CA    . VAL A 1 3797 ? 198.601 173.904 269.286 1.00 15.85 ? 3797 VAL A CA    1 
ATOM   17039 C  C     . VAL A 1 3797 ? 199.016 173.811 267.822 1.00 17.03 ? 3797 VAL A C     1 
ATOM   17040 O  O     . VAL A 1 3797 ? 198.430 173.052 267.043 1.00 24.07 ? 3797 VAL A O     1 
ATOM   17041 C  CB    . VAL A 1 3797 ? 197.706 175.131 269.543 1.00 20.56 ? 3797 VAL A CB    1 
ATOM   17042 C  CG1   . VAL A 1 3797 ? 196.559 175.177 268.545 1.00 11.19 ? 3797 VAL A CG1   1 
ATOM   17043 C  CG2   . VAL A 1 3797 ? 197.171 175.107 270.963 1.00 21.50 ? 3797 VAL A CG2   1 
ATOM   17044 N  N     . SER A 1 3798 ? 200.038 174.575 267.430 1.00 15.60 ? 3798 SER A N     1 
ATOM   17045 C  CA    . SER A 1 3798 ? 200.505 174.597 266.050 1.00 17.60 ? 3798 SER A CA    1 
ATOM   17046 C  C     . SER A 1 3798 ? 201.151 173.289 265.617 1.00 14.49 ? 3798 SER A C     1 
ATOM   17047 O  O     . SER A 1 3798 ? 201.291 173.061 264.412 1.00 21.02 ? 3798 SER A O     1 
ATOM   17048 C  CB    . SER A 1 3798 ? 201.498 175.744 265.853 1.00 19.14 ? 3798 SER A CB    1 
ATOM   17049 O  OG    . SER A 1 3798 ? 200.936 176.981 266.245 1.00 18.05 ? 3798 SER A OG    1 
ATOM   17050 N  N     . GLN A 1 3799 ? 201.547 172.433 266.564 1.00 14.53 ? 3799 GLN A N     1 
ATOM   17051 C  CA    . GLN A 1 3799 ? 202.176 171.166 266.204 1.00 12.39 ? 3799 GLN A CA    1 
ATOM   17052 C  C     . GLN A 1 3799 ? 201.211 170.243 265.468 1.00 17.14 ? 3799 GLN A C     1 
ATOM   17053 O  O     . GLN A 1 3799 ? 201.647 169.409 264.667 1.00 21.77 ? 3799 GLN A O     1 
ATOM   17054 C  CB    . GLN A 1 3799 ? 202.712 170.474 267.458 1.00 13.67 ? 3799 GLN A CB    1 
ATOM   17055 C  CG    . GLN A 1 3799 ? 204.070 170.973 267.909 1.00 17.16 ? 3799 GLN A CG    1 
ATOM   17056 C  CD    . GLN A 1 3799 ? 205.171 170.635 266.924 1.00 29.20 ? 3799 GLN A CD    1 
ATOM   17057 O  OE1   . GLN A 1 3799 ? 205.819 171.524 266.371 1.00 33.17 ? 3799 GLN A OE1   1 
ATOM   17058 N  NE2   . GLN A 1 3799 ? 205.390 169.343 266.699 1.00 26.01 ? 3799 GLN A NE2   1 
ATOM   17059 N  N     . GLN A 1 3800 ? 199.909 170.367 265.731 1.00 15.03 ? 3800 GLN A N     1 
ATOM   17060 C  CA    . GLN A 1 3800 ? 198.934 169.518 265.056 1.00 10.35 ? 3800 GLN A CA    1 
ATOM   17061 C  C     . GLN A 1 3800 ? 198.846 169.831 263.569 1.00 12.03 ? 3800 GLN A C     1 
ATOM   17062 O  O     . GLN A 1 3800 ? 198.613 168.928 262.759 1.00 13.64 ? 3800 GLN A O     1 
ATOM   17063 C  CB    . GLN A 1 3800 ? 197.562 169.672 265.712 1.00 13.62 ? 3800 GLN A CB    1 
ATOM   17064 C  CG    . GLN A 1 3800 ? 196.587 168.559 265.380 1.00 14.89 ? 3800 GLN A CG    1 
ATOM   17065 C  CD    . GLN A 1 3800 ? 195.174 168.876 265.812 1.00 18.24 ? 3800 GLN A CD    1 
ATOM   17066 O  OE1   . GLN A 1 3800 ? 194.875 169.998 266.222 1.00 25.34 ? 3800 GLN A OE1   1 
ATOM   17067 N  NE2   . GLN A 1 3800 ? 194.292 167.890 265.726 1.00 20.26 ? 3800 GLN A NE2   1 
ATOM   17068 N  N     . TYR A 1 3801 ? 199.034 171.092 263.192 1.00 11.76 ? 3801 TYR A N     1 
ATOM   17069 C  CA    . TYR A 1 3801 ? 198.925 171.520 261.805 1.00 5.46  ? 3801 TYR A CA    1 
ATOM   17070 C  C     . TYR A 1 3801 ? 200.254 171.493 261.066 1.00 7.45  ? 3801 TYR A C     1 
ATOM   17071 O  O     . TYR A 1 3801 ? 200.304 171.884 259.896 1.00 12.44 ? 3801 TYR A O     1 
ATOM   17072 C  CB    . TYR A 1 3801 ? 198.330 172.929 261.742 1.00 5.21  ? 3801 TYR A CB    1 
ATOM   17073 C  CG    . TYR A 1 3801 ? 196.968 173.036 262.380 1.00 8.35  ? 3801 TYR A CG    1 
ATOM   17074 C  CD1   . TYR A 1 3801 ? 195.818 172.780 261.651 1.00 8.18  ? 3801 TYR A CD1   1 
ATOM   17075 C  CD2   . TYR A 1 3801 ? 196.832 173.384 263.717 1.00 11.72 ? 3801 TYR A CD2   1 
ATOM   17076 C  CE1   . TYR A 1 3801 ? 194.571 172.870 262.230 1.00 6.45  ? 3801 TYR A CE1   1 
ATOM   17077 C  CE2   . TYR A 1 3801 ? 195.588 173.478 264.305 1.00 10.70 ? 3801 TYR A CE2   1 
ATOM   17078 C  CZ    . TYR A 1 3801 ? 194.461 173.220 263.557 1.00 8.74  ? 3801 TYR A CZ    1 
ATOM   17079 O  OH    . TYR A 1 3801 ? 193.218 173.313 264.137 1.00 19.06 ? 3801 TYR A OH    1 
ATOM   17080 N  N     . LEU A 1 3802 ? 201.328 171.052 261.719 1.00 8.67  ? 3802 LEU A N     1 
ATOM   17081 C  CA    . LEU A 1 3802 ? 202.629 170.988 261.054 1.00 7.77  ? 3802 LEU A CA    1 
ATOM   17082 C  C     . LEU A 1 3802 ? 202.646 170.035 259.864 1.00 4.39  ? 3802 LEU A C     1 
ATOM   17083 O  O     . LEU A 1 3802 ? 203.203 170.408 258.817 1.00 4.26  ? 3802 LEU A O     1 
ATOM   17084 C  CB    . LEU A 1 3802 ? 203.709 170.636 262.082 1.00 10.93 ? 3802 LEU A CB    1 
ATOM   17085 C  CG    . LEU A 1 3802 ? 205.151 170.588 261.578 1.00 13.47 ? 3802 LEU A CG    1 
ATOM   17086 C  CD1   . LEU A 1 3802 ? 205.579 171.954 261.078 1.00 8.44  ? 3802 LEU A CD1   1 
ATOM   17087 C  CD2   . LEU A 1 3802 ? 206.082 170.108 262.678 1.00 17.30 ? 3802 LEU A CD2   1 
ATOM   17088 N  N     . PRO A 1 3803 ? 202.093 168.815 259.937 1.00 9.24  ? 3803 PRO A N     1 
ATOM   17089 C  CA    . PRO A 1 3803 ? 202.109 167.947 258.745 1.00 3.73  ? 3803 PRO A CA    1 
ATOM   17090 C  C     . PRO A 1 3803 ? 201.382 168.529 257.544 1.00 3.88  ? 3803 PRO A C     1 
ATOM   17091 O  O     . PRO A 1 3803 ? 201.790 168.267 256.406 1.00 2.83  ? 3803 PRO A O     1 
ATOM   17092 C  CB    . PRO A 1 3803 ? 201.435 166.662 259.246 1.00 2.19  ? 3803 PRO A CB    1 
ATOM   17093 C  CG    . PRO A 1 3803 ? 201.693 166.663 260.701 1.00 4.11  ? 3803 PRO A CG    1 
ATOM   17094 C  CD    . PRO A 1 3803 ? 201.548 168.094 261.102 1.00 7.48  ? 3803 PRO A CD    1 
ATOM   17095 N  N     . LEU A 1 3804 ? 200.311 169.297 257.757 1.00 3.53  ? 3804 LEU A N     1 
ATOM   17096 C  CA    . LEU A 1 3804 ? 199.624 169.927 256.634 1.00 2.74  ? 3804 LEU A CA    1 
ATOM   17097 C  C     . LEU A 1 3804 ? 200.516 170.949 255.939 1.00 3.48  ? 3804 LEU A C     1 
ATOM   17098 O  O     . LEU A 1 3804 ? 200.537 171.027 254.707 1.00 2.83  ? 3804 LEU A O     1 
ATOM   17099 C  CB    . LEU A 1 3804 ? 198.329 170.580 257.112 1.00 2.89  ? 3804 LEU A CB    1 
ATOM   17100 C  CG    . LEU A 1 3804 ? 197.529 171.333 256.048 1.00 2.75  ? 3804 LEU A CG    1 
ATOM   17101 C  CD1   . LEU A 1 3804 ? 196.929 170.368 255.039 1.00 3.19  ? 3804 LEU A CD1   1 
ATOM   17102 C  CD2   . LEU A 1 3804 ? 196.452 172.192 256.686 1.00 1.77  ? 3804 LEU A CD2   1 
ATOM   17103 N  N     . SER A 1 3805 ? 201.257 171.744 256.716 1.00 3.73  ? 3805 SER A N     1 
ATOM   17104 C  CA    . SER A 1 3805 ? 202.154 172.733 256.126 1.00 2.06  ? 3805 SER A CA    1 
ATOM   17105 C  C     . SER A 1 3805 ? 203.281 172.065 255.347 1.00 2.42  ? 3805 SER A C     1 
ATOM   17106 O  O     . SER A 1 3805 ? 203.697 172.563 254.295 1.00 1.55  ? 3805 SER A O     1 
ATOM   17107 C  CB    . SER A 1 3805 ? 202.714 173.648 257.215 1.00 3.16  ? 3805 SER A CB    1 
ATOM   17108 O  OG    . SER A 1 3805 ? 203.519 172.928 258.129 1.00 7.78  ? 3805 SER A OG    1 
ATOM   17109 N  N     . THR A 1 3806 ? 203.795 170.941 255.855 1.00 2.71  ? 3806 THR A N     1 
ATOM   17110 C  CA    . THR A 1 3806 ? 204.783 170.177 255.100 1.00 2.10  ? 3806 THR A CA    1 
ATOM   17111 C  C     . THR A 1 3806 ? 204.192 169.654 253.799 1.00 2.52  ? 3806 THR A C     1 
ATOM   17112 O  O     . THR A 1 3806 ? 204.852 169.677 252.754 1.00 3.88  ? 3806 THR A O     1 
ATOM   17113 C  CB    . THR A 1 3806 ? 205.315 169.022 255.950 1.00 1.96  ? 3806 THR A CB    1 
ATOM   17114 O  OG1   . THR A 1 3806 ? 205.791 169.527 257.202 1.00 6.68  ? 3806 THR A OG1   1 
ATOM   17115 C  CG2   . THR A 1 3806 ? 206.449 168.310 255.233 1.00 1.55  ? 3806 THR A CG2   1 
ATOM   17116 N  N     . ALA A 1 3807 ? 202.946 169.176 253.844 1.00 2.05  ? 3807 ALA A N     1 
ATOM   17117 C  CA    . ALA A 1 3807 ? 202.280 168.738 252.623 1.00 1.58  ? 3807 ALA A CA    1 
ATOM   17118 C  C     . ALA A 1 3807 ? 202.103 169.896 251.650 1.00 1.14  ? 3807 ALA A C     1 
ATOM   17119 O  O     . ALA A 1 3807 ? 202.266 169.727 250.437 1.00 1.05  ? 3807 ALA A O     1 
ATOM   17120 C  CB    . ALA A 1 3807 ? 200.928 168.107 252.959 1.00 1.30  ? 3807 ALA A CB    1 
ATOM   17121 N  N     . CYS A 1 3808 ? 201.777 171.083 252.165 1.00 1.09  ? 3808 CYS A N     1 
ATOM   17122 C  CA    . CYS A 1 3808 ? 201.599 172.246 251.304 1.00 1.13  ? 3808 CYS A CA    1 
ATOM   17123 C  C     . CYS A 1 3808 ? 202.881 172.588 250.554 1.00 1.18  ? 3808 CYS A C     1 
ATOM   17124 O  O     . CYS A 1 3808 ? 202.849 172.865 249.349 1.00 1.08  ? 3808 CYS A O     1 
ATOM   17125 C  CB    . CYS A 1 3808 ? 201.135 173.442 252.130 1.00 1.05  ? 3808 CYS A CB    1 
ATOM   17126 S  SG    . CYS A 1 3808 ? 199.386 173.448 252.540 1.00 7.26  ? 3808 CYS A SG    1 
ATOM   17127 N  N     . SER A 1 3809 ? 204.021 172.578 251.249 1.00 1.60  ? 3809 SER A N     1 
ATOM   17128 C  CA    . SER A 1 3809 ? 205.279 172.918 250.595 1.00 1.71  ? 3809 SER A CA    1 
ATOM   17129 C  C     . SER A 1 3809 ? 205.687 171.852 249.586 1.00 1.09  ? 3809 SER A C     1 
ATOM   17130 O  O     . SER A 1 3809 ? 206.189 172.174 248.505 1.00 0.97  ? 3809 SER A O     1 
ATOM   17131 C  CB    . SER A 1 3809 ? 206.378 173.134 251.637 1.00 2.58  ? 3809 SER A CB    1 
ATOM   17132 O  OG    . SER A 1 3809 ? 206.677 171.939 252.334 1.00 7.34  ? 3809 SER A OG    1 
ATOM   17133 N  N     . SER A 1 3810 ? 205.479 170.575 249.919 1.00 1.40  ? 3810 SER A N     1 
ATOM   17134 C  CA    . SER A 1 3810 ? 205.803 169.510 248.976 1.00 1.15  ? 3810 SER A CA    1 
ATOM   17135 C  C     . SER A 1 3810 ? 204.929 169.592 247.730 1.00 1.02  ? 3810 SER A C     1 
ATOM   17136 O  O     . SER A 1 3810 ? 205.406 169.359 246.615 1.00 1.31  ? 3810 SER A O     1 
ATOM   17137 C  CB    . SER A 1 3810 ? 205.655 168.142 249.644 1.00 1.48  ? 3810 SER A CB    1 
ATOM   17138 O  OG    . SER A 1 3810 ? 206.297 168.109 250.904 1.00 5.44  ? 3810 SER A OG    1 
ATOM   17139 N  N     . ILE A 1 3811 ? 203.646 169.916 247.903 1.00 0.73  ? 3811 ILE A N     1 
ATOM   17140 C  CA    . ILE A 1 3811 ? 202.739 170.005 246.761 1.00 0.75  ? 3811 ILE A CA    1 
ATOM   17141 C  C     . ILE A 1 3811 ? 203.156 171.139 245.834 1.00 0.78  ? 3811 ILE A C     1 
ATOM   17142 O  O     . ILE A 1 3811 ? 203.220 170.971 244.610 1.00 2.46  ? 3811 ILE A O     1 
ATOM   17143 C  CB    . ILE A 1 3811 ? 201.284 170.174 247.239 1.00 0.73  ? 3811 ILE A CB    1 
ATOM   17144 C  CG1   . ILE A 1 3811 ? 200.760 168.863 247.829 1.00 0.52  ? 3811 ILE A CG1   1 
ATOM   17145 C  CG2   . ILE A 1 3811 ? 200.390 170.637 246.096 1.00 0.49  ? 3811 ILE A CG2   1 
ATOM   17146 C  CD1   . ILE A 1 3811 ? 199.389 168.978 248.439 1.00 0.59  ? 3811 ILE A CD1   1 
ATOM   17147 N  N     . TYR A 1 3812 ? 203.453 172.312 246.403 1.00 0.88  ? 3812 TYR A N     1 
ATOM   17148 C  CA    . TYR A 1 3812 ? 203.829 173.449 245.568 1.00 0.61  ? 3812 TYR A CA    1 
ATOM   17149 C  C     . TYR A 1 3812 ? 205.139 173.192 244.839 1.00 0.52  ? 3812 TYR A C     1 
ATOM   17150 O  O     . TYR A 1 3812 ? 205.261 173.491 243.645 1.00 0.79  ? 3812 TYR A O     1 
ATOM   17151 C  CB    . TYR A 1 3812 ? 203.936 174.723 246.403 1.00 0.88  ? 3812 TYR A CB    1 
ATOM   17152 C  CG    . TYR A 1 3812 ? 204.561 175.863 245.633 1.00 1.08  ? 3812 TYR A CG    1 
ATOM   17153 C  CD1   . TYR A 1 3812 ? 203.835 176.546 244.668 1.00 0.68  ? 3812 TYR A CD1   1 
ATOM   17154 C  CD2   . TYR A 1 3812 ? 205.882 176.241 245.847 1.00 0.57  ? 3812 TYR A CD2   1 
ATOM   17155 C  CE1   . TYR A 1 3812 ? 204.397 177.575 243.949 1.00 1.04  ? 3812 TYR A CE1   1 
ATOM   17156 C  CE2   . TYR A 1 3812 ? 206.453 177.273 245.132 1.00 0.55  ? 3812 TYR A CE2   1 
ATOM   17157 C  CZ    . TYR A 1 3812 ? 205.705 177.939 244.185 1.00 1.26  ? 3812 TYR A CZ    1 
ATOM   17158 O  OH    . TYR A 1 3812 ? 206.258 178.971 243.465 1.00 2.03  ? 3812 TYR A OH    1 
ATOM   17159 N  N     . PHE A 1 3813 ? 206.133 172.646 245.539 1.00 0.93  ? 3813 PHE A N     1 
ATOM   17160 C  CA    . PHE A 1 3813 ? 207.414 172.373 244.901 1.00 0.88  ? 3813 PHE A CA    1 
ATOM   17161 C  C     . PHE A 1 3813 ? 207.317 171.242 243.888 1.00 1.14  ? 3813 PHE A C     1 
ATOM   17162 O  O     . PHE A 1 3813 ? 208.144 171.177 242.973 1.00 1.31  ? 3813 PHE A O     1 
ATOM   17163 C  CB    . PHE A 1 3813 ? 208.471 172.078 245.965 1.00 1.36  ? 3813 PHE A CB    1 
ATOM   17164 C  CG    . PHE A 1 3813 ? 209.128 173.316 246.509 1.00 1.98  ? 3813 PHE A CG    1 
ATOM   17165 C  CD1   . PHE A 1 3813 ? 208.576 173.995 247.580 1.00 2.70  ? 3813 PHE A CD1   1 
ATOM   17166 C  CD2   . PHE A 1 3813 ? 210.280 173.815 245.930 1.00 3.78  ? 3813 PHE A CD2   1 
ATOM   17167 C  CE1   . PHE A 1 3813 ? 209.166 175.143 248.073 1.00 1.67  ? 3813 PHE A CE1   1 
ATOM   17168 C  CE2   . PHE A 1 3813 ? 210.879 174.963 246.419 1.00 4.50  ? 3813 PHE A CE2   1 
ATOM   17169 C  CZ    . PHE A 1 3813 ? 210.319 175.627 247.493 1.00 2.53  ? 3813 PHE A CZ    1 
ATOM   17170 N  N     . THR A 1 3814 ? 206.333 170.353 244.030 1.00 1.38  ? 3814 THR A N     1 
ATOM   17171 C  CA    . THR A 1 3814 ? 206.022 169.420 242.953 1.00 1.03  ? 3814 THR A CA    1 
ATOM   17172 C  C     . THR A 1 3814 ? 205.413 170.150 241.761 1.00 0.89  ? 3814 THR A C     1 
ATOM   17173 O  O     . THR A 1 3814 ? 205.783 169.887 240.611 1.00 0.94  ? 3814 THR A O     1 
ATOM   17174 C  CB    . THR A 1 3814 ? 205.079 168.328 243.460 1.00 1.25  ? 3814 THR A CB    1 
ATOM   17175 O  OG1   . THR A 1 3814 ? 205.752 167.537 244.449 1.00 3.89  ? 3814 THR A OG1   1 
ATOM   17176 C  CG2   . THR A 1 3814 ? 204.636 167.427 242.321 1.00 1.25  ? 3814 THR A CG2   1 
ATOM   17177 N  N     . MET A 1 3815 ? 204.492 171.081 242.021 1.00 0.79  ? 3815 MET A N     1 
ATOM   17178 C  CA    . MET A 1 3815 ? 203.925 171.897 240.950 1.00 0.74  ? 3815 MET A CA    1 
ATOM   17179 C  C     . MET A 1 3815 ? 204.998 172.726 240.259 1.00 0.97  ? 3815 MET A C     1 
ATOM   17180 O  O     . MET A 1 3815 ? 204.998 172.858 239.032 1.00 2.09  ? 3815 MET A O     1 
ATOM   17181 C  CB    . MET A 1 3815 ? 202.837 172.811 241.512 1.00 0.62  ? 3815 MET A CB    1 
ATOM   17182 C  CG    . MET A 1 3815 ? 201.626 172.103 242.083 1.00 0.47  ? 3815 MET A CG    1 
ATOM   17183 S  SD    . MET A 1 3815 ? 200.505 173.254 242.903 1.00 12.79 ? 3815 MET A SD    1 
ATOM   17184 C  CE    . MET A 1 3815 ? 200.123 174.379 241.567 1.00 0.52  ? 3815 MET A CE    1 
ATOM   17185 N  N     . GLU A 1 3816 ? 205.919 173.296 241.039 1.00 1.75  ? 3816 GLU A N     1 
ATOM   17186 C  CA    . GLU A 1 3816 ? 206.973 174.128 240.472 1.00 1.81  ? 3816 GLU A CA    1 
ATOM   17187 C  C     . GLU A 1 3816 ? 207.883 173.329 239.548 1.00 1.76  ? 3816 GLU A C     1 
ATOM   17188 O  O     . GLU A 1 3816 ? 208.442 173.883 238.595 1.00 4.28  ? 3816 GLU A O     1 
ATOM   17189 C  CB    . GLU A 1 3816 ? 207.778 174.774 241.602 1.00 2.07  ? 3816 GLU A CB    1 
ATOM   17190 C  CG    . GLU A 1 3816 ? 208.888 175.710 241.152 1.00 6.35  ? 3816 GLU A CG    1 
ATOM   17191 C  CD    . GLU A 1 3816 ? 208.362 176.940 240.436 1.00 22.30 ? 3816 GLU A CD    1 
ATOM   17192 O  OE1   . GLU A 1 3816 ? 207.203 177.332 240.694 1.00 22.74 ? 3816 GLU A OE1   1 
ATOM   17193 O  OE2   . GLU A 1 3816 ? 209.111 177.519 239.621 1.00 18.20 ? 3816 GLU A OE2   1 
ATOM   17194 N  N     . SER A 1 3817 ? 208.038 172.033 239.803 1.00 1.77  ? 3817 SER A N     1 
ATOM   17195 C  CA    . SER A 1 3817 ? 208.889 171.177 238.990 1.00 2.05  ? 3817 SER A CA    1 
ATOM   17196 C  C     . SER A 1 3817 ? 208.181 170.624 237.760 1.00 2.18  ? 3817 SER A C     1 
ATOM   17197 O  O     . SER A 1 3817 ? 208.834 170.000 236.919 1.00 3.50  ? 3817 SER A O     1 
ATOM   17198 C  CB    . SER A 1 3817 ? 209.425 170.017 239.833 1.00 2.03  ? 3817 SER A CB    1 
ATOM   17199 O  OG    . SER A 1 3817 ? 208.387 169.416 240.587 1.00 12.12 ? 3817 SER A OG    1 
ATOM   17200 N  N     . LEU A 1 3818 ? 206.870 170.844 237.628 1.00 2.15  ? 3818 LEU A N     1 
ATOM   17201 C  CA    . LEU A 1 3818 ? 206.144 170.339 236.469 1.00 1.16  ? 3818 LEU A CA    1 
ATOM   17202 C  C     . LEU A 1 3818 ? 206.566 171.025 235.176 1.00 1.61  ? 3818 LEU A C     1 
ATOM   17203 O  O     . LEU A 1 3818 ? 206.299 170.493 234.094 1.00 1.99  ? 3818 LEU A O     1 
ATOM   17204 C  CB    . LEU A 1 3818 ? 204.639 170.497 236.680 1.00 1.11  ? 3818 LEU A CB    1 
ATOM   17205 C  CG    . LEU A 1 3818 ? 203.981 169.406 237.529 1.00 0.60  ? 3818 LEU A CG    1 
ATOM   17206 C  CD1   . LEU A 1 3818 ? 202.596 169.831 237.982 1.00 0.33  ? 3818 LEU A CD1   1 
ATOM   17207 C  CD2   . LEU A 1 3818 ? 203.922 168.092 236.769 1.00 0.71  ? 3818 LEU A CD2   1 
ATOM   17208 N  N     . LYS A 1 3819 ? 207.222 172.184 235.260 1.00 2.20  ? 3819 LYS A N     1 
ATOM   17209 C  CA    . LYS A 1 3819 ? 207.756 172.832 234.069 1.00 1.51  ? 3819 LYS A CA    1 
ATOM   17210 C  C     . LYS A 1 3819 ? 208.873 172.022 233.423 1.00 2.46  ? 3819 LYS A C     1 
ATOM   17211 O  O     . LYS A 1 3819 ? 209.195 172.260 232.255 1.00 3.03  ? 3819 LYS A O     1 
ATOM   17212 C  CB    . LYS A 1 3819 ? 208.270 174.231 234.416 1.00 1.35  ? 3819 LYS A CB    1 
ATOM   17213 C  CG    . LYS A 1 3819 ? 209.552 174.230 235.230 1.00 1.30  ? 3819 LYS A CG    1 
ATOM   17214 C  CD    . LYS A 1 3819 ? 210.220 175.590 235.235 1.00 1.31  ? 3819 LYS A CD    1 
ATOM   17215 C  CE    . LYS A 1 3819 ? 209.458 176.586 236.087 1.00 3.02  ? 3819 LYS A CE    1 
ATOM   17216 N  NZ    . LYS A 1 3819 ? 209.519 176.239 237.528 1.00 3.49  ? 3819 LYS A NZ    1 
ATOM   17217 N  N     . GLN A 1 3820 ? 209.467 171.074 234.152 1.00 3.34  ? 3820 GLN A N     1 
ATOM   17218 C  CA    . GLN A 1 3820 ? 210.535 170.258 233.590 1.00 3.30  ? 3820 GLN A CA    1 
ATOM   17219 C  C     . GLN A 1 3820 ? 210.026 169.248 232.572 1.00 3.32  ? 3820 GLN A C     1 
ATOM   17220 O  O     . GLN A 1 3820 ? 210.791 168.834 231.696 1.00 11.08 ? 3820 GLN A O     1 
ATOM   17221 C  CB    . GLN A 1 3820 ? 211.292 169.529 234.702 1.00 4.11  ? 3820 GLN A CB    1 
ATOM   17222 C  CG    . GLN A 1 3820 ? 211.892 170.433 235.765 1.00 2.66  ? 3820 GLN A CG    1 
ATOM   17223 C  CD    . GLN A 1 3820 ? 212.783 171.513 235.185 1.00 9.73  ? 3820 GLN A CD    1 
ATOM   17224 O  OE1   . GLN A 1 3820 ? 212.605 172.697 235.469 1.00 12.82 ? 3820 GLN A OE1   1 
ATOM   17225 N  NE2   . GLN A 1 3820 ? 213.746 171.109 234.366 1.00 13.57 ? 3820 GLN A NE2   1 
ATOM   17226 N  N     . ILE A 1 3821 ? 208.761 168.838 232.664 1.00 2.47  ? 3821 ILE A N     1 
ATOM   17227 C  CA    . ILE A 1 3821 ? 208.228 167.828 231.757 1.00 2.55  ? 3821 ILE A CA    1 
ATOM   17228 C  C     . ILE A 1 3821 ? 207.415 168.424 230.610 1.00 2.83  ? 3821 ILE A C     1 
ATOM   17229 O  O     . ILE A 1 3821 ? 207.208 167.739 229.598 1.00 3.71  ? 3821 ILE A O     1 
ATOM   17230 C  CB    . ILE A 1 3821 ? 207.381 166.790 232.523 1.00 2.03  ? 3821 ILE A CB    1 
ATOM   17231 C  CG1   . ILE A 1 3821 ? 206.083 167.418 233.032 1.00 2.84  ? 3821 ILE A CG1   1 
ATOM   17232 C  CG2   . ILE A 1 3821 ? 208.179 166.206 233.676 1.00 2.04  ? 3821 ILE A CG2   1 
ATOM   17233 C  CD1   . ILE A 1 3821 ? 205.105 166.417 233.592 1.00 1.69  ? 3821 ILE A CD1   1 
ATOM   17234 N  N     . HIS A 1 3822 ? 206.952 169.665 230.733 1.00 2.74  ? 3822 HIS A N     1 
ATOM   17235 C  CA    . HIS A 1 3822 ? 206.254 170.332 229.644 1.00 1.17  ? 3822 HIS A CA    1 
ATOM   17236 C  C     . HIS A 1 3822 ? 206.362 171.836 229.843 1.00 1.25  ? 3822 HIS A C     1 
ATOM   17237 O  O     . HIS A 1 3822 ? 206.197 172.330 230.960 1.00 3.99  ? 3822 HIS A O     1 
ATOM   17238 C  CB    . HIS A 1 3822 ? 204.782 169.909 229.572 1.00 1.26  ? 3822 HIS A CB    1 
ATOM   17239 C  CG    . HIS A 1 3822 ? 204.180 170.058 228.210 1.00 1.11  ? 3822 HIS A CG    1 
ATOM   17240 N  ND1   . HIS A 1 3822 ? 203.853 171.284 227.672 1.00 1.79  ? 3822 HIS A ND1   1 
ATOM   17241 C  CD2   . HIS A 1 3822 ? 203.849 169.136 227.277 1.00 1.17  ? 3822 HIS A CD2   1 
ATOM   17242 C  CE1   . HIS A 1 3822 ? 203.347 171.110 226.465 1.00 1.75  ? 3822 HIS A CE1   1 
ATOM   17243 N  NE2   . HIS A 1 3822 ? 203.332 169.816 226.203 1.00 4.69  ? 3822 HIS A NE2   1 
ATOM   17244 N  N     . PHE A 1 3823 ? 206.635 172.554 228.752 1.00 1.60  ? 3823 PHE A N     1 
ATOM   17245 C  CA    . PHE A 1 3823 ? 206.777 174.004 228.827 1.00 1.62  ? 3823 PHE A CA    1 
ATOM   17246 C  C     . PHE A 1 3823 ? 205.483 174.696 229.233 1.00 1.23  ? 3823 PHE A C     1 
ATOM   17247 O  O     . PHE A 1 3823 ? 205.528 175.821 229.739 1.00 3.13  ? 3823 PHE A O     1 
ATOM   17248 C  CB    . PHE A 1 3823 ? 207.269 174.559 227.487 1.00 1.43  ? 3823 PHE A CB    1 
ATOM   17249 C  CG    . PHE A 1 3823 ? 206.332 174.306 226.335 1.00 2.05  ? 3823 PHE A CG    1 
ATOM   17250 C  CD1   . PHE A 1 3823 ? 205.277 175.165 226.076 1.00 1.77  ? 3823 PHE A CD1   1 
ATOM   17251 C  CD2   . PHE A 1 3823 ? 206.513 173.212 225.509 1.00 2.23  ? 3823 PHE A CD2   1 
ATOM   17252 C  CE1   . PHE A 1 3823 ? 204.418 174.930 225.026 1.00 0.92  ? 3823 PHE A CE1   1 
ATOM   17253 C  CE2   . PHE A 1 3823 ? 205.659 172.977 224.452 1.00 1.25  ? 3823 PHE A CE2   1 
ATOM   17254 C  CZ    . PHE A 1 3823 ? 204.611 173.836 224.210 1.00 0.99  ? 3823 PHE A CZ    1 
ATOM   17255 N  N     . LEU A 1 3824 ? 204.335 174.053 229.024 1.00 0.83  ? 3824 LEU A N     1 
ATOM   17256 C  CA    . LEU A 1 3824 ? 203.054 174.662 229.350 1.00 0.89  ? 3824 LEU A CA    1 
ATOM   17257 C  C     . LEU A 1 3824 ? 202.756 174.661 230.843 1.00 0.54  ? 3824 LEU A C     1 
ATOM   17258 O  O     . LEU A 1 3824 ? 201.930 175.459 231.295 1.00 0.39  ? 3824 LEU A O     1 
ATOM   17259 C  CB    . LEU A 1 3824 ? 201.933 173.941 228.598 1.00 0.91  ? 3824 LEU A CB    1 
ATOM   17260 C  CG    . LEU A 1 3824 ? 200.555 174.604 228.561 1.00 0.42  ? 3824 LEU A CG    1 
ATOM   17261 C  CD1   . LEU A 1 3824 ? 200.597 175.883 227.745 1.00 0.98  ? 3824 LEU A CD1   1 
ATOM   17262 C  CD2   . LEU A 1 3824 ? 199.514 173.648 228.013 1.00 0.27  ? 3824 LEU A CD2   1 
ATOM   17263 N  N     . TYR A 1 3825 ? 203.417 173.805 231.622 1.00 1.38  ? 3825 TYR A N     1 
ATOM   17264 C  CA    . TYR A 1 3825 ? 203.076 173.629 233.035 1.00 0.83  ? 3825 TYR A CA    1 
ATOM   17265 C  C     . TYR A 1 3825 ? 203.798 174.691 233.858 1.00 0.57  ? 3825 TYR A C     1 
ATOM   17266 O  O     . TYR A 1 3825 ? 204.785 174.433 234.550 1.00 1.52  ? 3825 TYR A O     1 
ATOM   17267 C  CB    . TYR A 1 3825 ? 203.422 172.222 233.507 1.00 0.63  ? 3825 TYR A CB    1 
ATOM   17268 C  CG    . TYR A 1 3825 ? 202.787 171.104 232.704 1.00 0.94  ? 3825 TYR A CG    1 
ATOM   17269 C  CD1   . TYR A 1 3825 ? 201.716 171.347 231.851 1.00 0.91  ? 3825 TYR A CD1   1 
ATOM   17270 C  CD2   . TYR A 1 3825 ? 203.254 169.802 232.811 1.00 1.01  ? 3825 TYR A CD2   1 
ATOM   17271 C  CE1   . TYR A 1 3825 ? 201.144 170.330 231.120 1.00 0.66  ? 3825 TYR A CE1   1 
ATOM   17272 C  CE2   . TYR A 1 3825 ? 202.683 168.779 232.087 1.00 0.71  ? 3825 TYR A CE2   1 
ATOM   17273 C  CZ    . TYR A 1 3825 ? 201.628 169.047 231.244 1.00 0.54  ? 3825 TYR A CZ    1 
ATOM   17274 O  OH    . TYR A 1 3825 ? 201.058 168.027 230.523 1.00 0.86  ? 3825 TYR A OH    1 
ATOM   17275 N  N     . GLN A 1 3826 ? 203.283 175.914 233.780 1.00 0.72  ? 3826 GLN A N     1 
ATOM   17276 C  CA    . GLN A 1 3826 ? 203.796 177.046 234.539 1.00 0.39  ? 3826 GLN A CA    1 
ATOM   17277 C  C     . GLN A 1 3826 ? 202.787 177.394 235.622 1.00 0.58  ? 3826 GLN A C     1 
ATOM   17278 O  O     . GLN A 1 3826 ? 201.615 177.646 235.321 1.00 0.95  ? 3826 GLN A O     1 
ATOM   17279 C  CB    . GLN A 1 3826 ? 204.046 178.252 233.635 1.00 0.64  ? 3826 GLN A CB    1 
ATOM   17280 C  CG    . GLN A 1 3826 ? 204.903 177.972 232.411 1.00 0.61  ? 3826 GLN A CG    1 
ATOM   17281 C  CD    . GLN A 1 3826 ? 206.221 177.310 232.743 1.00 0.90  ? 3826 GLN A CD    1 
ATOM   17282 O  OE1   . GLN A 1 3826 ? 207.026 177.844 233.503 1.00 1.77  ? 3826 GLN A OE1   1 
ATOM   17283 N  NE2   . GLN A 1 3826 ? 206.457 176.145 232.156 1.00 0.99  ? 3826 GLN A NE2   1 
ATOM   17284 N  N     . TYR A 1 3827 ? 203.233 177.410 236.873 1.00 0.92  ? 3827 TYR A N     1 
ATOM   17285 C  CA    . TYR A 1 3827 ? 202.353 177.655 238.007 1.00 1.31  ? 3827 TYR A CA    1 
ATOM   17286 C  C     . TYR A 1 3827 ? 203.022 178.605 238.984 1.00 1.88  ? 3827 TYR A C     1 
ATOM   17287 O  O     . TYR A 1 3827 ? 204.131 178.338 239.455 1.00 5.72  ? 3827 TYR A O     1 
ATOM   17288 C  CB    . TYR A 1 3827 ? 201.979 176.345 238.700 1.00 0.89  ? 3827 TYR A CB    1 
ATOM   17289 C  CG    . TYR A 1 3827 ? 201.349 175.357 237.754 1.00 0.88  ? 3827 TYR A CG    1 
ATOM   17290 C  CD1   . TYR A 1 3827 ? 200.094 175.596 237.212 1.00 0.70  ? 3827 TYR A CD1   1 
ATOM   17291 C  CD2   . TYR A 1 3827 ? 202.019 174.206 237.372 1.00 0.78  ? 3827 TYR A CD2   1 
ATOM   17292 C  CE1   . TYR A 1 3827 ? 199.520 174.707 236.336 1.00 1.61  ? 3827 TYR A CE1   1 
ATOM   17293 C  CE2   . TYR A 1 3827 ? 201.451 173.311 236.497 1.00 0.66  ? 3827 TYR A CE2   1 
ATOM   17294 C  CZ    . TYR A 1 3827 ? 200.202 173.565 235.979 1.00 0.74  ? 3827 TYR A CZ    1 
ATOM   17295 O  OH    . TYR A 1 3827 ? 199.629 172.672 235.105 1.00 1.42  ? 3827 TYR A OH    1 
ATOM   17296 N  N     . SER A 1 3828 ? 202.344 179.705 239.285 1.00 2.13  ? 3828 SER A N     1 
ATOM   17297 C  CA    . SER A 1 3828 ? 202.846 180.668 240.246 1.00 1.16  ? 3828 SER A CA    1 
ATOM   17298 C  C     . SER A 1 3828 ? 202.534 180.209 241.667 1.00 1.57  ? 3828 SER A C     1 
ATOM   17299 O  O     . SER A 1 3828 ? 201.785 179.254 241.895 1.00 2.72  ? 3828 SER A O     1 
ATOM   17300 C  CB    . SER A 1 3828 ? 202.244 182.046 239.985 1.00 1.18  ? 3828 SER A CB    1 
ATOM   17301 O  OG    . SER A 1 3828 ? 200.855 182.053 240.260 1.00 1.22  ? 3828 SER A OG    1 
ATOM   17302 N  N     . LEU A 1 3829 ? 203.131 180.901 242.637 1.00 1.78  ? 3829 LEU A N     1 
ATOM   17303 C  CA    . LEU A 1 3829 ? 202.804 180.631 244.030 1.00 0.96  ? 3829 LEU A CA    1 
ATOM   17304 C  C     . LEU A 1 3829 ? 201.375 181.040 244.353 1.00 0.86  ? 3829 LEU A C     1 
ATOM   17305 O  O     . LEU A 1 3829 ? 200.713 180.386 245.167 1.00 1.43  ? 3829 LEU A O     1 
ATOM   17306 C  CB    . LEU A 1 3829 ? 203.790 181.345 244.954 1.00 1.54  ? 3829 LEU A CB    1 
ATOM   17307 C  CG    . LEU A 1 3829 ? 203.518 181.224 246.454 1.00 2.21  ? 3829 LEU A CG    1 
ATOM   17308 C  CD1   . LEU A 1 3829 ? 203.540 179.770 246.889 1.00 0.70  ? 3829 LEU A CD1   1 
ATOM   17309 C  CD2   . LEU A 1 3829 ? 204.514 182.043 247.248 1.00 3.18  ? 3829 LEU A CD2   1 
ATOM   17310 N  N     . GLN A 1 3830 ? 200.879 182.105 243.721 1.00 1.12  ? 3830 GLN A N     1 
ATOM   17311 C  CA    . GLN A 1 3830 ? 199.514 182.546 243.978 1.00 2.07  ? 3830 GLN A CA    1 
ATOM   17312 C  C     . GLN A 1 3830 ? 198.503 181.490 243.550 1.00 2.13  ? 3830 GLN A C     1 
ATOM   17313 O  O     . GLN A 1 3830 ? 197.444 181.349 244.172 1.00 2.81  ? 3830 GLN A O     1 
ATOM   17314 C  CB    . GLN A 1 3830 ? 199.244 183.869 243.261 1.00 1.81  ? 3830 GLN A CB    1 
ATOM   17315 C  CG    . GLN A 1 3830 ? 197.986 184.574 243.735 1.00 4.18  ? 3830 GLN A CG    1 
ATOM   17316 C  CD    . GLN A 1 3830 ? 197.892 184.630 245.248 1.00 9.31  ? 3830 GLN A CD    1 
ATOM   17317 O  OE1   . GLN A 1 3830 ? 198.764 185.186 245.915 1.00 10.17 ? 3830 GLN A OE1   1 
ATOM   17318 N  NE2   . GLN A 1 3830 ? 196.834 184.046 245.798 1.00 8.45  ? 3830 GLN A NE2   1 
ATOM   17319 N  N     . PHE A 1 3831 ? 198.812 180.740 242.490 1.00 1.60  ? 3831 PHE A N     1 
ATOM   17320 C  CA    . PHE A 1 3831 ? 197.910 179.687 242.035 1.00 1.29  ? 3831 PHE A CA    1 
ATOM   17321 C  C     . PHE A 1 3831 ? 197.752 178.607 243.098 1.00 1.43  ? 3831 PHE A C     1 
ATOM   17322 O  O     . PHE A 1 3831 ? 196.640 178.128 243.352 1.00 1.82  ? 3831 PHE A O     1 
ATOM   17323 C  CB    . PHE A 1 3831 ? 198.420 179.094 240.720 1.00 1.67  ? 3831 PHE A CB    1 
ATOM   17324 C  CG    . PHE A 1 3831 ? 197.557 177.992 240.175 1.00 1.63  ? 3831 PHE A CG    1 
ATOM   17325 C  CD1   . PHE A 1 3831 ? 198.063 176.719 240.006 1.00 1.77  ? 3831 PHE A CD1   1 
ATOM   17326 C  CD2   . PHE A 1 3831 ? 196.239 178.233 239.831 1.00 4.28  ? 3831 PHE A CD2   1 
ATOM   17327 C  CE1   . PHE A 1 3831 ? 197.272 175.703 239.502 1.00 3.14  ? 3831 PHE A CE1   1 
ATOM   17328 C  CE2   . PHE A 1 3831 ? 195.443 177.219 239.329 1.00 6.27  ? 3831 PHE A CE2   1 
ATOM   17329 C  CZ    . PHE A 1 3831 ? 195.962 175.954 239.164 1.00 1.47  ? 3831 PHE A CZ    1 
ATOM   17330 N  N     . PHE A 1 3832 ? 198.857 178.212 243.736 1.00 0.99  ? 3832 PHE A N     1 
ATOM   17331 C  CA    . PHE A 1 3832 ? 198.764 177.254 244.830 1.00 0.99  ? 3832 PHE A CA    1 
ATOM   17332 C  C     . PHE A 1 3832 ? 198.086 177.868 246.051 1.00 1.50  ? 3832 PHE A C     1 
ATOM   17333 O  O     . PHE A 1 3832 ? 197.321 177.192 246.746 1.00 1.89  ? 3832 PHE A O     1 
ATOM   17334 C  CB    . PHE A 1 3832 ? 200.147 176.718 245.201 1.00 0.77  ? 3832 PHE A CB    1 
ATOM   17335 C  CG    . PHE A 1 3832 ? 200.163 175.943 246.487 1.00 1.20  ? 3832 PHE A CG    1 
ATOM   17336 C  CD1   . PHE A 1 3832 ? 199.826 174.600 246.501 1.00 1.11  ? 3832 PHE A CD1   1 
ATOM   17337 C  CD2   . PHE A 1 3832 ? 200.512 176.555 247.681 1.00 0.65  ? 3832 PHE A CD2   1 
ATOM   17338 C  CE1   . PHE A 1 3832 ? 199.827 173.887 247.680 1.00 1.23  ? 3832 PHE A CE1   1 
ATOM   17339 C  CE2   . PHE A 1 3832 ? 200.513 175.847 248.862 1.00 0.47  ? 3832 PHE A CE2   1 
ATOM   17340 C  CZ    . PHE A 1 3832 ? 200.172 174.510 248.862 1.00 1.36  ? 3832 PHE A CZ    1 
ATOM   17341 N  N     . LEU A 1 3833 ? 198.368 179.141 246.336 1.00 1.93  ? 3833 LEU A N     1 
ATOM   17342 C  CA    . LEU A 1 3833 ? 197.725 179.796 247.471 1.00 1.75  ? 3833 LEU A CA    1 
ATOM   17343 C  C     . LEU A 1 3833 ? 196.225 179.936 247.258 1.00 2.35  ? 3833 LEU A C     1 
ATOM   17344 O  O     . LEU A 1 3833 ? 195.458 179.891 248.227 1.00 4.68  ? 3833 LEU A O     1 
ATOM   17345 C  CB    . LEU A 1 3833 ? 198.365 181.160 247.720 1.00 2.71  ? 3833 LEU A CB    1 
ATOM   17346 C  CG    . LEU A 1 3833 ? 199.813 181.131 248.208 1.00 1.53  ? 3833 LEU A CG    1 
ATOM   17347 C  CD1   . LEU A 1 3833 ? 200.365 182.539 248.336 1.00 2.77  ? 3833 LEU A CD1   1 
ATOM   17348 C  CD2   . LEU A 1 3833 ? 199.923 180.386 249.528 1.00 2.61  ? 3833 LEU A CD2   1 
ATOM   17349 N  N     . ASP A 1 3834 ? 195.790 180.113 246.010 1.00 2.07  ? 3834 ASP A N     1 
ATOM   17350 C  CA    . ASP A 1 3834 ? 194.363 180.087 245.715 1.00 2.60  ? 3834 ASP A CA    1 
ATOM   17351 C  C     . ASP A 1 3834 ? 193.774 178.709 245.985 1.00 4.70  ? 3834 ASP A C     1 
ATOM   17352 O  O     . ASP A 1 3834 ? 192.645 178.591 246.477 1.00 4.13  ? 3834 ASP A O     1 
ATOM   17353 C  CB    . ASP A 1 3834 ? 194.123 180.502 244.263 1.00 3.74  ? 3834 ASP A CB    1 
ATOM   17354 C  CG    . ASP A 1 3834 ? 194.516 181.939 243.993 1.00 6.92  ? 3834 ASP A CG    1 
ATOM   17355 O  OD1   . ASP A 1 3834 ? 194.819 182.672 244.958 1.00 11.38 ? 3834 ASP A OD1   1 
ATOM   17356 O  OD2   . ASP A 1 3834 ? 194.535 182.334 242.810 1.00 8.68  ? 3834 ASP A OD2   1 
ATOM   17357 N  N     . ILE A 1 3835 ? 194.519 177.652 245.655 1.00 2.64  ? 3835 ILE A N     1 
ATOM   17358 C  CA    . ILE A 1 3835 ? 194.082 176.292 245.962 1.00 1.44  ? 3835 ILE A CA    1 
ATOM   17359 C  C     . ILE A 1 3835 ? 193.989 176.098 247.470 1.00 3.29  ? 3835 ILE A C     1 
ATOM   17360 O  O     . ILE A 1 3835 ? 193.008 175.553 247.988 1.00 2.87  ? 3835 ILE A O     1 
ATOM   17361 C  CB    . ILE A 1 3835 ? 195.038 175.271 245.322 1.00 2.32  ? 3835 ILE A CB    1 
ATOM   17362 C  CG1   . ILE A 1 3835 ? 194.841 175.219 243.807 1.00 2.08  ? 3835 ILE A CG1   1 
ATOM   17363 C  CG2   . ILE A 1 3835 ? 194.866 173.892 245.949 1.00 1.15  ? 3835 ILE A CG2   1 
ATOM   17364 C  CD1   . ILE A 1 3835 ? 195.937 174.473 243.080 1.00 0.90  ? 3835 ILE A CD1   1 
ATOM   17365 N  N     . TYR A 1 3836 ? 195.016 176.550 248.193 1.00 5.54  ? 3836 TYR A N     1 
ATOM   17366 C  CA    . TYR A 1 3836 ? 195.038 176.406 249.644 1.00 2.06  ? 3836 TYR A CA    1 
ATOM   17367 C  C     . TYR A 1 3836 ? 193.911 177.194 250.295 1.00 2.72  ? 3836 TYR A C     1 
ATOM   17368 O  O     . TYR A 1 3836 ? 193.273 176.716 251.240 1.00 3.21  ? 3836 TYR A O     1 
ATOM   17369 C  CB    . TYR A 1 3836 ? 196.397 176.856 250.174 1.00 2.81  ? 3836 TYR A CB    1 
ATOM   17370 C  CG    . TYR A 1 3836 ? 196.671 176.473 251.606 1.00 3.26  ? 3836 TYR A CG    1 
ATOM   17371 C  CD1   . TYR A 1 3836 ? 196.216 175.269 252.124 1.00 3.39  ? 3836 TYR A CD1   1 
ATOM   17372 C  CD2   . TYR A 1 3836 ? 197.390 177.316 252.437 1.00 1.75  ? 3836 TYR A CD2   1 
ATOM   17373 C  CE1   . TYR A 1 3836 ? 196.468 174.922 253.434 1.00 3.19  ? 3836 TYR A CE1   1 
ATOM   17374 C  CE2   . TYR A 1 3836 ? 197.647 176.977 253.742 1.00 2.14  ? 3836 TYR A CE2   1 
ATOM   17375 C  CZ    . TYR A 1 3836 ? 197.186 175.781 254.238 1.00 3.15  ? 3836 TYR A CZ    1 
ATOM   17376 O  OH    . TYR A 1 3836 ? 197.448 175.446 255.540 1.00 2.98  ? 3836 TYR A OH    1 
ATOM   17377 N  N     . HIS A 1 3837 ? 193.651 178.405 249.802 1.00 2.90  ? 3837 HIS A N     1 
ATOM   17378 C  CA    . HIS A 1 3837 ? 192.541 179.199 250.315 1.00 3.68  ? 3837 HIS A CA    1 
ATOM   17379 C  C     . HIS A 1 3837 ? 191.207 178.511 250.057 1.00 5.91  ? 3837 HIS A C     1 
ATOM   17380 O  O     . HIS A 1 3837 ? 190.305 178.550 250.901 1.00 7.29  ? 3837 HIS A O     1 
ATOM   17381 C  CB    . HIS A 1 3837 ? 192.563 180.590 249.681 1.00 5.26  ? 3837 HIS A CB    1 
ATOM   17382 C  CG    . HIS A 1 3837 ? 191.435 181.473 250.110 1.00 10.20 ? 3837 HIS A CG    1 
ATOM   17383 N  ND1   . HIS A 1 3837 ? 191.553 182.382 251.138 1.00 14.46 ? 3837 HIS A ND1   1 
ATOM   17384 C  CD2   . HIS A 1 3837 ? 190.170 181.591 249.647 1.00 8.37  ? 3837 HIS A CD2   1 
ATOM   17385 C  CE1   . HIS A 1 3837 ? 190.407 183.022 251.290 1.00 11.69 ? 3837 HIS A CE1   1 
ATOM   17386 N  NE2   . HIS A 1 3837 ? 189.550 182.559 250.398 1.00 13.25 ? 3837 HIS A NE2   1 
ATOM   17387 N  N     . ASN A 1 3838 ? 191.064 177.880 248.889 1.00 4.53  ? 3838 ASN A N     1 
ATOM   17388 C  CA    . ASN A 1 3838 ? 189.822 177.191 248.554 1.00 4.50  ? 3838 ASN A CA    1 
ATOM   17389 C  C     . ASN A 1 3838 ? 189.549 176.040 249.517 1.00 5.36  ? 3838 ASN A C     1 
ATOM   17390 O  O     . ASN A 1 3838 ? 188.410 175.846 249.956 1.00 6.99  ? 3838 ASN A O     1 
ATOM   17391 C  CB    . ASN A 1 3838 ? 189.888 176.686 247.113 1.00 5.64  ? 3838 ASN A CB    1 
ATOM   17392 C  CG    . ASN A 1 3838 ? 188.612 176.008 246.674 1.00 6.03  ? 3838 ASN A CG    1 
ATOM   17393 O  OD1   . ASN A 1 3838 ? 188.594 174.812 246.398 1.00 4.98  ? 3838 ASN A OD1   1 
ATOM   17394 N  ND2   . ASN A 1 3838 ? 187.533 176.775 246.602 1.00 7.90  ? 3838 ASN A ND2   1 
ATOM   17395 N  N     . VAL A 1 3839 ? 190.581 175.263 249.849 1.00 3.78  ? 3839 VAL A N     1 
ATOM   17396 C  CA    . VAL A 1 3839 ? 190.413 174.135 250.759 1.00 4.05  ? 3839 VAL A CA    1 
ATOM   17397 C  C     . VAL A 1 3839 ? 190.081 174.612 252.168 1.00 5.15  ? 3839 VAL A C     1 
ATOM   17398 O  O     . VAL A 1 3839 ? 189.333 173.948 252.895 1.00 10.33 ? 3839 VAL A O     1 
ATOM   17399 C  CB    . VAL A 1 3839 ? 191.677 173.253 250.733 1.00 3.52  ? 3839 VAL A CB    1 
ATOM   17400 C  CG1   . VAL A 1 3839 ? 191.579 172.134 251.750 1.00 6.41  ? 3839 VAL A CG1   1 
ATOM   17401 C  CG2   . VAL A 1 3839 ? 191.884 172.682 249.344 1.00 5.19  ? 3839 VAL A CG2   1 
ATOM   17402 N  N     . LEU A 1 3840 ? 190.625 175.753 252.581 1.00 4.62  ? 3840 LEU A N     1 
ATOM   17403 C  CA    . LEU A 1 3840 ? 190.432 176.232 253.944 1.00 3.76  ? 3840 LEU A CA    1 
ATOM   17404 C  C     . LEU A 1 3840 ? 189.127 176.993 254.142 1.00 5.90  ? 3840 LEU A C     1 
ATOM   17405 O  O     . LEU A 1 3840 ? 188.551 176.933 255.235 1.00 16.60 ? 3840 LEU A O     1 
ATOM   17406 C  CB    . LEU A 1 3840 ? 191.603 177.127 254.353 1.00 3.86  ? 3840 LEU A CB    1 
ATOM   17407 C  CG    . LEU A 1 3840 ? 192.950 176.432 254.548 1.00 4.45  ? 3840 LEU A CG    1 
ATOM   17408 C  CD1   . LEU A 1 3840 ? 194.034 177.454 254.837 1.00 3.26  ? 3840 LEU A CD1   1 
ATOM   17409 C  CD2   . LEU A 1 3840 ? 192.870 175.395 255.658 1.00 3.52  ? 3840 LEU A CD2   1 
ATOM   17410 N  N     . TYR A 1 3841 ? 188.643 177.702 253.127 1.00 5.24  ? 3841 TYR A N     1 
ATOM   17411 C  CA    . TYR A 1 3841 ? 187.510 178.601 253.301 1.00 7.19  ? 3841 TYR A CA    1 
ATOM   17412 C  C     . TYR A 1 3841 ? 186.308 178.285 252.427 1.00 8.62  ? 3841 TYR A C     1 
ATOM   17413 O  O     . TYR A 1 3841 ? 185.191 178.654 252.792 1.00 12.16 ? 3841 TYR A O     1 
ATOM   17414 C  CB    . TYR A 1 3841 ? 187.939 180.052 253.035 1.00 6.55  ? 3841 TYR A CB    1 
ATOM   17415 C  CG    . TYR A 1 3841 ? 188.936 180.581 254.036 1.00 13.01 ? 3841 TYR A CG    1 
ATOM   17416 C  CD1   . TYR A 1 3841 ? 188.537 180.931 255.318 1.00 11.97 ? 3841 TYR A CD1   1 
ATOM   17417 C  CD2   . TYR A 1 3841 ? 190.275 180.726 253.703 1.00 10.99 ? 3841 TYR A CD2   1 
ATOM   17418 C  CE1   . TYR A 1 3841 ? 189.440 181.417 256.237 1.00 9.92  ? 3841 TYR A CE1   1 
ATOM   17419 C  CE2   . TYR A 1 3841 ? 191.187 181.211 254.618 1.00 10.61 ? 3841 TYR A CE2   1 
ATOM   17420 C  CZ    . TYR A 1 3841 ? 190.764 181.554 255.884 1.00 16.94 ? 3841 TYR A CZ    1 
ATOM   17421 O  OH    . TYR A 1 3841 ? 191.668 182.037 256.804 1.00 19.23 ? 3841 TYR A OH    1 
ATOM   17422 N  N     . GLU A 1 3842 ? 186.496 177.619 251.293 1.00 7.58  ? 3842 GLU A N     1 
ATOM   17423 C  CA    . GLU A 1 3842 ? 185.409 177.307 250.375 1.00 8.98  ? 3842 GLU A CA    1 
ATOM   17424 C  C     . GLU A 1 3842 ? 185.247 175.800 250.220 1.00 10.68 ? 3842 GLU A C     1 
ATOM   17425 O  O     . GLU A 1 3842 ? 185.077 175.282 249.114 1.00 16.10 ? 3842 GLU A O     1 
ATOM   17426 C  CB    . GLU A 1 3842 ? 185.636 177.972 249.021 1.00 8.38  ? 3842 GLU A CB    1 
ATOM   17427 C  CG    . GLU A 1 3842 ? 185.898 179.465 249.106 1.00 11.85 ? 3842 GLU A CG    1 
ATOM   17428 C  CD    . GLU A 1 3842 ? 186.927 179.939 248.101 1.00 14.15 ? 3842 GLU A CD    1 
ATOM   17429 O  OE1   . GLU A 1 3842 ? 187.456 179.097 247.345 1.00 18.36 ? 3842 GLU A OE1   1 
ATOM   17430 O  OE2   . GLU A 1 3842 ? 187.209 181.154 248.066 1.00 16.59 ? 3842 GLU A OE2   1 
ATOM   17431 N  N     . ASN A 1 3843 ? 185.296 175.078 251.337 1.00 9.06  ? 3843 ASN A N     1 
ATOM   17432 C  CA    . ASN A 1 3843 ? 185.238 173.627 251.319 1.00 12.91 ? 3843 ASN A CA    1 
ATOM   17433 C  C     . ASN A 1 3843 ? 183.861 173.167 251.764 1.00 16.19 ? 3843 ASN A C     1 
ATOM   17434 O  O     . ASN A 1 3843 ? 183.493 173.381 252.930 1.00 19.30 ? 3843 ASN A O     1 
ATOM   17435 C  CB    . ASN A 1 3843 ? 186.315 173.045 252.228 1.00 11.18 ? 3843 ASN A CB    1 
ATOM   17436 C  CG    . ASN A 1 3843 ? 186.394 171.533 252.152 1.00 12.82 ? 3843 ASN A CG    1 
ATOM   17437 O  OD1   . ASN A 1 3843 ? 185.601 170.886 251.471 1.00 17.59 ? 3843 ASN A OD1   1 
ATOM   17438 N  ND2   . ASN A 1 3843 ? 187.375 170.963 252.842 1.00 13.62 ? 3843 ASN A ND2   1 
ATOM   17439 N  N     . PRO A 1 3844 ? 183.072 172.537 250.888 1.00 17.68 ? 3844 PRO A N     1 
ATOM   17440 C  CA    . PRO A 1 3844 ? 181.740 172.068 251.304 1.00 13.01 ? 3844 PRO A CA    1 
ATOM   17441 C  C     . PRO A 1 3844 ? 181.778 170.961 252.339 1.00 15.55 ? 3844 PRO A C     1 
ATOM   17442 O  O     . PRO A 1 3844 ? 180.753 170.699 252.979 1.00 29.14 ? 3844 PRO A O     1 
ATOM   17443 C  CB    . PRO A 1 3844 ? 181.110 171.579 249.990 1.00 17.98 ? 3844 PRO A CB    1 
ATOM   17444 C  CG    . PRO A 1 3844 ? 181.987 172.133 248.895 1.00 15.73 ? 3844 PRO A CG    1 
ATOM   17445 C  CD    . PRO A 1 3844 ? 183.354 172.215 249.482 1.00 12.23 ? 3844 PRO A CD    1 
ATOM   17446 N  N     . ASN A 1 3845 ? 182.917 170.302 252.524 1.00 15.10 ? 3845 ASN A N     1 
ATOM   17447 C  CA    . ASN A 1 3845 ? 183.034 169.198 253.466 1.00 13.34 ? 3845 ASN A CA    1 
ATOM   17448 C  C     . ASN A 1 3845 ? 183.263 169.659 254.901 1.00 15.82 ? 3845 ASN A C     1 
ATOM   17449 O  O     . ASN A 1 3845 ? 183.334 168.818 255.801 1.00 14.29 ? 3845 ASN A O     1 
ATOM   17450 C  CB    . ASN A 1 3845 ? 184.166 168.264 253.034 1.00 12.48 ? 3845 ASN A CB    1 
ATOM   17451 C  CG    . ASN A 1 3845 ? 183.898 167.606 251.694 1.00 18.94 ? 3845 ASN A CG    1 
ATOM   17452 O  OD1   . ASN A 1 3845 ? 184.603 167.851 250.718 1.00 15.01 ? 3845 ASN A OD1   1 
ATOM   17453 N  ND2   . ASN A 1 3845 ? 182.873 166.765 251.643 1.00 23.97 ? 3845 ASN A ND2   1 
ATOM   17454 N  N     . LEU A 1 3846 ? 183.382 170.968 255.133 1.00 12.88 ? 3846 LEU A N     1 
ATOM   17455 C  CA    . LEU A 1 3846 ? 183.578 171.520 256.469 1.00 14.65 ? 3846 LEU A CA    1 
ATOM   17456 C  C     . LEU A 1 3846 ? 182.362 172.300 256.959 1.00 19.51 ? 3846 LEU A C     1 
ATOM   17457 O  O     . LEU A 1 3846 ? 182.473 173.067 257.920 1.00 19.95 ? 3846 LEU A O     1 
ATOM   17458 C  CB    . LEU A 1 3846 ? 184.815 172.419 256.492 1.00 15.56 ? 3846 LEU A CB    1 
ATOM   17459 C  CG    . LEU A 1 3846 ? 186.174 171.811 256.150 1.00 10.80 ? 3846 LEU A CG    1 
ATOM   17460 C  CD1   . LEU A 1 3846 ? 187.175 172.913 255.878 1.00 7.29  ? 3846 LEU A CD1   1 
ATOM   17461 C  CD2   . LEU A 1 3846 ? 186.655 170.916 257.276 1.00 11.71 ? 3846 LEU A CD2   1 
ATOM   17462 N  N     . LYS A 1 3847 ? 181.204 172.119 256.316 1.00 20.82 ? 3847 LYS A N     1 
ATOM   17463 C  CA    . LYS A 1 3847 ? 180.043 172.949 256.622 1.00 20.41 ? 3847 LYS A CA    1 
ATOM   17464 C  C     . LYS A 1 3847 ? 179.578 172.761 258.061 1.00 23.96 ? 3847 LYS A C     1 
ATOM   17465 O  O     . LYS A 1 3847 ? 179.321 173.738 258.775 1.00 32.38 ? 3847 LYS A O     1 
ATOM   17466 C  CB    . LYS A 1 3847 ? 178.906 172.636 255.647 1.00 23.94 ? 3847 LYS A CB    1 
ATOM   17467 C  CG    . LYS A 1 3847 ? 177.713 173.567 255.766 1.00 23.56 ? 3847 LYS A CG    1 
ATOM   17468 C  CD    . LYS A 1 3847 ? 178.057 174.977 255.316 1.00 24.67 ? 3847 LYS A CD    1 
ATOM   17469 C  CE    . LYS A 1 3847 ? 178.466 175.005 253.854 1.00 23.32 ? 3847 LYS A CE    1 
ATOM   17470 N  NZ    . LYS A 1 3847 ? 178.815 176.380 253.404 1.00 24.96 ? 3847 LYS A NZ    1 
ATOM   17471 N  N     . GLY A 1 3848 ? 179.470 171.515 258.511 1.00 17.02 ? 3848 GLY A N     1 
ATOM   17472 C  CA    . GLY A 1 3848 ? 178.958 171.254 259.843 1.00 14.80 ? 3848 GLY A CA    1 
ATOM   17473 C  C     . GLY A 1 3848 ? 179.981 170.673 260.795 1.00 19.95 ? 3848 GLY A C     1 
ATOM   17474 O  O     . GLY A 1 3848 ? 179.687 170.448 261.972 1.00 27.00 ? 3848 GLY A O     1 
ATOM   17475 N  N     . VAL A 1 3849 ? 181.191 170.429 260.297 1.00 17.34 ? 3849 VAL A N     1 
ATOM   17476 C  CA    . VAL A 1 3849 ? 182.213 169.779 261.104 1.00 15.40 ? 3849 VAL A CA    1 
ATOM   17477 C  C     . VAL A 1 3849 ? 182.752 170.762 262.136 1.00 21.18 ? 3849 VAL A C     1 
ATOM   17478 O  O     . VAL A 1 3849 ? 183.096 171.906 261.810 1.00 18.76 ? 3849 VAL A O     1 
ATOM   17479 C  CB    . VAL A 1 3849 ? 183.335 169.235 260.210 1.00 16.79 ? 3849 VAL A CB    1 
ATOM   17480 C  CG1   . VAL A 1 3849 ? 184.310 168.430 261.035 1.00 11.65 ? 3849 VAL A CG1   1 
ATOM   17481 C  CG2   . VAL A 1 3849 ? 182.754 168.399 259.078 1.00 21.12 ? 3849 VAL A CG2   1 
ATOM   17482 N  N     . THR A 1 3850 ? 182.827 170.317 263.391 1.00 21.75 ? 3850 THR A N     1 
ATOM   17483 C  CA    . THR A 1 3850 ? 183.313 171.150 264.482 1.00 14.94 ? 3850 THR A CA    1 
ATOM   17484 C  C     . THR A 1 3850 ? 184.578 170.630 265.145 1.00 20.58 ? 3850 THR A C     1 
ATOM   17485 O  O     . THR A 1 3850 ? 185.304 171.427 265.748 1.00 24.99 ? 3850 THR A O     1 
ATOM   17486 C  CB    . THR A 1 3850 ? 182.232 171.311 265.561 1.00 18.77 ? 3850 THR A CB    1 
ATOM   17487 O  OG1   . THR A 1 3850 ? 181.655 170.033 265.857 1.00 20.64 ? 3850 THR A OG1   1 
ATOM   17488 C  CG2   . THR A 1 3850 ? 181.141 172.258 265.089 1.00 20.04 ? 3850 THR A CG2   1 
ATOM   17489 N  N     . ASP A 1 3851 ? 184.864 169.334 265.055 1.00 20.12 ? 3851 ASP A N     1 
ATOM   17490 C  CA    . ASP A 1 3851 ? 186.056 168.793 265.689 1.00 17.18 ? 3851 ASP A CA    1 
ATOM   17491 C  C     . ASP A 1 3851 ? 187.295 169.186 264.894 1.00 19.98 ? 3851 ASP A C     1 
ATOM   17492 O  O     . ASP A 1 3851 ? 187.368 168.956 263.684 1.00 20.94 ? 3851 ASP A O     1 
ATOM   17493 C  CB    . ASP A 1 3851 ? 185.950 167.275 265.803 1.00 14.46 ? 3851 ASP A CB    1 
ATOM   17494 C  CG    . ASP A 1 3851 ? 187.263 166.626 266.175 1.00 21.05 ? 3851 ASP A CG    1 
ATOM   17495 O  OD1   . ASP A 1 3851 ? 187.865 167.047 267.184 1.00 23.66 ? 3851 ASP A OD1   1 
ATOM   17496 O  OD2   . ASP A 1 3851 ? 187.689 165.689 265.466 1.00 21.93 ? 3851 ASP A OD2   1 
ATOM   17497 N  N     . HIS A 1 3852 ? 188.275 169.775 265.587 1.00 19.12 ? 3852 HIS A N     1 
ATOM   17498 C  CA    . HIS A 1 3852 ? 189.461 170.290 264.909 1.00 13.14 ? 3852 HIS A CA    1 
ATOM   17499 C  C     . HIS A 1 3852 ? 190.231 169.178 264.211 1.00 13.16 ? 3852 HIS A C     1 
ATOM   17500 O  O     . HIS A 1 3852 ? 190.720 169.360 263.090 1.00 15.64 ? 3852 HIS A O     1 
ATOM   17501 C  CB    . HIS A 1 3852 ? 190.361 171.017 265.908 1.00 15.22 ? 3852 HIS A CB    1 
ATOM   17502 C  CG    . HIS A 1 3852 ? 189.724 172.218 266.533 1.00 18.50 ? 3852 HIS A CG    1 
ATOM   17503 N  ND1   . HIS A 1 3852 ? 188.701 172.917 265.931 1.00 17.50 ? 3852 HIS A ND1   1 
ATOM   17504 C  CD2   . HIS A 1 3852 ? 189.970 172.847 267.707 1.00 17.37 ? 3852 HIS A CD2   1 
ATOM   17505 C  CE1   . HIS A 1 3852 ? 188.340 173.922 266.708 1.00 13.83 ? 3852 HIS A CE1   1 
ATOM   17506 N  NE2   . HIS A 1 3852 ? 189.095 173.902 267.792 1.00 20.41 ? 3852 HIS A NE2   1 
ATOM   17507 N  N     . THR A 1 3853 ? 190.356 168.019 264.860 1.00 11.61 ? 3853 THR A N     1 
ATOM   17508 C  CA    . THR A 1 3853 ? 191.081 166.908 264.252 1.00 13.27 ? 3853 THR A CA    1 
ATOM   17509 C  C     . THR A 1 3853 ? 190.402 166.439 262.971 1.00 13.17 ? 3853 THR A C     1 
ATOM   17510 O  O     . THR A 1 3853 ? 191.071 166.182 261.963 1.00 16.01 ? 3853 THR A O     1 
ATOM   17511 C  CB    . THR A 1 3853 ? 191.203 165.755 265.248 1.00 12.40 ? 3853 THR A CB    1 
ATOM   17512 O  OG1   . THR A 1 3853 ? 191.972 166.181 266.381 1.00 19.61 ? 3853 THR A OG1   1 
ATOM   17513 C  CG2   . THR A 1 3853 ? 191.885 164.561 264.602 1.00 11.63 ? 3853 THR A CG2   1 
ATOM   17514 N  N     . GLN A 1 3854 ? 189.073 166.328 262.988 1.00 11.10 ? 3854 GLN A N     1 
ATOM   17515 C  CA    . GLN A 1 3854 ? 188.364 165.838 261.812 1.00 13.83 ? 3854 GLN A CA    1 
ATOM   17516 C  C     . GLN A 1 3854 ? 188.379 166.875 260.694 1.00 13.43 ? 3854 GLN A C     1 
ATOM   17517 O  O     . GLN A 1 3854 ? 188.464 166.519 259.511 1.00 15.67 ? 3854 GLN A O     1 
ATOM   17518 C  CB    . GLN A 1 3854 ? 186.934 165.448 262.191 1.00 14.86 ? 3854 GLN A CB    1 
ATOM   17519 C  CG    . GLN A 1 3854 ? 185.978 165.330 261.021 1.00 16.29 ? 3854 GLN A CG    1 
ATOM   17520 C  CD    . GLN A 1 3854 ? 184.581 164.935 261.453 1.00 24.00 ? 3854 GLN A CD    1 
ATOM   17521 O  OE1   . GLN A 1 3854 ? 184.240 165.004 262.633 1.00 16.52 ? 3854 GLN A OE1   1 
ATOM   17522 N  NE2   . GLN A 1 3854 ? 183.763 164.519 260.493 1.00 23.79 ? 3854 GLN A NE2   1 
ATOM   17523 N  N     . ARG A 1 3855 ? 188.312 168.161 261.046 1.00 11.73 ? 3855 ARG A N     1 
ATOM   17524 C  CA    . ARG A 1 3855 ? 188.462 169.211 260.043 1.00 7.78  ? 3855 ARG A CA    1 
ATOM   17525 C  C     . ARG A 1 3855 ? 189.836 169.158 259.394 1.00 9.63  ? 3855 ARG A C     1 
ATOM   17526 O  O     . ARG A 1 3855 ? 189.969 169.373 258.183 1.00 12.99 ? 3855 ARG A O     1 
ATOM   17527 C  CB    . ARG A 1 3855 ? 188.230 170.584 260.672 1.00 8.25  ? 3855 ARG A CB    1 
ATOM   17528 C  CG    . ARG A 1 3855 ? 186.836 170.807 261.203 1.00 9.36  ? 3855 ARG A CG    1 
ATOM   17529 C  CD    . ARG A 1 3855 ? 186.590 172.265 261.527 1.00 13.57 ? 3855 ARG A CD    1 
ATOM   17530 N  NE    . ARG A 1 3855 ? 186.947 173.141 260.419 1.00 12.05 ? 3855 ARG A NE    1 
ATOM   17531 C  CZ    . ARG A 1 3855 ? 186.090 173.917 259.775 1.00 13.71 ? 3855 ARG A CZ    1 
ATOM   17532 N  NH1   . ARG A 1 3855 ? 184.809 173.952 260.100 1.00 14.34 ? 3855 ARG A NH1   1 
ATOM   17533 N  NH2   . ARG A 1 3855 ? 186.531 174.681 258.777 1.00 19.32 ? 3855 ARG A NH2   1 
ATOM   17534 N  N     . LEU A 1 3856 ? 190.872 168.882 260.187 1.00 8.30  ? 3856 LEU A N     1 
ATOM   17535 C  CA    . LEU A 1 3856 ? 192.223 168.797 259.643 1.00 6.66  ? 3856 LEU A CA    1 
ATOM   17536 C  C     . LEU A 1 3856 ? 192.346 167.655 258.643 1.00 10.20 ? 3856 LEU A C     1 
ATOM   17537 O  O     . LEU A 1 3856 ? 192.992 167.800 257.600 1.00 10.52 ? 3856 LEU A O     1 
ATOM   17538 C  CB    . LEU A 1 3856 ? 193.230 168.635 260.778 1.00 6.20  ? 3856 LEU A CB    1 
ATOM   17539 C  CG    . LEU A 1 3856 ? 194.701 168.853 260.430 1.00 5.15  ? 3856 LEU A CG    1 
ATOM   17540 C  CD1   . LEU A 1 3856 ? 194.870 170.084 259.556 1.00 6.38  ? 3856 LEU A CD1   1 
ATOM   17541 C  CD2   . LEU A 1 3856 ? 195.524 168.979 261.701 1.00 7.00  ? 3856 LEU A CD2   1 
ATOM   17542 N  N     . SER A 1 3857 ? 191.740 166.504 258.947 1.00 9.50  ? 3857 SER A N     1 
ATOM   17543 C  CA    . SER A 1 3857 ? 191.760 165.390 258.005 1.00 10.27 ? 3857 SER A CA    1 
ATOM   17544 C  C     . SER A 1 3857 ? 191.032 165.750 256.716 1.00 7.98  ? 3857 SER A C     1 
ATOM   17545 O  O     . SER A 1 3857 ? 191.490 165.410 255.620 1.00 10.23 ? 3857 SER A O     1 
ATOM   17546 C  CB    . SER A 1 3857 ? 191.139 164.147 258.642 1.00 11.35 ? 3857 SER A CB    1 
ATOM   17547 O  OG    . SER A 1 3857 ? 189.752 164.323 258.857 1.00 13.15 ? 3857 SER A OG    1 
ATOM   17548 N  N     . ILE A 1 3858 ? 189.893 166.436 256.832 1.00 7.48  ? 3858 ILE A N     1 
ATOM   17549 C  CA    . ILE A 1 3858 ? 189.165 166.880 255.648 1.00 7.76  ? 3858 ILE A CA    1 
ATOM   17550 C  C     . ILE A 1 3858 ? 190.003 167.867 254.845 1.00 9.49  ? 3858 ILE A C     1 
ATOM   17551 O  O     . ILE A 1 3858 ? 190.088 167.773 253.615 1.00 11.50 ? 3858 ILE A O     1 
ATOM   17552 C  CB    . ILE A 1 3858 ? 187.810 167.488 256.053 1.00 9.12  ? 3858 ILE A CB    1 
ATOM   17553 C  CG1   . ILE A 1 3858 ? 186.882 166.406 256.605 1.00 8.97  ? 3858 ILE A CG1   1 
ATOM   17554 C  CG2   . ILE A 1 3858 ? 187.178 168.209 254.877 1.00 10.23 ? 3858 ILE A CG2   1 
ATOM   17555 C  CD1   . ILE A 1 3858 ? 185.702 166.953 257.368 1.00 12.89 ? 3858 ILE A CD1   1 
ATOM   17556 N  N     . ILE A 1 3859 ? 190.633 168.824 255.528 1.00 7.70  ? 3859 ILE A N     1 
ATOM   17557 C  CA    . ILE A 1 3859 ? 191.471 169.804 254.843 1.00 6.49  ? 3859 ILE A CA    1 
ATOM   17558 C  C     . ILE A 1 3859 ? 192.648 169.119 254.164 1.00 5.26  ? 3859 ILE A C     1 
ATOM   17559 O  O     . ILE A 1 3859 ? 192.978 169.419 253.011 1.00 7.24  ? 3859 ILE A O     1 
ATOM   17560 C  CB    . ILE A 1 3859 ? 191.934 170.891 255.832 1.00 5.49  ? 3859 ILE A CB    1 
ATOM   17561 C  CG1   . ILE A 1 3859 ? 190.787 171.852 256.144 1.00 5.49  ? 3859 ILE A CG1   1 
ATOM   17562 C  CG2   . ILE A 1 3859 ? 193.134 171.645 255.287 1.00 4.53  ? 3859 ILE A CG2   1 
ATOM   17563 C  CD1   . ILE A 1 3859 ? 191.008 172.684 257.383 1.00 5.80  ? 3859 ILE A CD1   1 
ATOM   17564 N  N     . THR A 1 3860 ? 193.293 168.184 254.865 1.00 4.96  ? 3860 THR A N     1 
ATOM   17565 C  CA    . THR A 1 3860 ? 194.434 167.477 254.290 1.00 5.64  ? 3860 THR A CA    1 
ATOM   17566 C  C     . THR A 1 3860 ? 194.023 166.665 253.070 1.00 9.01  ? 3860 THR A C     1 
ATOM   17567 O  O     . THR A 1 3860 ? 194.703 166.693 252.037 1.00 7.19  ? 3860 THR A O     1 
ATOM   17568 C  CB    . THR A 1 3860 ? 195.071 166.568 255.341 1.00 5.67  ? 3860 THR A CB    1 
ATOM   17569 O  OG1   . THR A 1 3860 ? 195.392 167.334 256.508 1.00 9.38  ? 3860 THR A OG1   1 
ATOM   17570 C  CG2   . THR A 1 3860 ? 196.335 165.924 254.796 1.00 3.81  ? 3860 THR A CG2   1 
ATOM   17571 N  N     . LYS A 1 3861 ? 192.913 165.934 253.171 1.00 8.90  ? 3861 LYS A N     1 
ATOM   17572 C  CA    . LYS A 1 3861 ? 192.426 165.157 252.037 1.00 6.27  ? 3861 LYS A CA    1 
ATOM   17573 C  C     . LYS A 1 3861 ? 192.039 166.062 250.875 1.00 4.72  ? 3861 LYS A C     1 
ATOM   17574 O  O     . LYS A 1 3861 ? 192.392 165.795 249.721 1.00 4.21  ? 3861 LYS A O     1 
ATOM   17575 C  CB    . LYS A 1 3861 ? 191.234 164.302 252.470 1.00 6.75  ? 3861 LYS A CB    1 
ATOM   17576 C  CG    . LYS A 1 3861 ? 190.674 163.410 251.380 1.00 6.33  ? 3861 LYS A CG    1 
ATOM   17577 C  CD    . LYS A 1 3861 ? 189.570 162.513 251.914 1.00 8.70  ? 3861 LYS A CD    1 
ATOM   17578 C  CE    . LYS A 1 3861 ? 188.907 161.731 250.796 1.00 18.23 ? 3861 LYS A CE    1 
ATOM   17579 N  NZ    . LYS A 1 3861 ? 189.843 160.757 250.167 1.00 13.24 ? 3861 LYS A NZ    1 
ATOM   17580 N  N     . ASP A 1 3862 ? 191.321 167.148 251.167 1.00 7.05  ? 3862 ASP A N     1 
ATOM   17581 C  CA    . ASP A 1 3862 ? 190.779 167.974 250.098 1.00 3.24  ? 3862 ASP A CA    1 
ATOM   17582 C  C     . ASP A 1 3862 ? 191.882 168.796 249.439 1.00 3.67  ? 3862 ASP A C     1 
ATOM   17583 O  O     . ASP A 1 3862 ? 191.770 169.163 248.264 1.00 4.76  ? 3862 ASP A O     1 
ATOM   17584 C  CB    . ASP A 1 3862 ? 189.672 168.870 250.663 1.00 6.33  ? 3862 ASP A CB    1 
ATOM   17585 C  CG    . ASP A 1 3862 ? 188.887 169.599 249.588 1.00 23.33 ? 3862 ASP A CG    1 
ATOM   17586 O  OD1   . ASP A 1 3862 ? 189.196 169.448 248.395 1.00 21.22 ? 3862 ASP A OD1   1 
ATOM   17587 O  OD2   . ASP A 1 3862 ? 187.942 170.329 249.942 1.00 21.89 ? 3862 ASP A OD2   1 
ATOM   17588 N  N     . LEU A 1 3863 ? 192.965 169.075 250.173 1.00 5.19  ? 3863 LEU A N     1 
ATOM   17589 C  CA    . LEU A 1 3863 ? 194.097 169.792 249.593 1.00 1.88  ? 3863 LEU A CA    1 
ATOM   17590 C  C     . LEU A 1 3863 ? 194.706 169.018 248.433 1.00 1.59  ? 3863 LEU A C     1 
ATOM   17591 O  O     . LEU A 1 3863 ? 195.027 169.598 247.389 1.00 2.50  ? 3863 LEU A O     1 
ATOM   17592 C  CB    . LEU A 1 3863 ? 195.152 170.060 250.666 1.00 1.99  ? 3863 LEU A CB    1 
ATOM   17593 C  CG    . LEU A 1 3863 ? 196.472 170.671 250.190 1.00 3.79  ? 3863 LEU A CG    1 
ATOM   17594 C  CD1   . LEU A 1 3863 ? 196.276 172.102 249.720 1.00 1.35  ? 3863 LEU A CD1   1 
ATOM   17595 C  CD2   . LEU A 1 3863 ? 197.531 170.596 251.277 1.00 1.82  ? 3863 LEU A CD2   1 
ATOM   17596 N  N     . PHE A 1 3864 ? 194.878 167.707 248.597 1.00 1.71  ? 3864 PHE A N     1 
ATOM   17597 C  CA    . PHE A 1 3864 ? 195.411 166.890 247.513 1.00 1.98  ? 3864 PHE A CA    1 
ATOM   17598 C  C     . PHE A 1 3864 ? 194.439 166.819 246.345 1.00 0.97  ? 3864 PHE A C     1 
ATOM   17599 O  O     . PHE A 1 3864 ? 194.857 166.795 245.182 1.00 0.35  ? 3864 PHE A O     1 
ATOM   17600 C  CB    . PHE A 1 3864 ? 195.741 165.490 248.027 1.00 1.18  ? 3864 PHE A CB    1 
ATOM   17601 C  CG    . PHE A 1 3864 ? 197.045 165.404 248.762 1.00 0.94  ? 3864 PHE A CG    1 
ATOM   17602 C  CD1   . PHE A 1 3864 ? 198.225 165.185 248.076 1.00 1.59  ? 3864 PHE A CD1   1 
ATOM   17603 C  CD2   . PHE A 1 3864 ? 197.091 165.540 250.138 1.00 1.00  ? 3864 PHE A CD2   1 
ATOM   17604 C  CE1   . PHE A 1 3864 ? 199.430 165.107 248.751 1.00 2.89  ? 3864 PHE A CE1   1 
ATOM   17605 C  CE2   . PHE A 1 3864 ? 198.291 165.464 250.817 1.00 1.14  ? 3864 PHE A CE2   1 
ATOM   17606 C  CZ    . PHE A 1 3864 ? 199.460 165.246 250.122 1.00 1.70  ? 3864 PHE A CZ    1 
ATOM   17607 N  N     . GLN A 1 3865 ? 193.135 166.784 246.633 1.00 0.97  ? 3865 GLN A N     1 
ATOM   17608 C  CA    . GLN A 1 3865 ? 192.141 166.628 245.578 1.00 0.65  ? 3865 GLN A CA    1 
ATOM   17609 C  C     . GLN A 1 3865 ? 192.036 167.884 244.719 1.00 0.55  ? 3865 GLN A C     1 
ATOM   17610 O  O     . GLN A 1 3865 ? 192.034 167.803 243.486 1.00 0.58  ? 3865 GLN A O     1 
ATOM   17611 C  CB    . GLN A 1 3865 ? 190.784 166.274 246.187 1.00 0.77  ? 3865 GLN A CB    1 
ATOM   17612 C  CG    . GLN A 1 3865 ? 189.725 165.925 245.159 1.00 1.37  ? 3865 GLN A CG    1 
ATOM   17613 C  CD    . GLN A 1 3865 ? 190.027 164.630 244.432 1.00 0.98  ? 3865 GLN A CD    1 
ATOM   17614 O  OE1   . GLN A 1 3865 ? 189.865 163.545 244.984 1.00 2.53  ? 3865 GLN A OE1   1 
ATOM   17615 N  NE2   . GLN A 1 3865 ? 190.485 164.739 243.194 1.00 0.60  ? 3865 GLN A NE2   1 
ATOM   17616 N  N     . VAL A 1 3866 ? 191.946 169.055 245.351 1.00 0.45  ? 3866 VAL A N     1 
ATOM   17617 C  CA    . VAL A 1 3866 ? 191.835 170.296 244.591 1.00 0.59  ? 3866 VAL A CA    1 
ATOM   17618 C  C     . VAL A 1 3866 ? 193.128 170.579 243.838 1.00 0.43  ? 3866 VAL A C     1 
ATOM   17619 O  O     . VAL A 1 3866 ? 193.108 171.097 242.715 1.00 0.55  ? 3866 VAL A O     1 
ATOM   17620 C  CB    . VAL A 1 3866 ? 191.438 171.465 245.509 1.00 1.67  ? 3866 VAL A CB    1 
ATOM   17621 C  CG1   . VAL A 1 3866 ? 191.415 172.769 244.735 1.00 1.39  ? 3866 VAL A CG1   1 
ATOM   17622 C  CG2   . VAL A 1 3866 ? 190.076 171.213 246.102 1.00 1.19  ? 3866 VAL A CG2   1 
ATOM   17623 N  N     . ALA A 1 3867 ? 194.272 170.242 244.440 1.00 0.36  ? 3867 ALA A N     1 
ATOM   17624 C  CA    . ALA A 1 3867 ? 195.543 170.438 243.754 1.00 0.37  ? 3867 ALA A CA    1 
ATOM   17625 C  C     . ALA A 1 3867 ? 195.596 169.638 242.460 1.00 0.47  ? 3867 ALA A C     1 
ATOM   17626 O  O     . ALA A 1 3867 ? 196.038 170.148 241.426 1.00 1.02  ? 3867 ALA A O     1 
ATOM   17627 C  CB    . ALA A 1 3867 ? 196.704 170.058 244.672 1.00 0.38  ? 3867 ALA A CB    1 
ATOM   17628 N  N     . PHE A 1 3868 ? 195.141 168.385 242.496 1.00 0.26  ? 3868 PHE A N     1 
ATOM   17629 C  CA    . PHE A 1 3868 ? 195.113 167.594 241.272 1.00 0.22  ? 3868 PHE A CA    1 
ATOM   17630 C  C     . PHE A 1 3868 ? 194.085 168.133 240.286 1.00 0.29  ? 3868 PHE A C     1 
ATOM   17631 O  O     . PHE A 1 3868 ? 194.352 168.194 239.083 1.00 0.49  ? 3868 PHE A O     1 
ATOM   17632 C  CB    . PHE A 1 3868 ? 194.826 166.127 241.589 1.00 0.24  ? 3868 PHE A CB    1 
ATOM   17633 C  CG    . PHE A 1 3868 ? 194.797 165.248 240.372 1.00 0.21  ? 3868 PHE A CG    1 
ATOM   17634 C  CD1   . PHE A 1 3868 ? 195.973 164.839 239.768 1.00 0.26  ? 3868 PHE A CD1   1 
ATOM   17635 C  CD2   . PHE A 1 3868 ? 193.594 164.843 239.819 1.00 0.17  ? 3868 PHE A CD2   1 
ATOM   17636 C  CE1   . PHE A 1 3868 ? 195.953 164.039 238.647 1.00 0.50  ? 3868 PHE A CE1   1 
ATOM   17637 C  CE2   . PHE A 1 3868 ? 193.567 164.041 238.697 1.00 0.39  ? 3868 PHE A CE2   1 
ATOM   17638 C  CZ    . PHE A 1 3868 ? 194.746 163.638 238.111 1.00 0.67  ? 3868 PHE A CZ    1 
ATOM   17639 N  N     . ASN A 1 3869 ? 192.911 168.529 240.777 1.00 0.26  ? 3869 ASN A N     1 
ATOM   17640 C  CA    . ASN A 1 3869 ? 191.834 168.943 239.884 1.00 0.36  ? 3869 ASN A CA    1 
ATOM   17641 C  C     . ASN A 1 3869 ? 192.212 170.189 239.095 1.00 1.23  ? 3869 ASN A C     1 
ATOM   17642 O  O     . ASN A 1 3869 ? 192.040 170.239 237.872 1.00 3.71  ? 3869 ASN A O     1 
ATOM   17643 C  CB    . ASN A 1 3869 ? 190.551 169.173 240.682 1.00 0.46  ? 3869 ASN A CB    1 
ATOM   17644 C  CG    . ASN A 1 3869 ? 189.890 167.877 241.105 1.00 1.17  ? 3869 ASN A CG    1 
ATOM   17645 O  OD1   . ASN A 1 3869 ? 190.310 166.794 240.705 1.00 2.15  ? 3869 ASN A OD1   1 
ATOM   17646 N  ND2   . ASN A 1 3869 ? 188.849 167.982 241.921 1.00 2.27  ? 3869 ASN A ND2   1 
ATOM   17647 N  N     . ARG A 1 3870 ? 192.744 171.205 239.773 1.00 0.73  ? 3870 ARG A N     1 
ATOM   17648 C  CA    . ARG A 1 3870 ? 193.044 172.454 239.085 1.00 0.67  ? 3870 ARG A CA    1 
ATOM   17649 C  C     . ARG A 1 3870 ? 194.291 172.344 238.213 1.00 0.59  ? 3870 ARG A C     1 
ATOM   17650 O  O     . ARG A 1 3870 ? 194.332 172.911 237.116 1.00 2.66  ? 3870 ARG A O     1 
ATOM   17651 C  CB    . ARG A 1 3870 ? 193.189 173.587 240.099 1.00 1.05  ? 3870 ARG A CB    1 
ATOM   17652 C  CG    . ARG A 1 3870 ? 191.950 173.791 240.954 1.00 1.16  ? 3870 ARG A CG    1 
ATOM   17653 C  CD    . ARG A 1 3870 ? 191.948 175.153 241.609 1.00 1.95  ? 3870 ARG A CD    1 
ATOM   17654 N  NE    . ARG A 1 3870 ? 190.727 175.400 242.365 1.00 6.94  ? 3870 ARG A NE    1 
ATOM   17655 C  CZ    . ARG A 1 3870 ? 190.448 176.539 242.982 1.00 5.89  ? 3870 ARG A CZ    1 
ATOM   17656 N  NH1   . ARG A 1 3870 ? 191.287 177.559 242.956 1.00 3.93  ? 3870 ARG A NH1   1 
ATOM   17657 N  NH2   . ARG A 1 3870 ? 189.295 176.658 243.632 1.00 7.59  ? 3870 ARG A NH2   1 
ATOM   17658 N  N     . VAL A 1 3871 ? 195.315 171.626 238.678 1.00 0.38  ? 3871 VAL A N     1 
ATOM   17659 C  CA    . VAL A 1 3871 ? 196.539 171.506 237.890 1.00 0.48  ? 3871 VAL A CA    1 
ATOM   17660 C  C     . VAL A 1 3871 ? 196.310 170.635 236.659 1.00 0.38  ? 3871 VAL A C     1 
ATOM   17661 O  O     . VAL A 1 3871 ? 196.748 170.976 235.554 1.00 0.45  ? 3871 VAL A O     1 
ATOM   17662 C  CB    . VAL A 1 3871 ? 197.688 170.973 238.765 1.00 0.32  ? 3871 VAL A CB    1 
ATOM   17663 C  CG1   . VAL A 1 3871 ? 198.876 170.581 237.907 1.00 0.49  ? 3871 VAL A CG1   1 
ATOM   17664 C  CG2   . VAL A 1 3871 ? 198.101 172.012 239.790 1.00 0.20  ? 3871 VAL A CG2   1 
ATOM   17665 N  N     . ALA A 1 3872 ? 195.615 169.505 236.822 1.00 0.32  ? 3872 ALA A N     1 
ATOM   17666 C  CA    . ALA A 1 3872 ? 195.450 168.561 235.720 1.00 0.28  ? 3872 ALA A CA    1 
ATOM   17667 C  C     . ALA A 1 3872 ? 194.542 169.090 234.618 1.00 0.36  ? 3872 ALA A C     1 
ATOM   17668 O  O     . ALA A 1 3872 ? 194.655 168.639 233.475 1.00 0.25  ? 3872 ALA A O     1 
ATOM   17669 C  CB    . ALA A 1 3872 ? 194.911 167.224 236.232 1.00 0.35  ? 3872 ALA A CB    1 
ATOM   17670 N  N     . ARG A 1 3873 ? 193.646 170.031 234.926 1.00 0.90  ? 3873 ARG A N     1 
ATOM   17671 C  CA    . ARG A 1 3873 ? 192.850 170.643 233.872 1.00 0.72  ? 3873 ARG A CA    1 
ATOM   17672 C  C     . ARG A 1 3873 ? 193.730 171.413 232.898 1.00 0.47  ? 3873 ARG A C     1 
ATOM   17673 O  O     . ARG A 1 3873 ? 193.343 171.630 231.744 1.00 0.59  ? 3873 ARG A O     1 
ATOM   17674 C  CB    . ARG A 1 3873 ? 191.788 171.564 234.470 1.00 1.49  ? 3873 ARG A CB    1 
ATOM   17675 C  CG    . ARG A 1 3873 ? 190.637 170.840 235.140 1.00 2.93  ? 3873 ARG A CG    1 
ATOM   17676 C  CD    . ARG A 1 3873 ? 189.993 169.809 234.236 1.00 4.18  ? 3873 ARG A CD    1 
ATOM   17677 N  NE    . ARG A 1 3873 ? 188.684 169.406 234.740 1.00 7.41  ? 3873 ARG A NE    1 
ATOM   17678 C  CZ    . ARG A 1 3873 ? 187.916 168.479 234.187 1.00 6.50  ? 3873 ARG A CZ    1 
ATOM   17679 N  NH1   . ARG A 1 3873 ? 188.300 167.816 233.110 1.00 5.32  ? 3873 ARG A NH1   1 
ATOM   17680 N  NH2   . ARG A 1 3873 ? 186.734 168.208 234.731 1.00 8.38  ? 3873 ARG A NH2   1 
ATOM   17681 N  N     . GLY A 1 3874 ? 194.912 171.827 233.343 1.00 0.21  ? 3874 GLY A N     1 
ATOM   17682 C  CA    . GLY A 1 3874 ? 195.875 172.477 232.481 1.00 0.22  ? 3874 GLY A CA    1 
ATOM   17683 C  C     . GLY A 1 3874 ? 197.040 171.593 232.099 1.00 0.24  ? 3874 GLY A C     1 
ATOM   17684 O  O     . GLY A 1 3874 ? 198.100 172.089 231.713 1.00 0.42  ? 3874 GLY A O     1 
ATOM   17685 N  N     . MET A 1 3875 ? 196.862 170.280 232.200 1.00 0.41  ? 3875 MET A N     1 
ATOM   17686 C  CA    . MET A 1 3875 ? 197.883 169.324 231.797 1.00 0.39  ? 3875 MET A CA    1 
ATOM   17687 C  C     . MET A 1 3875 ? 197.342 168.440 230.687 1.00 0.36  ? 3875 MET A C     1 
ATOM   17688 O  O     . MET A 1 3875 ? 196.131 168.243 230.560 1.00 0.87  ? 3875 MET A O     1 
ATOM   17689 C  CB    . MET A 1 3875 ? 198.350 168.434 232.962 1.00 0.45  ? 3875 MET A CB    1 
ATOM   17690 C  CG    . MET A 1 3875 ? 199.095 169.158 234.062 1.00 0.55  ? 3875 MET A CG    1 
ATOM   17691 S  SD    . MET A 1 3875 ? 199.543 168.072 235.435 1.00 7.22  ? 3875 MET A SD    1 
ATOM   17692 C  CE    . MET A 1 3875 ? 200.814 167.066 234.691 1.00 1.00  ? 3875 MET A CE    1 
ATOM   17693 N  N     . LEU A 1 3876 ? 198.255 167.926 229.871 1.00 0.47  ? 3876 LEU A N     1 
ATOM   17694 C  CA    . LEU A 1 3876 ? 197.909 166.863 228.943 1.00 0.68  ? 3876 LEU A CA    1 
ATOM   17695 C  C     . LEU A 1 3876 ? 197.513 165.617 229.722 1.00 0.99  ? 3876 LEU A C     1 
ATOM   17696 O  O     . LEU A 1 3876 ? 198.100 165.306 230.762 1.00 2.95  ? 3876 LEU A O     1 
ATOM   17697 C  CB    . LEU A 1 3876 ? 199.082 166.560 228.015 1.00 1.32  ? 3876 LEU A CB    1 
ATOM   17698 C  CG    . LEU A 1 3876 ? 199.486 167.683 227.056 1.00 1.21  ? 3876 LEU A CG    1 
ATOM   17699 C  CD1   . LEU A 1 3876 ? 200.740 167.308 226.288 1.00 2.11  ? 3876 LEU A CD1   1 
ATOM   17700 C  CD2   . LEU A 1 3876 ? 198.348 168.012 226.106 1.00 0.69  ? 3876 LEU A CD2   1 
ATOM   17701 N  N     . HIS A 1 3877 ? 196.505 164.903 229.216 1.00 1.17  ? 3877 HIS A N     1 
ATOM   17702 C  CA    . HIS A 1 3877 ? 195.974 163.754 229.943 1.00 1.20  ? 3877 HIS A CA    1 
ATOM   17703 C  C     . HIS A 1 3877 ? 197.035 162.688 230.177 1.00 1.36  ? 3877 HIS A C     1 
ATOM   17704 O  O     . HIS A 1 3877 ? 196.976 161.965 231.178 1.00 1.80  ? 3877 HIS A O     1 
ATOM   17705 C  CB    . HIS A 1 3877 ? 194.786 163.165 229.183 1.00 0.92  ? 3877 HIS A CB    1 
ATOM   17706 C  CG    . HIS A 1 3877 ? 194.048 162.108 229.942 1.00 1.45  ? 3877 HIS A CG    1 
ATOM   17707 N  ND1   . HIS A 1 3877 ? 194.351 160.770 229.838 1.00 1.38  ? 3877 HIS A ND1   1 
ATOM   17708 C  CD2   . HIS A 1 3877 ? 193.019 162.195 230.816 1.00 4.45  ? 3877 HIS A CD2   1 
ATOM   17709 C  CE1   . HIS A 1 3877 ? 193.542 160.075 230.616 1.00 2.25  ? 3877 HIS A CE1   1 
ATOM   17710 N  NE2   . HIS A 1 3877 ? 192.722 160.916 231.220 1.00 7.03  ? 3877 HIS A NE2   1 
ATOM   17711 N  N     . GLN A 1 3878 ? 198.014 162.580 229.275 1.00 1.31  ? 3878 GLN A N     1 
ATOM   17712 C  CA    . GLN A 1 3878 ? 199.079 161.600 229.445 1.00 1.78  ? 3878 GLN A CA    1 
ATOM   17713 C  C     . GLN A 1 3878 ? 199.925 161.888 230.679 1.00 3.65  ? 3878 GLN A C     1 
ATOM   17714 O  O     . GLN A 1 3878 ? 200.528 160.970 231.245 1.00 6.22  ? 3878 GLN A O     1 
ATOM   17715 C  CB    . GLN A 1 3878 ? 199.958 161.565 228.195 1.00 3.86  ? 3878 GLN A CB    1 
ATOM   17716 C  CG    . GLN A 1 3878 ? 200.894 162.751 228.062 1.00 7.62  ? 3878 GLN A CG    1 
ATOM   17717 C  CD    . GLN A 1 3878 ? 201.535 162.838 226.697 1.00 13.16 ? 3878 GLN A CD    1 
ATOM   17718 O  OE1   . GLN A 1 3878 ? 202.759 162.906 226.575 1.00 18.64 ? 3878 GLN A OE1   1 
ATOM   17719 N  NE2   . GLN A 1 3878 ? 200.712 162.834 225.656 1.00 13.55 ? 3878 GLN A NE2   1 
ATOM   17720 N  N     . ASP A 1 3879 ? 199.984 163.144 231.112 1.00 3.28  ? 3879 ASP A N     1 
ATOM   17721 C  CA    . ASP A 1 3879 ? 200.763 163.522 232.280 1.00 2.17  ? 3879 ASP A CA    1 
ATOM   17722 C  C     . ASP A 1 3879 ? 199.953 163.512 233.571 1.00 1.22  ? 3879 ASP A C     1 
ATOM   17723 O  O     . ASP A 1 3879 ? 200.514 163.785 234.635 1.00 1.84  ? 3879 ASP A O     1 
ATOM   17724 C  CB    . ASP A 1 3879 ? 201.384 164.906 232.072 1.00 1.76  ? 3879 ASP A CB    1 
ATOM   17725 C  CG    . ASP A 1 3879 ? 202.371 164.940 230.926 1.00 6.16  ? 3879 ASP A CG    1 
ATOM   17726 O  OD1   . ASP A 1 3879 ? 203.319 164.131 230.931 1.00 10.65 ? 3879 ASP A OD1   1 
ATOM   17727 O  OD2   . ASP A 1 3879 ? 202.208 165.789 230.026 1.00 8.37  ? 3879 ASP A OD2   1 
ATOM   17728 N  N     . HIS A 1 3880 ? 198.656 163.203 233.503 1.00 1.14  ? 3880 HIS A N     1 
ATOM   17729 C  CA    . HIS A 1 3880 ? 197.828 163.205 234.706 1.00 0.90  ? 3880 HIS A CA    1 
ATOM   17730 C  C     . HIS A 1 3880 ? 198.294 162.152 235.702 1.00 1.19  ? 3880 HIS A C     1 
ATOM   17731 O  O     . HIS A 1 3880 ? 198.316 162.401 236.914 1.00 1.60  ? 3880 HIS A O     1 
ATOM   17732 C  CB    . HIS A 1 3880 ? 196.362 162.978 234.338 1.00 0.63  ? 3880 HIS A CB    1 
ATOM   17733 C  CG    . HIS A 1 3880 ? 195.725 164.146 233.653 1.00 1.03  ? 3880 HIS A CG    1 
ATOM   17734 N  ND1   . HIS A 1 3880 ? 194.376 164.198 233.379 1.00 0.58  ? 3880 HIS A ND1   1 
ATOM   17735 C  CD2   . HIS A 1 3880 ? 196.248 165.303 233.190 1.00 0.46  ? 3880 HIS A CD2   1 
ATOM   17736 C  CE1   . HIS A 1 3880 ? 194.095 165.338 232.774 1.00 0.33  ? 3880 HIS A CE1   1 
ATOM   17737 N  NE2   . HIS A 1 3880 ? 195.216 166.026 232.647 1.00 0.51  ? 3880 HIS A NE2   1 
ATOM   17738 N  N     . ILE A 1 3881 ? 198.664 160.968 235.214 1.00 2.27  ? 3881 ILE A N     1 
ATOM   17739 C  CA    . ILE A 1 3881 ? 199.120 159.910 236.108 1.00 1.31  ? 3881 ILE A CA    1 
ATOM   17740 C  C     . ILE A 1 3881 ? 200.429 160.298 236.778 1.00 1.28  ? 3881 ILE A C     1 
ATOM   17741 O  O     . ILE A 1 3881 ? 200.666 159.946 237.939 1.00 1.44  ? 3881 ILE A O     1 
ATOM   17742 C  CB    . ILE A 1 3881 ? 199.231 158.573 235.344 1.00 1.17  ? 3881 ILE A CB    1 
ATOM   17743 C  CG1   . ILE A 1 3881 ? 199.496 157.417 236.314 1.00 3.08  ? 3881 ILE A CG1   1 
ATOM   17744 C  CG2   . ILE A 1 3881 ? 200.299 158.642 234.259 1.00 1.17  ? 3881 ILE A CG2   1 
ATOM   17745 C  CD1   . ILE A 1 3881 ? 198.462 157.285 237.405 1.00 0.92  ? 3881 ILE A CD1   1 
ATOM   17746 N  N     . THR A 1 3882 ? 201.296 161.032 236.076 1.00 1.26  ? 3882 THR A N     1 
ATOM   17747 C  CA    . THR A 1 3882 ? 202.577 161.428 236.650 1.00 2.08  ? 3882 THR A CA    1 
ATOM   17748 C  C     . THR A 1 3882 ? 202.385 162.350 237.847 1.00 1.25  ? 3882 THR A C     1 
ATOM   17749 O  O     . THR A 1 3882 ? 203.016 162.167 238.893 1.00 2.68  ? 3882 THR A O     1 
ATOM   17750 C  CB    . THR A 1 3882 ? 203.440 162.100 235.584 1.00 3.01  ? 3882 THR A CB    1 
ATOM   17751 O  OG1   . THR A 1 3882 ? 203.524 161.252 234.433 1.00 6.09  ? 3882 THR A OG1   1 
ATOM   17752 C  CG2   . THR A 1 3882 ? 204.837 162.355 236.116 1.00 2.14  ? 3882 THR A CG2   1 
ATOM   17753 N  N     . PHE A 1 3883 ? 201.516 163.354 237.710 1.00 1.10  ? 3883 PHE A N     1 
ATOM   17754 C  CA    . PHE A 1 3883 ? 201.247 164.258 238.824 1.00 0.78  ? 3883 PHE A CA    1 
ATOM   17755 C  C     . PHE A 1 3883 ? 200.545 163.538 239.970 1.00 0.68  ? 3883 PHE A C     1 
ATOM   17756 O  O     . PHE A 1 3883 ? 200.872 163.762 241.141 1.00 0.75  ? 3883 PHE A O     1 
ATOM   17757 C  CB    . PHE A 1 3883 ? 200.417 165.451 238.350 1.00 0.45  ? 3883 PHE A CB    1 
ATOM   17758 C  CG    . PHE A 1 3883 ? 200.243 166.517 239.390 1.00 0.29  ? 3883 PHE A CG    1 
ATOM   17759 C  CD1   . PHE A 1 3883 ? 201.295 166.883 240.209 1.00 0.35  ? 3883 PHE A CD1   1 
ATOM   17760 C  CD2   . PHE A 1 3883 ? 199.023 167.144 239.560 1.00 0.35  ? 3883 PHE A CD2   1 
ATOM   17761 C  CE1   . PHE A 1 3883 ? 201.135 167.857 241.172 1.00 0.40  ? 3883 PHE A CE1   1 
ATOM   17762 C  CE2   . PHE A 1 3883 ? 198.859 168.120 240.521 1.00 0.25  ? 3883 PHE A CE2   1 
ATOM   17763 C  CZ    . PHE A 1 3883 ? 199.916 168.477 241.327 1.00 0.22  ? 3883 PHE A CZ    1 
ATOM   17764 N  N     . ALA A 1 3884 ? 199.577 162.677 239.654 1.00 0.96  ? 3884 ALA A N     1 
ATOM   17765 C  CA    . ALA A 1 3884 ? 198.895 161.917 240.697 1.00 0.62  ? 3884 ALA A CA    1 
ATOM   17766 C  C     . ALA A 1 3884 ? 199.837 160.942 241.389 1.00 0.91  ? 3884 ALA A C     1 
ATOM   17767 O  O     . ALA A 1 3884 ? 199.679 160.675 242.584 1.00 0.84  ? 3884 ALA A O     1 
ATOM   17768 C  CB    . ALA A 1 3884 ? 197.695 161.177 240.111 1.00 0.59  ? 3884 ALA A CB    1 
ATOM   17769 N  N     . MET A 1 3885 ? 200.814 160.402 240.656 1.00 0.71  ? 3885 MET A N     1 
ATOM   17770 C  CA    . MET A 1 3885 ? 201.806 159.522 241.263 1.00 0.83  ? 3885 MET A CA    1 
ATOM   17771 C  C     . MET A 1 3885 ? 202.619 160.264 242.317 1.00 1.76  ? 3885 MET A C     1 
ATOM   17772 O  O     . MET A 1 3885 ? 202.927 159.716 243.381 1.00 2.05  ? 3885 MET A O     1 
ATOM   17773 C  CB    . MET A 1 3885 ? 202.732 158.955 240.188 1.00 3.43  ? 3885 MET A CB    1 
ATOM   17774 C  CG    . MET A 1 3885 ? 202.246 157.677 239.523 1.00 1.92  ? 3885 MET A CG    1 
ATOM   17775 S  SD    . MET A 1 3885 ? 201.928 156.324 240.663 1.00 16.65 ? 3885 MET A SD    1 
ATOM   17776 C  CE    . MET A 1 3885 ? 203.530 155.527 240.692 1.00 11.80 ? 3885 MET A CE    1 
ATOM   17777 N  N     . LEU A 1 3886 ? 202.981 161.517 242.032 1.00 1.30  ? 3886 LEU A N     1 
ATOM   17778 C  CA    . LEU A 1 3886 ? 203.775 162.298 242.972 1.00 1.05  ? 3886 LEU A CA    1 
ATOM   17779 C  C     . LEU A 1 3886 ? 202.949 162.729 244.175 1.00 1.42  ? 3886 LEU A C     1 
ATOM   17780 O  O     . LEU A 1 3886 ? 203.442 162.715 245.310 1.00 5.14  ? 3886 LEU A O     1 
ATOM   17781 C  CB    . LEU A 1 3886 ? 204.370 163.512 242.266 1.00 1.12  ? 3886 LEU A CB    1 
ATOM   17782 C  CG    . LEU A 1 3886 ? 205.311 163.199 241.102 1.00 1.45  ? 3886 LEU A CG    1 
ATOM   17783 C  CD1   . LEU A 1 3886 ? 205.535 164.440 240.264 1.00 1.59  ? 3886 LEU A CD1   1 
ATOM   17784 C  CD2   . LEU A 1 3886 ? 206.629 162.639 241.607 1.00 1.36  ? 3886 LEU A CD2   1 
ATOM   17785 N  N     . LEU A 1 3887 ? 201.691 163.118 243.954 1.00 0.86  ? 3887 LEU A N     1 
ATOM   17786 C  CA    . LEU A 1 3887 ? 200.831 163.490 245.075 1.00 1.39  ? 3887 LEU A CA    1 
ATOM   17787 C  C     . LEU A 1 3887 ? 200.611 162.304 246.004 1.00 1.84  ? 3887 LEU A C     1 
ATOM   17788 O  O     . LEU A 1 3887 ? 200.533 162.468 247.225 1.00 3.42  ? 3887 LEU A O     1 
ATOM   17789 C  CB    . LEU A 1 3887 ? 199.495 164.029 244.564 1.00 1.35  ? 3887 LEU A CB    1 
ATOM   17790 C  CG    . LEU A 1 3887 ? 199.519 165.329 243.761 1.00 1.07  ? 3887 LEU A CG    1 
ATOM   17791 C  CD1   . LEU A 1 3887 ? 198.112 165.712 243.331 1.00 0.35  ? 3887 LEU A CD1   1 
ATOM   17792 C  CD2   . LEU A 1 3887 ? 200.170 166.455 244.550 1.00 0.51  ? 3887 LEU A CD2   1 
ATOM   17793 N  N     . ALA A 1 3888 ? 200.506 161.100 245.437 1.00 2.17  ? 3888 ALA A N     1 
ATOM   17794 C  CA    . ALA A 1 3888 ? 200.406 159.900 246.259 1.00 2.50  ? 3888 ALA A CA    1 
ATOM   17795 C  C     . ALA A 1 3888 ? 201.668 159.689 247.082 1.00 3.16  ? 3888 ALA A C     1 
ATOM   17796 O  O     . ALA A 1 3888 ? 201.596 159.313 248.258 1.00 5.87  ? 3888 ALA A O     1 
ATOM   17797 C  CB    . ALA A 1 3888 ? 200.129 158.685 245.374 1.00 2.93  ? 3888 ALA A CB    1 
ATOM   17798 N  N     . ARG A 1 3889 ? 202.837 159.925 246.485 1.00 3.44  ? 3889 ARG A N     1 
ATOM   17799 C  CA    . ARG A 1 3889 ? 204.090 159.761 247.214 1.00 3.07  ? 3889 ARG A CA    1 
ATOM   17800 C  C     . ARG A 1 3889 ? 204.227 160.799 248.321 1.00 5.54  ? 3889 ARG A C     1 
ATOM   17801 O  O     . ARG A 1 3889 ? 204.775 160.505 249.388 1.00 12.10 ? 3889 ARG A O     1 
ATOM   17802 C  CB    . ARG A 1 3889 ? 205.272 159.838 246.249 1.00 4.44  ? 3889 ARG A CB    1 
ATOM   17803 C  CG    . ARG A 1 3889 ? 205.344 158.668 245.283 1.00 3.83  ? 3889 ARG A CG    1 
ATOM   17804 C  CD    . ARG A 1 3889 ? 206.774 158.248 245.015 1.00 3.81  ? 3889 ARG A CD    1 
ATOM   17805 N  NE    . ARG A 1 3889 ? 207.539 158.094 246.244 1.00 8.69  ? 3889 ARG A NE    1 
ATOM   17806 C  CZ    . ARG A 1 3889 ? 208.863 158.122 246.309 1.00 9.13  ? 3889 ARG A CZ    1 
ATOM   17807 N  NH1   . ARG A 1 3889 ? 209.604 158.313 245.230 1.00 5.19  ? 3889 ARG A NH1   1 
ATOM   17808 N  NH2   . ARG A 1 3889 ? 209.457 157.952 247.487 1.00 11.56 ? 3889 ARG A NH2   1 
ATOM   17809 N  N     . ILE A 1 3890 ? 203.748 162.022 248.081 1.00 3.33  ? 3890 ILE A N     1 
ATOM   17810 C  CA    . ILE A 1 3890 ? 203.727 163.031 249.136 1.00 2.97  ? 3890 ILE A CA    1 
ATOM   17811 C  C     . ILE A 1 3890 ? 202.786 162.611 250.257 1.00 4.24  ? 3890 ILE A C     1 
ATOM   17812 O  O     . ILE A 1 3890 ? 203.120 162.727 251.442 1.00 9.23  ? 3890 ILE A O     1 
ATOM   17813 C  CB    . ILE A 1 3890 ? 203.344 164.405 248.556 1.00 2.54  ? 3890 ILE A CB    1 
ATOM   17814 C  CG1   . ILE A 1 3890 ? 204.399 164.881 247.561 1.00 1.32  ? 3890 ILE A CG1   1 
ATOM   17815 C  CG2   . ILE A 1 3890 ? 203.163 165.427 249.665 1.00 2.00  ? 3890 ILE A CG2   1 
ATOM   17816 C  CD1   . ILE A 1 3890 ? 204.037 166.172 246.871 1.00 1.44  ? 3890 ILE A CD1   1 
ATOM   17817 N  N     . LYS A 1 3891 ? 201.596 162.118 249.907 1.00 3.66  ? 3891 LYS A N     1 
ATOM   17818 C  CA    . LYS A 1 3891 ? 200.652 161.665 250.924 1.00 3.54  ? 3891 LYS A CA    1 
ATOM   17819 C  C     . LYS A 1 3891 ? 201.185 160.461 251.687 1.00 8.81  ? 3891 LYS A C     1 
ATOM   17820 O  O     . LYS A 1 3891 ? 200.918 160.322 252.887 1.00 6.04  ? 3891 LYS A O     1 
ATOM   17821 C  CB    . LYS A 1 3891 ? 199.305 161.329 250.287 1.00 3.80  ? 3891 LYS A CB    1 
ATOM   17822 C  CG    . LYS A 1 3891 ? 198.161 161.238 251.283 1.00 3.36  ? 3891 LYS A CG    1 
ATOM   17823 C  CD    . LYS A 1 3891 ? 197.057 160.331 250.774 1.00 6.76  ? 3891 LYS A CD    1 
ATOM   17824 C  CE    . LYS A 1 3891 ? 195.902 160.257 251.760 1.00 9.23  ? 3891 LYS A CE    1 
ATOM   17825 N  NZ    . LYS A 1 3891 ? 194.665 159.727 251.123 1.00 9.56  ? 3891 LYS A NZ    1 
ATOM   17826 N  N     . LEU A 1 3892 ? 201.926 159.584 251.010 1.00 7.83  ? 3892 LEU A N     1 
ATOM   17827 C  CA    . LEU A 1 3892 ? 202.502 158.422 251.677 1.00 9.03  ? 3892 LEU A CA    1 
ATOM   17828 C  C     . LEU A 1 3892 ? 203.497 158.840 252.752 1.00 12.64 ? 3892 LEU A C     1 
ATOM   17829 O  O     . LEU A 1 3892 ? 203.539 158.242 253.834 1.00 18.84 ? 3892 LEU A O     1 
ATOM   17830 C  CB    . LEU A 1 3892 ? 203.166 157.514 250.642 1.00 10.91 ? 3892 LEU A CB    1 
ATOM   17831 C  CG    . LEU A 1 3892 ? 203.700 156.165 251.113 1.00 11.09 ? 3892 LEU A CG    1 
ATOM   17832 C  CD1   . LEU A 1 3892 ? 202.658 155.445 251.947 1.00 10.28 ? 3892 LEU A CD1   1 
ATOM   17833 C  CD2   . LEU A 1 3892 ? 204.101 155.329 249.914 1.00 11.23 ? 3892 LEU A CD2   1 
ATOM   17834 N  N     . LYS A 1 3893 ? 204.302 159.869 252.473 1.00 10.53 ? 3893 LYS A N     1 
ATOM   17835 C  CA    . LYS A 1 3893 ? 205.239 160.376 253.470 1.00 8.91  ? 3893 LYS A CA    1 
ATOM   17836 C  C     . LYS A 1 3893 ? 204.523 160.931 254.694 1.00 13.92 ? 3893 LYS A C     1 
ATOM   17837 O  O     . LYS A 1 3893 ? 205.079 160.916 255.797 1.00 25.43 ? 3893 LYS A O     1 
ATOM   17838 C  CB    . LYS A 1 3893 ? 206.130 161.450 252.848 1.00 11.48 ? 3893 LYS A CB    1 
ATOM   17839 C  CG    . LYS A 1 3893 ? 207.228 160.905 251.951 1.00 11.61 ? 3893 LYS A CG    1 
ATOM   17840 C  CD    . LYS A 1 3893 ? 208.164 162.009 251.506 1.00 10.27 ? 3893 LYS A CD    1 
ATOM   17841 C  CE    . LYS A 1 3893 ? 208.738 162.764 252.690 1.00 10.25 ? 3893 LYS A CE    1 
ATOM   17842 N  NZ    . LYS A 1 3893 ? 209.719 163.798 252.261 1.00 19.11 ? 3893 LYS A NZ    1 
ATOM   17843 N  N     . GLY A 1 3894 ? 203.298 161.432 254.525 1.00 14.16 ? 3894 GLY A N     1 
ATOM   17844 C  CA    . GLY A 1 3894 ? 202.557 161.973 255.649 1.00 12.21 ? 3894 GLY A CA    1 
ATOM   17845 C  C     . GLY A 1 3894 ? 202.022 160.926 256.601 1.00 17.24 ? 3894 GLY A C     1 
ATOM   17846 O  O     . GLY A 1 3894 ? 201.683 161.255 257.741 1.00 25.37 ? 3894 GLY A O     1 
ATOM   17847 N  N     . THR A 1 3895 ? 201.942 159.672 256.162 1.00 20.73 ? 3895 THR A N     1 
ATOM   17848 C  CA    . THR A 1 3895 ? 201.421 158.593 256.995 1.00 21.16 ? 3895 THR A CA    1 
ATOM   17849 C  C     . THR A 1 3895 ? 202.527 158.110 257.927 1.00 25.29 ? 3895 THR A C     1 
ATOM   17850 O  O     . THR A 1 3895 ? 203.540 157.567 257.474 1.00 25.69 ? 3895 THR A O     1 
ATOM   17851 C  CB    . THR A 1 3895 ? 200.903 157.450 256.128 1.00 21.10 ? 3895 THR A CB    1 
ATOM   17852 O  OG1   . THR A 1 3895 ? 199.863 157.933 255.268 1.00 18.37 ? 3895 THR A OG1   1 
ATOM   17853 C  CG2   . THR A 1 3895 ? 200.343 156.343 257.005 1.00 19.24 ? 3895 THR A CG2   1 
ATOM   17854 N  N     . VAL A 1 3896 ? 202.332 158.310 259.233 1.00 24.38 ? 3896 VAL A N     1 
ATOM   17855 C  CA    . VAL A 1 3896 ? 203.339 157.906 260.210 1.00 25.72 ? 3896 VAL A CA    1 
ATOM   17856 C  C     . VAL A 1 3896 ? 203.463 156.386 260.256 1.00 24.22 ? 3896 VAL A C     1 
ATOM   17857 O  O     . VAL A 1 3896 ? 204.561 155.844 260.420 1.00 28.09 ? 3896 VAL A O     1 
ATOM   17858 C  CB    . VAL A 1 3896 ? 203.002 158.492 261.592 1.00 27.19 ? 3896 VAL A CB    1 
ATOM   17859 C  CG1   . VAL A 1 3896 ? 204.054 158.092 262.615 1.00 27.09 ? 3896 VAL A CG1   1 
ATOM   17860 C  CG2   . VAL A 1 3896 ? 202.881 160.006 261.510 1.00 20.76 ? 3896 VAL A CG2   1 
ATOM   17861 N  N     . GLY A 1 3897 ? 202.348 155.678 260.101 1.00 23.13 ? 3897 GLY A N     1 
ATOM   17862 C  CA    . GLY A 1 3897 ? 202.339 154.232 260.150 1.00 21.82 ? 3897 GLY A CA    1 
ATOM   17863 C  C     . GLY A 1 3897 ? 202.847 153.525 258.915 1.00 25.95 ? 3897 GLY A C     1 
ATOM   17864 O  O     . GLY A 1 3897 ? 202.919 152.293 258.908 1.00 24.45 ? 3897 GLY A O     1 
ATOM   17865 N  N     . GLU A 1 3898 ? 203.205 154.266 257.856 1.00 21.54 ? 3898 GLU A N     1 
ATOM   17866 C  CA    . GLU A 1 3898 ? 203.706 153.581 256.678 1.00 19.21 ? 3898 GLU A CA    1 
ATOM   17867 C  C     . GLU A 1 3898 ? 205.226 153.671 256.601 1.00 19.90 ? 3898 GLU A C     1 
ATOM   17868 O  O     . GLU A 1 3898 ? 205.820 154.661 257.037 1.00 23.28 ? 3898 GLU A O     1 
ATOM   17869 C  CB    . GLU A 1 3898 ? 203.106 154.179 255.402 1.00 18.00 ? 3898 GLU A CB    1 
ATOM   17870 C  CG    . GLU A 1 3898 ? 201.706 153.684 255.076 1.00 17.86 ? 3898 GLU A CG    1 
ATOM   17871 C  CD    . GLU A 1 3898 ? 201.634 152.183 254.928 1.00 18.55 ? 3898 GLU A CD    1 
ATOM   17872 O  OE1   . GLU A 1 3898 ? 202.322 151.634 254.043 1.00 17.01 ? 3898 GLU A OE1   1 
ATOM   17873 O  OE2   . GLU A 1 3898 ? 200.886 151.550 255.701 1.00 24.41 ? 3898 GLU A OE2   1 
ATOM   17874 N  N     . PRO A 1 3899 ? 205.878 152.649 256.055 1.00 19.15 ? 3899 PRO A N     1 
ATOM   17875 C  CA    . PRO A 1 3899 ? 207.320 152.733 255.806 1.00 17.01 ? 3899 PRO A CA    1 
ATOM   17876 C  C     . PRO A 1 3899 ? 207.628 153.695 254.668 1.00 19.92 ? 3899 PRO A C     1 
ATOM   17877 O  O     . PRO A 1 3899 ? 206.743 154.207 253.980 1.00 21.33 ? 3899 PRO A O     1 
ATOM   17878 C  CB    . PRO A 1 3899 ? 207.718 151.298 255.444 1.00 11.58 ? 3899 PRO A CB    1 
ATOM   17879 C  CG    . PRO A 1 3899 ? 206.567 150.444 255.878 1.00 14.03 ? 3899 PRO A CG    1 
ATOM   17880 C  CD    . PRO A 1 3899 ? 205.349 151.303 255.786 1.00 16.05 ? 3899 PRO A CD    1 
ATOM   17881 N  N     . THR A 1 3900 ? 208.925 153.935 254.474 1.00 20.23 ? 3900 THR A N     1 
ATOM   17882 C  CA    . THR A 1 3900 ? 209.367 154.882 253.455 1.00 19.11 ? 3900 THR A CA    1 
ATOM   17883 C  C     . THR A 1 3900 ? 209.252 154.307 252.049 1.00 16.18 ? 3900 THR A C     1 
ATOM   17884 O  O     . THR A 1 3900 ? 208.934 155.039 251.104 1.00 16.65 ? 3900 THR A O     1 
ATOM   17885 C  CB    . THR A 1 3900 ? 210.809 155.312 253.728 1.00 17.93 ? 3900 THR A CB    1 
ATOM   17886 O  OG1   . THR A 1 3900 ? 211.705 154.284 253.288 1.00 19.77 ? 3900 THR A OG1   1 
ATOM   17887 C  CG2   . THR A 1 3900 ? 211.021 155.560 255.212 1.00 19.32 ? 3900 THR A CG2   1 
ATOM   17888 N  N     . TYR A 1 3901 ? 209.517 153.010 251.891 1.00 15.44 ? 3901 TYR A N     1 
ATOM   17889 C  CA    . TYR A 1 3901 ? 209.583 152.357 250.581 1.00 13.36 ? 3901 TYR A CA    1 
ATOM   17890 C  C     . TYR A 1 3901 ? 210.581 153.045 249.653 1.00 16.94 ? 3901 TYR A C     1 
ATOM   17891 O  O     . TYR A 1 3901 ? 210.407 153.050 248.433 1.00 19.10 ? 3901 TYR A O     1 
ATOM   17892 C  CB    . TYR A 1 3901 ? 208.208 152.285 249.911 1.00 11.24 ? 3901 TYR A CB    1 
ATOM   17893 C  CG    . TYR A 1 3901 ? 207.110 151.722 250.779 1.00 12.64 ? 3901 TYR A CG    1 
ATOM   17894 C  CD1   . TYR A 1 3901 ? 207.053 150.364 251.066 1.00 9.25  ? 3901 TYR A CD1   1 
ATOM   17895 C  CD2   . TYR A 1 3901 ? 206.120 152.544 251.299 1.00 11.07 ? 3901 TYR A CD2   1 
ATOM   17896 C  CE1   . TYR A 1 3901 ? 206.049 149.844 251.853 1.00 8.60  ? 3901 TYR A CE1   1 
ATOM   17897 C  CE2   . TYR A 1 3901 ? 205.109 152.033 252.083 1.00 12.37 ? 3901 TYR A CE2   1 
ATOM   17898 C  CZ    . TYR A 1 3901 ? 205.079 150.681 252.358 1.00 13.22 ? 3901 TYR A CZ    1 
ATOM   17899 O  OH    . TYR A 1 3901 ? 204.071 150.169 253.142 1.00 17.14 ? 3901 TYR A OH    1 
ATOM   17900 N  N     . ASP A 1 3902 ? 211.639 153.627 250.224 1.00 16.11 ? 3902 ASP A N     1 
ATOM   17901 C  CA    . ASP A 1 3902 ? 212.609 154.352 249.410 1.00 16.25 ? 3902 ASP A CA    1 
ATOM   17902 C  C     . ASP A 1 3902 ? 213.344 153.418 248.458 1.00 18.72 ? 3902 ASP A C     1 
ATOM   17903 O  O     . ASP A 1 3902 ? 213.596 153.775 247.302 1.00 21.46 ? 3902 ASP A O     1 
ATOM   17904 C  CB    . ASP A 1 3902 ? 213.597 155.094 250.309 1.00 21.74 ? 3902 ASP A CB    1 
ATOM   17905 C  CG    . ASP A 1 3902 ? 212.956 156.257 251.040 1.00 29.64 ? 3902 ASP A CG    1 
ATOM   17906 O  OD1   . ASP A 1 3902 ? 211.764 156.531 250.788 1.00 26.85 ? 3902 ASP A OD1   1 
ATOM   17907 O  OD2   . ASP A 1 3902 ? 213.643 156.896 251.863 1.00 31.50 ? 3902 ASP A OD2   1 
ATOM   17908 N  N     . ALA A 1 3903 ? 213.701 152.219 248.925 1.00 16.87 ? 3903 ALA A N     1 
ATOM   17909 C  CA    . ALA A 1 3903 ? 214.387 151.266 248.059 1.00 19.13 ? 3903 ALA A CA    1 
ATOM   17910 C  C     . ALA A 1 3903 ? 213.496 150.818 246.907 1.00 17.52 ? 3903 ALA A C     1 
ATOM   17911 O  O     . ALA A 1 3903 ? 213.951 150.729 245.761 1.00 19.93 ? 3903 ALA A O     1 
ATOM   17912 C  CB    . ALA A 1 3903 ? 214.853 150.061 248.877 1.00 15.49 ? 3903 ALA A CB    1 
ATOM   17913 N  N     . GLU A 1 3904 ? 212.225 150.530 247.192 1.00 15.16 ? 3904 GLU A N     1 
ATOM   17914 C  CA    . GLU A 1 3904 ? 211.307 150.108 246.137 1.00 14.43 ? 3904 GLU A CA    1 
ATOM   17915 C  C     . GLU A 1 3904 ? 211.067 151.218 245.121 1.00 16.42 ? 3904 GLU A C     1 
ATOM   17916 O  O     . GLU A 1 3904 ? 211.017 150.958 243.914 1.00 23.24 ? 3904 GLU A O     1 
ATOM   17917 C  CB    . GLU A 1 3904 ? 209.992 149.627 246.750 1.00 17.08 ? 3904 GLU A CB    1 
ATOM   17918 C  CG    . GLU A 1 3904 ? 210.116 148.339 247.560 1.00 20.28 ? 3904 GLU A CG    1 
ATOM   17919 C  CD    . GLU A 1 3904 ? 210.606 148.564 248.975 1.00 24.44 ? 3904 GLU A CD    1 
ATOM   17920 O  OE1   . GLU A 1 3904 ? 210.798 149.734 249.365 1.00 22.42 ? 3904 GLU A OE1   1 
ATOM   17921 O  OE2   . GLU A 1 3904 ? 210.802 147.566 249.700 1.00 26.53 ? 3904 GLU A OE2   1 
ATOM   17922 N  N     . PHE A 1 3905 ? 210.914 152.460 245.583 1.00 12.56 ? 3905 PHE A N     1 
ATOM   17923 C  CA    . PHE A 1 3905 ? 210.801 153.566 244.640 1.00 10.17 ? 3905 PHE A CA    1 
ATOM   17924 C  C     . PHE A 1 3905 ? 212.134 153.856 243.962 1.00 13.78 ? 3905 PHE A C     1 
ATOM   17925 O  O     . PHE A 1 3905 ? 212.156 154.346 242.828 1.00 18.47 ? 3905 PHE A O     1 
ATOM   17926 C  CB    . PHE A 1 3905 ? 210.269 154.818 245.336 1.00 13.24 ? 3905 PHE A CB    1 
ATOM   17927 C  CG    . PHE A 1 3905 ? 208.786 154.795 245.567 1.00 7.06  ? 3905 PHE A CG    1 
ATOM   17928 C  CD1   . PHE A 1 3905 ? 207.909 154.809 244.498 1.00 5.03  ? 3905 PHE A CD1   1 
ATOM   17929 C  CD2   . PHE A 1 3905 ? 208.273 154.766 246.850 1.00 7.15  ? 3905 PHE A CD2   1 
ATOM   17930 C  CE1   . PHE A 1 3905 ? 206.547 154.784 244.705 1.00 6.98  ? 3905 PHE A CE1   1 
ATOM   17931 C  CE2   . PHE A 1 3905 ? 206.910 154.746 247.063 1.00 8.41  ? 3905 PHE A CE2   1 
ATOM   17932 C  CZ    . PHE A 1 3905 ? 206.045 154.754 245.989 1.00 10.25 ? 3905 PHE A CZ    1 
ATOM   17933 N  N     . GLN A 1 3906 ? 213.247 153.564 244.637 1.00 16.31 ? 3906 GLN A N     1 
ATOM   17934 C  CA    . GLN A 1 3906 ? 214.547 153.660 243.984 1.00 14.87 ? 3906 GLN A CA    1 
ATOM   17935 C  C     . GLN A 1 3906 ? 214.648 152.673 242.831 1.00 17.32 ? 3906 GLN A C     1 
ATOM   17936 O  O     . GLN A 1 3906 ? 215.211 152.990 241.778 1.00 18.78 ? 3906 GLN A O     1 
ATOM   17937 C  CB    . GLN A 1 3906 ? 215.665 153.412 244.998 1.00 16.96 ? 3906 GLN A CB    1 
ATOM   17938 C  CG    . GLN A 1 3906 ? 217.070 153.559 244.443 1.00 18.38 ? 3906 GLN A CG    1 
ATOM   17939 C  CD    . GLN A 1 3906 ? 217.356 154.959 243.944 1.00 28.40 ? 3906 GLN A CD    1 
ATOM   17940 O  OE1   . GLN A 1 3906 ? 217.386 155.209 242.741 1.00 27.89 ? 3906 GLN A OE1   1 
ATOM   17941 N  NE2   . GLN A 1 3906 ? 217.572 155.885 244.872 1.00 24.72 ? 3906 GLN A NE2   1 
ATOM   17942 N  N     . HIS A 1 3907 ? 214.106 151.467 243.013 1.00 15.08 ? 3907 HIS A N     1 
ATOM   17943 C  CA    . HIS A 1 3907 ? 214.111 150.483 241.938 1.00 13.51 ? 3907 HIS A CA    1 
ATOM   17944 C  C     . HIS A 1 3907 ? 213.064 150.795 240.878 1.00 17.04 ? 3907 HIS A C     1 
ATOM   17945 O  O     . HIS A 1 3907 ? 213.286 150.531 239.691 1.00 20.96 ? 3907 HIS A O     1 
ATOM   17946 C  CB    . HIS A 1 3907 ? 213.886 149.082 242.501 1.00 20.07 ? 3907 HIS A CB    1 
ATOM   17947 C  CG    . HIS A 1 3907 ? 214.188 147.994 241.522 1.00 19.22 ? 3907 HIS A CG    1 
ATOM   17948 N  ND1   . HIS A 1 3907 ? 215.473 147.598 241.223 1.00 19.23 ? 3907 HIS A ND1   1 
ATOM   17949 C  CD2   . HIS A 1 3907 ? 213.372 147.235 240.754 1.00 17.67 ? 3907 HIS A CD2   1 
ATOM   17950 C  CE1   . HIS A 1 3907 ? 215.435 146.635 240.320 1.00 22.86 ? 3907 HIS A CE1   1 
ATOM   17951 N  NE2   . HIS A 1 3907 ? 214.172 146.395 240.019 1.00 24.61 ? 3907 HIS A NE2   1 
ATOM   17952 N  N     . PHE A 1 3908 ? 211.916 151.341 241.284 1.00 15.09 ? 3908 PHE A N     1 
ATOM   17953 C  CA    . PHE A 1 3908 ? 210.871 151.668 240.319 1.00 14.69 ? 3908 PHE A CA    1 
ATOM   17954 C  C     . PHE A 1 3908 ? 211.352 152.721 239.331 1.00 12.70 ? 3908 PHE A C     1 
ATOM   17955 O  O     . PHE A 1 3908 ? 211.140 152.597 238.120 1.00 13.63 ? 3908 PHE A O     1 
ATOM   17956 C  CB    . PHE A 1 3908 ? 209.614 152.135 241.053 1.00 11.81 ? 3908 PHE A CB    1 
ATOM   17957 C  CG    . PHE A 1 3908 ? 208.456 152.426 240.145 1.00 10.99 ? 3908 PHE A CG    1 
ATOM   17958 C  CD1   . PHE A 1 3908 ? 207.864 151.414 239.411 1.00 9.43  ? 3908 PHE A CD1   1 
ATOM   17959 C  CD2   . PHE A 1 3908 ? 207.941 153.708 240.048 1.00 11.32 ? 3908 PHE A CD2   1 
ATOM   17960 C  CE1   . PHE A 1 3908 ? 206.799 151.677 238.580 1.00 11.19 ? 3908 PHE A CE1   1 
ATOM   17961 C  CE2   . PHE A 1 3908 ? 206.866 153.974 239.224 1.00 13.55 ? 3908 PHE A CE2   1 
ATOM   17962 C  CZ    . PHE A 1 3908 ? 206.292 152.958 238.492 1.00 9.38  ? 3908 PHE A CZ    1 
ATOM   17963 N  N     . LEU A 1 3909 ? 212.009 153.762 239.830 1.00 10.26 ? 3909 LEU A N     1 
ATOM   17964 C  CA    . LEU A 1 3909 ? 212.688 154.706 238.962 1.00 10.25 ? 3909 LEU A CA    1 
ATOM   17965 C  C     . LEU A 1 3909 ? 214.049 154.144 238.561 1.00 17.73 ? 3909 LEU A C     1 
ATOM   17966 O  O     . LEU A 1 3909 ? 214.539 153.169 239.136 1.00 22.32 ? 3909 LEU A O     1 
ATOM   17967 C  CB    . LEU A 1 3909 ? 212.843 156.058 239.654 1.00 13.05 ? 3909 LEU A CB    1 
ATOM   17968 C  CG    . LEU A 1 3909 ? 211.577 156.669 240.257 1.00 13.56 ? 3909 LEU A CG    1 
ATOM   17969 C  CD1   . LEU A 1 3909 ? 211.868 158.051 240.815 1.00 16.38 ? 3909 LEU A CD1   1 
ATOM   17970 C  CD2   . LEU A 1 3909 ? 210.461 156.727 239.230 1.00 10.10 ? 3909 LEU A CD2   1 
ATOM   17971 N  N     . ARG A 1 3910 ? 214.660 154.770 237.554 1.00 19.10 ? 3910 ARG A N     1 
ATOM   17972 C  CA    . ARG A 1 3910 ? 215.960 154.333 237.054 1.00 26.49 ? 3910 ARG A CA    1 
ATOM   17973 C  C     . ARG A 1 3910 ? 215.919 152.847 236.716 1.00 32.31 ? 3910 ARG A C     1 
ATOM   17974 O  O     . ARG A 1 3910 ? 215.450 152.465 235.637 1.00 29.90 ? 3910 ARG A O     1 
ATOM   17975 C  CB    . ARG A 1 3910 ? 217.057 154.639 238.082 1.00 21.06 ? 3910 ARG A CB    1 
ATOM   17976 C  CG    . ARG A 1 3910 ? 217.088 156.103 238.492 1.00 26.55 ? 3910 ARG A CG    1 
ATOM   17977 C  CD    . ARG A 1 3910 ? 217.830 156.350 239.793 1.00 23.50 ? 3910 ARG A CD    1 
ATOM   17978 N  NE    . ARG A 1 3910 ? 219.273 156.203 239.652 1.00 36.38 ? 3910 ARG A NE    1 
ATOM   17979 C  CZ    . ARG A 1 3910 ? 220.154 156.546 240.581 1.00 37.67 ? 3910 ARG A CZ    1 
ATOM   17980 N  NH1   . ARG A 1 3910 ? 219.773 157.071 241.735 1.00 28.79 ? 3910 ARG A NH1   1 
ATOM   17981 N  NH2   . ARG A 1 3910 ? 221.450 156.359 240.348 1.00 38.44 ? 3910 ARG A NH2   1 
ATOM   17982 N  N     . GLY A 1 3911 ? 216.402 152.003 237.625 1.00 23.19 ? 3911 GLY A N     1 
ATOM   17983 C  CA    . GLY A 1 3911 ? 216.240 150.567 237.484 1.00 22.47 ? 3911 GLY A CA    1 
ATOM   17984 C  C     . GLY A 1 3911 ? 217.121 149.939 236.425 1.00 23.75 ? 3911 GLY A C     1 
ATOM   17985 O  O     . GLY A 1 3911 ? 217.788 148.931 236.680 1.00 28.10 ? 3911 GLY A O     1 
ATOM   17986 N  N     . ASN A 1 3912 ? 217.123 150.520 235.226 1.00 26.39 ? 3912 ASN A N     1 
ATOM   17987 C  CA    . ASN A 1 3912 ? 217.980 150.043 234.149 1.00 26.32 ? 3912 ASN A CA    1 
ATOM   17988 C  C     . ASN A 1 3912 ? 219.460 150.257 234.435 1.00 30.39 ? 3912 ASN A C     1 
ATOM   17989 O  O     . ASN A 1 3912 ? 220.295 149.673 233.736 1.00 39.00 ? 3912 ASN A O     1 
ATOM   17990 C  CB    . ASN A 1 3912 ? 217.601 150.735 232.838 1.00 22.44 ? 3912 ASN A CB    1 
ATOM   17991 C  CG    . ASN A 1 3912 ? 217.536 152.245 232.974 1.00 35.31 ? 3912 ASN A CG    1 
ATOM   17992 O  OD1   . ASN A 1 3912 ? 217.784 152.797 234.047 1.00 37.44 ? 3912 ASN A OD1   1 
ATOM   17993 N  ND2   . ASN A 1 3912 ? 217.199 152.923 231.883 1.00 37.61 ? 3912 ASN A ND2   1 
ATOM   17994 N  N     . GLU A 1 3913 ? 219.800 151.070 235.437 1.00 23.90 ? 3913 GLU A N     1 
ATOM   17995 C  CA    . GLU A 1 3913 ? 221.199 151.333 235.751 1.00 28.83 ? 3913 GLU A CA    1 
ATOM   17996 C  C     . GLU A 1 3913 ? 221.908 150.111 236.319 1.00 34.17 ? 3913 GLU A C     1 
ATOM   17997 O  O     . GLU A 1 3913 ? 223.143 150.089 236.354 1.00 35.21 ? 3913 GLU A O     1 
ATOM   17998 C  CB    . GLU A 1 3913 ? 221.302 152.498 236.735 1.00 32.48 ? 3913 GLU A CB    1 
ATOM   17999 C  CG    . GLU A 1 3913 ? 220.708 153.794 236.217 1.00 29.44 ? 3913 GLU A CG    1 
ATOM   18000 C  CD    . GLU A 1 3913 ? 220.757 154.907 237.241 1.00 35.38 ? 3913 GLU A CD    1 
ATOM   18001 O  OE1   . GLU A 1 3913 ? 221.157 154.639 238.393 1.00 37.72 ? 3913 GLU A OE1   1 
ATOM   18002 O  OE2   . GLU A 1 3913 ? 220.394 156.050 236.895 1.00 36.99 ? 3913 GLU A OE2   1 
ATOM   18003 N  N     . ILE A 1 3914 ? 221.164 149.098 236.759 1.00 28.08 ? 3914 ILE A N     1 
ATOM   18004 C  CA    . ILE A 1 3914 ? 221.766 147.877 237.275 1.00 24.43 ? 3914 ILE A CA    1 
ATOM   18005 C  C     . ILE A 1 3914 ? 222.239 147.037 236.098 1.00 28.77 ? 3914 ILE A C     1 
ATOM   18006 O  O     . ILE A 1 3914 ? 221.459 146.288 235.499 1.00 27.68 ? 3914 ILE A O     1 
ATOM   18007 C  CB    . ILE A 1 3914 ? 220.778 147.094 238.161 1.00 26.21 ? 3914 ILE A CB    1 
ATOM   18008 C  CG1   . ILE A 1 3914 ? 220.191 148.007 239.239 1.00 20.17 ? 3914 ILE A CG1   1 
ATOM   18009 C  CG2   . ILE A 1 3914 ? 221.460 145.886 238.783 1.00 24.66 ? 3914 ILE A CG2   1 
ATOM   18010 C  CD1   . ILE A 1 3914 ? 219.229 147.312 240.175 1.00 17.14 ? 3914 ILE A CD1   1 
ATOM   18011 N  N     . VAL A 1 3915 ? 223.523 147.159 235.762 1.00 30.17 ? 3915 VAL A N     1 
ATOM   18012 C  CA    . VAL A 1 3915 ? 224.066 146.496 234.583 1.00 25.66 ? 3915 VAL A CA    1 
ATOM   18013 C  C     . VAL A 1 3915 ? 224.175 145.000 234.838 1.00 30.83 ? 3915 VAL A C     1 
ATOM   18014 O  O     . VAL A 1 3915 ? 224.697 144.566 235.875 1.00 27.74 ? 3915 VAL A O     1 
ATOM   18015 C  CB    . VAL A 1 3915 ? 225.426 147.101 234.208 1.00 32.28 ? 3915 VAL A CB    1 
ATOM   18016 C  CG1   . VAL A 1 3915 ? 226.014 146.386 233.001 1.00 28.07 ? 3915 VAL A CG1   1 
ATOM   18017 C  CG2   . VAL A 1 3915 ? 225.283 148.590 233.933 1.00 30.55 ? 3915 VAL A CG2   1 
ATOM   18018 N  N     . LEU A 1 3916 ? 223.682 144.205 233.894 1.00 27.50 ? 3916 LEU A N     1 
ATOM   18019 C  CA    . LEU A 1 3916 ? 223.703 142.753 233.988 1.00 28.77 ? 3916 LEU A CA    1 
ATOM   18020 C  C     . LEU A 1 3916 ? 224.630 142.186 232.923 1.00 34.60 ? 3916 LEU A C     1 
ATOM   18021 O  O     . LEU A 1 3916 ? 224.507 142.528 231.742 1.00 36.99 ? 3916 LEU A O     1 
ATOM   18022 C  CB    . LEU A 1 3916 ? 222.298 142.173 233.821 1.00 28.93 ? 3916 LEU A CB    1 
ATOM   18023 C  CG    . LEU A 1 3916 ? 221.213 142.729 234.741 1.00 29.68 ? 3916 LEU A CG    1 
ATOM   18024 C  CD1   . LEU A 1 3916 ? 219.898 142.006 234.496 1.00 27.15 ? 3916 LEU A CD1   1 
ATOM   18025 C  CD2   . LEU A 1 3916 ? 221.635 142.614 236.195 1.00 27.69 ? 3916 LEU A CD2   1 
ATOM   18026 N  N     . SER A 1 3917 ? 225.552 141.323 233.343 1.00 32.55 ? 3917 SER A N     1 
ATOM   18027 C  CA    . SER A 1 3917 ? 226.437 140.647 232.410 1.00 33.84 ? 3917 SER A CA    1 
ATOM   18028 C  C     . SER A 1 3917 ? 225.704 139.494 231.724 1.00 38.29 ? 3917 SER A C     1 
ATOM   18029 O  O     . SER A 1 3917 ? 224.567 139.156 232.060 1.00 37.87 ? 3917 SER A O     1 
ATOM   18030 C  CB    . SER A 1 3917 ? 227.684 140.137 233.129 1.00 34.97 ? 3917 SER A CB    1 
ATOM   18031 O  OG    . SER A 1 3917 ? 228.374 141.197 233.767 1.00 33.72 ? 3917 SER A OG    1 
ATOM   18032 N  N     . ALA A 1 3918 ? 226.376 138.894 230.739 1.00 35.18 ? 3918 ALA A N     1 
ATOM   18033 C  CA    . ALA A 1 3918 ? 225.778 137.777 230.012 1.00 31.72 ? 3918 ALA A CA    1 
ATOM   18034 C  C     . ALA A 1 3918 ? 225.524 136.590 230.933 1.00 31.16 ? 3918 ALA A C     1 
ATOM   18035 O  O     . ALA A 1 3918 ? 224.460 135.961 230.870 1.00 35.85 ? 3918 ALA A O     1 
ATOM   18036 C  CB    . ALA A 1 3918 ? 226.675 137.369 228.844 1.00 27.24 ? 3918 ALA A CB    1 
ATOM   18037 N  N     . GLY A 1 3919 ? 226.488 136.268 231.797 1.00 29.92 ? 3919 GLY A N     1 
ATOM   18038 C  CA    . GLY A 1 3919 ? 226.287 135.183 232.743 1.00 29.32 ? 3919 GLY A CA    1 
ATOM   18039 C  C     . GLY A 1 3919 ? 225.378 135.558 233.894 1.00 33.40 ? 3919 GLY A C     1 
ATOM   18040 O  O     . GLY A 1 3919 ? 224.814 134.679 234.555 1.00 33.87 ? 3919 GLY A O     1 
ATOM   18041 N  N     . SER A 1 3920 ? 225.224 136.858 234.156 1.00 33.65 ? 3920 SER A N     1 
ATOM   18042 C  CA    . SER A 1 3920 ? 224.356 137.297 235.244 1.00 33.65 ? 3920 SER A CA    1 
ATOM   18043 C  C     . SER A 1 3920 ? 222.895 136.986 234.947 1.00 33.41 ? 3920 SER A C     1 
ATOM   18044 O  O     . SER A 1 3920 ? 222.133 136.624 235.851 1.00 31.21 ? 3920 SER A O     1 
ATOM   18045 C  CB    . SER A 1 3920 ? 224.547 138.792 235.497 1.00 32.45 ? 3920 SER A CB    1 
ATOM   18046 O  OG    . SER A 1 3920 ? 225.908 139.101 235.735 1.00 36.94 ? 3920 SER A OG    1 
ATOM   18047 N  N     . THR A 1 3921 ? 222.482 137.122 233.686 1.00 30.86 ? 3921 THR A N     1 
ATOM   18048 C  CA    . THR A 1 3921 ? 221.098 136.885 233.313 1.00 29.52 ? 3921 THR A CA    1 
ATOM   18049 C  C     . THR A 1 3921 ? 220.963 135.493 232.721 1.00 28.40 ? 3921 THR A C     1 
ATOM   18050 O  O     . THR A 1 3921 ? 221.467 135.251 231.615 1.00 29.08 ? 3921 THR A O     1 
ATOM   18051 C  CB    . THR A 1 3921 ? 220.618 137.935 232.313 1.00 28.10 ? 3921 THR A CB    1 
ATOM   18052 O  OG1   . THR A 1 3921 ? 220.719 139.239 232.899 1.00 30.51 ? 3921 THR A OG1   1 
ATOM   18053 C  CG2   . THR A 1 3921 ? 219.172 137.674 231.919 1.00 26.28 ? 3921 THR A CG2   1 
ATOM   18054 N  N     . PRO A 1 3922 ? 220.305 134.558 233.396 1.00 25.91 ? 3922 PRO A N     1 
ATOM   18055 C  CA    . PRO A 1 3922 ? 220.092 133.225 232.833 1.00 27.24 ? 3922 PRO A CA    1 
ATOM   18056 C  C     . PRO A 1 3922 ? 218.885 133.232 231.902 1.00 33.11 ? 3922 PRO A C     1 
ATOM   18057 O  O     . PRO A 1 3922 ? 218.296 134.272 231.611 1.00 37.21 ? 3922 PRO A O     1 
ATOM   18058 C  CB    . PRO A 1 3922 ? 219.848 132.366 234.074 1.00 31.92 ? 3922 PRO A CB    1 
ATOM   18059 C  CG    . PRO A 1 3922 ? 219.179 133.300 235.024 1.00 29.65 ? 3922 PRO A CG    1 
ATOM   18060 C  CD    . PRO A 1 3922 ? 219.776 134.669 234.767 1.00 29.63 ? 3922 PRO A CD    1 
ATOM   18061 N  N     . ARG A 1 3923 ? 218.523 132.042 231.429 1.00 32.60 ? 3923 ARG A N     1 
ATOM   18062 C  CA    . ARG A 1 3923 ? 217.354 131.864 230.571 1.00 30.09 ? 3923 ARG A CA    1 
ATOM   18063 C  C     . ARG A 1 3923 ? 216.271 131.171 231.389 1.00 34.03 ? 3923 ARG A C     1 
ATOM   18064 O  O     . ARG A 1 3923 ? 216.308 129.953 231.585 1.00 35.02 ? 3923 ARG A O     1 
ATOM   18065 C  CB    . ARG A 1 3923 ? 217.708 131.064 229.320 1.00 32.40 ? 3923 ARG A CB    1 
ATOM   18066 C  CG    . ARG A 1 3923 ? 216.519 130.780 228.417 1.00 33.62 ? 3923 ARG A CG    1 
ATOM   18067 C  CD    . ARG A 1 3923 ? 216.887 129.833 227.289 1.00 31.12 ? 3923 ARG A CD    1 
ATOM   18068 N  NE    . ARG A 1 3923 ? 217.340 128.541 227.790 1.00 42.52 ? 3923 ARG A NE    1 
ATOM   18069 C  CZ    . ARG A 1 3923 ? 217.686 127.519 227.020 1.00 42.29 ? 3923 ARG A CZ    1 
ATOM   18070 N  NH1   . ARG A 1 3923 ? 217.641 127.601 225.701 1.00 36.12 ? 3923 ARG A NH1   1 
ATOM   18071 N  NH2   . ARG A 1 3923 ? 218.086 126.385 227.589 1.00 39.72 ? 3923 ARG A NH2   1 
ATOM   18072 N  N     . ILE A 1 3924 ? 215.306 131.947 231.868 1.00 33.73 ? 3924 ILE A N     1 
ATOM   18073 C  CA    . ILE A 1 3924 ? 214.161 131.406 232.592 1.00 30.12 ? 3924 ILE A CA    1 
ATOM   18074 C  C     . ILE A 1 3924 ? 213.115 130.980 231.572 1.00 29.87 ? 3924 ILE A C     1 
ATOM   18075 O  O     . ILE A 1 3924 ? 212.664 131.790 230.755 1.00 33.07 ? 3924 ILE A O     1 
ATOM   18076 C  CB    . ILE A 1 3924 ? 213.579 132.429 233.579 1.00 31.62 ? 3924 ILE A CB    1 
ATOM   18077 C  CG1   . ILE A 1 3924 ? 214.620 132.838 234.625 1.00 30.56 ? 3924 ILE A CG1   1 
ATOM   18078 C  CG2   . ILE A 1 3924 ? 212.339 131.861 234.255 1.00 29.66 ? 3924 ILE A CG2   1 
ATOM   18079 C  CD1   . ILE A 1 3924 ? 215.363 134.114 234.291 1.00 25.26 ? 3924 ILE A CD1   1 
ATOM   18080 N  N     . GLN A 1 3925 ? 212.732 129.704 231.612 1.00 32.11 ? 3925 GLN A N     1 
ATOM   18081 C  CA    . GLN A 1 3925 ? 211.706 129.210 230.708 1.00 28.79 ? 3925 GLN A CA    1 
ATOM   18082 C  C     . GLN A 1 3925 ? 210.364 129.851 231.038 1.00 28.99 ? 3925 GLN A C     1 
ATOM   18083 O  O     . GLN A 1 3925 ? 209.949 129.894 232.200 1.00 23.96 ? 3925 GLN A O     1 
ATOM   18084 C  CB    . GLN A 1 3925 ? 211.608 127.687 230.800 1.00 29.70 ? 3925 GLN A CB    1 
ATOM   18085 C  CG    . GLN A 1 3925 ? 210.557 127.075 229.890 1.00 27.88 ? 3925 GLN A CG    1 
ATOM   18086 C  CD    . GLN A 1 3925 ? 210.311 125.609 230.188 1.00 34.24 ? 3925 GLN A CD    1 
ATOM   18087 O  OE1   . GLN A 1 3925 ? 210.903 125.041 231.107 1.00 34.20 ? 3925 GLN A OE1   1 
ATOM   18088 N  NE2   . GLN A 1 3925 ? 209.437 124.984 229.408 1.00 36.88 ? 3925 GLN A NE2   1 
ATOM   18089 N  N     . GLY A 1 3926 ? 209.680 130.342 230.008 1.00 26.47 ? 3926 GLY A N     1 
ATOM   18090 C  CA    . GLY A 1 3926 ? 208.428 131.046 230.169 1.00 25.07 ? 3926 GLY A CA    1 
ATOM   18091 C  C     . GLY A 1 3926 ? 208.534 132.557 230.122 1.00 25.65 ? 3926 GLY A C     1 
ATOM   18092 O  O     . GLY A 1 3926 ? 207.500 133.233 230.170 1.00 25.80 ? 3926 GLY A O     1 
ATOM   18093 N  N     . LEU A 1 3927 ? 209.745 133.103 230.035 1.00 24.08 ? 3927 LEU A N     1 
ATOM   18094 C  CA    . LEU A 1 3927 ? 209.954 134.540 229.945 1.00 25.33 ? 3927 LEU A CA    1 
ATOM   18095 C  C     . LEU A 1 3927 ? 210.884 134.846 228.781 1.00 26.64 ? 3927 LEU A C     1 
ATOM   18096 O  O     . LEU A 1 3927 ? 211.665 134.000 228.342 1.00 29.26 ? 3927 LEU A O     1 
ATOM   18097 C  CB    . LEU A 1 3927 ? 210.541 135.116 231.239 1.00 22.02 ? 3927 LEU A CB    1 
ATOM   18098 C  CG    . LEU A 1 3927 ? 209.986 134.604 232.567 1.00 23.15 ? 3927 LEU A CG    1 
ATOM   18099 C  CD1   . LEU A 1 3927 ? 210.846 135.097 233.718 1.00 23.64 ? 3927 LEU A CD1   1 
ATOM   18100 C  CD2   . LEU A 1 3927 ? 208.547 135.044 232.750 1.00 21.30 ? 3927 LEU A CD2   1 
ATOM   18101 N  N     . THR A 1 3928 ? 210.789 136.074 228.282 1.00 20.48 ? 3928 THR A N     1 
ATOM   18102 C  CA    . THR A 1 3928 ? 211.640 136.528 227.197 1.00 22.01 ? 3928 THR A CA    1 
ATOM   18103 C  C     . THR A 1 3928 ? 212.957 137.049 227.770 1.00 22.44 ? 3928 THR A C     1 
ATOM   18104 O  O     . THR A 1 3928 ? 213.190 137.014 228.981 1.00 23.76 ? 3928 THR A O     1 
ATOM   18105 C  CB    . THR A 1 3928 ? 210.927 137.590 226.362 1.00 21.61 ? 3928 THR A CB    1 
ATOM   18106 O  OG1   . THR A 1 3928 ? 210.631 138.725 227.184 1.00 31.34 ? 3928 THR A OG1   1 
ATOM   18107 C  CG2   . THR A 1 3928 ? 209.635 137.034 225.794 1.00 21.81 ? 3928 THR A CG2   1 
ATOM   18108 N  N     . VAL A 1 3929 ? 213.837 137.536 226.894 1.00 25.65 ? 3929 VAL A N     1 
ATOM   18109 C  CA    . VAL A 1 3929 ? 215.129 138.045 227.339 1.00 21.59 ? 3929 VAL A CA    1 
ATOM   18110 C  C     . VAL A 1 3929 ? 214.946 139.289 228.201 1.00 26.74 ? 3929 VAL A C     1 
ATOM   18111 O  O     . VAL A 1 3929 ? 215.530 139.403 229.286 1.00 28.24 ? 3929 VAL A O     1 
ATOM   18112 C  CB    . VAL A 1 3929 ? 216.041 138.326 226.130 1.00 28.64 ? 3929 VAL A CB    1 
ATOM   18113 C  CG1   . VAL A 1 3929 ? 217.334 138.987 226.581 1.00 26.11 ? 3929 VAL A CG1   1 
ATOM   18114 C  CG2   . VAL A 1 3929 ? 216.329 137.039 225.374 1.00 22.75 ? 3929 VAL A CG2   1 
ATOM   18115 N  N     . GLU A 1 3930 ? 214.132 140.239 227.732 1.00 27.53 ? 3930 GLU A N     1 
ATOM   18116 C  CA    . GLU A 1 3930 ? 213.919 141.469 228.490 1.00 24.19 ? 3930 GLU A CA    1 
ATOM   18117 C  C     . GLU A 1 3930 ? 213.216 141.194 229.814 1.00 24.18 ? 3930 GLU A C     1 
ATOM   18118 O  O     . GLU A 1 3930 ? 213.544 141.812 230.833 1.00 24.09 ? 3930 GLU A O     1 
ATOM   18119 C  CB    . GLU A 1 3930 ? 213.131 142.479 227.653 1.00 20.20 ? 3930 GLU A CB    1 
ATOM   18120 C  CG    . GLU A 1 3930 ? 211.776 141.992 227.159 1.00 25.47 ? 3930 GLU A CG    1 
ATOM   18121 C  CD    . GLU A 1 3930 ? 211.865 141.270 225.828 1.00 30.86 ? 3930 GLU A CD    1 
ATOM   18122 O  OE1   . GLU A 1 3930 ? 212.996 141.018 225.362 1.00 31.41 ? 3930 GLU A OE1   1 
ATOM   18123 O  OE2   . GLU A 1 3930 ? 210.804 140.960 225.247 1.00 33.14 ? 3930 GLU A OE2   1 
ATOM   18124 N  N     . GLN A 1 3931 ? 212.248 140.274 229.821 1.00 19.42 ? 3931 GLN A N     1 
ATOM   18125 C  CA    . GLN A 1 3931 ? 211.580 139.920 231.070 1.00 22.30 ? 3931 GLN A CA    1 
ATOM   18126 C  C     . GLN A 1 3931 ? 212.554 139.286 232.051 1.00 25.98 ? 3931 GLN A C     1 
ATOM   18127 O  O     . GLN A 1 3931 ? 212.518 139.580 233.251 1.00 27.35 ? 3931 GLN A O     1 
ATOM   18128 C  CB    . GLN A 1 3931 ? 210.407 138.981 230.796 1.00 20.01 ? 3931 GLN A CB    1 
ATOM   18129 C  CG    . GLN A 1 3931 ? 209.155 139.674 230.289 1.00 19.53 ? 3931 GLN A CG    1 
ATOM   18130 C  CD    . GLN A 1 3931 ? 207.997 138.716 230.104 1.00 22.97 ? 3931 GLN A CD    1 
ATOM   18131 O  OE1   . GLN A 1 3931 ? 208.167 137.500 230.192 1.00 27.96 ? 3931 GLN A OE1   1 
ATOM   18132 N  NE2   . GLN A 1 3931 ? 206.812 139.259 229.860 1.00 19.60 ? 3931 GLN A NE2   1 
ATOM   18133 N  N     . ALA A 1 3932 ? 213.434 138.411 231.561 1.00 26.55 ? 3932 ALA A N     1 
ATOM   18134 C  CA    . ALA A 1 3932 ? 214.408 137.766 232.437 1.00 25.75 ? 3932 ALA A CA    1 
ATOM   18135 C  C     . ALA A 1 3932 ? 215.345 138.788 233.066 1.00 25.97 ? 3932 ALA A C     1 
ATOM   18136 O  O     . ALA A 1 3932 ? 215.669 138.694 234.255 1.00 27.58 ? 3932 ALA A O     1 
ATOM   18137 C  CB    . ALA A 1 3932 ? 215.200 136.716 231.658 1.00 30.37 ? 3932 ALA A CB    1 
ATOM   18138 N  N     . GLU A 1 3933 ? 215.793 139.773 232.283 1.00 23.14 ? 3933 GLU A N     1 
ATOM   18139 C  CA    . GLU A 1 3933 ? 216.650 140.819 232.833 1.00 23.47 ? 3933 GLU A CA    1 
ATOM   18140 C  C     . GLU A 1 3933 ? 215.921 141.618 233.906 1.00 23.64 ? 3933 GLU A C     1 
ATOM   18141 O  O     . GLU A 1 3933 ? 216.499 141.946 234.947 1.00 28.88 ? 3933 GLU A O     1 
ATOM   18142 C  CB    . GLU A 1 3933 ? 217.134 141.743 231.714 1.00 24.84 ? 3933 GLU A CB    1 
ATOM   18143 C  CG    . GLU A 1 3933 ? 217.984 141.051 230.664 1.00 23.95 ? 3933 GLU A CG    1 
ATOM   18144 C  CD    . GLU A 1 3933 ? 219.112 141.928 230.158 1.00 34.01 ? 3933 GLU A CD    1 
ATOM   18145 O  OE1   . GLU A 1 3933 ? 219.770 142.589 230.987 1.00 39.33 ? 3933 GLU A OE1   1 
ATOM   18146 O  OE2   . GLU A 1 3933 ? 219.340 141.957 228.931 1.00 33.35 ? 3933 GLU A OE2   1 
ATOM   18147 N  N     . ALA A 1 3934 ? 214.647 141.938 233.670 1.00 24.58 ? 3934 ALA A N     1 
ATOM   18148 C  CA    . ALA A 1 3934 ? 213.865 142.643 234.676 1.00 24.44 ? 3934 ALA A CA    1 
ATOM   18149 C  C     . ALA A 1 3934 ? 213.708 141.811 235.940 1.00 25.61 ? 3934 ALA A C     1 
ATOM   18150 O  O     . ALA A 1 3934 ? 213.602 142.365 237.040 1.00 24.27 ? 3934 ALA A O     1 
ATOM   18151 C  CB    . ALA A 1 3934 ? 212.498 143.020 234.108 1.00 19.43 ? 3934 ALA A CB    1 
ATOM   18152 N  N     . VAL A 1 3935 ? 213.682 140.484 235.807 1.00 22.20 ? 3935 VAL A N     1 
ATOM   18153 C  CA    . VAL A 1 3935 ? 213.662 139.616 236.980 1.00 20.49 ? 3935 VAL A CA    1 
ATOM   18154 C  C     . VAL A 1 3935 ? 214.978 139.719 237.739 1.00 27.65 ? 3935 VAL A C     1 
ATOM   18155 O  O     . VAL A 1 3935 ? 214.997 139.841 238.970 1.00 26.41 ? 3935 VAL A O     1 
ATOM   18156 C  CB    . VAL A 1 3935 ? 213.361 138.165 236.566 1.00 21.11 ? 3935 VAL A CB    1 
ATOM   18157 C  CG1   . VAL A 1 3935 ? 213.531 137.230 237.743 1.00 21.38 ? 3935 VAL A CG1   1 
ATOM   18158 C  CG2   . VAL A 1 3935 ? 211.961 138.057 236.005 1.00 23.33 ? 3935 VAL A CG2   1 
ATOM   18159 N  N     . VAL A 1 3936 ? 216.099 139.671 237.016 1.00 25.71 ? 3936 VAL A N     1 
ATOM   18160 C  CA    . VAL A 1 3936 ? 217.405 139.701 237.666 1.00 24.70 ? 3936 VAL A CA    1 
ATOM   18161 C  C     . VAL A 1 3936 ? 217.621 141.032 238.375 1.00 28.51 ? 3936 VAL A C     1 
ATOM   18162 O  O     . VAL A 1 3936 ? 218.118 141.074 239.506 1.00 30.20 ? 3936 VAL A O     1 
ATOM   18163 C  CB    . VAL A 1 3936 ? 218.518 139.414 236.642 1.00 27.45 ? 3936 VAL A CB    1 
ATOM   18164 C  CG1   . VAL A 1 3936 ? 219.886 139.491 237.306 1.00 25.24 ? 3936 VAL A CG1   1 
ATOM   18165 C  CG2   . VAL A 1 3936 ? 218.311 138.052 236.004 1.00 23.37 ? 3936 VAL A CG2   1 
ATOM   18166 N  N     . ARG A 1 3937 ? 217.260 142.140 237.722 1.00 28.41 ? 3937 ARG A N     1 
ATOM   18167 C  CA    . ARG A 1 3937 ? 217.406 143.445 238.361 1.00 21.58 ? 3937 ARG A CA    1 
ATOM   18168 C  C     . ARG A 1 3937 ? 216.499 143.563 239.580 1.00 22.87 ? 3937 ARG A C     1 
ATOM   18169 O  O     . ARG A 1 3937 ? 216.920 144.067 240.628 1.00 31.71 ? 3937 ARG A O     1 
ATOM   18170 C  CB    . ARG A 1 3937 ? 217.118 144.559 237.358 1.00 21.47 ? 3937 ARG A CB    1 
ATOM   18171 C  CG    . ARG A 1 3937 ? 218.093 144.595 236.198 1.00 22.27 ? 3937 ARG A CG    1 
ATOM   18172 C  CD    . ARG A 1 3937 ? 217.789 145.719 235.228 1.00 22.29 ? 3937 ARG A CD    1 
ATOM   18173 N  NE    . ARG A 1 3937 ? 218.331 145.440 233.903 1.00 25.08 ? 3937 ARG A NE    1 
ATOM   18174 C  CZ    . ARG A 1 3937 ? 219.292 146.144 233.322 1.00 27.06 ? 3937 ARG A CZ    1 
ATOM   18175 N  NH1   . ARG A 1 3937 ? 219.856 147.177 233.926 1.00 28.71 ? 3937 ARG A NH1   1 
ATOM   18176 N  NH2   . ARG A 1 3937 ? 219.699 145.802 232.104 1.00 28.62 ? 3937 ARG A NH2   1 
ATOM   18177 N  N     . LEU A 1 3938 ? 215.254 143.097 239.466 1.00 23.01 ? 3938 LEU A N     1 
ATOM   18178 C  CA    . LEU A 1 3938 ? 214.348 143.122 240.607 1.00 19.52 ? 3938 LEU A CA    1 
ATOM   18179 C  C     . LEU A 1 3938 ? 214.803 142.184 241.718 1.00 22.12 ? 3938 LEU A C     1 
ATOM   18180 O  O     . LEU A 1 3938 ? 214.409 142.373 242.873 1.00 23.65 ? 3938 LEU A O     1 
ATOM   18181 C  CB    . LEU A 1 3938 ? 212.928 142.765 240.160 1.00 15.64 ? 3938 LEU A CB    1 
ATOM   18182 C  CG    . LEU A 1 3938 ? 211.799 142.890 241.188 1.00 18.73 ? 3938 LEU A CG    1 
ATOM   18183 C  CD1   . LEU A 1 3938 ? 211.625 144.332 241.635 1.00 19.45 ? 3938 LEU A CD1   1 
ATOM   18184 C  CD2   . LEU A 1 3938 ? 210.498 142.344 240.631 1.00 17.86 ? 3938 LEU A CD2   1 
ATOM   18185 N  N     . SER A 1 3939 ? 215.635 141.193 241.397 1.00 24.52 ? 3939 SER A N     1 
ATOM   18186 C  CA    . SER A 1 3939 ? 216.139 140.266 242.402 1.00 23.20 ? 3939 SER A CA    1 
ATOM   18187 C  C     . SER A 1 3939 ? 217.053 140.935 243.419 1.00 26.18 ? 3939 SER A C     1 
ATOM   18188 O  O     . SER A 1 3939 ? 217.306 140.347 244.476 1.00 27.70 ? 3939 SER A O     1 
ATOM   18189 C  CB    . SER A 1 3939 ? 216.879 139.113 241.726 1.00 23.41 ? 3939 SER A CB    1 
ATOM   18190 O  OG    . SER A 1 3939 ? 218.150 139.534 241.265 1.00 34.46 ? 3939 SER A OG    1 
ATOM   18191 N  N     . CYS A 1 3940 ? 217.549 142.141 243.132 1.00 23.50 ? 3940 CYS A N     1 
ATOM   18192 C  CA    . CYS A 1 3940 ? 218.426 142.836 244.064 1.00 20.75 ? 3940 CYS A CA    1 
ATOM   18193 C  C     . CYS A 1 3940 ? 217.697 143.277 245.327 1.00 27.75 ? 3940 CYS A C     1 
ATOM   18194 O  O     . CYS A 1 3940 ? 218.348 143.537 246.345 1.00 30.84 ? 3940 CYS A O     1 
ATOM   18195 C  CB    . CYS A 1 3940 ? 219.065 144.045 243.377 1.00 20.70 ? 3940 CYS A CB    1 
ATOM   18196 S  SG    . CYS A 1 3940 ? 220.410 144.820 244.304 1.00 64.87 ? 3940 CYS A SG    1 
ATOM   18197 N  N     . LEU A 1 3941 ? 216.371 143.380 245.285 1.00 23.19 ? 3941 LEU A N     1 
ATOM   18198 C  CA    . LEU A 1 3941 ? 215.722 143.720 246.544 1.00 22.47 ? 3941 LEU A CA    1 
ATOM   18199 C  C     . LEU A 1 3941 ? 215.639 142.489 247.443 1.00 23.60 ? 3941 LEU A C     1 
ATOM   18200 O  O     . LEU A 1 3941 ? 215.504 141.367 246.947 1.00 30.53 ? 3941 LEU A O     1 
ATOM   18201 C  CB    . LEU A 1 3941 ? 214.319 144.268 246.306 1.00 28.56 ? 3941 LEU A CB    1 
ATOM   18202 C  CG    . LEU A 1 3941 ? 214.178 145.573 245.522 1.00 24.28 ? 3941 LEU A CG    1 
ATOM   18203 C  CD1   . LEU A 1 3941 ? 212.832 146.210 245.819 1.00 17.23 ? 3941 LEU A CD1   1 
ATOM   18204 C  CD2   . LEU A 1 3941 ? 215.312 146.534 245.841 1.00 27.19 ? 3941 LEU A CD2   1 
ATOM   18205 N  N     . PRO A 1 3942 ? 215.730 142.684 248.761 1.00 24.61 ? 3942 PRO A N     1 
ATOM   18206 C  CA    . PRO A 1 3942 ? 215.562 141.542 249.674 1.00 21.09 ? 3942 PRO A CA    1 
ATOM   18207 C  C     . PRO A 1 3942 ? 214.218 140.849 249.533 1.00 21.45 ? 3942 PRO A C     1 
ATOM   18208 O  O     . PRO A 1 3942 ? 214.137 139.625 249.698 1.00 25.80 ? 3942 PRO A O     1 
ATOM   18209 C  CB    . PRO A 1 3942 ? 215.735 142.185 251.055 1.00 21.01 ? 3942 PRO A CB    1 
ATOM   18210 C  CG    . PRO A 1 3942 ? 216.629 143.350 250.802 1.00 20.97 ? 3942 PRO A CG    1 
ATOM   18211 C  CD    . PRO A 1 3942 ? 216.208 143.887 249.461 1.00 23.96 ? 3942 PRO A CD    1 
ATOM   18212 N  N     . ALA A 1 3943 ? 213.156 141.598 249.233 1.00 20.64 ? 3943 ALA A N     1 
ATOM   18213 C  CA    . ALA A 1 3943 ? 211.840 140.984 249.085 1.00 25.80 ? 3943 ALA A CA    1 
ATOM   18214 C  C     . ALA A 1 3943 ? 211.765 140.098 247.848 1.00 23.62 ? 3943 ALA A C     1 
ATOM   18215 O  O     . ALA A 1 3943 ? 211.049 139.090 247.851 1.00 26.56 ? 3943 ALA A O     1 
ATOM   18216 C  CB    . ALA A 1 3943 ? 210.756 142.060 249.034 1.00 19.80 ? 3943 ALA A CB    1 
ATOM   18217 N  N     . PHE A 1 3944 ? 212.489 140.452 246.787 1.00 19.48 ? 3944 PHE A N     1 
ATOM   18218 C  CA    . PHE A 1 3944 ? 212.493 139.679 245.553 1.00 24.79 ? 3944 PHE A CA    1 
ATOM   18219 C  C     . PHE A 1 3944 ? 213.790 138.902 245.356 1.00 27.36 ? 3944 PHE A C     1 
ATOM   18220 O  O     . PHE A 1 3944 ? 214.162 138.614 244.216 1.00 27.33 ? 3944 PHE A O     1 
ATOM   18221 C  CB    . PHE A 1 3944 ? 212.239 140.591 244.350 1.00 24.26 ? 3944 PHE A CB    1 
ATOM   18222 C  CG    . PHE A 1 3944 ? 210.911 141.293 244.384 1.00 22.16 ? 3944 PHE A CG    1 
ATOM   18223 C  CD1   . PHE A 1 3944 ? 209.754 140.630 244.017 1.00 21.12 ? 3944 PHE A CD1   1 
ATOM   18224 C  CD2   . PHE A 1 3944 ? 210.822 142.619 244.773 1.00 20.77 ? 3944 PHE A CD2   1 
ATOM   18225 C  CE1   . PHE A 1 3944 ? 208.533 141.272 244.041 1.00 22.73 ? 3944 PHE A CE1   1 
ATOM   18226 C  CE2   . PHE A 1 3944 ? 209.603 143.266 244.800 1.00 21.83 ? 3944 PHE A CE2   1 
ATOM   18227 C  CZ    . PHE A 1 3944 ? 208.457 142.592 244.435 1.00 21.78 ? 3944 PHE A CZ    1 
ATOM   18228 N  N     . LYS A 1 3945 ? 214.494 138.562 246.440 1.00 25.92 ? 3945 LYS A N     1 
ATOM   18229 C  CA    . LYS A 1 3945 ? 215.727 137.796 246.294 1.00 24.84 ? 3945 LYS A CA    1 
ATOM   18230 C  C     . LYS A 1 3945 ? 215.449 136.410 245.722 1.00 26.19 ? 3945 LYS A C     1 
ATOM   18231 O  O     . LYS A 1 3945 ? 216.197 135.923 244.867 1.00 23.33 ? 3945 LYS A O     1 
ATOM   18232 C  CB    . LYS A 1 3945 ? 216.464 137.706 247.635 1.00 26.87 ? 3945 LYS A CB    1 
ATOM   18233 C  CG    . LYS A 1 3945 ? 215.770 136.890 248.720 1.00 27.24 ? 3945 LYS A CG    1 
ATOM   18234 C  CD    . LYS A 1 3945 ? 216.579 136.891 250.007 1.00 25.52 ? 3945 LYS A CD    1 
ATOM   18235 C  CE    . LYS A 1 3945 ? 215.876 136.114 251.110 1.00 29.77 ? 3945 LYS A CE    1 
ATOM   18236 N  NZ    . LYS A 1 3945 ? 215.794 134.660 250.806 1.00 34.26 ? 3945 LYS A NZ    1 
ATOM   18237 N  N     . ASP A 1 3946 ? 214.375 135.764 246.173 1.00 24.22 ? 3946 ASP A N     1 
ATOM   18238 C  CA    . ASP A 1 3946 ? 213.960 134.468 245.635 1.00 22.40 ? 3946 ASP A CA    1 
ATOM   18239 C  C     . ASP A 1 3946 ? 212.892 134.644 244.551 1.00 26.95 ? 3946 ASP A C     1 
ATOM   18240 O  O     . ASP A 1 3946 ? 211.819 134.040 244.573 1.00 25.98 ? 3946 ASP A O     1 
ATOM   18241 C  CB    . ASP A 1 3946 ? 213.485 133.560 246.768 1.00 22.69 ? 3946 ASP A CB    1 
ATOM   18242 C  CG    . ASP A 1 3946 ? 212.268 134.104 247.498 1.00 37.13 ? 3946 ASP A CG    1 
ATOM   18243 O  OD1   . ASP A 1 3946 ? 211.798 135.214 247.164 1.00 37.34 ? 3946 ASP A OD1   1 
ATOM   18244 O  OD2   . ASP A 1 3946 ? 211.775 133.415 248.415 1.00 35.38 ? 3946 ASP A OD2   1 
ATOM   18245 N  N     . LEU A 1 3947 ? 213.220 135.484 243.570 1.00 29.23 ? 3947 LEU A N     1 
ATOM   18246 C  CA    . LEU A 1 3947 ? 212.292 135.817 242.496 1.00 23.40 ? 3947 LEU A CA    1 
ATOM   18247 C  C     . LEU A 1 3947 ? 212.288 134.769 241.387 1.00 26.14 ? 3947 LEU A C     1 
ATOM   18248 O  O     . LEU A 1 3947 ? 211.219 134.348 240.936 1.00 27.59 ? 3947 LEU A O     1 
ATOM   18249 C  CB    . LEU A 1 3947 ? 212.638 137.194 241.920 1.00 21.96 ? 3947 LEU A CB    1 
ATOM   18250 C  CG    . LEU A 1 3947 ? 211.697 137.799 240.876 1.00 25.55 ? 3947 LEU A CG    1 
ATOM   18251 C  CD1   . LEU A 1 3947 ? 210.300 137.935 241.428 1.00 18.51 ? 3947 LEU A CD1   1 
ATOM   18252 C  CD2   . LEU A 1 3947 ? 212.218 139.152 240.436 1.00 23.82 ? 3947 LEU A CD2   1 
ATOM   18253 N  N     . ILE A 1 3948 ? 213.473 134.345 240.936 1.00 22.23 ? 3948 ILE A N     1 
ATOM   18254 C  CA    . ILE A 1 3948 ? 213.554 133.361 239.860 1.00 23.33 ? 3948 ILE A CA    1 
ATOM   18255 C  C     . ILE A 1 3948 ? 212.917 132.046 240.291 1.00 25.49 ? 3948 ILE A C     1 
ATOM   18256 O  O     . ILE A 1 3948 ? 212.189 131.408 239.521 1.00 25.75 ? 3948 ILE A O     1 
ATOM   18257 C  CB    . ILE A 1 3948 ? 215.019 133.163 239.425 1.00 25.29 ? 3948 ILE A CB    1 
ATOM   18258 C  CG1   . ILE A 1 3948 ? 215.537 134.408 238.706 1.00 20.06 ? 3948 ILE A CG1   1 
ATOM   18259 C  CG2   . ILE A 1 3948 ? 215.160 131.935 238.536 1.00 26.37 ? 3948 ILE A CG2   1 
ATOM   18260 C  CD1   . ILE A 1 3948 ? 216.962 134.288 238.232 1.00 25.80 ? 3948 ILE A CD1   1 
ATOM   18261 N  N     . ALA A 1 3949 ? 213.184 131.622 241.528 1.00 24.30 ? 3949 ALA A N     1 
ATOM   18262 C  CA    . ALA A 1 3949 ? 212.605 130.381 242.028 1.00 23.27 ? 3949 ALA A CA    1 
ATOM   18263 C  C     . ALA A 1 3949 ? 211.089 130.471 242.129 1.00 27.55 ? 3949 ALA A C     1 
ATOM   18264 O  O     . ALA A 1 3949 ? 210.379 129.527 241.766 1.00 31.13 ? 3949 ALA A O     1 
ATOM   18265 C  CB    . ALA A 1 3949 ? 213.214 130.028 243.385 1.00 19.38 ? 3949 ALA A CB    1 
ATOM   18266 N  N     . LYS A 1 3950 ? 210.572 131.599 242.625 1.00 27.81 ? 3950 LYS A N     1 
ATOM   18267 C  CA    . LYS A 1 3950 ? 209.132 131.729 242.820 1.00 25.34 ? 3950 LYS A CA    1 
ATOM   18268 C  C     . LYS A 1 3950 ? 208.382 131.657 241.494 1.00 27.32 ? 3950 LYS A C     1 
ATOM   18269 O  O     . LYS A 1 3950 ? 207.306 131.055 241.413 1.00 27.35 ? 3950 LYS A O     1 
ATOM   18270 C  CB    . LYS A 1 3950 ? 208.811 133.030 243.553 1.00 26.75 ? 3950 LYS A CB    1 
ATOM   18271 C  CG    . LYS A 1 3950 ? 208.527 132.843 245.034 1.00 23.15 ? 3950 LYS A CG    1 
ATOM   18272 C  CD    . LYS A 1 3950 ? 208.550 134.168 245.778 1.00 23.67 ? 3950 LYS A CD    1 
ATOM   18273 C  CE    . LYS A 1 3950 ? 208.289 133.971 247.259 1.00 27.97 ? 3950 LYS A CE    1 
ATOM   18274 N  NZ    . LYS A 1 3950 ? 209.262 133.024 247.873 1.00 30.79 ? 3950 LYS A NZ    1 
ATOM   18275 N  N     . VAL A 1 3951 ? 208.929 132.280 240.448 1.00 25.92 ? 3951 VAL A N     1 
ATOM   18276 C  CA    . VAL A 1 3951 ? 208.332 132.154 239.121 1.00 23.41 ? 3951 VAL A CA    1 
ATOM   18277 C  C     . VAL A 1 3951 ? 208.423 130.717 238.626 1.00 27.49 ? 3951 VAL A C     1 
ATOM   18278 O  O     . VAL A 1 3951 ? 207.446 130.162 238.107 1.00 36.05 ? 3951 VAL A O     1 
ATOM   18279 C  CB    . VAL A 1 3951 ? 208.999 133.132 238.139 1.00 21.90 ? 3951 VAL A CB    1 
ATOM   18280 C  CG1   . VAL A 1 3951 ? 208.460 132.918 236.738 1.00 21.91 ? 3951 VAL A CG1   1 
ATOM   18281 C  CG2   . VAL A 1 3951 ? 208.766 134.564 238.582 1.00 24.86 ? 3951 VAL A CG2   1 
ATOM   18282 N  N     . GLN A 1 3952 ? 209.591 130.089 238.780 1.00 26.47 ? 3952 GLN A N     1 
ATOM   18283 C  CA    . GLN A 1 3952 ? 209.752 128.711 238.329 1.00 28.00 ? 3952 GLN A CA    1 
ATOM   18284 C  C     . GLN A 1 3952 ? 208.859 127.761 239.119 1.00 26.88 ? 3952 GLN A C     1 
ATOM   18285 O  O     . GLN A 1 3952 ? 208.286 126.825 238.552 1.00 31.03 ? 3952 GLN A O     1 
ATOM   18286 C  CB    . GLN A 1 3952 ? 211.219 128.292 238.434 1.00 25.16 ? 3952 GLN A CB    1 
ATOM   18287 C  CG    . GLN A 1 3952 ? 212.074 128.755 237.267 1.00 27.06 ? 3952 GLN A CG    1 
ATOM   18288 C  CD    . GLN A 1 3952 ? 213.557 128.691 237.566 1.00 31.51 ? 3952 GLN A CD    1 
ATOM   18289 O  OE1   . GLN A 1 3952 ? 213.964 128.435 238.699 1.00 32.18 ? 3952 GLN A OE1   1 
ATOM   18290 N  NE2   . GLN A 1 3952 ? 214.377 128.920 236.547 1.00 27.67 ? 3952 GLN A NE2   1 
ATOM   18291 N  N     . ALA A 1 3953 ? 208.724 127.990 240.427 1.00 25.45 ? 3953 ALA A N     1 
ATOM   18292 C  CA    . ALA A 1 3953 ? 207.850 127.153 241.239 1.00 28.51 ? 3953 ALA A CA    1 
ATOM   18293 C  C     . ALA A 1 3953 ? 206.377 127.349 240.905 1.00 30.18 ? 3953 ALA A C     1 
ATOM   18294 O  O     . ALA A 1 3953 ? 205.553 126.514 241.287 1.00 35.10 ? 3953 ALA A O     1 
ATOM   18295 C  CB    . ALA A 1 3953 ? 208.087 127.427 242.724 1.00 25.32 ? 3953 ALA A CB    1 
ATOM   18296 N  N     . ASP A 1 3954 ? 206.028 128.428 240.207 1.00 30.40 ? 3954 ASP A N     1 
ATOM   18297 C  CA    . ASP A 1 3954 ? 204.641 128.735 239.865 1.00 30.17 ? 3954 ASP A CA    1 
ATOM   18298 C  C     . ASP A 1 3954 ? 204.437 128.487 238.374 1.00 30.79 ? 3954 ASP A C     1 
ATOM   18299 O  O     . ASP A 1 3954 ? 204.808 129.315 237.538 1.00 33.61 ? 3954 ASP A O     1 
ATOM   18300 C  CB    . ASP A 1 3954 ? 204.300 130.174 240.239 1.00 29.16 ? 3954 ASP A CB    1 
ATOM   18301 C  CG    . ASP A 1 3954 ? 202.822 130.480 240.097 1.00 31.54 ? 3954 ASP A CG    1 
ATOM   18302 O  OD1   . ASP A 1 3954 ? 202.037 129.536 239.874 1.00 30.23 ? 3954 ASP A OD1   1 
ATOM   18303 O  OD2   . ASP A 1 3954 ? 202.448 131.666 240.202 1.00 36.44 ? 3954 ASP A OD2   1 
ATOM   18304 N  N     . GLU A 1 3955 ? 203.836 127.343 238.039 1.00 30.17 ? 3955 GLU A N     1 
ATOM   18305 C  CA    . GLU A 1 3955 ? 203.485 127.074 236.650 1.00 32.50 ? 3955 GLU A CA    1 
ATOM   18306 C  C     . GLU A 1 3955 ? 202.278 127.886 236.199 1.00 35.34 ? 3955 GLU A C     1 
ATOM   18307 O  O     . GLU A 1 3955 ? 202.112 128.105 234.995 1.00 33.95 ? 3955 GLU A O     1 
ATOM   18308 C  CB    . GLU A 1 3955 ? 203.219 125.580 236.444 1.00 29.47 ? 3955 GLU A CB    1 
ATOM   18309 C  CG    . GLU A 1 3955 ? 202.221 124.967 237.418 1.00 29.37 ? 3955 GLU A CG    1 
ATOM   18310 C  CD    . GLU A 1 3955 ? 202.850 124.578 238.742 1.00 37.69 ? 3955 GLU A CD    1 
ATOM   18311 O  OE1   . GLU A 1 3955 ? 204.077 124.762 238.898 1.00 35.51 ? 3955 GLU A OE1   1 
ATOM   18312 O  OE2   . GLU A 1 3955 ? 202.119 124.087 239.627 1.00 34.58 ? 3955 GLU A OE2   1 
ATOM   18313 N  N     . GLN A 1 3956 ? 201.437 128.333 237.134 1.00 29.95 ? 3956 GLN A N     1 
ATOM   18314 C  CA    . GLN A 1 3956 ? 200.337 129.228 236.800 1.00 28.43 ? 3956 GLN A CA    1 
ATOM   18315 C  C     . GLN A 1 3956 ? 200.814 130.630 236.448 1.00 27.22 ? 3956 GLN A C     1 
ATOM   18316 O  O     . GLN A 1 3956 ? 200.010 131.438 235.970 1.00 24.81 ? 3956 GLN A O     1 
ATOM   18317 C  CB    . GLN A 1 3956 ? 199.334 129.305 237.955 1.00 25.39 ? 3956 GLN A CB    1 
ATOM   18318 C  CG    . GLN A 1 3956 ? 198.484 128.055 238.169 1.00 29.80 ? 3956 GLN A CG    1 
ATOM   18319 C  CD    . GLN A 1 3956 ? 199.289 126.848 238.611 1.00 34.71 ? 3956 GLN A CD    1 
ATOM   18320 O  OE1   . GLN A 1 3956 ? 200.105 126.934 239.529 1.00 33.90 ? 3956 GLN A OE1   1 
ATOM   18321 N  NE2   . GLN A 1 3956 ? 199.057 125.713 237.964 1.00 36.41 ? 3956 GLN A NE2   1 
ATOM   18322 N  N     . PHE A 1 3957 ? 202.092 130.937 236.682 1.00 25.41 ? 3957 PHE A N     1 
ATOM   18323 C  CA    . PHE A 1 3957 ? 202.625 132.245 236.320 1.00 25.27 ? 3957 PHE A CA    1 
ATOM   18324 C  C     . PHE A 1 3957 ? 202.542 132.490 234.819 1.00 23.49 ? 3957 PHE A C     1 
ATOM   18325 O  O     . PHE A 1 3957 ? 202.416 133.642 234.386 1.00 27.94 ? 3957 PHE A O     1 
ATOM   18326 C  CB    . PHE A 1 3957 ? 204.070 132.369 236.804 1.00 20.15 ? 3957 PHE A CB    1 
ATOM   18327 C  CG    . PHE A 1 3957 ? 204.615 133.762 236.737 1.00 21.30 ? 3957 PHE A CG    1 
ATOM   18328 C  CD1   . PHE A 1 3957 ? 204.403 134.651 237.776 1.00 22.57 ? 3957 PHE A CD1   1 
ATOM   18329 C  CD2   . PHE A 1 3957 ? 205.349 134.183 235.641 1.00 13.88 ? 3957 PHE A CD2   1 
ATOM   18330 C  CE1   . PHE A 1 3957 ? 204.906 135.931 237.721 1.00 21.31 ? 3957 PHE A CE1   1 
ATOM   18331 C  CE2   . PHE A 1 3957 ? 205.855 135.462 235.582 1.00 16.68 ? 3957 PHE A CE2   1 
ATOM   18332 C  CZ    . PHE A 1 3957 ? 205.632 136.338 236.624 1.00 16.35 ? 3957 PHE A CZ    1 
ATOM   18333 N  N     . GLY A 1 3958 ? 202.607 131.429 234.014 1.00 21.11 ? 3958 GLY A N     1 
ATOM   18334 C  CA    . GLY A 1 3958 ? 202.471 131.594 232.577 1.00 15.61 ? 3958 GLY A CA    1 
ATOM   18335 C  C     . GLY A 1 3958 ? 201.099 132.096 232.174 1.00 23.18 ? 3958 GLY A C     1 
ATOM   18336 O  O     . GLY A 1 3958 ? 200.972 132.910 231.254 1.00 24.38 ? 3958 GLY A O     1 
ATOM   18337 N  N     . ILE A 1 3959 ? 200.053 131.615 232.848 1.00 23.05 ? 3959 ILE A N     1 
ATOM   18338 C  CA    . ILE A 1 3959 ? 198.699 132.073 232.546 1.00 17.80 ? 3959 ILE A CA    1 
ATOM   18339 C  C     . ILE A 1 3959 ? 198.529 133.539 232.926 1.00 23.77 ? 3959 ILE A C     1 
ATOM   18340 O  O     . ILE A 1 3959 ? 197.981 134.334 232.154 1.00 32.10 ? 3959 ILE A O     1 
ATOM   18341 C  CB    . ILE A 1 3959 ? 197.666 131.179 233.254 1.00 19.84 ? 3959 ILE A CB    1 
ATOM   18342 C  CG1   . ILE A 1 3959 ? 197.788 129.735 232.766 1.00 25.80 ? 3959 ILE A CG1   1 
ATOM   18343 C  CG2   . ILE A 1 3959 ? 196.260 131.704 233.027 1.00 16.62 ? 3959 ILE A CG2   1 
ATOM   18344 C  CD1   . ILE A 1 3959 ? 197.642 129.583 231.268 1.00 21.22 ? 3959 ILE A CD1   1 
ATOM   18345 N  N     . TRP A 1 3960 ? 198.994 133.922 234.119 1.00 24.48 ? 3960 TRP A N     1 
ATOM   18346 C  CA    . TRP A 1 3960 ? 198.885 135.312 234.544 1.00 15.57 ? 3960 TRP A CA    1 
ATOM   18347 C  C     . TRP A 1 3960 ? 199.716 136.235 233.663 1.00 15.90 ? 3960 TRP A C     1 
ATOM   18348 O  O     . TRP A 1 3960 ? 199.324 137.383 233.426 1.00 22.45 ? 3960 TRP A O     1 
ATOM   18349 C  CB    . TRP A 1 3960 ? 199.311 135.455 236.006 1.00 18.79 ? 3960 TRP A CB    1 
ATOM   18350 C  CG    . TRP A 1 3960 ? 199.445 136.881 236.460 1.00 18.26 ? 3960 TRP A CG    1 
ATOM   18351 C  CD1   . TRP A 1 3960 ? 198.458 137.681 236.949 1.00 15.81 ? 3960 TRP A CD1   1 
ATOM   18352 C  CD2   . TRP A 1 3960 ? 200.640 137.673 236.463 1.00 15.87 ? 3960 TRP A CD2   1 
ATOM   18353 N  NE1   . TRP A 1 3960 ? 198.960 138.920 237.257 1.00 15.92 ? 3960 TRP A NE1   1 
ATOM   18354 C  CE2   . TRP A 1 3960 ? 200.298 138.941 236.965 1.00 14.43 ? 3960 TRP A CE2   1 
ATOM   18355 C  CE3   . TRP A 1 3960 ? 201.964 137.432 236.088 1.00 12.91 ? 3960 TRP A CE3   1 
ATOM   18356 C  CZ2   . TRP A 1 3960 ? 201.230 139.966 237.105 1.00 16.69 ? 3960 TRP A CZ2   1 
ATOM   18357 C  CZ3   . TRP A 1 3960 ? 202.887 138.449 236.227 1.00 13.40 ? 3960 TRP A CZ3   1 
ATOM   18358 C  CH2   . TRP A 1 3960 ? 202.518 139.701 236.731 1.00 18.59 ? 3960 TRP A CH2   1 
ATOM   18359 N  N     . LEU A 1 3961 ? 200.856 135.752 233.170 1.00 20.19 ? 3961 LEU A N     1 
ATOM   18360 C  CA    . LEU A 1 3961 ? 201.728 136.579 232.345 1.00 18.58 ? 3961 LEU A CA    1 
ATOM   18361 C  C     . LEU A 1 3961 ? 201.077 136.977 231.027 1.00 20.65 ? 3961 LEU A C     1 
ATOM   18362 O  O     . LEU A 1 3961 ? 201.443 138.011 230.455 1.00 23.34 ? 3961 LEU A O     1 
ATOM   18363 C  CB    . LEU A 1 3961 ? 203.043 135.843 232.081 1.00 16.25 ? 3961 LEU A CB    1 
ATOM   18364 C  CG    . LEU A 1 3961 ? 204.175 136.657 231.455 1.00 20.94 ? 3961 LEU A CG    1 
ATOM   18365 C  CD1   . LEU A 1 3961 ? 204.609 137.759 232.397 1.00 17.61 ? 3961 LEU A CD1   1 
ATOM   18366 C  CD2   . LEU A 1 3961 ? 205.350 135.762 231.097 1.00 20.01 ? 3961 LEU A CD2   1 
ATOM   18367 N  N     . ASP A 1 3962 ? 200.125 136.191 230.531 1.00 20.09 ? 3962 ASP A N     1 
ATOM   18368 C  CA    . ASP A 1 3962 ? 199.477 136.459 229.252 1.00 20.77 ? 3962 ASP A CA    1 
ATOM   18369 C  C     . ASP A 1 3962 ? 197.992 136.759 229.421 1.00 23.78 ? 3962 ASP A C     1 
ATOM   18370 O  O     . ASP A 1 3962 ? 197.186 136.454 228.542 1.00 28.83 ? 3962 ASP A O     1 
ATOM   18371 C  CB    . ASP A 1 3962 ? 199.686 135.290 228.291 1.00 21.19 ? 3962 ASP A CB    1 
ATOM   18372 C  CG    . ASP A 1 3962 ? 201.150 134.966 228.084 1.00 25.03 ? 3962 ASP A CG    1 
ATOM   18373 O  OD1   . ASP A 1 3962 ? 201.894 135.852 227.617 1.00 26.71 ? 3962 ASP A OD1   1 
ATOM   18374 O  OD2   . ASP A 1 3962 ? 201.557 133.826 228.390 1.00 28.21 ? 3962 ASP A OD2   1 
ATOM   18375 N  N     . SER A 1 3963 ? 197.616 137.356 230.547 1.00 25.58 ? 3963 SER A N     1 
ATOM   18376 C  CA    . SER A 1 3963 ? 196.243 137.761 230.797 1.00 19.43 ? 3963 SER A CA    1 
ATOM   18377 C  C     . SER A 1 3963 ? 196.033 139.210 230.376 1.00 19.51 ? 3963 SER A C     1 
ATOM   18378 O  O     . SER A 1 3963 ? 196.978 140.001 230.280 1.00 23.34 ? 3963 SER A O     1 
ATOM   18379 C  CB    . SER A 1 3963 ? 195.884 137.581 232.274 1.00 18.90 ? 3963 SER A CB    1 
ATOM   18380 O  OG    . SER A 1 3963 ? 196.708 138.378 233.104 1.00 23.22 ? 3963 SER A OG    1 
ATOM   18381 N  N     . SER A 1 3964 ? 194.770 139.549 230.113 1.00 20.36 ? 3964 SER A N     1 
ATOM   18382 C  CA    . SER A 1 3964 ? 194.439 140.890 229.643 1.00 14.40 ? 3964 SER A CA    1 
ATOM   18383 C  C     . SER A 1 3964 ? 194.714 141.942 230.711 1.00 18.76 ? 3964 SER A C     1 
ATOM   18384 O  O     . SER A 1 3964 ? 195.184 143.042 230.401 1.00 18.24 ? 3964 SER A O     1 
ATOM   18385 C  CB    . SER A 1 3964 ? 192.978 140.945 229.202 1.00 12.31 ? 3964 SER A CB    1 
ATOM   18386 O  OG    . SER A 1 3964 ? 192.111 140.681 230.289 1.00 15.68 ? 3964 SER A OG    1 
ATOM   18387 N  N     . SER A 1 3965 ? 194.423 141.627 231.970 1.00 18.93 ? 3965 SER A N     1 
ATOM   18388 C  CA    . SER A 1 3965 ? 194.565 142.570 233.079 1.00 14.70 ? 3965 SER A CA    1 
ATOM   18389 C  C     . SER A 1 3965 ? 195.372 141.918 234.193 1.00 16.16 ? 3965 SER A C     1 
ATOM   18390 O  O     . SER A 1 3965 ? 194.842 141.611 235.266 1.00 22.34 ? 3965 SER A O     1 
ATOM   18391 C  CB    . SER A 1 3965 ? 193.195 143.020 233.585 1.00 17.89 ? 3965 SER A CB    1 
ATOM   18392 O  OG    . SER A 1 3965 ? 192.430 143.597 232.542 1.00 18.18 ? 3965 SER A OG    1 
ATOM   18393 N  N     . PRO A 1 3966 ? 196.673 141.701 233.974 1.00 11.93 ? 3966 PRO A N     1 
ATOM   18394 C  CA    . PRO A 1 3966 ? 197.495 141.071 235.016 1.00 13.66 ? 3966 PRO A CA    1 
ATOM   18395 C  C     . PRO A 1 3966 ? 197.664 141.927 236.258 1.00 16.84 ? 3966 PRO A C     1 
ATOM   18396 O  O     . PRO A 1 3966 ? 198.067 141.399 237.301 1.00 22.87 ? 3966 PRO A O     1 
ATOM   18397 C  CB    . PRO A 1 3966 ? 198.836 140.841 234.308 1.00 13.80 ? 3966 PRO A CB    1 
ATOM   18398 C  CG    . PRO A 1 3966 ? 198.892 141.922 233.296 1.00 11.09 ? 3966 PRO A CG    1 
ATOM   18399 C  CD    . PRO A 1 3966 ? 197.481 142.093 232.805 1.00 13.27 ? 3966 PRO A CD    1 
ATOM   18400 N  N     . GLU A 1 3967 ? 197.377 143.228 236.181 1.00 13.38 ? 3967 GLU A N     1 
ATOM   18401 C  CA    . GLU A 1 3967 ? 197.578 144.120 237.317 1.00 12.48 ? 3967 GLU A CA    1 
ATOM   18402 C  C     . GLU A 1 3967 ? 196.536 143.924 238.409 1.00 15.49 ? 3967 GLU A C     1 
ATOM   18403 O  O     . GLU A 1 3967 ? 196.763 144.351 239.546 1.00 23.01 ? 3967 GLU A O     1 
ATOM   18404 C  CB    . GLU A 1 3967 ? 197.565 145.576 236.853 1.00 9.43  ? 3967 GLU A CB    1 
ATOM   18405 C  CG    . GLU A 1 3967 ? 196.203 146.061 236.388 1.00 13.05 ? 3967 GLU A CG    1 
ATOM   18406 C  CD    . GLU A 1 3967 ? 195.903 145.677 234.952 1.00 13.76 ? 3967 GLU A CD    1 
ATOM   18407 O  OE1   . GLU A 1 3967 ? 196.824 145.202 234.258 1.00 14.28 ? 3967 GLU A OE1   1 
ATOM   18408 O  OE2   . GLU A 1 3967 ? 194.744 145.839 234.520 1.00 18.57 ? 3967 GLU A OE2   1 
ATOM   18409 N  N     . GLN A 1 3968 ? 195.401 143.304 238.096 1.00 14.57 ? 3968 GLN A N     1 
ATOM   18410 C  CA    . GLN A 1 3968 ? 194.351 143.095 239.081 1.00 14.76 ? 3968 GLN A CA    1 
ATOM   18411 C  C     . GLN A 1 3968 ? 194.478 141.774 239.825 1.00 18.28 ? 3968 GLN A C     1 
ATOM   18412 O  O     . GLN A 1 3968 ? 193.766 141.570 240.816 1.00 21.39 ? 3968 GLN A O     1 
ATOM   18413 C  CB    . GLN A 1 3968 ? 192.976 143.169 238.411 1.00 16.61 ? 3968 GLN A CB    1 
ATOM   18414 C  CG    . GLN A 1 3968 ? 192.699 144.484 237.705 1.00 16.95 ? 3968 GLN A CG    1 
ATOM   18415 C  CD    . GLN A 1 3968 ? 191.363 144.487 236.993 1.00 25.67 ? 3968 GLN A CD    1 
ATOM   18416 O  OE1   . GLN A 1 3968 ? 190.628 143.502 237.027 1.00 30.82 ? 3968 GLN A OE1   1 
ATOM   18417 N  NE2   . GLN A 1 3968 ? 191.041 145.598 236.342 1.00 23.51 ? 3968 GLN A NE2   1 
ATOM   18418 N  N     . THR A 1 3969 ? 195.351 140.878 239.378 1.00 18.53 ? 3969 THR A N     1 
ATOM   18419 C  CA    . THR A 1 3969 ? 195.544 139.569 239.994 1.00 15.74 ? 3969 THR A CA    1 
ATOM   18420 C  C     . THR A 1 3969 ? 197.026 139.246 240.108 1.00 18.12 ? 3969 THR A C     1 
ATOM   18421 O  O     . THR A 1 3969 ? 197.451 138.116 239.859 1.00 22.62 ? 3969 THR A O     1 
ATOM   18422 C  CB    . THR A 1 3969 ? 194.826 138.475 239.209 1.00 22.23 ? 3969 THR A CB    1 
ATOM   18423 O  OG1   . THR A 1 3969 ? 195.305 138.459 237.860 1.00 22.64 ? 3969 THR A OG1   1 
ATOM   18424 C  CG2   . THR A 1 3969 ? 193.316 138.696 239.214 1.00 18.44 ? 3969 THR A CG2   1 
ATOM   18425 N  N     . VAL A 1 3970 ? 197.823 140.272 240.422 1.00 22.70 ? 3970 VAL A N     1 
ATOM   18426 C  CA    . VAL A 1 3970 ? 199.303 140.088 240.520 1.00 17.78 ? 3970 VAL A CA    1 
ATOM   18427 C  C     . VAL A 1 3970 ? 199.589 139.044 241.608 1.00 20.23 ? 3970 VAL A C     1 
ATOM   18428 O  O     . VAL A 1 3970 ? 199.187 139.271 242.769 1.00 24.70 ? 3970 VAL A O     1 
ATOM   18429 C  CB    . VAL A 1 3970 ? 200.030 141.414 240.815 1.00 15.47 ? 3970 VAL A CB    1 
ATOM   18430 C  CG1   . VAL A 1 3970 ? 201.541 141.226 240.883 1.00 18.46 ? 3970 VAL A CG1   1 
ATOM   18431 C  CG2   . VAL A 1 3970 ? 199.670 142.498 239.808 1.00 12.54 ? 3970 VAL A CG2   1 
ATOM   18432 N  N     . PRO A 1 3971 ? 200.261 137.920 241.283 1.00 25.62 ? 3971 PRO A N     1 
ATOM   18433 C  CA    . PRO A 1 3971 ? 200.500 136.875 242.266 1.00 23.62 ? 3971 PRO A CA    1 
ATOM   18434 C  C     . PRO A 1 3971 ? 201.376 137.369 243.404 1.00 25.30 ? 3971 PRO A C     1 
ATOM   18435 O  O     . PRO A 1 3971 ? 202.263 138.213 243.163 1.00 30.73 ? 3971 PRO A O     1 
ATOM   18436 C  CB    . PRO A 1 3971 ? 201.189 135.777 241.439 1.00 19.09 ? 3971 PRO A CB    1 
ATOM   18437 C  CG    . PRO A 1 3971 ? 201.807 136.523 240.279 1.00 19.43 ? 3971 PRO A CG    1 
ATOM   18438 C  CD    . PRO A 1 3971 ? 200.814 137.630 239.971 1.00 17.37 ? 3971 PRO A CD    1 
ATOM   18439 N  N     . TYR A 1 3972 ? 201.144 136.857 244.615 1.00 23.44 ? 3972 TYR A N     1 
ATOM   18440 C  CA    . TYR A 1 3972 ? 202.005 137.223 245.771 1.00 23.21 ? 3972 TYR A CA    1 
ATOM   18441 C  C     . TYR A 1 3972 ? 203.355 136.553 245.559 1.00 26.33 ? 3972 TYR A C     1 
ATOM   18442 O  O     . TYR A 1 3972 ? 203.623 135.509 246.192 1.00 34.57 ? 3972 TYR A O     1 
ATOM   18443 C  CB    . TYR A 1 3972 ? 201.308 136.781 247.061 1.00 24.46 ? 3972 TYR A CB    1 
ATOM   18444 C  CG    . TYR A 1 3972 ? 202.070 137.088 248.342 1.00 26.69 ? 3972 TYR A CG    1 
ATOM   18445 C  CD1   . TYR A 1 3972 ? 202.886 138.209 248.443 1.00 25.45 ? 3972 TYR A CD1   1 
ATOM   18446 C  CD2   . TYR A 1 3972 ? 201.977 136.251 249.446 1.00 26.33 ? 3972 TYR A CD2   1 
ATOM   18447 C  CE1   . TYR A 1 3972 ? 203.579 138.490 249.609 1.00 25.52 ? 3972 TYR A CE1   1 
ATOM   18448 C  CE2   . TYR A 1 3972 ? 202.666 136.521 250.615 1.00 27.34 ? 3972 TYR A CE2   1 
ATOM   18449 C  CZ    . TYR A 1 3972 ? 203.470 137.643 250.696 1.00 26.76 ? 3972 TYR A CZ    1 
ATOM   18450 O  OH    . TYR A 1 3972 ? 204.150 137.907 251.848 1.00 32.46 ? 3972 TYR A OH    1 
ATOM   18451 N  N     . LEU A 1 3973 ? 204.186 137.130 244.689 1.00 25.13 ? 3973 LEU A N     1 
ATOM   18452 C  CA    . LEU A 1 3973 ? 205.486 136.499 244.340 1.00 21.68 ? 3973 LEU A CA    1 
ATOM   18453 C  C     . LEU A 1 3973 ? 206.642 137.218 245.055 1.00 24.62 ? 3973 LEU A C     1 
ATOM   18454 O  O     . LEU A 1 3973 ? 207.787 137.124 244.560 1.00 26.30 ? 3973 LEU A O     1 
ATOM   18455 C  CB    . LEU A 1 3973 ? 205.617 136.579 242.823 1.00 20.01 ? 3973 LEU A CB    1 
ATOM   18456 C  CG    . LEU A 1 3973 ? 206.563 135.572 242.163 1.00 24.80 ? 3973 LEU A CG    1 
ATOM   18457 C  CD1   . LEU A 1 3973 ? 205.941 134.188 242.154 1.00 22.14 ? 3973 LEU A CD1   1 
ATOM   18458 C  CD2   . LEU A 1 3973 ? 206.870 136.032 240.751 1.00 24.20 ? 3973 LEU A CD2   1 
ATOM   18459 N  N     . TRP A 1 3974 ? 206.360 137.909 246.164 1.00 22.83 ? 3974 TRP A N     1 
ATOM   18460 C  CA    . TRP A 1 3974 ? 207.442 138.572 246.940 1.00 21.87 ? 3974 TRP A CA    1 
ATOM   18461 C  C     . TRP A 1 3974 ? 207.471 138.035 248.373 1.00 25.59 ? 3974 TRP A C     1 
ATOM   18462 O  O     . TRP A 1 3974 ? 206.388 137.818 248.958 1.00 27.53 ? 3974 TRP A O     1 
ATOM   18463 C  CB    . TRP A 1 3974 ? 207.281 140.099 246.918 1.00 21.98 ? 3974 TRP A CB    1 
ATOM   18464 C  CG    . TRP A 1 3974 ? 206.042 140.607 247.603 1.00 21.19 ? 3974 TRP A CG    1 
ATOM   18465 C  CD1   . TRP A 1 3974 ? 205.915 140.964 248.915 1.00 20.98 ? 3974 TRP A CD1   1 
ATOM   18466 C  CD2   . TRP A 1 3974 ? 204.749 140.830 247.000 1.00 21.39 ? 3974 TRP A CD2   1 
ATOM   18467 N  NE1   . TRP A 1 3974 ? 204.638 141.388 249.171 1.00 23.47 ? 3974 TRP A NE1   1 
ATOM   18468 C  CE2   . TRP A 1 3974 ? 203.900 141.317 248.017 1.00 23.78 ? 3974 TRP A CE2   1 
ATOM   18469 C  CE3   . TRP A 1 3974 ? 204.231 140.665 245.712 1.00 20.21 ? 3974 TRP A CE3   1 
ATOM   18470 C  CZ2   . TRP A 1 3974 ? 202.566 141.638 247.779 1.00 21.47 ? 3974 TRP A CZ2   1 
ATOM   18471 C  CZ3   . TRP A 1 3974 ? 202.911 140.982 245.478 1.00 21.55 ? 3974 TRP A CZ3   1 
ATOM   18472 C  CH2   . TRP A 1 3974 ? 202.093 141.463 246.500 1.00 19.88 ? 3974 TRP A CH2   1 
ATOM   18473 N  N     . SER A 1 3975 ? 208.673 137.828 248.919 1.00 23.87 ? 3975 SER A N     1 
ATOM   18474 C  CA    . SER A 1 3975 ? 208.813 137.311 250.306 1.00 28.16 ? 3975 SER A CA    1 
ATOM   18475 C  C     . SER A 1 3975 ? 208.828 138.479 251.301 1.00 28.01 ? 3975 SER A C     1 
ATOM   18476 O  O     . SER A 1 3975 ? 209.193 139.601 250.886 1.00 27.13 ? 3975 SER A O     1 
ATOM   18477 C  CB    . SER A 1 3975 ? 210.052 136.464 250.442 1.00 29.88 ? 3975 SER A CB    1 
ATOM   18478 O  OG    . SER A 1 3975 ? 211.209 137.200 250.071 1.00 30.03 ? 3975 SER A OG    1 
ATOM   18479 N  N     . GLU A 1 3976 ? 208.449 138.222 252.558 1.00 29.52 ? 3976 GLU A N     1 
ATOM   18480 C  CA    . GLU A 1 3976 ? 208.455 139.281 253.603 1.00 28.56 ? 3976 GLU A CA    1 
ATOM   18481 C  C     . GLU A 1 3976 ? 208.341 138.630 254.991 1.00 34.16 ? 3976 GLU A C     1 
ATOM   18482 O  O     . GLU A 1 3976 ? 207.975 137.436 255.054 1.00 26.83 ? 3976 GLU A O     1 
ATOM   18483 C  CB    . GLU A 1 3976 ? 207.317 140.272 253.369 1.00 27.29 ? 3976 GLU A CB    1 
ATOM   18484 C  CG    . GLU A 1 3976 ? 205.934 139.640 253.498 1.00 24.24 ? 3976 GLU A CG    1 
ATOM   18485 C  CD    . GLU A 1 3976 ? 204.794 140.572 253.129 1.00 30.90 ? 3976 GLU A CD    1 
ATOM   18486 O  OE1   . GLU A 1 3976 ? 204.779 141.052 251.976 1.00 33.13 ? 3976 GLU A OE1   1 
ATOM   18487 O  OE2   . GLU A 1 3976 ? 203.922 140.810 253.988 1.00 30.05 ? 3976 GLU A OE2   1 
ATOM   18488 N  N     . GLU A 1 3977 ? 208.640 139.383 256.054 1.00 33.07 ? 3977 GLU A N     1 
ATOM   18489 C  CA    . GLU A 1 3977 ? 208.572 138.848 257.412 1.00 32.49 ? 3977 GLU A CA    1 
ATOM   18490 C  C     . GLU A 1 3977 ? 207.231 139.162 258.069 1.00 31.38 ? 3977 GLU A C     1 
ATOM   18491 O  O     . GLU A 1 3977 ? 206.485 138.250 258.441 1.00 35.92 ? 3977 GLU A O     1 
ATOM   18492 C  CB    . GLU A 1 3977 ? 209.726 139.402 258.255 1.00 32.39 ? 3977 GLU A CB    1 
ATOM   18493 C  CG    . GLU A 1 3977 ? 211.109 138.955 257.803 1.00 33.83 ? 3977 GLU A CG    1 
ATOM   18494 C  CD    . GLU A 1 3977 ? 211.644 139.775 256.643 1.00 41.07 ? 3977 GLU A CD    1 
ATOM   18495 O  OE1   . GLU A 1 3977 ? 210.956 140.730 256.220 1.00 35.48 ? 3977 GLU A OE1   1 
ATOM   18496 O  OE2   . GLU A 1 3977 ? 212.751 139.466 256.155 1.00 41.16 ? 3977 GLU A OE2   1 
ATOM   18497 N  N     . THR A 1 3978 ? 206.917 140.432 258.215 1.00 33.42 ? 3978 THR A N     1 
ATOM   18498 C  CA    . THR A 1 3978 ? 205.639 140.860 258.763 1.00 32.32 ? 3978 THR A CA    1 
ATOM   18499 C  C     . THR A 1 3978 ? 204.629 141.066 257.637 1.00 31.08 ? 3978 THR A C     1 
ATOM   18500 O  O     . THR A 1 3978 ? 205.012 141.372 256.504 1.00 29.07 ? 3978 THR A O     1 
ATOM   18501 C  CB    . THR A 1 3978 ? 205.807 142.158 259.552 1.00 35.03 ? 3978 THR A CB    1 
ATOM   18502 O  OG1   . THR A 1 3978 ? 204.529 142.630 259.994 1.00 36.32 ? 3978 THR A OG1   1 
ATOM   18503 C  CG2   . THR A 1 3978 ? 206.469 143.227 258.693 1.00 28.02 ? 3978 THR A CG2   1 
ATOM   18504 N  N     . PRO A 1 3979 ? 203.339 140.874 257.910 1.00 32.34 ? 3979 PRO A N     1 
ATOM   18505 C  CA    . PRO A 1 3979 ? 202.326 141.139 256.877 1.00 29.52 ? 3979 PRO A CA    1 
ATOM   18506 C  C     . PRO A 1 3979 ? 202.424 142.570 256.370 1.00 28.90 ? 3979 PRO A C     1 
ATOM   18507 O  O     . PRO A 1 3979 ? 202.541 143.518 257.148 1.00 31.39 ? 3979 PRO A O     1 
ATOM   18508 C  CB    . PRO A 1 3979 ? 201.006 140.885 257.609 1.00 29.04 ? 3979 PRO A CB    1 
ATOM   18509 C  CG    . PRO A 1 3979 ? 201.355 139.879 258.647 1.00 29.58 ? 3979 PRO A CG    1 
ATOM   18510 C  CD    . PRO A 1 3979 ? 202.759 140.208 259.089 1.00 31.77 ? 3979 PRO A CD    1 
ATOM   18511 N  N     . ALA A 1 3980 ? 202.370 142.718 255.049 1.00 29.17 ? 3980 ALA A N     1 
ATOM   18512 C  CA    . ALA A 1 3980 ? 202.552 144.016 254.425 1.00 25.53 ? 3980 ALA A CA    1 
ATOM   18513 C  C     . ALA A 1 3980 ? 201.275 144.844 254.513 1.00 23.00 ? 3980 ALA A C     1 
ATOM   18514 O  O     . ALA A 1 3980 ? 200.188 144.343 254.823 1.00 25.29 ? 3980 ALA A O     1 
ATOM   18515 C  CB    . ALA A 1 3980 ? 202.983 143.856 252.968 1.00 22.32 ? 3980 ALA A CB    1 
ATOM   18516 N  N     . THR A 1 3981 ? 201.416 146.123 254.240 1.00 18.58 ? 3981 THR A N     1 
ATOM   18517 C  CA    . THR A 1 3981 ? 200.317 147.072 254.228 1.00 17.58 ? 3981 THR A CA    1 
ATOM   18518 C  C     . THR A 1 3981 ? 199.688 147.138 252.838 1.00 16.29 ? 3981 THR A C     1 
ATOM   18519 O  O     . THR A 1 3981 ? 200.342 146.815 251.842 1.00 18.03 ? 3981 THR A O     1 
ATOM   18520 C  CB    . THR A 1 3981 ? 200.807 148.457 254.640 1.00 17.89 ? 3981 THR A CB    1 
ATOM   18521 O  OG1   . THR A 1 3981 ? 201.783 148.923 253.701 1.00 20.51 ? 3981 THR A OG1   1 
ATOM   18522 C  CG2   . THR A 1 3981 ? 201.436 148.397 256.020 1.00 14.65 ? 3981 THR A CG2   1 
ATOM   18523 N  N     . PRO A 1 3982 ? 198.416 147.544 252.742 1.00 17.23 ? 3982 PRO A N     1 
ATOM   18524 C  CA    . PRO A 1 3982 ? 197.794 147.663 251.410 1.00 13.78 ? 3982 PRO A CA    1 
ATOM   18525 C  C     . PRO A 1 3982 ? 198.555 148.581 250.471 1.00 13.67 ? 3982 PRO A C     1 
ATOM   18526 O  O     . PRO A 1 3982 ? 198.639 148.299 249.270 1.00 15.16 ? 3982 PRO A O     1 
ATOM   18527 C  CB    . PRO A 1 3982 ? 196.395 148.203 251.730 1.00 13.27 ? 3982 PRO A CB    1 
ATOM   18528 C  CG    . PRO A 1 3982 ? 196.138 147.770 253.129 1.00 8.38  ? 3982 PRO A CG    1 
ATOM   18529 C  CD    . PRO A 1 3982 ? 197.464 147.852 253.821 1.00 17.34 ? 3982 PRO A CD    1 
ATOM   18530 N  N     . ILE A 1 3983 ? 199.118 149.674 250.985 1.00 13.79 ? 3983 ILE A N     1 
ATOM   18531 C  CA    . ILE A 1 3983 ? 199.976 150.521 250.164 1.00 14.08 ? 3983 ILE A CA    1 
ATOM   18532 C  C     . ILE A 1 3983 ? 201.275 149.794 249.834 1.00 13.02 ? 3983 ILE A C     1 
ATOM   18533 O  O     . ILE A 1 3983 ? 201.782 149.870 248.710 1.00 13.39 ? 3983 ILE A O     1 
ATOM   18534 C  CB    . ILE A 1 3983 ? 200.236 151.865 250.868 1.00 12.88 ? 3983 ILE A CB    1 
ATOM   18535 C  CG1   . ILE A 1 3983 ? 198.921 152.625 251.049 1.00 8.68  ? 3983 ILE A CG1   1 
ATOM   18536 C  CG2   . ILE A 1 3983 ? 201.222 152.699 250.077 1.00 9.29  ? 3983 ILE A CG2   1 
ATOM   18537 C  CD1   . ILE A 1 3983 ? 199.027 153.825 251.957 1.00 17.19 ? 3983 ILE A CD1   1 
ATOM   18538 N  N     . GLY A 1 3984 ? 201.831 149.074 250.812 1.00 14.70 ? 3984 GLY A N     1 
ATOM   18539 C  CA    . GLY A 1 3984 ? 203.039 148.311 250.563 1.00 11.61 ? 3984 GLY A CA    1 
ATOM   18540 C  C     . GLY A 1 3984 ? 202.840 147.181 249.572 1.00 16.57 ? 3984 GLY A C     1 
ATOM   18541 O  O     . GLY A 1 3984 ? 203.742 146.870 248.789 1.00 11.66 ? 3984 GLY A O     1 
ATOM   18542 N  N     . GLN A 1 3985 ? 201.668 146.542 249.599 1.00 15.33 ? 3985 GLN A N     1 
ATOM   18543 C  CA    . GLN A 1 3985 ? 201.373 145.496 248.625 1.00 15.24 ? 3985 GLN A CA    1 
ATOM   18544 C  C     . GLN A 1 3985 ? 201.263 146.066 247.217 1.00 14.05 ? 3985 GLN A C     1 
ATOM   18545 O  O     . GLN A 1 3985 ? 201.694 145.431 246.247 1.00 16.95 ? 3985 GLN A O     1 
ATOM   18546 C  CB    . GLN A 1 3985 ? 200.086 144.766 249.005 1.00 14.52 ? 3985 GLN A CB    1 
ATOM   18547 C  CG    . GLN A 1 3985 ? 200.166 143.959 250.282 1.00 20.34 ? 3985 GLN A CG    1 
ATOM   18548 C  CD    . GLN A 1 3985 ? 198.853 143.277 250.611 1.00 27.54 ? 3985 GLN A CD    1 
ATOM   18549 O  OE1   . GLN A 1 3985 ? 197.854 143.461 249.916 1.00 22.89 ? 3985 GLN A OE1   1 
ATOM   18550 N  NE2   . GLN A 1 3985 ? 198.848 142.487 251.678 1.00 30.69 ? 3985 GLN A NE2   1 
ATOM   18551 N  N     . ALA A 1 3986 ? 200.677 147.257 247.085 1.00 15.82 ? 3986 ALA A N     1 
ATOM   18552 C  CA    . ALA A 1 3986 ? 200.554 147.885 245.773 1.00 9.91  ? 3986 ALA A CA    1 
ATOM   18553 C  C     . ALA A 1 3986 ? 201.922 148.196 245.179 1.00 9.45  ? 3986 ALA A C     1 
ATOM   18554 O  O     . ALA A 1 3986 ? 202.129 148.035 243.970 1.00 12.94 ? 3986 ALA A O     1 
ATOM   18555 C  CB    . ALA A 1 3986 ? 199.712 149.156 245.879 1.00 6.12  ? 3986 ALA A CB    1 
ATOM   18556 N  N     . ILE A 1 3987 ? 202.864 148.645 246.009 1.00 8.42  ? 3987 ILE A N     1 
ATOM   18557 C  CA    . ILE A 1 3987 ? 204.199 148.969 245.516 1.00 11.44 ? 3987 ILE A CA    1 
ATOM   18558 C  C     . ILE A 1 3987 ? 204.904 147.711 245.024 1.00 13.20 ? 3987 ILE A C     1 
ATOM   18559 O  O     . ILE A 1 3987 ? 205.612 147.737 244.009 1.00 11.73 ? 3987 ILE A O     1 
ATOM   18560 C  CB    . ILE A 1 3987 ? 205.008 149.686 246.610 1.00 13.05 ? 3987 ILE A CB    1 
ATOM   18561 C  CG1   . ILE A 1 3987 ? 204.340 151.010 246.962 1.00 11.93 ? 3987 ILE A CG1   1 
ATOM   18562 C  CG2   . ILE A 1 3987 ? 206.424 149.955 246.137 1.00 12.05 ? 3987 ILE A CG2   1 
ATOM   18563 C  CD1   . ILE A 1 3987 ? 204.899 151.660 248.183 1.00 14.14 ? 3987 ILE A CD1   1 
ATOM   18564 N  N     . HIS A 1 3988 ? 204.734 146.596 245.736 1.00 15.24 ? 3988 HIS A N     1 
ATOM   18565 C  CA    . HIS A 1 3988 ? 205.302 145.332 245.279 1.00 12.92 ? 3988 HIS A CA    1 
ATOM   18566 C  C     . HIS A 1 3988 ? 204.668 144.883 243.970 1.00 14.08 ? 3988 HIS A C     1 
ATOM   18567 O  O     . HIS A 1 3988 ? 205.365 144.409 243.066 1.00 18.60 ? 3988 HIS A O     1 
ATOM   18568 C  CB    . HIS A 1 3988 ? 205.137 144.263 246.359 1.00 13.43 ? 3988 HIS A CB    1 
ATOM   18569 C  CG    . HIS A 1 3988 ? 206.033 144.460 247.542 1.00 16.70 ? 3988 HIS A CG    1 
ATOM   18570 N  ND1   . HIS A 1 3988 ? 205.638 144.172 248.830 1.00 22.16 ? 3988 HIS A ND1   1 
ATOM   18571 C  CD2   . HIS A 1 3988 ? 207.304 144.914 247.631 1.00 16.92 ? 3988 HIS A CD2   1 
ATOM   18572 C  CE1   . HIS A 1 3988 ? 206.627 144.443 249.663 1.00 17.27 ? 3988 HIS A CE1   1 
ATOM   18573 N  NE2   . HIS A 1 3988 ? 207.650 144.895 248.959 1.00 18.78 ? 3988 HIS A NE2   1 
ATOM   18574 N  N     . ARG A 1 3989 ? 203.344 145.017 243.850 1.00 14.36 ? 3989 ARG A N     1 
ATOM   18575 C  CA    . ARG A 1 3989 ? 202.697 144.724 242.575 1.00 11.82 ? 3989 ARG A CA    1 
ATOM   18576 C  C     . ARG A 1 3989 ? 203.169 145.672 241.481 1.00 8.11  ? 3989 ARG A C     1 
ATOM   18577 O  O     . ARG A 1 3989 ? 203.270 145.271 240.318 1.00 13.91 ? 3989 ARG A O     1 
ATOM   18578 C  CB    . ARG A 1 3989 ? 201.176 144.801 242.705 1.00 8.04  ? 3989 ARG A CB    1 
ATOM   18579 C  CG    . ARG A 1 3989 ? 200.551 143.718 243.565 1.00 8.83  ? 3989 ARG A CG    1 
ATOM   18580 C  CD    . ARG A 1 3989 ? 199.044 143.889 243.616 1.00 10.89 ? 3989 ARG A CD    1 
ATOM   18581 N  NE    . ARG A 1 3989 ? 198.389 142.855 244.407 1.00 18.15 ? 3989 ARG A NE    1 
ATOM   18582 C  CZ    . ARG A 1 3989 ? 198.135 142.945 245.705 1.00 18.96 ? 3989 ARG A CZ    1 
ATOM   18583 N  NH1   . ARG A 1 3989 ? 198.425 144.037 246.390 1.00 25.03 ? 3989 ARG A NH1   1 
ATOM   18584 N  NH2   . ARG A 1 3989 ? 197.558 141.920 246.326 1.00 24.21 ? 3989 ARG A NH2   1 
ATOM   18585 N  N     . LEU A 1 3990 ? 203.447 146.926 241.834 1.00 7.53  ? 3990 LEU A N     1 
ATOM   18586 C  CA    . LEU A 1 3990 ? 203.916 147.889 240.845 1.00 8.46  ? 3990 LEU A CA    1 
ATOM   18587 C  C     . LEU A 1 3990 ? 205.280 147.490 240.295 1.00 11.21 ? 3990 LEU A C     1 
ATOM   18588 O  O     . LEU A 1 3990 ? 205.533 147.611 239.090 1.00 14.81 ? 3990 LEU A O     1 
ATOM   18589 C  CB    . LEU A 1 3990 ? 203.958 149.281 241.471 1.00 8.83  ? 3990 LEU A CB    1 
ATOM   18590 C  CG    . LEU A 1 3990 ? 204.348 150.456 240.585 1.00 6.45  ? 3990 LEU A CG    1 
ATOM   18591 C  CD1   . LEU A 1 3990 ? 203.341 150.634 239.460 1.00 6.90  ? 3990 LEU A CD1   1 
ATOM   18592 C  CD2   . LEU A 1 3990 ? 204.451 151.717 241.420 1.00 9.50  ? 3990 LEU A CD2   1 
ATOM   18593 N  N     . LEU A 1 3991 ? 206.173 147.012 241.165 1.00 15.90 ? 3991 LEU A N     1 
ATOM   18594 C  CA    . LEU A 1 3991 ? 207.471 146.527 240.706 1.00 9.85  ? 3991 LEU A CA    1 
ATOM   18595 C  C     . LEU A 1 3991 ? 207.327 145.250 239.886 1.00 11.14 ? 3991 LEU A C     1 
ATOM   18596 O  O     . LEU A 1 3991 ? 208.042 145.062 238.895 1.00 11.69 ? 3991 LEU A O     1 
ATOM   18597 C  CB    . LEU A 1 3991 ? 208.392 146.297 241.901 1.00 10.01 ? 3991 LEU A CB    1 
ATOM   18598 C  CG    . LEU A 1 3991 ? 208.887 147.534 242.649 1.00 10.95 ? 3991 LEU A CG    1 
ATOM   18599 C  CD1   . LEU A 1 3991 ? 209.531 147.135 243.961 1.00 16.84 ? 3991 LEU A CD1   1 
ATOM   18600 C  CD2   . LEU A 1 3991 ? 209.863 148.321 241.792 1.00 13.66 ? 3991 LEU A CD2   1 
ATOM   18601 N  N     . LEU A 1 3992 ? 206.419 144.359 240.292 1.00 11.12 ? 3992 LEU A N     1 
ATOM   18602 C  CA    . LEU A 1 3992 ? 206.208 143.124 239.542 1.00 9.61  ? 3992 LEU A CA    1 
ATOM   18603 C  C     . LEU A 1 3992 ? 205.650 143.405 238.154 1.00 11.83 ? 3992 LEU A C     1 
ATOM   18604 O  O     . LEU A 1 3992 ? 206.092 142.802 237.170 1.00 14.64 ? 3992 LEU A O     1 
ATOM   18605 C  CB    . LEU A 1 3992 ? 205.274 142.193 240.314 1.00 10.94 ? 3992 LEU A CB    1 
ATOM   18606 C  CG    . LEU A 1 3992 ? 205.906 141.426 241.475 1.00 14.23 ? 3992 LEU A CG    1 
ATOM   18607 C  CD1   . LEU A 1 3992 ? 204.841 140.737 242.308 1.00 12.71 ? 3992 LEU A CD1   1 
ATOM   18608 C  CD2   . LEU A 1 3992 ? 206.924 140.420 240.958 1.00 10.13 ? 3992 LEU A CD2   1 
ATOM   18609 N  N     . ILE A 1 3993 ? 204.681 144.316 238.052 1.00 11.52 ? 3993 ILE A N     1 
ATOM   18610 C  CA    . ILE A 1 3993 ? 204.099 144.637 236.753 1.00 10.28 ? 3993 ILE A CA    1 
ATOM   18611 C  C     . ILE A 1 3993 ? 205.147 145.254 235.837 1.00 10.18 ? 3993 ILE A C     1 
ATOM   18612 O  O     . ILE A 1 3993 ? 205.251 144.897 234.660 1.00 11.92 ? 3993 ILE A O     1 
ATOM   18613 C  CB    . ILE A 1 3993 ? 202.877 145.558 236.927 1.00 11.22 ? 3993 ILE A CB    1 
ATOM   18614 C  CG1   . ILE A 1 3993 ? 201.686 144.759 237.457 1.00 9.17  ? 3993 ILE A CG1   1 
ATOM   18615 C  CG2   . ILE A 1 3993 ? 202.525 146.241 235.615 1.00 4.37  ? 3993 ILE A CG2   1 
ATOM   18616 C  CD1   . ILE A 1 3993 ? 201.230 143.656 236.531 1.00 9.46  ? 3993 ILE A CD1   1 
ATOM   18617 N  N     . GLN A 1 3994 ? 205.953 146.176 236.371 1.00 11.19 ? 3994 GLN A N     1 
ATOM   18618 C  CA    . GLN A 1 3994 ? 207.005 146.791 235.568 1.00 8.02  ? 3994 GLN A CA    1 
ATOM   18619 C  C     . GLN A 1 3994 ? 208.004 145.758 235.064 1.00 10.53 ? 3994 GLN A C     1 
ATOM   18620 O  O     . GLN A 1 3994 ? 208.544 145.902 233.960 1.00 12.86 ? 3994 GLN A O     1 
ATOM   18621 C  CB    . GLN A 1 3994 ? 207.715 147.867 236.388 1.00 9.20  ? 3994 GLN A CB    1 
ATOM   18622 C  CG    . GLN A 1 3994 ? 208.962 148.444 235.741 1.00 10.60 ? 3994 GLN A CG    1 
ATOM   18623 C  CD    . GLN A 1 3994 ? 209.597 149.528 236.583 1.00 11.80 ? 3994 GLN A CD    1 
ATOM   18624 O  OE1   . GLN A 1 3994 ? 209.996 149.289 237.721 1.00 19.16 ? 3994 GLN A OE1   1 
ATOM   18625 N  NE2   . GLN A 1 3994 ? 209.690 150.730 236.029 1.00 10.78 ? 3994 GLN A NE2   1 
ATOM   18626 N  N     . ALA A 1 3995 ? 208.256 144.711 235.849 1.00 14.45 ? 3995 ALA A N     1 
ATOM   18627 C  CA    . ALA A 1 3995 ? 209.208 143.690 235.430 1.00 15.50 ? 3995 ALA A CA    1 
ATOM   18628 C  C     . ALA A 1 3995 ? 208.625 142.789 234.347 1.00 15.96 ? 3995 ALA A C     1 
ATOM   18629 O  O     . ALA A 1 3995 ? 209.307 142.464 233.370 1.00 19.39 ? 3995 ALA A O     1 
ATOM   18630 C  CB    . ALA A 1 3995 ? 209.655 142.863 236.636 1.00 13.41 ? 3995 ALA A CB    1 
ATOM   18631 N  N     . PHE A 1 3996 ? 207.366 142.382 234.494 1.00 13.25 ? 3996 PHE A N     1 
ATOM   18632 C  CA    . PHE A 1 3996 ? 206.775 141.373 233.624 1.00 13.04 ? 3996 PHE A CA    1 
ATOM   18633 C  C     . PHE A 1 3996 ? 205.836 141.938 232.567 1.00 18.76 ? 3996 PHE A C     1 
ATOM   18634 O  O     . PHE A 1 3996 ? 205.872 141.490 231.419 1.00 23.54 ? 3996 PHE A O     1 
ATOM   18635 C  CB    . PHE A 1 3996 ? 206.029 140.333 234.463 1.00 13.99 ? 3996 PHE A CB    1 
ATOM   18636 C  CG    . PHE A 1 3996 ? 206.921 139.542 235.369 1.00 18.42 ? 3996 PHE A CG    1 
ATOM   18637 C  CD1   . PHE A 1 3996 ? 207.717 138.531 234.863 1.00 17.79 ? 3996 PHE A CD1   1 
ATOM   18638 C  CD2   . PHE A 1 3996 ? 206.970 139.812 236.725 1.00 16.68 ? 3996 PHE A CD2   1 
ATOM   18639 C  CE1   . PHE A 1 3996 ? 208.540 137.801 235.692 1.00 19.94 ? 3996 PHE A CE1   1 
ATOM   18640 C  CE2   . PHE A 1 3996 ? 207.791 139.086 237.559 1.00 17.25 ? 3996 PHE A CE2   1 
ATOM   18641 C  CZ    . PHE A 1 3996 ? 208.577 138.079 237.044 1.00 21.11 ? 3996 PHE A CZ    1 
ATOM   18642 N  N     . ARG A 1 3997 ? 204.996 142.911 232.914 1.00 11.02 ? 3997 ARG A N     1 
ATOM   18643 C  CA    . ARG A 1 3997 ? 204.006 143.464 231.990 1.00 10.00 ? 3997 ARG A CA    1 
ATOM   18644 C  C     . ARG A 1 3997 ? 204.114 144.983 231.966 1.00 8.13  ? 3997 ARG A C     1 
ATOM   18645 O  O     . ARG A 1 3997 ? 203.248 145.690 232.493 1.00 11.96 ? 3997 ARG A O     1 
ATOM   18646 C  CB    . ARG A 1 3997 ? 202.594 143.023 232.379 1.00 10.25 ? 3997 ARG A CB    1 
ATOM   18647 C  CG    . ARG A 1 3997 ? 202.344 141.534 232.207 1.00 14.08 ? 3997 ARG A CG    1 
ATOM   18648 C  CD    . ARG A 1 3997 ? 202.630 141.090 230.782 1.00 12.25 ? 3997 ARG A CD    1 
ATOM   18649 N  NE    . ARG A 1 3997 ? 201.729 141.720 229.824 1.00 15.04 ? 3997 ARG A NE    1 
ATOM   18650 C  CZ    . ARG A 1 3997 ? 200.446 141.416 229.684 1.00 15.19 ? 3997 ARG A CZ    1 
ATOM   18651 N  NH1   . ARG A 1 3997 ? 199.877 140.462 230.404 1.00 15.51 ? 3997 ARG A NH1   1 
ATOM   18652 N  NH2   . ARG A 1 3997 ? 199.715 142.083 228.798 1.00 18.41 ? 3997 ARG A NH2   1 
ATOM   18653 N  N     . PRO A 1 3998 ? 205.172 145.520 231.355 1.00 7.79  ? 3998 PRO A N     1 
ATOM   18654 C  CA    . PRO A 1 3998 ? 205.318 146.983 231.305 1.00 8.18  ? 3998 PRO A CA    1 
ATOM   18655 C  C     . PRO A 1 3998 ? 204.207 147.680 230.537 1.00 8.28  ? 3998 PRO A C     1 
ATOM   18656 O  O     . PRO A 1 3998 ? 203.997 148.880 230.742 1.00 11.15 ? 3998 PRO A O     1 
ATOM   18657 C  CB    . PRO A 1 3998 ? 206.684 147.177 230.630 1.00 5.81  ? 3998 PRO A CB    1 
ATOM   18658 C  CG    . PRO A 1 3998 ? 206.904 145.925 229.860 1.00 7.81  ? 3998 PRO A CG    1 
ATOM   18659 C  CD    . PRO A 1 3998 ? 206.275 144.831 230.665 1.00 8.60  ? 3998 PRO A CD    1 
ATOM   18660 N  N     . ASP A 1 3999 ? 203.491 146.972 229.662 1.00 6.86  ? 3999 ASP A N     1 
ATOM   18661 C  CA    . ASP A 1 3999 ? 202.341 147.566 228.991 1.00 5.44  ? 3999 ASP A CA    1 
ATOM   18662 C  C     . ASP A 1 3999 ? 201.195 147.845 229.953 1.00 5.68  ? 3999 ASP A C     1 
ATOM   18663 O  O     . ASP A 1 3999 ? 200.341 148.685 229.655 1.00 7.23  ? 3999 ASP A O     1 
ATOM   18664 C  CB    . ASP A 1 3999 ? 201.864 146.656 227.859 1.00 7.46  ? 3999 ASP A CB    1 
ATOM   18665 C  CG    . ASP A 1 3999 ? 201.753 145.206 228.282 1.00 13.45 ? 3999 ASP A CG    1 
ATOM   18666 O  OD1   . ASP A 1 3999 ? 202.768 144.639 228.735 1.00 12.82 ? 3999 ASP A OD1   1 
ATOM   18667 O  OD2   . ASP A 1 3999 ? 200.651 144.632 228.159 1.00 13.60 ? 3999 ASP A OD2   1 
ATOM   18668 N  N     . ARG A 1 4000 ? 201.161 147.167 231.099 1.00 6.23  ? 4000 ARG A N     1 
ATOM   18669 C  CA    . ARG A 1 4000 ? 200.162 147.404 232.128 1.00 4.40  ? 4000 ARG A CA    1 
ATOM   18670 C  C     . ARG A 1 4000 ? 200.681 148.289 233.252 1.00 3.51  ? 4000 ARG A C     1 
ATOM   18671 O  O     . ARG A 1 4000 ? 200.030 148.398 234.294 1.00 4.68  ? 4000 ARG A O     1 
ATOM   18672 C  CB    . ARG A 1 4000 ? 199.664 146.073 232.690 1.00 6.26  ? 4000 ARG A CB    1 
ATOM   18673 C  CG    . ARG A 1 4000 ? 199.164 145.114 231.629 1.00 7.38  ? 4000 ARG A CG    1 
ATOM   18674 C  CD    . ARG A 1 4000 ? 198.030 145.722 230.832 1.00 8.73  ? 4000 ARG A CD    1 
ATOM   18675 N  NE    . ARG A 1 4000 ? 196.872 146.017 231.665 1.00 11.29 ? 4000 ARG A NE    1 
ATOM   18676 C  CZ    . ARG A 1 4000 ? 195.775 146.622 231.233 1.00 9.06  ? 4000 ARG A CZ    1 
ATOM   18677 N  NH1   . ARG A 1 4000 ? 195.659 147.030 229.979 1.00 10.14 ? 4000 ARG A NH1   1 
ATOM   18678 N  NH2   . ARG A 1 4000 ? 194.770 146.826 232.079 1.00 7.53  ? 4000 ARG A NH2   1 
ATOM   18679 N  N     . LEU A 1 4001 ? 201.841 148.920 233.062 1.00 3.79  ? 4001 LEU A N     1 
ATOM   18680 C  CA    . LEU A 1 4001 ? 202.422 149.747 234.114 1.00 4.53  ? 4001 LEU A CA    1 
ATOM   18681 C  C     . LEU A 1 4001 ? 201.539 150.949 234.430 1.00 3.09  ? 4001 LEU A C     1 
ATOM   18682 O  O     . LEU A 1 4001 ? 201.407 151.340 235.596 1.00 4.70  ? 4001 LEU A O     1 
ATOM   18683 C  CB    . LEU A 1 4001 ? 203.825 150.197 233.710 1.00 5.04  ? 4001 LEU A CB    1 
ATOM   18684 C  CG    . LEU A 1 4001 ? 204.627 150.941 234.775 1.00 3.66  ? 4001 LEU A CG    1 
ATOM   18685 C  CD1   . LEU A 1 4001 ? 204.732 150.098 236.036 1.00 6.19  ? 4001 LEU A CD1   1 
ATOM   18686 C  CD2   . LEU A 1 4001 ? 205.999 151.295 234.245 1.00 4.96  ? 4001 LEU A CD2   1 
ATOM   18687 N  N     . LEU A 1 4002 ? 200.935 151.554 233.405 1.00 2.36  ? 4002 LEU A N     1 
ATOM   18688 C  CA    . LEU A 1 4002 ? 200.001 152.650 233.642 1.00 2.19  ? 4002 LEU A CA    1 
ATOM   18689 C  C     . LEU A 1 4002 ? 198.782 152.178 234.425 1.00 2.41  ? 4002 LEU A C     1 
ATOM   18690 O  O     . LEU A 1 4002 ? 198.319 152.868 235.340 1.00 4.39  ? 4002 LEU A O     1 
ATOM   18691 C  CB    . LEU A 1 4002 ? 199.569 153.273 232.317 1.00 2.48  ? 4002 LEU A CB    1 
ATOM   18692 C  CG    . LEU A 1 4002 ? 200.632 154.040 231.536 1.00 2.78  ? 4002 LEU A CG    1 
ATOM   18693 C  CD1   . LEU A 1 4002 ? 200.021 154.627 230.278 1.00 1.87  ? 4002 LEU A CD1   1 
ATOM   18694 C  CD2   . LEU A 1 4002 ? 201.260 155.127 232.398 1.00 1.77  ? 4002 LEU A CD2   1 
ATOM   18695 N  N     . ALA A 1 4003 ? 198.247 151.007 234.075 1.00 2.89  ? 4003 ALA A N     1 
ATOM   18696 C  CA    . ALA A 1 4003 ? 197.099 150.474 234.798 1.00 3.07  ? 4003 ALA A CA    1 
ATOM   18697 C  C     . ALA A 1 4003 ? 197.450 150.192 236.255 1.00 3.21  ? 4003 ALA A C     1 
ATOM   18698 O  O     . ALA A 1 4003 ? 196.651 150.467 237.158 1.00 3.14  ? 4003 ALA A O     1 
ATOM   18699 C  CB    . ALA A 1 4003 ? 196.588 149.208 234.111 1.00 2.66  ? 4003 ALA A CB    1 
ATOM   18700 N  N     . MET A 1 4004 ? 198.640 149.642 236.500 1.00 4.05  ? 4004 MET A N     1 
ATOM   18701 C  CA    . MET A 1 4004 ? 199.080 149.414 237.872 1.00 4.54  ? 4004 MET A CA    1 
ATOM   18702 C  C     . MET A 1 4004 ? 199.342 150.725 238.602 1.00 3.87  ? 4004 MET A C     1 
ATOM   18703 O  O     . MET A 1 4004 ? 199.079 150.828 239.804 1.00 3.99  ? 4004 MET A O     1 
ATOM   18704 C  CB    . MET A 1 4004 ? 200.333 148.537 237.879 1.00 5.00  ? 4004 MET A CB    1 
ATOM   18705 C  CG    . MET A 1 4004 ? 200.702 147.984 239.240 1.00 4.87  ? 4004 MET A CG    1 
ATOM   18706 S  SD    . MET A 1 4004 ? 199.399 146.990 239.983 1.00 14.52 ? 4004 MET A SD    1 
ATOM   18707 C  CE    . MET A 1 4004 ? 199.092 147.899 241.491 1.00 6.42  ? 4004 MET A CE    1 
ATOM   18708 N  N     . ALA A 1 4005 ? 199.860 151.735 237.895 1.00 2.64  ? 4005 ALA A N     1 
ATOM   18709 C  CA    . ALA A 1 4005 ? 200.086 153.037 238.514 1.00 1.71  ? 4005 ALA A CA    1 
ATOM   18710 C  C     . ALA A 1 4005 ? 198.774 153.673 238.950 1.00 3.69  ? 4005 ALA A C     1 
ATOM   18711 O  O     . ALA A 1 4005 ? 198.702 154.299 240.015 1.00 3.44  ? 4005 ALA A O     1 
ATOM   18712 C  CB    . ALA A 1 4005 ? 200.835 153.956 237.551 1.00 1.59  ? 4005 ALA A CB    1 
ATOM   18713 N  N     . HIS A 1 4006 ? 197.727 153.530 238.137 1.00 2.64  ? 4006 HIS A N     1 
ATOM   18714 C  CA    . HIS A 1 4006 ? 196.414 154.045 238.518 1.00 2.21  ? 4006 HIS A CA    1 
ATOM   18715 C  C     . HIS A 1 4006 ? 195.888 153.337 239.759 1.00 2.75  ? 4006 HIS A C     1 
ATOM   18716 O  O     . HIS A 1 4006 ? 195.232 153.957 240.606 1.00 4.17  ? 4006 HIS A O     1 
ATOM   18717 C  CB    . HIS A 1 4006 ? 195.434 153.901 237.354 1.00 1.74  ? 4006 HIS A CB    1 
ATOM   18718 C  CG    . HIS A 1 4006 ? 195.503 155.026 236.369 1.00 3.06  ? 4006 HIS A CG    1 
ATOM   18719 N  ND1   . HIS A 1 4006 ? 196.412 155.054 235.332 1.00 4.66  ? 4006 HIS A ND1   1 
ATOM   18720 C  CD2   . HIS A 1 4006 ? 194.776 156.163 236.262 1.00 1.38  ? 4006 HIS A CD2   1 
ATOM   18721 C  CE1   . HIS A 1 4006 ? 196.243 156.160 234.631 1.00 2.47  ? 4006 HIS A CE1   1 
ATOM   18722 N  NE2   . HIS A 1 4006 ? 195.257 156.851 235.175 1.00 1.56  ? 4006 HIS A NE2   1 
ATOM   18723 N  N     . MET A 1 4007 ? 196.158 152.036 239.882 1.00 2.68  ? 4007 MET A N     1 
ATOM   18724 C  CA    . MET A 1 4007 ? 195.753 151.310 241.081 1.00 3.69  ? 4007 MET A CA    1 
ATOM   18725 C  C     . MET A 1 4007 ? 196.559 151.759 242.295 1.00 3.85  ? 4007 MET A C     1 
ATOM   18726 O  O     . MET A 1 4007 ? 196.030 151.821 243.410 1.00 3.50  ? 4007 MET A O     1 
ATOM   18727 C  CB    . MET A 1 4007 ? 195.901 149.806 240.857 1.00 4.91  ? 4007 MET A CB    1 
ATOM   18728 C  CG    . MET A 1 4007 ? 194.736 149.183 240.113 1.00 4.92  ? 4007 MET A CG    1 
ATOM   18729 S  SD    . MET A 1 4007 ? 195.065 147.496 239.575 1.00 26.38 ? 4007 MET A SD    1 
ATOM   18730 C  CE    . MET A 1 4007 ? 194.931 146.614 241.126 1.00 11.79 ? 4007 MET A CE    1 
ATOM   18731 N  N     . PHE A 1 4008 ? 197.843 152.071 242.098 1.00 4.91  ? 4008 PHE A N     1 
ATOM   18732 C  CA    . PHE A 1 4008 ? 198.648 152.614 243.188 1.00 4.59  ? 4008 PHE A CA    1 
ATOM   18733 C  C     . PHE A 1 4008 ? 198.100 153.955 243.659 1.00 3.73  ? 4008 PHE A C     1 
ATOM   18734 O  O     . PHE A 1 4008 ? 198.046 154.222 244.865 1.00 8.33  ? 4008 PHE A O     1 
ATOM   18735 C  CB    . PHE A 1 4008 ? 200.105 152.750 242.746 1.00 5.19  ? 4008 PHE A CB    1 
ATOM   18736 C  CG    . PHE A 1 4008 ? 200.975 153.485 243.725 1.00 6.54  ? 4008 PHE A CG    1 
ATOM   18737 C  CD1   . PHE A 1 4008 ? 201.541 152.827 244.802 1.00 8.87  ? 4008 PHE A CD1   1 
ATOM   18738 C  CD2   . PHE A 1 4008 ? 201.235 154.834 243.564 1.00 9.75  ? 4008 PHE A CD2   1 
ATOM   18739 C  CE1   . PHE A 1 4008 ? 202.340 153.506 245.701 1.00 8.97  ? 4008 PHE A CE1   1 
ATOM   18740 C  CE2   . PHE A 1 4008 ? 202.036 155.515 244.457 1.00 7.91  ? 4008 PHE A CE2   1 
ATOM   18741 C  CZ    . PHE A 1 4008 ? 202.589 154.850 245.527 1.00 6.32  ? 4008 PHE A CZ    1 
ATOM   18742 N  N     . VAL A 1 4009 ? 197.693 154.813 242.721 1.00 3.07  ? 4009 VAL A N     1 
ATOM   18743 C  CA    . VAL A 1 4009 ? 197.090 156.090 243.091 1.00 2.96  ? 4009 VAL A CA    1 
ATOM   18744 C  C     . VAL A 1 4009 ? 195.764 155.859 243.805 1.00 3.37  ? 4009 VAL A C     1 
ATOM   18745 O  O     . VAL A 1 4009 ? 195.438 156.543 244.782 1.00 4.06  ? 4009 VAL A O     1 
ATOM   18746 C  CB    . VAL A 1 4009 ? 196.924 156.980 241.845 1.00 2.67  ? 4009 VAL A CB    1 
ATOM   18747 C  CG1   . VAL A 1 4009 ? 196.114 158.225 242.172 1.00 1.22  ? 4009 VAL A CG1   1 
ATOM   18748 C  CG2   . VAL A 1 4009 ? 198.282 157.358 241.282 1.00 1.27  ? 4009 VAL A CG2   1 
ATOM   18749 N  N     . SER A 1 4010 ? 194.986 154.884 243.332 1.00 6.95  ? 4010 SER A N     1 
ATOM   18750 C  CA    . SER A 1 4010 ? 193.720 154.554 243.982 1.00 3.81  ? 4010 SER A CA    1 
ATOM   18751 C  C     . SER A 1 4010 ? 193.941 154.050 245.403 1.00 4.43  ? 4010 SER A C     1 
ATOM   18752 O  O     . SER A 1 4010 ? 193.148 154.344 246.304 1.00 6.28  ? 4010 SER A O     1 
ATOM   18753 C  CB    . SER A 1 4010 ? 192.968 153.515 243.154 1.00 4.05  ? 4010 SER A CB    1 
ATOM   18754 O  OG    . SER A 1 4010 ? 191.649 153.335 243.632 1.00 14.46 ? 4010 SER A OG    1 
ATOM   18755 N  N     . THR A 1 4011 ? 195.002 153.272 245.621 1.00 6.70  ? 4011 THR A N     1 
ATOM   18756 C  CA    . THR A 1 4011 ? 195.292 152.777 246.963 1.00 6.74  ? 4011 THR A CA    1 
ATOM   18757 C  C     . THR A 1 4011 ? 195.644 153.918 247.911 1.00 7.35  ? 4011 THR A C     1 
ATOM   18758 O  O     . THR A 1 4011 ? 195.200 153.935 249.064 1.00 4.89  ? 4011 THR A O     1 
ATOM   18759 C  CB    . THR A 1 4011 ? 196.425 151.753 246.908 1.00 6.15  ? 4011 THR A CB    1 
ATOM   18760 O  OG1   . THR A 1 4011 ? 196.041 150.658 246.069 1.00 9.84  ? 4011 THR A OG1   1 
ATOM   18761 C  CG2   . THR A 1 4011 ? 196.736 151.226 248.297 1.00 6.87  ? 4011 THR A CG2   1 
ATOM   18762 N  N     . ASN A 1 4012 ? 196.435 154.883 247.439 1.00 6.86  ? 4012 ASN A N     1 
ATOM   18763 C  CA    . ASN A 1 4012 ? 196.883 155.971 248.301 1.00 5.35  ? 4012 ASN A CA    1 
ATOM   18764 C  C     . ASN A 1 4012 ? 195.843 157.079 248.419 1.00 2.17  ? 4012 ASN A C     1 
ATOM   18765 O  O     . ASN A 1 4012 ? 195.573 157.560 249.523 1.00 3.73  ? 4012 ASN A O     1 
ATOM   18766 C  CB    . ASN A 1 4012 ? 198.202 156.539 247.776 1.00 4.90  ? 4012 ASN A CB    1 
ATOM   18767 C  CG    . ASN A 1 4012 ? 199.410 155.849 248.366 1.00 7.26  ? 4012 ASN A CG    1 
ATOM   18768 O  OD1   . ASN A 1 4012 ? 199.672 155.945 249.564 1.00 14.12 ? 4012 ASN A OD1   1 
ATOM   18769 N  ND2   . ASN A 1 4012 ? 200.155 155.143 247.528 1.00 11.43 ? 4012 ASN A ND2   1 
ATOM   18770 N  N     . LEU A 1 4013 ? 195.243 157.488 247.303 1.00 3.40  ? 4013 LEU A N     1 
ATOM   18771 C  CA    . LEU A 1 4013 ? 194.394 158.671 247.275 1.00 3.02  ? 4013 LEU A CA    1 
ATOM   18772 C  C     . LEU A 1 4013 ? 192.909 158.375 247.119 1.00 2.52  ? 4013 LEU A C     1 
ATOM   18773 O  O     . LEU A 1 4013 ? 192.097 159.289 247.292 1.00 4.76  ? 4013 LEU A O     1 
ATOM   18774 C  CB    . LEU A 1 4013 ? 194.845 159.611 246.147 1.00 1.06  ? 4013 LEU A CB    1 
ATOM   18775 C  CG    . LEU A 1 4013 ? 196.264 160.165 246.292 1.00 0.98  ? 4013 LEU A CG    1 
ATOM   18776 C  CD1   . LEU A 1 4013 ? 196.784 160.689 244.969 1.00 0.92  ? 4013 LEU A CD1   1 
ATOM   18777 C  CD2   . LEU A 1 4013 ? 196.308 161.255 247.349 1.00 1.23  ? 4013 LEU A CD2   1 
ATOM   18778 N  N     . GLY A 1 4014 ? 192.530 157.146 246.802 1.00 2.67  ? 4014 GLY A N     1 
ATOM   18779 C  CA    . GLY A 1 4014 ? 191.131 156.796 246.672 1.00 3.45  ? 4014 GLY A CA    1 
ATOM   18780 C  C     . GLY A 1 4014 ? 190.747 156.492 245.229 1.00 5.89  ? 4014 GLY A C     1 
ATOM   18781 O  O     . GLY A 1 4014 ? 191.424 156.879 244.272 1.00 5.97  ? 4014 GLY A O     1 
ATOM   18782 N  N     . GLU A 1 4015 ? 189.620 155.788 245.087 1.00 9.64  ? 4015 GLU A N     1 
ATOM   18783 C  CA    . GLU A 1 4015 ? 189.185 155.326 243.772 1.00 6.16  ? 4015 GLU A CA    1 
ATOM   18784 C  C     . GLU A 1 4015 ? 188.708 156.474 242.893 1.00 7.11  ? 4015 GLU A C     1 
ATOM   18785 O  O     . GLU A 1 4015 ? 188.899 156.437 241.672 1.00 11.35 ? 4015 GLU A O     1 
ATOM   18786 C  CB    . GLU A 1 4015 ? 188.080 154.276 243.929 1.00 8.66  ? 4015 GLU A CB    1 
ATOM   18787 C  CG    . GLU A 1 4015 ? 187.701 153.541 242.645 1.00 19.16 ? 4015 GLU A CG    1 
ATOM   18788 C  CD    . GLU A 1 4015 ? 186.700 154.302 241.789 1.00 26.83 ? 4015 GLU A CD    1 
ATOM   18789 O  OE1   . GLU A 1 4015 ? 185.897 155.075 242.352 1.00 24.03 ? 4015 GLU A OE1   1 
ATOM   18790 O  OE2   . GLU A 1 4015 ? 186.726 154.132 240.551 1.00 24.55 ? 4015 GLU A OE2   1 
ATOM   18791 N  N     . SER A 1 4016 ? 188.101 157.498 243.485 1.00 7.48  ? 4016 SER A N     1 
ATOM   18792 C  CA    . SER A 1 4016 ? 187.531 158.609 242.739 1.00 5.88  ? 4016 SER A CA    1 
ATOM   18793 C  C     . SER A 1 4016 ? 188.464 159.809 242.657 1.00 6.71  ? 4016 SER A C     1 
ATOM   18794 O  O     . SER A 1 4016 ? 188.025 160.894 242.268 1.00 7.92  ? 4016 SER A O     1 
ATOM   18795 C  CB    . SER A 1 4016 ? 186.197 159.026 243.360 1.00 10.70 ? 4016 SER A CB    1 
ATOM   18796 O  OG    . SER A 1 4016 ? 186.284 159.049 244.773 1.00 19.27 ? 4016 SER A OG    1 
ATOM   18797 N  N     . PHE A 1 4017 ? 189.737 159.640 243.020 1.00 8.41  ? 4017 PHE A N     1 
ATOM   18798 C  CA    . PHE A 1 4017 ? 190.662 160.767 243.026 1.00 2.35  ? 4017 PHE A CA    1 
ATOM   18799 C  C     . PHE A 1 4017 ? 190.860 161.340 241.627 1.00 2.39  ? 4017 PHE A C     1 
ATOM   18800 O  O     . PHE A 1 4017 ? 190.878 162.561 241.447 1.00 1.95  ? 4017 PHE A O     1 
ATOM   18801 C  CB    . PHE A 1 4017 ? 192.001 160.341 243.628 1.00 1.14  ? 4017 PHE A CB    1 
ATOM   18802 C  CG    . PHE A 1 4017 ? 192.993 161.458 243.745 1.00 1.23  ? 4017 PHE A CG    1 
ATOM   18803 C  CD1   . PHE A 1 4017 ? 192.969 162.311 244.832 1.00 0.51  ? 4017 PHE A CD1   1 
ATOM   18804 C  CD2   . PHE A 1 4017 ? 193.949 161.659 242.762 1.00 0.92  ? 4017 PHE A CD2   1 
ATOM   18805 C  CE1   . PHE A 1 4017 ? 193.878 163.342 244.940 1.00 0.50  ? 4017 PHE A CE1   1 
ATOM   18806 C  CE2   . PHE A 1 4017 ? 194.859 162.690 242.865 1.00 0.50  ? 4017 PHE A CE2   1 
ATOM   18807 C  CZ    . PHE A 1 4017 ? 194.823 163.531 243.958 1.00 0.57  ? 4017 PHE A CZ    1 
ATOM   18808 N  N     . MET A 1 4018 ? 191.004 160.475 240.626 1.00 2.28  ? 4018 MET A N     1 
ATOM   18809 C  CA    . MET A 1 4018 ? 191.263 160.903 239.258 1.00 1.38  ? 4018 MET A CA    1 
ATOM   18810 C  C     . MET A 1 4018 ? 190.001 160.950 238.405 1.00 4.22  ? 4018 MET A C     1 
ATOM   18811 O  O     . MET A 1 4018 ? 190.094 161.145 237.190 1.00 7.92  ? 4018 MET A O     1 
ATOM   18812 C  CB    . MET A 1 4018 ? 192.298 159.982 238.614 1.00 1.46  ? 4018 MET A CB    1 
ATOM   18813 C  CG    . MET A 1 4018 ? 193.709 160.183 239.134 1.00 1.69  ? 4018 MET A CG    1 
ATOM   18814 S  SD    . MET A 1 4018 ? 194.904 159.087 238.350 1.00 13.64 ? 4018 MET A SD    1 
ATOM   18815 C  CE    . MET A 1 4018 ? 195.603 160.183 237.121 1.00 1.18  ? 4018 MET A CE    1 
ATOM   18816 N  N     . SER A 1 4019 ? 188.826 160.790 239.017 1.00 5.71  ? 4019 SER A N     1 
ATOM   18817 C  CA    . SER A 1 4019 ? 187.592 160.648 238.256 1.00 5.50  ? 4019 SER A CA    1 
ATOM   18818 C  C     . SER A 1 4019 ? 187.120 161.954 237.628 1.00 7.52  ? 4019 SER A C     1 
ATOM   18819 O  O     . SER A 1 4019 ? 186.343 161.914 236.669 1.00 14.85 ? 4019 SER A O     1 
ATOM   18820 C  CB    . SER A 1 4019 ? 186.495 160.078 239.156 1.00 8.68  ? 4019 SER A CB    1 
ATOM   18821 O  OG    . SER A 1 4019 ? 186.737 158.711 239.443 1.00 14.84 ? 4019 SER A OG    1 
ATOM   18822 N  N     . ILE A 1 4020 ? 187.565 163.104 238.135 1.00 6.74  ? 4020 ILE A N     1 
ATOM   18823 C  CA    . ILE A 1 4020 ? 187.112 164.380 237.588 1.00 4.67  ? 4020 ILE A CA    1 
ATOM   18824 C  C     . ILE A 1 4020 ? 187.617 164.564 236.163 1.00 7.51  ? 4020 ILE A C     1 
ATOM   18825 O  O     . ILE A 1 4020 ? 186.913 165.110 235.305 1.00 11.73 ? 4020 ILE A O     1 
ATOM   18826 C  CB    . ILE A 1 4020 ? 187.552 165.540 238.503 1.00 5.71  ? 4020 ILE A CB    1 
ATOM   18827 C  CG1   . ILE A 1 4020 ? 186.975 165.353 239.905 1.00 8.18  ? 4020 ILE A CG1   1 
ATOM   18828 C  CG2   . ILE A 1 4020 ? 187.113 166.879 237.934 1.00 3.27  ? 4020 ILE A CG2   1 
ATOM   18829 C  CD1   . ILE A 1 4020 ? 185.465 165.337 239.944 1.00 3.84  ? 4020 ILE A CD1   1 
ATOM   18830 N  N     . MET A 1 4021 ? 188.837 164.106 235.882 1.00 7.11  ? 4021 MET A N     1 
ATOM   18831 C  CA    . MET A 1 4021 ? 189.408 164.283 234.554 1.00 6.02  ? 4021 MET A CA    1 
ATOM   18832 C  C     . MET A 1 4021 ? 188.643 163.511 233.487 1.00 9.87  ? 4021 MET A C     1 
ATOM   18833 O  O     . MET A 1 4021 ? 188.718 163.868 232.306 1.00 15.57 ? 4021 MET A O     1 
ATOM   18834 C  CB    . MET A 1 4021 ? 190.876 163.859 234.559 1.00 5.72  ? 4021 MET A CB    1 
ATOM   18835 C  CG    . MET A 1 4021 ? 191.818 164.817 235.282 1.00 6.34  ? 4021 MET A CG    1 
ATOM   18836 S  SD    . MET A 1 4021 ? 191.421 166.572 235.129 1.00 12.12 ? 4021 MET A SD    1 
ATOM   18837 C  CE    . MET A 1 4021 ? 190.571 166.877 236.677 1.00 2.74  ? 4021 MET A CE    1 
ATOM   18838 N  N     . GLU A 1 4022 ? 187.910 162.466 233.872 1.00 11.79 ? 4022 GLU A N     1 
ATOM   18839 C  CA    . GLU A 1 4022 ? 187.090 161.725 232.921 1.00 8.03  ? 4022 GLU A CA    1 
ATOM   18840 C  C     . GLU A 1 4022 ? 185.819 162.471 232.542 1.00 8.05  ? 4022 GLU A C     1 
ATOM   18841 O  O     . GLU A 1 4022 ? 185.261 162.210 231.471 1.00 6.82  ? 4022 GLU A O     1 
ATOM   18842 C  CB    . GLU A 1 4022 ? 186.721 160.357 233.500 1.00 11.50 ? 4022 GLU A CB    1 
ATOM   18843 C  CG    . GLU A 1 4022 ? 187.818 159.308 233.398 1.00 11.79 ? 4022 GLU A CG    1 
ATOM   18844 C  CD    . GLU A 1 4022 ? 188.694 159.493 232.179 1.00 17.93 ? 4022 GLU A CD    1 
ATOM   18845 O  OE1   . GLU A 1 4022 ? 189.871 159.878 232.344 1.00 20.91 ? 4022 GLU A OE1   1 
ATOM   18846 O  OE2   . GLU A 1 4022 ? 188.205 159.250 231.055 1.00 18.17 ? 4022 GLU A OE2   1 
ATOM   18847 N  N     . GLN A 1 4023 ? 185.350 163.382 233.393 1.00 11.18 ? 4023 GLN A N     1 
ATOM   18848 C  CA    . GLN A 1 4023 ? 184.142 164.146 233.136 1.00 7.79  ? 4023 GLN A CA    1 
ATOM   18849 C  C     . GLN A 1 4023 ? 184.430 165.319 232.200 1.00 6.91  ? 4023 GLN A C     1 
ATOM   18850 O  O     . GLN A 1 4023 ? 185.561 165.807 232.133 1.00 7.87  ? 4023 GLN A O     1 
ATOM   18851 C  CB    . GLN A 1 4023 ? 183.557 164.672 234.442 1.00 8.93  ? 4023 GLN A CB    1 
ATOM   18852 C  CG    . GLN A 1 4023 ? 182.879 163.617 235.294 1.00 12.21 ? 4023 GLN A CG    1 
ATOM   18853 C  CD    . GLN A 1 4023 ? 181.766 162.905 234.557 1.00 20.30 ? 4023 GLN A CD    1 
ATOM   18854 O  OE1   . GLN A 1 4023 ? 180.858 163.538 234.021 1.00 19.90 ? 4023 GLN A OE1   1 
ATOM   18855 N  NE2   . GLN A 1 4023 ? 181.828 161.580 234.525 1.00 16.60 ? 4023 GLN A NE2   1 
ATOM   18856 N  N     . PRO A 1 4024 ? 183.425 165.781 231.453 1.00 7.40  ? 4024 PRO A N     1 
ATOM   18857 C  CA    . PRO A 1 4024 ? 183.607 166.991 230.648 1.00 6.28  ? 4024 PRO A CA    1 
ATOM   18858 C  C     . PRO A 1 4024 ? 183.842 168.211 231.527 1.00 9.02  ? 4024 PRO A C     1 
ATOM   18859 O  O     . PRO A 1 4024 ? 183.350 168.301 232.654 1.00 11.29 ? 4024 PRO A O     1 
ATOM   18860 C  CB    . PRO A 1 4024 ? 182.290 167.104 229.870 1.00 7.37  ? 4024 PRO A CB    1 
ATOM   18861 C  CG    . PRO A 1 4024 ? 181.314 166.295 230.655 1.00 8.93  ? 4024 PRO A CG    1 
ATOM   18862 C  CD    . PRO A 1 4024 ? 182.102 165.170 231.237 1.00 8.51  ? 4024 PRO A CD    1 
ATOM   18863 N  N     . LEU A 1 4025 ? 184.611 169.155 230.992 1.00 6.44  ? 4025 LEU A N     1 
ATOM   18864 C  CA    . LEU A 1 4025 ? 185.013 170.330 231.754 1.00 6.68  ? 4025 LEU A CA    1 
ATOM   18865 C  C     . LEU A 1 4025 ? 183.805 171.196 232.096 1.00 10.76 ? 4025 LEU A C     1 
ATOM   18866 O  O     . LEU A 1 4025 ? 183.006 171.542 231.222 1.00 12.16 ? 4025 LEU A O     1 
ATOM   18867 C  CB    . LEU A 1 4025 ? 186.039 171.139 230.961 1.00 5.51  ? 4025 LEU A CB    1 
ATOM   18868 C  CG    . LEU A 1 4025 ? 186.662 172.350 231.653 1.00 7.24  ? 4025 LEU A CG    1 
ATOM   18869 C  CD1   . LEU A 1 4025 ? 187.403 171.922 232.902 1.00 10.52 ? 4025 LEU A CD1   1 
ATOM   18870 C  CD2   . LEU A 1 4025 ? 187.594 173.075 230.701 1.00 5.28  ? 4025 LEU A CD2   1 
ATOM   18871 N  N     . ASP A 1 4026 ? 183.684 171.552 233.372 1.00 13.22 ? 4026 ASP A N     1 
ATOM   18872 C  CA    . ASP A 1 4026 ? 182.594 172.395 233.863 1.00 11.30 ? 4026 ASP A CA    1 
ATOM   18873 C  C     . ASP A 1 4026 ? 183.089 173.838 233.824 1.00 14.54 ? 4026 ASP A C     1 
ATOM   18874 O  O     . ASP A 1 4026 ? 183.464 174.416 234.845 1.00 15.52 ? 4026 ASP A O     1 
ATOM   18875 C  CB    . ASP A 1 4026 ? 182.172 171.975 235.266 1.00 13.93 ? 4026 ASP A CB    1 
ATOM   18876 C  CG    . ASP A 1 4026 ? 180.908 172.670 235.733 1.00 20.14 ? 4026 ASP A CG    1 
ATOM   18877 O  OD1   . ASP A 1 4026 ? 180.380 173.528 234.995 1.00 20.11 ? 4026 ASP A OD1   1 
ATOM   18878 O  OD2   . ASP A 1 4026 ? 180.439 172.356 236.846 1.00 28.61 ? 4026 ASP A OD2   1 
ATOM   18879 N  N     . LEU A 1 4027 ? 183.085 174.421 232.624 1.00 12.88 ? 4027 LEU A N     1 
ATOM   18880 C  CA    . LEU A 1 4027 ? 183.602 175.774 232.453 1.00 9.86  ? 4027 LEU A CA    1 
ATOM   18881 C  C     . LEU A 1 4027 ? 182.742 176.806 233.173 1.00 14.65 ? 4027 LEU A C     1 
ATOM   18882 O  O     . LEU A 1 4027 ? 183.245 177.868 233.554 1.00 17.97 ? 4027 LEU A O     1 
ATOM   18883 C  CB    . LEU A 1 4027 ? 183.700 176.104 230.964 1.00 9.11  ? 4027 LEU A CB    1 
ATOM   18884 C  CG    . LEU A 1 4027 ? 184.832 177.035 230.532 1.00 15.37 ? 4027 LEU A CG    1 
ATOM   18885 C  CD1   . LEU A 1 4027 ? 186.178 176.405 230.823 1.00 12.18 ? 4027 LEU A CD1   1 
ATOM   18886 C  CD2   . LEU A 1 4027 ? 184.706 177.366 229.054 1.00 11.92 ? 4027 LEU A CD2   1 
ATOM   18887 N  N     . THR A 1 4028 ? 181.457 176.509 233.373 1.00 11.88 ? 4028 THR A N     1 
ATOM   18888 C  CA    . THR A 1 4028 ? 180.570 177.457 234.039 1.00 13.95 ? 4028 THR A CA    1 
ATOM   18889 C  C     . THR A 1 4028 ? 180.992 177.689 235.485 1.00 14.83 ? 4028 THR A C     1 
ATOM   18890 O  O     . THR A 1 4028 ? 181.131 178.834 235.929 1.00 19.04 ? 4028 THR A O     1 
ATOM   18891 C  CB    . THR A 1 4028 ? 179.128 176.952 233.982 1.00 14.30 ? 4028 THR A CB    1 
ATOM   18892 O  OG1   . THR A 1 4028 ? 178.722 176.813 232.614 1.00 16.75 ? 4028 THR A OG1   1 
ATOM   18893 C  CG2   . THR A 1 4028 ? 178.195 177.917 234.692 1.00 10.28 ? 4028 THR A CG2   1 
ATOM   18894 N  N     . HIS A 1 4029 ? 181.199 176.607 236.237 1.00 14.90 ? 4029 HIS A N     1 
ATOM   18895 C  CA    . HIS A 1 4029 ? 181.524 176.740 237.651 1.00 14.10 ? 4029 HIS A CA    1 
ATOM   18896 C  C     . HIS A 1 4029 ? 182.894 177.376 237.855 1.00 12.56 ? 4029 HIS A C     1 
ATOM   18897 O  O     . HIS A 1 4029 ? 183.071 178.210 238.749 1.00 13.73 ? 4029 HIS A O     1 
ATOM   18898 C  CB    . HIS A 1 4029 ? 181.460 175.373 238.332 1.00 18.48 ? 4029 HIS A CB    1 
ATOM   18899 C  CG    . HIS A 1 4029 ? 181.818 175.406 239.784 1.00 17.10 ? 4029 HIS A CG    1 
ATOM   18900 N  ND1   . HIS A 1 4029 ? 181.390 176.404 240.632 1.00 14.45 ? 4029 HIS A ND1   1 
ATOM   18901 C  CD2   . HIS A 1 4029 ? 182.570 174.567 240.536 1.00 17.43 ? 4029 HIS A CD2   1 
ATOM   18902 C  CE1   . HIS A 1 4029 ? 181.858 176.176 241.847 1.00 18.35 ? 4029 HIS A CE1   1 
ATOM   18903 N  NE2   . HIS A 1 4029 ? 182.578 175.069 241.816 1.00 23.78 ? 4029 HIS A NE2   1 
ATOM   18904 N  N     . ILE A 1 4030 ? 183.875 176.993 237.037 1.00 14.22 ? 4030 ILE A N     1 
ATOM   18905 C  CA    . ILE A 1 4030 ? 185.235 177.486 237.228 1.00 14.39 ? 4030 ILE A CA    1 
ATOM   18906 C  C     . ILE A 1 4030 ? 185.323 178.978 236.936 1.00 9.95  ? 4030 ILE A C     1 
ATOM   18907 O  O     . ILE A 1 4030 ? 185.931 179.736 237.701 1.00 11.74 ? 4030 ILE A O     1 
ATOM   18908 C  CB    . ILE A 1 4030 ? 186.219 176.682 236.359 1.00 9.20  ? 4030 ILE A CB    1 
ATOM   18909 C  CG1   . ILE A 1 4030 ? 186.082 175.186 236.650 1.00 4.08  ? 4030 ILE A CG1   1 
ATOM   18910 C  CG2   . ILE A 1 4030 ? 187.637 177.154 236.601 1.00 8.59  ? 4030 ILE A CG2   1 
ATOM   18911 C  CD1   . ILE A 1 4030 ? 186.929 174.312 235.768 1.00 5.98  ? 4030 ILE A CD1   1 
ATOM   18912 N  N     . VAL A 1 4031 ? 184.726 179.427 235.832 1.00 12.04 ? 4031 VAL A N     1 
ATOM   18913 C  CA    . VAL A 1 4031 ? 184.813 180.837 235.465 1.00 8.82  ? 4031 VAL A CA    1 
ATOM   18914 C  C     . VAL A 1 4031 ? 184.058 181.701 236.469 1.00 8.34  ? 4031 VAL A C     1 
ATOM   18915 O  O     . VAL A 1 4031 ? 184.507 182.795 236.827 1.00 15.27 ? 4031 VAL A O     1 
ATOM   18916 C  CB    . VAL A 1 4031 ? 184.301 181.046 234.026 1.00 10.45 ? 4031 VAL A CB    1 
ATOM   18917 C  CG1   . VAL A 1 4031 ? 184.102 182.526 233.730 1.00 10.44 ? 4031 VAL A CG1   1 
ATOM   18918 C  CG2   . VAL A 1 4031 ? 185.269 180.433 233.031 1.00 4.90  ? 4031 VAL A CG2   1 
ATOM   18919 N  N     . GLY A 1 4032 ? 182.908 181.221 236.949 1.00 10.46 ? 4032 GLY A N     1 
ATOM   18920 C  CA    . GLY A 1 4032 ? 182.098 182.022 237.848 1.00 10.53 ? 4032 GLY A CA    1 
ATOM   18921 C  C     . GLY A 1 4032 ? 182.609 182.109 239.270 1.00 15.31 ? 4032 GLY A C     1 
ATOM   18922 O  O     . GLY A 1 4032 ? 182.303 183.075 239.974 1.00 20.02 ? 4032 GLY A O     1 
ATOM   18923 N  N     . THR A 1 4033 ? 183.380 181.122 239.720 1.00 16.96 ? 4033 THR A N     1 
ATOM   18924 C  CA    . THR A 1 4033 ? 183.782 181.062 241.120 1.00 12.12 ? 4033 THR A CA    1 
ATOM   18925 C  C     . THR A 1 4033 ? 185.285 180.986 241.334 1.00 11.82 ? 4033 THR A C     1 
ATOM   18926 O  O     . THR A 1 4033 ? 185.793 181.579 242.290 1.00 18.74 ? 4033 THR A O     1 
ATOM   18927 C  CB    . THR A 1 4033 ? 183.121 179.858 241.814 1.00 15.35 ? 4033 THR A CB    1 
ATOM   18928 O  OG1   . THR A 1 4033 ? 183.545 178.644 241.180 1.00 19.76 ? 4033 THR A OG1   1 
ATOM   18929 C  CG2   . THR A 1 4033 ? 181.608 179.961 241.749 1.00 17.42 ? 4033 THR A CG2   1 
ATOM   18930 N  N     . GLU A 1 4034 ? 186.016 180.272 240.482 1.00 11.21 ? 4034 GLU A N     1 
ATOM   18931 C  CA    . GLU A 1 4034 ? 187.430 180.025 240.734 1.00 8.28  ? 4034 GLU A CA    1 
ATOM   18932 C  C     . GLU A 1 4034 ? 188.357 181.022 240.052 1.00 9.51  ? 4034 GLU A C     1 
ATOM   18933 O  O     . GLU A 1 4034 ? 189.511 181.158 240.475 1.00 13.38 ? 4034 GLU A O     1 
ATOM   18934 C  CB    . GLU A 1 4034 ? 187.808 178.610 240.289 1.00 8.27  ? 4034 GLU A CB    1 
ATOM   18935 C  CG    . GLU A 1 4034 ? 187.170 177.503 241.107 1.00 10.94 ? 4034 GLU A CG    1 
ATOM   18936 C  CD    . GLU A 1 4034 ? 187.556 176.119 240.620 1.00 14.83 ? 4034 GLU A CD    1 
ATOM   18937 O  OE1   . GLU A 1 4034 ? 188.221 176.022 239.570 1.00 13.73 ? 4034 GLU A OE1   1 
ATOM   18938 O  OE2   . GLU A 1 4034 ? 187.193 175.128 241.285 1.00 25.10 ? 4034 GLU A OE2   1 
ATOM   18939 N  N     . VAL A 1 4035 ? 187.897 181.718 239.019 1.00 11.60 ? 4035 VAL A N     1 
ATOM   18940 C  CA    . VAL A 1 4035 ? 188.752 182.591 238.223 1.00 8.56  ? 4035 VAL A CA    1 
ATOM   18941 C  C     . VAL A 1 4035 ? 188.550 184.030 238.677 1.00 7.42  ? 4035 VAL A C     1 
ATOM   18942 O  O     . VAL A 1 4035 ? 187.418 184.527 238.714 1.00 10.23 ? 4035 VAL A O     1 
ATOM   18943 C  CB    . VAL A 1 4035 ? 188.466 182.439 236.721 1.00 4.86  ? 4035 VAL A CB    1 
ATOM   18944 C  CG1   . VAL A 1 4035 ? 189.142 183.551 235.939 1.00 5.06  ? 4035 VAL A CG1   1 
ATOM   18945 C  CG2   . VAL A 1 4035 ? 188.934 181.080 236.232 1.00 5.57  ? 4035 VAL A CG2   1 
ATOM   18946 N  N     . LYS A 1 4036 ? 189.643 184.692 239.031 1.00 6.64  ? 4036 LYS A N     1 
ATOM   18947 C  CA    . LYS A 1 4036 ? 189.605 186.108 239.347 1.00 7.62  ? 4036 LYS A CA    1 
ATOM   18948 C  C     . LYS A 1 4036 ? 189.525 186.928 238.062 1.00 5.63  ? 4036 LYS A C     1 
ATOM   18949 O  O     . LYS A 1 4036 ? 190.045 186.517 237.022 1.00 8.00  ? 4036 LYS A O     1 
ATOM   18950 C  CB    . LYS A 1 4036 ? 190.843 186.510 240.137 1.00 8.18  ? 4036 LYS A CB    1 
ATOM   18951 C  CG    . LYS A 1 4036 ? 190.982 185.800 241.468 1.00 9.02  ? 4036 LYS A CG    1 
ATOM   18952 C  CD    . LYS A 1 4036 ? 189.918 186.234 242.453 1.00 9.13  ? 4036 LYS A CD    1 
ATOM   18953 C  CE    . LYS A 1 4036 ? 190.074 185.501 243.774 1.00 21.95 ? 4036 LYS A CE    1 
ATOM   18954 N  NZ    . LYS A 1 4036 ? 191.313 185.907 244.490 1.00 19.75 ? 4036 LYS A NZ    1 
ATOM   18955 N  N     . PRO A 1 4037 ? 188.869 188.091 238.105 1.00 5.86  ? 4037 PRO A N     1 
ATOM   18956 C  CA    . PRO A 1 4037 ? 188.774 188.919 236.890 1.00 4.69  ? 4037 PRO A CA    1 
ATOM   18957 C  C     . PRO A 1 4037 ? 190.122 189.345 236.338 1.00 5.32  ? 4037 PRO A C     1 
ATOM   18958 O  O     . PRO A 1 4037 ? 190.272 189.456 235.115 1.00 9.28  ? 4037 PRO A O     1 
ATOM   18959 C  CB    . PRO A 1 4037 ? 187.938 190.124 237.349 1.00 5.13  ? 4037 PRO A CB    1 
ATOM   18960 C  CG    . PRO A 1 4037 ? 187.998 190.104 238.842 1.00 7.92  ? 4037 PRO A CG    1 
ATOM   18961 C  CD    . PRO A 1 4037 ? 188.132 188.674 239.236 1.00 5.21  ? 4037 PRO A CD    1 
ATOM   18962 N  N     . ASN A 1 4038 ? 191.112 189.582 237.199 1.00 7.13  ? 4038 ASN A N     1 
ATOM   18963 C  CA    . ASN A 1 4038 ? 192.447 189.939 236.735 1.00 6.94  ? 4038 ASN A CA    1 
ATOM   18964 C  C     . ASN A 1 4038 ? 193.197 188.758 236.135 1.00 4.50  ? 4038 ASN A C     1 
ATOM   18965 O  O     . ASN A 1 4038 ? 194.226 188.967 235.483 1.00 4.56  ? 4038 ASN A O     1 
ATOM   18966 C  CB    . ASN A 1 4038 ? 193.262 190.530 237.888 1.00 7.71  ? 4038 ASN A CB    1 
ATOM   18967 C  CG    . ASN A 1 4038 ? 193.294 189.621 239.101 1.00 19.60 ? 4038 ASN A CG    1 
ATOM   18968 O  OD1   . ASN A 1 4038 ? 194.184 188.781 239.239 1.00 18.25 ? 4038 ASN A OD1   1 
ATOM   18969 N  ND2   . ASN A 1 4038 ? 192.319 189.780 239.988 1.00 15.21 ? 4038 ASN A ND2   1 
ATOM   18970 N  N     . THR A 1 4039 ? 192.716 187.534 236.337 1.00 3.75  ? 4039 THR A N     1 
ATOM   18971 C  CA    . THR A 1 4039 ? 193.399 186.350 235.837 1.00 3.09  ? 4039 THR A CA    1 
ATOM   18972 C  C     . THR A 1 4039 ? 192.838 185.968 234.475 1.00 3.02  ? 4039 THR A C     1 
ATOM   18973 O  O     . THR A 1 4039 ? 191.648 185.638 234.380 1.00 8.32  ? 4039 THR A O     1 
ATOM   18974 C  CB    . THR A 1 4039 ? 193.239 185.192 236.806 1.00 3.29  ? 4039 THR A CB    1 
ATOM   18975 O  OG1   . THR A 1 4039 ? 193.880 185.512 238.048 1.00 10.34 ? 4039 THR A OG1   1 
ATOM   18976 C  CG2   . THR A 1 4039 ? 193.859 183.930 236.236 1.00 1.62  ? 4039 THR A CG2   1 
ATOM   18977 N  N     . PRO A 1 4040 ? 193.633 186.003 233.411 1.00 1.06  ? 4040 PRO A N     1 
ATOM   18978 C  CA    . PRO A 1 4040 ? 193.139 185.539 232.111 1.00 0.37  ? 4040 PRO A CA    1 
ATOM   18979 C  C     . PRO A 1 4040 ? 192.882 184.041 232.118 1.00 0.39  ? 4040 PRO A C     1 
ATOM   18980 O  O     . PRO A 1 4040 ? 193.533 183.275 232.833 1.00 0.34  ? 4040 PRO A O     1 
ATOM   18981 C  CB    . PRO A 1 4040 ? 194.274 185.905 231.150 1.00 0.25  ? 4040 PRO A CB    1 
ATOM   18982 C  CG    . PRO A 1 4040 ? 195.486 185.966 232.006 1.00 0.36  ? 4040 PRO A CG    1 
ATOM   18983 C  CD    . PRO A 1 4040 ? 195.027 186.471 233.341 1.00 0.71  ? 4040 PRO A CD    1 
ATOM   18984 N  N     . VAL A 1 4041 ? 191.913 183.626 231.310 1.00 0.53  ? 4041 VAL A N     1 
ATOM   18985 C  CA    . VAL A 1 4041 ? 191.582 182.218 231.149 1.00 0.24  ? 4041 VAL A CA    1 
ATOM   18986 C  C     . VAL A 1 4041 ? 192.220 181.749 229.849 1.00 0.24  ? 4041 VAL A C     1 
ATOM   18987 O  O     . VAL A 1 4041 ? 191.794 182.143 228.758 1.00 0.31  ? 4041 VAL A O     1 
ATOM   18988 C  CB    . VAL A 1 4041 ? 190.066 181.984 231.146 1.00 0.33  ? 4041 VAL A CB    1 
ATOM   18989 C  CG1   . VAL A 1 4041 ? 189.770 180.512 230.974 1.00 0.28  ? 4041 VAL A CG1   1 
ATOM   18990 C  CG2   . VAL A 1 4041 ? 189.444 182.514 232.425 1.00 0.96  ? 4041 VAL A CG2   1 
ATOM   18991 N  N     . LEU A 1 4042 ? 193.237 180.902 229.959 1.00 0.36  ? 4042 LEU A N     1 
ATOM   18992 C  CA    . LEU A 1 4042 ? 193.997 180.445 228.804 1.00 0.46  ? 4042 LEU A CA    1 
ATOM   18993 C  C     . LEU A 1 4042 ? 193.365 179.173 228.252 1.00 0.61  ? 4042 LEU A C     1 
ATOM   18994 O  O     . LEU A 1 4042 ? 193.330 178.144 228.933 1.00 0.57  ? 4042 LEU A O     1 
ATOM   18995 C  CB    . LEU A 1 4042 ? 195.459 180.209 229.179 1.00 0.44  ? 4042 LEU A CB    1 
ATOM   18996 C  CG    . LEU A 1 4042 ? 196.131 181.316 229.998 1.00 0.68  ? 4042 LEU A CG    1 
ATOM   18997 C  CD1   . LEU A 1 4042 ? 197.595 180.998 230.236 1.00 0.83  ? 4042 LEU A CD1   1 
ATOM   18998 C  CD2   . LEU A 1 4042 ? 195.978 182.673 229.324 1.00 0.24  ? 4042 LEU A CD2   1 
ATOM   18999 N  N     . MET A 1 4043 ? 192.867 179.249 227.022 1.00 1.42  ? 4043 MET A N     1 
ATOM   19000 C  CA    . MET A 1 4043 ? 192.244 178.114 226.344 1.00 0.78  ? 4043 MET A CA    1 
ATOM   19001 C  C     . MET A 1 4043 ? 193.299 177.507 225.424 1.00 0.91  ? 4043 MET A C     1 
ATOM   19002 O  O     . MET A 1 4043 ? 193.408 177.868 224.253 1.00 1.91  ? 4043 MET A O     1 
ATOM   19003 C  CB    . MET A 1 4043 ? 191.010 178.554 225.566 1.00 1.36  ? 4043 MET A CB    1 
ATOM   19004 C  CG    . MET A 1 4043 ? 189.852 179.083 226.401 1.00 0.78  ? 4043 MET A CG    1 
ATOM   19005 S  SD    . MET A 1 4043 ? 189.135 177.862 227.507 1.00 33.78 ? 4043 MET A SD    1 
ATOM   19006 C  CE    . MET A 1 4043 ? 188.005 178.861 228.458 1.00 18.30 ? 4043 MET A CE    1 
ATOM   19007 N  N     . CYS A 1 4044 ? 194.090 176.584 225.965 1.00 1.05  ? 4044 CYS A N     1 
ATOM   19008 C  CA    . CYS A 1 4044 ? 195.164 175.938 225.223 1.00 0.59  ? 4044 CYS A CA    1 
ATOM   19009 C  C     . CYS A 1 4044 ? 194.656 174.631 224.630 1.00 0.71  ? 4044 CYS A C     1 
ATOM   19010 O  O     . CYS A 1 4044 ? 194.083 173.803 225.345 1.00 1.04  ? 4044 CYS A O     1 
ATOM   19011 C  CB    . CYS A 1 4044 ? 196.371 175.674 226.123 1.00 0.81  ? 4044 CYS A CB    1 
ATOM   19012 S  SG    . CYS A 1 4044 ? 196.901 177.083 227.116 1.00 6.85  ? 4044 CYS A SG    1 
ATOM   19013 N  N     . SER A 1 4045 ? 194.870 174.446 223.333 1.00 1.00  ? 4045 SER A N     1 
ATOM   19014 C  CA    . SER A 1 4045 ? 194.352 173.281 222.636 1.00 1.65  ? 4045 SER A CA    1 
ATOM   19015 C  C     . SER A 1 4045 ? 195.424 172.672 221.745 1.00 1.51  ? 4045 SER A C     1 
ATOM   19016 O  O     . SER A 1 4045 ? 196.308 173.368 221.239 1.00 1.80  ? 4045 SER A O     1 
ATOM   19017 C  CB    . SER A 1 4045 ? 193.116 173.638 221.799 1.00 1.27  ? 4045 SER A CB    1 
ATOM   19018 O  OG    . SER A 1 4045 ? 193.415 174.642 220.852 1.00 5.16  ? 4045 SER A OG    1 
ATOM   19019 N  N     . VAL A 1 4046 ? 195.336 171.358 221.574 1.00 2.22  ? 4046 VAL A N     1 
ATOM   19020 C  CA    . VAL A 1 4046 ? 196.180 170.625 220.634 1.00 4.55  ? 4046 VAL A CA    1 
ATOM   19021 C  C     . VAL A 1 4046 ? 195.653 170.888 219.228 1.00 5.11  ? 4046 VAL A C     1 
ATOM   19022 O  O     . VAL A 1 4046 ? 194.496 171.308 219.078 1.00 6.92  ? 4046 VAL A O     1 
ATOM   19023 C  CB    . VAL A 1 4046 ? 196.204 169.124 220.967 1.00 4.23  ? 4046 VAL A CB    1 
ATOM   19024 C  CG1   . VAL A 1 4046 ? 196.697 168.907 222.391 1.00 1.34  ? 4046 VAL A CG1   1 
ATOM   19025 C  CG2   . VAL A 1 4046 ? 194.826 168.517 220.774 1.00 4.84  ? 4046 VAL A CG2   1 
ATOM   19026 N  N     . PRO A 1 4047 ? 196.452 170.677 218.181 1.00 6.02  ? 4047 PRO A N     1 
ATOM   19027 C  CA    . PRO A 1 4047 ? 195.971 170.953 216.822 1.00 5.31  ? 4047 PRO A CA    1 
ATOM   19028 C  C     . PRO A 1 4047 ? 194.711 170.166 216.490 1.00 8.70  ? 4047 PRO A C     1 
ATOM   19029 O  O     . PRO A 1 4047 ? 194.576 168.991 216.840 1.00 14.05 ? 4047 PRO A O     1 
ATOM   19030 C  CB    . PRO A 1 4047 ? 197.149 170.524 215.945 1.00 7.29  ? 4047 PRO A CB    1 
ATOM   19031 C  CG    . PRO A 1 4047 ? 198.336 170.752 216.810 1.00 9.24  ? 4047 PRO A CG    1 
ATOM   19032 C  CD    . PRO A 1 4047 ? 197.894 170.377 218.198 1.00 6.69  ? 4047 PRO A CD    1 
ATOM   19033 N  N     . GLY A 1 4048 ? 193.790 170.830 215.799 1.00 12.00 ? 4048 GLY A N     1 
ATOM   19034 C  CA    . GLY A 1 4048 ? 192.494 170.267 215.494 1.00 10.70 ? 4048 GLY A CA    1 
ATOM   19035 C  C     . GLY A 1 4048 ? 191.424 170.553 216.520 1.00 11.02 ? 4048 GLY A C     1 
ATOM   19036 O  O     . GLY A 1 4048 ? 190.247 170.271 216.262 1.00 13.22 ? 4048 GLY A O     1 
ATOM   19037 N  N     . TYR A 1 4049 ? 191.787 171.110 217.670 1.00 8.49  ? 4049 TYR A N     1 
ATOM   19038 C  CA    . TYR A 1 4049 ? 190.843 171.451 218.721 1.00 5.81  ? 4049 TYR A CA    1 
ATOM   19039 C  C     . TYR A 1 4049 ? 190.908 172.946 218.985 1.00 10.92 ? 4049 TYR A C     1 
ATOM   19040 O  O     . TYR A 1 4049 ? 191.968 173.568 218.874 1.00 11.51 ? 4049 TYR A O     1 
ATOM   19041 C  CB    . TYR A 1 4049 ? 191.122 170.650 220.002 1.00 5.97  ? 4049 TYR A CB    1 
ATOM   19042 C  CG    . TYR A 1 4049 ? 190.718 169.197 219.882 1.00 7.55  ? 4049 TYR A CG    1 
ATOM   19043 C  CD1   . TYR A 1 4049 ? 191.395 168.336 219.027 1.00 5.81  ? 4049 TYR A CD1   1 
ATOM   19044 C  CD2   . TYR A 1 4049 ? 189.648 168.691 220.605 1.00 3.06  ? 4049 TYR A CD2   1 
ATOM   19045 C  CE1   . TYR A 1 4049 ? 191.020 167.018 218.897 1.00 6.49  ? 4049 TYR A CE1   1 
ATOM   19046 C  CE2   . TYR A 1 4049 ? 189.267 167.369 220.485 1.00 4.41  ? 4049 TYR A CE2   1 
ATOM   19047 C  CZ    . TYR A 1 4049 ? 189.959 166.538 219.630 1.00 8.36  ? 4049 TYR A CZ    1 
ATOM   19048 O  OH    . TYR A 1 4049 ? 189.588 165.220 219.504 1.00 8.00  ? 4049 TYR A OH    1 
ATOM   19049 N  N     . ASP A 1 4050 ? 189.756 173.524 219.309 1.00 11.61 ? 4050 ASP A N     1 
ATOM   19050 C  CA    . ASP A 1 4050 ? 189.646 174.965 219.488 1.00 11.03 ? 4050 ASP A CA    1 
ATOM   19051 C  C     . ASP A 1 4050 ? 188.527 175.230 220.480 1.00 8.03  ? 4050 ASP A C     1 
ATOM   19052 O  O     . ASP A 1 4050 ? 187.386 174.818 220.253 1.00 7.78  ? 4050 ASP A O     1 
ATOM   19053 C  CB    . ASP A 1 4050 ? 189.375 175.663 218.151 1.00 8.29  ? 4050 ASP A CB    1 
ATOM   19054 C  CG    . ASP A 1 4050 ? 188.918 177.096 218.318 1.00 15.20 ? 4050 ASP A CG    1 
ATOM   19055 O  OD1   . ASP A 1 4050 ? 189.671 177.896 218.912 1.00 14.92 ? 4050 ASP A OD1   1 
ATOM   19056 O  OD2   . ASP A 1 4050 ? 187.807 177.423 217.852 1.00 15.59 ? 4050 ASP A OD2   1 
ATOM   19057 N  N     . ALA A 1 4051 ? 188.856 175.911 221.574 1.00 7.02  ? 4051 ALA A N     1 
ATOM   19058 C  CA    . ALA A 1 4051 ? 187.924 176.142 222.667 1.00 6.66  ? 4051 ALA A CA    1 
ATOM   19059 C  C     . ALA A 1 4051 ? 187.107 177.413 222.489 1.00 5.65  ? 4051 ALA A C     1 
ATOM   19060 O  O     . ALA A 1 4051 ? 186.344 177.773 223.391 1.00 7.95  ? 4051 ALA A O     1 
ATOM   19061 C  CB    . ALA A 1 4051 ? 188.678 176.192 223.997 1.00 4.36  ? 4051 ALA A CB    1 
ATOM   19062 N  N     . SER A 1 4052 ? 187.250 178.097 221.352 1.00 5.69  ? 4052 SER A N     1 
ATOM   19063 C  CA    . SER A 1 4052 ? 186.519 179.341 221.136 1.00 7.08  ? 4052 SER A CA    1 
ATOM   19064 C  C     . SER A 1 4052 ? 185.015 179.111 221.176 1.00 8.99  ? 4052 SER A C     1 
ATOM   19065 O  O     . SER A 1 4052 ? 184.273 179.908 221.759 1.00 5.02  ? 4052 SER A O     1 
ATOM   19066 C  CB    . SER A 1 4052 ? 186.929 179.963 219.801 1.00 9.21  ? 4052 SER A CB    1 
ATOM   19067 O  OG    . SER A 1 4052 ? 188.338 179.961 219.651 1.00 9.31  ? 4052 SER A OG    1 
ATOM   19068 N  N     . GLY A 1 4053 ? 184.549 178.019 220.565 1.00 7.18  ? 4053 GLY A N     1 
ATOM   19069 C  CA    . GLY A 1 4053 ? 183.127 177.720 220.586 1.00 5.11  ? 4053 GLY A CA    1 
ATOM   19070 C  C     . GLY A 1 4053 ? 182.596 177.479 221.985 1.00 10.18 ? 4053 GLY A C     1 
ATOM   19071 O  O     . GLY A 1 4053 ? 181.484 177.897 222.315 1.00 13.63 ? 4053 GLY A O     1 
ATOM   19072 N  N     . HIS A 1 4054 ? 183.384 176.807 222.829 1.00 7.53  ? 4054 HIS A N     1 
ATOM   19073 C  CA    . HIS A 1 4054 ? 182.952 176.564 224.203 1.00 8.65  ? 4054 HIS A CA    1 
ATOM   19074 C  C     . HIS A 1 4054 ? 182.730 177.873 224.950 1.00 9.33  ? 4054 HIS A C     1 
ATOM   19075 O  O     . HIS A 1 4054 ? 181.748 178.015 225.688 1.00 15.14 ? 4054 HIS A O     1 
ATOM   19076 C  CB    . HIS A 1 4054 ? 183.977 175.699 224.937 1.00 6.72  ? 4054 HIS A CB    1 
ATOM   19077 C  CG    . HIS A 1 4054 ? 184.344 174.446 224.207 1.00 15.32 ? 4054 HIS A CG    1 
ATOM   19078 N  ND1   . HIS A 1 4054 ? 183.415 173.667 223.554 1.00 22.85 ? 4054 HIS A ND1   1 
ATOM   19079 C  CD2   . HIS A 1 4054 ? 185.540 173.839 224.025 1.00 14.10 ? 4054 HIS A CD2   1 
ATOM   19080 C  CE1   . HIS A 1 4054 ? 184.023 172.631 223.003 1.00 21.62 ? 4054 HIS A CE1   1 
ATOM   19081 N  NE2   . HIS A 1 4054 ? 185.312 172.711 223.274 1.00 15.59 ? 4054 HIS A NE2   1 
ATOM   19082 N  N     . VAL A 1 4055 ? 183.634 178.839 224.775 1.00 5.23  ? 4055 VAL A N     1 
ATOM   19083 C  CA    . VAL A 1 4055 ? 183.456 180.143 225.405 1.00 8.16  ? 4055 VAL A CA    1 
ATOM   19084 C  C     . VAL A 1 4055 ? 182.223 180.841 224.849 1.00 6.88  ? 4055 VAL A C     1 
ATOM   19085 O  O     . VAL A 1 4055 ? 181.436 181.433 225.595 1.00 7.08  ? 4055 VAL A O     1 
ATOM   19086 C  CB    . VAL A 1 4055 ? 184.721 181.002 225.224 1.00 6.16  ? 4055 VAL A CB    1 
ATOM   19087 C  CG1   . VAL A 1 4055 ? 184.578 182.316 225.972 1.00 1.50  ? 4055 VAL A CG1   1 
ATOM   19088 C  CG2   . VAL A 1 4055 ? 185.951 180.244 225.692 1.00 4.86  ? 4055 VAL A CG2   1 
ATOM   19089 N  N     . GLU A 1 4056 ? 182.036 180.782 223.528 1.00 10.41 ? 4056 GLU A N     1 
ATOM   19090 C  CA    . GLU A 1 4056 ? 180.872 181.405 222.908 1.00 9.99  ? 4056 GLU A CA    1 
ATOM   19091 C  C     . GLU A 1 4056 ? 179.578 180.793 223.423 1.00 12.17 ? 4056 GLU A C     1 
ATOM   19092 O  O     . GLU A 1 4056 ? 178.610 181.510 223.707 1.00 14.21 ? 4056 GLU A O     1 
ATOM   19093 C  CB    . GLU A 1 4056 ? 180.966 181.275 221.389 1.00 8.14  ? 4056 GLU A CB    1 
ATOM   19094 C  CG    . GLU A 1 4056 ? 182.105 182.072 220.782 1.00 11.70 ? 4056 GLU A CG    1 
ATOM   19095 C  CD    . GLU A 1 4056 ? 182.198 181.913 219.280 1.00 16.63 ? 4056 GLU A CD    1 
ATOM   19096 O  OE1   . GLU A 1 4056 ? 181.453 181.081 218.718 1.00 14.57 ? 4056 GLU A OE1   1 
ATOM   19097 O  OE2   . GLU A 1 4056 ? 183.027 182.613 218.662 1.00 19.81 ? 4056 GLU A OE2   1 
ATOM   19098 N  N     . ASP A 1 4057 ? 179.538 179.465 223.547 1.00 11.26 ? 4057 ASP A N     1 
ATOM   19099 C  CA    . ASP A 1 4057 ? 178.368 178.813 224.127 1.00 13.64 ? 4057 ASP A CA    1 
ATOM   19100 C  C     . ASP A 1 4057 ? 178.210 179.176 225.599 1.00 14.11 ? 4057 ASP A C     1 
ATOM   19101 O  O     . ASP A 1 4057 ? 177.090 179.395 226.072 1.00 18.23 ? 4057 ASP A O     1 
ATOM   19102 C  CB    . ASP A 1 4057 ? 178.468 177.298 223.956 1.00 12.67 ? 4057 ASP A CB    1 
ATOM   19103 C  CG    . ASP A 1 4057 ? 178.630 176.887 222.508 1.00 18.89 ? 4057 ASP A CG    1 
ATOM   19104 O  OD1   . ASP A 1 4057 ? 177.978 177.497 221.638 1.00 21.54 ? 4057 ASP A OD1   1 
ATOM   19105 O  OD2   . ASP A 1 4057 ? 179.409 175.948 222.241 1.00 22.48 ? 4057 ASP A OD2   1 
ATOM   19106 N  N     . LEU A 1 4058 ? 179.323 179.254 226.332 1.00 13.04 ? 4058 LEU A N     1 
ATOM   19107 C  CA    . LEU A 1 4058 ? 179.262 179.580 227.752 1.00 12.48 ? 4058 LEU A CA    1 
ATOM   19108 C  C     . LEU A 1 4058 ? 178.663 180.962 227.978 1.00 15.72 ? 4058 LEU A C     1 
ATOM   19109 O  O     . LEU A 1 4058 ? 177.879 181.163 228.912 1.00 16.85 ? 4058 LEU A O     1 
ATOM   19110 C  CB    . LEU A 1 4058 ? 180.659 179.497 228.366 1.00 13.05 ? 4058 LEU A CB    1 
ATOM   19111 C  CG    . LEU A 1 4058 ? 180.831 180.088 229.766 1.00 17.12 ? 4058 LEU A CG    1 
ATOM   19112 C  CD1   . LEU A 1 4058 ? 180.059 179.275 230.793 1.00 7.09  ? 4058 LEU A CD1   1 
ATOM   19113 C  CD2   . LEU A 1 4058 ? 182.303 180.176 230.132 1.00 10.96 ? 4058 LEU A CD2   1 
ATOM   19114 N  N     . ALA A 1 4059 ? 179.029 181.932 227.137 1.00 14.15 ? 4059 ALA A N     1 
ATOM   19115 C  CA    . ALA A 1 4059 ? 178.444 183.263 227.249 1.00 12.02 ? 4059 ALA A CA    1 
ATOM   19116 C  C     . ALA A 1 4059 ? 176.947 183.232 226.971 1.00 17.47 ? 4059 ALA A C     1 
ATOM   19117 O  O     . ALA A 1 4059 ? 176.175 183.961 227.603 1.00 15.78 ? 4059 ALA A O     1 
ATOM   19118 C  CB    . ALA A 1 4059 ? 179.154 184.228 226.300 1.00 7.00  ? 4059 ALA A CB    1 
ATOM   19119 N  N     . ALA A 1 4060 ? 176.520 182.399 226.019 1.00 16.19 ? 4060 ALA A N     1 
ATOM   19120 C  CA    . ALA A 1 4060 ? 175.096 182.275 225.729 1.00 16.53 ? 4060 ALA A CA    1 
ATOM   19121 C  C     . ALA A 1 4060 ? 174.330 181.699 226.915 1.00 19.58 ? 4060 ALA A C     1 
ATOM   19122 O  O     . ALA A 1 4060 ? 173.240 182.180 227.250 1.00 24.13 ? 4060 ALA A O     1 
ATOM   19123 C  CB    . ALA A 1 4060 ? 174.889 181.410 224.487 1.00 13.79 ? 4060 ALA A CB    1 
ATOM   19124 N  N     . GLU A 1 4061 ? 174.884 180.672 227.566 1.00 17.94 ? 4061 GLU A N     1 
ATOM   19125 C  CA    . GLU A 1 4061 ? 174.218 180.079 228.723 1.00 19.93 ? 4061 GLU A CA    1 
ATOM   19126 C  C     . GLU A 1 4061 ? 174.054 181.097 229.842 1.00 20.35 ? 4061 GLU A C     1 
ATOM   19127 O  O     . GLU A 1 4061 ? 172.980 181.208 230.448 1.00 29.14 ? 4061 GLU A O     1 
ATOM   19128 C  CB    . GLU A 1 4061 ? 175.004 178.865 229.221 1.00 23.86 ? 4061 GLU A CB    1 
ATOM   19129 C  CG    . GLU A 1 4061 ? 175.337 177.840 228.151 1.00 21.35 ? 4061 GLU A CG    1 
ATOM   19130 C  CD    . GLU A 1 4061 ? 176.641 177.118 228.427 1.00 29.84 ? 4061 GLU A CD    1 
ATOM   19131 O  OE1   . GLU A 1 4061 ? 177.269 177.401 229.470 1.00 31.13 ? 4061 GLU A OE1   1 
ATOM   19132 O  OE2   . GLU A 1 4061 ? 177.042 176.273 227.602 1.00 30.83 ? 4061 GLU A OE2   1 
ATOM   19133 N  N     . GLN A 1 4062 ? 175.109 181.858 230.126 1.00 18.42 ? 4062 GLN A N     1 
ATOM   19134 C  CA    . GLN A 1 4062 ? 175.053 182.878 231.162 1.00 22.17 ? 4062 GLN A CA    1 
ATOM   19135 C  C     . GLN A 1 4062 ? 174.293 184.120 230.723 1.00 22.95 ? 4062 GLN A C     1 
ATOM   19136 O  O     . GLN A 1 4062 ? 174.075 185.014 231.548 1.00 23.94 ? 4062 GLN A O     1 
ATOM   19137 C  CB    . GLN A 1 4062 ? 176.471 183.266 231.590 1.00 20.24 ? 4062 GLN A CB    1 
ATOM   19138 C  CG    . GLN A 1 4062 ? 177.241 182.138 232.262 1.00 14.92 ? 4062 GLN A CG    1 
ATOM   19139 C  CD    . GLN A 1 4062 ? 176.595 181.677 233.550 1.00 24.49 ? 4062 GLN A CD    1 
ATOM   19140 O  OE1   . GLN A 1 4062 ? 176.041 180.580 233.621 1.00 28.62 ? 4062 GLN A OE1   1 
ATOM   19141 N  NE2   . GLN A 1 4062 ? 176.657 182.516 234.579 1.00 30.51 ? 4062 GLN A NE2   1 
ATOM   19142 N  N     . ASN A 1 4063 ? 173.891 184.194 229.450 1.00 22.74 ? 4063 ASN A N     1 
ATOM   19143 C  CA    . ASN A 1 4063 ? 173.228 185.371 228.888 1.00 19.76 ? 4063 ASN A CA    1 
ATOM   19144 C  C     . ASN A 1 4063 ? 174.071 186.625 229.106 1.00 22.60 ? 4063 ASN A C     1 
ATOM   19145 O  O     . ASN A 1 4063 ? 173.553 187.708 229.385 1.00 32.15 ? 4063 ASN A O     1 
ATOM   19146 C  CB    . ASN A 1 4063 ? 171.819 185.549 229.460 1.00 20.16 ? 4063 ASN A CB    1 
ATOM   19147 C  CG    . ASN A 1 4063 ? 170.774 184.781 228.678 1.00 28.95 ? 4063 ASN A CG    1 
ATOM   19148 O  OD1   . ASN A 1 4063 ? 170.262 183.760 229.138 1.00 29.66 ? 4063 ASN A OD1   1 
ATOM   19149 N  ND2   . ASN A 1 4063 ? 170.454 185.268 227.484 1.00 32.38 ? 4063 ASN A ND2   1 
ATOM   19150 N  N     . THR A 1 4064 ? 175.384 186.468 228.986 1.00 17.22 ? 4064 THR A N     1 
ATOM   19151 C  CA    . THR A 1 4064 ? 176.333 187.564 229.098 1.00 13.76 ? 4064 THR A CA    1 
ATOM   19152 C  C     . THR A 1 4064 ? 176.874 187.926 227.722 1.00 18.63 ? 4064 THR A C     1 
ATOM   19153 O  O     . THR A 1 4064 ? 176.919 187.096 226.809 1.00 17.75 ? 4064 THR A O     1 
ATOM   19154 C  CB    . THR A 1 4064 ? 177.482 187.200 230.045 1.00 16.68 ? 4064 THR A CB    1 
ATOM   19155 O  OG1   . THR A 1 4064 ? 178.311 188.348 230.268 1.00 18.02 ? 4064 THR A OG1   1 
ATOM   19156 C  CG2   . THR A 1 4064 ? 178.324 186.075 229.476 1.00 14.23 ? 4064 THR A CG2   1 
ATOM   19157 N  N     . GLN A 1 4065 ? 177.271 189.184 227.575 1.00 14.40 ? 4065 GLN A N     1 
ATOM   19158 C  CA    . GLN A 1 4065 ? 177.785 189.691 226.314 1.00 15.05 ? 4065 GLN A CA    1 
ATOM   19159 C  C     . GLN A 1 4065 ? 179.286 189.459 226.233 1.00 11.67 ? 4065 GLN A C     1 
ATOM   19160 O  O     . GLN A 1 4065 ? 180.000 189.582 227.232 1.00 16.26 ? 4065 GLN A O     1 
ATOM   19161 C  CB    . GLN A 1 4065 ? 177.466 191.178 226.165 1.00 15.17 ? 4065 GLN A CB    1 
ATOM   19162 C  CG    . GLN A 1 4065 ? 175.982 191.486 226.134 1.00 16.69 ? 4065 GLN A CG    1 
ATOM   19163 C  CD    . GLN A 1 4065 ? 175.240 190.649 225.111 1.00 24.90 ? 4065 GLN A CD    1 
ATOM   19164 O  OE1   . GLN A 1 4065 ? 175.457 190.783 223.908 1.00 27.46 ? 4065 GLN A OE1   1 
ATOM   19165 N  NE2   . GLN A 1 4065 ? 174.360 189.774 225.588 1.00 22.75 ? 4065 GLN A NE2   1 
ATOM   19166 N  N     . ILE A 1 4066 ? 179.762 189.108 225.042 1.00 8.69  ? 4066 ILE A N     1 
ATOM   19167 C  CA    . ILE A 1 4066 ? 181.170 188.802 224.830 1.00 6.58  ? 4066 ILE A CA    1 
ATOM   19168 C  C     . ILE A 1 4066 ? 181.622 189.404 223.507 1.00 8.22  ? 4066 ILE A C     1 
ATOM   19169 O  O     . ILE A 1 4066 ? 180.888 189.378 222.513 1.00 14.71 ? 4066 ILE A O     1 
ATOM   19170 C  CB    . ILE A 1 4066 ? 181.432 187.280 224.871 1.00 6.44  ? 4066 ILE A CB    1 
ATOM   19171 C  CG1   . ILE A 1 4066 ? 182.920 186.984 224.662 1.00 3.98  ? 4066 ILE A CG1   1 
ATOM   19172 C  CG2   . ILE A 1 4066 ? 180.573 186.552 223.849 1.00 5.02  ? 4066 ILE A CG2   1 
ATOM   19173 C  CD1   . ILE A 1 4066 ? 183.377 185.694 225.282 1.00 2.96  ? 4066 ILE A CD1   1 
ATOM   19174 N  N     . THR A 1 4067 ? 182.830 189.960 223.501 1.00 7.13  ? 4067 THR A N     1 
ATOM   19175 C  CA    . THR A 1 4067 ? 183.469 190.475 222.299 1.00 4.94  ? 4067 THR A CA    1 
ATOM   19176 C  C     . THR A 1 4067 ? 184.605 189.531 221.925 1.00 4.32  ? 4067 THR A C     1 
ATOM   19177 O  O     . THR A 1 4067 ? 185.521 189.314 222.725 1.00 3.08  ? 4067 THR A O     1 
ATOM   19178 C  CB    . THR A 1 4067 ? 183.996 191.894 222.518 1.00 7.80  ? 4067 THR A CB    1 
ATOM   19179 O  OG1   . THR A 1 4067 ? 182.896 192.796 222.672 1.00 17.27 ? 4067 THR A OG1   1 
ATOM   19180 C  CG2   . THR A 1 4067 ? 184.849 192.341 221.337 1.00 2.02  ? 4067 THR A CG2   1 
ATOM   19181 N  N     . SER A 1 4068 ? 184.540 188.976 220.719 1.00 3.15  ? 4068 SER A N     1 
ATOM   19182 C  CA    . SER A 1 4068 ? 185.532 188.028 220.232 1.00 1.61  ? 4068 SER A CA    1 
ATOM   19183 C  C     . SER A 1 4068 ? 186.374 188.696 219.156 1.00 1.35  ? 4068 SER A C     1 
ATOM   19184 O  O     . SER A 1 4068 ? 185.834 189.321 218.237 1.00 2.21  ? 4068 SER A O     1 
ATOM   19185 C  CB    . SER A 1 4068 ? 184.863 186.770 219.675 1.00 2.83  ? 4068 SER A CB    1 
ATOM   19186 O  OG    . SER A 1 4068 ? 183.968 186.216 220.619 1.00 8.40  ? 4068 SER A OG    1 
ATOM   19187 N  N     . ILE A 1 4069 ? 187.693 188.574 219.277 1.00 1.75  ? 4069 ILE A N     1 
ATOM   19188 C  CA    . ILE A 1 4069 ? 188.632 189.234 218.380 1.00 1.04  ? 4069 ILE A CA    1 
ATOM   19189 C  C     . ILE A 1 4069 ? 189.713 188.245 217.973 1.00 0.78  ? 4069 ILE A C     1 
ATOM   19190 O  O     . ILE A 1 4069 ? 190.288 187.560 218.825 1.00 1.46  ? 4069 ILE A O     1 
ATOM   19191 C  CB    . ILE A 1 4069 ? 189.262 190.478 219.035 1.00 2.23  ? 4069 ILE A CB    1 
ATOM   19192 C  CG1   . ILE A 1 4069 ? 188.171 191.432 219.526 1.00 1.73  ? 4069 ILE A CG1   1 
ATOM   19193 C  CG2   . ILE A 1 4069 ? 190.191 191.181 218.068 1.00 1.37  ? 4069 ILE A CG2   1 
ATOM   19194 C  CD1   . ILE A 1 4069 ? 188.685 192.587 220.312 1.00 3.42  ? 4069 ILE A CD1   1 
ATOM   19195 N  N     . ALA A 1 4070 ? 189.982 188.166 216.672 1.00 1.98  ? 4070 ALA A N     1 
ATOM   19196 C  CA    . ALA A 1 4070 ? 191.186 187.514 216.179 1.00 0.93  ? 4070 ALA A CA    1 
ATOM   19197 C  C     . ALA A 1 4070 ? 192.367 188.473 216.281 1.00 3.04  ? 4070 ALA A C     1 
ATOM   19198 O  O     . ALA A 1 4070 ? 192.213 189.693 216.183 1.00 9.36  ? 4070 ALA A O     1 
ATOM   19199 C  CB    . ALA A 1 4070 ? 190.998 187.054 214.737 1.00 1.50  ? 4070 ALA A CB    1 
ATOM   19200 N  N     . ILE A 1 4071 ? 193.559 187.910 216.462 1.00 1.50  ? 4071 ILE A N     1 
ATOM   19201 C  CA    . ILE A 1 4071 ? 194.691 188.681 216.969 1.00 4.91  ? 4071 ILE A CA    1 
ATOM   19202 C  C     . ILE A 1 4071 ? 195.640 189.146 215.868 1.00 9.66  ? 4071 ILE A C     1 
ATOM   19203 O  O     . ILE A 1 4071 ? 196.276 190.199 215.993 1.00 10.07 ? 4071 ILE A O     1 
ATOM   19204 C  CB    . ILE A 1 4071 ? 195.429 187.858 218.045 1.00 2.77  ? 4071 ILE A CB    1 
ATOM   19205 C  CG1   . ILE A 1 4071 ? 194.574 187.800 219.309 1.00 3.87  ? 4071 ILE A CG1   1 
ATOM   19206 C  CG2   . ILE A 1 4071 ? 196.794 188.429 218.360 1.00 1.16  ? 4071 ILE A CG2   1 
ATOM   19207 C  CD1   . ILE A 1 4071 ? 194.069 189.155 219.753 1.00 5.29  ? 4071 ILE A CD1   1 
ATOM   19208 N  N     . GLY A 1 4072 ? 195.708 188.396 214.766 1.00 2.84  ? 4072 GLY A N     1 
ATOM   19209 C  CA    . GLY A 1 4072 ? 196.790 188.582 213.810 1.00 1.57  ? 4072 GLY A CA    1 
ATOM   19210 C  C     . GLY A 1 4072 ? 196.884 189.974 213.210 1.00 2.91  ? 4072 GLY A C     1 
ATOM   19211 O  O     . GLY A 1 4072 ? 197.986 190.474 212.972 1.00 5.69  ? 4072 GLY A O     1 
ATOM   19212 N  N     . SER A 1 4073 ? 195.749 190.612 212.945 1.00 4.21  ? 4073 SER A N     1 
ATOM   19213 C  CA    . SER A 1 4073 ? 195.758 191.906 212.274 1.00 3.05  ? 4073 SER A CA    1 
ATOM   19214 C  C     . SER A 1 4073 ? 196.283 193.008 213.189 1.00 7.65  ? 4073 SER A C     1 
ATOM   19215 O  O     . SER A 1 4073 ? 196.195 192.927 214.417 1.00 9.06  ? 4073 SER A O     1 
ATOM   19216 C  CB    . SER A 1 4073 ? 194.351 192.267 211.795 1.00 3.47  ? 4073 SER A CB    1 
ATOM   19217 O  OG    . SER A 1 4073 ? 194.299 193.591 211.300 1.00 7.93  ? 4073 SER A OG    1 
ATOM   19218 N  N     . ALA A 1 4074 ? 196.836 194.052 212.568 1.00 9.55  ? 4074 ALA A N     1 
ATOM   19219 C  CA    . ALA A 1 4074 ? 197.203 195.250 213.316 1.00 4.39  ? 4074 ALA A CA    1 
ATOM   19220 C  C     . ALA A 1 4074 ? 195.968 195.926 213.897 1.00 7.25  ? 4074 ALA A C     1 
ATOM   19221 O  O     . ALA A 1 4074 ? 196.002 196.438 215.022 1.00 15.22 ? 4074 ALA A O     1 
ATOM   19222 C  CB    . ALA A 1 4074 ? 197.977 196.216 212.423 1.00 2.82  ? 4074 ALA A CB    1 
ATOM   19223 N  N     . GLU A 1 4075 ? 194.870 195.946 213.137 1.00 5.57  ? 4075 GLU A N     1 
ATOM   19224 C  CA    . GLU A 1 4075 ? 193.612 196.464 213.664 1.00 8.43  ? 4075 GLU A CA    1 
ATOM   19225 C  C     . GLU A 1 4075 ? 193.089 195.608 214.808 1.00 7.82  ? 4075 GLU A C     1 
ATOM   19226 O  O     . GLU A 1 4075 ? 192.412 196.118 215.707 1.00 9.25  ? 4075 GLU A O     1 
ATOM   19227 C  CB    . GLU A 1 4075 ? 192.576 196.553 212.542 1.00 8.11  ? 4075 GLU A CB    1 
ATOM   19228 C  CG    . GLU A 1 4075 ? 191.232 197.121 212.969 1.00 8.66  ? 4075 GLU A CG    1 
ATOM   19229 C  CD    . GLU A 1 4075 ? 191.320 198.572 213.406 1.00 20.96 ? 4075 GLU A CD    1 
ATOM   19230 O  OE1   . GLU A 1 4075 ? 192.241 199.283 212.950 1.00 21.29 ? 4075 GLU A OE1   1 
ATOM   19231 O  OE2   . GLU A 1 4075 ? 190.468 199.000 214.212 1.00 21.58 ? 4075 GLU A OE2   1 
ATOM   19232 N  N     . GLY A 1 4076 ? 193.393 194.307 214.794 1.00 6.37  ? 4076 GLY A N     1 
ATOM   19233 C  CA    . GLY A 1 4076 ? 192.959 193.448 215.883 1.00 3.40  ? 4076 GLY A CA    1 
ATOM   19234 C  C     . GLY A 1 4076 ? 193.577 193.835 217.213 1.00 5.29  ? 4076 GLY A C     1 
ATOM   19235 O  O     . GLY A 1 4076 ? 192.927 193.754 218.257 1.00 4.23  ? 4076 GLY A O     1 
ATOM   19236 N  N     . PHE A 1 4077 ? 194.845 194.254 217.192 1.00 8.34  ? 4077 PHE A N     1 
ATOM   19237 C  CA    . PHE A 1 4077 ? 195.497 194.709 218.418 1.00 4.46  ? 4077 PHE A CA    1 
ATOM   19238 C  C     . PHE A 1 4077 ? 194.818 195.952 218.974 1.00 6.01  ? 4077 PHE A C     1 
ATOM   19239 O  O     . PHE A 1 4077 ? 194.570 196.045 220.182 1.00 9.13  ? 4077 PHE A O     1 
ATOM   19240 C  CB    . PHE A 1 4077 ? 196.975 194.980 218.149 1.00 2.40  ? 4077 PHE A CB    1 
ATOM   19241 C  CG    . PHE A 1 4077 ? 197.771 193.747 217.854 1.00 3.45  ? 4077 PHE A CG    1 
ATOM   19242 C  CD1   . PHE A 1 4077 ? 197.695 192.643 218.684 1.00 2.52  ? 4077 PHE A CD1   1 
ATOM   19243 C  CD2   . PHE A 1 4077 ? 198.576 193.682 216.731 1.00 5.73  ? 4077 PHE A CD2   1 
ATOM   19244 C  CE1   . PHE A 1 4077 ? 198.425 191.508 218.410 1.00 4.20  ? 4077 PHE A CE1   1 
ATOM   19245 C  CE2   . PHE A 1 4077 ? 199.302 192.547 216.449 1.00 4.20  ? 4077 PHE A CE2   1 
ATOM   19246 C  CZ    . PHE A 1 4077 ? 199.227 191.458 217.288 1.00 4.80  ? 4077 PHE A CZ    1 
ATOM   19247 N  N     . ASN A 1 4078 ? 194.511 196.920 218.108 1.00 6.37  ? 4078 ASN A N     1 
ATOM   19248 C  CA    . ASN A 1 4078 ? 193.813 198.118 218.561 1.00 5.36  ? 4078 ASN A CA    1 
ATOM   19249 C  C     . ASN A 1 4078 ? 192.429 197.777 219.091 1.00 5.16  ? 4078 ASN A C     1 
ATOM   19250 O  O     . ASN A 1 4078 ? 192.006 198.295 220.131 1.00 5.86  ? 4078 ASN A O     1 
ATOM   19251 C  CB    . ASN A 1 4078 ? 193.711 199.137 217.424 1.00 5.92  ? 4078 ASN A CB    1 
ATOM   19252 C  CG    . ASN A 1 4078 ? 195.060 199.502 216.842 1.00 13.40 ? 4078 ASN A CG    1 
ATOM   19253 O  OD1   . ASN A 1 4078 ? 196.059 199.577 217.557 1.00 17.61 ? 4078 ASN A OD1   1 
ATOM   19254 N  ND2   . ASN A 1 4078 ? 195.094 199.739 215.536 1.00 19.38 ? 4078 ASN A ND2   1 
ATOM   19255 N  N     . GLN A 1 4079 ? 191.708 196.901 218.386 1.00 6.59  ? 4079 GLN A N     1 
ATOM   19256 C  CA    . GLN A 1 4079 ? 190.374 196.518 218.830 1.00 6.63  ? 4079 GLN A CA    1 
ATOM   19257 C  C     . GLN A 1 4079 ? 190.428 195.764 220.152 1.00 5.34  ? 4079 GLN A C     1 
ATOM   19258 O  O     . GLN A 1 4079 ? 189.551 195.937 221.006 1.00 6.08  ? 4079 GLN A O     1 
ATOM   19259 C  CB    . GLN A 1 4079 ? 189.688 195.675 217.757 1.00 6.01  ? 4079 GLN A CB    1 
ATOM   19260 C  CG    . GLN A 1 4079 ? 188.262 195.306 218.096 1.00 11.21 ? 4079 GLN A CG    1 
ATOM   19261 C  CD    . GLN A 1 4079 ? 187.578 194.520 216.999 1.00 19.56 ? 4079 GLN A CD    1 
ATOM   19262 O  OE1   . GLN A 1 4079 ? 188.181 194.204 215.976 1.00 14.26 ? 4079 GLN A OE1   1 
ATOM   19263 N  NE2   . GLN A 1 4079 ? 186.307 194.197 217.210 1.00 27.68 ? 4079 GLN A NE2   1 
ATOM   19264 N  N     . ALA A 1 4080 ? 191.449 194.924 220.340 1.00 5.01  ? 4080 ALA A N     1 
ATOM   19265 C  CA    . ALA A 1 4080 ? 191.571 194.167 221.582 1.00 3.51  ? 4080 ALA A CA    1 
ATOM   19266 C  C     . ALA A 1 4080 ? 191.750 195.094 222.776 1.00 4.51  ? 4080 ALA A C     1 
ATOM   19267 O  O     . ALA A 1 4080 ? 191.122 194.905 223.822 1.00 6.82  ? 4080 ALA A O     1 
ATOM   19268 C  CB    . ALA A 1 4080 ? 192.734 193.179 221.485 1.00 2.35  ? 4080 ALA A CB    1 
ATOM   19269 N  N     . ASP A 1 4081 ? 192.602 196.111 222.631 1.00 5.53  ? 4081 ASP A N     1 
ATOM   19270 C  CA    . ASP A 1 4081 ? 192.833 197.040 223.731 1.00 4.50  ? 4081 ASP A CA    1 
ATOM   19271 C  C     . ASP A 1 4081 ? 191.567 197.812 224.083 1.00 9.39  ? 4081 ASP A C     1 
ATOM   19272 O  O     . ASP A 1 4081 ? 191.236 197.966 225.264 1.00 9.18  ? 4081 ASP A O     1 
ATOM   19273 C  CB    . ASP A 1 4081 ? 193.968 197.999 223.377 1.00 6.98  ? 4081 ASP A CB    1 
ATOM   19274 C  CG    . ASP A 1 4081 ? 194.209 199.037 224.451 1.00 15.79 ? 4081 ASP A CG    1 
ATOM   19275 O  OD1   . ASP A 1 4081 ? 193.675 200.160 224.323 1.00 20.66 ? 4081 ASP A OD1   1 
ATOM   19276 O  OD2   . ASP A 1 4081 ? 194.931 198.734 225.422 1.00 14.26 ? 4081 ASP A OD2   1 
ATOM   19277 N  N     . LYS A 1 4082 ? 190.839 198.299 223.074 1.00 7.06  ? 4082 LYS A N     1 
ATOM   19278 C  CA    . LYS A 1 4082 ? 189.601 199.021 223.350 1.00 6.36  ? 4082 LYS A CA    1 
ATOM   19279 C  C     . LYS A 1 4082 ? 188.552 198.108 223.974 1.00 7.10  ? 4082 LYS A C     1 
ATOM   19280 O  O     . LYS A 1 4082 ? 187.847 198.512 224.905 1.00 8.37  ? 4082 LYS A O     1 
ATOM   19281 C  CB    . LYS A 1 4082 ? 189.054 199.674 222.080 1.00 9.13  ? 4082 LYS A CB    1 
ATOM   19282 C  CG    . LYS A 1 4082 ? 189.947 200.748 221.480 1.00 13.78 ? 4082 LYS A CG    1 
ATOM   19283 C  CD    . LYS A 1 4082 ? 189.291 201.396 220.264 1.00 15.58 ? 4082 LYS A CD    1 
ATOM   19284 C  CE    . LYS A 1 4082 ? 189.227 200.466 219.064 1.00 13.57 ? 4082 LYS A CE    1 
ATOM   19285 N  NZ    . LYS A 1 4082 ? 190.575 200.138 218.536 1.00 10.96 ? 4082 LYS A NZ    1 
ATOM   19286 N  N     . ALA A 1 4083 ? 188.427 196.877 223.470 1.00 7.79  ? 4083 ALA A N     1 
ATOM   19287 C  CA    . ALA A 1 4083 ? 187.455 195.946 224.035 1.00 5.51  ? 4083 ALA A CA    1 
ATOM   19288 C  C     . ALA A 1 4083 ? 187.788 195.616 225.484 1.00 6.03  ? 4083 ALA A C     1 
ATOM   19289 O  O     . ALA A 1 4083 ? 186.896 195.572 226.338 1.00 5.83  ? 4083 ALA A O     1 
ATOM   19290 C  CB    . ALA A 1 4083 ? 187.393 194.673 223.193 1.00 3.91  ? 4083 ALA A CB    1 
ATOM   19291 N  N     . ILE A 1 4084 ? 189.068 195.386 225.777 1.00 4.32  ? 4084 ILE A N     1 
ATOM   19292 C  CA    . ILE A 1 4084 ? 189.483 195.079 227.144 1.00 3.95  ? 4084 ILE A CA    1 
ATOM   19293 C  C     . ILE A 1 4084 ? 189.235 196.274 228.058 1.00 7.21  ? 4084 ILE A C     1 
ATOM   19294 O  O     . ILE A 1 4084 ? 188.707 196.131 229.167 1.00 9.31  ? 4084 ILE A O     1 
ATOM   19295 C  CB    . ILE A 1 4084 ? 190.958 194.642 227.165 1.00 4.63  ? 4084 ILE A CB    1 
ATOM   19296 C  CG1   . ILE A 1 4084 ? 191.094 193.217 226.623 1.00 2.26  ? 4084 ILE A CG1   1 
ATOM   19297 C  CG2   . ILE A 1 4084 ? 191.538 194.753 228.565 1.00 3.60  ? 4084 ILE A CG2   1 
ATOM   19298 C  CD1   . ILE A 1 4084 ? 192.518 192.793 226.376 1.00 2.46  ? 4084 ILE A CD1   1 
ATOM   19299 N  N     . ASN A 1 4085 ? 189.601 197.473 227.600 1.00 6.49  ? 4085 ASN A N     1 
ATOM   19300 C  CA    . ASN A 1 4085 ? 189.428 198.669 228.419 1.00 5.00  ? 4085 ASN A CA    1 
ATOM   19301 C  C     . ASN A 1 4085 ? 187.957 198.934 228.712 1.00 7.12  ? 4085 ASN A C     1 
ATOM   19302 O  O     . ASN A 1 4085 ? 187.599 199.341 229.823 1.00 12.86 ? 4085 ASN A O     1 
ATOM   19303 C  CB    . ASN A 1 4085 ? 190.064 199.876 227.729 1.00 6.85  ? 4085 ASN A CB    1 
ATOM   19304 C  CG    . ASN A 1 4085 ? 191.576 199.797 227.699 1.00 6.28  ? 4085 ASN A CG    1 
ATOM   19305 O  OD1   . ASN A 1 4085 ? 192.182 198.995 228.408 1.00 6.85  ? 4085 ASN A OD1   1 
ATOM   19306 N  ND2   . ASN A 1 4085 ? 192.195 200.627 226.870 1.00 6.89  ? 4085 ASN A ND2   1 
ATOM   19307 N  N     . THR A 1 4086 ? 187.090 198.731 227.719 1.00 7.76  ? 4086 THR A N     1 
ATOM   19308 C  CA    . THR A 1 4086 ? 185.658 198.884 227.951 1.00 7.38  ? 4086 THR A CA    1 
ATOM   19309 C  C     . THR A 1 4086 ? 185.129 197.800 228.883 1.00 5.94  ? 4086 THR A C     1 
ATOM   19310 O  O     . THR A 1 4086 ? 184.294 198.072 229.753 1.00 6.89  ? 4086 THR A O     1 
ATOM   19311 C  CB    . THR A 1 4086 ? 184.905 198.860 226.622 1.00 5.54  ? 4086 THR A CB    1 
ATOM   19312 O  OG1   . THR A 1 4086 ? 185.522 199.772 225.707 1.00 8.59  ? 4086 THR A OG1   1 
ATOM   19313 C  CG2   . THR A 1 4086 ? 183.458 199.267 226.825 1.00 6.84  ? 4086 THR A CG2   1 
ATOM   19314 N  N     . ALA A 1 4087 ? 185.609 196.565 228.716 1.00 8.07  ? 4087 ALA A N     1 
ATOM   19315 C  CA    . ALA A 1 4087 ? 185.069 195.443 229.475 1.00 6.92  ? 4087 ALA A CA    1 
ATOM   19316 C  C     . ALA A 1 4087 ? 185.450 195.504 230.948 1.00 9.30  ? 4087 ALA A C     1 
ATOM   19317 O  O     . ALA A 1 4087 ? 184.652 195.113 231.806 1.00 9.92  ? 4087 ALA A O     1 
ATOM   19318 C  CB    . ALA A 1 4087 ? 185.537 194.125 228.863 1.00 7.01  ? 4087 ALA A CB    1 
ATOM   19319 N  N     . VAL A 1 4088 ? 186.657 195.979 231.263 1.00 6.84  ? 4088 VAL A N     1 
ATOM   19320 C  CA    . VAL A 1 4088 ? 187.101 196.015 232.652 1.00 5.88  ? 4088 VAL A CA    1 
ATOM   19321 C  C     . VAL A 1 4088 ? 186.346 197.040 233.482 1.00 11.89 ? 4088 VAL A C     1 
ATOM   19322 O  O     . VAL A 1 4088 ? 186.482 197.049 234.710 1.00 18.26 ? 4088 VAL A O     1 
ATOM   19323 C  CB    . VAL A 1 4088 ? 188.615 196.292 232.737 1.00 8.19  ? 4088 VAL A CB    1 
ATOM   19324 C  CG1   . VAL A 1 4088 ? 189.395 195.156 232.096 1.00 3.33  ? 4088 VAL A CG1   1 
ATOM   19325 C  CG2   . VAL A 1 4088 ? 188.957 197.623 232.099 1.00 7.92  ? 4088 VAL A CG2   1 
ATOM   19326 N  N     . LYS A 1 4089 ? 185.557 197.901 232.845 1.00 10.18 ? 4089 LYS A N     1 
ATOM   19327 C  CA    . LYS A 1 4089 ? 184.725 198.860 233.554 1.00 8.83  ? 4089 LYS A CA    1 
ATOM   19328 C  C     . LYS A 1 4089 ? 183.246 198.511 233.537 1.00 9.67  ? 4089 LYS A C     1 
ATOM   19329 O  O     . LYS A 1 4089 ? 182.457 199.217 234.174 1.00 23.73 ? 4089 LYS A O     1 
ATOM   19330 C  CB    . LYS A 1 4089 ? 184.913 200.268 232.966 1.00 10.31 ? 4089 LYS A CB    1 
ATOM   19331 C  CG    . LYS A 1 4089 ? 186.290 200.859 233.183 1.00 13.51 ? 4089 LYS A CG    1 
ATOM   19332 C  CD    . LYS A 1 4089 ? 186.331 202.303 232.718 1.00 11.92 ? 4089 LYS A CD    1 
ATOM   19333 C  CE    . LYS A 1 4089 ? 186.332 202.399 231.202 1.00 18.93 ? 4089 LYS A CE    1 
ATOM   19334 N  NZ    . LYS A 1 4089 ? 186.482 203.803 230.734 1.00 26.90 ? 4089 LYS A NZ    1 
ATOM   19335 N  N     . SER A 1 4090 ? 182.844 197.453 232.829 1.00 8.63  ? 4090 SER A N     1 
ATOM   19336 C  CA    . SER A 1 4090 ? 181.440 197.088 232.713 1.00 9.50  ? 4090 SER A CA    1 
ATOM   19337 C  C     . SER A 1 4090 ? 181.139 195.629 233.020 1.00 13.39 ? 4090 SER A C     1 
ATOM   19338 O  O     . SER A 1 4090 ? 179.963 195.250 232.997 1.00 19.35 ? 4090 SER A O     1 
ATOM   19339 C  CB    . SER A 1 4090 ? 180.916 197.405 231.302 1.00 7.86  ? 4090 SER A CB    1 
ATOM   19340 O  OG    . SER A 1 4090 ? 181.595 196.643 230.321 1.00 12.93 ? 4090 SER A OG    1 
ATOM   19341 N  N     . GLY A 1 4091 ? 182.146 194.805 233.296 1.00 9.74  ? 4091 GLY A N     1 
ATOM   19342 C  CA    . GLY A 1 4091 ? 181.928 193.387 233.498 1.00 6.42  ? 4091 GLY A CA    1 
ATOM   19343 C  C     . GLY A 1 4091 ? 181.772 192.582 232.231 1.00 8.55  ? 4091 GLY A C     1 
ATOM   19344 O  O     . GLY A 1 4091 ? 181.414 191.401 232.303 1.00 10.13 ? 4091 GLY A O     1 
ATOM   19345 N  N     . ARG A 1 4092 ? 182.022 193.188 231.074 1.00 13.21 ? 4092 ARG A N     1 
ATOM   19346 C  CA    . ARG A 1 4092 ? 181.920 192.538 229.779 1.00 7.23  ? 4092 ARG A CA    1 
ATOM   19347 C  C     . ARG A 1 4092 ? 182.996 191.456 229.646 1.00 6.50  ? 4092 ARG A C     1 
ATOM   19348 O  O     . ARG A 1 4092 ? 184.049 191.506 230.285 1.00 9.16  ? 4092 ARG A O     1 
ATOM   19349 C  CB    . ARG A 1 4092 ? 182.049 193.597 228.680 1.00 12.44 ? 4092 ARG A CB    1 
ATOM   19350 C  CG    . ARG A 1 4092 ? 181.969 193.136 227.236 1.00 15.70 ? 4092 ARG A CG    1 
ATOM   19351 C  CD    . ARG A 1 4092 ? 180.585 192.650 226.892 1.00 17.17 ? 4092 ARG A CD    1 
ATOM   19352 N  NE    . ARG A 1 4092 ? 180.489 192.227 225.500 1.00 22.77 ? 4092 ARG A NE    1 
ATOM   19353 C  CZ    . ARG A 1 4092 ? 180.161 193.032 224.501 1.00 12.39 ? 4092 ARG A CZ    1 
ATOM   19354 N  NH1   . ARG A 1 4092 ? 179.869 194.306 224.708 1.00 15.54 ? 4092 ARG A NH1   1 
ATOM   19355 N  NH2   . ARG A 1 4092 ? 180.121 192.548 223.263 1.00 10.11 ? 4092 ARG A NH2   1 
ATOM   19356 N  N     . TRP A 1 4093 ? 182.714 190.457 228.816 1.00 8.64  ? 4093 TRP A N     1 
ATOM   19357 C  CA    . TRP A 1 4093 ? 183.646 189.377 228.526 1.00 3.02  ? 4093 TRP A CA    1 
ATOM   19358 C  C     . TRP A 1 4093 ? 184.368 189.644 227.211 1.00 2.71  ? 4093 TRP A C     1 
ATOM   19359 O  O     . TRP A 1 4093 ? 183.763 190.114 226.244 1.00 4.19  ? 4093 TRP A O     1 
ATOM   19360 C  CB    . TRP A 1 4093 ? 182.924 188.029 228.458 1.00 2.67  ? 4093 TRP A CB    1 
ATOM   19361 C  CG    . TRP A 1 4093 ? 182.602 187.432 229.792 1.00 3.25  ? 4093 TRP A CG    1 
ATOM   19362 C  CD1   . TRP A 1 4093 ? 182.648 188.055 231.002 1.00 2.47  ? 4093 TRP A CD1   1 
ATOM   19363 C  CD2   . TRP A 1 4093 ? 182.138 186.100 230.046 1.00 2.92  ? 4093 TRP A CD2   1 
ATOM   19364 N  NE1   . TRP A 1 4093 ? 182.266 187.191 231.996 1.00 1.67  ? 4093 TRP A NE1   1 
ATOM   19365 C  CE2   . TRP A 1 4093 ? 181.944 185.984 231.434 1.00 1.36  ? 4093 TRP A CE2   1 
ATOM   19366 C  CE3   . TRP A 1 4093 ? 181.875 184.993 229.234 1.00 2.29  ? 4093 TRP A CE3   1 
ATOM   19367 C  CZ2   . TRP A 1 4093 ? 181.503 184.807 232.029 1.00 2.85  ? 4093 TRP A CZ2   1 
ATOM   19368 C  CZ3   . TRP A 1 4093 ? 181.438 183.826 229.826 1.00 3.38  ? 4093 TRP A CZ3   1 
ATOM   19369 C  CH2   . TRP A 1 4093 ? 181.255 183.741 231.210 1.00 5.56  ? 4093 TRP A CH2   1 
ATOM   19370 N  N     . VAL A 1 4094 ? 185.664 189.349 227.185 1.00 1.15  ? 4094 VAL A N     1 
ATOM   19371 C  CA    . VAL A 1 4094 ? 186.495 189.503 225.996 1.00 1.48  ? 4094 VAL A CA    1 
ATOM   19372 C  C     . VAL A 1 4094 ? 187.217 188.189 225.741 1.00 0.81  ? 4094 VAL A C     1 
ATOM   19373 O  O     . VAL A 1 4094 ? 187.838 187.633 226.652 1.00 0.74  ? 4094 VAL A O     1 
ATOM   19374 C  CB    . VAL A 1 4094 ? 187.504 190.658 226.149 1.00 0.95  ? 4094 VAL A CB    1 
ATOM   19375 C  CG1   . VAL A 1 4094 ? 188.442 190.708 224.956 1.00 0.57  ? 4094 VAL A CG1   1 
ATOM   19376 C  CG2   . VAL A 1 4094 ? 186.785 191.979 226.312 1.00 1.35  ? 4094 VAL A CG2   1 
ATOM   19377 N  N     . MET A 1 4095 ? 187.137 187.695 224.507 1.00 0.67  ? 4095 MET A N     1 
ATOM   19378 C  CA    . MET A 1 4095 ? 187.885 186.515 224.092 1.00 0.41  ? 4095 MET A CA    1 
ATOM   19379 C  C     . MET A 1 4095 ? 188.789 186.885 222.926 1.00 0.32  ? 4095 MET A C     1 
ATOM   19380 O  O     . MET A 1 4095 ? 188.325 187.443 221.927 1.00 0.51  ? 4095 MET A O     1 
ATOM   19381 C  CB    . MET A 1 4095 ? 186.957 185.361 223.707 1.00 0.71  ? 4095 MET A CB    1 
ATOM   19382 C  CG    . MET A 1 4095 ? 187.689 184.197 223.054 1.00 0.51  ? 4095 MET A CG    1 
ATOM   19383 S  SD    . MET A 1 4095 ? 186.645 182.781 222.671 1.00 8.70  ? 4095 MET A SD    1 
ATOM   19384 C  CE    . MET A 1 4095 ? 185.276 183.577 221.844 1.00 2.96  ? 4095 MET A CE    1 
ATOM   19385 N  N     . LEU A 1 4096 ? 190.075 186.573 223.057 1.00 0.31  ? 4096 LEU A N     1 
ATOM   19386 C  CA    . LEU A 1 4096 ? 191.062 186.804 222.014 1.00 0.24  ? 4096 LEU A CA    1 
ATOM   19387 C  C     . LEU A 1 4096 ? 191.553 185.453 221.510 1.00 0.43  ? 4096 LEU A C     1 
ATOM   19388 O  O     . LEU A 1 4096 ? 192.045 184.636 222.294 1.00 0.42  ? 4096 LEU A O     1 
ATOM   19389 C  CB    . LEU A 1 4096 ? 192.217 187.654 222.542 1.00 0.27  ? 4096 LEU A CB    1 
ATOM   19390 C  CG    . LEU A 1 4096 ? 191.782 188.951 223.237 1.00 0.29  ? 4096 LEU A CG    1 
ATOM   19391 C  CD1   . LEU A 1 4096 ? 192.972 189.749 223.721 1.00 0.30  ? 4096 LEU A CD1   1 
ATOM   19392 C  CD2   . LEU A 1 4096 ? 190.910 189.797 222.323 1.00 0.33  ? 4096 LEU A CD2   1 
ATOM   19393 N  N     . LYS A 1 4097 ? 191.417 185.223 220.208 1.00 0.70  ? 4097 LYS A N     1 
ATOM   19394 C  CA    . LYS A 1 4097 ? 191.713 183.931 219.609 1.00 0.48  ? 4097 LYS A CA    1 
ATOM   19395 C  C     . LYS A 1 4097 ? 193.062 183.951 218.907 1.00 0.43  ? 4097 LYS A C     1 
ATOM   19396 O  O     . LYS A 1 4097 ? 193.480 184.969 218.350 1.00 1.25  ? 4097 LYS A O     1 
ATOM   19397 C  CB    . LYS A 1 4097 ? 190.625 183.527 218.612 1.00 0.84  ? 4097 LYS A CB    1 
ATOM   19398 C  CG    . LYS A 1 4097 ? 189.213 183.828 219.060 1.00 1.56  ? 4097 LYS A CG    1 
ATOM   19399 C  CD    . LYS A 1 4097 ? 188.218 183.437 217.981 1.00 5.14  ? 4097 LYS A CD    1 
ATOM   19400 C  CE    . LYS A 1 4097 ? 187.038 184.387 217.945 1.00 4.20  ? 4097 LYS A CE    1 
ATOM   19401 N  NZ    . LYS A 1 4097 ? 186.137 184.093 216.800 1.00 5.79  ? 4097 LYS A NZ    1 
ATOM   19402 N  N     . ASN A 1 4098 ? 193.736 182.799 218.932 1.00 0.45  ? 4098 ASN A N     1 
ATOM   19403 C  CA    . ASN A 1 4098 ? 195.015 182.599 218.247 1.00 0.69  ? 4098 ASN A CA    1 
ATOM   19404 C  C     . ASN A 1 4098 ? 196.073 183.586 218.733 1.00 0.65  ? 4098 ASN A C     1 
ATOM   19405 O  O     . ASN A 1 4098 ? 196.832 184.147 217.943 1.00 1.26  ? 4098 ASN A O     1 
ATOM   19406 C  CB    . ASN A 1 4098 ? 194.845 182.685 216.728 1.00 0.74  ? 4098 ASN A CB    1 
ATOM   19407 C  CG    . ASN A 1 4098 ? 193.693 181.843 216.219 1.00 0.39  ? 4098 ASN A CG    1 
ATOM   19408 O  OD1   . ASN A 1 4098 ? 193.710 180.621 216.331 1.00 0.87  ? 4098 ASN A OD1   1 
ATOM   19409 N  ND2   . ASN A 1 4098 ? 192.687 182.496 215.653 1.00 0.28  ? 4098 ASN A ND2   1 
ATOM   19410 N  N     . VAL A 1 4099 ? 196.132 183.794 220.050 1.00 0.61  ? 4099 VAL A N     1 
ATOM   19411 C  CA    . VAL A 1 4099 ? 197.091 184.740 220.608 1.00 0.56  ? 4099 VAL A CA    1 
ATOM   19412 C  C     . VAL A 1 4099 ? 198.518 184.220 220.514 1.00 0.77  ? 4099 VAL A C     1 
ATOM   19413 O  O     . VAL A 1 4099 ? 199.466 185.001 220.653 1.00 0.88  ? 4099 VAL A O     1 
ATOM   19414 C  CB    . VAL A 1 4099 ? 196.729 185.084 222.064 1.00 0.31  ? 4099 VAL A CB    1 
ATOM   19415 C  CG1   . VAL A 1 4099 ? 195.305 185.603 222.143 1.00 0.36  ? 4099 VAL A CG1   1 
ATOM   19416 C  CG2   . VAL A 1 4099 ? 196.920 183.879 222.966 1.00 0.52  ? 4099 VAL A CG2   1 
ATOM   19417 N  N     . HIS A 1 4100 ? 198.700 182.919 220.276 1.00 0.53  ? 4100 HIS A N     1 
ATOM   19418 C  CA    . HIS A 1 4100 ? 200.031 182.369 220.056 1.00 0.63  ? 4100 HIS A CA    1 
ATOM   19419 C  C     . HIS A 1 4100 ? 200.681 182.906 218.789 1.00 0.98  ? 4100 HIS A C     1 
ATOM   19420 O  O     . HIS A 1 4100 ? 201.893 182.747 218.620 1.00 2.95  ? 4100 HIS A O     1 
ATOM   19421 C  CB    . HIS A 1 4100 ? 199.965 180.843 219.998 1.00 1.08  ? 4100 HIS A CB    1 
ATOM   19422 C  CG    . HIS A 1 4100 ? 199.206 180.313 218.821 1.00 1.44  ? 4100 HIS A CG    1 
ATOM   19423 N  ND1   . HIS A 1 4100 ? 197.830 180.278 218.780 1.00 0.85  ? 4100 HIS A ND1   1 
ATOM   19424 C  CD2   . HIS A 1 4100 ? 199.632 179.800 217.643 1.00 1.63  ? 4100 HIS A CD2   1 
ATOM   19425 C  CE1   . HIS A 1 4100 ? 197.440 179.766 217.627 1.00 0.70  ? 4100 HIS A CE1   1 
ATOM   19426 N  NE2   . HIS A 1 4100 ? 198.513 179.469 216.920 1.00 3.07  ? 4100 HIS A NE2   1 
ATOM   19427 N  N     . LEU A 1 4101 ? 199.908 183.529 217.901 1.00 0.85  ? 4101 LEU A N     1 
ATOM   19428 C  CA    . LEU A 1 4101 ? 200.454 184.147 216.701 1.00 0.97  ? 4101 LEU A CA    1 
ATOM   19429 C  C     . LEU A 1 4101 ? 201.122 185.486 216.976 1.00 1.96  ? 4101 LEU A C     1 
ATOM   19430 O  O     . LEU A 1 4101 ? 201.797 186.014 216.086 1.00 4.23  ? 4101 LEU A O     1 
ATOM   19431 C  CB    . LEU A 1 4101 ? 199.347 184.326 215.660 1.00 1.49  ? 4101 LEU A CB    1 
ATOM   19432 C  CG    . LEU A 1 4101 ? 198.657 183.048 215.182 1.00 2.03  ? 4101 LEU A CG    1 
ATOM   19433 C  CD1   . LEU A 1 4101 ? 197.548 183.371 214.194 1.00 1.16  ? 4101 LEU A CD1   1 
ATOM   19434 C  CD2   . LEU A 1 4101 ? 199.658 182.084 214.570 1.00 0.53  ? 4101 LEU A CD2   1 
ATOM   19435 N  N     . ALA A 1 4102 ? 200.955 186.048 218.170 1.00 2.76  ? 4102 ALA A N     1 
ATOM   19436 C  CA    . ALA A 1 4102 ? 201.568 187.322 218.549 1.00 1.62  ? 4102 ALA A CA    1 
ATOM   19437 C  C     . ALA A 1 4102 ? 202.248 187.178 219.905 1.00 2.60  ? 4102 ALA A C     1 
ATOM   19438 O  O     . ALA A 1 4102 ? 201.796 187.746 220.906 1.00 2.42  ? 4102 ALA A O     1 
ATOM   19439 C  CB    . ALA A 1 4102 ? 200.526 188.439 218.577 1.00 0.76  ? 4102 ALA A CB    1 
ATOM   19440 N  N     . PRO A 1 4103 ? 203.344 186.415 219.975 1.00 4.00  ? 4103 PRO A N     1 
ATOM   19441 C  CA    . PRO A 1 4103 ? 204.025 186.244 221.271 1.00 4.15  ? 4103 PRO A CA    1 
ATOM   19442 C  C     . PRO A 1 4103 ? 204.531 187.544 221.869 1.00 3.65  ? 4103 PRO A C     1 
ATOM   19443 O  O     . PRO A 1 4103 ? 204.479 187.719 223.091 1.00 4.94  ? 4103 PRO A O     1 
ATOM   19444 C  CB    . PRO A 1 4103 ? 205.175 185.284 220.936 1.00 4.04  ? 4103 PRO A CB    1 
ATOM   19445 C  CG    . PRO A 1 4103 ? 205.379 185.427 219.472 1.00 4.43  ? 4103 PRO A CG    1 
ATOM   19446 C  CD    . PRO A 1 4103 ? 204.031 185.692 218.893 1.00 2.94  ? 4103 PRO A CD    1 
ATOM   19447 N  N     . GLY A 1 4104 ? 205.015 188.469 221.037 1.00 3.80  ? 4104 GLY A N     1 
ATOM   19448 C  CA    . GLY A 1 4104 ? 205.508 189.733 221.558 1.00 1.45  ? 4104 GLY A CA    1 
ATOM   19449 C  C     . GLY A 1 4104 ? 204.415 190.583 222.175 1.00 2.46  ? 4104 GLY A C     1 
ATOM   19450 O  O     . GLY A 1 4104 ? 204.602 191.172 223.242 1.00 8.42  ? 4104 GLY A O     1 
ATOM   19451 N  N     . TRP A 1 4105 ? 203.259 190.657 221.513 1.00 1.87  ? 4105 TRP A N     1 
ATOM   19452 C  CA    . TRP A 1 4105 ? 202.144 191.422 222.056 1.00 1.45  ? 4105 TRP A CA    1 
ATOM   19453 C  C     . TRP A 1 4105 ? 201.577 190.765 223.309 1.00 2.21  ? 4105 TRP A C     1 
ATOM   19454 O  O     . TRP A 1 4105 ? 201.023 191.453 224.174 1.00 2.04  ? 4105 TRP A O     1 
ATOM   19455 C  CB    . TRP A 1 4105 ? 201.065 191.586 220.984 1.00 1.45  ? 4105 TRP A CB    1 
ATOM   19456 C  CG    . TRP A 1 4105 ? 199.727 191.985 221.508 1.00 1.03  ? 4105 TRP A CG    1 
ATOM   19457 C  CD1   . TRP A 1 4105 ? 199.293 193.252 221.770 1.00 0.92  ? 4105 TRP A CD1   1 
ATOM   19458 C  CD2   . TRP A 1 4105 ? 198.640 191.115 221.835 1.00 1.23  ? 4105 TRP A CD2   1 
ATOM   19459 N  NE1   . TRP A 1 4105 ? 198.002 193.224 222.238 1.00 1.64  ? 4105 TRP A NE1   1 
ATOM   19460 C  CE2   . TRP A 1 4105 ? 197.580 191.922 222.289 1.00 1.23  ? 4105 TRP A CE2   1 
ATOM   19461 C  CE3   . TRP A 1 4105 ? 198.460 189.729 221.788 1.00 2.17  ? 4105 TRP A CE3   1 
ATOM   19462 C  CZ2   . TRP A 1 4105 ? 196.360 191.390 222.692 1.00 1.90  ? 4105 TRP A CZ2   1 
ATOM   19463 C  CZ3   . TRP A 1 4105 ? 197.250 189.205 222.187 1.00 2.42  ? 4105 TRP A CZ3   1 
ATOM   19464 C  CH2   . TRP A 1 4105 ? 196.215 190.033 222.634 1.00 2.01  ? 4105 TRP A CH2   1 
ATOM   19465 N  N     . LEU A 1 4106 ? 201.718 189.441 223.427 1.00 3.19  ? 4106 LEU A N     1 
ATOM   19466 C  CA    . LEU A 1 4106 ? 201.222 188.731 224.604 1.00 2.41  ? 4106 LEU A CA    1 
ATOM   19467 C  C     . LEU A 1 4106 ? 201.964 189.152 225.865 1.00 5.53  ? 4106 LEU A C     1 
ATOM   19468 O  O     . LEU A 1 4106 ? 201.361 189.255 226.939 1.00 10.30 ? 4106 LEU A O     1 
ATOM   19469 C  CB    . LEU A 1 4106 ? 201.340 187.223 224.392 1.00 2.93  ? 4106 LEU A CB    1 
ATOM   19470 C  CG    . LEU A 1 4106 ? 200.098 186.507 223.859 1.00 1.01  ? 4106 LEU A CG    1 
ATOM   19471 C  CD1   . LEU A 1 4106 ? 200.314 185.006 223.859 1.00 0.61  ? 4106 LEU A CD1   1 
ATOM   19472 C  CD2   . LEU A 1 4106 ? 198.870 186.878 224.670 1.00 0.49  ? 4106 LEU A CD2   1 
ATOM   19473 N  N     . MET A 1 4107 ? 203.277 189.383 225.762 1.00 5.24  ? 4107 MET A N     1 
ATOM   19474 C  CA    . MET A 1 4107 ? 204.035 189.854 226.916 1.00 4.82  ? 4107 MET A CA    1 
ATOM   19475 C  C     . MET A 1 4107 ? 203.521 191.203 227.395 1.00 5.01  ? 4107 MET A C     1 
ATOM   19476 O  O     . MET A 1 4107 ? 203.418 191.447 228.603 1.00 8.65  ? 4107 MET A O     1 
ATOM   19477 C  CB    . MET A 1 4107 ? 205.522 189.944 226.578 1.00 8.13  ? 4107 MET A CB    1 
ATOM   19478 C  CG    . MET A 1 4107 ? 206.124 188.667 226.027 1.00 12.60 ? 4107 MET A CG    1 
ATOM   19479 S  SD    . MET A 1 4107 ? 207.755 188.935 225.310 1.00 42.64 ? 4107 MET A SD    1 
ATOM   19480 C  CE    . MET A 1 4107 ? 207.665 187.898 223.855 1.00 13.27 ? 4107 MET A CE    1 
ATOM   19481 N  N     . GLN A 1 4108 ? 203.198 192.096 226.461 1.00 4.71  ? 4108 GLN A N     1 
ATOM   19482 C  CA    . GLN A 1 4108 ? 202.682 193.406 226.839 1.00 3.60  ? 4108 GLN A CA    1 
ATOM   19483 C  C     . GLN A 1 4108 ? 201.283 193.309 227.431 1.00 4.33  ? 4108 GLN A C     1 
ATOM   19484 O  O     . GLN A 1 4108 ? 200.911 194.135 228.271 1.00 4.77  ? 4108 GLN A O     1 
ATOM   19485 C  CB    . GLN A 1 4108 ? 202.697 194.336 225.628 1.00 5.29  ? 4108 GLN A CB    1 
ATOM   19486 C  CG    . GLN A 1 4108 ? 204.096 194.662 225.134 1.00 9.04  ? 4108 GLN A CG    1 
ATOM   19487 C  CD    . GLN A 1 4108 ? 205.099 194.800 226.266 1.00 18.20 ? 4108 GLN A CD    1 
ATOM   19488 O  OE1   . GLN A 1 4108 ? 205.013 195.717 227.083 1.00 14.25 ? 4108 GLN A OE1   1 
ATOM   19489 N  NE2   . GLN A 1 4108 ? 206.057 193.883 226.317 1.00 12.64 ? 4108 GLN A NE2   1 
ATOM   19490 N  N     . LEU A 1 4109 ? 200.496 192.318 227.005 1.00 9.18  ? 4109 LEU A N     1 
ATOM   19491 C  CA    . LEU A 1 4109 ? 199.173 192.121 227.588 1.00 3.87  ? 4109 LEU A CA    1 
ATOM   19492 C  C     . LEU A 1 4109 ? 199.274 191.634 229.028 1.00 2.94  ? 4109 LEU A C     1 
ATOM   19493 O  O     . LEU A 1 4109 ? 198.463 192.017 229.877 1.00 4.61  ? 4109 LEU A O     1 
ATOM   19494 C  CB    . LEU A 1 4109 ? 198.367 191.138 226.741 1.00 4.47  ? 4109 LEU A CB    1 
ATOM   19495 C  CG    . LEU A 1 4109 ? 196.971 190.809 227.279 1.00 2.68  ? 4109 LEU A CG    1 
ATOM   19496 C  CD1   . LEU A 1 4109 ? 196.046 191.995 227.083 1.00 1.60  ? 4109 LEU A CD1   1 
ATOM   19497 C  CD2   . LEU A 1 4109 ? 196.407 189.559 226.631 1.00 1.88  ? 4109 LEU A CD2   1 
ATOM   19498 N  N     . GLU A 1 4110 ? 200.262 190.784 229.318 1.00 4.53  ? 4110 GLU A N     1 
ATOM   19499 C  CA    . GLU A 1 4110 ? 200.451 190.302 230.683 1.00 4.06  ? 4110 GLU A CA    1 
ATOM   19500 C  C     . GLU A 1 4110 ? 200.782 191.450 231.628 1.00 4.77  ? 4110 GLU A C     1 
ATOM   19501 O  O     . GLU A 1 4110 ? 200.281 191.500 232.757 1.00 7.39  ? 4110 GLU A O     1 
ATOM   19502 C  CB    . GLU A 1 4110 ? 201.547 189.236 230.711 1.00 3.04  ? 4110 GLU A CB    1 
ATOM   19503 C  CG    . GLU A 1 4110 ? 201.660 188.462 232.017 1.00 5.48  ? 4110 GLU A CG    1 
ATOM   19504 C  CD    . GLU A 1 4110 ? 202.483 189.184 233.068 1.00 7.74  ? 4110 GLU A CD    1 
ATOM   19505 O  OE1   . GLU A 1 4110 ? 203.608 189.621 232.746 1.00 9.47  ? 4110 GLU A OE1   1 
ATOM   19506 O  OE2   . GLU A 1 4110 ? 202.009 189.310 234.217 1.00 4.50  ? 4110 GLU A OE2   1 
ATOM   19507 N  N     . LYS A 1 4111 ? 201.627 192.383 231.183 1.00 4.56  ? 4111 LYS A N     1 
ATOM   19508 C  CA    . LYS A 1 4111 ? 201.936 193.554 231.996 1.00 4.74  ? 4111 LYS A CA    1 
ATOM   19509 C  C     . LYS A 1 4111 ? 200.716 194.452 232.159 1.00 3.19  ? 4111 LYS A C     1 
ATOM   19510 O  O     . LYS A 1 4111 ? 200.517 195.048 233.224 1.00 5.69  ? 4111 LYS A O     1 
ATOM   19511 C  CB    . LYS A 1 4111 ? 203.105 194.321 231.380 1.00 5.72  ? 4111 LYS A CB    1 
ATOM   19512 C  CG    . LYS A 1 4111 ? 204.458 193.676 231.628 1.00 8.42  ? 4111 LYS A CG    1 
ATOM   19513 C  CD    . LYS A 1 4111 ? 205.398 193.882 230.455 1.00 11.55 ? 4111 LYS A CD    1 
ATOM   19514 C  CE    . LYS A 1 4111 ? 206.832 193.532 230.818 1.00 7.89  ? 4111 LYS A CE    1 
ATOM   19515 N  NZ    . LYS A 1 4111 ? 206.978 192.144 231.324 1.00 8.21  ? 4111 LYS A NZ    1 
ATOM   19516 N  N     . LYS A 1 4112 ? 199.891 194.567 231.115 1.00 4.07  ? 4112 LYS A N     1 
ATOM   19517 C  CA    . LYS A 1 4112 ? 198.679 195.376 231.209 1.00 3.22  ? 4112 LYS A CA    1 
ATOM   19518 C  C     . LYS A 1 4112 ? 197.691 194.788 232.208 1.00 4.66  ? 4112 LYS A C     1 
ATOM   19519 O  O     . LYS A 1 4112 ? 197.078 195.523 232.991 1.00 6.00  ? 4112 LYS A O     1 
ATOM   19520 C  CB    . LYS A 1 4112 ? 198.029 195.507 229.831 1.00 3.93  ? 4112 LYS A CB    1 
ATOM   19521 C  CG    . LYS A 1 4112 ? 196.645 196.125 229.865 1.00 5.03  ? 4112 LYS A CG    1 
ATOM   19522 C  CD    . LYS A 1 4112 ? 196.023 196.185 228.486 1.00 4.33  ? 4112 LYS A CD    1 
ATOM   19523 C  CE    . LYS A 1 4112 ? 194.662 196.856 228.541 1.00 7.29  ? 4112 LYS A CE    1 
ATOM   19524 N  NZ    . LYS A 1 4112 ? 194.061 197.031 227.192 1.00 6.97  ? 4112 LYS A NZ    1 
ATOM   19525 N  N     . LEU A 1 4113 ? 197.516 193.465 232.192 1.00 7.00  ? 4113 LEU A N     1 
ATOM   19526 C  CA    . LEU A 1 4113 ? 196.565 192.830 233.097 1.00 5.99  ? 4113 LEU A CA    1 
ATOM   19527 C  C     . LEU A 1 4113 ? 197.010 192.929 234.549 1.00 7.16  ? 4113 LEU A C     1 
ATOM   19528 O  O     . LEU A 1 4113 ? 196.166 193.000 235.450 1.00 9.03  ? 4113 LEU A O     1 
ATOM   19529 C  CB    . LEU A 1 4113 ? 196.370 191.366 232.711 1.00 4.96  ? 4113 LEU A CB    1 
ATOM   19530 C  CG    . LEU A 1 4113 ? 195.691 191.100 231.371 1.00 6.96  ? 4113 LEU A CG    1 
ATOM   19531 C  CD1   . LEU A 1 4113 ? 195.809 189.631 231.006 1.00 4.35  ? 4113 LEU A CD1   1 
ATOM   19532 C  CD2   . LEU A 1 4113 ? 194.236 191.535 231.430 1.00 7.07  ? 4113 LEU A CD2   1 
ATOM   19533 N  N     . HIS A 1 4114 ? 198.321 192.927 234.794 1.00 8.93  ? 4114 HIS A N     1 
ATOM   19534 C  CA    . HIS A 1 4114 ? 198.823 192.947 236.162 1.00 7.34  ? 4114 HIS A CA    1 
ATOM   19535 C  C     . HIS A 1 4114 ? 198.402 194.214 236.894 1.00 8.54  ? 4114 HIS A C     1 
ATOM   19536 O  O     . HIS A 1 4114 ? 197.978 194.158 238.055 1.00 8.61  ? 4114 HIS A O     1 
ATOM   19537 C  CB    . HIS A 1 4114 ? 200.346 192.813 236.156 1.00 7.09  ? 4114 HIS A CB    1 
ATOM   19538 C  CG    . HIS A 1 4114 ? 200.951 192.736 237.521 1.00 6.15  ? 4114 HIS A CG    1 
ATOM   19539 N  ND1   . HIS A 1 4114 ? 201.053 191.556 238.224 1.00 5.76  ? 4114 HIS A ND1   1 
ATOM   19540 C  CD2   . HIS A 1 4114 ? 201.483 193.695 238.316 1.00 4.85  ? 4114 HIS A CD2   1 
ATOM   19541 C  CE1   . HIS A 1 4114 ? 201.622 191.789 239.393 1.00 8.25  ? 4114 HIS A CE1   1 
ATOM   19542 N  NE2   . HIS A 1 4114 ? 201.893 193.079 239.473 1.00 7.67  ? 4114 HIS A NE2   1 
ATOM   19543 N  N     . SER A 1 4115 ? 198.503 195.364 236.232 1.00 9.60  ? 4115 SER A N     1 
ATOM   19544 C  CA    . SER A 1 4115 ? 198.156 196.645 236.840 1.00 10.14 ? 4115 SER A CA    1 
ATOM   19545 C  C     . SER A 1 4115 ? 196.735 197.037 236.441 1.00 14.74 ? 4115 SER A C     1 
ATOM   19546 O  O     . SER A 1 4115 ? 196.496 198.008 235.723 1.00 17.48 ? 4115 SER A O     1 
ATOM   19547 C  CB    . SER A 1 4115 ? 199.166 197.712 236.432 1.00 9.24  ? 4115 SER A CB    1 
ATOM   19548 O  OG    . SER A 1 4115 ? 199.229 197.833 235.023 1.00 17.12 ? 4115 SER A OG    1 
ATOM   19549 N  N     . LEU A 1 4116 ? 195.777 196.255 236.932 1.00 13.45 ? 4116 LEU A N     1 
ATOM   19550 C  CA    . LEU A 1 4116 ? 194.386 196.469 236.566 1.00 12.58 ? 4116 LEU A CA    1 
ATOM   19551 C  C     . LEU A 1 4116 ? 193.486 195.788 237.587 1.00 15.91 ? 4116 LEU A C     1 
ATOM   19552 O  O     . LEU A 1 4116 ? 193.750 194.657 238.000 1.00 21.12 ? 4116 LEU A O     1 
ATOM   19553 C  CB    . LEU A 1 4116 ? 194.116 195.934 235.156 1.00 12.87 ? 4116 LEU A CB    1 
ATOM   19554 C  CG    . LEU A 1 4116 ? 192.707 196.009 234.581 1.00 15.75 ? 4116 LEU A CG    1 
ATOM   19555 C  CD1   . LEU A 1 4116 ? 192.142 197.413 234.724 1.00 14.08 ? 4116 LEU A CD1   1 
ATOM   19556 C  CD2   . LEU A 1 4116 ? 192.768 195.608 233.125 1.00 9.78  ? 4116 LEU A CD2   1 
ATOM   19557 N  N     . GLN A 1 4117 ? 192.426 196.489 237.989 1.00 12.52 ? 4117 GLN A N     1 
ATOM   19558 C  CA    . GLN A 1 4117 ? 191.439 195.980 238.943 1.00 15.35 ? 4117 GLN A CA    1 
ATOM   19559 C  C     . GLN A 1 4117 ? 190.075 196.079 238.279 1.00 15.19 ? 4117 GLN A C     1 
ATOM   19560 O  O     . GLN A 1 4117 ? 189.325 197.038 238.504 1.00 18.21 ? 4117 GLN A O     1 
ATOM   19561 C  CB    . GLN A 1 4117 ? 191.470 196.753 240.263 1.00 17.71 ? 4117 GLN A CB    1 
ATOM   19562 C  CG    . GLN A 1 4117 ? 192.678 196.479 241.150 1.00 19.72 ? 4117 GLN A CG    1 
ATOM   19563 C  CD    . GLN A 1 4117 ? 193.972 197.027 240.578 1.00 27.43 ? 4117 GLN A CD    1 
ATOM   19564 O  OE1   . GLN A 1 4117 ? 194.914 196.281 240.315 1.00 32.12 ? 4117 GLN A OE1   1 
ATOM   19565 N  NE2   . GLN A 1 4117 ? 194.023 198.340 240.386 1.00 22.70 ? 4117 GLN A NE2   1 
ATOM   19566 N  N     . PRO A 1 4118 ? 189.718 195.104 237.457 1.00 14.65 ? 4118 PRO A N     1 
ATOM   19567 C  CA    . PRO A 1 4118 ? 188.512 195.210 236.634 1.00 10.92 ? 4118 PRO A CA    1 
ATOM   19568 C  C     . PRO A 1 4118 ? 187.245 194.955 237.442 1.00 10.22 ? 4118 PRO A C     1 
ATOM   19569 O  O     . PRO A 1 4118 ? 187.272 194.727 238.649 1.00 13.85 ? 4118 PRO A O     1 
ATOM   19570 C  CB    . PRO A 1 4118 ? 188.724 194.130 235.573 1.00 6.82  ? 4118 PRO A CB    1 
ATOM   19571 C  CG    . PRO A 1 4118 ? 189.592 193.122 236.227 1.00 11.07 ? 4118 PRO A CG    1 
ATOM   19572 C  CD    . PRO A 1 4118 ? 190.452 193.848 237.220 1.00 8.99  ? 4118 PRO A CD    1 
ATOM   19573 N  N     . HIS A 1 4119 ? 186.118 195.016 236.739 1.00 9.85  ? 4119 HIS A N     1 
ATOM   19574 C  CA    . HIS A 1 4119 ? 184.833 194.689 237.334 1.00 9.96  ? 4119 HIS A CA    1 
ATOM   19575 C  C     . HIS A 1 4119 ? 184.808 193.225 237.755 1.00 11.53 ? 4119 HIS A C     1 
ATOM   19576 O  O     . HIS A 1 4119 ? 185.461 192.375 237.144 1.00 14.56 ? 4119 HIS A O     1 
ATOM   19577 C  CB    . HIS A 1 4119 ? 183.714 194.984 236.334 1.00 9.04  ? 4119 HIS A CB    1 
ATOM   19578 C  CG    . HIS A 1 4119 ? 182.336 194.828 236.893 1.00 11.90 ? 4119 HIS A CG    1 
ATOM   19579 N  ND1   . HIS A 1 4119 ? 181.667 193.624 236.900 1.00 16.86 ? 4119 HIS A ND1   1 
ATOM   19580 C  CD2   . HIS A 1 4119 ? 181.496 195.728 237.456 1.00 14.70 ? 4119 HIS A CD2   1 
ATOM   19581 C  CE1   . HIS A 1 4119 ? 180.475 193.787 237.445 1.00 17.39 ? 4119 HIS A CE1   1 
ATOM   19582 N  NE2   . HIS A 1 4119 ? 180.347 195.055 237.791 1.00 21.91 ? 4119 HIS A NE2   1 
ATOM   19583 N  N     . ALA A 1 4120 ? 184.050 192.933 238.815 1.00 8.63  ? 4120 ALA A N     1 
ATOM   19584 C  CA    . ALA A 1 4120 ? 184.041 191.584 239.372 1.00 7.55  ? 4120 ALA A CA    1 
ATOM   19585 C  C     . ALA A 1 4120 ? 183.559 190.550 238.363 1.00 10.28 ? 4120 ALA A C     1 
ATOM   19586 O  O     . ALA A 1 4120 ? 183.946 189.378 238.443 1.00 14.81 ? 4120 ALA A O     1 
ATOM   19587 C  CB    . ALA A 1 4120 ? 183.175 191.542 240.629 1.00 10.84 ? 4120 ALA A CB    1 
ATOM   19588 N  N     . CYS A 1 4121 ? 182.723 190.956 237.412 1.00 9.22  ? 4121 CYS A N     1 
ATOM   19589 C  CA    . CYS A 1 4121 ? 182.203 190.045 236.400 1.00 6.62  ? 4121 CYS A CA    1 
ATOM   19590 C  C     . CYS A 1 4121 ? 183.061 189.979 235.145 1.00 4.55  ? 4121 CYS A C     1 
ATOM   19591 O  O     . CYS A 1 4121 ? 182.789 189.145 234.276 1.00 3.72  ? 4121 CYS A O     1 
ATOM   19592 C  CB    . CYS A 1 4121 ? 180.774 190.446 236.014 1.00 9.21  ? 4121 CYS A CB    1 
ATOM   19593 S  SG    . CYS A 1 4121 ? 179.491 189.769 237.082 1.00 38.83 ? 4121 CYS A SG    1 
ATOM   19594 N  N     . PHE A 1 4122 ? 184.084 190.823 235.023 1.00 4.81  ? 4122 PHE A N     1 
ATOM   19595 C  CA    . PHE A 1 4122 ? 184.917 190.809 233.828 1.00 3.08  ? 4122 PHE A CA    1 
ATOM   19596 C  C     . PHE A 1 4122 ? 185.702 189.509 233.731 1.00 2.55  ? 4122 PHE A C     1 
ATOM   19597 O  O     . PHE A 1 4122 ? 186.269 189.026 234.714 1.00 3.64  ? 4122 PHE A O     1 
ATOM   19598 C  CB    . PHE A 1 4122 ? 185.884 191.992 233.825 1.00 1.83  ? 4122 PHE A CB    1 
ATOM   19599 C  CG    . PHE A 1 4122 ? 187.039 191.824 232.873 1.00 1.98  ? 4122 PHE A CG    1 
ATOM   19600 C  CD1   . PHE A 1 4122 ? 186.870 192.042 231.516 1.00 1.58  ? 4122 PHE A CD1   1 
ATOM   19601 C  CD2   . PHE A 1 4122 ? 188.286 191.436 233.330 1.00 1.44  ? 4122 PHE A CD2   1 
ATOM   19602 C  CE1   . PHE A 1 4122 ? 187.920 191.882 230.638 1.00 0.84  ? 4122 PHE A CE1   1 
ATOM   19603 C  CE2   . PHE A 1 4122 ? 189.339 191.274 232.454 1.00 0.59  ? 4122 PHE A CE2   1 
ATOM   19604 C  CZ    . PHE A 1 4122 ? 189.157 191.498 231.108 1.00 0.57  ? 4122 PHE A CZ    1 
ATOM   19605 N  N     . ARG A 1 4123 ? 185.743 188.949 232.527 1.00 1.55  ? 4123 ARG A N     1 
ATOM   19606 C  CA    . ARG A 1 4123 ? 186.549 187.774 232.241 1.00 1.23  ? 4123 ARG A CA    1 
ATOM   19607 C  C     . ARG A 1 4123 ? 187.249 187.970 230.907 1.00 0.50  ? 4123 ARG A C     1 
ATOM   19608 O  O     . ARG A 1 4123 ? 186.650 188.473 229.953 1.00 0.45  ? 4123 ARG A O     1 
ATOM   19609 C  CB    . ARG A 1 4123 ? 185.698 186.498 232.211 1.00 0.97  ? 4123 ARG A CB    1 
ATOM   19610 C  CG    . ARG A 1 4123 ? 185.124 186.101 233.557 1.00 1.44  ? 4123 ARG A CG    1 
ATOM   19611 C  CD    . ARG A 1 4123 ? 186.223 185.740 234.545 1.00 2.74  ? 4123 ARG A CD    1 
ATOM   19612 N  NE    . ARG A 1 4123 ? 185.693 185.423 235.864 1.00 6.51  ? 4123 ARG A NE    1 
ATOM   19613 C  CZ    . ARG A 1 4123 ? 185.221 186.318 236.724 1.00 4.73  ? 4123 ARG A CZ    1 
ATOM   19614 N  NH1   . ARG A 1 4123 ? 185.237 187.612 236.455 1.00 3.24  ? 4123 ARG A NH1   1 
ATOM   19615 N  NH2   . ARG A 1 4123 ? 184.725 185.901 237.884 1.00 7.65  ? 4123 ARG A NH2   1 
ATOM   19616 N  N     . LEU A 1 4124 ? 188.519 187.586 230.849 1.00 0.67  ? 4124 LEU A N     1 
ATOM   19617 C  CA    . LEU A 1 4124 ? 189.297 187.619 229.616 1.00 0.38  ? 4124 LEU A CA    1 
ATOM   19618 C  C     . LEU A 1 4124 ? 189.669 186.194 229.237 1.00 0.22  ? 4124 LEU A C     1 
ATOM   19619 O  O     . LEU A 1 4124 ? 190.301 185.484 230.026 1.00 0.41  ? 4124 LEU A O     1 
ATOM   19620 C  CB    . LEU A 1 4124 ? 190.550 188.480 229.773 1.00 0.25  ? 4124 LEU A CB    1 
ATOM   19621 C  CG    . LEU A 1 4124 ? 191.496 188.455 228.572 1.00 0.37  ? 4124 LEU A CG    1 
ATOM   19622 C  CD1   . LEU A 1 4124 ? 190.853 189.125 227.367 1.00 0.24  ? 4124 LEU A CD1   1 
ATOM   19623 C  CD2   . LEU A 1 4124 ? 192.827 189.099 228.907 1.00 0.55  ? 4124 LEU A CD2   1 
ATOM   19624 N  N     . PHE A 1 4125 ? 189.278 185.780 228.037 1.00 0.18  ? 4125 PHE A N     1 
ATOM   19625 C  CA    . PHE A 1 4125 ? 189.587 184.455 227.517 1.00 0.41  ? 4125 PHE A CA    1 
ATOM   19626 C  C     . PHE A 1 4125 ? 190.626 184.582 226.414 1.00 0.15  ? 4125 PHE A C     1 
ATOM   19627 O  O     . PHE A 1 4125 ? 190.460 185.379 225.487 1.00 0.15  ? 4125 PHE A O     1 
ATOM   19628 C  CB    . PHE A 1 4125 ? 188.335 183.757 226.979 1.00 0.43  ? 4125 PHE A CB    1 
ATOM   19629 C  CG    . PHE A 1 4125 ? 187.280 183.507 228.017 1.00 0.48  ? 4125 PHE A CG    1 
ATOM   19630 C  CD1   . PHE A 1 4125 ? 186.341 184.476 228.322 1.00 0.42  ? 4125 PHE A CD1   1 
ATOM   19631 C  CD2   . PHE A 1 4125 ? 187.225 182.295 228.684 1.00 0.23  ? 4125 PHE A CD2   1 
ATOM   19632 C  CE1   . PHE A 1 4125 ? 185.370 184.244 229.275 1.00 0.47  ? 4125 PHE A CE1   1 
ATOM   19633 C  CE2   . PHE A 1 4125 ? 186.257 182.056 229.637 1.00 0.24  ? 4125 PHE A CE2   1 
ATOM   19634 C  CZ    . PHE A 1 4125 ? 185.329 183.031 229.932 1.00 0.93  ? 4125 PHE A CZ    1 
ATOM   19635 N  N     . LEU A 1 4126 ? 191.698 183.807 226.523 1.00 0.27  ? 4126 LEU A N     1 
ATOM   19636 C  CA    . LEU A 1 4126 ? 192.742 183.772 225.508 1.00 0.43  ? 4126 LEU A CA    1 
ATOM   19637 C  C     . LEU A 1 4126 ? 192.768 182.382 224.896 1.00 0.56  ? 4126 LEU A C     1 
ATOM   19638 O  O     . LEU A 1 4126 ? 192.941 181.387 225.607 1.00 0.97  ? 4126 LEU A O     1 
ATOM   19639 C  CB    . LEU A 1 4126 ? 194.105 184.135 226.099 1.00 0.43  ? 4126 LEU A CB    1 
ATOM   19640 C  CG    . LEU A 1 4126 ? 194.206 185.492 226.799 1.00 0.25  ? 4126 LEU A CG    1 
ATOM   19641 C  CD1   . LEU A 1 4126 ? 195.636 185.764 227.236 1.00 0.13  ? 4126 LEU A CD1   1 
ATOM   19642 C  CD2   . LEU A 1 4126 ? 193.696 186.599 225.896 1.00 0.12  ? 4126 LEU A CD2   1 
ATOM   19643 N  N     . THR A 1 4127 ? 192.594 182.319 223.583 1.00 1.38  ? 4127 THR A N     1 
ATOM   19644 C  CA    . THR A 1 4127 ? 192.639 181.071 222.839 1.00 0.62  ? 4127 THR A CA    1 
ATOM   19645 C  C     . THR A 1 4127 ? 193.976 180.976 222.123 1.00 0.61  ? 4127 THR A C     1 
ATOM   19646 O  O     . THR A 1 4127 ? 194.376 181.909 221.416 1.00 2.04  ? 4127 THR A O     1 
ATOM   19647 C  CB    . THR A 1 4127 ? 191.485 180.990 221.837 1.00 0.98  ? 4127 THR A CB    1 
ATOM   19648 O  OG1   . THR A 1 4127 ? 190.246 180.842 222.541 1.00 1.71  ? 4127 THR A OG1   1 
ATOM   19649 C  CG2   . THR A 1 4127 ? 191.674 179.826 220.887 1.00 5.74  ? 4127 THR A CG2   1 
ATOM   19650 N  N     . MET A 1 4128 ? 194.673 179.865 222.324 1.00 1.01  ? 4128 MET A N     1 
ATOM   19651 C  CA    . MET A 1 4128 ? 195.948 179.645 221.665 1.00 1.10  ? 4128 MET A CA    1 
ATOM   19652 C  C     . MET A 1 4128 ? 196.157 178.153 221.479 1.00 1.04  ? 4128 MET A C     1 
ATOM   19653 O  O     . MET A 1 4128 ? 195.562 177.328 222.176 1.00 1.70  ? 4128 MET A O     1 
ATOM   19654 C  CB    . MET A 1 4128 ? 197.112 180.249 222.460 1.00 1.12  ? 4128 MET A CB    1 
ATOM   19655 C  CG    . MET A 1 4128 ? 197.457 179.484 223.725 1.00 1.90  ? 4128 MET A CG    1 
ATOM   19656 S  SD    . MET A 1 4128 ? 196.169 179.620 224.975 1.00 31.07 ? 4128 MET A SD    1 
ATOM   19657 C  CE    . MET A 1 4128 ? 196.319 181.340 225.431 1.00 4.24  ? 4128 MET A CE    1 
ATOM   19658 N  N     . GLU A 1 4129 ? 197.000 177.817 220.513 1.00 1.37  ? 4129 GLU A N     1 
ATOM   19659 C  CA    . GLU A 1 4129 ? 197.489 176.459 220.392 1.00 1.70  ? 4129 GLU A CA    1 
ATOM   19660 C  C     . GLU A 1 4129 ? 198.582 176.220 221.427 1.00 2.99  ? 4129 GLU A C     1 
ATOM   19661 O  O     . GLU A 1 4129 ? 199.186 177.155 221.959 1.00 8.77  ? 4129 GLU A O     1 
ATOM   19662 C  CB    . GLU A 1 4129 ? 198.027 176.199 218.986 1.00 4.16  ? 4129 GLU A CB    1 
ATOM   19663 C  CG    . GLU A 1 4129 ? 196.983 176.292 217.894 1.00 7.20  ? 4129 GLU A CG    1 
ATOM   19664 C  CD    . GLU A 1 4129 ? 197.488 175.774 216.562 1.00 18.36 ? 4129 GLU A CD    1 
ATOM   19665 O  OE1   . GLU A 1 4129 ? 198.713 175.816 216.332 1.00 20.86 ? 4129 GLU A OE1   1 
ATOM   19666 O  OE2   . GLU A 1 4129 ? 196.658 175.325 215.743 1.00 16.50 ? 4129 GLU A OE2   1 
ATOM   19667 N  N     . ILE A 1 4130 ? 198.838 174.947 221.714 1.00 2.27  ? 4130 ILE A N     1 
ATOM   19668 C  CA    . ILE A 1 4130 ? 199.912 174.606 222.637 1.00 2.47  ? 4130 ILE A CA    1 
ATOM   19669 C  C     . ILE A 1 4130 ? 201.225 174.849 221.908 1.00 2.95  ? 4130 ILE A C     1 
ATOM   19670 O  O     . ILE A 1 4130 ? 201.674 174.023 221.108 1.00 10.47 ? 4130 ILE A O     1 
ATOM   19671 C  CB    . ILE A 1 4130 ? 199.789 173.159 223.144 1.00 3.42  ? 4130 ILE A CB    1 
ATOM   19672 C  CG1   . ILE A 1 4130 ? 198.459 172.978 223.882 1.00 1.25  ? 4130 ILE A CG1   1 
ATOM   19673 C  CG2   . ILE A 1 4130 ? 200.965 172.805 224.039 1.00 1.17  ? 4130 ILE A CG2   1 
ATOM   19674 C  CD1   . ILE A 1 4130 ? 198.291 171.630 224.536 1.00 0.56  ? 4130 ILE A CD1   1 
ATOM   19675 N  N     . ASN A 1 4131 ? 201.837 175.999 222.177 1.00 2.80  ? 4131 ASN A N     1 
ATOM   19676 C  CA    . ASN A 1 4131 ? 202.976 176.482 221.420 1.00 3.53  ? 4131 ASN A CA    1 
ATOM   19677 C  C     . ASN A 1 4131 ? 204.057 176.948 222.385 1.00 2.64  ? 4131 ASN A C     1 
ATOM   19678 O  O     . ASN A 1 4131 ? 203.761 177.693 223.335 1.00 3.15  ? 4131 ASN A O     1 
ATOM   19679 C  CB    . ASN A 1 4131 ? 202.551 177.631 220.492 1.00 3.56  ? 4131 ASN A CB    1 
ATOM   19680 C  CG    . ASN A 1 4131 ? 203.510 177.838 219.339 1.00 6.70  ? 4131 ASN A CG    1 
ATOM   19681 O  OD1   . ASN A 1 4131 ? 204.707 178.031 219.540 1.00 10.94 ? 4131 ASN A OD1   1 
ATOM   19682 N  ND2   . ASN A 1 4131 ? 202.986 177.803 218.123 1.00 10.11 ? 4131 ASN A ND2   1 
ATOM   19683 N  N     . PRO A 1 4132 ? 205.313 176.544 222.184 1.00 2.69  ? 4132 PRO A N     1 
ATOM   19684 C  CA    . PRO A 1 4132 ? 206.397 177.054 223.040 1.00 2.21  ? 4132 PRO A CA    1 
ATOM   19685 C  C     . PRO A 1 4132 ? 206.626 178.551 222.908 1.00 4.75  ? 4132 PRO A C     1 
ATOM   19686 O  O     . PRO A 1 4132 ? 207.307 179.128 223.765 1.00 7.22  ? 4132 PRO A O     1 
ATOM   19687 C  CB    . PRO A 1 4132 ? 207.623 176.254 222.571 1.00 2.41  ? 4132 PRO A CB    1 
ATOM   19688 C  CG    . PRO A 1 4132 ? 207.267 175.767 221.207 1.00 2.36  ? 4132 PRO A CG    1 
ATOM   19689 C  CD    . PRO A 1 4132 ? 205.792 175.533 221.227 1.00 2.18  ? 4132 PRO A CD    1 
ATOM   19690 N  N     . LYS A 1 4133 ? 206.096 179.191 221.866 1.00 5.64  ? 4133 LYS A N     1 
ATOM   19691 C  CA    . LYS A 1 4133 ? 206.249 180.631 221.707 1.00 4.69  ? 4133 LYS A CA    1 
ATOM   19692 C  C     . LYS A 1 4133 ? 205.457 181.424 222.739 1.00 5.70  ? 4133 LYS A C     1 
ATOM   19693 O  O     . LYS A 1 4133 ? 205.772 182.597 222.969 1.00 11.84 ? 4133 LYS A O     1 
ATOM   19694 C  CB    . LYS A 1 4133 ? 205.823 181.053 220.299 1.00 8.60  ? 4133 LYS A CB    1 
ATOM   19695 C  CG    . LYS A 1 4133 ? 206.798 180.647 219.208 1.00 8.35  ? 4133 LYS A CG    1 
ATOM   19696 C  CD    . LYS A 1 4133 ? 208.146 181.319 219.393 1.00 11.04 ? 4133 LYS A CD    1 
ATOM   19697 C  CE    . LYS A 1 4133 ? 208.027 182.831 219.317 1.00 16.94 ? 4133 LYS A CE    1 
ATOM   19698 N  NZ    . LYS A 1 4133 ? 207.464 183.272 218.011 1.00 16.56 ? 4133 LYS A NZ    1 
ATOM   19699 N  N     . VAL A 1 4134 ? 204.442 180.823 223.354 1.00 2.43  ? 4134 VAL A N     1 
ATOM   19700 C  CA    . VAL A 1 4134 ? 203.639 181.549 224.346 1.00 1.68  ? 4134 VAL A CA    1 
ATOM   19701 C  C     . VAL A 1 4134 ? 204.519 181.909 225.538 1.00 2.10  ? 4134 VAL A C     1 
ATOM   19702 O  O     . VAL A 1 4134 ? 205.223 181.032 226.075 1.00 5.20  ? 4134 VAL A O     1 
ATOM   19703 C  CB    . VAL A 1 4134 ? 202.429 180.707 224.786 1.00 2.53  ? 4134 VAL A CB    1 
ATOM   19704 C  CG1   . VAL A 1 4134 ? 201.786 181.298 226.031 1.00 0.97  ? 4134 VAL A CG1   1 
ATOM   19705 C  CG2   . VAL A 1 4134 ? 201.411 180.611 223.658 1.00 1.38  ? 4134 VAL A CG2   1 
ATOM   19706 N  N     . PRO A 1 4135 ? 204.533 183.166 225.982 1.00 2.82  ? 4135 PRO A N     1 
ATOM   19707 C  CA    . PRO A 1 4135 ? 205.438 183.560 227.068 1.00 2.82  ? 4135 PRO A CA    1 
ATOM   19708 C  C     . PRO A 1 4135 ? 205.114 182.842 228.370 1.00 2.20  ? 4135 PRO A C     1 
ATOM   19709 O  O     . PRO A 1 4135 ? 203.955 182.574 228.689 1.00 1.68  ? 4135 PRO A O     1 
ATOM   19710 C  CB    . PRO A 1 4135 ? 205.207 185.070 227.194 1.00 2.16  ? 4135 PRO A CB    1 
ATOM   19711 C  CG    . PRO A 1 4135 ? 204.503 185.471 225.939 1.00 3.20  ? 4135 PRO A CG    1 
ATOM   19712 C  CD    . PRO A 1 4135 ? 203.703 184.289 225.524 1.00 1.37  ? 4135 PRO A CD    1 
ATOM   19713 N  N     . VAL A 1 4136 ? 206.170 182.544 229.129 1.00 2.84  ? 4136 VAL A N     1 
ATOM   19714 C  CA    . VAL A 1 4136 ? 206.004 181.925 230.441 1.00 2.46  ? 4136 VAL A CA    1 
ATOM   19715 C  C     . VAL A 1 4136 ? 205.262 182.858 231.386 1.00 1.59  ? 4136 VAL A C     1 
ATOM   19716 O  O     . VAL A 1 4136 ? 204.407 182.422 232.166 1.00 1.92  ? 4136 VAL A O     1 
ATOM   19717 C  CB    . VAL A 1 4136 ? 207.376 181.515 231.010 1.00 3.88  ? 4136 VAL A CB    1 
ATOM   19718 C  CG1   . VAL A 1 4136 ? 207.228 180.971 232.420 1.00 6.22  ? 4136 VAL A CG1   1 
ATOM   19719 C  CG2   . VAL A 1 4136 ? 208.030 180.482 230.114 1.00 2.35  ? 4136 VAL A CG2   1 
ATOM   19720 N  N     . ASN A 1 4137 ? 205.570 184.155 231.330 1.00 1.99  ? 4137 ASN A N     1 
ATOM   19721 C  CA    . ASN A 1 4137 ? 204.972 185.102 232.264 1.00 2.08  ? 4137 ASN A CA    1 
ATOM   19722 C  C     . ASN A 1 4137 ? 203.459 185.169 232.097 1.00 1.76  ? 4137 ASN A C     1 
ATOM   19723 O  O     . ASN A 1 4137 ? 202.725 185.299 233.082 1.00 3.49  ? 4137 ASN A O     1 
ATOM   19724 C  CB    . ASN A 1 4137 ? 205.598 186.485 232.081 1.00 3.53  ? 4137 ASN A CB    1 
ATOM   19725 C  CG    . ASN A 1 4137 ? 205.922 187.155 233.401 1.00 11.36 ? 4137 ASN A CG    1 
ATOM   19726 O  OD1   . ASN A 1 4137 ? 206.171 186.484 234.403 1.00 10.95 ? 4137 ASN A OD1   1 
ATOM   19727 N  ND2   . ASN A 1 4137 ? 205.919 188.482 233.409 1.00 10.80 ? 4137 ASN A ND2   1 
ATOM   19728 N  N     . LEU A 1 4138 ? 202.974 185.097 230.856 1.00 2.25  ? 4138 LEU A N     1 
ATOM   19729 C  CA    . LEU A 1 4138 ? 201.535 185.040 230.632 1.00 0.85  ? 4138 LEU A CA    1 
ATOM   19730 C  C     . LEU A 1 4138 ? 200.939 183.753 231.189 1.00 0.82  ? 4138 LEU A C     1 
ATOM   19731 O  O     . LEU A 1 4138 ? 199.858 183.768 231.787 1.00 1.15  ? 4138 LEU A O     1 
ATOM   19732 C  CB    . LEU A 1 4138 ? 201.223 185.168 229.143 1.00 1.97  ? 4138 LEU A CB    1 
ATOM   19733 C  CG    . LEU A 1 4138 ? 199.734 185.025 228.818 1.00 0.60  ? 4138 LEU A CG    1 
ATOM   19734 C  CD1   . LEU A 1 4138 ? 199.010 186.346 229.012 1.00 0.38  ? 4138 LEU A CD1   1 
ATOM   19735 C  CD2   . LEU A 1 4138 ? 199.524 184.478 227.421 1.00 0.42  ? 4138 LEU A CD2   1 
ATOM   19736 N  N     . LEU A 1 4139 ? 201.634 182.629 231.005 1.00 0.74  ? 4139 LEU A N     1 
ATOM   19737 C  CA    . LEU A 1 4139 ? 201.126 181.348 231.485 1.00 0.48  ? 4139 LEU A CA    1 
ATOM   19738 C  C     . LEU A 1 4139 ? 200.978 181.343 233.002 1.00 0.97  ? 4139 LEU A C     1 
ATOM   19739 O  O     . LEU A 1 4139 ? 199.991 180.825 233.535 1.00 2.07  ? 4139 LEU A O     1 
ATOM   19740 C  CB    . LEU A 1 4139 ? 202.044 180.215 231.034 1.00 0.61  ? 4139 LEU A CB    1 
ATOM   19741 C  CG    . LEU A 1 4139 ? 202.070 179.889 229.540 1.00 1.15  ? 4139 LEU A CG    1 
ATOM   19742 C  CD1   . LEU A 1 4139 ? 203.130 178.846 229.243 1.00 0.45  ? 4139 LEU A CD1   1 
ATOM   19743 C  CD2   . LEU A 1 4139 ? 200.707 179.418 229.063 1.00 0.68  ? 4139 LEU A CD2   1 
ATOM   19744 N  N     . ARG A 1 4140 ? 201.953 181.910 233.714 1.00 0.77  ? 4140 ARG A N     1 
ATOM   19745 C  CA    . ARG A 1 4140 ? 201.871 181.964 235.169 1.00 0.99  ? 4140 ARG A CA    1 
ATOM   19746 C  C     . ARG A 1 4140 ? 200.734 182.862 235.639 1.00 0.87  ? 4140 ARG A C     1 
ATOM   19747 O  O     . ARG A 1 4140 ? 200.074 182.552 236.638 1.00 0.89  ? 4140 ARG A O     1 
ATOM   19748 C  CB    . ARG A 1 4140 ? 203.201 182.439 235.751 1.00 1.56  ? 4140 ARG A CB    1 
ATOM   19749 C  CG    . ARG A 1 4140 ? 204.375 181.539 235.409 1.00 1.77  ? 4140 ARG A CG    1 
ATOM   19750 C  CD    . ARG A 1 4140 ? 205.682 182.102 235.933 1.00 1.49  ? 4140 ARG A CD    1 
ATOM   19751 N  NE    . ARG A 1 4140 ? 205.506 182.803 237.196 1.00 5.75  ? 4140 ARG A NE    1 
ATOM   19752 C  CZ    . ARG A 1 4140 ? 205.887 182.329 238.375 1.00 4.95  ? 4140 ARG A CZ    1 
ATOM   19753 N  NH1   . ARG A 1 4140 ? 206.471 181.148 238.486 1.00 4.99  ? 4140 ARG A NH1   1 
ATOM   19754 N  NH2   . ARG A 1 4140 ? 205.669 183.055 239.466 1.00 1.87  ? 4140 ARG A NH2   1 
ATOM   19755 N  N     . ALA A 1 4141 ? 200.489 183.968 234.938 1.00 1.13  ? 4141 ALA A N     1 
ATOM   19756 C  CA    . ALA A 1 4141 ? 199.454 184.913 235.339 1.00 0.95  ? 4141 ALA A CA    1 
ATOM   19757 C  C     . ALA A 1 4141 ? 198.045 184.371 235.149 1.00 1.43  ? 4141 ALA A C     1 
ATOM   19758 O  O     . ALA A 1 4141 ? 197.144 184.750 235.903 1.00 3.03  ? 4141 ALA A O     1 
ATOM   19759 C  CB    . ALA A 1 4141 ? 199.608 186.219 234.561 1.00 1.05  ? 4141 ALA A CB    1 
ATOM   19760 N  N     . GLY A 1 4142 ? 197.831 183.502 234.163 1.00 0.59  ? 4142 GLY A N     1 
ATOM   19761 C  CA    . GLY A 1 4142 ? 196.522 182.967 233.872 1.00 0.77  ? 4142 GLY A CA    1 
ATOM   19762 C  C     . GLY A 1 4142 ? 196.356 181.549 234.394 1.00 0.59  ? 4142 GLY A C     1 
ATOM   19763 O  O     . GLY A 1 4142 ? 197.280 180.927 234.911 1.00 0.74  ? 4142 GLY A O     1 
ATOM   19764 N  N     . ARG A 1 4143 ? 195.135 181.047 234.259 1.00 0.39  ? 4143 ARG A N     1 
ATOM   19765 C  CA    . ARG A 1 4143 ? 194.833 179.660 234.579 1.00 0.40  ? 4143 ARG A CA    1 
ATOM   19766 C  C     . ARG A 1 4143 ? 194.666 178.887 233.278 1.00 0.26  ? 4143 ARG A C     1 
ATOM   19767 O  O     . ARG A 1 4143 ? 193.888 179.285 232.406 1.00 0.91  ? 4143 ARG A O     1 
ATOM   19768 C  CB    . ARG A 1 4143 ? 193.595 179.536 235.462 1.00 0.56  ? 4143 ARG A CB    1 
ATOM   19769 C  CG    . ARG A 1 4143 ? 193.324 178.103 235.877 1.00 2.52  ? 4143 ARG A CG    1 
ATOM   19770 C  CD    . ARG A 1 4143 ? 192.156 177.980 236.825 1.00 7.27  ? 4143 ARG A CD    1 
ATOM   19771 N  NE    . ARG A 1 4143 ? 191.901 176.588 237.169 1.00 8.71  ? 4143 ARG A NE    1 
ATOM   19772 C  CZ    . ARG A 1 4143 ? 190.948 176.183 237.995 1.00 7.39  ? 4143 ARG A CZ    1 
ATOM   19773 N  NH1   . ARG A 1 4143 ? 190.207 177.045 238.670 1.00 5.18  ? 4143 ARG A NH1   1 
ATOM   19774 N  NH2   . ARG A 1 4143 ? 190.729 174.881 238.147 1.00 9.84  ? 4143 ARG A NH2   1 
ATOM   19775 N  N     . ILE A 1 4144 ? 195.397 177.790 233.157 1.00 0.24  ? 4144 ILE A N     1 
ATOM   19776 C  CA    . ILE A 1 4144 ? 195.520 177.054 231.907 1.00 0.44  ? 4144 ILE A CA    1 
ATOM   19777 C  C     . ILE A 1 4144 ? 194.482 175.943 231.870 1.00 0.38  ? 4144 ILE A C     1 
ATOM   19778 O  O     . ILE A 1 4144 ? 194.303 175.213 232.852 1.00 0.30  ? 4144 ILE A O     1 
ATOM   19779 C  CB    . ILE A 1 4144 ? 196.942 176.491 231.752 1.00 0.38  ? 4144 ILE A CB    1 
ATOM   19780 C  CG1   . ILE A 1 4144 ? 197.965 177.621 231.887 1.00 0.56  ? 4144 ILE A CG1   1 
ATOM   19781 C  CG2   . ILE A 1 4144 ? 197.091 175.749 230.437 1.00 0.45  ? 4144 ILE A CG2   1 
ATOM   19782 C  CD1   . ILE A 1 4144 ? 199.362 177.156 232.199 1.00 0.97  ? 4144 ILE A CD1   1 
ATOM   19783 N  N     . PHE A 1 4145 ? 193.784 175.825 230.745 1.00 0.66  ? 4145 PHE A N     1 
ATOM   19784 C  CA    . PHE A 1 4145 ? 192.883 174.712 230.480 1.00 0.24  ? 4145 PHE A CA    1 
ATOM   19785 C  C     . PHE A 1 4145 ? 193.298 174.068 229.168 1.00 0.29  ? 4145 PHE A C     1 
ATOM   19786 O  O     . PHE A 1 4145 ? 193.342 174.740 228.131 1.00 1.56  ? 4145 PHE A O     1 
ATOM   19787 C  CB    . PHE A 1 4145 ? 191.427 175.174 230.426 1.00 0.52  ? 4145 PHE A CB    1 
ATOM   19788 C  CG    . PHE A 1 4145 ? 190.928 175.734 231.720 1.00 1.59  ? 4145 PHE A CG    1 
ATOM   19789 C  CD1   . PHE A 1 4145 ? 190.428 174.900 232.704 1.00 1.86  ? 4145 PHE A CD1   1 
ATOM   19790 C  CD2   . PHE A 1 4145 ? 190.967 177.097 231.957 1.00 1.60  ? 4145 PHE A CD2   1 
ATOM   19791 C  CE1   . PHE A 1 4145 ? 189.976 175.417 233.899 1.00 5.21  ? 4145 PHE A CE1   1 
ATOM   19792 C  CE2   . PHE A 1 4145 ? 190.515 177.617 233.147 1.00 1.13  ? 4145 PHE A CE2   1 
ATOM   19793 C  CZ    . PHE A 1 4145 ? 190.019 176.777 234.119 1.00 4.80  ? 4145 PHE A CZ    1 
ATOM   19794 N  N     . VAL A 1 4146 ? 193.610 172.782 229.213 1.00 0.25  ? 4146 VAL A N     1 
ATOM   19795 C  CA    . VAL A 1 4146 ? 194.050 172.047 228.034 1.00 0.44  ? 4146 VAL A CA    1 
ATOM   19796 C  C     . VAL A 1 4146 ? 192.840 171.393 227.383 1.00 0.31  ? 4146 VAL A C     1 
ATOM   19797 O  O     . VAL A 1 4146 ? 192.052 170.715 228.050 1.00 0.23  ? 4146 VAL A O     1 
ATOM   19798 C  CB    . VAL A 1 4146 ? 195.117 171.002 228.400 1.00 0.30  ? 4146 VAL A CB    1 
ATOM   19799 C  CG1   . VAL A 1 4146 ? 195.285 169.991 227.273 1.00 0.59  ? 4146 VAL A CG1   1 
ATOM   19800 C  CG2   . VAL A 1 4146 ? 196.435 171.679 228.704 1.00 0.14  ? 4146 VAL A CG2   1 
ATOM   19801 N  N     . PHE A 1 4147 ? 192.687 171.606 226.082 1.00 0.46  ? 4147 PHE A N     1 
ATOM   19802 C  CA    . PHE A 1 4147 ? 191.631 170.981 225.297 1.00 0.64  ? 4147 PHE A CA    1 
ATOM   19803 C  C     . PHE A 1 4147 ? 192.266 170.034 224.292 1.00 0.60  ? 4147 PHE A C     1 
ATOM   19804 O  O     . PHE A 1 4147 ? 193.110 170.441 223.490 1.00 0.94  ? 4147 PHE A O     1 
ATOM   19805 C  CB    . PHE A 1 4147 ? 190.767 172.034 224.607 1.00 0.91  ? 4147 PHE A CB    1 
ATOM   19806 C  CG    . PHE A 1 4147 ? 189.938 172.828 225.560 1.00 1.09  ? 4147 PHE A CG    1 
ATOM   19807 C  CD1   . PHE A 1 4147 ? 190.461 173.942 226.186 1.00 0.88  ? 4147 PHE A CD1   1 
ATOM   19808 C  CD2   . PHE A 1 4147 ? 188.639 172.450 225.850 1.00 1.04  ? 4147 PHE A CD2   1 
ATOM   19809 C  CE1   . PHE A 1 4147 ? 189.708 174.665 227.076 1.00 0.59  ? 4147 PHE A CE1   1 
ATOM   19810 C  CE2   . PHE A 1 4147 ? 187.876 173.176 226.738 1.00 1.89  ? 4147 PHE A CE2   1 
ATOM   19811 C  CZ    . PHE A 1 4147 ? 188.411 174.287 227.351 1.00 2.12  ? 4147 PHE A CZ    1 
ATOM   19812 N  N     . GLU A 1 4148 ? 191.855 168.776 224.346 1.00 0.94  ? 4148 GLU A N     1 
ATOM   19813 C  CA    . GLU A 1 4148 ? 192.483 167.712 223.580 1.00 1.56  ? 4148 GLU A CA    1 
ATOM   19814 C  C     . GLU A 1 4148 ? 191.428 166.652 223.326 1.00 2.66  ? 4148 GLU A C     1 
ATOM   19815 O  O     . GLU A 1 4148 ? 190.300 166.758 223.822 1.00 4.18  ? 4148 GLU A O     1 
ATOM   19816 C  CB    . GLU A 1 4148 ? 193.693 167.136 224.330 1.00 2.26  ? 4148 GLU A CB    1 
ATOM   19817 C  CG    . GLU A 1 4148 ? 193.356 166.383 225.602 1.00 2.95  ? 4148 GLU A CG    1 
ATOM   19818 C  CD    . GLU A 1 4148 ? 194.590 166.022 226.404 1.00 6.17  ? 4148 GLU A CD    1 
ATOM   19819 O  OE1   . GLU A 1 4148 ? 195.512 165.402 225.833 1.00 3.92  ? 4148 GLU A OE1   1 
ATOM   19820 O  OE2   . GLU A 1 4148 ? 194.638 166.352 227.606 1.00 9.18  ? 4148 GLU A OE2   1 
ATOM   19821 N  N     . PRO A 1 4149 ? 191.743 165.633 222.526 1.00 3.72  ? 4149 PRO A N     1 
ATOM   19822 C  CA    . PRO A 1 4149 ? 190.806 164.521 222.357 1.00 3.52  ? 4149 PRO A CA    1 
ATOM   19823 C  C     . PRO A 1 4149 ? 190.448 163.904 223.696 1.00 3.49  ? 4149 PRO A C     1 
ATOM   19824 O  O     . PRO A 1 4149 ? 191.308 163.773 224.578 1.00 5.88  ? 4149 PRO A O     1 
ATOM   19825 C  CB    . PRO A 1 4149 ? 191.590 163.533 221.483 1.00 5.03  ? 4149 PRO A CB    1 
ATOM   19826 C  CG    . PRO A 1 4149 ? 192.479 164.389 220.684 1.00 5.56  ? 4149 PRO A CG    1 
ATOM   19827 C  CD    . PRO A 1 4149 ? 192.846 165.561 221.549 1.00 3.91  ? 4149 PRO A CD    1 
ATOM   19828 N  N     . PRO A 1 4150 ? 189.184 163.535 223.892 1.00 3.04  ? 4150 PRO A N     1 
ATOM   19829 C  CA    . PRO A 1 4150 ? 188.800 162.904 225.150 1.00 3.86  ? 4150 PRO A CA    1 
ATOM   19830 C  C     . PRO A 1 4150 ? 189.555 161.610 225.352 1.00 3.95  ? 4150 PRO A C     1 
ATOM   19831 O  O     . PRO A 1 4150 ? 189.901 160.909 224.380 1.00 4.15  ? 4150 PRO A O     1 
ATOM   19832 C  CB    . PRO A 1 4150 ? 187.294 162.663 224.982 1.00 3.35  ? 4150 PRO A CB    1 
ATOM   19833 C  CG    . PRO A 1 4150 ? 186.863 163.624 223.939 1.00 2.14  ? 4150 PRO A CG    1 
ATOM   19834 C  CD    . PRO A 1 4150 ? 188.029 163.791 223.017 1.00 2.44  ? 4150 PRO A CD    1 
ATOM   19835 N  N     . PRO A 1 4151 ? 189.854 161.253 226.602 1.00 6.99  ? 4151 PRO A N     1 
ATOM   19836 C  CA    . PRO A 1 4151 ? 190.718 160.087 226.854 1.00 6.79  ? 4151 PRO A CA    1 
ATOM   19837 C  C     . PRO A 1 4151 ? 190.187 158.772 226.302 1.00 9.58  ? 4151 PRO A C     1 
ATOM   19838 O  O     . PRO A 1 4151 ? 190.993 157.893 225.974 1.00 21.82 ? 4151 PRO A O     1 
ATOM   19839 C  CB    . PRO A 1 4151 ? 190.829 160.054 228.386 1.00 5.63  ? 4151 PRO A CB    1 
ATOM   19840 C  CG    . PRO A 1 4151 ? 189.798 161.014 228.896 1.00 7.11  ? 4151 PRO A CG    1 
ATOM   19841 C  CD    . PRO A 1 4151 ? 189.578 162.019 227.828 1.00 4.78  ? 4151 PRO A CD    1 
ATOM   19842 N  N     . GLY A 1 4152 ? 188.876 158.597 226.189 1.00 4.04  ? 4152 GLY A N     1 
ATOM   19843 C  CA    . GLY A 1 4152 ? 188.360 157.342 225.692 1.00 1.65  ? 4152 GLY A CA    1 
ATOM   19844 C  C     . GLY A 1 4152 ? 186.954 157.465 225.150 1.00 1.30  ? 4152 GLY A C     1 
ATOM   19845 O  O     . GLY A 1 4152 ? 186.398 158.559 225.048 1.00 3.79  ? 4152 GLY A O     1 
ATOM   19846 N  N     . VAL A 1 4153 ? 186.386 156.306 224.802 1.00 1.11  ? 4153 VAL A N     1 
ATOM   19847 C  CA    . VAL A 1 4153 ? 185.056 156.264 224.196 1.00 0.70  ? 4153 VAL A CA    1 
ATOM   19848 C  C     . VAL A 1 4153 ? 184.008 156.803 225.159 1.00 0.53  ? 4153 VAL A C     1 
ATOM   19849 O  O     . VAL A 1 4153 ? 183.134 157.586 224.772 1.00 0.73  ? 4153 VAL A O     1 
ATOM   19850 C  CB    . VAL A 1 4153 ? 184.723 154.828 223.743 1.00 0.77  ? 4153 VAL A CB    1 
ATOM   19851 C  CG1   . VAL A 1 4153 ? 183.251 154.709 223.376 1.00 0.52  ? 4153 VAL A CG1   1 
ATOM   19852 C  CG2   . VAL A 1 4153 ? 185.603 154.426 222.576 1.00 0.37  ? 4153 VAL A CG2   1 
ATOM   19853 N  N     . LYS A 1 4154 ? 184.072 156.387 226.425 1.00 1.29  ? 4154 LYS A N     1 
ATOM   19854 C  CA    . LYS A 1 4154 ? 183.124 156.877 227.421 1.00 1.21  ? 4154 LYS A CA    1 
ATOM   19855 C  C     . LYS A 1 4154 ? 183.229 158.388 227.581 1.00 0.79  ? 4154 LYS A C     1 
ATOM   19856 O  O     . LYS A 1 4154 ? 182.216 159.097 227.580 1.00 1.10  ? 4154 LYS A O     1 
ATOM   19857 C  CB    . LYS A 1 4154 ? 183.366 156.176 228.756 1.00 1.93  ? 4154 LYS A CB    1 
ATOM   19858 C  CG    . LYS A 1 4154 ? 182.458 156.633 229.877 1.00 2.33  ? 4154 LYS A CG    1 
ATOM   19859 C  CD    . LYS A 1 4154 ? 182.739 155.858 231.149 1.00 4.80  ? 4154 LYS A CD    1 
ATOM   19860 C  CE    . LYS A 1 4154 ? 181.720 156.170 232.226 1.00 6.93  ? 4154 LYS A CE    1 
ATOM   19861 N  NZ    . LYS A 1 4154 ? 181.906 155.301 233.414 1.00 12.41 ? 4154 LYS A NZ    1 
ATOM   19862 N  N     . ALA A 1 4155 ? 184.453 158.902 227.706 1.00 1.07  ? 4155 ALA A N     1 
ATOM   19863 C  CA    . ALA A 1 4155 ? 184.637 160.337 227.877 1.00 1.43  ? 4155 ALA A CA    1 
ATOM   19864 C  C     . ALA A 1 4155 ? 184.256 161.102 226.616 1.00 2.70  ? 4155 ALA A C     1 
ATOM   19865 O  O     . ALA A 1 4155 ? 183.726 162.215 226.697 1.00 5.24  ? 4155 ALA A O     1 
ATOM   19866 C  CB    . ALA A 1 4155 ? 186.083 160.635 228.272 1.00 2.80  ? 4155 ALA A CB    1 
ATOM   19867 N  N     . ASN A 1 4156 ? 184.518 160.519 225.443 1.00 1.42  ? 4156 ASN A N     1 
ATOM   19868 C  CA    . ASN A 1 4156 ? 184.148 161.168 224.190 1.00 0.71  ? 4156 ASN A CA    1 
ATOM   19869 C  C     . ASN A 1 4156 ? 182.641 161.340 224.081 1.00 0.79  ? 4156 ASN A C     1 
ATOM   19870 O  O     . ASN A 1 4156 ? 182.156 162.406 223.681 1.00 1.38  ? 4156 ASN A O     1 
ATOM   19871 C  CB    . ASN A 1 4156 ? 184.684 160.358 223.008 1.00 0.94  ? 4156 ASN A CB    1 
ATOM   19872 C  CG    . ASN A 1 4156 ? 184.686 161.140 221.709 1.00 0.63  ? 4156 ASN A CG    1 
ATOM   19873 O  OD1   . ASN A 1 4156 ? 183.650 161.613 221.249 1.00 0.60  ? 4156 ASN A OD1   1 
ATOM   19874 N  ND2   . ASN A 1 4156 ? 185.858 161.265 221.103 1.00 1.26  ? 4156 ASN A ND2   1 
ATOM   19875 N  N     . MET A 1 4157 ? 181.883 160.307 224.440 1.00 0.52  ? 4157 MET A N     1 
ATOM   19876 C  CA    . MET A 1 4157 ? 180.436 160.356 224.279 1.00 0.50  ? 4157 MET A CA    1 
ATOM   19877 C  C     . MET A 1 4157 ? 179.775 161.236 225.330 1.00 1.87  ? 4157 MET A C     1 
ATOM   19878 O  O     . MET A 1 4157 ? 178.758 161.876 225.043 1.00 2.59  ? 4157 MET A O     1 
ATOM   19879 C  CB    . MET A 1 4157 ? 179.867 158.939 224.322 1.00 0.42  ? 4157 MET A CB    1 
ATOM   19880 C  CG    . MET A 1 4157 ? 179.695 158.327 222.944 1.00 0.38  ? 4157 MET A CG    1 
ATOM   19881 S  SD    . MET A 1 4157 ? 179.297 156.576 222.976 1.00 1.69  ? 4157 MET A SD    1 
ATOM   19882 C  CE    . MET A 1 4157 ? 177.521 156.661 222.845 1.00 0.79  ? 4157 MET A CE    1 
ATOM   19883 N  N     . LEU A 1 4158 ? 180.332 161.285 226.541 1.00 3.40  ? 4158 LEU A N     1 
ATOM   19884 C  CA    . LEU A 1 4158 ? 179.801 162.183 227.560 1.00 2.17  ? 4158 LEU A CA    1 
ATOM   19885 C  C     . LEU A 1 4158 ? 180.023 163.640 227.178 1.00 3.82  ? 4158 LEU A C     1 
ATOM   19886 O  O     . LEU A 1 4158 ? 179.173 164.496 227.451 1.00 6.28  ? 4158 LEU A O     1 
ATOM   19887 C  CB    . LEU A 1 4158 ? 180.436 161.873 228.914 1.00 3.44  ? 4158 LEU A CB    1 
ATOM   19888 C  CG    . LEU A 1 4158 ? 179.924 160.605 229.598 1.00 1.88  ? 4158 LEU A CG    1 
ATOM   19889 C  CD1   . LEU A 1 4158 ? 180.754 160.272 230.824 1.00 2.61  ? 4158 LEU A CD1   1 
ATOM   19890 C  CD2   . LEU A 1 4158 ? 178.456 160.748 229.961 1.00 3.52  ? 4158 LEU A CD2   1 
ATOM   19891 N  N     . ARG A 1 4159 ? 181.163 163.942 226.554 1.00 2.25  ? 4159 ARG A N     1 
ATOM   19892 C  CA    . ARG A 1 4159 ? 181.411 165.296 226.076 1.00 2.39  ? 4159 ARG A CA    1 
ATOM   19893 C  C     . ARG A 1 4159 ? 180.430 165.675 224.974 1.00 3.60  ? 4159 ARG A C     1 
ATOM   19894 O  O     . ARG A 1 4159 ? 179.969 166.820 224.906 1.00 9.02  ? 4159 ARG A O     1 
ATOM   19895 C  CB    . ARG A 1 4159 ? 182.851 165.425 225.580 1.00 4.62  ? 4159 ARG A CB    1 
ATOM   19896 C  CG    . ARG A 1 4159 ? 183.222 166.825 225.124 1.00 8.01  ? 4159 ARG A CG    1 
ATOM   19897 C  CD    . ARG A 1 4159 ? 184.680 166.919 224.713 1.00 11.92 ? 4159 ARG A CD    1 
ATOM   19898 N  NE    . ARG A 1 4159 ? 185.580 166.753 225.850 1.00 16.13 ? 4159 ARG A NE    1 
ATOM   19899 C  CZ    . ARG A 1 4159 ? 186.896 166.629 225.753 1.00 11.36 ? 4159 ARG A CZ    1 
ATOM   19900 N  NH1   . ARG A 1 4159 ? 187.516 166.734 224.589 1.00 7.22  ? 4159 ARG A NH1   1 
ATOM   19901 N  NH2   . ARG A 1 4159 ? 187.609 166.405 226.853 1.00 6.22  ? 4159 ARG A NH2   1 
ATOM   19902 N  N     . THR A 1 4160 ? 180.105 164.724 224.096 1.00 4.01  ? 4160 THR A N     1 
ATOM   19903 C  CA    . THR A 1 4160 ? 179.170 164.998 223.010 1.00 3.61  ? 4160 THR A CA    1 
ATOM   19904 C  C     . THR A 1 4160 ? 177.773 165.300 223.538 1.00 5.18  ? 4160 THR A C     1 
ATOM   19905 O  O     . THR A 1 4160 ? 177.120 166.247 223.082 1.00 5.19  ? 4160 THR A O     1 
ATOM   19906 C  CB    . THR A 1 4160 ? 179.133 163.814 222.043 1.00 1.72  ? 4160 THR A CB    1 
ATOM   19907 O  OG1   . THR A 1 4160 ? 180.382 163.726 221.349 1.00 2.25  ? 4160 THR A OG1   1 
ATOM   19908 C  CG2   . THR A 1 4160 ? 178.007 163.973 221.035 1.00 1.04  ? 4160 THR A CG2   1 
ATOM   19909 N  N     . PHE A 1 4161 ? 177.297 164.510 224.501 1.00 7.05  ? 4161 PHE A N     1 
ATOM   19910 C  CA    . PHE A 1 4161 ? 175.936 164.697 224.988 1.00 6.69  ? 4161 PHE A CA    1 
ATOM   19911 C  C     . PHE A 1 4161 ? 175.801 165.962 225.824 1.00 8.30  ? 4161 PHE A C     1 
ATOM   19912 O  O     . PHE A 1 4161 ? 174.703 166.519 225.926 1.00 14.48 ? 4161 PHE A O     1 
ATOM   19913 C  CB    . PHE A 1 4161 ? 175.487 163.471 225.781 1.00 3.55  ? 4161 PHE A CB    1 
ATOM   19914 C  CG    . PHE A 1 4161 ? 174.875 162.399 224.930 1.00 2.28  ? 4161 PHE A CG    1 
ATOM   19915 C  CD1   . PHE A 1 4161 ? 173.569 162.514 224.488 1.00 4.68  ? 4161 PHE A CD1   1 
ATOM   19916 C  CD2   . PHE A 1 4161 ? 175.607 161.285 224.563 1.00 2.37  ? 4161 PHE A CD2   1 
ATOM   19917 C  CE1   . PHE A 1 4161 ? 173.002 161.530 223.699 1.00 6.97  ? 4161 PHE A CE1   1 
ATOM   19918 C  CE2   . PHE A 1 4161 ? 175.048 160.301 223.777 1.00 2.38  ? 4161 PHE A CE2   1 
ATOM   19919 C  CZ    . PHE A 1 4161 ? 173.743 160.423 223.343 1.00 4.96  ? 4161 PHE A CZ    1 
ATOM   19920 N  N     . SER A 1 4162 ? 176.894 166.428 226.429 1.00 6.57  ? 4162 SER A N     1 
ATOM   19921 C  CA    . SER A 1 4162 ? 176.851 167.695 227.147 1.00 6.58  ? 4162 SER A CA    1 
ATOM   19922 C  C     . SER A 1 4162 ? 176.880 168.889 226.202 1.00 11.57 ? 4162 SER A C     1 
ATOM   19923 O  O     . SER A 1 4162 ? 176.275 169.925 226.502 1.00 19.32 ? 4162 SER A O     1 
ATOM   19924 C  CB    . SER A 1 4162 ? 178.013 167.780 228.138 1.00 6.98  ? 4162 SER A CB    1 
ATOM   19925 O  OG    . SER A 1 4162 ? 179.258 167.824 227.465 1.00 13.26 ? 4162 SER A OG    1 
ATOM   19926 N  N     . SER A 1 4163 ? 177.565 168.765 225.064 1.00 9.59  ? 4163 SER A N     1 
ATOM   19927 C  CA    . SER A 1 4163 ? 177.692 169.887 224.141 1.00 7.22  ? 4163 SER A CA    1 
ATOM   19928 C  C     . SER A 1 4163 ? 176.409 170.148 223.359 1.00 9.06  ? 4163 SER A C     1 
ATOM   19929 O  O     . SER A 1 4163 ? 176.162 171.290 222.955 1.00 18.45 ? 4163 SER A O     1 
ATOM   19930 C  CB    . SER A 1 4163 ? 178.855 169.648 223.178 1.00 5.33  ? 4163 SER A CB    1 
ATOM   19931 O  OG    . SER A 1 4163 ? 178.659 168.472 222.414 1.00 13.82 ? 4163 SER A OG    1 
ATOM   19932 N  N     . ILE A 1 4164 ? 175.593 169.126 223.131 1.00 7.46  ? 4164 ILE A N     1 
ATOM   19933 C  CA    . ILE A 1 4164 ? 174.366 169.262 222.353 1.00 8.69  ? 4164 ILE A CA    1 
ATOM   19934 C  C     . ILE A 1 4164 ? 173.224 169.557 223.320 1.00 14.37 ? 4164 ILE A C     1 
ATOM   19935 O  O     . ILE A 1 4164 ? 173.028 168.789 224.277 1.00 18.38 ? 4164 ILE A O     1 
ATOM   19936 C  CB    . ILE A 1 4164 ? 174.074 168.004 221.528 1.00 11.50 ? 4164 ILE A CB    1 
ATOM   19937 C  CG1   . ILE A 1 4164 ? 175.287 167.628 220.679 1.00 6.71  ? 4164 ILE A CG1   1 
ATOM   19938 C  CG2   . ILE A 1 4164 ? 172.895 168.245 220.615 1.00 12.74 ? 4164 ILE A CG2   1 
ATOM   19939 C  CD1   . ILE A 1 4164 ? 175.155 166.292 219.999 1.00 5.15  ? 4164 ILE A CD1   1 
ATOM   19940 N  N     . PRO A 1 4165 ? 172.470 170.639 223.126 1.00 15.61 ? 4165 PRO A N     1 
ATOM   19941 C  CA    . PRO A 1 4165 ? 171.360 170.948 224.036 1.00 9.56  ? 4165 PRO A CA    1 
ATOM   19942 C  C     . PRO A 1 4165 ? 170.321 169.838 224.067 1.00 11.32 ? 4165 PRO A C     1 
ATOM   19943 O  O     . PRO A 1 4165 ? 170.077 169.157 223.072 1.00 14.55 ? 4165 PRO A O     1 
ATOM   19944 C  CB    . PRO A 1 4165 ? 170.774 172.235 223.449 1.00 10.84 ? 4165 PRO A CB    1 
ATOM   19945 C  CG    . PRO A 1 4165 ? 171.916 172.866 222.730 1.00 12.27 ? 4165 PRO A CG    1 
ATOM   19946 C  CD    . PRO A 1 4165 ? 172.716 171.727 222.165 1.00 12.14 ? 4165 PRO A CD    1 
ATOM   19947 N  N     . VAL A 1 4166 ? 169.697 169.669 225.236 1.00 12.49 ? 4166 VAL A N     1 
ATOM   19948 C  CA    . VAL A 1 4166 ? 168.737 168.584 225.429 1.00 14.41 ? 4166 VAL A CA    1 
ATOM   19949 C  C     . VAL A 1 4166 ? 167.538 168.749 224.504 1.00 17.98 ? 4166 VAL A C     1 
ATOM   19950 O  O     . VAL A 1 4166 ? 167.050 167.775 223.918 1.00 18.39 ? 4166 VAL A O     1 
ATOM   19951 C  CB    . VAL A 1 4166 ? 168.310 168.509 226.907 1.00 12.81 ? 4166 VAL A CB    1 
ATOM   19952 C  CG1   . VAL A 1 4166 ? 167.234 167.457 227.098 1.00 12.10 ? 4166 VAL A CG1   1 
ATOM   19953 C  CG2   . VAL A 1 4166 ? 169.508 168.207 227.784 1.00 10.32 ? 4166 VAL A CG2   1 
ATOM   19954 N  N     . SER A 1 4167 ? 167.039 169.980 224.362 1.00 13.41 ? 4167 SER A N     1 
ATOM   19955 C  CA    . SER A 1 4167 ? 165.892 170.219 223.490 1.00 10.84 ? 4167 SER A CA    1 
ATOM   19956 C  C     . SER A 1 4167 ? 166.192 169.843 222.046 1.00 16.76 ? 4167 SER A C     1 
ATOM   19957 O  O     . SER A 1 4167 ? 165.275 169.512 221.285 1.00 18.13 ? 4167 SER A O     1 
ATOM   19958 C  CB    . SER A 1 4167 ? 165.467 171.684 223.577 1.00 13.57 ? 4167 SER A CB    1 
ATOM   19959 O  OG    . SER A 1 4167 ? 166.578 172.543 223.405 1.00 23.95 ? 4167 SER A OG    1 
ATOM   19960 N  N     . ARG A 1 4168 ? 167.466 169.894 221.650 1.00 17.16 ? 4168 ARG A N     1 
ATOM   19961 C  CA    . ARG A 1 4168 ? 167.859 169.463 220.314 1.00 12.84 ? 4168 ARG A CA    1 
ATOM   19962 C  C     . ARG A 1 4168 ? 167.540 167.986 220.096 1.00 12.86 ? 4168 ARG A C     1 
ATOM   19963 O  O     . ARG A 1 4168 ? 166.958 167.617 219.069 1.00 17.41 ? 4168 ARG A O     1 
ATOM   19964 C  CB    . ARG A 1 4168 ? 169.352 169.726 220.119 1.00 11.70 ? 4168 ARG A CB    1 
ATOM   19965 C  CG    . ARG A 1 4168 ? 169.941 169.349 218.773 1.00 10.31 ? 4168 ARG A CG    1 
ATOM   19966 C  CD    . ARG A 1 4168 ? 169.449 170.239 217.659 1.00 10.08 ? 4168 ARG A CD    1 
ATOM   19967 N  NE    . ARG A 1 4168 ? 170.041 169.857 216.382 1.00 17.82 ? 4168 ARG A NE    1 
ATOM   19968 C  CZ    . ARG A 1 4168 ? 171.189 170.331 215.915 1.00 9.18  ? 4168 ARG A CZ    1 
ATOM   19969 N  NH1   . ARG A 1 4168 ? 171.916 171.189 216.610 1.00 6.48  ? 4168 ARG A NH1   1 
ATOM   19970 N  NH2   . ARG A 1 4168 ? 171.616 169.931 214.722 1.00 3.39  ? 4168 ARG A NH2   1 
ATOM   19971 N  N     . ILE A 1 4169 ? 167.904 167.132 221.055 1.00 11.72 ? 4169 ILE A N     1 
ATOM   19972 C  CA    . ILE A 1 4169 ? 167.672 165.696 220.911 1.00 12.11 ? 4169 ILE A CA    1 
ATOM   19973 C  C     . ILE A 1 4169 ? 166.194 165.362 221.077 1.00 12.52 ? 4169 ILE A C     1 
ATOM   19974 O  O     . ILE A 1 4169 ? 165.664 164.477 220.397 1.00 16.47 ? 4169 ILE A O     1 
ATOM   19975 C  CB    . ILE A 1 4169 ? 168.540 164.894 221.902 1.00 12.30 ? 4169 ILE A CB    1 
ATOM   19976 C  CG1   . ILE A 1 4169 ? 170.035 165.084 221.638 1.00 10.09 ? 4169 ILE A CG1   1 
ATOM   19977 C  CG2   . ILE A 1 4169 ? 168.200 163.423 221.862 1.00 13.42 ? 4169 ILE A CG2   1 
ATOM   19978 C  CD1   . ILE A 1 4169 ? 170.649 166.232 222.359 1.00 13.68 ? 4169 ILE A CD1   1 
ATOM   19979 N  N     . CYS A 1 4170 ? 165.501 166.071 221.969 1.00 17.55 ? 4170 CYS A N     1 
ATOM   19980 C  CA    . CYS A 1 4170 ? 164.170 165.680 222.415 1.00 15.20 ? 4170 CYS A CA    1 
ATOM   19981 C  C     . CYS A 1 4170 ? 163.053 166.277 221.564 1.00 19.12 ? 4170 CYS A C     1 
ATOM   19982 O  O     . CYS A 1 4170 ? 161.954 166.520 222.081 1.00 23.74 ? 4170 CYS A O     1 
ATOM   19983 C  CB    . CYS A 1 4170 ? 163.981 166.065 223.883 1.00 14.43 ? 4170 CYS A CB    1 
ATOM   19984 S  SG    . CYS A 1 4170 ? 165.163 165.293 225.010 1.00 43.43 ? 4170 CYS A SG    1 
ATOM   19985 N  N     . LYS A 1 4171 ? 163.297 166.520 220.279 1.00 20.80 ? 4171 LYS A N     1 
ATOM   19986 C  CA    . LYS A 1 4171 ? 162.256 167.050 219.411 1.00 15.75 ? 4171 LYS A CA    1 
ATOM   19987 C  C     . LYS A 1 4171 ? 161.197 165.979 219.136 1.00 21.93 ? 4171 LYS A C     1 
ATOM   19988 O  O     . LYS A 1 4171 ? 161.275 164.846 219.621 1.00 27.51 ? 4171 LYS A O     1 
ATOM   19989 C  CB    . LYS A 1 4171 ? 162.862 167.588 218.118 1.00 14.10 ? 4171 LYS A CB    1 
ATOM   19990 C  CG    . LYS A 1 4171 ? 162.986 169.105 218.097 1.00 7.12  ? 4171 LYS A CG    1 
ATOM   19991 C  CD    . LYS A 1 4171 ? 163.895 169.598 216.983 1.00 13.35 ? 4171 LYS A CD    1 
ATOM   19992 C  CE    . LYS A 1 4171 ? 163.426 169.132 215.616 1.00 15.37 ? 4171 LYS A CE    1 
ATOM   19993 N  NZ    . LYS A 1 4171 ? 162.111 169.711 215.235 1.00 10.97 ? 4171 LYS A NZ    1 
ATOM   19994 N  N     . SER A 1 4172 ? 160.191 166.354 218.342 1.00 21.01 ? 4172 SER A N     1 
ATOM   19995 C  CA    . SER A 1 4172 ? 158.957 165.589 218.166 1.00 17.70 ? 4172 SER A CA    1 
ATOM   19996 C  C     . SER A 1 4172 ? 159.187 164.133 217.758 1.00 23.45 ? 4172 SER A C     1 
ATOM   19997 O  O     . SER A 1 4172 ? 158.559 163.242 218.342 1.00 27.17 ? 4172 SER A O     1 
ATOM   19998 C  CB    . SER A 1 4172 ? 158.047 166.284 217.149 1.00 23.70 ? 4172 SER A CB    1 
ATOM   19999 O  OG    . SER A 1 4172 ? 157.745 167.609 217.552 1.00 31.43 ? 4172 SER A OG    1 
ATOM   20000 N  N     . PRO A 1 4173 ? 160.045 163.830 216.781 1.00 22.33 ? 4173 PRO A N     1 
ATOM   20001 C  CA    . PRO A 1 4173 ? 160.315 162.416 216.478 1.00 14.49 ? 4173 PRO A CA    1 
ATOM   20002 C  C     . PRO A 1 4173 ? 161.095 161.760 217.606 1.00 20.17 ? 4173 PRO A C     1 
ATOM   20003 O  O     . PRO A 1 4173 ? 162.223 162.152 217.913 1.00 21.90 ? 4173 PRO A O     1 
ATOM   20004 C  CB    . PRO A 1 4173 ? 161.127 162.476 215.179 1.00 10.31 ? 4173 PRO A CB    1 
ATOM   20005 C  CG    . PRO A 1 4173 ? 160.875 163.824 214.621 1.00 15.85 ? 4173 PRO A CG    1 
ATOM   20006 C  CD    . PRO A 1 4173 ? 160.702 164.714 215.801 1.00 17.09 ? 4173 PRO A CD    1 
ATOM   20007 N  N     . ASN A 1 4174 ? 160.480 160.750 218.227 1.00 17.75 ? 4174 ASN A N     1 
ATOM   20008 C  CA    . ASN A 1 4174 ? 161.120 160.062 219.342 1.00 17.66 ? 4174 ASN A CA    1 
ATOM   20009 C  C     . ASN A 1 4174 ? 162.364 159.300 218.914 1.00 15.38 ? 4174 ASN A C     1 
ATOM   20010 O  O     . ASN A 1 4174 ? 163.253 159.071 219.740 1.00 17.04 ? 4174 ASN A O     1 
ATOM   20011 C  CB    . ASN A 1 4174 ? 160.131 159.103 220.004 1.00 19.74 ? 4174 ASN A CB    1 
ATOM   20012 C  CG    . ASN A 1 4174 ? 159.047 159.826 220.772 1.00 19.81 ? 4174 ASN A CG    1 
ATOM   20013 O  OD1   . ASN A 1 4174 ? 159.059 161.052 220.877 1.00 22.37 ? 4174 ASN A OD1   1 
ATOM   20014 N  ND2   . ASN A 1 4174 ? 158.098 159.071 221.309 1.00 19.87 ? 4174 ASN A ND2   1 
ATOM   20015 N  N     . GLU A 1 4175 ? 162.446 158.909 217.645 1.00 13.13 ? 4175 GLU A N     1 
ATOM   20016 C  CA    . GLU A 1 4175 ? 163.596 158.183 217.127 1.00 11.67 ? 4175 GLU A CA    1 
ATOM   20017 C  C     . GLU A 1 4175 ? 164.821 159.070 216.952 1.00 10.94 ? 4175 GLU A C     1 
ATOM   20018 O  O     . GLU A 1 4175 ? 165.903 158.552 216.663 1.00 15.29 ? 4175 GLU A O     1 
ATOM   20019 C  CB    . GLU A 1 4175 ? 163.234 157.523 215.792 1.00 10.39 ? 4175 GLU A CB    1 
ATOM   20020 C  CG    . GLU A 1 4175 ? 162.241 156.368 215.907 1.00 12.07 ? 4175 GLU A CG    1 
ATOM   20021 C  CD    . GLU A 1 4175 ? 160.824 156.816 216.235 1.00 17.52 ? 4175 GLU A CD    1 
ATOM   20022 O  OE1   . GLU A 1 4175 ? 160.570 158.039 216.284 1.00 21.37 ? 4175 GLU A OE1   1 
ATOM   20023 O  OE2   . GLU A 1 4175 ? 159.962 155.941 216.452 1.00 18.95 ? 4175 GLU A OE2   1 
ATOM   20024 N  N     . ARG A 1 4176 ? 164.671 160.385 217.123 1.00 8.42  ? 4176 ARG A N     1 
ATOM   20025 C  CA    . ARG A 1 4176 ? 165.806 161.293 216.985 1.00 8.34  ? 4176 ARG A CA    1 
ATOM   20026 C  C     . ARG A 1 4176 ? 166.859 161.023 218.051 1.00 8.16  ? 4176 ARG A C     1 
ATOM   20027 O  O     . ARG A 1 4176 ? 168.059 161.184 217.802 1.00 9.18  ? 4176 ARG A O     1 
ATOM   20028 C  CB    . ARG A 1 4176 ? 165.318 162.741 217.058 1.00 8.75  ? 4176 ARG A CB    1 
ATOM   20029 C  CG    . ARG A 1 4176 ? 166.402 163.786 216.872 1.00 7.95  ? 4176 ARG A CG    1 
ATOM   20030 C  CD    . ARG A 1 4176 ? 165.827 165.190 216.938 1.00 9.34  ? 4176 ARG A CD    1 
ATOM   20031 N  NE    . ARG A 1 4176 ? 164.595 165.314 216.167 1.00 13.24 ? 4176 ARG A NE    1 
ATOM   20032 C  CZ    . ARG A 1 4176 ? 164.488 165.977 215.026 1.00 13.28 ? 4176 ARG A CZ    1 
ATOM   20033 N  NH1   . ARG A 1 4176 ? 165.527 166.589 214.482 1.00 11.78 ? 4176 ARG A NH1   1 
ATOM   20034 N  NH2   . ARG A 1 4176 ? 163.311 166.030 214.411 1.00 11.84 ? 4176 ARG A NH2   1 
ATOM   20035 N  N     . ALA A 1 4177 ? 166.429 160.611 219.247 1.00 12.25 ? 4177 ALA A N     1 
ATOM   20036 C  CA    . ALA A 1 4177 ? 167.373 160.369 220.334 1.00 7.85  ? 4177 ALA A CA    1 
ATOM   20037 C  C     . ALA A 1 4177 ? 168.327 159.229 220.005 1.00 3.47  ? 4177 ALA A C     1 
ATOM   20038 O  O     . ALA A 1 4177 ? 169.528 159.314 220.285 1.00 3.42  ? 4177 ALA A O     1 
ATOM   20039 C  CB    . ALA A 1 4177 ? 166.618 160.082 221.630 1.00 9.64  ? 4177 ALA A CB    1 
ATOM   20040 N  N     . ARG A 1 4178 ? 167.812 158.150 219.417 1.00 2.53  ? 4178 ARG A N     1 
ATOM   20041 C  CA    . ARG A 1 4178 ? 168.666 157.018 219.078 1.00 3.77  ? 4178 ARG A CA    1 
ATOM   20042 C  C     . ARG A 1 4178 ? 169.629 157.360 217.949 1.00 4.46  ? 4178 ARG A C     1 
ATOM   20043 O  O     . ARG A 1 4178 ? 170.758 156.857 217.928 1.00 3.53  ? 4178 ARG A O     1 
ATOM   20044 C  CB    . ARG A 1 4178 ? 167.804 155.812 218.710 1.00 5.75  ? 4178 ARG A CB    1 
ATOM   20045 C  CG    . ARG A 1 4178 ? 168.553 154.498 218.640 1.00 3.53  ? 4178 ARG A CG    1 
ATOM   20046 C  CD    . ARG A 1 4178 ? 167.586 153.333 218.623 1.00 8.92  ? 4178 ARG A CD    1 
ATOM   20047 N  NE    . ARG A 1 4178 ? 168.135 152.152 219.279 1.00 14.24 ? 4178 ARG A NE    1 
ATOM   20048 C  CZ    . ARG A 1 4178 ? 167.697 151.665 220.432 1.00 16.17 ? 4178 ARG A CZ    1 
ATOM   20049 N  NH1   . ARG A 1 4178 ? 166.710 152.242 221.095 1.00 12.41 ? 4178 ARG A NH1   1 
ATOM   20050 N  NH2   . ARG A 1 4178 ? 168.270 150.575 220.932 1.00 20.56 ? 4178 ARG A NH2   1 
ATOM   20051 N  N     . LEU A 1 4179 ? 169.205 158.205 217.006 1.00 3.56  ? 4179 LEU A N     1 
ATOM   20052 C  CA    . LEU A 1 4179 ? 170.108 158.649 215.949 1.00 2.63  ? 4179 LEU A CA    1 
ATOM   20053 C  C     . LEU A 1 4179 ? 171.276 159.439 216.521 1.00 2.08  ? 4179 LEU A C     1 
ATOM   20054 O  O     . LEU A 1 4179 ? 172.425 159.254 216.103 1.00 1.99  ? 4179 LEU A O     1 
ATOM   20055 C  CB    . LEU A 1 4179 ? 169.349 159.492 214.926 1.00 5.62  ? 4179 LEU A CB    1 
ATOM   20056 C  CG    . LEU A 1 4179 ? 168.206 158.816 214.169 1.00 4.07  ? 4179 LEU A CG    1 
ATOM   20057 C  CD1   . LEU A 1 4179 ? 167.581 159.788 213.191 1.00 4.79  ? 4179 LEU A CD1   1 
ATOM   20058 C  CD2   . LEU A 1 4179 ? 168.703 157.584 213.450 1.00 3.56  ? 4179 LEU A CD2   1 
ATOM   20059 N  N     . TYR A 1 4180 ? 171.003 160.327 217.477 1.00 3.73  ? 4180 TYR A N     1 
ATOM   20060 C  CA    . TYR A 1 4180 ? 172.074 161.093 218.106 1.00 2.17  ? 4180 TYR A CA    1 
ATOM   20061 C  C     . TYR A 1 4180 ? 173.019 160.185 218.879 1.00 1.48  ? 4180 TYR A C     1 
ATOM   20062 O  O     . TYR A 1 4180 ? 174.235 160.405 218.888 1.00 1.54  ? 4180 TYR A O     1 
ATOM   20063 C  CB    . TYR A 1 4180 ? 171.487 162.168 219.016 1.00 3.13  ? 4180 TYR A CB    1 
ATOM   20064 C  CG    . TYR A 1 4180 ? 171.212 163.471 218.307 1.00 3.96  ? 4180 TYR A CG    1 
ATOM   20065 C  CD1   . TYR A 1 4180 ? 170.080 163.630 217.521 1.00 5.34  ? 4180 TYR A CD1   1 
ATOM   20066 C  CD2   . TYR A 1 4180 ? 172.088 164.539 218.418 1.00 4.85  ? 4180 TYR A CD2   1 
ATOM   20067 C  CE1   . TYR A 1 4180 ? 169.828 164.820 216.866 1.00 6.85  ? 4180 TYR A CE1   1 
ATOM   20068 C  CE2   . TYR A 1 4180 ? 171.846 165.729 217.770 1.00 6.38  ? 4180 TYR A CE2   1 
ATOM   20069 C  CZ    . TYR A 1 4180 ? 170.715 165.864 216.995 1.00 6.87  ? 4180 TYR A CZ    1 
ATOM   20070 O  OH    . TYR A 1 4180 ? 170.472 167.052 216.350 1.00 8.99  ? 4180 TYR A OH    1 
ATOM   20071 N  N     . PHE A 1 4181 ? 172.476 159.161 219.542 1.00 1.98  ? 4181 PHE A N     1 
ATOM   20072 C  CA    . PHE A 1 4181 ? 173.330 158.195 220.223 1.00 1.16  ? 4181 PHE A CA    1 
ATOM   20073 C  C     . PHE A 1 4181 ? 174.233 157.470 219.233 1.00 0.60  ? 4181 PHE A C     1 
ATOM   20074 O  O     . PHE A 1 4181 ? 175.432 157.303 219.483 1.00 0.50  ? 4181 PHE A O     1 
ATOM   20075 C  CB    . PHE A 1 4181 ? 172.476 157.194 221.002 1.00 1.59  ? 4181 PHE A CB    1 
ATOM   20076 C  CG    . PHE A 1 4181 ? 173.270 156.081 221.616 1.00 2.86  ? 4181 PHE A CG    1 
ATOM   20077 C  CD1   . PHE A 1 4181 ? 173.800 156.214 222.885 1.00 3.10  ? 4181 PHE A CD1   1 
ATOM   20078 C  CD2   . PHE A 1 4181 ? 173.499 154.904 220.921 1.00 2.30  ? 4181 PHE A CD2   1 
ATOM   20079 C  CE1   . PHE A 1 4181 ? 174.531 155.198 223.450 1.00 4.05  ? 4181 PHE A CE1   1 
ATOM   20080 C  CE2   . PHE A 1 4181 ? 174.239 153.888 221.482 1.00 3.29  ? 4181 PHE A CE2   1 
ATOM   20081 C  CZ    . PHE A 1 4181 ? 174.756 154.035 222.746 1.00 3.51  ? 4181 PHE A CZ    1 
ATOM   20082 N  N     . LEU A 1 4182 ? 173.672 157.029 218.105 1.00 0.73  ? 4182 LEU A N     1 
ATOM   20083 C  CA    . LEU A 1 4182 ? 174.477 156.366 217.086 1.00 0.82  ? 4182 LEU A CA    1 
ATOM   20084 C  C     . LEU A 1 4182 ? 175.543 157.301 216.541 1.00 0.42  ? 4182 LEU A C     1 
ATOM   20085 O  O     . LEU A 1 4182 ? 176.686 156.891 216.312 1.00 0.44  ? 4182 LEU A O     1 
ATOM   20086 C  CB    . LEU A 1 4182 ? 173.580 155.865 215.957 1.00 1.07  ? 4182 LEU A CB    1 
ATOM   20087 C  CG    . LEU A 1 4182 ? 172.715 154.647 216.271 1.00 2.48  ? 4182 LEU A CG    1 
ATOM   20088 C  CD1   . LEU A 1 4182 ? 171.624 154.509 215.226 1.00 5.38  ? 4182 LEU A CD1   1 
ATOM   20089 C  CD2   . LEU A 1 4182 ? 173.566 153.390 216.348 1.00 2.17  ? 4182 LEU A CD2   1 
ATOM   20090 N  N     . LEU A 1 4183 ? 175.183 158.566 216.326 1.00 0.40  ? 4183 LEU A N     1 
ATOM   20091 C  CA    . LEU A 1 4183 ? 176.160 159.557 215.901 1.00 0.38  ? 4183 LEU A CA    1 
ATOM   20092 C  C     . LEU A 1 4183 ? 177.234 159.766 216.961 1.00 0.42  ? 4183 LEU A C     1 
ATOM   20093 O  O     . LEU A 1 4183 ? 178.421 159.878 216.637 1.00 0.50  ? 4183 LEU A O     1 
ATOM   20094 C  CB    . LEU A 1 4183 ? 175.449 160.870 215.581 1.00 1.35  ? 4183 LEU A CB    1 
ATOM   20095 C  CG    . LEU A 1 4183 ? 176.299 161.988 214.983 1.00 2.76  ? 4183 LEU A CG    1 
ATOM   20096 C  CD1   . LEU A 1 4183 ? 177.107 161.462 213.810 1.00 1.50  ? 4183 LEU A CD1   1 
ATOM   20097 C  CD2   . LEU A 1 4183 ? 175.405 163.135 214.561 1.00 5.33  ? 4183 LEU A CD2   1 
ATOM   20098 N  N     . ALA A 1 4184 ? 176.837 159.822 218.236 1.00 0.29  ? 4184 ALA A N     1 
ATOM   20099 C  CA    . ALA A 1 4184 ? 177.815 159.983 219.306 1.00 0.30  ? 4184 ALA A CA    1 
ATOM   20100 C  C     . ALA A 1 4184 ? 178.741 158.777 219.394 1.00 0.26  ? 4184 ALA A C     1 
ATOM   20101 O  O     . ALA A 1 4184 ? 179.958 158.929 219.551 1.00 0.29  ? 4184 ALA A O     1 
ATOM   20102 C  CB    . ALA A 1 4184 ? 177.107 160.214 220.641 1.00 0.60  ? 4184 ALA A CB    1 
ATOM   20103 N  N     . TRP A 1 4185 ? 178.183 157.569 219.297 1.00 0.24  ? 4185 TRP A N     1 
ATOM   20104 C  CA    . TRP A 1 4185 ? 179.017 156.374 219.291 1.00 0.30  ? 4185 TRP A CA    1 
ATOM   20105 C  C     . TRP A 1 4185 ? 179.935 156.354 218.077 1.00 0.45  ? 4185 TRP A C     1 
ATOM   20106 O  O     . TRP A 1 4185 ? 181.127 156.052 218.196 1.00 0.53  ? 4185 TRP A O     1 
ATOM   20107 C  CB    . TRP A 1 4185 ? 178.143 155.120 219.321 1.00 0.90  ? 4185 TRP A CB    1 
ATOM   20108 C  CG    . TRP A 1 4185 ? 178.927 153.856 219.155 1.00 0.93  ? 4185 TRP A CG    1 
ATOM   20109 C  CD1   . TRP A 1 4185 ? 179.177 153.193 217.991 1.00 0.66  ? 4185 TRP A CD1   1 
ATOM   20110 C  CD2   . TRP A 1 4185 ? 179.576 153.108 220.189 1.00 1.58  ? 4185 TRP A CD2   1 
ATOM   20111 N  NE1   . TRP A 1 4185 ? 179.939 152.077 218.234 1.00 1.19  ? 4185 TRP A NE1   1 
ATOM   20112 C  CE2   . TRP A 1 4185 ? 180.196 152.002 219.577 1.00 1.83  ? 4185 TRP A CE2   1 
ATOM   20113 C  CE3   . TRP A 1 4185 ? 179.689 153.265 221.574 1.00 0.91  ? 4185 TRP A CE3   1 
ATOM   20114 C  CZ2   . TRP A 1 4185 ? 180.920 151.058 220.301 1.00 1.53  ? 4185 TRP A CZ2   1 
ATOM   20115 C  CZ3   . TRP A 1 4185 ? 180.408 152.330 222.288 1.00 1.25  ? 4185 TRP A CZ3   1 
ATOM   20116 C  CH2   . TRP A 1 4185 ? 181.014 151.240 221.651 1.00 1.59  ? 4185 TRP A CH2   1 
ATOM   20117 N  N     . PHE A 1 4186 ? 179.397 156.681 216.899 1.00 0.27  ? 4186 PHE A N     1 
ATOM   20118 C  CA    . PHE A 1 4186 ? 180.214 156.698 215.695 1.00 0.12  ? 4186 PHE A CA    1 
ATOM   20119 C  C     . PHE A 1 4186 ? 181.320 157.739 215.802 1.00 0.09  ? 4186 PHE A C     1 
ATOM   20120 O  O     . PHE A 1 4186 ? 182.462 157.484 215.411 1.00 0.12  ? 4186 PHE A O     1 
ATOM   20121 C  CB    . PHE A 1 4186 ? 179.333 156.961 214.469 1.00 0.19  ? 4186 PHE A CB    1 
ATOM   20122 C  CG    . PHE A 1 4186 ? 180.105 157.260 213.217 1.00 0.10  ? 4186 PHE A CG    1 
ATOM   20123 C  CD1   . PHE A 1 4186 ? 180.566 156.235 212.411 1.00 0.14  ? 4186 PHE A CD1   1 
ATOM   20124 C  CD2   . PHE A 1 4186 ? 180.365 158.570 212.839 1.00 0.23  ? 4186 PHE A CD2   1 
ATOM   20125 C  CE1   . PHE A 1 4186 ? 181.276 156.508 211.260 1.00 0.19  ? 4186 PHE A CE1   1 
ATOM   20126 C  CE2   . PHE A 1 4186 ? 181.076 158.846 211.690 1.00 0.21  ? 4186 PHE A CE2   1 
ATOM   20127 C  CZ    . PHE A 1 4186 ? 181.529 157.813 210.901 1.00 0.17  ? 4186 PHE A CZ    1 
ATOM   20128 N  N     . HIS A 1 4187 ? 180.996 158.916 216.336 1.00 0.23  ? 4187 HIS A N     1 
ATOM   20129 C  CA    . HIS A 1 4187 ? 182.002 159.961 216.486 1.00 0.13  ? 4187 HIS A CA    1 
ATOM   20130 C  C     . HIS A 1 4187 ? 183.081 159.553 217.484 1.00 0.13  ? 4187 HIS A C     1 
ATOM   20131 O  O     . HIS A 1 4187 ? 184.257 159.886 217.302 1.00 0.16  ? 4187 HIS A O     1 
ATOM   20132 C  CB    . HIS A 1 4187 ? 181.334 161.268 216.902 1.00 0.14  ? 4187 HIS A CB    1 
ATOM   20133 C  CG    . HIS A 1 4187 ? 182.278 162.421 217.019 1.00 0.31  ? 4187 HIS A CG    1 
ATOM   20134 N  ND1   . HIS A 1 4187 ? 182.741 163.116 215.924 1.00 0.23  ? 4187 HIS A ND1   1 
ATOM   20135 C  CD2   . HIS A 1 4187 ? 182.846 163.004 218.101 1.00 0.22  ? 4187 HIS A CD2   1 
ATOM   20136 C  CE1   . HIS A 1 4187 ? 183.557 164.073 216.326 1.00 0.34  ? 4187 HIS A CE1   1 
ATOM   20137 N  NE2   . HIS A 1 4187 ? 183.636 164.028 217.644 1.00 0.28  ? 4187 HIS A NE2   1 
ATOM   20138 N  N     . ALA A 1 4188 ? 182.703 158.842 218.546 1.00 0.12  ? 4188 ALA A N     1 
ATOM   20139 C  CA    . ALA A 1 4188 ? 183.691 158.394 219.521 1.00 0.15  ? 4188 ALA A CA    1 
ATOM   20140 C  C     . ALA A 1 4188 ? 184.616 157.339 218.932 1.00 0.34  ? 4188 ALA A C     1 
ATOM   20141 O  O     . ALA A 1 4188 ? 185.835 157.403 219.121 1.00 0.67  ? 4188 ALA A O     1 
ATOM   20142 C  CB    . ALA A 1 4188 ? 182.996 157.860 220.773 1.00 0.23  ? 4188 ALA A CB    1 
ATOM   20143 N  N     . ILE A 1 4189 ? 184.056 156.364 218.212 1.00 0.27  ? 4189 ILE A N     1 
ATOM   20144 C  CA    . ILE A 1 4189 ? 184.870 155.294 217.640 1.00 0.39  ? 4189 ILE A CA    1 
ATOM   20145 C  C     . ILE A 1 4189 ? 185.851 155.855 216.621 1.00 0.46  ? 4189 ILE A C     1 
ATOM   20146 O  O     . ILE A 1 4189 ? 187.032 155.488 216.607 1.00 1.94  ? 4189 ILE A O     1 
ATOM   20147 C  CB    . ILE A 1 4189 ? 183.973 154.206 217.023 1.00 0.57  ? 4189 ILE A CB    1 
ATOM   20148 C  CG1   . ILE A 1 4189 ? 183.041 153.607 218.078 1.00 1.13  ? 4189 ILE A CG1   1 
ATOM   20149 C  CG2   . ILE A 1 4189 ? 184.814 153.122 216.368 1.00 0.59  ? 4189 ILE A CG2   1 
ATOM   20150 C  CD1   . ILE A 1 4189 ? 183.722 153.216 219.364 1.00 0.48  ? 4189 ILE A CD1   1 
ATOM   20151 N  N     . ILE A 1 4190 ? 185.381 156.756 215.758 1.00 0.26  ? 4190 ILE A N     1 
ATOM   20152 C  CA    . ILE A 1 4190 ? 186.242 157.312 214.718 1.00 0.46  ? 4190 ILE A CA    1 
ATOM   20153 C  C     . ILE A 1 4190 ? 187.369 158.134 215.331 1.00 0.42  ? 4190 ILE A C     1 
ATOM   20154 O  O     . ILE A 1 4190 ? 188.524 158.047 214.901 1.00 0.47  ? 4190 ILE A O     1 
ATOM   20155 C  CB    . ILE A 1 4190 ? 185.403 158.137 213.720 1.00 0.29  ? 4190 ILE A CB    1 
ATOM   20156 C  CG1   . ILE A 1 4190 ? 184.380 157.248 213.011 1.00 0.29  ? 4190 ILE A CG1   1 
ATOM   20157 C  CG2   . ILE A 1 4190 ? 186.288 158.825 212.706 1.00 0.38  ? 4190 ILE A CG2   1 
ATOM   20158 C  CD1   . ILE A 1 4190 ? 184.910 155.903 212.590 1.00 0.96  ? 4190 ILE A CD1   1 
ATOM   20159 N  N     . GLN A 1 4191 ? 187.053 158.944 216.343 1.00 0.73  ? 4191 GLN A N     1 
ATOM   20160 C  CA    . GLN A 1 4191 ? 188.078 159.777 216.967 1.00 1.10  ? 4191 GLN A CA    1 
ATOM   20161 C  C     . GLN A 1 4191 ? 189.078 158.942 217.755 1.00 0.85  ? 4191 GLN A C     1 
ATOM   20162 O  O     . GLN A 1 4191 ? 190.282 159.226 217.734 1.00 2.76  ? 4191 GLN A O     1 
ATOM   20163 C  CB    . GLN A 1 4191 ? 187.430 160.827 217.866 1.00 0.77  ? 4191 GLN A CB    1 
ATOM   20164 C  CG    . GLN A 1 4191 ? 186.801 161.984 217.111 1.00 0.82  ? 4191 GLN A CG    1 
ATOM   20165 C  CD    . GLN A 1 4191 ? 186.658 163.227 217.964 1.00 2.40  ? 4191 GLN A CD    1 
ATOM   20166 O  OE1   . GLN A 1 4191 ? 186.036 163.199 219.023 1.00 7.40  ? 4191 GLN A OE1   1 
ATOM   20167 N  NE2   . GLN A 1 4191 ? 187.230 164.330 217.500 1.00 1.86  ? 4191 GLN A NE2   1 
ATOM   20168 N  N     . GLU A 1 4192 ? 188.594 157.901 218.438 1.00 0.59  ? 4192 GLU A N     1 
ATOM   20169 C  CA    . GLU A 1 4192 ? 189.488 157.074 219.295 1.00 0.88  ? 4192 GLU A CA    1 
ATOM   20170 C  C     . GLU A 1 4192 ? 190.476 156.274 218.426 1.00 1.75  ? 4192 GLU A C     1 
ATOM   20171 O  O     . GLU A 1 4192 ? 191.584 155.973 218.921 1.00 5.62  ? 4192 GLU A O     1 
ATOM   20172 C  CB    . GLU A 1 4192 ? 188.656 156.162 220.199 1.00 0.81  ? 4192 GLU A CB    1 
ATOM   20173 C  CG    . GLU A 1 4192 ? 188.082 156.881 221.417 1.00 0.84  ? 4192 GLU A CG    1 
ATOM   20174 C  CD    . GLU A 1 4192 ? 189.142 157.301 222.420 1.00 10.12 ? 4192 GLU A CD    1 
ATOM   20175 O  OE1   . GLU A 1 4192 ? 189.847 156.411 222.936 1.00 14.74 ? 4192 GLU A OE1   1 
ATOM   20176 O  OE2   . GLU A 1 4192 ? 189.264 158.515 222.684 1.00 11.24 ? 4192 GLU A OE2   1 
ATOM   20177 N  N     . ARG A 1 4193 ? 190.089 155.944 217.191 1.00 1.03  ? 4193 ARG A N     1 
ATOM   20178 C  CA    . ARG A 1 4193 ? 190.972 155.162 216.284 1.00 0.85  ? 4193 ARG A CA    1 
ATOM   20179 C  C     . ARG A 1 4193 ? 192.192 156.013 215.897 1.00 1.39  ? 4193 ARG A C     1 
ATOM   20180 O  O     . ARG A 1 4193 ? 193.235 155.423 215.543 1.00 3.98  ? 4193 ARG A O     1 
ATOM   20181 C  CB    . ARG A 1 4193 ? 190.195 154.677 215.054 1.00 0.75  ? 4193 ARG A CB    1 
ATOM   20182 C  CG    . ARG A 1 4193 ? 189.160 153.607 215.367 1.00 0.97  ? 4193 ARG A CG    1 
ATOM   20183 C  CD    . ARG A 1 4193 ? 188.580 152.986 214.107 1.00 1.47  ? 4193 ARG A CD    1 
ATOM   20184 N  NE    . ARG A 1 4193 ? 189.627 152.400 213.264 1.00 1.11  ? 4193 ARG A NE    1 
ATOM   20185 C  CZ    . ARG A 1 4193 ? 189.714 151.114 212.950 1.00 0.77  ? 4193 ARG A CZ    1 
ATOM   20186 N  NH1   . ARG A 1 4193 ? 188.828 150.256 213.422 1.00 0.70  ? 4193 ARG A NH1   1 
ATOM   20187 N  NH2   . ARG A 1 4193 ? 190.690 150.690 212.169 1.00 1.09  ? 4193 ARG A NH2   1 
ATOM   20188 N  N     . LEU A 1 4194 ? 192.069 157.342 215.972 1.00 2.15  ? 4194 LEU A N     1 
ATOM   20189 C  CA    . LEU A 1 4194 ? 193.205 158.245 215.656 1.00 1.87  ? 4194 LEU A CA    1 
ATOM   20190 C  C     . LEU A 1 4194 ? 194.346 157.998 216.656 1.00 2.94  ? 4194 LEU A C     1 
ATOM   20191 O  O     . LEU A 1 4194 ? 195.521 158.173 216.268 1.00 3.91  ? 4194 LEU A O     1 
ATOM   20192 C  CB    . LEU A 1 4194 ? 192.730 159.698 215.679 1.00 1.93  ? 4194 LEU A CB    1 
ATOM   20193 C  CG    . LEU A 1 4194 ? 191.704 160.081 214.608 1.00 3.56  ? 4194 LEU A CG    1 
ATOM   20194 C  CD1   . LEU A 1 4194 ? 191.143 161.470 214.859 1.00 2.48  ? 4194 LEU A CD1   1 
ATOM   20195 C  CD2   . LEU A 1 4194 ? 192.316 159.995 213.220 1.00 1.47  ? 4194 LEU A CD2   1 
ATOM   20196 N  N     . ARG A 1 4195 ? 194.010 157.599 217.887 1.00 2.88  ? 4195 ARG A N     1 
ATOM   20197 C  CA    . ARG A 1 4195 ? 195.047 157.298 218.909 1.00 2.92  ? 4195 ARG A CA    1 
ATOM   20198 C  C     . ARG A 1 4195 ? 195.976 156.210 218.351 1.00 4.49  ? 4195 ARG A C     1 
ATOM   20199 O  O     . ARG A 1 4195 ? 197.197 156.290 218.600 1.00 6.99  ? 4195 ARG A O     1 
ATOM   20200 C  CB    . ARG A 1 4195 ? 194.384 156.892 220.231 1.00 3.32  ? 4195 ARG A CB    1 
ATOM   20201 C  CG    . ARG A 1 4195 ? 193.572 158.015 220.859 1.00 8.06  ? 4195 ARG A CG    1 
ATOM   20202 C  CD    . ARG A 1 4195 ? 192.802 157.565 222.092 1.00 6.82  ? 4195 ARG A CD    1 
ATOM   20203 N  NE    . ARG A 1 4195 ? 192.183 158.697 222.791 1.00 18.64 ? 4195 ARG A NE    1 
ATOM   20204 C  CZ    . ARG A 1 4195 ? 192.863 159.703 223.330 1.00 10.31 ? 4195 ARG A CZ    1 
ATOM   20205 N  NH1   . ARG A 1 4195 ? 194.120 159.530 223.693 1.00 6.56  ? 4195 ARG A NH1   1 
ATOM   20206 N  NH2   . ARG A 1 4195 ? 192.280 160.874 223.508 1.00 8.84  ? 4195 ARG A NH2   1 
ATOM   20207 N  N     . TYR A 1 4196 ? 195.418 155.232 217.632 1.00 3.63  ? 4196 TYR A N     1 
ATOM   20208 C  CA    . TYR A 1 4196 ? 196.262 154.199 216.973 1.00 4.04  ? 4196 TYR A CA    1 
ATOM   20209 C  C     . TYR A 1 4196 ? 196.720 154.796 215.649 1.00 7.21  ? 4196 TYR A C     1 
ATOM   20210 O  O     . TYR A 1 4196 ? 196.323 154.286 214.580 1.00 4.89  ? 4196 TYR A O     1 
ATOM   20211 C  CB    . TYR A 1 4196 ? 195.432 152.913 216.922 1.00 3.77  ? 4196 TYR A CB    1 
ATOM   20212 C  CG    . TYR A 1 4196 ? 194.943 152.499 218.304 1.00 5.05  ? 4196 TYR A CG    1 
ATOM   20213 C  CD1   . TYR A 1 4196 ? 195.704 151.666 219.114 1.00 5.10  ? 4196 TYR A CD1   1 
ATOM   20214 C  CD2   . TYR A 1 4196 ? 193.737 152.969 218.810 1.00 3.89  ? 4196 TYR A CD2   1 
ATOM   20215 C  CE1   . TYR A 1 4196 ? 195.271 151.297 220.375 1.00 8.03  ? 4196 TYR A CE1   1 
ATOM   20216 C  CE2   . TYR A 1 4196 ? 193.295 152.607 220.071 1.00 4.55  ? 4196 TYR A CE2   1 
ATOM   20217 C  CZ    . TYR A 1 4196 ? 194.064 151.768 220.857 1.00 5.86  ? 4196 TYR A CZ    1 
ATOM   20218 O  OH    . TYR A 1 4196 ? 193.634 151.406 222.100 1.00 7.12  ? 4196 TYR A OH    1 
ATOM   20219 N  N     . ALA A 1 4197 ? 197.542 155.848 215.721 1.00 16.48 ? 4197 ALA A N     1 
ATOM   20220 C  CA    . ALA A 1 4197 ? 197.998 156.582 214.512 1.00 8.60  ? 4197 ALA A CA    1 
ATOM   20221 C  C     . ALA A 1 4197 ? 197.867 155.749 213.233 1.00 7.10  ? 4197 ALA A C     1 
ATOM   20222 O  O     . ALA A 1 4197 ? 197.032 156.135 212.393 1.00 8.44  ? 4197 ALA A O     1 
ATOM   20223 C  CB    . ALA A 1 4197 ? 199.416 157.085 214.716 1.00 8.34  ? 4197 ALA A CB    1 
ATOM   20224 N  N     . PRO A 1 4198 ? 198.634 154.656 213.021 1.00 30.00 ? 4198 PRO A N     1 
ATOM   20225 C  CA    . PRO A 1 4198 ? 198.591 153.942 211.743 1.00 30.00 ? 4198 PRO A CA    1 
ATOM   20226 C  C     . PRO A 1 4198 ? 197.466 152.927 211.522 1.00 30.00 ? 4198 PRO A C     1 
ATOM   20227 O  O     . PRO A 1 4198 ? 196.891 152.921 210.417 1.00 30.00 ? 4198 PRO A O     1 
ATOM   20228 C  CB    . PRO A 1 4198 ? 199.978 153.269 211.761 1.00 30.00 ? 4198 PRO A CB    1 
ATOM   20229 C  CG    . PRO A 1 4198 ? 200.187 152.911 213.213 1.00 30.00 ? 4198 PRO A CG    1 
ATOM   20230 C  CD    . PRO A 1 4198 ? 199.542 154.050 213.986 1.00 30.00 ? 4198 PRO A CD    1 
ATOM   20231 N  N     . LEU A 1 4199 ? 197.167 152.093 212.521 1.00 2.46  ? 4199 LEU A N     1 
ATOM   20232 C  CA    . LEU A 1 4199 ? 196.158 151.014 212.337 1.00 2.37  ? 4199 LEU A CA    1 
ATOM   20233 C  C     . LEU A 1 4199 ? 194.731 151.592 212.286 1.00 3.82  ? 4199 LEU A C     1 
ATOM   20234 O  O     . LEU A 1 4199 ? 193.982 151.218 211.360 1.00 5.74  ? 4199 LEU A O     1 
ATOM   20235 C  CB    . LEU A 1 4199 ? 196.313 149.992 213.464 1.00 3.87  ? 4199 LEU A CB    1 
ATOM   20236 C  CG    . LEU A 1 4199 ? 195.875 148.562 213.134 1.00 3.83  ? 4199 LEU A CG    1 
ATOM   20237 C  CD1   . LEU A 1 4199 ? 196.674 148.027 211.962 1.00 4.08  ? 4199 LEU A CD1   1 
ATOM   20238 C  CD2   . LEU A 1 4199 ? 196.035 147.660 214.345 1.00 2.85  ? 4199 LEU A CD2   1 
ATOM   20239 N  N     . GLY A 1 4200 ? 194.370 152.456 213.239 1.00 2.34  ? 4200 GLY A N     1 
ATOM   20240 C  CA    . GLY A 1 4200 ? 193.002 153.009 213.282 1.00 1.50  ? 4200 GLY A CA    1 
ATOM   20241 C  C     . GLY A 1 4200 ? 192.680 153.720 211.987 1.00 1.34  ? 4200 GLY A C     1 
ATOM   20242 O  O     . GLY A 1 4200 ? 191.571 153.506 211.457 1.00 1.16  ? 4200 GLY A O     1 
ATOM   20243 N  N     . TRP A 1 4201 ? 193.609 154.543 211.496 1.00 1.55  ? 4201 TRP A N     1 
ATOM   20244 C  CA    . TRP A 1 4201 ? 193.437 155.228 210.193 1.00 1.07  ? 4201 TRP A CA    1 
ATOM   20245 C  C     . TRP A 1 4201 ? 194.822 155.382 209.570 1.00 1.71  ? 4201 TRP A C     1 
ATOM   20246 O  O     . TRP A 1 4201 ? 195.791 155.565 210.327 1.00 4.86  ? 4201 TRP A O     1 
ATOM   20247 C  CB    . TRP A 1 4201 ? 192.765 156.596 210.372 1.00 1.40  ? 4201 TRP A CB    1 
ATOM   20248 C  CG    . TRP A 1 4201 ? 191.369 156.541 210.932 1.00 0.59  ? 4201 TRP A CG    1 
ATOM   20249 C  CD1   . TRP A 1 4201 ? 190.998 156.670 212.239 1.00 0.61  ? 4201 TRP A CD1   1 
ATOM   20250 C  CD2   . TRP A 1 4201 ? 190.149 156.330 210.188 1.00 0.76  ? 4201 TRP A CD2   1 
ATOM   20251 N  NE1   . TRP A 1 4201 ? 189.639 156.564 212.359 1.00 0.41  ? 4201 TRP A NE1   1 
ATOM   20252 C  CE2   . TRP A 1 4201 ? 189.091 156.353 211.121 1.00 0.56  ? 4201 TRP A CE2   1 
ATOM   20253 C  CE3   . TRP A 1 4201 ? 189.854 156.128 208.835 1.00 0.61  ? 4201 TRP A CE3   1 
ATOM   20254 C  CZ2   . TRP A 1 4201 ? 187.763 156.181 210.740 1.00 0.44  ? 4201 TRP A CZ2   1 
ATOM   20255 C  CZ3   . TRP A 1 4201 ? 188.539 155.956 208.462 1.00 0.66  ? 4201 TRP A CZ3   1 
ATOM   20256 C  CH2   . TRP A 1 4201 ? 187.510 155.984 209.403 1.00 0.50  ? 4201 TRP A CH2   1 
ATOM   20257 N  N     . SER A 1 4202 ? 194.919 155.301 208.242 1.00 2.65  ? 4202 SER A N     1 
ATOM   20258 C  CA    . SER A 1 4202 ? 196.241 155.398 207.575 1.00 2.54  ? 4202 SER A CA    1 
ATOM   20259 C  C     . SER A 1 4202 ? 196.857 156.765 207.898 1.00 1.48  ? 4202 SER A C     1 
ATOM   20260 O  O     . SER A 1 4202 ? 198.102 156.860 207.934 1.00 7.15  ? 4202 SER A O     1 
ATOM   20261 C  CB    . SER A 1 4202 ? 196.129 155.185 206.090 1.00 2.84  ? 4202 SER A CB    1 
ATOM   20262 O  OG    . SER A 1 4202 ? 195.586 156.331 205.448 1.00 5.05  ? 4202 SER A OG    1 
ATOM   20263 N  N     . LYS A 1 4203 ? 196.017 157.776 208.132 1.00 3.30  ? 4203 LYS A N     1 
ATOM   20264 C  CA    . LYS A 1 4203 ? 196.528 159.148 208.379 1.00 2.67  ? 4203 LYS A CA    1 
ATOM   20265 C  C     . LYS A 1 4203 ? 195.861 159.746 209.625 1.00 2.78  ? 4203 LYS A C     1 
ATOM   20266 O  O     . LYS A 1 4203 ? 194.832 159.194 210.069 1.00 4.17  ? 4203 LYS A O     1 
ATOM   20267 C  CB    . LYS A 1 4203 ? 196.247 160.027 207.154 1.00 3.70  ? 4203 LYS A CB    1 
ATOM   20268 C  CG    . LYS A 1 4203 ? 196.543 159.364 205.818 1.00 8.54  ? 4203 LYS A CG    1 
ATOM   20269 C  CD    . LYS A 1 4203 ? 196.361 160.286 204.620 1.00 7.88  ? 4203 LYS A CD    1 
ATOM   20270 C  CE    . LYS A 1 4203 ? 197.282 161.463 204.679 1.00 12.22 ? 4203 LYS A CE    1 
ATOM   20271 N  NZ    . LYS A 1 4203 ? 197.192 162.285 203.471 1.00 20.16 ? 4203 LYS A NZ    1 
ATOM   20272 N  N     . LYS A 1 4204 ? 196.427 160.832 210.158 1.00 4.11  ? 4204 LYS A N     1 
ATOM   20273 C  CA    . LYS A 1 4204 ? 195.861 161.503 211.327 1.00 2.85  ? 4204 LYS A CA    1 
ATOM   20274 C  C     . LYS A 1 4204 ? 194.859 162.564 210.865 1.00 4.14  ? 4204 LYS A C     1 
ATOM   20275 O  O     . LYS A 1 4204 ? 195.137 163.763 210.822 1.00 14.52 ? 4204 LYS A O     1 
ATOM   20276 C  CB    . LYS A 1 4204 ? 196.970 162.108 212.175 1.00 4.95  ? 4204 LYS A CB    1 
ATOM   20277 C  CG    . LYS A 1 4204 ? 196.491 162.783 213.444 1.00 9.70  ? 4204 LYS A CG    1 
ATOM   20278 C  CD    . LYS A 1 4204 ? 195.822 161.784 214.361 1.00 11.87 ? 4204 LYS A CD    1 
ATOM   20279 C  CE    . LYS A 1 4204 ? 196.832 160.765 214.845 1.00 9.20  ? 4204 LYS A CE    1 
ATOM   20280 N  NZ    . LYS A 1 4204 ? 197.835 161.385 215.754 1.00 18.69 ? 4204 LYS A NZ    1 
ATOM   20281 N  N     . TYR A 1 4205 ? 193.669 162.094 210.499 1.00 3.02  ? 4205 TYR A N     1 
ATOM   20282 C  CA    . TYR A 1 4205 ? 192.623 163.009 210.066 1.00 3.92  ? 4205 TYR A CA    1 
ATOM   20283 C  C     . TYR A 1 4205 ? 192.118 163.843 211.235 1.00 3.36  ? 4205 TYR A C     1 
ATOM   20284 O  O     . TYR A 1 4205 ? 192.150 163.421 212.394 1.00 4.16  ? 4205 TYR A O     1 
ATOM   20285 C  CB    . TYR A 1 4205 ? 191.454 162.256 209.438 1.00 1.51  ? 4205 TYR A CB    1 
ATOM   20286 C  CG    . TYR A 1 4205 ? 191.828 161.369 208.282 1.00 1.60  ? 4205 TYR A CG    1 
ATOM   20287 C  CD1   . TYR A 1 4205 ? 192.101 161.907 207.030 1.00 1.21  ? 4205 TYR A CD1   1 
ATOM   20288 C  CD2   . TYR A 1 4205 ? 191.876 159.993 208.431 1.00 1.37  ? 4205 TYR A CD2   1 
ATOM   20289 C  CE1   . TYR A 1 4205 ? 192.435 161.099 205.968 1.00 1.56  ? 4205 TYR A CE1   1 
ATOM   20290 C  CE2   . TYR A 1 4205 ? 192.206 159.178 207.375 1.00 1.69  ? 4205 TYR A CE2   1 
ATOM   20291 C  CZ    . TYR A 1 4205 ? 192.485 159.735 206.145 1.00 4.41  ? 4205 TYR A CZ    1 
ATOM   20292 O  OH    . TYR A 1 4205 ? 192.816 158.921 205.088 1.00 5.77  ? 4205 TYR A OH    1 
ATOM   20293 N  N     . GLU A 1 4206 ? 191.646 165.045 210.918 1.00 3.34  ? 4206 GLU A N     1 
ATOM   20294 C  CA    . GLU A 1 4206 ? 191.122 165.959 211.929 1.00 3.93  ? 4206 GLU A CA    1 
ATOM   20295 C  C     . GLU A 1 4206 ? 189.600 165.838 212.033 1.00 2.05  ? 4206 GLU A C     1 
ATOM   20296 O  O     . GLU A 1 4206 ? 188.856 166.794 211.826 1.00 5.07  ? 4206 GLU A O     1 
ATOM   20297 C  CB    . GLU A 1 4206 ? 191.549 167.388 211.620 1.00 2.88  ? 4206 GLU A CB    1 
ATOM   20298 C  CG    . GLU A 1 4206 ? 193.046 167.619 211.702 1.00 3.40  ? 4206 GLU A CG    1 
ATOM   20299 C  CD    . GLU A 1 4206 ? 193.402 169.078 211.907 1.00 14.86 ? 4206 GLU A CD    1 
ATOM   20300 O  OE1   . GLU A 1 4206 ? 192.864 169.932 211.170 1.00 23.29 ? 4206 GLU A OE1   1 
ATOM   20301 O  OE2   . GLU A 1 4206 ? 194.221 169.371 212.804 1.00 15.05 ? 4206 GLU A OE2   1 
ATOM   20302 N  N     . PHE A 1 4207 ? 189.139 164.632 212.350 1.00 1.68  ? 4207 PHE A N     1 
ATOM   20303 C  CA    . PHE A 1 4207 ? 187.743 164.459 212.728 1.00 1.60  ? 4207 PHE A CA    1 
ATOM   20304 C  C     . PHE A 1 4207 ? 187.496 165.209 214.031 1.00 3.07  ? 4207 PHE A C     1 
ATOM   20305 O  O     . PHE A 1 4207 ? 188.124 164.913 215.052 1.00 8.97  ? 4207 PHE A O     1 
ATOM   20306 C  CB    . PHE A 1 4207 ? 187.385 162.983 212.891 1.00 1.06  ? 4207 PHE A CB    1 
ATOM   20307 C  CG    . PHE A 1 4207 ? 187.697 162.134 211.696 1.00 0.98  ? 4207 PHE A CG    1 
ATOM   20308 C  CD1   . PHE A 1 4207 ? 187.000 162.295 210.511 1.00 0.76  ? 4207 PHE A CD1   1 
ATOM   20309 C  CD2   . PHE A 1 4207 ? 188.653 161.133 211.772 1.00 1.28  ? 4207 PHE A CD2   1 
ATOM   20310 C  CE1   . PHE A 1 4207 ? 187.273 161.499 209.417 1.00 0.59  ? 4207 PHE A CE1   1 
ATOM   20311 C  CE2   . PHE A 1 4207 ? 188.924 160.328 210.684 1.00 0.67  ? 4207 PHE A CE2   1 
ATOM   20312 C  CZ    . PHE A 1 4207 ? 188.236 160.514 209.503 1.00 0.78  ? 4207 PHE A CZ    1 
ATOM   20313 N  N     . GLY A 1 4208 ? 186.588 166.178 214.001 1.00 1.80  ? 4208 GLY A N     1 
ATOM   20314 C  CA    . GLY A 1 4208 ? 186.399 167.029 215.155 1.00 1.18  ? 4208 GLY A CA    1 
ATOM   20315 C  C     . GLY A 1 4208 ? 184.980 167.498 215.383 1.00 1.23  ? 4208 GLY A C     1 
ATOM   20316 O  O     . GLY A 1 4208 ? 184.024 166.885 214.903 1.00 2.57  ? 4208 GLY A O     1 
ATOM   20317 N  N     . GLU A 1 4209 ? 184.842 168.597 216.127 1.00 2.16  ? 4209 GLU A N     1 
ATOM   20318 C  CA    . GLU A 1 4209 ? 183.523 169.092 216.502 1.00 3.09  ? 4209 GLU A CA    1 
ATOM   20319 C  C     . GLU A 1 4209 ? 182.748 169.579 215.285 1.00 2.58  ? 4209 GLU A C     1 
ATOM   20320 O  O     . GLU A 1 4209 ? 181.521 169.420 215.219 1.00 1.73  ? 4209 GLU A O     1 
ATOM   20321 C  CB    . GLU A 1 4209 ? 183.672 170.206 217.542 1.00 3.10  ? 4209 GLU A CB    1 
ATOM   20322 C  CG    . GLU A 1 4209 ? 182.464 171.125 217.722 1.00 5.99  ? 4209 GLU A CG    1 
ATOM   20323 C  CD    . GLU A 1 4209 ? 181.263 170.441 218.370 1.00 14.81 ? 4209 GLU A CD    1 
ATOM   20324 O  OE1   . GLU A 1 4209 ? 181.265 169.203 218.529 1.00 5.10  ? 4209 GLU A OE1   1 
ATOM   20325 O  OE2   . GLU A 1 4209 ? 180.310 171.158 218.742 1.00 23.81 ? 4209 GLU A OE2   1 
ATOM   20326 N  N     . SER A 1 4210 ? 183.441 170.174 214.311 1.00 2.01  ? 4210 SER A N     1 
ATOM   20327 C  CA    . SER A 1 4210 ? 182.764 170.658 213.113 1.00 1.75  ? 4210 SER A CA    1 
ATOM   20328 C  C     . SER A 1 4210 ? 182.121 169.514 212.342 1.00 1.61  ? 4210 SER A C     1 
ATOM   20329 O  O     . SER A 1 4210 ? 181.000 169.647 211.837 1.00 2.58  ? 4210 SER A O     1 
ATOM   20330 C  CB    . SER A 1 4210 ? 183.748 171.421 212.224 1.00 2.17  ? 4210 SER A CB    1 
ATOM   20331 O  OG    . SER A 1 4210 ? 184.761 170.565 211.733 1.00 4.35  ? 4210 SER A OG    1 
ATOM   20332 N  N     . ASP A 1 4211 ? 182.816 168.380 212.237 1.00 1.48  ? 4211 ASP A N     1 
ATOM   20333 C  CA    . ASP A 1 4211 ? 182.227 167.209 211.601 1.00 1.40  ? 4211 ASP A CA    1 
ATOM   20334 C  C     . ASP A 1 4211 ? 181.014 166.715 212.376 1.00 1.68  ? 4211 ASP A C     1 
ATOM   20335 O  O     . ASP A 1 4211 ? 179.995 166.348 211.779 1.00 4.55  ? 4211 ASP A O     1 
ATOM   20336 C  CB    . ASP A 1 4211 ? 183.270 166.099 211.473 1.00 1.39  ? 4211 ASP A CB    1 
ATOM   20337 C  CG    . ASP A 1 4211 ? 184.328 166.408 210.435 1.00 4.31  ? 4211 ASP A CG    1 
ATOM   20338 O  OD1   . ASP A 1 4211 ? 184.239 167.470 209.787 1.00 7.84  ? 4211 ASP A OD1   1 
ATOM   20339 O  OD2   . ASP A 1 4211 ? 185.250 165.588 210.267 1.00 9.31  ? 4211 ASP A OD2   1 
ATOM   20340 N  N     . LEU A 1 4212 ? 181.101 166.704 213.706 1.00 1.45  ? 4212 LEU A N     1 
ATOM   20341 C  CA    . LEU A 1 4212 ? 179.981 166.250 214.522 1.00 0.71  ? 4212 LEU A CA    1 
ATOM   20342 C  C     . LEU A 1 4212 ? 178.782 167.185 214.397 1.00 0.89  ? 4212 LEU A C     1 
ATOM   20343 O  O     . LEU A 1 4212 ? 177.641 166.725 214.280 1.00 0.96  ? 4212 LEU A O     1 
ATOM   20344 C  CB    . LEU A 1 4212 ? 180.421 166.114 215.978 1.00 0.58  ? 4212 LEU A CB    1 
ATOM   20345 C  CG    . LEU A 1 4212 ? 179.365 165.692 217.000 1.00 0.49  ? 4212 LEU A CG    1 
ATOM   20346 C  CD1   . LEU A 1 4212 ? 178.819 164.310 216.682 1.00 0.34  ? 4212 LEU A CD1   1 
ATOM   20347 C  CD2   . LEU A 1 4212 ? 179.950 165.732 218.399 1.00 0.54  ? 4212 LEU A CD2   1 
ATOM   20348 N  N     . ARG A 1 4213 ? 179.016 168.502 214.425 1.00 1.70  ? 4213 ARG A N     1 
ATOM   20349 C  CA    . ARG A 1 4213 ? 177.905 169.442 214.284 1.00 1.77  ? 4213 ARG A CA    1 
ATOM   20350 C  C     . ARG A 1 4213 ? 177.248 169.335 212.915 1.00 1.77  ? 4213 ARG A C     1 
ATOM   20351 O  O     . ARG A 1 4213 ? 176.017 169.385 212.811 1.00 2.92  ? 4213 ARG A O     1 
ATOM   20352 C  CB    . ARG A 1 4213 ? 178.365 170.879 214.533 1.00 2.89  ? 4213 ARG A CB    1 
ATOM   20353 C  CG    . ARG A 1 4213 ? 178.777 171.190 215.958 1.00 5.93  ? 4213 ARG A CG    1 
ATOM   20354 C  CD    . ARG A 1 4213 ? 179.209 172.644 216.075 1.00 15.22 ? 4213 ARG A CD    1 
ATOM   20355 N  NE    . ARG A 1 4213 ? 179.635 172.999 217.423 1.00 10.51 ? 4213 ARG A NE    1 
ATOM   20356 C  CZ    . ARG A 1 4213 ? 180.106 174.190 217.768 1.00 22.36 ? 4213 ARG A CZ    1 
ATOM   20357 N  NH1   . ARG A 1 4213 ? 180.227 175.168 216.885 1.00 30.10 ? 4213 ARG A NH1   1 
ATOM   20358 N  NH2   . ARG A 1 4213 ? 180.468 174.404 219.030 1.00 24.98 ? 4213 ARG A NH2   1 
ATOM   20359 N  N     . SER A 1 4214 ? 178.046 169.196 211.854 1.00 1.63  ? 4214 SER A N     1 
ATOM   20360 C  CA    . SER A 1 4214 ? 177.476 169.026 210.522 1.00 1.11  ? 4214 SER A CA    1 
ATOM   20361 C  C     . SER A 1 4214 ? 176.654 167.747 210.439 1.00 1.50  ? 4214 SER A C     1 
ATOM   20362 O  O     . SER A 1 4214 ? 175.580 167.729 209.827 1.00 2.21  ? 4214 SER A O     1 
ATOM   20363 C  CB    . SER A 1 4214 ? 178.583 169.023 209.468 1.00 1.67  ? 4214 SER A CB    1 
ATOM   20364 O  OG    . SER A 1 4214 ? 179.243 170.273 209.418 1.00 5.86  ? 4214 SER A OG    1 
ATOM   20365 N  N     . ALA A 1 4215 ? 177.142 166.670 211.050 1.00 1.33  ? 4215 ALA A N     1 
ATOM   20366 C  CA    . ALA A 1 4215 ? 176.387 165.422 211.070 1.00 1.75  ? 4215 ALA A CA    1 
ATOM   20367 C  C     . ALA A 1 4215 ? 175.084 165.575 211.846 1.00 2.96  ? 4215 ALA A C     1 
ATOM   20368 O  O     . ALA A 1 4215 ? 174.060 164.994 211.470 1.00 4.25  ? 4215 ALA A O     1 
ATOM   20369 C  CB    . ALA A 1 4215 ? 177.244 164.304 211.661 1.00 1.00  ? 4215 ALA A CB    1 
ATOM   20370 N  N     . CYS A 1 4216 ? 175.103 166.350 212.934 1.00 2.84  ? 4216 CYS A N     1 
ATOM   20371 C  CA    . CYS A 1 4216 ? 173.876 166.595 213.687 1.00 2.58  ? 4216 CYS A CA    1 
ATOM   20372 C  C     . CYS A 1 4216 ? 172.869 167.393 212.870 1.00 3.36  ? 4216 CYS A C     1 
ATOM   20373 O  O     . CYS A 1 4216 ? 171.667 167.105 212.908 1.00 2.75  ? 4216 CYS A O     1 
ATOM   20374 C  CB    . CYS A 1 4216 ? 174.192 167.311 215.001 1.00 4.69  ? 4216 CYS A CB    1 
ATOM   20375 S  SG    . CYS A 1 4216 ? 175.103 166.314 216.203 1.00 8.86  ? 4216 CYS A SG    1 
ATOM   20376 N  N     . ASP A 1 4217 ? 173.333 168.406 212.132 1.00 4.66  ? 4217 ASP A N     1 
ATOM   20377 C  CA    . ASP A 1 4217 ? 172.428 169.165 211.274 1.00 3.05  ? 4217 ASP A CA    1 
ATOM   20378 C  C     . ASP A 1 4217 ? 171.853 168.287 210.171 1.00 2.72  ? 4217 ASP A C     1 
ATOM   20379 O  O     . ASP A 1 4217 ? 170.664 168.387 209.844 1.00 4.33  ? 4217 ASP A O     1 
ATOM   20380 C  CB    . ASP A 1 4217 ? 173.142 170.376 210.673 1.00 2.86  ? 4217 ASP A CB    1 
ATOM   20381 C  CG    . ASP A 1 4217 ? 173.655 171.339 211.726 1.00 12.53 ? 4217 ASP A CG    1 
ATOM   20382 O  OD1   . ASP A 1 4217 ? 172.849 171.787 212.568 1.00 19.90 ? 4217 ASP A OD1   1 
ATOM   20383 O  OD2   . ASP A 1 4217 ? 174.857 171.673 211.694 1.00 19.72 ? 4217 ASP A OD2   1 
ATOM   20384 N  N     . THR A 1 4218 ? 172.683 167.425 209.583 1.00 1.69  ? 4218 THR A N     1 
ATOM   20385 C  CA    . THR A 1 4218 ? 172.208 166.528 208.535 1.00 1.51  ? 4218 THR A CA    1 
ATOM   20386 C  C     . THR A 1 4218 ? 171.165 165.556 209.072 1.00 1.59  ? 4218 THR A C     1 
ATOM   20387 O  O     . THR A 1 4218 ? 170.151 165.290 208.415 1.00 1.71  ? 4218 THR A O     1 
ATOM   20388 C  CB    . THR A 1 4218 ? 173.389 165.777 207.920 1.00 1.24  ? 4218 THR A CB    1 
ATOM   20389 O  OG1   . THR A 1 4218 ? 174.244 166.708 207.251 1.00 4.16  ? 4218 THR A OG1   1 
ATOM   20390 C  CG2   . THR A 1 4218 ? 172.909 164.733 206.928 1.00 0.99  ? 4218 THR A CG2   1 
ATOM   20391 N  N     . VAL A 1 4219 ? 171.393 165.022 210.272 1.00 2.22  ? 4219 VAL A N     1 
ATOM   20392 C  CA    . VAL A 1 4219 ? 170.418 164.123 210.882 1.00 2.90  ? 4219 VAL A CA    1 
ATOM   20393 C  C     . VAL A 1 4219 ? 169.095 164.845 211.092 1.00 4.20  ? 4219 VAL A C     1 
ATOM   20394 O  O     . VAL A 1 4219 ? 168.021 164.314 210.790 1.00 10.11 ? 4219 VAL A O     1 
ATOM   20395 C  CB    . VAL A 1 4219 ? 170.967 163.550 212.203 1.00 2.98  ? 4219 VAL A CB    1 
ATOM   20396 C  CG1   . VAL A 1 4219 ? 169.837 163.012 213.066 1.00 5.36  ? 4219 VAL A CG1   1 
ATOM   20397 C  CG2   . VAL A 1 4219 ? 171.978 162.458 211.922 1.00 2.71  ? 4219 VAL A CG2   1 
ATOM   20398 N  N     . ASP A 1 4220 ? 169.154 166.078 211.600 1.00 3.14  ? 4220 ASP A N     1 
ATOM   20399 C  CA    . ASP A 1 4220 ? 167.933 166.831 211.865 1.00 3.43  ? 4220 ASP A CA    1 
ATOM   20400 C  C     . ASP A 1 4220 ? 167.241 167.242 210.570 1.00 5.05  ? 4220 ASP A C     1 
ATOM   20401 O  O     . ASP A 1 4220 ? 166.009 167.221 210.479 1.00 9.46  ? 4220 ASP A O     1 
ATOM   20402 C  CB    . ASP A 1 4220 ? 168.251 168.055 212.720 1.00 5.29  ? 4220 ASP A CB    1 
ATOM   20403 C  CG    . ASP A 1 4220 ? 168.463 167.704 214.174 1.00 10.97 ? 4220 ASP A CG    1 
ATOM   20404 O  OD1   . ASP A 1 4220 ? 169.326 168.332 214.813 1.00 12.99 ? 4220 ASP A OD1   1 
ATOM   20405 O  OD2   . ASP A 1 4220 ? 167.774 166.796 214.680 1.00 10.71 ? 4220 ASP A OD2   1 
ATOM   20406 N  N     . THR A 1 4221 ? 168.020 167.631 209.558 1.00 4.57  ? 4221 THR A N     1 
ATOM   20407 C  CA    . THR A 1 4221 ? 167.435 168.067 208.294 1.00 3.33  ? 4221 THR A CA    1 
ATOM   20408 C  C     . THR A 1 4221 ? 166.632 166.949 207.643 1.00 3.24  ? 4221 THR A C     1 
ATOM   20409 O  O     . THR A 1 4221 ? 165.478 167.144 207.245 1.00 5.43  ? 4221 THR A O     1 
ATOM   20410 C  CB    . THR A 1 4221 ? 168.533 168.559 207.349 1.00 2.99  ? 4221 THR A CB    1 
ATOM   20411 O  OG1   . THR A 1 4221 ? 169.124 169.754 207.875 1.00 6.80  ? 4221 THR A OG1   1 
ATOM   20412 C  CG2   . THR A 1 4221 ? 167.969 168.844 205.969 1.00 1.44  ? 4221 THR A CG2   1 
ATOM   20413 N  N     . TRP A 1 4222 ? 167.223 165.759 207.539 1.00 2.89  ? 4222 TRP A N     1 
ATOM   20414 C  CA    . TRP A 1 4222 ? 166.581 164.670 206.815 1.00 3.39  ? 4222 TRP A CA    1 
ATOM   20415 C  C     . TRP A 1 4222 ? 165.545 163.937 207.655 1.00 6.85  ? 4222 TRP A C     1 
ATOM   20416 O  O     . TRP A 1 4222 ? 164.588 163.386 207.100 1.00 7.12  ? 4222 TRP A O     1 
ATOM   20417 C  CB    . TRP A 1 4222 ? 167.644 163.706 206.293 1.00 1.81  ? 4222 TRP A CB    1 
ATOM   20418 C  CG    . TRP A 1 4222 ? 168.481 164.345 205.239 1.00 1.59  ? 4222 TRP A CG    1 
ATOM   20419 C  CD1   . TRP A 1 4222 ? 169.643 165.030 205.417 1.00 1.05  ? 4222 TRP A CD1   1 
ATOM   20420 C  CD2   . TRP A 1 4222 ? 168.205 164.380 203.836 1.00 0.87  ? 4222 TRP A CD2   1 
ATOM   20421 N  NE1   . TRP A 1 4222 ? 170.114 165.486 204.213 1.00 0.91  ? 4222 TRP A NE1   1 
ATOM   20422 C  CE2   . TRP A 1 4222 ? 169.251 165.098 203.224 1.00 0.91  ? 4222 TRP A CE2   1 
ATOM   20423 C  CE3   . TRP A 1 4222 ? 167.179 163.870 203.037 1.00 0.69  ? 4222 TRP A CE3   1 
ATOM   20424 C  CZ2   . TRP A 1 4222 ? 169.300 165.318 201.851 1.00 0.91  ? 4222 TRP A CZ2   1 
ATOM   20425 C  CZ3   . TRP A 1 4222 ? 167.229 164.090 201.675 1.00 0.97  ? 4222 TRP A CZ3   1 
ATOM   20426 C  CH2   . TRP A 1 4222 ? 168.282 164.807 201.095 1.00 1.30  ? 4222 TRP A CH2   1 
ATOM   20427 N  N     . LEU A 1 4223 ? 165.710 163.909 208.977 1.00 7.41  ? 4223 LEU A N     1 
ATOM   20428 C  CA    . LEU A 1 4223 ? 164.674 163.330 209.822 1.00 6.80  ? 4223 LEU A CA    1 
ATOM   20429 C  C     . LEU A 1 4223 ? 163.421 164.198 209.822 1.00 7.97  ? 4223 LEU A C     1 
ATOM   20430 O  O     . LEU A 1 4223 ? 162.300 163.680 209.779 1.00 11.52 ? 4223 LEU A O     1 
ATOM   20431 C  CB    . LEU A 1 4223 ? 165.195 163.138 211.244 1.00 11.22 ? 4223 LEU A CB    1 
ATOM   20432 C  CG    . LEU A 1 4223 ? 164.246 162.436 212.209 1.00 10.07 ? 4223 LEU A CG    1 
ATOM   20433 C  CD1   . LEU A 1 4223 ? 163.803 161.099 211.641 1.00 11.94 ? 4223 LEU A CD1   1 
ATOM   20434 C  CD2   . LEU A 1 4223 ? 164.921 162.258 213.549 1.00 8.03  ? 4223 LEU A CD2   1 
ATOM   20435 N  N     . ASP A 1 4224 ? 163.594 165.518 209.864 1.00 7.87  ? 4224 ASP A N     1 
ATOM   20436 C  CA    . ASP A 1 4224 ? 162.453 166.422 209.773 1.00 9.85  ? 4224 ASP A CA    1 
ATOM   20437 C  C     . ASP A 1 4224 ? 161.788 166.328 208.406 1.00 10.82 ? 4224 ASP A C     1 
ATOM   20438 O  O     . ASP A 1 4224 ? 160.563 166.450 208.296 1.00 20.04 ? 4224 ASP A O     1 
ATOM   20439 C  CB    . ASP A 1 4224 ? 162.895 167.857 210.060 1.00 10.93 ? 4224 ASP A CB    1 
ATOM   20440 C  CG    . ASP A 1 4224 ? 162.969 168.160 211.545 1.00 19.61 ? 4224 ASP A CG    1 
ATOM   20441 O  OD1   . ASP A 1 4224 ? 163.983 168.737 211.986 1.00 17.62 ? 4224 ASP A OD1   1 
ATOM   20442 O  OD2   . ASP A 1 4224 ? 162.008 167.825 212.269 1.00 24.65 ? 4224 ASP A OD2   1 
ATOM   20443 N  N     . ASP A 1 4225 ? 162.583 166.121 207.354 1.00 11.09 ? 4225 ASP A N     1 
ATOM   20444 C  CA    . ASP A 1 4225 ? 162.026 165.995 206.012 1.00 11.89 ? 4225 ASP A CA    1 
ATOM   20445 C  C     . ASP A 1 4225 ? 161.135 164.765 205.894 1.00 11.35 ? 4225 ASP A C     1 
ATOM   20446 O  O     . ASP A 1 4225 ? 160.065 164.823 205.277 1.00 21.31 ? 4225 ASP A O     1 
ATOM   20447 C  CB    . ASP A 1 4225 ? 163.157 165.947 204.984 1.00 14.69 ? 4225 ASP A CB    1 
ATOM   20448 C  CG    . ASP A 1 4225 ? 162.704 165.412 203.641 1.00 21.89 ? 4225 ASP A CG    1 
ATOM   20449 O  OD1   . ASP A 1 4225 ? 163.017 164.245 203.329 1.00 28.85 ? 4225 ASP A OD1   1 
ATOM   20450 O  OD2   . ASP A 1 4225 ? 162.038 166.159 202.894 1.00 27.99 ? 4225 ASP A OD2   1 
ATOM   20451 N  N     . THR A 1 4226 ? 161.552 163.643 206.480 1.00 10.66 ? 4226 THR A N     1 
ATOM   20452 C  CA    . THR A 1 4226 ? 160.767 162.416 206.371 1.00 16.25 ? 4226 THR A CA    1 
ATOM   20453 C  C     . THR A 1 4226 ? 159.636 162.390 207.394 1.00 21.55 ? 4226 THR A C     1 
ATOM   20454 O  O     . THR A 1 4226 ? 158.466 162.220 207.036 1.00 19.63 ? 4226 THR A O     1 
ATOM   20455 C  CB    . THR A 1 4226 ? 161.672 161.195 206.534 1.00 14.84 ? 4226 THR A CB    1 
ATOM   20456 O  OG1   . THR A 1 4226 ? 162.543 161.092 205.403 1.00 22.41 ? 4226 THR A OG1   1 
ATOM   20457 C  CG2   . THR A 1 4226 ? 160.833 159.938 206.617 1.00 16.04 ? 4226 THR A CG2   1 
ATOM   20458 N  N     . ALA A 1 4227 ? 159.968 162.552 208.672 1.00 19.67 ? 4227 ALA A N     1 
ATOM   20459 C  CA    . ALA A 1 4227 ? 158.961 162.625 209.729 1.00 18.53 ? 4227 ALA A CA    1 
ATOM   20460 C  C     . ALA A 1 4227 ? 158.405 164.041 209.740 1.00 23.21 ? 4227 ALA A C     1 
ATOM   20461 O  O     . ALA A 1 4227 ? 158.886 164.918 210.458 1.00 27.83 ? 4227 ALA A O     1 
ATOM   20462 C  CB    . ALA A 1 4227 ? 159.557 162.241 211.078 1.00 19.32 ? 4227 ALA A CB    1 
ATOM   20463 N  N     . LYS A 1 4228 ? 157.378 164.266 208.923 1.00 23.42 ? 4228 LYS A N     1 
ATOM   20464 C  CA    . LYS A 1 4228 ? 156.809 165.601 208.738 1.00 21.42 ? 4228 LYS A CA    1 
ATOM   20465 C  C     . LYS A 1 4228 ? 155.954 165.940 209.956 1.00 22.17 ? 4228 LYS A C     1 
ATOM   20466 O  O     . LYS A 1 4228 ? 154.730 165.788 209.965 1.00 23.11 ? 4228 LYS A O     1 
ATOM   20467 C  CB    . LYS A 1 4228 ? 156.006 165.669 207.447 1.00 14.34 ? 4228 LYS A CB    1 
ATOM   20468 C  CG    . LYS A 1 4228 ? 156.833 165.459 206.194 1.00 16.26 ? 4228 LYS A CG    1 
ATOM   20469 C  CD    . LYS A 1 4228 ? 156.163 166.080 204.980 1.00 26.05 ? 4228 LYS A CD    1 
ATOM   20470 C  CE    . LYS A 1 4228 ? 156.995 165.869 203.726 1.00 21.20 ? 4228 LYS A CE    1 
ATOM   20471 N  NZ    . LYS A 1 4228 ? 157.562 164.493 203.665 1.00 21.66 ? 4228 LYS A NZ    1 
ATOM   20472 N  N     . GLY A 1 4229 ? 156.626 166.412 211.000 1.00 20.06 ? 4229 GLY A N     1 
ATOM   20473 C  CA    . GLY A 1 4229 ? 155.939 166.803 212.222 1.00 21.62 ? 4229 GLY A CA    1 
ATOM   20474 C  C     . GLY A 1 4229 ? 155.181 165.675 212.887 1.00 21.95 ? 4229 GLY A C     1 
ATOM   20475 O  O     . GLY A 1 4229 ? 154.032 165.868 213.306 1.00 27.83 ? 4229 GLY A O     1 
ATOM   20476 N  N     . ARG A 1 4230 ? 155.792 164.501 212.988 1.00 22.25 ? 4230 ARG A N     1 
ATOM   20477 C  CA    . ARG A 1 4230 ? 155.159 163.331 213.576 1.00 20.83 ? 4230 ARG A CA    1 
ATOM   20478 C  C     . ARG A 1 4230 ? 155.855 162.959 214.878 1.00 22.39 ? 4230 ARG A C     1 
ATOM   20479 O  O     . ARG A 1 4230 ? 156.963 163.412 215.177 1.00 24.18 ? 4230 ARG A O     1 
ATOM   20480 C  CB    . ARG A 1 4230 ? 155.171 162.148 212.600 1.00 19.01 ? 4230 ARG A CB    1 
ATOM   20481 C  CG    . ARG A 1 4230 ? 153.962 162.103 211.679 1.00 14.18 ? 4230 ARG A CG    1 
ATOM   20482 C  CD    . ARG A 1 4230 ? 153.800 160.739 211.026 1.00 15.50 ? 4230 ARG A CD    1 
ATOM   20483 N  NE    . ARG A 1 4230 ? 154.454 160.670 209.724 1.00 28.38 ? 4230 ARG A NE    1 
ATOM   20484 C  CZ    . ARG A 1 4230 ? 155.718 160.315 209.532 1.00 28.21 ? 4230 ARG A CZ    1 
ATOM   20485 N  NH1   . ARG A 1 4230 ? 156.503 159.976 210.541 1.00 24.55 ? 4230 ARG A NH1   1 
ATOM   20486 N  NH2   . ARG A 1 4230 ? 156.206 160.297 208.296 1.00 27.65 ? 4230 ARG A NH2   1 
ATOM   20487 N  N     . GLN A 1 4231 ? 155.181 162.118 215.661 1.00 24.92 ? 4231 GLN A N     1 
ATOM   20488 C  CA    . GLN A 1 4231 ? 155.675 161.738 216.978 1.00 24.05 ? 4231 GLN A CA    1 
ATOM   20489 C  C     . GLN A 1 4231 ? 156.600 160.530 216.933 1.00 25.06 ? 4231 GLN A C     1 
ATOM   20490 O  O     . GLN A 1 4231 ? 157.625 160.510 217.622 1.00 26.32 ? 4231 GLN A O     1 
ATOM   20491 C  CB    . GLN A 1 4231 ? 154.497 161.452 217.914 1.00 18.64 ? 4231 GLN A CB    1 
ATOM   20492 C  CG    . GLN A 1 4231 ? 154.814 161.611 219.393 1.00 22.39 ? 4231 GLN A CG    1 
ATOM   20493 C  CD    . GLN A 1 4231 ? 155.784 162.744 219.674 1.00 24.71 ? 4231 GLN A CD    1 
ATOM   20494 O  OE1   . GLN A 1 4231 ? 156.817 162.553 220.315 1.00 26.23 ? 4231 GLN A OE1   1 
ATOM   20495 N  NE2   . GLN A 1 4231 ? 155.449 163.936 219.194 1.00 23.21 ? 4231 GLN A NE2   1 
ATOM   20496 N  N     . ASN A 1 4232 ? 156.263 159.518 216.135 1.00 22.49 ? 4232 ASN A N     1 
ATOM   20497 C  CA    . ASN A 1 4232 ? 157.031 158.273 216.085 1.00 19.28 ? 4232 ASN A CA    1 
ATOM   20498 C  C     . ASN A 1 4232 ? 157.177 157.857 214.626 1.00 24.47 ? 4232 ASN A C     1 
ATOM   20499 O  O     . ASN A 1 4232 ? 156.219 157.387 214.006 1.00 34.28 ? 4232 ASN A O     1 
ATOM   20500 C  CB    . ASN A 1 4232 ? 156.357 157.182 216.907 1.00 16.36 ? 4232 ASN A CB    1 
ATOM   20501 C  CG    . ASN A 1 4232 ? 156.378 157.479 218.392 1.00 24.87 ? 4232 ASN A CG    1 
ATOM   20502 O  OD1   . ASN A 1 4232 ? 157.428 157.426 219.032 1.00 28.18 ? 4232 ASN A OD1   1 
ATOM   20503 N  ND2   . ASN A 1 4232 ? 155.218 157.808 218.946 1.00 25.19 ? 4232 ASN A ND2   1 
ATOM   20504 N  N     . ILE A 1 4233 ? 158.372 158.022 214.089 1.00 21.70 ? 4233 ILE A N     1 
ATOM   20505 C  CA    . ILE A 1 4233 ? 158.687 157.603 212.730 1.00 18.87 ? 4233 ILE A CA    1 
ATOM   20506 C  C     . ILE A 1 4233 ? 159.122 156.146 212.754 1.00 18.33 ? 4233 ILE A C     1 
ATOM   20507 O  O     . ILE A 1 4233 ? 159.853 155.712 213.653 1.00 21.05 ? 4233 ILE A O     1 
ATOM   20508 C  CB    . ILE A 1 4233 ? 159.773 158.510 212.117 1.00 18.30 ? 4233 ILE A CB    1 
ATOM   20509 C  CG1   . ILE A 1 4233 ? 160.080 158.093 210.679 1.00 11.72 ? 4233 ILE A CG1   1 
ATOM   20510 C  CG2   . ILE A 1 4233 ? 161.034 158.511 212.974 1.00 16.18 ? 4233 ILE A CG2   1 
ATOM   20511 C  CD1   . ILE A 1 4233 ? 161.109 158.960 210.012 1.00 15.52 ? 4233 ILE A CD1   1 
ATOM   20512 N  N     . SER A 1 4234 ? 158.658 155.377 211.776 1.00 21.34 ? 4234 SER A N     1 
ATOM   20513 C  CA    . SER A 1 4234 ? 159.060 153.981 211.693 1.00 13.91 ? 4234 SER A CA    1 
ATOM   20514 C  C     . SER A 1 4234 ? 160.561 153.891 211.427 1.00 17.27 ? 4234 SER A C     1 
ATOM   20515 O  O     . SER A 1 4234 ? 161.095 154.660 210.620 1.00 26.78 ? 4234 SER A O     1 
ATOM   20516 C  CB    . SER A 1 4234 ? 158.285 153.262 210.589 1.00 19.14 ? 4234 SER A CB    1 
ATOM   20517 O  OG    . SER A 1 4234 ? 158.825 151.974 210.349 1.00 23.45 ? 4234 SER A OG    1 
ATOM   20518 N  N     . PRO A 1 4235 ? 161.271 152.980 212.097 1.00 18.05 ? 4235 PRO A N     1 
ATOM   20519 C  CA    . PRO A 1 4235 ? 162.726 152.884 211.886 1.00 15.39 ? 4235 PRO A CA    1 
ATOM   20520 C  C     . PRO A 1 4235 ? 163.117 152.603 210.449 1.00 14.41 ? 4235 PRO A C     1 
ATOM   20521 O  O     . PRO A 1 4235 ? 164.142 153.115 209.984 1.00 19.04 ? 4235 PRO A O     1 
ATOM   20522 C  CB    . PRO A 1 4235 ? 163.134 151.736 212.818 1.00 10.26 ? 4235 PRO A CB    1 
ATOM   20523 C  CG    . PRO A 1 4235 ? 162.074 151.720 213.869 1.00 14.33 ? 4235 PRO A CG    1 
ATOM   20524 C  CD    . PRO A 1 4235 ? 160.807 152.057 213.145 1.00 13.97 ? 4235 PRO A CD    1 
ATOM   20525 N  N     . ASP A 1 4236 ? 162.334 151.805 209.726 1.00 18.33 ? 4236 ASP A N     1 
ATOM   20526 C  CA    . ASP A 1 4236 ? 162.641 151.516 208.333 1.00 18.51 ? 4236 ASP A CA    1 
ATOM   20527 C  C     . ASP A 1 4236 ? 162.326 152.679 207.403 1.00 17.04 ? 4236 ASP A C     1 
ATOM   20528 O  O     . ASP A 1 4236 ? 162.762 152.662 206.248 1.00 20.02 ? 4236 ASP A O     1 
ATOM   20529 C  CB    . ASP A 1 4236 ? 161.897 150.253 207.887 1.00 13.64 ? 4236 ASP A CB    1 
ATOM   20530 C  CG    . ASP A 1 4236 ? 160.386 150.406 207.944 1.00 27.84 ? 4236 ASP A CG    1 
ATOM   20531 O  OD1   . ASP A 1 4236 ? 159.897 151.474 208.366 1.00 27.28 ? 4236 ASP A OD1   1 
ATOM   20532 O  OD2   . ASP A 1 4236 ? 159.682 149.443 207.574 1.00 31.45 ? 4236 ASP A OD2   1 
ATOM   20533 N  N     . LYS A 1 4237 ? 161.581 153.678 207.872 1.00 15.00 ? 4237 LYS A N     1 
ATOM   20534 C  CA    . LYS A 1 4237 ? 161.324 154.890 207.110 1.00 10.82 ? 4237 LYS A CA    1 
ATOM   20535 C  C     . LYS A 1 4237 ? 162.352 155.979 207.380 1.00 10.05 ? 4237 LYS A C     1 
ATOM   20536 O  O     . LYS A 1 4237 ? 162.306 157.030 206.732 1.00 13.68 ? 4237 LYS A O     1 
ATOM   20537 C  CB    . LYS A 1 4237 ? 159.919 155.421 207.414 1.00 12.41 ? 4237 LYS A CB    1 
ATOM   20538 C  CG    . LYS A 1 4237 ? 158.766 154.470 207.077 1.00 15.94 ? 4237 LYS A CG    1 
ATOM   20539 C  CD    . LYS A 1 4237 ? 158.545 154.290 205.578 1.00 16.29 ? 4237 LYS A CD    1 
ATOM   20540 C  CE    . LYS A 1 4237 ? 159.281 153.079 205.017 1.00 23.00 ? 4237 LYS A CE    1 
ATOM   20541 N  NZ    . LYS A 1 4237 ? 158.964 152.861 203.578 1.00 24.00 ? 4237 LYS A NZ    1 
ATOM   20542 N  N     . ILE A 1 4238 ? 163.264 155.759 208.317 1.00 12.61 ? 4238 ILE A N     1 
ATOM   20543 C  CA    . ILE A 1 4238 ? 164.362 156.702 208.548 1.00 10.06 ? 4238 ILE A CA    1 
ATOM   20544 C  C     . ILE A 1 4238 ? 165.256 156.733 207.313 1.00 11.49 ? 4238 ILE A C     1 
ATOM   20545 O  O     . ILE A 1 4238 ? 165.609 155.667 206.780 1.00 10.77 ? 4238 ILE A O     1 
ATOM   20546 C  CB    . ILE A 1 4238 ? 165.154 156.297 209.796 1.00 8.66  ? 4238 ILE A CB    1 
ATOM   20547 C  CG1   . ILE A 1 4238 ? 164.245 156.327 211.030 1.00 11.11 ? 4238 ILE A CG1   1 
ATOM   20548 C  CG2   . ILE A 1 4238 ? 166.365 157.194 209.988 1.00 5.79  ? 4238 ILE A CG2   1 
ATOM   20549 C  CD1   . ILE A 1 4238 ? 164.917 155.868 212.299 1.00 12.26 ? 4238 ILE A CD1   1 
ATOM   20550 N  N     . PRO A 1 4239 ? 165.636 157.909 206.812 1.00 11.30 ? 4239 PRO A N     1 
ATOM   20551 C  CA    . PRO A 1 4239 ? 166.465 157.958 205.602 1.00 7.09  ? 4239 PRO A CA    1 
ATOM   20552 C  C     . PRO A 1 4239 ? 167.899 157.519 205.853 1.00 6.69  ? 4239 PRO A C     1 
ATOM   20553 O  O     . PRO A 1 4239 ? 168.813 158.349 205.910 1.00 3.53  ? 4239 PRO A O     1 
ATOM   20554 C  CB    . PRO A 1 4239 ? 166.385 159.433 205.193 1.00 6.89  ? 4239 PRO A CB    1 
ATOM   20555 C  CG    . PRO A 1 4239 ? 166.169 160.151 206.476 1.00 5.51  ? 4239 PRO A CG    1 
ATOM   20556 C  CD    . PRO A 1 4239 ? 165.278 159.254 207.291 1.00 5.97  ? 4239 PRO A CD    1 
ATOM   20557 N  N     . TRP A 1 4240 ? 168.102 156.209 205.998 1.00 5.50  ? 4240 TRP A N     1 
ATOM   20558 C  CA    . TRP A 1 4240 ? 169.440 155.683 206.252 1.00 3.42  ? 4240 TRP A CA    1 
ATOM   20559 C  C     . TRP A 1 4240 ? 170.368 155.942 205.076 1.00 2.89  ? 4240 TRP A C     1 
ATOM   20560 O  O     . TRP A 1 4240 ? 171.552 156.250 205.265 1.00 2.41  ? 4240 TRP A O     1 
ATOM   20561 C  CB    . TRP A 1 4240 ? 169.365 154.188 206.557 1.00 3.85  ? 4240 TRP A CB    1 
ATOM   20562 C  CG    . TRP A 1 4240 ? 168.539 153.871 207.751 1.00 3.31  ? 4240 TRP A CG    1 
ATOM   20563 C  CD1   . TRP A 1 4240 ? 167.342 153.220 207.768 1.00 3.98  ? 4240 TRP A CD1   1 
ATOM   20564 C  CD2   . TRP A 1 4240 ? 168.839 154.195 209.112 1.00 5.26  ? 4240 TRP A CD2   1 
ATOM   20565 N  NE1   . TRP A 1 4240 ? 166.877 153.119 209.053 1.00 8.58  ? 4240 TRP A NE1   1 
ATOM   20566 C  CE2   . TRP A 1 4240 ? 167.780 153.709 209.899 1.00 5.69  ? 4240 TRP A CE2   1 
ATOM   20567 C  CE3   . TRP A 1 4240 ? 169.901 154.848 209.740 1.00 3.78  ? 4240 TRP A CE3   1 
ATOM   20568 C  CZ2   . TRP A 1 4240 ? 167.749 153.859 211.280 1.00 5.99  ? 4240 TRP A CZ2   1 
ATOM   20569 C  CZ3   . TRP A 1 4240 ? 169.871 154.993 211.111 1.00 3.59  ? 4240 TRP A CZ3   1 
ATOM   20570 C  CH2   . TRP A 1 4240 ? 168.805 154.497 211.866 1.00 4.60  ? 4240 TRP A CH2   1 
ATOM   20571 N  N     . SER A 1 4241 ? 169.852 155.813 203.853 1.00 5.85  ? 4241 SER A N     1 
ATOM   20572 C  CA    . SER A 1 4241 ? 170.673 156.057 202.673 1.00 3.20  ? 4241 SER A CA    1 
ATOM   20573 C  C     . SER A 1 4241 ? 171.151 157.501 202.621 1.00 2.01  ? 4241 SER A C     1 
ATOM   20574 O  O     . SER A 1 4241 ? 172.311 157.765 202.288 1.00 1.91  ? 4241 SER A O     1 
ATOM   20575 C  CB    . SER A 1 4241 ? 169.888 155.701 201.410 1.00 3.76  ? 4241 SER A CB    1 
ATOM   20576 O  OG    . SER A 1 4241 ? 170.650 155.960 200.247 1.00 14.94 ? 4241 SER A OG    1 
ATOM   20577 N  N     . ALA A 1 4242 ? 170.273 158.450 202.946 1.00 2.34  ? 4242 ALA A N     1 
ATOM   20578 C  CA    . ALA A 1 4242 ? 170.667 159.854 202.948 1.00 1.30  ? 4242 ALA A CA    1 
ATOM   20579 C  C     . ALA A 1 4242 ? 171.726 160.131 204.008 1.00 3.55  ? 4242 ALA A C     1 
ATOM   20580 O  O     . ALA A 1 4242 ? 172.716 160.821 203.740 1.00 4.22  ? 4242 ALA A O     1 
ATOM   20581 C  CB    . ALA A 1 4242 ? 169.445 160.743 203.172 1.00 1.38  ? 4242 ALA A CB    1 
ATOM   20582 N  N     . LEU A 1 4243 ? 171.533 159.603 205.221 1.00 2.08  ? 4243 LEU A N     1 
ATOM   20583 C  CA    . LEU A 1 4243 ? 172.479 159.869 206.301 1.00 1.06  ? 4243 LEU A CA    1 
ATOM   20584 C  C     . LEU A 1 4243 ? 173.834 159.236 206.023 1.00 1.32  ? 4243 LEU A C     1 
ATOM   20585 O  O     . LEU A 1 4243 ? 174.874 159.878 206.214 1.00 3.83  ? 4243 LEU A O     1 
ATOM   20586 C  CB    . LEU A 1 4243 ? 171.917 159.366 207.630 1.00 2.70  ? 4243 LEU A CB    1 
ATOM   20587 C  CG    . LEU A 1 4243 ? 170.599 159.974 208.106 1.00 3.18  ? 4243 LEU A CG    1 
ATOM   20588 C  CD1   . LEU A 1 4243 ? 170.195 159.385 209.447 1.00 1.69  ? 4243 LEU A CD1   1 
ATOM   20589 C  CD2   . LEU A 1 4243 ? 170.687 161.492 208.180 1.00 1.48  ? 4243 LEU A CD2   1 
ATOM   20590 N  N     . LYS A 1 4244 ? 173.846 157.980 205.573 1.00 1.50  ? 4244 LYS A N     1 
ATOM   20591 C  CA    . LYS A 1 4244 ? 175.108 157.282 205.358 1.00 0.98  ? 4244 LYS A CA    1 
ATOM   20592 C  C     . LYS A 1 4244 ? 175.905 157.913 204.225 1.00 0.66  ? 4244 LYS A C     1 
ATOM   20593 O  O     . LYS A 1 4244 ? 177.108 158.155 204.362 1.00 1.01  ? 4244 LYS A O     1 
ATOM   20594 C  CB    . LYS A 1 4244 ? 174.849 155.802 205.073 1.00 1.77  ? 4244 LYS A CB    1 
ATOM   20595 C  CG    . LYS A 1 4244 ? 174.608 154.966 206.315 1.00 2.47  ? 4244 LYS A CG    1 
ATOM   20596 C  CD    . LYS A 1 4244 ? 174.426 153.499 205.962 1.00 3.57  ? 4244 LYS A CD    1 
ATOM   20597 C  CE    . LYS A 1 4244 ? 173.266 153.306 205.002 1.00 6.04  ? 4244 LYS A CE    1 
ATOM   20598 N  NZ    . LYS A 1 4244 ? 172.977 151.869 204.775 1.00 10.30 ? 4244 LYS A NZ    1 
ATOM   20599 N  N     . THR A 1 4245 ? 175.247 158.190 203.096 1.00 0.88  ? 4245 THR A N     1 
ATOM   20600 C  CA    . THR A 1 4245 ? 175.951 158.742 201.944 1.00 0.65  ? 4245 THR A CA    1 
ATOM   20601 C  C     . THR A 1 4245 ? 176.536 160.114 202.253 1.00 0.46  ? 4245 THR A C     1 
ATOM   20602 O  O     . THR A 1 4245 ? 177.685 160.400 201.897 1.00 0.45  ? 4245 THR A O     1 
ATOM   20603 C  CB    . THR A 1 4245 ? 175.009 158.830 200.746 1.00 0.92  ? 4245 THR A CB    1 
ATOM   20604 O  OG1   . THR A 1 4245 ? 174.333 157.578 200.570 1.00 3.46  ? 4245 THR A OG1   1 
ATOM   20605 C  CG2   . THR A 1 4245 ? 175.779 159.177 199.481 1.00 0.40  ? 4245 THR A CG2   1 
ATOM   20606 N  N     . LEU A 1 4246 ? 175.762 160.976 202.915 1.00 0.57  ? 4246 LEU A N     1 
ATOM   20607 C  CA    . LEU A 1 4246 ? 176.255 162.310 203.230 1.00 0.48  ? 4246 LEU A CA    1 
ATOM   20608 C  C     . LEU A 1 4246 ? 177.440 162.246 204.183 1.00 0.53  ? 4246 LEU A C     1 
ATOM   20609 O  O     . LEU A 1 4246 ? 178.393 163.020 204.053 1.00 0.73  ? 4246 LEU A O     1 
ATOM   20610 C  CB    . LEU A 1 4246 ? 175.126 163.163 203.809 1.00 0.58  ? 4246 LEU A CB    1 
ATOM   20611 C  CG    . LEU A 1 4246 ? 174.227 163.767 202.728 1.00 0.50  ? 4246 LEU A CG    1 
ATOM   20612 C  CD1   . LEU A 1 4246 ? 173.111 164.590 203.326 1.00 0.69  ? 4246 LEU A CD1   1 
ATOM   20613 C  CD2   . LEU A 1 4246 ? 175.050 164.604 201.758 1.00 0.16  ? 4246 LEU A CD2   1 
ATOM   20614 N  N     . MET A 1 4247 ? 177.402 161.322 205.142 1.00 0.99  ? 4247 MET A N     1 
ATOM   20615 C  CA    . MET A 1 4247 ? 178.559 161.105 205.999 1.00 0.80  ? 4247 MET A CA    1 
ATOM   20616 C  C     . MET A 1 4247 ? 179.670 160.344 205.281 1.00 0.82  ? 4247 MET A C     1 
ATOM   20617 O  O     . MET A 1 4247 ? 180.846 160.507 205.615 1.00 2.88  ? 4247 MET A O     1 
ATOM   20618 C  CB    . MET A 1 4247 ? 178.141 160.365 207.269 1.00 1.12  ? 4247 MET A CB    1 
ATOM   20619 C  CG    . MET A 1 4247 ? 177.535 161.270 208.328 1.00 1.46  ? 4247 MET A CG    1 
ATOM   20620 S  SD    . MET A 1 4247 ? 177.248 160.437 209.895 1.00 23.95 ? 4247 MET A SD    1 
ATOM   20621 C  CE    . MET A 1 4247 ? 175.633 159.726 209.598 1.00 3.57  ? 4247 MET A CE    1 
ATOM   20622 N  N     . ALA A 1 4248 ? 179.335 159.510 204.300 1.00 0.47  ? 4248 ALA A N     1 
ATOM   20623 C  CA    . ALA A 1 4248 ? 180.384 158.814 203.568 1.00 0.47  ? 4248 ALA A CA    1 
ATOM   20624 C  C     . ALA A 1 4248 ? 181.156 159.770 202.669 1.00 0.68  ? 4248 ALA A C     1 
ATOM   20625 O  O     . ALA A 1 4248 ? 182.376 159.637 202.517 1.00 1.54  ? 4248 ALA A O     1 
ATOM   20626 C  CB    . ALA A 1 4248 ? 179.790 157.669 202.753 1.00 2.47  ? 4248 ALA A CB    1 
ATOM   20627 N  N     . GLN A 1 4249 ? 180.471 160.742 202.076 1.00 0.50  ? 4249 GLN A N     1 
ATOM   20628 C  CA    . GLN A 1 4249 ? 181.051 161.598 201.049 1.00 0.72  ? 4249 GLN A CA    1 
ATOM   20629 C  C     . GLN A 1 4249 ? 181.417 162.991 201.532 1.00 1.00  ? 4249 GLN A C     1 
ATOM   20630 O  O     . GLN A 1 4249 ? 182.410 163.552 201.069 1.00 1.48  ? 4249 GLN A O     1 
ATOM   20631 C  CB    . GLN A 1 4249 ? 180.084 161.719 199.865 1.00 1.02  ? 4249 GLN A CB    1 
ATOM   20632 C  CG    . GLN A 1 4249 ? 179.722 160.388 199.228 1.00 0.83  ? 4249 GLN A CG    1 
ATOM   20633 C  CD    . GLN A 1 4249 ? 180.945 159.596 198.807 1.00 2.79  ? 4249 GLN A CD    1 
ATOM   20634 O  OE1   . GLN A 1 4249 ? 181.658 159.983 197.882 1.00 6.22  ? 4249 GLN A OE1   1 
ATOM   20635 N  NE2   . GLN A 1 4249 ? 181.199 158.492 199.497 1.00 2.19  ? 4249 GLN A NE2   1 
ATOM   20636 N  N     . SER A 1 4250 ? 180.645 163.570 202.453 1.00 1.57  ? 4250 SER A N     1 
ATOM   20637 C  CA    . SER A 1 4250 ? 180.792 164.976 202.807 1.00 1.32  ? 4250 SER A CA    1 
ATOM   20638 C  C     . SER A 1 4250 ? 181.203 165.180 204.260 1.00 2.16  ? 4250 SER A C     1 
ATOM   20639 O  O     . SER A 1 4250 ? 182.152 165.920 204.531 1.00 7.82  ? 4250 SER A O     1 
ATOM   20640 C  CB    . SER A 1 4250 ? 179.482 165.716 202.510 1.00 1.12  ? 4250 SER A CB    1 
ATOM   20641 O  OG    . SER A 1 4250 ? 179.090 165.518 201.165 1.00 1.03  ? 4250 SER A OG    1 
ATOM   20642 N  N     . ILE A 1 4251 ? 180.516 164.549 205.205 1.00 2.10  ? 4251 ILE A N     1 
ATOM   20643 C  CA    . ILE A 1 4251 ? 180.767 164.736 206.629 1.00 1.49  ? 4251 ILE A CA    1 
ATOM   20644 C  C     . ILE A 1 4251 ? 181.594 163.557 207.119 1.00 7.46  ? 4251 ILE A C     1 
ATOM   20645 O  O     . ILE A 1 4251 ? 181.093 162.431 207.158 1.00 17.96 ? 4251 ILE A O     1 
ATOM   20646 C  CB    . ILE A 1 4251 ? 179.454 164.828 207.416 1.00 2.01  ? 4251 ILE A CB    1 
ATOM   20647 C  CG1   . ILE A 1 4251 ? 178.629 166.020 206.955 1.00 1.74  ? 4251 ILE A CG1   1 
ATOM   20648 C  CG2   . ILE A 1 4251 ? 179.739 164.967 208.895 1.00 3.14  ? 4251 ILE A CG2   1 
ATOM   20649 C  CD1   . ILE A 1 4251 ? 177.239 165.996 207.495 1.00 0.97  ? 4251 ILE A CD1   1 
ATOM   20650 N  N     . TYR A 1 4252 ? 182.835 163.823 207.531 1.00 2.51  ? 4252 TYR A N     1 
ATOM   20651 C  CA    . TYR A 1 4252 ? 183.854 162.823 207.868 1.00 1.93  ? 4252 TYR A CA    1 
ATOM   20652 C  C     . TYR A 1 4252 ? 184.434 162.181 206.612 1.00 2.47  ? 4252 TYR A C     1 
ATOM   20653 O  O     . TYR A 1 4252 ? 185.439 161.469 206.688 1.00 8.60  ? 4252 TYR A O     1 
ATOM   20654 C  CB    . TYR A 1 4252 ? 183.324 161.700 208.772 1.00 0.57  ? 4252 TYR A CB    1 
ATOM   20655 C  CG    . TYR A 1 4252 ? 182.694 162.111 210.081 1.00 0.79  ? 4252 TYR A CG    1 
ATOM   20656 C  CD1   . TYR A 1 4252 ? 183.472 162.363 211.202 1.00 0.45  ? 4252 TYR A CD1   1 
ATOM   20657 C  CD2   . TYR A 1 4252 ? 181.313 162.189 210.211 1.00 0.98  ? 4252 TYR A CD2   1 
ATOM   20658 C  CE1   . TYR A 1 4252 ? 182.896 162.715 212.402 1.00 0.60  ? 4252 TYR A CE1   1 
ATOM   20659 C  CE2   . TYR A 1 4252 ? 180.729 162.543 211.406 1.00 0.87  ? 4252 TYR A CE2   1 
ATOM   20660 C  CZ    . TYR A 1 4252 ? 181.524 162.805 212.499 1.00 0.46  ? 4252 TYR A CZ    1 
ATOM   20661 O  OH    . TYR A 1 4252 ? 180.945 163.157 213.693 1.00 0.46  ? 4252 TYR A OH    1 
ATOM   20662 N  N     . GLY A 1 4253 ? 183.833 162.442 205.458 1.00 5.57  ? 4253 GLY A N     1 
ATOM   20663 C  CA    . GLY A 1 4253 ? 184.282 161.824 204.228 1.00 0.87  ? 4253 GLY A CA    1 
ATOM   20664 C  C     . GLY A 1 4253 ? 185.161 162.747 203.416 1.00 1.01  ? 4253 GLY A C     1 
ATOM   20665 O  O     . GLY A 1 4253 ? 186.055 162.295 202.696 1.00 3.47  ? 4253 GLY A O     1 
ATOM   20666 N  N     . GLY A 1 4254 ? 184.920 164.053 203.543 1.00 1.11  ? 4254 GLY A N     1 
ATOM   20667 C  CA    . GLY A 1 4254 ? 185.702 165.032 202.815 1.00 0.61  ? 4254 GLY A CA    1 
ATOM   20668 C  C     . GLY A 1 4254 ? 187.162 165.073 203.208 1.00 1.08  ? 4254 GLY A C     1 
ATOM   20669 O  O     . GLY A 1 4254 ? 188.000 165.487 202.402 1.00 5.76  ? 4254 GLY A O     1 
ATOM   20670 N  N     . ARG A 1 4255 ? 187.487 164.651 204.430 1.00 1.59  ? 4255 ARG A N     1 
ATOM   20671 C  CA    . ARG A 1 4255 ? 188.869 164.650 204.882 1.00 2.00  ? 4255 ARG A CA    1 
ATOM   20672 C  C     . ARG A 1 4255 ? 189.665 163.470 204.344 1.00 1.54  ? 4255 ARG A C     1 
ATOM   20673 O  O     . ARG A 1 4255 ? 190.898 163.529 204.335 1.00 3.77  ? 4255 ARG A O     1 
ATOM   20674 C  CB    . ARG A 1 4255 ? 188.915 164.638 206.409 1.00 1.47  ? 4255 ARG A CB    1 
ATOM   20675 C  CG    . ARG A 1 4255 ? 188.006 165.663 207.045 1.00 3.06  ? 4255 ARG A CG    1 
ATOM   20676 C  CD    . ARG A 1 4255 ? 188.024 165.561 208.557 1.00 3.56  ? 4255 ARG A CD    1 
ATOM   20677 N  NE    . ARG A 1 4255 ? 187.343 166.686 209.184 1.00 2.44  ? 4255 ARG A NE    1 
ATOM   20678 C  CZ    . ARG A 1 4255 ? 187.788 167.936 209.177 1.00 2.40  ? 4255 ARG A CZ    1 
ATOM   20679 N  NH1   . ARG A 1 4255 ? 188.935 168.258 208.600 1.00 2.20  ? 4255 ARG A NH1   1 
ATOM   20680 N  NH2   . ARG A 1 4255 ? 187.071 168.881 209.773 1.00 2.48  ? 4255 ARG A NH2   1 
ATOM   20681 N  N     . VAL A 1 4256 ? 188.998 162.418 203.890 1.00 1.08  ? 4256 VAL A N     1 
ATOM   20682 C  CA    . VAL A 1 4256 ? 189.673 161.172 203.545 1.00 1.68  ? 4256 VAL A CA    1 
ATOM   20683 C  C     . VAL A 1 4256 ? 190.232 161.267 202.132 1.00 1.54  ? 4256 VAL A C     1 
ATOM   20684 O  O     . VAL A 1 4256 ? 189.501 161.559 201.178 1.00 3.01  ? 4256 VAL A O     1 
ATOM   20685 C  CB    . VAL A 1 4256 ? 188.715 159.980 203.687 1.00 1.93  ? 4256 VAL A CB    1 
ATOM   20686 C  CG1   . VAL A 1 4256 ? 189.437 158.681 203.391 1.00 1.31  ? 4256 VAL A CG1   1 
ATOM   20687 C  CG2   . VAL A 1 4256 ? 188.113 159.954 205.083 1.00 0.90  ? 4256 VAL A CG2   1 
ATOM   20688 N  N     . ASP A 1 4257 ? 191.533 161.015 201.997 1.00 1.84  ? 4257 ASP A N     1 
ATOM   20689 C  CA    . ASP A 1 4257 ? 192.216 161.014 200.709 1.00 4.26  ? 4257 ASP A CA    1 
ATOM   20690 C  C     . ASP A 1 4257 ? 192.806 159.640 200.403 1.00 4.09  ? 4257 ASP A C     1 
ATOM   20691 O  O     . ASP A 1 4257 ? 193.753 159.519 199.623 1.00 4.64  ? 4257 ASP A O     1 
ATOM   20692 C  CB    . ASP A 1 4257 ? 193.303 162.086 200.675 1.00 4.50  ? 4257 ASP A CB    1 
ATOM   20693 C  CG    . ASP A 1 4257 ? 194.213 162.039 201.887 1.00 8.46  ? 4257 ASP A CG    1 
ATOM   20694 O  OD1   . ASP A 1 4257 ? 194.020 161.158 202.749 1.00 9.36  ? 4257 ASP A OD1   1 
ATOM   20695 O  OD2   . ASP A 1 4257 ? 195.124 162.886 201.980 1.00 20.93 ? 4257 ASP A OD2   1 
ATOM   20696 N  N     . ASN A 1 4258 ? 192.251 158.599 201.018 1.00 3.34  ? 4258 ASN A N     1 
ATOM   20697 C  CA    . ASN A 1 4258 ? 192.761 157.240 200.908 1.00 3.59  ? 4258 ASN A CA    1 
ATOM   20698 C  C     . ASN A 1 4258 ? 191.572 156.310 200.730 1.00 2.72  ? 4258 ASN A C     1 
ATOM   20699 O  O     . ASN A 1 4258 ? 190.606 156.391 201.493 1.00 5.09  ? 4258 ASN A O     1 
ATOM   20700 C  CB    . ASN A 1 4258 ? 193.584 156.877 202.157 1.00 2.64  ? 4258 ASN A CB    1 
ATOM   20701 C  CG    . ASN A 1 4258 ? 194.057 155.436 202.166 1.00 5.22  ? 4258 ASN A CG    1 
ATOM   20702 O  OD1   . ASN A 1 4258 ? 193.259 154.503 202.194 1.00 10.75 ? 4258 ASN A OD1   1 
ATOM   20703 N  ND2   . ASN A 1 4258 ? 195.370 155.250 202.166 1.00 4.76  ? 4258 ASN A ND2   1 
ATOM   20704 N  N     . GLU A 1 4259 ? 191.639 155.431 199.727 1.00 3.36  ? 4259 GLU A N     1 
ATOM   20705 C  CA    . GLU A 1 4259 ? 190.492 154.576 199.432 1.00 3.59  ? 4259 GLU A CA    1 
ATOM   20706 C  C     . GLU A 1 4259 ? 190.264 153.545 200.531 1.00 1.79  ? 4259 GLU A C     1 
ATOM   20707 O  O     . GLU A 1 4259 ? 189.122 153.159 200.801 1.00 1.51  ? 4259 GLU A O     1 
ATOM   20708 C  CB    . GLU A 1 4259 ? 190.673 153.889 198.077 1.00 3.35  ? 4259 GLU A CB    1 
ATOM   20709 C  CG    . GLU A 1 4259 ? 191.826 152.903 198.014 1.00 6.60  ? 4259 GLU A CG    1 
ATOM   20710 C  CD    . GLU A 1 4259 ? 192.003 152.296 196.636 1.00 19.69 ? 4259 GLU A CD    1 
ATOM   20711 O  OE1   . GLU A 1 4259 ? 191.237 152.663 195.720 1.00 25.07 ? 4259 GLU A OE1   1 
ATOM   20712 O  OE2   . GLU A 1 4259 ? 192.909 151.453 196.469 1.00 21.82 ? 4259 GLU A OE2   1 
ATOM   20713 N  N     . PHE A 1 4260 ? 191.337 153.082 201.172 1.00 2.56  ? 4260 PHE A N     1 
ATOM   20714 C  CA    . PHE A 1 4260 ? 191.192 152.078 202.220 1.00 3.59  ? 4260 PHE A CA    1 
ATOM   20715 C  C     . PHE A 1 4260 ? 190.668 152.702 203.506 1.00 2.25  ? 4260 PHE A C     1 
ATOM   20716 O  O     . PHE A 1 4260 ? 189.934 152.058 204.263 1.00 1.53  ? 4260 PHE A O     1 
ATOM   20717 C  CB    . PHE A 1 4260 ? 192.529 151.377 202.444 1.00 3.82  ? 4260 PHE A CB    1 
ATOM   20718 C  CG    . PHE A 1 4260 ? 193.049 150.694 201.217 1.00 6.01  ? 4260 PHE A CG    1 
ATOM   20719 C  CD1   . PHE A 1 4260 ? 192.621 149.426 200.884 1.00 6.15  ? 4260 PHE A CD1   1 
ATOM   20720 C  CD2   . PHE A 1 4260 ? 193.937 151.340 200.377 1.00 4.02  ? 4260 PHE A CD2   1 
ATOM   20721 C  CE1   . PHE A 1 4260 ? 193.083 148.804 199.750 1.00 6.71  ? 4260 PHE A CE1   1 
ATOM   20722 C  CE2   . PHE A 1 4260 ? 194.400 150.724 199.241 1.00 4.16  ? 4260 PHE A CE2   1 
ATOM   20723 C  CZ    . PHE A 1 4260 ? 193.974 149.452 198.928 1.00 5.40  ? 4260 PHE A CZ    1 
ATOM   20724 N  N     . ASP A 1 4261 ? 191.036 153.958 203.766 1.00 1.93  ? 4261 ASP A N     1 
ATOM   20725 C  CA    . ASP A 1 4261 ? 190.412 154.697 204.855 1.00 1.47  ? 4261 ASP A CA    1 
ATOM   20726 C  C     . ASP A 1 4261 ? 188.962 155.029 204.526 1.00 1.28  ? 4261 ASP A C     1 
ATOM   20727 O  O     . ASP A 1 4261 ? 188.109 155.065 205.421 1.00 1.57  ? 4261 ASP A O     1 
ATOM   20728 C  CB    . ASP A 1 4261 ? 191.212 155.962 205.150 1.00 1.86  ? 4261 ASP A CB    1 
ATOM   20729 C  CG    . ASP A 1 4261 ? 192.464 155.684 205.954 1.00 2.59  ? 4261 ASP A CG    1 
ATOM   20730 O  OD1   . ASP A 1 4261 ? 192.683 154.515 206.335 1.00 2.64  ? 4261 ASP A OD1   1 
ATOM   20731 O  OD2   . ASP A 1 4261 ? 193.243 156.626 206.191 1.00 3.18  ? 4261 ASP A OD2   1 
ATOM   20732 N  N     . GLN A 1 4262 ? 188.666 155.282 203.249 1.00 1.27  ? 4262 GLN A N     1 
ATOM   20733 C  CA    . GLN A 1 4262 ? 187.285 155.493 202.829 1.00 0.94  ? 4262 GLN A CA    1 
ATOM   20734 C  C     . GLN A 1 4262 ? 186.454 154.230 203.005 1.00 1.14  ? 4262 GLN A C     1 
ATOM   20735 O  O     . GLN A 1 4262 ? 185.296 154.297 203.436 1.00 1.82  ? 4262 GLN A O     1 
ATOM   20736 C  CB    . GLN A 1 4262 ? 187.244 155.966 201.375 1.00 1.21  ? 4262 GLN A CB    1 
ATOM   20737 C  CG    . GLN A 1 4262 ? 185.854 156.305 200.856 1.00 1.05  ? 4262 GLN A CG    1 
ATOM   20738 C  CD    . GLN A 1 4262 ? 185.222 157.475 201.584 1.00 2.28  ? 4262 GLN A CD    1 
ATOM   20739 O  OE1   . GLN A 1 4262 ? 185.784 158.567 201.637 1.00 3.18  ? 4262 GLN A OE1   1 
ATOM   20740 N  NE2   . GLN A 1 4262 ? 184.037 157.254 202.139 1.00 1.09  ? 4262 GLN A NE2   1 
ATOM   20741 N  N     . ARG A 1 4263 ? 187.021 153.070 202.668 1.00 1.32  ? 4263 ARG A N     1 
ATOM   20742 C  CA    . ARG A 1 4263 ? 186.307 151.812 202.856 1.00 1.29  ? 4263 ARG A CA    1 
ATOM   20743 C  C     . ARG A 1 4263 ? 186.034 151.558 204.330 1.00 2.37  ? 4263 ARG A C     1 
ATOM   20744 O  O     . ARG A 1 4263 ? 184.957 151.076 204.700 1.00 3.21  ? 4263 ARG A O     1 
ATOM   20745 C  CB    . ARG A 1 4263 ? 187.107 150.659 202.255 1.00 3.58  ? 4263 ARG A CB    1 
ATOM   20746 C  CG    . ARG A 1 4263 ? 186.600 149.282 202.639 1.00 4.91  ? 4263 ARG A CG    1 
ATOM   20747 C  CD    . ARG A 1 4263 ? 187.447 148.195 202.017 1.00 7.17  ? 4263 ARG A CD    1 
ATOM   20748 N  NE    . ARG A 1 4263 ? 188.824 148.236 202.493 1.00 6.61  ? 4263 ARG A NE    1 
ATOM   20749 C  CZ    . ARG A 1 4263 ? 189.789 147.439 202.059 1.00 10.34 ? 4263 ARG A CZ    1 
ATOM   20750 N  NH1   . ARG A 1 4263 ? 189.590 146.593 201.060 1.00 7.83  ? 4263 ARG A NH1   1 
ATOM   20751 N  NH2   . ARG A 1 4263 ? 190.982 147.486 202.643 1.00 9.08  ? 4263 ARG A NH2   1 
ATOM   20752 N  N     . LEU A 1 4264 ? 187.007 151.869 205.187 1.00 1.23  ? 4264 LEU A N     1 
ATOM   20753 C  CA    . LEU A 1 4264 ? 186.820 151.721 206.625 1.00 0.91  ? 4264 LEU A CA    1 
ATOM   20754 C  C     . LEU A 1 4264 ? 185.704 152.628 207.126 1.00 1.35  ? 4264 LEU A C     1 
ATOM   20755 O  O     . LEU A 1 4264 ? 184.869 152.216 207.939 1.00 1.30  ? 4264 LEU A O     1 
ATOM   20756 C  CB    . LEU A 1 4264 ? 188.132 152.023 207.347 1.00 2.38  ? 4264 LEU A CB    1 
ATOM   20757 C  CG    . LEU A 1 4264 ? 188.119 151.851 208.862 1.00 1.31  ? 4264 LEU A CG    1 
ATOM   20758 C  CD1   . LEU A 1 4264 ? 187.797 150.418 209.205 1.00 0.90  ? 4264 LEU A CD1   1 
ATOM   20759 C  CD2   . LEU A 1 4264 ? 189.455 152.261 209.442 1.00 0.88  ? 4264 LEU A CD2   1 
ATOM   20760 N  N     . LEU A 1 4265 ? 185.671 153.871 206.640 1.00 1.92  ? 4265 LEU A N     1 
ATOM   20761 C  CA    . LEU A 1 4265 ? 184.593 154.785 207.003 1.00 0.73  ? 4265 LEU A CA    1 
ATOM   20762 C  C     . LEU A 1 4265 ? 183.243 154.256 206.530 1.00 1.00  ? 4265 LEU A C     1 
ATOM   20763 O  O     . LEU A 1 4265 ? 182.244 154.354 207.252 1.00 0.96  ? 4265 LEU A O     1 
ATOM   20764 C  CB    . LEU A 1 4265 ? 184.868 156.167 206.417 1.00 0.43  ? 4265 LEU A CB    1 
ATOM   20765 C  CG    . LEU A 1 4265 ? 183.807 157.245 206.633 1.00 0.71  ? 4265 LEU A CG    1 
ATOM   20766 C  CD1   . LEU A 1 4265 ? 183.664 157.558 208.111 1.00 1.08  ? 4265 LEU A CD1   1 
ATOM   20767 C  CD2   . LEU A 1 4265 ? 184.151 158.495 205.846 1.00 0.56  ? 4265 LEU A CD2   1 
ATOM   20768 N  N     . ASN A 1 4266 ? 183.196 153.693 205.320 1.00 0.89  ? 4266 ASN A N     1 
ATOM   20769 C  CA    . ASN A 1 4266 ? 181.954 153.115 204.817 1.00 1.56  ? 4266 ASN A CA    1 
ATOM   20770 C  C     . ASN A 1 4266 ? 181.520 151.918 205.650 1.00 1.54  ? 4266 ASN A C     1 
ATOM   20771 O  O     . ASN A 1 4266 ? 180.322 151.715 205.877 1.00 2.55  ? 4266 ASN A O     1 
ATOM   20772 C  CB    . ASN A 1 4266 ? 182.116 152.707 203.352 1.00 2.06  ? 4266 ASN A CB    1 
ATOM   20773 C  CG    . ASN A 1 4266 ? 182.146 153.895 202.417 1.00 2.71  ? 4266 ASN A CG    1 
ATOM   20774 O  OD1   . ASN A 1 4266 ? 181.358 154.825 202.556 1.00 8.52  ? 4266 ASN A OD1   1 
ATOM   20775 N  ND2   . ASN A 1 4266 ? 183.058 153.867 201.454 1.00 3.13  ? 4266 ASN A ND2   1 
ATOM   20776 N  N     . THR A 1 4267 ? 182.479 151.108 206.102 1.00 1.97  ? 4267 THR A N     1 
ATOM   20777 C  CA    . THR A 1 4267 ? 182.149 149.903 206.858 1.00 1.80  ? 4267 THR A CA    1 
ATOM   20778 C  C     . THR A 1 4267 ? 181.449 150.245 208.169 1.00 1.61  ? 4267 THR A C     1 
ATOM   20779 O  O     . THR A 1 4267 ? 180.440 149.624 208.524 1.00 3.93  ? 4267 THR A O     1 
ATOM   20780 C  CB    . THR A 1 4267 ? 183.420 149.090 207.115 1.00 3.07  ? 4267 THR A CB    1 
ATOM   20781 O  OG1   . THR A 1 4267 ? 183.974 148.663 205.867 1.00 5.34  ? 4267 THR A OG1   1 
ATOM   20782 C  CG2   . THR A 1 4267 ? 183.118 147.868 207.967 1.00 4.91  ? 4267 THR A CG2   1 
ATOM   20783 N  N     . PHE A 1 4268 ? 181.961 151.239 208.897 1.00 1.61  ? 4268 PHE A N     1 
ATOM   20784 C  CA    . PHE A 1 4268 ? 181.331 151.635 210.153 1.00 1.51  ? 4268 PHE A CA    1 
ATOM   20785 C  C     . PHE A 1 4268 ? 179.948 152.226 209.917 1.00 1.83  ? 4268 PHE A C     1 
ATOM   20786 O  O     . PHE A 1 4268 ? 178.993 151.908 210.634 1.00 3.49  ? 4268 PHE A O     1 
ATOM   20787 C  CB    . PHE A 1 4268 ? 182.214 152.633 210.903 1.00 1.06  ? 4268 PHE A CB    1 
ATOM   20788 C  CG    . PHE A 1 4268 ? 183.336 151.995 211.665 1.00 3.02  ? 4268 PHE A CG    1 
ATOM   20789 C  CD1   . PHE A 1 4268 ? 183.107 151.417 212.901 1.00 3.47  ? 4268 PHE A CD1   1 
ATOM   20790 C  CD2   . PHE A 1 4268 ? 184.624 151.996 211.161 1.00 4.21  ? 4268 PHE A CD2   1 
ATOM   20791 C  CE1   . PHE A 1 4268 ? 184.138 150.831 213.607 1.00 4.70  ? 4268 PHE A CE1   1 
ATOM   20792 C  CE2   . PHE A 1 4268 ? 185.659 151.415 211.868 1.00 3.03  ? 4268 PHE A CE2   1 
ATOM   20793 C  CZ    . PHE A 1 4268 ? 185.415 150.832 213.091 1.00 3.05  ? 4268 PHE A CZ    1 
ATOM   20794 N  N     . LEU A 1 4269 ? 179.822 153.094 208.910 1.00 2.01  ? 4269 LEU A N     1 
ATOM   20795 C  CA    . LEU A 1 4269 ? 178.534 153.717 208.629 1.00 1.46  ? 4269 LEU A CA    1 
ATOM   20796 C  C     . LEU A 1 4269 ? 177.499 152.680 208.217 1.00 2.08  ? 4269 LEU A C     1 
ATOM   20797 O  O     . LEU A 1 4269 ? 176.330 152.769 208.609 1.00 3.06  ? 4269 LEU A O     1 
ATOM   20798 C  CB    . LEU A 1 4269 ? 178.690 154.781 207.542 1.00 1.31  ? 4269 LEU A CB    1 
ATOM   20799 C  CG    . LEU A 1 4269 ? 179.409 156.072 207.937 1.00 0.91  ? 4269 LEU A CG    1 
ATOM   20800 C  CD1   . LEU A 1 4269 ? 179.732 156.903 206.704 1.00 0.62  ? 4269 LEU A CD1   1 
ATOM   20801 C  CD2   . LEU A 1 4269 ? 178.577 156.873 208.925 1.00 0.58  ? 4269 LEU A CD2   1 
ATOM   20802 N  N     . GLU A 1 4270 ? 177.909 151.688 207.424 1.00 1.84  ? 4270 GLU A N     1 
ATOM   20803 C  CA    . GLU A 1 4270 ? 176.970 150.656 207.002 1.00 3.87  ? 4270 GLU A CA    1 
ATOM   20804 C  C     . GLU A 1 4270 ? 176.535 149.782 208.170 1.00 5.43  ? 4270 GLU A C     1 
ATOM   20805 O  O     . GLU A 1 4270 ? 175.387 149.331 208.205 1.00 7.28  ? 4270 GLU A O     1 
ATOM   20806 C  CB    . GLU A 1 4270 ? 177.587 149.802 205.895 1.00 4.77  ? 4270 GLU A CB    1 
ATOM   20807 C  CG    . GLU A 1 4270 ? 176.611 148.823 205.260 1.00 9.24  ? 4270 GLU A CG    1 
ATOM   20808 C  CD    . GLU A 1 4270 ? 175.293 149.478 204.892 1.00 17.04 ? 4270 GLU A CD    1 
ATOM   20809 O  OE1   . GLU A 1 4270 ? 175.305 150.428 204.080 1.00 17.50 ? 4270 GLU A OE1   1 
ATOM   20810 O  OE2   . GLU A 1 4270 ? 174.248 149.048 205.419 1.00 15.46 ? 4270 GLU A OE2   1 
ATOM   20811 N  N     . ARG A 1 4271 ? 177.424 149.533 209.131 1.00 6.77  ? 4271 ARG A N     1 
ATOM   20812 C  CA    . ARG A 1 4271 ? 177.080 148.710 210.282 1.00 5.24  ? 4271 ARG A CA    1 
ATOM   20813 C  C     . ARG A 1 4271 ? 176.224 149.432 211.311 1.00 5.04  ? 4271 ARG A C     1 
ATOM   20814 O  O     . ARG A 1 4271 ? 175.374 148.794 211.940 1.00 11.26 ? 4271 ARG A O     1 
ATOM   20815 C  CB    . ARG A 1 4271 ? 178.350 148.191 210.967 1.00 4.81  ? 4271 ARG A CB    1 
ATOM   20816 C  CG    . ARG A 1 4271 ? 178.079 147.086 211.976 1.00 5.58  ? 4271 ARG A CG    1 
ATOM   20817 C  CD    . ARG A 1 4271 ? 179.323 146.275 212.302 1.00 9.38  ? 4271 ARG A CD    1 
ATOM   20818 N  NE    . ARG A 1 4271 ? 180.499 147.088 212.584 1.00 17.30 ? 4271 ARG A NE    1 
ATOM   20819 C  CZ    . ARG A 1 4271 ? 180.605 147.960 213.580 1.00 14.43 ? 4271 ARG A CZ    1 
ATOM   20820 N  NH1   . ARG A 1 4271 ? 179.626 148.140 214.450 1.00 13.48 ? 4271 ARG A NH1   1 
ATOM   20821 N  NH2   . ARG A 1 4271 ? 181.730 148.654 213.715 1.00 13.19 ? 4271 ARG A NH2   1 
ATOM   20822 N  N     . LEU A 1 4272 ? 176.417 150.739 211.496 1.00 2.39  ? 4272 LEU A N     1 
ATOM   20823 C  CA    . LEU A 1 4272 ? 175.778 151.458 212.590 1.00 3.56  ? 4272 LEU A CA    1 
ATOM   20824 C  C     . LEU A 1 4272 ? 174.479 152.153 212.211 1.00 3.76  ? 4272 LEU A C     1 
ATOM   20825 O  O     . LEU A 1 4272 ? 173.649 152.388 213.095 1.00 4.27  ? 4272 LEU A O     1 
ATOM   20826 C  CB    . LEU A 1 4272 ? 176.738 152.501 213.177 1.00 2.44  ? 4272 LEU A CB    1 
ATOM   20827 C  CG    . LEU A 1 4272 ? 177.990 151.963 213.869 1.00 3.09  ? 4272 LEU A CG    1 
ATOM   20828 C  CD1   . LEU A 1 4272 ? 178.920 153.099 214.250 1.00 1.29  ? 4272 LEU A CD1   1 
ATOM   20829 C  CD2   . LEU A 1 4272 ? 177.605 151.148 215.092 1.00 4.44  ? 4272 LEU A CD2   1 
ATOM   20830 N  N     . PHE A 1 4273 ? 174.278 152.501 210.943 1.00 5.38  ? 4273 PHE A N     1 
ATOM   20831 C  CA    . PHE A 1 4273 ? 173.103 153.267 210.533 1.00 3.45  ? 4273 PHE A CA    1 
ATOM   20832 C  C     . PHE A 1 4273 ? 172.242 152.404 209.617 1.00 4.35  ? 4273 PHE A C     1 
ATOM   20833 O  O     . PHE A 1 4273 ? 172.301 152.515 208.391 1.00 8.91  ? 4273 PHE A O     1 
ATOM   20834 C  CB    . PHE A 1 4273 ? 173.529 154.582 209.864 1.00 2.75  ? 4273 PHE A CB    1 
ATOM   20835 C  CG    . PHE A 1 4273 ? 174.187 155.550 210.805 1.00 1.51  ? 4273 PHE A CG    1 
ATOM   20836 C  CD1   . PHE A 1 4273 ? 173.428 156.453 211.536 1.00 2.88  ? 4273 PHE A CD1   1 
ATOM   20837 C  CD2   . PHE A 1 4273 ? 175.558 155.549 210.977 1.00 2.48  ? 4273 PHE A CD2   1 
ATOM   20838 C  CE1   . PHE A 1 4273 ? 174.028 157.338 212.412 1.00 1.17  ? 4273 PHE A CE1   1 
ATOM   20839 C  CE2   . PHE A 1 4273 ? 176.167 156.432 211.851 1.00 3.80  ? 4273 PHE A CE2   1 
ATOM   20840 C  CZ    . PHE A 1 4273 ? 175.399 157.328 212.568 1.00 1.03  ? 4273 PHE A CZ    1 
ATOM   20841 N  N     . THR A 1 4274 ? 171.421 151.553 210.232 1.00 4.53  ? 4274 THR A N     1 
ATOM   20842 C  CA    . THR A 1 4274 ? 170.436 150.726 209.546 1.00 3.13  ? 4274 THR A CA    1 
ATOM   20843 C  C     . THR A 1 4274 ? 169.198 150.635 210.424 1.00 7.42  ? 4274 THR A C     1 
ATOM   20844 O  O     . THR A 1 4274 ? 169.153 151.180 211.530 1.00 17.08 ? 4274 THR A O     1 
ATOM   20845 C  CB    . THR A 1 4274 ? 170.952 149.308 209.248 1.00 7.72  ? 4274 THR A CB    1 
ATOM   20846 O  OG1   . THR A 1 4274 ? 171.083 148.577 210.474 1.00 17.71 ? 4274 THR A OG1   1 
ATOM   20847 C  CG2   . THR A 1 4274 ? 172.281 149.327 208.522 1.00 7.45  ? 4274 THR A CG2   1 
ATOM   20848 N  N     . THR A 1 4275 ? 168.186 149.922 209.929 1.00 11.24 ? 4275 THR A N     1 
ATOM   20849 C  CA    . THR A 1 4275 ? 167.018 149.629 210.751 1.00 11.32 ? 4275 THR A CA    1 
ATOM   20850 C  C     . THR A 1 4275 ? 167.347 148.675 211.894 1.00 14.59 ? 4275 THR A C     1 
ATOM   20851 O  O     . THR A 1 4275 ? 166.657 148.690 212.917 1.00 18.69 ? 4275 THR A O     1 
ATOM   20852 C  CB    . THR A 1 4275 ? 165.899 149.048 209.884 1.00 12.04 ? 4275 THR A CB    1 
ATOM   20853 O  OG1   . THR A 1 4275 ? 165.814 149.784 208.659 1.00 13.10 ? 4275 THR A OG1   1 
ATOM   20854 C  CG2   . THR A 1 4275 ? 164.567 149.146 210.603 1.00 13.90 ? 4275 THR A CG2   1 
ATOM   20855 N  N     . ARG A 1 4276 ? 168.389 147.852 211.745 1.00 11.07 ? 4276 ARG A N     1 
ATOM   20856 C  CA    . ARG A 1 4276 ? 168.772 146.919 212.800 1.00 14.66 ? 4276 ARG A CA    1 
ATOM   20857 C  C     . ARG A 1 4276 ? 169.254 147.624 214.059 1.00 11.72 ? 4276 ARG A C     1 
ATOM   20858 O  O     . ARG A 1 4276 ? 169.256 147.014 215.132 1.00 12.55 ? 4276 ARG A O     1 
ATOM   20859 C  CB    . ARG A 1 4276 ? 169.855 145.965 212.294 1.00 10.88 ? 4276 ARG A CB    1 
ATOM   20860 C  CG    . ARG A 1 4276 ? 169.421 145.078 211.137 1.00 15.80 ? 4276 ARG A CG    1 
ATOM   20861 C  CD    . ARG A 1 4276 ? 168.509 143.940 211.588 1.00 18.05 ? 4276 ARG A CD    1 
ATOM   20862 N  NE    . ARG A 1 4276 ? 167.162 144.399 211.905 1.00 22.18 ? 4276 ARG A NE    1 
ATOM   20863 C  CZ    . ARG A 1 4276 ? 166.234 144.689 211.005 1.00 26.16 ? 4276 ARG A CZ    1 
ATOM   20864 N  NH1   . ARG A 1 4276 ? 166.464 144.557 209.708 1.00 22.43 ? 4276 ARG A NH1   1 
ATOM   20865 N  NH2   . ARG A 1 4276 ? 165.048 145.130 211.414 1.00 24.42 ? 4276 ARG A NH2   1 
ATOM   20866 N  N     . SER A 1 4277 ? 169.661 148.891 213.955 1.00 14.23 ? 4277 SER A N     1 
ATOM   20867 C  CA    . SER A 1 4277 ? 170.093 149.633 215.133 1.00 11.18 ? 4277 SER A CA    1 
ATOM   20868 C  C     . SER A 1 4277 ? 168.961 149.848 216.125 1.00 10.83 ? 4277 SER A C     1 
ATOM   20869 O  O     . SER A 1 4277 ? 169.226 150.094 217.306 1.00 17.47 ? 4277 SER A O     1 
ATOM   20870 C  CB    . SER A 1 4277 ? 170.685 150.978 214.717 1.00 10.92 ? 4277 SER A CB    1 
ATOM   20871 O  OG    . SER A 1 4277 ? 171.960 150.811 214.129 1.00 14.06 ? 4277 SER A OG    1 
ATOM   20872 N  N     . PHE A 1 4278 ? 167.713 149.767 215.676 1.00 10.88 ? 4278 PHE A N     1 
ATOM   20873 C  CA    . PHE A 1 4278 ? 166.555 149.920 216.541 1.00 11.00 ? 4278 PHE A CA    1 
ATOM   20874 C  C     . PHE A 1 4278 ? 166.040 148.590 217.079 1.00 16.41 ? 4278 PHE A C     1 
ATOM   20875 O  O     . PHE A 1 4278 ? 165.044 148.579 217.807 1.00 15.03 ? 4278 PHE A O     1 
ATOM   20876 C  CB    . PHE A 1 4278 ? 165.436 150.652 215.795 1.00 10.09 ? 4278 PHE A CB    1 
ATOM   20877 C  CG    . PHE A 1 4278 ? 165.617 152.140 215.750 1.00 7.94  ? 4278 PHE A CG    1 
ATOM   20878 C  CD1   . PHE A 1 4278 ? 166.616 152.706 214.978 1.00 11.65 ? 4278 PHE A CD1   1 
ATOM   20879 C  CD2   . PHE A 1 4278 ? 164.792 152.973 216.485 1.00 8.42  ? 4278 PHE A CD2   1 
ATOM   20880 C  CE1   . PHE A 1 4278 ? 166.788 154.072 214.940 1.00 7.73  ? 4278 PHE A CE1   1 
ATOM   20881 C  CE2   . PHE A 1 4278 ? 164.963 154.340 216.449 1.00 7.43  ? 4278 PHE A CE2   1 
ATOM   20882 C  CZ    . PHE A 1 4278 ? 165.961 154.890 215.675 1.00 9.65  ? 4278 PHE A CZ    1 
ATOM   20883 N  N     . ASP A 1 4279 ? 166.689 147.482 216.737 1.00 17.15 ? 4279 ASP A N     1 
ATOM   20884 C  CA    . ASP A 1 4279 ? 166.334 146.188 217.296 1.00 17.44 ? 4279 ASP A CA    1 
ATOM   20885 C  C     . ASP A 1 4279 ? 166.834 146.068 218.730 1.00 26.93 ? 4279 ASP A C     1 
ATOM   20886 O  O     . ASP A 1 4279 ? 167.756 146.768 219.160 1.00 27.20 ? 4279 ASP A O     1 
ATOM   20887 C  CB    . ASP A 1 4279 ? 166.907 145.052 216.449 1.00 16.47 ? 4279 ASP A CB    1 
ATOM   20888 C  CG    . ASP A 1 4279 ? 166.419 145.088 215.018 1.00 18.30 ? 4279 ASP A CG    1 
ATOM   20889 O  OD1   . ASP A 1 4279 ? 165.697 146.039 214.656 1.00 23.40 ? 4279 ASP A OD1   1 
ATOM   20890 O  OD2   . ASP A 1 4279 ? 166.753 144.158 214.258 1.00 19.49 ? 4279 ASP A OD2   1 
ATOM   20891 N  N     . SER A 1 4280 ? 166.201 145.159 219.477 1.00 27.58 ? 4280 SER A N     1 
ATOM   20892 C  CA    . SER A 1 4280 ? 166.543 144.981 220.883 1.00 23.00 ? 4280 SER A CA    1 
ATOM   20893 C  C     . SER A 1 4280 ? 167.965 144.457 221.055 1.00 28.81 ? 4280 SER A C     1 
ATOM   20894 O  O     . SER A 1 4280 ? 168.680 144.880 221.969 1.00 32.57 ? 4280 SER A O     1 
ATOM   20895 C  CB    . SER A 1 4280 ? 165.543 144.032 221.545 1.00 27.86 ? 4280 SER A CB    1 
ATOM   20896 O  OG    . SER A 1 4280 ? 164.218 144.510 221.406 1.00 33.83 ? 4280 SER A OG    1 
ATOM   20897 N  N     . GLU A 1 4281 ? 168.394 143.537 220.190 1.00 25.73 ? 4281 GLU A N     1 
ATOM   20898 C  CA    . GLU A 1 4281 ? 169.670 142.850 220.345 1.00 27.49 ? 4281 GLU A CA    1 
ATOM   20899 C  C     . GLU A 1 4281 ? 170.758 143.404 219.427 1.00 23.05 ? 4281 GLU A C     1 
ATOM   20900 O  O     . GLU A 1 4281 ? 171.674 142.669 219.046 1.00 18.08 ? 4281 GLU A O     1 
ATOM   20901 C  CB    . GLU A 1 4281 ? 169.496 141.350 220.105 1.00 26.68 ? 4281 GLU A CB    1 
ATOM   20902 C  CG    . GLU A 1 4281 ? 168.579 140.664 221.103 1.00 31.28 ? 4281 GLU A CG    1 
ATOM   20903 C  CD    . GLU A 1 4281 ? 169.003 140.900 222.537 1.00 38.71 ? 4281 GLU A CD    1 
ATOM   20904 O  OE1   . GLU A 1 4281 ? 170.142 140.529 222.889 1.00 37.79 ? 4281 GLU A OE1   1 
ATOM   20905 O  OE2   . GLU A 1 4281 ? 168.198 141.458 223.312 1.00 44.44 ? 4281 GLU A OE2   1 
ATOM   20906 N  N     . PHE A 1 4282 ? 170.677 144.683 219.065 1.00 18.68 ? 4282 PHE A N     1 
ATOM   20907 C  CA    . PHE A 1 4282 ? 171.717 145.284 218.240 1.00 12.00 ? 4282 PHE A CA    1 
ATOM   20908 C  C     . PHE A 1 4282 ? 173.036 145.334 219.001 1.00 14.61 ? 4282 PHE A C     1 
ATOM   20909 O  O     . PHE A 1 4282 ? 173.064 145.543 220.217 1.00 14.37 ? 4282 PHE A O     1 
ATOM   20910 C  CB    . PHE A 1 4282 ? 171.307 146.688 217.797 1.00 11.30 ? 4282 PHE A CB    1 
ATOM   20911 C  CG    . PHE A 1 4282 ? 172.277 147.327 216.848 1.00 8.40  ? 4282 PHE A CG    1 
ATOM   20912 C  CD1   . PHE A 1 4282 ? 172.596 146.714 215.649 1.00 9.92  ? 4282 PHE A CD1   1 
ATOM   20913 C  CD2   . PHE A 1 4282 ? 172.874 148.535 217.156 1.00 10.27 ? 4282 PHE A CD2   1 
ATOM   20914 C  CE1   . PHE A 1 4282 ? 173.491 147.294 214.774 1.00 10.53 ? 4282 PHE A CE1   1 
ATOM   20915 C  CE2   . PHE A 1 4282 ? 173.770 149.123 216.283 1.00 11.19 ? 4282 PHE A CE2   1 
ATOM   20916 C  CZ    . PHE A 1 4282 ? 174.077 148.500 215.092 1.00 15.93 ? 4282 PHE A CZ    1 
ATOM   20917 N  N     . LYS A 1 4283 ? 174.136 145.149 218.276 1.00 15.15 ? 4283 LYS A N     1 
ATOM   20918 C  CA    . LYS A 1 4283 ? 175.447 144.918 218.875 1.00 12.01 ? 4283 LYS A CA    1 
ATOM   20919 C  C     . LYS A 1 4283 ? 176.409 145.983 218.365 1.00 10.21 ? 4283 LYS A C     1 
ATOM   20920 O  O     . LYS A 1 4283 ? 176.857 145.918 217.215 1.00 19.43 ? 4283 LYS A O     1 
ATOM   20921 C  CB    . LYS A 1 4283 ? 175.938 143.513 218.529 1.00 16.10 ? 4283 LYS A CB    1 
ATOM   20922 C  CG    . LYS A 1 4283 ? 175.598 142.473 219.578 1.00 17.25 ? 4283 LYS A CG    1 
ATOM   20923 C  CD    . LYS A 1 4283 ? 176.105 141.098 219.191 1.00 22.21 ? 4283 LYS A CD    1 
ATOM   20924 C  CE    . LYS A 1 4283 ? 175.914 140.107 220.324 1.00 25.92 ? 4283 LYS A CE    1 
ATOM   20925 N  NZ    . LYS A 1 4283 ? 176.798 138.920 220.182 1.00 26.57 ? 4283 LYS A NZ    1 
ATOM   20926 N  N     . LEU A 1 4284 ? 176.722 146.966 219.214 1.00 9.81  ? 4284 LEU A N     1 
ATOM   20927 C  CA    . LEU A 1 4284 ? 177.636 148.031 218.810 1.00 10.73 ? 4284 LEU A CA    1 
ATOM   20928 C  C     . LEU A 1 4284 ? 179.038 147.492 218.545 1.00 10.74 ? 4284 LEU A C     1 
ATOM   20929 O  O     . LEU A 1 4284 ? 179.686 147.885 217.570 1.00 9.46  ? 4284 LEU A O     1 
ATOM   20930 C  CB    . LEU A 1 4284 ? 177.672 149.129 219.872 1.00 4.27  ? 4284 LEU A CB    1 
ATOM   20931 C  CG    . LEU A 1 4284 ? 176.392 149.954 220.017 1.00 5.98  ? 4284 LEU A CG    1 
ATOM   20932 C  CD1   . LEU A 1 4284 ? 176.209 150.431 221.449 1.00 5.88  ? 4284 LEU A CD1   1 
ATOM   20933 C  CD2   . LEU A 1 4284 ? 176.393 151.127 219.051 1.00 4.71  ? 4284 LEU A CD2   1 
ATOM   20934 N  N     . ALA A 1 4285 ? 179.521 146.599 219.405 1.00 10.43 ? 4285 ALA A N     1 
ATOM   20935 C  CA    . ALA A 1 4285 ? 180.811 145.953 219.222 1.00 7.58  ? 4285 ALA A CA    1 
ATOM   20936 C  C     . ALA A 1 4285 ? 180.680 144.489 219.612 1.00 14.45 ? 4285 ALA A C     1 
ATOM   20937 O  O     . ALA A 1 4285 ? 179.875 144.136 220.478 1.00 17.43 ? 4285 ALA A O     1 
ATOM   20938 C  CB    . ALA A 1 4285 ? 181.909 146.635 220.047 1.00 5.29  ? 4285 ALA A CB    1 
ATOM   20939 N  N     . CYS A 1 4286 ? 181.473 143.639 218.965 1.00 13.94 ? 4286 CYS A N     1 
ATOM   20940 C  CA    . CYS A 1 4286 ? 181.368 142.193 219.124 1.00 20.94 ? 4286 CYS A CA    1 
ATOM   20941 C  C     . CYS A 1 4286 ? 182.674 141.633 219.673 1.00 19.02 ? 4286 CYS A C     1 
ATOM   20942 O  O     . CYS A 1 4286 ? 183.737 141.838 219.082 1.00 16.18 ? 4286 CYS A O     1 
ATOM   20943 C  CB    . CYS A 1 4286 ? 181.015 141.523 217.794 1.00 23.30 ? 4286 CYS A CB    1 
ATOM   20944 S  SG    . CYS A 1 4286 ? 179.396 141.979 217.140 1.00 47.31 ? 4286 CYS A SG    1 
ATOM   20945 N  N     . LYS A 1 4287 ? 182.579 140.921 220.799 1.00 25.76 ? 4287 LYS A N     1 
ATOM   20946 C  CA    . LYS A 1 4287 ? 183.694 140.181 221.394 1.00 26.89 ? 4287 LYS A CA    1 
ATOM   20947 C  C     . LYS A 1 4287 ? 184.887 141.097 221.674 1.00 25.41 ? 4287 LYS A C     1 
ATOM   20948 O  O     . LYS A 1 4287 ? 185.962 140.970 221.085 1.00 25.56 ? 4287 LYS A O     1 
ATOM   20949 C  CB    . LYS A 1 4287 ? 184.096 138.994 220.509 1.00 28.33 ? 4287 LYS A CB    1 
ATOM   20950 C  CG    . LYS A 1 4287 ? 183.366 137.690 220.825 1.00 30.47 ? 4287 LYS A CG    1 
ATOM   20951 C  CD    . LYS A 1 4287 ? 181.854 137.830 220.725 1.00 30.63 ? 4287 LYS A CD    1 
ATOM   20952 C  CE    . LYS A 1 4287 ? 181.411 138.090 219.294 1.00 29.36 ? 4287 LYS A CE    1 
ATOM   20953 N  NZ    . LYS A 1 4287 ? 179.933 138.248 219.192 1.00 33.20 ? 4287 LYS A NZ    1 
ATOM   20954 N  N     . VAL A 1 4288 ? 184.670 142.043 222.588 1.00 22.89 ? 4288 VAL A N     1 
ATOM   20955 C  CA    . VAL A 1 4288 ? 185.733 142.971 222.957 1.00 20.28 ? 4288 VAL A CA    1 
ATOM   20956 C  C     . VAL A 1 4288 ? 186.815 142.258 223.762 1.00 26.71 ? 4288 VAL A C     1 
ATOM   20957 O  O     . VAL A 1 4288 ? 188.012 142.415 223.500 1.00 24.48 ? 4288 VAL A O     1 
ATOM   20958 C  CB    . VAL A 1 4288 ? 185.149 144.177 223.719 1.00 12.31 ? 4288 VAL A CB    1 
ATOM   20959 C  CG1   . VAL A 1 4288 ? 184.425 145.098 222.757 1.00 12.64 ? 4288 VAL A CG1   1 
ATOM   20960 C  CG2   . VAL A 1 4288 ? 184.196 143.714 224.809 1.00 19.22 ? 4288 VAL A CG2   1 
ATOM   20961 N  N     . ASP A 1 4289 ? 186.413 141.451 224.744 1.00 26.22 ? 4289 ASP A N     1 
ATOM   20962 C  CA    . ASP A 1 4289 ? 187.342 140.693 225.568 1.00 26.31 ? 4289 ASP A CA    1 
ATOM   20963 C  C     . ASP A 1 4289 ? 187.312 139.201 225.257 1.00 24.89 ? 4289 ASP A C     1 
ATOM   20964 O  O     . ASP A 1 4289 ? 187.698 138.389 226.104 1.00 31.91 ? 4289 ASP A O     1 
ATOM   20965 C  CB    . ASP A 1 4289 ? 187.060 140.942 227.052 1.00 28.49 ? 4289 ASP A CB    1 
ATOM   20966 C  CG    . ASP A 1 4289 ? 185.671 140.492 227.472 1.00 32.24 ? 4289 ASP A CG    1 
ATOM   20967 O  OD1   . ASP A 1 4289 ? 184.895 140.025 226.614 1.00 34.55 ? 4289 ASP A OD1   1 
ATOM   20968 O  OD2   . ASP A 1 4289 ? 185.354 140.608 228.675 1.00 36.54 ? 4289 ASP A OD2   1 
ATOM   20969 N  N     . GLY A 1 4290 ? 186.854 138.829 224.064 1.00 28.18 ? 4290 GLY A N     1 
ATOM   20970 C  CA    . GLY A 1 4290 ? 186.727 137.449 223.667 1.00 29.17 ? 4290 GLY A CA    1 
ATOM   20971 C  C     . GLY A 1 4290 ? 185.378 136.828 223.969 1.00 35.89 ? 4290 GLY A C     1 
ATOM   20972 O  O     . GLY A 1 4290 ? 184.894 136.008 223.182 1.00 37.64 ? 4290 GLY A O     1 
ATOM   20973 N  N     . HIS A 1 4291 ? 184.760 137.197 225.090 1.00 32.69 ? 4291 HIS A N     1 
ATOM   20974 C  CA    . HIS A 1 4291 ? 183.469 136.649 225.483 1.00 36.28 ? 4291 HIS A CA    1 
ATOM   20975 C  C     . HIS A 1 4291 ? 182.384 137.710 225.562 1.00 35.85 ? 4291 HIS A C     1 
ATOM   20976 O  O     . HIS A 1 4291 ? 181.334 137.567 224.923 1.00 35.80 ? 4291 HIS A O     1 
ATOM   20977 C  CB    . HIS A 1 4291 ? 183.595 135.927 226.834 1.00 29.59 ? 4291 HIS A CB    1 
ATOM   20978 C  CG    . HIS A 1 4291 ? 184.472 134.716 226.790 1.00 36.37 ? 4291 HIS A CG    1 
ATOM   20979 N  ND1   . HIS A 1 4291 ? 185.832 134.774 227.002 1.00 36.74 ? 4291 HIS A ND1   1 
ATOM   20980 C  CD2   . HIS A 1 4291 ? 184.182 133.413 226.561 1.00 40.94 ? 4291 HIS A CD2   1 
ATOM   20981 C  CE1   . HIS A 1 4291 ? 186.344 133.560 226.906 1.00 36.14 ? 4291 HIS A CE1   1 
ATOM   20982 N  NE2   . HIS A 1 4291 ? 185.365 132.716 226.639 1.00 42.03 ? 4291 HIS A NE2   1 
ATOM   20983 N  N     . LYS A 1 4292 ? 182.608 138.776 226.324 1.00 30.98 ? 4292 LYS A N     1 
ATOM   20984 C  CA    . LYS A 1 4292 ? 181.613 139.828 226.472 1.00 28.10 ? 4292 LYS A CA    1 
ATOM   20985 C  C     . LYS A 1 4292 ? 181.660 140.777 225.284 1.00 27.86 ? 4292 LYS A C     1 
ATOM   20986 O  O     . LYS A 1 4292 ? 182.648 140.824 224.546 1.00 28.23 ? 4292 LYS A O     1 
ATOM   20987 C  CB    . LYS A 1 4292 ? 181.842 140.603 227.769 1.00 29.88 ? 4292 LYS A CB    1 
ATOM   20988 C  CG    . LYS A 1 4292 ? 181.964 139.731 229.006 1.00 32.05 ? 4292 LYS A CG    1 
ATOM   20989 C  CD    . LYS A 1 4292 ? 182.249 140.569 230.243 1.00 34.72 ? 4292 LYS A CD    1 
ATOM   20990 C  CE    . LYS A 1 4292 ? 182.688 139.702 231.413 1.00 36.07 ? 4292 LYS A CE    1 
ATOM   20991 N  NZ    . LYS A 1 4292 ? 183.932 138.943 231.106 1.00 34.05 ? 4292 LYS A NZ    1 
ATOM   20992 N  N     . ASP A 1 4293 ? 180.580 141.531 225.098 1.00 26.20 ? 4293 ASP A N     1 
ATOM   20993 C  CA    . ASP A 1 4293 ? 180.495 142.518 224.035 1.00 20.61 ? 4293 ASP A CA    1 
ATOM   20994 C  C     . ASP A 1 4293 ? 179.483 143.600 224.389 1.00 19.63 ? 4293 ASP A C     1 
ATOM   20995 O  O     . ASP A 1 4293 ? 178.698 143.457 225.332 1.00 22.96 ? 4293 ASP A O     1 
ATOM   20996 C  CB    . ASP A 1 4293 ? 180.191 141.840 222.677 1.00 21.83 ? 4293 ASP A CB    1 
ATOM   20997 C  CG    . ASP A 1 4293 ? 178.769 141.308 222.557 1.00 22.30 ? 4293 ASP A CG    1 
ATOM   20998 O  OD1   . ASP A 1 4293 ? 177.844 141.758 223.259 1.00 27.94 ? 4293 ASP A OD1   1 
ATOM   20999 O  OD2   . ASP A 1 4293 ? 178.588 140.394 221.732 1.00 24.31 ? 4293 ASP A OD2   1 
ATOM   21000 N  N     . ILE A 1 4294 ? 179.519 144.688 223.630 1.00 16.45 ? 4294 ILE A N     1 
ATOM   21001 C  CA    . ILE A 1 4294 ? 178.772 145.892 223.974 1.00 12.10 ? 4294 ILE A CA    1 
ATOM   21002 C  C     . ILE A 1 4294 ? 177.424 145.871 223.268 1.00 13.31 ? 4294 ILE A C     1 
ATOM   21003 O  O     . ILE A 1 4294 ? 177.354 145.813 222.036 1.00 15.59 ? 4294 ILE A O     1 
ATOM   21004 C  CB    . ILE A 1 4294 ? 179.581 147.145 223.607 1.00 8.30  ? 4294 ILE A CB    1 
ATOM   21005 C  CG1   . ILE A 1 4294 ? 180.982 147.053 224.216 1.00 12.29 ? 4294 ILE A CG1   1 
ATOM   21006 C  CG2   . ILE A 1 4294 ? 178.870 148.399 224.080 1.00 7.68  ? 4294 ILE A CG2   1 
ATOM   21007 C  CD1   . ILE A 1 4294 ? 181.868 148.235 223.922 1.00 7.55  ? 4294 ILE A CD1   1 
ATOM   21008 N  N     . GLN A 1 4295 ? 176.350 145.927 224.051 1.00 15.18 ? 4295 GLN A N     1 
ATOM   21009 C  CA    . GLN A 1 4295 ? 174.989 145.876 223.536 1.00 13.39 ? 4295 GLN A CA    1 
ATOM   21010 C  C     . GLN A 1 4295 ? 174.439 147.279 223.323 1.00 9.27  ? 4295 GLN A C     1 
ATOM   21011 O  O     . GLN A 1 4295 ? 174.806 148.227 224.020 1.00 15.15 ? 4295 GLN A O     1 
ATOM   21012 C  CB    . GLN A 1 4295 ? 174.068 145.109 224.489 1.00 14.17 ? 4295 GLN A CB    1 
ATOM   21013 C  CG    . GLN A 1 4295 ? 174.397 143.639 224.644 1.00 17.58 ? 4295 GLN A CG    1 
ATOM   21014 C  CD    . GLN A 1 4295 ? 174.258 142.873 223.345 1.00 24.26 ? 4295 GLN A CD    1 
ATOM   21015 O  OE1   . GLN A 1 4295 ? 175.248 142.453 222.752 1.00 28.18 ? 4295 GLN A OE1   1 
ATOM   21016 N  NE2   . GLN A 1 4295 ? 173.023 142.679 222.898 1.00 23.07 ? 4295 GLN A NE2   1 
ATOM   21017 N  N     . MET A 1 4296 ? 173.551 147.396 222.352 1.00 12.50 ? 4296 MET A N     1 
ATOM   21018 C  CA    . MET A 1 4296 ? 172.870 148.658 222.097 1.00 11.51 ? 4296 MET A CA    1 
ATOM   21019 C  C     . MET A 1 4296 ? 171.829 148.910 223.181 1.00 11.43 ? 4296 MET A C     1 
ATOM   21020 O  O     . MET A 1 4296 ? 170.980 148.048 223.427 1.00 20.19 ? 4296 MET A O     1 
ATOM   21021 C  CB    . MET A 1 4296 ? 172.205 148.635 220.727 1.00 11.90 ? 4296 MET A CB    1 
ATOM   21022 C  CG    . MET A 1 4296 ? 171.458 149.902 220.377 1.00 12.79 ? 4296 MET A CG    1 
ATOM   21023 S  SD    . MET A 1 4296 ? 172.569 151.245 219.930 1.00 7.43  ? 4296 MET A SD    1 
ATOM   21024 C  CE    . MET A 1 4296 ? 171.442 152.336 219.077 1.00 9.99  ? 4296 MET A CE    1 
ATOM   21025 N  N     . PRO A 1 4297 ? 171.870 150.057 223.856 1.00 8.99  ? 4297 PRO A N     1 
ATOM   21026 C  CA    . PRO A 1 4297 ? 170.848 150.351 224.866 1.00 10.86 ? 4297 PRO A CA    1 
ATOM   21027 C  C     . PRO A 1 4297 ? 169.457 150.410 224.251 1.00 18.16 ? 4297 PRO A C     1 
ATOM   21028 O  O     . PRO A 1 4297 ? 169.273 150.886 223.129 1.00 22.82 ? 4297 PRO A O     1 
ATOM   21029 C  CB    . PRO A 1 4297 ? 171.274 151.717 225.419 1.00 6.08  ? 4297 PRO A CB    1 
ATOM   21030 C  CG    . PRO A 1 4297 ? 172.156 152.300 224.364 1.00 9.45  ? 4297 PRO A CG    1 
ATOM   21031 C  CD    . PRO A 1 4297 ? 172.850 151.146 223.716 1.00 7.00  ? 4297 PRO A CD    1 
ATOM   21032 N  N     . ASP A 1 4298 ? 168.478 149.915 224.999 1.00 19.04 ? 4298 ASP A N     1 
ATOM   21033 C  CA    . ASP A 1 4298 ? 167.086 149.908 224.555 1.00 20.39 ? 4298 ASP A CA    1 
ATOM   21034 C  C     . ASP A 1 4298 ? 166.335 151.156 225.017 1.00 20.58 ? 4298 ASP A C     1 
ATOM   21035 O  O     . ASP A 1 4298 ? 165.220 151.098 225.529 1.00 21.95 ? 4298 ASP A O     1 
ATOM   21036 C  CB    . ASP A 1 4298 ? 166.406 148.627 225.031 1.00 23.18 ? 4298 ASP A CB    1 
ATOM   21037 C  CG    . ASP A 1 4298 ? 166.253 148.563 226.543 1.00 31.98 ? 4298 ASP A CG    1 
ATOM   21038 O  OD1   . ASP A 1 4298 ? 167.205 148.112 227.213 1.00 31.33 ? 4298 ASP A OD1   1 
ATOM   21039 O  OD2   . ASP A 1 4298 ? 165.177 148.932 227.057 1.00 35.99 ? 4298 ASP A OD2   1 
ATOM   21040 N  N     . GLY A 1 4299 ? 166.940 152.316 224.787 1.00 17.69 ? 4299 GLY A N     1 
ATOM   21041 C  CA    . GLY A 1 4299 ? 166.350 153.567 225.210 1.00 21.52 ? 4299 GLY A CA    1 
ATOM   21042 C  C     . GLY A 1 4299 ? 165.561 154.255 224.109 1.00 23.45 ? 4299 GLY A C     1 
ATOM   21043 O  O     . GLY A 1 4299 ? 165.855 154.118 222.925 1.00 22.96 ? 4299 GLY A O     1 
ATOM   21044 N  N     . ILE A 1 4300 ? 164.536 154.995 224.525 1.00 18.77 ? 4300 ILE A N     1 
ATOM   21045 C  CA    . ILE A 1 4300 ? 163.757 155.844 223.635 1.00 14.02 ? 4300 ILE A CA    1 
ATOM   21046 C  C     . ILE A 1 4300 ? 163.882 157.316 223.983 1.00 19.80 ? 4300 ILE A C     1 
ATOM   21047 O  O     . ILE A 1 4300 ? 163.338 158.160 223.263 1.00 26.09 ? 4300 ILE A O     1 
ATOM   21048 C  CB    . ILE A 1 4300 ? 162.272 155.425 223.614 1.00 16.84 ? 4300 ILE A CB    1 
ATOM   21049 C  CG1   . ILE A 1 4300 ? 161.638 155.629 224.989 1.00 25.10 ? 4300 ILE A CG1   1 
ATOM   21050 C  CG2   . ILE A 1 4300 ? 162.131 153.981 223.160 1.00 20.39 ? 4300 ILE A CG2   1 
ATOM   21051 C  CD1   . ILE A 1 4300 ? 160.178 155.237 225.055 1.00 28.64 ? 4300 ILE A CD1   1 
ATOM   21052 N  N     . ARG A 1 4301 ? 164.583 157.653 225.065 1.00 16.29 ? 4301 ARG A N     1 
ATOM   21053 C  CA    . ARG A 1 4301 ? 164.760 159.028 225.501 1.00 17.02 ? 4301 ARG A CA    1 
ATOM   21054 C  C     . ARG A 1 4301 ? 166.243 159.302 225.708 1.00 15.53 ? 4301 ARG A C     1 
ATOM   21055 O  O     . ARG A 1 4301 ? 167.043 158.384 225.903 1.00 11.48 ? 4301 ARG A O     1 
ATOM   21056 C  CB    . ARG A 1 4301 ? 163.980 159.315 226.794 1.00 20.00 ? 4301 ARG A CB    1 
ATOM   21057 C  CG    . ARG A 1 4301 ? 162.474 159.170 226.654 1.00 22.40 ? 4301 ARG A CG    1 
ATOM   21058 C  CD    . ARG A 1 4301 ? 161.796 159.077 228.013 1.00 24.53 ? 4301 ARG A CD    1 
ATOM   21059 N  NE    . ARG A 1 4301 ? 162.132 157.840 228.709 1.00 29.73 ? 4301 ARG A NE    1 
ATOM   21060 C  CZ    . ARG A 1 4301 ? 162.764 157.786 229.873 1.00 29.78 ? 4301 ARG A CZ    1 
ATOM   21061 N  NH1   . ARG A 1 4301 ? 163.151 158.883 230.502 1.00 20.31 ? 4301 ARG A NH1   1 
ATOM   21062 N  NH2   . ARG A 1 4301 ? 163.015 156.600 230.418 1.00 32.23 ? 4301 ARG A NH2   1 
ATOM   21063 N  N     . ARG A 1 4302 ? 166.601 160.588 225.658 1.00 13.17 ? 4302 ARG A N     1 
ATOM   21064 C  CA    . ARG A 1 4302 ? 168.008 160.970 225.743 1.00 11.40 ? 4302 ARG A CA    1 
ATOM   21065 C  C     . ARG A 1 4302 ? 168.628 160.544 227.069 1.00 12.72 ? 4302 ARG A C     1 
ATOM   21066 O  O     . ARG A 1 4302 ? 169.751 160.029 227.099 1.00 17.05 ? 4302 ARG A O     1 
ATOM   21067 C  CB    . ARG A 1 4302 ? 168.159 162.477 225.553 1.00 11.76 ? 4302 ARG A CB    1 
ATOM   21068 C  CG    . ARG A 1 4302 ? 169.535 162.992 225.935 1.00 10.54 ? 4302 ARG A CG    1 
ATOM   21069 C  CD    . ARG A 1 4302 ? 169.631 164.500 225.833 1.00 13.28 ? 4302 ARG A CD    1 
ATOM   21070 N  NE    . ARG A 1 4302 ? 170.867 165.003 226.419 1.00 18.19 ? 4302 ARG A NE    1 
ATOM   21071 C  CZ    . ARG A 1 4302 ? 171.135 165.014 227.718 1.00 13.83 ? 4302 ARG A CZ    1 
ATOM   21072 N  NH1   . ARG A 1 4302 ? 170.252 164.595 228.610 1.00 11.03 ? 4302 ARG A NH1   1 
ATOM   21073 N  NH2   . ARG A 1 4302 ? 172.315 165.464 228.133 1.00 12.06 ? 4302 ARG A NH2   1 
ATOM   21074 N  N     . GLU A 1 4303 ? 167.910 160.751 228.175 1.00 17.50 ? 4303 GLU A N     1 
ATOM   21075 C  CA    . GLU A 1 4303 ? 168.467 160.456 229.493 1.00 13.85 ? 4303 GLU A CA    1 
ATOM   21076 C  C     . GLU A 1 4303 ? 168.806 158.981 229.649 1.00 16.44 ? 4303 GLU A C     1 
ATOM   21077 O  O     . GLU A 1 4303 ? 169.736 158.635 230.387 1.00 15.22 ? 4303 GLU A O     1 
ATOM   21078 C  CB    . GLU A 1 4303 ? 167.493 160.900 230.585 1.00 12.87 ? 4303 GLU A CB    1 
ATOM   21079 C  CG    . GLU A 1 4303 ? 166.066 160.431 230.375 1.00 20.97 ? 4303 GLU A CG    1 
ATOM   21080 C  CD    . GLU A 1 4303 ? 165.234 161.422 229.585 1.00 31.25 ? 4303 GLU A CD    1 
ATOM   21081 O  OE1   . GLU A 1 4303 ? 165.591 161.707 228.421 1.00 28.19 ? 4303 GLU A OE1   1 
ATOM   21082 O  OE2   . GLU A 1 4303 ? 164.223 161.916 230.126 1.00 35.90 ? 4303 GLU A OE2   1 
ATOM   21083 N  N     . GLU A 1 4304 ? 168.068 158.096 228.976 1.00 17.30 ? 4304 GLU A N     1 
ATOM   21084 C  CA    . GLU A 1 4304 ? 168.397 156.676 229.021 1.00 13.91 ? 4304 GLU A CA    1 
ATOM   21085 C  C     . GLU A 1 4304 ? 169.743 156.396 228.362 1.00 15.01 ? 4304 GLU A C     1 
ATOM   21086 O  O     . GLU A 1 4304 ? 170.531 155.590 228.870 1.00 22.30 ? 4304 GLU A O     1 
ATOM   21087 C  CB    . GLU A 1 4304 ? 167.295 155.857 228.354 1.00 19.08 ? 4304 GLU A CB    1 
ATOM   21088 C  CG    . GLU A 1 4304 ? 165.886 156.328 228.674 1.00 22.88 ? 4304 GLU A CG    1 
ATOM   21089 C  CD    . GLU A 1 4304 ? 164.828 155.461 228.021 1.00 26.82 ? 4304 GLU A CD    1 
ATOM   21090 O  OE1   . GLU A 1 4304 ? 164.942 154.221 228.107 1.00 30.94 ? 4304 GLU A OE1   1 
ATOM   21091 O  OE2   . GLU A 1 4304 ? 163.886 156.020 227.422 1.00 24.61 ? 4304 GLU A OE2   1 
ATOM   21092 N  N     . PHE A 1 4305 ? 170.019 157.043 227.226 1.00 13.61 ? 4305 PHE A N     1 
ATOM   21093 C  CA    . PHE A 1 4305 ? 171.299 156.842 226.558 1.00 8.64  ? 4305 PHE A CA    1 
ATOM   21094 C  C     . PHE A 1 4305 ? 172.449 157.409 227.381 1.00 8.94  ? 4305 PHE A C     1 
ATOM   21095 O  O     . PHE A 1 4305 ? 173.530 156.810 227.437 1.00 16.07 ? 4305 PHE A O     1 
ATOM   21096 C  CB    . PHE A 1 4305 ? 171.276 157.469 225.163 1.00 9.41  ? 4305 PHE A CB    1 
ATOM   21097 C  CG    . PHE A 1 4305 ? 170.321 156.805 224.212 1.00 6.50  ? 4305 PHE A CG    1 
ATOM   21098 C  CD1   . PHE A 1 4305 ? 170.586 155.540 223.713 1.00 8.23  ? 4305 PHE A CD1   1 
ATOM   21099 C  CD2   . PHE A 1 4305 ? 169.166 157.448 223.805 1.00 5.96  ? 4305 PHE A CD2   1 
ATOM   21100 C  CE1   . PHE A 1 4305 ? 169.712 154.929 222.836 1.00 8.05  ? 4305 PHE A CE1   1 
ATOM   21101 C  CE2   . PHE A 1 4305 ? 168.289 156.842 222.928 1.00 5.87  ? 4305 PHE A CE2   1 
ATOM   21102 C  CZ    . PHE A 1 4305 ? 168.563 155.582 222.444 1.00 10.88 ? 4305 PHE A CZ    1 
ATOM   21103 N  N     . VAL A 1 4306 ? 172.240 158.562 228.019 1.00 9.51  ? 4306 VAL A N     1 
ATOM   21104 C  CA    . VAL A 1 4306 ? 173.294 159.155 228.838 1.00 10.96 ? 4306 VAL A CA    1 
ATOM   21105 C  C     . VAL A 1 4306 ? 173.578 158.283 230.056 1.00 11.52 ? 4306 VAL A C     1 
ATOM   21106 O  O     . VAL A 1 4306 ? 174.726 158.172 230.502 1.00 11.06 ? 4306 VAL A O     1 
ATOM   21107 C  CB    . VAL A 1 4306 ? 172.916 160.594 229.233 1.00 13.39 ? 4306 VAL A CB    1 
ATOM   21108 C  CG1   . VAL A 1 4306 ? 174.060 161.265 229.969 1.00 8.12  ? 4306 VAL A CG1   1 
ATOM   21109 C  CG2   . VAL A 1 4306 ? 172.546 161.401 227.996 1.00 11.76 ? 4306 VAL A CG2   1 
ATOM   21110 N  N     . GLN A 1 4307 ? 172.541 157.654 230.615 1.00 11.71 ? 4307 GLN A N     1 
ATOM   21111 C  CA    . GLN A 1 4307 ? 172.757 156.702 231.700 1.00 10.59 ? 4307 GLN A CA    1 
ATOM   21112 C  C     . GLN A 1 4307 ? 173.576 155.507 231.224 1.00 10.02 ? 4307 GLN A C     1 
ATOM   21113 O  O     . GLN A 1 4307 ? 174.458 155.024 231.941 1.00 12.61 ? 4307 GLN A O     1 
ATOM   21114 C  CB    . GLN A 1 4307 ? 171.418 156.238 232.272 1.00 14.53 ? 4307 GLN A CB    1 
ATOM   21115 C  CG    . GLN A 1 4307 ? 170.795 157.206 233.262 1.00 21.86 ? 4307 GLN A CG    1 
ATOM   21116 C  CD    . GLN A 1 4307 ? 169.316 156.953 233.471 1.00 27.78 ? 4307 GLN A CD    1 
ATOM   21117 O  OE1   . GLN A 1 4307 ? 168.566 156.754 232.515 1.00 28.50 ? 4307 GLN A OE1   1 
ATOM   21118 N  NE2   . GLN A 1 4307 ? 168.887 156.957 234.728 1.00 30.98 ? 4307 GLN A NE2   1 
ATOM   21119 N  N     . TRP A 1 4308 ? 173.293 155.021 230.014 1.00 10.93 ? 4308 TRP A N     1 
ATOM   21120 C  CA    . TRP A 1 4308 ? 174.043 153.893 229.469 1.00 4.72  ? 4308 TRP A CA    1 
ATOM   21121 C  C     . TRP A 1 4308 ? 175.513 154.247 229.284 1.00 5.56  ? 4308 TRP A C     1 
ATOM   21122 O  O     . TRP A 1 4308 ? 176.395 153.424 229.559 1.00 9.23  ? 4308 TRP A O     1 
ATOM   21123 C  CB    . TRP A 1 4308 ? 173.417 153.454 228.145 1.00 6.27  ? 4308 TRP A CB    1 
ATOM   21124 C  CG    . TRP A 1 4308 ? 174.116 152.316 227.468 1.00 7.42  ? 4308 TRP A CG    1 
ATOM   21125 C  CD1   . TRP A 1 4308 ? 173.822 150.991 227.579 1.00 3.42  ? 4308 TRP A CD1   1 
ATOM   21126 C  CD2   . TRP A 1 4308 ? 175.222 152.404 226.562 1.00 4.11  ? 4308 TRP A CD2   1 
ATOM   21127 N  NE1   . TRP A 1 4308 ? 174.674 150.248 226.804 1.00 4.76  ? 4308 TRP A NE1   1 
ATOM   21128 C  CE2   . TRP A 1 4308 ? 175.544 151.092 226.168 1.00 4.49  ? 4308 TRP A CE2   1 
ATOM   21129 C  CE3   . TRP A 1 4308 ? 175.972 153.464 226.047 1.00 3.56  ? 4308 TRP A CE3   1 
ATOM   21130 C  CZ2   . TRP A 1 4308 ? 176.583 150.814 225.285 1.00 4.57  ? 4308 TRP A CZ2   1 
ATOM   21131 C  CZ3   . TRP A 1 4308 ? 177.002 153.184 225.172 1.00 2.80  ? 4308 TRP A CZ3   1 
ATOM   21132 C  CH2   . TRP A 1 4308 ? 177.299 151.871 224.800 1.00 3.83  ? 4308 TRP A CH2   1 
ATOM   21133 N  N     . VAL A 1 4309 ? 175.796 155.463 228.815 1.00 4.17  ? 4309 VAL A N     1 
ATOM   21134 C  CA    . VAL A 1 4309 ? 177.181 155.881 228.620 1.00 5.01  ? 4309 VAL A CA    1 
ATOM   21135 C  C     . VAL A 1 4309 ? 177.908 155.970 229.958 1.00 5.01  ? 4309 VAL A C     1 
ATOM   21136 O  O     . VAL A 1 4309 ? 179.069 155.561 230.074 1.00 8.13  ? 4309 VAL A O     1 
ATOM   21137 C  CB    . VAL A 1 4309 ? 177.231 157.214 227.850 1.00 6.86  ? 4309 VAL A CB    1 
ATOM   21138 C  CG1   . VAL A 1 4309 ? 178.659 157.718 227.740 1.00 2.01  ? 4309 VAL A CG1   1 
ATOM   21139 C  CG2   . VAL A 1 4309 ? 176.618 157.049 226.471 1.00 2.38  ? 4309 VAL A CG2   1 
ATOM   21140 N  N     . GLU A 1 4310 ? 177.240 156.503 230.986 1.00 10.69 ? 4310 GLU A N     1 
ATOM   21141 C  CA    . GLU A 1 4310 ? 177.858 156.607 232.303 1.00 5.72  ? 4310 GLU A CA    1 
ATOM   21142 C  C     . GLU A 1 4310 ? 178.105 155.248 232.942 1.00 9.31  ? 4310 GLU A C     1 
ATOM   21143 O  O     . GLU A 1 4310 ? 178.980 155.138 233.806 1.00 14.56 ? 4310 GLU A O     1 
ATOM   21144 C  CB    . GLU A 1 4310 ? 176.993 157.456 233.233 1.00 8.46  ? 4310 GLU A CB    1 
ATOM   21145 C  CG    . GLU A 1 4310 ? 176.920 158.924 232.867 1.00 8.23  ? 4310 GLU A CG    1 
ATOM   21146 C  CD    . GLU A 1 4310 ? 175.570 159.527 233.189 1.00 17.81 ? 4310 GLU A CD    1 
ATOM   21147 O  OE1   . GLU A 1 4310 ? 174.729 158.814 233.777 1.00 19.17 ? 4310 GLU A OE1   1 
ATOM   21148 O  OE2   . GLU A 1 4310 ? 175.350 160.711 232.862 1.00 16.97 ? 4310 GLU A OE2   1 
ATOM   21149 N  N     . LEU A 1 4311 ? 177.364 154.218 232.545 1.00 6.52  ? 4311 LEU A N     1 
ATOM   21150 C  CA    . LEU A 1 4311 ? 177.528 152.884 233.100 1.00 5.63  ? 4311 LEU A CA    1 
ATOM   21151 C  C     . LEU A 1 4311 ? 178.529 152.037 232.326 1.00 10.49 ? 4311 LEU A C     1 
ATOM   21152 O  O     . LEU A 1 4311 ? 178.697 150.858 232.648 1.00 14.02 ? 4311 LEU A O     1 
ATOM   21153 C  CB    . LEU A 1 4311 ? 176.180 152.160 233.159 1.00 6.67  ? 4311 LEU A CB    1 
ATOM   21154 C  CG    . LEU A 1 4311 ? 175.161 152.681 234.177 1.00 9.98  ? 4311 LEU A CG    1 
ATOM   21155 C  CD1   . LEU A 1 4311 ? 174.092 151.636 234.438 1.00 8.70  ? 4311 LEU A CD1   1 
ATOM   21156 C  CD2   . LEU A 1 4311 ? 175.838 153.094 235.473 1.00 9.42  ? 4311 LEU A CD2   1 
ATOM   21157 N  N     . LEU A 1 4312 ? 179.179 152.598 231.313 1.00 7.98  ? 4312 LEU A N     1 
ATOM   21158 C  CA    . LEU A 1 4312 ? 180.220 151.865 230.613 1.00 7.22  ? 4312 LEU A CA    1 
ATOM   21159 C  C     . LEU A 1 4312 ? 181.399 151.620 231.552 1.00 10.29 ? 4312 LEU A C     1 
ATOM   21160 O  O     . LEU A 1 4312 ? 181.760 152.497 232.342 1.00 11.00 ? 4312 LEU A O     1 
ATOM   21161 C  CB    . LEU A 1 4312 ? 180.690 152.631 229.378 1.00 6.34  ? 4312 LEU A CB    1 
ATOM   21162 C  CG    . LEU A 1 4312 ? 179.777 152.627 228.150 1.00 4.08  ? 4312 LEU A CG    1 
ATOM   21163 C  CD1   . LEU A 1 4312 ? 180.281 153.610 227.110 1.00 1.90  ? 4312 LEU A CD1   1 
ATOM   21164 C  CD2   . LEU A 1 4312 ? 179.662 151.231 227.558 1.00 2.87  ? 4312 LEU A CD2   1 
ATOM   21165 N  N     . PRO A 1 4313 ? 182.016 150.444 231.495 1.00 12.87 ? 4313 PRO A N     1 
ATOM   21166 C  CA    . PRO A 1 4313 ? 183.160 150.166 232.367 1.00 9.96  ? 4313 PRO A CA    1 
ATOM   21167 C  C     . PRO A 1 4313 ? 184.371 150.993 231.966 1.00 8.36  ? 4313 PRO A C     1 
ATOM   21168 O  O     . PRO A 1 4313 ? 184.457 151.541 230.866 1.00 15.42 ? 4313 PRO A O     1 
ATOM   21169 C  CB    . PRO A 1 4313 ? 183.406 148.671 232.157 1.00 11.01 ? 4313 PRO A CB    1 
ATOM   21170 C  CG    . PRO A 1 4313 ? 182.886 148.408 230.785 1.00 6.68  ? 4313 PRO A CG    1 
ATOM   21171 C  CD    . PRO A 1 4313 ? 181.684 149.295 230.636 1.00 6.30  ? 4313 PRO A CD    1 
ATOM   21172 N  N     . ASP A 1 4314 ? 185.326 151.077 232.892 1.00 10.57 ? 4314 ASP A N     1 
ATOM   21173 C  CA    . ASP A 1 4314 ? 186.597 151.741 232.640 1.00 13.36 ? 4314 ASP A CA    1 
ATOM   21174 C  C     . ASP A 1 4314 ? 187.636 150.765 232.103 1.00 13.84 ? 4314 ASP A C     1 
ATOM   21175 O  O     . ASP A 1 4314 ? 188.835 150.904 232.372 1.00 20.74 ? 4314 ASP A O     1 
ATOM   21176 C  CB    . ASP A 1 4314 ? 187.089 152.429 233.918 1.00 14.26 ? 4314 ASP A CB    1 
ATOM   21177 C  CG    . ASP A 1 4314 ? 188.242 153.396 233.671 1.00 21.82 ? 4314 ASP A CG    1 
ATOM   21178 O  OD1   . ASP A 1 4314 ? 188.678 153.546 232.511 1.00 18.02 ? 4314 ASP A OD1   1 
ATOM   21179 O  OD2   . ASP A 1 4314 ? 188.716 154.012 234.650 1.00 24.22 ? 4314 ASP A OD2   1 
ATOM   21180 N  N     . THR A 1 4315 ? 187.191 149.752 231.368 1.00 12.85 ? 4315 THR A N     1 
ATOM   21181 C  CA    . THR A 1 4315 ? 188.047 148.709 230.821 1.00 9.80  ? 4315 THR A CA    1 
ATOM   21182 C  C     . THR A 1 4315 ? 188.072 148.760 229.297 1.00 9.61  ? 4315 THR A C     1 
ATOM   21183 O  O     . THR A 1 4315 ? 188.021 147.729 228.625 1.00 16.02 ? 4315 THR A O     1 
ATOM   21184 C  CB    . THR A 1 4315 ? 187.589 147.335 231.301 1.00 18.37 ? 4315 THR A CB    1 
ATOM   21185 O  OG1   . THR A 1 4315 ? 186.354 146.993 230.659 1.00 17.66 ? 4315 THR A OG1   1 
ATOM   21186 C  CG2   . THR A 1 4315 ? 187.380 147.346 232.806 1.00 11.71 ? 4315 THR A CG2   1 
ATOM   21187 N  N     . GLN A 1 4316 ? 188.134 149.966 228.740 1.00 11.34 ? 4316 GLN A N     1 
ATOM   21188 C  CA    . GLN A 1 4316 ? 188.166 150.121 227.294 1.00 3.46  ? 4316 GLN A CA    1 
ATOM   21189 C  C     . GLN A 1 4316 ? 189.439 149.525 226.714 1.00 4.48  ? 4316 GLN A C     1 
ATOM   21190 O  O     . GLN A 1 4316 ? 190.539 149.728 227.234 1.00 8.39  ? 4316 GLN A O     1 
ATOM   21191 C  CB    . GLN A 1 4316 ? 188.064 151.595 226.907 1.00 3.44  ? 4316 GLN A CB    1 
ATOM   21192 C  CG    . GLN A 1 4316 ? 188.084 151.838 225.406 1.00 2.71  ? 4316 GLN A CG    1 
ATOM   21193 C  CD    . GLN A 1 4316 ? 188.167 153.307 225.048 1.00 5.47  ? 4316 GLN A CD    1 
ATOM   21194 O  OE1   . GLN A 1 4316 ? 187.389 154.122 225.540 1.00 7.07  ? 4316 GLN A OE1   1 
ATOM   21195 N  NE2   . GLN A 1 4316 ? 189.110 153.653 224.183 1.00 4.98  ? 4316 GLN A NE2   1 
ATOM   21196 N  N     . THR A 1 4317 ? 189.279 148.793 225.624 1.00 6.46  ? 4317 THR A N     1 
ATOM   21197 C  CA    . THR A 1 4317 ? 190.361 148.197 224.860 1.00 4.55  ? 4317 THR A CA    1 
ATOM   21198 C  C     . THR A 1 4317 ? 190.177 148.594 223.406 1.00 4.43  ? 4317 THR A C     1 
ATOM   21199 O  O     . THR A 1 4317 ? 189.078 148.982 222.999 1.00 5.95  ? 4317 THR A O     1 
ATOM   21200 C  CB    . THR A 1 4317 ? 190.365 146.667 224.997 1.00 9.34  ? 4317 THR A CB    1 
ATOM   21201 O  OG1   . THR A 1 4317 ? 189.082 146.149 224.626 1.00 8.38  ? 4317 THR A OG1   1 
ATOM   21202 C  CG2   . THR A 1 4317 ? 190.681 146.257 226.424 1.00 3.35  ? 4317 THR A CG2   1 
ATOM   21203 N  N     . PRO A 1 4318 ? 191.236 148.525 222.596 1.00 7.69  ? 4318 PRO A N     1 
ATOM   21204 C  CA    . PRO A 1 4318 ? 191.078 148.846 221.169 1.00 4.50  ? 4318 PRO A CA    1 
ATOM   21205 C  C     . PRO A 1 4318 ? 190.085 147.949 220.449 1.00 2.83  ? 4318 PRO A C     1 
ATOM   21206 O  O     . PRO A 1 4318 ? 189.638 148.306 219.352 1.00 4.63  ? 4318 PRO A O     1 
ATOM   21207 C  CB    . PRO A 1 4318 ? 192.499 148.690 220.606 1.00 6.90  ? 4318 PRO A CB    1 
ATOM   21208 C  CG    . PRO A 1 4318 ? 193.275 147.974 221.660 1.00 5.52  ? 4318 PRO A CG    1 
ATOM   21209 C  CD    . PRO A 1 4318 ? 192.647 148.327 222.961 1.00 4.87  ? 4318 PRO A CD    1 
ATOM   21210 N  N     . SER A 1 4319 ? 189.724 146.800 221.025 1.00 1.94  ? 4319 SER A N     1 
ATOM   21211 C  CA    . SER A 1 4319 ? 188.664 145.976 220.456 1.00 3.00  ? 4319 SER A CA    1 
ATOM   21212 C  C     . SER A 1 4319 ? 187.307 146.668 220.495 1.00 3.56  ? 4319 SER A C     1 
ATOM   21213 O  O     . SER A 1 4319 ? 186.408 146.283 219.740 1.00 6.56  ? 4319 SER A O     1 
ATOM   21214 C  CB    . SER A 1 4319 ? 188.589 144.634 221.184 1.00 6.03  ? 4319 SER A CB    1 
ATOM   21215 O  OG    . SER A 1 4319 ? 188.332 144.817 222.565 1.00 7.12  ? 4319 SER A OG    1 
ATOM   21216 N  N     . TRP A 1 4320 ? 187.133 147.668 221.362 1.00 3.21  ? 4320 TRP A N     1 
ATOM   21217 C  CA    . TRP A 1 4320 ? 185.931 148.495 221.301 1.00 2.97  ? 4320 TRP A CA    1 
ATOM   21218 C  C     . TRP A 1 4320 ? 185.816 149.192 219.955 1.00 2.80  ? 4320 TRP A C     1 
ATOM   21219 O  O     . TRP A 1 4320 ? 184.706 149.447 219.477 1.00 2.08  ? 4320 TRP A O     1 
ATOM   21220 C  CB    . TRP A 1 4320 ? 185.947 149.543 222.415 1.00 6.58  ? 4320 TRP A CB    1 
ATOM   21221 C  CG    . TRP A 1 4320 ? 185.694 149.017 223.787 1.00 4.40  ? 4320 TRP A CG    1 
ATOM   21222 C  CD1   . TRP A 1 4320 ? 186.014 147.783 224.269 1.00 4.94  ? 4320 TRP A CD1   1 
ATOM   21223 C  CD2   . TRP A 1 4320 ? 185.069 149.719 224.866 1.00 3.79  ? 4320 TRP A CD2   1 
ATOM   21224 N  NE1   . TRP A 1 4320 ? 185.625 147.672 225.579 1.00 5.83  ? 4320 TRP A NE1   1 
ATOM   21225 C  CE2   . TRP A 1 4320 ? 185.042 148.847 225.970 1.00 3.77  ? 4320 TRP A CE2   1 
ATOM   21226 C  CE3   . TRP A 1 4320 ? 184.529 151.000 225.002 1.00 5.11  ? 4320 TRP A CE3   1 
ATOM   21227 C  CZ2   . TRP A 1 4320 ? 184.496 149.215 227.197 1.00 5.25  ? 4320 TRP A CZ2   1 
ATOM   21228 C  CZ3   . TRP A 1 4320 ? 183.984 151.363 226.220 1.00 4.61  ? 4320 TRP A CZ3   1 
ATOM   21229 C  CH2   . TRP A 1 4320 ? 183.974 150.475 227.301 1.00 5.78  ? 4320 TRP A CH2   1 
ATOM   21230 N  N     . LEU A 1 4321 ? 186.950 149.505 219.340 1.00 3.40  ? 4321 LEU A N     1 
ATOM   21231 C  CA    . LEU A 1 4321 ? 187.010 150.233 218.083 1.00 1.13  ? 4321 LEU A CA    1 
ATOM   21232 C  C     . LEU A 1 4321 ? 187.063 149.315 216.872 1.00 2.55  ? 4321 LEU A C     1 
ATOM   21233 O  O     . LEU A 1 4321 ? 187.139 149.808 215.744 1.00 8.02  ? 4321 LEU A O     1 
ATOM   21234 C  CB    . LEU A 1 4321 ? 188.235 151.150 218.086 1.00 1.18  ? 4321 LEU A CB    1 
ATOM   21235 C  CG    . LEU A 1 4321 ? 188.465 151.941 219.376 1.00 0.96  ? 4321 LEU A CG    1 
ATOM   21236 C  CD1   . LEU A 1 4321 ? 189.766 152.714 219.307 1.00 0.51  ? 4321 LEU A CD1   1 
ATOM   21237 C  CD2   . LEU A 1 4321 ? 187.303 152.868 219.670 1.00 0.83  ? 4321 LEU A CD2   1 
ATOM   21238 N  N     . GLY A 1 4322 ? 187.023 147.999 217.076 1.00 1.31  ? 4322 GLY A N     1 
ATOM   21239 C  CA    . GLY A 1 4322 ? 187.223 147.046 216.008 1.00 1.75  ? 4322 GLY A CA    1 
ATOM   21240 C  C     . GLY A 1 4322 ? 188.667 146.677 215.745 1.00 2.28  ? 4322 GLY A C     1 
ATOM   21241 O  O     . GLY A 1 4322 ? 188.926 145.844 214.869 1.00 2.67  ? 4322 GLY A O     1 
ATOM   21242 N  N     . LEU A 1 4323 ? 189.605 147.267 216.469 1.00 1.99  ? 4323 LEU A N     1 
ATOM   21243 C  CA    . LEU A 1 4323 ? 191.030 147.009 216.352 1.00 2.03  ? 4323 LEU A CA    1 
ATOM   21244 C  C     . LEU A 1 4323 ? 191.423 145.789 217.172 1.00 2.32  ? 4323 LEU A C     1 
ATOM   21245 O  O     . LEU A 1 4323 ? 190.705 145.386 218.090 1.00 4.46  ? 4323 LEU A O     1 
ATOM   21246 C  CB    . LEU A 1 4323 ? 191.816 148.232 216.819 1.00 1.80  ? 4323 LEU A CB    1 
ATOM   21247 C  CG    . LEU A 1 4323 ? 191.853 149.421 215.858 1.00 1.36  ? 4323 LEU A CG    1 
ATOM   21248 C  CD1   . LEU A 1 4323 ? 192.381 150.658 216.556 1.00 1.83  ? 4323 LEU A CD1   1 
ATOM   21249 C  CD2   . LEU A 1 4323 ? 192.699 149.093 214.639 1.00 1.65  ? 4323 LEU A CD2   1 
ATOM   21250 N  N     . PRO A 1 4324 ? 192.550 145.155 216.852 1.00 3.76  ? 4324 PRO A N     1 
ATOM   21251 C  CA    . PRO A 1 4324 ? 193.069 144.105 217.735 1.00 4.68  ? 4324 PRO A CA    1 
ATOM   21252 C  C     . PRO A 1 4324 ? 193.520 144.682 219.067 1.00 4.55  ? 4324 PRO A C     1 
ATOM   21253 O  O     . PRO A 1 4324 ? 193.958 145.832 219.158 1.00 4.53  ? 4324 PRO A O     1 
ATOM   21254 C  CB    . PRO A 1 4324 ? 194.247 143.526 216.945 1.00 3.26  ? 4324 PRO A CB    1 
ATOM   21255 C  CG    . PRO A 1 4324 ? 194.653 144.613 216.015 1.00 3.82  ? 4324 PRO A CG    1 
ATOM   21256 C  CD    . PRO A 1 4324 ? 193.395 145.344 215.659 1.00 2.16  ? 4324 PRO A CD    1 
ATOM   21257 N  N     . ASN A 1 4325 ? 193.408 143.863 220.112 1.00 4.34  ? 4325 ASN A N     1 
ATOM   21258 C  CA    . ASN A 1 4325 ? 193.748 144.310 221.457 1.00 4.42  ? 4325 ASN A CA    1 
ATOM   21259 C  C     . ASN A 1 4325 ? 195.238 144.558 221.654 1.00 6.67  ? 4325 ASN A C     1 
ATOM   21260 O  O     . ASN A 1 4325 ? 195.611 145.220 222.627 1.00 16.37 ? 4325 ASN A O     1 
ATOM   21261 C  CB    . ASN A 1 4325 ? 193.245 143.298 222.483 1.00 7.25  ? 4325 ASN A CB    1 
ATOM   21262 C  CG    . ASN A 1 4325 ? 191.860 143.632 222.984 1.00 6.76  ? 4325 ASN A CG    1 
ATOM   21263 O  OD1   . ASN A 1 4325 ? 191.335 144.704 222.699 1.00 9.78  ? 4325 ASN A OD1   1 
ATOM   21264 N  ND2   . ASN A 1 4325 ? 191.254 142.710 223.717 1.00 9.30  ? 4325 ASN A ND2   1 
ATOM   21265 N  N     . ASN A 1 4326 ? 196.089 144.063 220.760 1.00 6.68  ? 4326 ASN A N     1 
ATOM   21266 C  CA    . ASN A 1 4326 ? 197.518 144.329 220.840 1.00 5.10  ? 4326 ASN A CA    1 
ATOM   21267 C  C     . ASN A 1 4326 ? 197.899 145.690 220.272 1.00 6.75  ? 4326 ASN A C     1 
ATOM   21268 O  O     . ASN A 1 4326 ? 199.073 146.066 220.347 1.00 11.38 ? 4326 ASN A O     1 
ATOM   21269 C  CB    . ASN A 1 4326 ? 198.303 143.233 220.114 1.00 6.15  ? 4326 ASN A CB    1 
ATOM   21270 C  CG    . ASN A 1 4326 ? 197.910 143.100 218.657 1.00 8.54  ? 4326 ASN A CG    1 
ATOM   21271 O  OD1   . ASN A 1 4326 ? 198.221 143.960 217.835 1.00 9.98  ? 4326 ASN A OD1   1 
ATOM   21272 N  ND2   . ASN A 1 4326 ? 197.224 142.014 218.329 1.00 11.52 ? 4326 ASN A ND2   1 
ATOM   21273 N  N     . ALA A 1 4327 ? 196.942 146.427 219.701 1.00 4.20  ? 4327 ALA A N     1 
ATOM   21274 C  CA    . ALA A 1 4327 ? 197.252 147.722 219.105 1.00 4.21  ? 4327 ALA A CA    1 
ATOM   21275 C  C     . ALA A 1 4327 ? 197.747 148.721 220.141 1.00 6.06  ? 4327 ALA A C     1 
ATOM   21276 O  O     . ALA A 1 4327 ? 198.521 149.623 219.809 1.00 10.16 ? 4327 ALA A O     1 
ATOM   21277 C  CB    . ALA A 1 4327 ? 196.024 148.274 218.382 1.00 5.13  ? 4327 ALA A CB    1 
ATOM   21278 N  N     . GLU A 1 4328 ? 197.311 148.582 221.390 1.00 7.23  ? 4328 GLU A N     1 
ATOM   21279 C  CA    . GLU A 1 4328 ? 197.713 149.494 222.450 1.00 5.29  ? 4328 GLU A CA    1 
ATOM   21280 C  C     . GLU A 1 4328 ? 198.954 149.036 223.206 1.00 7.27  ? 4328 GLU A C     1 
ATOM   21281 O  O     . GLU A 1 4328 ? 199.453 149.790 224.046 1.00 10.02 ? 4328 GLU A O     1 
ATOM   21282 C  CB    . GLU A 1 4328 ? 196.557 149.687 223.439 1.00 6.11  ? 4328 GLU A CB    1 
ATOM   21283 C  CG    . GLU A 1 4328 ? 196.440 148.585 224.481 1.00 6.44  ? 4328 GLU A CG    1 
ATOM   21284 C  CD    . GLU A 1 4328 ? 195.154 148.662 225.279 1.00 11.65 ? 4328 GLU A CD    1 
ATOM   21285 O  OE1   . GLU A 1 4328 ? 194.677 149.786 225.539 1.00 10.92 ? 4328 GLU A OE1   1 
ATOM   21286 O  OE2   . GLU A 1 4328 ? 194.619 147.596 225.649 1.00 18.41 ? 4328 GLU A OE2   1 
ATOM   21287 N  N     . ARG A 1 4329 ? 199.475 147.841 222.917 1.00 5.13  ? 4329 ARG A N     1 
ATOM   21288 C  CA    . ARG A 1 4329 ? 200.565 147.288 223.717 1.00 6.13  ? 4329 ARG A CA    1 
ATOM   21289 C  C     . ARG A 1 4329 ? 201.815 148.154 223.641 1.00 6.74  ? 4329 ARG A C     1 
ATOM   21290 O  O     . ARG A 1 4329 ? 202.403 148.506 224.669 1.00 10.81 ? 4329 ARG A O     1 
ATOM   21291 C  CB    . ARG A 1 4329 ? 200.873 145.860 223.268 1.00 5.14  ? 4329 ARG A CB    1 
ATOM   21292 C  CG    . ARG A 1 4329 ? 201.310 144.946 224.395 1.00 5.12  ? 4329 ARG A CG    1 
ATOM   21293 C  CD    . ARG A 1 4329 ? 201.899 143.654 223.861 1.00 11.28 ? 4329 ARG A CD    1 
ATOM   21294 N  NE    . ARG A 1 4329 ? 202.295 142.736 224.923 1.00 17.14 ? 4329 ARG A NE    1 
ATOM   21295 C  CZ    . ARG A 1 4329 ? 201.450 142.075 225.702 1.00 12.06 ? 4329 ARG A CZ    1 
ATOM   21296 N  NH1   . ARG A 1 4329 ? 200.141 142.204 225.572 1.00 10.66 ? 4329 ARG A NH1   1 
ATOM   21297 N  NH2   . ARG A 1 4329 ? 201.934 141.256 226.633 1.00 14.09 ? 4329 ARG A NH2   1 
ATOM   21298 N  N     . VAL A 1 4330 ? 202.244 148.502 222.428 1.00 5.83  ? 4330 VAL A N     1 
ATOM   21299 C  CA    . VAL A 1 4330 ? 203.433 149.333 222.275 1.00 7.01  ? 4330 VAL A CA    1 
ATOM   21300 C  C     . VAL A 1 4330 ? 203.165 150.747 222.777 1.00 7.93  ? 4330 VAL A C     1 
ATOM   21301 O  O     . VAL A 1 4330 ? 204.006 151.356 223.447 1.00 7.02  ? 4330 VAL A O     1 
ATOM   21302 C  CB    . VAL A 1 4330 ? 203.900 149.324 220.810 1.00 2.88  ? 4330 VAL A CB    1 
ATOM   21303 C  CG1   . VAL A 1 4330 ? 204.926 150.415 220.565 1.00 1.55  ? 4330 VAL A CG1   1 
ATOM   21304 C  CG2   . VAL A 1 4330 ? 204.462 147.960 220.445 1.00 2.74  ? 4330 VAL A CG2   1 
ATOM   21305 N  N     . LEU A 1 4331 ? 201.983 151.285 222.466 1.00 7.46  ? 4331 LEU A N     1 
ATOM   21306 C  CA    . LEU A 1 4331 ? 201.637 152.638 222.888 1.00 7.04  ? 4331 LEU A CA    1 
ATOM   21307 C  C     . LEU A 1 4331 ? 201.587 152.749 224.409 1.00 6.90  ? 4331 LEU A C     1 
ATOM   21308 O  O     . LEU A 1 4331 ? 202.055 153.741 224.979 1.00 8.01  ? 4331 LEU A O     1 
ATOM   21309 C  CB    . LEU A 1 4331 ? 200.302 153.039 222.252 1.00 11.67 ? 4331 LEU A CB    1 
ATOM   21310 C  CG    . LEU A 1 4331 ? 199.736 154.455 222.357 1.00 15.57 ? 4331 LEU A CG    1 
ATOM   21311 C  CD1   . LEU A 1 4331 ? 198.846 154.724 221.164 1.00 11.69 ? 4331 LEU A CD1   1 
ATOM   21312 C  CD2   . LEU A 1 4331 ? 198.919 154.607 223.616 1.00 12.69 ? 4331 LEU A CD2   1 
ATOM   21313 N  N     . LEU A 1 4332 ? 201.022 151.744 225.080 1.00 5.46  ? 4332 LEU A N     1 
ATOM   21314 C  CA    . LEU A 1 4332 ? 201.000 151.751 226.541 1.00 5.74  ? 4332 LEU A CA    1 
ATOM   21315 C  C     . LEU A 1 4332 ? 202.399 151.588 227.120 1.00 6.46  ? 4332 LEU A C     1 
ATOM   21316 O  O     . LEU A 1 4332 ? 202.746 152.240 228.110 1.00 6.98  ? 4332 LEU A O     1 
ATOM   21317 C  CB    . LEU A 1 4332 ? 200.075 150.655 227.061 1.00 6.79  ? 4332 LEU A CB    1 
ATOM   21318 C  CG    . LEU A 1 4332 ? 198.572 150.888 226.909 1.00 3.85  ? 4332 LEU A CG    1 
ATOM   21319 C  CD1   . LEU A 1 4332 ? 197.788 149.782 227.591 1.00 2.55  ? 4332 LEU A CD1   1 
ATOM   21320 C  CD2   . LEU A 1 4332 ? 198.185 152.249 227.456 1.00 1.74  ? 4332 LEU A CD2   1 
ATOM   21321 N  N     . THR A 1 4333 ? 203.211 150.713 226.521 1.00 8.61  ? 4333 THR A N     1 
ATOM   21322 C  CA    . THR A 1 4333 ? 204.553 150.463 227.037 1.00 6.68  ? 4333 THR A CA    1 
ATOM   21323 C  C     . THR A 1 4333 ? 205.417 151.716 226.964 1.00 5.54  ? 4333 THR A C     1 
ATOM   21324 O  O     . THR A 1 4333 ? 206.183 152.004 227.891 1.00 6.70  ? 4333 THR A O     1 
ATOM   21325 C  CB    . THR A 1 4333 ? 205.199 149.312 226.265 1.00 6.48  ? 4333 THR A CB    1 
ATOM   21326 O  OG1   . THR A 1 4333 ? 204.355 148.157 226.340 1.00 6.19  ? 4333 THR A OG1   1 
ATOM   21327 C  CG2   . THR A 1 4333 ? 206.560 148.969 226.845 1.00 4.85  ? 4333 THR A CG2   1 
ATOM   21328 N  N     . THR A 1 4334 ? 205.311 152.472 225.870 1.00 3.81  ? 4334 THR A N     1 
ATOM   21329 C  CA    . THR A 1 4334 ? 206.084 153.702 225.744 1.00 4.04  ? 4334 THR A CA    1 
ATOM   21330 C  C     . THR A 1 4334 ? 205.662 154.732 226.787 1.00 7.73  ? 4334 THR A C     1 
ATOM   21331 O  O     . THR A 1 4334 ? 206.514 155.397 227.386 1.00 6.92  ? 4334 THR A O     1 
ATOM   21332 C  CB    . THR A 1 4334 ? 205.937 154.275 224.334 1.00 5.97  ? 4334 THR A CB    1 
ATOM   21333 O  OG1   . THR A 1 4334 ? 206.228 153.259 223.370 1.00 8.21  ? 4334 THR A OG1   1 
ATOM   21334 C  CG2   . THR A 1 4334 ? 206.891 155.437 224.133 1.00 5.09  ? 4334 THR A CG2   1 
ATOM   21335 N  N     . GLN A 1 4335 ? 204.355 154.876 227.019 1.00 9.22  ? 4335 GLN A N     1 
ATOM   21336 C  CA    . GLN A 1 4335 ? 203.888 155.841 228.011 1.00 4.92  ? 4335 GLN A CA    1 
ATOM   21337 C  C     . GLN A 1 4335 ? 204.350 155.467 229.411 1.00 4.79  ? 4335 GLN A C     1 
ATOM   21338 O  O     . GLN A 1 4335 ? 204.730 156.340 230.200 1.00 8.43  ? 4335 GLN A O     1 
ATOM   21339 C  CB    . GLN A 1 4335 ? 202.365 155.958 227.979 1.00 7.32  ? 4335 GLN A CB    1 
ATOM   21340 C  CG    . GLN A 1 4335 ? 201.811 156.848 226.892 1.00 5.37  ? 4335 GLN A CG    1 
ATOM   21341 C  CD    . GLN A 1 4335 ? 200.298 156.912 226.931 1.00 16.23 ? 4335 GLN A CD    1 
ATOM   21342 O  OE1   . GLN A 1 4335 ? 199.720 157.858 227.467 1.00 12.65 ? 4335 GLN A OE1   1 
ATOM   21343 N  NE2   . GLN A 1 4335 ? 199.649 155.885 226.399 1.00 10.43 ? 4335 GLN A NE2   1 
ATOM   21344 N  N     . GLY A 1 4336 ? 204.309 154.175 229.744 1.00 5.57  ? 4336 GLY A N     1 
ATOM   21345 C  CA    . GLY A 1 4336 ? 204.790 153.745 231.046 1.00 4.61  ? 4336 GLY A CA    1 
ATOM   21346 C  C     . GLY A 1 4336 ? 206.250 154.089 231.264 1.00 6.90  ? 4336 GLY A C     1 
ATOM   21347 O  O     . GLY A 1 4336 ? 206.637 154.545 232.342 1.00 8.63  ? 4336 GLY A O     1 
ATOM   21348 N  N     . VAL A 1 4337 ? 207.080 153.877 230.240 1.00 5.99  ? 4337 VAL A N     1 
ATOM   21349 C  CA    . VAL A 1 4337 ? 208.469 154.317 230.308 1.00 6.75  ? 4337 VAL A CA    1 
ATOM   21350 C  C     . VAL A 1 4337 ? 208.539 155.840 230.326 1.00 7.54  ? 4337 VAL A C     1 
ATOM   21351 O  O     . VAL A 1 4337 ? 209.390 156.430 231.002 1.00 7.98  ? 4337 VAL A O     1 
ATOM   21352 C  CB    . VAL A 1 4337 ? 209.269 153.716 229.139 1.00 4.01  ? 4337 VAL A CB    1 
ATOM   21353 C  CG1   . VAL A 1 4337 ? 210.671 154.292 229.088 1.00 7.18  ? 4337 VAL A CG1   1 
ATOM   21354 C  CG2   . VAL A 1 4337 ? 209.313 152.202 229.256 1.00 4.85  ? 4337 VAL A CG2   1 
ATOM   21355 N  N     . ASP A 1 4338 ? 207.638 156.498 229.592 1.00 7.87  ? 4338 ASP A N     1 
ATOM   21356 C  CA    . ASP A 1 4338 ? 207.587 157.956 229.601 1.00 5.70  ? 4338 ASP A CA    1 
ATOM   21357 C  C     . ASP A 1 4338 ? 207.238 158.490 230.986 1.00 7.48  ? 4338 ASP A C     1 
ATOM   21358 O  O     . ASP A 1 4338 ? 207.788 159.505 231.424 1.00 6.13  ? 4338 ASP A O     1 
ATOM   21359 C  CB    . ASP A 1 4338 ? 206.582 158.443 228.557 1.00 8.21  ? 4338 ASP A CB    1 
ATOM   21360 C  CG    . ASP A 1 4338 ? 206.446 159.950 228.530 1.00 20.85 ? 4338 ASP A CG    1 
ATOM   21361 O  OD1   . ASP A 1 4338 ? 207.445 160.638 228.236 1.00 21.50 ? 4338 ASP A OD1   1 
ATOM   21362 O  OD2   . ASP A 1 4338 ? 205.330 160.445 228.797 1.00 26.54 ? 4338 ASP A OD2   1 
ATOM   21363 N  N     . MET A 1 4339 ? 206.324 157.817 231.690 1.00 7.96  ? 4339 MET A N     1 
ATOM   21364 C  CA    . MET A 1 4339 ? 205.988 158.227 233.051 1.00 5.73  ? 4339 MET A CA    1 
ATOM   21365 C  C     . MET A 1 4339 ? 207.185 158.086 233.984 1.00 9.02  ? 4339 MET A C     1 
ATOM   21366 O  O     . MET A 1 4339 ? 207.409 158.940 234.849 1.00 9.85  ? 4339 MET A O     1 
ATOM   21367 C  CB    . MET A 1 4339 ? 204.804 157.412 233.570 1.00 6.62  ? 4339 MET A CB    1 
ATOM   21368 C  CG    . MET A 1 4339 ? 204.579 157.538 235.067 1.00 8.27  ? 4339 MET A CG    1 
ATOM   21369 S  SD    . MET A 1 4339 ? 203.183 156.577 235.672 1.00 21.56 ? 4339 MET A SD    1 
ATOM   21370 C  CE    . MET A 1 4339 ? 203.902 154.939 235.718 1.00 4.85  ? 4339 MET A CE    1 
ATOM   21371 N  N     . ILE A 1 4340 ? 207.962 157.010 233.828 1.00 10.86 ? 4340 ILE A N     1 
ATOM   21372 C  CA    . ILE A 1 4340 ? 209.155 156.830 234.652 1.00 8.64  ? 4340 ILE A CA    1 
ATOM   21373 C  C     . ILE A 1 4340 ? 210.156 157.946 234.393 1.00 7.80  ? 4340 ILE A C     1 
ATOM   21374 O  O     . ILE A 1 4340 ? 210.728 158.517 235.329 1.00 9.48  ? 4340 ILE A O     1 
ATOM   21375 C  CB    . ILE A 1 4340 ? 209.783 155.448 234.395 1.00 12.01 ? 4340 ILE A CB    1 
ATOM   21376 C  CG1   . ILE A 1 4340 ? 208.785 154.336 234.703 1.00 8.09  ? 4340 ILE A CG1   1 
ATOM   21377 C  CG2   . ILE A 1 4340 ? 211.040 155.272 235.235 1.00 9.46  ? 4340 ILE A CG2   1 
ATOM   21378 C  CD1   . ILE A 1 4340 ? 208.338 154.320 236.124 1.00 8.86  ? 4340 ILE A CD1   1 
ATOM   21379 N  N     . SER A 1 4341 ? 210.385 158.272 233.119 1.00 6.56  ? 4341 SER A N     1 
ATOM   21380 C  CA    . SER A 1 4341 ? 211.340 159.321 232.779 1.00 5.56  ? 4341 SER A CA    1 
ATOM   21381 C  C     . SER A 1 4341 ? 210.903 160.669 233.335 1.00 8.64  ? 4341 SER A C     1 
ATOM   21382 O  O     . SER A 1 4341 ? 211.727 161.441 233.834 1.00 9.58  ? 4341 SER A O     1 
ATOM   21383 C  CB    . SER A 1 4341 ? 211.514 159.397 231.263 1.00 8.21  ? 4341 SER A CB    1 
ATOM   21384 O  OG    . SER A 1 4341 ? 212.078 158.201 230.756 1.00 20.12 ? 4341 SER A OG    1 
ATOM   21385 N  N     . LYS A 1 4342 ? 209.607 160.972 233.244 1.00 8.56  ? 4342 LYS A N     1 
ATOM   21386 C  CA    . LYS A 1 4342 ? 209.103 162.240 233.759 1.00 5.59  ? 4342 LYS A CA    1 
ATOM   21387 C  C     . LYS A 1 4342 ? 209.192 162.299 235.278 1.00 8.13  ? 4342 LYS A C     1 
ATOM   21388 O  O     . LYS A 1 4342 ? 209.563 163.333 235.844 1.00 7.80  ? 4342 LYS A O     1 
ATOM   21389 C  CB    . LYS A 1 4342 ? 207.667 162.461 233.288 1.00 4.60  ? 4342 LYS A CB    1 
ATOM   21390 C  CG    . LYS A 1 4342 ? 207.565 163.113 231.923 1.00 5.34  ? 4342 LYS A CG    1 
ATOM   21391 C  CD    . LYS A 1 4342 ? 206.338 162.649 231.162 1.00 8.05  ? 4342 LYS A CD    1 
ATOM   21392 C  CE    . LYS A 1 4342 ? 206.265 163.313 229.797 1.00 9.82  ? 4342 LYS A CE    1 
ATOM   21393 N  NZ    . LYS A 1 4342 ? 204.942 163.097 229.150 1.00 11.52 ? 4342 LYS A NZ    1 
ATOM   21394 N  N     . MET A 1 4343 ? 208.855 161.199 235.957 1.00 7.34  ? 4343 MET A N     1 
ATOM   21395 C  CA    . MET A 1 4343 ? 208.975 161.162 237.411 1.00 5.49  ? 4343 MET A CA    1 
ATOM   21396 C  C     . MET A 1 4343 ? 210.426 161.310 237.845 1.00 9.93  ? 4343 MET A C     1 
ATOM   21397 O  O     . MET A 1 4343 ? 210.727 162.039 238.796 1.00 15.34 ? 4343 MET A O     1 
ATOM   21398 C  CB    . MET A 1 4343 ? 208.388 159.860 237.958 1.00 5.94  ? 4343 MET A CB    1 
ATOM   21399 C  CG    . MET A 1 4343 ? 206.910 159.928 238.295 1.00 4.04  ? 4343 MET A CG    1 
ATOM   21400 S  SD    . MET A 1 4343 ? 206.228 158.308 238.693 1.00 14.49 ? 4343 MET A SD    1 
ATOM   21401 C  CE    . MET A 1 4343 ? 207.110 157.935 240.206 1.00 9.12  ? 4343 MET A CE    1 
ATOM   21402 N  N     . LEU A 1 4344 ? 211.339 160.623 237.156 1.00 11.76 ? 4344 LEU A N     1 
ATOM   21403 C  CA    . LEU A 1 4344 ? 212.755 160.706 237.496 1.00 13.22 ? 4344 LEU A CA    1 
ATOM   21404 C  C     . LEU A 1 4344 ? 213.295 162.113 237.282 1.00 12.83 ? 4344 LEU A C     1 
ATOM   21405 O  O     . LEU A 1 4344 ? 214.097 162.604 238.083 1.00 17.02 ? 4344 LEU A O     1 
ATOM   21406 C  CB    . LEU A 1 4344 ? 213.548 159.698 236.670 1.00 11.49 ? 4344 LEU A CB    1 
ATOM   21407 C  CG    . LEU A 1 4344 ? 215.025 159.524 237.025 1.00 18.43 ? 4344 LEU A CG    1 
ATOM   21408 C  CD1   . LEU A 1 4344 ? 215.205 159.252 238.513 1.00 14.71 ? 4344 LEU A CD1   1 
ATOM   21409 C  CD2   . LEU A 1 4344 ? 215.632 158.412 236.187 1.00 18.11 ? 4344 LEU A CD2   1 
ATOM   21410 N  N     . LYS A 1 4345 ? 212.874 162.769 236.200 1.00 8.45  ? 4345 LYS A N     1 
ATOM   21411 C  CA    . LYS A 1 4345 ? 213.375 164.105 235.899 1.00 8.52  ? 4345 LYS A CA    1 
ATOM   21412 C  C     . LYS A 1 4345 ? 212.974 165.105 236.977 1.00 15.62 ? 4345 LYS A C     1 
ATOM   21413 O  O     . LYS A 1 4345 ? 213.760 165.989 237.336 1.00 24.37 ? 4345 LYS A O     1 
ATOM   21414 C  CB    . LYS A 1 4345 ? 212.873 164.549 234.526 1.00 8.34  ? 4345 LYS A CB    1 
ATOM   21415 C  CG    . LYS A 1 4345 ? 213.340 165.927 234.108 1.00 14.75 ? 4345 LYS A CG    1 
ATOM   21416 C  CD    . LYS A 1 4345 ? 212.733 166.340 232.779 1.00 17.13 ? 4345 LYS A CD    1 
ATOM   21417 C  CE    . LYS A 1 4345 ? 212.917 165.259 231.727 1.00 17.16 ? 4345 LYS A CE    1 
ATOM   21418 N  NZ    . LYS A 1 4345 ? 212.225 165.600 230.454 1.00 18.07 ? 4345 LYS A NZ    1 
ATOM   21419 N  N     . MET A 1 4346 ? 211.754 164.986 237.505 1.00 10.37 ? 4346 MET A N     1 
ATOM   21420 C  CA    . MET A 1 4346 ? 211.318 165.908 238.548 1.00 10.14 ? 4346 MET A CA    1 
ATOM   21421 C  C     . MET A 1 4346 ? 211.926 165.595 239.911 1.00 13.13 ? 4346 MET A C     1 
ATOM   21422 O  O     . MET A 1 4346 ? 211.822 166.425 240.820 1.00 17.05 ? 4346 MET A O     1 
ATOM   21423 C  CB    . MET A 1 4346 ? 209.792 165.929 238.645 1.00 7.76  ? 4346 MET A CB    1 
ATOM   21424 C  CG    . MET A 1 4346 ? 209.129 166.830 237.616 1.00 8.37  ? 4346 MET A CG    1 
ATOM   21425 S  SD    . MET A 1 4346 ? 207.335 166.694 237.544 1.00 13.73 ? 4346 MET A SD    1 
ATOM   21426 C  CE    . MET A 1 4346 ? 207.140 164.974 237.115 1.00 6.00  ? 4346 MET A CE    1 
ATOM   21427 N  N     . GLN A 1 4347 ? 212.549 164.432 240.082 1.00 15.79 ? 4347 GLN A N     1 
ATOM   21428 C  CA    . GLN A 1 4347 ? 213.235 164.135 241.338 1.00 14.66 ? 4347 GLN A CA    1 
ATOM   21429 C  C     . GLN A 1 4347 ? 214.502 164.971 241.459 1.00 17.72 ? 4347 GLN A C     1 
ATOM   21430 O  O     . GLN A 1 4347 ? 215.202 165.197 240.472 1.00 25.57 ? 4347 GLN A O     1 
ATOM   21431 C  CB    . GLN A 1 4347 ? 213.579 162.647 241.454 1.00 14.76 ? 4347 GLN A CB    1 
ATOM   21432 C  CG    . GLN A 1 4347 ? 212.381 161.719 241.534 1.00 21.77 ? 4347 GLN A CG    1 
ATOM   21433 C  CD    . GLN A 1 4347 ? 211.530 161.966 242.764 1.00 27.16 ? 4347 GLN A CD    1 
ATOM   21434 O  OE1   . GLN A 1 4347 ? 210.412 162.472 242.667 1.00 23.78 ? 4347 GLN A OE1   1 
ATOM   21435 N  NE2   . GLN A 1 4347 ? 212.059 161.617 243.930 1.00 25.08 ? 4347 GLN A NE2   1 
ATOM   21436 N  N     . PRO A 1 4374 ? 240.403 165.221 218.839 1.00 28.80 ? 4374 PRO A N     1 
ATOM   21437 C  CA    . PRO A 1 4374 ? 239.208 165.191 219.692 1.00 27.17 ? 4374 PRO A CA    1 
ATOM   21438 C  C     . PRO A 1 4374 ? 238.586 163.800 219.785 1.00 31.60 ? 4374 PRO A C     1 
ATOM   21439 O  O     . PRO A 1 4374 ? 238.890 162.936 218.964 1.00 34.84 ? 4374 PRO A O     1 
ATOM   21440 C  CB    . PRO A 1 4374 ? 238.253 166.170 218.999 1.00 28.26 ? 4374 PRO A CB    1 
ATOM   21441 C  CG    . PRO A 1 4374 ? 239.130 167.036 218.158 1.00 28.60 ? 4374 PRO A CG    1 
ATOM   21442 C  CD    . PRO A 1 4374 ? 240.251 166.155 217.713 1.00 32.59 ? 4374 PRO A CD    1 
ATOM   21443 N  N     . ALA A 1 4375 ? 237.730 163.596 220.787 1.00 27.35 ? 4375 ALA A N     1 
ATOM   21444 C  CA    . ALA A 1 4375 ? 237.078 162.300 220.954 1.00 28.87 ? 4375 ALA A CA    1 
ATOM   21445 C  C     . ALA A 1 4375 ? 236.153 161.989 219.784 1.00 36.31 ? 4375 ALA A C     1 
ATOM   21446 O  O     . ALA A 1 4375 ? 236.107 160.849 219.310 1.00 35.68 ? 4375 ALA A O     1 
ATOM   21447 C  CB    . ALA A 1 4375 ? 236.308 162.266 222.274 1.00 30.19 ? 4375 ALA A CB    1 
ATOM   21448 N  N     . TRP A 1 4376 ? 235.406 162.989 219.312 1.00 35.34 ? 4376 TRP A N     1 
ATOM   21449 C  CA    . TRP A 1 4376 ? 234.520 162.775 218.170 1.00 27.87 ? 4376 TRP A CA    1 
ATOM   21450 C  C     . TRP A 1 4376 ? 235.310 162.431 216.915 1.00 28.33 ? 4376 TRP A C     1 
ATOM   21451 O  O     . TRP A 1 4376 ? 234.860 161.625 216.093 1.00 29.74 ? 4376 TRP A O     1 
ATOM   21452 C  CB    . TRP A 1 4376 ? 233.648 164.015 217.946 1.00 26.45 ? 4376 TRP A CB    1 
ATOM   21453 C  CG    . TRP A 1 4376 ? 234.377 165.179 217.337 1.00 28.68 ? 4376 TRP A CG    1 
ATOM   21454 C  CD1   . TRP A 1 4376 ? 234.917 166.239 218.001 1.00 31.83 ? 4376 TRP A CD1   1 
ATOM   21455 C  CD2   . TRP A 1 4376 ? 234.637 165.404 215.944 1.00 34.56 ? 4376 TRP A CD2   1 
ATOM   21456 N  NE1   . TRP A 1 4376 ? 235.503 167.106 217.112 1.00 32.93 ? 4376 TRP A NE1   1 
ATOM   21457 C  CE2   . TRP A 1 4376 ? 235.345 166.616 215.844 1.00 30.99 ? 4376 TRP A CE2   1 
ATOM   21458 C  CE3   . TRP A 1 4376 ? 234.345 164.695 214.775 1.00 26.84 ? 4376 TRP A CE3   1 
ATOM   21459 C  CZ2   . TRP A 1 4376 ? 235.764 167.137 214.622 1.00 27.23 ? 4376 TRP A CZ2   1 
ATOM   21460 C  CZ3   . TRP A 1 4376 ? 234.766 165.210 213.565 1.00 26.15 ? 4376 TRP A CZ3   1 
ATOM   21461 C  CH2   . TRP A 1 4376 ? 235.465 166.421 213.497 1.00 31.72 ? 4376 TRP A CH2   1 
ATOM   21462 N  N     . MET A 1 4377 ? 236.488 163.035 216.747 1.00 28.90 ? 4377 MET A N     1 
ATOM   21463 C  CA    . MET A 1 4377 ? 237.268 162.816 215.536 1.00 31.85 ? 4377 MET A CA    1 
ATOM   21464 C  C     . MET A 1 4377 ? 237.723 161.365 215.429 1.00 29.33 ? 4377 MET A C     1 
ATOM   21465 O  O     . MET A 1 4377 ? 237.743 160.792 214.334 1.00 31.06 ? 4377 MET A O     1 
ATOM   21466 C  CB    . MET A 1 4377 ? 238.459 163.774 215.513 1.00 27.30 ? 4377 MET A CB    1 
ATOM   21467 C  CG    . MET A 1 4377 ? 239.308 163.725 214.252 1.00 32.12 ? 4377 MET A CG    1 
ATOM   21468 S  SD    . MET A 1 4377 ? 240.608 164.976 214.314 1.00 53.08 ? 4377 MET A SD    1 
ATOM   21469 C  CE    . MET A 1 4377 ? 241.499 164.648 212.798 1.00 33.00 ? 4377 MET A CE    1 
ATOM   21470 N  N     . ARG A 1 4378 ? 238.092 160.753 216.557 1.00 29.78 ? 4378 ARG A N     1 
ATOM   21471 C  CA    . ARG A 1 4378 ? 238.499 159.351 216.539 1.00 27.30 ? 4378 ARG A CA    1 
ATOM   21472 C  C     . ARG A 1 4378 ? 237.301 158.419 216.382 1.00 26.83 ? 4378 ARG A C     1 
ATOM   21473 O  O     . ARG A 1 4378 ? 237.360 157.450 215.618 1.00 21.17 ? 4378 ARG A O     1 
ATOM   21474 C  CB    . ARG A 1 4378 ? 239.285 159.009 217.807 1.00 27.71 ? 4378 ARG A CB    1 
ATOM   21475 C  CG    . ARG A 1 4378 ? 240.785 159.305 217.739 1.00 27.51 ? 4378 ARG A CG    1 
ATOM   21476 C  CD    . ARG A 1 4378 ? 241.088 160.771 217.470 1.00 32.59 ? 4378 ARG A CD    1 
ATOM   21477 N  NE    . ARG A 1 4378 ? 242.514 161.010 217.276 1.00 34.52 ? 4378 ARG A NE    1 
ATOM   21478 C  CZ    . ARG A 1 4378 ? 243.046 162.195 217.009 1.00 37.22 ? 4378 ARG A CZ    1 
ATOM   21479 N  NH1   . ARG A 1 4378 ? 242.298 163.280 216.897 1.00 36.46 ? 4378 ARG A NH1   1 
ATOM   21480 N  NH2   . ARG A 1 4378 ? 244.364 162.293 216.851 1.00 30.14 ? 4378 ARG A NH2   1 
ATOM   21481 N  N     . THR A 1 4379 ? 236.207 158.693 217.100 1.00 26.96 ? 4379 THR A N     1 
ATOM   21482 C  CA    . THR A 1 4379 ? 235.038 157.819 217.030 1.00 26.64 ? 4379 THR A CA    1 
ATOM   21483 C  C     . THR A 1 4379 ? 234.413 157.830 215.640 1.00 26.99 ? 4379 THR A C     1 
ATOM   21484 O  O     . THR A 1 4379 ? 234.000 156.780 215.132 1.00 27.46 ? 4379 THR A O     1 
ATOM   21485 C  CB    . THR A 1 4379 ? 234.005 158.227 218.081 1.00 26.87 ? 4379 THR A CB    1 
ATOM   21486 O  OG1   . THR A 1 4379 ? 233.671 159.611 217.914 1.00 26.07 ? 4379 THR A OG1   1 
ATOM   21487 C  CG2   . THR A 1 4379 ? 234.549 158.000 219.486 1.00 30.30 ? 4379 THR A CG2   1 
ATOM   21488 N  N     . LEU A 1 4380 ? 234.330 159.005 215.014 1.00 24.54 ? 4380 LEU A N     1 
ATOM   21489 C  CA    . LEU A 1 4380 ? 233.748 159.087 213.679 1.00 21.53 ? 4380 LEU A CA    1 
ATOM   21490 C  C     . LEU A 1 4380 ? 234.633 158.413 212.636 1.00 19.90 ? 4380 LEU A C     1 
ATOM   21491 O  O     . LEU A 1 4380 ? 234.126 157.909 211.630 1.00 22.19 ? 4380 LEU A O     1 
ATOM   21492 C  CB    . LEU A 1 4380 ? 233.496 160.551 213.311 1.00 22.91 ? 4380 LEU A CB    1 
ATOM   21493 C  CG    . LEU A 1 4380 ? 232.807 160.860 211.979 1.00 18.77 ? 4380 LEU A CG    1 
ATOM   21494 C  CD1   . LEU A 1 4380 ? 231.589 159.978 211.783 1.00 14.91 ? 4380 LEU A CD1   1 
ATOM   21495 C  CD2   . LEU A 1 4380 ? 232.420 162.330 211.913 1.00 18.10 ? 4380 LEU A CD2   1 
ATOM   21496 N  N     . HIS A 1 4381 ? 235.950 158.396 212.857 1.00 20.68 ? 4381 HIS A N     1 
ATOM   21497 C  CA    . HIS A 1 4381 ? 236.845 157.733 211.914 1.00 27.62 ? 4381 HIS A CA    1 
ATOM   21498 C  C     . HIS A 1 4381 ? 236.572 156.236 211.850 1.00 22.73 ? 4381 HIS A C     1 
ATOM   21499 O  O     . HIS A 1 4381 ? 236.534 155.651 210.760 1.00 24.60 ? 4381 HIS A O     1 
ATOM   21500 C  CB    . HIS A 1 4381 ? 238.302 157.995 212.295 1.00 22.69 ? 4381 HIS A CB    1 
ATOM   21501 C  CG    . HIS A 1 4381 ? 239.289 157.310 211.403 1.00 23.95 ? 4381 HIS A CG    1 
ATOM   21502 N  ND1   . HIS A 1 4381 ? 239.669 155.997 211.582 1.00 32.87 ? 4381 HIS A ND1   1 
ATOM   21503 C  CD2   . HIS A 1 4381 ? 239.970 157.753 210.319 1.00 25.26 ? 4381 HIS A CD2   1 
ATOM   21504 C  CE1   . HIS A 1 4381 ? 240.542 155.663 210.649 1.00 26.92 ? 4381 HIS A CE1   1 
ATOM   21505 N  NE2   . HIS A 1 4381 ? 240.742 156.711 209.872 1.00 27.03 ? 4381 HIS A NE2   1 
ATOM   21506 N  N     . THR A 1 4382 ? 236.384 155.598 213.006 1.00 23.16 ? 4382 THR A N     1 
ATOM   21507 C  CA    . THR A 1 4382 ? 236.086 154.169 213.019 1.00 27.36 ? 4382 THR A CA    1 
ATOM   21508 C  C     . THR A 1 4382 ? 234.752 153.881 212.343 1.00 31.78 ? 4382 THR A C     1 
ATOM   21509 O  O     . THR A 1 4382 ? 234.632 152.921 211.574 1.00 31.91 ? 4382 THR A O     1 
ATOM   21510 C  CB    . THR A 1 4382 ? 236.078 153.645 214.454 1.00 27.48 ? 4382 THR A CB    1 
ATOM   21511 O  OG1   . THR A 1 4382 ? 235.134 154.393 215.230 1.00 31.37 ? 4382 THR A OG1   1 
ATOM   21512 C  CG2   . THR A 1 4382 ? 237.461 153.783 215.078 1.00 21.73 ? 4382 THR A CG2   1 
ATOM   21513 N  N     . THR A 1 4383 ? 233.741 154.709 212.616 1.00 23.27 ? 4383 THR A N     1 
ATOM   21514 C  CA    . THR A 1 4383 ? 232.414 154.480 212.055 1.00 22.89 ? 4383 THR A CA    1 
ATOM   21515 C  C     . THR A 1 4383 ? 232.419 154.604 210.536 1.00 25.72 ? 4383 THR A C     1 
ATOM   21516 O  O     . THR A 1 4383 ? 231.832 153.770 209.837 1.00 30.66 ? 4383 THR A O     1 
ATOM   21517 C  CB    . THR A 1 4383 ? 231.417 155.464 212.668 1.00 23.53 ? 4383 THR A CB    1 
ATOM   21518 O  OG1   . THR A 1 4383 ? 231.370 155.274 214.087 1.00 25.33 ? 4383 THR A OG1   1 
ATOM   21519 C  CG2   . THR A 1 4383 ? 230.029 155.240 212.094 1.00 19.64 ? 4383 THR A CG2   1 
ATOM   21520 N  N     . ALA A 1 4384 ? 233.076 155.638 210.008 1.00 27.56 ? 4384 ALA A N     1 
ATOM   21521 C  CA    . ALA A 1 4384 ? 233.103 155.835 208.562 1.00 23.39 ? 4384 ALA A CA    1 
ATOM   21522 C  C     . ALA A 1 4384 ? 233.892 154.733 207.866 1.00 26.45 ? 4384 ALA A C     1 
ATOM   21523 O  O     . ALA A 1 4384 ? 233.485 154.248 206.802 1.00 29.05 ? 4384 ALA A O     1 
ATOM   21524 C  CB    . ALA A 1 4384 ? 233.682 157.208 208.233 1.00 26.44 ? 4384 ALA A CB    1 
ATOM   21525 N  N     . SER A 1 4385 ? 235.026 154.327 208.442 1.00 29.10 ? 4385 SER A N     1 
ATOM   21526 C  CA    . SER A 1 4385 ? 235.794 153.228 207.866 1.00 29.93 ? 4385 SER A CA    1 
ATOM   21527 C  C     . SER A 1 4385 ? 234.995 151.931 207.891 1.00 29.86 ? 4385 SER A C     1 
ATOM   21528 O  O     . SER A 1 4385 ? 235.032 151.153 206.931 1.00 31.97 ? 4385 SER A O     1 
ATOM   21529 C  CB    . SER A 1 4385 ? 237.116 153.060 208.615 1.00 25.55 ? 4385 SER A CB    1 
ATOM   21530 O  OG    . SER A 1 4385 ? 237.902 154.236 208.536 1.00 29.63 ? 4385 SER A OG    1 
ATOM   21531 N  N     . ASN A 1 4386 ? 234.273 151.680 208.985 1.00 27.54 ? 4386 ASN A N     1 
ATOM   21532 C  CA    . ASN A 1 4386 ? 233.446 150.482 209.069 1.00 25.54 ? 4386 ASN A CA    1 
ATOM   21533 C  C     . ASN A 1 4386 ? 232.329 150.508 208.033 1.00 31.74 ? 4386 ASN A C     1 
ATOM   21534 O  O     . ASN A 1 4386 ? 232.024 149.483 207.415 1.00 34.18 ? 4386 ASN A O     1 
ATOM   21535 C  CB    . ASN A 1 4386 ? 232.870 150.340 210.478 1.00 23.82 ? 4386 ASN A CB    1 
ATOM   21536 C  CG    . ASN A 1 4386 ? 233.923 149.972 211.502 1.00 30.40 ? 4386 ASN A CG    1 
ATOM   21537 O  OD1   . ASN A 1 4386 ? 235.070 149.687 211.157 1.00 37.06 ? 4386 ASN A OD1   1 
ATOM   21538 N  ND2   . ASN A 1 4386 ? 233.541 149.981 212.773 1.00 31.13 ? 4386 ASN A ND2   1 
ATOM   21539 N  N     . TRP A 1 4387 ? 231.708 151.674 207.832 1.00 29.36 ? 4387 TRP A N     1 
ATOM   21540 C  CA    . TRP A 1 4387 ? 230.639 151.781 206.845 1.00 21.93 ? 4387 TRP A CA    1 
ATOM   21541 C  C     . TRP A 1 4387 ? 231.152 151.496 205.437 1.00 24.63 ? 4387 TRP A C     1 
ATOM   21542 O  O     . TRP A 1 4387 ? 230.440 150.900 204.621 1.00 33.54 ? 4387 TRP A O     1 
ATOM   21543 C  CB    . TRP A 1 4387 ? 229.996 153.165 206.911 1.00 18.72 ? 4387 TRP A CB    1 
ATOM   21544 C  CG    . TRP A 1 4387 ? 229.048 153.335 208.059 1.00 19.30 ? 4387 TRP A CG    1 
ATOM   21545 C  CD1   . TRP A 1 4387 ? 228.517 152.348 208.834 1.00 18.77 ? 4387 TRP A CD1   1 
ATOM   21546 C  CD2   . TRP A 1 4387 ? 228.507 154.566 208.550 1.00 18.47 ? 4387 TRP A CD2   1 
ATOM   21547 N  NE1   . TRP A 1 4387 ? 227.683 152.888 209.781 1.00 17.64 ? 4387 TRP A NE1   1 
ATOM   21548 C  CE2   . TRP A 1 4387 ? 227.660 154.248 209.628 1.00 15.98 ? 4387 TRP A CE2   1 
ATOM   21549 C  CE3   . TRP A 1 4387 ? 228.660 155.906 208.183 1.00 16.80 ? 4387 TRP A CE3   1 
ATOM   21550 C  CZ2   . TRP A 1 4387 ? 226.968 155.220 210.343 1.00 15.46 ? 4387 TRP A CZ2   1 
ATOM   21551 C  CZ3   . TRP A 1 4387 ? 227.972 156.868 208.895 1.00 18.32 ? 4387 TRP A CZ3   1 
ATOM   21552 C  CH2   . TRP A 1 4387 ? 227.139 156.522 209.963 1.00 21.01 ? 4387 TRP A CH2   1 
ATOM   21553 N  N     . LEU A 1 4388 ? 232.379 151.922 205.132 1.00 24.01 ? 4388 LEU A N     1 
ATOM   21554 C  CA    . LEU A 1 4388 ? 232.949 151.630 203.820 1.00 25.48 ? 4388 LEU A CA    1 
ATOM   21555 C  C     . LEU A 1 4388 ? 233.176 150.139 203.626 1.00 28.37 ? 4388 LEU A C     1 
ATOM   21556 O  O     . LEU A 1 4388 ? 233.212 149.661 202.486 1.00 28.62 ? 4388 LEU A O     1 
ATOM   21557 C  CB    . LEU A 1 4388 ? 234.256 152.397 203.627 1.00 23.10 ? 4388 LEU A CB    1 
ATOM   21558 C  CG    . LEU A 1 4388 ? 234.110 153.870 203.244 1.00 24.06 ? 4388 LEU A CG    1 
ATOM   21559 C  CD1   . LEU A 1 4388 ? 235.462 154.467 202.892 1.00 23.32 ? 4388 LEU A CD1   1 
ATOM   21560 C  CD2   . LEU A 1 4388 ? 233.135 154.023 202.089 1.00 27.84 ? 4388 LEU A CD2   1 
ATOM   21561 N  N     . HIS A 1 4389 ? 233.344 149.392 204.718 1.00 27.38 ? 4389 HIS A N     1 
ATOM   21562 C  CA    . HIS A 1 4389 ? 233.450 147.942 204.607 1.00 30.39 ? 4389 HIS A CA    1 
ATOM   21563 C  C     . HIS A 1 4389 ? 232.100 147.312 204.286 1.00 27.36 ? 4389 HIS A C     1 
ATOM   21564 O  O     . HIS A 1 4389 ? 232.012 146.429 203.426 1.00 28.17 ? 4389 HIS A O     1 
ATOM   21565 C  CB    . HIS A 1 4389 ? 234.024 147.360 205.899 1.00 27.90 ? 4389 HIS A CB    1 
ATOM   21566 C  CG    . HIS A 1 4389 ? 235.309 147.995 206.327 1.00 34.33 ? 4389 HIS A CG    1 
ATOM   21567 N  ND1   . HIS A 1 4389 ? 235.650 148.163 207.653 1.00 35.38 ? 4389 HIS A ND1   1 
ATOM   21568 C  CD2   . HIS A 1 4389 ? 236.339 148.497 205.607 1.00 33.90 ? 4389 HIS A CD2   1 
ATOM   21569 C  CE1   . HIS A 1 4389 ? 236.833 148.746 207.729 1.00 35.60 ? 4389 HIS A CE1   1 
ATOM   21570 N  NE2   . HIS A 1 4389 ? 237.274 148.959 206.502 1.00 39.97 ? 4389 HIS A NE2   1 
ATOM   21571 N  N     . LEU A 1 4390 ? 231.040 147.749 204.968 1.00 27.73 ? 4390 LEU A N     1 
ATOM   21572 C  CA    . LEU A 1 4390 ? 229.725 147.148 204.764 1.00 30.19 ? 4390 LEU A CA    1 
ATOM   21573 C  C     . LEU A 1 4390 ? 229.151 147.517 203.402 1.00 27.77 ? 4390 LEU A C     1 
ATOM   21574 O  O     . LEU A 1 4390 ? 228.657 146.651 202.670 1.00 31.74 ? 4390 LEU A O     1 
ATOM   21575 C  CB    . LEU A 1 4390 ? 228.771 147.579 205.879 1.00 24.19 ? 4390 LEU A CB    1 
ATOM   21576 C  CG    . LEU A 1 4390 ? 229.303 147.530 207.310 1.00 26.69 ? 4390 LEU A CG    1 
ATOM   21577 C  CD1   . LEU A 1 4390 ? 228.257 148.058 208.280 1.00 26.57 ? 4390 LEU A CD1   1 
ATOM   21578 C  CD2   . LEU A 1 4390 ? 229.721 146.115 207.685 1.00 24.74 ? 4390 LEU A CD2   1 
ATOM   21579 N  N     . ILE A 1 4391 ? 229.205 148.795 203.046 1.00 26.24 ? 4391 ILE A N     1 
ATOM   21580 C  CA    . ILE A 1 4391 ? 228.602 149.251 201.790 1.00 22.86 ? 4391 ILE A CA    1 
ATOM   21581 C  C     . ILE A 1 4391 ? 229.376 148.659 200.615 1.00 23.01 ? 4391 ILE A C     1 
ATOM   21582 O  O     . ILE A 1 4391 ? 230.618 148.697 200.614 1.00 25.69 ? 4391 ILE A O     1 
ATOM   21583 C  CB    . ILE A 1 4391 ? 228.587 150.781 201.731 1.00 21.76 ? 4391 ILE A CB    1 
ATOM   21584 C  CG1   . ILE A 1 4391 ? 227.711 151.347 202.850 1.00 21.22 ? 4391 ILE A CG1   1 
ATOM   21585 C  CG2   . ILE A 1 4391 ? 228.088 151.263 200.382 1.00 23.59 ? 4391 ILE A CG2   1 
ATOM   21586 C  CD1   . ILE A 1 4391 ? 227.837 152.843 203.035 1.00 25.23 ? 4391 ILE A CD1   1 
ATOM   21587 N  N     . PRO A 1 4392 ? 228.702 148.096 199.616 1.00 28.64 ? 4392 PRO A N     1 
ATOM   21588 C  CA    . PRO A 1 4392 ? 229.410 147.558 198.449 1.00 24.29 ? 4392 PRO A CA    1 
ATOM   21589 C  C     . PRO A 1 4392 ? 230.072 148.666 197.642 1.00 22.58 ? 4392 PRO A C     1 
ATOM   21590 O  O     . PRO A 1 4392 ? 229.817 149.858 197.827 1.00 30.43 ? 4392 PRO A O     1 
ATOM   21591 C  CB    . PRO A 1 4392 ? 228.303 146.864 197.651 1.00 26.82 ? 4392 PRO A CB    1 
ATOM   21592 C  CG    . PRO A 1 4392 ? 227.204 146.630 198.644 1.00 24.85 ? 4392 PRO A CG    1 
ATOM   21593 C  CD    . PRO A 1 4392 ? 227.261 147.804 199.563 1.00 27.76 ? 4392 PRO A CD    1 
ATOM   21594 N  N     . GLN A 1 4393 ? 230.938 148.247 196.719 1.00 24.24 ? 4393 GLN A N     1 
ATOM   21595 C  CA    . GLN A 1 4393 ? 231.794 149.174 195.994 1.00 23.31 ? 4393 GLN A CA    1 
ATOM   21596 C  C     . GLN A 1 4393 ? 231.545 149.230 194.494 1.00 27.76 ? 4393 GLN A C     1 
ATOM   21597 O  O     . GLN A 1 4393 ? 232.007 150.181 193.853 1.00 30.61 ? 4393 GLN A O     1 
ATOM   21598 C  CB    . GLN A 1 4393 ? 233.271 148.822 196.233 1.00 18.57 ? 4393 GLN A CB    1 
ATOM   21599 C  CG    . GLN A 1 4393 ? 233.556 148.265 197.617 1.00 24.48 ? 4393 GLN A CG    1 
ATOM   21600 C  CD    . GLN A 1 4393 ? 235.038 148.159 197.911 1.00 30.88 ? 4393 GLN A CD    1 
ATOM   21601 O  OE1   . GLN A 1 4393 ? 235.875 148.539 197.091 1.00 34.79 ? 4393 GLN A OE1   1 
ATOM   21602 N  NE2   . GLN A 1 4393 ? 235.373 147.639 199.084 1.00 26.22 ? 4393 GLN A NE2   1 
ATOM   21603 N  N     . THR A 1 4394 ? 230.833 148.265 193.914 1.00 24.20 ? 4394 THR A N     1 
ATOM   21604 C  CA    . THR A 1 4394 ? 230.678 148.179 192.468 1.00 25.92 ? 4394 THR A CA    1 
ATOM   21605 C  C     . THR A 1 4394 ? 229.205 148.141 192.090 1.00 24.61 ? 4394 THR A C     1 
ATOM   21606 O  O     . THR A 1 4394 ? 228.392 147.516 192.775 1.00 28.03 ? 4394 THR A O     1 
ATOM   21607 C  CB    . THR A 1 4394 ? 231.381 146.936 191.903 1.00 32.09 ? 4394 THR A CB    1 
ATOM   21608 O  OG1   . THR A 1 4394 ? 230.762 145.753 192.427 1.00 31.42 ? 4394 THR A OG1   1 
ATOM   21609 C  CG2   . THR A 1 4394 ? 232.856 146.938 192.279 1.00 25.83 ? 4394 THR A CG2   1 
ATOM   21610 N  N     . LEU A 1 4395 ? 228.867 148.815 190.987 1.00 21.76 ? 4395 LEU A N     1 
ATOM   21611 C  CA    . LEU A 1 4395 ? 227.513 148.760 190.437 1.00 24.22 ? 4395 LEU A CA    1 
ATOM   21612 C  C     . LEU A 1 4395 ? 227.618 149.102 188.950 1.00 29.48 ? 4395 LEU A C     1 
ATOM   21613 O  O     . LEU A 1 4395 ? 227.807 150.269 188.594 1.00 31.84 ? 4395 LEU A O     1 
ATOM   21614 C  CB    . LEU A 1 4395 ? 226.576 149.710 191.163 1.00 24.33 ? 4395 LEU A CB    1 
ATOM   21615 C  CG    . LEU A 1 4395 ? 225.086 149.381 191.045 1.00 23.03 ? 4395 LEU A CG    1 
ATOM   21616 C  CD1   . LEU A 1 4395 ? 224.852 147.892 191.257 1.00 25.94 ? 4395 LEU A CD1   1 
ATOM   21617 C  CD2   . LEU A 1 4395 ? 224.267 150.200 192.023 1.00 18.19 ? 4395 LEU A CD2   1 
ATOM   21618 N  N     . SER A 1 4396 ? 227.495 148.085 188.099 1.00 24.92 ? 4396 SER A N     1 
ATOM   21619 C  CA    . SER A 1 4396 ? 227.645 148.259 186.661 1.00 20.41 ? 4396 SER A CA    1 
ATOM   21620 C  C     . SER A 1 4396 ? 226.296 148.569 186.025 1.00 33.77 ? 4396 SER A C     1 
ATOM   21621 O  O     . SER A 1 4396 ? 225.309 147.867 186.268 1.00 34.85 ? 4396 SER A O     1 
ATOM   21622 C  CB    . SER A 1 4396 ? 228.253 147.006 186.030 1.00 23.65 ? 4396 SER A CB    1 
ATOM   21623 O  OG    . SER A 1 4396 ? 227.461 145.862 186.300 1.00 37.27 ? 4396 SER A OG    1 
ATOM   21624 N  N     . HIS A 1 4397 ? 226.261 149.620 185.208 1.00 26.56 ? 4397 HIS A N     1 
ATOM   21625 C  CA    . HIS A 1 4397 ? 225.036 150.000 184.523 1.00 21.31 ? 4397 HIS A CA    1 
ATOM   21626 C  C     . HIS A 1 4397 ? 224.608 148.917 183.540 1.00 33.21 ? 4397 HIS A C     1 
ATOM   21627 O  O     . HIS A 1 4397 ? 225.433 148.189 182.982 1.00 36.11 ? 4397 HIS A O     1 
ATOM   21628 C  CB    . HIS A 1 4397 ? 225.224 151.322 183.779 1.00 22.76 ? 4397 HIS A CB    1 
ATOM   21629 C  CG    . HIS A 1 4397 ? 225.234 152.526 184.668 1.00 29.92 ? 4397 HIS A CG    1 
ATOM   21630 N  ND1   . HIS A 1 4397 ? 224.661 153.724 184.302 1.00 34.59 ? 4397 HIS A ND1   1 
ATOM   21631 C  CD2   . HIS A 1 4397 ? 225.749 152.717 185.907 1.00 30.11 ? 4397 HIS A CD2   1 
ATOM   21632 C  CE1   . HIS A 1 4397 ? 224.821 154.602 185.276 1.00 29.47 ? 4397 HIS A CE1   1 
ATOM   21633 N  NE2   . HIS A 1 4397 ? 225.478 154.016 186.261 1.00 30.44 ? 4397 HIS A NE2   1 
ATOM   21634 N  N     . LEU A 1 4398 ? 223.297 148.809 183.341 1.00 29.60 ? 4398 LEU A N     1 
ATOM   21635 C  CA    . LEU A 1 4398 ? 222.767 147.873 182.362 1.00 24.69 ? 4398 LEU A CA    1 
ATOM   21636 C  C     . LEU A 1 4398 ? 223.129 148.324 180.952 1.00 25.43 ? 4398 LEU A C     1 
ATOM   21637 O  O     . LEU A 1 4398 ? 223.024 149.507 180.615 1.00 28.66 ? 4398 LEU A O     1 
ATOM   21638 C  CB    . LEU A 1 4398 ? 221.249 147.754 182.501 1.00 27.49 ? 4398 LEU A CB    1 
ATOM   21639 C  CG    . LEU A 1 4398 ? 220.669 147.337 183.856 1.00 28.48 ? 4398 LEU A CG    1 
ATOM   21640 C  CD1   . LEU A 1 4398 ? 219.186 147.027 183.723 1.00 22.45 ? 4398 LEU A CD1   1 
ATOM   21641 C  CD2   . LEU A 1 4398 ? 221.420 146.147 184.429 1.00 21.21 ? 4398 LEU A CD2   1 
ATOM   21642 N  N     . LYS A 1 4399 ? 223.553 147.374 180.125 1.00 30.00 ? 4399 LYS A N     1 
ATOM   21643 C  CA    . LYS A 1 4399 ? 223.952 147.679 178.756 1.00 26.14 ? 4399 LYS A CA    1 
ATOM   21644 C  C     . LYS A 1 4399 ? 222.712 147.839 177.887 1.00 25.76 ? 4399 LYS A C     1 
ATOM   21645 O  O     . LYS A 1 4399 ? 221.967 146.878 177.675 1.00 25.02 ? 4399 LYS A O     1 
ATOM   21646 C  CB    . LYS A 1 4399 ? 224.860 146.582 178.207 1.00 24.26 ? 4399 LYS A CB    1 
ATOM   21647 C  CG    . LYS A 1 4399 ? 225.330 146.827 176.782 1.00 22.39 ? 4399 LYS A CG    1 
ATOM   21648 C  CD    . LYS A 1 4399 ? 225.711 145.526 176.098 1.00 26.49 ? 4399 LYS A CD    1 
ATOM   21649 C  CE    . LYS A 1 4399 ? 224.515 144.602 175.954 1.00 25.59 ? 4399 LYS A CE    1 
ATOM   21650 N  NZ    . LYS A 1 4399 ? 224.876 143.331 175.270 1.00 29.58 ? 4399 LYS A NZ    1 
ATOM   21651 N  N     . ARG A 1 4400 ? 222.492 149.053 177.384 1.00 26.52 ? 4400 ARG A N     1 
ATOM   21652 C  CA    . ARG A 1 4400 ? 221.332 149.316 176.545 1.00 23.67 ? 4400 ARG A CA    1 
ATOM   21653 C  C     . ARG A 1 4400 ? 221.497 148.646 175.187 1.00 26.54 ? 4400 ARG A C     1 
ATOM   21654 O  O     . ARG A 1 4400 ? 222.564 148.712 174.569 1.00 33.06 ? 4400 ARG A O     1 
ATOM   21655 C  CB    . ARG A 1 4400 ? 221.125 150.820 176.383 1.00 18.35 ? 4400 ARG A CB    1 
ATOM   21656 C  CG    . ARG A 1 4400 ? 220.970 151.554 177.702 1.00 20.72 ? 4400 ARG A CG    1 
ATOM   21657 C  CD    . ARG A 1 4400 ? 220.503 152.986 177.506 1.00 24.13 ? 4400 ARG A CD    1 
ATOM   21658 N  NE    . ARG A 1 4400 ? 219.180 153.049 176.901 1.00 26.44 ? 4400 ARG A NE    1 
ATOM   21659 C  CZ    . ARG A 1 4400 ? 218.460 154.157 176.786 1.00 20.20 ? 4400 ARG A CZ    1 
ATOM   21660 N  NH1   . ARG A 1 4400 ? 218.883 155.311 177.272 1.00 17.35 ? 4400 ARG A NH1   1 
ATOM   21661 N  NH2   . ARG A 1 4400 ? 217.281 154.104 176.175 1.00 22.58 ? 4400 ARG A NH2   1 
ATOM   21662 N  N     . THR A 1 4401 ? 220.431 147.997 174.726 1.00 29.37 ? 4401 THR A N     1 
ATOM   21663 C  CA    . THR A 1 4401 ? 220.438 147.246 173.480 1.00 29.66 ? 4401 THR A CA    1 
ATOM   21664 C  C     . THR A 1 4401 ? 219.150 147.570 172.737 1.00 33.39 ? 4401 THR A C     1 
ATOM   21665 O  O     . THR A 1 4401 ? 218.163 148.002 173.336 1.00 30.56 ? 4401 THR A O     1 
ATOM   21666 C  CB    . THR A 1 4401 ? 220.576 145.735 173.752 1.00 27.68 ? 4401 THR A CB    1 
ATOM   21667 O  OG1   . THR A 1 4401 ? 221.786 145.493 174.478 1.00 26.41 ? 4401 THR A OG1   1 
ATOM   21668 C  CG2   . THR A 1 4401 ? 220.636 144.932 172.461 1.00 26.51 ? 4401 THR A CG2   1 
ATOM   21669 N  N     . VAL A 1 4402 ? 219.171 147.379 171.413 1.00 34.21 ? 4402 VAL A N     1 
ATOM   21670 C  CA    . VAL A 1 4402 ? 218.010 147.715 170.592 1.00 30.32 ? 4402 VAL A CA    1 
ATOM   21671 C  C     . VAL A 1 4402 ? 216.780 146.938 171.048 1.00 27.92 ? 4402 VAL A C     1 
ATOM   21672 O  O     . VAL A 1 4402 ? 215.667 147.476 171.080 1.00 32.17 ? 4402 VAL A O     1 
ATOM   21673 C  CB    . VAL A 1 4402 ? 218.317 147.474 169.102 1.00 31.50 ? 4402 VAL A CB    1 
ATOM   21674 C  CG1   . VAL A 1 4402 ? 219.250 148.551 168.575 1.00 27.49 ? 4402 VAL A CG1   1 
ATOM   21675 C  CG2   . VAL A 1 4402 ? 218.928 146.094 168.895 1.00 29.85 ? 4402 VAL A CG2   1 
ATOM   21676 N  N     . GLU A 1 4403 ? 216.955 145.666 171.410 1.00 28.09 ? 4403 GLU A N     1 
ATOM   21677 C  CA    . GLU A 1 4403 ? 215.833 144.861 171.878 1.00 26.08 ? 4403 GLU A CA    1 
ATOM   21678 C  C     . GLU A 1 4403 ? 215.679 144.871 173.394 1.00 30.26 ? 4403 GLU A C     1 
ATOM   21679 O  O     . GLU A 1 4403 ? 214.667 144.371 173.900 1.00 29.64 ? 4403 GLU A O     1 
ATOM   21680 C  CB    . GLU A 1 4403 ? 215.963 143.420 171.365 1.00 25.39 ? 4403 GLU A CB    1 
ATOM   21681 C  CG    . GLU A 1 4403 ? 217.202 142.657 171.817 1.00 30.97 ? 4403 GLU A CG    1 
ATOM   21682 C  CD    . GLU A 1 4403 ? 217.018 141.958 173.149 1.00 36.19 ? 4403 GLU A CD    1 
ATOM   21683 O  OE1   . GLU A 1 4403 ? 215.857 141.748 173.559 1.00 39.88 ? 4403 GLU A OE1   1 
ATOM   21684 O  OE2   . GLU A 1 4403 ? 218.035 141.594 173.777 1.00 37.74 ? 4403 GLU A OE2   1 
ATOM   21685 N  N     . ASN A 1 4404 ? 216.645 145.428 174.127 1.00 26.20 ? 4404 ASN A N     1 
ATOM   21686 C  CA    . ASN A 1 4404 ? 216.474 145.620 175.564 1.00 25.37 ? 4404 ASN A CA    1 
ATOM   21687 C  C     . ASN A 1 4404 ? 215.586 146.817 175.876 1.00 28.19 ? 4404 ASN A C     1 
ATOM   21688 O  O     . ASN A 1 4404 ? 214.890 146.815 176.898 1.00 29.38 ? 4404 ASN A O     1 
ATOM   21689 C  CB    . ASN A 1 4404 ? 217.834 145.783 176.246 1.00 23.68 ? 4404 ASN A CB    1 
ATOM   21690 C  CG    . ASN A 1 4404 ? 218.598 144.477 176.345 1.00 28.48 ? 4404 ASN A CG    1 
ATOM   21691 O  OD1   . ASN A 1 4404 ? 218.645 143.699 175.394 1.00 35.06 ? 4404 ASN A OD1   1 
ATOM   21692 N  ND2   . ASN A 1 4404 ? 219.218 144.239 177.493 1.00 26.97 ? 4404 ASN A ND2   1 
ATOM   21693 N  N     . ILE A 1 4405 ? 215.601 147.843 175.023 1.00 25.72 ? 4405 ILE A N     1 
ATOM   21694 C  CA    . ILE A 1 4405 ? 214.768 149.019 175.255 1.00 24.20 ? 4405 ILE A CA    1 
ATOM   21695 C  C     . ILE A 1 4405 ? 213.292 148.653 175.168 1.00 25.44 ? 4405 ILE A C     1 
ATOM   21696 O  O     . ILE A 1 4405 ? 212.463 149.201 175.906 1.00 27.94 ? 4405 ILE A O     1 
ATOM   21697 C  CB    . ILE A 1 4405 ? 215.138 150.139 174.262 1.00 23.10 ? 4405 ILE A CB    1 
ATOM   21698 C  CG1   . ILE A 1 4405 ? 216.614 150.510 174.392 1.00 25.38 ? 4405 ILE A CG1   1 
ATOM   21699 C  CG2   . ILE A 1 4405 ? 214.301 151.370 174.509 1.00 27.63 ? 4405 ILE A CG2   1 
ATOM   21700 C  CD1   . ILE A 1 4405 ? 217.073 150.721 175.819 1.00 24.95 ? 4405 ILE A CD1   1 
ATOM   21701 N  N     . LYS A 1 4406 ? 212.942 147.719 174.284 1.00 26.27 ? 4406 LYS A N     1 
ATOM   21702 C  CA    . LYS A 1 4406 ? 211.566 147.263 174.148 1.00 22.49 ? 4406 LYS A CA    1 
ATOM   21703 C  C     . LYS A 1 4406 ? 211.090 146.422 175.327 1.00 24.15 ? 4406 LYS A C     1 
ATOM   21704 O  O     . LYS A 1 4406 ? 209.890 146.145 175.423 1.00 26.56 ? 4406 LYS A O     1 
ATOM   21705 C  CB    . LYS A 1 4406 ? 211.405 146.462 172.853 1.00 23.37 ? 4406 LYS A CB    1 
ATOM   21706 C  CG    . LYS A 1 4406 ? 211.858 147.204 171.606 1.00 33.05 ? 4406 LYS A CG    1 
ATOM   21707 C  CD    . LYS A 1 4406 ? 211.642 146.370 170.353 1.00 30.20 ? 4406 LYS A CD    1 
ATOM   21708 C  CE    . LYS A 1 4406 ? 212.357 145.032 170.447 1.00 31.27 ? 4406 LYS A CE    1 
ATOM   21709 N  NZ    . LYS A 1 4406 ? 212.203 144.231 169.203 1.00 27.23 ? 4406 LYS A NZ    1 
ATOM   21710 N  N     . ASP A 1 4407 ? 211.989 146.008 176.216 1.00 27.46 ? 4407 ASP A N     1 
ATOM   21711 C  CA    . ASP A 1 4407 ? 211.612 145.193 177.363 1.00 24.00 ? 4407 ASP A CA    1 
ATOM   21712 C  C     . ASP A 1 4407 ? 211.224 146.096 178.526 1.00 26.42 ? 4407 ASP A C     1 
ATOM   21713 O  O     . ASP A 1 4407 ? 212.072 146.859 179.009 1.00 27.58 ? 4407 ASP A O     1 
ATOM   21714 C  CB    . ASP A 1 4407 ? 212.758 144.278 177.767 1.00 25.61 ? 4407 ASP A CB    1 
ATOM   21715 C  CG    . ASP A 1 4407 ? 212.364 143.281 178.838 1.00 29.36 ? 4407 ASP A CG    1 
ATOM   21716 O  OD1   . ASP A 1 4407 ? 211.177 143.246 179.228 1.00 29.69 ? 4407 ASP A OD1   1 
ATOM   21717 O  OD2   . ASP A 1 4407 ? 213.245 142.519 179.288 1.00 36.18 ? 4407 ASP A OD2   1 
ATOM   21718 N  N     . PRO A 1 4408 ? 209.975 146.053 178.997 1.00 24.97 ? 4408 PRO A N     1 
ATOM   21719 C  CA    . PRO A 1 4408 ? 209.586 146.916 180.128 1.00 22.32 ? 4408 PRO A CA    1 
ATOM   21720 C  C     . PRO A 1 4408 ? 210.374 146.655 181.399 1.00 18.49 ? 4408 PRO A C     1 
ATOM   21721 O  O     . PRO A 1 4408 ? 210.648 147.596 182.155 1.00 20.64 ? 4408 PRO A O     1 
ATOM   21722 C  CB    . PRO A 1 4408 ? 208.096 146.595 180.311 1.00 22.83 ? 4408 PRO A CB    1 
ATOM   21723 C  CG    . PRO A 1 4408 ? 207.897 145.279 179.634 1.00 20.11 ? 4408 PRO A CG    1 
ATOM   21724 C  CD    . PRO A 1 4408 ? 208.835 145.281 178.479 1.00 19.62 ? 4408 PRO A CD    1 
ATOM   21725 N  N     . LEU A 1 4409 ? 210.734 145.398 181.666 1.00 21.67 ? 4409 LEU A N     1 
ATOM   21726 C  CA    . LEU A 1 4409 ? 211.504 145.089 182.866 1.00 20.99 ? 4409 LEU A CA    1 
ATOM   21727 C  C     . LEU A 1 4409 ? 212.874 145.753 182.821 1.00 25.71 ? 4409 LEU A C     1 
ATOM   21728 O  O     . LEU A 1 4409 ? 213.351 146.280 183.832 1.00 25.51 ? 4409 LEU A O     1 
ATOM   21729 C  CB    . LEU A 1 4409 ? 211.643 143.576 183.028 1.00 16.92 ? 4409 LEU A CB    1 
ATOM   21730 C  CG    . LEU A 1 4409 ? 210.638 142.903 183.964 1.00 21.62 ? 4409 LEU A CG    1 
ATOM   21731 C  CD1   . LEU A 1 4409 ? 210.893 141.409 184.032 1.00 19.31 ? 4409 LEU A CD1   1 
ATOM   21732 C  CD2   . LEU A 1 4409 ? 210.693 143.520 185.353 1.00 17.85 ? 4409 LEU A CD2   1 
ATOM   21733 N  N     . PHE A 1 4410 ? 213.516 145.738 181.651 1.00 23.76 ? 4410 PHE A N     1 
ATOM   21734 C  CA    . PHE A 1 4410 ? 214.803 146.406 181.501 1.00 21.16 ? 4410 PHE A CA    1 
ATOM   21735 C  C     . PHE A 1 4410 ? 214.667 147.908 181.720 1.00 22.82 ? 4410 PHE A C     1 
ATOM   21736 O  O     . PHE A 1 4410 ? 215.532 148.532 182.343 1.00 21.10 ? 4410 PHE A O     1 
ATOM   21737 C  CB    . PHE A 1 4410 ? 215.379 146.105 180.116 1.00 23.86 ? 4410 PHE A CB    1 
ATOM   21738 C  CG    . PHE A 1 4410 ? 216.810 146.529 179.942 1.00 27.60 ? 4410 PHE A CG    1 
ATOM   21739 C  CD1   . PHE A 1 4410 ? 217.844 145.664 180.257 1.00 22.37 ? 4410 PHE A CD1   1 
ATOM   21740 C  CD2   . PHE A 1 4410 ? 217.121 147.783 179.447 1.00 30.35 ? 4410 PHE A CD2   1 
ATOM   21741 C  CE1   . PHE A 1 4410 ? 219.159 146.046 180.091 1.00 20.28 ? 4410 PHE A CE1   1 
ATOM   21742 C  CE2   . PHE A 1 4410 ? 218.434 148.172 179.279 1.00 28.76 ? 4410 PHE A CE2   1 
ATOM   21743 C  CZ    . PHE A 1 4410 ? 219.455 147.302 179.598 1.00 27.49 ? 4410 PHE A CZ    1 
ATOM   21744 N  N     . ARG A 1 4411 ? 213.579 148.502 181.223 1.00 20.09 ? 4411 ARG A N     1 
ATOM   21745 C  CA    . ARG A 1 4411 ? 213.392 149.944 181.356 1.00 22.46 ? 4411 ARG A CA    1 
ATOM   21746 C  C     . ARG A 1 4411 ? 213.286 150.365 182.818 1.00 25.00 ? 4411 ARG A C     1 
ATOM   21747 O  O     . ARG A 1 4411 ? 213.879 151.369 183.226 1.00 31.58 ? 4411 ARG A O     1 
ATOM   21748 C  CB    . ARG A 1 4411 ? 212.156 150.386 180.577 1.00 20.37 ? 4411 ARG A CB    1 
ATOM   21749 C  CG    . ARG A 1 4411 ? 212.231 150.131 179.085 1.00 13.03 ? 4411 ARG A CG    1 
ATOM   21750 C  CD    . ARG A 1 4411 ? 211.073 150.795 178.363 1.00 22.46 ? 4411 ARG A CD    1 
ATOM   21751 N  NE    . ARG A 1 4411 ? 209.792 150.194 178.714 1.00 23.91 ? 4411 ARG A NE    1 
ATOM   21752 C  CZ    . ARG A 1 4411 ? 208.936 149.688 177.837 1.00 25.41 ? 4411 ARG A CZ    1 
ATOM   21753 N  NH1   . ARG A 1 4411 ? 209.188 149.702 176.539 1.00 20.77 ? 4411 ARG A NH1   1 
ATOM   21754 N  NH2   . ARG A 1 4411 ? 207.799 149.157 178.273 1.00 28.17 ? 4411 ARG A NH2   1 
ATOM   21755 N  N     . PHE A 1 4412 ? 212.533 149.612 183.623 1.00 26.40 ? 4412 PHE A N     1 
ATOM   21756 C  CA    . PHE A 1 4412 ? 212.462 149.914 185.049 1.00 26.93 ? 4412 PHE A CA    1 
ATOM   21757 C  C     . PHE A 1 4412 ? 213.781 149.597 185.744 1.00 24.08 ? 4412 PHE A C     1 
ATOM   21758 O  O     . PHE A 1 4412 ? 214.286 150.399 186.538 1.00 26.99 ? 4412 PHE A O     1 
ATOM   21759 C  CB    . PHE A 1 4412 ? 211.317 149.140 185.704 1.00 22.25 ? 4412 PHE A CB    1 
ATOM   21760 C  CG    . PHE A 1 4412 ? 211.500 148.937 187.179 1.00 19.53 ? 4412 PHE A CG    1 
ATOM   21761 C  CD1   . PHE A 1 4412 ? 211.245 149.965 188.067 1.00 21.28 ? 4412 PHE A CD1   1 
ATOM   21762 C  CD2   . PHE A 1 4412 ? 211.951 147.725 187.675 1.00 16.71 ? 4412 PHE A CD2   1 
ATOM   21763 C  CE1   . PHE A 1 4412 ? 211.422 149.788 189.422 1.00 20.48 ? 4412 PHE A CE1   1 
ATOM   21764 C  CE2   . PHE A 1 4412 ? 212.133 147.543 189.028 1.00 15.03 ? 4412 PHE A CE2   1 
ATOM   21765 C  CZ    . PHE A 1 4412 ? 211.870 148.575 189.902 1.00 18.23 ? 4412 PHE A CZ    1 
ATOM   21766 N  N     . PHE A 1 4413 ? 214.351 148.424 185.462 1.00 19.19 ? 4413 PHE A N     1 
ATOM   21767 C  CA    . PHE A 1 4413 ? 215.581 148.012 186.132 1.00 19.46 ? 4413 PHE A CA    1 
ATOM   21768 C  C     . PHE A 1 4413 ? 216.762 148.896 185.751 1.00 25.44 ? 4413 PHE A C     1 
ATOM   21769 O  O     . PHE A 1 4413 ? 217.680 149.077 186.559 1.00 28.29 ? 4413 PHE A O     1 
ATOM   21770 C  CB    . PHE A 1 4413 ? 215.883 146.549 185.819 1.00 17.70 ? 4413 PHE A CB    1 
ATOM   21771 C  CG    . PHE A 1 4413 ? 215.158 145.578 186.705 1.00 21.62 ? 4413 PHE A CG    1 
ATOM   21772 C  CD1   . PHE A 1 4413 ? 215.049 145.814 188.065 1.00 19.71 ? 4413 PHE A CD1   1 
ATOM   21773 C  CD2   . PHE A 1 4413 ? 214.586 144.432 186.178 1.00 21.25 ? 4413 PHE A CD2   1 
ATOM   21774 C  CE1   . PHE A 1 4413 ? 214.385 144.925 188.882 1.00 19.92 ? 4413 PHE A CE1   1 
ATOM   21775 C  CE2   . PHE A 1 4413 ? 213.924 143.537 186.993 1.00 22.93 ? 4413 PHE A CE2   1 
ATOM   21776 C  CZ    . PHE A 1 4413 ? 213.821 143.785 188.348 1.00 25.67 ? 4413 PHE A CZ    1 
ATOM   21777 N  N     . GLU A 1 4414 ? 216.768 149.442 184.534 1.00 23.80 ? 4414 GLU A N     1 
ATOM   21778 C  CA    . GLU A 1 4414 ? 217.834 150.360 184.148 1.00 25.15 ? 4414 GLU A CA    1 
ATOM   21779 C  C     . GLU A 1 4414 ? 217.794 151.629 184.989 1.00 24.47 ? 4414 GLU A C     1 
ATOM   21780 O  O     . GLU A 1 4414 ? 218.840 152.162 185.378 1.00 26.38 ? 4414 GLU A O     1 
ATOM   21781 C  CB    . GLU A 1 4414 ? 217.726 150.694 182.659 1.00 24.26 ? 4414 GLU A CB    1 
ATOM   21782 C  CG    . GLU A 1 4414 ? 218.722 151.725 182.177 1.00 23.04 ? 4414 GLU A CG    1 
ATOM   21783 C  CD    . GLU A 1 4414 ? 218.202 152.519 180.999 1.00 31.08 ? 4414 GLU A CD    1 
ATOM   21784 O  OE1   . GLU A 1 4414 ? 217.498 153.526 181.225 1.00 35.71 ? 4414 GLU A OE1   1 
ATOM   21785 O  OE2   . GLU A 1 4414 ? 218.490 152.132 179.848 1.00 32.07 ? 4414 GLU A OE2   1 
ATOM   21786 N  N     . ARG A 1 4415 ? 216.591 152.129 185.280 1.00 24.24 ? 4415 ARG A N     1 
ATOM   21787 C  CA    . ARG A 1 4415 ? 216.462 153.296 186.146 1.00 19.30 ? 4415 ARG A CA    1 
ATOM   21788 C  C     . ARG A 1 4415 ? 217.020 153.018 187.533 1.00 26.09 ? 4415 ARG A C     1 
ATOM   21789 O  O     . ARG A 1 4415 ? 217.693 153.871 188.121 1.00 29.78 ? 4415 ARG A O     1 
ATOM   21790 C  CB    . ARG A 1 4415 ? 214.999 153.720 186.245 1.00 20.53 ? 4415 ARG A CB    1 
ATOM   21791 C  CG    . ARG A 1 4415 ? 214.461 154.422 185.022 1.00 24.49 ? 4415 ARG A CG    1 
ATOM   21792 C  CD    . ARG A 1 4415 ? 213.134 155.071 185.341 1.00 18.55 ? 4415 ARG A CD    1 
ATOM   21793 N  NE    . ARG A 1 4415 ? 213.090 155.527 186.724 1.00 18.82 ? 4415 ARG A NE    1 
ATOM   21794 C  CZ    . ARG A 1 4415 ? 212.129 156.284 187.236 1.00 24.40 ? 4415 ARG A CZ    1 
ATOM   21795 N  NH1   . ARG A 1 4415 ? 211.118 156.710 186.498 1.00 16.60 ? 4415 ARG A NH1   1 
ATOM   21796 N  NH2   . ARG A 1 4415 ? 212.188 156.625 188.521 1.00 23.92 ? 4415 ARG A NH2   1 
ATOM   21797 N  N     . GLU A 1 4416 ? 216.748 151.826 188.071 1.00 26.05 ? 4416 GLU A N     1 
ATOM   21798 C  CA    . GLU A 1 4416 ? 217.167 151.502 189.432 1.00 25.82 ? 4416 GLU A CA    1 
ATOM   21799 C  C     . GLU A 1 4416 ? 218.682 151.559 189.574 1.00 25.89 ? 4416 GLU A C     1 
ATOM   21800 O  O     . GLU A 1 4416 ? 219.208 152.151 190.525 1.00 31.04 ? 4416 GLU A O     1 
ATOM   21801 C  CB    . GLU A 1 4416 ? 216.642 150.122 189.825 1.00 23.55 ? 4416 GLU A CB    1 
ATOM   21802 C  CG    . GLU A 1 4416 ? 215.169 150.098 190.186 1.00 23.44 ? 4416 GLU A CG    1 
ATOM   21803 C  CD    . GLU A 1 4416 ? 214.863 150.895 191.435 1.00 25.14 ? 4416 GLU A CD    1 
ATOM   21804 O  OE1   . GLU A 1 4416 ? 215.454 150.595 192.494 1.00 28.51 ? 4416 GLU A OE1   1 
ATOM   21805 O  OE2   . GLU A 1 4416 ? 214.026 151.821 191.362 1.00 24.97 ? 4416 GLU A OE2   1 
ATOM   21806 N  N     . VAL A 1 4417 ? 219.406 150.946 188.635 1.00 23.02 ? 4417 VAL A N     1 
ATOM   21807 C  CA    . VAL A 1 4417 ? 220.864 150.960 188.709 1.00 24.78 ? 4417 VAL A CA    1 
ATOM   21808 C  C     . VAL A 1 4417 ? 221.405 152.355 188.424 1.00 24.26 ? 4417 VAL A C     1 
ATOM   21809 O  O     . VAL A 1 4417 ? 222.350 152.810 189.076 1.00 25.34 ? 4417 VAL A O     1 
ATOM   21810 C  CB    . VAL A 1 4417 ? 221.459 149.908 187.757 1.00 23.95 ? 4417 VAL A CB    1 
ATOM   21811 C  CG1   . VAL A 1 4417 ? 222.973 149.995 187.750 1.00 22.52 ? 4417 VAL A CG1   1 
ATOM   21812 C  CG2   . VAL A 1 4417 ? 221.032 148.522 188.193 1.00 22.08 ? 4417 VAL A CG2   1 
ATOM   21813 N  N     . LYS A 1 4418 ? 220.817 153.058 187.452 1.00 26.88 ? 4418 LYS A N     1 
ATOM   21814 C  CA    . LYS A 1 4418 ? 221.319 154.380 187.089 1.00 25.72 ? 4418 LYS A CA    1 
ATOM   21815 C  C     . LYS A 1 4418 ? 221.235 155.344 188.267 1.00 26.98 ? 4418 LYS A C     1 
ATOM   21816 O  O     . LYS A 1 4418 ? 222.205 156.046 188.577 1.00 31.00 ? 4418 LYS A O     1 
ATOM   21817 C  CB    . LYS A 1 4418 ? 220.551 154.928 185.888 1.00 24.19 ? 4418 LYS A CB    1 
ATOM   21818 C  CG    . LYS A 1 4418 ? 221.397 155.808 184.979 1.00 26.43 ? 4418 LYS A CG    1 
ATOM   21819 C  CD    . LYS A 1 4418 ? 220.653 156.202 183.715 1.00 23.29 ? 4418 LYS A CD    1 
ATOM   21820 C  CE    . LYS A 1 4418 ? 220.108 154.989 182.984 1.00 23.74 ? 4418 LYS A CE    1 
ATOM   21821 N  NZ    . LYS A 1 4418 ? 219.304 155.381 181.793 1.00 21.88 ? 4418 LYS A NZ    1 
ATOM   21822 N  N     . MET A 1 4419 ? 220.088 155.384 188.946 1.00 30.32 ? 4419 MET A N     1 
ATOM   21823 C  CA    . MET A 1 4419 ? 219.994 156.214 190.142 1.00 31.08 ? 4419 MET A CA    1 
ATOM   21824 C  C     . MET A 1 4419 ? 220.719 155.566 191.314 1.00 23.68 ? 4419 MET A C     1 
ATOM   21825 O  O     . MET A 1 4419 ? 221.215 156.262 192.207 1.00 28.13 ? 4419 MET A O     1 
ATOM   21826 C  CB    . MET A 1 4419 ? 218.530 156.487 190.497 1.00 24.97 ? 4419 MET A CB    1 
ATOM   21827 C  CG    . MET A 1 4419 ? 217.730 155.265 190.898 1.00 27.96 ? 4419 MET A CG    1 
ATOM   21828 S  SD    . MET A 1 4419 ? 216.028 155.687 191.315 1.00 57.74 ? 4419 MET A SD    1 
ATOM   21829 C  CE    . MET A 1 4419 ? 216.268 156.519 192.883 1.00 20.82 ? 4419 MET A CE    1 
ATOM   21830 N  N     . GLY A 1 4420 ? 220.794 154.234 191.324 1.00 20.57 ? 4420 GLY A N     1 
ATOM   21831 C  CA    . GLY A 1 4420 ? 221.497 153.543 192.389 1.00 19.46 ? 4420 GLY A CA    1 
ATOM   21832 C  C     . GLY A 1 4420 ? 223.002 153.674 192.307 1.00 22.83 ? 4420 GLY A C     1 
ATOM   21833 O  O     . GLY A 1 4420 ? 223.674 153.789 193.335 1.00 26.25 ? 4420 GLY A O     1 
ATOM   21834 N  N     . ALA A 1 4421 ? 223.557 153.642 191.092 1.00 23.12 ? 4421 ALA A N     1 
ATOM   21835 C  CA    . ALA A 1 4421 ? 225.001 153.781 190.940 1.00 18.22 ? 4421 ALA A CA    1 
ATOM   21836 C  C     . ALA A 1 4421 ? 225.468 155.171 191.344 1.00 19.89 ? 4421 ALA A C     1 
ATOM   21837 O  O     . ALA A 1 4421 ? 226.516 155.318 191.983 1.00 20.90 ? 4421 ALA A O     1 
ATOM   21838 C  CB    . ALA A 1 4421 ? 225.410 153.472 189.501 1.00 21.42 ? 4421 ALA A CB    1 
ATOM   21839 N  N     . LYS A 1 4422 ? 224.706 156.206 190.977 1.00 20.47 ? 4422 LYS A N     1 
ATOM   21840 C  CA    . LYS A 1 4422 ? 225.077 157.569 191.339 1.00 17.21 ? 4422 LYS A CA    1 
ATOM   21841 C  C     . LYS A 1 4422 ? 225.076 157.757 192.851 1.00 23.10 ? 4422 LYS A C     1 
ATOM   21842 O  O     . LYS A 1 4422 ? 225.995 158.367 193.408 1.00 27.55 ? 4422 LYS A O     1 
ATOM   21843 C  CB    . LYS A 1 4422 ? 224.128 158.563 190.673 1.00 22.92 ? 4422 LYS A CB    1 
ATOM   21844 C  CG    . LYS A 1 4422 ? 224.297 159.998 191.142 1.00 22.02 ? 4422 LYS A CG    1 
ATOM   21845 C  CD    . LYS A 1 4422 ? 223.175 160.883 190.628 1.00 16.85 ? 4422 LYS A CD    1 
ATOM   21846 C  CE    . LYS A 1 4422 ? 223.298 162.300 191.162 1.00 25.56 ? 4422 LYS A CE    1 
ATOM   21847 N  NZ    . LYS A 1 4422 ? 222.188 163.172 190.688 1.00 25.40 ? 4422 LYS A NZ    1 
ATOM   21848 N  N     . LEU A 1 4423 ? 224.053 157.236 193.532 1.00 23.79 ? 4423 LEU A N     1 
ATOM   21849 C  CA    . LEU A 1 4423 ? 224.001 157.339 194.985 1.00 21.09 ? 4423 LEU A CA    1 
ATOM   21850 C  C     . LEU A 1 4423 ? 225.130 156.552 195.639 1.00 15.24 ? 4423 LEU A C     1 
ATOM   21851 O  O     . LEU A 1 4423 ? 225.692 156.986 196.651 1.00 18.04 ? 4423 LEU A O     1 
ATOM   21852 C  CB    . LEU A 1 4423 ? 222.640 156.863 195.494 1.00 21.69 ? 4423 LEU A CB    1 
ATOM   21853 C  CG    . LEU A 1 4423 ? 222.386 156.895 197.002 1.00 23.48 ? 4423 LEU A CG    1 
ATOM   21854 C  CD1   . LEU A 1 4423 ? 222.782 158.235 197.599 1.00 19.28 ? 4423 LEU A CD1   1 
ATOM   21855 C  CD2   . LEU A 1 4423 ? 220.927 156.587 197.291 1.00 21.38 ? 4423 LEU A CD2   1 
ATOM   21856 N  N     . LEU A 1 4424 ? 225.474 155.393 195.076 1.00 18.33 ? 4424 LEU A N     1 
ATOM   21857 C  CA    . LEU A 1 4424 ? 226.539 154.573 195.645 1.00 17.31 ? 4424 LEU A CA    1 
ATOM   21858 C  C     . LEU A 1 4424 ? 227.880 155.295 195.600 1.00 20.62 ? 4424 LEU A C     1 
ATOM   21859 O  O     . LEU A 1 4424 ? 228.635 155.286 196.578 1.00 22.84 ? 4424 LEU A O     1 
ATOM   21860 C  CB    . LEU A 1 4424 ? 226.617 153.238 194.906 1.00 16.98 ? 4424 LEU A CB    1 
ATOM   21861 C  CG    . LEU A 1 4424 ? 227.645 152.230 195.421 1.00 23.86 ? 4424 LEU A CG    1 
ATOM   21862 C  CD1   . LEU A 1 4424 ? 227.328 151.817 196.842 1.00 18.97 ? 4424 LEU A CD1   1 
ATOM   21863 C  CD2   . LEU A 1 4424 ? 227.695 151.020 194.508 1.00 21.24 ? 4424 LEU A CD2   1 
ATOM   21864 N  N     . GLN A 1 4425 ? 228.194 155.927 194.467 1.00 22.77 ? 4425 GLN A N     1 
ATOM   21865 C  CA    . GLN A 1 4425 ? 229.462 156.643 194.350 1.00 22.91 ? 4425 GLN A CA    1 
ATOM   21866 C  C     . GLN A 1 4425 ? 229.505 157.857 195.270 1.00 21.20 ? 4425 GLN A C     1 
ATOM   21867 O  O     . GLN A 1 4425 ? 230.547 158.150 195.869 1.00 15.50 ? 4425 GLN A O     1 
ATOM   21868 C  CB    . GLN A 1 4425 ? 229.697 157.056 192.897 1.00 18.35 ? 4425 GLN A CB    1 
ATOM   21869 C  CG    . GLN A 1 4425 ? 229.801 155.886 191.929 1.00 23.11 ? 4425 GLN A CG    1 
ATOM   21870 C  CD    . GLN A 1 4425 ? 229.584 156.296 190.486 1.00 30.52 ? 4425 GLN A CD    1 
ATOM   21871 O  OE1   . GLN A 1 4425 ? 228.679 155.799 189.817 1.00 31.23 ? 4425 GLN A OE1   1 
ATOM   21872 N  NE2   . GLN A 1 4425 ? 230.416 157.209 189.999 1.00 23.18 ? 4425 GLN A NE2   1 
ATOM   21873 N  N     . ASP A 1 4426 ? 228.388 158.580 195.390 1.00 18.58 ? 4426 ASP A N     1 
ATOM   21874 C  CA    . ASP A 1 4426 ? 228.373 159.786 196.214 1.00 17.24 ? 4426 ASP A CA    1 
ATOM   21875 C  C     . ASP A 1 4426 ? 228.608 159.461 197.684 1.00 19.35 ? 4426 ASP A C     1 
ATOM   21876 O  O     . ASP A 1 4426 ? 229.384 160.145 198.361 1.00 20.21 ? 4426 ASP A O     1 
ATOM   21877 C  CB    . ASP A 1 4426 ? 227.051 160.529 196.035 1.00 21.21 ? 4426 ASP A CB    1 
ATOM   21878 C  CG    . ASP A 1 4426 ? 226.839 161.007 194.615 1.00 29.39 ? 4426 ASP A CG    1 
ATOM   21879 O  OD1   . ASP A 1 4426 ? 227.747 160.809 193.780 1.00 26.67 ? 4426 ASP A OD1   1 
ATOM   21880 O  OD2   . ASP A 1 4426 ? 225.765 161.580 194.331 1.00 34.43 ? 4426 ASP A OD2   1 
ATOM   21881 N  N     . VAL A 1 4427 ? 227.950 158.419 198.197 1.00 16.47 ? 4427 VAL A N     1 
ATOM   21882 C  CA    . VAL A 1 4427 ? 228.107 158.065 199.604 1.00 18.14 ? 4427 VAL A CA    1 
ATOM   21883 C  C     . VAL A 1 4427 ? 229.525 157.585 199.882 1.00 17.35 ? 4427 VAL A C     1 
ATOM   21884 O  O     . VAL A 1 4427 ? 230.136 157.961 200.889 1.00 18.26 ? 4427 VAL A O     1 
ATOM   21885 C  CB    . VAL A 1 4427 ? 227.060 157.013 200.011 1.00 13.75 ? 4427 VAL A CB    1 
ATOM   21886 C  CG1   . VAL A 1 4427 ? 227.316 156.531 201.425 1.00 11.98 ? 4427 VAL A CG1   1 
ATOM   21887 C  CG2   . VAL A 1 4427 ? 225.659 157.586 199.886 1.00 17.52 ? 4427 VAL A CG2   1 
ATOM   21888 N  N     . ARG A 1 4428 ? 230.070 156.741 199.002 1.00 17.00 ? 4428 ARG A N     1 
ATOM   21889 C  CA    . ARG A 1 4428 ? 231.422 156.232 199.207 1.00 20.55 ? 4428 ARG A CA    1 
ATOM   21890 C  C     . ARG A 1 4428 ? 232.448 157.356 199.167 1.00 19.47 ? 4428 ARG A C     1 
ATOM   21891 O  O     . ARG A 1 4428 ? 233.384 157.382 199.977 1.00 21.55 ? 4428 ARG A O     1 
ATOM   21892 C  CB    . ARG A 1 4428 ? 231.746 155.166 198.159 1.00 21.02 ? 4428 ARG A CB    1 
ATOM   21893 C  CG    . ARG A 1 4428 ? 230.949 153.882 198.313 1.00 24.22 ? 4428 ARG A CG    1 
ATOM   21894 C  CD    . ARG A 1 4428 ? 231.525 152.761 197.460 1.00 23.13 ? 4428 ARG A CD    1 
ATOM   21895 N  NE    . ARG A 1 4428 ? 232.883 152.407 197.854 1.00 26.24 ? 4428 ARG A NE    1 
ATOM   21896 C  CZ    . ARG A 1 4428 ? 233.203 151.776 198.976 1.00 24.76 ? 4428 ARG A CZ    1 
ATOM   21897 N  NH1   . ARG A 1 4428 ? 232.279 151.379 199.836 1.00 25.85 ? 4428 ARG A NH1   1 
ATOM   21898 N  NH2   . ARG A 1 4428 ? 234.483 151.530 199.239 1.00 22.52 ? 4428 ARG A NH2   1 
ATOM   21899 N  N     . GLN A 1 4429 ? 232.297 158.292 198.227 1.00 18.13 ? 4429 GLN A N     1 
ATOM   21900 C  CA    . GLN A 1 4429 ? 233.223 159.418 198.151 1.00 21.46 ? 4429 GLN A CA    1 
ATOM   21901 C  C     . GLN A 1 4429 ? 233.128 160.298 199.390 1.00 18.74 ? 4429 GLN A C     1 
ATOM   21902 O  O     . GLN A 1 4429 ? 234.154 160.730 199.930 1.00 26.80 ? 4429 GLN A O     1 
ATOM   21903 C  CB    . GLN A 1 4429 ? 232.955 160.235 196.888 1.00 20.95 ? 4429 GLN A CB    1 
ATOM   21904 C  CG    . GLN A 1 4429 ? 234.095 161.157 196.468 1.00 22.12 ? 4429 GLN A CG    1 
ATOM   21905 C  CD    . GLN A 1 4429 ? 235.470 160.539 196.667 1.00 27.51 ? 4429 GLN A CD    1 
ATOM   21906 O  OE1   . GLN A 1 4429 ? 236.062 160.638 197.742 1.00 26.97 ? 4429 GLN A OE1   1 
ATOM   21907 N  NE2   . GLN A 1 4429 ? 235.983 159.896 195.626 1.00 29.86 ? 4429 GLN A NE2   1 
ATOM   21908 N  N     . ASP A 1 4430 ? 231.906 160.573 199.855 1.00 16.31 ? 4430 ASP A N     1 
ATOM   21909 C  CA    . ASP A 1 4430 ? 231.740 161.382 201.060 1.00 17.56 ? 4430 ASP A CA    1 
ATOM   21910 C  C     . ASP A 1 4430 ? 232.349 160.696 202.274 1.00 19.07 ? 4430 ASP A C     1 
ATOM   21911 O  O     . ASP A 1 4430 ? 233.013 161.340 203.093 1.00 21.61 ? 4430 ASP A O     1 
ATOM   21912 C  CB    . ASP A 1 4430 ? 230.258 161.672 201.301 1.00 17.46 ? 4430 ASP A CB    1 
ATOM   21913 C  CG    . ASP A 1 4430 ? 229.667 162.592 200.259 1.00 21.36 ? 4430 ASP A CG    1 
ATOM   21914 O  OD1   . ASP A 1 4430 ? 230.437 163.159 199.457 1.00 22.82 ? 4430 ASP A OD1   1 
ATOM   21915 O  OD2   . ASP A 1 4430 ? 228.428 162.749 200.242 1.00 29.05 ? 4430 ASP A OD2   1 
ATOM   21916 N  N     . LEU A 1 4431 ? 232.130 159.386 202.408 1.00 19.83 ? 4431 LEU A N     1 
ATOM   21917 C  CA    . LEU A 1 4431 ? 232.690 158.651 203.538 1.00 20.09 ? 4431 LEU A CA    1 
ATOM   21918 C  C     . LEU A 1 4431 ? 234.212 158.630 203.485 1.00 20.33 ? 4431 LEU A C     1 
ATOM   21919 O  O     . LEU A 1 4431 ? 234.876 158.749 204.521 1.00 25.60 ? 4431 LEU A O     1 
ATOM   21920 C  CB    . LEU A 1 4431 ? 232.128 157.233 203.567 1.00 21.05 ? 4431 LEU A CB    1 
ATOM   21921 C  CG    . LEU A 1 4431 ? 230.734 157.088 204.179 1.00 20.36 ? 4431 LEU A CG    1 
ATOM   21922 C  CD1   . LEU A 1 4431 ? 230.223 155.667 204.021 1.00 22.38 ? 4431 LEU A CD1   1 
ATOM   21923 C  CD2   . LEU A 1 4431 ? 230.748 157.499 205.643 1.00 15.33 ? 4431 LEU A CD2   1 
ATOM   21924 N  N     . ALA A 1 4432 ? 234.785 158.478 202.288 1.00 21.05 ? 4432 ALA A N     1 
ATOM   21925 C  CA    . ALA A 1 4432 ? 236.237 158.464 202.160 1.00 18.79 ? 4432 ALA A CA    1 
ATOM   21926 C  C     . ALA A 1 4432 ? 236.839 159.807 202.553 1.00 24.70 ? 4432 ALA A C     1 
ATOM   21927 O  O     . ALA A 1 4432 ? 237.903 159.859 203.178 1.00 27.55 ? 4432 ALA A O     1 
ATOM   21928 C  CB    . ALA A 1 4432 ? 236.637 158.090 200.734 1.00 16.39 ? 4432 ALA A CB    1 
ATOM   21929 N  N     . ASP A 1 4433 ? 236.175 160.905 202.184 1.00 23.14 ? 4433 ASP A N     1 
ATOM   21930 C  CA    . ASP A 1 4433 ? 236.655 162.226 202.578 1.00 18.52 ? 4433 ASP A CA    1 
ATOM   21931 C  C     . ASP A 1 4433 ? 236.603 162.403 204.091 1.00 21.44 ? 4433 ASP A C     1 
ATOM   21932 O  O     . ASP A 1 4433 ? 237.518 162.984 204.686 1.00 28.94 ? 4433 ASP A O     1 
ATOM   21933 C  CB    . ASP A 1 4433 ? 235.841 163.311 201.879 1.00 20.22 ? 4433 ASP A CB    1 
ATOM   21934 C  CG    . ASP A 1 4433 ? 236.137 163.394 200.394 1.00 32.53 ? 4433 ASP A CG    1 
ATOM   21935 O  OD1   . ASP A 1 4433 ? 237.034 162.664 199.925 1.00 35.10 ? 4433 ASP A OD1   1 
ATOM   21936 O  OD2   . ASP A 1 4433 ? 235.472 164.190 199.697 1.00 32.59 ? 4433 ASP A OD2   1 
ATOM   21937 N  N     . VAL A 1 4434 ? 235.541 161.905 204.733 1.00 19.33 ? 4434 VAL A N     1 
ATOM   21938 C  CA    . VAL A 1 4434 ? 235.427 162.018 206.185 1.00 20.26 ? 4434 VAL A CA    1 
ATOM   21939 C  C     . VAL A 1 4434 ? 236.560 161.262 206.870 1.00 25.14 ? 4434 VAL A C     1 
ATOM   21940 O  O     . VAL A 1 4434 ? 237.162 161.754 207.831 1.00 23.26 ? 4434 VAL A O     1 
ATOM   21941 C  CB    . VAL A 1 4434 ? 234.048 161.520 206.656 1.00 23.35 ? 4434 VAL A CB    1 
ATOM   21942 C  CG1   . VAL A 1 4434 ? 234.031 161.349 208.166 1.00 19.29 ? 4434 VAL A CG1   1 
ATOM   21943 C  CG2   . VAL A 1 4434 ? 232.963 162.488 206.224 1.00 15.36 ? 4434 VAL A CG2   1 
ATOM   21944 N  N     . VAL A 1 4435 ? 236.870 160.057 206.383 1.00 27.68 ? 4435 VAL A N     1 
ATOM   21945 C  CA    . VAL A 1 4435 ? 237.989 159.299 206.937 1.00 28.44 ? 4435 VAL A CA    1 
ATOM   21946 C  C     . VAL A 1 4435 ? 239.287 160.076 206.774 1.00 29.30 ? 4435 VAL A C     1 
ATOM   21947 O  O     . VAL A 1 4435 ? 240.088 160.181 207.710 1.00 32.45 ? 4435 VAL A O     1 
ATOM   21948 C  CB    . VAL A 1 4435 ? 238.081 157.914 206.270 1.00 20.83 ? 4435 VAL A CB    1 
ATOM   21949 C  CG1   . VAL A 1 4435 ? 239.311 157.171 206.761 1.00 25.05 ? 4435 VAL A CG1   1 
ATOM   21950 C  CG2   . VAL A 1 4435 ? 236.828 157.109 206.543 1.00 28.81 ? 4435 VAL A CG2   1 
ATOM   21951 N  N     . GLN A 1 4436 ? 239.511 160.637 205.586 1.00 27.43 ? 4436 GLN A N     1 
ATOM   21952 C  CA    . GLN A 1 4436 ? 240.737 161.387 205.345 1.00 27.05 ? 4436 GLN A CA    1 
ATOM   21953 C  C     . GLN A 1 4436 ? 240.775 162.660 206.184 1.00 25.69 ? 4436 GLN A C     1 
ATOM   21954 O  O     . GLN A 1 4436 ? 241.846 163.075 206.644 1.00 26.39 ? 4436 GLN A O     1 
ATOM   21955 C  CB    . GLN A 1 4436 ? 240.863 161.699 203.855 1.00 19.16 ? 4436 GLN A CB    1 
ATOM   21956 C  CG    . GLN A 1 4436 ? 242.058 162.547 203.488 1.00 31.18 ? 4436 GLN A CG    1 
ATOM   21957 C  CD    . GLN A 1 4436 ? 242.289 162.611 201.994 1.00 34.42 ? 4436 GLN A CD    1 
ATOM   21958 O  OE1   . GLN A 1 4436 ? 241.572 161.980 201.217 1.00 32.60 ? 4436 GLN A OE1   1 
ATOM   21959 N  NE2   . GLN A 1 4436 ? 243.294 163.373 201.581 1.00 29.25 ? 4436 GLN A NE2   1 
ATOM   21960 N  N     . VAL A 1 4437 ? 239.618 163.291 206.399 1.00 24.86 ? 4437 VAL A N     1 
ATOM   21961 C  CA    . VAL A 1 4437 ? 239.555 164.450 207.287 1.00 24.36 ? 4437 VAL A CA    1 
ATOM   21962 C  C     . VAL A 1 4437 ? 239.921 164.044 208.710 1.00 22.15 ? 4437 VAL A C     1 
ATOM   21963 O  O     . VAL A 1 4437 ? 240.717 164.708 209.381 1.00 25.70 ? 4437 VAL A O     1 
ATOM   21964 C  CB    . VAL A 1 4437 ? 238.160 165.097 207.228 1.00 20.31 ? 4437 VAL A CB    1 
ATOM   21965 C  CG1   . VAL A 1 4437 ? 237.922 165.967 208.455 1.00 14.96 ? 4437 VAL A CG1   1 
ATOM   21966 C  CG2   . VAL A 1 4437 ? 238.010 165.913 205.965 1.00 19.78 ? 4437 VAL A CG2   1 
ATOM   21967 N  N     . CYS A 1 4438 ? 239.352 162.932 209.183 1.00 26.23 ? 4438 CYS A N     1 
ATOM   21968 C  CA    . CYS A 1 4438 ? 239.617 162.462 210.536 1.00 27.38 ? 4438 CYS A CA    1 
ATOM   21969 C  C     . CYS A 1 4438 ? 241.025 161.907 210.702 1.00 27.34 ? 4438 CYS A C     1 
ATOM   21970 O  O     . CYS A 1 4438 ? 241.431 161.625 211.835 1.00 33.98 ? 4438 CYS A O     1 
ATOM   21971 C  CB    . CYS A 1 4438 ? 238.585 161.407 210.934 1.00 22.33 ? 4438 CYS A CB    1 
ATOM   21972 S  SG    . CYS A 1 4438 ? 236.892 162.036 211.010 1.00 55.20 ? 4438 CYS A SG    1 
ATOM   21973 N  N     . GLU A 1 4439 ? 241.766 161.726 209.616 1.00 25.73 ? 4439 GLU A N     1 
ATOM   21974 C  CA    . GLU A 1 4439 ? 243.187 161.420 209.686 1.00 22.07 ? 4439 GLU A CA    1 
ATOM   21975 C  C     . GLU A 1 4439 ? 244.054 162.656 209.505 1.00 27.41 ? 4439 GLU A C     1 
ATOM   21976 O  O     . GLU A 1 4439 ? 245.283 162.535 209.463 1.00 34.31 ? 4439 GLU A O     1 
ATOM   21977 C  CB    . GLU A 1 4439 ? 243.555 160.361 208.644 1.00 25.83 ? 4439 GLU A CB    1 
ATOM   21978 C  CG    . GLU A 1 4439 ? 243.236 158.941 209.075 1.00 25.76 ? 4439 GLU A CG    1 
ATOM   21979 C  CD    . GLU A 1 4439 ? 243.513 157.923 207.985 1.00 34.30 ? 4439 GLU A CD    1 
ATOM   21980 O  OE1   . GLU A 1 4439 ? 243.924 158.330 206.879 1.00 35.20 ? 4439 GLU A OE1   1 
ATOM   21981 O  OE2   . GLU A 1 4439 ? 243.318 156.714 208.236 1.00 37.10 ? 4439 GLU A OE2   1 
ATOM   21982 N  N     . GLY A 1 4440 ? 243.446 163.834 209.403 1.00 28.04 ? 4440 GLY A N     1 
ATOM   21983 C  CA    . GLY A 1 4440 ? 244.197 165.067 209.236 1.00 23.27 ? 4440 GLY A CA    1 
ATOM   21984 C  C     . GLY A 1 4440 ? 244.989 165.138 207.950 1.00 27.55 ? 4440 GLY A C     1 
ATOM   21985 O  O     . GLY A 1 4440 ? 246.145 165.578 207.960 1.00 32.90 ? 4440 GLY A O     1 
ATOM   21986 N  N     . LYS A 1 4441 ? 244.390 164.716 206.834 1.00 25.86 ? 4441 LYS A N     1 
ATOM   21987 C  CA    . LYS A 1 4441 ? 245.068 164.736 205.548 1.00 27.07 ? 4441 LYS A CA    1 
ATOM   21988 C  C     . LYS A 1 4441 ? 244.430 165.659 204.518 1.00 28.13 ? 4441 LYS A C     1 
ATOM   21989 O  O     . LYS A 1 4441 ? 245.120 166.063 203.577 1.00 35.52 ? 4441 LYS A O     1 
ATOM   21990 C  CB    . LYS A 1 4441 ? 245.152 163.319 204.958 1.00 28.48 ? 4441 LYS A CB    1 
ATOM   21991 C  CG    . LYS A 1 4441 ? 245.866 162.315 205.849 1.00 29.43 ? 4441 LYS A CG    1 
ATOM   21992 C  CD    . LYS A 1 4441 ? 245.858 160.929 205.226 1.00 31.79 ? 4441 LYS A CD    1 
ATOM   21993 C  CE    . LYS A 1 4441 ? 246.672 159.946 206.049 1.00 34.04 ? 4441 LYS A CE    1 
ATOM   21994 N  NZ    . LYS A 1 4441 ? 246.635 158.577 205.466 1.00 33.58 ? 4441 LYS A NZ    1 
ATOM   21995 N  N     . LYS A 1 4442 ? 243.153 166.002 204.658 1.00 26.04 ? 4442 LYS A N     1 
ATOM   21996 C  CA    . LYS A 1 4442 ? 242.523 167.004 203.813 1.00 24.97 ? 4442 LYS A CA    1 
ATOM   21997 C  C     . LYS A 1 4442 ? 241.742 167.978 204.683 1.00 21.64 ? 4442 LYS A C     1 
ATOM   21998 O  O     . LYS A 1 4442 ? 241.184 167.594 205.716 1.00 14.92 ? 4442 LYS A O     1 
ATOM   21999 C  CB    . LYS A 1 4442 ? 241.608 166.369 202.752 1.00 25.31 ? 4442 LYS A CB    1 
ATOM   22000 C  CG    . LYS A 1 4442 ? 240.361 165.700 203.291 1.00 25.72 ? 4442 LYS A CG    1 
ATOM   22001 C  CD    . LYS A 1 4442 ? 239.369 165.410 202.178 1.00 22.36 ? 4442 LYS A CD    1 
ATOM   22002 C  CE    . LYS A 1 4442 ? 238.994 166.676 201.431 1.00 23.50 ? 4442 LYS A CE    1 
ATOM   22003 N  NZ    . LYS A 1 4442 ? 237.968 166.428 200.382 1.00 25.39 ? 4442 LYS A NZ    1 
ATOM   22004 N  N     . LYS A 1 4443 ? 241.715 169.239 204.263 1.00 24.09 ? 4443 LYS A N     1 
ATOM   22005 C  CA    . LYS A 1 4443 ? 241.146 170.307 205.073 1.00 16.96 ? 4443 LYS A CA    1 
ATOM   22006 C  C     . LYS A 1 4443 ? 239.622 170.284 205.015 1.00 17.49 ? 4443 LYS A C     1 
ATOM   22007 O  O     . LYS A 1 4443 ? 239.018 169.941 203.996 1.00 24.73 ? 4443 LYS A O     1 
ATOM   22008 C  CB    . LYS A 1 4443 ? 241.700 171.658 204.604 1.00 14.84 ? 4443 LYS A CB    1 
ATOM   22009 C  CG    . LYS A 1 4443 ? 241.221 172.889 205.363 1.00 18.02 ? 4443 LYS A CG    1 
ATOM   22010 C  CD    . LYS A 1 4443 ? 240.015 173.525 204.691 1.00 20.76 ? 4443 LYS A CD    1 
ATOM   22011 C  CE    . LYS A 1 4443 ? 240.410 174.183 203.381 1.00 23.16 ? 4443 LYS A CE    1 
ATOM   22012 N  NZ    . LYS A 1 4443 ? 239.250 174.824 202.704 1.00 25.99 ? 4443 LYS A NZ    1 
ATOM   22013 N  N     . GLN A 1 4444 ? 239.000 170.660 206.132 1.00 16.49 ? 4444 GLN A N     1 
ATOM   22014 C  CA    . GLN A 1 4444 ? 237.548 170.607 206.248 1.00 18.93 ? 4444 GLN A CA    1 
ATOM   22015 C  C     . GLN A 1 4444 ? 236.895 171.738 205.462 1.00 17.39 ? 4444 GLN A C     1 
ATOM   22016 O  O     . GLN A 1 4444 ? 237.122 172.918 205.747 1.00 21.31 ? 4444 GLN A O     1 
ATOM   22017 C  CB    . GLN A 1 4444 ? 237.140 170.687 207.715 1.00 15.69 ? 4444 GLN A CB    1 
ATOM   22018 C  CG    . GLN A 1 4444 ? 235.982 169.789 208.097 1.00 18.72 ? 4444 GLN A CG    1 
ATOM   22019 C  CD    . GLN A 1 4444 ? 235.844 169.636 209.597 1.00 24.01 ? 4444 GLN A CD    1 
ATOM   22020 O  OE1   . GLN A 1 4444 ? 236.728 170.030 210.356 1.00 31.98 ? 4444 GLN A OE1   1 
ATOM   22021 N  NE2   . GLN A 1 4444 ? 234.724 169.073 210.036 1.00 22.00 ? 4444 GLN A NE2   1 
ATOM   22022 N  N     . THR A 1 4445 ? 236.062 171.379 204.489 1.00 17.33 ? 4445 THR A N     1 
ATOM   22023 C  CA    . THR A 1 4445 ? 235.322 172.341 203.692 1.00 11.95 ? 4445 THR A CA    1 
ATOM   22024 C  C     . THR A 1 4445 ? 233.936 172.560 204.299 1.00 10.51 ? 4445 THR A C     1 
ATOM   22025 O  O     . THR A 1 4445 ? 233.554 171.924 205.283 1.00 15.12 ? 4445 THR A O     1 
ATOM   22026 C  CB    . THR A 1 4445 ? 235.216 171.870 202.240 1.00 7.28  ? 4445 THR A CB    1 
ATOM   22027 O  OG1   . THR A 1 4445 ? 234.201 170.864 202.131 1.00 8.76  ? 4445 THR A OG1   1 
ATOM   22028 C  CG2   . THR A 1 4445 ? 236.541 171.294 201.775 1.00 8.15  ? 4445 THR A CG2   1 
ATOM   22029 N  N     . ASN A 1 4446 ? 233.177 173.481 203.699 1.00 9.03  ? 4446 ASN A N     1 
ATOM   22030 C  CA    . ASN A 1 4446 ? 231.823 173.747 204.179 1.00 11.36 ? 4446 ASN A CA    1 
ATOM   22031 C  C     . ASN A 1 4446 ? 230.935 172.517 204.045 1.00 9.68  ? 4446 ASN A C     1 
ATOM   22032 O  O     . ASN A 1 4446 ? 230.164 172.198 204.957 1.00 13.52 ? 4446 ASN A O     1 
ATOM   22033 C  CB    . ASN A 1 4446 ? 231.213 174.925 203.419 1.00 5.86  ? 4446 ASN A CB    1 
ATOM   22034 C  CG    . ASN A 1 4446 ? 231.761 176.256 203.877 1.00 6.29  ? 4446 ASN A CG    1 
ATOM   22035 O  OD1   . ASN A 1 4446 ? 232.144 176.415 205.034 1.00 15.85 ? 4446 ASN A OD1   1 
ATOM   22036 N  ND2   . ASN A 1 4446 ? 231.803 177.223 202.969 1.00 4.13  ? 4446 ASN A ND2   1 
ATOM   22037 N  N     . TYR A 1 4447 ? 231.025 171.818 202.911 1.00 6.19  ? 4447 TYR A N     1 
ATOM   22038 C  CA    . TYR A 1 4447 ? 230.240 170.603 202.729 1.00 11.89 ? 4447 TYR A CA    1 
ATOM   22039 C  C     . TYR A 1 4447 ? 230.629 169.540 203.746 1.00 15.74 ? 4447 TYR A C     1 
ATOM   22040 O  O     . TYR A 1 4447 ? 229.762 168.885 204.335 1.00 12.64 ? 4447 TYR A O     1 
ATOM   22041 C  CB    . TYR A 1 4447 ? 230.420 170.071 201.307 1.00 8.59  ? 4447 TYR A CB    1 
ATOM   22042 C  CG    . TYR A 1 4447 ? 229.738 168.747 201.061 1.00 13.80 ? 4447 TYR A CG    1 
ATOM   22043 C  CD1   . TYR A 1 4447 ? 228.369 168.683 200.838 1.00 16.80 ? 4447 TYR A CD1   1 
ATOM   22044 C  CD2   . TYR A 1 4447 ? 230.459 167.560 201.060 1.00 19.25 ? 4447 TYR A CD2   1 
ATOM   22045 C  CE1   . TYR A 1 4447 ? 227.739 167.474 200.616 1.00 21.81 ? 4447 TYR A CE1   1 
ATOM   22046 C  CE2   . TYR A 1 4447 ? 229.837 166.347 200.839 1.00 18.76 ? 4447 TYR A CE2   1 
ATOM   22047 C  CZ    . TYR A 1 4447 ? 228.476 166.310 200.617 1.00 24.34 ? 4447 TYR A CZ    1 
ATOM   22048 O  OH    . TYR A 1 4447 ? 227.850 165.106 200.398 1.00 28.56 ? 4447 TYR A OH    1 
ATOM   22049 N  N     . LEU A 1 4448 ? 231.931 169.359 203.969 1.00 15.21 ? 4448 LEU A N     1 
ATOM   22050 C  CA    . LEU A 1 4448 ? 232.389 168.371 204.937 1.00 10.50 ? 4448 LEU A CA    1 
ATOM   22051 C  C     . LEU A 1 4448 ? 231.985 168.756 206.355 1.00 15.54 ? 4448 LEU A C     1 
ATOM   22052 O  O     . LEU A 1 4448 ? 231.612 167.891 207.153 1.00 24.80 ? 4448 LEU A O     1 
ATOM   22053 C  CB    . LEU A 1 4448 ? 233.901 168.194 204.828 1.00 12.51 ? 4448 LEU A CB    1 
ATOM   22054 C  CG    . LEU A 1 4448 ? 234.364 167.461 203.567 1.00 14.75 ? 4448 LEU A CG    1 
ATOM   22055 C  CD1   . LEU A 1 4448 ? 235.876 167.410 203.493 1.00 15.48 ? 4448 LEU A CD1   1 
ATOM   22056 C  CD2   . LEU A 1 4448 ? 233.773 166.058 203.513 1.00 11.32 ? 4448 LEU A CD2   1 
ATOM   22057 N  N     . ARG A 1 4449 ? 232.044 170.051 206.683 1.00 12.94 ? 4449 ARG A N     1 
ATOM   22058 C  CA    . ARG A 1 4449 ? 231.593 170.496 207.997 1.00 12.28 ? 4449 ARG A CA    1 
ATOM   22059 C  C     . ARG A 1 4449 ? 230.118 170.179 208.205 1.00 15.07 ? 4449 ARG A C     1 
ATOM   22060 O  O     . ARG A 1 4449 ? 229.717 169.723 209.284 1.00 16.55 ? 4449 ARG A O     1 
ATOM   22061 C  CB    . ARG A 1 4449 ? 231.848 171.994 208.167 1.00 12.18 ? 4449 ARG A CB    1 
ATOM   22062 C  CG    . ARG A 1 4449 ? 233.293 172.356 208.461 1.00 16.60 ? 4449 ARG A CG    1 
ATOM   22063 C  CD    . ARG A 1 4449 ? 233.429 173.820 208.865 1.00 15.62 ? 4449 ARG A CD    1 
ATOM   22064 N  NE    . ARG A 1 4449 ? 233.736 174.684 207.730 1.00 12.12 ? 4449 ARG A NE    1 
ATOM   22065 C  CZ    . ARG A 1 4449 ? 234.909 174.733 207.114 1.00 15.76 ? 4449 ARG A CZ    1 
ATOM   22066 N  NH1   . ARG A 1 4449 ? 235.931 173.992 207.512 1.00 17.61 ? 4449 ARG A NH1   1 
ATOM   22067 N  NH2   . ARG A 1 4449 ? 235.062 175.547 206.074 1.00 10.53 ? 4449 ARG A NH2   1 
ATOM   22068 N  N     . THR A 1 4450 ? 229.292 170.417 207.184 1.00 14.59 ? 4450 THR A N     1 
ATOM   22069 C  CA    . THR A 1 4450 ? 227.873 170.089 207.283 1.00 14.08 ? 4450 THR A CA    1 
ATOM   22070 C  C     . THR A 1 4450 ? 227.661 168.584 207.401 1.00 20.65 ? 4450 THR A C     1 
ATOM   22071 O  O     . THR A 1 4450 ? 226.855 168.124 208.220 1.00 16.88 ? 4450 THR A O     1 
ATOM   22072 C  CB    . THR A 1 4450 ? 227.125 170.646 206.071 1.00 10.15 ? 4450 THR A CB    1 
ATOM   22073 O  OG1   . THR A 1 4450 ? 227.072 172.075 206.157 1.00 24.96 ? 4450 THR A OG1   1 
ATOM   22074 C  CG2   . THR A 1 4450 ? 225.710 170.097 206.007 1.00 9.91  ? 4450 THR A CG2   1 
ATOM   22075 N  N     . LEU A 1 4451 ? 228.380 167.802 206.594 1.00 15.40 ? 4451 LEU A N     1 
ATOM   22076 C  CA    . LEU A 1 4451 ? 228.233 166.351 206.642 1.00 14.44 ? 4451 LEU A CA    1 
ATOM   22077 C  C     . LEU A 1 4451 ? 228.735 165.783 207.963 1.00 19.78 ? 4451 LEU A C     1 
ATOM   22078 O  O     . LEU A 1 4451 ? 228.106 164.890 208.539 1.00 23.75 ? 4451 LEU A O     1 
ATOM   22079 C  CB    . LEU A 1 4451 ? 228.975 165.716 205.466 1.00 16.71 ? 4451 LEU A CB    1 
ATOM   22080 C  CG    . LEU A 1 4451 ? 229.056 164.190 205.413 1.00 12.68 ? 4451 LEU A CG    1 
ATOM   22081 C  CD1   . LEU A 1 4451 ? 227.708 163.592 205.072 1.00 18.11 ? 4451 LEU A CD1   1 
ATOM   22082 C  CD2   . LEU A 1 4451 ? 230.100 163.760 204.402 1.00 15.33 ? 4451 LEU A CD2   1 
ATOM   22083 N  N     . ILE A 1 4452 ? 229.865 166.292 208.455 1.00 20.80 ? 4452 ILE A N     1 
ATOM   22084 C  CA    . ILE A 1 4452 ? 230.437 165.770 209.691 1.00 18.34 ? 4452 ILE A CA    1 
ATOM   22085 C  C     . ILE A 1 4452 ? 229.531 166.080 210.877 1.00 15.50 ? 4452 ILE A C     1 
ATOM   22086 O  O     . ILE A 1 4452 ? 229.365 165.250 211.780 1.00 19.95 ? 4452 ILE A O     1 
ATOM   22087 C  CB    . ILE A 1 4452 ? 231.862 166.320 209.885 1.00 14.64 ? 4452 ILE A CB    1 
ATOM   22088 C  CG1   . ILE A 1 4452 ? 232.835 165.559 208.982 1.00 18.55 ? 4452 ILE A CG1   1 
ATOM   22089 C  CG2   . ILE A 1 4452 ? 232.290 166.240 211.340 1.00 15.50 ? 4452 ILE A CG2   1 
ATOM   22090 C  CD1   . ILE A 1 4452 ? 234.286 165.925 209.182 1.00 19.22 ? 4452 ILE A CD1   1 
ATOM   22091 N  N     . ASN A 1 4453 ? 228.918 167.266 210.891 1.00 17.66 ? 4453 ASN A N     1 
ATOM   22092 C  CA    . ASN A 1 4453 ? 227.999 167.606 211.973 1.00 20.57 ? 4453 ASN A CA    1 
ATOM   22093 C  C     . ASN A 1 4453 ? 226.813 166.651 212.015 1.00 19.22 ? 4453 ASN A C     1 
ATOM   22094 O  O     . ASN A 1 4453 ? 226.405 166.206 213.094 1.00 20.55 ? 4453 ASN A O     1 
ATOM   22095 C  CB    . ASN A 1 4453 ? 227.523 169.052 211.830 1.00 18.03 ? 4453 ASN A CB    1 
ATOM   22096 C  CG    . ASN A 1 4453 ? 228.467 170.043 212.485 1.00 31.16 ? 4453 ASN A CG    1 
ATOM   22097 O  OD1   . ASN A 1 4453 ? 228.940 170.985 211.846 1.00 31.11 ? 4453 ASN A OD1   1 
ATOM   22098 N  ND2   . ASN A 1 4453 ? 228.750 169.834 213.765 1.00 28.58 ? 4453 ASN A ND2   1 
ATOM   22099 N  N     . GLU A 1 4454 ? 226.247 166.322 210.850 1.00 17.84 ? 4454 GLU A N     1 
ATOM   22100 C  CA    . GLU A 1 4454 ? 225.136 165.374 210.810 1.00 14.82 ? 4454 GLU A CA    1 
ATOM   22101 C  C     . GLU A 1 4454 ? 225.562 163.999 211.306 1.00 15.89 ? 4454 GLU A C     1 
ATOM   22102 O  O     . GLU A 1 4454 ? 224.835 163.352 212.068 1.00 15.49 ? 4454 GLU A O     1 
ATOM   22103 C  CB    . GLU A 1 4454 ? 224.580 165.275 209.390 1.00 16.19 ? 4454 GLU A CB    1 
ATOM   22104 C  CG    . GLU A 1 4454 ? 223.749 166.463 208.952 1.00 16.90 ? 4454 GLU A CG    1 
ATOM   22105 C  CD    . GLU A 1 4454 ? 223.732 166.628 207.445 1.00 24.88 ? 4454 GLU A CD    1 
ATOM   22106 O  OE1   . GLU A 1 4454 ? 224.459 165.880 206.758 1.00 22.25 ? 4454 GLU A OE1   1 
ATOM   22107 O  OE2   . GLU A 1 4454 ? 222.992 167.502 206.946 1.00 28.50 ? 4454 GLU A OE2   1 
ATOM   22108 N  N     . LEU A 1 4455 ? 226.741 163.536 210.886 1.00 16.88 ? 4455 LEU A N     1 
ATOM   22109 C  CA    . LEU A 1 4455 ? 227.203 162.208 211.274 1.00 19.03 ? 4455 LEU A CA    1 
ATOM   22110 C  C     . LEU A 1 4455 ? 227.449 162.118 212.777 1.00 20.21 ? 4455 LEU A C     1 
ATOM   22111 O  O     . LEU A 1 4455 ? 227.186 161.077 213.390 1.00 25.01 ? 4455 LEU A O     1 
ATOM   22112 C  CB    . LEU A 1 4455 ? 228.467 161.850 210.497 1.00 19.87 ? 4455 LEU A CB    1 
ATOM   22113 C  CG    . LEU A 1 4455 ? 228.258 161.582 209.005 1.00 20.55 ? 4455 LEU A CG    1 
ATOM   22114 C  CD1   . LEU A 1 4455 ? 229.551 161.128 208.345 1.00 14.98 ? 4455 LEU A CD1   1 
ATOM   22115 C  CD2   . LEU A 1 4455 ? 227.154 160.556 208.798 1.00 13.86 ? 4455 LEU A CD2   1 
ATOM   22116 N  N     . VAL A 1 4456 ? 227.964 163.190 213.383 1.00 18.64 ? 4456 VAL A N     1 
ATOM   22117 C  CA    . VAL A 1 4456 ? 228.155 163.201 214.831 1.00 20.54 ? 4456 VAL A CA    1 
ATOM   22118 C  C     . VAL A 1 4456 ? 226.814 163.119 215.549 1.00 20.18 ? 4456 VAL A C     1 
ATOM   22119 O  O     . VAL A 1 4456 ? 226.660 162.376 216.524 1.00 24.08 ? 4456 VAL A O     1 
ATOM   22120 C  CB    . VAL A 1 4456 ? 228.956 164.445 215.260 1.00 19.85 ? 4456 VAL A CB    1 
ATOM   22121 C  CG1   . VAL A 1 4456 ? 229.045 164.519 216.771 1.00 19.11 ? 4456 VAL A CG1   1 
ATOM   22122 C  CG2   . VAL A 1 4456 ? 230.351 164.400 214.665 1.00 12.21 ? 4456 VAL A CG2   1 
ATOM   22123 N  N     . LYS A 1 4457 ? 225.822 163.872 215.075 1.00 17.89 ? 4457 LYS A N     1 
ATOM   22124 C  CA    . LYS A 1 4457 ? 224.499 163.850 215.685 1.00 22.14 ? 4457 LYS A CA    1 
ATOM   22125 C  C     . LYS A 1 4457 ? 223.682 162.624 215.297 1.00 24.56 ? 4457 LYS A C     1 
ATOM   22126 O  O     . LYS A 1 4457 ? 222.595 162.427 215.849 1.00 27.47 ? 4457 LYS A O     1 
ATOM   22127 C  CB    . LYS A 1 4457 ? 223.720 165.115 215.316 1.00 21.95 ? 4457 LYS A CB    1 
ATOM   22128 C  CG    . LYS A 1 4457 ? 224.370 166.408 215.784 1.00 22.16 ? 4457 LYS A CG    1 
ATOM   22129 C  CD    . LYS A 1 4457 ? 223.604 167.625 215.285 1.00 22.94 ? 4457 LYS A CD    1 
ATOM   22130 C  CE    . LYS A 1 4457 ? 223.564 167.681 213.768 1.00 25.72 ? 4457 LYS A CE    1 
ATOM   22131 N  NZ    . LYS A 1 4457 ? 222.780 168.849 213.278 1.00 31.93 ? 4457 LYS A NZ    1 
ATOM   22132 N  N     . GLY A 1 4458 ? 224.167 161.806 214.364 1.00 21.26 ? 4458 GLY A N     1 
ATOM   22133 C  CA    . GLY A 1 4458 ? 223.446 160.621 213.957 1.00 19.42 ? 4458 GLY A CA    1 
ATOM   22134 C  C     . GLY A 1 4458 ? 222.296 160.861 213.007 1.00 23.15 ? 4458 GLY A C     1 
ATOM   22135 O  O     . GLY A 1 4458 ? 221.532 159.928 212.738 1.00 24.28 ? 4458 GLY A O     1 
ATOM   22136 N  N     . ILE A 1 4459 ? 222.143 162.077 212.498 1.00 21.49 ? 4459 ILE A N     1 
ATOM   22137 C  CA    . ILE A 1 4459 ? 221.083 162.381 211.546 1.00 18.74 ? 4459 ILE A CA    1 
ATOM   22138 C  C     . ILE A 1 4459 ? 221.520 161.937 210.158 1.00 25.46 ? 4459 ILE A C     1 
ATOM   22139 O  O     . ILE A 1 4459 ? 222.679 162.111 209.766 1.00 23.48 ? 4459 ILE A O     1 
ATOM   22140 C  CB    . ILE A 1 4459 ? 220.746 163.883 211.575 1.00 18.32 ? 4459 ILE A CB    1 
ATOM   22141 C  CG1   . ILE A 1 4459 ? 220.310 164.302 212.980 1.00 25.37 ? 4459 ILE A CG1   1 
ATOM   22142 C  CG2   . ILE A 1 4459 ? 219.664 164.213 210.560 1.00 20.18 ? 4459 ILE A CG2   1 
ATOM   22143 C  CD1   . ILE A 1 4459 ? 220.041 165.785 213.116 1.00 22.57 ? 4459 ILE A CD1   1 
ATOM   22144 N  N     . LEU A 1 4460 ? 220.593 161.337 209.418 1.00 24.68 ? 4460 LEU A N     1 
ATOM   22145 C  CA    . LEU A 1 4460 ? 220.877 160.932 208.052 1.00 19.54 ? 4460 LEU A CA    1 
ATOM   22146 C  C     . LEU A 1 4460 ? 221.111 162.167 207.187 1.00 22.70 ? 4460 LEU A C     1 
ATOM   22147 O  O     . LEU A 1 4460 ? 220.273 163.079 207.179 1.00 25.99 ? 4460 LEU A O     1 
ATOM   22148 C  CB    . LEU A 1 4460 ? 219.719 160.107 207.494 1.00 23.28 ? 4460 LEU A CB    1 
ATOM   22149 C  CG    . LEU A 1 4460 ? 219.706 159.834 205.991 1.00 20.96 ? 4460 LEU A CG    1 
ATOM   22150 C  CD1   . LEU A 1 4460 ? 220.878 158.957 205.594 1.00 18.27 ? 4460 LEU A CD1   1 
ATOM   22151 C  CD2   . LEU A 1 4460 ? 218.391 159.197 205.580 1.00 18.75 ? 4460 LEU A CD2   1 
ATOM   22152 N  N     . PRO A 1 4461 ? 222.232 162.248 206.469 1.00 24.44 ? 4461 PRO A N     1 
ATOM   22153 C  CA    . PRO A 1 4461 ? 222.488 163.421 205.626 1.00 17.96 ? 4461 PRO A CA    1 
ATOM   22154 C  C     . PRO A 1 4461 ? 221.414 163.589 204.561 1.00 22.54 ? 4461 PRO A C     1 
ATOM   22155 O  O     . PRO A 1 4461 ? 220.927 162.614 203.986 1.00 30.20 ? 4461 PRO A O     1 
ATOM   22156 C  CB    . PRO A 1 4461 ? 223.852 163.116 205.005 1.00 17.52 ? 4461 PRO A CB    1 
ATOM   22157 C  CG    . PRO A 1 4461 ? 224.500 162.200 205.981 1.00 17.13 ? 4461 PRO A CG    1 
ATOM   22158 C  CD    . PRO A 1 4461 ? 223.392 161.343 206.511 1.00 19.58 ? 4461 PRO A CD    1 
ATOM   22159 N  N     . ARG A 1 4462 ? 221.050 164.847 204.301 1.00 25.89 ? 4462 ARG A N     1 
ATOM   22160 C  CA    . ARG A 1 4462 ? 220.033 165.121 203.293 1.00 22.11 ? 4462 ARG A CA    1 
ATOM   22161 C  C     . ARG A 1 4462 ? 220.544 164.835 201.889 1.00 23.36 ? 4462 ARG A C     1 
ATOM   22162 O  O     . ARG A 1 4462 ? 219.749 164.520 200.995 1.00 24.87 ? 4462 ARG A O     1 
ATOM   22163 C  CB    . ARG A 1 4462 ? 219.556 166.569 203.406 1.00 19.76 ? 4462 ARG A CB    1 
ATOM   22164 C  CG    . ARG A 1 4462 ? 218.883 166.921 204.730 1.00 27.11 ? 4462 ARG A CG    1 
ATOM   22165 C  CD    . ARG A 1 4462 ? 217.640 166.073 205.000 1.00 28.89 ? 4462 ARG A CD    1 
ATOM   22166 N  NE    . ARG A 1 4462 ? 217.955 164.811 205.662 1.00 30.67 ? 4462 ARG A NE    1 
ATOM   22167 C  CZ    . ARG A 1 4462 ? 217.066 163.866 205.937 1.00 36.81 ? 4462 ARG A CZ    1 
ATOM   22168 N  NH1   . ARG A 1 4462 ? 215.789 164.003 205.621 1.00 37.98 ? 4462 ARG A NH1   1 
ATOM   22169 N  NH2   . ARG A 1 4462 ? 217.470 162.753 206.545 1.00 30.19 ? 4462 ARG A NH2   1 
ATOM   22170 N  N     . SER A 1 4463 ? 221.857 164.940 201.672 1.00 24.72 ? 4463 SER A N     1 
ATOM   22171 C  CA    . SER A 1 4463 ? 222.424 164.570 200.381 1.00 16.96 ? 4463 SER A CA    1 
ATOM   22172 C  C     . SER A 1 4463 ? 222.239 163.084 200.110 1.00 26.27 ? 4463 SER A C     1 
ATOM   22173 O  O     . SER A 1 4463 ? 221.924 162.683 198.982 1.00 24.33 ? 4463 SER A O     1 
ATOM   22174 C  CB    . SER A 1 4463 ? 223.906 164.942 200.333 1.00 20.23 ? 4463 SER A CB    1 
ATOM   22175 O  OG    . SER A 1 4463 ? 224.103 166.298 200.688 1.00 29.03 ? 4463 SER A OG    1 
ATOM   22176 N  N     . TRP A 1 4464 ? 222.430 162.251 201.137 1.00 21.98 ? 4464 TRP A N     1 
ATOM   22177 C  CA    . TRP A 1 4464 ? 222.280 160.811 200.974 1.00 17.61 ? 4464 TRP A CA    1 
ATOM   22178 C  C     . TRP A 1 4464 ? 220.832 160.420 200.710 1.00 17.43 ? 4464 TRP A C     1 
ATOM   22179 O  O     . TRP A 1 4464 ? 220.577 159.423 200.023 1.00 19.67 ? 4464 TRP A O     1 
ATOM   22180 C  CB    . TRP A 1 4464 ? 222.806 160.094 202.219 1.00 17.91 ? 4464 TRP A CB    1 
ATOM   22181 C  CG    . TRP A 1 4464 ? 224.296 160.165 202.372 1.00 20.06 ? 4464 TRP A CG    1 
ATOM   22182 C  CD1   . TRP A 1 4464 ? 225.159 160.929 201.645 1.00 19.42 ? 4464 TRP A CD1   1 
ATOM   22183 C  CD2   . TRP A 1 4464 ? 225.095 159.462 203.330 1.00 15.69 ? 4464 TRP A CD2   1 
ATOM   22184 N  NE1   . TRP A 1 4464 ? 226.445 160.736 202.080 1.00 20.47 ? 4464 TRP A NE1   1 
ATOM   22185 C  CE2   . TRP A 1 4464 ? 226.433 159.841 203.114 1.00 16.55 ? 4464 TRP A CE2   1 
ATOM   22186 C  CE3   . TRP A 1 4464 ? 224.808 158.543 204.344 1.00 16.14 ? 4464 TRP A CE3   1 
ATOM   22187 C  CZ2   . TRP A 1 4464 ? 227.484 159.336 203.877 1.00 20.37 ? 4464 TRP A CZ2   1 
ATOM   22188 C  CZ3   . TRP A 1 4464 ? 225.852 158.042 205.098 1.00 14.09 ? 4464 TRP A CZ3   1 
ATOM   22189 C  CH2   . TRP A 1 4464 ? 227.172 158.439 204.860 1.00 17.64 ? 4464 TRP A CH2   1 
ATOM   22190 N  N     . SER A 1 4465 ? 219.878 161.185 201.237 1.00 18.52 ? 4465 SER A N     1 
ATOM   22191 C  CA    . SER A 1 4465 ? 218.464 160.854 201.099 1.00 20.28 ? 4465 SER A CA    1 
ATOM   22192 C  C     . SER A 1 4465 ? 218.032 161.041 199.650 1.00 18.23 ? 4465 SER A C     1 
ATOM   22193 O  O     . SER A 1 4465 ? 217.808 162.168 199.199 1.00 28.53 ? 4465 SER A O     1 
ATOM   22194 C  CB    . SER A 1 4465 ? 217.627 161.719 202.034 1.00 21.60 ? 4465 SER A CB    1 
ATOM   22195 O  OG    . SER A 1 4465 ? 217.828 163.096 201.771 1.00 30.13 ? 4465 SER A OG    1 
ATOM   22196 N  N     . HIS A 1 4466 ? 217.913 159.934 198.921 1.00 19.65 ? 4466 HIS A N     1 
ATOM   22197 C  CA    . HIS A 1 4466 ? 217.486 159.957 197.529 1.00 23.47 ? 4466 HIS A CA    1 
ATOM   22198 C  C     . HIS A 1 4466 ? 216.323 159.028 197.230 1.00 22.35 ? 4466 HIS A C     1 
ATOM   22199 O  O     . HIS A 1 4466 ? 215.644 159.233 196.216 1.00 30.39 ? 4466 HIS A O     1 
ATOM   22200 C  CB    . HIS A 1 4466 ? 218.657 159.600 196.601 1.00 22.40 ? 4466 HIS A CB    1 
ATOM   22201 C  CG    . HIS A 1 4466 ? 219.660 160.699 196.449 1.00 25.26 ? 4466 HIS A CG    1 
ATOM   22202 N  ND1   . HIS A 1 4466 ? 220.960 160.473 196.051 1.00 28.78 ? 4466 HIS A ND1   1 
ATOM   22203 C  CD2   . HIS A 1 4466 ? 219.555 162.036 196.646 1.00 21.74 ? 4466 HIS A CD2   1 
ATOM   22204 C  CE1   . HIS A 1 4466 ? 221.612 161.621 196.008 1.00 29.84 ? 4466 HIS A CE1   1 
ATOM   22205 N  NE2   . HIS A 1 4466 ? 220.782 162.585 196.364 1.00 26.92 ? 4466 HIS A NE2   1 
ATOM   22206 N  N     . TYR A 1 4467 ? 216.071 158.022 198.059 1.00 18.59 ? 4467 TYR A N     1 
ATOM   22207 C  CA    . TYR A 1 4467 ? 214.895 157.176 197.949 1.00 19.64 ? 4467 TYR A CA    1 
ATOM   22208 C  C     . TYR A 1 4467 ? 214.046 157.333 199.201 1.00 21.05 ? 4467 TYR A C     1 
ATOM   22209 O  O     . TYR A 1 4467 ? 214.565 157.555 200.299 1.00 19.86 ? 4467 TYR A O     1 
ATOM   22210 C  CB    . TYR A 1 4467 ? 215.278 155.703 197.741 1.00 17.15 ? 4467 TYR A CB    1 
ATOM   22211 C  CG    . TYR A 1 4467 ? 216.238 155.151 198.770 1.00 14.10 ? 4467 TYR A CG    1 
ATOM   22212 C  CD1   . TYR A 1 4467 ? 215.777 154.590 199.951 1.00 18.05 ? 4467 TYR A CD1   1 
ATOM   22213 C  CD2   . TYR A 1 4467 ? 217.608 155.189 198.556 1.00 15.56 ? 4467 TYR A CD2   1 
ATOM   22214 C  CE1   . TYR A 1 4467 ? 216.654 154.081 200.889 1.00 15.86 ? 4467 TYR A CE1   1 
ATOM   22215 C  CE2   . TYR A 1 4467 ? 218.493 154.681 199.486 1.00 13.40 ? 4467 TYR A CE2   1 
ATOM   22216 C  CZ    . TYR A 1 4467 ? 218.009 154.131 200.652 1.00 15.32 ? 4467 TYR A CZ    1 
ATOM   22217 O  OH    . TYR A 1 4467 ? 218.886 153.626 201.584 1.00 17.35 ? 4467 TYR A OH    1 
ATOM   22218 N  N     . THR A 1 4468 ? 212.731 157.225 199.021 1.00 19.15 ? 4468 THR A N     1 
ATOM   22219 C  CA    . THR A 1 4468 ? 211.799 157.459 200.116 1.00 17.01 ? 4468 THR A CA    1 
ATOM   22220 C  C     . THR A 1 4468 ? 212.022 156.471 201.259 1.00 20.10 ? 4468 THR A C     1 
ATOM   22221 O  O     . THR A 1 4468 ? 212.220 155.272 201.043 1.00 21.61 ? 4468 THR A O     1 
ATOM   22222 C  CB    . THR A 1 4468 ? 210.360 157.391 199.594 1.00 18.64 ? 4468 THR A CB    1 
ATOM   22223 O  OG1   . THR A 1 4468 ? 209.444 157.775 200.630 1.00 33.53 ? 4468 THR A OG1   1 
ATOM   22224 C  CG2   . THR A 1 4468 ? 210.020 156.013 199.063 1.00 15.53 ? 4468 THR A CG2   1 
ATOM   22225 N  N     . VAL A 1 4469 ? 212.020 156.996 202.480 1.00 20.58 ? 4469 VAL A N     1 
ATOM   22226 C  CA    . VAL A 1 4469 ? 212.292 156.213 203.682 1.00 18.49 ? 4469 VAL A CA    1 
ATOM   22227 C  C     . VAL A 1 4469 ? 211.263 156.586 204.737 1.00 23.12 ? 4469 VAL A C     1 
ATOM   22228 O  O     . VAL A 1 4469 ? 210.677 157.680 204.691 1.00 24.71 ? 4469 VAL A O     1 
ATOM   22229 C  CB    . VAL A 1 4469 ? 213.731 156.449 204.203 1.00 16.32 ? 4469 VAL A CB    1 
ATOM   22230 C  CG1   . VAL A 1 4469 ? 214.748 155.876 203.242 1.00 21.34 ? 4469 VAL A CG1   1 
ATOM   22231 C  CG2   . VAL A 1 4469 ? 213.976 157.932 204.429 1.00 26.34 ? 4469 VAL A CG2   1 
ATOM   22232 N  N     . PRO A 1 4470 ? 211.006 155.698 205.699 1.00 23.62 ? 4470 PRO A N     1 
ATOM   22233 C  CA    . PRO A 1 4470 ? 210.092 156.055 206.787 1.00 18.08 ? 4470 PRO A CA    1 
ATOM   22234 C  C     . PRO A 1 4470 ? 210.636 157.223 207.595 1.00 22.77 ? 4470 PRO A C     1 
ATOM   22235 O  O     . PRO A 1 4470 ? 211.844 157.343 207.813 1.00 23.70 ? 4470 PRO A O     1 
ATOM   22236 C  CB    . PRO A 1 4470 ? 210.013 154.774 207.622 1.00 14.78 ? 4470 PRO A CB    1 
ATOM   22237 C  CG    . PRO A 1 4470 ? 211.289 154.076 207.349 1.00 12.74 ? 4470 PRO A CG    1 
ATOM   22238 C  CD    . PRO A 1 4470 ? 211.624 154.377 205.918 1.00 15.66 ? 4470 PRO A CD    1 
ATOM   22239 N  N     . ALA A 1 4471 ? 209.727 158.090 208.034 1.00 29.20 ? 4471 ALA A N     1 
ATOM   22240 C  CA    . ALA A 1 4471 ? 210.125 159.265 208.796 1.00 25.34 ? 4471 ALA A CA    1 
ATOM   22241 C  C     . ALA A 1 4471 ? 210.757 158.855 210.119 1.00 27.04 ? 4471 ALA A C     1 
ATOM   22242 O  O     . ALA A 1 4471 ? 210.314 157.909 210.774 1.00 26.99 ? 4471 ALA A O     1 
ATOM   22243 C  CB    . ALA A 1 4471 ? 208.917 160.168 209.042 1.00 23.16 ? 4471 ALA A CB    1 
ATOM   22244 N  N     . GLY A 1 4472 ? 211.805 159.576 210.511 1.00 23.71 ? 4472 GLY A N     1 
ATOM   22245 C  CA    . GLY A 1 4472 ? 212.505 159.286 211.744 1.00 22.98 ? 4472 GLY A CA    1 
ATOM   22246 C  C     . GLY A 1 4472 ? 213.554 158.201 211.660 1.00 28.43 ? 4472 GLY A C     1 
ATOM   22247 O  O     . GLY A 1 4472 ? 213.883 157.602 212.688 1.00 25.59 ? 4472 GLY A O     1 
ATOM   22248 N  N     . MET A 1 4473 ? 214.084 157.927 210.472 1.00 28.58 ? 4473 MET A N     1 
ATOM   22249 C  CA    . MET A 1 4473 ? 215.095 156.891 210.309 1.00 24.36 ? 4473 MET A CA    1 
ATOM   22250 C  C     . MET A 1 4473 ? 216.483 157.494 210.486 1.00 24.15 ? 4473 MET A C     1 
ATOM   22251 O  O     . MET A 1 4473 ? 216.818 158.497 209.849 1.00 28.03 ? 4473 MET A O     1 
ATOM   22252 C  CB    . MET A 1 4473 ? 214.957 156.240 208.933 1.00 20.30 ? 4473 MET A CB    1 
ATOM   22253 C  CG    . MET A 1 4473 ? 216.145 155.414 208.487 1.00 21.32 ? 4473 MET A CG    1 
ATOM   22254 S  SD    . MET A 1 4473 ? 215.827 154.640 206.892 1.00 38.00 ? 4473 MET A SD    1 
ATOM   22255 C  CE    . MET A 1 4473 ? 216.685 153.084 207.085 1.00 16.76 ? 4473 MET A CE    1 
ATOM   22256 N  N     . THR A 1 4474 ? 217.291 156.886 211.352 1.00 18.21 ? 4474 THR A N     1 
ATOM   22257 C  CA    . THR A 1 4474 ? 218.600 157.431 211.677 1.00 18.63 ? 4474 THR A CA    1 
ATOM   22258 C  C     . THR A 1 4474 ? 219.657 156.910 210.705 1.00 21.97 ? 4474 THR A C     1 
ATOM   22259 O  O     . THR A 1 4474 ? 219.408 156.026 209.884 1.00 27.81 ? 4474 THR A O     1 
ATOM   22260 C  CB    . THR A 1 4474 ? 218.975 157.111 213.125 1.00 24.79 ? 4474 THR A CB    1 
ATOM   22261 O  OG1   . THR A 1 4474 ? 220.181 157.804 213.470 1.00 35.34 ? 4474 THR A OG1   1 
ATOM   22262 C  CG2   . THR A 1 4474 ? 219.192 155.626 213.306 1.00 18.22 ? 4474 THR A CG2   1 
ATOM   22263 N  N     . VAL A 1 4475 ? 220.863 157.474 210.803 1.00 23.84 ? 4475 VAL A N     1 
ATOM   22264 C  CA    . VAL A 1 4475 ? 221.904 157.196 209.819 1.00 18.60 ? 4475 VAL A CA    1 
ATOM   22265 C  C     . VAL A 1 4475 ? 222.442 155.772 209.947 1.00 16.93 ? 4475 VAL A C     1 
ATOM   22266 O  O     . VAL A 1 4475 ? 222.851 155.172 208.946 1.00 17.34 ? 4475 VAL A O     1 
ATOM   22267 C  CB    . VAL A 1 4475 ? 223.030 158.243 209.925 1.00 20.36 ? 4475 VAL A CB    1 
ATOM   22268 C  CG1   . VAL A 1 4475 ? 223.823 158.072 211.211 1.00 18.97 ? 4475 VAL A CG1   1 
ATOM   22269 C  CG2   . VAL A 1 4475 ? 223.946 158.171 208.707 1.00 15.55 ? 4475 VAL A CG2   1 
ATOM   22270 N  N     . ILE A 1 4476 ? 222.461 155.206 211.157 1.00 19.13 ? 4476 ILE A N     1 
ATOM   22271 C  CA    . ILE A 1 4476 ? 223.000 153.857 211.318 1.00 15.96 ? 4476 ILE A CA    1 
ATOM   22272 C  C     . ILE A 1 4476 ? 222.097 152.826 210.648 1.00 22.47 ? 4476 ILE A C     1 
ATOM   22273 O  O     . ILE A 1 4476 ? 222.586 151.827 210.106 1.00 24.40 ? 4476 ILE A O     1 
ATOM   22274 C  CB    . ILE A 1 4476 ? 223.240 153.544 212.809 1.00 19.30 ? 4476 ILE A CB    1 
ATOM   22275 C  CG1   . ILE A 1 4476 ? 224.290 152.444 212.959 1.00 19.17 ? 4476 ILE A CG1   1 
ATOM   22276 C  CG2   . ILE A 1 4476 ? 221.951 153.153 213.518 1.00 21.25 ? 4476 ILE A CG2   1 
ATOM   22277 C  CD1   . ILE A 1 4476 ? 224.686 152.174 214.393 1.00 22.00 ? 4476 ILE A CD1   1 
ATOM   22278 N  N     . GLN A 1 4477 ? 220.779 153.046 210.659 1.00 15.63 ? 4477 GLN A N     1 
ATOM   22279 C  CA    . GLN A 1 4477 ? 219.874 152.125 209.980 1.00 18.35 ? 4477 GLN A CA    1 
ATOM   22280 C  C     . GLN A 1 4477 ? 219.924 152.318 208.472 1.00 19.81 ? 4477 GLN A C     1 
ATOM   22281 O  O     . GLN A 1 4477 ? 219.789 151.353 207.712 1.00 20.54 ? 4477 GLN A O     1 
ATOM   22282 C  CB    . GLN A 1 4477 ? 218.444 152.313 210.491 1.00 23.61 ? 4477 GLN A CB    1 
ATOM   22283 C  CG    . GLN A 1 4477 ? 218.336 152.492 211.991 1.00 16.86 ? 4477 GLN A CG    1 
ATOM   22284 C  CD    . GLN A 1 4477 ? 216.902 152.648 212.454 1.00 21.92 ? 4477 GLN A CD    1 
ATOM   22285 O  OE1   . GLN A 1 4477 ? 216.401 153.765 212.585 1.00 21.47 ? 4477 GLN A OE1   1 
ATOM   22286 N  NE2   . GLN A 1 4477 ? 216.235 151.529 212.703 1.00 25.41 ? 4477 GLN A NE2   1 
ATOM   22287 N  N     . TRP A 1 4478 ? 220.110 153.560 208.022 1.00 22.88 ? 4478 TRP A N     1 
ATOM   22288 C  CA    . TRP A 1 4478 ? 220.160 153.833 206.590 1.00 14.94 ? 4478 TRP A CA    1 
ATOM   22289 C  C     . TRP A 1 4478 ? 221.351 153.149 205.931 1.00 15.32 ? 4478 TRP A C     1 
ATOM   22290 O  O     . TRP A 1 4478 ? 221.230 152.618 204.821 1.00 15.79 ? 4478 TRP A O     1 
ATOM   22291 C  CB    . TRP A 1 4478 ? 220.204 155.340 206.346 1.00 11.41 ? 4478 TRP A CB    1 
ATOM   22292 C  CG    . TRP A 1 4478 ? 219.908 155.722 204.934 1.00 13.99 ? 4478 TRP A CG    1 
ATOM   22293 C  CD1   . TRP A 1 4478 ? 218.689 156.017 204.401 1.00 15.18 ? 4478 TRP A CD1   1 
ATOM   22294 C  CD2   . TRP A 1 4478 ? 220.855 155.855 203.870 1.00 12.92 ? 4478 TRP A CD2   1 
ATOM   22295 N  NE1   . TRP A 1 4478 ? 218.818 156.327 203.070 1.00 17.63 ? 4478 TRP A NE1   1 
ATOM   22296 C  CE2   . TRP A 1 4478 ? 220.139 156.235 202.719 1.00 15.12 ? 4478 TRP A CE2   1 
ATOM   22297 C  CE3   . TRP A 1 4478 ? 222.240 155.692 203.776 1.00 14.13 ? 4478 TRP A CE3   1 
ATOM   22298 C  CZ2   . TRP A 1 4478 ? 220.758 156.449 201.493 1.00 17.14 ? 4478 TRP A CZ2   1 
ATOM   22299 C  CZ3   . TRP A 1 4478 ? 222.853 155.906 202.559 1.00 18.49 ? 4478 TRP A CZ3   1 
ATOM   22300 C  CH2   . TRP A 1 4478 ? 222.114 156.281 201.433 1.00 17.44 ? 4478 TRP A CH2   1 
ATOM   22301 N  N     . VAL A 1 4479 ? 222.508 153.154 206.593 1.00 14.15 ? 4479 VAL A N     1 
ATOM   22302 C  CA    . VAL A 1 4479 ? 223.696 152.533 206.012 1.00 15.97 ? 4479 VAL A CA    1 
ATOM   22303 C  C     . VAL A 1 4479 ? 223.474 151.036 205.829 1.00 14.64 ? 4479 VAL A C     1 
ATOM   22304 O  O     . VAL A 1 4479 ? 223.801 150.463 204.783 1.00 22.32 ? 4479 VAL A O     1 
ATOM   22305 C  CB    . VAL A 1 4479 ? 224.936 152.820 206.879 1.00 18.36 ? 4479 VAL A CB    1 
ATOM   22306 C  CG1   . VAL A 1 4479 ? 226.101 151.952 206.442 1.00 18.05 ? 4479 VAL A CG1   1 
ATOM   22307 C  CG2   . VAL A 1 4479 ? 225.308 154.290 206.797 1.00 15.43 ? 4479 VAL A CG2   1 
ATOM   22308 N  N     . SER A 1 4480 ? 222.909 150.380 206.847 1.00 17.48 ? 4480 SER A N     1 
ATOM   22309 C  CA    . SER A 1 4480 ? 222.584 148.963 206.722 1.00 14.20 ? 4480 SER A CA    1 
ATOM   22310 C  C     . SER A 1 4480 ? 221.521 148.733 205.656 1.00 16.54 ? 4480 SER A C     1 
ATOM   22311 O  O     . SER A 1 4480 ? 221.621 147.791 204.860 1.00 23.34 ? 4480 SER A O     1 
ATOM   22312 C  CB    . SER A 1 4480 ? 222.120 148.413 208.069 1.00 17.40 ? 4480 SER A CB    1 
ATOM   22313 O  OG    . SER A 1 4480 ? 221.171 149.275 208.667 1.00 23.78 ? 4480 SER A OG    1 
ATOM   22314 N  N     . ASP A 1 4481 ? 220.492 149.582 205.625 1.00 15.28 ? 4481 ASP A N     1 
ATOM   22315 C  CA    . ASP A 1 4481 ? 219.467 149.464 204.595 1.00 16.12 ? 4481 ASP A CA    1 
ATOM   22316 C  C     . ASP A 1 4481 ? 220.043 149.729 203.208 1.00 18.51 ? 4481 ASP A C     1 
ATOM   22317 O  O     . ASP A 1 4481 ? 219.747 148.996 202.256 1.00 16.67 ? 4481 ASP A O     1 
ATOM   22318 C  CB    . ASP A 1 4481 ? 218.318 150.428 204.892 1.00 12.67 ? 4481 ASP A CB    1 
ATOM   22319 C  CG    . ASP A 1 4481 ? 217.031 150.041 204.188 1.00 20.37 ? 4481 ASP A CG    1 
ATOM   22320 O  OD1   . ASP A 1 4481 ? 217.091 149.296 203.187 1.00 25.80 ? 4481 ASP A OD1   1 
ATOM   22321 O  OD2   . ASP A 1 4481 ? 215.955 150.482 204.640 1.00 28.85 ? 4481 ASP A OD2   1 
ATOM   22322 N  N     . PHE A 1 4482 ? 220.874 150.766 203.078 1.00 17.10 ? 4482 PHE A N     1 
ATOM   22323 C  CA    . PHE A 1 4482 ? 221.454 151.091 201.780 1.00 14.74 ? 4482 PHE A CA    1 
ATOM   22324 C  C     . PHE A 1 4482 ? 222.366 149.980 201.282 1.00 17.67 ? 4482 PHE A C     1 
ATOM   22325 O  O     . PHE A 1 4482 ? 222.436 149.732 200.072 1.00 22.37 ? 4482 PHE A O     1 
ATOM   22326 C  CB    . PHE A 1 4482 ? 222.214 152.414 201.863 1.00 16.38 ? 4482 PHE A CB    1 
ATOM   22327 C  CG    . PHE A 1 4482 ? 222.921 152.790 200.596 1.00 14.82 ? 4482 PHE A CG    1 
ATOM   22328 C  CD1   . PHE A 1 4482 ? 222.204 153.185 199.481 1.00 14.99 ? 4482 PHE A CD1   1 
ATOM   22329 C  CD2   . PHE A 1 4482 ? 224.302 152.753 200.521 1.00 17.62 ? 4482 PHE A CD2   1 
ATOM   22330 C  CE1   . PHE A 1 4482 ? 222.850 153.531 198.313 1.00 17.09 ? 4482 PHE A CE1   1 
ATOM   22331 C  CE2   . PHE A 1 4482 ? 224.954 153.100 199.356 1.00 16.59 ? 4482 PHE A CE2   1 
ATOM   22332 C  CZ    . PHE A 1 4482 ? 224.228 153.489 198.252 1.00 17.90 ? 4482 PHE A CZ    1 
ATOM   22333 N  N     . SER A 1 4483 ? 223.072 149.306 202.190 1.00 16.81 ? 4483 SER A N     1 
ATOM   22334 C  CA    . SER A 1 4483 ? 223.953 148.219 201.781 1.00 18.64 ? 4483 SER A CA    1 
ATOM   22335 C  C     . SER A 1 4483 ? 223.163 147.056 201.187 1.00 19.56 ? 4483 SER A C     1 
ATOM   22336 O  O     . SER A 1 4483 ? 223.584 146.461 200.188 1.00 22.30 ? 4483 SER A O     1 
ATOM   22337 C  CB    . SER A 1 4483 ? 224.792 147.752 202.968 1.00 18.63 ? 4483 SER A CB    1 
ATOM   22338 O  OG    . SER A 1 4483 ? 225.636 146.675 202.603 1.00 32.12 ? 4483 SER A OG    1 
ATOM   22339 N  N     . GLU A 1 4484 ? 222.018 146.720 201.786 1.00 14.53 ? 4484 GLU A N     1 
ATOM   22340 C  CA    . GLU A 1 4484 ? 221.201 145.629 201.261 1.00 15.63 ? 4484 GLU A CA    1 
ATOM   22341 C  C     . GLU A 1 4484 ? 220.649 145.962 199.879 1.00 18.79 ? 4484 GLU A C     1 
ATOM   22342 O  O     . GLU A 1 4484 ? 220.601 145.095 198.999 1.00 17.93 ? 4484 GLU A O     1 
ATOM   22343 C  CB    . GLU A 1 4484 ? 220.059 145.311 202.228 1.00 17.46 ? 4484 GLU A CB    1 
ATOM   22344 C  CG    . GLU A 1 4484 ? 220.466 144.903 203.651 1.00 20.75 ? 4484 GLU A CG    1 
ATOM   22345 C  CD    . GLU A 1 4484 ? 221.754 144.088 203.750 1.00 27.22 ? 4484 GLU A CD    1 
ATOM   22346 O  OE1   . GLU A 1 4484 ? 222.051 143.272 202.851 1.00 26.67 ? 4484 GLU A OE1   1 
ATOM   22347 O  OE2   . GLU A 1 4484 ? 222.478 144.271 204.751 1.00 31.05 ? 4484 GLU A OE2   1 
ATOM   22348 N  N     . ARG A 1 4485 ? 220.218 147.209 199.675 1.00 20.08 ? 4485 ARG A N     1 
ATOM   22349 C  CA    . ARG A 1 4485 ? 219.662 147.599 198.385 1.00 16.59 ? 4485 ARG A CA    1 
ATOM   22350 C  C     . ARG A 1 4485 ? 220.702 147.492 197.277 1.00 19.26 ? 4485 ARG A C     1 
ATOM   22351 O  O     . ARG A 1 4485 ? 220.383 147.091 196.151 1.00 24.02 ? 4485 ARG A O     1 
ATOM   22352 C  CB    . ARG A 1 4485 ? 219.103 149.018 198.461 1.00 15.48 ? 4485 ARG A CB    1 
ATOM   22353 C  CG    . ARG A 1 4485 ? 218.004 149.196 199.494 1.00 13.39 ? 4485 ARG A CG    1 
ATOM   22354 C  CD    . ARG A 1 4485 ? 217.481 150.621 199.514 1.00 16.30 ? 4485 ARG A CD    1 
ATOM   22355 N  NE    . ARG A 1 4485 ? 216.370 150.773 200.444 1.00 16.38 ? 4485 ARG A NE    1 
ATOM   22356 C  CZ    . ARG A 1 4485 ? 215.148 151.155 200.100 1.00 15.93 ? 4485 ARG A CZ    1 
ATOM   22357 N  NH1   . ARG A 1 4485 ? 214.844 151.448 198.847 1.00 14.82 ? 4485 ARG A NH1   1 
ATOM   22358 N  NH2   . ARG A 1 4485 ? 214.210 151.246 201.037 1.00 22.55 ? 4485 ARG A NH2   1 
ATOM   22359 N  N     . ILE A 1 4486 ? 221.952 147.855 197.572 1.00 18.01 ? 4486 ILE A N     1 
ATOM   22360 C  CA    . ILE A 1 4486 ? 222.999 147.797 196.557 1.00 20.14 ? 4486 ILE A CA    1 
ATOM   22361 C  C     . ILE A 1 4486 ? 223.299 146.353 196.175 1.00 21.52 ? 4486 ILE A C     1 
ATOM   22362 O  O     . ILE A 1 4486 ? 223.548 146.050 195.002 1.00 25.75 ? 4486 ILE A O     1 
ATOM   22363 C  CB    . ILE A 1 4486 ? 224.260 148.535 197.044 1.00 19.31 ? 4486 ILE A CB    1 
ATOM   22364 C  CG1   . ILE A 1 4486 ? 223.956 150.017 197.278 1.00 17.51 ? 4486 ILE A CG1   1 
ATOM   22365 C  CG2   . ILE A 1 4486 ? 225.384 148.403 196.035 1.00 20.25 ? 4486 ILE A CG2   1 
ATOM   22366 C  CD1   . ILE A 1 4486 ? 223.362 150.716 196.084 1.00 13.03 ? 4486 ILE A CD1   1 
ATOM   22367 N  N     . LYS A 1 4487 ? 223.276 145.437 197.150 1.00 18.78 ? 4487 LYS A N     1 
ATOM   22368 C  CA    . LYS A 1 4487 ? 223.520 144.028 196.845 1.00 18.59 ? 4487 LYS A CA    1 
ATOM   22369 C  C     . LYS A 1 4487 ? 222.488 143.494 195.859 1.00 21.96 ? 4487 LYS A C     1 
ATOM   22370 O  O     . LYS A 1 4487 ? 222.834 142.808 194.891 1.00 23.93 ? 4487 LYS A O     1 
ATOM   22371 C  CB    . LYS A 1 4487 ? 223.510 143.193 198.127 1.00 18.27 ? 4487 LYS A CB    1 
ATOM   22372 C  CG    . LYS A 1 4487 ? 224.598 143.543 199.128 1.00 22.74 ? 4487 LYS A CG    1 
ATOM   22373 C  CD    . LYS A 1 4487 ? 224.315 142.894 200.473 1.00 20.30 ? 4487 LYS A CD    1 
ATOM   22374 C  CE    . LYS A 1 4487 ? 225.279 143.380 201.545 1.00 26.80 ? 4487 LYS A CE    1 
ATOM   22375 N  NZ    . LYS A 1 4487 ? 226.691 143.026 201.228 1.00 29.76 ? 4487 LYS A NZ    1 
ATOM   22376 N  N     . GLN A 1 4488 ? 221.210 143.807 196.087 1.00 19.81 ? 4488 GLN A N     1 
ATOM   22377 C  CA    . GLN A 1 4488 ? 220.176 143.411 195.139 1.00 17.14 ? 4488 GLN A CA    1 
ATOM   22378 C  C     . GLN A 1 4488 ? 220.394 144.065 193.783 1.00 21.34 ? 4488 GLN A C     1 
ATOM   22379 O  O     . GLN A 1 4488 ? 220.196 143.429 192.739 1.00 20.67 ? 4488 GLN A O     1 
ATOM   22380 C  CB    . GLN A 1 4488 ? 218.795 143.767 195.684 1.00 17.58 ? 4488 GLN A CB    1 
ATOM   22381 C  CG    . GLN A 1 4488 ? 217.684 143.519 194.680 1.00 19.14 ? 4488 GLN A CG    1 
ATOM   22382 C  CD    . GLN A 1 4488 ? 216.321 143.441 195.315 1.00 15.75 ? 4488 GLN A CD    1 
ATOM   22383 O  OE1   . GLN A 1 4488 ? 215.521 142.561 195.001 1.00 22.26 ? 4488 GLN A OE1   1 
ATOM   22384 N  NE2   . GLN A 1 4488 ? 216.050 144.361 196.227 1.00 14.10 ? 4488 GLN A NE2   1 
ATOM   22385 N  N     . LEU A 1 4489 ? 220.802 145.334 193.778 1.00 23.47 ? 4489 LEU A N     1 
ATOM   22386 C  CA    . LEU A 1 4489 ? 221.081 146.017 192.520 1.00 16.33 ? 4489 LEU A CA    1 
ATOM   22387 C  C     . LEU A 1 4489 ? 222.222 145.340 191.773 1.00 24.10 ? 4489 LEU A C     1 
ATOM   22388 O  O     . LEU A 1 4489 ? 222.190 145.231 190.541 1.00 28.31 ? 4489 LEU A O     1 
ATOM   22389 C  CB    . LEU A 1 4489 ? 221.403 147.486 192.788 1.00 16.34 ? 4489 LEU A CB    1 
ATOM   22390 C  CG    . LEU A 1 4489 ? 220.209 148.382 193.112 1.00 17.95 ? 4489 LEU A CG    1 
ATOM   22391 C  CD1   . LEU A 1 4489 ? 220.667 149.655 193.806 1.00 17.82 ? 4489 LEU A CD1   1 
ATOM   22392 C  CD2   . LEU A 1 4489 ? 219.415 148.709 191.858 1.00 17.65 ? 4489 LEU A CD2   1 
ATOM   22393 N  N     . GLN A 1 4490 ? 223.243 144.881 192.502 1.00 19.85 ? 4490 GLN A N     1 
ATOM   22394 C  CA    . GLN A 1 4490 ? 224.348 144.169 191.866 1.00 22.86 ? 4490 GLN A CA    1 
ATOM   22395 C  C     . GLN A 1 4490 ? 223.878 142.871 191.226 1.00 24.08 ? 4490 GLN A C     1 
ATOM   22396 O  O     . GLN A 1 4490 ? 224.275 142.546 190.101 1.00 25.45 ? 4490 GLN A O     1 
ATOM   22397 C  CB    . GLN A 1 4490 ? 225.448 143.885 192.887 1.00 24.69 ? 4490 GLN A CB    1 
ATOM   22398 C  CG    . GLN A 1 4490 ? 226.289 145.086 193.253 1.00 22.44 ? 4490 GLN A CG    1 
ATOM   22399 C  CD    . GLN A 1 4490 ? 227.257 144.783 194.373 1.00 27.24 ? 4490 GLN A CD    1 
ATOM   22400 O  OE1   . GLN A 1 4490 ? 227.211 143.712 194.975 1.00 25.67 ? 4490 GLN A OE1   1 
ATOM   22401 N  NE2   . GLN A 1 4490 ? 228.152 145.722 194.649 1.00 32.38 ? 4490 GLN A NE2   1 
ATOM   22402 N  N     . ASN A 1 4491 ? 223.033 142.111 191.929 1.00 20.90 ? 4491 ASN A N     1 
ATOM   22403 C  CA    . ASN A 1 4491 ? 222.566 140.837 191.392 1.00 20.71 ? 4491 ASN A CA    1 
ATOM   22404 C  C     . ASN A 1 4491 ? 221.728 141.041 190.139 1.00 18.92 ? 4491 ASN A C     1 
ATOM   22405 O  O     . ASN A 1 4491 ? 221.830 140.262 189.183 1.00 21.82 ? 4491 ASN A O     1 
ATOM   22406 C  CB    . ASN A 1 4491 ? 221.773 140.079 192.454 1.00 17.89 ? 4491 ASN A CB    1 
ATOM   22407 C  CG    . ASN A 1 4491 ? 222.543 139.912 193.748 1.00 21.50 ? 4491 ASN A CG    1 
ATOM   22408 O  OD1   . ASN A 1 4491 ? 223.706 140.303 193.847 1.00 21.49 ? 4491 ASN A OD1   1 
ATOM   22409 N  ND2   . ASN A 1 4491 ? 221.897 139.335 194.752 1.00 25.61 ? 4491 ASN A ND2   1 
ATOM   22410 N  N     . ILE A 1 4492 ? 220.892 142.080 190.127 1.00 23.97 ? 4492 ILE A N     1 
ATOM   22411 C  CA    . ILE A 1 4492 ? 220.069 142.369 188.955 1.00 19.27 ? 4492 ILE A CA    1 
ATOM   22412 C  C     . ILE A 1 4492 ? 220.949 142.693 187.754 1.00 24.09 ? 4492 ILE A C     1 
ATOM   22413 O  O     . ILE A 1 4492 ? 220.714 142.200 186.643 1.00 26.62 ? 4492 ILE A O     1 
ATOM   22414 C  CB    . ILE A 1 4492 ? 219.088 143.512 189.270 1.00 19.87 ? 4492 ILE A CB    1 
ATOM   22415 C  CG1   . ILE A 1 4492 ? 218.086 143.071 190.339 1.00 18.69 ? 4492 ILE A CG1   1 
ATOM   22416 C  CG2   . ILE A 1 4492 ? 218.359 143.953 188.017 1.00 19.08 ? 4492 ILE A CG2   1 
ATOM   22417 C  CD1   . ILE A 1 4492 ? 217.238 144.198 190.877 1.00 17.61 ? 4492 ILE A CD1   1 
ATOM   22418 N  N     . SER A 1 4493 ? 221.975 143.521 187.957 1.00 26.95 ? 4493 SER A N     1 
ATOM   22419 C  CA    . SER A 1 4493 ? 222.878 143.863 186.863 1.00 22.98 ? 4493 SER A CA    1 
ATOM   22420 C  C     . SER A 1 4493 ? 223.727 142.668 186.448 1.00 27.04 ? 4493 SER A C     1 
ATOM   22421 O  O     . SER A 1 4493 ? 224.058 142.515 185.266 1.00 29.96 ? 4493 SER A O     1 
ATOM   22422 C  CB    . SER A 1 4493 ? 223.765 145.041 187.262 1.00 26.29 ? 4493 SER A CB    1 
ATOM   22423 O  OG    . SER A 1 4493 ? 224.649 145.391 186.213 1.00 30.58 ? 4493 SER A OG    1 
ATOM   22424 N  N     . LEU A 1 4494 ? 224.101 141.817 187.407 1.00 25.87 ? 4494 LEU A N     1 
ATOM   22425 C  CA    . LEU A 1 4494 ? 224.879 140.626 187.076 1.00 23.39 ? 4494 LEU A CA    1 
ATOM   22426 C  C     . LEU A 1 4494 ? 224.091 139.687 186.173 1.00 29.62 ? 4494 LEU A C     1 
ATOM   22427 O  O     . LEU A 1 4494 ? 224.639 139.123 185.218 1.00 32.37 ? 4494 LEU A O     1 
ATOM   22428 C  CB    . LEU A 1 4494 ? 225.310 139.909 188.356 1.00 26.40 ? 4494 LEU A CB    1 
ATOM   22429 C  CG    . LEU A 1 4494 ? 226.061 138.587 188.196 1.00 24.92 ? 4494 LEU A CG    1 
ATOM   22430 C  CD1   . LEU A 1 4494 ? 227.255 138.748 187.263 1.00 28.38 ? 4494 LEU A CD1   1 
ATOM   22431 C  CD2   . LEU A 1 4494 ? 226.505 138.058 189.549 1.00 17.84 ? 4494 LEU A CD2   1 
ATOM   22432 N  N     . ALA A 1 4495 ? 222.801 139.499 186.463 1.00 26.59 ? 4495 ALA A N     1 
ATOM   22433 C  CA    . ALA A 1 4495 ? 221.966 138.669 185.605 1.00 25.76 ? 4495 ALA A CA    1 
ATOM   22434 C  C     . ALA A 1 4495 ? 221.844 139.265 184.208 1.00 28.11 ? 4495 ALA A C     1 
ATOM   22435 O  O     . ALA A 1 4495 ? 221.937 138.546 183.206 1.00 33.36 ? 4495 ALA A O     1 
ATOM   22436 C  CB    . ALA A 1 4495 ? 220.585 138.487 186.233 1.00 24.79 ? 4495 ALA A CB    1 
ATOM   22437 N  N     . ALA A 1 4496 ? 221.637 140.582 184.121 1.00 29.32 ? 4496 ALA A N     1 
ATOM   22438 C  CA    . ALA A 1 4496 ? 221.544 141.232 182.818 1.00 26.09 ? 4496 ALA A CA    1 
ATOM   22439 C  C     . ALA A 1 4496 ? 222.869 141.162 182.069 1.00 28.62 ? 4496 ALA A C     1 
ATOM   22440 O  O     . ALA A 1 4496 ? 222.890 140.939 180.853 1.00 28.96 ? 4496 ALA A O     1 
ATOM   22441 C  CB    . ALA A 1 4496 ? 221.096 142.683 182.984 1.00 24.03 ? 4496 ALA A CB    1 
ATOM   22442 N  N     . ALA A 1 4497 ? 223.984 141.358 182.775 1.00 27.58 ? 4497 ALA A N     1 
ATOM   22443 C  CA    . ALA A 1 4497 ? 225.292 141.267 182.132 1.00 28.87 ? 4497 ALA A CA    1 
ATOM   22444 C  C     . ALA A 1 4497 ? 225.601 139.834 181.713 1.00 28.97 ? 4497 ALA A C     1 
ATOM   22445 O  O     . ALA A 1 4497 ? 226.080 139.592 180.600 1.00 29.55 ? 4497 ALA A O     1 
ATOM   22446 C  CB    . ALA A 1 4497 ? 226.377 141.803 183.066 1.00 26.95 ? 4497 ALA A CB    1 
ATOM   22447 N  N     . SER A 1 4498 ? 225.333 138.872 182.592 1.00 27.46 ? 4498 SER A N     1 
ATOM   22448 C  CA    . SER A 1 4498 ? 225.595 137.460 182.332 1.00 28.61 ? 4498 SER A CA    1 
ATOM   22449 C  C     . SER A 1 4498 ? 224.257 136.738 182.209 1.00 29.30 ? 4498 SER A C     1 
ATOM   22450 O  O     . SER A 1 4498 ? 223.678 136.308 183.210 1.00 31.91 ? 4498 SER A O     1 
ATOM   22451 C  CB    . SER A 1 4498 ? 226.455 136.852 183.437 1.00 29.51 ? 4498 SER A CB    1 
ATOM   22452 O  OG    . SER A 1 4498 ? 227.674 137.561 183.581 1.00 37.99 ? 4498 SER A OG    1 
ATOM   22453 N  N     . GLY A 1 4499 ? 223.772 136.601 180.973 1.00 31.00 ? 4499 GLY A N     1 
ATOM   22454 C  CA    . GLY A 1 4499 ? 222.508 135.945 180.681 1.00 30.52 ? 4499 GLY A CA    1 
ATOM   22455 C  C     . GLY A 1 4499 ? 221.551 136.804 179.879 1.00 30.64 ? 4499 GLY A C     1 
ATOM   22456 O  O     . GLY A 1 4499 ? 220.729 136.269 179.127 1.00 35.96 ? 4499 GLY A O     1 
ATOM   22457 N  N     . GLY A 1 4500 ? 221.641 138.121 180.023 1.00 28.47 ? 4500 GLY A N     1 
ATOM   22458 C  CA    . GLY A 1 4500 ? 220.809 139.039 179.268 1.00 28.16 ? 4500 GLY A CA    1 
ATOM   22459 C  C     . GLY A 1 4500 ? 219.633 139.551 180.078 1.00 34.09 ? 4500 GLY A C     1 
ATOM   22460 O  O     . GLY A 1 4500 ? 219.401 139.168 181.229 1.00 34.61 ? 4500 GLY A O     1 
ATOM   22461 N  N     . ALA A 1 4501 ? 218.872 140.441 179.439 1.00 24.32 ? 4501 ALA A N     1 
ATOM   22462 C  CA    . ALA A 1 4501 ? 217.711 141.039 180.086 1.00 31.33 ? 4501 ALA A CA    1 
ATOM   22463 C  C     . ALA A 1 4501 ? 216.600 140.028 180.342 1.00 33.75 ? 4501 ALA A C     1 
ATOM   22464 O  O     . ALA A 1 4501 ? 215.691 140.313 181.127 1.00 33.80 ? 4501 ALA A O     1 
ATOM   22465 C  CB    . ALA A 1 4501 ? 217.174 142.198 179.244 1.00 28.41 ? 4501 ALA A CB    1 
ATOM   22466 N  N     . LYS A 1 4502 ? 216.647 138.860 179.696 1.00 30.22 ? 4502 LYS A N     1 
ATOM   22467 C  CA    . LYS A 1 4502 ? 215.648 137.830 179.946 1.00 27.42 ? 4502 LYS A CA    1 
ATOM   22468 C  C     . LYS A 1 4502 ? 215.758 137.247 181.348 1.00 31.94 ? 4502 LYS A C     1 
ATOM   22469 O  O     . LYS A 1 4502 ? 214.776 136.692 181.854 1.00 29.20 ? 4502 LYS A O     1 
ATOM   22470 C  CB    . LYS A 1 4502 ? 215.768 136.715 178.907 1.00 28.05 ? 4502 LYS A CB    1 
ATOM   22471 C  CG    . LYS A 1 4502 ? 217.097 135.980 178.935 1.00 28.69 ? 4502 LYS A CG    1 
ATOM   22472 C  CD    . LYS A 1 4502 ? 217.053 134.722 178.082 1.00 29.22 ? 4502 LYS A CD    1 
ATOM   22473 C  CE    . LYS A 1 4502 ? 218.340 133.925 178.206 1.00 29.77 ? 4502 LYS A CE    1 
ATOM   22474 N  NZ    . LYS A 1 4502 ? 218.296 132.671 177.405 1.00 26.26 ? 4502 LYS A NZ    1 
ATOM   22475 N  N     . GLU A 1 4503 ? 216.926 137.351 181.984 1.00 29.62 ? 4503 GLU A N     1 
ATOM   22476 C  CA    . GLU A 1 4503 ? 217.087 136.877 183.352 1.00 25.75 ? 4503 GLU A CA    1 
ATOM   22477 C  C     . GLU A 1 4503 ? 216.445 137.803 184.376 1.00 24.70 ? 4503 GLU A C     1 
ATOM   22478 O  O     . GLU A 1 4503 ? 216.350 137.428 185.549 1.00 28.42 ? 4503 GLU A O     1 
ATOM   22479 C  CB    . GLU A 1 4503 ? 218.573 136.699 183.675 1.00 25.84 ? 4503 GLU A CB    1 
ATOM   22480 C  CG    . GLU A 1 4503 ? 219.371 136.012 182.577 1.00 31.54 ? 4503 GLU A CG    1 
ATOM   22481 C  CD    . GLU A 1 4503 ? 219.120 134.517 182.510 1.00 35.91 ? 4503 GLU A CD    1 
ATOM   22482 O  OE1   . GLU A 1 4503 ? 218.434 133.984 183.409 1.00 32.05 ? 4503 GLU A OE1   1 
ATOM   22483 O  OE2   . GLU A 1 4503 ? 219.612 133.874 181.558 1.00 35.02 ? 4503 GLU A OE2   1 
ATOM   22484 N  N     . LEU A 1 4504 ? 216.014 138.998 183.966 1.00 18.52 ? 4504 LEU A N     1 
ATOM   22485 C  CA    . LEU A 1 4504 ? 215.323 139.902 184.878 1.00 24.14 ? 4504 LEU A CA    1 
ATOM   22486 C  C     . LEU A 1 4504 ? 213.990 139.336 185.346 1.00 25.12 ? 4504 LEU A C     1 
ATOM   22487 O  O     . LEU A 1 4504 ? 213.533 139.679 186.442 1.00 26.16 ? 4504 LEU A O     1 
ATOM   22488 C  CB    . LEU A 1 4504 ? 215.098 141.257 184.204 1.00 26.62 ? 4504 LEU A CB    1 
ATOM   22489 C  CG    . LEU A 1 4504 ? 216.343 142.044 183.786 1.00 26.78 ? 4504 LEU A CG    1 
ATOM   22490 C  CD1   . LEU A 1 4504 ? 215.945 143.351 183.119 1.00 26.85 ? 4504 LEU A CD1   1 
ATOM   22491 C  CD2   . LEU A 1 4504 ? 217.246 142.296 184.978 1.00 18.13 ? 4504 LEU A CD2   1 
ATOM   22492 N  N     . LYS A 1 4505 ? 213.360 138.482 184.539 1.00 26.12 ? 4505 LYS A N     1 
ATOM   22493 C  CA    . LYS A 1 4505 ? 212.053 137.934 184.885 1.00 23.24 ? 4505 LYS A CA    1 
ATOM   22494 C  C     . LYS A 1 4505 ? 212.148 136.832 185.933 1.00 23.64 ? 4505 LYS A C     1 
ATOM   22495 O  O     . LYS A 1 4505 ? 211.235 136.685 186.753 1.00 31.32 ? 4505 LYS A O     1 
ATOM   22496 C  CB    . LYS A 1 4505 ? 211.366 137.414 183.618 1.00 17.77 ? 4505 LYS A CB    1 
ATOM   22497 C  CG    . LYS A 1 4505 ? 209.975 136.837 183.819 1.00 19.89 ? 4505 LYS A CG    1 
ATOM   22498 C  CD    . LYS A 1 4505 ? 210.001 135.323 183.913 1.00 21.33 ? 4505 LYS A CD    1 
ATOM   22499 C  CE    . LYS A 1 4505 ? 208.796 134.800 184.664 1.00 23.09 ? 4505 LYS A CE    1 
ATOM   22500 N  NZ    . LYS A 1 4505 ? 208.912 133.343 184.941 1.00 29.22 ? 4505 LYS A NZ    1 
ATOM   22501 N  N     . ASN A 1 4506 ? 213.226 136.056 185.928 1.00 21.08 ? 4506 ASN A N     1 
ATOM   22502 C  CA    . ASN A 1 4506 ? 213.328 134.866 186.761 1.00 25.98 ? 4506 ASN A CA    1 
ATOM   22503 C  C     . ASN A 1 4506 ? 213.897 135.171 188.145 1.00 22.50 ? 4506 ASN A C     1 
ATOM   22504 O  O     . ASN A 1 4506 ? 213.816 134.322 189.038 1.00 20.54 ? 4506 ASN A O     1 
ATOM   22505 C  CB    . ASN A 1 4506 ? 214.192 133.819 186.038 1.00 21.35 ? 4506 ASN A CB    1 
ATOM   22506 C  CG    . ASN A 1 4506 ? 214.114 132.435 186.664 1.00 29.07 ? 4506 ASN A CG    1 
ATOM   22507 O  OD1   . ASN A 1 4506 ? 213.413 132.213 187.650 1.00 35.45 ? 4506 ASN A OD1   1 
ATOM   22508 N  ND2   . ASN A 1 4506 ? 214.844 131.491 186.082 1.00 30.04 ? 4506 ASN A ND2   1 
ATOM   22509 N  N     . ILE A 1 4507 ? 214.441 136.363 188.357 1.00 22.25 ? 4507 ILE A N     1 
ATOM   22510 C  CA    . ILE A 1 4507 ? 215.070 136.712 189.625 1.00 20.56 ? 4507 ILE A CA    1 
ATOM   22511 C  C     . ILE A 1 4507 ? 214.008 137.172 190.616 1.00 23.65 ? 4507 ILE A C     1 
ATOM   22512 O  O     . ILE A 1 4507 ? 213.095 137.929 190.264 1.00 21.94 ? 4507 ILE A O     1 
ATOM   22513 C  CB    . ILE A 1 4507 ? 216.161 137.782 189.428 1.00 17.66 ? 4507 ILE A CB    1 
ATOM   22514 C  CG1   . ILE A 1 4507 ? 217.016 137.912 190.691 1.00 19.98 ? 4507 ILE A CG1   1 
ATOM   22515 C  CG2   . ILE A 1 4507 ? 215.570 139.126 189.022 1.00 12.50 ? 4507 ILE A CG2   1 
ATOM   22516 C  CD1   . ILE A 1 4507 ? 217.831 136.681 191.007 1.00 19.38 ? 4507 ILE A CD1   1 
ATOM   22517 N  N     . HIS A 1 4508 ? 214.108 136.683 191.850 1.00 21.06 ? 4508 HIS A N     1 
ATOM   22518 C  CA    . HIS A 1 4508 ? 213.216 137.132 192.909 1.00 18.41 ? 4508 HIS A CA    1 
ATOM   22519 C  C     . HIS A 1 4508 ? 213.627 138.518 193.388 1.00 22.74 ? 4508 HIS A C     1 
ATOM   22520 O  O     . HIS A 1 4508 ? 214.816 138.840 193.464 1.00 24.23 ? 4508 HIS A O     1 
ATOM   22521 C  CB    . HIS A 1 4508 ? 213.227 136.144 194.073 1.00 18.13 ? 4508 HIS A CB    1 
ATOM   22522 C  CG    . HIS A 1 4508 ? 212.793 134.764 193.695 1.00 16.76 ? 4508 HIS A CG    1 
ATOM   22523 N  ND1   . HIS A 1 4508 ? 213.104 133.653 194.450 1.00 20.07 ? 4508 HIS A ND1   1 
ATOM   22524 C  CD2   . HIS A 1 4508 ? 212.074 134.313 192.641 1.00 16.55 ? 4508 HIS A CD2   1 
ATOM   22525 C  CE1   . HIS A 1 4508 ? 212.591 132.577 193.879 1.00 21.30 ? 4508 HIS A CE1   1 
ATOM   22526 N  NE2   . HIS A 1 4508 ? 211.961 132.950 192.779 1.00 23.53 ? 4508 HIS A NE2   1 
ATOM   22527 N  N     . VAL A 1 4509 ? 212.634 139.340 193.720 1.00 19.46 ? 4509 VAL A N     1 
ATOM   22528 C  CA    . VAL A 1 4509 ? 212.845 140.752 194.003 1.00 17.72 ? 4509 VAL A CA    1 
ATOM   22529 C  C     . VAL A 1 4509 ? 212.314 141.067 195.394 1.00 19.72 ? 4509 VAL A C     1 
ATOM   22530 O  O     . VAL A 1 4509 ? 211.188 140.690 195.736 1.00 24.29 ? 4509 VAL A O     1 
ATOM   22531 C  CB    . VAL A 1 4509 ? 212.167 141.644 192.946 1.00 19.99 ? 4509 VAL A CB    1 
ATOM   22532 C  CG1   . VAL A 1 4509 ? 211.933 143.035 193.492 1.00 14.26 ? 4509 VAL A CG1   1 
ATOM   22533 C  CG2   . VAL A 1 4509 ? 213.006 141.696 191.678 1.00 23.83 ? 4509 VAL A CG2   1 
ATOM   22534 N  N     . CYS A 1 4510 ? 213.129 141.749 196.195 1.00 15.83 ? 4510 CYS A N     1 
ATOM   22535 C  CA    . CYS A 1 4510 ? 212.686 142.339 197.452 1.00 13.31 ? 4510 CYS A CA    1 
ATOM   22536 C  C     . CYS A 1 4510 ? 212.124 143.722 197.150 1.00 14.34 ? 4510 CYS A C     1 
ATOM   22537 O  O     . CYS A 1 4510 ? 212.877 144.653 196.844 1.00 15.71 ? 4510 CYS A O     1 
ATOM   22538 C  CB    . CYS A 1 4510 ? 213.837 142.413 198.451 1.00 14.28 ? 4510 CYS A CB    1 
ATOM   22539 S  SG    . CYS A 1 4510 ? 213.387 143.069 200.070 1.00 34.97 ? 4510 CYS A SG    1 
ATOM   22540 N  N     . LEU A 1 4511 ? 210.797 143.856 197.228 1.00 16.60 ? 4511 LEU A N     1 
ATOM   22541 C  CA    . LEU A 1 4511 ? 210.158 145.121 196.877 1.00 12.03 ? 4511 LEU A CA    1 
ATOM   22542 C  C     . LEU A 1 4511 ? 210.600 146.254 197.791 1.00 11.26 ? 4511 LEU A C     1 
ATOM   22543 O  O     . LEU A 1 4511 ? 210.649 147.412 197.363 1.00 15.16 ? 4511 LEU A O     1 
ATOM   22544 C  CB    . LEU A 1 4511 ? 208.639 144.973 196.918 1.00 12.13 ? 4511 LEU A CB    1 
ATOM   22545 C  CG    . LEU A 1 4511 ? 207.975 144.583 195.600 1.00 10.91 ? 4511 LEU A CG    1 
ATOM   22546 C  CD1   . LEU A 1 4511 ? 206.477 144.452 195.783 1.00 9.65  ? 4511 LEU A CD1   1 
ATOM   22547 C  CD2   . LEU A 1 4511 ? 208.305 145.595 194.516 1.00 16.64 ? 4511 LEU A CD2   1 
ATOM   22548 N  N     . GLY A 1 4512 ? 210.917 145.947 199.049 1.00 14.87 ? 4512 GLY A N     1 
ATOM   22549 C  CA    . GLY A 1 4512 ? 211.407 146.980 199.945 1.00 12.25 ? 4512 GLY A CA    1 
ATOM   22550 C  C     . GLY A 1 4512 ? 212.722 147.574 199.484 1.00 12.60 ? 4512 GLY A C     1 
ATOM   22551 O  O     . GLY A 1 4512 ? 212.939 148.784 199.586 1.00 17.05 ? 4512 GLY A O     1 
ATOM   22552 N  N     . GLY A 1 4513 ? 213.618 146.730 198.964 1.00 14.70 ? 4513 GLY A N     1 
ATOM   22553 C  CA    . GLY A 1 4513 ? 214.910 147.211 198.509 1.00 12.14 ? 4513 GLY A CA    1 
ATOM   22554 C  C     . GLY A 1 4513 ? 214.831 148.131 197.308 1.00 15.77 ? 4513 GLY A C     1 
ATOM   22555 O  O     . GLY A 1 4513 ? 215.652 149.043 197.170 1.00 18.53 ? 4513 GLY A O     1 
ATOM   22556 N  N     . LEU A 1 4514 ? 213.861 147.908 196.423 1.00 14.07 ? 4514 LEU A N     1 
ATOM   22557 C  CA    . LEU A 1 4514 ? 213.754 148.714 195.216 1.00 15.98 ? 4514 LEU A CA    1 
ATOM   22558 C  C     . LEU A 1 4514 ? 213.472 150.171 195.557 1.00 15.95 ? 4514 LEU A C     1 
ATOM   22559 O  O     . LEU A 1 4514 ? 212.743 150.479 196.502 1.00 18.27 ? 4514 LEU A O     1 
ATOM   22560 C  CB    . LEU A 1 4514 ? 212.655 148.174 194.303 1.00 17.77 ? 4514 LEU A CB    1 
ATOM   22561 C  CG    . LEU A 1 4514 ? 212.882 146.795 193.690 1.00 19.48 ? 4514 LEU A CG    1 
ATOM   22562 C  CD1   . LEU A 1 4514 ? 211.749 146.472 192.743 1.00 15.55 ? 4514 LEU A CD1   1 
ATOM   22563 C  CD2   . LEU A 1 4514 ? 214.222 146.737 192.977 1.00 17.66 ? 4514 LEU A CD2   1 
ATOM   22564 N  N     . PHE A 1 4515 ? 214.061 151.071 194.768 1.00 16.05 ? 4515 PHE A N     1 
ATOM   22565 C  CA    . PHE A 1 4515 ? 213.895 152.497 195.023 1.00 17.99 ? 4515 PHE A CA    1 
ATOM   22566 C  C     . PHE A 1 4515 ? 212.489 152.961 194.661 1.00 19.67 ? 4515 PHE A C     1 
ATOM   22567 O  O     . PHE A 1 4515 ? 211.926 153.834 195.331 1.00 20.22 ? 4515 PHE A O     1 
ATOM   22568 C  CB    . PHE A 1 4515 ? 214.945 153.286 194.243 1.00 20.05 ? 4515 PHE A CB    1 
ATOM   22569 C  CG    . PHE A 1 4515 ? 216.344 153.091 194.752 1.00 20.66 ? 4515 PHE A CG    1 
ATOM   22570 C  CD1   . PHE A 1 4515 ? 216.573 152.753 196.075 1.00 20.29 ? 4515 PHE A CD1   1 
ATOM   22571 C  CD2   . PHE A 1 4515 ? 217.428 153.238 193.907 1.00 20.57 ? 4515 PHE A CD2   1 
ATOM   22572 C  CE1   . PHE A 1 4515 ? 217.858 152.564 196.542 1.00 19.58 ? 4515 PHE A CE1   1 
ATOM   22573 C  CE2   . PHE A 1 4515 ? 218.713 153.054 194.372 1.00 22.44 ? 4515 PHE A CE2   1 
ATOM   22574 C  CZ    . PHE A 1 4515 ? 218.931 152.719 195.692 1.00 21.87 ? 4515 PHE A CZ    1 
ATOM   22575 N  N     . VAL A 1 4516 ? 211.912 152.396 193.605 1.00 20.18 ? 4516 VAL A N     1 
ATOM   22576 C  CA    . VAL A 1 4516 ? 210.538 152.694 193.200 1.00 19.24 ? 4516 VAL A CA    1 
ATOM   22577 C  C     . VAL A 1 4516 ? 209.778 151.379 193.068 1.00 19.24 ? 4516 VAL A C     1 
ATOM   22578 O  O     . VAL A 1 4516 ? 209.635 150.856 191.955 1.00 20.14 ? 4516 VAL A O     1 
ATOM   22579 C  CB    . VAL A 1 4516 ? 210.493 153.493 191.887 1.00 20.41 ? 4516 VAL A CB    1 
ATOM   22580 C  CG1   . VAL A 1 4516 ? 209.103 154.060 191.665 1.00 22.88 ? 4516 VAL A CG1   1 
ATOM   22581 C  CG2   . VAL A 1 4516 ? 211.528 154.608 191.894 1.00 19.55 ? 4516 VAL A CG2   1 
ATOM   22582 N  N     . PRO A 1 4517 ? 209.293 150.805 194.171 1.00 19.78 ? 4517 PRO A N     1 
ATOM   22583 C  CA    . PRO A 1 4517 ? 208.575 149.522 194.074 1.00 17.84 ? 4517 PRO A CA    1 
ATOM   22584 C  C     . PRO A 1 4517 ? 207.302 149.586 193.246 1.00 18.55 ? 4517 PRO A C     1 
ATOM   22585 O  O     . PRO A 1 4517 ? 206.911 148.572 192.656 1.00 18.05 ? 4517 PRO A O     1 
ATOM   22586 C  CB    . PRO A 1 4517 ? 208.282 149.177 195.540 1.00 11.67 ? 4517 PRO A CB    1 
ATOM   22587 C  CG    . PRO A 1 4517 ? 208.341 150.481 196.257 1.00 16.12 ? 4517 PRO A CG    1 
ATOM   22588 C  CD    . PRO A 1 4517 ? 209.384 151.287 195.559 1.00 13.77 ? 4517 PRO A CD    1 
ATOM   22589 N  N     . GLU A 1 4518 ? 206.635 150.743 193.186 1.00 15.65 ? 4518 GLU A N     1 
ATOM   22590 C  CA    . GLU A 1 4518 ? 205.414 150.847 192.394 1.00 17.71 ? 4518 GLU A CA    1 
ATOM   22591 C  C     . GLU A 1 4518 ? 205.699 150.643 190.911 1.00 20.39 ? 4518 GLU A C     1 
ATOM   22592 O  O     . GLU A 1 4518 ? 204.911 150.011 190.199 1.00 20.18 ? 4518 GLU A O     1 
ATOM   22593 C  CB    . GLU A 1 4518 ? 204.744 152.202 192.624 1.00 19.06 ? 4518 GLU A CB    1 
ATOM   22594 C  CG    . GLU A 1 4518 ? 204.695 152.635 194.074 1.00 20.36 ? 4518 GLU A CG    1 
ATOM   22595 C  CD    . GLU A 1 4518 ? 205.815 153.592 194.430 1.00 24.95 ? 4518 GLU A CD    1 
ATOM   22596 O  OE1   . GLU A 1 4518 ? 206.988 153.261 194.156 1.00 26.35 ? 4518 GLU A OE1   1 
ATOM   22597 O  OE2   . GLU A 1 4518 ? 205.522 154.673 194.981 1.00 35.12 ? 4518 GLU A OE2   1 
ATOM   22598 N  N     . ALA A 1 4519 ? 206.824 151.179 190.428 1.00 21.26 ? 4519 ALA A N     1 
ATOM   22599 C  CA    . ALA A 1 4519 ? 207.170 151.042 189.019 1.00 16.64 ? 4519 ALA A CA    1 
ATOM   22600 C  C     . ALA A 1 4519 ? 207.432 149.590 188.639 1.00 15.73 ? 4519 ALA A C     1 
ATOM   22601 O  O     . ALA A 1 4519 ? 207.140 149.188 187.508 1.00 22.29 ? 4519 ALA A O     1 
ATOM   22602 C  CB    . ALA A 1 4519 ? 208.386 151.907 188.696 1.00 15.91 ? 4519 ALA A CB    1 
ATOM   22603 N  N     . TYR A 1 4520 ? 207.983 148.793 189.559 1.00 17.13 ? 4520 TYR A N     1 
ATOM   22604 C  CA    . TYR A 1 4520 ? 208.186 147.375 189.283 1.00 11.99 ? 4520 TYR A CA    1 
ATOM   22605 C  C     . TYR A 1 4520 ? 206.856 146.662 189.072 1.00 15.67 ? 4520 TYR A C     1 
ATOM   22606 O  O     . TYR A 1 4520 ? 206.740 145.794 188.200 1.00 20.06 ? 4520 TYR A O     1 
ATOM   22607 C  CB    . TYR A 1 4520 ? 208.968 146.725 190.422 1.00 13.23 ? 4520 TYR A CB    1 
ATOM   22608 C  CG    . TYR A 1 4520 ? 209.141 145.228 190.288 1.00 14.26 ? 4520 TYR A CG    1 
ATOM   22609 C  CD1   . TYR A 1 4520 ? 210.114 144.692 189.456 1.00 14.45 ? 4520 TYR A CD1   1 
ATOM   22610 C  CD2   . TYR A 1 4520 ? 208.339 144.350 191.008 1.00 14.07 ? 4520 TYR A CD2   1 
ATOM   22611 C  CE1   . TYR A 1 4520 ? 210.277 143.329 189.335 1.00 13.81 ? 4520 TYR A CE1   1 
ATOM   22612 C  CE2   . TYR A 1 4520 ? 208.497 142.986 190.893 1.00 14.74 ? 4520 TYR A CE2   1 
ATOM   22613 C  CZ    . TYR A 1 4520 ? 209.467 142.479 190.055 1.00 15.99 ? 4520 TYR A CZ    1 
ATOM   22614 O  OH    . TYR A 1 4520 ? 209.628 141.119 189.936 1.00 19.76 ? 4520 TYR A OH    1 
ATOM   22615 N  N     . ILE A 1 4521 ? 205.841 147.016 189.863 1.00 15.43 ? 4521 ILE A N     1 
ATOM   22616 C  CA    . ILE A 1 4521 ? 204.524 146.411 189.705 1.00 12.39 ? 4521 ILE A CA    1 
ATOM   22617 C  C     . ILE A 1 4521 ? 203.956 146.738 188.331 1.00 16.65 ? 4521 ILE A C     1 
ATOM   22618 O  O     . ILE A 1 4521 ? 203.394 145.871 187.650 1.00 20.54 ? 4521 ILE A O     1 
ATOM   22619 C  CB    . ILE A 1 4521 ? 203.585 146.876 190.835 1.00 16.10 ? 4521 ILE A CB    1 
ATOM   22620 C  CG1   . ILE A 1 4521 ? 204.102 146.385 192.188 1.00 16.17 ? 4521 ILE A CG1   1 
ATOM   22621 C  CG2   . ILE A 1 4521 ? 202.169 146.369 190.605 1.00 11.76 ? 4521 ILE A CG2   1 
ATOM   22622 C  CD1   . ILE A 1 4521 ? 204.264 144.895 192.273 1.00 13.69 ? 4521 ILE A CD1   1 
ATOM   22623 N  N     . THR A 1 4522 ? 204.098 147.995 187.901 1.00 18.05 ? 4522 THR A N     1 
ATOM   22624 C  CA    . THR A 1 4522 ? 203.642 148.391 186.572 1.00 17.61 ? 4522 THR A CA    1 
ATOM   22625 C  C     . THR A 1 4522 ? 204.436 147.688 185.477 1.00 21.15 ? 4522 THR A C     1 
ATOM   22626 O  O     . THR A 1 4522 ? 203.864 147.256 184.469 1.00 18.93 ? 4522 THR A O     1 
ATOM   22627 C  CB    . THR A 1 4522 ? 203.741 149.911 186.420 1.00 18.19 ? 4522 THR A CB    1 
ATOM   22628 O  OG1   . THR A 1 4522 ? 202.755 150.539 187.248 1.00 25.96 ? 4522 THR A OG1   1 
ATOM   22629 C  CG2   . THR A 1 4522 ? 203.518 150.329 184.973 1.00 23.71 ? 4522 THR A CG2   1 
ATOM   22630 N  N     . ALA A 1 4523 ? 205.752 147.557 185.659 1.00 19.72 ? 4523 ALA A N     1 
ATOM   22631 C  CA    . ALA A 1 4523 ? 206.582 146.919 184.642 1.00 17.16 ? 4523 ALA A CA    1 
ATOM   22632 C  C     . ALA A 1 4523 ? 206.184 145.465 184.429 1.00 19.34 ? 4523 ALA A C     1 
ATOM   22633 O  O     . ALA A 1 4523 ? 206.108 144.995 183.287 1.00 25.25 ? 4523 ALA A O     1 
ATOM   22634 C  CB    . ALA A 1 4523 ? 208.056 147.021 185.032 1.00 12.35 ? 4523 ALA A CB    1 
ATOM   22635 N  N     . THR A 1 4524 ? 205.927 144.734 185.516 1.00 24.43 ? 4524 THR A N     1 
ATOM   22636 C  CA    . THR A 1 4524 ? 205.485 143.349 185.390 1.00 19.41 ? 4524 THR A CA    1 
ATOM   22637 C  C     . THR A 1 4524 ? 204.124 143.266 184.710 1.00 17.23 ? 4524 THR A C     1 
ATOM   22638 O  O     . THR A 1 4524 ? 203.875 142.359 183.910 1.00 22.63 ? 4524 THR A O     1 
ATOM   22639 C  CB    . THR A 1 4524 ? 205.442 142.686 186.766 1.00 18.40 ? 4524 THR A CB    1 
ATOM   22640 O  OG1   . THR A 1 4524 ? 204.717 143.521 187.676 1.00 22.54 ? 4524 THR A OG1   1 
ATOM   22641 C  CG2   . THR A 1 4524 ? 206.850 142.473 187.294 1.00 16.21 ? 4524 THR A CG2   1 
ATOM   22642 N  N     . ARG A 1 4525 ? 203.228 144.201 185.029 1.00 16.47 ? 4525 ARG A N     1 
ATOM   22643 C  CA    . ARG A 1 4525 ? 201.945 144.268 184.337 1.00 16.10 ? 4525 ARG A CA    1 
ATOM   22644 C  C     . ARG A 1 4525 ? 202.138 144.571 182.857 1.00 20.33 ? 4525 ARG A C     1 
ATOM   22645 O  O     . ARG A 1 4525 ? 201.472 143.979 181.999 1.00 23.11 ? 4525 ARG A O     1 
ATOM   22646 C  CB    . ARG A 1 4525 ? 201.060 145.325 184.994 1.00 14.93 ? 4525 ARG A CB    1 
ATOM   22647 C  CG    . ARG A 1 4525 ? 199.633 145.367 184.490 1.00 15.43 ? 4525 ARG A CG    1 
ATOM   22648 C  CD    . ARG A 1 4525 ? 198.951 146.647 184.936 1.00 19.69 ? 4525 ARG A CD    1 
ATOM   22649 N  NE    . ARG A 1 4525 ? 197.504 146.500 185.038 1.00 23.66 ? 4525 ARG A NE    1 
ATOM   22650 C  CZ    . ARG A 1 4525 ? 196.807 146.739 186.141 1.00 25.99 ? 4525 ARG A CZ    1 
ATOM   22651 N  NH1   . ARG A 1 4525 ? 197.397 147.137 187.257 1.00 20.56 ? 4525 ARG A NH1   1 
ATOM   22652 N  NH2   . ARG A 1 4525 ? 195.488 146.577 186.122 1.00 24.49 ? 4525 ARG A NH2   1 
ATOM   22653 N  N     . GLN A 1 4526 ? 203.051 145.491 182.539 1.00 19.57 ? 4526 GLN A N     1 
ATOM   22654 C  CA    . GLN A 1 4526 ? 203.335 145.818 181.147 1.00 18.50 ? 4526 GLN A CA    1 
ATOM   22655 C  C     . GLN A 1 4526 ? 204.034 144.671 180.428 1.00 20.51 ? 4526 GLN A C     1 
ATOM   22656 O  O     . GLN A 1 4526 ? 203.849 144.493 179.220 1.00 29.62 ? 4526 GLN A O     1 
ATOM   22657 C  CB    . GLN A 1 4526 ? 204.172 147.097 181.083 1.00 21.22 ? 4526 GLN A CB    1 
ATOM   22658 C  CG    . GLN A 1 4526 ? 204.681 147.470 179.704 1.00 23.69 ? 4526 GLN A CG    1 
ATOM   22659 C  CD    . GLN A 1 4526 ? 203.566 147.697 178.710 1.00 23.81 ? 4526 GLN A CD    1 
ATOM   22660 O  OE1   . GLN A 1 4526 ? 202.729 148.579 178.888 1.00 19.53 ? 4526 GLN A OE1   1 
ATOM   22661 N  NE2   . GLN A 1 4526 ? 203.548 146.894 177.650 1.00 32.43 ? 4526 GLN A NE2   1 
ATOM   22662 N  N     . TYR A 1 4527 ? 204.836 143.884 181.151 1.00 16.66 ? 4527 TYR A N     1 
ATOM   22663 C  CA    . TYR A 1 4527 ? 205.542 142.765 180.534 1.00 21.26 ? 4527 TYR A CA    1 
ATOM   22664 C  C     . TYR A 1 4527 ? 204.569 141.700 180.043 1.00 21.46 ? 4527 TYR A C     1 
ATOM   22665 O  O     . TYR A 1 4527 ? 204.695 141.196 178.920 1.00 27.69 ? 4527 TYR A O     1 
ATOM   22666 C  CB    . TYR A 1 4527 ? 206.548 142.188 181.539 1.00 18.01 ? 4527 TYR A CB    1 
ATOM   22667 C  CG    . TYR A 1 4527 ? 207.262 140.907 181.139 1.00 20.61 ? 4527 TYR A CG    1 
ATOM   22668 C  CD1   . TYR A 1 4527 ? 206.615 139.675 181.163 1.00 17.57 ? 4527 TYR A CD1   1 
ATOM   22669 C  CD2   . TYR A 1 4527 ? 208.599 140.931 180.761 1.00 23.78 ? 4527 TYR A CD2   1 
ATOM   22670 C  CE1   . TYR A 1 4527 ? 207.273 138.515 180.808 1.00 22.46 ? 4527 TYR A CE1   1 
ATOM   22671 C  CE2   . TYR A 1 4527 ? 209.266 139.777 180.405 1.00 19.93 ? 4527 TYR A CE2   1 
ATOM   22672 C  CZ    . TYR A 1 4527 ? 208.599 138.572 180.431 1.00 24.12 ? 4527 TYR A CZ    1 
ATOM   22673 O  OH    . TYR A 1 4527 ? 209.259 137.420 180.076 1.00 32.10 ? 4527 TYR A OH    1 
ATOM   22674 N  N     . VAL A 1 4528 ? 203.594 141.335 180.878 1.00 20.04 ? 4528 VAL A N     1 
ATOM   22675 C  CA    . VAL A 1 4528 ? 202.687 140.245 180.531 1.00 19.30 ? 4528 VAL A CA    1 
ATOM   22676 C  C     . VAL A 1 4528 ? 201.737 140.661 179.416 1.00 26.20 ? 4528 VAL A C     1 
ATOM   22677 O  O     . VAL A 1 4528 ? 201.477 139.888 178.486 1.00 32.58 ? 4528 VAL A O     1 
ATOM   22678 C  CB    . VAL A 1 4528 ? 201.927 139.771 181.784 1.00 22.96 ? 4528 VAL A CB    1 
ATOM   22679 C  CG1   . VAL A 1 4528 ? 200.986 138.631 181.437 1.00 17.16 ? 4528 VAL A CG1   1 
ATOM   22680 C  CG2   . VAL A 1 4528 ? 202.913 139.342 182.861 1.00 16.23 ? 4528 VAL A CG2   1 
ATOM   22681 N  N     . ALA A 1 4529 ? 201.209 141.886 179.482 1.00 23.43 ? 4529 ALA A N     1 
ATOM   22682 C  CA    . ALA A 1 4529 ? 200.300 142.351 178.438 1.00 25.26 ? 4529 ALA A CA    1 
ATOM   22683 C  C     . ALA A 1 4529 ? 201.002 142.471 177.092 1.00 30.87 ? 4529 ALA A C     1 
ATOM   22684 O  O     . ALA A 1 4529 ? 200.350 142.384 176.045 1.00 29.38 ? 4529 ALA A O     1 
ATOM   22685 C  CB    . ALA A 1 4529 ? 199.685 143.691 178.830 1.00 26.67 ? 4529 ALA A CB    1 
ATOM   22686 N  N     . GLN A 1 4530 ? 202.320 142.678 177.096 1.00 27.90 ? 4530 GLN A N     1 
ATOM   22687 C  CA    . GLN A 1 4530 ? 203.052 142.765 175.838 1.00 25.43 ? 4530 GLN A CA    1 
ATOM   22688 C  C     . GLN A 1 4530 ? 203.104 141.419 175.128 1.00 31.53 ? 4530 GLN A C     1 
ATOM   22689 O  O     . GLN A 1 4530 ? 202.869 141.343 173.915 1.00 38.68 ? 4530 GLN A O     1 
ATOM   22690 C  CB    . GLN A 1 4530 ? 204.460 143.293 176.095 1.00 26.02 ? 4530 GLN A CB    1 
ATOM   22691 C  CG    . GLN A 1 4530 ? 205.206 143.690 174.839 1.00 25.22 ? 4530 GLN A CG    1 
ATOM   22692 C  CD    . GLN A 1 4530 ? 206.342 144.650 175.122 1.00 33.52 ? 4530 GLN A CD    1 
ATOM   22693 O  OE1   . GLN A 1 4530 ? 206.552 145.057 176.263 1.00 32.23 ? 4530 GLN A OE1   1 
ATOM   22694 N  NE2   . GLN A 1 4530 ? 207.083 145.016 174.082 1.00 36.59 ? 4530 GLN A NE2   1 
ATOM   22695 N  N     . ALA A 1 4531 ? 203.402 140.345 175.863 1.00 26.43 ? 4531 ALA A N     1 
ATOM   22696 C  CA    . ALA A 1 4531 ? 203.501 139.028 175.240 1.00 26.53 ? 4531 ALA A CA    1 
ATOM   22697 C  C     . ALA A 1 4531 ? 202.152 138.562 174.711 1.00 30.50 ? 4531 ALA A C     1 
ATOM   22698 O  O     . ALA A 1 4531 ? 202.077 137.952 173.637 1.00 34.70 ? 4531 ALA A O     1 
ATOM   22699 C  CB    . ALA A 1 4531 ? 204.065 138.016 176.237 1.00 24.32 ? 4531 ALA A CB    1 
ATOM   22700 N  N     . ASN A 1 4532 ? 201.080 138.842 175.443 1.00 31.16 ? 4532 ASN A N     1 
ATOM   22701 C  CA    . ASN A 1 4532 ? 199.742 138.398 175.085 1.00 29.35 ? 4532 ASN A CA    1 
ATOM   22702 C  C     . ASN A 1 4532 ? 198.972 139.437 174.278 1.00 31.41 ? 4532 ASN A C     1 
ATOM   22703 O  O     . ASN A 1 4532 ? 197.788 139.228 173.997 1.00 31.78 ? 4532 ASN A O     1 
ATOM   22704 C  CB    . ASN A 1 4532 ? 198.964 138.034 176.350 1.00 29.36 ? 4532 ASN A CB    1 
ATOM   22705 C  CG    . ASN A 1 4532 ? 199.728 137.085 177.250 1.00 33.34 ? 4532 ASN A CG    1 
ATOM   22706 O  OD1   . ASN A 1 4532 ? 199.972 137.383 178.420 1.00 34.63 ? 4532 ASN A OD1   1 
ATOM   22707 N  ND2   . ASN A 1 4532 ? 200.124 135.940 176.706 1.00 34.20 ? 4532 ASN A ND2   1 
ATOM   22708 N  N     . SER A 1 4533 ? 199.620 140.545 173.909 1.00 29.98 ? 4533 SER A N     1 
ATOM   22709 C  CA    . SER A 1 4533 ? 199.010 141.600 173.098 1.00 28.51 ? 4533 SER A CA    1 
ATOM   22710 C  C     . SER A 1 4533 ? 197.739 142.149 173.748 1.00 29.42 ? 4533 SER A C     1 
ATOM   22711 O  O     . SER A 1 4533 ? 196.741 142.416 173.076 1.00 30.43 ? 4533 SER A O     1 
ATOM   22712 C  CB    . SER A 1 4533 ? 198.723 141.111 171.676 1.00 28.42 ? 4533 SER A CB    1 
ATOM   22713 O  OG    . SER A 1 4533 ? 198.249 142.167 170.860 1.00 29.99 ? 4533 SER A OG    1 
ATOM   22714 N  N     . TRP A 1 4534 ? 197.778 142.326 175.063 1.00 27.74 ? 4534 TRP A N     1 
ATOM   22715 C  CA    . TRP A 1 4534 ? 196.647 142.840 175.820 1.00 25.28 ? 4534 TRP A CA    1 
ATOM   22716 C  C     . TRP A 1 4534 ? 196.940 144.245 176.329 1.00 25.68 ? 4534 TRP A C     1 
ATOM   22717 O  O     . TRP A 1 4534 ? 198.048 144.771 176.190 1.00 27.45 ? 4534 TRP A O     1 
ATOM   22718 C  CB    . TRP A 1 4534 ? 196.307 141.914 176.993 1.00 25.98 ? 4534 TRP A CB    1 
ATOM   22719 C  CG    . TRP A 1 4534 ? 195.769 140.582 176.583 1.00 27.98 ? 4534 TRP A CG    1 
ATOM   22720 C  CD1   . TRP A 1 4534 ? 195.064 140.296 175.452 1.00 28.16 ? 4534 TRP A CD1   1 
ATOM   22721 C  CD2   . TRP A 1 4534 ? 195.876 139.353 177.311 1.00 27.46 ? 4534 TRP A CD2   1 
ATOM   22722 N  NE1   . TRP A 1 4534 ? 194.733 138.963 175.426 1.00 32.23 ? 4534 TRP A NE1   1 
ATOM   22723 C  CE2   . TRP A 1 4534 ? 195.218 138.364 176.557 1.00 27.30 ? 4534 TRP A CE2   1 
ATOM   22724 C  CE3   . TRP A 1 4534 ? 196.467 138.994 178.527 1.00 29.03 ? 4534 TRP A CE3   1 
ATOM   22725 C  CZ2   . TRP A 1 4534 ? 195.137 137.037 176.975 1.00 29.05 ? 4534 TRP A CZ2   1 
ATOM   22726 C  CZ3   . TRP A 1 4534 ? 196.385 137.677 178.940 1.00 30.05 ? 4534 TRP A CZ3   1 
ATOM   22727 C  CH2   . TRP A 1 4534 ? 195.725 136.715 178.168 1.00 29.73 ? 4534 TRP A CH2   1 
ATOM   22728 N  N     . SER A 1 4535 ? 195.916 144.855 176.915 1.00 25.76 ? 4535 SER A N     1 
ATOM   22729 C  CA    . SER A 1 4535 ? 196.043 146.154 177.554 1.00 27.37 ? 4535 SER A CA    1 
ATOM   22730 C  C     . SER A 1 4535 ? 196.290 145.983 179.047 1.00 31.07 ? 4535 SER A C     1 
ATOM   22731 O  O     . SER A 1 4535 ? 195.915 144.970 179.645 1.00 33.00 ? 4535 SER A O     1 
ATOM   22732 C  CB    . SER A 1 4535 ? 194.786 146.995 177.324 1.00 27.69 ? 4535 SER A CB    1 
ATOM   22733 O  OG    . SER A 1 4535 ? 194.826 148.189 178.084 1.00 32.65 ? 4535 SER A OG    1 
ATOM   22734 N  N     . LEU A 1 4536 ? 196.928 146.992 179.647 1.00 24.35 ? 4536 LEU A N     1 
ATOM   22735 C  CA    . LEU A 1 4536 ? 197.229 146.923 181.073 1.00 26.22 ? 4536 LEU A CA    1 
ATOM   22736 C  C     . LEU A 1 4536 ? 195.958 146.864 181.907 1.00 32.76 ? 4536 LEU A C     1 
ATOM   22737 O  O     . LEU A 1 4536 ? 195.931 146.199 182.950 1.00 32.26 ? 4536 LEU A O     1 
ATOM   22738 C  CB    . LEU A 1 4536 ? 198.085 148.116 181.499 1.00 26.07 ? 4536 LEU A CB    1 
ATOM   22739 C  CG    . LEU A 1 4536 ? 199.472 148.266 180.870 1.00 29.55 ? 4536 LEU A CG    1 
ATOM   22740 C  CD1   . LEU A 1 4536 ? 199.402 149.103 179.596 1.00 25.09 ? 4536 LEU A CD1   1 
ATOM   22741 C  CD2   . LEU A 1 4536 ? 200.456 148.862 181.859 1.00 22.50 ? 4536 LEU A CD2   1 
ATOM   22742 N  N     . GLU A 1 4537 ? 194.900 147.550 181.469 1.00 32.26 ? 4537 GLU A N     1 
ATOM   22743 C  CA    . GLU A 1 4537 ? 193.631 147.500 182.187 1.00 25.63 ? 4537 GLU A CA    1 
ATOM   22744 C  C     . GLU A 1 4537 ? 192.992 146.121 182.109 1.00 30.05 ? 4537 GLU A C     1 
ATOM   22745 O  O     . GLU A 1 4537 ? 192.156 145.778 182.954 1.00 36.34 ? 4537 GLU A O     1 
ATOM   22746 C  CB    . GLU A 1 4537 ? 192.672 148.556 181.636 1.00 27.43 ? 4537 GLU A CB    1 
ATOM   22747 C  CG    . GLU A 1 4537 ? 193.201 149.977 181.713 1.00 30.96 ? 4537 GLU A CG    1 
ATOM   22748 C  CD    . GLU A 1 4537 ? 192.265 150.981 181.072 1.00 35.51 ? 4537 GLU A CD    1 
ATOM   22749 O  OE1   . GLU A 1 4537 ? 191.100 151.076 181.511 1.00 31.75 ? 4537 GLU A OE1   1 
ATOM   22750 O  OE2   . GLU A 1 4537 ? 192.696 151.679 180.128 1.00 32.45 ? 4537 GLU A OE2   1 
ATOM   22751 N  N     . GLU A 1 4538 ? 193.365 145.319 181.114 1.00 25.04 ? 4538 GLU A N     1 
ATOM   22752 C  CA    . GLU A 1 4538 ? 192.781 143.995 180.944 1.00 31.00 ? 4538 GLU A CA    1 
ATOM   22753 C  C     . GLU A 1 4538 ? 193.466 142.928 181.787 1.00 27.28 ? 4538 GLU A C     1 
ATOM   22754 O  O     . GLU A 1 4538 ? 193.097 141.755 181.675 1.00 25.61 ? 4538 GLU A O     1 
ATOM   22755 C  CB    . GLU A 1 4538 ? 192.820 143.591 179.468 1.00 32.69 ? 4538 GLU A CB    1 
ATOM   22756 C  CG    . GLU A 1 4538 ? 192.219 144.622 178.529 1.00 32.88 ? 4538 GLU A CG    1 
ATOM   22757 C  CD    . GLU A 1 4538 ? 192.545 144.345 177.075 1.00 39.56 ? 4538 GLU A CD    1 
ATOM   22758 O  OE1   . GLU A 1 4538 ? 193.257 143.356 176.801 1.00 40.24 ? 4538 GLU A OE1   1 
ATOM   22759 O  OE2   . GLU A 1 4538 ? 192.087 145.116 176.205 1.00 39.94 ? 4538 GLU A OE2   1 
ATOM   22760 N  N     . LEU A 1 4539 ? 194.446 143.294 182.610 1.00 28.07 ? 4539 LEU A N     1 
ATOM   22761 C  CA    . LEU A 1 4539 ? 195.146 142.349 183.474 1.00 23.03 ? 4539 LEU A CA    1 
ATOM   22762 C  C     . LEU A 1 4539 ? 194.798 142.650 184.926 1.00 23.03 ? 4539 LEU A C     1 
ATOM   22763 O  O     . LEU A 1 4539 ? 194.969 143.781 185.393 1.00 27.78 ? 4539 LEU A O     1 
ATOM   22764 C  CB    . LEU A 1 4539 ? 196.654 142.422 183.261 1.00 18.40 ? 4539 LEU A CB    1 
ATOM   22765 C  CG    . LEU A 1 4539 ? 197.209 141.978 181.911 1.00 18.92 ? 4539 LEU A CG    1 
ATOM   22766 C  CD1   . LEU A 1 4539 ? 198.694 142.252 181.874 1.00 24.80 ? 4539 LEU A CD1   1 
ATOM   22767 C  CD2   . LEU A 1 4539 ? 196.930 140.505 181.677 1.00 20.09 ? 4539 LEU A CD2   1 
ATOM   22768 N  N     . CYS A 1 4540 ? 194.315 141.637 185.634 1.00 19.89 ? 4540 CYS A N     1 
ATOM   22769 C  CA    . CYS A 1 4540 ? 194.144 141.695 187.075 1.00 18.06 ? 4540 CYS A CA    1 
ATOM   22770 C  C     . CYS A 1 4540 ? 195.261 140.902 187.741 1.00 24.14 ? 4540 CYS A C     1 
ATOM   22771 O  O     . CYS A 1 4540 ? 195.766 139.924 187.185 1.00 24.14 ? 4540 CYS A O     1 
ATOM   22772 C  CB    . CYS A 1 4540 ? 192.779 141.145 187.493 1.00 17.90 ? 4540 CYS A CB    1 
ATOM   22773 S  SG    . CYS A 1 4540 ? 192.551 139.382 187.178 1.00 51.10 ? 4540 CYS A SG    1 
ATOM   22774 N  N     . LEU A 1 4541 ? 195.653 141.341 188.931 1.00 22.09 ? 4541 LEU A N     1 
ATOM   22775 C  CA    . LEU A 1 4541 ? 196.784 140.756 189.642 1.00 17.38 ? 4541 LEU A CA    1 
ATOM   22776 C  C     . LEU A 1 4541 ? 196.291 139.654 190.569 1.00 15.41 ? 4541 LEU A C     1 
ATOM   22777 O  O     . LEU A 1 4541 ? 195.526 139.918 191.502 1.00 25.07 ? 4541 LEU A O     1 
ATOM   22778 C  CB    . LEU A 1 4541 ? 197.542 141.822 190.431 1.00 15.60 ? 4541 LEU A CB    1 
ATOM   22779 C  CG    . LEU A 1 4541 ? 198.727 141.325 191.261 1.00 19.57 ? 4541 LEU A CG    1 
ATOM   22780 C  CD1   . LEU A 1 4541 ? 199.697 140.537 190.395 1.00 18.93 ? 4541 LEU A CD1   1 
ATOM   22781 C  CD2   . LEU A 1 4541 ? 199.434 142.491 191.932 1.00 16.38 ? 4541 LEU A CD2   1 
ATOM   22782 N  N     . GLU A 1 4542 ? 196.731 138.427 190.309 1.00 18.35 ? 4542 GLU A N     1 
ATOM   22783 C  CA    . GLU A 1 4542 ? 196.483 137.299 191.193 1.00 14.75 ? 4542 GLU A CA    1 
ATOM   22784 C  C     . GLU A 1 4542 ? 197.731 137.034 192.023 1.00 15.92 ? 4542 GLU A C     1 
ATOM   22785 O  O     . GLU A 1 4542 ? 198.852 137.073 191.508 1.00 20.55 ? 4542 GLU A O     1 
ATOM   22786 C  CB    . GLU A 1 4542 ? 196.099 136.046 190.403 1.00 16.44 ? 4542 GLU A CB    1 
ATOM   22787 C  CG    . GLU A 1 4542 ? 194.696 136.081 189.831 1.00 20.38 ? 4542 GLU A CG    1 
ATOM   22788 C  CD    . GLU A 1 4542 ? 193.654 136.476 190.861 1.00 33.42 ? 4542 GLU A CD    1 
ATOM   22789 O  OE1   . GLU A 1 4542 ? 193.108 137.592 190.757 1.00 29.95 ? 4542 GLU A OE1   1 
ATOM   22790 O  OE2   . GLU A 1 4542 ? 193.381 135.666 191.772 1.00 28.74 ? 4542 GLU A OE2   1 
ATOM   22791 N  N     . VAL A 1 4543 ? 197.532 136.774 193.311 1.00 15.95 ? 4543 VAL A N     1 
ATOM   22792 C  CA    . VAL A 1 4543 ? 198.620 136.658 194.271 1.00 11.77 ? 4543 VAL A CA    1 
ATOM   22793 C  C     . VAL A 1 4543 ? 198.650 135.235 194.808 1.00 11.45 ? 4543 VAL A C     1 
ATOM   22794 O  O     . VAL A 1 4543 ? 197.619 134.707 195.237 1.00 17.13 ? 4543 VAL A O     1 
ATOM   22795 C  CB    . VAL A 1 4543 ? 198.470 137.674 195.417 1.00 14.35 ? 4543 VAL A CB    1 
ATOM   22796 C  CG1   . VAL A 1 4543 ? 199.326 137.276 196.604 1.00 9.71  ? 4543 VAL A CG1   1 
ATOM   22797 C  CG2   . VAL A 1 4543 ? 198.834 139.069 194.933 1.00 12.60 ? 4543 VAL A CG2   1 
ATOM   22798 N  N     . ASN A 1 4544 ? 199.827 134.617 194.771 1.00 15.39 ? 4544 ASN A N     1 
ATOM   22799 C  CA    . ASN A 1 4544 ? 200.047 133.302 195.354 1.00 11.56 ? 4544 ASN A CA    1 
ATOM   22800 C  C     . ASN A 1 4544 ? 201.236 133.379 196.299 1.00 13.96 ? 4544 ASN A C     1 
ATOM   22801 O  O     . ASN A 1 4544 ? 202.287 133.919 195.937 1.00 17.00 ? 4544 ASN A O     1 
ATOM   22802 C  CB    . ASN A 1 4544 ? 200.289 132.243 194.275 1.00 17.05 ? 4544 ASN A CB    1 
ATOM   22803 C  CG    . ASN A 1 4544 ? 200.747 130.919 194.849 1.00 21.03 ? 4544 ASN A CG    1 
ATOM   22804 O  OD1   . ASN A 1 4544 ? 199.939 130.127 195.328 1.00 22.95 ? 4544 ASN A OD1   1 
ATOM   22805 N  ND2   . ASN A 1 4544 ? 202.049 130.671 194.802 1.00 22.46 ? 4544 ASN A ND2   1 
ATOM   22806 N  N     . VAL A 1 4545 ? 201.066 132.845 197.504 1.00 15.77 ? 4545 VAL A N     1 
ATOM   22807 C  CA    . VAL A 1 4545 ? 202.088 132.861 198.542 1.00 15.19 ? 4545 VAL A CA    1 
ATOM   22808 C  C     . VAL A 1 4545 ? 202.574 131.437 198.751 1.00 17.82 ? 4545 VAL A C     1 
ATOM   22809 O  O     . VAL A 1 4545 ? 201.767 130.524 198.965 1.00 24.83 ? 4545 VAL A O     1 
ATOM   22810 C  CB    . VAL A 1 4545 ? 201.548 133.463 199.852 1.00 18.98 ? 4545 VAL A CB    1 
ATOM   22811 C  CG1   . VAL A 1 4545 ? 202.517 133.205 200.995 1.00 23.25 ? 4545 VAL A CG1   1 
ATOM   22812 C  CG2   . VAL A 1 4545 ? 201.289 134.953 199.687 1.00 10.75 ? 4545 VAL A CG2   1 
ATOM   22813 N  N     . THR A 1 4546 ? 203.888 131.246 198.685 1.00 18.86 ? 4546 THR A N     1 
ATOM   22814 C  CA    . THR A 1 4546 ? 204.497 129.930 198.784 1.00 16.97 ? 4546 THR A CA    1 
ATOM   22815 C  C     . THR A 1 4546 ? 205.012 129.679 200.195 1.00 25.09 ? 4546 THR A C     1 
ATOM   22816 O  O     . THR A 1 4546 ? 205.396 130.606 200.913 1.00 28.31 ? 4546 THR A O     1 
ATOM   22817 C  CB    . THR A 1 4546 ? 205.649 129.785 197.789 1.00 22.04 ? 4546 THR A CB    1 
ATOM   22818 O  OG1   . THR A 1 4546 ? 206.829 130.388 198.335 1.00 30.80 ? 4546 THR A OG1   1 
ATOM   22819 C  CG2   . THR A 1 4546 ? 205.306 130.468 196.481 1.00 20.05 ? 4546 THR A CG2   1 
ATOM   22820 N  N     . THR A 1 4547 ? 205.017 128.402 200.583 1.00 26.80 ? 4547 THR A N     1 
ATOM   22821 C  CA    . THR A 1 4547 ? 205.559 128.023 201.883 1.00 29.66 ? 4547 THR A CA    1 
ATOM   22822 C  C     . THR A 1 4547 ? 207.053 128.307 201.959 1.00 32.00 ? 4547 THR A C     1 
ATOM   22823 O  O     . THR A 1 4547 ? 207.556 128.757 202.995 1.00 34.03 ? 4547 THR A O     1 
ATOM   22824 C  CB    . THR A 1 4547 ? 205.279 126.545 202.159 1.00 30.30 ? 4547 THR A CB    1 
ATOM   22825 O  OG1   . THR A 1 4547 ? 203.881 126.283 201.985 1.00 35.57 ? 4547 THR A OG1   1 
ATOM   22826 C  CG2   . THR A 1 4547 ? 205.684 126.180 203.580 1.00 25.31 ? 4547 THR A CG2   1 
ATOM   22827 N  N     . SER A 1 4548 ? 207.779 128.054 200.874 1.00 29.72 ? 4548 SER A N     1 
ATOM   22828 C  CA    . SER A 1 4548 ? 209.213 128.298 200.826 1.00 31.01 ? 4548 SER A CA    1 
ATOM   22829 C  C     . SER A 1 4548 ? 209.559 128.993 199.518 1.00 30.50 ? 4548 SER A C     1 
ATOM   22830 O  O     . SER A 1 4548 ? 208.836 128.892 198.524 1.00 28.30 ? 4548 SER A O     1 
ATOM   22831 C  CB    . SER A 1 4548 ? 210.016 126.998 200.963 1.00 29.17 ? 4548 SER A CB    1 
ATOM   22832 O  OG    . SER A 1 4548 ? 209.832 126.164 199.832 1.00 30.02 ? 4548 SER A OG    1 
ATOM   22833 N  N     . GLN A 1 4549 ? 210.684 129.703 199.533 1.00 33.72 ? 4549 GLN A N     1 
ATOM   22834 C  CA    . GLN A 1 4549 ? 211.167 130.378 198.340 1.00 28.35 ? 4549 GLN A CA    1 
ATOM   22835 C  C     . GLN A 1 4549 ? 211.754 129.364 197.360 1.00 29.41 ? 4549 GLN A C     1 
ATOM   22836 O  O     . GLN A 1 4549 ? 211.975 128.194 197.684 1.00 34.83 ? 4549 GLN A O     1 
ATOM   22837 C  CB    . GLN A 1 4549 ? 212.213 131.431 198.707 1.00 23.31 ? 4549 GLN A CB    1 
ATOM   22838 C  CG    . GLN A 1 4549 ? 211.681 132.573 199.561 1.00 24.15 ? 4549 GLN A CG    1 
ATOM   22839 C  CD    . GLN A 1 4549 ? 211.778 132.283 201.046 1.00 31.31 ? 4549 GLN A CD    1 
ATOM   22840 O  OE1   . GLN A 1 4549 ? 212.060 131.155 201.454 1.00 29.85 ? 4549 GLN A OE1   1 
ATOM   22841 N  NE2   . GLN A 1 4549 ? 211.553 133.304 201.865 1.00 28.23 ? 4549 GLN A NE2   1 
ATOM   22842 N  N     . GLY A 1 4550 ? 212.007 129.832 196.141 1.00 28.58 ? 4550 GLY A N     1 
ATOM   22843 C  CA    . GLY A 1 4550 ? 212.564 128.980 195.108 1.00 28.49 ? 4550 GLY A CA    1 
ATOM   22844 C  C     . GLY A 1 4550 ? 211.575 127.960 194.583 1.00 35.30 ? 4550 GLY A C     1 
ATOM   22845 O  O     . GLY A 1 4550 ? 211.788 126.752 194.715 1.00 34.41 ? 4550 GLY A O     1 
ATOM   22846 N  N     . ALA A 1 4551 ? 210.487 128.439 193.984 1.00 34.28 ? 4551 ALA A N     1 
ATOM   22847 C  CA    . ALA A 1 4551 ? 209.449 127.580 193.439 1.00 33.38 ? 4551 ALA A CA    1 
ATOM   22848 C  C     . ALA A 1 4551 ? 209.370 127.774 191.931 1.00 33.23 ? 4551 ALA A C     1 
ATOM   22849 O  O     . ALA A 1 4551 ? 210.029 128.649 191.361 1.00 36.21 ? 4551 ALA A O     1 
ATOM   22850 C  CB    . ALA A 1 4551 ? 208.085 127.866 194.081 1.00 28.51 ? 4551 ALA A CB    1 
ATOM   22851 N  N     . THR A 1 4552 ? 208.558 126.938 191.290 1.00 31.91 ? 4552 THR A N     1 
ATOM   22852 C  CA    . THR A 1 4552 ? 208.383 127.012 189.844 1.00 30.54 ? 4552 THR A CA    1 
ATOM   22853 C  C     . THR A 1 4552 ? 207.779 128.352 189.448 1.00 32.39 ? 4552 THR A C     1 
ATOM   22854 O  O     . THR A 1 4552 ? 206.688 128.713 189.899 1.00 35.55 ? 4552 THR A O     1 
ATOM   22855 C  CB    . THR A 1 4552 ? 207.491 125.865 189.365 1.00 32.53 ? 4552 THR A CB    1 
ATOM   22856 O  OG1   . THR A 1 4552 ? 206.202 125.972 189.978 1.00 37.30 ? 4552 THR A OG1   1 
ATOM   22857 C  CG2   . THR A 1 4552 ? 208.111 124.524 189.727 1.00 24.54 ? 4552 THR A CG2   1 
ATOM   22858 N  N     . LEU A 1 4553 ? 208.491 129.087 188.598 1.00 30.88 ? 4553 LEU A N     1 
ATOM   22859 C  CA    . LEU A 1 4553 ? 208.067 130.409 188.157 1.00 28.55 ? 4553 LEU A CA    1 
ATOM   22860 C  C     . LEU A 1 4553 ? 207.419 130.288 186.782 1.00 29.71 ? 4553 LEU A C     1 
ATOM   22861 O  O     . LEU A 1 4553 ? 208.089 129.957 185.797 1.00 34.38 ? 4553 LEU A O     1 
ATOM   22862 C  CB    . LEU A 1 4553 ? 209.247 131.377 188.130 1.00 27.28 ? 4553 LEU A CB    1 
ATOM   22863 C  CG    . LEU A 1 4553 ? 209.593 132.035 189.469 1.00 30.54 ? 4553 LEU A CG    1 
ATOM   22864 C  CD1   . LEU A 1 4553 ? 210.581 133.176 189.276 1.00 24.39 ? 4553 LEU A CD1   1 
ATOM   22865 C  CD2   . LEU A 1 4553 ? 208.332 132.521 190.164 1.00 17.43 ? 4553 LEU A CD2   1 
ATOM   22866 N  N     . ASP A 1 4554 ? 206.119 130.556 186.721 1.00 30.24 ? 4554 ASP A N     1 
ATOM   22867 C  CA    . ASP A 1 4554 ? 205.400 130.542 185.460 1.00 25.05 ? 4554 ASP A CA    1 
ATOM   22868 C  C     . ASP A 1 4554 ? 205.807 131.745 184.612 1.00 26.53 ? 4554 ASP A C     1 
ATOM   22869 O  O     . ASP A 1 4554 ? 206.410 132.707 185.097 1.00 30.40 ? 4554 ASP A O     1 
ATOM   22870 C  CB    . ASP A 1 4554 ? 203.890 130.543 185.713 1.00 26.61 ? 4554 ASP A CB    1 
ATOM   22871 C  CG    . ASP A 1 4554 ? 203.074 130.295 184.455 1.00 34.37 ? 4554 ASP A CG    1 
ATOM   22872 O  OD1   . ASP A 1 4554 ? 203.670 130.146 183.366 1.00 35.21 ? 4554 ASP A OD1   1 
ATOM   22873 O  OD2   . ASP A 1 4554 ? 201.831 130.247 184.557 1.00 40.28 ? 4554 ASP A OD2   1 
ATOM   22874 N  N     . ALA A 1 4555 ? 205.476 131.675 183.320 1.00 29.44 ? 4555 ALA A N     1 
ATOM   22875 C  CA    . ALA A 1 4555 ? 205.831 132.751 182.400 1.00 26.34 ? 4555 ALA A CA    1 
ATOM   22876 C  C     . ALA A 1 4555 ? 205.177 134.065 182.808 1.00 23.56 ? 4555 ALA A C     1 
ATOM   22877 O  O     . ALA A 1 4555 ? 205.797 135.131 182.731 1.00 27.89 ? 4555 ALA A O     1 
ATOM   22878 C  CB    . ALA A 1 4555 ? 205.436 132.371 180.974 1.00 21.27 ? 4555 ALA A CB    1 
ATOM   22879 N  N     . CYS A 1 4556 ? 203.917 134.008 183.245 1.00 24.44 ? 4556 CYS A N     1 
ATOM   22880 C  CA    . CYS A 1 4556 ? 203.176 135.192 183.665 1.00 23.18 ? 4556 CYS A CA    1 
ATOM   22881 C  C     . CYS A 1 4556 ? 203.194 135.395 185.176 1.00 24.83 ? 4556 CYS A C     1 
ATOM   22882 O  O     . CYS A 1 4556 ? 202.238 135.952 185.731 1.00 21.91 ? 4556 CYS A O     1 
ATOM   22883 C  CB    . CYS A 1 4556 ? 201.739 135.115 183.153 1.00 21.44 ? 4556 CYS A CB    1 
ATOM   22884 S  SG    . CYS A 1 4556 ? 200.825 133.653 183.705 1.00 53.93 ? 4556 CYS A SG    1 
ATOM   22885 N  N     . SER A 1 4557 ? 204.256 134.962 185.857 1.00 25.38 ? 4557 SER A N     1 
ATOM   22886 C  CA    . SER A 1 4557 ? 204.357 135.070 187.304 1.00 20.31 ? 4557 SER A CA    1 
ATOM   22887 C  C     . SER A 1 4557 ? 205.699 135.676 187.689 1.00 21.35 ? 4557 SER A C     1 
ATOM   22888 O  O     . SER A 1 4557 ? 206.693 135.531 186.973 1.00 29.57 ? 4557 SER A O     1 
ATOM   22889 C  CB    . SER A 1 4557 ? 204.189 133.706 187.977 1.00 21.26 ? 4557 SER A CB    1 
ATOM   22890 O  OG    . SER A 1 4557 ? 202.827 133.316 188.008 1.00 32.21 ? 4557 SER A OG    1 
ATOM   22891 N  N     . PHE A 1 4558 ? 205.718 136.362 188.830 1.00 15.87 ? 4558 PHE A N     1 
ATOM   22892 C  CA    . PHE A 1 4558 ? 206.924 137.015 189.319 1.00 16.60 ? 4558 PHE A CA    1 
ATOM   22893 C  C     . PHE A 1 4558 ? 207.065 136.772 190.814 1.00 14.00 ? 4558 PHE A C     1 
ATOM   22894 O  O     . PHE A 1 4558 ? 206.081 136.833 191.554 1.00 17.60 ? 4558 PHE A O     1 
ATOM   22895 C  CB    . PHE A 1 4558 ? 206.899 138.518 189.027 1.00 13.96 ? 4558 PHE A CB    1 
ATOM   22896 C  CG    . PHE A 1 4558 ? 206.839 138.847 187.568 1.00 17.18 ? 4558 PHE A CG    1 
ATOM   22897 C  CD1   . PHE A 1 4558 ? 207.997 138.946 186.819 1.00 18.68 ? 4558 PHE A CD1   1 
ATOM   22898 C  CD2   . PHE A 1 4558 ? 205.621 139.043 186.938 1.00 19.99 ? 4558 PHE A CD2   1 
ATOM   22899 C  CE1   . PHE A 1 4558 ? 207.943 139.242 185.474 1.00 15.17 ? 4558 PHE A CE1   1 
ATOM   22900 C  CE2   . PHE A 1 4558 ? 205.562 139.336 185.592 1.00 18.21 ? 4558 PHE A CE2   1 
ATOM   22901 C  CZ    . PHE A 1 4558 ? 206.724 139.438 184.861 1.00 17.36 ? 4558 PHE A CZ    1 
ATOM   22902 N  N     . GLY A 1 4559 ? 208.292 136.507 191.251 1.00 15.62 ? 4559 GLY A N     1 
ATOM   22903 C  CA    . GLY A 1 4559 ? 208.574 136.226 192.648 1.00 18.18 ? 4559 GLY A CA    1 
ATOM   22904 C  C     . GLY A 1 4559 ? 208.998 137.481 193.386 1.00 14.15 ? 4559 GLY A C     1 
ATOM   22905 O  O     . GLY A 1 4559 ? 209.872 138.222 192.928 1.00 21.94 ? 4559 GLY A O     1 
ATOM   22906 N  N     . VAL A 1 4560 ? 208.369 137.710 194.536 1.00 14.21 ? 4560 VAL A N     1 
ATOM   22907 C  CA    . VAL A 1 4560 ? 208.630 138.873 195.373 1.00 12.63 ? 4560 VAL A CA    1 
ATOM   22908 C  C     . VAL A 1 4560 ? 208.926 138.391 196.787 1.00 12.60 ? 4560 VAL A C     1 
ATOM   22909 O  O     . VAL A 1 4560 ? 208.209 137.536 197.317 1.00 18.76 ? 4560 VAL A O     1 
ATOM   22910 C  CB    . VAL A 1 4560 ? 207.447 139.861 195.366 1.00 12.20 ? 4560 VAL A CB    1 
ATOM   22911 C  CG1   . VAL A 1 4560 ? 207.661 140.969 196.381 1.00 13.68 ? 4560 VAL A CG1   1 
ATOM   22912 C  CG2   . VAL A 1 4560 ? 207.262 140.446 193.981 1.00 10.19 ? 4560 VAL A CG2   1 
ATOM   22913 N  N     . THR A 1 4561 ? 209.981 138.929 197.389 1.00 17.38 ? 4561 THR A N     1 
ATOM   22914 C  CA    . THR A 1 4561 ? 210.377 138.577 198.744 1.00 17.77 ? 4561 THR A CA    1 
ATOM   22915 C  C     . THR A 1 4561 ? 210.299 139.803 199.645 1.00 13.61 ? 4561 THR A C     1 
ATOM   22916 O  O     . THR A 1 4561 ? 210.372 140.945 199.185 1.00 16.45 ? 4561 THR A O     1 
ATOM   22917 C  CB    . THR A 1 4561 ? 211.798 137.997 198.785 1.00 15.79 ? 4561 THR A CB    1 
ATOM   22918 O  OG1   . THR A 1 4561 ? 212.753 139.061 198.705 1.00 21.03 ? 4561 THR A OG1   1 
ATOM   22919 C  CG2   . THR A 1 4561 ? 212.019 137.041 197.628 1.00 18.49 ? 4561 THR A CG2   1 
ATOM   22920 N  N     . GLY A 1 4562 ? 210.144 139.551 200.944 1.00 13.56 ? 4562 GLY A N     1 
ATOM   22921 C  CA    . GLY A 1 4562 ? 210.140 140.607 201.933 1.00 12.56 ? 4562 GLY A CA    1 
ATOM   22922 C  C     . GLY A 1 4562 ? 208.787 141.190 202.279 1.00 15.16 ? 4562 GLY A C     1 
ATOM   22923 O  O     . GLY A 1 4562 ? 208.724 142.096 203.119 1.00 14.64 ? 4562 GLY A O     1 
ATOM   22924 N  N     . LEU A 1 4563 ? 207.708 140.719 201.661 1.00 17.87 ? 4563 LEU A N     1 
ATOM   22925 C  CA    . LEU A 1 4563 ? 206.377 141.179 202.036 1.00 10.31 ? 4563 LEU A CA    1 
ATOM   22926 C  C     . LEU A 1 4563 ? 206.039 140.717 203.447 1.00 11.61 ? 4563 LEU A C     1 
ATOM   22927 O  O     . LEU A 1 4563 ? 206.270 139.560 203.811 1.00 13.14 ? 4563 LEU A O     1 
ATOM   22928 C  CB    . LEU A 1 4563 ? 205.332 140.663 201.049 1.00 9.35  ? 4563 LEU A CB    1 
ATOM   22929 C  CG    . LEU A 1 4563 ? 205.377 141.196 199.616 1.00 9.62  ? 4563 LEU A CG    1 
ATOM   22930 C  CD1   . LEU A 1 4563 ? 204.150 140.742 198.846 1.00 6.80  ? 4563 LEU A CD1   1 
ATOM   22931 C  CD2   . LEU A 1 4563 ? 205.494 142.709 199.599 1.00 8.59  ? 4563 LEU A CD2   1 
ATOM   22932 N  N     . LYS A 1 4564 ? 205.490 141.628 204.247 1.00 12.53 ? 4564 LYS A N     1 
ATOM   22933 C  CA    . LYS A 1 4564 ? 205.145 141.351 205.636 1.00 9.88  ? 4564 LYS A CA    1 
ATOM   22934 C  C     . LYS A 1 4564 ? 203.649 141.546 205.822 1.00 9.00  ? 4564 LYS A C     1 
ATOM   22935 O  O     . LYS A 1 4564 ? 203.120 142.628 205.548 1.00 10.28 ? 4564 LYS A O     1 
ATOM   22936 C  CB    . LYS A 1 4564 ? 205.928 142.259 206.587 1.00 8.97  ? 4564 LYS A CB    1 
ATOM   22937 C  CG    . LYS A 1 4564 ? 207.429 142.025 206.587 1.00 13.00 ? 4564 LYS A CG    1 
ATOM   22938 C  CD    . LYS A 1 4564 ? 207.771 140.628 207.073 1.00 15.46 ? 4564 LYS A CD    1 
ATOM   22939 C  CE    . LYS A 1 4564 ? 209.269 140.455 207.262 1.00 16.58 ? 4564 LYS A CE    1 
ATOM   22940 N  NZ    . LYS A 1 4564 ? 210.022 140.642 205.992 1.00 20.28 ? 4564 LYS A NZ    1 
ATOM   22941 N  N     . LEU A 1 4565 ? 202.971 140.503 206.292 1.00 7.44  ? 4565 LEU A N     1 
ATOM   22942 C  CA    . LEU A 1 4565 ? 201.534 140.560 206.520 1.00 4.32  ? 4565 LEU A CA    1 
ATOM   22943 C  C     . LEU A 1 4565 ? 201.262 141.087 207.925 1.00 6.65  ? 4565 LEU A C     1 
ATOM   22944 O  O     . LEU A 1 4565 ? 201.756 140.526 208.910 1.00 5.07  ? 4565 LEU A O     1 
ATOM   22945 C  CB    . LEU A 1 4565 ? 200.918 139.178 206.328 1.00 4.27  ? 4565 LEU A CB    1 
ATOM   22946 C  CG    . LEU A 1 4565 ? 199.405 139.042 206.507 1.00 5.89  ? 4565 LEU A CG    1 
ATOM   22947 C  CD1   . LEU A 1 4565 ? 198.659 140.039 205.641 1.00 3.37  ? 4565 LEU A CD1   1 
ATOM   22948 C  CD2   . LEU A 1 4565 ? 198.975 137.626 206.195 1.00 8.24  ? 4565 LEU A CD2   1 
ATOM   22949 N  N     . GLN A 1 4566 ? 200.479 142.156 208.021 1.00 4.90  ? 4566 GLN A N     1 
ATOM   22950 C  CA    . GLN A 1 4566 ? 200.191 142.810 209.292 1.00 6.22  ? 4566 GLN A CA    1 
ATOM   22951 C  C     . GLN A 1 4566 ? 198.796 142.419 209.762 1.00 7.51  ? 4566 GLN A C     1 
ATOM   22952 O  O     . GLN A 1 4566 ? 197.808 142.664 209.061 1.00 8.42  ? 4566 GLN A O     1 
ATOM   22953 C  CB    . GLN A 1 4566 ? 200.302 144.328 209.161 1.00 7.08  ? 4566 GLN A CB    1 
ATOM   22954 C  CG    . GLN A 1 4566 ? 201.525 144.810 208.408 1.00 5.82  ? 4566 GLN A CG    1 
ATOM   22955 C  CD    . GLN A 1 4566 ? 202.823 144.508 209.132 1.00 9.36  ? 4566 GLN A CD    1 
ATOM   22956 O  OE1   . GLN A 1 4566 ? 203.675 143.779 208.624 1.00 8.66  ? 4566 GLN A OE1   1 
ATOM   22957 N  NE2   . GLN A 1 4566 ? 202.984 145.077 210.319 1.00 9.85  ? 4566 GLN A NE2   1 
ATOM   22958 N  N     . GLY A 1 4567 ? 198.717 141.821 210.950 1.00 7.13  ? 4567 GLY A N     1 
ATOM   22959 C  CA    . GLY A 1 4567 ? 197.452 141.497 211.572 1.00 6.22  ? 4567 GLY A CA    1 
ATOM   22960 C  C     . GLY A 1 4567 ? 196.791 140.219 211.103 1.00 6.59  ? 4567 GLY A C     1 
ATOM   22961 O  O     . GLY A 1 4567 ? 195.660 139.943 211.519 1.00 7.97  ? 4567 GLY A O     1 
ATOM   22962 N  N     . ALA A 1 4568 ? 197.452 139.430 210.260 1.00 9.80  ? 4568 ALA A N     1 
ATOM   22963 C  CA    . ALA A 1 4568 ? 196.868 138.192 209.765 1.00 6.66  ? 4568 ALA A CA    1 
ATOM   22964 C  C     . ALA A 1 4568 ? 197.982 137.199 209.472 1.00 5.92  ? 4568 ALA A C     1 
ATOM   22965 O  O     . ALA A 1 4568 ? 199.166 137.542 209.468 1.00 10.06 ? 4568 ALA A O     1 
ATOM   22966 C  CB    . ALA A 1 4568 ? 196.015 138.436 208.517 1.00 7.60  ? 4568 ALA A CB    1 
ATOM   22967 N  N     . THR A 1 4569 ? 197.585 135.952 209.233 1.00 8.69  ? 4569 THR A N     1 
ATOM   22968 C  CA    . THR A 1 4569 ? 198.493 134.902 208.796 1.00 10.98 ? 4569 THR A CA    1 
ATOM   22969 C  C     . THR A 1 4569 ? 198.001 134.327 207.478 1.00 10.28 ? 4569 THR A C     1 
ATOM   22970 O  O     . THR A 1 4569 ? 196.793 134.222 207.247 1.00 14.68 ? 4569 THR A O     1 
ATOM   22971 C  CB    . THR A 1 4569 ? 198.608 133.780 209.835 1.00 11.64 ? 4569 THR A CB    1 
ATOM   22972 O  OG1   . THR A 1 4569 ? 197.297 133.374 210.251 1.00 14.40 ? 4569 THR A OG1   1 
ATOM   22973 C  CG2   . THR A 1 4569 ? 199.402 134.249 211.042 1.00 11.46 ? 4569 THR A CG2   1 
ATOM   22974 N  N     . CYS A 1 4570 ? 198.940 133.956 206.614 1.00 18.10 ? 4570 CYS A N     1 
ATOM   22975 C  CA    . CYS A 1 4570 ? 198.628 133.366 205.319 1.00 17.47 ? 4570 CYS A CA    1 
ATOM   22976 C  C     . CYS A 1 4570 ? 198.946 131.880 205.368 1.00 14.74 ? 4570 CYS A C     1 
ATOM   22977 O  O     . CYS A 1 4570 ? 200.081 131.494 205.662 1.00 20.60 ? 4570 CYS A O     1 
ATOM   22978 C  CB    . CYS A 1 4570 ? 199.412 134.050 204.200 1.00 10.54 ? 4570 CYS A CB    1 
ATOM   22979 S  SG    . CYS A 1 4570 ? 198.881 133.585 202.543 1.00 33.37 ? 4570 CYS A SG    1 
ATOM   22980 N  N     . ASN A 1 4571 ? 197.944 131.052 205.080 1.00 15.13 ? 4571 ASN A N     1 
ATOM   22981 C  CA    . ASN A 1 4571 ? 198.107 129.604 205.043 1.00 16.16 ? 4571 ASN A CA    1 
ATOM   22982 C  C     . ASN A 1 4571 ? 197.357 129.065 203.835 1.00 20.44 ? 4571 ASN A C     1 
ATOM   22983 O  O     . ASN A 1 4571 ? 196.126 129.141 203.784 1.00 18.84 ? 4571 ASN A O     1 
ATOM   22984 C  CB    . ASN A 1 4571 ? 197.597 128.956 206.331 1.00 14.45 ? 4571 ASN A CB    1 
ATOM   22985 C  CG    . ASN A 1 4571 ? 198.696 128.746 207.351 1.00 23.18 ? 4571 ASN A CG    1 
ATOM   22986 O  OD1   . ASN A 1 4571 ? 199.309 127.681 207.411 1.00 30.35 ? 4571 ASN A OD1   1 
ATOM   22987 N  ND2   . ASN A 1 4571 ? 198.954 129.767 208.162 1.00 20.96 ? 4571 ASN A ND2   1 
ATOM   22988 N  N     . ASN A 1 4572 ? 198.103 128.520 202.872 1.00 20.90 ? 4572 ASN A N     1 
ATOM   22989 C  CA    . ASN A 1 4572 ? 197.530 127.961 201.645 1.00 22.47 ? 4572 ASN A CA    1 
ATOM   22990 C  C     . ASN A 1 4572 ? 196.692 128.998 200.902 1.00 22.56 ? 4572 ASN A C     1 
ATOM   22991 O  O     . ASN A 1 4572 ? 195.599 128.704 200.416 1.00 23.75 ? 4572 ASN A O     1 
ATOM   22992 C  CB    . ASN A 1 4572 ? 196.705 126.707 201.942 1.00 21.79 ? 4572 ASN A CB    1 
ATOM   22993 C  CG    . ASN A 1 4572 ? 197.414 125.754 202.875 1.00 24.24 ? 4572 ASN A CG    1 
ATOM   22994 O  OD1   . ASN A 1 4572 ? 198.464 125.207 202.542 1.00 29.48 ? 4572 ASN A OD1   1 
ATOM   22995 N  ND2   . ASN A 1 4572 ? 196.847 125.555 204.060 1.00 27.18 ? 4572 ASN A ND2   1 
ATOM   22996 N  N     . ASN A 1 4573 ? 197.210 130.228 200.827 1.00 19.32 ? 4573 ASN A N     1 
ATOM   22997 C  CA    . ASN A 1 4573 ? 196.544 131.338 200.147 1.00 16.57 ? 4573 ASN A CA    1 
ATOM   22998 C  C     . ASN A 1 4573 ? 195.193 131.665 200.768 1.00 18.73 ? 4573 ASN A C     1 
ATOM   22999 O  O     . ASN A 1 4573 ? 194.282 132.134 200.083 1.00 25.65 ? 4573 ASN A O     1 
ATOM   23000 C  CB    . ASN A 1 4573 ? 196.383 131.061 198.652 1.00 18.33 ? 4573 ASN A CB    1 
ATOM   23001 C  CG    . ASN A 1 4573 ? 197.700 130.938 197.946 1.00 20.58 ? 4573 ASN A CG    1 
ATOM   23002 O  OD1   . ASN A 1 4573 ? 198.465 131.897 197.851 1.00 18.32 ? 4573 ASN A OD1   1 
ATOM   23003 N  ND2   . ASN A 1 4573 ? 197.978 129.752 197.440 1.00 25.21 ? 4573 ASN A ND2   1 
ATOM   23004 N  N     . LYS A 1 4574 ? 195.052 131.426 202.069 1.00 19.08 ? 4574 LYS A N     1 
ATOM   23005 C  CA    . LYS A 1 4574 ? 193.806 131.678 202.782 1.00 14.62 ? 4574 LYS A CA    1 
ATOM   23006 C  C     . LYS A 1 4574 ? 194.132 132.423 204.067 1.00 18.81 ? 4574 LYS A C     1 
ATOM   23007 O  O     . LYS A 1 4574 ? 194.663 131.835 205.013 1.00 19.25 ? 4574 LYS A O     1 
ATOM   23008 C  CB    . LYS A 1 4574 ? 193.061 130.374 203.066 1.00 16.00 ? 4574 LYS A CB    1 
ATOM   23009 C  CG    . LYS A 1 4574 ? 192.515 129.705 201.815 1.00 21.50 ? 4574 LYS A CG    1 
ATOM   23010 C  CD    . LYS A 1 4574 ? 191.846 128.377 202.129 1.00 24.77 ? 4574 LYS A CD    1 
ATOM   23011 C  CE    . LYS A 1 4574 ? 190.541 128.585 202.874 1.00 27.10 ? 4574 LYS A CE    1 
ATOM   23012 N  NZ    . LYS A 1 4574 ? 189.511 129.232 202.018 1.00 26.44 ? 4574 LYS A NZ    1 
ATOM   23013 N  N     . LEU A 1 4575 ? 193.816 133.716 204.095 1.00 21.05 ? 4575 LEU A N     1 
ATOM   23014 C  CA    . LEU A 1 4575 ? 194.128 134.551 205.242 1.00 10.94 ? 4575 LEU A CA    1 
ATOM   23015 C  C     . LEU A 1 4575 ? 193.192 134.255 206.403 1.00 13.84 ? 4575 LEU A C     1 
ATOM   23016 O  O     . LEU A 1 4575 ? 191.993 134.032 206.214 1.00 20.21 ? 4575 LEU A O     1 
ATOM   23017 C  CB    . LEU A 1 4575 ? 194.022 136.031 204.881 1.00 11.97 ? 4575 LEU A CB    1 
ATOM   23018 C  CG    . LEU A 1 4575 ? 194.986 136.611 203.855 1.00 10.15 ? 4575 LEU A CG    1 
ATOM   23019 C  CD1   . LEU A 1 4575 ? 194.784 138.108 203.781 1.00 7.09  ? 4575 LEU A CD1   1 
ATOM   23020 C  CD2   . LEU A 1 4575 ? 196.426 136.265 204.172 1.00 11.18 ? 4575 LEU A CD2   1 
ATOM   23021 N  N     . SER A 1 4576 ? 193.747 134.261 207.609 1.00 15.01 ? 4576 SER A N     1 
ATOM   23022 C  CA    . SER A 1 4576 ? 192.969 134.211 208.836 1.00 14.28 ? 4576 SER A CA    1 
ATOM   23023 C  C     . SER A 1 4576 ? 193.469 135.310 209.757 1.00 10.65 ? 4576 SER A C     1 
ATOM   23024 O  O     . SER A 1 4576 ? 194.652 135.657 209.733 1.00 11.95 ? 4576 SER A O     1 
ATOM   23025 C  CB    . SER A 1 4576 ? 193.078 132.847 209.529 1.00 16.88 ? 4576 SER A CB    1 
ATOM   23026 O  OG    . SER A 1 4576 ? 194.395 132.612 209.992 1.00 26.28 ? 4576 SER A OG    1 
ATOM   23027 N  N     . LEU A 1 4577 ? 192.563 135.866 210.556 1.00 13.11 ? 4577 LEU A N     1 
ATOM   23028 C  CA    . LEU A 1 4577 ? 192.944 136.937 211.466 1.00 8.77  ? 4577 LEU A CA    1 
ATOM   23029 C  C     . LEU A 1 4577 ? 193.903 136.416 212.525 1.00 10.51 ? 4577 LEU A C     1 
ATOM   23030 O  O     . LEU A 1 4577 ? 193.757 135.301 213.032 1.00 15.15 ? 4577 LEU A O     1 
ATOM   23031 C  CB    . LEU A 1 4577 ? 191.705 137.547 212.120 1.00 6.96  ? 4577 LEU A CB    1 
ATOM   23032 C  CG    . LEU A 1 4577 ? 190.921 138.507 211.221 1.00 8.60  ? 4577 LEU A CG    1 
ATOM   23033 C  CD1   . LEU A 1 4577 ? 189.639 138.964 211.893 1.00 11.12 ? 4577 LEU A CD1   1 
ATOM   23034 C  CD2   . LEU A 1 4577 ? 191.780 139.696 210.830 1.00 5.75  ? 4577 LEU A CD2   1 
ATOM   23035 N  N     . SER A 1 4578 ? 194.895 137.236 212.855 1.00 5.78  ? 4578 SER A N     1 
ATOM   23036 C  CA    . SER A 1 4578 ? 195.935 136.871 213.802 1.00 7.11  ? 4578 SER A CA    1 
ATOM   23037 C  C     . SER A 1 4578 ? 196.106 137.979 214.831 1.00 11.32 ? 4578 SER A C     1 
ATOM   23038 O  O     . SER A 1 4578 ? 195.872 139.156 214.543 1.00 14.81 ? 4578 SER A O     1 
ATOM   23039 C  CB    . SER A 1 4578 ? 197.269 136.612 213.091 1.00 13.38 ? 4578 SER A CB    1 
ATOM   23040 O  OG    . SER A 1 4578 ? 198.341 136.534 214.011 1.00 13.95 ? 4578 SER A OG    1 
ATOM   23041 N  N     . ASN A 1 4579 ? 196.516 137.591 216.033 1.00 11.65 ? 4579 ASN A N     1 
ATOM   23042 C  CA    . ASN A 1 4579 ? 196.826 138.543 217.086 1.00 9.22  ? 4579 ASN A CA    1 
ATOM   23043 C  C     . ASN A 1 4579 ? 198.292 138.951 217.095 1.00 9.84  ? 4579 ASN A C     1 
ATOM   23044 O  O     . ASN A 1 4579 ? 198.702 139.711 217.977 1.00 15.15 ? 4579 ASN A O     1 
ATOM   23045 C  CB    . ASN A 1 4579 ? 196.431 137.971 218.452 1.00 11.85 ? 4579 ASN A CB    1 
ATOM   23046 C  CG    . ASN A 1 4579 ? 194.927 137.950 218.657 1.00 19.62 ? 4579 ASN A CG    1 
ATOM   23047 O  OD1   . ASN A 1 4579 ? 194.339 136.902 218.923 1.00 21.00 ? 4579 ASN A OD1   1 
ATOM   23048 N  ND2   . ASN A 1 4579 ? 194.298 139.112 218.528 1.00 13.52 ? 4579 ASN A ND2   1 
ATOM   23049 N  N     . ALA A 1 4580 ? 199.083 138.468 216.142 1.00 11.25 ? 4580 ALA A N     1 
ATOM   23050 C  CA    . ALA A 1 4580 ? 200.470 138.881 216.011 1.00 6.96  ? 4580 ALA A CA    1 
ATOM   23051 C  C     . ALA A 1 4580 ? 200.569 140.160 215.184 1.00 10.00 ? 4580 ALA A C     1 
ATOM   23052 O  O     . ALA A 1 4580 ? 199.641 140.542 214.468 1.00 16.04 ? 4580 ALA A O     1 
ATOM   23053 C  CB    . ALA A 1 4580 ? 201.307 137.772 215.371 1.00 6.75  ? 4580 ALA A CB    1 
ATOM   23054 N  N     . ILE A 1 4581 ? 201.720 140.823 215.289 1.00 11.38 ? 4581 ILE A N     1 
ATOM   23055 C  CA    . ILE A 1 4581 ? 201.897 142.112 214.628 1.00 8.80  ? 4581 ILE A CA    1 
ATOM   23056 C  C     . ILE A 1 4581 ? 202.221 141.924 213.152 1.00 11.19 ? 4581 ILE A C     1 
ATOM   23057 O  O     . ILE A 1 4581 ? 201.470 142.365 212.276 1.00 11.87 ? 4581 ILE A O     1 
ATOM   23058 C  CB    . ILE A 1 4581 ? 202.986 142.933 215.342 1.00 11.75 ? 4581 ILE A CB    1 
ATOM   23059 C  CG1   . ILE A 1 4581 ? 202.606 143.159 216.806 1.00 14.40 ? 4581 ILE A CG1   1 
ATOM   23060 C  CG2   . ILE A 1 4581 ? 203.193 144.264 214.642 1.00 10.63 ? 4581 ILE A CG2   1 
ATOM   23061 C  CD1   . ILE A 1 4581 ? 201.322 143.925 216.990 1.00 10.54 ? 4581 ILE A CD1   1 
ATOM   23062 N  N     . SER A 1 4582 ? 203.337 141.268 212.851 1.00 12.00 ? 4582 SER A N     1 
ATOM   23063 C  CA    . SER A 1 4582 ? 203.782 141.070 211.481 1.00 9.36  ? 4582 SER A CA    1 
ATOM   23064 C  C     . SER A 1 4582 ? 204.060 139.596 211.250 1.00 10.88 ? 4582 SER A C     1 
ATOM   23065 O  O     . SER A 1 4582 ? 204.716 138.948 212.072 1.00 15.86 ? 4582 SER A O     1 
ATOM   23066 C  CB    . SER A 1 4582 ? 205.033 141.896 211.174 1.00 10.70 ? 4582 SER A CB    1 
ATOM   23067 O  OG    . SER A 1 4582 ? 204.769 143.281 211.270 1.00 18.73 ? 4582 SER A OG    1 
ATOM   23068 N  N     . THR A 1 4583 ? 203.556 139.071 210.139 1.00 8.75  ? 4583 THR A N     1 
ATOM   23069 C  CA    . THR A 1 4583 ? 203.826 137.706 209.711 1.00 8.18  ? 4583 THR A CA    1 
ATOM   23070 C  C     . THR A 1 4583 ? 204.582 137.765 208.393 1.00 13.32 ? 4583 THR A C     1 
ATOM   23071 O  O     . THR A 1 4583 ? 204.112 138.379 207.432 1.00 13.72 ? 4583 THR A O     1 
ATOM   23072 C  CB    . THR A 1 4583 ? 202.530 136.907 209.557 1.00 12.15 ? 4583 THR A CB    1 
ATOM   23073 O  OG1   . THR A 1 4583 ? 202.014 136.571 210.852 1.00 24.50 ? 4583 THR A OG1   1 
ATOM   23074 C  CG2   . THR A 1 4583 ? 202.781 135.629 208.774 1.00 10.56 ? 4583 THR A CG2   1 
ATOM   23075 N  N     . ALA A 1 4584 ? 205.749 137.130 208.351 1.00 20.92 ? 4584 ALA A N     1 
ATOM   23076 C  CA    . ALA A 1 4584 ? 206.563 137.153 207.145 1.00 14.98 ? 4584 ALA A CA    1 
ATOM   23077 C  C     . ALA A 1 4584 ? 205.962 136.248 206.078 1.00 17.43 ? 4584 ALA A C     1 
ATOM   23078 O  O     . ALA A 1 4584 ? 205.585 135.106 206.356 1.00 16.93 ? 4584 ALA A O     1 
ATOM   23079 C  CB    . ALA A 1 4584 ? 207.992 136.722 207.462 1.00 17.12 ? 4584 ALA A CB    1 
ATOM   23080 N  N     . LEU A 1 4585 ? 205.860 136.768 204.855 1.00 14.55 ? 4585 LEU A N     1 
ATOM   23081 C  CA    . LEU A 1 4585 ? 205.469 135.962 203.709 1.00 13.78 ? 4585 LEU A CA    1 
ATOM   23082 C  C     . LEU A 1 4585 ? 206.723 135.474 203.009 1.00 17.71 ? 4585 LEU A C     1 
ATOM   23083 O  O     . LEU A 1 4585 ? 207.513 136.305 202.533 1.00 24.08 ? 4585 LEU A O     1 
ATOM   23084 C  CB    . LEU A 1 4585 ? 204.605 136.769 202.745 1.00 13.87 ? 4585 LEU A CB    1 
ATOM   23085 C  CG    . LEU A 1 4585 ? 203.334 137.405 203.312 1.00 11.40 ? 4585 LEU A CG    1 
ATOM   23086 C  CD1   . LEU A 1 4585 ? 202.697 138.323 202.284 1.00 7.42  ? 4585 LEU A CD1   1 
ATOM   23087 C  CD2   . LEU A 1 4585 ? 202.352 136.342 203.759 1.00 12.79 ? 4585 LEU A CD2   1 
ATOM   23088 N  N     . PRO A 1 4586 ? 206.963 134.162 202.939 1.00 19.78 ? 4586 PRO A N     1 
ATOM   23089 C  CA    . PRO A 1 4586 ? 208.240 133.666 202.397 1.00 15.29 ? 4586 PRO A CA    1 
ATOM   23090 C  C     . PRO A 1 4586 ? 208.501 134.113 200.967 1.00 16.19 ? 4586 PRO A C     1 
ATOM   23091 O  O     . PRO A 1 4586 ? 209.516 134.759 200.689 1.00 24.00 ? 4586 PRO A O     1 
ATOM   23092 C  CB    . PRO A 1 4586 ? 208.087 132.143 202.482 1.00 20.11 ? 4586 PRO A CB    1 
ATOM   23093 C  CG    . PRO A 1 4586 ? 207.056 131.923 203.541 1.00 22.44 ? 4586 PRO A CG    1 
ATOM   23094 C  CD    . PRO A 1 4586 ? 206.106 133.071 203.429 1.00 15.93 ? 4586 PRO A CD    1 
ATOM   23095 N  N     . LEU A 1 4587 ? 207.593 133.777 200.058 1.00 19.06 ? 4587 LEU A N     1 
ATOM   23096 C  CA    . LEU A 1 4587 ? 207.739 134.148 198.656 1.00 13.47 ? 4587 LEU A CA    1 
ATOM   23097 C  C     . LEU A 1 4587 ? 206.355 134.334 198.059 1.00 17.18 ? 4587 LEU A C     1 
ATOM   23098 O  O     . LEU A 1 4587 ? 205.556 133.393 198.038 1.00 18.70 ? 4587 LEU A O     1 
ATOM   23099 C  CB    . LEU A 1 4587 ? 208.519 133.086 197.880 1.00 17.94 ? 4587 LEU A CB    1 
ATOM   23100 C  CG    . LEU A 1 4587 ? 208.742 133.369 196.395 1.00 16.23 ? 4587 LEU A CG    1 
ATOM   23101 C  CD1   . LEU A 1 4587 ? 209.924 134.296 196.194 1.00 15.41 ? 4587 LEU A CD1   1 
ATOM   23102 C  CD2   . LEU A 1 4587 ? 208.936 132.069 195.639 1.00 20.78 ? 4587 LEU A CD2   1 
ATOM   23103 N  N     . THR A 1 4588 ? 206.078 135.540 197.576 1.00 16.07 ? 4588 THR A N     1 
ATOM   23104 C  CA    . THR A 1 4588 ? 204.787 135.877 196.993 1.00 17.10 ? 4588 THR A CA    1 
ATOM   23105 C  C     . THR A 1 4588 ? 204.923 135.909 195.476 1.00 18.07 ? 4588 THR A C     1 
ATOM   23106 O  O     . THR A 1 4588 ? 205.754 136.651 194.940 1.00 15.74 ? 4588 THR A O     1 
ATOM   23107 C  CB    . THR A 1 4588 ? 204.293 137.225 197.521 1.00 15.52 ? 4588 THR A CB    1 
ATOM   23108 O  OG1   . THR A 1 4588 ? 204.152 137.158 198.945 1.00 21.06 ? 4588 THR A OG1   1 
ATOM   23109 C  CG2   . THR A 1 4588 ? 202.952 137.578 196.910 1.00 11.40 ? 4588 THR A CG2   1 
ATOM   23110 N  N     . GLN A 1 4589 ? 204.112 135.107 194.791 1.00 14.56 ? 4589 GLN A N     1 
ATOM   23111 C  CA    . GLN A 1 4589 ? 204.103 135.077 193.332 1.00 11.62 ? 4589 GLN A CA    1 
ATOM   23112 C  C     . GLN A 1 4589 ? 203.047 136.053 192.825 1.00 16.51 ? 4589 GLN A C     1 
ATOM   23113 O  O     . GLN A 1 4589 ? 201.852 135.866 193.067 1.00 27.24 ? 4589 GLN A O     1 
ATOM   23114 C  CB    . GLN A 1 4589 ? 203.837 133.669 192.807 1.00 14.39 ? 4589 GLN A CB    1 
ATOM   23115 C  CG    . GLN A 1 4589 ? 204.513 132.554 193.577 1.00 15.55 ? 4589 GLN A CG    1 
ATOM   23116 C  CD    . GLN A 1 4589 ? 204.831 131.368 192.691 1.00 19.79 ? 4589 GLN A CD    1 
ATOM   23117 O  OE1   . GLN A 1 4589 ? 204.399 131.307 191.541 1.00 28.18 ? 4589 GLN A OE1   1 
ATOM   23118 N  NE2   . GLN A 1 4589 ? 205.593 130.419 193.219 1.00 27.98 ? 4589 GLN A NE2   1 
ATOM   23119 N  N     . LEU A 1 4590 ? 203.492 137.087 192.120 1.00 11.66 ? 4590 LEU A N     1 
ATOM   23120 C  CA    . LEU A 1 4590 ? 202.593 138.050 191.499 1.00 11.93 ? 4590 LEU A CA    1 
ATOM   23121 C  C     . LEU A 1 4590 ? 202.331 137.601 190.068 1.00 18.63 ? 4590 LEU A C     1 
ATOM   23122 O  O     . LEU A 1 4590 ? 203.211 137.703 189.206 1.00 25.07 ? 4590 LEU A O     1 
ATOM   23123 C  CB    . LEU A 1 4590 ? 203.191 139.453 191.540 1.00 14.33 ? 4590 LEU A CB    1 
ATOM   23124 C  CG    . LEU A 1 4590 ? 203.580 139.949 192.932 1.00 14.93 ? 4590 LEU A CG    1 
ATOM   23125 C  CD1   . LEU A 1 4590 ? 203.959 141.412 192.880 1.00 16.82 ? 4590 LEU A CD1   1 
ATOM   23126 C  CD2   . LEU A 1 4590 ? 202.448 139.725 193.916 1.00 10.69 ? 4590 LEU A CD2   1 
ATOM   23127 N  N     . ARG A 1 4591 ? 201.127 137.104 189.813 1.00 19.65 ? 4591 ARG A N     1 
ATOM   23128 C  CA    . ARG A 1 4591 ? 200.762 136.547 188.520 1.00 18.99 ? 4591 ARG A CA    1 
ATOM   23129 C  C     . ARG A 1 4591 ? 199.739 137.450 187.846 1.00 21.36 ? 4591 ARG A C     1 
ATOM   23130 O  O     . ARG A 1 4591 ? 198.727 137.812 188.454 1.00 22.17 ? 4591 ARG A O     1 
ATOM   23131 C  CB    . ARG A 1 4591 ? 200.207 135.130 188.676 1.00 17.13 ? 4591 ARG A CB    1 
ATOM   23132 C  CG    . ARG A 1 4591 ? 199.345 134.666 187.520 1.00 20.00 ? 4591 ARG A CG    1 
ATOM   23133 C  CD    . ARG A 1 4591 ? 198.731 133.307 187.806 1.00 23.41 ? 4591 ARG A CD    1 
ATOM   23134 N  NE    . ARG A 1 4591 ? 199.497 132.222 187.206 1.00 28.04 ? 4591 ARG A NE    1 
ATOM   23135 C  CZ    . ARG A 1 4591 ? 200.201 131.334 187.894 1.00 33.32 ? 4591 ARG A CZ    1 
ATOM   23136 N  NH1   . ARG A 1 4591 ? 200.261 131.374 189.216 1.00 23.37 ? 4591 ARG A NH1   1 
ATOM   23137 N  NH2   . ARG A 1 4591 ? 200.863 130.383 187.240 1.00 28.54 ? 4591 ARG A NH2   1 
ATOM   23138 N  N     . TRP A 1 4592 ? 200.007 137.810 186.595 1.00 19.45 ? 4592 TRP A N     1 
ATOM   23139 C  CA    . TRP A 1 4592 ? 199.109 138.639 185.803 1.00 14.44 ? 4592 TRP A CA    1 
ATOM   23140 C  C     . TRP A 1 4592 ? 198.324 137.745 184.852 1.00 20.44 ? 4592 TRP A C     1 
ATOM   23141 O  O     . TRP A 1 4592 ? 198.915 136.993 184.070 1.00 23.02 ? 4592 TRP A O     1 
ATOM   23142 C  CB    . TRP A 1 4592 ? 199.894 139.700 185.034 1.00 17.84 ? 4592 TRP A CB    1 
ATOM   23143 C  CG    . TRP A 1 4592 ? 200.538 140.709 185.927 1.00 18.91 ? 4592 TRP A CG    1 
ATOM   23144 C  CD1   . TRP A 1 4592 ? 201.844 140.744 186.316 1.00 15.19 ? 4592 TRP A CD1   1 
ATOM   23145 C  CD2   . TRP A 1 4592 ? 199.900 141.823 186.562 1.00 18.91 ? 4592 TRP A CD2   1 
ATOM   23146 N  NE1   . TRP A 1 4592 ? 202.061 141.813 187.146 1.00 16.09 ? 4592 TRP A NE1   1 
ATOM   23147 C  CE2   . TRP A 1 4592 ? 200.884 142.493 187.316 1.00 18.66 ? 4592 TRP A CE2   1 
ATOM   23148 C  CE3   . TRP A 1 4592 ? 198.594 142.320 186.564 1.00 18.10 ? 4592 TRP A CE3   1 
ATOM   23149 C  CZ2   . TRP A 1 4592 ? 200.602 143.632 188.063 1.00 13.61 ? 4592 TRP A CZ2   1 
ATOM   23150 C  CZ3   . TRP A 1 4592 ? 198.318 143.450 187.305 1.00 19.08 ? 4592 TRP A CZ3   1 
ATOM   23151 C  CH2   . TRP A 1 4592 ? 199.316 144.095 188.043 1.00 15.01 ? 4592 TRP A CH2   1 
ATOM   23152 N  N     . VAL A 1 4593 ? 196.996 137.825 184.927 1.00 19.16 ? 4593 VAL A N     1 
ATOM   23153 C  CA    . VAL A 1 4593 ? 196.114 137.009 184.107 1.00 20.06 ? 4593 VAL A CA    1 
ATOM   23154 C  C     . VAL A 1 4593 ? 195.099 137.910 183.421 1.00 27.05 ? 4593 VAL A C     1 
ATOM   23155 O  O     . VAL A 1 4593 ? 194.862 139.048 183.832 1.00 25.52 ? 4593 VAL A O     1 
ATOM   23156 C  CB    . VAL A 1 4593 ? 195.385 135.918 184.921 1.00 21.79 ? 4593 VAL A CB    1 
ATOM   23157 C  CG1   . VAL A 1 4593 ? 196.380 135.017 185.622 1.00 19.52 ? 4593 VAL A CG1   1 
ATOM   23158 C  CG2   . VAL A 1 4593 ? 194.431 136.549 185.921 1.00 18.01 ? 4593 VAL A CG2   1 
ATOM   23159 N  N     . LYS A 1 4594 ? 194.501 137.380 182.356 1.00 28.68 ? 4594 LYS A N     1 
ATOM   23160 C  CA    . LYS A 1 4594 ? 193.450 138.101 181.654 1.00 28.06 ? 4594 LYS A CA    1 
ATOM   23161 C  C     . LYS A 1 4594 ? 192.260 138.314 182.581 1.00 27.38 ? 4594 LYS A C     1 
ATOM   23162 O  O     . LYS A 1 4594 ? 191.762 137.368 183.199 1.00 28.24 ? 4594 LYS A O     1 
ATOM   23163 C  CB    . LYS A 1 4594 ? 193.025 137.326 180.407 1.00 30.82 ? 4594 LYS A CB    1 
ATOM   23164 C  CG    . LYS A 1 4594 ? 192.141 138.105 179.449 1.00 30.02 ? 4594 LYS A CG    1 
ATOM   23165 C  CD    . LYS A 1 4594 ? 192.831 139.368 178.964 1.00 26.88 ? 4594 LYS A CD    1 
ATOM   23166 C  CE    . LYS A 1 4594 ? 191.855 140.283 178.243 1.00 34.15 ? 4594 LYS A CE    1 
ATOM   23167 N  NZ    . LYS A 1 4594 ? 190.800 140.795 179.160 1.00 34.24 ? 4594 LYS A NZ    1 
ATOM   23168 N  N     . GLN A 1 4595 ? 191.808 139.562 182.679 1.00 28.57 ? 4595 GLN A N     1 
ATOM   23169 C  CA    . GLN A 1 4595 ? 190.704 139.883 183.571 1.00 28.30 ? 4595 GLN A CA    1 
ATOM   23170 C  C     . GLN A 1 4595 ? 189.404 139.283 183.051 1.00 33.38 ? 4595 GLN A C     1 
ATOM   23171 O  O     . GLN A 1 4595 ? 189.128 139.302 181.848 1.00 37.47 ? 4595 GLN A O     1 
ATOM   23172 C  CB    . GLN A 1 4595 ? 190.564 141.398 183.720 1.00 26.64 ? 4595 GLN A CB    1 
ATOM   23173 C  CG    . GLN A 1 4595 ? 189.607 141.826 184.819 1.00 27.43 ? 4595 GLN A CG    1 
ATOM   23174 C  CD    . GLN A 1 4595 ? 189.520 143.332 184.964 1.00 36.84 ? 4595 GLN A CD    1 
ATOM   23175 O  OE1   . GLN A 1 4595 ? 190.168 144.076 184.227 1.00 38.25 ? 4595 GLN A OE1   1 
ATOM   23176 N  NE2   . GLN A 1 4595 ? 188.717 143.791 185.916 1.00 36.03 ? 4595 GLN A NE2   1 
ATOM   23177 N  N     . THR A 1 4596 ? 188.604 138.741 183.969 1.00 32.45 ? 4596 THR A N     1 
ATOM   23178 C  CA    . THR A 1 4596 ? 187.334 138.113 183.625 1.00 32.69 ? 4596 THR A CA    1 
ATOM   23179 C  C     . THR A 1 4596 ? 186.143 138.792 184.292 1.00 36.05 ? 4596 THR A C     1 
ATOM   23180 O  O     . THR A 1 4596 ? 185.037 138.242 184.250 1.00 39.19 ? 4596 THR A O     1 
ATOM   23181 C  CB    . THR A 1 4596 ? 187.356 136.628 183.997 1.00 33.41 ? 4596 THR A CB    1 
ATOM   23182 O  OG1   . THR A 1 4596 ? 187.537 136.489 185.411 1.00 40.32 ? 4596 THR A OG1   1 
ATOM   23183 C  CG2   . THR A 1 4596 ? 188.488 135.913 183.274 1.00 32.84 ? 4596 THR A CG2   1 
ATOM   23184 N  N     . ASN A 1 4597 ? 186.361 139.941 184.942 1.00 30.67 ? 4597 ASN A N     1 
ATOM   23185 C  CA    . ASN A 1 4597 ? 185.349 140.814 185.542 1.00 34.04 ? 4597 ASN A CA    1 
ATOM   23186 C  C     . ASN A 1 4597 ? 184.159 140.070 186.145 1.00 36.49 ? 4597 ASN A C     1 
ATOM   23187 O  O     . ASN A 1 4597 ? 183.004 140.441 185.918 1.00 37.77 ? 4597 ASN A O     1 
ATOM   23188 C  CB    . ASN A 1 4597 ? 184.888 141.881 184.528 1.00 31.16 ? 4597 ASN A CB    1 
ATOM   23189 C  CG    . ASN A 1 4597 ? 184.183 141.310 183.297 1.00 37.75 ? 4597 ASN A CG    1 
ATOM   23190 O  OD1   . ASN A 1 4597 ? 183.679 140.190 183.296 1.00 34.84 ? 4597 ASN A OD1   1 
ATOM   23191 N  ND2   . ASN A 1 4597 ? 184.152 142.102 182.233 1.00 36.24 ? 4597 ASN A ND2   1 
ATOM   23192 N  N     . THR A 1 4598 ? 184.436 139.035 186.941 1.00 37.81 ? 4598 THR A N     1 
ATOM   23193 C  CA    . THR A 1 4598 ? 183.404 138.265 187.620 1.00 33.88 ? 4598 THR A CA    1 
ATOM   23194 C  C     . THR A 1 4598 ? 183.156 138.750 189.044 1.00 36.87 ? 4598 THR A C     1 
ATOM   23195 O  O     . THR A 1 4598 ? 182.698 137.970 189.886 1.00 38.88 ? 4598 THR A O     1 
ATOM   23196 C  CB    . THR A 1 4598 ? 183.767 136.779 187.630 1.00 36.69 ? 4598 THR A CB    1 
ATOM   23197 O  OG1   . THR A 1 4598 ? 185.128 136.618 188.047 1.00 43.12 ? 4598 THR A OG1   1 
ATOM   23198 C  CG2   . THR A 1 4598 ? 183.588 136.174 186.244 1.00 29.89 ? 4598 THR A CG2   1 
ATOM   23199 N  N     . GLU A 1 4599 ? 183.465 140.019 189.328 1.00 37.50 ? 4599 GLU A N     1 
ATOM   23200 C  CA    . GLU A 1 4599 ? 183.268 140.616 190.647 1.00 31.28 ? 4599 GLU A CA    1 
ATOM   23201 C  C     . GLU A 1 4599 ? 184.051 139.870 191.719 1.00 32.71 ? 4599 GLU A C     1 
ATOM   23202 O  O     . GLU A 1 4599 ? 184.982 139.119 191.410 1.00 37.17 ? 4599 GLU A O     1 
ATOM   23203 C  CB    . GLU A 1 4599 ? 181.780 140.660 191.006 1.00 31.67 ? 4599 GLU A CB    1 
ATOM   23204 C  CG    . GLU A 1 4599 ? 180.918 141.403 189.999 1.00 33.90 ? 4599 GLU A CG    1 
ATOM   23205 C  CD    . GLU A 1 4599 ? 179.444 141.357 190.352 1.00 36.90 ? 4599 GLU A CD    1 
ATOM   23206 O  OE1   . GLU A 1 4599 ? 179.075 141.850 191.437 1.00 32.49 ? 4599 GLU A OE1   1 
ATOM   23207 O  OE2   . GLU A 1 4599 ? 178.656 140.825 189.542 1.00 39.54 ? 4599 GLU A OE2   1 
ATOM   23208 N  N     . LYS A 1 4600 ? 183.687 140.076 192.982 1.00 31.13 ? 4600 LYS A N     1 
ATOM   23209 C  CA    . LYS A 1 4600 ? 184.356 139.412 194.093 1.00 31.55 ? 4600 LYS A CA    1 
ATOM   23210 C  C     . LYS A 1 4600 ? 183.757 138.021 194.288 1.00 33.64 ? 4600 LYS A C     1 
ATOM   23211 O  O     . LYS A 1 4600 ? 182.976 137.530 193.467 1.00 35.78 ? 4600 LYS A O     1 
ATOM   23212 C  CB    . LYS A 1 4600 ? 184.260 140.269 195.353 1.00 32.07 ? 4600 LYS A CB    1 
ATOM   23213 C  CG    . LYS A 1 4600 ? 184.956 141.617 195.236 1.00 36.70 ? 4600 LYS A CG    1 
ATOM   23214 C  CD    . LYS A 1 4600 ? 186.410 141.455 194.817 1.00 34.49 ? 4600 LYS A CD    1 
ATOM   23215 C  CE    . LYS A 1 4600 ? 187.104 142.802 194.701 1.00 33.84 ? 4600 LYS A CE    1 
ATOM   23216 N  NZ    . LYS A 1 4600 ? 188.550 142.660 194.370 1.00 35.92 ? 4600 LYS A NZ    1 
ATOM   23217 N  N     . LYS A 1 4601 ? 184.120 137.361 195.389 1.00 32.22 ? 4601 LYS A N     1 
ATOM   23218 C  CA    . LYS A 1 4601 ? 183.664 136.003 195.661 1.00 34.14 ? 4601 LYS A CA    1 
ATOM   23219 C  C     . LYS A 1 4601 ? 183.018 135.873 197.038 1.00 34.65 ? 4601 LYS A C     1 
ATOM   23220 O  O     . LYS A 1 4601 ? 182.850 134.749 197.525 1.00 32.18 ? 4601 LYS A O     1 
ATOM   23221 C  CB    . LYS A 1 4601 ? 184.832 135.017 195.531 1.00 31.59 ? 4601 LYS A CB    1 
ATOM   23222 C  CG    . LYS A 1 4601 ? 184.429 133.587 195.193 1.00 29.57 ? 4601 LYS A CG    1 
ATOM   23223 C  CD    . LYS A 1 4601 ? 185.622 132.649 195.254 1.00 37.25 ? 4601 LYS A CD    1 
ATOM   23224 C  CE    . LYS A 1 4601 ? 186.757 133.137 194.368 1.00 34.73 ? 4601 LYS A CE    1 
ATOM   23225 N  NZ    . LYS A 1 4601 ? 187.923 132.212 194.399 1.00 31.96 ? 4601 LYS A NZ    1 
ATOM   23226 N  N     . ALA A 1 4602 ? 182.666 136.988 197.680 1.00 31.54 ? 4602 ALA A N     1 
ATOM   23227 C  CA    . ALA A 1 4602 ? 182.056 137.063 199.006 1.00 25.43 ? 4602 ALA A CA    1 
ATOM   23228 C  C     . ALA A 1 4602 ? 182.986 136.566 200.105 1.00 31.00 ? 4602 ALA A C     1 
ATOM   23229 O  O     . ALA A 1 4602 ? 182.599 136.584 201.281 1.00 29.28 ? 4602 ALA A O     1 
ATOM   23230 C  CB    . ALA A 1 4602 ? 180.726 136.297 199.091 1.00 26.55 ? 4602 ALA A CB    1 
ATOM   23231 N  N     . SER A 1 4603 ? 184.196 136.123 199.768 1.00 26.59 ? 4603 SER A N     1 
ATOM   23232 C  CA    . SER A 1 4603 ? 185.202 135.731 200.745 1.00 18.98 ? 4603 SER A CA    1 
ATOM   23233 C  C     . SER A 1 4603 ? 186.571 136.286 200.374 1.00 20.19 ? 4603 SER A C     1 
ATOM   23234 O  O     . SER A 1 4603 ? 187.594 135.694 200.729 1.00 25.99 ? 4603 SER A O     1 
ATOM   23235 C  CB    . SER A 1 4603 ? 185.267 134.208 200.881 1.00 22.81 ? 4603 SER A CB    1 
ATOM   23236 O  OG    . SER A 1 4603 ? 185.296 133.585 199.608 1.00 27.68 ? 4603 SER A OG    1 
ATOM   23237 N  N     . VAL A 1 4604 ? 186.609 137.410 199.663 1.00 18.35 ? 4604 VAL A N     1 
ATOM   23238 C  CA    . VAL A 1 4604 ? 187.843 137.996 199.157 1.00 17.93 ? 4604 VAL A CA    1 
ATOM   23239 C  C     . VAL A 1 4604 ? 188.000 139.383 199.761 1.00 17.02 ? 4604 VAL A C     1 
ATOM   23240 O  O     . VAL A 1 4604 ? 187.058 140.183 199.747 1.00 17.67 ? 4604 VAL A O     1 
ATOM   23241 C  CB    . VAL A 1 4604 ? 187.846 138.066 197.618 1.00 16.90 ? 4604 VAL A CB    1 
ATOM   23242 C  CG1   . VAL A 1 4604 ? 188.977 138.956 197.122 1.00 13.76 ? 4604 VAL A CG1   1 
ATOM   23243 C  CG2   . VAL A 1 4604 ? 187.962 136.672 197.032 1.00 18.14 ? 4604 VAL A CG2   1 
ATOM   23244 N  N     . VAL A 1 4605 ? 189.185 139.659 200.300 1.00 12.51 ? 4605 VAL A N     1 
ATOM   23245 C  CA    . VAL A 1 4605 ? 189.527 140.970 200.836 1.00 9.39  ? 4605 VAL A CA    1 
ATOM   23246 C  C     . VAL A 1 4605 ? 190.649 141.553 199.991 1.00 9.59  ? 4605 VAL A C     1 
ATOM   23247 O  O     . VAL A 1 4605 ? 191.591 140.844 199.618 1.00 9.06  ? 4605 VAL A O     1 
ATOM   23248 C  CB    . VAL A 1 4605 ? 189.926 140.901 202.324 1.00 8.62  ? 4605 VAL A CB    1 
ATOM   23249 C  CG1   . VAL A 1 4605 ? 188.772 140.398 203.152 1.00 11.67 ? 4605 VAL A CG1   1 
ATOM   23250 C  CG2   . VAL A 1 4605 ? 191.145 140.012 202.533 1.00 14.72 ? 4605 VAL A CG2   1 
ATOM   23251 N  N     . THR A 1 4606 ? 190.526 142.834 199.656 1.00 13.08 ? 4606 THR A N     1 
ATOM   23252 C  CA    . THR A 1 4606 ? 191.588 143.560 198.977 1.00 6.77  ? 4606 THR A CA    1 
ATOM   23253 C  C     . THR A 1 4606 ? 192.457 144.237 200.029 1.00 6.76  ? 4606 THR A C     1 
ATOM   23254 O  O     . THR A 1 4606 ? 191.980 145.100 200.773 1.00 10.65 ? 4606 THR A O     1 
ATOM   23255 C  CB    . THR A 1 4606 ? 191.022 144.587 197.997 1.00 9.27  ? 4606 THR A CB    1 
ATOM   23256 O  OG1   . THR A 1 4606 ? 190.278 143.914 196.976 1.00 16.76 ? 4606 THR A OG1   1 
ATOM   23257 C  CG2   . THR A 1 4606 ? 192.144 145.380 197.356 1.00 7.71  ? 4606 THR A CG2   1 
ATOM   23258 N  N     . LEU A 1 4607 ? 193.719 143.840 200.097 1.00 9.22  ? 4607 LEU A N     1 
ATOM   23259 C  CA    . LEU A 1 4607 ? 194.623 144.354 201.107 1.00 7.03  ? 4607 LEU A CA    1 
ATOM   23260 C  C     . LEU A 1 4607 ? 195.548 145.394 200.508 1.00 4.26  ? 4607 LEU A C     1 
ATOM   23261 O  O     . LEU A 1 4607 ? 196.189 145.126 199.483 1.00 6.16  ? 4607 LEU A O     1 
ATOM   23262 C  CB    . LEU A 1 4607 ? 195.449 143.224 201.722 1.00 4.25  ? 4607 LEU A CB    1 
ATOM   23263 C  CG    . LEU A 1 4607 ? 194.725 142.268 202.669 1.00 6.41  ? 4607 LEU A CG    1 
ATOM   23264 C  CD1   . LEU A 1 4607 ? 195.743 141.484 203.470 1.00 4.95  ? 4607 LEU A CD1   1 
ATOM   23265 C  CD2   . LEU A 1 4607 ? 193.768 143.015 203.583 1.00 6.08  ? 4607 LEU A CD2   1 
ATOM   23266 N  N     . PRO A 1 4608 ? 195.637 146.583 201.094 1.00 4.59  ? 4608 PRO A N     1 
ATOM   23267 C  CA    . PRO A 1 4608 ? 196.659 147.534 200.656 1.00 6.39  ? 4608 PRO A CA    1 
ATOM   23268 C  C     . PRO A 1 4608 ? 198.049 146.999 200.950 1.00 6.97  ? 4608 PRO A C     1 
ATOM   23269 O  O     . PRO A 1 4608 ? 198.271 146.314 201.952 1.00 7.08  ? 4608 PRO A O     1 
ATOM   23270 C  CB    . PRO A 1 4608 ? 196.353 148.788 201.479 1.00 3.87  ? 4608 PRO A CB    1 
ATOM   23271 C  CG    . PRO A 1 4608 ? 195.683 148.272 202.701 1.00 2.92  ? 4608 PRO A CG    1 
ATOM   23272 C  CD    . PRO A 1 4608 ? 194.905 147.059 202.280 1.00 4.59  ? 4608 PRO A CD    1 
ATOM   23273 N  N     . VAL A 1 4609 ? 198.986 147.309 200.062 1.00 3.29  ? 4609 VAL A N     1 
ATOM   23274 C  CA    . VAL A 1 4609 ? 200.394 146.985 200.255 1.00 4.56  ? 4609 VAL A CA    1 
ATOM   23275 C  C     . VAL A 1 4609 ? 201.146 148.301 200.370 1.00 5.39  ? 4609 VAL A C     1 
ATOM   23276 O  O     . VAL A 1 4609 ? 201.339 149.003 199.370 1.00 8.17  ? 4609 VAL A O     1 
ATOM   23277 C  CB    . VAL A 1 4609 ? 200.958 146.123 199.119 1.00 5.29  ? 4609 VAL A CB    1 
ATOM   23278 C  CG1   . VAL A 1 4609 ? 202.396 145.740 199.417 1.00 3.95  ? 4609 VAL A CG1   1 
ATOM   23279 C  CG2   . VAL A 1 4609 ? 200.111 144.883 198.933 1.00 4.96  ? 4609 VAL A CG2   1 
ATOM   23280 N  N     . TYR A 1 4610 ? 201.564 148.638 201.582 1.00 6.69  ? 4610 TYR A N     1 
ATOM   23281 C  CA    . TYR A 1 4610 ? 202.304 149.865 201.822 1.00 5.04  ? 4610 TYR A CA    1 
ATOM   23282 C  C     . TYR A 1 4610 ? 203.802 149.593 201.805 1.00 7.45  ? 4610 TYR A C     1 
ATOM   23283 O  O     . TYR A 1 4610 ? 204.256 148.456 201.942 1.00 14.69 ? 4610 TYR A O     1 
ATOM   23284 C  CB    . TYR A 1 4610 ? 201.894 150.494 203.155 1.00 4.84  ? 4610 TYR A CB    1 
ATOM   23285 C  CG    . TYR A 1 4610 ? 200.445 150.911 203.208 1.00 3.57  ? 4610 TYR A CG    1 
ATOM   23286 C  CD1   . TYR A 1 4610 ? 200.016 152.064 202.567 1.00 6.04  ? 4610 TYR A CD1   1 
ATOM   23287 C  CD2   . TYR A 1 4610 ? 199.509 150.156 203.897 1.00 3.53  ? 4610 TYR A CD2   1 
ATOM   23288 C  CE1   . TYR A 1 4610 ? 198.693 152.452 202.613 1.00 4.82  ? 4610 TYR A CE1   1 
ATOM   23289 C  CE2   . TYR A 1 4610 ? 198.184 150.536 203.949 1.00 3.67  ? 4610 TYR A CE2   1 
ATOM   23290 C  CZ    . TYR A 1 4610 ? 197.783 151.685 203.304 1.00 4.39  ? 4610 TYR A CZ    1 
ATOM   23291 O  OH    . TYR A 1 4610 ? 196.465 152.070 203.350 1.00 7.07  ? 4610 TYR A OH    1 
ATOM   23292 N  N     . LEU A 1 4611 ? 204.572 150.665 201.623 1.00 7.82  ? 4611 LEU A N     1 
ATOM   23293 C  CA    . LEU A 1 4611 ? 206.020 150.522 201.531 1.00 9.32  ? 4611 LEU A CA    1 
ATOM   23294 C  C     . LEU A 1 4611 ? 206.632 150.164 202.880 1.00 11.20 ? 4611 LEU A C     1 
ATOM   23295 O  O     . LEU A 1 4611 ? 207.459 149.250 202.974 1.00 19.29 ? 4611 LEU A O     1 
ATOM   23296 C  CB    . LEU A 1 4611 ? 206.636 151.803 200.979 1.00 7.70  ? 4611 LEU A CB    1 
ATOM   23297 C  CG    . LEU A 1 4611 ? 208.156 151.771 200.849 1.00 13.19 ? 4611 LEU A CG    1 
ATOM   23298 C  CD1   . LEU A 1 4611 ? 208.595 150.666 199.903 1.00 14.37 ? 4611 LEU A CD1   1 
ATOM   23299 C  CD2   . LEU A 1 4611 ? 208.653 153.110 200.374 1.00 11.60 ? 4611 LEU A CD2   1 
ATOM   23300 N  N     . ASN A 1 4612 ? 206.237 150.867 203.938 1.00 11.19 ? 4612 ASN A N     1 
ATOM   23301 C  CA    . ASN A 1 4612 ? 206.795 150.634 205.264 1.00 9.27  ? 4612 ASN A CA    1 
ATOM   23302 C  C     . ASN A 1 4612 ? 205.686 150.788 206.299 1.00 8.97  ? 4612 ASN A C     1 
ATOM   23303 O  O     . ASN A 1 4612 ? 204.512 150.974 205.963 1.00 9.84  ? 4612 ASN A O     1 
ATOM   23304 C  CB    . ASN A 1 4612 ? 207.980 151.572 205.530 1.00 7.81  ? 4612 ASN A CB    1 
ATOM   23305 C  CG    . ASN A 1 4612 ? 207.659 153.018 205.238 1.00 9.00  ? 4612 ASN A CG    1 
ATOM   23306 O  OD1   . ASN A 1 4612 ? 206.870 153.643 205.941 1.00 12.39 ? 4612 ASN A OD1   1 
ATOM   23307 N  ND2   . ASN A 1 4612 ? 208.274 153.560 204.196 1.00 13.45 ? 4612 ASN A ND2   1 
ATOM   23308 N  N     . PHE A 1 4613 ? 206.074 150.712 207.575 1.00 8.93  ? 4613 PHE A N     1 
ATOM   23309 C  CA    . PHE A 1 4613 ? 205.118 150.691 208.676 1.00 4.57  ? 4613 PHE A CA    1 
ATOM   23310 C  C     . PHE A 1 4613 ? 204.325 151.984 208.797 1.00 5.90  ? 4613 PHE A C     1 
ATOM   23311 O  O     . PHE A 1 4613 ? 203.238 151.970 209.383 1.00 10.61 ? 4613 PHE A O     1 
ATOM   23312 C  CB    . PHE A 1 4613 ? 205.850 150.401 209.988 1.00 6.63  ? 4613 PHE A CB    1 
ATOM   23313 C  CG    . PHE A 1 4613 ? 206.775 151.501 210.426 1.00 6.79  ? 4613 PHE A CG    1 
ATOM   23314 C  CD1   . PHE A 1 4613 ? 206.327 152.520 211.252 1.00 8.41  ? 4613 PHE A CD1   1 
ATOM   23315 C  CD2   . PHE A 1 4613 ? 208.091 151.527 209.995 1.00 10.36 ? 4613 PHE A CD2   1 
ATOM   23316 C  CE1   . PHE A 1 4613 ? 207.173 153.534 211.645 1.00 11.88 ? 4613 PHE A CE1   1 
ATOM   23317 C  CE2   . PHE A 1 4613 ? 208.943 152.541 210.387 1.00 14.86 ? 4613 PHE A CE2   1 
ATOM   23318 C  CZ    . PHE A 1 4613 ? 208.483 153.545 211.212 1.00 19.45 ? 4613 PHE A CZ    1 
ATOM   23319 N  N     . THR A 1 4614 ? 204.837 153.098 208.272 1.00 7.49  ? 4614 THR A N     1 
ATOM   23320 C  CA    . THR A 1 4614 ? 204.109 154.359 208.367 1.00 7.76  ? 4614 THR A CA    1 
ATOM   23321 C  C     . THR A 1 4614 ? 202.846 154.367 207.516 1.00 8.68  ? 4614 THR A C     1 
ATOM   23322 O  O     . THR A 1 4614 ? 201.956 155.186 207.766 1.00 15.91 ? 4614 THR A O     1 
ATOM   23323 C  CB    . THR A 1 4614 ? 205.012 155.527 207.967 1.00 6.86  ? 4614 THR A CB    1 
ATOM   23324 O  OG1   . THR A 1 4614 ? 205.184 155.542 206.545 1.00 12.78 ? 4614 THR A OG1   1 
ATOM   23325 C  CG2   . THR A 1 4614 ? 206.366 155.408 208.641 1.00 7.31  ? 4614 THR A CG2   1 
ATOM   23326 N  N     . ARG A 1 4615 ? 202.757 153.484 206.519 1.00 6.47  ? 4615 ARG A N     1 
ATOM   23327 C  CA    . ARG A 1 4615 ? 201.588 153.363 205.645 1.00 5.65  ? 4615 ARG A CA    1 
ATOM   23328 C  C     . ARG A 1 4615 ? 201.280 154.670 204.923 1.00 5.06  ? 4615 ARG A C     1 
ATOM   23329 O  O     . ARG A 1 4615 ? 200.128 154.944 204.577 1.00 11.06 ? 4615 ARG A O     1 
ATOM   23330 C  CB    . ARG A 1 4615 ? 200.359 152.877 206.419 1.00 4.70  ? 4615 ARG A CB    1 
ATOM   23331 C  CG    . ARG A 1 4615 ? 200.544 151.515 207.058 1.00 3.04  ? 4615 ARG A CG    1 
ATOM   23332 C  CD    . ARG A 1 4615 ? 199.238 150.937 207.562 1.00 3.67  ? 4615 ARG A CD    1 
ATOM   23333 N  NE    . ARG A 1 4615 ? 199.457 149.673 208.252 1.00 6.51  ? 4615 ARG A NE    1 
ATOM   23334 C  CZ    . ARG A 1 4615 ? 198.494 148.882 208.703 1.00 2.20  ? 4615 ARG A CZ    1 
ATOM   23335 N  NH1   . ARG A 1 4615 ? 197.217 149.183 208.536 1.00 2.18  ? 4615 ARG A NH1   1 
ATOM   23336 N  NH2   . ARG A 1 4615 ? 198.821 147.757 209.330 1.00 2.41  ? 4615 ARG A NH2   1 
ATOM   23337 N  N     . ALA A 1 4616 ? 202.303 155.486 204.686 1.00 6.95  ? 4616 ALA A N     1 
ATOM   23338 C  CA    . ALA A 1 4616 ? 202.128 156.759 204.005 1.00 5.92  ? 4616 ALA A CA    1 
ATOM   23339 C  C     . ALA A 1 4616 ? 202.179 156.640 202.489 1.00 8.80  ? 4616 ALA A C     1 
ATOM   23340 O  O     . ALA A 1 4616 ? 201.824 157.601 201.798 1.00 17.80 ? 4616 ALA A O     1 
ATOM   23341 C  CB    . ALA A 1 4616 ? 203.192 157.757 204.471 1.00 6.21  ? 4616 ALA A CB    1 
ATOM   23342 N  N     . ASP A 1 4617 ? 202.601 155.496 201.957 1.00 11.57 ? 4617 ASP A N     1 
ATOM   23343 C  CA    . ASP A 1 4617 ? 202.796 155.329 200.518 1.00 14.13 ? 4617 ASP A CA    1 
ATOM   23344 C  C     . ASP A 1 4617 ? 202.219 153.985 200.098 1.00 9.23  ? 4617 ASP A C     1 
ATOM   23345 O  O     . ASP A 1 4617 ? 202.718 152.936 200.516 1.00 10.43 ? 4617 ASP A O     1 
ATOM   23346 C  CB    . ASP A 1 4617 ? 204.276 155.425 200.150 1.00 10.27 ? 4617 ASP A CB    1 
ATOM   23347 C  CG    . ASP A 1 4617 ? 204.915 156.710 200.634 1.00 20.40 ? 4617 ASP A CG    1 
ATOM   23348 O  OD1   . ASP A 1 4617 ? 205.699 156.658 201.603 1.00 19.30 ? 4617 ASP A OD1   1 
ATOM   23349 O  OD2   . ASP A 1 4617 ? 204.630 157.773 200.044 1.00 24.06 ? 4617 ASP A OD2   1 
ATOM   23350 N  N     . LEU A 1 4618 ? 201.182 154.017 199.269 1.00 9.04  ? 4618 LEU A N     1 
ATOM   23351 C  CA    . LEU A 1 4618 ? 200.607 152.795 198.724 1.00 8.23  ? 4618 LEU A CA    1 
ATOM   23352 C  C     . LEU A 1 4618 ? 201.390 152.359 197.493 1.00 9.92  ? 4618 LEU A C     1 
ATOM   23353 O  O     . LEU A 1 4618 ? 201.694 153.176 196.618 1.00 17.40 ? 4618 LEU A O     1 
ATOM   23354 C  CB    . LEU A 1 4618 ? 199.137 153.007 198.371 1.00 8.25  ? 4618 LEU A CB    1 
ATOM   23355 C  CG    . LEU A 1 4618 ? 198.394 151.766 197.875 1.00 10.31 ? 4618 LEU A CG    1 
ATOM   23356 C  CD1   . LEU A 1 4618 ? 198.220 150.762 199.003 1.00 7.67  ? 4618 LEU A CD1   1 
ATOM   23357 C  CD2   . LEU A 1 4618 ? 197.053 152.141 197.270 1.00 8.65  ? 4618 LEU A CD2   1 
ATOM   23358 N  N     . ILE A 1 4619 ? 201.722 151.072 197.431 1.00 5.06  ? 4619 ILE A N     1 
ATOM   23359 C  CA    . ILE A 1 4619 ? 202.465 150.523 196.303 1.00 10.03 ? 4619 ILE A CA    1 
ATOM   23360 C  C     . ILE A 1 4619 ? 201.488 149.892 195.319 1.00 8.79  ? 4619 ILE A C     1 
ATOM   23361 O  O     . ILE A 1 4619 ? 201.415 150.295 194.154 1.00 10.18 ? 4619 ILE A O     1 
ATOM   23362 C  CB    . ILE A 1 4619 ? 203.518 149.502 196.768 1.00 10.71 ? 4619 ILE A CB    1 
ATOM   23363 C  CG1   . ILE A 1 4619 ? 204.394 150.099 197.871 1.00 13.17 ? 4619 ILE A CG1   1 
ATOM   23364 C  CG2   . ILE A 1 4619 ? 204.375 149.051 195.598 1.00 7.71  ? 4619 ILE A CG2   1 
ATOM   23365 C  CD1   . ILE A 1 4619 ? 205.036 151.415 197.499 1.00 10.83 ? 4619 ILE A CD1   1 
ATOM   23366 N  N     . PHE A 1 4620 ? 200.734 148.900 195.783 1.00 5.65  ? 4620 PHE A N     1 
ATOM   23367 C  CA    . PHE A 1 4620 ? 199.736 148.231 194.959 1.00 5.56  ? 4620 PHE A CA    1 
ATOM   23368 C  C     . PHE A 1 4620 ? 198.754 147.524 195.885 1.00 8.29  ? 4620 PHE A C     1 
ATOM   23369 O  O     . PHE A 1 4620 ? 198.814 147.661 197.109 1.00 9.00  ? 4620 PHE A O     1 
ATOM   23370 C  CB    . PHE A 1 4620 ? 200.390 147.270 193.959 1.00 6.10  ? 4620 PHE A CB    1 
ATOM   23371 C  CG    . PHE A 1 4620 ? 201.077 146.091 194.590 1.00 5.75  ? 4620 PHE A CG    1 
ATOM   23372 C  CD1   . PHE A 1 4620 ? 202.289 146.242 195.242 1.00 8.75  ? 4620 PHE A CD1   1 
ATOM   23373 C  CD2   . PHE A 1 4620 ? 200.530 144.825 194.500 1.00 5.93  ? 4620 PHE A CD2   1 
ATOM   23374 C  CE1   . PHE A 1 4620 ? 202.928 145.159 195.812 1.00 5.65  ? 4620 PHE A CE1   1 
ATOM   23375 C  CE2   . PHE A 1 4620 ? 201.169 143.737 195.062 1.00 6.25  ? 4620 PHE A CE2   1 
ATOM   23376 C  CZ    . PHE A 1 4620 ? 202.367 143.904 195.722 1.00 7.27  ? 4620 PHE A CZ    1 
ATOM   23377 N  N     . THR A 1 4621 ? 197.834 146.774 195.287 1.00 8.00  ? 4621 THR A N     1 
ATOM   23378 C  CA    . THR A 1 4621 ? 196.787 146.082 196.022 1.00 6.28  ? 4621 THR A CA    1 
ATOM   23379 C  C     . THR A 1 4621 ? 196.830 144.596 195.700 1.00 11.07 ? 4621 THR A C     1 
ATOM   23380 O  O     . THR A 1 4621 ? 197.092 144.203 194.559 1.00 12.46 ? 4621 THR A O     1 
ATOM   23381 C  CB    . THR A 1 4621 ? 195.400 146.640 195.680 1.00 10.78 ? 4621 THR A CB    1 
ATOM   23382 O  OG1   . THR A 1 4621 ? 195.134 146.442 194.287 1.00 12.85 ? 4621 THR A OG1   1 
ATOM   23383 C  CG2   . THR A 1 4621 ? 195.335 148.124 195.990 1.00 9.14  ? 4621 THR A CG2   1 
ATOM   23384 N  N     . VAL A 1 4622 ? 196.571 143.777 196.711 1.00 8.43  ? 4622 VAL A N     1 
ATOM   23385 C  CA    . VAL A 1 4622 ? 196.495 142.332 196.555 1.00 8.71  ? 4622 VAL A CA    1 
ATOM   23386 C  C     . VAL A 1 4622 ? 195.103 141.867 196.952 1.00 10.39 ? 4622 VAL A C     1 
ATOM   23387 O  O     . VAL A 1 4622 ? 194.415 142.499 197.759 1.00 12.41 ? 4622 VAL A O     1 
ATOM   23388 C  CB    . VAL A 1 4622 ? 197.571 141.601 197.387 1.00 10.82 ? 4622 VAL A CB    1 
ATOM   23389 C  CG1   . VAL A 1 4622 ? 198.941 142.107 197.032 1.00 11.19 ? 4622 VAL A CG1   1 
ATOM   23390 C  CG2   . VAL A 1 4622 ? 197.321 141.816 198.866 1.00 8.56  ? 4622 VAL A CG2   1 
ATOM   23391 N  N     . ASP A 1 4623 ? 194.688 140.748 196.364 1.00 12.39 ? 4623 ASP A N     1 
ATOM   23392 C  CA    . ASP A 1 4623 ? 193.419 140.111 196.680 1.00 12.00 ? 4623 ASP A CA    1 
ATOM   23393 C  C     . ASP A 1 4623 ? 193.707 138.749 197.291 1.00 9.89  ? 4623 ASP A C     1 
ATOM   23394 O  O     . ASP A 1 4623 ? 194.440 137.945 196.703 1.00 13.09 ? 4623 ASP A O     1 
ATOM   23395 C  CB    . ASP A 1 4623 ? 192.541 139.968 195.436 1.00 10.73 ? 4623 ASP A CB    1 
ATOM   23396 C  CG    . ASP A 1 4623 ? 192.041 141.296 194.922 1.00 18.88 ? 4623 ASP A CG    1 
ATOM   23397 O  OD1   . ASP A 1 4623 ? 191.872 142.225 195.739 1.00 23.12 ? 4623 ASP A OD1   1 
ATOM   23398 O  OD2   . ASP A 1 4623 ? 191.813 141.415 193.699 1.00 30.85 ? 4623 ASP A OD2   1 
ATOM   23399 N  N     . PHE A 1 4624 ? 193.144 138.499 198.465 1.00 11.18 ? 4624 PHE A N     1 
ATOM   23400 C  CA    . PHE A 1 4624 ? 193.263 137.218 199.135 1.00 10.18 ? 4624 PHE A CA    1 
ATOM   23401 C  C     . PHE A 1 4624 ? 191.879 136.665 199.432 1.00 12.82 ? 4624 PHE A C     1 
ATOM   23402 O  O     . PHE A 1 4624 ? 190.900 137.404 199.542 1.00 16.82 ? 4624 PHE A O     1 
ATOM   23403 C  CB    . PHE A 1 4624 ? 194.048 137.331 200.443 1.00 8.49  ? 4624 PHE A CB    1 
ATOM   23404 C  CG    . PHE A 1 4624 ? 195.531 137.410 200.263 1.00 7.40  ? 4624 PHE A CG    1 
ATOM   23405 C  CD1   . PHE A 1 4624 ? 196.278 136.259 200.078 1.00 10.16 ? 4624 PHE A CD1   1 
ATOM   23406 C  CD2   . PHE A 1 4624 ? 196.186 138.626 200.309 1.00 8.89  ? 4624 PHE A CD2   1 
ATOM   23407 C  CE1   . PHE A 1 4624 ? 197.648 136.324 199.924 1.00 14.90 ? 4624 PHE A CE1   1 
ATOM   23408 C  CE2   . PHE A 1 4624 ? 197.556 138.694 200.156 1.00 10.90 ? 4624 PHE A CE2   1 
ATOM   23409 C  CZ    . PHE A 1 4624 ? 198.286 137.543 199.963 1.00 12.80 ? 4624 PHE A CZ    1 
ATOM   23410 N  N     . GLU A 1 4625 ? 191.806 135.342 199.589 1.00 12.06 ? 4625 GLU A N     1 
ATOM   23411 C  CA    . GLU A 1 4625 ? 190.519 134.715 199.983 1.00 14.26 ? 4625 GLU A CA    1 
ATOM   23412 C  C     . GLU A 1 4625 ? 190.575 134.435 201.492 1.00 17.02 ? 4625 GLU A C     1 
ATOM   23413 O  O     . GLU A 1 4625 ? 191.550 133.791 201.937 1.00 20.05 ? 4625 GLU A O     1 
ATOM   23414 C  CB    . GLU A 1 4625 ? 190.267 133.418 199.218 1.00 14.96 ? 4625 GLU A CB    1 
ATOM   23415 C  CG    . GLU A 1 4625 ? 189.056 132.650 199.735 1.00 17.06 ? 4625 GLU A CG    1 
ATOM   23416 C  CD    . GLU A 1 4625 ? 188.964 131.221 199.234 1.00 28.49 ? 4625 GLU A CD    1 
ATOM   23417 O  OE1   . GLU A 1 4625 ? 189.854 130.809 198.460 1.00 32.56 ? 4625 GLU A OE1   1 
ATOM   23418 O  OE2   . GLU A 1 4625 ? 188.006 130.521 199.617 1.00 28.61 ? 4625 GLU A OE2   1 
ATOM   23419 N  N     . ILE A 1 4626 ? 189.581 134.911 202.240 1.00 13.85 ? 4626 ILE A N     1 
ATOM   23420 C  CA    . ILE A 1 4626 ? 189.541 134.680 203.715 1.00 17.32 ? 4626 ILE A CA    1 
ATOM   23421 C  C     . ILE A 1 4626 ? 189.075 133.238 203.974 1.00 19.37 ? 4626 ILE A C     1 
ATOM   23422 O  O     . ILE A 1 4626 ? 188.579 132.599 203.022 1.00 22.00 ? 4626 ILE A O     1 
ATOM   23423 C  CB    . ILE A 1 4626 ? 188.628 135.712 204.400 1.00 18.34 ? 4626 ILE A CB    1 
ATOM   23424 C  CG1   . ILE A 1 4626 ? 187.185 135.585 203.924 1.00 17.33 ? 4626 ILE A CG1   1 
ATOM   23425 C  CG2   . ILE A 1 4626 ? 189.166 137.128 204.196 1.00 15.57 ? 4626 ILE A CG2   1 
ATOM   23426 C  CD1   . ILE A 1 4626 ? 186.323 136.792 204.239 1.00 21.74 ? 4626 ILE A CD1   1 
ATOM   23427 N  N     . ALA A 1 4627 ? 189.222 132.758 205.212 1.00 21.36 ? 4627 ALA A N     1 
ATOM   23428 C  CA    . ALA A 1 4627 ? 188.846 131.363 205.539 1.00 25.35 ? 4627 ALA A CA    1 
ATOM   23429 C  C     . ALA A 1 4627 ? 187.774 131.342 206.629 1.00 28.12 ? 4627 ALA A C     1 
ATOM   23430 O  O     . ALA A 1 4627 ? 187.448 132.421 207.171 1.00 31.56 ? 4627 ALA A O     1 
ATOM   23431 C  CB    . ALA A 1 4627 ? 190.076 130.592 205.965 1.00 21.46 ? 4627 ALA A CB    1 
ATOM   23432 N  N     . THR A 1 4628 ? 187.226 130.158 206.925 1.00 29.19 ? 4628 THR A N     1 
ATOM   23433 C  CA    . THR A 1 4628 ? 186.221 130.013 208.003 1.00 35.08 ? 4628 THR A CA    1 
ATOM   23434 C  C     . THR A 1 4628 ? 185.102 131.015 207.809 1.00 31.16 ? 4628 THR A C     1 
ATOM   23435 O  O     . THR A 1 4628 ? 184.726 131.267 206.644 1.00 31.25 ? 4628 THR A O     1 
ATOM   23436 C  CB    . THR A 1 4628 ? 186.890 130.173 209.369 1.00 28.98 ? 4628 THR A CB    1 
ATOM   23437 O  OG1   . THR A 1 4628 ? 187.149 131.565 209.526 1.00 27.59 ? 4628 THR A OG1   1 
ATOM   23438 C  CG2   . THR A 1 4628 ? 188.185 129.388 209.476 1.00 26.52 ? 4628 THR A CG2   1 
ATOM   23439 N  N     . LYS A 1 4629 ? 184.584 131.568 208.910 1.00 26.01 ? 4629 LYS A N     1 
ATOM   23440 C  CA    . LYS A 1 4629 ? 183.460 132.535 208.834 1.00 34.15 ? 4629 LYS A CA    1 
ATOM   23441 C  C     . LYS A 1 4629 ? 184.005 133.958 209.030 1.00 33.34 ? 4629 LYS A C     1 
ATOM   23442 O  O     . LYS A 1 4629 ? 183.191 134.873 209.290 1.00 34.17 ? 4629 LYS A O     1 
ATOM   23443 C  CB    . LYS A 1 4629 ? 182.408 132.201 209.896 1.00 31.43 ? 4629 LYS A CB    1 
ATOM   23444 C  CG    . LYS A 1 4629 ? 182.922 132.238 211.329 1.00 31.81 ? 4629 LYS A CG    1 
ATOM   23445 C  CD    . LYS A 1 4629 ? 181.873 131.814 212.351 1.00 32.82 ? 4629 LYS A CD    1 
ATOM   23446 C  CE    . LYS A 1 4629 ? 181.384 130.422 212.112 1.00 35.60 ? 4629 LYS A CE    1 
ATOM   23447 N  NZ    . LYS A 1 4629 ? 180.373 130.027 213.097 1.00 37.30 ? 4629 LYS A NZ    1 
ATOM   23448 N  N     . GLU A 1 4630 ? 185.323 134.132 208.906 1.00 26.47 ? 4630 GLU A N     1 
ATOM   23449 C  CA    . GLU A 1 4630 ? 185.941 135.467 209.111 1.00 24.22 ? 4630 GLU A CA    1 
ATOM   23450 C  C     . GLU A 1 4630 ? 185.172 136.505 208.282 1.00 28.73 ? 4630 GLU A C     1 
ATOM   23451 O  O     . GLU A 1 4630 ? 185.086 136.329 207.048 1.00 22.35 ? 4630 GLU A O     1 
ATOM   23452 C  CB    . GLU A 1 4630 ? 187.416 135.450 208.714 1.00 20.53 ? 4630 GLU A CB    1 
ATOM   23453 C  CG    . GLU A 1 4630 ? 188.242 134.438 209.503 1.00 24.84 ? 4630 GLU A CG    1 
ATOM   23454 C  CD    . GLU A 1 4630 ? 188.150 134.614 211.007 1.00 34.20 ? 4630 GLU A CD    1 
ATOM   23455 O  OE1   . GLU A 1 4630 ? 188.540 135.692 211.503 1.00 33.74 ? 4630 GLU A OE1   1 
ATOM   23456 O  OE2   . GLU A 1 4630 ? 187.680 133.672 211.681 1.00 32.61 ? 4630 GLU A OE2   1 
ATOM   23457 N  N     . ASP A 1 4631 ? 184.639 137.542 208.933 1.00 25.11 ? 4631 ASP A N     1 
ATOM   23458 C  CA    . ASP A 1 4631 ? 183.932 138.628 208.202 1.00 17.54 ? 4631 ASP A CA    1 
ATOM   23459 C  C     . ASP A 1 4631 ? 184.977 139.499 207.500 1.00 14.75 ? 4631 ASP A C     1 
ATOM   23460 O  O     . ASP A 1 4631 ? 185.873 140.020 208.192 1.00 17.94 ? 4631 ASP A O     1 
ATOM   23461 C  CB    . ASP A 1 4631 ? 183.050 139.446 209.132 1.00 20.23 ? 4631 ASP A CB    1 
ATOM   23462 C  CG    . ASP A 1 4631 ? 182.321 140.622 208.496 1.00 24.07 ? 4631 ASP A CG    1 
ATOM   23463 O  OD1   . ASP A 1 4631 ? 182.465 140.814 207.270 1.00 20.85 ? 4631 ASP A OD1   1 
ATOM   23464 O  OD2   . ASP A 1 4631 ? 181.615 141.342 209.235 1.00 28.15 ? 4631 ASP A OD2   1 
ATOM   23465 N  N     . PRO A 1 4632 ? 184.913 139.688 206.166 1.00 13.90 ? 4632 PRO A N     1 
ATOM   23466 C  CA    . PRO A 1 4632 ? 185.851 140.584 205.472 1.00 15.16 ? 4632 PRO A CA    1 
ATOM   23467 C  C     . PRO A 1 4632 ? 185.863 141.987 206.048 1.00 13.88 ? 4632 PRO A C     1 
ATOM   23468 O  O     . PRO A 1 4632 ? 186.876 142.689 205.939 1.00 10.77 ? 4632 PRO A O     1 
ATOM   23469 C  CB    . PRO A 1 4632 ? 185.344 140.565 204.021 1.00 13.02 ? 4632 PRO A CB    1 
ATOM   23470 C  CG    . PRO A 1 4632 ? 183.943 140.040 204.103 1.00 15.98 ? 4632 PRO A CG    1 
ATOM   23471 C  CD    . PRO A 1 4632 ? 183.961 139.067 205.232 1.00 13.76 ? 4632 PRO A CD    1 
ATOM   23472 N  N     . ARG A 1 4633 ? 184.759 142.412 206.660 1.00 17.18 ? 4633 ARG A N     1 
ATOM   23473 C  CA    . ARG A 1 4633 ? 184.706 143.729 207.284 1.00 13.26 ? 4633 ARG A CA    1 
ATOM   23474 C  C     . ARG A 1 4633 ? 185.617 143.803 208.505 1.00 12.56 ? 4633 ARG A C     1 
ATOM   23475 O  O     . ARG A 1 4633 ? 186.146 144.874 208.827 1.00 13.93 ? 4633 ARG A O     1 
ATOM   23476 C  CB    . ARG A 1 4633 ? 183.259 144.057 207.649 1.00 10.69 ? 4633 ARG A CB    1 
ATOM   23477 C  CG    . ARG A 1 4633 ? 182.369 144.213 206.424 1.00 14.62 ? 4633 ARG A CG    1 
ATOM   23478 C  CD    . ARG A 1 4633 ? 180.995 144.751 206.772 1.00 17.20 ? 4633 ARG A CD    1 
ATOM   23479 N  NE    . ARG A 1 4633 ? 180.229 143.808 207.579 1.00 14.01 ? 4633 ARG A NE    1 
ATOM   23480 C  CZ    . ARG A 1 4633 ? 179.773 144.069 208.795 1.00 18.85 ? 4633 ARG A CZ    1 
ATOM   23481 N  NH1   . ARG A 1 4633 ? 179.991 145.234 209.379 1.00 24.29 ? 4633 ARG A NH1   1 
ATOM   23482 N  NH2   . ARG A 1 4633 ? 179.078 143.136 209.440 1.00 20.56 ? 4633 ARG A NH2   1 
ATOM   23483 N  N     . SER A 1 4634 ? 185.808 142.679 209.199 1.00 9.02  ? 4634 SER A N     1 
ATOM   23484 C  CA    . SER A 1 4634 ? 186.725 142.657 210.334 1.00 6.69  ? 4634 SER A CA    1 
ATOM   23485 C  C     . SER A 1 4634 ? 188.162 142.885 209.883 1.00 8.47  ? 4634 SER A C     1 
ATOM   23486 O  O     . SER A 1 4634 ? 188.953 143.513 210.598 1.00 11.92 ? 4634 SER A O     1 
ATOM   23487 C  CB    . SER A 1 4634 ? 186.603 141.335 211.092 1.00 8.98  ? 4634 SER A CB    1 
ATOM   23488 O  OG    . SER A 1 4634 ? 187.007 140.243 210.286 1.00 17.77 ? 4634 SER A OG    1 
ATOM   23489 N  N     . PHE A 1 4635 ? 188.520 142.371 208.705 1.00 9.62  ? 4635 PHE A N     1 
ATOM   23490 C  CA    . PHE A 1 4635 ? 189.832 142.661 208.138 1.00 5.68  ? 4635 PHE A CA    1 
ATOM   23491 C  C     . PHE A 1 4635 ? 190.005 144.153 207.894 1.00 5.97  ? 4635 PHE A C     1 
ATOM   23492 O  O     . PHE A 1 4635 ? 191.092 144.704 208.098 1.00 6.79  ? 4635 PHE A O     1 
ATOM   23493 C  CB    . PHE A 1 4635 ? 190.026 141.877 206.840 1.00 6.72  ? 4635 PHE A CB    1 
ATOM   23494 C  CG    . PHE A 1 4635 ? 190.361 140.433 207.050 1.00 7.99  ? 4635 PHE A CG    1 
ATOM   23495 C  CD1   . PHE A 1 4635 ? 189.362 139.498 207.250 1.00 8.66  ? 4635 PHE A CD1   1 
ATOM   23496 C  CD2   . PHE A 1 4635 ? 191.678 140.003 207.032 1.00 8.20  ? 4635 PHE A CD2   1 
ATOM   23497 C  CE1   . PHE A 1 4635 ? 189.669 138.167 207.445 1.00 10.29 ? 4635 PHE A CE1   1 
ATOM   23498 C  CE2   . PHE A 1 4635 ? 191.991 138.672 207.224 1.00 6.65  ? 4635 PHE A CE2   1 
ATOM   23499 C  CZ    . PHE A 1 4635 ? 190.985 137.753 207.429 1.00 9.72  ? 4635 PHE A CZ    1 
ATOM   23500 N  N     . TYR A 1 4636 ? 188.939 144.823 207.451 1.00 8.33  ? 4636 TYR A N     1 
ATOM   23501 C  CA    . TYR A 1 4636 ? 189.016 146.256 207.204 1.00 5.05  ? 4636 TYR A CA    1 
ATOM   23502 C  C     . TYR A 1 4636 ? 189.175 147.026 208.509 1.00 4.29  ? 4636 TYR A C     1 
ATOM   23503 O  O     . TYR A 1 4636 ? 189.942 147.993 208.578 1.00 5.61  ? 4636 TYR A O     1 
ATOM   23504 C  CB    . TYR A 1 4636 ? 187.764 146.722 206.463 1.00 7.58  ? 4636 TYR A CB    1 
ATOM   23505 C  CG    . TYR A 1 4636 ? 187.513 146.007 205.158 1.00 7.63  ? 4636 TYR A CG    1 
ATOM   23506 C  CD1   . TYR A 1 4636 ? 186.224 145.858 204.669 1.00 10.45 ? 4636 TYR A CD1   1 
ATOM   23507 C  CD2   . TYR A 1 4636 ? 188.556 145.450 204.434 1.00 6.54  ? 4636 TYR A CD2   1 
ATOM   23508 C  CE1   . TYR A 1 4636 ? 185.983 145.196 203.487 1.00 11.82 ? 4636 TYR A CE1   1 
ATOM   23509 C  CE2   . TYR A 1 4636 ? 188.322 144.780 203.253 1.00 8.92  ? 4636 TYR A CE2   1 
ATOM   23510 C  CZ    . TYR A 1 4636 ? 187.035 144.661 202.782 1.00 12.89 ? 4636 TYR A CZ    1 
ATOM   23511 O  OH    . TYR A 1 4636 ? 186.797 143.997 201.600 1.00 18.38 ? 4636 TYR A OH    1 
ATOM   23512 N  N     . GLU A 1 4637 ? 188.465 146.599 209.558 1.00 4.43  ? 4637 GLU A N     1 
ATOM   23513 C  CA    . GLU A 1 4637 ? 188.464 147.339 210.817 1.00 3.99  ? 4637 GLU A CA    1 
ATOM   23514 C  C     . GLU A 1 4637 ? 189.757 147.135 211.595 1.00 4.18  ? 4637 GLU A C     1 
ATOM   23515 O  O     . GLU A 1 4637 ? 190.193 148.030 212.327 1.00 11.67 ? 4637 GLU A O     1 
ATOM   23516 C  CB    . GLU A 1 4637 ? 187.260 146.924 211.662 1.00 5.25  ? 4637 GLU A CB    1 
ATOM   23517 C  CG    . GLU A 1 4637 ? 185.937 147.427 211.127 1.00 7.20  ? 4637 GLU A CG    1 
ATOM   23518 C  CD    . GLU A 1 4637 ? 184.813 147.268 212.122 1.00 18.45 ? 4637 GLU A CD    1 
ATOM   23519 O  OE1   . GLU A 1 4637 ? 185.066 146.741 213.224 1.00 12.78 ? 4637 GLU A OE1   1 
ATOM   23520 O  OE2   . GLU A 1 4637 ? 183.676 147.673 211.803 1.00 25.75 ? 4637 GLU A OE2   1 
ATOM   23521 N  N     . ARG A 1 4638 ? 190.379 145.969 211.461 1.00 4.99  ? 4638 ARG A N     1 
ATOM   23522 C  CA    . ARG A 1 4638 ? 191.609 145.694 212.190 1.00 3.94  ? 4638 ARG A CA    1 
ATOM   23523 C  C     . ARG A 1 4638 ? 192.841 146.257 211.493 1.00 5.79  ? 4638 ARG A C     1 
ATOM   23524 O  O     . ARG A 1 4638 ? 193.949 146.112 212.016 1.00 6.19  ? 4638 ARG A O     1 
ATOM   23525 C  CB    . ARG A 1 4638 ? 191.763 144.188 212.406 1.00 3.10  ? 4638 ARG A CB    1 
ATOM   23526 C  CG    . ARG A 1 4638 ? 190.734 143.616 213.369 1.00 3.14  ? 4638 ARG A CG    1 
ATOM   23527 C  CD    . ARG A 1 4638 ? 190.823 142.110 213.485 1.00 5.73  ? 4638 ARG A CD    1 
ATOM   23528 N  NE    . ARG A 1 4638 ? 192.153 141.660 213.876 1.00 7.94  ? 4638 ARG A NE    1 
ATOM   23529 C  CZ    . ARG A 1 4638 ? 192.412 140.969 214.978 1.00 5.80  ? 4638 ARG A CZ    1 
ATOM   23530 N  NH1   . ARG A 1 4638 ? 191.458 140.635 215.827 1.00 3.18  ? 4638 ARG A NH1   1 
ATOM   23531 N  NH2   . ARG A 1 4638 ? 193.666 140.606 215.234 1.00 12.31 ? 4638 ARG A NH2   1 
ATOM   23532 N  N     . GLY A 1 4639 ? 192.669 146.900 210.343 1.00 4.01  ? 4639 GLY A N     1 
ATOM   23533 C  CA    . GLY A 1 4639 ? 193.791 147.468 209.620 1.00 3.28  ? 4639 GLY A CA    1 
ATOM   23534 C  C     . GLY A 1 4639 ? 194.742 146.436 209.061 1.00 4.22  ? 4639 GLY A C     1 
ATOM   23535 O  O     . GLY A 1 4639 ? 195.962 146.635 209.105 1.00 9.33  ? 4639 GLY A O     1 
ATOM   23536 N  N     . VAL A 1 4640 ? 194.212 145.328 208.540 1.00 4.06  ? 4640 VAL A N     1 
ATOM   23537 C  CA    . VAL A 1 4640 ? 195.062 144.315 207.935 1.00 3.87  ? 4640 VAL A CA    1 
ATOM   23538 C  C     . VAL A 1 4640 ? 195.651 144.861 206.644 1.00 5.69  ? 4640 VAL A C     1 
ATOM   23539 O  O     . VAL A 1 4640 ? 194.938 145.392 205.783 1.00 8.65  ? 4640 VAL A O     1 
ATOM   23540 C  CB    . VAL A 1 4640 ? 194.265 143.025 207.691 1.00 3.94  ? 4640 VAL A CB    1 
ATOM   23541 C  CG1   . VAL A 1 4640 ? 195.154 141.960 207.077 1.00 5.48  ? 4640 VAL A CG1   1 
ATOM   23542 C  CG2   . VAL A 1 4640 ? 193.648 142.534 208.987 1.00 4.97  ? 4640 VAL A CG2   1 
ATOM   23543 N  N     . ALA A 1 4641 ? 196.966 144.734 206.505 1.00 8.24  ? 4641 ALA A N     1 
ATOM   23544 C  CA    . ALA A 1 4641 ? 197.680 145.290 205.365 1.00 3.48  ? 4641 ALA A CA    1 
ATOM   23545 C  C     . ALA A 1 4641 ? 198.956 144.487 205.154 1.00 5.87  ? 4641 ALA A C     1 
ATOM   23546 O  O     . ALA A 1 4641 ? 199.290 143.594 205.936 1.00 5.98  ? 4641 ALA A O     1 
ATOM   23547 C  CB    . ALA A 1 4641 ? 197.982 146.778 205.573 1.00 3.24  ? 4641 ALA A CB    1 
ATOM   23548 N  N     . VAL A 1 4642 ? 199.670 144.819 204.082 1.00 8.28  ? 4642 VAL A N     1 
ATOM   23549 C  CA    . VAL A 1 4642 ? 200.937 144.188 203.738 1.00 3.64  ? 4642 VAL A CA    1 
ATOM   23550 C  C     . VAL A 1 4642 ? 201.992 145.276 203.622 1.00 4.68  ? 4642 VAL A C     1 
ATOM   23551 O  O     . VAL A 1 4642 ? 201.743 146.333 203.034 1.00 5.31  ? 4642 VAL A O     1 
ATOM   23552 C  CB    . VAL A 1 4642 ? 200.832 143.378 202.427 1.00 5.64  ? 4642 VAL A CB    1 
ATOM   23553 C  CG1   . VAL A 1 4642 ? 202.193 142.837 202.015 1.00 4.76  ? 4642 VAL A CG1   1 
ATOM   23554 C  CG2   . VAL A 1 4642 ? 199.830 142.245 202.581 1.00 3.75  ? 4642 VAL A CG2   1 
ATOM   23555 N  N     . LEU A 1 4643 ? 203.163 145.028 204.199 1.00 7.50  ? 4643 LEU A N     1 
ATOM   23556 C  CA    . LEU A 1 4643 ? 204.278 145.962 204.145 1.00 5.09  ? 4643 LEU A CA    1 
ATOM   23557 C  C     . LEU A 1 4643 ? 205.370 145.417 203.235 1.00 7.81  ? 4643 LEU A C     1 
ATOM   23558 O  O     . LEU A 1 4643 ? 205.672 144.221 203.259 1.00 10.28 ? 4643 LEU A O     1 
ATOM   23559 C  CB    . LEU A 1 4643 ? 204.854 146.224 205.537 1.00 7.42  ? 4643 LEU A CB    1 
ATOM   23560 C  CG    . LEU A 1 4643 ? 203.907 146.771 206.604 1.00 4.86  ? 4643 LEU A CG    1 
ATOM   23561 C  CD1   . LEU A 1 4643 ? 204.685 147.126 207.860 1.00 4.60  ? 4643 LEU A CD1   1 
ATOM   23562 C  CD2   . LEU A 1 4643 ? 203.126 147.967 206.091 1.00 5.03  ? 4643 LEU A CD2   1 
ATOM   23563 N  N     . CYS A 1 4644 ? 205.956 146.304 202.430 1.00 10.70 ? 4644 CYS A N     1 
ATOM   23564 C  CA    . CYS A 1 4644 ? 207.048 145.893 201.552 1.00 11.80 ? 4644 CYS A CA    1 
ATOM   23565 C  C     . CYS A 1 4644 ? 208.334 145.654 202.333 1.00 8.77  ? 4644 CYS A C     1 
ATOM   23566 O  O     . CYS A 1 4644 ? 209.147 144.812 201.937 1.00 15.47 ? 4644 CYS A O     1 
ATOM   23567 C  CB    . CYS A 1 4644 ? 207.275 146.943 200.463 1.00 11.64 ? 4644 CYS A CB    1 
ATOM   23568 S  SG    . CYS A 1 4644 ? 205.981 147.006 199.206 1.00 38.35 ? 4644 CYS A SG    1 
ATOM   23569 N  N     . THR A 1 4645 ? 208.537 146.377 203.429 1.00 8.55  ? 4645 THR A N     1 
ATOM   23570 C  CA    . THR A 1 4645 ? 209.740 146.217 204.238 1.00 12.85 ? 4645 THR A CA    1 
ATOM   23571 C  C     . THR A 1 4645 ? 209.440 146.382 205.725 1.00 10.61 ? 4645 THR A C     1 
ATOM   23572 O  O     . THR A 1 4645 ? 208.283 146.476 206.128 1.00 13.35 ? 4645 THR A O     1 
ATOM   23573 C  CB    . THR A 1 4645 ? 210.830 147.227 203.836 1.00 22.72 ? 4645 THR A CB    1 
ATOM   23574 O  OG1   . THR A 1 4645 ? 212.063 146.883 204.478 1.00 31.56 ? 4645 THR A OG1   1 
ATOM   23575 C  CG2   . THR A 1 4645 ? 210.428 148.639 204.242 1.00 8.63  ? 4645 THR A CG2   1 
HETATM 23576 P  PB    . ADP B 2 .    ? 193.974 172.233 190.694 1.00 0.03  ? 4701 ADP A PB    1 
HETATM 23577 O  O1B   . ADP B 2 .    ? 195.442 172.532 190.557 1.00 0.73  ? 4701 ADP A O1B   1 
HETATM 23578 O  O2B   . ADP B 2 .    ? 193.692 171.029 191.552 1.00 1.20  ? 4701 ADP A O2B   1 
HETATM 23579 O  O3B   . ADP B 2 .    ? 193.167 173.439 191.093 1.00 0.36  ? 4701 ADP A O3B   1 
HETATM 23580 P  PA    . ADP B 2 .    ? 192.780 172.705 188.070 1.00 0.07  ? 4701 ADP A PA    1 
HETATM 23581 O  O1A   . ADP B 2 .    ? 191.409 173.072 188.529 1.00 0.10  ? 4701 ADP A O1A   1 
HETATM 23582 O  O2A   . ADP B 2 .    ? 193.709 173.798 187.664 1.00 11.38 ? 4701 ADP A O2A   1 
HETATM 23583 O  O3A   . ADP B 2 .    ? 193.475 171.839 189.220 1.00 0.72  ? 4701 ADP A O3A   1 
HETATM 23584 O  "O5'" . ADP B 2 .    ? 192.689 171.622 186.894 1.00 1.64  ? 4701 ADP A "O5'" 1 
HETATM 23585 C  "C5'" . ADP B 2 .    ? 193.925 171.100 186.344 1.00 0.68  ? 4701 ADP A "C5'" 1 
HETATM 23586 C  "C4'" . ADP B 2 .    ? 193.706 170.710 184.903 1.00 0.84  ? 4701 ADP A "C4'" 1 
HETATM 23587 O  "O4'" . ADP B 2 .    ? 192.816 169.565 184.853 1.00 2.06  ? 4701 ADP A "O4'" 1 
HETATM 23588 C  "C3'" . ADP B 2 .    ? 193.043 171.774 184.018 1.00 0.86  ? 4701 ADP A "C3'" 1 
HETATM 23589 O  "O3'" . ADP B 2 .    ? 193.503 171.673 182.676 1.00 9.72  ? 4701 ADP A "O3'" 1 
HETATM 23590 C  "C2'" . ADP B 2 .    ? 191.565 171.394 184.131 1.00 0.35  ? 4701 ADP A "C2'" 1 
HETATM 23591 O  "O2'" . ADP B 2 .    ? 190.759 171.908 183.093 1.00 1.76  ? 4701 ADP A "O2'" 1 
HETATM 23592 C  "C1'" . ADP B 2 .    ? 191.674 169.875 184.090 1.00 0.82  ? 4701 ADP A "C1'" 1 
HETATM 23593 N  N9    . ADP B 2 .    ? 190.528 169.195 184.678 1.00 0.92  ? 4701 ADP A N9    1 
HETATM 23594 C  C8    . ADP B 2 .    ? 190.339 168.912 186.007 1.00 0.23  ? 4701 ADP A C8    1 
HETATM 23595 N  N7    . ADP B 2 .    ? 189.212 168.295 186.252 1.00 0.11  ? 4701 ADP A N7    1 
HETATM 23596 C  C5    . ADP B 2 .    ? 188.618 168.158 185.007 1.00 0.16  ? 4701 ADP A C5    1 
HETATM 23597 C  C6    . ADP B 2 .    ? 187.400 167.581 184.598 1.00 0.17  ? 4701 ADP A C6    1 
HETATM 23598 N  N6    . ADP B 2 .    ? 186.532 167.017 185.431 1.00 0.22  ? 4701 ADP A N6    1 
HETATM 23599 N  N1    . ADP B 2 .    ? 187.109 167.611 183.277 1.00 0.27  ? 4701 ADP A N1    1 
HETATM 23600 C  C2    . ADP B 2 .    ? 187.986 168.181 182.441 1.00 0.30  ? 4701 ADP A C2    1 
HETATM 23601 N  N3    . ADP B 2 .    ? 189.156 168.753 182.711 1.00 0.25  ? 4701 ADP A N3    1 
HETATM 23602 C  C4    . ADP B 2 .    ? 189.420 168.708 184.027 1.00 0.29  ? 4701 ADP A C4    1 
HETATM 23603 P  PG    . ATP C 3 .    ? 222.648 180.772 180.267 1.00 0.00  ? 4702 ATP A PG    1 
HETATM 23604 O  O1G   . ATP C 3 .    ? 222.473 179.412 180.879 1.00 0.13  ? 4702 ATP A O1G   1 
HETATM 23605 O  O2G   . ATP C 3 .    ? 221.400 181.606 180.334 1.00 0.08  ? 4702 ATP A O2G   1 
HETATM 23606 O  O3G   . ATP C 3 .    ? 223.849 181.494 180.796 1.00 0.32  ? 4702 ATP A O3G   1 
HETATM 23607 P  PB    . ATP C 3 .    ? 222.124 179.831 177.514 1.00 0.00  ? 4702 ATP A PB    1 
HETATM 23608 O  O1B   . ATP C 3 .    ? 222.019 178.374 177.800 1.00 0.06  ? 4702 ATP A O1B   1 
HETATM 23609 O  O2B   . ATP C 3 .    ? 220.892 180.627 177.262 1.00 0.02  ? 4702 ATP A O2B   1 
HETATM 23610 O  O3B   . ATP C 3 .    ? 222.941 180.523 178.704 1.00 0.05  ? 4702 ATP A O3B   1 
HETATM 23611 P  PA    . ATP C 3 .    ? 223.330 181.162 175.184 1.00 0.00  ? 4702 ATP A PA    1 
HETATM 23612 O  O1A   . ATP C 3 .    ? 222.936 182.481 175.751 1.00 3.21  ? 4702 ATP A O1A   1 
HETATM 23613 O  O2A   . ATP C 3 .    ? 222.663 180.715 173.929 1.00 0.02  ? 4702 ATP A O2A   1 
HETATM 23614 O  O3A   . ATP C 3 .    ? 223.145 180.030 176.301 1.00 0.03  ? 4702 ATP A O3A   1 
HETATM 23615 O  "O5'" . ATP C 3 .    ? 224.920 181.137 174.995 1.00 5.30  ? 4702 ATP A "O5'" 1 
HETATM 23616 C  "C5'" . ATP C 3 .    ? 225.549 180.038 174.296 1.00 1.34  ? 4702 ATP A "C5'" 1 
HETATM 23617 C  "C4'" . ATP C 3 .    ? 226.938 180.452 173.883 1.00 0.91  ? 4702 ATP A "C4'" 1 
HETATM 23618 O  "O4'" . ATP C 3 .    ? 227.269 179.803 172.633 1.00 4.12  ? 4702 ATP A "O4'" 1 
HETATM 23619 C  "C3'" . ATP C 3 .    ? 227.120 181.935 173.558 1.00 1.62  ? 4702 ATP A "C3'" 1 
HETATM 23620 O  "O3'" . ATP C 3 .    ? 228.495 182.290 173.528 1.00 23.47 ? 4702 ATP A "O3'" 1 
HETATM 23621 C  "C2'" . ATP C 3 .    ? 226.503 181.997 172.160 1.00 1.27  ? 4702 ATP A "C2'" 1 
HETATM 23622 O  "O2'" . ATP C 3 .    ? 226.979 183.078 171.388 1.00 11.03 ? 4702 ATP A "O2'" 1 
HETATM 23623 C  "C1'" . ATP C 3 .    ? 226.920 180.652 171.563 1.00 1.12  ? 4702 ATP A "C1'" 1 
HETATM 23624 N  N9    . ATP C 3 .    ? 225.852 180.014 170.805 1.00 0.46  ? 4702 ATP A N9    1 
HETATM 23625 C  C8    . ATP C 3 .    ? 224.567 179.771 171.218 1.00 0.22  ? 4702 ATP A C8    1 
HETATM 23626 N  N7    . ATP C 3 .    ? 223.840 179.191 170.291 1.00 0.30  ? 4702 ATP A N7    1 
HETATM 23627 C  C5    . ATP C 3 .    ? 224.695 179.066 169.204 1.00 0.33  ? 4702 ATP A C5    1 
HETATM 23628 C  C6    . ATP C 3 .    ? 224.522 178.533 167.913 1.00 0.46  ? 4702 ATP A C6    1 
HETATM 23629 N  N6    . ATP C 3 .    ? 223.380 178.009 167.478 1.00 0.46  ? 4702 ATP A N6    1 
HETATM 23630 N  N1    . ATP C 3 .    ? 225.587 178.565 167.080 1.00 0.79  ? 4702 ATP A N1    1 
HETATM 23631 C  C2    . ATP C 3 .    ? 226.734 179.094 167.524 1.00 0.73  ? 4702 ATP A C2    1 
HETATM 23632 N  N3    . ATP C 3 .    ? 227.012 179.625 168.712 1.00 0.84  ? 4702 ATP A N3    1 
HETATM 23633 C  C4    . ATP C 3 .    ? 225.936 179.575 169.514 1.00 0.42  ? 4702 ATP A C4    1 
HETATM 23634 P  PB    . ADP D 2 .    ? 243.977 190.180 199.420 1.00 0.01  ? 4703 ADP A PB    1 
HETATM 23635 O  O1B   . ADP D 2 .    ? 243.447 191.057 198.322 1.00 1.10  ? 4703 ADP A O1B   1 
HETATM 23636 O  O2B   . ADP D 2 .    ? 243.079 190.143 200.623 1.00 1.80  ? 4703 ADP A O2B   1 
HETATM 23637 O  O3B   . ADP D 2 .    ? 244.359 188.808 198.930 1.00 0.24  ? 4703 ADP A O3B   1 
HETATM 23638 P  PA    . ADP D 2 .    ? 245.915 192.357 199.824 1.00 0.11  ? 4703 ADP A PA    1 
HETATM 23639 O  O1A   . ADP D 2 .    ? 246.327 192.630 198.417 1.00 0.29  ? 4703 ADP A O1A   1 
HETATM 23640 O  O2A   . ADP D 2 .    ? 244.925 193.275 200.458 1.00 3.75  ? 4703 ADP A O2A   1 
HETATM 23641 O  O3A   . ADP D 2 .    ? 245.353 190.860 199.909 1.00 1.85  ? 4703 ADP A O3A   1 
HETATM 23642 O  "O5'" . ADP D 2 .    ? 247.210 192.256 200.760 1.00 1.08  ? 4703 ADP A "O5'" 1 
HETATM 23643 C  "C5'" . ADP D 2 .    ? 248.265 191.326 200.419 1.00 1.21  ? 4703 ADP A "C5'" 1 
HETATM 23644 C  "C4'" . ADP D 2 .    ? 249.388 191.469 201.415 1.00 0.60  ? 4703 ADP A "C4'" 1 
HETATM 23645 O  "O4'" . ADP D 2 .    ? 250.539 190.730 200.934 1.00 0.64  ? 4703 ADP A "O4'" 1 
HETATM 23646 C  "C3'" . ADP D 2 .    ? 249.895 192.897 201.654 1.00 1.07  ? 4703 ADP A "C3'" 1 
HETATM 23647 O  "O3'" . ADP D 2 .    ? 250.345 193.052 202.994 1.00 9.37  ? 4703 ADP A "O3'" 1 
HETATM 23648 C  "C2'" . ADP D 2 .    ? 251.050 192.992 200.657 1.00 0.59  ? 4703 ADP A "C2'" 1 
HETATM 23649 O  "O2'" . ADP D 2 .    ? 251.989 193.994 200.982 1.00 3.64  ? 4703 ADP A "O2'" 1 
HETATM 23650 C  "C1'" . ADP D 2 .    ? 251.641 191.591 200.768 1.00 0.52  ? 4703 ADP A "C1'" 1 
HETATM 23651 N  N9    . ADP D 2 .    ? 252.362 191.170 199.574 1.00 0.46  ? 4703 ADP A N9    1 
HETATM 23652 C  C8    . ADP D 2 .    ? 252.290 189.935 198.982 1.00 0.38  ? 4703 ADP A C8    1 
HETATM 23653 N  N7    . ADP D 2 .    ? 253.044 189.824 197.919 1.00 0.90  ? 4703 ADP A N7    1 
HETATM 23654 C  C5    . ADP D 2 .    ? 253.663 191.060 197.804 1.00 0.43  ? 4703 ADP A C5    1 
HETATM 23655 C  C6    . ADP D 2 .    ? 254.586 191.569 196.873 1.00 0.30  ? 4703 ADP A C6    1 
HETATM 23656 N  N6    . ADP D 2 .    ? 255.063 190.871 195.848 1.00 0.58  ? 4703 ADP A N6    1 
HETATM 23657 N  N1    . ADP D 2 .    ? 255.007 192.843 197.046 1.00 0.51  ? 4703 ADP A N1    1 
HETATM 23658 C  C2    . ADP D 2 .    ? 254.522 193.541 198.082 1.00 0.57  ? 4703 ADP A C2    1 
HETATM 23659 N  N3    . ADP D 2 .    ? 253.653 193.166 199.015 1.00 0.35  ? 4703 ADP A N3    1 
HETATM 23660 C  C4    . ADP D 2 .    ? 253.254 191.900 198.822 1.00 0.31  ? 4703 ADP A C4    1 
HETATM 23661 P  PB    . ADP E 2 .    ? 233.752 196.775 229.381 1.00 0.44  ? 4704 ADP A PB    1 
HETATM 23662 O  O1B   . ADP E 2 .    ? 234.771 195.674 229.511 1.00 1.06  ? 4704 ADP A O1B   1 
HETATM 23663 O  O2B   . ADP E 2 .    ? 234.045 197.711 228.239 1.00 1.45  ? 4704 ADP A O2B   1 
HETATM 23664 O  O3B   . ADP E 2 .    ? 232.339 196.260 229.364 1.00 1.03  ? 4704 ADP A O3B   1 
HETATM 23665 P  PA    . ADP E 2 .    ? 233.876 199.235 230.988 1.00 0.14  ? 4704 ADP A PA    1 
HETATM 23666 O  O1A   . ADP E 2 .    ? 235.082 199.836 230.351 1.00 0.49  ? 4704 ADP A O1A   1 
HETATM 23667 O  O2A   . ADP E 2 .    ? 232.537 199.779 230.618 1.00 3.90  ? 4704 ADP A O2A   1 
HETATM 23668 O  O3A   . ADP E 2 .    ? 233.890 197.657 230.720 1.00 0.95  ? 4704 ADP A O3A   1 
HETATM 23669 O  "O5'" . ADP E 2 .    ? 234.040 199.270 232.582 1.00 1.57  ? 4704 ADP A "O5'" 1 
HETATM 23670 C  "C5'" . ADP E 2 .    ? 232.913 198.895 233.411 1.00 1.25  ? 4704 ADP A "C5'" 1 
HETATM 23671 C  "C4'" . ADP E 2 .    ? 233.232 199.219 234.848 1.00 1.41  ? 4704 ADP A "C4'" 1 
HETATM 23672 O  "O4'" . ADP E 2 .    ? 234.120 198.209 235.393 1.00 2.11  ? 4704 ADP A "O4'" 1 
HETATM 23673 C  "C3'" . ADP E 2 .    ? 233.982 200.531 235.093 1.00 1.91  ? 4704 ADP A "C3'" 1 
HETATM 23674 O  "O3'" . ADP E 2 .    ? 233.105 201.650 235.089 1.00 12.37 ? 4704 ADP A "O3'" 1 
HETATM 23675 C  "C2'" . ADP E 2 .    ? 234.592 200.270 236.471 1.00 2.55  ? 4704 ADP A "C2'" 1 
HETATM 23676 O  "O2'" . ADP E 2 .    ? 233.668 200.483 237.513 1.00 2.11  ? 4704 ADP A "O2'" 1 
HETATM 23677 C  "C1'" . ADP E 2 .    ? 234.960 198.791 236.367 1.00 0.76  ? 4704 ADP A "C1'" 1 
HETATM 23678 N  N9    . ADP E 2 .    ? 236.348 198.546 235.990 1.00 0.60  ? 4704 ADP A N9    1 
HETATM 23679 C  C8    . ADP E 2 .    ? 236.812 198.172 234.754 1.00 1.29  ? 4704 ADP A C8    1 
HETATM 23680 N  N7    . ADP E 2 .    ? 238.111 198.024 234.712 1.00 1.66  ? 4704 ADP A N7    1 
HETATM 23681 C  C5    . ADP E 2 .    ? 238.535 198.331 235.994 1.00 0.72  ? 4704 ADP A C5    1 
HETATM 23682 C  C6    . ADP E 2 .    ? 239.812 198.368 236.586 1.00 0.99  ? 4704 ADP A C6    1 
HETATM 23683 N  N6    . ADP E 2 .    ? 240.935 198.078 235.941 1.00 0.77  ? 4704 ADP A N6    1 
HETATM 23684 N  N1    . ADP E 2 .    ? 239.885 198.718 237.892 1.00 1.61  ? 4704 ADP A N1    1 
HETATM 23685 C  C2    . ADP E 2 .    ? 238.750 199.009 238.539 1.00 1.18  ? 4704 ADP A C2    1 
HETATM 23686 N  N3    . ADP E 2 .    ? 237.500 199.010 238.088 1.00 0.85  ? 4704 ADP A N3    1 
HETATM 23687 C  C4    . ADP E 2 .    ? 237.457 198.660 236.791 1.00 0.57  ? 4704 ADP A C4    1 
HETATM 23688 MG MG    . MG  F 4 .    ? 193.957 175.363 191.401 1.00 0.63  ? 4705 MG  A MG    1 
HETATM 23689 MG MG    . MG  G 4 .    ? 220.579 182.296 178.561 1.00 0.04  ? 4706 MG  A MG    1 
# 
