data_9BM1
# 
_entry.id   9BM1 
# 
_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   9BM1         pdb_00009bm1 10.2210/pdb9bm1/pdb 
WWPDB D_1000283516 ?            ?                   
EMDB  EMD-44684    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1  'Structure model' 1 0 2025-04-23 ? 
2  'EM metadata'     1 0 2025-04-23 ? 
3  'Additional map'  1 0 2025-04-23 1 
4  FSC               1 0 2025-04-23 ? 
5  'Half map'        1 0 2025-04-23 1 
6  'Half map'        1 0 2025-04-23 2 
7  Image             1 0 2025-04-23 ? 
8  Mask              1 0 2025-04-23 1 
9  'Primary map'     1 0 2025-04-23 ? 
10 'Structure model' 1 1 2025-04-30 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Additional map'  repository 'Initial release' ? ? 
4 4 FSC               repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 'Half map'        repository 'Initial release' ? ? 
7 7 Image             repository 'Initial release' ? ? 
8 8 Mask              repository 'Initial release' ? ? 
9 9 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 10 'Structure model' 'Data collection'     
2 10 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 10 'Structure model' citation        
2 10 'Structure model' citation_author 
3 10 'Structure model' em_admin        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 10 'Structure model' '_citation.country'                 
2 10 'Structure model' '_citation.journal_abbrev'          
3 10 'Structure model' '_citation.journal_id_CSD'          
4 10 'Structure model' '_citation.journal_id_ISSN'         
5 10 'Structure model' '_citation.pdbx_database_id_DOI'    
6 10 'Structure model' '_citation.pdbx_database_id_PubMed' 
7 10 'Structure model' '_citation.title'                   
8 10 'Structure model' '_citation.year'                    
9 10 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BM1 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'State-3 of motor domain from full-length human dynein-1 in 5mM ATP' 
_pdbx_database_related.db_id          EMD-44684 
_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               ? 
_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 ?    ?   ?   A . n 
A 1 1458 ALA 1458 1458 ?    ?   ?   A . n 
A 1 1459 LEU 1459 1459 ?    ?   ?   A . n 
A 1 1460 GLU 1460 1460 ?    ?   ?   A . n 
A 1 1461 GLU 1461 1461 ?    ?   ?   A . n 
A 1 1462 PHE 1462 1462 ?    ?   ?   A . n 
A 1 1463 LEU 1463 1463 ?    ?   ?   A . n 
A 1 1464 LYS 1464 1464 ?    ?   ?   A . n 
A 1 1465 GLN 1465 1465 ?    ?   ?   A . n 
A 1 1466 ILE 1466 1466 ?    ?   ?   A . n 
A 1 1467 ARG 1467 1467 ?    ?   ?   A . n 
A 1 1468 GLU 1468 1468 ?    ?   ?   A . n 
A 1 1469 VAL 1469 1469 ?    ?   ?   A . n 
A 1 1470 TRP 1470 1470 ?    ?   ?   A . n 
A 1 1471 ASN 1471 1471 ?    ?   ?   A . n 
A 1 1472 THR 1472 1472 ?    ?   ?   A . n 
A 1 1473 TYR 1473 1473 ?    ?   ?   A . n 
A 1 1474 GLU 1474 1474 ?    ?   ?   A . n 
A 1 1475 LEU 1475 1475 ?    ?   ?   A . n 
A 1 1476 ASP 1476 1476 ?    ?   ?   A . n 
A 1 1477 LEU 1477 1477 ?    ?   ?   A . n 
A 1 1478 VAL 1478 1478 ?    ?   ?   A . n 
A 1 1479 ASN 1479 1479 ?    ?   ?   A . n 
A 1 1480 TYR 1480 1480 ?    ?   ?   A . n 
A 1 1481 GLN 1481 1481 ?    ?   ?   A . n 
A 1 1482 ASN 1482 1482 ?    ?   ?   A . n 
A 1 1483 LYS 1483 1483 ?    ?   ?   A . n 
A 1 1484 CYS 1484 1484 ?    ?   ?   A . n 
A 1 1485 ARG 1485 1485 ?    ?   ?   A . n 
A 1 1486 LEU 1486 1486 ?    ?   ?   A . n 
A 1 1487 ILE 1487 1487 ?    ?   ?   A . n 
A 1 1488 ARG 1488 1488 ?    ?   ?   A . n 
A 1 1489 GLY 1489 1489 ?    ?   ?   A . n 
A 1 1490 TRP 1490 1490 ?    ?   ?   A . n 
A 1 1491 ASP 1491 1491 ?    ?   ?   A . n 
A 1 1492 ASP 1492 1492 ?    ?   ?   A . n 
A 1 1493 LEU 1493 1493 ?    ?   ?   A . n 
A 1 1494 PHE 1494 1494 ?    ?   ?   A . n 
A 1 1495 ASN 1495 1495 ?    ?   ?   A . n 
A 1 1496 LYS 1496 1496 ?    ?   ?   A . n 
A 1 1497 VAL 1497 1497 ?    ?   ?   A . n 
A 1 1498 LYS 1498 1498 ?    ?   ?   A . n 
A 1 1499 GLU 1499 1499 ?    ?   ?   A . n 
A 1 1500 HIS 1500 1500 ?    ?   ?   A . n 
A 1 1501 ILE 1501 1501 ?    ?   ?   A . n 
A 1 1502 ASN 1502 1502 ?    ?   ?   A . n 
A 1 1503 SER 1503 1503 ?    ?   ?   A . n 
A 1 1504 VAL 1504 1504 ?    ?   ?   A . n 
A 1 1505 SER 1505 1505 ?    ?   ?   A . n 
A 1 1506 ALA 1506 1506 ?    ?   ?   A . n 
A 1 1507 MET 1507 1507 ?    ?   ?   A . n 
A 1 1508 LYS 1508 1508 ?    ?   ?   A . n 
A 1 1509 LEU 1509 1509 ?    ?   ?   A . n 
A 1 1510 SER 1510 1510 ?    ?   ?   A . n 
A 1 1511 PRO 1511 1511 ?    ?   ?   A . n 
A 1 1512 TYR 1512 1512 ?    ?   ?   A . n 
A 1 1513 TYR 1513 1513 ?    ?   ?   A . n 
A 1 1514 LYS 1514 1514 ?    ?   ?   A . n 
A 1 1515 VAL 1515 1515 ?    ?   ?   A . n 
A 1 1516 PHE 1516 1516 ?    ?   ?   A . n 
A 1 1517 GLU 1517 1517 ?    ?   ?   A . n 
A 1 1518 GLU 1518 1518 ?    ?   ?   A . n 
A 1 1519 ASP 1519 1519 ?    ?   ?   A . n 
A 1 1520 ALA 1520 1520 ?    ?   ?   A . n 
A 1 1521 LEU 1521 1521 ?    ?   ?   A . n 
A 1 1522 SER 1522 1522 ?    ?   ?   A . n 
A 1 1523 TRP 1523 1523 ?    ?   ?   A . n 
A 1 1524 GLU 1524 1524 ?    ?   ?   A . n 
A 1 1525 ASP 1525 1525 ?    ?   ?   A . n 
A 1 1526 LYS 1526 1526 ?    ?   ?   A . n 
A 1 1527 LEU 1527 1527 ?    ?   ?   A . n 
A 1 1528 ASN 1528 1528 ?    ?   ?   A . n 
A 1 1529 ARG 1529 1529 ?    ?   ?   A . n 
A 1 1530 ILE 1530 1530 ?    ?   ?   A . n 
A 1 1531 MET 1531 1531 ?    ?   ?   A . n 
A 1 1532 ALA 1532 1532 ?    ?   ?   A . n 
A 1 1533 LEU 1533 1533 ?    ?   ?   A . n 
A 1 1534 PHE 1534 1534 ?    ?   ?   A . n 
A 1 1535 ASP 1535 1535 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 2389 GLU GLU 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 3242 LYS LYS 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                   9BM1 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BM1 
_struct.title                        'State-3 of motor domain from full-length human dynein-1 in 5mM ATP' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BM1 
_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              9BM1 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 4646 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q14204 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  4646 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       4646 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,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   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 ASP A 1535 ? SER A 1554 ? ASP A 1535 SER A 1554 1 ? 20 
HELX_P HELX_P2   AA2 ASP A 1556 ? LEU A 1561 ? ASP A 1556 LEU A 1561 1 ? 6  
HELX_P HELX_P3   AA3 LEU A 1561 ? SER A 1585 ? LEU A 1561 SER A 1585 1 ? 25 
HELX_P HELX_P4   AA4 LEU A 1587 ? ASN A 1593 ? LEU A 1587 ASN A 1593 1 ? 7  
HELX_P HELX_P5   AA5 GLY A 1596 ? ALA A 1614 ? GLY A 1596 ALA A 1614 1 ? 19 
HELX_P HELX_P6   AA6 LEU A 1615 ? PHE A 1626 ? LEU A 1615 PHE A 1626 1 ? 12 
HELX_P HELX_P7   AA7 PRO A 1627 ? VAL A 1632 ? PRO A 1627 VAL A 1632 5 ? 6  
HELX_P HELX_P8   AA8 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P9   AA9 ASN A 1646 ? GLN A 1651 ? ASN A 1646 GLN A 1651 5 ? 6  
HELX_P HELX_P10  AB1 HIS A 1653 ? PHE A 1658 ? HIS A 1653 PHE A 1658 1 ? 6  
HELX_P HELX_P11  AB2 LYS A 1697 ? GLY A 1728 ? LYS A 1697 GLY A 1728 1 ? 32 
HELX_P HELX_P12  AB3 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P13  AB4 GLN A 1746 ? MET A 1769 ? GLN A 1746 MET A 1769 1 ? 24 
HELX_P HELX_P14  AB5 GLY A 1770 ? GLY A 1772 ? GLY A 1770 GLY A 1772 5 ? 3  
HELX_P HELX_P15  AB6 PRO A 1777 ? MET A 1798 ? PRO A 1777 MET A 1798 1 ? 22 
HELX_P HELX_P16  AB7 PRO A 1801 ? SER A 1828 ? PRO A 1801 SER A 1828 1 ? 28 
HELX_P HELX_P17  AB8 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P18  AB9 ASP A 1852 ? GLN A 1855 ? ASP A 1852 GLN A 1855 5 ? 4  
HELX_P HELX_P19  AC1 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P20  AC2 GLY A 1911 ? LEU A 1923 ? GLY A 1911 LEU A 1923 1 ? 13 
HELX_P HELX_P21  AC3 ASP A 1937 ? GLY A 1952 ? ASP A 1937 GLY A 1952 1 ? 16 
HELX_P HELX_P22  AC4 PHE A 1960 ? LEU A 1963 ? PHE A 1960 LEU A 1963 5 ? 4  
HELX_P HELX_P23  AC5 GLU A 1964 ? ASN A 1987 ? GLU A 1964 ASN A 1987 1 ? 24 
HELX_P HELX_P24  AC6 PRO A 2029 ? LYS A 2034 ? PRO A 2029 LYS A 2034 1 ? 6  
HELX_P HELX_P25  AC7 ASP A 2045 ? GLN A 2057 ? ASP A 2045 GLN A 2057 1 ? 13 
HELX_P HELX_P26  AC8 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P27  AC9 GLY A 2089 ? ARG A 2118 ? GLY A 2089 ARG A 2118 1 ? 30 
HELX_P HELX_P28  AD1 ASP A 2123 ? ASN A 2130 ? ASP A 2123 ASN A 2130 1 ? 8  
HELX_P HELX_P29  AD2 PRO A 2132 ? MET A 2145 ? PRO A 2132 MET A 2145 1 ? 14 
HELX_P HELX_P30  AD3 VAL A 2146 ? LEU A 2149 ? VAL A 2146 LEU A 2149 5 ? 4  
HELX_P HELX_P31  AD4 ASP A 2153 ? PHE A 2165 ? ASP A 2153 PHE A 2165 1 ? 13 
HELX_P HELX_P32  AD5 MET A 2175 ? MET A 2189 ? MET A 2175 MET A 2189 1 ? 15 
HELX_P HELX_P33  AD6 GLY A 2200 ? ASN A 2217 ? GLY A 2200 ASN A 2217 1 ? 18 
HELX_P HELX_P34  AD7 GLY A 2229 ? GLY A 2246 ? GLY A 2229 GLY A 2246 1 ? 18 
HELX_P HELX_P35  AD8 ASP A 2255 ? ILE A 2259 ? ASP A 2255 ILE A 2259 5 ? 5  
HELX_P HELX_P36  AD9 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P37  AE1 GLY A 2278 ? SER A 2290 ? GLY A 2278 SER A 2290 1 ? 13 
HELX_P HELX_P38  AE2 GLY A 2293 ? LYS A 2297 ? GLY A 2293 LYS A 2297 5 ? 5  
HELX_P HELX_P39  AE3 TRP A 2311 ? ASN A 2314 ? TRP A 2311 ASN A 2314 5 ? 4  
HELX_P HELX_P40  AE4 LEU A 2315 ? ASP A 2320 ? LEU A 2315 ASP A 2320 1 ? 6  
HELX_P HELX_P41  AE5 THR A 2352 ? SER A 2357 ? THR A 2352 SER A 2357 1 ? 6  
HELX_P HELX_P42  AE6 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P43  AE7 PRO A 2411 ? GLN A 2424 ? PRO A 2411 GLN A 2424 1 ? 14 
HELX_P HELX_P44  AE8 PRO A 2425 ? THR A 2428 ? PRO A 2425 THR A 2428 5 ? 4  
HELX_P HELX_P45  AE9 GLY A 2431 ? PHE A 2441 ? GLY A 2431 PHE A 2441 1 ? 11 
HELX_P HELX_P46  AF1 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P47  AF2 GLN A 2482 ? SER A 2503 ? GLN A 2482 SER A 2503 1 ? 22 
HELX_P HELX_P48  AF3 ARG A 2507 ? THR A 2522 ? ARG A 2507 THR A 2522 1 ? 16 
HELX_P HELX_P49  AF4 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P50  AF5 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P51  AF6 GLU A 2558 ? VAL A 2562 ? GLU A 2558 VAL A 2562 5 ? 5  
HELX_P HELX_P52  AF7 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P53  AF8 GLY A 2600 ? ALA A 2611 ? GLY A 2600 ALA A 2611 1 ? 12 
HELX_P HELX_P54  AF9 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P55  AG1 GLN A 2677 ? HIS A 2689 ? GLN A 2677 HIS A 2689 1 ? 13 
HELX_P HELX_P56  AG2 SER A 2724 ? ARG A 2729 ? SER A 2724 ARG A 2729 1 ? 6  
HELX_P HELX_P57  AG3 GLY A 2740 ? ARG A 2757 ? GLY A 2740 ARG A 2757 1 ? 18 
HELX_P HELX_P58  AG4 LEU A 2758 ? THR A 2764 ? LEU A 2758 THR A 2764 5 ? 7  
HELX_P HELX_P59  AG5 TYR A 2765 ? PHE A 2784 ? TYR A 2765 PHE A 2784 1 ? 20 
HELX_P HELX_P60  AG6 SER A 2795 ? ARG A 2811 ? SER A 2795 ARG A 2811 1 ? 17 
HELX_P HELX_P61  AG7 PRO A 2817 ? GLN A 2834 ? PRO A 2817 GLN A 2834 1 ? 18 
HELX_P HELX_P62  AG8 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P63  AG9 ASP A 2862 ? SER A 2868 ? ASP A 2862 SER A 2868 1 ? 7  
HELX_P HELX_P64  AH1 ASP A 2885 ? GLU A 2904 ? ASP A 2885 GLU A 2904 1 ? 20 
HELX_P HELX_P65  AH2 PHE A 2912 ? ARG A 2927 ? PHE A 2912 ARG A 2927 1 ? 16 
HELX_P HELX_P66  AH3 GLY A 2942 ? ASN A 2954 ? GLY A 2942 ASN A 2954 1 ? 13 
HELX_P HELX_P67  AH4 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P68  AH5 SER A 2997 ? VAL A 2999 ? SER A 2997 VAL A 2999 5 ? 3  
HELX_P HELX_P69  AH6 ASP A 3001 ? GLY A 3015 ? ASP A 3001 GLY A 3015 1 ? 15 
HELX_P HELX_P70  AH7 GLY A 3023 ? GLY A 3041 ? GLY A 3023 GLY A 3041 1 ? 19 
HELX_P HELX_P71  AH8 SER A 3046 ? ASN A 3061 ? SER A 3046 ASN A 3061 1 ? 16 
HELX_P HELX_P72  AH9 SER A 3071 ? SER A 3082 ? SER A 3071 SER A 3082 1 ? 12 
HELX_P HELX_P73  AI1 PRO A 3083 ? ARG A 3088 ? PRO A 3083 ARG A 3088 1 ? 6  
HELX_P HELX_P74  AI2 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P75  AI3 SER A 3138 ? GLY A 3165 ? SER A 3138 GLY A 3165 1 ? 28 
HELX_P HELX_P76  AI4 THR A 3172 ? LYS A 3241 ? THR A 3172 LYS A 3241 1 ? 70 
HELX_P HELX_P77  AI5 GLU A 3450 ? THR A 3495 ? GLU A 3450 THR A 3495 1 ? 46 
HELX_P HELX_P78  AI6 THR A 3495 ? ALA A 3517 ? THR A 3495 ALA A 3517 1 ? 23 
HELX_P HELX_P79  AI7 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P80  AI8 ALA A 3548 ? SER A 3554 ? ALA A 3548 SER A 3554 1 ? 7  
HELX_P HELX_P81  AI9 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P82  AJ1 ASP A 3570 ? ARG A 3582 ? ASP A 3570 ARG A 3582 1 ? 13 
HELX_P HELX_P83  AJ2 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P84  AJ3 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P85  AJ4 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P86  AJ5 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P87  AJ6 LEU A 3645 ? ASN A 3650 ? LEU A 3645 ASN A 3650 1 ? 6  
HELX_P HELX_P88  AJ7 PRO A 3689 ? VAL A 3696 ? PRO A 3689 VAL A 3696 1 ? 8  
HELX_P HELX_P89  AJ8 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P90  AJ9 ARG A 3721 ? VAL A 3756 ? ARG A 3721 VAL A 3756 1 ? 36 
HELX_P HELX_P91  AK1 ASP A 3763 ? SER A 3817 ? ASP A 3763 SER A 3817 1 ? 55 
HELX_P HELX_P92  AK2 LEU A 3818 ? ILE A 3821 ? LEU A 3818 ILE A 3821 5 ? 4  
HELX_P HELX_P93  AK3 SER A 3828 ? TYR A 3841 ? SER A 3828 TYR A 3841 1 ? 14 
HELX_P HELX_P94  AK4 ASN A 3843 ? LYS A 3847 ? ASN A 3843 LYS A 3847 5 ? 5  
HELX_P HELX_P95  AK5 ASP A 3851 ? GLY A 3874 ? ASP A 3851 GLY A 3874 1 ? 24 
HELX_P HELX_P96  AK6 LEU A 3876 ? GLY A 3894 ? LEU A 3876 GLY A 3894 1 ? 19 
HELX_P HELX_P97  AK7 TYR A 3901 ? ARG A 3910 ? TYR A 3901 ARG A 3910 1 ? 10 
HELX_P HELX_P98  AK8 GLY A 3911 ? ILE A 3914 ? GLY A 3911 ILE A 3914 5 ? 4  
HELX_P HELX_P99  AK9 SER A 3917 ? THR A 3921 ? SER A 3917 THR A 3921 5 ? 5  
HELX_P HELX_P100 AL1 THR A 3928 ? SER A 3939 ? THR A 3928 SER A 3939 1 ? 12 
HELX_P HELX_P101 AL2 CYS A 3940 ? LYS A 3945 ? CYS A 3940 LYS A 3945 5 ? 6  
HELX_P HELX_P102 AL3 ASP A 3946 ? ASP A 3954 ? ASP A 3946 ASP A 3954 1 ? 9  
HELX_P HELX_P103 AL4 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P104 AL5 THR A 3981 ? ARG A 3997 ? THR A 3981 ARG A 3997 1 ? 17 
HELX_P HELX_P105 AL6 ARG A 4000 ? GLY A 4014 ? ARG A 4000 GLY A 4014 1 ? 15 
HELX_P HELX_P106 AL7 ASP A 4026 ? THR A 4033 ? ASP A 4026 THR A 4033 1 ? 8  
HELX_P HELX_P107 AL8 ALA A 4051 ? ASN A 4063 ? ALA A 4051 ASN A 4063 1 ? 13 
HELX_P HELX_P108 AL9 SER A 4073 ? GLY A 4091 ? SER A 4073 GLY A 4091 1 ? 19 
HELX_P HELX_P109 AM1 ASN A 4098 ? LEU A 4101 ? ASN A 4098 LEU A 4101 5 ? 4  
HELX_P HELX_P110 AM2 ALA A 4102 ? SER A 4115 ? ALA A 4102 SER A 4115 1 ? 14 
HELX_P HELX_P111 AM3 PRO A 4135 ? GLY A 4142 ? PRO A 4135 GLY A 4142 1 ? 8  
HELX_P HELX_P112 AM4 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P113 AM5 PRO A 4165 ? CYS A 4170 ? PRO A 4165 CYS A 4170 1 ? 6  
HELX_P HELX_P114 AM6 ASN A 4174 ? ARG A 4193 ? ASN A 4174 ARG A 4193 1 ? 20 
HELX_P HELX_P115 AM7 TYR A 4196 ? TRP A 4201 ? TYR A 4196 TRP A 4201 1 ? 6  
HELX_P HELX_P116 AM8 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P117 AM9 SER A 4234 ? ILE A 4238 ? SER A 4234 ILE A 4238 5 ? 5  
HELX_P HELX_P118 AN1 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P119 AN2 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P120 AN3 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P121 AN4 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P122 AN5 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
HELX_P HELX_P123 AN6 PRO A 4324 ? ALA A 4327 ? PRO A 4324 ALA A 4327 5 ? 4  
HELX_P HELX_P124 AN7 GLU A 4328 ? MET A 4346 ? GLU A 4328 MET A 4346 1 ? 19 
HELX_P HELX_P125 AN8 ALA A 4375 ? ILE A 4391 ? ALA A 4375 ILE A 4391 1 ? 17 
HELX_P HELX_P126 AN9 THR A 4401 ? LYS A 4406 ? THR A 4401 LYS A 4406 1 ? 6  
HELX_P HELX_P127 AO1 ASP A 4407 ? GLU A 4439 ? ASP A 4407 GLU A 4439 1 ? 33 
HELX_P HELX_P128 AO2 THR A 4445 ? GLY A 4458 ? THR A 4445 GLY A 4458 1 ? 14 
HELX_P HELX_P129 AO3 THR A 4474 ? GLY A 4499 ? THR A 4474 GLY A 4499 1 ? 26 
HELX_P HELX_P130 AO4 GLY A 4500 ? ASN A 4506 ? GLY A 4500 ASN A 4506 1 ? 7  
HELX_P HELX_P131 AO5 VAL A 4516 ? SER A 4533 ? VAL A 4516 SER A 4533 1 ? 18 
HELX_P HELX_P132 AO6 SER A 4535 ? GLU A 4537 ? SER A 4535 GLU A 4537 5 ? 3  
HELX_P HELX_P133 AO7 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 ? ? ? ? ? ? ? 2.270 ? ? 
metalc2 metalc ? ? C ATP .    O2G ? ? ? 1_555 G MG . MG ? ? A ATP 4702 A MG 4706 1_555 ? ? ? ? ? ? ? 2.563 ? ? 
metalc3 metalc ? ? C ATP .    O2B ? ? ? 1_555 G MG . MG ? ? A ATP 4702 A MG 4706 1_555 ? ? ? ? ? ? ? 2.815 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   O2G 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   C 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   ATP 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    ATP 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     4702 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   G 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    MG 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     4706 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O2B 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   C 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   ATP 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    ATP 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     4702 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 74.4 
_pdbx_struct_conn_angle.value_esd             ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 5 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 5 ? 
AB2 ? 4 ? 
AB3 ? 2 ? 
AB4 ? 5 ? 
AB5 ? 5 ? 
AB6 ? 3 ? 
AB7 ? 5 ? 
AB8 ? 2 ? 
AB9 ? 4 ? 
AC1 ? 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 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB1 4 5 ? parallel      
AB2 1 2 ? anti-parallel 
AB2 2 3 ? parallel      
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB4 4 5 ? parallel      
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? parallel      
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB7 1 2 ? parallel      
AB7 2 3 ? parallel      
AB7 3 4 ? parallel      
AB7 4 5 ? parallel      
AB8 1 2 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? parallel      
AC1 3 4 ? anti-parallel 
AC1 4 5 ? parallel      
AC1 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 1663 ? LEU A 1666 ? SER A 1663 LEU A 1666 
AA1 2 VAL A 1672 ? SER A 1677 ? VAL A 1672 SER A 1677 
AA1 3 GLU A 1683 ? SER A 1691 ? GLU A 1683 SER A 1691 
AA2 1 MET A 1842 ? PHE A 1846 ? MET A 1842 PHE A 1846 
AA2 2 LEU A 1857 ? MET A 1861 ? LEU A 1857 MET A 1861 
AA2 3 ALA A 1864 ? ASN A 1867 ? ALA A 1864 ASN A 1867 
AA3 1 GLY A 1901 ? PHE A 1905 ? GLY A 1901 PHE A 1905 
AA3 2 PHE A 2036 ? ALA A 2040 ? PHE A 2036 ALA A 2040 
AA4 1 VAL A 1927 ? ASN A 1931 ? VAL A 1927 ASN A 1931 
AA4 2 TRP A 1954 ? ASP A 1958 ? TRP A 1954 ASP A 1958 
AA4 3 ALA A 2013 ? THR A 2017 ? ALA A 2013 THR A 2017 
AA5 1 THR A 1998 ? LEU A 2001 ? THR A 1998 LEU A 2001 
AA5 2 LYS A 2004 ? LYS A 2007 ? LYS A 2004 LYS A 2007 
AA6 1 GLY A 2249 ? ILE A 2254 ? GLY A 2249 ILE A 2254 
AA6 2 ARG A 2298 ? ASP A 2304 ? ARG A 2298 ASP A 2304 
AA6 3 VAL A 2339 ? VAL A 2345 ? VAL A 2339 VAL A 2345 
AA6 4 GLY A 2219 ? VAL A 2223 ? GLY A 2219 VAL A 2223 
AA6 5 GLY A 2360 ? TRP A 2363 ? GLY A 2360 TRP A 2363 
AA7 1 GLY A 2266 ? LEU A 2268 ? GLY A 2266 LEU A 2268 
AA7 2 TRP A 2275 ? ASP A 2277 ? TRP A 2275 ASP A 2277 
AA8 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AA8 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AA9 1 TYR A 2537 ? VAL A 2539 ? TYR A 2537 VAL A 2539 
AA9 2 TRP A 2545 ? PRO A 2547 ? TRP A 2545 PRO A 2547 
AB1 1 MET A 2615 ? LEU A 2620 ? MET A 2615 LEU A 2620 
AB1 2 TRP A 2658 ? CYS A 2663 ? TRP A 2658 CYS A 2663 
AB1 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB1 4 LEU A 2591 ? CYS A 2594 ? LEU A 2591 CYS A 2594 
AB1 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB2 1 CYS A 2639 ? THR A 2644 ? CYS A 2639 THR A 2644 
AB2 2 GLY A 2647 ? PRO A 2652 ? GLY A 2647 PRO A 2652 
AB2 3 THR A 2699 ? LEU A 2703 ? THR A 2699 LEU A 2703 
AB2 4 GLY A 2691 ? ARG A 2694 ? GLY A 2691 ARG A 2694 
AB3 1 TYR A 2873 ? SER A 2874 ? TYR A 2873 SER A 2874 
AB3 2 ILE A 2882 ? PRO A 2883 ? ILE A 2882 PRO A 2883 
AB4 1 SER A 2957 ? TYR A 2959 ? SER A 2957 TYR A 2959 
AB4 2 ILE A 2990 ? ASP A 2995 ? ILE A 2990 ASP A 2995 
AB4 3 LEU A 3062 ? MET A 3068 ? LEU A 3062 MET A 3068 
AB4 4 HIS A 2932 ? ILE A 2936 ? HIS A 2932 ILE A 2936 
AB4 5 CYS A 3089 ? TRP A 3093 ? CYS A 3089 TRP A 3093 
AB5 1 THR A 3610 ? THR A 3612 ? THR A 3610 THR A 3612 
AB5 2 LEU A 3633 ? VAL A 3635 ? LEU A 3633 VAL A 3635 
AB5 3 ILE A 3677 ? THR A 3681 ? ILE A 3677 THR A 3681 
AB5 4 PRO A 3587 ? ILE A 3590 ? PRO A 3587 ILE A 3590 
AB5 5 THR A 3697 ? ASN A 3700 ? THR A 3697 ASN A 3700 
AB6 1 ARG A 3654 ? THR A 3656 ? ARG A 3654 THR A 3656 
AB6 2 ARG A 3659 ? LEU A 3664 ? ARG A 3659 LEU A 3664 
AB6 3 GLN A 3667 ? ASP A 3670 ? GLN A 3667 ASP A 3670 
AB7 1 ILE A 4066 ? ALA A 4070 ? ILE A 4066 ALA A 4070 
AB7 2 TRP A 4093 ? LYS A 4097 ? TRP A 4093 LYS A 4097 
AB7 3 ARG A 4123 ? GLU A 4129 ? ARG A 4123 GLU A 4129 
AB7 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB7 5 ARG A 4143 ? ILE A 4144 ? ARG A 4143 ILE A 4144 
AB8 1 LYS A 4283 ? ASP A 4289 ? LYS A 4283 ASP A 4289 
AB8 2 LYS A 4292 ? GLN A 4295 ? LYS A 4292 GLN A 4295 
AB9 1 VAL A 4509 ? CYS A 4510 ? VAL A 4509 CYS A 4510 
AB9 2 SER A 4557 ? THR A 4561 ? SER A 4557 THR A 4561 
AB9 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AB9 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AC1 1 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
AC1 2 LYS A 4574 ? ALA A 4584 ? LYS A 4574 ALA A 4584 
AC1 3 LEU A 4618 ? ILE A 4626 ? LEU A 4618 ILE A 4626 
AC1 4 VAL A 4604 ? TYR A 4610 ? VAL A 4604 TYR A 4610 
AC1 5 ALA A 4641 ? LEU A 4643 ? ALA A 4641 LEU A 4643 
AC1 6 LYS A 4564 ? 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 ILE A 1665 ? N ILE A 1665 O GLY A 1675 ? O GLY A 1675 
AA1 2 3 N VAL A 1673 ? N VAL A 1673 O VAL A 1690 ? O VAL A 1690 
AA2 1 2 N ARG A 1843 ? N ARG A 1843 O GLN A 1860 ? O GLN A 1860 
AA2 2 3 N ILE A 1859 ? N ILE A 1859 O PHE A 1866 ? O PHE A 1866 
AA3 1 2 N PHE A 1905 ? N PHE A 1905 O LEU A 2039 ? O LEU A 2039 
AA4 1 2 N LEU A 1928 ? N LEU A 1928 O TRP A 1954 ? O TRP A 1954 
AA4 2 3 N PHE A 1957 ? N PHE A 1957 O PHE A 2015 ? O PHE A 2015 
AA5 1 2 N CYS A 1999 ? N CYS A 1999 O VAL A 2006 ? O VAL A 2006 
AA6 1 2 N ILE A 2254 ? N ILE A 2254 O VAL A 2302 ? O VAL A 2302 
AA6 2 3 N PHE A 2303 ? N PHE A 2303 O MET A 2342 ? O MET A 2342 
AA6 3 4 O PHE A 2343 ? O PHE A 2343 N MET A 2222 ? N MET A 2222 
AA6 4 5 N MET A 2221 ? N MET A 2221 O VAL A 2362 ? O VAL A 2362 
AA7 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA8 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AA9 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB1 1 2 N LEU A 2620 ? N LEU A 2620 O PHE A 2662 ? O PHE A 2662 
AB1 2 3 N LEU A 2661 ? N LEU A 2661 O VAL A 2709 ? O VAL A 2709 
AB1 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 2593 ? N LEU A 2593 
AB1 4 5 N CYS A 2594 ? N CYS A 2594 O VAL A 2734 ? O VAL A 2734 
AB2 1 2 N ARG A 2642 ? N ARG A 2642 O VAL A 2649 ? O VAL A 2649 
AB2 2 3 N LEU A 2650 ? N LEU A 2650 O LYS A 2702 ? O LYS A 2702 
AB2 3 4 O VAL A 2701 ? O VAL A 2701 N PHE A 2692 ? N PHE A 2692 
AB3 1 2 N SER A 2874 ? N SER A 2874 O ILE A 2882 ? O ILE A 2882 
AB4 1 2 N SER A 2957 ? N SER A 2957 O ALA A 2991 ? O ALA A 2991 
AB4 2 3 N MET A 2994 ? N MET A 2994 O VAL A 3065 ? O VAL A 3065 
AB4 3 4 O VAL A 3064 ? O VAL A 3064 N LEU A 2933 ? N LEU A 2933 
AB4 4 5 N LEU A 2934 ? N LEU A 2934 O VAL A 3090 ? O VAL A 3090 
AB5 1 2 N THR A 3612 ? N THR A 3612 O LEU A 3634 ? O LEU A 3634 
AB5 2 3 N VAL A 3635 ? N VAL A 3635 O PHE A 3678 ? O PHE A 3678 
AB5 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB5 4 5 N LEU A 3588 ? N LEU A 3588 O VAL A 3699 ? O VAL A 3699 
AB6 1 2 N ARG A 3654 ? N ARG A 3654 O LEU A 3661 ? O LEU A 3661 
AB6 2 3 N ILE A 3662 ? N ILE A 3662 O ILE A 3669 ? O ILE A 3669 
AB7 1 2 N THR A 4067 ? N THR A 4067 O MET A 4095 ? O MET A 4095 
AB7 2 3 N VAL A 4094 ? N VAL A 4094 O PHE A 4125 ? O PHE A 4125 
AB7 3 4 O LEU A 4124 ? O LEU A 4124 N VAL A 4041 ? N VAL A 4041 
AB7 4 5 N LEU A 4042 ? N LEU A 4042 O ARG A 4143 ? O ARG A 4143 
AB8 1 2 N VAL A 4288 ? N VAL A 4288 O LYS A 4292 ? O LYS A 4292 
AB9 1 2 N VAL A 4509 ? N VAL A 4509 O GLY A 4559 ? O GLY A 4559 
AB9 2 3 N VAL A 4560 ? N VAL A 4560 O THR A 4588 ? O THR A 4588 
AB9 3 4 O ARG A 4591 ? O ARG A 4591 N GLU A 4542 ? N GLU A 4542 
AC1 1 2 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
AC1 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AC1 3 4 O PHE A 4624 ? O PHE A 4624 N VAL A 4605 ? N VAL A 4605 
AC1 4 5 N PRO A 4608 ? N PRO A 4608 O VAL A 4642 ? O VAL A 4642 
AC1 5 6 O LEU A 4643 ? O LEU A 4643 N LYS A 4564 ? N LYS A 4564 
# 
_pdbx_entry_details.entry_id                   9BM1 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 A GLU 2344 ? ? MG  A MG  4706 ? ? 1.69 
2 1 O   A LEU 1561 ? ? OG1 A THR 1565 ? ? 2.17 
# 
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 ? ? -96.96  33.18   
2  1 LYS A 1729 ? ? 38.28   49.53   
3  1 ALA A 1862 ? ? 61.53   -125.16 
4  1 ASN A 2130 ? ? -94.37  52.45   
5  1 ASP A 2505 ? ? -97.36  32.80   
6  1 ASP A 2672 ? ? -69.14  -178.08 
7  1 VAL A 2838 ? ? -97.28  -61.60  
8  1 ASN A 2860 ? ? -95.17  57.64   
9  1 GLU A 2904 ? ? -126.93 -166.44 
10 1 LEU A 2905 ? ? -36.38  127.96  
11 1 SER A 3082 ? ? -151.78 79.43   
12 1 LYS A 3608 ? ? 39.50   58.56   
13 1 PRO A 3643 ? ? -66.25  3.83    
14 1 GLU A 3842 ? ? 39.44   42.96   
15 1 ASP A 3946 ? ? -98.38  59.55   
16 1 LEU A 3973 ? ? -93.62  52.63   
17 1 GLU A 4034 ? ? 67.58   -1.43   
18 1 GLU A 4206 ? ? -92.95  53.83   
19 1 ASN A 4506 ? ? -96.45  33.17   
20 1 GLU A 4599 ? ? 59.96   -145.77 
21 1 LYS A 4629 ? ? 72.75   -5.53   
# 
_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     2025 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.100 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             TYR 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              2022 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             B 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -10.30 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BM1 
_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                    9BM1 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.02 
_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               105800 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       '25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 5 mM ATP' 
_em_buffer.pH            7.2 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'State-3 of motor domain from full-length human dynein-1 in 5mM ATP' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BM1 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             3000 
_em_imaging.calibrated_defocus_min          1200 
_em_imaging.calibrated_defocus_max          3000 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_em_imaging.calibrated_magnification        105000 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            50 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    GOLD 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R2/1' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9BM1 
_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                9BM1 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A MET 1    ? A MET 1    
2    1 Y 1 A SER 2    ? A SER 2    
3    1 Y 1 A GLU 3    ? A GLU 3    
4    1 Y 1 A PRO 4    ? A PRO 4    
5    1 Y 1 A GLY 5    ? A GLY 5    
6    1 Y 1 A GLY 6    ? A GLY 6    
7    1 Y 1 A GLY 7    ? A GLY 7    
8    1 Y 1 A GLY 8    ? A GLY 8    
9    1 Y 1 A GLY 9    ? A GLY 9    
10   1 Y 1 A GLU 10   ? A GLU 10   
11   1 Y 1 A ASP 11   ? A ASP 11   
12   1 Y 1 A GLY 12   ? A GLY 12   
13   1 Y 1 A SER 13   ? A SER 13   
14   1 Y 1 A ALA 14   ? A ALA 14   
15   1 Y 1 A GLY 15   ? A GLY 15   
16   1 Y 1 A LEU 16   ? A LEU 16   
17   1 Y 1 A GLU 17   ? A GLU 17   
18   1 Y 1 A VAL 18   ? A VAL 18   
19   1 Y 1 A SER 19   ? A SER 19   
20   1 Y 1 A ALA 20   ? A ALA 20   
21   1 Y 1 A VAL 21   ? A VAL 21   
22   1 Y 1 A GLN 22   ? A GLN 22   
23   1 Y 1 A ASN 23   ? A ASN 23   
24   1 Y 1 A VAL 24   ? A VAL 24   
25   1 Y 1 A ALA 25   ? A ALA 25   
26   1 Y 1 A ASP 26   ? A ASP 26   
27   1 Y 1 A VAL 27   ? A VAL 27   
28   1 Y 1 A SER 28   ? A SER 28   
29   1 Y 1 A VAL 29   ? A VAL 29   
30   1 Y 1 A LEU 30   ? A LEU 30   
31   1 Y 1 A GLN 31   ? A GLN 31   
32   1 Y 1 A LYS 32   ? A LYS 32   
33   1 Y 1 A HIS 33   ? A HIS 33   
34   1 Y 1 A LEU 34   ? A LEU 34   
35   1 Y 1 A ARG 35   ? A ARG 35   
36   1 Y 1 A LYS 36   ? A LYS 36   
37   1 Y 1 A LEU 37   ? A LEU 37   
38   1 Y 1 A VAL 38   ? A VAL 38   
39   1 Y 1 A PRO 39   ? A PRO 39   
40   1 Y 1 A LEU 40   ? A LEU 40   
41   1 Y 1 A LEU 41   ? A LEU 41   
42   1 Y 1 A LEU 42   ? A LEU 42   
43   1 Y 1 A GLU 43   ? A GLU 43   
44   1 Y 1 A ASP 44   ? A ASP 44   
45   1 Y 1 A GLY 45   ? A GLY 45   
46   1 Y 1 A GLY 46   ? A GLY 46   
47   1 Y 1 A GLU 47   ? A GLU 47   
48   1 Y 1 A ALA 48   ? A ALA 48   
49   1 Y 1 A PRO 49   ? A PRO 49   
50   1 Y 1 A ALA 50   ? A ALA 50   
51   1 Y 1 A ALA 51   ? A ALA 51   
52   1 Y 1 A LEU 52   ? A LEU 52   
53   1 Y 1 A GLU 53   ? A GLU 53   
54   1 Y 1 A ALA 54   ? A ALA 54   
55   1 Y 1 A ALA 55   ? A ALA 55   
56   1 Y 1 A LEU 56   ? A LEU 56   
57   1 Y 1 A GLU 57   ? A GLU 57   
58   1 Y 1 A GLU 58   ? A GLU 58   
59   1 Y 1 A LYS 59   ? A LYS 59   
60   1 Y 1 A SER 60   ? A SER 60   
61   1 Y 1 A ALA 61   ? A ALA 61   
62   1 Y 1 A LEU 62   ? A LEU 62   
63   1 Y 1 A GLU 63   ? A GLU 63   
64   1 Y 1 A GLN 64   ? A GLN 64   
65   1 Y 1 A MET 65   ? A MET 65   
66   1 Y 1 A ARG 66   ? A ARG 66   
67   1 Y 1 A LYS 67   ? A LYS 67   
68   1 Y 1 A PHE 68   ? A PHE 68   
69   1 Y 1 A LEU 69   ? A LEU 69   
70   1 Y 1 A SER 70   ? A SER 70   
71   1 Y 1 A ASP 71   ? A ASP 71   
72   1 Y 1 A PRO 72   ? A PRO 72   
73   1 Y 1 A GLN 73   ? A GLN 73   
74   1 Y 1 A VAL 74   ? A VAL 74   
75   1 Y 1 A HIS 75   ? A HIS 75   
76   1 Y 1 A THR 76   ? A THR 76   
77   1 Y 1 A VAL 77   ? A VAL 77   
78   1 Y 1 A LEU 78   ? A LEU 78   
79   1 Y 1 A VAL 79   ? A VAL 79   
80   1 Y 1 A GLU 80   ? A GLU 80   
81   1 Y 1 A ARG 81   ? A ARG 81   
82   1 Y 1 A SER 82   ? A SER 82   
83   1 Y 1 A THR 83   ? A THR 83   
84   1 Y 1 A LEU 84   ? A LEU 84   
85   1 Y 1 A LYS 85   ? A LYS 85   
86   1 Y 1 A GLU 86   ? A GLU 86   
87   1 Y 1 A ASP 87   ? A ASP 87   
88   1 Y 1 A VAL 88   ? A VAL 88   
89   1 Y 1 A GLY 89   ? A GLY 89   
90   1 Y 1 A ASP 90   ? A ASP 90   
91   1 Y 1 A GLU 91   ? A GLU 91   
92   1 Y 1 A GLY 92   ? A GLY 92   
93   1 Y 1 A GLU 93   ? A GLU 93   
94   1 Y 1 A GLU 94   ? A GLU 94   
95   1 Y 1 A GLU 95   ? A GLU 95   
96   1 Y 1 A LYS 96   ? A LYS 96   
97   1 Y 1 A GLU 97   ? A GLU 97   
98   1 Y 1 A PHE 98   ? A PHE 98   
99   1 Y 1 A ILE 99   ? A ILE 99   
100  1 Y 1 A SER 100  ? A SER 100  
101  1 Y 1 A TYR 101  ? A TYR 101  
102  1 Y 1 A ASN 102  ? A ASN 102  
103  1 Y 1 A ILE 103  ? A ILE 103  
104  1 Y 1 A ASN 104  ? A ASN 104  
105  1 Y 1 A ILE 105  ? A ILE 105  
106  1 Y 1 A ASP 106  ? A ASP 106  
107  1 Y 1 A ILE 107  ? A ILE 107  
108  1 Y 1 A HIS 108  ? A HIS 108  
109  1 Y 1 A TYR 109  ? A TYR 109  
110  1 Y 1 A GLY 110  ? A GLY 110  
111  1 Y 1 A VAL 111  ? A VAL 111  
112  1 Y 1 A LYS 112  ? A LYS 112  
113  1 Y 1 A SER 113  ? A SER 113  
114  1 Y 1 A ASN 114  ? A ASN 114  
115  1 Y 1 A SER 115  ? A SER 115  
116  1 Y 1 A LEU 116  ? A LEU 116  
117  1 Y 1 A ALA 117  ? A ALA 117  
118  1 Y 1 A PHE 118  ? A PHE 118  
119  1 Y 1 A ILE 119  ? A ILE 119  
120  1 Y 1 A LYS 120  ? A LYS 120  
121  1 Y 1 A ARG 121  ? A ARG 121  
122  1 Y 1 A THR 122  ? A THR 122  
123  1 Y 1 A PRO 123  ? A PRO 123  
124  1 Y 1 A VAL 124  ? A VAL 124  
125  1 Y 1 A ILE 125  ? A ILE 125  
126  1 Y 1 A ASP 126  ? A ASP 126  
127  1 Y 1 A ALA 127  ? A ALA 127  
128  1 Y 1 A ASP 128  ? A ASP 128  
129  1 Y 1 A LYS 129  ? A LYS 129  
130  1 Y 1 A PRO 130  ? A PRO 130  
131  1 Y 1 A VAL 131  ? A VAL 131  
132  1 Y 1 A SER 132  ? A SER 132  
133  1 Y 1 A SER 133  ? A SER 133  
134  1 Y 1 A GLN 134  ? A GLN 134  
135  1 Y 1 A LEU 135  ? A LEU 135  
136  1 Y 1 A ARG 136  ? A ARG 136  
137  1 Y 1 A VAL 137  ? A VAL 137  
138  1 Y 1 A LEU 138  ? A LEU 138  
139  1 Y 1 A THR 139  ? A THR 139  
140  1 Y 1 A LEU 140  ? A LEU 140  
141  1 Y 1 A SER 141  ? A SER 141  
142  1 Y 1 A GLU 142  ? A GLU 142  
143  1 Y 1 A ASP 143  ? A ASP 143  
144  1 Y 1 A SER 144  ? A SER 144  
145  1 Y 1 A PRO 145  ? A PRO 145  
146  1 Y 1 A TYR 146  ? A TYR 146  
147  1 Y 1 A GLU 147  ? A GLU 147  
148  1 Y 1 A THR 148  ? A THR 148  
149  1 Y 1 A LEU 149  ? A LEU 149  
150  1 Y 1 A HIS 150  ? A HIS 150  
151  1 Y 1 A SER 151  ? A SER 151  
152  1 Y 1 A PHE 152  ? A PHE 152  
153  1 Y 1 A ILE 153  ? A ILE 153  
154  1 Y 1 A SER 154  ? A SER 154  
155  1 Y 1 A ASN 155  ? A ASN 155  
156  1 Y 1 A ALA 156  ? A ALA 156  
157  1 Y 1 A VAL 157  ? A VAL 157  
158  1 Y 1 A ALA 158  ? A ALA 158  
159  1 Y 1 A PRO 159  ? A PRO 159  
160  1 Y 1 A PHE 160  ? A PHE 160  
161  1 Y 1 A PHE 161  ? A PHE 161  
162  1 Y 1 A LYS 162  ? A LYS 162  
163  1 Y 1 A SER 163  ? A SER 163  
164  1 Y 1 A TYR 164  ? A TYR 164  
165  1 Y 1 A ILE 165  ? A ILE 165  
166  1 Y 1 A ARG 166  ? A ARG 166  
167  1 Y 1 A GLU 167  ? A GLU 167  
168  1 Y 1 A SER 168  ? A SER 168  
169  1 Y 1 A GLY 169  ? A GLY 169  
170  1 Y 1 A LYS 170  ? A LYS 170  
171  1 Y 1 A ALA 171  ? A ALA 171  
172  1 Y 1 A ASP 172  ? A ASP 172  
173  1 Y 1 A ARG 173  ? A ARG 173  
174  1 Y 1 A ASP 174  ? A ASP 174  
175  1 Y 1 A GLY 175  ? A GLY 175  
176  1 Y 1 A ASP 176  ? A ASP 176  
177  1 Y 1 A LYS 177  ? A LYS 177  
178  1 Y 1 A MET 178  ? A MET 178  
179  1 Y 1 A ALA 179  ? A ALA 179  
180  1 Y 1 A PRO 180  ? A PRO 180  
181  1 Y 1 A SER 181  ? A SER 181  
182  1 Y 1 A VAL 182  ? A VAL 182  
183  1 Y 1 A GLU 183  ? A GLU 183  
184  1 Y 1 A LYS 184  ? A LYS 184  
185  1 Y 1 A LYS 185  ? A LYS 185  
186  1 Y 1 A ILE 186  ? A ILE 186  
187  1 Y 1 A ALA 187  ? A ALA 187  
188  1 Y 1 A GLU 188  ? A GLU 188  
189  1 Y 1 A LEU 189  ? A LEU 189  
190  1 Y 1 A GLU 190  ? A GLU 190  
191  1 Y 1 A MET 191  ? A MET 191  
192  1 Y 1 A GLY 192  ? A GLY 192  
193  1 Y 1 A LEU 193  ? A LEU 193  
194  1 Y 1 A LEU 194  ? A LEU 194  
195  1 Y 1 A HIS 195  ? A HIS 195  
196  1 Y 1 A LEU 196  ? A LEU 196  
197  1 Y 1 A GLN 197  ? A GLN 197  
198  1 Y 1 A GLN 198  ? A GLN 198  
199  1 Y 1 A ASN 199  ? A ASN 199  
200  1 Y 1 A ILE 200  ? A ILE 200  
201  1 Y 1 A GLU 201  ? A GLU 201  
202  1 Y 1 A ILE 202  ? A ILE 202  
203  1 Y 1 A PRO 203  ? A PRO 203  
204  1 Y 1 A GLU 204  ? A GLU 204  
205  1 Y 1 A ILE 205  ? A ILE 205  
206  1 Y 1 A SER 206  ? A SER 206  
207  1 Y 1 A LEU 207  ? A LEU 207  
208  1 Y 1 A PRO 208  ? A PRO 208  
209  1 Y 1 A ILE 209  ? A ILE 209  
210  1 Y 1 A HIS 210  ? A HIS 210  
211  1 Y 1 A PRO 211  ? A PRO 211  
212  1 Y 1 A MET 212  ? A MET 212  
213  1 Y 1 A ILE 213  ? A ILE 213  
214  1 Y 1 A THR 214  ? A THR 214  
215  1 Y 1 A ASN 215  ? A ASN 215  
216  1 Y 1 A VAL 216  ? A VAL 216  
217  1 Y 1 A ALA 217  ? A ALA 217  
218  1 Y 1 A LYS 218  ? A LYS 218  
219  1 Y 1 A GLN 219  ? A GLN 219  
220  1 Y 1 A CYS 220  ? A CYS 220  
221  1 Y 1 A TYR 221  ? A TYR 221  
222  1 Y 1 A GLU 222  ? A GLU 222  
223  1 Y 1 A ARG 223  ? A ARG 223  
224  1 Y 1 A GLY 224  ? A GLY 224  
225  1 Y 1 A GLU 225  ? A GLU 225  
226  1 Y 1 A LYS 226  ? A LYS 226  
227  1 Y 1 A PRO 227  ? A PRO 227  
228  1 Y 1 A LYS 228  ? A LYS 228  
229  1 Y 1 A VAL 229  ? A VAL 229  
230  1 Y 1 A THR 230  ? A THR 230  
231  1 Y 1 A ASP 231  ? A ASP 231  
232  1 Y 1 A PHE 232  ? A PHE 232  
233  1 Y 1 A GLY 233  ? A GLY 233  
234  1 Y 1 A ASP 234  ? A ASP 234  
235  1 Y 1 A LYS 235  ? A LYS 235  
236  1 Y 1 A VAL 236  ? A VAL 236  
237  1 Y 1 A GLU 237  ? A GLU 237  
238  1 Y 1 A ASP 238  ? A ASP 238  
239  1 Y 1 A PRO 239  ? A PRO 239  
240  1 Y 1 A THR 240  ? A THR 240  
241  1 Y 1 A PHE 241  ? A PHE 241  
242  1 Y 1 A LEU 242  ? A LEU 242  
243  1 Y 1 A ASN 243  ? A ASN 243  
244  1 Y 1 A GLN 244  ? A GLN 244  
245  1 Y 1 A LEU 245  ? A LEU 245  
246  1 Y 1 A GLN 246  ? A GLN 246  
247  1 Y 1 A SER 247  ? A SER 247  
248  1 Y 1 A GLY 248  ? A GLY 248  
249  1 Y 1 A VAL 249  ? A VAL 249  
250  1 Y 1 A ASN 250  ? A ASN 250  
251  1 Y 1 A ARG 251  ? A ARG 251  
252  1 Y 1 A TRP 252  ? A TRP 252  
253  1 Y 1 A ILE 253  ? A ILE 253  
254  1 Y 1 A ARG 254  ? A ARG 254  
255  1 Y 1 A GLU 255  ? A GLU 255  
256  1 Y 1 A ILE 256  ? A ILE 256  
257  1 Y 1 A GLN 257  ? A GLN 257  
258  1 Y 1 A LYS 258  ? A LYS 258  
259  1 Y 1 A VAL 259  ? A VAL 259  
260  1 Y 1 A THR 260  ? A THR 260  
261  1 Y 1 A LYS 261  ? A LYS 261  
262  1 Y 1 A LEU 262  ? A LEU 262  
263  1 Y 1 A ASP 263  ? A ASP 263  
264  1 Y 1 A ARG 264  ? A ARG 264  
265  1 Y 1 A ASP 265  ? A ASP 265  
266  1 Y 1 A PRO 266  ? A PRO 266  
267  1 Y 1 A ALA 267  ? A ALA 267  
268  1 Y 1 A SER 268  ? A SER 268  
269  1 Y 1 A GLY 269  ? A GLY 269  
270  1 Y 1 A THR 270  ? A THR 270  
271  1 Y 1 A ALA 271  ? A ALA 271  
272  1 Y 1 A LEU 272  ? A LEU 272  
273  1 Y 1 A GLN 273  ? A GLN 273  
274  1 Y 1 A GLU 274  ? A GLU 274  
275  1 Y 1 A ILE 275  ? A ILE 275  
276  1 Y 1 A SER 276  ? A SER 276  
277  1 Y 1 A PHE 277  ? A PHE 277  
278  1 Y 1 A TRP 278  ? A TRP 278  
279  1 Y 1 A LEU 279  ? A LEU 279  
280  1 Y 1 A ASN 280  ? A ASN 280  
281  1 Y 1 A LEU 281  ? A LEU 281  
282  1 Y 1 A GLU 282  ? A GLU 282  
283  1 Y 1 A ARG 283  ? A ARG 283  
284  1 Y 1 A ALA 284  ? A ALA 284  
285  1 Y 1 A LEU 285  ? A LEU 285  
286  1 Y 1 A TYR 286  ? A TYR 286  
287  1 Y 1 A ARG 287  ? A ARG 287  
288  1 Y 1 A ILE 288  ? A ILE 288  
289  1 Y 1 A GLN 289  ? A GLN 289  
290  1 Y 1 A GLU 290  ? A GLU 290  
291  1 Y 1 A LYS 291  ? A LYS 291  
292  1 Y 1 A ARG 292  ? A ARG 292  
293  1 Y 1 A GLU 293  ? A GLU 293  
294  1 Y 1 A SER 294  ? A SER 294  
295  1 Y 1 A PRO 295  ? A PRO 295  
296  1 Y 1 A GLU 296  ? A GLU 296  
297  1 Y 1 A VAL 297  ? A VAL 297  
298  1 Y 1 A LEU 298  ? A LEU 298  
299  1 Y 1 A LEU 299  ? A LEU 299  
300  1 Y 1 A THR 300  ? A THR 300  
301  1 Y 1 A LEU 301  ? A LEU 301  
302  1 Y 1 A ASP 302  ? A ASP 302  
303  1 Y 1 A ILE 303  ? A ILE 303  
304  1 Y 1 A LEU 304  ? A LEU 304  
305  1 Y 1 A LYS 305  ? A LYS 305  
306  1 Y 1 A HIS 306  ? A HIS 306  
307  1 Y 1 A GLY 307  ? A GLY 307  
308  1 Y 1 A LYS 308  ? A LYS 308  
309  1 Y 1 A ARG 309  ? A ARG 309  
310  1 Y 1 A PHE 310  ? A PHE 310  
311  1 Y 1 A HIS 311  ? A HIS 311  
312  1 Y 1 A ALA 312  ? A ALA 312  
313  1 Y 1 A THR 313  ? A THR 313  
314  1 Y 1 A VAL 314  ? A VAL 314  
315  1 Y 1 A SER 315  ? A SER 315  
316  1 Y 1 A PHE 316  ? A PHE 316  
317  1 Y 1 A ASP 317  ? A ASP 317  
318  1 Y 1 A THR 318  ? A THR 318  
319  1 Y 1 A ASP 319  ? A ASP 319  
320  1 Y 1 A THR 320  ? A THR 320  
321  1 Y 1 A GLY 321  ? A GLY 321  
322  1 Y 1 A LEU 322  ? A LEU 322  
323  1 Y 1 A LYS 323  ? A LYS 323  
324  1 Y 1 A GLN 324  ? A GLN 324  
325  1 Y 1 A ALA 325  ? A ALA 325  
326  1 Y 1 A LEU 326  ? A LEU 326  
327  1 Y 1 A GLU 327  ? A GLU 327  
328  1 Y 1 A THR 328  ? A THR 328  
329  1 Y 1 A VAL 329  ? A VAL 329  
330  1 Y 1 A ASN 330  ? A ASN 330  
331  1 Y 1 A ASP 331  ? A ASP 331  
332  1 Y 1 A TYR 332  ? A TYR 332  
333  1 Y 1 A ASN 333  ? A ASN 333  
334  1 Y 1 A PRO 334  ? A PRO 334  
335  1 Y 1 A LEU 335  ? A LEU 335  
336  1 Y 1 A MET 336  ? A MET 336  
337  1 Y 1 A LYS 337  ? A LYS 337  
338  1 Y 1 A ASP 338  ? A ASP 338  
339  1 Y 1 A PHE 339  ? A PHE 339  
340  1 Y 1 A PRO 340  ? A PRO 340  
341  1 Y 1 A LEU 341  ? A LEU 341  
342  1 Y 1 A ASN 342  ? A ASN 342  
343  1 Y 1 A ASP 343  ? A ASP 343  
344  1 Y 1 A LEU 344  ? A LEU 344  
345  1 Y 1 A LEU 345  ? A LEU 345  
346  1 Y 1 A SER 346  ? A SER 346  
347  1 Y 1 A ALA 347  ? A ALA 347  
348  1 Y 1 A THR 348  ? A THR 348  
349  1 Y 1 A GLU 349  ? A GLU 349  
350  1 Y 1 A LEU 350  ? A LEU 350  
351  1 Y 1 A ASP 351  ? A ASP 351  
352  1 Y 1 A LYS 352  ? A LYS 352  
353  1 Y 1 A ILE 353  ? A ILE 353  
354  1 Y 1 A ARG 354  ? A ARG 354  
355  1 Y 1 A GLN 355  ? A GLN 355  
356  1 Y 1 A ALA 356  ? A ALA 356  
357  1 Y 1 A LEU 357  ? A LEU 357  
358  1 Y 1 A VAL 358  ? A VAL 358  
359  1 Y 1 A ALA 359  ? A ALA 359  
360  1 Y 1 A ILE 360  ? A ILE 360  
361  1 Y 1 A PHE 361  ? A PHE 361  
362  1 Y 1 A THR 362  ? A THR 362  
363  1 Y 1 A HIS 363  ? A HIS 363  
364  1 Y 1 A LEU 364  ? A LEU 364  
365  1 Y 1 A ARG 365  ? A ARG 365  
366  1 Y 1 A LYS 366  ? A LYS 366  
367  1 Y 1 A ILE 367  ? A ILE 367  
368  1 Y 1 A ARG 368  ? A ARG 368  
369  1 Y 1 A ASN 369  ? A ASN 369  
370  1 Y 1 A THR 370  ? A THR 370  
371  1 Y 1 A LYS 371  ? A LYS 371  
372  1 Y 1 A TYR 372  ? A TYR 372  
373  1 Y 1 A PRO 373  ? A PRO 373  
374  1 Y 1 A ILE 374  ? A ILE 374  
375  1 Y 1 A GLN 375  ? A GLN 375  
376  1 Y 1 A ARG 376  ? A ARG 376  
377  1 Y 1 A ALA 377  ? A ALA 377  
378  1 Y 1 A LEU 378  ? A LEU 378  
379  1 Y 1 A ARG 379  ? A ARG 379  
380  1 Y 1 A LEU 380  ? A LEU 380  
381  1 Y 1 A VAL 381  ? A VAL 381  
382  1 Y 1 A GLU 382  ? A GLU 382  
383  1 Y 1 A ALA 383  ? A ALA 383  
384  1 Y 1 A ILE 384  ? A ILE 384  
385  1 Y 1 A SER 385  ? A SER 385  
386  1 Y 1 A ARG 386  ? A ARG 386  
387  1 Y 1 A ASP 387  ? A ASP 387  
388  1 Y 1 A LEU 388  ? A LEU 388  
389  1 Y 1 A SER 389  ? A SER 389  
390  1 Y 1 A SER 390  ? A SER 390  
391  1 Y 1 A GLN 391  ? A GLN 391  
392  1 Y 1 A LEU 392  ? A LEU 392  
393  1 Y 1 A LEU 393  ? A LEU 393  
394  1 Y 1 A LYS 394  ? A LYS 394  
395  1 Y 1 A VAL 395  ? A VAL 395  
396  1 Y 1 A LEU 396  ? A LEU 396  
397  1 Y 1 A GLY 397  ? A GLY 397  
398  1 Y 1 A THR 398  ? A THR 398  
399  1 Y 1 A ARG 399  ? A ARG 399  
400  1 Y 1 A LYS 400  ? A LYS 400  
401  1 Y 1 A LEU 401  ? A LEU 401  
402  1 Y 1 A MET 402  ? A MET 402  
403  1 Y 1 A HIS 403  ? A HIS 403  
404  1 Y 1 A VAL 404  ? A VAL 404  
405  1 Y 1 A ALA 405  ? A ALA 405  
406  1 Y 1 A TYR 406  ? A TYR 406  
407  1 Y 1 A GLU 407  ? A GLU 407  
408  1 Y 1 A GLU 408  ? A GLU 408  
409  1 Y 1 A PHE 409  ? A PHE 409  
410  1 Y 1 A GLU 410  ? A GLU 410  
411  1 Y 1 A LYS 411  ? A LYS 411  
412  1 Y 1 A VAL 412  ? A VAL 412  
413  1 Y 1 A MET 413  ? A MET 413  
414  1 Y 1 A VAL 414  ? A VAL 414  
415  1 Y 1 A ALA 415  ? A ALA 415  
416  1 Y 1 A CYS 416  ? A CYS 416  
417  1 Y 1 A PHE 417  ? A PHE 417  
418  1 Y 1 A GLU 418  ? A GLU 418  
419  1 Y 1 A VAL 419  ? A VAL 419  
420  1 Y 1 A PHE 420  ? A PHE 420  
421  1 Y 1 A GLN 421  ? A GLN 421  
422  1 Y 1 A THR 422  ? A THR 422  
423  1 Y 1 A TRP 423  ? A TRP 423  
424  1 Y 1 A ASP 424  ? A ASP 424  
425  1 Y 1 A ASP 425  ? A ASP 425  
426  1 Y 1 A GLU 426  ? A GLU 426  
427  1 Y 1 A TYR 427  ? A TYR 427  
428  1 Y 1 A GLU 428  ? A GLU 428  
429  1 Y 1 A LYS 429  ? A LYS 429  
430  1 Y 1 A LEU 430  ? A LEU 430  
431  1 Y 1 A GLN 431  ? A GLN 431  
432  1 Y 1 A VAL 432  ? A VAL 432  
433  1 Y 1 A LEU 433  ? A LEU 433  
434  1 Y 1 A LEU 434  ? A LEU 434  
435  1 Y 1 A ARG 435  ? A ARG 435  
436  1 Y 1 A ASP 436  ? A ASP 436  
437  1 Y 1 A ILE 437  ? A ILE 437  
438  1 Y 1 A VAL 438  ? A VAL 438  
439  1 Y 1 A LYS 439  ? A LYS 439  
440  1 Y 1 A ARG 440  ? A ARG 440  
441  1 Y 1 A LYS 441  ? A LYS 441  
442  1 Y 1 A ARG 442  ? A ARG 442  
443  1 Y 1 A GLU 443  ? A GLU 443  
444  1 Y 1 A GLU 444  ? A GLU 444  
445  1 Y 1 A ASN 445  ? A ASN 445  
446  1 Y 1 A LEU 446  ? A LEU 446  
447  1 Y 1 A LYS 447  ? A LYS 447  
448  1 Y 1 A MET 448  ? A MET 448  
449  1 Y 1 A VAL 449  ? A VAL 449  
450  1 Y 1 A TRP 450  ? A TRP 450  
451  1 Y 1 A ARG 451  ? A ARG 451  
452  1 Y 1 A ILE 452  ? A ILE 452  
453  1 Y 1 A ASN 453  ? A ASN 453  
454  1 Y 1 A PRO 454  ? A PRO 454  
455  1 Y 1 A ALA 455  ? A ALA 455  
456  1 Y 1 A HIS 456  ? A HIS 456  
457  1 Y 1 A ARG 457  ? A ARG 457  
458  1 Y 1 A LYS 458  ? A LYS 458  
459  1 Y 1 A LEU 459  ? A LEU 459  
460  1 Y 1 A GLN 460  ? A GLN 460  
461  1 Y 1 A ALA 461  ? A ALA 461  
462  1 Y 1 A ARG 462  ? A ARG 462  
463  1 Y 1 A LEU 463  ? A LEU 463  
464  1 Y 1 A ASP 464  ? A ASP 464  
465  1 Y 1 A GLN 465  ? A GLN 465  
466  1 Y 1 A MET 466  ? A MET 466  
467  1 Y 1 A ARG 467  ? A ARG 467  
468  1 Y 1 A LYS 468  ? A LYS 468  
469  1 Y 1 A PHE 469  ? A PHE 469  
470  1 Y 1 A ARG 470  ? A ARG 470  
471  1 Y 1 A ARG 471  ? A ARG 471  
472  1 Y 1 A GLN 472  ? A GLN 472  
473  1 Y 1 A HIS 473  ? A HIS 473  
474  1 Y 1 A GLU 474  ? A GLU 474  
475  1 Y 1 A GLN 475  ? A GLN 475  
476  1 Y 1 A LEU 476  ? A LEU 476  
477  1 Y 1 A ARG 477  ? A ARG 477  
478  1 Y 1 A ALA 478  ? A ALA 478  
479  1 Y 1 A VAL 479  ? A VAL 479  
480  1 Y 1 A ILE 480  ? A ILE 480  
481  1 Y 1 A VAL 481  ? A VAL 481  
482  1 Y 1 A ARG 482  ? A ARG 482  
483  1 Y 1 A VAL 483  ? A VAL 483  
484  1 Y 1 A LEU 484  ? A LEU 484  
485  1 Y 1 A ARG 485  ? A ARG 485  
486  1 Y 1 A PRO 486  ? A PRO 486  
487  1 Y 1 A GLN 487  ? A GLN 487  
488  1 Y 1 A VAL 488  ? A VAL 488  
489  1 Y 1 A THR 489  ? A THR 489  
490  1 Y 1 A ALA 490  ? A ALA 490  
491  1 Y 1 A VAL 491  ? A VAL 491  
492  1 Y 1 A ALA 492  ? A ALA 492  
493  1 Y 1 A GLN 493  ? A GLN 493  
494  1 Y 1 A GLN 494  ? A GLN 494  
495  1 Y 1 A ASN 495  ? A ASN 495  
496  1 Y 1 A GLN 496  ? A GLN 496  
497  1 Y 1 A GLY 497  ? A GLY 497  
498  1 Y 1 A GLU 498  ? A GLU 498  
499  1 Y 1 A VAL 499  ? A VAL 499  
500  1 Y 1 A PRO 500  ? A PRO 500  
501  1 Y 1 A GLU 501  ? A GLU 501  
502  1 Y 1 A PRO 502  ? A PRO 502  
503  1 Y 1 A GLN 503  ? A GLN 503  
504  1 Y 1 A ASP 504  ? A ASP 504  
505  1 Y 1 A MET 505  ? A MET 505  
506  1 Y 1 A LYS 506  ? A LYS 506  
507  1 Y 1 A VAL 507  ? A VAL 507  
508  1 Y 1 A ALA 508  ? A ALA 508  
509  1 Y 1 A GLU 509  ? A GLU 509  
510  1 Y 1 A VAL 510  ? A VAL 510  
511  1 Y 1 A LEU 511  ? A LEU 511  
512  1 Y 1 A PHE 512  ? A PHE 512  
513  1 Y 1 A ASP 513  ? A ASP 513  
514  1 Y 1 A ALA 514  ? A ALA 514  
515  1 Y 1 A ALA 515  ? A ALA 515  
516  1 Y 1 A ASP 516  ? A ASP 516  
517  1 Y 1 A ALA 517  ? A ALA 517  
518  1 Y 1 A ASN 518  ? A ASN 518  
519  1 Y 1 A ALA 519  ? A ALA 519  
520  1 Y 1 A ILE 520  ? A ILE 520  
521  1 Y 1 A GLU 521  ? A GLU 521  
522  1 Y 1 A GLU 522  ? A GLU 522  
523  1 Y 1 A VAL 523  ? A VAL 523  
524  1 Y 1 A ASN 524  ? A ASN 524  
525  1 Y 1 A LEU 525  ? A LEU 525  
526  1 Y 1 A ALA 526  ? A ALA 526  
527  1 Y 1 A TYR 527  ? A TYR 527  
528  1 Y 1 A GLU 528  ? A GLU 528  
529  1 Y 1 A ASN 529  ? A ASN 529  
530  1 Y 1 A VAL 530  ? A VAL 530  
531  1 Y 1 A LYS 531  ? A LYS 531  
532  1 Y 1 A GLU 532  ? A GLU 532  
533  1 Y 1 A VAL 533  ? A VAL 533  
534  1 Y 1 A ASP 534  ? A ASP 534  
535  1 Y 1 A GLY 535  ? A GLY 535  
536  1 Y 1 A LEU 536  ? A LEU 536  
537  1 Y 1 A ASP 537  ? A ASP 537  
538  1 Y 1 A VAL 538  ? A VAL 538  
539  1 Y 1 A SER 539  ? A SER 539  
540  1 Y 1 A LYS 540  ? A LYS 540  
541  1 Y 1 A GLU 541  ? A GLU 541  
542  1 Y 1 A GLY 542  ? A GLY 542  
543  1 Y 1 A THR 543  ? A THR 543  
544  1 Y 1 A GLU 544  ? A GLU 544  
545  1 Y 1 A ALA 545  ? A ALA 545  
546  1 Y 1 A TRP 546  ? A TRP 546  
547  1 Y 1 A GLU 547  ? A GLU 547  
548  1 Y 1 A ALA 548  ? A ALA 548  
549  1 Y 1 A ALA 549  ? A ALA 549  
550  1 Y 1 A MET 550  ? A MET 550  
551  1 Y 1 A LYS 551  ? A LYS 551  
552  1 Y 1 A ARG 552  ? A ARG 552  
553  1 Y 1 A TYR 553  ? A TYR 553  
554  1 Y 1 A ASP 554  ? A ASP 554  
555  1 Y 1 A GLU 555  ? A GLU 555  
556  1 Y 1 A ARG 556  ? A ARG 556  
557  1 Y 1 A ILE 557  ? A ILE 557  
558  1 Y 1 A ASP 558  ? A ASP 558  
559  1 Y 1 A ARG 559  ? A ARG 559  
560  1 Y 1 A VAL 560  ? A VAL 560  
561  1 Y 1 A GLU 561  ? A GLU 561  
562  1 Y 1 A THR 562  ? A THR 562  
563  1 Y 1 A ARG 563  ? A ARG 563  
564  1 Y 1 A ILE 564  ? A ILE 564  
565  1 Y 1 A THR 565  ? A THR 565  
566  1 Y 1 A ALA 566  ? A ALA 566  
567  1 Y 1 A ARG 567  ? A ARG 567  
568  1 Y 1 A LEU 568  ? A LEU 568  
569  1 Y 1 A ARG 569  ? A ARG 569  
570  1 Y 1 A ASP 570  ? A ASP 570  
571  1 Y 1 A GLN 571  ? A GLN 571  
572  1 Y 1 A LEU 572  ? A LEU 572  
573  1 Y 1 A GLY 573  ? A GLY 573  
574  1 Y 1 A THR 574  ? A THR 574  
575  1 Y 1 A ALA 575  ? A ALA 575  
576  1 Y 1 A LYS 576  ? A LYS 576  
577  1 Y 1 A ASN 577  ? A ASN 577  
578  1 Y 1 A ALA 578  ? A ALA 578  
579  1 Y 1 A ASN 579  ? A ASN 579  
580  1 Y 1 A GLU 580  ? A GLU 580  
581  1 Y 1 A MET 581  ? A MET 581  
582  1 Y 1 A PHE 582  ? A PHE 582  
583  1 Y 1 A ARG 583  ? A ARG 583  
584  1 Y 1 A ILE 584  ? A ILE 584  
585  1 Y 1 A PHE 585  ? A PHE 585  
586  1 Y 1 A SER 586  ? A SER 586  
587  1 Y 1 A ARG 587  ? A ARG 587  
588  1 Y 1 A PHE 588  ? A PHE 588  
589  1 Y 1 A ASN 589  ? A ASN 589  
590  1 Y 1 A ALA 590  ? A ALA 590  
591  1 Y 1 A LEU 591  ? A LEU 591  
592  1 Y 1 A PHE 592  ? A PHE 592  
593  1 Y 1 A VAL 593  ? A VAL 593  
594  1 Y 1 A ARG 594  ? A ARG 594  
595  1 Y 1 A PRO 595  ? A PRO 595  
596  1 Y 1 A HIS 596  ? A HIS 596  
597  1 Y 1 A ILE 597  ? A ILE 597  
598  1 Y 1 A ARG 598  ? A ARG 598  
599  1 Y 1 A GLY 599  ? A GLY 599  
600  1 Y 1 A ALA 600  ? A ALA 600  
601  1 Y 1 A ILE 601  ? A ILE 601  
602  1 Y 1 A ARG 602  ? A ARG 602  
603  1 Y 1 A GLU 603  ? A GLU 603  
604  1 Y 1 A TYR 604  ? A TYR 604  
605  1 Y 1 A GLN 605  ? A GLN 605  
606  1 Y 1 A THR 606  ? A THR 606  
607  1 Y 1 A GLN 607  ? A GLN 607  
608  1 Y 1 A LEU 608  ? A LEU 608  
609  1 Y 1 A ILE 609  ? A ILE 609  
610  1 Y 1 A GLN 610  ? A GLN 610  
611  1 Y 1 A ARG 611  ? A ARG 611  
612  1 Y 1 A VAL 612  ? A VAL 612  
613  1 Y 1 A LYS 613  ? A LYS 613  
614  1 Y 1 A ASP 614  ? A ASP 614  
615  1 Y 1 A ASP 615  ? A ASP 615  
616  1 Y 1 A ILE 616  ? A ILE 616  
617  1 Y 1 A GLU 617  ? A GLU 617  
618  1 Y 1 A SER 618  ? A SER 618  
619  1 Y 1 A LEU 619  ? A LEU 619  
620  1 Y 1 A HIS 620  ? A HIS 620  
621  1 Y 1 A ASP 621  ? A ASP 621  
622  1 Y 1 A LYS 622  ? A LYS 622  
623  1 Y 1 A PHE 623  ? A PHE 623  
624  1 Y 1 A LYS 624  ? A LYS 624  
625  1 Y 1 A VAL 625  ? A VAL 625  
626  1 Y 1 A GLN 626  ? A GLN 626  
627  1 Y 1 A TYR 627  ? A TYR 627  
628  1 Y 1 A PRO 628  ? A PRO 628  
629  1 Y 1 A GLN 629  ? A GLN 629  
630  1 Y 1 A SER 630  ? A SER 630  
631  1 Y 1 A GLN 631  ? A GLN 631  
632  1 Y 1 A ALA 632  ? A ALA 632  
633  1 Y 1 A CYS 633  ? A CYS 633  
634  1 Y 1 A LYS 634  ? A LYS 634  
635  1 Y 1 A MET 635  ? A MET 635  
636  1 Y 1 A SER 636  ? A SER 636  
637  1 Y 1 A HIS 637  ? A HIS 637  
638  1 Y 1 A VAL 638  ? A VAL 638  
639  1 Y 1 A ARG 639  ? A ARG 639  
640  1 Y 1 A ASP 640  ? A ASP 640  
641  1 Y 1 A LEU 641  ? A LEU 641  
642  1 Y 1 A PRO 642  ? A PRO 642  
643  1 Y 1 A PRO 643  ? A PRO 643  
644  1 Y 1 A VAL 644  ? A VAL 644  
645  1 Y 1 A SER 645  ? A SER 645  
646  1 Y 1 A GLY 646  ? A GLY 646  
647  1 Y 1 A SER 647  ? A SER 647  
648  1 Y 1 A ILE 648  ? A ILE 648  
649  1 Y 1 A ILE 649  ? A ILE 649  
650  1 Y 1 A TRP 650  ? A TRP 650  
651  1 Y 1 A ALA 651  ? A ALA 651  
652  1 Y 1 A LYS 652  ? A LYS 652  
653  1 Y 1 A GLN 653  ? A GLN 653  
654  1 Y 1 A ILE 654  ? A ILE 654  
655  1 Y 1 A ASP 655  ? A ASP 655  
656  1 Y 1 A ARG 656  ? A ARG 656  
657  1 Y 1 A GLN 657  ? A GLN 657  
658  1 Y 1 A LEU 658  ? A LEU 658  
659  1 Y 1 A THR 659  ? A THR 659  
660  1 Y 1 A ALA 660  ? A ALA 660  
661  1 Y 1 A TYR 661  ? A TYR 661  
662  1 Y 1 A MET 662  ? A MET 662  
663  1 Y 1 A LYS 663  ? A LYS 663  
664  1 Y 1 A ARG 664  ? A ARG 664  
665  1 Y 1 A VAL 665  ? A VAL 665  
666  1 Y 1 A GLU 666  ? A GLU 666  
667  1 Y 1 A ASP 667  ? A ASP 667  
668  1 Y 1 A VAL 668  ? A VAL 668  
669  1 Y 1 A LEU 669  ? A LEU 669  
670  1 Y 1 A GLY 670  ? A GLY 670  
671  1 Y 1 A LYS 671  ? A LYS 671  
672  1 Y 1 A GLY 672  ? A GLY 672  
673  1 Y 1 A TRP 673  ? A TRP 673  
674  1 Y 1 A GLU 674  ? A GLU 674  
675  1 Y 1 A ASN 675  ? A ASN 675  
676  1 Y 1 A HIS 676  ? A HIS 676  
677  1 Y 1 A VAL 677  ? A VAL 677  
678  1 Y 1 A GLU 678  ? A GLU 678  
679  1 Y 1 A GLY 679  ? A GLY 679  
680  1 Y 1 A GLN 680  ? A GLN 680  
681  1 Y 1 A LYS 681  ? A LYS 681  
682  1 Y 1 A LEU 682  ? A LEU 682  
683  1 Y 1 A LYS 683  ? A LYS 683  
684  1 Y 1 A GLN 684  ? A GLN 684  
685  1 Y 1 A ASP 685  ? A ASP 685  
686  1 Y 1 A GLY 686  ? A GLY 686  
687  1 Y 1 A ASP 687  ? A ASP 687  
688  1 Y 1 A SER 688  ? A SER 688  
689  1 Y 1 A PHE 689  ? A PHE 689  
690  1 Y 1 A ARG 690  ? A ARG 690  
691  1 Y 1 A MET 691  ? A MET 691  
692  1 Y 1 A LYS 692  ? A LYS 692  
693  1 Y 1 A LEU 693  ? A LEU 693  
694  1 Y 1 A ASN 694  ? A ASN 694  
695  1 Y 1 A THR 695  ? A THR 695  
696  1 Y 1 A GLN 696  ? A GLN 696  
697  1 Y 1 A GLU 697  ? A GLU 697  
698  1 Y 1 A ILE 698  ? A ILE 698  
699  1 Y 1 A PHE 699  ? A PHE 699  
700  1 Y 1 A ASP 700  ? A ASP 700  
701  1 Y 1 A ASP 701  ? A ASP 701  
702  1 Y 1 A TRP 702  ? A TRP 702  
703  1 Y 1 A ALA 703  ? A ALA 703  
704  1 Y 1 A ARG 704  ? A ARG 704  
705  1 Y 1 A LYS 705  ? A LYS 705  
706  1 Y 1 A VAL 706  ? A VAL 706  
707  1 Y 1 A GLN 707  ? A GLN 707  
708  1 Y 1 A GLN 708  ? A GLN 708  
709  1 Y 1 A ARG 709  ? A ARG 709  
710  1 Y 1 A ASN 710  ? A ASN 710  
711  1 Y 1 A LEU 711  ? A LEU 711  
712  1 Y 1 A GLY 712  ? A GLY 712  
713  1 Y 1 A VAL 713  ? A VAL 713  
714  1 Y 1 A SER 714  ? A SER 714  
715  1 Y 1 A GLY 715  ? A GLY 715  
716  1 Y 1 A ARG 716  ? A ARG 716  
717  1 Y 1 A ILE 717  ? A ILE 717  
718  1 Y 1 A PHE 718  ? A PHE 718  
719  1 Y 1 A THR 719  ? A THR 719  
720  1 Y 1 A ILE 720  ? A ILE 720  
721  1 Y 1 A GLU 721  ? A GLU 721  
722  1 Y 1 A SER 722  ? A SER 722  
723  1 Y 1 A THR 723  ? A THR 723  
724  1 Y 1 A ARG 724  ? A ARG 724  
725  1 Y 1 A VAL 725  ? A VAL 725  
726  1 Y 1 A ARG 726  ? A ARG 726  
727  1 Y 1 A GLY 727  ? A GLY 727  
728  1 Y 1 A ARG 728  ? A ARG 728  
729  1 Y 1 A THR 729  ? A THR 729  
730  1 Y 1 A GLY 730  ? A GLY 730  
731  1 Y 1 A ASN 731  ? A ASN 731  
732  1 Y 1 A VAL 732  ? A VAL 732  
733  1 Y 1 A LEU 733  ? A LEU 733  
734  1 Y 1 A LYS 734  ? A LYS 734  
735  1 Y 1 A LEU 735  ? A LEU 735  
736  1 Y 1 A LYS 736  ? A LYS 736  
737  1 Y 1 A VAL 737  ? A VAL 737  
738  1 Y 1 A ASN 738  ? A ASN 738  
739  1 Y 1 A PHE 739  ? A PHE 739  
740  1 Y 1 A LEU 740  ? A LEU 740  
741  1 Y 1 A PRO 741  ? A PRO 741  
742  1 Y 1 A GLU 742  ? A GLU 742  
743  1 Y 1 A ILE 743  ? A ILE 743  
744  1 Y 1 A ILE 744  ? A ILE 744  
745  1 Y 1 A THR 745  ? A THR 745  
746  1 Y 1 A LEU 746  ? A LEU 746  
747  1 Y 1 A SER 747  ? A SER 747  
748  1 Y 1 A LYS 748  ? A LYS 748  
749  1 Y 1 A GLU 749  ? A GLU 749  
750  1 Y 1 A VAL 750  ? A VAL 750  
751  1 Y 1 A ARG 751  ? A ARG 751  
752  1 Y 1 A ASN 752  ? A ASN 752  
753  1 Y 1 A LEU 753  ? A LEU 753  
754  1 Y 1 A LYS 754  ? A LYS 754  
755  1 Y 1 A TRP 755  ? A TRP 755  
756  1 Y 1 A LEU 756  ? A LEU 756  
757  1 Y 1 A GLY 757  ? A GLY 757  
758  1 Y 1 A PHE 758  ? A PHE 758  
759  1 Y 1 A ARG 759  ? A ARG 759  
760  1 Y 1 A VAL 760  ? A VAL 760  
761  1 Y 1 A PRO 761  ? A PRO 761  
762  1 Y 1 A LEU 762  ? A LEU 762  
763  1 Y 1 A ALA 763  ? A ALA 763  
764  1 Y 1 A ILE 764  ? A ILE 764  
765  1 Y 1 A VAL 765  ? A VAL 765  
766  1 Y 1 A ASN 766  ? A ASN 766  
767  1 Y 1 A LYS 767  ? A LYS 767  
768  1 Y 1 A ALA 768  ? A ALA 768  
769  1 Y 1 A HIS 769  ? A HIS 769  
770  1 Y 1 A GLN 770  ? A GLN 770  
771  1 Y 1 A ALA 771  ? A ALA 771  
772  1 Y 1 A ASN 772  ? A ASN 772  
773  1 Y 1 A GLN 773  ? A GLN 773  
774  1 Y 1 A LEU 774  ? A LEU 774  
775  1 Y 1 A TYR 775  ? A TYR 775  
776  1 Y 1 A PRO 776  ? A PRO 776  
777  1 Y 1 A PHE 777  ? A PHE 777  
778  1 Y 1 A ALA 778  ? A ALA 778  
779  1 Y 1 A ILE 779  ? A ILE 779  
780  1 Y 1 A SER 780  ? A SER 780  
781  1 Y 1 A LEU 781  ? A LEU 781  
782  1 Y 1 A ILE 782  ? A ILE 782  
783  1 Y 1 A GLU 783  ? A GLU 783  
784  1 Y 1 A SER 784  ? A SER 784  
785  1 Y 1 A VAL 785  ? A VAL 785  
786  1 Y 1 A ARG 786  ? A ARG 786  
787  1 Y 1 A THR 787  ? A THR 787  
788  1 Y 1 A TYR 788  ? A TYR 788  
789  1 Y 1 A GLU 789  ? A GLU 789  
790  1 Y 1 A ARG 790  ? A ARG 790  
791  1 Y 1 A THR 791  ? A THR 791  
792  1 Y 1 A CYS 792  ? A CYS 792  
793  1 Y 1 A GLU 793  ? A GLU 793  
794  1 Y 1 A LYS 794  ? A LYS 794  
795  1 Y 1 A VAL 795  ? A VAL 795  
796  1 Y 1 A GLU 796  ? A GLU 796  
797  1 Y 1 A GLU 797  ? A GLU 797  
798  1 Y 1 A ARG 798  ? A ARG 798  
799  1 Y 1 A ASN 799  ? A ASN 799  
800  1 Y 1 A THR 800  ? A THR 800  
801  1 Y 1 A ILE 801  ? A ILE 801  
802  1 Y 1 A SER 802  ? A SER 802  
803  1 Y 1 A LEU 803  ? A LEU 803  
804  1 Y 1 A LEU 804  ? A LEU 804  
805  1 Y 1 A VAL 805  ? A VAL 805  
806  1 Y 1 A ALA 806  ? A ALA 806  
807  1 Y 1 A GLY 807  ? A GLY 807  
808  1 Y 1 A LEU 808  ? A LEU 808  
809  1 Y 1 A LYS 809  ? A LYS 809  
810  1 Y 1 A LYS 810  ? A LYS 810  
811  1 Y 1 A GLU 811  ? A GLU 811  
812  1 Y 1 A VAL 812  ? A VAL 812  
813  1 Y 1 A GLN 813  ? A GLN 813  
814  1 Y 1 A ALA 814  ? A ALA 814  
815  1 Y 1 A LEU 815  ? A LEU 815  
816  1 Y 1 A ILE 816  ? A ILE 816  
817  1 Y 1 A ALA 817  ? A ALA 817  
818  1 Y 1 A GLU 818  ? A GLU 818  
819  1 Y 1 A GLY 819  ? A GLY 819  
820  1 Y 1 A ILE 820  ? A ILE 820  
821  1 Y 1 A ALA 821  ? A ALA 821  
822  1 Y 1 A LEU 822  ? A LEU 822  
823  1 Y 1 A VAL 823  ? A VAL 823  
824  1 Y 1 A TRP 824  ? A TRP 824  
825  1 Y 1 A GLU 825  ? A GLU 825  
826  1 Y 1 A SER 826  ? A SER 826  
827  1 Y 1 A TYR 827  ? A TYR 827  
828  1 Y 1 A LYS 828  ? A LYS 828  
829  1 Y 1 A LEU 829  ? A LEU 829  
830  1 Y 1 A ASP 830  ? A ASP 830  
831  1 Y 1 A PRO 831  ? A PRO 831  
832  1 Y 1 A TYR 832  ? A TYR 832  
833  1 Y 1 A VAL 833  ? A VAL 833  
834  1 Y 1 A GLN 834  ? A GLN 834  
835  1 Y 1 A ARG 835  ? A ARG 835  
836  1 Y 1 A LEU 836  ? A LEU 836  
837  1 Y 1 A ALA 837  ? A ALA 837  
838  1 Y 1 A GLU 838  ? A GLU 838  
839  1 Y 1 A THR 839  ? A THR 839  
840  1 Y 1 A VAL 840  ? A VAL 840  
841  1 Y 1 A PHE 841  ? A PHE 841  
842  1 Y 1 A ASN 842  ? A ASN 842  
843  1 Y 1 A PHE 843  ? A PHE 843  
844  1 Y 1 A GLN 844  ? A GLN 844  
845  1 Y 1 A GLU 845  ? A GLU 845  
846  1 Y 1 A LYS 846  ? A LYS 846  
847  1 Y 1 A VAL 847  ? A VAL 847  
848  1 Y 1 A ASP 848  ? A ASP 848  
849  1 Y 1 A ASP 849  ? A ASP 849  
850  1 Y 1 A LEU 850  ? A LEU 850  
851  1 Y 1 A LEU 851  ? A LEU 851  
852  1 Y 1 A ILE 852  ? A ILE 852  
853  1 Y 1 A ILE 853  ? A ILE 853  
854  1 Y 1 A GLU 854  ? A GLU 854  
855  1 Y 1 A GLU 855  ? A GLU 855  
856  1 Y 1 A LYS 856  ? A LYS 856  
857  1 Y 1 A ILE 857  ? A ILE 857  
858  1 Y 1 A ASP 858  ? A ASP 858  
859  1 Y 1 A LEU 859  ? A LEU 859  
860  1 Y 1 A GLU 860  ? A GLU 860  
861  1 Y 1 A VAL 861  ? A VAL 861  
862  1 Y 1 A ARG 862  ? A ARG 862  
863  1 Y 1 A SER 863  ? A SER 863  
864  1 Y 1 A LEU 864  ? A LEU 864  
865  1 Y 1 A GLU 865  ? A GLU 865  
866  1 Y 1 A THR 866  ? A THR 866  
867  1 Y 1 A CYS 867  ? A CYS 867  
868  1 Y 1 A MET 868  ? A MET 868  
869  1 Y 1 A TYR 869  ? A TYR 869  
870  1 Y 1 A ASP 870  ? A ASP 870  
871  1 Y 1 A HIS 871  ? A HIS 871  
872  1 Y 1 A LYS 872  ? A LYS 872  
873  1 Y 1 A THR 873  ? A THR 873  
874  1 Y 1 A PHE 874  ? A PHE 874  
875  1 Y 1 A SER 875  ? A SER 875  
876  1 Y 1 A GLU 876  ? A GLU 876  
877  1 Y 1 A ILE 877  ? A ILE 877  
878  1 Y 1 A LEU 878  ? A LEU 878  
879  1 Y 1 A ASN 879  ? A ASN 879  
880  1 Y 1 A ARG 880  ? A ARG 880  
881  1 Y 1 A VAL 881  ? A VAL 881  
882  1 Y 1 A GLN 882  ? A GLN 882  
883  1 Y 1 A LYS 883  ? A LYS 883  
884  1 Y 1 A ALA 884  ? A ALA 884  
885  1 Y 1 A VAL 885  ? A VAL 885  
886  1 Y 1 A ASP 886  ? A ASP 886  
887  1 Y 1 A ASP 887  ? A ASP 887  
888  1 Y 1 A LEU 888  ? A LEU 888  
889  1 Y 1 A ASN 889  ? A ASN 889  
890  1 Y 1 A LEU 890  ? A LEU 890  
891  1 Y 1 A HIS 891  ? A HIS 891  
892  1 Y 1 A SER 892  ? A SER 892  
893  1 Y 1 A TYR 893  ? A TYR 893  
894  1 Y 1 A SER 894  ? A SER 894  
895  1 Y 1 A ASN 895  ? A ASN 895  
896  1 Y 1 A LEU 896  ? A LEU 896  
897  1 Y 1 A PRO 897  ? A PRO 897  
898  1 Y 1 A ILE 898  ? A ILE 898  
899  1 Y 1 A TRP 899  ? A TRP 899  
900  1 Y 1 A VAL 900  ? A VAL 900  
901  1 Y 1 A ASN 901  ? A ASN 901  
902  1 Y 1 A LYS 902  ? A LYS 902  
903  1 Y 1 A LEU 903  ? A LEU 903  
904  1 Y 1 A ASP 904  ? A ASP 904  
905  1 Y 1 A MET 905  ? A MET 905  
906  1 Y 1 A GLU 906  ? A GLU 906  
907  1 Y 1 A ILE 907  ? A ILE 907  
908  1 Y 1 A GLU 908  ? A GLU 908  
909  1 Y 1 A ARG 909  ? A ARG 909  
910  1 Y 1 A ILE 910  ? A ILE 910  
911  1 Y 1 A LEU 911  ? A LEU 911  
912  1 Y 1 A GLY 912  ? A GLY 912  
913  1 Y 1 A VAL 913  ? A VAL 913  
914  1 Y 1 A ARG 914  ? A ARG 914  
915  1 Y 1 A LEU 915  ? A LEU 915  
916  1 Y 1 A GLN 916  ? A GLN 916  
917  1 Y 1 A ALA 917  ? A ALA 917  
918  1 Y 1 A GLY 918  ? A GLY 918  
919  1 Y 1 A LEU 919  ? A LEU 919  
920  1 Y 1 A ARG 920  ? A ARG 920  
921  1 Y 1 A ALA 921  ? A ALA 921  
922  1 Y 1 A TRP 922  ? A TRP 922  
923  1 Y 1 A THR 923  ? A THR 923  
924  1 Y 1 A GLN 924  ? A GLN 924  
925  1 Y 1 A VAL 925  ? A VAL 925  
926  1 Y 1 A LEU 926  ? A LEU 926  
927  1 Y 1 A LEU 927  ? A LEU 927  
928  1 Y 1 A GLY 928  ? A GLY 928  
929  1 Y 1 A GLN 929  ? A GLN 929  
930  1 Y 1 A ALA 930  ? A ALA 930  
931  1 Y 1 A GLU 931  ? A GLU 931  
932  1 Y 1 A ASP 932  ? A ASP 932  
933  1 Y 1 A LYS 933  ? A LYS 933  
934  1 Y 1 A ALA 934  ? A ALA 934  
935  1 Y 1 A GLU 935  ? A GLU 935  
936  1 Y 1 A VAL 936  ? A VAL 936  
937  1 Y 1 A ASP 937  ? A ASP 937  
938  1 Y 1 A MET 938  ? A MET 938  
939  1 Y 1 A ASP 939  ? A ASP 939  
940  1 Y 1 A THR 940  ? A THR 940  
941  1 Y 1 A ASP 941  ? A ASP 941  
942  1 Y 1 A ALA 942  ? A ALA 942  
943  1 Y 1 A PRO 943  ? A PRO 943  
944  1 Y 1 A GLN 944  ? A GLN 944  
945  1 Y 1 A VAL 945  ? A VAL 945  
946  1 Y 1 A SER 946  ? A SER 946  
947  1 Y 1 A HIS 947  ? A HIS 947  
948  1 Y 1 A LYS 948  ? A LYS 948  
949  1 Y 1 A PRO 949  ? A PRO 949  
950  1 Y 1 A GLY 950  ? A GLY 950  
951  1 Y 1 A GLY 951  ? A GLY 951  
952  1 Y 1 A GLU 952  ? A GLU 952  
953  1 Y 1 A PRO 953  ? A PRO 953  
954  1 Y 1 A LYS 954  ? A LYS 954  
955  1 Y 1 A ILE 955  ? A ILE 955  
956  1 Y 1 A LYS 956  ? A LYS 956  
957  1 Y 1 A ASN 957  ? A ASN 957  
958  1 Y 1 A VAL 958  ? A VAL 958  
959  1 Y 1 A VAL 959  ? A VAL 959  
960  1 Y 1 A HIS 960  ? A HIS 960  
961  1 Y 1 A GLU 961  ? A GLU 961  
962  1 Y 1 A LEU 962  ? A LEU 962  
963  1 Y 1 A ARG 963  ? A ARG 963  
964  1 Y 1 A ILE 964  ? A ILE 964  
965  1 Y 1 A THR 965  ? A THR 965  
966  1 Y 1 A ASN 966  ? A ASN 966  
967  1 Y 1 A GLN 967  ? A GLN 967  
968  1 Y 1 A VAL 968  ? A VAL 968  
969  1 Y 1 A ILE 969  ? A ILE 969  
970  1 Y 1 A TYR 970  ? A TYR 970  
971  1 Y 1 A LEU 971  ? A LEU 971  
972  1 Y 1 A ASN 972  ? A ASN 972  
973  1 Y 1 A PRO 973  ? A PRO 973  
974  1 Y 1 A PRO 974  ? A PRO 974  
975  1 Y 1 A ILE 975  ? A ILE 975  
976  1 Y 1 A GLU 976  ? A GLU 976  
977  1 Y 1 A GLU 977  ? A GLU 977  
978  1 Y 1 A CYS 978  ? A CYS 978  
979  1 Y 1 A ARG 979  ? A ARG 979  
980  1 Y 1 A TYR 980  ? A TYR 980  
981  1 Y 1 A LYS 981  ? A LYS 981  
982  1 Y 1 A LEU 982  ? A LEU 982  
983  1 Y 1 A TYR 983  ? A TYR 983  
984  1 Y 1 A GLN 984  ? A GLN 984  
985  1 Y 1 A GLU 985  ? A GLU 985  
986  1 Y 1 A MET 986  ? A MET 986  
987  1 Y 1 A PHE 987  ? A PHE 987  
988  1 Y 1 A ALA 988  ? A ALA 988  
989  1 Y 1 A TRP 989  ? A TRP 989  
990  1 Y 1 A LYS 990  ? A LYS 990  
991  1 Y 1 A MET 991  ? A MET 991  
992  1 Y 1 A VAL 992  ? A VAL 992  
993  1 Y 1 A VAL 993  ? A VAL 993  
994  1 Y 1 A LEU 994  ? A LEU 994  
995  1 Y 1 A SER 995  ? A SER 995  
996  1 Y 1 A LEU 996  ? A LEU 996  
997  1 Y 1 A PRO 997  ? A PRO 997  
998  1 Y 1 A ARG 998  ? A ARG 998  
999  1 Y 1 A ILE 999  ? A ILE 999  
1000 1 Y 1 A GLN 1000 ? A GLN 1000 
1001 1 Y 1 A SER 1001 ? A SER 1001 
1002 1 Y 1 A GLN 1002 ? A GLN 1002 
1003 1 Y 1 A ARG 1003 ? A ARG 1003 
1004 1 Y 1 A TYR 1004 ? A TYR 1004 
1005 1 Y 1 A GLN 1005 ? A GLN 1005 
1006 1 Y 1 A VAL 1006 ? A VAL 1006 
1007 1 Y 1 A GLY 1007 ? A GLY 1007 
1008 1 Y 1 A VAL 1008 ? A VAL 1008 
1009 1 Y 1 A HIS 1009 ? A HIS 1009 
1010 1 Y 1 A TYR 1010 ? A TYR 1010 
1011 1 Y 1 A GLU 1011 ? A GLU 1011 
1012 1 Y 1 A LEU 1012 ? A LEU 1012 
1013 1 Y 1 A THR 1013 ? A THR 1013 
1014 1 Y 1 A GLU 1014 ? A GLU 1014 
1015 1 Y 1 A GLU 1015 ? A GLU 1015 
1016 1 Y 1 A GLU 1016 ? A GLU 1016 
1017 1 Y 1 A LYS 1017 ? A LYS 1017 
1018 1 Y 1 A PHE 1018 ? A PHE 1018 
1019 1 Y 1 A TYR 1019 ? A TYR 1019 
1020 1 Y 1 A ARG 1020 ? A ARG 1020 
1021 1 Y 1 A ASN 1021 ? A ASN 1021 
1022 1 Y 1 A ALA 1022 ? A ALA 1022 
1023 1 Y 1 A LEU 1023 ? A LEU 1023 
1024 1 Y 1 A THR 1024 ? A THR 1024 
1025 1 Y 1 A ARG 1025 ? A ARG 1025 
1026 1 Y 1 A MET 1026 ? A MET 1026 
1027 1 Y 1 A PRO 1027 ? A PRO 1027 
1028 1 Y 1 A ASP 1028 ? A ASP 1028 
1029 1 Y 1 A GLY 1029 ? A GLY 1029 
1030 1 Y 1 A PRO 1030 ? A PRO 1030 
1031 1 Y 1 A VAL 1031 ? A VAL 1031 
1032 1 Y 1 A ALA 1032 ? A ALA 1032 
1033 1 Y 1 A LEU 1033 ? A LEU 1033 
1034 1 Y 1 A GLU 1034 ? A GLU 1034 
1035 1 Y 1 A GLU 1035 ? A GLU 1035 
1036 1 Y 1 A SER 1036 ? A SER 1036 
1037 1 Y 1 A TYR 1037 ? A TYR 1037 
1038 1 Y 1 A SER 1038 ? A SER 1038 
1039 1 Y 1 A ALA 1039 ? A ALA 1039 
1040 1 Y 1 A VAL 1040 ? A VAL 1040 
1041 1 Y 1 A MET 1041 ? A MET 1041 
1042 1 Y 1 A GLY 1042 ? A GLY 1042 
1043 1 Y 1 A ILE 1043 ? A ILE 1043 
1044 1 Y 1 A VAL 1044 ? A VAL 1044 
1045 1 Y 1 A SER 1045 ? A SER 1045 
1046 1 Y 1 A GLU 1046 ? A GLU 1046 
1047 1 Y 1 A VAL 1047 ? A VAL 1047 
1048 1 Y 1 A GLU 1048 ? A GLU 1048 
1049 1 Y 1 A GLN 1049 ? A GLN 1049 
1050 1 Y 1 A TYR 1050 ? A TYR 1050 
1051 1 Y 1 A VAL 1051 ? A VAL 1051 
1052 1 Y 1 A LYS 1052 ? A LYS 1052 
1053 1 Y 1 A VAL 1053 ? A VAL 1053 
1054 1 Y 1 A TRP 1054 ? A TRP 1054 
1055 1 Y 1 A LEU 1055 ? A LEU 1055 
1056 1 Y 1 A GLN 1056 ? A GLN 1056 
1057 1 Y 1 A TYR 1057 ? A TYR 1057 
1058 1 Y 1 A GLN 1058 ? A GLN 1058 
1059 1 Y 1 A CYS 1059 ? A CYS 1059 
1060 1 Y 1 A LEU 1060 ? A LEU 1060 
1061 1 Y 1 A TRP 1061 ? A TRP 1061 
1062 1 Y 1 A ASP 1062 ? A ASP 1062 
1063 1 Y 1 A MET 1063 ? A MET 1063 
1064 1 Y 1 A GLN 1064 ? A GLN 1064 
1065 1 Y 1 A ALA 1065 ? A ALA 1065 
1066 1 Y 1 A GLU 1066 ? A GLU 1066 
1067 1 Y 1 A ASN 1067 ? A ASN 1067 
1068 1 Y 1 A ILE 1068 ? A ILE 1068 
1069 1 Y 1 A TYR 1069 ? A TYR 1069 
1070 1 Y 1 A ASN 1070 ? A ASN 1070 
1071 1 Y 1 A ARG 1071 ? A ARG 1071 
1072 1 Y 1 A LEU 1072 ? A LEU 1072 
1073 1 Y 1 A GLY 1073 ? A GLY 1073 
1074 1 Y 1 A GLU 1074 ? A GLU 1074 
1075 1 Y 1 A ASP 1075 ? A ASP 1075 
1076 1 Y 1 A LEU 1076 ? A LEU 1076 
1077 1 Y 1 A ASN 1077 ? A ASN 1077 
1078 1 Y 1 A LYS 1078 ? A LYS 1078 
1079 1 Y 1 A TRP 1079 ? A TRP 1079 
1080 1 Y 1 A GLN 1080 ? A GLN 1080 
1081 1 Y 1 A ALA 1081 ? A ALA 1081 
1082 1 Y 1 A LEU 1082 ? A LEU 1082 
1083 1 Y 1 A LEU 1083 ? A LEU 1083 
1084 1 Y 1 A VAL 1084 ? A VAL 1084 
1085 1 Y 1 A GLN 1085 ? A GLN 1085 
1086 1 Y 1 A ILE 1086 ? A ILE 1086 
1087 1 Y 1 A ARG 1087 ? A ARG 1087 
1088 1 Y 1 A LYS 1088 ? A LYS 1088 
1089 1 Y 1 A ALA 1089 ? A ALA 1089 
1090 1 Y 1 A ARG 1090 ? A ARG 1090 
1091 1 Y 1 A GLY 1091 ? A GLY 1091 
1092 1 Y 1 A THR 1092 ? A THR 1092 
1093 1 Y 1 A PHE 1093 ? A PHE 1093 
1094 1 Y 1 A ASP 1094 ? A ASP 1094 
1095 1 Y 1 A ASN 1095 ? A ASN 1095 
1096 1 Y 1 A ALA 1096 ? A ALA 1096 
1097 1 Y 1 A GLU 1097 ? A GLU 1097 
1098 1 Y 1 A THR 1098 ? A THR 1098 
1099 1 Y 1 A LYS 1099 ? A LYS 1099 
1100 1 Y 1 A LYS 1100 ? A LYS 1100 
1101 1 Y 1 A GLU 1101 ? A GLU 1101 
1102 1 Y 1 A PHE 1102 ? A PHE 1102 
1103 1 Y 1 A GLY 1103 ? A GLY 1103 
1104 1 Y 1 A PRO 1104 ? A PRO 1104 
1105 1 Y 1 A VAL 1105 ? A VAL 1105 
1106 1 Y 1 A VAL 1106 ? A VAL 1106 
1107 1 Y 1 A ILE 1107 ? A ILE 1107 
1108 1 Y 1 A ASP 1108 ? A ASP 1108 
1109 1 Y 1 A TYR 1109 ? A TYR 1109 
1110 1 Y 1 A GLY 1110 ? A GLY 1110 
1111 1 Y 1 A LYS 1111 ? A LYS 1111 
1112 1 Y 1 A VAL 1112 ? A VAL 1112 
1113 1 Y 1 A GLN 1113 ? A GLN 1113 
1114 1 Y 1 A SER 1114 ? A SER 1114 
1115 1 Y 1 A LYS 1115 ? A LYS 1115 
1116 1 Y 1 A VAL 1116 ? A VAL 1116 
1117 1 Y 1 A ASN 1117 ? A ASN 1117 
1118 1 Y 1 A LEU 1118 ? A LEU 1118 
1119 1 Y 1 A LYS 1119 ? A LYS 1119 
1120 1 Y 1 A TYR 1120 ? A TYR 1120 
1121 1 Y 1 A ASP 1121 ? A ASP 1121 
1122 1 Y 1 A SER 1122 ? A SER 1122 
1123 1 Y 1 A TRP 1123 ? A TRP 1123 
1124 1 Y 1 A HIS 1124 ? A HIS 1124 
1125 1 Y 1 A LYS 1125 ? A LYS 1125 
1126 1 Y 1 A GLU 1126 ? A GLU 1126 
1127 1 Y 1 A VAL 1127 ? A VAL 1127 
1128 1 Y 1 A LEU 1128 ? A LEU 1128 
1129 1 Y 1 A SER 1129 ? A SER 1129 
1130 1 Y 1 A LYS 1130 ? A LYS 1130 
1131 1 Y 1 A PHE 1131 ? A PHE 1131 
1132 1 Y 1 A GLY 1132 ? A GLY 1132 
1133 1 Y 1 A GLN 1133 ? A GLN 1133 
1134 1 Y 1 A MET 1134 ? A MET 1134 
1135 1 Y 1 A LEU 1135 ? A LEU 1135 
1136 1 Y 1 A GLY 1136 ? A GLY 1136 
1137 1 Y 1 A SER 1137 ? A SER 1137 
1138 1 Y 1 A ASN 1138 ? A ASN 1138 
1139 1 Y 1 A MET 1139 ? A MET 1139 
1140 1 Y 1 A THR 1140 ? A THR 1140 
1141 1 Y 1 A GLU 1141 ? A GLU 1141 
1142 1 Y 1 A PHE 1142 ? A PHE 1142 
1143 1 Y 1 A HIS 1143 ? A HIS 1143 
1144 1 Y 1 A SER 1144 ? A SER 1144 
1145 1 Y 1 A GLN 1145 ? A GLN 1145 
1146 1 Y 1 A ILE 1146 ? A ILE 1146 
1147 1 Y 1 A SER 1147 ? A SER 1147 
1148 1 Y 1 A LYS 1148 ? A LYS 1148 
1149 1 Y 1 A SER 1149 ? A SER 1149 
1150 1 Y 1 A ARG 1150 ? A ARG 1150 
1151 1 Y 1 A GLN 1151 ? A GLN 1151 
1152 1 Y 1 A GLU 1152 ? A GLU 1152 
1153 1 Y 1 A LEU 1153 ? A LEU 1153 
1154 1 Y 1 A GLU 1154 ? A GLU 1154 
1155 1 Y 1 A GLN 1155 ? A GLN 1155 
1156 1 Y 1 A HIS 1156 ? A HIS 1156 
1157 1 Y 1 A SER 1157 ? A SER 1157 
1158 1 Y 1 A VAL 1158 ? A VAL 1158 
1159 1 Y 1 A ASP 1159 ? A ASP 1159 
1160 1 Y 1 A THR 1160 ? A THR 1160 
1161 1 Y 1 A ALA 1161 ? A ALA 1161 
1162 1 Y 1 A SER 1162 ? A SER 1162 
1163 1 Y 1 A THR 1163 ? A THR 1163 
1164 1 Y 1 A SER 1164 ? A SER 1164 
1165 1 Y 1 A ASP 1165 ? A ASP 1165 
1166 1 Y 1 A ALA 1166 ? A ALA 1166 
1167 1 Y 1 A VAL 1167 ? A VAL 1167 
1168 1 Y 1 A THR 1168 ? A THR 1168 
1169 1 Y 1 A PHE 1169 ? A PHE 1169 
1170 1 Y 1 A ILE 1170 ? A ILE 1170 
1171 1 Y 1 A THR 1171 ? A THR 1171 
1172 1 Y 1 A TYR 1172 ? A TYR 1172 
1173 1 Y 1 A VAL 1173 ? A VAL 1173 
1174 1 Y 1 A GLN 1174 ? A GLN 1174 
1175 1 Y 1 A SER 1175 ? A SER 1175 
1176 1 Y 1 A LEU 1176 ? A LEU 1176 
1177 1 Y 1 A LYS 1177 ? A LYS 1177 
1178 1 Y 1 A ARG 1178 ? A ARG 1178 
1179 1 Y 1 A LYS 1179 ? A LYS 1179 
1180 1 Y 1 A ILE 1180 ? A ILE 1180 
1181 1 Y 1 A LYS 1181 ? A LYS 1181 
1182 1 Y 1 A GLN 1182 ? A GLN 1182 
1183 1 Y 1 A PHE 1183 ? A PHE 1183 
1184 1 Y 1 A GLU 1184 ? A GLU 1184 
1185 1 Y 1 A LYS 1185 ? A LYS 1185 
1186 1 Y 1 A GLN 1186 ? A GLN 1186 
1187 1 Y 1 A VAL 1187 ? A VAL 1187 
1188 1 Y 1 A GLU 1188 ? A GLU 1188 
1189 1 Y 1 A LEU 1189 ? A LEU 1189 
1190 1 Y 1 A TYR 1190 ? A TYR 1190 
1191 1 Y 1 A ARG 1191 ? A ARG 1191 
1192 1 Y 1 A ASN 1192 ? A ASN 1192 
1193 1 Y 1 A GLY 1193 ? A GLY 1193 
1194 1 Y 1 A GLN 1194 ? A GLN 1194 
1195 1 Y 1 A ARG 1195 ? A ARG 1195 
1196 1 Y 1 A LEU 1196 ? A LEU 1196 
1197 1 Y 1 A LEU 1197 ? A LEU 1197 
1198 1 Y 1 A GLU 1198 ? A GLU 1198 
1199 1 Y 1 A LYS 1199 ? A LYS 1199 
1200 1 Y 1 A GLN 1200 ? A GLN 1200 
1201 1 Y 1 A ARG 1201 ? A ARG 1201 
1202 1 Y 1 A PHE 1202 ? A PHE 1202 
1203 1 Y 1 A GLN 1203 ? A GLN 1203 
1204 1 Y 1 A PHE 1204 ? A PHE 1204 
1205 1 Y 1 A PRO 1205 ? A PRO 1205 
1206 1 Y 1 A PRO 1206 ? A PRO 1206 
1207 1 Y 1 A SER 1207 ? A SER 1207 
1208 1 Y 1 A TRP 1208 ? A TRP 1208 
1209 1 Y 1 A LEU 1209 ? A LEU 1209 
1210 1 Y 1 A TYR 1210 ? A TYR 1210 
1211 1 Y 1 A ILE 1211 ? A ILE 1211 
1212 1 Y 1 A ASP 1212 ? A ASP 1212 
1213 1 Y 1 A ASN 1213 ? A ASN 1213 
1214 1 Y 1 A ILE 1214 ? A ILE 1214 
1215 1 Y 1 A GLU 1215 ? A GLU 1215 
1216 1 Y 1 A GLY 1216 ? A GLY 1216 
1217 1 Y 1 A GLU 1217 ? A GLU 1217 
1218 1 Y 1 A TRP 1218 ? A TRP 1218 
1219 1 Y 1 A GLY 1219 ? A GLY 1219 
1220 1 Y 1 A ALA 1220 ? A ALA 1220 
1221 1 Y 1 A PHE 1221 ? A PHE 1221 
1222 1 Y 1 A ASN 1222 ? A ASN 1222 
1223 1 Y 1 A ASP 1223 ? A ASP 1223 
1224 1 Y 1 A ILE 1224 ? A ILE 1224 
1225 1 Y 1 A MET 1225 ? A MET 1225 
1226 1 Y 1 A ARG 1226 ? A ARG 1226 
1227 1 Y 1 A ARG 1227 ? A ARG 1227 
1228 1 Y 1 A LYS 1228 ? A LYS 1228 
1229 1 Y 1 A ASP 1229 ? A ASP 1229 
1230 1 Y 1 A SER 1230 ? A SER 1230 
1231 1 Y 1 A ALA 1231 ? A ALA 1231 
1232 1 Y 1 A ILE 1232 ? A ILE 1232 
1233 1 Y 1 A GLN 1233 ? A GLN 1233 
1234 1 Y 1 A GLN 1234 ? A GLN 1234 
1235 1 Y 1 A GLN 1235 ? A GLN 1235 
1236 1 Y 1 A VAL 1236 ? A VAL 1236 
1237 1 Y 1 A ALA 1237 ? A ALA 1237 
1238 1 Y 1 A ASN 1238 ? A ASN 1238 
1239 1 Y 1 A LEU 1239 ? A LEU 1239 
1240 1 Y 1 A GLN 1240 ? A GLN 1240 
1241 1 Y 1 A MET 1241 ? A MET 1241 
1242 1 Y 1 A LYS 1242 ? A LYS 1242 
1243 1 Y 1 A ILE 1243 ? A ILE 1243 
1244 1 Y 1 A VAL 1244 ? A VAL 1244 
1245 1 Y 1 A GLN 1245 ? A GLN 1245 
1246 1 Y 1 A GLU 1246 ? A GLU 1246 
1247 1 Y 1 A ASP 1247 ? A ASP 1247 
1248 1 Y 1 A ARG 1248 ? A ARG 1248 
1249 1 Y 1 A ALA 1249 ? A ALA 1249 
1250 1 Y 1 A VAL 1250 ? A VAL 1250 
1251 1 Y 1 A GLU 1251 ? A GLU 1251 
1252 1 Y 1 A SER 1252 ? A SER 1252 
1253 1 Y 1 A ARG 1253 ? A ARG 1253 
1254 1 Y 1 A THR 1254 ? A THR 1254 
1255 1 Y 1 A THR 1255 ? A THR 1255 
1256 1 Y 1 A ASP 1256 ? A ASP 1256 
1257 1 Y 1 A LEU 1257 ? A LEU 1257 
1258 1 Y 1 A LEU 1258 ? A LEU 1258 
1259 1 Y 1 A THR 1259 ? A THR 1259 
1260 1 Y 1 A ASP 1260 ? A ASP 1260 
1261 1 Y 1 A TRP 1261 ? A TRP 1261 
1262 1 Y 1 A GLU 1262 ? A GLU 1262 
1263 1 Y 1 A LYS 1263 ? A LYS 1263 
1264 1 Y 1 A THR 1264 ? A THR 1264 
1265 1 Y 1 A LYS 1265 ? A LYS 1265 
1266 1 Y 1 A PRO 1266 ? A PRO 1266 
1267 1 Y 1 A VAL 1267 ? A VAL 1267 
1268 1 Y 1 A THR 1268 ? A THR 1268 
1269 1 Y 1 A GLY 1269 ? A GLY 1269 
1270 1 Y 1 A ASN 1270 ? A ASN 1270 
1271 1 Y 1 A LEU 1271 ? A LEU 1271 
1272 1 Y 1 A ARG 1272 ? A ARG 1272 
1273 1 Y 1 A PRO 1273 ? A PRO 1273 
1274 1 Y 1 A GLU 1274 ? A GLU 1274 
1275 1 Y 1 A GLU 1275 ? A GLU 1275 
1276 1 Y 1 A ALA 1276 ? A ALA 1276 
1277 1 Y 1 A LEU 1277 ? A LEU 1277 
1278 1 Y 1 A GLN 1278 ? A GLN 1278 
1279 1 Y 1 A ALA 1279 ? A ALA 1279 
1280 1 Y 1 A LEU 1280 ? A LEU 1280 
1281 1 Y 1 A THR 1281 ? A THR 1281 
1282 1 Y 1 A ILE 1282 ? A ILE 1282 
1283 1 Y 1 A TYR 1283 ? A TYR 1283 
1284 1 Y 1 A GLU 1284 ? A GLU 1284 
1285 1 Y 1 A GLY 1285 ? A GLY 1285 
1286 1 Y 1 A LYS 1286 ? A LYS 1286 
1287 1 Y 1 A PHE 1287 ? A PHE 1287 
1288 1 Y 1 A GLY 1288 ? A GLY 1288 
1289 1 Y 1 A ARG 1289 ? A ARG 1289 
1290 1 Y 1 A LEU 1290 ? A LEU 1290 
1291 1 Y 1 A LYS 1291 ? A LYS 1291 
1292 1 Y 1 A ASP 1292 ? A ASP 1292 
1293 1 Y 1 A ASP 1293 ? A ASP 1293 
1294 1 Y 1 A ARG 1294 ? A ARG 1294 
1295 1 Y 1 A GLU 1295 ? A GLU 1295 
1296 1 Y 1 A LYS 1296 ? A LYS 1296 
1297 1 Y 1 A CYS 1297 ? A CYS 1297 
1298 1 Y 1 A ALA 1298 ? A ALA 1298 
1299 1 Y 1 A LYS 1299 ? A LYS 1299 
1300 1 Y 1 A ALA 1300 ? A ALA 1300 
1301 1 Y 1 A LYS 1301 ? A LYS 1301 
1302 1 Y 1 A GLU 1302 ? A GLU 1302 
1303 1 Y 1 A ALA 1303 ? A ALA 1303 
1304 1 Y 1 A LEU 1304 ? A LEU 1304 
1305 1 Y 1 A GLU 1305 ? A GLU 1305 
1306 1 Y 1 A LEU 1306 ? A LEU 1306 
1307 1 Y 1 A THR 1307 ? A THR 1307 
1308 1 Y 1 A ASP 1308 ? A ASP 1308 
1309 1 Y 1 A THR 1309 ? A THR 1309 
1310 1 Y 1 A GLY 1310 ? A GLY 1310 
1311 1 Y 1 A LEU 1311 ? A LEU 1311 
1312 1 Y 1 A LEU 1312 ? A LEU 1312 
1313 1 Y 1 A SER 1313 ? A SER 1313 
1314 1 Y 1 A GLY 1314 ? A GLY 1314 
1315 1 Y 1 A SER 1315 ? A SER 1315 
1316 1 Y 1 A GLU 1316 ? A GLU 1316 
1317 1 Y 1 A GLU 1317 ? A GLU 1317 
1318 1 Y 1 A ARG 1318 ? A ARG 1318 
1319 1 Y 1 A VAL 1319 ? A VAL 1319 
1320 1 Y 1 A GLN 1320 ? A GLN 1320 
1321 1 Y 1 A VAL 1321 ? A VAL 1321 
1322 1 Y 1 A ALA 1322 ? A ALA 1322 
1323 1 Y 1 A LEU 1323 ? A LEU 1323 
1324 1 Y 1 A GLU 1324 ? A GLU 1324 
1325 1 Y 1 A GLU 1325 ? A GLU 1325 
1326 1 Y 1 A LEU 1326 ? A LEU 1326 
1327 1 Y 1 A GLN 1327 ? A GLN 1327 
1328 1 Y 1 A ASP 1328 ? A ASP 1328 
1329 1 Y 1 A LEU 1329 ? A LEU 1329 
1330 1 Y 1 A LYS 1330 ? A LYS 1330 
1331 1 Y 1 A GLY 1331 ? A GLY 1331 
1332 1 Y 1 A VAL 1332 ? A VAL 1332 
1333 1 Y 1 A TRP 1333 ? A TRP 1333 
1334 1 Y 1 A SER 1334 ? A SER 1334 
1335 1 Y 1 A GLU 1335 ? A GLU 1335 
1336 1 Y 1 A LEU 1336 ? A LEU 1336 
1337 1 Y 1 A SER 1337 ? A SER 1337 
1338 1 Y 1 A LYS 1338 ? A LYS 1338 
1339 1 Y 1 A VAL 1339 ? A VAL 1339 
1340 1 Y 1 A TRP 1340 ? A TRP 1340 
1341 1 Y 1 A GLU 1341 ? A GLU 1341 
1342 1 Y 1 A GLN 1342 ? A GLN 1342 
1343 1 Y 1 A ILE 1343 ? A ILE 1343 
1344 1 Y 1 A ASP 1344 ? A ASP 1344 
1345 1 Y 1 A GLN 1345 ? A GLN 1345 
1346 1 Y 1 A MET 1346 ? A MET 1346 
1347 1 Y 1 A LYS 1347 ? A LYS 1347 
1348 1 Y 1 A GLU 1348 ? A GLU 1348 
1349 1 Y 1 A GLN 1349 ? A GLN 1349 
1350 1 Y 1 A PRO 1350 ? A PRO 1350 
1351 1 Y 1 A TRP 1351 ? A TRP 1351 
1352 1 Y 1 A VAL 1352 ? A VAL 1352 
1353 1 Y 1 A SER 1353 ? A SER 1353 
1354 1 Y 1 A VAL 1354 ? A VAL 1354 
1355 1 Y 1 A GLN 1355 ? A GLN 1355 
1356 1 Y 1 A PRO 1356 ? A PRO 1356 
1357 1 Y 1 A ARG 1357 ? A ARG 1357 
1358 1 Y 1 A LYS 1358 ? A LYS 1358 
1359 1 Y 1 A LEU 1359 ? A LEU 1359 
1360 1 Y 1 A ARG 1360 ? A ARG 1360 
1361 1 Y 1 A GLN 1361 ? A GLN 1361 
1362 1 Y 1 A ASN 1362 ? A ASN 1362 
1363 1 Y 1 A LEU 1363 ? A LEU 1363 
1364 1 Y 1 A ASP 1364 ? A ASP 1364 
1365 1 Y 1 A ALA 1365 ? A ALA 1365 
1366 1 Y 1 A LEU 1366 ? A LEU 1366 
1367 1 Y 1 A LEU 1367 ? A LEU 1367 
1368 1 Y 1 A ASN 1368 ? A ASN 1368 
1369 1 Y 1 A GLN 1369 ? A GLN 1369 
1370 1 Y 1 A LEU 1370 ? A LEU 1370 
1371 1 Y 1 A LYS 1371 ? A LYS 1371 
1372 1 Y 1 A SER 1372 ? A SER 1372 
1373 1 Y 1 A PHE 1373 ? A PHE 1373 
1374 1 Y 1 A PRO 1374 ? A PRO 1374 
1375 1 Y 1 A ALA 1375 ? A ALA 1375 
1376 1 Y 1 A ARG 1376 ? A ARG 1376 
1377 1 Y 1 A LEU 1377 ? A LEU 1377 
1378 1 Y 1 A ARG 1378 ? A ARG 1378 
1379 1 Y 1 A GLN 1379 ? A GLN 1379 
1380 1 Y 1 A TYR 1380 ? A TYR 1380 
1381 1 Y 1 A ALA 1381 ? A ALA 1381 
1382 1 Y 1 A SER 1382 ? A SER 1382 
1383 1 Y 1 A TYR 1383 ? A TYR 1383 
1384 1 Y 1 A GLU 1384 ? A GLU 1384 
1385 1 Y 1 A PHE 1385 ? A PHE 1385 
1386 1 Y 1 A VAL 1386 ? A VAL 1386 
1387 1 Y 1 A GLN 1387 ? A GLN 1387 
1388 1 Y 1 A ARG 1388 ? A ARG 1388 
1389 1 Y 1 A LEU 1389 ? A LEU 1389 
1390 1 Y 1 A LEU 1390 ? A LEU 1390 
1391 1 Y 1 A LYS 1391 ? A LYS 1391 
1392 1 Y 1 A GLY 1392 ? A GLY 1392 
1393 1 Y 1 A TYR 1393 ? A TYR 1393 
1394 1 Y 1 A MET 1394 ? A MET 1394 
1395 1 Y 1 A LYS 1395 ? A LYS 1395 
1396 1 Y 1 A ILE 1396 ? A ILE 1396 
1397 1 Y 1 A ASN 1397 ? A ASN 1397 
1398 1 Y 1 A MET 1398 ? A MET 1398 
1399 1 Y 1 A LEU 1399 ? A LEU 1399 
1400 1 Y 1 A VAL 1400 ? A VAL 1400 
1401 1 Y 1 A ILE 1401 ? A ILE 1401 
1402 1 Y 1 A GLU 1402 ? A GLU 1402 
1403 1 Y 1 A LEU 1403 ? A LEU 1403 
1404 1 Y 1 A LYS 1404 ? A LYS 1404 
1405 1 Y 1 A SER 1405 ? A SER 1405 
1406 1 Y 1 A GLU 1406 ? A GLU 1406 
1407 1 Y 1 A ALA 1407 ? A ALA 1407 
1408 1 Y 1 A LEU 1408 ? A LEU 1408 
1409 1 Y 1 A LYS 1409 ? A LYS 1409 
1410 1 Y 1 A ASP 1410 ? A ASP 1410 
1411 1 Y 1 A ARG 1411 ? A ARG 1411 
1412 1 Y 1 A HIS 1412 ? A HIS 1412 
1413 1 Y 1 A TRP 1413 ? A TRP 1413 
1414 1 Y 1 A LYS 1414 ? A LYS 1414 
1415 1 Y 1 A GLN 1415 ? A GLN 1415 
1416 1 Y 1 A LEU 1416 ? A LEU 1416 
1417 1 Y 1 A MET 1417 ? A MET 1417 
1418 1 Y 1 A LYS 1418 ? A LYS 1418 
1419 1 Y 1 A ARG 1419 ? A ARG 1419 
1420 1 Y 1 A LEU 1420 ? A LEU 1420 
1421 1 Y 1 A HIS 1421 ? A HIS 1421 
1422 1 Y 1 A VAL 1422 ? A VAL 1422 
1423 1 Y 1 A ASN 1423 ? A ASN 1423 
1424 1 Y 1 A TRP 1424 ? A TRP 1424 
1425 1 Y 1 A VAL 1425 ? A VAL 1425 
1426 1 Y 1 A VAL 1426 ? A VAL 1426 
1427 1 Y 1 A SER 1427 ? A SER 1427 
1428 1 Y 1 A GLU 1428 ? A GLU 1428 
1429 1 Y 1 A LEU 1429 ? A LEU 1429 
1430 1 Y 1 A THR 1430 ? A THR 1430 
1431 1 Y 1 A LEU 1431 ? A LEU 1431 
1432 1 Y 1 A GLY 1432 ? A GLY 1432 
1433 1 Y 1 A GLN 1433 ? A GLN 1433 
1434 1 Y 1 A ILE 1434 ? A ILE 1434 
1435 1 Y 1 A TRP 1435 ? A TRP 1435 
1436 1 Y 1 A ASP 1436 ? A ASP 1436 
1437 1 Y 1 A VAL 1437 ? A VAL 1437 
1438 1 Y 1 A ASP 1438 ? A ASP 1438 
1439 1 Y 1 A LEU 1439 ? A LEU 1439 
1440 1 Y 1 A GLN 1440 ? A GLN 1440 
1441 1 Y 1 A LYS 1441 ? A LYS 1441 
1442 1 Y 1 A ASN 1442 ? A ASN 1442 
1443 1 Y 1 A GLU 1443 ? A GLU 1443 
1444 1 Y 1 A ALA 1444 ? A ALA 1444 
1445 1 Y 1 A ILE 1445 ? A ILE 1445 
1446 1 Y 1 A VAL 1446 ? A VAL 1446 
1447 1 Y 1 A LYS 1447 ? A LYS 1447 
1448 1 Y 1 A ASP 1448 ? A ASP 1448 
1449 1 Y 1 A VAL 1449 ? A VAL 1449 
1450 1 Y 1 A LEU 1450 ? A LEU 1450 
1451 1 Y 1 A LEU 1451 ? A LEU 1451 
1452 1 Y 1 A VAL 1452 ? A VAL 1452 
1453 1 Y 1 A ALA 1453 ? A ALA 1453 
1454 1 Y 1 A GLN 1454 ? A GLN 1454 
1455 1 Y 1 A GLY 1455 ? A GLY 1455 
1456 1 Y 1 A GLU 1456 ? A GLU 1456 
1457 1 Y 1 A MET 1457 ? A MET 1457 
1458 1 Y 1 A ALA 1458 ? A ALA 1458 
1459 1 Y 1 A LEU 1459 ? A LEU 1459 
1460 1 Y 1 A GLU 1460 ? A GLU 1460 
1461 1 Y 1 A GLU 1461 ? A GLU 1461 
1462 1 Y 1 A PHE 1462 ? A PHE 1462 
1463 1 Y 1 A LEU 1463 ? A LEU 1463 
1464 1 Y 1 A LYS 1464 ? A LYS 1464 
1465 1 Y 1 A GLN 1465 ? A GLN 1465 
1466 1 Y 1 A ILE 1466 ? A ILE 1466 
1467 1 Y 1 A ARG 1467 ? A ARG 1467 
1468 1 Y 1 A GLU 1468 ? A GLU 1468 
1469 1 Y 1 A VAL 1469 ? A VAL 1469 
1470 1 Y 1 A TRP 1470 ? A TRP 1470 
1471 1 Y 1 A ASN 1471 ? A ASN 1471 
1472 1 Y 1 A THR 1472 ? A THR 1472 
1473 1 Y 1 A TYR 1473 ? A TYR 1473 
1474 1 Y 1 A GLU 1474 ? A GLU 1474 
1475 1 Y 1 A LEU 1475 ? A LEU 1475 
1476 1 Y 1 A ASP 1476 ? A ASP 1476 
1477 1 Y 1 A LEU 1477 ? A LEU 1477 
1478 1 Y 1 A VAL 1478 ? A VAL 1478 
1479 1 Y 1 A ASN 1479 ? A ASN 1479 
1480 1 Y 1 A TYR 1480 ? A TYR 1480 
1481 1 Y 1 A GLN 1481 ? A GLN 1481 
1482 1 Y 1 A ASN 1482 ? A ASN 1482 
1483 1 Y 1 A LYS 1483 ? A LYS 1483 
1484 1 Y 1 A CYS 1484 ? A CYS 1484 
1485 1 Y 1 A ARG 1485 ? A ARG 1485 
1486 1 Y 1 A LEU 1486 ? A LEU 1486 
1487 1 Y 1 A ILE 1487 ? A ILE 1487 
1488 1 Y 1 A ARG 1488 ? A ARG 1488 
1489 1 Y 1 A GLY 1489 ? A GLY 1489 
1490 1 Y 1 A TRP 1490 ? A TRP 1490 
1491 1 Y 1 A ASP 1491 ? A ASP 1491 
1492 1 Y 1 A ASP 1492 ? A ASP 1492 
1493 1 Y 1 A LEU 1493 ? A LEU 1493 
1494 1 Y 1 A PHE 1494 ? A PHE 1494 
1495 1 Y 1 A ASN 1495 ? A ASN 1495 
1496 1 Y 1 A LYS 1496 ? A LYS 1496 
1497 1 Y 1 A VAL 1497 ? A VAL 1497 
1498 1 Y 1 A LYS 1498 ? A LYS 1498 
1499 1 Y 1 A GLU 1499 ? A GLU 1499 
1500 1 Y 1 A HIS 1500 ? A HIS 1500 
1501 1 Y 1 A ILE 1501 ? A ILE 1501 
1502 1 Y 1 A ASN 1502 ? A ASN 1502 
1503 1 Y 1 A SER 1503 ? A SER 1503 
1504 1 Y 1 A VAL 1504 ? A VAL 1504 
1505 1 Y 1 A SER 1505 ? A SER 1505 
1506 1 Y 1 A ALA 1506 ? A ALA 1506 
1507 1 Y 1 A MET 1507 ? A MET 1507 
1508 1 Y 1 A LYS 1508 ? A LYS 1508 
1509 1 Y 1 A LEU 1509 ? A LEU 1509 
1510 1 Y 1 A SER 1510 ? A SER 1510 
1511 1 Y 1 A PRO 1511 ? A PRO 1511 
1512 1 Y 1 A TYR 1512 ? A TYR 1512 
1513 1 Y 1 A TYR 1513 ? A TYR 1513 
1514 1 Y 1 A LYS 1514 ? A LYS 1514 
1515 1 Y 1 A VAL 1515 ? A VAL 1515 
1516 1 Y 1 A PHE 1516 ? A PHE 1516 
1517 1 Y 1 A GLU 1517 ? A GLU 1517 
1518 1 Y 1 A GLU 1518 ? A GLU 1518 
1519 1 Y 1 A ASP 1519 ? A ASP 1519 
1520 1 Y 1 A ALA 1520 ? A ALA 1520 
1521 1 Y 1 A LEU 1521 ? A LEU 1521 
1522 1 Y 1 A SER 1522 ? A SER 1522 
1523 1 Y 1 A TRP 1523 ? A TRP 1523 
1524 1 Y 1 A GLU 1524 ? A GLU 1524 
1525 1 Y 1 A ASP 1525 ? A ASP 1525 
1526 1 Y 1 A LYS 1526 ? A LYS 1526 
1527 1 Y 1 A LEU 1527 ? A LEU 1527 
1528 1 Y 1 A ASN 1528 ? A ASN 1528 
1529 1 Y 1 A ARG 1529 ? A ARG 1529 
1530 1 Y 1 A ILE 1530 ? A ILE 1530 
1531 1 Y 1 A MET 1531 ? A MET 1531 
1532 1 Y 1 A ALA 1532 ? A ALA 1532 
1533 1 Y 1 A LEU 1533 ? A LEU 1533 
1534 1 Y 1 A PHE 1534 ? A PHE 1534 
1535 1 Y 1 A GLY 2390 ? A GLY 2390 
1536 1 Y 1 A GLU 2391 ? A GLU 2391 
1537 1 Y 1 A ASP 2392 ? A ASP 2392 
1538 1 Y 1 A GLU 2393 ? A GLU 2393 
1539 1 Y 1 A ALA 2394 ? A ALA 2394 
1540 1 Y 1 A GLN 2395 ? A GLN 2395 
1541 1 Y 1 A ARG 2396 ? A ARG 2396 
1542 1 Y 1 A ARG 2397 ? A ARG 2397 
1543 1 Y 1 A ARG 2398 ? A ARG 2398 
1544 1 Y 1 A LYS 2399 ? A LYS 2399 
1545 1 Y 1 A GLY 2400 ? A GLY 2400 
1546 1 Y 1 A LYS 2401 ? A LYS 2401 
1547 1 Y 1 A GLU 2402 ? A GLU 2402 
1548 1 Y 1 A ASP 2403 ? A ASP 2403 
1549 1 Y 1 A GLU 2404 ? A GLU 2404 
1550 1 Y 1 A GLY 2405 ? A GLY 2405 
1551 1 Y 1 A GLU 2406 ? A GLU 2406 
1552 1 Y 1 A GLU 2407 ? A GLU 2407 
1553 1 Y 1 A ALA 2408 ? A ALA 2408 
1554 1 Y 1 A ALA 2409 ? A ALA 2409 
1555 1 Y 1 A MET 3243 ? A MET 3243 
1556 1 Y 1 A VAL 3244 ? A VAL 3244 
1557 1 Y 1 A LYS 3245 ? A LYS 3245 
1558 1 Y 1 A ASP 3246 ? A ASP 3246 
1559 1 Y 1 A GLN 3247 ? A GLN 3247 
1560 1 Y 1 A GLN 3248 ? A GLN 3248 
1561 1 Y 1 A GLU 3249 ? A GLU 3249 
1562 1 Y 1 A ALA 3250 ? A ALA 3250 
1563 1 Y 1 A GLU 3251 ? A GLU 3251 
1564 1 Y 1 A LYS 3252 ? A LYS 3252 
1565 1 Y 1 A LYS 3253 ? A LYS 3253 
1566 1 Y 1 A LYS 3254 ? A LYS 3254 
1567 1 Y 1 A VAL 3255 ? A VAL 3255 
1568 1 Y 1 A MET 3256 ? A MET 3256 
1569 1 Y 1 A SER 3257 ? A SER 3257 
1570 1 Y 1 A GLN 3258 ? A GLN 3258 
1571 1 Y 1 A GLU 3259 ? A GLU 3259 
1572 1 Y 1 A ILE 3260 ? A ILE 3260 
1573 1 Y 1 A GLN 3261 ? A GLN 3261 
1574 1 Y 1 A GLU 3262 ? A GLU 3262 
1575 1 Y 1 A GLN 3263 ? A GLN 3263 
1576 1 Y 1 A LEU 3264 ? A LEU 3264 
1577 1 Y 1 A HIS 3265 ? A HIS 3265 
1578 1 Y 1 A LYS 3266 ? A LYS 3266 
1579 1 Y 1 A GLN 3267 ? A GLN 3267 
1580 1 Y 1 A GLN 3268 ? A GLN 3268 
1581 1 Y 1 A GLU 3269 ? A GLU 3269 
1582 1 Y 1 A VAL 3270 ? A VAL 3270 
1583 1 Y 1 A ILE 3271 ? A ILE 3271 
1584 1 Y 1 A ALA 3272 ? A ALA 3272 
1585 1 Y 1 A ASP 3273 ? A ASP 3273 
1586 1 Y 1 A LYS 3274 ? A LYS 3274 
1587 1 Y 1 A GLN 3275 ? A GLN 3275 
1588 1 Y 1 A MET 3276 ? A MET 3276 
1589 1 Y 1 A SER 3277 ? A SER 3277 
1590 1 Y 1 A VAL 3278 ? A VAL 3278 
1591 1 Y 1 A LYS 3279 ? A LYS 3279 
1592 1 Y 1 A GLU 3280 ? A GLU 3280 
1593 1 Y 1 A ASP 3281 ? A ASP 3281 
1594 1 Y 1 A LEU 3282 ? A LEU 3282 
1595 1 Y 1 A ASP 3283 ? A ASP 3283 
1596 1 Y 1 A LYS 3284 ? A LYS 3284 
1597 1 Y 1 A VAL 3285 ? A VAL 3285 
1598 1 Y 1 A GLU 3286 ? A GLU 3286 
1599 1 Y 1 A PRO 3287 ? A PRO 3287 
1600 1 Y 1 A ALA 3288 ? A ALA 3288 
1601 1 Y 1 A VAL 3289 ? A VAL 3289 
1602 1 Y 1 A ILE 3290 ? A ILE 3290 
1603 1 Y 1 A GLU 3291 ? A GLU 3291 
1604 1 Y 1 A ALA 3292 ? A ALA 3292 
1605 1 Y 1 A GLN 3293 ? A GLN 3293 
1606 1 Y 1 A ASN 3294 ? A ASN 3294 
1607 1 Y 1 A ALA 3295 ? A ALA 3295 
1608 1 Y 1 A VAL 3296 ? A VAL 3296 
1609 1 Y 1 A LYS 3297 ? A LYS 3297 
1610 1 Y 1 A SER 3298 ? A SER 3298 
1611 1 Y 1 A ILE 3299 ? A ILE 3299 
1612 1 Y 1 A LYS 3300 ? A LYS 3300 
1613 1 Y 1 A LYS 3301 ? A LYS 3301 
1614 1 Y 1 A GLN 3302 ? A GLN 3302 
1615 1 Y 1 A HIS 3303 ? A HIS 3303 
1616 1 Y 1 A LEU 3304 ? A LEU 3304 
1617 1 Y 1 A VAL 3305 ? A VAL 3305 
1618 1 Y 1 A GLU 3306 ? A GLU 3306 
1619 1 Y 1 A VAL 3307 ? A VAL 3307 
1620 1 Y 1 A ARG 3308 ? A ARG 3308 
1621 1 Y 1 A SER 3309 ? A SER 3309 
1622 1 Y 1 A MET 3310 ? A MET 3310 
1623 1 Y 1 A ALA 3311 ? A ALA 3311 
1624 1 Y 1 A ASN 3312 ? A ASN 3312 
1625 1 Y 1 A PRO 3313 ? A PRO 3313 
1626 1 Y 1 A PRO 3314 ? A PRO 3314 
1627 1 Y 1 A ALA 3315 ? A ALA 3315 
1628 1 Y 1 A ALA 3316 ? A ALA 3316 
1629 1 Y 1 A VAL 3317 ? A VAL 3317 
1630 1 Y 1 A LYS 3318 ? A LYS 3318 
1631 1 Y 1 A LEU 3319 ? A LEU 3319 
1632 1 Y 1 A ALA 3320 ? A ALA 3320 
1633 1 Y 1 A LEU 3321 ? A LEU 3321 
1634 1 Y 1 A GLU 3322 ? A GLU 3322 
1635 1 Y 1 A SER 3323 ? A SER 3323 
1636 1 Y 1 A ILE 3324 ? A ILE 3324 
1637 1 Y 1 A CYS 3325 ? A CYS 3325 
1638 1 Y 1 A LEU 3326 ? A LEU 3326 
1639 1 Y 1 A LEU 3327 ? A LEU 3327 
1640 1 Y 1 A LEU 3328 ? A LEU 3328 
1641 1 Y 1 A GLY 3329 ? A GLY 3329 
1642 1 Y 1 A GLU 3330 ? A GLU 3330 
1643 1 Y 1 A SER 3331 ? A SER 3331 
1644 1 Y 1 A THR 3332 ? A THR 3332 
1645 1 Y 1 A THR 3333 ? A THR 3333 
1646 1 Y 1 A ASP 3334 ? A ASP 3334 
1647 1 Y 1 A TRP 3335 ? A TRP 3335 
1648 1 Y 1 A LYS 3336 ? A LYS 3336 
1649 1 Y 1 A GLN 3337 ? A GLN 3337 
1650 1 Y 1 A ILE 3338 ? A ILE 3338 
1651 1 Y 1 A ARG 3339 ? A ARG 3339 
1652 1 Y 1 A SER 3340 ? A SER 3340 
1653 1 Y 1 A ILE 3341 ? A ILE 3341 
1654 1 Y 1 A ILE 3342 ? A ILE 3342 
1655 1 Y 1 A MET 3343 ? A MET 3343 
1656 1 Y 1 A ARG 3344 ? A ARG 3344 
1657 1 Y 1 A GLU 3345 ? A GLU 3345 
1658 1 Y 1 A ASN 3346 ? A ASN 3346 
1659 1 Y 1 A PHE 3347 ? A PHE 3347 
1660 1 Y 1 A ILE 3348 ? A ILE 3348 
1661 1 Y 1 A PRO 3349 ? A PRO 3349 
1662 1 Y 1 A THR 3350 ? A THR 3350 
1663 1 Y 1 A ILE 3351 ? A ILE 3351 
1664 1 Y 1 A VAL 3352 ? A VAL 3352 
1665 1 Y 1 A ASN 3353 ? A ASN 3353 
1666 1 Y 1 A PHE 3354 ? A PHE 3354 
1667 1 Y 1 A SER 3355 ? A SER 3355 
1668 1 Y 1 A ALA 3356 ? A ALA 3356 
1669 1 Y 1 A GLU 3357 ? A GLU 3357 
1670 1 Y 1 A GLU 3358 ? A GLU 3358 
1671 1 Y 1 A ILE 3359 ? A ILE 3359 
1672 1 Y 1 A SER 3360 ? A SER 3360 
1673 1 Y 1 A ASP 3361 ? A ASP 3361 
1674 1 Y 1 A ALA 3362 ? A ALA 3362 
1675 1 Y 1 A ILE 3363 ? A ILE 3363 
1676 1 Y 1 A ARG 3364 ? A ARG 3364 
1677 1 Y 1 A GLU 3365 ? A GLU 3365 
1678 1 Y 1 A LYS 3366 ? A LYS 3366 
1679 1 Y 1 A MET 3367 ? A MET 3367 
1680 1 Y 1 A LYS 3368 ? A LYS 3368 
1681 1 Y 1 A LYS 3369 ? A LYS 3369 
1682 1 Y 1 A ASN 3370 ? A ASN 3370 
1683 1 Y 1 A TYR 3371 ? A TYR 3371 
1684 1 Y 1 A MET 3372 ? A MET 3372 
1685 1 Y 1 A SER 3373 ? A SER 3373 
1686 1 Y 1 A ASN 3374 ? A ASN 3374 
1687 1 Y 1 A PRO 3375 ? A PRO 3375 
1688 1 Y 1 A SER 3376 ? A SER 3376 
1689 1 Y 1 A TYR 3377 ? A TYR 3377 
1690 1 Y 1 A ASN 3378 ? A ASN 3378 
1691 1 Y 1 A TYR 3379 ? A TYR 3379 
1692 1 Y 1 A GLU 3380 ? A GLU 3380 
1693 1 Y 1 A ILE 3381 ? A ILE 3381 
1694 1 Y 1 A VAL 3382 ? A VAL 3382 
1695 1 Y 1 A ASN 3383 ? A ASN 3383 
1696 1 Y 1 A ARG 3384 ? A ARG 3384 
1697 1 Y 1 A ALA 3385 ? A ALA 3385 
1698 1 Y 1 A SER 3386 ? A SER 3386 
1699 1 Y 1 A LEU 3387 ? A LEU 3387 
1700 1 Y 1 A ALA 3388 ? A ALA 3388 
1701 1 Y 1 A CYS 3389 ? A CYS 3389 
1702 1 Y 1 A GLY 3390 ? A GLY 3390 
1703 1 Y 1 A PRO 3391 ? A PRO 3391 
1704 1 Y 1 A MET 3392 ? A MET 3392 
1705 1 Y 1 A VAL 3393 ? A VAL 3393 
1706 1 Y 1 A LYS 3394 ? A LYS 3394 
1707 1 Y 1 A TRP 3395 ? A TRP 3395 
1708 1 Y 1 A ALA 3396 ? A ALA 3396 
1709 1 Y 1 A ILE 3397 ? A ILE 3397 
1710 1 Y 1 A ALA 3398 ? A ALA 3398 
1711 1 Y 1 A GLN 3399 ? A GLN 3399 
1712 1 Y 1 A LEU 3400 ? A LEU 3400 
1713 1 Y 1 A ASN 3401 ? A ASN 3401 
1714 1 Y 1 A TYR 3402 ? A TYR 3402 
1715 1 Y 1 A ALA 3403 ? A ALA 3403 
1716 1 Y 1 A ASP 3404 ? A ASP 3404 
1717 1 Y 1 A MET 3405 ? A MET 3405 
1718 1 Y 1 A LEU 3406 ? A LEU 3406 
1719 1 Y 1 A LYS 3407 ? A LYS 3407 
1720 1 Y 1 A ARG 3408 ? A ARG 3408 
1721 1 Y 1 A VAL 3409 ? A VAL 3409 
1722 1 Y 1 A GLU 3410 ? A GLU 3410 
1723 1 Y 1 A PRO 3411 ? A PRO 3411 
1724 1 Y 1 A LEU 3412 ? A LEU 3412 
1725 1 Y 1 A ARG 3413 ? A ARG 3413 
1726 1 Y 1 A ASN 3414 ? A ASN 3414 
1727 1 Y 1 A GLU 3415 ? A GLU 3415 
1728 1 Y 1 A LEU 3416 ? A LEU 3416 
1729 1 Y 1 A GLN 3417 ? A GLN 3417 
1730 1 Y 1 A LYS 3418 ? A LYS 3418 
1731 1 Y 1 A LEU 3419 ? A LEU 3419 
1732 1 Y 1 A GLU 3420 ? A GLU 3420 
1733 1 Y 1 A ASP 3421 ? A ASP 3421 
1734 1 Y 1 A ASP 3422 ? A ASP 3422 
1735 1 Y 1 A ALA 3423 ? A ALA 3423 
1736 1 Y 1 A LYS 3424 ? A LYS 3424 
1737 1 Y 1 A ASP 3425 ? A ASP 3425 
1738 1 Y 1 A ASN 3426 ? A ASN 3426 
1739 1 Y 1 A GLN 3427 ? A GLN 3427 
1740 1 Y 1 A GLN 3428 ? A GLN 3428 
1741 1 Y 1 A LYS 3429 ? A LYS 3429 
1742 1 Y 1 A ALA 3430 ? A ALA 3430 
1743 1 Y 1 A ASN 3431 ? A ASN 3431 
1744 1 Y 1 A GLU 3432 ? A GLU 3432 
1745 1 Y 1 A VAL 3433 ? A VAL 3433 
1746 1 Y 1 A GLU 3434 ? A GLU 3434 
1747 1 Y 1 A GLN 3435 ? A GLN 3435 
1748 1 Y 1 A MET 3436 ? A MET 3436 
1749 1 Y 1 A ILE 3437 ? A ILE 3437 
1750 1 Y 1 A ARG 3438 ? A ARG 3438 
1751 1 Y 1 A ASP 3439 ? A ASP 3439 
1752 1 Y 1 A LEU 3440 ? A LEU 3440 
1753 1 Y 1 A GLU 3441 ? A GLU 3441 
1754 1 Y 1 A ALA 3442 ? A ALA 3442 
1755 1 Y 1 A SER 3443 ? A SER 3443 
1756 1 Y 1 A ILE 3444 ? A ILE 3444 
1757 1 Y 1 A ALA 3445 ? A ALA 3445 
1758 1 Y 1 A ARG 3446 ? A ARG 3446 
1759 1 Y 1 A TYR 3447 ? A TYR 3447 
1760 1 Y 1 A LYS 3448 ? A LYS 3448 
1761 1 Y 1 A MET 4348 ? A MET 4348 
1762 1 Y 1 A LEU 4349 ? A LEU 4349 
1763 1 Y 1 A GLU 4350 ? A GLU 4350 
1764 1 Y 1 A ASP 4351 ? A ASP 4351 
1765 1 Y 1 A GLU 4352 ? A GLU 4352 
1766 1 Y 1 A ASP 4353 ? A ASP 4353 
1767 1 Y 1 A ASP 4354 ? A ASP 4354 
1768 1 Y 1 A LEU 4355 ? A LEU 4355 
1769 1 Y 1 A ALA 4356 ? A ALA 4356 
1770 1 Y 1 A TYR 4357 ? A TYR 4357 
1771 1 Y 1 A ALA 4358 ? A ALA 4358 
1772 1 Y 1 A GLU 4359 ? A GLU 4359 
1773 1 Y 1 A THR 4360 ? A THR 4360 
1774 1 Y 1 A GLU 4361 ? A GLU 4361 
1775 1 Y 1 A LYS 4362 ? A LYS 4362 
1776 1 Y 1 A LYS 4363 ? A LYS 4363 
1777 1 Y 1 A THR 4364 ? A THR 4364 
1778 1 Y 1 A ARG 4365 ? A ARG 4365 
1779 1 Y 1 A THR 4366 ? A THR 4366 
1780 1 Y 1 A ASP 4367 ? A ASP 4367 
1781 1 Y 1 A SER 4368 ? A SER 4368 
1782 1 Y 1 A THR 4369 ? A THR 4369 
1783 1 Y 1 A SER 4370 ? A SER 4370 
1784 1 Y 1 A ASP 4371 ? A ASP 4371 
1785 1 Y 1 A GLY 4372 ? A GLY 4372 
1786 1 Y 1 A ARG 4373 ? A ARG 4373 
1787 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    2024-05-02 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BM1 
_em_admin.last_update        2025-04-30 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-3 of motor domain from full-length human dynein-1 in 5mM ATP' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    YES 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                1.5 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         40 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?         ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 SerialEM  4 
MASKING                    ? 3  ? ? ? ?         ? 
'CTF CORRECTION'           ? 4  1 ? ? ?         ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?         ? 
'MODEL FITTING'            ? 7  ? ? ? ?         ? 
'MODEL REFINEMENT'         ? 8  ? ? ? ?         ? 
OTHER                      ? 9  ? ? ? ?         ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?         ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? cryoSPARC 4 
CLASSIFICATION             ? 12 1 ? ? ?         ? 
RECONSTRUCTION             ? 13 1 ? ? cryoSPARC 4 
# 
_em_specimen.concentration           2 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM142959 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM139483 2 
# 
_atom_sites.entry_id                    9BM1 
_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     . ASP A 1 1535 ? 135.309 204.519 160.266 1.00 106.30 ? 1535 ASP A N     1 
ATOM   2     C  CA    . ASP A 1 1535 ? 136.061 203.271 160.214 1.00 116.69 ? 1535 ASP A CA    1 
ATOM   3     C  C     . ASP A 1 1535 ? 135.163 202.078 160.524 1.00 124.61 ? 1535 ASP A C     1 
ATOM   4     O  O     . ASP A 1 1535 ? 135.423 200.960 160.080 1.00 129.44 ? 1535 ASP A O     1 
ATOM   5     C  CB    . ASP A 1 1535 ? 137.239 203.314 161.189 1.00 118.87 ? 1535 ASP A CB    1 
ATOM   6     C  CG    . ASP A 1 1535 ? 138.342 204.248 160.729 1.00 117.09 ? 1535 ASP A CG    1 
ATOM   7     O  OD1   . ASP A 1 1535 ? 138.509 204.413 159.502 1.00 111.83 ? 1535 ASP A OD1   1 
ATOM   8     O  OD2   . ASP A 1 1535 ? 139.041 204.816 161.594 1.00 118.83 ? 1535 ASP A OD2   1 
ATOM   9     N  N     . VAL A 1 1536 ? 134.105 202.324 161.292 1.00 125.01 ? 1536 VAL A N     1 
ATOM   10    C  CA    . VAL A 1 1536 ? 133.146 201.290 161.652 1.00 126.26 ? 1536 VAL A CA    1 
ATOM   11    C  C     . VAL A 1 1536 ? 131.967 201.256 160.686 1.00 132.33 ? 1536 VAL A C     1 
ATOM   12    O  O     . VAL A 1 1536 ? 131.442 200.185 160.383 1.00 136.87 ? 1536 VAL A O     1 
ATOM   13    C  CB    . VAL A 1 1536 ? 132.667 201.493 163.106 1.00 121.99 ? 1536 VAL A CB    1 
ATOM   14    C  CG1   . VAL A 1 1536 ? 131.846 200.299 163.571 1.00 125.39 ? 1536 VAL A CG1   1 
ATOM   15    C  CG2   . VAL A 1 1536 ? 133.854 201.723 164.029 1.00 119.56 ? 1536 VAL A CG2   1 
ATOM   16    N  N     . TRP A 1 1537 ? 131.546 202.424 160.195 1.00 130.86 ? 1537 TRP A N     1 
ATOM   17    C  CA    . TRP A 1 1537 ? 130.405 202.491 159.286 1.00 129.90 ? 1537 TRP A CA    1 
ATOM   18    C  C     . TRP A 1 1537 ? 130.679 201.736 157.990 1.00 127.63 ? 1537 TRP A C     1 
ATOM   19    O  O     . TRP A 1 1537 ? 129.822 200.983 157.508 1.00 128.05 ? 1537 TRP A O     1 
ATOM   20    C  CB    . TRP A 1 1537 ? 130.071 203.952 158.987 1.00 130.15 ? 1537 TRP A CB    1 
ATOM   21    C  CG    . TRP A 1 1537 ? 128.825 204.147 158.178 1.00 132.68 ? 1537 TRP A CG    1 
ATOM   22    C  CD1   . TRP A 1 1537 ? 128.746 204.362 156.833 1.00 133.37 ? 1537 TRP A CD1   1 
ATOM   23    C  CD2   . TRP A 1 1537 ? 127.481 204.192 158.670 1.00 132.04 ? 1537 TRP A CD2   1 
ATOM   24    N  NE1   . TRP A 1 1537 ? 127.435 204.511 156.454 1.00 130.88 ? 1537 TRP A NE1   1 
ATOM   25    C  CE2   . TRP A 1 1537 ? 126.638 204.414 157.564 1.00 131.34 ? 1537 TRP A CE2   1 
ATOM   26    C  CE3   . TRP A 1 1537 ? 126.907 204.056 159.938 1.00 131.89 ? 1537 TRP A CE3   1 
ATOM   27    C  CZ2   . TRP A 1 1537 ? 125.253 204.503 157.686 1.00 133.11 ? 1537 TRP A CZ2   1 
ATOM   28    C  CZ3   . TRP A 1 1537 ? 125.533 204.144 160.057 1.00 130.58 ? 1537 TRP A CZ3   1 
ATOM   29    C  CH2   . TRP A 1 1537 ? 124.721 204.365 158.939 1.00 133.41 ? 1537 TRP A CH2   1 
ATOM   30    N  N     . ILE A 1 1538 ? 131.870 201.924 157.416 1.00 127.10 ? 1538 ILE A N     1 
ATOM   31    C  CA    . ILE A 1 1538 ? 132.174 201.345 156.109 1.00 126.83 ? 1538 ILE A CA    1 
ATOM   32    C  C     . ILE A 1 1538 ? 132.219 199.824 156.188 1.00 129.46 ? 1538 ILE A C     1 
ATOM   33    O  O     . ILE A 1 1538 ? 131.716 199.129 155.297 1.00 130.69 ? 1538 ILE A O     1 
ATOM   34    C  CB    . ILE A 1 1538 ? 133.487 201.934 155.558 1.00 117.70 ? 1538 ILE A CB    1 
ATOM   35    C  CG1   . ILE A 1 1538 ? 133.884 201.244 154.251 1.00 112.33 ? 1538 ILE A CG1   1 
ATOM   36    C  CG2   . ILE A 1 1538 ? 134.604 201.847 156.592 1.00 114.33 ? 1538 ILE A CG2   1 
ATOM   37    C  CD1   . ILE A 1 1538 ? 134.879 202.031 153.426 1.00 93.81  ? 1538 ILE A CD1   1 
ATOM   38    N  N     . ASP A 1 1539 ? 132.820 199.282 157.251 1.00 130.97 ? 1539 ASP A N     1 
ATOM   39    C  CA    . ASP A 1 1539 ? 132.886 197.831 157.401 1.00 130.66 ? 1539 ASP A CA    1 
ATOM   40    C  C     . ASP A 1 1539 ? 131.495 197.227 157.541 1.00 129.72 ? 1539 ASP A C     1 
ATOM   41    O  O     . ASP A 1 1539 ? 131.190 196.199 156.924 1.00 126.44 ? 1539 ASP A O     1 
ATOM   42    C  CB    . ASP A 1 1539 ? 133.753 197.468 158.606 1.00 127.81 ? 1539 ASP A CB    1 
ATOM   43    C  CG    . ASP A 1 1539 ? 135.213 197.817 158.402 1.00 127.46 ? 1539 ASP A CG    1 
ATOM   44    O  OD1   . ASP A 1 1539 ? 135.680 197.776 157.244 1.00 126.93 ? 1539 ASP A OD1   1 
ATOM   45    O  OD2   . ASP A 1 1539 ? 135.895 198.132 159.399 1.00 125.42 ? 1539 ASP A OD2   1 
ATOM   46    N  N     . VAL A 1 1540 ? 130.636 197.858 158.345 1.00 129.72 ? 1540 VAL A N     1 
ATOM   47    C  CA    . VAL A 1 1540 ? 129.279 197.352 158.533 1.00 130.91 ? 1540 VAL A CA    1 
ATOM   48    C  C     . VAL A 1 1540 ? 128.504 197.405 157.223 1.00 131.59 ? 1540 VAL A C     1 
ATOM   49    O  O     . VAL A 1 1540 ? 127.796 196.456 156.867 1.00 130.87 ? 1540 VAL A O     1 
ATOM   50    C  CB    . VAL A 1 1540 ? 128.565 198.135 159.650 1.00 134.61 ? 1540 VAL A CB    1 
ATOM   51    C  CG1   . VAL A 1 1540 ? 127.096 197.745 159.721 1.00 133.65 ? 1540 VAL A CG1   1 
ATOM   52    C  CG2   . VAL A 1 1540 ? 129.246 197.889 160.986 1.00 134.91 ? 1540 VAL A CG2   1 
ATOM   53    N  N     . GLN A 1 1541 ? 128.625 198.512 156.485 1.00 131.14 ? 1541 GLN A N     1 
ATOM   54    C  CA    . GLN A 1 1541 ? 127.926 198.628 155.208 1.00 124.86 ? 1541 GLN A CA    1 
ATOM   55    C  C     . GLN A 1 1541 ? 128.407 197.573 154.219 1.00 126.70 ? 1541 GLN A C     1 
ATOM   56    O  O     . GLN A 1 1541 ? 127.600 196.928 153.535 1.00 131.77 ? 1541 GLN A O     1 
ATOM   57    C  CB    . GLN A 1 1541 ? 128.117 200.033 154.635 1.00 120.32 ? 1541 GLN A CB    1 
ATOM   58    C  CG    . GLN A 1 1541 ? 127.602 200.199 153.214 1.00 120.88 ? 1541 GLN A CG    1 
ATOM   59    C  CD    . GLN A 1 1541 ? 127.614 201.644 152.756 1.00 123.50 ? 1541 GLN A CD    1 
ATOM   60    O  OE1   . GLN A 1 1541 ? 126.848 202.470 153.251 1.00 126.74 ? 1541 GLN A OE1   1 
ATOM   61    N  NE2   . GLN A 1 1541 ? 128.487 201.955 151.805 1.00 120.97 ? 1541 GLN A NE2   1 
ATOM   62    N  N     . ARG A 1 1542 ? 129.726 197.380 154.133 1.00 125.37 ? 1542 ARG A N     1 
ATOM   63    C  CA    . ARG A 1 1542 ? 130.278 196.397 153.208 1.00 123.97 ? 1542 ARG A CA    1 
ATOM   64    C  C     . ARG A 1 1542 ? 129.822 194.989 153.563 1.00 124.44 ? 1542 ARG A C     1 
ATOM   65    O  O     . ARG A 1 1542 ? 129.464 194.204 152.678 1.00 127.26 ? 1542 ARG A O     1 
ATOM   66    C  CB    . ARG A 1 1542 ? 131.804 196.482 153.205 1.00 124.17 ? 1542 ARG A CB    1 
ATOM   67    C  CG    . ARG A 1 1542 ? 132.487 195.443 152.334 1.00 119.60 ? 1542 ARG A CG    1 
ATOM   68    C  CD    . ARG A 1 1542 ? 133.987 195.676 152.280 1.00 119.50 ? 1542 ARG A CD    1 
ATOM   69    N  NE    . ARG A 1 1542 ? 134.548 195.929 153.602 1.00 123.26 ? 1542 ARG A NE    1 
ATOM   70    C  CZ    . ARG A 1 1542 ? 134.806 194.989 154.500 1.00 128.43 ? 1542 ARG A CZ    1 
ATOM   71    N  NH1   . ARG A 1 1542 ? 134.570 193.711 154.252 1.00 126.32 ? 1542 ARG A NH1   1 
ATOM   72    N  NH2   . ARG A 1 1542 ? 135.316 195.340 155.678 1.00 125.90 ? 1542 ARG A NH2   1 
ATOM   73    N  N     . ARG A 1 1543 ? 129.828 194.650 154.854 1.00 123.55 ? 1543 ARG A N     1 
ATOM   74    C  CA    . ARG A 1 1543 ? 129.355 193.335 155.274 1.00 122.79 ? 1543 ARG A CA    1 
ATOM   75    C  C     . ARG A 1 1543 ? 127.877 193.157 154.949 1.00 124.78 ? 1543 ARG A C     1 
ATOM   76    O  O     . ARG A 1 1543 ? 127.467 192.118 154.412 1.00 123.51 ? 1543 ARG A O     1 
ATOM   77    C  CB    . ARG A 1 1543 ? 129.606 193.145 156.770 1.00 124.18 ? 1543 ARG A CB    1 
ATOM   78    C  CG    . ARG A 1 1543 ? 130.011 191.737 157.162 1.00 121.65 ? 1543 ARG A CG    1 
ATOM   79    C  CD    . ARG A 1 1543 ? 130.904 191.751 158.389 1.00 123.17 ? 1543 ARG A CD    1 
ATOM   80    N  NE    . ARG A 1 1543 ? 132.086 192.578 158.182 1.00 119.17 ? 1543 ARG A NE    1 
ATOM   81    C  CZ    . ARG A 1 1543 ? 133.254 192.122 157.749 1.00 117.89 ? 1543 ARG A CZ    1 
ATOM   82    N  NH1   . ARG A 1 1543 ? 133.435 190.842 157.468 1.00 118.06 ? 1543 ARG A NH1   1 
ATOM   83    N  NH2   . ARG A 1 1543 ? 134.265 192.972 157.593 1.00 118.91 ? 1543 ARG A NH2   1 
ATOM   84    N  N     . TRP A 1 1544 ? 127.066 194.176 155.253 1.00 128.72 ? 1544 TRP A N     1 
ATOM   85    C  CA    . TRP A 1 1544 ? 125.626 194.072 155.058 1.00 129.12 ? 1544 TRP A CA    1 
ATOM   86    C  C     . TRP A 1 1544 ? 125.262 193.934 153.590 1.00 126.81 ? 1544 TRP A C     1 
ATOM   87    O  O     . TRP A 1 1544 ? 124.306 193.225 153.265 1.00 128.52 ? 1544 TRP A O     1 
ATOM   88    C  CB    . TRP A 1 1544 ? 124.917 195.287 155.657 1.00 126.66 ? 1544 TRP A CB    1 
ATOM   89    C  CG    . TRP A 1 1544 ? 123.427 195.243 155.476 1.00 129.42 ? 1544 TRP A CG    1 
ATOM   90    C  CD1   . TRP A 1 1544 ? 122.516 194.668 156.314 1.00 127.30 ? 1544 TRP A CD1   1 
ATOM   91    C  CD2   . TRP A 1 1544 ? 122.678 195.784 154.380 1.00 128.16 ? 1544 TRP A CD2   1 
ATOM   92    N  NE1   . TRP A 1 1544 ? 121.247 194.823 155.812 1.00 129.25 ? 1544 TRP A NE1   1 
ATOM   93    C  CE2   . TRP A 1 1544 ? 121.319 195.504 154.625 1.00 129.56 ? 1544 TRP A CE2   1 
ATOM   94    C  CE3   . TRP A 1 1544 ? 123.024 196.479 153.217 1.00 119.36 ? 1544 TRP A CE3   1 
ATOM   95    C  CZ2   . TRP A 1 1544 ? 120.307 195.896 153.751 1.00 124.12 ? 1544 TRP A CZ2   1 
ATOM   96    C  CZ3   . TRP A 1 1544 ? 122.018 196.867 152.351 1.00 114.66 ? 1544 TRP A CZ3   1 
ATOM   97    C  CH2   . TRP A 1 1544 ? 120.676 196.574 152.623 1.00 116.98 ? 1544 TRP A CH2   1 
ATOM   98    N  N     . VAL A 1 1545 ? 125.996 194.598 152.694 1.00 123.45 ? 1545 VAL A N     1 
ATOM   99    C  CA    . VAL A 1 1545 ? 125.684 194.508 151.267 1.00 120.86 ? 1545 VAL A CA    1 
ATOM   100   C  C     . VAL A 1 1545 ? 125.657 193.049 150.820 1.00 122.64 ? 1545 VAL A C     1 
ATOM   101   O  O     . VAL A 1 1545 ? 124.626 192.535 150.365 1.00 123.67 ? 1545 VAL A O     1 
ATOM   102   C  CB    . VAL A 1 1545 ? 126.684 195.334 150.439 1.00 120.91 ? 1545 VAL A CB    1 
ATOM   103   C  CG1   . VAL A 1 1545 ? 126.634 194.920 148.975 1.00 116.11 ? 1545 VAL A CG1   1 
ATOM   104   C  CG2   . VAL A 1 1545 ? 126.388 196.818 150.578 1.00 119.22 ? 1545 VAL A CG2   1 
ATOM   105   N  N     . TYR A 1 1546 ? 126.783 192.349 150.974 1.00 122.81 ? 1546 TYR A N     1 
ATOM   106   C  CA    . TYR A 1 1546 ? 126.836 190.978 150.482 1.00 121.83 ? 1546 TYR A CA    1 
ATOM   107   C  C     . TYR A 1 1546 ? 126.066 190.010 151.373 1.00 125.79 ? 1546 TYR A C     1 
ATOM   108   O  O     . TYR A 1 1546 ? 125.565 188.996 150.874 1.00 129.79 ? 1546 TYR A O     1 
ATOM   109   C  CB    . TYR A 1 1546 ? 128.291 190.527 150.290 1.00 113.00 ? 1546 TYR A CB    1 
ATOM   110   C  CG    . TYR A 1 1546 ? 129.145 190.404 151.535 1.00 113.52 ? 1546 TYR A CG    1 
ATOM   111   C  CD1   . TYR A 1 1546 ? 128.990 189.342 152.418 1.00 115.67 ? 1546 TYR A CD1   1 
ATOM   112   C  CD2   . TYR A 1 1546 ? 130.143 191.332 151.801 1.00 114.05 ? 1546 TYR A CD2   1 
ATOM   113   C  CE1   . TYR A 1 1546 ? 129.783 189.227 153.544 1.00 114.80 ? 1546 TYR A CE1   1 
ATOM   114   C  CE2   . TYR A 1 1546 ? 130.940 191.224 152.921 1.00 117.47 ? 1546 TYR A CE2   1 
ATOM   115   C  CZ    . TYR A 1 1546 ? 130.756 190.170 153.789 1.00 117.17 ? 1546 TYR A CZ    1 
ATOM   116   O  OH    . TYR A 1 1546 ? 131.551 190.062 154.905 1.00 122.63 ? 1546 TYR A OH    1 
ATOM   117   N  N     . LEU A 1 1547 ? 125.924 190.296 152.672 1.00 123.65 ? 1547 LEU A N     1 
ATOM   118   C  CA    . LEU A 1 1547 ? 125.097 189.423 153.497 1.00 123.68 ? 1547 LEU A CA    1 
ATOM   119   C  C     . LEU A 1 1547 ? 123.637 189.473 153.060 1.00 128.45 ? 1547 LEU A C     1 
ATOM   120   O  O     . LEU A 1 1547 ? 122.979 188.431 152.953 1.00 128.11 ? 1547 LEU A O     1 
ATOM   121   C  CB    . LEU A 1 1547 ? 125.245 189.796 154.971 1.00 123.75 ? 1547 LEU A CB    1 
ATOM   122   C  CG    . LEU A 1 1547 ? 126.488 189.220 155.655 1.00 125.10 ? 1547 LEU A CG    1 
ATOM   123   C  CD1   . LEU A 1 1547 ? 126.454 189.472 157.153 1.00 129.48 ? 1547 LEU A CD1   1 
ATOM   124   C  CD2   . LEU A 1 1547 ? 126.623 187.733 155.364 1.00 121.17 ? 1547 LEU A CD2   1 
ATOM   125   N  N     . GLU A 1 1548 ? 123.117 190.673 152.784 1.00 129.71 ? 1548 GLU A N     1 
ATOM   126   C  CA    . GLU A 1 1548 ? 121.762 190.798 152.263 1.00 129.48 ? 1548 GLU A CA    1 
ATOM   127   C  C     . GLU A 1 1548 ? 121.647 190.171 150.883 1.00 129.94 ? 1548 GLU A C     1 
ATOM   128   O  O     . GLU A 1 1548 ? 120.637 189.531 150.568 1.00 131.45 ? 1548 GLU A O     1 
ATOM   129   C  CB    . GLU A 1 1548 ? 121.348 192.269 152.224 1.00 126.10 ? 1548 GLU A CB    1 
ATOM   130   C  CG    . GLU A 1 1548 ? 119.847 192.490 152.153 1.00 124.38 ? 1548 GLU A CG    1 
ATOM   131   C  CD    . GLU A 1 1548 ? 119.352 192.673 150.731 1.00 129.66 ? 1548 GLU A CD    1 
ATOM   132   O  OE1   . GLU A 1 1548 ? 120.183 192.954 149.842 1.00 129.68 ? 1548 GLU A OE1   1 
ATOM   133   O  OE2   . GLU A 1 1548 ? 118.132 192.536 150.503 1.00 130.29 ? 1548 GLU A OE2   1 
ATOM   134   N  N     . GLY A 1 1549 ? 122.671 190.342 150.043 1.00 126.13 ? 1549 GLY A N     1 
ATOM   135   C  CA    . GLY A 1 1549 ? 122.653 189.694 148.741 1.00 122.01 ? 1549 GLY A CA    1 
ATOM   136   C  C     . GLY A 1 1549 ? 122.517 188.186 148.849 1.00 124.87 ? 1549 GLY A C     1 
ATOM   137   O  O     . GLY A 1 1549 ? 121.718 187.568 148.141 1.00 130.74 ? 1549 GLY A O     1 
ATOM   138   N  N     . ILE A 1 1550 ? 123.287 187.577 149.753 1.00 122.35 ? 1550 ILE A N     1 
ATOM   139   C  CA    . ILE A 1 1550 ? 123.224 186.128 149.935 1.00 123.64 ? 1550 ILE A CA    1 
ATOM   140   C  C     . ILE A 1 1550 ? 121.872 185.715 150.504 1.00 130.11 ? 1550 ILE A C     1 
ATOM   141   O  O     . ILE A 1 1550 ? 121.231 184.779 150.011 1.00 134.48 ? 1550 ILE A O     1 
ATOM   142   C  CB    . ILE A 1 1550 ? 124.381 185.647 150.828 1.00 121.67 ? 1550 ILE A CB    1 
ATOM   143   C  CG1   . ILE A 1 1550 ? 125.700 185.712 150.062 1.00 119.23 ? 1550 ILE A CG1   1 
ATOM   144   C  CG2   . ILE A 1 1550 ? 124.122 184.235 151.331 1.00 123.22 ? 1550 ILE A CG2   1 
ATOM   145   C  CD1   . ILE A 1 1550 ? 126.911 185.801 150.944 1.00 112.68 ? 1550 ILE A CD1   1 
ATOM   146   N  N     . PHE A 1 1551 ? 121.414 186.409 151.548 1.00 129.88 ? 1551 PHE A N     1 
ATOM   147   C  CA    . PHE A 1 1551 ? 120.176 186.017 152.210 1.00 130.57 ? 1551 PHE A CA    1 
ATOM   148   C  C     . PHE A 1 1551 ? 118.931 186.325 151.387 1.00 133.11 ? 1551 PHE A C     1 
ATOM   149   O  O     . PHE A 1 1551 ? 117.854 185.818 151.720 1.00 134.60 ? 1551 PHE A O     1 
ATOM   150   C  CB    . PHE A 1 1551 ? 120.077 186.694 153.579 1.00 129.76 ? 1551 PHE A CB    1 
ATOM   151   C  CG    . PHE A 1 1551 ? 120.840 185.983 154.664 1.00 128.11 ? 1551 PHE A CG    1 
ATOM   152   C  CD1   . PHE A 1 1551 ? 120.350 184.813 155.219 1.00 130.60 ? 1551 PHE A CD1   1 
ATOM   153   C  CD2   . PHE A 1 1551 ? 122.050 186.478 155.121 1.00 125.68 ? 1551 PHE A CD2   1 
ATOM   154   C  CE1   . PHE A 1 1551 ? 121.047 184.156 156.215 1.00 134.99 ? 1551 PHE A CE1   1 
ATOM   155   C  CE2   . PHE A 1 1551 ? 122.752 185.825 156.116 1.00 124.89 ? 1551 PHE A CE2   1 
ATOM   156   C  CZ    . PHE A 1 1551 ? 122.251 184.662 156.663 1.00 131.83 ? 1551 PHE A CZ    1 
ATOM   157   N  N     . THR A 1 1552 ? 119.042 187.132 150.333 1.00 136.66 ? 1552 THR A N     1 
ATOM   158   C  CA    . THR A 1 1552 ? 117.904 187.438 149.476 1.00 135.68 ? 1552 THR A CA    1 
ATOM   159   C  C     . THR A 1 1552 ? 117.914 186.646 148.174 1.00 138.74 ? 1552 THR A C     1 
ATOM   160   O  O     . THR A 1 1552 ? 116.889 186.074 147.792 1.00 143.76 ? 1552 THR A O     1 
ATOM   161   C  CB    . THR A 1 1552 ? 117.867 188.940 149.167 1.00 132.43 ? 1552 THR A CB    1 
ATOM   162   O  OG1   . THR A 1 1552 ? 117.964 189.683 150.389 1.00 136.32 ? 1552 THR A OG1   1 
ATOM   163   C  CG2   . THR A 1 1552 ? 116.573 189.307 148.460 1.00 127.21 ? 1552 THR A CG2   1 
ATOM   164   N  N     . GLY A 1 1553 ? 119.053 186.603 147.479 1.00 136.68 ? 1553 GLY A N     1 
ATOM   165   C  CA    . GLY A 1 1553 ? 119.104 185.900 146.208 1.00 136.61 ? 1553 GLY A CA    1 
ATOM   166   C  C     . GLY A 1 1553 ? 118.899 184.403 146.348 1.00 140.94 ? 1553 GLY A C     1 
ATOM   167   O  O     . GLY A 1 1553 ? 118.175 183.791 145.557 1.00 139.29 ? 1553 GLY A O     1 
ATOM   168   N  N     . SER A 1 1554 ? 119.526 183.795 147.351 1.00 143.85 ? 1554 SER A N     1 
ATOM   169   C  CA    . SER A 1 1554 ? 119.433 182.358 147.565 1.00 145.32 ? 1554 SER A CA    1 
ATOM   170   C  C     . SER A 1 1554 ? 118.126 182.018 148.270 1.00 145.72 ? 1554 SER A C     1 
ATOM   171   O  O     . SER A 1 1554 ? 117.722 182.709 149.211 1.00 143.66 ? 1554 SER A O     1 
ATOM   172   C  CB    . SER A 1 1554 ? 120.624 181.859 148.385 1.00 143.71 ? 1554 SER A CB    1 
ATOM   173   O  OG    . SER A 1 1554 ? 120.633 182.439 149.677 1.00 140.43 ? 1554 SER A OG    1 
ATOM   174   N  N     . ALA A 1 1555 ? 117.472 180.952 147.813 1.00 149.38 ? 1555 ALA A N     1 
ATOM   175   C  CA    . ALA A 1 1555 ? 116.209 180.511 148.391 1.00 152.43 ? 1555 ALA A CA    1 
ATOM   176   C  C     . ALA A 1 1555 ? 116.352 179.297 149.297 1.00 150.60 ? 1555 ALA A C     1 
ATOM   177   O  O     . ALA A 1 1555 ? 115.519 179.106 150.189 1.00 145.94 ? 1555 ALA A O     1 
ATOM   178   C  CB    . ALA A 1 1555 ? 115.200 180.191 147.282 1.00 153.40 ? 1555 ALA A CB    1 
ATOM   179   N  N     . ASP A 1 1556 ? 117.382 178.475 149.094 1.00 150.69 ? 1556 ASP A N     1 
ATOM   180   C  CA    . ASP A 1 1556 ? 117.588 177.304 149.937 1.00 148.84 ? 1556 ASP A CA    1 
ATOM   181   C  C     . ASP A 1 1556 ? 118.184 177.654 151.294 1.00 147.12 ? 1556 ASP A C     1 
ATOM   182   O  O     . ASP A 1 1556 ? 118.202 176.799 152.186 1.00 142.58 ? 1556 ASP A O     1 
ATOM   183   C  CB    . ASP A 1 1556 ? 118.492 176.293 149.228 1.00 145.17 ? 1556 ASP A CB    1 
ATOM   184   C  CG    . ASP A 1 1556 ? 117.747 175.469 148.198 1.00 148.34 ? 1556 ASP A CG    1 
ATOM   185   O  OD1   . ASP A 1 1556 ? 116.758 175.978 147.630 1.00 148.48 ? 1556 ASP A OD1   1 
ATOM   186   O  OD2   . ASP A 1 1556 ? 118.148 174.311 147.958 1.00 156.77 ? 1556 ASP A OD2   1 
ATOM   187   N  N     . ILE A 1 1557 ? 118.672 178.885 151.468 1.00 148.26 ? 1557 ILE A N     1 
ATOM   188   C  CA    . ILE A 1 1557 ? 119.260 179.281 152.741 1.00 147.56 ? 1557 ILE A CA    1 
ATOM   189   C  C     . ILE A 1 1557 ? 118.208 179.393 153.839 1.00 146.54 ? 1557 ILE A C     1 
ATOM   190   O  O     . ILE A 1 1557 ? 118.548 179.329 155.026 1.00 145.91 ? 1557 ILE A O     1 
ATOM   191   C  CB    . ILE A 1 1557 ? 120.035 180.604 152.575 1.00 144.03 ? 1557 ILE A CB    1 
ATOM   192   C  CG1   . ILE A 1 1557 ? 121.029 180.797 153.722 1.00 141.51 ? 1557 ILE A CG1   1 
ATOM   193   C  CG2   . ILE A 1 1557 ? 119.078 181.785 152.493 1.00 141.15 ? 1557 ILE A CG2   1 
ATOM   194   C  CD1   . ILE A 1 1557 ? 121.934 181.995 153.544 1.00 133.24 ? 1557 ILE A CD1   1 
ATOM   195   N  N     . LYS A 1 1558 ? 116.932 179.551 153.475 1.00 142.27 ? 1558 LYS A N     1 
ATOM   196   C  CA    . LYS A 1 1558 ? 115.888 179.669 154.488 1.00 137.81 ? 1558 LYS A CA    1 
ATOM   197   C  C     . LYS A 1 1558 ? 115.579 178.327 155.141 1.00 143.40 ? 1558 LYS A C     1 
ATOM   198   O  O     . LYS A 1 1558 ? 115.119 178.292 156.288 1.00 141.77 ? 1558 LYS A O     1 
ATOM   199   C  CB    . LYS A 1 1558 ? 114.622 180.268 153.873 1.00 131.30 ? 1558 LYS A CB    1 
ATOM   200   C  CG    . LYS A 1 1558 ? 113.850 179.315 152.977 1.00 132.74 ? 1558 LYS A CG    1 
ATOM   201   C  CD    . LYS A 1 1558 ? 112.792 180.040 152.163 1.00 128.58 ? 1558 LYS A CD    1 
ATOM   202   C  CE    . LYS A 1 1558 ? 111.537 180.288 152.984 1.00 124.57 ? 1558 LYS A CE    1 
ATOM   203   N  NZ    . LYS A 1 1558 ? 110.304 180.203 152.153 1.00 107.90 ? 1558 LYS A NZ    1 
ATOM   204   N  N     . HIS A 1 1559 ? 115.820 177.221 154.437 1.00 147.14 ? 1559 HIS A N     1 
ATOM   205   C  CA    . HIS A 1 1559 ? 115.554 175.898 154.990 1.00 142.81 ? 1559 HIS A CA    1 
ATOM   206   C  C     . HIS A 1 1559 ? 116.751 175.335 155.743 1.00 145.64 ? 1559 HIS A C     1 
ATOM   207   O  O     . HIS A 1 1559 ? 116.588 174.759 156.824 1.00 148.68 ? 1559 HIS A O     1 
ATOM   208   C  CB    . HIS A 1 1559 ? 115.147 174.929 153.876 1.00 133.75 ? 1559 HIS A CB    1 
ATOM   209   C  CG    . HIS A 1 1559 ? 114.282 175.544 152.821 1.00 132.85 ? 1559 HIS A CG    1 
ATOM   210   N  ND1   . HIS A 1 1559 ? 114.797 176.136 151.688 1.00 136.72 ? 1559 HIS A ND1   1 
ATOM   211   C  CD2   . HIS A 1 1559 ? 112.936 175.657 152.725 1.00 127.79 ? 1559 HIS A CD2   1 
ATOM   212   C  CE1   . HIS A 1 1559 ? 113.806 176.586 150.939 1.00 133.86 ? 1559 HIS A CE1   1 
ATOM   213   N  NE2   . HIS A 1 1559 ? 112.666 176.310 151.547 1.00 130.07 ? 1559 HIS A NE2   1 
ATOM   214   N  N     . LEU A 1 1560 ? 117.955 175.488 155.188 1.00 145.96 ? 1560 LEU A N     1 
ATOM   215   C  CA    . LEU A 1 1560 ? 119.145 174.939 155.830 1.00 146.59 ? 1560 LEU A CA    1 
ATOM   216   C  C     . LEU A 1 1560 ? 119.474 175.683 157.118 1.00 149.47 ? 1560 LEU A C     1 
ATOM   217   O  O     . LEU A 1 1560 ? 119.739 175.064 158.155 1.00 146.97 ? 1560 LEU A O     1 
ATOM   218   C  CB    . LEU A 1 1560 ? 120.328 174.988 154.863 1.00 142.00 ? 1560 LEU A CB    1 
ATOM   219   C  CG    . LEU A 1 1560 ? 121.443 173.963 155.079 1.00 132.39 ? 1560 LEU A CG    1 
ATOM   220   C  CD1   . LEU A 1 1560 ? 120.912 172.545 154.924 1.00 122.53 ? 1560 LEU A CD1   1 
ATOM   221   C  CD2   . LEU A 1 1560 ? 122.597 174.216 154.120 1.00 123.67 ? 1560 LEU A CD2   1 
ATOM   222   N  N     . LEU A 1 1561 ? 119.461 177.014 157.073 1.00 151.45 ? 1561 LEU A N     1 
ATOM   223   C  CA    . LEU A 1 1561 ? 119.904 177.853 158.187 1.00 150.69 ? 1561 LEU A CA    1 
ATOM   224   C  C     . LEU A 1 1561 ? 118.857 178.926 158.458 1.00 147.59 ? 1561 LEU A C     1 
ATOM   225   O  O     . LEU A 1 1561 ? 119.037 180.093 158.088 1.00 143.87 ? 1561 LEU A O     1 
ATOM   226   C  CB    . LEU A 1 1561 ? 121.266 178.477 157.882 1.00 150.16 ? 1561 LEU A CB    1 
ATOM   227   C  CG    . LEU A 1 1561 ? 122.430 177.500 157.700 1.00 150.22 ? 1561 LEU A CG    1 
ATOM   228   C  CD1   . LEU A 1 1561 ? 123.627 178.197 157.070 1.00 144.87 ? 1561 LEU A CD1   1 
ATOM   229   C  CD2   . LEU A 1 1561 ? 122.814 176.846 159.020 1.00 144.20 ? 1561 LEU A CD2   1 
ATOM   230   N  N     . PRO A 1 1562 ? 117.747 178.567 159.108 1.00 150.43 ? 1562 PRO A N     1 
ATOM   231   C  CA    . PRO A 1 1562 ? 116.662 179.539 159.306 1.00 148.73 ? 1562 PRO A CA    1 
ATOM   232   C  C     . PRO A 1 1562 ? 116.866 180.481 160.485 1.00 148.56 ? 1562 PRO A C     1 
ATOM   233   O  O     . PRO A 1 1562 ? 116.415 181.631 160.441 1.00 143.70 ? 1562 PRO A O     1 
ATOM   234   C  CB    . PRO A 1 1562 ? 115.428 178.647 159.527 1.00 147.54 ? 1562 PRO A CB    1 
ATOM   235   C  CG    . PRO A 1 1562 ? 115.904 177.213 159.334 1.00 146.87 ? 1562 PRO A CG    1 
ATOM   236   C  CD    . PRO A 1 1562 ? 117.370 177.230 159.587 1.00 148.06 ? 1562 PRO A CD    1 
ATOM   237   N  N     . VAL A 1 1563 ? 117.530 180.014 161.545 1.00 150.62 ? 1563 VAL A N     1 
ATOM   238   C  CA    . VAL A 1 1563 ? 117.578 180.788 162.784 1.00 145.34 ? 1563 VAL A CA    1 
ATOM   239   C  C     . VAL A 1 1563 ? 118.417 182.053 162.608 1.00 144.68 ? 1563 VAL A C     1 
ATOM   240   O  O     . VAL A 1 1563 ? 117.973 183.162 162.939 1.00 143.51 ? 1563 VAL A O     1 
ATOM   241   C  CB    . VAL A 1 1563 ? 118.071 179.911 163.952 1.00 139.64 ? 1563 VAL A CB    1 
ATOM   242   C  CG1   . VAL A 1 1563 ? 117.069 178.803 164.223 1.00 132.74 ? 1563 VAL A CG1   1 
ATOM   243   C  CG2   . VAL A 1 1563 ? 119.426 179.296 163.650 1.00 139.23 ? 1563 VAL A CG2   1 
ATOM   244   N  N     . GLU A 1 1564 ? 119.624 181.927 162.052 1.00 147.46 ? 1564 GLU A N     1 
ATOM   245   C  CA    . GLU A 1 1564 ? 120.381 183.146 161.804 1.00 147.33 ? 1564 GLU A CA    1 
ATOM   246   C  C     . GLU A 1 1564 ? 119.877 183.890 160.578 1.00 145.82 ? 1564 GLU A C     1 
ATOM   247   O  O     . GLU A 1 1564 ? 120.190 185.070 160.425 1.00 140.67 ? 1564 GLU A O     1 
ATOM   248   C  CB    . GLU A 1 1564 ? 121.885 182.874 161.678 1.00 144.25 ? 1564 GLU A CB    1 
ATOM   249   C  CG    . GLU A 1 1564 ? 122.349 182.106 160.458 1.00 144.30 ? 1564 GLU A CG    1 
ATOM   250   C  CD    . GLU A 1 1564 ? 122.348 180.611 160.677 1.00 148.95 ? 1564 GLU A CD    1 
ATOM   251   O  OE1   . GLU A 1 1564 ? 121.693 180.145 161.630 1.00 145.38 ? 1564 GLU A OE1   1 
ATOM   252   O  OE2   . GLU A 1 1564 ? 123.044 179.907 159.920 1.00 155.14 ? 1564 GLU A OE2   1 
ATOM   253   N  N     . THR A 1 1565 ? 119.068 183.251 159.729 1.00 146.75 ? 1565 THR A N     1 
ATOM   254   C  CA    . THR A 1 1565 ? 118.354 184.008 158.705 1.00 143.38 ? 1565 THR A CA    1 
ATOM   255   C  C     . THR A 1 1565 ? 117.364 184.980 159.337 1.00 143.50 ? 1565 THR A C     1 
ATOM   256   O  O     . THR A 1 1565 ? 117.277 186.141 158.924 1.00 141.40 ? 1565 THR A O     1 
ATOM   257   C  CB    . THR A 1 1565 ? 117.637 183.062 157.742 1.00 142.61 ? 1565 THR A CB    1 
ATOM   258   O  OG1   . THR A 1 1565 ? 118.547 182.049 157.298 1.00 147.86 ? 1565 THR A OG1   1 
ATOM   259   C  CG2   . THR A 1 1565 ? 117.112 183.827 156.537 1.00 133.59 ? 1565 THR A CG2   1 
ATOM   260   N  N     . GLN A 1 1566 ? 116.619 184.530 160.350 1.00 143.87 ? 1566 GLN A N     1 
ATOM   261   C  CA    . GLN A 1 1566 ? 115.727 185.436 161.072 1.00 141.63 ? 1566 GLN A CA    1 
ATOM   262   C  C     . GLN A 1 1566 ? 116.516 186.482 161.854 1.00 141.59 ? 1566 GLN A C     1 
ATOM   263   O  O     . GLN A 1 1566 ? 116.120 187.657 161.915 1.00 139.11 ? 1566 GLN A O     1 
ATOM   264   C  CB    . GLN A 1 1566 ? 114.815 184.641 162.005 1.00 140.51 ? 1566 GLN A CB    1 
ATOM   265   C  CG    . GLN A 1 1566 ? 113.855 183.707 161.286 1.00 141.01 ? 1566 GLN A CG    1 
ATOM   266   C  CD    . GLN A 1 1566 ? 112.901 184.446 160.369 1.00 142.81 ? 1566 GLN A CD    1 
ATOM   267   O  OE1   . GLN A 1 1566 ? 112.978 184.326 159.146 1.00 142.95 ? 1566 GLN A OE1   1 
ATOM   268   N  NE2   . GLN A 1 1566 ? 111.994 185.218 160.957 1.00 139.39 ? 1566 GLN A NE2   1 
ATOM   269   N  N     . ARG A 1 1567 ? 117.628 186.067 162.470 1.00 143.62 ? 1567 ARG A N     1 
ATOM   270   C  CA    . ARG A 1 1567 ? 118.510 187.022 163.136 1.00 138.55 ? 1567 ARG A CA    1 
ATOM   271   C  C     . ARG A 1 1567 ? 118.950 188.120 162.175 1.00 138.79 ? 1567 ARG A C     1 
ATOM   272   O  O     . ARG A 1 1567 ? 118.880 189.313 162.494 1.00 140.34 ? 1567 ARG A O     1 
ATOM   273   C  CB    . ARG A 1 1567 ? 119.731 186.299 163.709 1.00 137.43 ? 1567 ARG A CB    1 
ATOM   274   C  CG    . ARG A 1 1567 ? 119.444 185.382 164.885 1.00 135.45 ? 1567 ARG A CG    1 
ATOM   275   C  CD    . ARG A 1 1567 ? 120.721 185.102 165.666 1.00 138.05 ? 1567 ARG A CD    1 
ATOM   276   N  NE    . ARG A 1 1567 ? 120.583 183.975 166.581 1.00 143.20 ? 1567 ARG A NE    1 
ATOM   277   C  CZ    . ARG A 1 1567 ? 119.979 184.034 167.760 1.00 142.17 ? 1567 ARG A CZ    1 
ATOM   278   N  NH1   . ARG A 1 1567 ? 119.442 185.157 168.206 1.00 139.56 ? 1567 ARG A NH1   1 
ATOM   279   N  NH2   . ARG A 1 1567 ? 119.917 182.939 168.512 1.00 136.78 ? 1567 ARG A NH2   1 
ATOM   280   N  N     . PHE A 1 1568 ? 119.398 187.728 160.980 1.00 138.39 ? 1568 PHE A N     1 
ATOM   281   C  CA    . PHE A 1 1568 ? 119.842 188.697 159.989 1.00 136.33 ? 1568 PHE A CA    1 
ATOM   282   C  C     . PHE A 1 1568 ? 118.687 189.527 159.455 1.00 138.01 ? 1568 PHE A C     1 
ATOM   283   O  O     . PHE A 1 1568 ? 118.890 190.682 159.083 1.00 139.11 ? 1568 PHE A O     1 
ATOM   284   C  CB    . PHE A 1 1568 ? 120.553 187.995 158.835 1.00 134.64 ? 1568 PHE A CB    1 
ATOM   285   C  CG    . PHE A 1 1568 ? 121.004 188.932 157.755 1.00 134.35 ? 1568 PHE A CG    1 
ATOM   286   C  CD1   . PHE A 1 1568 ? 122.102 189.750 157.949 1.00 134.13 ? 1568 PHE A CD1   1 
ATOM   287   C  CD2   . PHE A 1 1568 ? 120.318 189.010 156.554 1.00 127.58 ? 1568 PHE A CD2   1 
ATOM   288   C  CE1   . PHE A 1 1568 ? 122.517 190.621 156.964 1.00 129.92 ? 1568 PHE A CE1   1 
ATOM   289   C  CE2   . PHE A 1 1568 ? 120.729 189.877 155.564 1.00 126.18 ? 1568 PHE A CE2   1 
ATOM   290   C  CZ    . PHE A 1 1568 ? 121.830 190.685 155.770 1.00 129.30 ? 1568 PHE A CZ    1 
ATOM   291   N  N     . GLN A 1 1569 ? 117.481 188.964 159.392 1.00 138.92 ? 1569 GLN A N     1 
ATOM   292   C  CA    . GLN A 1 1569 ? 116.328 189.765 158.995 1.00 139.89 ? 1569 GLN A CA    1 
ATOM   293   C  C     . GLN A 1 1569 ? 116.076 190.884 159.995 1.00 140.69 ? 1569 GLN A C     1 
ATOM   294   O  O     . GLN A 1 1569 ? 115.849 192.037 159.608 1.00 138.66 ? 1569 GLN A O     1 
ATOM   295   C  CB    . GLN A 1 1569 ? 115.092 188.878 158.853 1.00 139.55 ? 1569 GLN A CB    1 
ATOM   296   C  CG    . GLN A 1 1569 ? 113.861 189.614 158.348 1.00 139.33 ? 1569 GLN A CG    1 
ATOM   297   C  CD    . GLN A 1 1569 ? 114.095 190.284 157.008 1.00 133.37 ? 1569 GLN A CD    1 
ATOM   298   O  OE1   . GLN A 1 1569 ? 114.245 191.503 156.928 1.00 128.82 ? 1569 GLN A OE1   1 
ATOM   299   N  NE2   . GLN A 1 1569 ? 114.128 189.488 155.945 1.00 123.67 ? 1569 GLN A NE2   1 
ATOM   300   N  N     . SER A 1 1570 ? 116.137 190.568 161.291 1.00 143.32 ? 1570 SER A N     1 
ATOM   301   C  CA    . SER A 1 1570 ? 115.978 191.608 162.308 1.00 139.86 ? 1570 SER A CA    1 
ATOM   302   C  C     . SER A 1 1570 ? 117.112 192.630 162.241 1.00 142.13 ? 1570 SER A C     1 
ATOM   303   O  O     . SER A 1 1570 ? 116.879 193.844 162.343 1.00 144.94 ? 1570 SER A O     1 
ATOM   304   C  CB    . SER A 1 1570 ? 115.905 190.976 163.697 1.00 133.68 ? 1570 SER A CB    1 
ATOM   305   O  OG    . SER A 1 1570 ? 115.027 189.864 163.706 1.00 129.70 ? 1570 SER A OG    1 
ATOM   306   N  N     . ILE A 1 1571 ? 118.347 192.155 162.065 1.00 142.22 ? 1571 ILE A N     1 
ATOM   307   C  CA    . ILE A 1 1571 ? 119.492 193.058 162.005 1.00 144.32 ? 1571 ILE A CA    1 
ATOM   308   C  C     . ILE A 1 1571 ? 119.407 193.958 160.777 1.00 144.67 ? 1571 ILE A C     1 
ATOM   309   O  O     . ILE A 1 1571 ? 119.740 195.146 160.837 1.00 145.49 ? 1571 ILE A O     1 
ATOM   310   C  CB    . ILE A 1 1571 ? 120.803 192.252 162.043 1.00 140.11 ? 1571 ILE A CB    1 
ATOM   311   C  CG1   . ILE A 1 1571 ? 120.986 191.625 163.426 1.00 142.41 ? 1571 ILE A CG1   1 
ATOM   312   C  CG2   . ILE A 1 1571 ? 121.994 193.130 161.694 1.00 133.61 ? 1571 ILE A CG2   1 
ATOM   313   C  CD1   . ILE A 1 1571 ? 121.766 190.338 163.420 1.00 141.05 ? 1571 ILE A CD1   1 
ATOM   314   N  N     . SER A 1 1572 ? 118.947 193.416 159.648 1.00 141.02 ? 1572 SER A N     1 
ATOM   315   C  CA    . SER A 1 1572 ? 118.770 194.219 158.446 1.00 139.71 ? 1572 SER A CA    1 
ATOM   316   C  C     . SER A 1 1572 ? 117.614 195.196 158.593 1.00 145.17 ? 1572 SER A C     1 
ATOM   317   O  O     . SER A 1 1572 ? 117.654 196.283 158.013 1.00 147.59 ? 1572 SER A O     1 
ATOM   318   C  CB    . SER A 1 1572 ? 118.550 193.313 157.235 1.00 132.56 ? 1572 SER A CB    1 
ATOM   319   O  OG    . SER A 1 1572 ? 118.535 194.064 156.034 1.00 130.98 ? 1572 SER A OG    1 
ATOM   320   N  N     . THR A 1 1573 ? 116.580 194.834 159.354 1.00 146.08 ? 1573 THR A N     1 
ATOM   321   C  CA    . THR A 1 1573 ? 115.533 195.801 159.667 1.00 145.70 ? 1573 THR A CA    1 
ATOM   322   C  C     . THR A 1 1573 ? 116.100 196.973 160.458 1.00 148.77 ? 1573 THR A C     1 
ATOM   323   O  O     . THR A 1 1573 ? 115.790 198.138 160.173 1.00 148.83 ? 1573 THR A O     1 
ATOM   324   C  CB    . THR A 1 1573 ? 114.403 195.123 160.444 1.00 144.34 ? 1573 THR A CB    1 
ATOM   325   O  OG1   . THR A 1 1573 ? 113.844 194.067 159.653 1.00 149.11 ? 1573 THR A OG1   1 
ATOM   326   C  CG2   . THR A 1 1573 ? 113.310 196.126 160.783 1.00 136.23 ? 1573 THR A CG2   1 
ATOM   327   N  N     . GLU A 1 1574 ? 116.946 196.682 161.450 1.00 147.98 ? 1574 GLU A N     1 
ATOM   328   C  CA    . GLU A 1 1574 ? 117.610 197.755 162.190 1.00 146.47 ? 1574 GLU A CA    1 
ATOM   329   C  C     . GLU A 1 1574 ? 118.504 198.587 161.275 1.00 148.72 ? 1574 GLU A C     1 
ATOM   330   O  O     . GLU A 1 1574 ? 118.545 199.820 161.380 1.00 150.19 ? 1574 GLU A O     1 
ATOM   331   C  CB    . GLU A 1 1574 ? 118.423 197.173 163.347 1.00 140.96 ? 1574 GLU A CB    1 
ATOM   332   C  CG    . GLU A 1 1574 ? 117.615 196.332 164.320 1.00 139.89 ? 1574 GLU A CG    1 
ATOM   333   C  CD    . GLU A 1 1574 ? 118.432 195.880 165.515 1.00 140.18 ? 1574 GLU A CD    1 
ATOM   334   O  OE1   . GLU A 1 1574 ? 119.677 195.933 165.440 1.00 139.48 ? 1574 GLU A OE1   1 
ATOM   335   O  OE2   . GLU A 1 1574 ? 117.829 195.473 166.531 1.00 139.26 ? 1574 GLU A OE2   1 
ATOM   336   N  N     . PHE A 1 1575 ? 119.229 197.926 160.371 1.00 146.40 ? 1575 PHE A N     1 
ATOM   337   C  CA    . PHE A 1 1575 ? 120.107 198.633 159.444 1.00 144.40 ? 1575 PHE A CA    1 
ATOM   338   C  C     . PHE A 1 1575 ? 119.312 199.543 158.515 1.00 147.12 ? 1575 PHE A C     1 
ATOM   339   O  O     . PHE A 1 1575 ? 119.747 200.657 158.205 1.00 148.68 ? 1575 PHE A O     1 
ATOM   340   C  CB    . PHE A 1 1575 ? 120.933 197.627 158.641 1.00 136.50 ? 1575 PHE A CB    1 
ATOM   341   C  CG    . PHE A 1 1575 ? 122.039 198.251 157.839 1.00 133.72 ? 1575 PHE A CG    1 
ATOM   342   C  CD1   . PHE A 1 1575 ? 123.248 198.573 158.435 1.00 133.95 ? 1575 PHE A CD1   1 
ATOM   343   C  CD2   . PHE A 1 1575 ? 121.875 198.507 156.488 1.00 129.28 ? 1575 PHE A CD2   1 
ATOM   344   C  CE1   . PHE A 1 1575 ? 124.269 199.145 157.699 1.00 131.99 ? 1575 PHE A CE1   1 
ATOM   345   C  CE2   . PHE A 1 1575 ? 122.892 199.078 155.747 1.00 124.96 ? 1575 PHE A CE2   1 
ATOM   346   C  CZ    . PHE A 1 1575 ? 124.090 199.397 156.354 1.00 126.83 ? 1575 PHE A CZ    1 
ATOM   347   N  N     . LEU A 1 1576 ? 118.149 199.082 158.051 1.00 149.57 ? 1576 LEU A N     1 
ATOM   348   C  CA    . LEU A 1 1576 ? 117.319 199.905 157.178 1.00 148.67 ? 1576 LEU A CA    1 
ATOM   349   C  C     . LEU A 1 1576 ? 116.688 201.060 157.944 1.00 150.32 ? 1576 LEU A C     1 
ATOM   350   O  O     . LEU A 1 1576 ? 116.520 202.155 157.396 1.00 149.76 ? 1576 LEU A O     1 
ATOM   351   C  CB    . LEU A 1 1576 ? 116.251 199.047 156.500 1.00 147.21 ? 1576 LEU A CB    1 
ATOM   352   C  CG    . LEU A 1 1576 ? 116.785 198.043 155.475 1.00 141.25 ? 1576 LEU A CG    1 
ATOM   353   C  CD1   . LEU A 1 1576 ? 115.811 196.894 155.279 1.00 140.98 ? 1576 LEU A CD1   1 
ATOM   354   C  CD2   . LEU A 1 1576 ? 117.076 198.736 154.153 1.00 133.31 ? 1576 LEU A CD2   1 
ATOM   355   N  N     . ALA A 1 1577 ? 116.347 200.844 159.216 1.00 151.33 ? 1577 ALA A N     1 
ATOM   356   C  CA    . ALA A 1 1577 ? 115.913 201.961 160.050 1.00 150.93 ? 1577 ALA A CA    1 
ATOM   357   C  C     . ALA A 1 1577 ? 117.014 203.008 160.171 1.00 152.80 ? 1577 ALA A C     1 
ATOM   358   O  O     . ALA A 1 1577 ? 116.757 204.214 160.051 1.00 151.65 ? 1577 ALA A O     1 
ATOM   359   C  CB    . ALA A 1 1577 ? 115.499 201.456 161.432 1.00 145.13 ? 1577 ALA A CB    1 
ATOM   360   N  N     . LEU A 1 1578 ? 118.252 202.561 160.393 1.00 153.95 ? 1578 LEU A N     1 
ATOM   361   C  CA    . LEU A 1 1578 ? 119.372 203.493 160.494 1.00 153.91 ? 1578 LEU A CA    1 
ATOM   362   C  C     . LEU A 1 1578 ? 119.610 204.225 159.177 1.00 153.55 ? 1578 LEU A C     1 
ATOM   363   O  O     . LEU A 1 1578 ? 119.882 205.432 159.171 1.00 154.02 ? 1578 LEU A O     1 
ATOM   364   C  CB    . LEU A 1 1578 ? 120.636 202.751 160.931 1.00 150.17 ? 1578 LEU A CB    1 
ATOM   365   C  CG    . LEU A 1 1578 ? 121.840 203.618 161.308 1.00 146.37 ? 1578 LEU A CG    1 
ATOM   366   C  CD1   . LEU A 1 1578 ? 121.416 204.805 162.158 1.00 143.45 ? 1578 LEU A CD1   1 
ATOM   367   C  CD2   . LEU A 1 1578 ? 122.888 202.788 162.034 1.00 138.59 ? 1578 LEU A CD2   1 
ATOM   368   N  N     . MET A 1 1579 ? 119.524 203.512 158.051 1.00 150.68 ? 1579 MET A N     1 
ATOM   369   C  CA    . MET A 1 1579 ? 119.707 204.158 156.755 1.00 149.50 ? 1579 MET A CA    1 
ATOM   370   C  C     . MET A 1 1579 ? 118.602 205.166 156.473 1.00 155.63 ? 1579 MET A C     1 
ATOM   371   O  O     . MET A 1 1579 ? 118.877 206.230 155.913 1.00 157.44 ? 1579 MET A O     1 
ATOM   372   C  CB    . MET A 1 1579 ? 119.817 203.107 155.636 1.00 145.48 ? 1579 MET A CB    1 
ATOM   373   C  CG    . MET A 1 1579 ? 118.516 202.510 155.081 1.00 149.59 ? 1579 MET A CG    1 
ATOM   374   S  SD    . MET A 1 1579 ? 117.544 203.547 153.959 1.00 156.69 ? 1579 MET A SD    1 
ATOM   375   C  CE    . MET A 1 1579 ? 118.472 203.380 152.434 1.00 138.25 ? 1579 MET A CE    1 
ATOM   376   N  N     . LYS A 1 1580 ? 117.357 204.860 156.852 1.00 156.28 ? 1580 LYS A N     1 
ATOM   377   C  CA    . LYS A 1 1580 ? 116.282 205.835 156.707 1.00 155.76 ? 1580 LYS A CA    1 
ATOM   378   C  C     . LYS A 1 1580 ? 116.539 207.064 157.568 1.00 154.63 ? 1580 LYS A C     1 
ATOM   379   O  O     . LYS A 1 1580 ? 116.332 208.199 157.121 1.00 153.48 ? 1580 LYS A O     1 
ATOM   380   C  CB    . LYS A 1 1580 ? 114.941 205.196 157.067 1.00 152.90 ? 1580 LYS A CB    1 
ATOM   381   C  CG    . LYS A 1 1580 ? 113.731 206.054 156.728 1.00 149.57 ? 1580 LYS A CG    1 
ATOM   382   C  CD    . LYS A 1 1580 ? 113.578 206.210 155.223 1.00 143.25 ? 1580 LYS A CD    1 
ATOM   383   C  CE    . LYS A 1 1580 ? 113.079 204.924 154.584 1.00 130.90 ? 1580 LYS A CE    1 
ATOM   384   N  NZ    . LYS A 1 1580 ? 112.806 205.091 153.132 1.00 112.55 ? 1580 LYS A NZ    1 
ATOM   385   N  N     . LYS A 1 1581 ? 117.003 206.858 158.805 1.00 155.67 ? 1581 LYS A N     1 
ATOM   386   C  CA    . LYS A 1 1581 ? 117.317 207.988 159.674 1.00 156.04 ? 1581 LYS A CA    1 
ATOM   387   C  C     . LYS A 1 1581 ? 118.416 208.858 159.076 1.00 157.97 ? 1581 LYS A C     1 
ATOM   388   O  O     . LYS A 1 1581 ? 118.341 210.092 159.130 1.00 157.15 ? 1581 LYS A O     1 
ATOM   389   C  CB    . LYS A 1 1581 ? 117.725 207.492 161.062 1.00 150.22 ? 1581 LYS A CB    1 
ATOM   390   C  CG    . LYS A 1 1581 ? 116.590 206.882 161.866 1.00 146.39 ? 1581 LYS A CG    1 
ATOM   391   C  CD    . LYS A 1 1581 ? 116.934 206.821 163.347 1.00 138.11 ? 1581 LYS A CD    1 
ATOM   392   C  CE    . LYS A 1 1581 ? 117.934 205.714 163.639 1.00 136.61 ? 1581 LYS A CE    1 
ATOM   393   N  NZ    . LYS A 1 1581 ? 117.757 205.153 165.007 1.00 119.33 ? 1581 LYS A NZ    1 
ATOM   394   N  N     . VAL A 1 1582 ? 119.449 208.232 158.510 1.00 157.68 ? 1582 VAL A N     1 
ATOM   395   C  CA    . VAL A 1 1582 ? 120.516 208.989 157.859 1.00 155.82 ? 1582 VAL A CA    1 
ATOM   396   C  C     . VAL A 1 1582 ? 119.981 209.727 156.636 1.00 159.02 ? 1582 VAL A C     1 
ATOM   397   O  O     . VAL A 1 1582 ? 120.367 210.871 156.366 1.00 159.35 ? 1582 VAL A O     1 
ATOM   398   C  CB    . VAL A 1 1582 ? 121.686 208.056 157.496 1.00 151.73 ? 1582 VAL A CB    1 
ATOM   399   C  CG1   . VAL A 1 1582 ? 122.737 208.799 156.684 1.00 143.78 ? 1582 VAL A CG1   1 
ATOM   400   C  CG2   . VAL A 1 1582 ? 122.307 207.477 158.757 1.00 150.54 ? 1582 VAL A CG2   1 
ATOM   401   N  N     . SER A 1 1583 ? 119.085 209.089 155.880 1.00 160.11 ? 1583 SER A N     1 
ATOM   402   C  CA    . SER A 1 1583 ? 118.521 209.722 154.693 1.00 158.83 ? 1583 SER A CA    1 
ATOM   403   C  C     . SER A 1 1583 ? 117.652 210.921 155.049 1.00 158.70 ? 1583 SER A C     1 
ATOM   404   O  O     . SER A 1 1583 ? 117.544 211.861 154.252 1.00 155.06 ? 1583 SER A O     1 
ATOM   405   C  CB    . SER A 1 1583 ? 117.712 208.704 153.890 1.00 157.15 ? 1583 SER A CB    1 
ATOM   406   O  OG    . SER A 1 1583 ? 117.074 209.320 152.785 1.00 164.14 ? 1583 SER A OG    1 
ATOM   407   N  N     . LYS A 1 1584 ? 117.016 210.903 156.224 1.00 161.39 ? 1584 LYS A N     1 
ATOM   408   C  CA    . LYS A 1 1584 ? 116.235 212.061 156.650 1.00 161.71 ? 1584 LYS A CA    1 
ATOM   409   C  C     . LYS A 1 1584 ? 117.113 213.299 156.790 1.00 160.33 ? 1584 LYS A C     1 
ATOM   410   O  O     . LYS A 1 1584 ? 116.725 214.395 156.369 1.00 160.56 ? 1584 LYS A O     1 
ATOM   411   C  CB    . LYS A 1 1584 ? 115.520 211.766 157.969 1.00 159.00 ? 1584 LYS A CB    1 
ATOM   412   C  CG    . LYS A 1 1584 ? 114.552 210.597 157.917 1.00 154.36 ? 1584 LYS A CG    1 
ATOM   413   C  CD    . LYS A 1 1584 ? 113.306 210.937 157.118 1.00 144.50 ? 1584 LYS A CD    1 
ATOM   414   C  CE    . LYS A 1 1584 ? 112.363 209.748 157.047 1.00 136.66 ? 1584 LYS A CE    1 
ATOM   415   N  NZ    . LYS A 1 1584 ? 112.169 209.120 158.384 1.00 128.58 ? 1584 LYS A NZ    1 
ATOM   416   N  N     . SER A 1 1585 ? 118.297 213.144 157.379 1.00 160.70 ? 1585 SER A N     1 
ATOM   417   C  CA    . SER A 1 1585 ? 119.242 214.244 157.568 1.00 159.96 ? 1585 SER A CA    1 
ATOM   418   C  C     . SER A 1 1585 ? 120.608 213.798 157.067 1.00 163.08 ? 1585 SER A C     1 
ATOM   419   O  O     . SER A 1 1585 ? 121.402 213.219 157.822 1.00 162.84 ? 1585 SER A O     1 
ATOM   420   C  CB    . SER A 1 1585 ? 119.304 214.676 159.031 1.00 157.47 ? 1585 SER A CB    1 
ATOM   421   O  OG    . SER A 1 1585 ? 119.623 213.582 159.873 1.00 160.43 ? 1585 SER A OG    1 
ATOM   422   N  N     . PRO A 1 1586 ? 120.921 214.048 155.791 1.00 164.08 ? 1586 PRO A N     1 
ATOM   423   C  CA    . PRO A 1 1586 ? 122.219 213.621 155.249 1.00 161.73 ? 1586 PRO A CA    1 
ATOM   424   C  C     . PRO A 1 1586 ? 123.406 214.408 155.780 1.00 157.69 ? 1586 PRO A C     1 
ATOM   425   O  O     . PRO A 1 1586 ? 124.536 214.152 155.348 1.00 154.24 ? 1586 PRO A O     1 
ATOM   426   C  CB    . PRO A 1 1586 ? 122.050 213.834 153.738 1.00 158.84 ? 1586 PRO A CB    1 
ATOM   427   C  CG    . PRO A 1 1586 ? 121.046 214.928 153.629 1.00 156.68 ? 1586 PRO A CG    1 
ATOM   428   C  CD    . PRO A 1 1586 ? 120.100 214.749 154.788 1.00 161.09 ? 1586 PRO A CD    1 
ATOM   429   N  N     . LEU A 1 1587 ? 123.195 215.354 156.692 1.00 156.15 ? 1587 LEU A N     1 
ATOM   430   C  CA    . LEU A 1 1587 ? 124.306 216.089 157.280 1.00 153.60 ? 1587 LEU A CA    1 
ATOM   431   C  C     . LEU A 1 1587 ? 125.139 215.172 158.167 1.00 155.74 ? 1587 LEU A C     1 
ATOM   432   O  O     . LEU A 1 1587 ? 124.605 214.333 158.898 1.00 159.13 ? 1587 LEU A O     1 
ATOM   433   C  CB    . LEU A 1 1587 ? 123.787 217.279 158.087 1.00 151.76 ? 1587 LEU A CB    1 
ATOM   434   C  CG    . LEU A 1 1587 ? 124.684 218.518 158.126 1.00 143.02 ? 1587 LEU A CG    1 
ATOM   435   C  CD1   . LEU A 1 1587 ? 125.091 218.930 156.720 1.00 134.30 ? 1587 LEU A CD1   1 
ATOM   436   C  CD2   . LEU A 1 1587 ? 123.982 219.663 158.840 1.00 133.63 ? 1587 LEU A CD2   1 
ATOM   437   N  N     . VAL A 1 1588 ? 126.461 215.333 158.090 1.00 152.68 ? 1588 VAL A N     1 
ATOM   438   C  CA    . VAL A 1 1588 ? 127.368 214.467 158.840 1.00 150.19 ? 1588 VAL A CA    1 
ATOM   439   C  C     . VAL A 1 1588 ? 127.193 214.674 160.340 1.00 151.39 ? 1588 VAL A C     1 
ATOM   440   O  O     . VAL A 1 1588 ? 127.124 213.711 161.113 1.00 147.39 ? 1588 VAL A O     1 
ATOM   441   C  CB    . VAL A 1 1588 ? 128.824 214.712 158.402 1.00 143.08 ? 1588 VAL A CB    1 
ATOM   442   C  CG1   . VAL A 1 1588 ? 129.781 213.873 159.238 1.00 140.62 ? 1588 VAL A CG1   1 
ATOM   443   C  CG2   . VAL A 1 1588 ? 128.994 214.414 156.919 1.00 134.21 ? 1588 VAL A CG2   1 
ATOM   444   N  N     . MET A 1 1589 ? 127.117 215.935 160.775 1.00 153.29 ? 1589 MET A N     1 
ATOM   445   C  CA    . MET A 1 1589 ? 127.037 216.214 162.206 1.00 156.52 ? 1589 MET A CA    1 
ATOM   446   C  C     . MET A 1 1589 ? 125.697 215.788 162.794 1.00 155.07 ? 1589 MET A C     1 
ATOM   447   O  O     . MET A 1 1589 ? 125.637 215.389 163.963 1.00 155.96 ? 1589 MET A O     1 
ATOM   448   C  CB    . MET A 1 1589 ? 127.291 217.699 162.468 1.00 151.82 ? 1589 MET A CB    1 
ATOM   449   C  CG    . MET A 1 1589 ? 128.163 217.971 163.684 1.00 148.98 ? 1589 MET A CG    1 
ATOM   450   S  SD    . MET A 1 1589 ? 129.746 217.112 163.613 1.00 154.58 ? 1589 MET A SD    1 
ATOM   451   C  CE    . MET A 1 1589 ? 130.535 217.965 162.251 1.00 138.21 ? 1589 MET A CE    1 
ATOM   452   N  N     . ASP A 1 1590 ? 124.618 215.868 162.012 1.00 152.77 ? 1590 ASP A N     1 
ATOM   453   C  CA    . ASP A 1 1590 ? 123.327 215.385 162.491 1.00 154.50 ? 1590 ASP A CA    1 
ATOM   454   C  C     . ASP A 1 1590 ? 123.361 213.882 162.734 1.00 155.96 ? 1590 ASP A C     1 
ATOM   455   O  O     . ASP A 1 1590 ? 122.808 213.391 163.726 1.00 154.44 ? 1590 ASP A O     1 
ATOM   456   C  CB    . ASP A 1 1590 ? 122.228 215.743 161.492 1.00 158.33 ? 1590 ASP A CB    1 
ATOM   457   C  CG    . ASP A 1 1590 ? 120.926 216.122 162.169 1.00 162.65 ? 1590 ASP A CG    1 
ATOM   458   O  OD1   . ASP A 1 1590 ? 120.721 215.719 163.333 1.00 161.53 ? 1590 ASP A OD1   1 
ATOM   459   O  OD2   . ASP A 1 1590 ? 120.109 216.824 161.538 1.00 162.70 ? 1590 ASP A OD2   1 
ATOM   460   N  N     . VAL A 1 1591 ? 124.004 213.134 161.835 1.00 156.43 ? 1591 VAL A N     1 
ATOM   461   C  CA    . VAL A 1 1591 ? 124.150 211.695 162.029 1.00 154.53 ? 1591 VAL A CA    1 
ATOM   462   C  C     . VAL A 1 1591 ? 125.054 211.408 163.222 1.00 152.80 ? 1591 VAL A C     1 
ATOM   463   O  O     . VAL A 1 1591 ? 124.802 210.482 164.003 1.00 151.86 ? 1591 VAL A O     1 
ATOM   464   C  CB    . VAL A 1 1591 ? 124.676 211.038 160.740 1.00 149.06 ? 1591 VAL A CB    1 
ATOM   465   C  CG1   . VAL A 1 1591 ? 125.077 209.591 160.996 1.00 146.41 ? 1591 VAL A CG1   1 
ATOM   466   C  CG2   . VAL A 1 1591 ? 123.630 211.121 159.639 1.00 148.72 ? 1591 VAL A CG2   1 
ATOM   467   N  N     . LEU A 1 1592 ? 126.118 212.199 163.386 1.00 149.67 ? 1592 LEU A N     1 
ATOM   468   C  CA    . LEU A 1 1592 ? 127.023 212.000 164.514 1.00 147.21 ? 1592 LEU A CA    1 
ATOM   469   C  C     . LEU A 1 1592 ? 126.336 212.272 165.847 1.00 151.76 ? 1592 LEU A C     1 
ATOM   470   O  O     . LEU A 1 1592 ? 126.760 211.745 166.882 1.00 148.99 ? 1592 LEU A O     1 
ATOM   471   C  CB    . LEU A 1 1592 ? 128.255 212.892 164.361 1.00 140.13 ? 1592 LEU A CB    1 
ATOM   472   C  CG    . LEU A 1 1592 ? 129.480 212.518 165.198 1.00 130.05 ? 1592 LEU A CG    1 
ATOM   473   C  CD1   . LEU A 1 1592 ? 130.279 211.416 164.522 1.00 122.92 ? 1592 LEU A CD1   1 
ATOM   474   C  CD2   . LEU A 1 1592 ? 130.349 213.739 165.451 1.00 130.02 ? 1592 LEU A CD2   1 
ATOM   475   N  N     . ASN A 1 1593 ? 125.280 213.083 165.845 1.00 154.73 ? 1593 ASN A N     1 
ATOM   476   C  CA    . ASN A 1 1593 ? 124.562 213.426 167.065 1.00 152.12 ? 1593 ASN A CA    1 
ATOM   477   C  C     . ASN A 1 1593 ? 123.473 212.423 167.421 1.00 149.48 ? 1593 ASN A C     1 
ATOM   478   O  O     . ASN A 1 1593 ? 122.786 212.611 168.431 1.00 148.37 ? 1593 ASN A O     1 
ATOM   479   C  CB    . ASN A 1 1593 ? 123.950 214.826 166.942 1.00 150.13 ? 1593 ASN A CB    1 
ATOM   480   C  CG    . ASN A 1 1593 ? 124.997 215.922 166.963 1.00 147.73 ? 1593 ASN A CG    1 
ATOM   481   O  OD1   . ASN A 1 1593 ? 126.198 215.650 166.989 1.00 144.74 ? 1593 ASN A OD1   1 
ATOM   482   N  ND2   . ASN A 1 1593 ? 124.546 217.171 166.953 1.00 143.91 ? 1593 ASN A ND2   1 
ATOM   483   N  N     . ILE A 1 1594 ? 123.294 211.371 166.622 1.00 150.79 ? 1594 ILE A N     1 
ATOM   484   C  CA    . ILE A 1 1594 ? 122.322 210.335 166.950 1.00 150.49 ? 1594 ILE A CA    1 
ATOM   485   C  C     . ILE A 1 1594 ? 122.781 209.600 168.202 1.00 153.38 ? 1594 ILE A C     1 
ATOM   486   O  O     . ILE A 1 1594 ? 123.950 209.211 168.319 1.00 152.94 ? 1594 ILE A O     1 
ATOM   487   C  CB    . ILE A 1 1594 ? 122.139 209.373 165.767 1.00 149.26 ? 1594 ILE A CB    1 
ATOM   488   C  CG1   . ILE A 1 1594 ? 121.615 210.129 164.544 1.00 148.36 ? 1594 ILE A CG1   1 
ATOM   489   C  CG2   . ILE A 1 1594 ? 121.196 208.239 166.139 1.00 143.72 ? 1594 ILE A CG2   1 
ATOM   490   C  CD1   . ILE A 1 1594 ? 121.426 209.259 163.322 1.00 143.71 ? 1594 ILE A CD1   1 
ATOM   491   N  N     . GLN A 1 1595 ? 121.861 209.411 169.146 1.00 157.72 ? 1595 GLN A N     1 
ATOM   492   C  CA    . GLN A 1 1595 ? 122.217 208.831 170.434 1.00 158.74 ? 1595 GLN A CA    1 
ATOM   493   C  C     . GLN A 1 1595 ? 122.655 207.378 170.274 1.00 157.56 ? 1595 GLN A C     1 
ATOM   494   O  O     . GLN A 1 1595 ? 121.985 206.580 169.611 1.00 154.16 ? 1595 GLN A O     1 
ATOM   495   C  CB    . GLN A 1 1595 ? 121.039 208.938 171.407 1.00 152.63 ? 1595 GLN A CB    1 
ATOM   496   C  CG    . GLN A 1 1595 ? 119.776 208.199 170.979 1.00 148.22 ? 1595 GLN A CG    1 
ATOM   497   C  CD    . GLN A 1 1595 ? 118.871 209.043 170.103 1.00 145.09 ? 1595 GLN A CD    1 
ATOM   498   O  OE1   . GLN A 1 1595 ? 119.269 209.488 169.026 1.00 144.68 ? 1595 GLN A OE1   1 
ATOM   499   N  NE2   . GLN A 1 1595 ? 117.645 209.267 170.561 1.00 138.30 ? 1595 GLN A NE2   1 
ATOM   500   N  N     . GLY A 1 1596 ? 123.795 207.046 170.873 1.00 155.90 ? 1596 GLY A N     1 
ATOM   501   C  CA    . GLY A 1 1596 ? 124.307 205.685 170.839 1.00 149.70 ? 1596 GLY A CA    1 
ATOM   502   C  C     . GLY A 1 1596 ? 124.599 205.165 169.449 1.00 153.01 ? 1596 GLY A C     1 
ATOM   503   O  O     . GLY A 1 1596 ? 124.412 203.970 169.185 1.00 153.85 ? 1596 GLY A O     1 
ATOM   504   N  N     . VAL A 1 1597 ? 125.055 206.037 168.547 1.00 154.90 ? 1597 VAL A N     1 
ATOM   505   C  CA    . VAL A 1 1597 ? 125.336 205.601 167.183 1.00 153.60 ? 1597 VAL A CA    1 
ATOM   506   C  C     . VAL A 1 1597 ? 126.576 204.712 167.143 1.00 151.95 ? 1597 VAL A C     1 
ATOM   507   O  O     . VAL A 1 1597 ? 126.607 203.702 166.429 1.00 151.16 ? 1597 VAL A O     1 
ATOM   508   C  CB    . VAL A 1 1597 ? 125.456 206.817 166.242 1.00 151.89 ? 1597 VAL A CB    1 
ATOM   509   C  CG1   . VAL A 1 1597 ? 126.636 207.705 166.623 1.00 149.89 ? 1597 VAL A CG1   1 
ATOM   510   C  CG2   . VAL A 1 1597 ? 125.571 206.359 164.795 1.00 149.58 ? 1597 VAL A CG2   1 
ATOM   511   N  N     . GLN A 1 1598 ? 127.611 205.061 167.912 1.00 148.37 ? 1598 GLN A N     1 
ATOM   512   C  CA    . GLN A 1 1598 ? 128.830 204.258 167.920 1.00 143.65 ? 1598 GLN A CA    1 
ATOM   513   C  C     . GLN A 1 1598 ? 128.566 202.867 168.484 1.00 145.19 ? 1598 GLN A C     1 
ATOM   514   O  O     . GLN A 1 1598 ? 129.014 201.861 167.922 1.00 143.05 ? 1598 GLN A O     1 
ATOM   515   C  CB    . GLN A 1 1598 ? 129.921 204.970 168.721 1.00 137.97 ? 1598 GLN A CB    1 
ATOM   516   C  CG    . GLN A 1 1598 ? 131.253 204.242 168.737 1.00 136.45 ? 1598 GLN A CG    1 
ATOM   517   C  CD    . GLN A 1 1598 ? 132.062 204.481 167.479 1.00 126.93 ? 1598 GLN A CD    1 
ATOM   518   O  OE1   . GLN A 1 1598 ? 132.456 205.610 167.185 1.00 115.12 ? 1598 GLN A OE1   1 
ATOM   519   N  NE2   . GLN A 1 1598 ? 132.314 203.417 166.726 1.00 130.51 ? 1598 GLN A NE2   1 
ATOM   520   N  N     . ARG A 1 1599 ? 127.829 202.793 169.596 1.00 144.68 ? 1599 ARG A N     1 
ATOM   521   C  CA    . ARG A 1 1599 ? 127.474 201.498 170.165 1.00 141.17 ? 1599 ARG A CA    1 
ATOM   522   C  C     . ARG A 1 1599 ? 126.605 200.697 169.206 1.00 144.19 ? 1599 ARG A C     1 
ATOM   523   O  O     . ARG A 1 1599 ? 126.762 199.476 169.086 1.00 144.91 ? 1599 ARG A O     1 
ATOM   524   C  CB    . ARG A 1 1599 ? 126.761 201.692 171.503 1.00 141.82 ? 1599 ARG A CB    1 
ATOM   525   C  CG    . ARG A 1 1599 ? 126.590 200.413 172.306 1.00 139.91 ? 1599 ARG A CG    1 
ATOM   526   C  CD    . ARG A 1 1599 ? 125.286 200.431 173.086 1.00 141.68 ? 1599 ARG A CD    1 
ATOM   527   N  NE    . ARG A 1 1599 ? 124.173 199.918 172.296 1.00 145.68 ? 1599 ARG A NE    1 
ATOM   528   C  CZ    . ARG A 1 1599 ? 123.293 200.679 171.659 1.00 144.42 ? 1599 ARG A CZ    1 
ATOM   529   N  NH1   . ARG A 1 1599 ? 123.364 201.999 171.701 1.00 144.89 ? 1599 ARG A NH1   1 
ATOM   530   N  NH2   . ARG A 1 1599 ? 122.319 200.101 170.963 1.00 138.36 ? 1599 ARG A NH2   1 
ATOM   531   N  N     . SER A 1 1600 ? 125.678 201.368 168.517 1.00 146.27 ? 1600 SER A N     1 
ATOM   532   C  CA    . SER A 1 1600 ? 124.835 200.680 167.546 1.00 145.08 ? 1600 SER A CA    1 
ATOM   533   C  C     . SER A 1 1600 ? 125.667 200.080 166.420 1.00 142.72 ? 1600 SER A C     1 
ATOM   534   O  O     . SER A 1 1600 ? 125.449 198.928 166.025 1.00 140.28 ? 1600 SER A O     1 
ATOM   535   C  CB    . SER A 1 1600 ? 123.788 201.643 166.985 1.00 142.26 ? 1600 SER A CB    1 
ATOM   536   O  OG    . SER A 1 1600 ? 122.974 201.004 166.016 1.00 143.30 ? 1600 SER A OG    1 
ATOM   537   N  N     . LEU A 1 1601 ? 126.631 200.841 165.895 1.00 142.84 ? 1601 LEU A N     1 
ATOM   538   C  CA    . LEU A 1 1601 ? 127.476 200.319 164.823 1.00 140.53 ? 1601 LEU A CA    1 
ATOM   539   C  C     . LEU A 1 1601 ? 128.370 199.185 165.311 1.00 143.24 ? 1601 LEU A C     1 
ATOM   540   O  O     . LEU A 1 1601 ? 128.597 198.214 164.581 1.00 145.00 ? 1601 LEU A O     1 
ATOM   541   C  CB    . LEU A 1 1601 ? 128.312 201.438 164.203 1.00 136.49 ? 1601 LEU A CB    1 
ATOM   542   C  CG    . LEU A 1 1601 ? 127.678 202.194 163.030 1.00 132.96 ? 1601 LEU A CG    1 
ATOM   543   C  CD1   . LEU A 1 1601 ? 127.459 201.230 161.872 1.00 131.08 ? 1601 LEU A CD1   1 
ATOM   544   C  CD2   . LEU A 1 1601 ? 126.376 202.884 163.404 1.00 134.49 ? 1601 LEU A CD2   1 
ATOM   545   N  N     . GLU A 1 1602 ? 128.896 199.286 166.535 1.00 142.28 ? 1602 GLU A N     1 
ATOM   546   C  CA    . GLU A 1 1602 ? 129.704 198.189 167.064 1.00 142.29 ? 1602 GLU A CA    1 
ATOM   547   C  C     . GLU A 1 1602 ? 128.874 196.921 167.235 1.00 142.77 ? 1602 GLU A C     1 
ATOM   548   O  O     . GLU A 1 1602 ? 129.333 195.820 166.901 1.00 146.51 ? 1602 GLU A O     1 
ATOM   549   C  CB    . GLU A 1 1602 ? 130.354 198.594 168.388 1.00 147.25 ? 1602 GLU A CB    1 
ATOM   550   C  CG    . GLU A 1 1602 ? 131.286 199.790 168.282 1.00 144.25 ? 1602 GLU A CG    1 
ATOM   551   C  CD    . GLU A 1 1602 ? 132.497 199.668 169.185 1.00 143.26 ? 1602 GLU A CD    1 
ATOM   552   O  OE1   . GLU A 1 1602 ? 132.341 199.201 170.332 1.00 142.79 ? 1602 GLU A OE1   1 
ATOM   553   O  OE2   . GLU A 1 1602 ? 133.606 200.040 168.746 1.00 139.43 ? 1602 GLU A OE2   1 
ATOM   554   N  N     . ARG A 1 1603 ? 127.648 197.056 167.749 1.00 140.55 ? 1603 ARG A N     1 
ATOM   555   C  CA    . ARG A 1 1603 ? 126.767 195.899 167.879 1.00 138.48 ? 1603 ARG A CA    1 
ATOM   556   C  C     . ARG A 1 1603 ? 126.429 195.310 166.516 1.00 143.66 ? 1603 ARG A C     1 
ATOM   557   O  O     . ARG A 1 1603 ? 126.402 194.084 166.350 1.00 143.21 ? 1603 ARG A O     1 
ATOM   558   C  CB    . ARG A 1 1603 ? 125.492 196.293 168.624 1.00 137.68 ? 1603 ARG A CB    1 
ATOM   559   C  CG    . ARG A 1 1603 ? 124.678 195.116 169.132 1.00 139.28 ? 1603 ARG A CG    1 
ATOM   560   C  CD    . ARG A 1 1603 ? 123.357 195.580 169.723 1.00 138.73 ? 1603 ARG A CD    1 
ATOM   561   N  NE    . ARG A 1 1603 ? 122.699 196.561 168.870 1.00 142.21 ? 1603 ARG A NE    1 
ATOM   562   C  CZ    . ARG A 1 1603 ? 121.895 196.257 167.860 1.00 142.68 ? 1603 ARG A CZ    1 
ATOM   563   N  NH1   . ARG A 1 1603 ? 121.624 195.001 167.546 1.00 141.10 ? 1603 ARG A NH1   1 
ATOM   564   N  NH2   . ARG A 1 1603 ? 121.351 197.238 167.146 1.00 140.18 ? 1603 ARG A NH2   1 
ATOM   565   N  N     . LEU A 1 1604 ? 126.162 196.169 165.529 1.00 145.79 ? 1604 LEU A N     1 
ATOM   566   C  CA    . LEU A 1 1604 ? 125.880 195.687 164.182 1.00 142.63 ? 1604 LEU A CA    1 
ATOM   567   C  C     . LEU A 1 1604 ? 127.071 194.932 163.610 1.00 141.64 ? 1604 LEU A C     1 
ATOM   568   O  O     . LEU A 1 1604 ? 126.905 193.875 162.993 1.00 142.95 ? 1604 LEU A O     1 
ATOM   569   C  CB    . LEU A 1 1604 ? 125.500 196.854 163.271 1.00 140.18 ? 1604 LEU A CB    1 
ATOM   570   C  CG    . LEU A 1 1604 ? 124.098 197.439 163.443 1.00 140.24 ? 1604 LEU A CG    1 
ATOM   571   C  CD1   . LEU A 1 1604 ? 123.922 198.672 162.571 1.00 135.50 ? 1604 LEU A CD1   1 
ATOM   572   C  CD2   . LEU A 1 1604 ? 123.039 196.396 163.123 1.00 138.48 ? 1604 LEU A CD2   1 
ATOM   573   N  N     . ALA A 1 1605 ? 128.282 195.458 163.806 1.00 141.69 ? 1605 ALA A N     1 
ATOM   574   C  CA    . ALA A 1 1605 ? 129.475 194.777 163.316 1.00 141.70 ? 1605 ALA A CA    1 
ATOM   575   C  C     . ALA A 1 1605 ? 129.652 193.421 163.987 1.00 145.54 ? 1605 ALA A C     1 
ATOM   576   O  O     . ALA A 1 1605 ? 129.967 192.428 163.321 1.00 147.51 ? 1605 ALA A O     1 
ATOM   577   C  CB    . ALA A 1 1605 ? 130.709 195.651 163.539 1.00 133.08 ? 1605 ALA A CB    1 
ATOM   578   N  N     . ASP A 1 1606 ? 129.443 193.358 165.304 1.00 144.63 ? 1606 ASP A N     1 
ATOM   579   C  CA    . ASP A 1 1606 ? 129.580 192.089 166.013 1.00 145.85 ? 1606 ASP A CA    1 
ATOM   580   C  C     . ASP A 1 1606 ? 128.565 191.067 165.512 1.00 147.32 ? 1606 ASP A C     1 
ATOM   581   O  O     . ASP A 1 1606 ? 128.910 189.907 165.248 1.00 147.65 ? 1606 ASP A O     1 
ATOM   582   C  CB    . ASP A 1 1606 ? 129.423 192.309 167.518 1.00 145.98 ? 1606 ASP A CB    1 
ATOM   583   C  CG    . ASP A 1 1606 ? 130.723 192.706 168.188 1.00 144.83 ? 1606 ASP A CG    1 
ATOM   584   O  OD1   . ASP A 1 1606 ? 131.755 192.784 167.489 1.00 146.04 ? 1606 ASP A OD1   1 
ATOM   585   O  OD2   . ASP A 1 1606 ? 130.713 192.940 169.415 1.00 141.83 ? 1606 ASP A OD2   1 
ATOM   586   N  N     . LEU A 1 1607 ? 127.304 191.483 165.368 1.00 147.67 ? 1607 LEU A N     1 
ATOM   587   C  CA    . LEU A 1 1607 ? 126.270 190.563 164.906 1.00 146.24 ? 1607 LEU A CA    1 
ATOM   588   C  C     . LEU A 1 1607 ? 126.529 190.108 163.474 1.00 144.18 ? 1607 LEU A C     1 
ATOM   589   O  O     . LEU A 1 1607 ? 126.345 188.928 163.149 1.00 141.25 ? 1607 LEU A O     1 
ATOM   590   C  CB    . LEU A 1 1607 ? 124.895 191.219 165.030 1.00 145.91 ? 1607 LEU A CB    1 
ATOM   591   C  CG    . LEU A 1 1607 ? 124.448 191.552 166.456 1.00 141.79 ? 1607 LEU A CG    1 
ATOM   592   C  CD1   . LEU A 1 1607 ? 122.977 191.934 166.497 1.00 139.28 ? 1607 LEU A CD1   1 
ATOM   593   C  CD2   . LEU A 1 1607 ? 124.726 190.388 167.394 1.00 136.21 ? 1607 LEU A CD2   1 
ATOM   594   N  N     . LEU A 1 1608 ? 126.959 191.027 162.605 1.00 145.62 ? 1608 LEU A N     1 
ATOM   595   C  CA    . LEU A 1 1608 ? 127.271 190.657 161.230 1.00 143.55 ? 1608 LEU A CA    1 
ATOM   596   C  C     . LEU A 1 1608 ? 128.435 189.678 161.176 1.00 144.62 ? 1608 LEU A C     1 
ATOM   597   O  O     . LEU A 1 1608 ? 128.419 188.733 160.381 1.00 146.35 ? 1608 LEU A O     1 
ATOM   598   C  CB    . LEU A 1 1608 ? 127.577 191.908 160.405 1.00 135.55 ? 1608 LEU A CB    1 
ATOM   599   C  CG    . LEU A 1 1608 ? 126.386 192.804 160.052 1.00 132.58 ? 1608 LEU A CG    1 
ATOM   600   C  CD1   . LEU A 1 1608 ? 126.809 193.924 159.112 1.00 124.69 ? 1608 LEU A CD1   1 
ATOM   601   C  CD2   . LEU A 1 1608 ? 125.244 191.996 159.454 1.00 135.42 ? 1608 LEU A CD2   1 
ATOM   602   N  N     . GLY A 1 1609 ? 129.452 189.884 162.015 1.00 144.18 ? 1609 GLY A N     1 
ATOM   603   C  CA    . GLY A 1 1609 ? 130.553 188.935 162.069 1.00 144.90 ? 1609 GLY A CA    1 
ATOM   604   C  C     . GLY A 1 1609 ? 130.117 187.561 162.541 1.00 146.03 ? 1609 GLY A C     1 
ATOM   605   O  O     . GLY A 1 1609 ? 130.537 186.541 161.987 1.00 144.79 ? 1609 GLY A O     1 
ATOM   606   N  N     . LYS A 1 1610 ? 129.267 187.516 163.571 1.00 145.82 ? 1610 LYS A N     1 
ATOM   607   C  CA    . LYS A 1 1610 ? 128.768 186.231 164.057 1.00 144.20 ? 1610 LYS A CA    1 
ATOM   608   C  C     . LYS A 1 1610 ? 127.965 185.511 162.980 1.00 145.75 ? 1610 LYS A C     1 
ATOM   609   O  O     . LYS A 1 1610 ? 128.092 184.294 162.805 1.00 144.20 ? 1610 LYS A O     1 
ATOM   610   C  CB    . LYS A 1 1610 ? 127.922 186.427 165.317 1.00 141.07 ? 1610 LYS A CB    1 
ATOM   611   C  CG    . LYS A 1 1610 ? 128.665 187.048 166.488 1.00 139.05 ? 1610 LYS A CG    1 
ATOM   612   C  CD    . LYS A 1 1610 ? 127.913 186.839 167.795 1.00 133.99 ? 1610 LYS A CD    1 
ATOM   613   C  CE    . LYS A 1 1610 ? 126.413 187.025 167.618 1.00 137.74 ? 1610 LYS A CE    1 
ATOM   614   N  NZ    . LYS A 1 1610 ? 125.764 187.526 168.860 1.00 138.06 ? 1610 LYS A NZ    1 
ATOM   615   N  N     . ILE A 1 1611 ? 127.124 186.250 162.252 1.00 147.63 ? 1611 ILE A N     1 
ATOM   616   C  CA    . ILE A 1 1611 ? 126.346 185.638 161.176 1.00 147.71 ? 1611 ILE A CA    1 
ATOM   617   C  C     . ILE A 1 1611 ? 127.262 185.150 160.061 1.00 145.41 ? 1611 ILE A C     1 
ATOM   618   O  O     . ILE A 1 1611 ? 127.068 184.058 159.510 1.00 142.90 ? 1611 ILE A O     1 
ATOM   619   C  CB    . ILE A 1 1611 ? 125.288 186.625 160.651 1.00 144.53 ? 1611 ILE A CB    1 
ATOM   620   C  CG1   . ILE A 1 1611 ? 124.285 186.960 161.753 1.00 140.09 ? 1611 ILE A CG1   1 
ATOM   621   C  CG2   . ILE A 1 1611 ? 124.575 186.053 159.434 1.00 140.28 ? 1611 ILE A CG2   1 
ATOM   622   C  CD1   . ILE A 1 1611 ? 123.175 187.862 161.297 1.00 137.67 ? 1611 ILE A CD1   1 
ATOM   623   N  N     . GLN A 1 1612 ? 128.274 185.947 159.711 1.00 144.05 ? 1612 GLN A N     1 
ATOM   624   C  CA    . GLN A 1 1612 ? 129.175 185.578 158.625 1.00 140.12 ? 1612 GLN A CA    1 
ATOM   625   C  C     . GLN A 1 1612 ? 129.970 184.326 158.968 1.00 139.03 ? 1612 GLN A C     1 
ATOM   626   O  O     . GLN A 1 1612 ? 130.200 183.471 158.105 1.00 135.39 ? 1612 GLN A O     1 
ATOM   627   C  CB    . GLN A 1 1612 ? 130.110 186.745 158.310 1.00 135.18 ? 1612 GLN A CB    1 
ATOM   628   C  CG    . GLN A 1 1612 ? 131.020 186.516 157.121 1.00 126.36 ? 1612 GLN A CG    1 
ATOM   629   C  CD    . GLN A 1 1612 ? 131.881 187.722 156.815 1.00 125.59 ? 1612 GLN A CD    1 
ATOM   630   O  OE1   . GLN A 1 1612 ? 131.842 188.724 157.529 1.00 126.47 ? 1612 GLN A OE1   1 
ATOM   631   N  NE2   . GLN A 1 1612 ? 132.650 187.642 155.738 1.00 121.70 ? 1612 GLN A NE2   1 
ATOM   632   N  N     . LYS A 1 1613 ? 130.401 184.199 160.226 1.00 139.54 ? 1613 LYS A N     1 
ATOM   633   C  CA    . LYS A 1 1613 ? 131.111 182.994 160.641 1.00 137.28 ? 1613 LYS A CA    1 
ATOM   634   C  C     . LYS A 1 1613 ? 130.197 181.776 160.721 1.00 142.15 ? 1613 LYS A C     1 
ATOM   635   O  O     . LYS A 1 1613 ? 130.695 180.654 160.860 1.00 142.85 ? 1613 LYS A O     1 
ATOM   636   C  CB    . LYS A 1 1613 ? 131.793 183.221 161.991 1.00 129.78 ? 1613 LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 1613 ? 133.299 183.414 161.898 1.00 112.23 ? 1613 LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 1613 ? 133.654 184.791 161.363 1.00 111.80 ? 1613 LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 1613 ? 135.156 185.024 161.404 1.00 100.00 ? 1613 LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 1613 ? 135.535 186.318 160.774 1.00 93.35  ? 1613 LYS A NZ    1 
ATOM   641   N  N     . ALA A 1 1614 ? 128.882 181.967 160.635 1.00 143.85 ? 1614 ALA A N     1 
ATOM   642   C  CA    . ALA A 1 1614 ? 127.915 180.873 160.731 1.00 145.43 ? 1614 ALA A CA    1 
ATOM   643   C  C     . ALA A 1 1614 ? 127.378 180.444 159.372 1.00 143.33 ? 1614 ALA A C     1 
ATOM   644   O  O     . ALA A 1 1614 ? 126.206 180.074 159.254 1.00 141.19 ? 1614 ALA A O     1 
ATOM   645   C  CB    . ALA A 1 1614 ? 126.775 181.279 161.658 1.00 143.09 ? 1614 ALA A CB    1 
ATOM   646   N  N     . LEU A 1 1615 ? 128.208 180.479 158.325 1.00 141.22 ? 1615 LEU A N     1 
ATOM   647   C  CA    . LEU A 1 1615 ? 127.766 180.139 156.977 1.00 137.46 ? 1615 LEU A CA    1 
ATOM   648   C  C     . LEU A 1 1615 ? 128.689 179.126 156.306 1.00 131.42 ? 1615 LEU A C     1 
ATOM   649   O  O     . LEU A 1 1615 ? 128.758 179.084 155.074 1.00 127.01 ? 1615 LEU A O     1 
ATOM   650   C  CB    . LEU A 1 1615 ? 127.658 181.399 156.113 1.00 131.89 ? 1615 LEU A CB    1 
ATOM   651   C  CG    . LEU A 1 1615 ? 126.482 182.340 156.387 1.00 132.65 ? 1615 LEU A CG    1 
ATOM   652   C  CD1   . LEU A 1 1615 ? 126.379 183.395 155.297 1.00 126.68 ? 1615 LEU A CD1   1 
ATOM   653   C  CD2   . LEU A 1 1615 ? 125.182 181.562 156.504 1.00 138.91 ? 1615 LEU A CD2   1 
ATOM   654   N  N     . GLY A 1 1616 ? 129.393 178.305 157.088 1.00 128.90 ? 1616 GLY A N     1 
ATOM   655   C  CA    . GLY A 1 1616 ? 130.373 177.400 156.506 1.00 120.05 ? 1616 GLY A CA    1 
ATOM   656   C  C     . GLY A 1 1616 ? 129.759 176.327 155.625 1.00 122.40 ? 1616 GLY A C     1 
ATOM   657   O  O     . GLY A 1 1616 ? 130.270 176.038 154.539 1.00 124.06 ? 1616 GLY A O     1 
ATOM   658   N  N     . GLU A 1 1617 ? 128.665 175.713 156.083 1.00 121.87 ? 1617 GLU A N     1 
ATOM   659   C  CA    . GLU A 1 1617 ? 128.046 174.636 155.314 1.00 123.70 ? 1617 GLU A CA    1 
ATOM   660   C  C     . GLU A 1 1617 ? 127.501 175.144 153.984 1.00 122.17 ? 1617 GLU A C     1 
ATOM   661   O  O     . GLU A 1 1617 ? 127.647 174.478 152.951 1.00 118.85 ? 1617 GLU A O     1 
ATOM   662   C  CB    . GLU A 1 1617 ? 126.941 173.975 156.137 1.00 126.66 ? 1617 GLU A CB    1 
ATOM   663   C  CG    . GLU A 1 1617 ? 127.424 173.384 157.453 1.00 125.31 ? 1617 GLU A CG    1 
ATOM   664   C  CD    . GLU A 1 1617 ? 126.350 172.587 158.166 1.00 134.17 ? 1617 GLU A CD    1 
ATOM   665   O  OE1   . GLU A 1 1617 ? 125.193 172.588 157.694 1.00 133.75 ? 1617 GLU A OE1   1 
ATOM   666   O  OE2   . GLU A 1 1617 ? 126.662 171.959 159.200 1.00 133.70 ? 1617 GLU A OE2   1 
ATOM   667   N  N     . TYR A 1 1618 ? 126.869 176.320 153.989 1.00 121.89 ? 1618 TYR A N     1 
ATOM   668   C  CA    . TYR A 1 1618 ? 126.406 176.909 152.737 1.00 117.78 ? 1618 TYR A CA    1 
ATOM   669   C  C     . TYR A 1 1618 ? 127.578 177.237 151.820 1.00 116.98 ? 1618 TYR A C     1 
ATOM   670   O  O     . TYR A 1 1618 ? 127.470 177.110 150.595 1.00 112.00 ? 1618 TYR A O     1 
ATOM   671   C  CB    . TYR A 1 1618 ? 125.573 178.159 153.016 1.00 116.40 ? 1618 TYR A CB    1 
ATOM   672   C  CG    . TYR A 1 1618 ? 125.046 178.823 151.765 1.00 120.02 ? 1618 TYR A CG    1 
ATOM   673   C  CD1   . TYR A 1 1618 ? 124.044 178.227 151.010 1.00 119.20 ? 1618 TYR A CD1   1 
ATOM   674   C  CD2   . TYR A 1 1618 ? 125.551 180.043 151.338 1.00 121.00 ? 1618 TYR A CD2   1 
ATOM   675   C  CE1   . TYR A 1 1618 ? 123.561 178.829 149.864 1.00 118.87 ? 1618 TYR A CE1   1 
ATOM   676   C  CE2   . TYR A 1 1618 ? 125.074 180.652 150.194 1.00 122.24 ? 1618 TYR A CE2   1 
ATOM   677   C  CZ    . TYR A 1 1618 ? 124.080 180.041 149.461 1.00 122.66 ? 1618 TYR A CZ    1 
ATOM   678   O  OH    . TYR A 1 1618 ? 123.602 180.645 148.321 1.00 125.23 ? 1618 TYR A OH    1 
ATOM   679   N  N     . LEU A 1 1619 ? 128.706 177.660 152.395 1.00 118.46 ? 1619 LEU A N     1 
ATOM   680   C  CA    . LEU A 1 1619 ? 129.893 177.917 151.587 1.00 108.41 ? 1619 LEU A CA    1 
ATOM   681   C  C     . LEU A 1 1619 ? 130.397 176.642 150.926 1.00 106.34 ? 1619 LEU A C     1 
ATOM   682   O  O     . LEU A 1 1619 ? 130.771 176.653 149.749 1.00 104.87 ? 1619 LEU A O     1 
ATOM   683   C  CB    . LEU A 1 1619 ? 130.990 178.541 152.446 1.00 101.59 ? 1619 LEU A CB    1 
ATOM   684   C  CG    . LEU A 1 1619 ? 130.806 180.010 152.819 1.00 102.98 ? 1619 LEU A CG    1 
ATOM   685   C  CD1   . LEU A 1 1619 ? 132.138 180.598 153.233 1.00 101.65 ? 1619 LEU A CD1   1 
ATOM   686   C  CD2   . LEU A 1 1619 ? 130.191 180.797 151.671 1.00 98.70  ? 1619 LEU A CD2   1 
ATOM   687   N  N     . GLU A 1 1620 ? 130.424 175.533 151.670 1.00 107.64 ? 1620 GLU A N     1 
ATOM   688   C  CA    . GLU A 1 1620 ? 130.826 174.261 151.076 1.00 103.21 ? 1620 GLU A CA    1 
ATOM   689   C  C     . GLU A 1 1620 ? 129.856 173.838 149.979 1.00 104.52 ? 1620 GLU A C     1 
ATOM   690   O  O     . GLU A 1 1620 ? 130.273 173.336 148.927 1.00 104.50 ? 1620 GLU A O     1 
ATOM   691   C  CB    . GLU A 1 1620 ? 130.922 173.181 152.154 1.00 104.65 ? 1620 GLU A CB    1 
ATOM   692   C  CG    . GLU A 1 1620 ? 131.838 173.537 153.314 1.00 110.72 ? 1620 GLU A CG    1 
ATOM   693   C  CD    . GLU A 1 1620 ? 133.137 174.171 152.858 1.00 110.17 ? 1620 GLU A CD    1 
ATOM   694   O  OE1   . GLU A 1 1620 ? 133.903 173.503 152.131 1.00 104.45 ? 1620 GLU A OE1   1 
ATOM   695   O  OE2   . GLU A 1 1620 ? 133.391 175.338 153.224 1.00 109.59 ? 1620 GLU A OE2   1 
ATOM   696   N  N     . ARG A 1 1621 ? 128.556 174.039 150.208 1.00 105.89 ? 1621 ARG A N     1 
ATOM   697   C  CA    . ARG A 1 1621 ? 127.565 173.718 149.187 1.00 103.72 ? 1621 ARG A CA    1 
ATOM   698   C  C     . ARG A 1 1621 ? 127.794 174.535 147.922 1.00 102.78 ? 1621 ARG A C     1 
ATOM   699   O  O     . ARG A 1 1621 ? 127.691 174.011 146.806 1.00 94.22  ? 1621 ARG A O     1 
ATOM   700   C  CB    . ARG A 1 1621 ? 126.156 173.958 149.731 1.00 105.96 ? 1621 ARG A CB    1 
ATOM   701   C  CG    . ARG A 1 1621 ? 125.090 173.061 149.126 1.00 101.81 ? 1621 ARG A CG    1 
ATOM   702   C  CD    . ARG A 1 1621 ? 123.977 172.787 150.123 1.00 100.84 ? 1621 ARG A CD    1 
ATOM   703   N  NE    . ARG A 1 1621 ? 124.497 172.450 151.442 1.00 110.02 ? 1621 ARG A NE    1 
ATOM   704   C  CZ    . ARG A 1 1621 ? 124.870 171.232 151.812 1.00 106.95 ? 1621 ARG A CZ    1 
ATOM   705   N  NH1   . ARG A 1 1621 ? 124.795 170.204 150.983 1.00 99.52  ? 1621 ARG A NH1   1 
ATOM   706   N  NH2   . ARG A 1 1621 ? 125.331 171.042 153.045 1.00 103.51 ? 1621 ARG A NH2   1 
ATOM   707   N  N     . GLU A 1 1622 ? 128.102 175.825 148.076 1.00 107.10 ? 1622 GLU A N     1 
ATOM   708   C  CA    . GLU A 1 1622 ? 128.350 176.672 146.914 1.00 103.87 ? 1622 GLU A CA    1 
ATOM   709   C  C     . GLU A 1 1622 ? 129.636 176.271 146.198 1.00 100.27 ? 1622 GLU A C     1 
ATOM   710   O  O     . GLU A 1 1622 ? 129.696 176.284 144.963 1.00 95.41  ? 1622 GLU A O     1 
ATOM   711   C  CB    . GLU A 1 1622 ? 128.404 178.140 147.337 1.00 105.93 ? 1622 GLU A CB    1 
ATOM   712   C  CG    . GLU A 1 1622 ? 127.050 178.841 147.342 1.00 114.61 ? 1622 GLU A CG    1 
ATOM   713   C  CD    . GLU A 1 1622 ? 126.319 178.728 146.016 1.00 114.22 ? 1622 GLU A CD    1 
ATOM   714   O  OE1   . GLU A 1 1622 ? 126.512 179.609 145.152 1.00 107.14 ? 1622 GLU A OE1   1 
ATOM   715   O  OE2   . GLU A 1 1622 ? 125.543 177.765 145.840 1.00 108.48 ? 1622 GLU A OE2   1 
ATOM   716   N  N     . ARG A 1 1623 ? 130.679 175.920 146.958 1.00 99.14  ? 1623 ARG A N     1 
ATOM   717   C  CA    . ARG A 1 1623 ? 131.922 175.459 146.345 1.00 85.39  ? 1623 ARG A CA    1 
ATOM   718   C  C     . ARG A 1 1623 ? 131.721 174.161 145.578 1.00 84.76  ? 1623 ARG A C     1 
ATOM   719   O  O     . ARG A 1 1623 ? 132.397 173.925 144.570 1.00 80.63  ? 1623 ARG A O     1 
ATOM   720   C  CB    . ARG A 1 1623 ? 133.006 175.266 147.408 1.00 74.01  ? 1623 ARG A CB    1 
ATOM   721   C  CG    . ARG A 1 1623 ? 133.421 176.524 148.147 1.00 71.93  ? 1623 ARG A CG    1 
ATOM   722   C  CD    . ARG A 1 1623 ? 134.209 176.171 149.402 1.00 73.90  ? 1623 ARG A CD    1 
ATOM   723   N  NE    . ARG A 1 1623 ? 134.558 177.340 150.201 1.00 77.20  ? 1623 ARG A NE    1 
ATOM   724   C  CZ    . ARG A 1 1623 ? 135.475 178.238 149.866 1.00 73.03  ? 1623 ARG A CZ    1 
ATOM   725   N  NH1   . ARG A 1 1623 ? 136.179 178.125 148.752 1.00 72.11  ? 1623 ARG A NH1   1 
ATOM   726   N  NH2   . ARG A 1 1623 ? 135.696 179.271 150.673 1.00 74.76  ? 1623 ARG A NH2   1 
ATOM   727   N  N     . SER A 1 1624 ? 130.812 173.303 146.045 1.00 89.12  ? 1624 SER A N     1 
ATOM   728   C  CA    . SER A 1 1624 ? 130.588 172.028 145.370 1.00 91.28  ? 1624 SER A CA    1 
ATOM   729   C  C     . SER A 1 1624 ? 130.075 172.230 143.948 1.00 86.15  ? 1624 SER A C     1 
ATOM   730   O  O     . SER A 1 1624 ? 130.502 171.531 143.022 1.00 72.67  ? 1624 SER A O     1 
ATOM   731   C  CB    . SER A 1 1624 ? 129.608 171.174 146.176 1.00 99.16  ? 1624 SER A CB    1 
ATOM   732   O  OG    . SER A 1 1624 ? 130.059 170.998 147.507 1.00 97.34  ? 1624 SER A OG    1 
ATOM   733   N  N     . SER A 1 1625 ? 129.156 173.179 143.756 1.00 92.34  ? 1625 SER A N     1 
ATOM   734   C  CA    . SER A 1 1625 ? 128.538 173.364 142.445 1.00 88.82  ? 1625 SER A CA    1 
ATOM   735   C  C     . SER A 1 1625 ? 129.542 173.878 141.419 1.00 83.55  ? 1625 SER A C     1 
ATOM   736   O  O     . SER A 1 1625 ? 129.651 173.330 140.316 1.00 75.51  ? 1625 SER A O     1 
ATOM   737   C  CB    . SER A 1 1625 ? 127.346 174.313 142.561 1.00 82.59  ? 1625 SER A CB    1 
ATOM   738   O  OG    . SER A 1 1625 ? 127.747 175.577 143.061 1.00 82.25  ? 1625 SER A OG    1 
ATOM   739   N  N     . PHE A 1 1626 ? 130.281 174.932 141.758 1.00 83.78  ? 1626 PHE A N     1 
ATOM   740   C  CA    . PHE A 1 1626 ? 131.307 175.469 140.870 1.00 74.03  ? 1626 PHE A CA    1 
ATOM   741   C  C     . PHE A 1 1626 ? 132.676 175.096 141.417 1.00 75.26  ? 1626 PHE A C     1 
ATOM   742   O  O     . PHE A 1 1626 ? 133.083 175.627 142.463 1.00 76.51  ? 1626 PHE A O     1 
ATOM   743   C  CB    . PHE A 1 1626 ? 131.177 176.987 140.737 1.00 71.31  ? 1626 PHE A CB    1 
ATOM   744   C  CG    . PHE A 1 1626 ? 131.992 177.573 139.617 1.00 72.03  ? 1626 PHE A CG    1 
ATOM   745   C  CD1   . PHE A 1 1626 ? 131.795 177.160 138.310 1.00 67.07  ? 1626 PHE A CD1   1 
ATOM   746   C  CD2   . PHE A 1 1626 ? 132.951 178.539 139.872 1.00 69.92  ? 1626 PHE A CD2   1 
ATOM   747   C  CE1   . PHE A 1 1626 ? 132.542 177.697 137.279 1.00 62.16  ? 1626 PHE A CE1   1 
ATOM   748   C  CE2   . PHE A 1 1626 ? 133.700 179.080 138.844 1.00 58.24  ? 1626 PHE A CE2   1 
ATOM   749   C  CZ    . PHE A 1 1626 ? 133.495 178.659 137.547 1.00 56.29  ? 1626 PHE A CZ    1 
ATOM   750   N  N     . PRO A 1 1627 ? 133.416 174.204 140.755 1.00 70.19  ? 1627 PRO A N     1 
ATOM   751   C  CA    . PRO A 1 1627 ? 134.655 173.683 141.358 1.00 61.20  ? 1627 PRO A CA    1 
ATOM   752   C  C     . PRO A 1 1627 ? 135.702 174.745 141.642 1.00 57.53  ? 1627 PRO A C     1 
ATOM   753   O  O     . PRO A 1 1627 ? 136.475 174.595 142.597 1.00 57.37  ? 1627 PRO A O     1 
ATOM   754   C  CB    . PRO A 1 1627 ? 135.146 172.668 140.316 1.00 51.21  ? 1627 PRO A CB    1 
ATOM   755   C  CG    . PRO A 1 1627 ? 134.531 173.115 139.031 1.00 49.75  ? 1627 PRO A CG    1 
ATOM   756   C  CD    . PRO A 1 1627 ? 133.191 173.674 139.400 1.00 62.53  ? 1627 PRO A CD    1 
ATOM   757   N  N     . ARG A 1 1628 ? 135.757 175.815 140.848 1.00 53.63  ? 1628 ARG A N     1 
ATOM   758   C  CA    . ARG A 1 1628 ? 136.795 176.822 141.030 1.00 51.52  ? 1628 ARG A CA    1 
ATOM   759   C  C     . ARG A 1 1628 ? 136.617 177.641 142.302 1.00 60.04  ? 1628 ARG A C     1 
ATOM   760   O  O     . ARG A 1 1628 ? 137.539 178.374 142.675 1.00 63.25  ? 1628 ARG A O     1 
ATOM   761   C  CB    . ARG A 1 1628 ? 136.846 177.748 139.813 1.00 51.66  ? 1628 ARG A CB    1 
ATOM   762   C  CG    . ARG A 1 1628 ? 137.089 177.016 138.504 1.00 47.50  ? 1628 ARG A CG    1 
ATOM   763   C  CD    . ARG A 1 1628 ? 137.509 177.968 137.401 1.00 47.09  ? 1628 ARG A CD    1 
ATOM   764   N  NE    . ARG A 1 1628 ? 137.888 177.258 136.185 1.00 40.39  ? 1628 ARG A NE    1 
ATOM   765   C  CZ    . ARG A 1 1628 ? 139.111 177.250 135.673 1.00 36.03  ? 1628 ARG A CZ    1 
ATOM   766   N  NH1   . ARG A 1 1628 ? 140.106 177.905 136.249 1.00 33.49  ? 1628 ARG A NH1   1 
ATOM   767   N  NH2   . ARG A 1 1628 ? 139.342 176.567 134.556 1.00 44.70  ? 1628 ARG A NH2   1 
ATOM   768   N  N     . PHE A 1 1629 ? 135.470 177.536 142.977 1.00 64.07  ? 1629 PHE A N     1 
ATOM   769   C  CA    . PHE A 1 1629 ? 135.285 178.215 144.254 1.00 67.85  ? 1629 PHE A CA    1 
ATOM   770   C  C     . PHE A 1 1629 ? 136.122 177.610 145.373 1.00 66.23  ? 1629 PHE A C     1 
ATOM   771   O  O     . PHE A 1 1629 ? 136.202 178.206 146.452 1.00 63.87  ? 1629 PHE A O     1 
ATOM   772   C  CB    . PHE A 1 1629 ? 133.809 178.199 144.658 1.00 71.63  ? 1629 PHE A CB    1 
ATOM   773   C  CG    . PHE A 1 1629 ? 132.975 179.233 143.958 1.00 74.53  ? 1629 PHE A CG    1 
ATOM   774   C  CD1   . PHE A 1 1629 ? 133.475 180.501 143.721 1.00 69.30  ? 1629 PHE A CD1   1 
ATOM   775   C  CD2   . PHE A 1 1629 ? 131.686 178.940 143.548 1.00 74.32  ? 1629 PHE A CD2   1 
ATOM   776   C  CE1   . PHE A 1 1629 ? 132.709 181.456 143.081 1.00 70.53  ? 1629 PHE A CE1   1 
ATOM   777   C  CE2   . PHE A 1 1629 ? 130.915 179.890 142.906 1.00 72.92  ? 1629 PHE A CE2   1 
ATOM   778   C  CZ    . PHE A 1 1629 ? 131.427 181.149 142.672 1.00 72.74  ? 1629 PHE A CZ    1 
ATOM   779   N  N     . TYR A 1 1630 ? 136.734 176.444 145.154 1.00 61.96  ? 1630 TYR A N     1 
ATOM   780   C  CA    . TYR A 1 1630 ? 137.561 175.840 146.192 1.00 53.09  ? 1630 TYR A CA    1 
ATOM   781   C  C     . TYR A 1 1630 ? 138.824 176.650 146.455 1.00 54.69  ? 1630 TYR A C     1 
ATOM   782   O  O     . TYR A 1 1630 ? 139.392 176.569 147.550 1.00 58.14  ? 1630 TYR A O     1 
ATOM   783   C  CB    . TYR A 1 1630 ? 137.923 174.407 145.804 1.00 45.43  ? 1630 TYR A CB    1 
ATOM   784   C  CG    . TYR A 1 1630 ? 136.833 173.400 146.093 1.00 55.64  ? 1630 TYR A CG    1 
ATOM   785   C  CD1   . TYR A 1 1630 ? 136.411 173.157 147.394 1.00 54.74  ? 1630 TYR A CD1   1 
ATOM   786   C  CD2   . TYR A 1 1630 ? 136.223 172.696 145.065 1.00 58.11  ? 1630 TYR A CD2   1 
ATOM   787   C  CE1   . TYR A 1 1630 ? 135.414 172.238 147.661 1.00 60.44  ? 1630 TYR A CE1   1 
ATOM   788   C  CE2   . TYR A 1 1630 ? 135.226 171.778 145.322 1.00 60.85  ? 1630 TYR A CE2   1 
ATOM   789   C  CZ    . TYR A 1 1630 ? 134.825 171.552 146.621 1.00 66.40  ? 1630 TYR A CZ    1 
ATOM   790   O  OH    . TYR A 1 1630 ? 133.831 170.636 146.880 1.00 66.60  ? 1630 TYR A OH    1 
ATOM   791   N  N     . PHE A 1 1631 ? 139.276 177.432 145.476 1.00 51.52  ? 1631 PHE A N     1 
ATOM   792   C  CA    . PHE A 1 1631 ? 140.517 178.184 145.600 1.00 50.59  ? 1631 PHE A CA    1 
ATOM   793   C  C     . PHE A 1 1631 ? 140.325 179.587 146.160 1.00 57.70  ? 1631 PHE A C     1 
ATOM   794   O  O     . PHE A 1 1631 ? 141.317 180.299 146.349 1.00 54.14  ? 1631 PHE A O     1 
ATOM   795   C  CB    . PHE A 1 1631 ? 141.217 178.284 144.240 1.00 47.38  ? 1631 PHE A CB    1 
ATOM   796   C  CG    . PHE A 1 1631 ? 141.342 176.972 143.522 1.00 48.01  ? 1631 PHE A CG    1 
ATOM   797   C  CD1   . PHE A 1 1631 ? 141.743 175.831 144.196 1.00 46.99  ? 1631 PHE A CD1   1 
ATOM   798   C  CD2   . PHE A 1 1631 ? 141.072 176.884 142.167 1.00 37.80  ? 1631 PHE A CD2   1 
ATOM   799   C  CE1   . PHE A 1 1631 ? 141.863 174.625 143.534 1.00 33.72  ? 1631 PHE A CE1   1 
ATOM   800   C  CE2   . PHE A 1 1631 ? 141.192 175.683 141.500 1.00 32.17  ? 1631 PHE A CE2   1 
ATOM   801   C  CZ    . PHE A 1 1631 ? 141.587 174.552 142.184 1.00 30.99  ? 1631 PHE A CZ    1 
ATOM   802   N  N     . VAL A 1 1632 ? 139.092 180.004 146.429 1.00 65.78  ? 1632 VAL A N     1 
ATOM   803   C  CA    . VAL A 1 1632 ? 138.810 181.358 146.890 1.00 70.73  ? 1632 VAL A CA    1 
ATOM   804   C  C     . VAL A 1 1632 ? 138.525 181.317 148.385 1.00 71.68  ? 1632 VAL A C     1 
ATOM   805   O  O     . VAL A 1 1632 ? 138.001 180.323 148.906 1.00 70.85  ? 1632 VAL A O     1 
ATOM   806   C  CB    . VAL A 1 1632 ? 137.637 181.980 146.103 1.00 69.00  ? 1632 VAL A CB    1 
ATOM   807   C  CG1   . VAL A 1 1632 ? 136.311 181.339 146.485 1.00 68.39  ? 1632 VAL A CG1   1 
ATOM   808   C  CG2   . VAL A 1 1632 ? 137.599 183.485 146.287 1.00 72.47  ? 1632 VAL A CG2   1 
ATOM   809   N  N     . GLY A 1 1633 ? 138.892 182.388 149.083 1.00 73.23  ? 1633 GLY A N     1 
ATOM   810   C  CA    . GLY A 1 1633 ? 138.749 182.429 150.523 1.00 76.01  ? 1633 GLY A CA    1 
ATOM   811   C  C     . GLY A 1 1633 ? 137.302 182.531 150.967 1.00 88.67  ? 1633 GLY A C     1 
ATOM   812   O  O     . GLY A 1 1633 ? 136.388 182.807 150.190 1.00 89.78  ? 1633 GLY A O     1 
ATOM   813   N  N     . ASP A 1 1634 ? 137.099 182.294 152.265 1.00 90.35  ? 1634 ASP A N     1 
ATOM   814   C  CA    . ASP A 1 1634 ? 135.750 182.320 152.822 1.00 88.00  ? 1634 ASP A CA    1 
ATOM   815   C  C     . ASP A 1 1634 ? 135.154 183.722 152.749 1.00 91.68  ? 1634 ASP A C     1 
ATOM   816   O  O     . ASP A 1 1634 ? 134.004 183.901 152.332 1.00 98.49  ? 1634 ASP A O     1 
ATOM   817   C  CB    . ASP A 1 1634 ? 135.772 181.816 154.266 1.00 88.03  ? 1634 ASP A CB    1 
ATOM   818   C  CG    . ASP A 1 1634 ? 135.426 180.343 154.375 1.00 93.22  ? 1634 ASP A CG    1 
ATOM   819   O  OD1   . ASP A 1 1634 ? 135.144 179.718 153.332 1.00 92.57  ? 1634 ASP A OD1   1 
ATOM   820   O  OD2   . ASP A 1 1634 ? 135.432 179.811 155.506 1.00 94.17  ? 1634 ASP A OD2   1 
ATOM   821   N  N     . GLU A 1 1635 ? 135.931 184.733 153.148 1.00 94.32  ? 1635 GLU A N     1 
ATOM   822   C  CA    . GLU A 1 1635 ? 135.464 186.113 153.057 1.00 94.31  ? 1635 GLU A CA    1 
ATOM   823   C  C     . GLU A 1 1635 ? 135.219 186.511 151.608 1.00 93.63  ? 1635 GLU A C     1 
ATOM   824   O  O     . GLU A 1 1635 ? 134.206 187.148 151.285 1.00 97.73  ? 1635 GLU A O     1 
ATOM   825   C  CB    . GLU A 1 1635 ? 136.489 187.051 153.698 1.00 100.58 ? 1635 GLU A CB    1 
ATOM   826   C  CG    . GLU A 1 1635 ? 136.792 186.755 155.158 1.00 106.21 ? 1635 GLU A CG    1 
ATOM   827   C  CD    . GLU A 1 1635 ? 135.648 187.117 156.080 1.00 113.20 ? 1635 GLU A CD    1 
ATOM   828   O  OE1   . GLU A 1 1635 ? 134.942 188.104 155.790 1.00 117.57 ? 1635 GLU A OE1   1 
ATOM   829   O  OE2   . GLU A 1 1635 ? 135.455 186.414 157.095 1.00 105.75 ? 1635 GLU A OE2   1 
ATOM   830   N  N     . ASP A 1 1636 ? 136.140 186.140 150.718 1.00 92.09  ? 1636 ASP A N     1 
ATOM   831   C  CA    . ASP A 1 1636 ? 135.975 186.456 149.307 1.00 96.50  ? 1636 ASP A CA    1 
ATOM   832   C  C     . ASP A 1 1636 ? 134.792 185.713 148.703 1.00 93.18  ? 1636 ASP A C     1 
ATOM   833   O  O     . ASP A 1 1636 ? 134.106 186.254 147.832 1.00 94.59  ? 1636 ASP A O     1 
ATOM   834   C  CB    . ASP A 1 1636 ? 137.260 186.136 148.547 1.00 96.47  ? 1636 ASP A CB    1 
ATOM   835   C  CG    . ASP A 1 1636 ? 138.334 187.185 148.750 1.00 102.21 ? 1636 ASP A CG    1 
ATOM   836   O  OD1   . ASP A 1 1636 ? 138.327 188.198 148.020 1.00 97.32  ? 1636 ASP A OD1   1 
ATOM   837   O  OD2   . ASP A 1 1636 ? 139.187 186.998 149.644 1.00 102.13 ? 1636 ASP A OD2   1 
ATOM   838   N  N     . LEU A 1 1637 ? 134.532 184.481 149.150 1.00 85.69  ? 1637 LEU A N     1 
ATOM   839   C  CA    . LEU A 1 1637 ? 133.346 183.768 148.684 1.00 81.45  ? 1637 LEU A CA    1 
ATOM   840   C  C     . LEU A 1 1637 ? 132.071 184.453 149.166 1.00 91.17  ? 1637 LEU A C     1 
ATOM   841   O  O     . LEU A 1 1637 ? 131.096 184.564 148.411 1.00 96.08  ? 1637 LEU A O     1 
ATOM   842   C  CB    . LEU A 1 1637 ? 133.387 182.314 149.152 1.00 77.34  ? 1637 LEU A CB    1 
ATOM   843   C  CG    . LEU A 1 1637 ? 132.258 181.402 148.666 1.00 77.78  ? 1637 LEU A CG    1 
ATOM   844   C  CD1   . LEU A 1 1637 ? 132.005 181.598 147.180 1.00 76.35  ? 1637 LEU A CD1   1 
ATOM   845   C  CD2   . LEU A 1 1637 ? 132.575 179.949 148.967 1.00 85.18  ? 1637 LEU A CD2   1 
ATOM   846   N  N     . LEU A 1 1638 ? 132.060 184.912 150.422 1.00 95.05  ? 1638 LEU A N     1 
ATOM   847   C  CA    . LEU A 1 1638 ? 130.943 185.709 150.924 1.00 95.12  ? 1638 LEU A CA    1 
ATOM   848   C  C     . LEU A 1 1638 ? 130.700 186.922 150.038 1.00 97.76  ? 1638 LEU A C     1 
ATOM   849   O  O     . LEU A 1 1638 ? 129.559 187.223 149.670 1.00 101.48 ? 1638 LEU A O     1 
ATOM   850   C  CB    . LEU A 1 1638 ? 131.218 186.156 152.363 1.00 102.56 ? 1638 LEU A CB    1 
ATOM   851   C  CG    . LEU A 1 1638 ? 130.669 185.370 153.557 1.00 105.76 ? 1638 LEU A CG    1 
ATOM   852   C  CD1   . LEU A 1 1638 ? 129.163 185.522 153.663 1.00 112.80 ? 1638 LEU A CD1   1 
ATOM   853   C  CD2   . LEU A 1 1638 ? 131.041 183.911 153.466 1.00 91.35  ? 1638 LEU A CD2   1 
ATOM   854   N  N     . GLU A 1 1639 ? 131.772 187.633 149.687 1.00 98.89  ? 1639 GLU A N     1 
ATOM   855   C  CA    . GLU A 1 1639 ? 131.625 188.810 148.836 1.00 97.86  ? 1639 GLU A CA    1 
ATOM   856   C  C     . GLU A 1 1639 ? 131.148 188.440 147.434 1.00 103.50 ? 1639 GLU A C     1 
ATOM   857   O  O     . GLU A 1 1639 ? 130.356 189.178 146.836 1.00 107.65 ? 1639 GLU A O     1 
ATOM   858   C  CB    . GLU A 1 1639 ? 132.944 189.579 148.767 1.00 92.23  ? 1639 GLU A CB    1 
ATOM   859   C  CG    . GLU A 1 1639 ? 132.863 190.877 147.980 1.00 98.94  ? 1639 GLU A CG    1 
ATOM   860   C  CD    . GLU A 1 1639 ? 134.169 191.646 147.988 1.00 101.78 ? 1639 GLU A CD    1 
ATOM   861   O  OE1   . GLU A 1 1639 ? 135.147 191.153 148.588 1.00 105.33 ? 1639 GLU A OE1   1 
ATOM   862   O  OE2   . GLU A 1 1639 ? 134.218 192.745 147.396 1.00 94.49  ? 1639 GLU A OE2   1 
ATOM   863   N  N     . ILE A 1 1640 ? 131.617 187.312 146.895 1.00 103.13 ? 1640 ILE A N     1 
ATOM   864   C  CA    . ILE A 1 1640 ? 131.250 186.917 145.537 1.00 98.33  ? 1640 ILE A CA    1 
ATOM   865   C  C     . ILE A 1 1640 ? 129.773 186.551 145.464 1.00 96.49  ? 1640 ILE A C     1 
ATOM   866   O  O     . ILE A 1 1640 ? 129.044 187.014 144.578 1.00 96.27  ? 1640 ILE A O     1 
ATOM   867   C  CB    . ILE A 1 1640 ? 132.140 185.755 145.059 1.00 92.74  ? 1640 ILE A CB    1 
ATOM   868   C  CG1   . ILE A 1 1640 ? 133.531 186.263 144.677 1.00 82.78  ? 1640 ILE A CG1   1 
ATOM   869   C  CG2   . ILE A 1 1640 ? 131.498 185.032 143.884 1.00 85.94  ? 1640 ILE A CG2   1 
ATOM   870   C  CD1   . ILE A 1 1640 ? 134.547 185.159 144.495 1.00 79.17  ? 1640 ILE A CD1   1 
ATOM   871   N  N     . ILE A 1 1641 ? 129.308 185.711 146.392 1.00 99.48  ? 1641 ILE A N     1 
ATOM   872   C  CA    . ILE A 1 1641 ? 127.916 185.270 146.349 1.00 102.07 ? 1641 ILE A CA    1 
ATOM   873   C  C     . ILE A 1 1641 ? 126.974 186.434 146.631 1.00 108.15 ? 1641 ILE A C     1 
ATOM   874   O  O     . ILE A 1 1641 ? 125.922 186.567 145.994 1.00 109.88 ? 1641 ILE A O     1 
ATOM   875   C  CB    . ILE A 1 1641 ? 127.686 184.105 147.328 1.00 97.28  ? 1641 ILE A CB    1 
ATOM   876   C  CG1   . ILE A 1 1641 ? 128.707 182.994 147.082 1.00 94.03  ? 1641 ILE A CG1   1 
ATOM   877   C  CG2   . ILE A 1 1641 ? 126.271 183.563 147.190 1.00 99.21  ? 1641 ILE A CG2   1 
ATOM   878   C  CD1   . ILE A 1 1641 ? 128.426 182.162 145.852 1.00 90.35  ? 1641 ILE A CD1   1 
ATOM   879   N  N     . GLY A 1 1642 ? 127.332 187.292 147.588 1.00 108.83 ? 1642 GLY A N     1 
ATOM   880   C  CA    . GLY A 1 1642 ? 126.472 188.417 147.917 1.00 111.21 ? 1642 GLY A CA    1 
ATOM   881   C  C     . GLY A 1 1642 ? 126.347 189.419 146.787 1.00 108.47 ? 1642 GLY A C     1 
ATOM   882   O  O     . GLY A 1 1642 ? 125.289 190.023 146.595 1.00 111.18 ? 1642 GLY A O     1 
ATOM   883   N  N     . ASN A 1 1643 ? 127.424 189.612 146.024 1.00 102.82 ? 1643 ASN A N     1 
ATOM   884   C  CA    . ASN A 1 1643 ? 127.445 190.571 144.927 1.00 102.08 ? 1643 ASN A CA    1 
ATOM   885   C  C     . ASN A 1 1643 ? 127.172 189.921 143.576 1.00 104.49 ? 1643 ASN A C     1 
ATOM   886   O  O     . ASN A 1 1643 ? 127.730 190.355 142.560 1.00 107.29 ? 1643 ASN A O     1 
ATOM   887   C  CB    . ASN A 1 1643 ? 128.783 191.309 144.907 1.00 106.95 ? 1643 ASN A CB    1 
ATOM   888   C  CG    . ASN A 1 1643 ? 128.888 192.351 146.002 1.00 107.76 ? 1643 ASN A CG    1 
ATOM   889   O  OD1   . ASN A 1 1643 ? 127.902 192.996 146.358 1.00 106.75 ? 1643 ASN A OD1   1 
ATOM   890   N  ND2   . ASN A 1 1643 ? 130.086 192.512 146.552 1.00 102.85 ? 1643 ASN A ND2   1 
ATOM   891   N  N     . SER A 1 1644 ? 126.339 188.879 143.540 1.00 103.65 ? 1644 SER A N     1 
ATOM   892   C  CA    . SER A 1 1644 ? 125.992 188.256 142.267 1.00 102.07 ? 1644 SER A CA    1 
ATOM   893   C  C     . SER A 1 1644 ? 125.231 189.225 141.371 1.00 100.78 ? 1644 SER A C     1 
ATOM   894   O  O     . SER A 1 1644 ? 125.465 189.275 140.157 1.00 95.47  ? 1644 SER A O     1 
ATOM   895   C  CB    . SER A 1 1644 ? 125.173 186.989 142.509 1.00 97.84  ? 1644 SER A CB    1 
ATOM   896   O  OG    . SER A 1 1644 ? 123.930 187.294 143.116 1.00 101.34 ? 1644 SER A OG    1 
ATOM   897   N  N     . LYS A 1 1645 ? 124.309 189.997 141.950 1.00 102.94 ? 1645 LYS A N     1 
ATOM   898   C  CA    . LYS A 1 1645 ? 123.568 190.982 141.169 1.00 101.46 ? 1645 LYS A CA    1 
ATOM   899   C  C     . LYS A 1 1645 ? 124.483 192.085 140.651 1.00 98.84  ? 1645 LYS A C     1 
ATOM   900   O  O     . LYS A 1 1645 ? 124.351 192.518 139.500 1.00 98.54  ? 1645 LYS A O     1 
ATOM   901   C  CB    . LYS A 1 1645 ? 122.436 191.572 142.009 1.00 99.84  ? 1645 LYS A CB    1 
ATOM   902   C  CG    . LYS A 1 1645 ? 121.467 190.540 142.567 1.00 98.86  ? 1645 LYS A CG    1 
ATOM   903   C  CD    . LYS A 1 1645 ? 121.017 189.562 141.494 1.00 91.64  ? 1645 LYS A CD    1 
ATOM   904   C  CE    . LYS A 1 1645 ? 120.904 188.149 142.044 1.00 88.12  ? 1645 LYS A CE    1 
ATOM   905   N  NZ    . LYS A 1 1645 ? 119.864 188.048 143.105 1.00 90.38  ? 1645 LYS A NZ    1 
ATOM   906   N  N     . ASN A 1 1646 ? 125.414 192.553 141.480 1.00 96.29  ? 1646 ASN A N     1 
ATOM   907   C  CA    . ASN A 1 1646 ? 126.322 193.639 141.111 1.00 95.29  ? 1646 ASN A CA    1 
ATOM   908   C  C     . ASN A 1 1646 ? 127.668 193.022 140.743 1.00 98.52  ? 1646 ASN A C     1 
ATOM   909   O  O     . ASN A 1 1646 ? 128.519 192.777 141.599 1.00 98.82  ? 1646 ASN A O     1 
ATOM   910   C  CB    . ASN A 1 1646 ? 126.450 194.650 142.244 1.00 92.44  ? 1646 ASN A CB    1 
ATOM   911   C  CG    . ASN A 1 1646 ? 127.531 195.679 141.984 1.00 95.53  ? 1646 ASN A CG    1 
ATOM   912   O  OD1   . ASN A 1 1646 ? 128.558 195.701 142.658 1.00 98.59  ? 1646 ASN A OD1   1 
ATOM   913   N  ND2   . ASN A 1 1646 ? 127.300 196.542 141.001 1.00 95.60  ? 1646 ASN A ND2   1 
ATOM   914   N  N     . VAL A 1 1647 ? 127.861 192.787 139.443 1.00 96.14  ? 1647 VAL A N     1 
ATOM   915   C  CA    . VAL A 1 1647 ? 129.070 192.128 138.954 1.00 89.51  ? 1647 VAL A CA    1 
ATOM   916   C  C     . VAL A 1 1647 ? 130.302 192.998 139.186 1.00 87.42  ? 1647 VAL A C     1 
ATOM   917   O  O     . VAL A 1 1647 ? 131.430 192.491 139.247 1.00 87.82  ? 1647 VAL A O     1 
ATOM   918   C  CB    . VAL A 1 1647 ? 128.879 191.766 137.463 1.00 84.28  ? 1647 VAL A CB    1 
ATOM   919   C  CG1   . VAL A 1 1647 ? 130.184 191.321 136.813 1.00 85.30  ? 1647 VAL A CG1   1 
ATOM   920   C  CG2   . VAL A 1 1647 ? 127.812 190.691 137.313 1.00 76.26  ? 1647 VAL A CG2   1 
ATOM   921   N  N     . ALA A 1 1648 ? 130.106 194.308 139.368 1.00 84.60  ? 1648 ALA A N     1 
ATOM   922   C  CA    . ALA A 1 1648 ? 131.223 195.249 139.399 1.00 86.33  ? 1648 ALA A CA    1 
ATOM   923   C  C     . ALA A 1 1648 ? 132.251 194.906 140.473 1.00 86.85  ? 1648 ALA A C     1 
ATOM   924   O  O     . ALA A 1 1648 ? 133.454 195.091 140.254 1.00 84.15  ? 1648 ALA A O     1 
ATOM   925   C  CB    . ALA A 1 1648 ? 130.701 196.670 139.608 1.00 84.36  ? 1648 ALA A CB    1 
ATOM   926   N  N     . LYS A 1 1649 ? 131.812 194.411 141.628 1.00 88.13  ? 1649 LYS A N     1 
ATOM   927   C  CA    . LYS A 1 1649 ? 132.740 194.114 142.714 1.00 87.47  ? 1649 LYS A CA    1 
ATOM   928   C  C     . LYS A 1 1649 ? 133.382 192.737 142.601 1.00 88.12  ? 1649 LYS A C     1 
ATOM   929   O  O     . LYS A 1 1649 ? 134.178 192.373 143.474 1.00 85.35  ? 1649 LYS A O     1 
ATOM   930   C  CB    . LYS A 1 1649 ? 132.037 194.243 144.069 1.00 92.43  ? 1649 LYS A CB    1 
ATOM   931   C  CG    . LYS A 1 1649 ? 131.365 195.587 144.302 1.00 91.02  ? 1649 LYS A CG    1 
ATOM   932   C  CD    . LYS A 1 1649 ? 130.641 195.616 145.640 1.00 98.91  ? 1649 LYS A CD    1 
ATOM   933   C  CE    . LYS A 1 1649 ? 129.409 196.506 145.596 1.00 104.01 ? 1649 LYS A CE    1 
ATOM   934   N  NZ    . LYS A 1 1649 ? 129.262 197.315 146.838 1.00 106.96 ? 1649 LYS A NZ    1 
ATOM   935   N  N     . LEU A 1 1650 ? 133.063 191.966 141.564 1.00 91.20  ? 1650 LEU A N     1 
ATOM   936   C  CA    . LEU A 1 1650 ? 133.670 190.658 141.350 1.00 82.90  ? 1650 LEU A CA    1 
ATOM   937   C  C     . LEU A 1 1650 ? 134.919 190.714 140.480 1.00 73.51  ? 1650 LEU A C     1 
ATOM   938   O  O     . LEU A 1 1650 ? 135.542 189.673 140.251 1.00 69.30  ? 1650 LEU A O     1 
ATOM   939   C  CB    . LEU A 1 1650 ? 132.656 189.697 140.716 1.00 75.19  ? 1650 LEU A CB    1 
ATOM   940   C  CG    . LEU A 1 1650 ? 131.769 188.844 141.628 1.00 77.57  ? 1650 LEU A CG    1 
ATOM   941   C  CD1   . LEU A 1 1650 ? 131.220 189.645 142.798 1.00 89.02  ? 1650 LEU A CD1   1 
ATOM   942   C  CD2   . LEU A 1 1650 ? 130.637 188.216 140.828 1.00 75.49  ? 1650 LEU A CD2   1 
ATOM   943   N  N     . GLN A 1 1651 ? 135.303 191.898 139.995 1.00 73.99  ? 1651 GLN A N     1 
ATOM   944   C  CA    . GLN A 1 1651 ? 136.398 191.990 139.037 1.00 76.28  ? 1651 GLN A CA    1 
ATOM   945   C  C     . GLN A 1 1651 ? 137.763 191.747 139.667 1.00 79.33  ? 1651 GLN A C     1 
ATOM   946   O  O     . GLN A 1 1651 ? 138.730 191.508 138.936 1.00 77.88  ? 1651 GLN A O     1 
ATOM   947   C  CB    . GLN A 1 1651 ? 136.380 193.357 138.349 1.00 80.77  ? 1651 GLN A CB    1 
ATOM   948   C  CG    . GLN A 1 1651 ? 135.052 193.703 137.692 1.00 83.71  ? 1651 GLN A CG    1 
ATOM   949   C  CD    . GLN A 1 1651 ? 134.886 193.065 136.325 1.00 77.35  ? 1651 GLN A CD    1 
ATOM   950   O  OE1   . GLN A 1 1651 ? 135.638 192.165 135.949 1.00 68.94  ? 1651 GLN A OE1   1 
ATOM   951   N  NE2   . GLN A 1 1651 ? 133.896 193.530 135.572 1.00 83.09  ? 1651 GLN A NE2   1 
ATOM   952   N  N     . LYS A 1 1652 ? 137.875 191.810 140.992 1.00 78.79  ? 1652 LYS A N     1 
ATOM   953   C  CA    . LYS A 1 1652 ? 139.133 191.534 141.670 1.00 69.45  ? 1652 LYS A CA    1 
ATOM   954   C  C     . LYS A 1 1652 ? 139.193 190.123 142.238 1.00 67.11  ? 1652 LYS A C     1 
ATOM   955   O  O     . LYS A 1 1652 ? 140.145 189.792 142.952 1.00 68.95  ? 1652 LYS A O     1 
ATOM   956   C  CB    . LYS A 1 1652 ? 139.377 192.557 142.783 1.00 68.34  ? 1652 LYS A CB    1 
ATOM   957   C  CG    . LYS A 1 1652 ? 138.410 192.461 143.949 1.00 71.74  ? 1652 LYS A CG    1 
ATOM   958   C  CD    . LYS A 1 1652 ? 138.777 193.454 145.039 1.00 72.07  ? 1652 LYS A CD    1 
ATOM   959   C  CE    . LYS A 1 1652 ? 137.856 193.327 146.239 1.00 74.07  ? 1652 LYS A CE    1 
ATOM   960   N  NZ    . LYS A 1 1652 ? 138.209 194.302 147.308 1.00 71.29  ? 1652 LYS A NZ    1 
ATOM   961   N  N     . HIS A 1 1653 ? 138.200 189.284 141.938 1.00 67.81  ? 1653 HIS A N     1 
ATOM   962   C  CA    . HIS A 1 1653 ? 138.156 187.921 142.445 1.00 68.19  ? 1653 HIS A CA    1 
ATOM   963   C  C     . HIS A 1 1653 ? 138.411 186.860 141.386 1.00 64.17  ? 1653 HIS A C     1 
ATOM   964   O  O     . HIS A 1 1653 ? 138.627 185.698 141.743 1.00 66.83  ? 1653 HIS A O     1 
ATOM   965   C  CB    . HIS A 1 1653 ? 136.797 187.643 143.104 1.00 70.88  ? 1653 HIS A CB    1 
ATOM   966   C  CG    . HIS A 1 1653 ? 136.565 188.422 144.361 1.00 84.66  ? 1653 HIS A CG    1 
ATOM   967   N  ND1   . HIS A 1 1653 ? 136.426 189.793 144.373 1.00 82.41  ? 1653 HIS A ND1   1 
ATOM   968   C  CD2   . HIS A 1 1653 ? 136.445 188.021 145.649 1.00 87.85  ? 1653 HIS A CD2   1 
ATOM   969   C  CE1   . HIS A 1 1653 ? 136.233 190.203 145.613 1.00 81.64  ? 1653 HIS A CE1   1 
ATOM   970   N  NE2   . HIS A 1 1653 ? 136.240 189.148 146.407 1.00 87.76  ? 1653 HIS A NE2   1 
ATOM   971   N  N     . PHE A 1 1654 ? 138.389 187.223 140.101 1.00 62.12  ? 1654 PHE A N     1 
ATOM   972   C  CA    . PHE A 1 1654 ? 138.628 186.244 139.049 1.00 52.27  ? 1654 PHE A CA    1 
ATOM   973   C  C     . PHE A 1 1654 ? 140.086 185.814 138.978 1.00 51.47  ? 1654 PHE A C     1 
ATOM   974   O  O     . PHE A 1 1654 ? 140.378 184.739 138.443 1.00 53.49  ? 1654 PHE A O     1 
ATOM   975   C  CB    . PHE A 1 1654 ? 138.180 186.804 137.699 1.00 52.17  ? 1654 PHE A CB    1 
ATOM   976   C  CG    . PHE A 1 1654 ? 136.691 186.876 137.541 1.00 53.56  ? 1654 PHE A CG    1 
ATOM   977   C  CD1   . PHE A 1 1654 ? 135.941 185.721 137.402 1.00 53.28  ? 1654 PHE A CD1   1 
ATOM   978   C  CD2   . PHE A 1 1654 ? 136.039 188.096 137.537 1.00 58.28  ? 1654 PHE A CD2   1 
ATOM   979   C  CE1   . PHE A 1 1654 ? 134.570 185.782 137.259 1.00 53.38  ? 1654 PHE A CE1   1 
ATOM   980   C  CE2   . PHE A 1 1654 ? 134.668 188.163 137.395 1.00 61.49  ? 1654 PHE A CE2   1 
ATOM   981   C  CZ    . PHE A 1 1654 ? 133.933 187.004 137.256 1.00 56.28  ? 1654 PHE A CZ    1 
ATOM   982   N  N     . LYS A 1 1655 ? 141.006 186.621 139.509 1.00 50.88  ? 1655 LYS A N     1 
ATOM   983   C  CA    . LYS A 1 1655 ? 142.417 186.254 139.512 1.00 52.83  ? 1655 LYS A CA    1 
ATOM   984   C  C     . LYS A 1 1655 ? 142.719 185.100 140.457 1.00 49.79  ? 1655 LYS A C     1 
ATOM   985   O  O     . LYS A 1 1655 ? 143.829 184.560 140.414 1.00 50.04  ? 1655 LYS A O     1 
ATOM   986   C  CB    . LYS A 1 1655 ? 143.273 187.466 139.886 1.00 56.07  ? 1655 LYS A CB    1 
ATOM   987   C  CG    . LYS A 1 1655 ? 143.380 187.715 141.381 1.00 58.47  ? 1655 LYS A CG    1 
ATOM   988   C  CD    . LYS A 1 1655 ? 144.216 188.949 141.677 1.00 54.38  ? 1655 LYS A CD    1 
ATOM   989   C  CE    . LYS A 1 1655 ? 143.980 189.446 143.093 1.00 58.64  ? 1655 LYS A CE    1 
ATOM   990   N  NZ    . LYS A 1 1655 ? 144.150 190.921 143.201 1.00 51.20  ? 1655 LYS A NZ    1 
ATOM   991   N  N     . LYS A 1 1656 ? 141.765 184.715 141.302 1.00 46.81  ? 1656 LYS A N     1 
ATOM   992   C  CA    . LYS A 1 1656 ? 141.930 183.602 142.226 1.00 46.27  ? 1656 LYS A CA    1 
ATOM   993   C  C     . LYS A 1 1656 ? 141.421 182.283 141.668 1.00 42.70  ? 1656 LYS A C     1 
ATOM   994   O  O     . LYS A 1 1656 ? 141.977 181.229 141.993 1.00 46.27  ? 1656 LYS A O     1 
ATOM   995   C  CB    . LYS A 1 1656 ? 141.200 183.903 143.538 1.00 50.66  ? 1656 LYS A CB    1 
ATOM   996   C  CG    . LYS A 1 1656 ? 141.995 184.751 144.512 1.00 54.45  ? 1656 LYS A CG    1 
ATOM   997   C  CD    . LYS A 1 1656 ? 141.340 184.769 145.879 1.00 58.60  ? 1656 LYS A CD    1 
ATOM   998   C  CE    . LYS A 1 1656 ? 142.061 183.862 146.855 1.00 50.85  ? 1656 LYS A CE    1 
ATOM   999   N  NZ    . LYS A 1 1656 ? 141.960 184.388 148.241 1.00 51.23  ? 1656 LYS A NZ    1 
ATOM   1000  N  N     . MET A 1 1657 ? 140.381 182.320 140.837 1.00 40.99  ? 1657 MET A N     1 
ATOM   1001  C  CA    . MET A 1 1657 ? 139.771 181.118 140.289 1.00 39.77  ? 1657 MET A CA    1 
ATOM   1002  C  C     . MET A 1 1657 ? 140.306 180.745 138.914 1.00 42.08  ? 1657 MET A C     1 
ATOM   1003  O  O     . MET A 1 1657 ? 140.126 179.599 138.488 1.00 44.99  ? 1657 MET A O     1 
ATOM   1004  C  CB    . MET A 1 1657 ? 138.253 181.299 140.203 1.00 44.75  ? 1657 MET A CB    1 
ATOM   1005  C  CG    . MET A 1 1657 ? 137.564 181.414 141.549 1.00 57.68  ? 1657 MET A CG    1 
ATOM   1006  S  SD    . MET A 1 1657 ? 135.778 181.564 141.383 1.00 76.19  ? 1657 MET A SD    1 
ATOM   1007  C  CE    . MET A 1 1657 ? 135.636 183.251 140.800 1.00 57.43  ? 1657 MET A CE    1 
ATOM   1008  N  N     . PHE A 1 1658 ? 140.952 181.672 138.214 1.00 42.69  ? 1658 PHE A N     1 
ATOM   1009  C  CA    . PHE A 1 1658 ? 141.430 181.443 136.861 1.00 35.33  ? 1658 PHE A CA    1 
ATOM   1010  C  C     . PHE A 1 1658 ? 142.931 181.694 136.791 1.00 34.70  ? 1658 PHE A C     1 
ATOM   1011  O  O     . PHE A 1 1658 ? 143.497 182.439 137.595 1.00 34.50  ? 1658 PHE A O     1 
ATOM   1012  C  CB    . PHE A 1 1658 ? 140.702 182.341 135.852 1.00 35.86  ? 1658 PHE A CB    1 
ATOM   1013  C  CG    . PHE A 1 1658 ? 139.259 181.975 135.638 1.00 38.04  ? 1658 PHE A CG    1 
ATOM   1014  C  CD1   . PHE A 1 1658 ? 138.310 182.239 136.611 1.00 36.82  ? 1658 PHE A CD1   1 
ATOM   1015  C  CD2   . PHE A 1 1658 ? 138.852 181.372 134.461 1.00 41.36  ? 1658 PHE A CD2   1 
ATOM   1016  C  CE1   . PHE A 1 1658 ? 136.984 181.905 136.416 1.00 35.14  ? 1658 PHE A CE1   1 
ATOM   1017  C  CE2   . PHE A 1 1658 ? 137.526 181.036 134.260 1.00 36.32  ? 1658 PHE A CE2   1 
ATOM   1018  C  CZ    . PHE A 1 1658 ? 136.592 181.303 135.239 1.00 33.31  ? 1658 PHE A CZ    1 
ATOM   1019  N  N     . ALA A 1 1659 ? 143.573 181.053 135.813 1.00 32.51  ? 1659 ALA A N     1 
ATOM   1020  C  CA    . ALA A 1 1659 ? 145.021 181.169 135.674 1.00 33.48  ? 1659 ALA A CA    1 
ATOM   1021  C  C     . ALA A 1 1659 ? 145.430 182.573 135.248 1.00 39.19  ? 1659 ALA A C     1 
ATOM   1022  O  O     . ALA A 1 1659 ? 146.359 183.159 135.816 1.00 52.54  ? 1659 ALA A O     1 
ATOM   1023  C  CB    . ALA A 1 1659 ? 145.537 180.133 134.677 1.00 31.89  ? 1659 ALA A CB    1 
ATOM   1024  N  N     . GLY A 1 1660 ? 144.751 183.131 134.249 1.00 35.21  ? 1660 GLY A N     1 
ATOM   1025  C  CA    . GLY A 1 1660 ? 145.135 184.426 133.724 1.00 32.61  ? 1660 GLY A CA    1 
ATOM   1026  C  C     . GLY A 1 1660 ? 143.995 185.410 133.576 1.00 34.34  ? 1660 GLY A C     1 
ATOM   1027  O  O     . GLY A 1 1660 ? 144.213 186.559 133.182 1.00 46.58  ? 1660 GLY A O     1 
ATOM   1028  N  N     . VAL A 1 1661 ? 142.774 184.979 133.885 1.00 34.58  ? 1661 VAL A N     1 
ATOM   1029  C  CA    . VAL A 1 1661 ? 141.596 185.835 133.764 1.00 35.29  ? 1661 VAL A CA    1 
ATOM   1030  C  C     . VAL A 1 1661 ? 141.504 186.671 135.037 1.00 40.31  ? 1661 VAL A C     1 
ATOM   1031  O  O     . VAL A 1 1661 ? 141.040 186.194 136.073 1.00 44.08  ? 1661 VAL A O     1 
ATOM   1032  C  CB    . VAL A 1 1661 ? 140.320 185.023 133.530 1.00 37.08  ? 1661 VAL A CB    1 
ATOM   1033  C  CG1   . VAL A 1 1661 ? 139.117 185.947 133.414 1.00 39.81  ? 1661 VAL A CG1   1 
ATOM   1034  C  CG2   . VAL A 1 1661 ? 140.462 184.156 132.292 1.00 38.17  ? 1661 VAL A CG2   1 
ATOM   1035  N  N     . SER A 1 1662 ? 141.953 187.925 134.966 1.00 41.29  ? 1662 SER A N     1 
ATOM   1036  C  CA    . SER A 1 1662 ? 141.836 188.811 136.118 1.00 45.75  ? 1662 SER A CA    1 
ATOM   1037  C  C     . SER A 1 1662 ? 140.461 189.464 136.181 1.00 52.76  ? 1662 SER A C     1 
ATOM   1038  O  O     . SER A 1 1662 ? 139.902 189.633 137.269 1.00 58.50  ? 1662 SER A O     1 
ATOM   1039  C  CB    . SER A 1 1662 ? 142.926 189.881 136.078 1.00 42.40  ? 1662 SER A CB    1 
ATOM   1040  O  OG    . SER A 1 1662 ? 143.019 190.456 134.789 1.00 44.21  ? 1662 SER A OG    1 
ATOM   1041  N  N     . SER A 1 1663 ? 139.902 189.830 135.030 1.00 49.68  ? 1663 SER A N     1 
ATOM   1042  C  CA    . SER A 1 1663 ? 138.611 190.498 134.984 1.00 47.88  ? 1663 SER A CA    1 
ATOM   1043  C  C     . SER A 1 1663 ? 137.870 190.068 133.727 1.00 46.84  ? 1663 SER A C     1 
ATOM   1044  O  O     . SER A 1 1663 ? 138.466 189.571 132.769 1.00 52.61  ? 1663 SER A O     1 
ATOM   1045  C  CB    . SER A 1 1663 ? 138.764 192.023 135.017 1.00 50.12  ? 1663 SER A CB    1 
ATOM   1046  O  OG    . SER A 1 1663 ? 139.471 192.489 133.881 1.00 45.77  ? 1663 SER A OG    1 
ATOM   1047  N  N     . ILE A 1 1664 ? 136.557 190.266 133.746 1.00 49.68  ? 1664 ILE A N     1 
ATOM   1048  C  CA    . ILE A 1 1664 ? 135.699 189.931 132.620 1.00 49.69  ? 1664 ILE A CA    1 
ATOM   1049  C  C     . ILE A 1 1664 ? 135.173 191.219 131.998 1.00 51.49  ? 1664 ILE A C     1 
ATOM   1050  O  O     . ILE A 1 1664 ? 135.056 192.259 132.652 1.00 56.10  ? 1664 ILE A O     1 
ATOM   1051  C  CB    . ILE A 1 1664 ? 134.541 189.000 133.033 1.00 49.31  ? 1664 ILE A CB    1 
ATOM   1052  C  CG1   . ILE A 1 1664 ? 133.725 189.629 134.161 1.00 50.25  ? 1664 ILE A CG1   1 
ATOM   1053  C  CG2   . ILE A 1 1664 ? 135.073 187.641 133.452 1.00 49.88  ? 1664 ILE A CG2   1 
ATOM   1054  C  CD1   . ILE A 1 1664 ? 132.520 188.813 134.566 1.00 51.43  ? 1664 ILE A CD1   1 
ATOM   1055  N  N     . ILE A 1 1665 ? 134.854 191.139 130.709 1.00 50.70  ? 1665 ILE A N     1 
ATOM   1056  C  CA    . ILE A 1 1665 ? 134.444 192.294 129.917 1.00 52.91  ? 1665 ILE A CA    1 
ATOM   1057  C  C     . ILE A 1 1665 ? 132.944 192.203 129.678 1.00 61.54  ? 1665 ILE A C     1 
ATOM   1058  O  O     . ILE A 1 1665 ? 132.450 191.198 129.152 1.00 62.55  ? 1665 ILE A O     1 
ATOM   1059  C  CB    . ILE A 1 1665 ? 135.207 192.366 128.587 1.00 54.99  ? 1665 ILE A CB    1 
ATOM   1060  C  CG1   . ILE A 1 1665 ? 136.703 192.554 128.840 1.00 50.83  ? 1665 ILE A CG1   1 
ATOM   1061  C  CG2   . ILE A 1 1665 ? 134.664 193.493 127.723 1.00 60.60  ? 1665 ILE A CG2   1 
ATOM   1062  C  CD1   . ILE A 1 1665 ? 137.550 192.377 127.605 1.00 52.43  ? 1665 ILE A CD1   1 
ATOM   1063  N  N     . LEU A 1 1666 ? 132.221 193.253 130.060 1.00 67.64  ? 1666 LEU A N     1 
ATOM   1064  C  CA    . LEU A 1 1666 ? 130.781 193.327 129.868 1.00 70.12  ? 1666 LEU A CA    1 
ATOM   1065  C  C     . LEU A 1 1666 ? 130.430 194.619 129.145 1.00 73.95  ? 1666 LEU A C     1 
ATOM   1066  O  O     . LEU A 1 1666 ? 131.239 195.545 129.052 1.00 75.69  ? 1666 LEU A O     1 
ATOM   1067  C  CB    . LEU A 1 1666 ? 130.015 193.258 131.200 1.00 68.74  ? 1666 LEU A CB    1 
ATOM   1068  C  CG    . LEU A 1 1666 ? 129.844 191.898 131.884 1.00 68.12  ? 1666 LEU A CG    1 
ATOM   1069  C  CD1   . LEU A 1 1666 ? 131.151 191.411 132.469 1.00 67.99  ? 1666 LEU A CD1   1 
ATOM   1070  C  CD2   . LEU A 1 1666 ? 128.774 191.967 132.960 1.00 78.92  ? 1666 LEU A CD2   1 
ATOM   1071  N  N     . ASN A 1 1667 ? 129.205 194.668 128.631 1.00 73.88  ? 1667 ASN A N     1 
ATOM   1072  C  CA    . ASN A 1 1667 ? 128.700 195.860 127.971 1.00 79.20  ? 1667 ASN A CA    1 
ATOM   1073  C  C     . ASN A 1 1667 ? 128.309 196.908 129.012 1.00 89.60  ? 1667 ASN A C     1 
ATOM   1074  O  O     . ASN A 1 1667 ? 128.459 196.711 130.222 1.00 91.74  ? 1667 ASN A O     1 
ATOM   1075  C  CB    . ASN A 1 1667 ? 127.518 195.507 127.072 1.00 73.45  ? 1667 ASN A CB    1 
ATOM   1076  C  CG    . ASN A 1 1667 ? 126.418 194.781 127.819 1.00 78.68  ? 1667 ASN A CG    1 
ATOM   1077  O  OD1   . ASN A 1 1667 ? 126.655 194.188 128.871 1.00 74.67  ? 1667 ASN A OD1   1 
ATOM   1078  N  ND2   . ASN A 1 1667 ? 125.207 194.821 127.276 1.00 85.81  ? 1667 ASN A ND2   1 
ATOM   1079  N  N     . GLU A 1 1668 ? 127.801 198.047 128.534 1.00 91.82  ? 1668 GLU A N     1 
ATOM   1080  C  CA    . GLU A 1 1668 ? 127.373 199.102 129.446 1.00 92.76  ? 1668 GLU A CA    1 
ATOM   1081  C  C     . GLU A 1 1668 ? 126.194 198.659 130.304 1.00 93.02  ? 1668 GLU A C     1 
ATOM   1082  O  O     . GLU A 1 1668 ? 126.023 199.150 131.426 1.00 91.50  ? 1668 GLU A O     1 
ATOM   1083  C  CB    . GLU A 1 1668 ? 127.022 200.366 128.658 1.00 96.98  ? 1668 GLU A CB    1 
ATOM   1084  C  CG    . GLU A 1 1668 ? 125.834 200.212 127.723 1.00 106.56 ? 1668 GLU A CG    1 
ATOM   1085  C  CD    . GLU A 1 1668 ? 125.565 201.464 126.911 1.00 117.19 ? 1668 GLU A CD    1 
ATOM   1086  O  OE1   . GLU A 1 1668 ? 126.318 202.448 127.067 1.00 115.40 ? 1668 GLU A OE1   1 
ATOM   1087  O  OE2   . GLU A 1 1668 ? 124.601 201.464 126.117 1.00 125.74 ? 1668 GLU A OE2   1 
ATOM   1088  N  N     . ASP A 1 1669 ? 125.376 197.736 129.798 1.00 88.99  ? 1669 ASP A N     1 
ATOM   1089  C  CA    . ASP A 1 1669 ? 124.241 197.211 130.545 1.00 85.56  ? 1669 ASP A CA    1 
ATOM   1090  C  C     . ASP A 1 1669 ? 124.674 196.248 131.645 1.00 85.85  ? 1669 ASP A C     1 
ATOM   1091  O  O     . ASP A 1 1669 ? 123.924 196.053 132.608 1.00 85.06  ? 1669 ASP A O     1 
ATOM   1092  C  CB    . ASP A 1 1669 ? 123.275 196.518 129.572 1.00 83.11  ? 1669 ASP A CB    1 
ATOM   1093  C  CG    . ASP A 1 1669 ? 121.865 196.356 130.132 1.00 95.35  ? 1669 ASP A CG    1 
ATOM   1094  O  OD1   . ASP A 1 1669 ? 121.686 196.250 131.361 1.00 91.60  ? 1669 ASP A OD1   1 
ATOM   1095  O  OD2   . ASP A 1 1669 ? 120.917 196.337 129.318 1.00 101.48 ? 1669 ASP A OD2   1 
ATOM   1096  N  N     . ASN A 1 1670 ? 125.876 195.675 131.540 1.00 84.63  ? 1670 ASN A N     1 
ATOM   1097  C  CA    . ASN A 1 1670 ? 126.366 194.668 132.484 1.00 77.22  ? 1670 ASN A CA    1 
ATOM   1098  C  C     . ASN A 1 1670 ? 125.429 193.464 132.541 1.00 70.74  ? 1670 ASN A C     1 
ATOM   1099  O  O     . ASN A 1 1670 ? 125.167 192.905 133.608 1.00 63.34  ? 1670 ASN A O     1 
ATOM   1100  C  CB    . ASN A 1 1670 ? 126.578 195.261 133.880 1.00 75.33  ? 1670 ASN A CB    1 
ATOM   1101  C  CG    . ASN A 1 1670 ? 127.823 196.120 133.966 1.00 76.30  ? 1670 ASN A CG    1 
ATOM   1102  O  OD1   . ASN A 1 1670 ? 128.587 196.226 133.008 1.00 75.31  ? 1670 ASN A OD1   1 
ATOM   1103  N  ND2   . ASN A 1 1670 ? 128.036 196.739 135.122 1.00 76.77  ? 1670 ASN A ND2   1 
ATOM   1104  N  N     . SER A 1 1671 ? 124.921 193.060 131.376 1.00 72.29  ? 1671 SER A N     1 
ATOM   1105  C  CA    . SER A 1 1671 ? 124.028 191.916 131.278 1.00 74.39  ? 1671 SER A CA    1 
ATOM   1106  C  C     . SER A 1 1671 ? 124.566 190.789 130.409 1.00 75.03  ? 1671 SER A C     1 
ATOM   1107  O  O     . SER A 1 1671 ? 123.996 189.693 130.438 1.00 77.17  ? 1671 SER A O     1 
ATOM   1108  C  CB    . SER A 1 1671 ? 122.659 192.350 130.732 1.00 83.41  ? 1671 SER A CB    1 
ATOM   1109  O  OG    . SER A 1 1671 ? 122.648 192.342 129.315 1.00 84.99  ? 1671 SER A OG    1 
ATOM   1110  N  N     . VAL A 1 1672 ? 125.628 191.016 129.643 1.00 72.39  ? 1672 VAL A N     1 
ATOM   1111  C  CA    . VAL A 1 1672 ? 126.228 189.989 128.800 1.00 69.33  ? 1672 VAL A CA    1 
ATOM   1112  C  C     . VAL A 1 1672 ? 127.742 190.081 128.935 1.00 68.38  ? 1672 VAL A C     1 
ATOM   1113  O  O     . VAL A 1 1672 ? 128.309 191.179 128.974 1.00 70.45  ? 1672 VAL A O     1 
ATOM   1114  C  CB    . VAL A 1 1672 ? 125.776 190.127 127.328 1.00 64.56  ? 1672 VAL A CB    1 
ATOM   1115  C  CG1   . VAL A 1 1672 ? 126.189 191.473 126.751 1.00 63.63  ? 1672 VAL A CG1   1 
ATOM   1116  C  CG2   . VAL A 1 1672 ? 126.323 188.987 126.488 1.00 66.75  ? 1672 VAL A CG2   1 
ATOM   1117  N  N     . VAL A 1 1673 ? 128.396 188.926 129.035 1.00 65.88  ? 1673 VAL A N     1 
ATOM   1118  C  CA    . VAL A 1 1673 ? 129.847 188.860 129.181 1.00 61.78  ? 1673 VAL A CA    1 
ATOM   1119  C  C     . VAL A 1 1673 ? 130.438 188.817 127.776 1.00 60.91  ? 1673 VAL A C     1 
ATOM   1120  O  O     . VAL A 1 1673 ? 130.399 187.787 127.101 1.00 58.41  ? 1673 VAL A O     1 
ATOM   1121  C  CB    . VAL A 1 1673 ? 130.281 187.656 130.018 1.00 60.17  ? 1673 VAL A CB    1 
ATOM   1122  C  CG1   . VAL A 1 1673 ? 131.798 187.570 130.071 1.00 54.35  ? 1673 VAL A CG1   1 
ATOM   1123  C  CG2   . VAL A 1 1673 ? 129.699 187.747 131.419 1.00 63.07  ? 1673 VAL A CG2   1 
ATOM   1124  N  N     . LEU A 1 1674 ? 130.990 189.948 127.332 1.00 63.16  ? 1674 LEU A N     1 
ATOM   1125  C  CA    . LEU A 1 1674 ? 131.566 190.010 125.992 1.00 62.44  ? 1674 LEU A CA    1 
ATOM   1126  C  C     . LEU A 1 1674 ? 132.875 189.235 125.913 1.00 57.91  ? 1674 LEU A C     1 
ATOM   1127  O  O     . LEU A 1 1674 ? 133.168 188.605 124.890 1.00 57.58  ? 1674 LEU A O     1 
ATOM   1128  C  CB    . LEU A 1 1674 ? 131.775 191.466 125.579 1.00 64.37  ? 1674 LEU A CB    1 
ATOM   1129  C  CG    . LEU A 1 1674 ? 130.510 192.318 125.469 1.00 63.99  ? 1674 LEU A CG    1 
ATOM   1130  C  CD1   . LEU A 1 1674 ? 130.850 193.732 125.025 1.00 66.85  ? 1674 LEU A CD1   1 
ATOM   1131  C  CD2   . LEU A 1 1674 ? 129.518 191.677 124.512 1.00 58.11  ? 1674 LEU A CD2   1 
ATOM   1132  N  N     . GLY A 1 1675 ? 133.671 189.268 126.973 1.00 55.66  ? 1675 GLY A N     1 
ATOM   1133  C  CA    . GLY A 1 1675 ? 134.943 188.579 126.946 1.00 49.06  ? 1675 GLY A CA    1 
ATOM   1134  C  C     . GLY A 1 1675 ? 135.637 188.640 128.288 1.00 49.54  ? 1675 GLY A C     1 
ATOM   1135  O  O     . GLY A 1 1675 ? 135.041 188.997 129.305 1.00 57.42  ? 1675 GLY A O     1 
ATOM   1136  N  N     . ILE A 1 1676 ? 136.921 188.281 128.269 1.00 43.79  ? 1676 ILE A N     1 
ATOM   1137  C  CA    . ILE A 1 1676 ? 137.753 188.232 129.461 1.00 38.32  ? 1676 ILE A CA    1 
ATOM   1138  C  C     . ILE A 1 1676 ? 139.033 189.010 129.193 1.00 40.10  ? 1676 ILE A C     1 
ATOM   1139  O  O     . ILE A 1 1676 ? 139.421 189.239 128.046 1.00 47.06  ? 1676 ILE A O     1 
ATOM   1140  C  CB    . ILE A 1 1676 ? 138.084 186.785 129.880 1.00 39.37  ? 1676 ILE A CB    1 
ATOM   1141  C  CG1   . ILE A 1 1676 ? 138.578 185.992 128.669 1.00 43.26  ? 1676 ILE A CG1   1 
ATOM   1142  C  CG2   . ILE A 1 1676 ? 136.867 186.119 130.498 1.00 43.11  ? 1676 ILE A CG2   1 
ATOM   1143  C  CD1   . ILE A 1 1676 ? 139.032 184.596 128.997 1.00 33.67  ? 1676 ILE A CD1   1 
ATOM   1144  N  N     . SER A 1 1677 ? 139.693 189.417 130.276 1.00 38.15  ? 1677 SER A N     1 
ATOM   1145  C  CA    . SER A 1 1677 ? 140.912 190.206 130.185 1.00 36.68  ? 1677 SER A CA    1 
ATOM   1146  C  C     . SER A 1 1677 ? 141.953 189.657 131.149 1.00 37.72  ? 1677 SER A C     1 
ATOM   1147  O  O     . SER A 1 1677 ? 141.619 189.045 132.167 1.00 39.29  ? 1677 SER A O     1 
ATOM   1148  C  CB    . SER A 1 1677 ? 140.649 191.686 130.488 1.00 41.49  ? 1677 SER A CB    1 
ATOM   1149  O  OG    . SER A 1 1677 ? 141.859 192.422 130.526 1.00 46.59  ? 1677 SER A OG    1 
ATOM   1150  N  N     . SER A 1 1678 ? 143.219 189.882 130.816 1.00 40.50  ? 1678 SER A N     1 
ATOM   1151  C  CA    . SER A 1 1678 ? 144.339 189.464 131.644 1.00 38.01  ? 1678 SER A CA    1 
ATOM   1152  C  C     . SER A 1 1678 ? 144.852 190.635 132.476 1.00 47.23  ? 1678 SER A C     1 
ATOM   1153  O  O     . SER A 1 1678 ? 144.417 191.779 132.325 1.00 52.71  ? 1678 SER A O     1 
ATOM   1154  C  CB    . SER A 1 1678 ? 145.466 188.890 130.779 1.00 39.33  ? 1678 SER A CB    1 
ATOM   1155  O  OG    . SER A 1 1678 ? 146.136 189.916 130.070 1.00 46.72  ? 1678 SER A OG    1 
ATOM   1156  N  N     . ARG A 1 1679 ? 145.789 190.327 133.376 1.00 48.91  ? 1679 ARG A N     1 
ATOM   1157  C  CA    . ARG A 1 1679 ? 146.346 191.359 134.245 1.00 49.88  ? 1679 ARG A CA    1 
ATOM   1158  C  C     . ARG A 1 1679 ? 147.109 192.405 133.444 1.00 53.83  ? 1679 ARG A C     1 
ATOM   1159  O  O     . ARG A 1 1679 ? 147.034 193.603 133.741 1.00 56.10  ? 1679 ARG A O     1 
ATOM   1160  C  CB    . ARG A 1 1679 ? 147.252 190.724 135.300 1.00 49.29  ? 1679 ARG A CB    1 
ATOM   1161  C  CG    . ARG A 1 1679 ? 147.800 191.710 136.318 1.00 58.55  ? 1679 ARG A CG    1 
ATOM   1162  C  CD    . ARG A 1 1679 ? 148.895 191.085 137.167 1.00 67.11  ? 1679 ARG A CD    1 
ATOM   1163  N  NE    . ARG A 1 1679 ? 150.181 191.075 136.480 1.00 72.28  ? 1679 ARG A NE    1 
ATOM   1164  C  CZ    . ARG A 1 1679 ? 151.252 190.417 136.903 1.00 81.00  ? 1679 ARG A CZ    1 
ATOM   1165  N  NH1   . ARG A 1 1679 ? 151.227 189.699 138.014 1.00 77.89  ? 1679 ARG A NH1   1 
ATOM   1166  N  NH2   . ARG A 1 1679 ? 152.375 190.481 136.194 1.00 83.63  ? 1679 ARG A NH2   1 
ATOM   1167  N  N     . GLU A 1 1680 ? 147.848 191.972 132.421 1.00 54.69  ? 1680 GLU A N     1 
ATOM   1168  C  CA    . GLU A 1 1680 ? 148.619 192.892 131.594 1.00 52.96  ? 1680 GLU A CA    1 
ATOM   1169  C  C     . GLU A 1 1680 ? 147.746 193.751 130.690 1.00 52.29  ? 1680 GLU A C     1 
ATOM   1170  O  O     . GLU A 1 1680 ? 148.262 194.687 130.070 1.00 60.04  ? 1680 GLU A O     1 
ATOM   1171  C  CB    . GLU A 1 1680 ? 149.627 192.114 130.746 1.00 53.21  ? 1680 GLU A CB    1 
ATOM   1172  C  CG    . GLU A 1 1680 ? 150.750 191.474 131.546 1.00 58.51  ? 1680 GLU A CG    1 
ATOM   1173  C  CD    . GLU A 1 1680 ? 150.377 190.108 132.089 1.00 56.61  ? 1680 GLU A CD    1 
ATOM   1174  O  OE1   . GLU A 1 1680 ? 149.239 189.658 131.839 1.00 52.96  ? 1680 GLU A OE1   1 
ATOM   1175  O  OE2   . GLU A 1 1680 ? 151.221 189.486 132.767 1.00 51.73  ? 1680 GLU A OE2   1 
ATOM   1176  N  N     . GLY A 1 1681 ? 146.450 193.463 130.600 1.00 46.56  ? 1681 GLY A N     1 
ATOM   1177  C  CA    . GLY A 1 1681 ? 145.550 194.186 129.730 1.00 50.16  ? 1681 GLY A CA    1 
ATOM   1178  C  C     . GLY A 1 1681 ? 145.145 193.442 128.477 1.00 49.55  ? 1681 GLY A C     1 
ATOM   1179  O  O     . GLY A 1 1681 ? 144.187 193.859 127.813 1.00 56.34  ? 1681 GLY A O     1 
ATOM   1180  N  N     . GLU A 1 1682 ? 145.844 192.363 128.131 1.00 44.66  ? 1682 GLU A N     1 
ATOM   1181  C  CA    . GLU A 1 1682 ? 145.449 191.548 126.991 1.00 44.66  ? 1682 GLU A CA    1 
ATOM   1182  C  C     . GLU A 1 1682 ? 144.084 190.923 127.246 1.00 42.15  ? 1682 GLU A C     1 
ATOM   1183  O  O     . GLU A 1 1682 ? 143.818 190.408 128.335 1.00 45.55  ? 1682 GLU A O     1 
ATOM   1184  C  CB    . GLU A 1 1682 ? 146.494 190.464 126.733 1.00 49.28  ? 1682 GLU A CB    1 
ATOM   1185  C  CG    . GLU A 1 1682 ? 146.261 189.660 125.468 1.00 43.55  ? 1682 GLU A CG    1 
ATOM   1186  C  CD    . GLU A 1 1682 ? 147.128 188.421 125.403 1.00 41.90  ? 1682 GLU A CD    1 
ATOM   1187  O  OE1   . GLU A 1 1682 ? 146.853 187.462 126.154 1.00 42.52  ? 1682 GLU A OE1   1 
ATOM   1188  O  OE2   . GLU A 1 1682 ? 148.086 188.407 124.603 1.00 44.02  ? 1682 GLU A OE2   1 
ATOM   1189  N  N     . GLU A 1 1683 ? 143.218 190.968 126.237 1.00 45.34  ? 1683 GLU A N     1 
ATOM   1190  C  CA    . GLU A 1 1683 ? 141.836 190.542 126.390 1.00 48.30  ? 1683 GLU A CA    1 
ATOM   1191  C  C     . GLU A 1 1683 ? 141.439 189.604 125.259 1.00 49.85  ? 1683 GLU A C     1 
ATOM   1192  O  O     . GLU A 1 1683 ? 141.974 189.676 124.149 1.00 51.48  ? 1683 GLU A O     1 
ATOM   1193  C  CB    . GLU A 1 1683 ? 140.888 191.749 126.433 1.00 49.24  ? 1683 GLU A CB    1 
ATOM   1194  C  CG    . GLU A 1 1683 ? 140.606 192.376 125.080 1.00 57.06  ? 1683 GLU A CG    1 
ATOM   1195  C  CD    . GLU A 1 1683 ? 139.821 193.668 125.191 1.00 72.20  ? 1683 GLU A CD    1 
ATOM   1196  O  OE1   . GLU A 1 1683 ? 139.831 194.279 126.281 1.00 76.89  ? 1683 GLU A OE1   1 
ATOM   1197  O  OE2   . GLU A 1 1683 ? 139.192 194.072 124.191 1.00 74.04  ? 1683 GLU A OE2   1 
ATOM   1198  N  N     . VAL A 1 1684 ? 140.498 188.713 125.562 1.00 44.09  ? 1684 VAL A N     1 
ATOM   1199  C  CA    . VAL A 1 1684 ? 139.943 187.770 124.599 1.00 44.86  ? 1684 VAL A CA    1 
ATOM   1200  C  C     . VAL A 1 1684 ? 138.445 188.015 124.503 1.00 48.42  ? 1684 VAL A C     1 
ATOM   1201  O  O     . VAL A 1 1684 ? 137.750 188.039 125.525 1.00 53.41  ? 1684 VAL A O     1 
ATOM   1202  C  CB    . VAL A 1 1684 ? 140.228 186.311 124.997 1.00 39.88  ? 1684 VAL A CB    1 
ATOM   1203  C  CG1   . VAL A 1 1684 ? 139.783 185.364 123.895 1.00 44.14  ? 1684 VAL A CG1   1 
ATOM   1204  C  CG2   . VAL A 1 1684 ? 141.701 186.124 125.293 1.00 39.52  ? 1684 VAL A CG2   1 
ATOM   1205  N  N     . MET A 1 1685 ? 137.951 188.192 123.281 1.00 48.01  ? 1685 MET A N     1 
ATOM   1206  C  CA    . MET A 1 1685 ? 136.530 188.400 123.047 1.00 53.06  ? 1685 MET A CA    1 
ATOM   1207  C  C     . MET A 1 1685 ? 135.868 187.071 122.706 1.00 53.00  ? 1685 MET A C     1 
ATOM   1208  O  O     . MET A 1 1685 ? 136.321 186.356 121.807 1.00 54.88  ? 1685 MET A O     1 
ATOM   1209  C  CB    . MET A 1 1685 ? 136.309 189.410 121.921 1.00 53.44  ? 1685 MET A CB    1 
ATOM   1210  C  CG    . MET A 1 1685 ? 137.161 190.663 122.038 1.00 62.70  ? 1685 MET A CG    1 
ATOM   1211  S  SD    . MET A 1 1685 ? 137.187 191.331 123.712 1.00 80.57  ? 1685 MET A SD    1 
ATOM   1212  C  CE    . MET A 1 1685 ? 135.613 192.183 123.762 1.00 62.82  ? 1685 MET A CE    1 
ATOM   1213  N  N     . PHE A 1 1686 ? 134.800 186.744 123.432 1.00 52.59  ? 1686 PHE A N     1 
ATOM   1214  C  CA    . PHE A 1 1686 ? 134.103 185.485 123.211 1.00 53.40  ? 1686 PHE A CA    1 
ATOM   1215  C  C     . PHE A 1 1686 ? 133.453 185.466 121.834 1.00 61.01  ? 1686 PHE A C     1 
ATOM   1216  O  O     . PHE A 1 1686 ? 132.926 186.477 121.363 1.00 63.90  ? 1686 PHE A O     1 
ATOM   1217  C  CB    . PHE A 1 1686 ? 133.043 185.267 124.292 1.00 51.08  ? 1686 PHE A CB    1 
ATOM   1218  C  CG    . PHE A 1 1686 ? 133.609 185.003 125.658 1.00 49.15  ? 1686 PHE A CG    1 
ATOM   1219  C  CD1   . PHE A 1 1686 ? 134.946 184.681 125.823 1.00 50.73  ? 1686 PHE A CD1   1 
ATOM   1220  C  CD2   . PHE A 1 1686 ? 132.801 185.075 126.780 1.00 48.79  ? 1686 PHE A CD2   1 
ATOM   1221  C  CE1   . PHE A 1 1686 ? 135.464 184.438 127.079 1.00 48.00  ? 1686 PHE A CE1   1 
ATOM   1222  C  CE2   . PHE A 1 1686 ? 133.313 184.834 128.038 1.00 44.35  ? 1686 PHE A CE2   1 
ATOM   1223  C  CZ    . PHE A 1 1686 ? 134.646 184.514 128.188 1.00 45.51  ? 1686 PHE A CZ    1 
ATOM   1224  N  N     . LYS A 1 1687 ? 133.502 184.302 121.181 1.00 56.69  ? 1687 LYS A N     1 
ATOM   1225  C  CA    . LYS A 1 1687 ? 132.825 184.148 119.898 1.00 55.50  ? 1687 LYS A CA    1 
ATOM   1226  C  C     . LYS A 1 1687 ? 131.319 184.320 120.056 1.00 67.47  ? 1687 LYS A C     1 
ATOM   1227  O  O     . LYS A 1 1687 ? 130.673 185.015 119.263 1.00 72.51  ? 1687 LYS A O     1 
ATOM   1228  C  CB    . LYS A 1 1687 ? 133.154 182.782 119.294 1.00 52.22  ? 1687 LYS A CB    1 
ATOM   1229  C  CG    . LYS A 1 1687 ? 134.622 182.593 118.949 1.00 48.53  ? 1687 LYS A CG    1 
ATOM   1230  C  CD    . LYS A 1 1687 ? 135.128 183.708 118.050 1.00 48.20  ? 1687 LYS A CD    1 
ATOM   1231  C  CE    . LYS A 1 1687 ? 136.255 183.225 117.154 1.00 46.78  ? 1687 LYS A CE    1 
ATOM   1232  N  NZ    . LYS A 1 1687 ? 137.273 184.287 116.926 1.00 47.34  ? 1687 LYS A NZ    1 
ATOM   1233  N  N     . THR A 1 1688 ? 130.745 183.694 121.079 1.00 65.71  ? 1688 THR A N     1 
ATOM   1234  C  CA    . THR A 1 1688 ? 129.339 183.880 121.437 1.00 66.19  ? 1688 THR A CA    1 
ATOM   1235  C  C     . THR A 1 1688 ? 129.279 184.396 122.867 1.00 62.80  ? 1688 THR A C     1 
ATOM   1236  O  O     . THR A 1 1688 ? 129.443 183.611 123.819 1.00 67.78  ? 1688 THR A O     1 
ATOM   1237  C  CB    . THR A 1 1688 ? 128.549 182.579 121.300 1.00 67.54  ? 1688 THR A CB    1 
ATOM   1238  O  OG1   . THR A 1 1688 ? 129.085 181.594 122.191 1.00 63.75  ? 1688 THR A OG1   1 
ATOM   1239  C  CG2   . THR A 1 1688 ? 128.626 182.057 119.873 1.00 65.41  ? 1688 THR A CG2   1 
ATOM   1240  N  N     . PRO A 1 1689 ? 129.063 185.695 123.073 1.00 62.50  ? 1689 PRO A N     1 
ATOM   1241  C  CA    . PRO A 1 1689 ? 129.092 186.242 124.434 1.00 62.64  ? 1689 PRO A CA    1 
ATOM   1242  C  C     . PRO A 1 1689 ? 128.029 185.614 125.322 1.00 59.74  ? 1689 PRO A C     1 
ATOM   1243  O  O     . PRO A 1 1689 ? 126.914 185.320 124.886 1.00 64.15  ? 1689 PRO A O     1 
ATOM   1244  C  CB    . PRO A 1 1689 ? 128.834 187.739 124.223 1.00 63.45  ? 1689 PRO A CB    1 
ATOM   1245  C  CG    . PRO A 1 1689 ? 128.182 187.836 122.883 1.00 65.95  ? 1689 PRO A CG    1 
ATOM   1246  C  CD    . PRO A 1 1689 ? 128.753 186.721 122.064 1.00 64.47  ? 1689 PRO A CD    1 
ATOM   1247  N  N     . VAL A 1 1690 ? 128.391 185.413 126.585 1.00 60.08  ? 1690 VAL A N     1 
ATOM   1248  C  CA    . VAL A 1 1690 ? 127.517 184.766 127.557 1.00 65.68  ? 1690 VAL A CA    1 
ATOM   1249  C  C     . VAL A 1 1690 ? 126.628 185.829 128.188 1.00 71.09  ? 1690 VAL A C     1 
ATOM   1250  O  O     . VAL A 1 1690 ? 127.124 186.801 128.768 1.00 69.43  ? 1690 VAL A O     1 
ATOM   1251  C  CB    . VAL A 1 1690 ? 128.332 184.021 128.625 1.00 62.27  ? 1690 VAL A CB    1 
ATOM   1252  C  CG1   . VAL A 1 1690 ? 127.474 183.735 129.849 1.00 62.02  ? 1690 VAL A CG1   1 
ATOM   1253  C  CG2   . VAL A 1 1690 ? 128.907 182.736 128.051 1.00 58.62  ? 1690 VAL A CG2   1 
ATOM   1254  N  N     . SER A 1 1691 ? 125.315 185.641 128.081 1.00 77.63  ? 1691 SER A N     1 
ATOM   1255  C  CA    . SER A 1 1691 ? 124.349 186.604 128.594 1.00 78.76  ? 1691 SER A CA    1 
ATOM   1256  C  C     . SER A 1 1691 ? 123.938 186.211 130.008 1.00 77.55  ? 1691 SER A C     1 
ATOM   1257  O  O     . SER A 1 1691 ? 123.499 185.079 130.242 1.00 78.71  ? 1691 SER A O     1 
ATOM   1258  C  CB    . SER A 1 1691 ? 123.127 186.680 127.680 1.00 81.42  ? 1691 SER A CB    1 
ATOM   1259  O  OG    . SER A 1 1691 ? 122.168 187.591 128.187 1.00 85.43  ? 1691 SER A OG    1 
ATOM   1260  N  N     . ILE A 1 1692 ? 124.084 187.147 130.947 1.00 76.12  ? 1692 ILE A N     1 
ATOM   1261  C  CA    . ILE A 1 1692 ? 123.712 186.879 132.332 1.00 77.33  ? 1692 ILE A CA    1 
ATOM   1262  C  C     . ILE A 1 1692 ? 122.200 186.749 132.476 1.00 87.48  ? 1692 ILE A C     1 
ATOM   1263  O  O     . ILE A 1 1692 ? 121.715 185.996 133.328 1.00 88.83  ? 1692 ILE A O     1 
ATOM   1264  C  CB    . ILE A 1 1692 ? 124.279 187.976 133.253 1.00 68.10  ? 1692 ILE A CB    1 
ATOM   1265  C  CG1   . ILE A 1 1692 ? 125.778 188.151 133.006 1.00 66.49  ? 1692 ILE A CG1   1 
ATOM   1266  C  CG2   . ILE A 1 1692 ? 124.024 187.640 134.714 1.00 66.37  ? 1692 ILE A CG2   1 
ATOM   1267  C  CD1   . ILE A 1 1692 ? 126.438 189.146 133.934 1.00 63.17  ? 1692 ILE A CD1   1 
ATOM   1268  N  N     . THR A 1 1693 ? 121.432 187.475 131.660 1.00 91.64  ? 1693 THR A N     1 
ATOM   1269  C  CA    . THR A 1 1693 ? 119.977 187.442 131.786 1.00 90.93  ? 1693 THR A CA    1 
ATOM   1270  C  C     . THR A 1 1693 ? 119.421 186.049 131.514 1.00 91.07  ? 1693 THR A C     1 
ATOM   1271  O  O     . THR A 1 1693 ? 118.535 185.576 132.236 1.00 89.95  ? 1693 THR A O     1 
ATOM   1272  C  CB    . THR A 1 1693 ? 119.342 188.460 130.840 1.00 92.86  ? 1693 THR A CB    1 
ATOM   1273  O  OG1   . THR A 1 1693 ? 119.267 187.907 129.520 1.00 93.64  ? 1693 THR A OG1   1 
ATOM   1274  C  CG2   . THR A 1 1693 ? 120.165 189.736 130.803 1.00 85.63  ? 1693 THR A CG2   1 
ATOM   1275  N  N     . GLU A 1 1694 ? 119.924 185.375 130.477 1.00 87.83  ? 1694 GLU A N     1 
ATOM   1276  C  CA    . GLU A 1 1694 ? 119.431 184.041 130.155 1.00 87.68  ? 1694 GLU A CA    1 
ATOM   1277  C  C     . GLU A 1 1694 ? 119.883 182.994 131.165 1.00 91.41  ? 1694 GLU A C     1 
ATOM   1278  O  O     . GLU A 1 1694 ? 119.231 181.953 131.291 1.00 94.30  ? 1694 GLU A O     1 
ATOM   1279  C  CB    . GLU A 1 1694 ? 119.876 183.637 128.749 1.00 84.02  ? 1694 GLU A CB    1 
ATOM   1280  C  CG    . GLU A 1 1694 ? 119.036 184.250 127.639 1.00 89.31  ? 1694 GLU A CG    1 
ATOM   1281  C  CD    . GLU A 1 1694 ? 119.876 184.779 126.494 1.00 94.54  ? 1694 GLU A CD    1 
ATOM   1282  O  OE1   . GLU A 1 1694 ? 121.093 184.504 126.471 1.00 96.46  ? 1694 GLU A OE1   1 
ATOM   1283  O  OE2   . GLU A 1 1694 ? 119.318 185.471 125.617 1.00 89.70  ? 1694 GLU A OE2   1 
ATOM   1284  N  N     . HIS A 1 1695 ? 120.977 183.244 131.883 1.00 90.77  ? 1695 HIS A N     1 
ATOM   1285  C  CA    . HIS A 1 1695 ? 121.480 182.341 132.918 1.00 87.14  ? 1695 HIS A CA    1 
ATOM   1286  C  C     . HIS A 1 1695 ? 121.712 183.162 134.179 1.00 86.94  ? 1695 HIS A C     1 
ATOM   1287  O  O     . HIS A 1 1695 ? 122.858 183.473 134.531 1.00 83.80  ? 1695 HIS A O     1 
ATOM   1288  C  CB    . HIS A 1 1695 ? 122.756 181.632 132.464 1.00 81.71  ? 1695 HIS A CB    1 
ATOM   1289  C  CG    . HIS A 1 1695 ? 122.729 181.202 131.030 1.00 85.12  ? 1695 HIS A CG    1 
ATOM   1290  N  ND1   . HIS A 1 1695 ? 123.582 181.721 130.080 1.00 81.18  ? 1695 HIS A ND1   1 
ATOM   1291  C  CD2   . HIS A 1 1695 ? 121.948 180.305 130.383 1.00 84.13  ? 1695 HIS A CD2   1 
ATOM   1292  C  CE1   . HIS A 1 1695 ? 123.329 181.162 128.911 1.00 81.68  ? 1695 HIS A CE1   1 
ATOM   1293  N  NE2   . HIS A 1 1695 ? 122.342 180.298 129.067 1.00 82.23  ? 1695 HIS A NE2   1 
ATOM   1294  N  N     . PRO A 1 1696 ? 120.640 183.542 134.879 1.00 88.90  ? 1696 PRO A N     1 
ATOM   1295  C  CA    . PRO A 1 1696 ? 120.800 184.431 136.043 1.00 79.49  ? 1696 PRO A CA    1 
ATOM   1296  C  C     . PRO A 1 1696 ? 121.624 183.829 137.167 1.00 76.83  ? 1696 PRO A C     1 
ATOM   1297  O  O     . PRO A 1 1696 ? 122.263 184.576 137.918 1.00 71.76  ? 1696 PRO A O     1 
ATOM   1298  C  CB    . PRO A 1 1696 ? 119.354 184.705 136.488 1.00 83.12  ? 1696 PRO A CB    1 
ATOM   1299  C  CG    . PRO A 1 1696 ? 118.471 184.153 135.406 1.00 87.93  ? 1696 PRO A CG    1 
ATOM   1300  C  CD    . PRO A 1 1696 ? 119.248 183.102 134.696 1.00 87.65  ? 1696 PRO A CD    1 
ATOM   1301  N  N     . LYS A 1 1697 ? 121.623 182.507 137.312 1.00 80.05  ? 1697 LYS A N     1 
ATOM   1302  C  CA    . LYS A 1 1697 ? 122.376 181.870 138.382 1.00 78.66  ? 1697 LYS A CA    1 
ATOM   1303  C  C     . LYS A 1 1697 ? 123.868 182.123 138.208 1.00 75.91  ? 1697 LYS A C     1 
ATOM   1304  O  O     . LYS A 1 1697 ? 124.402 182.042 137.098 1.00 75.63  ? 1697 LYS A O     1 
ATOM   1305  C  CB    . LYS A 1 1697 ? 122.092 180.368 138.408 1.00 80.41  ? 1697 LYS A CB    1 
ATOM   1306  C  CG    . LYS A 1 1697 ? 122.811 179.614 139.513 1.00 77.94  ? 1697 LYS A CG    1 
ATOM   1307  C  CD    . LYS A 1 1697 ? 122.253 179.985 140.877 1.00 77.44  ? 1697 LYS A CD    1 
ATOM   1308  C  CE    . LYS A 1 1697 ? 122.891 179.158 141.981 1.00 86.51  ? 1697 LYS A CE    1 
ATOM   1309  N  NZ    . LYS A 1 1697 ? 122.400 179.561 143.327 1.00 98.00  ? 1697 LYS A NZ    1 
ATOM   1310  N  N     . ILE A 1 1698 ? 124.541 182.432 139.320 1.00 70.57  ? 1698 ILE A N     1 
ATOM   1311  C  CA    . ILE A 1 1698 ? 125.970 182.737 139.276 1.00 65.57  ? 1698 ILE A CA    1 
ATOM   1312  C  C     . ILE A 1 1698 ? 126.753 181.547 138.734 1.00 69.92  ? 1698 ILE A C     1 
ATOM   1313  O  O     . ILE A 1 1698 ? 127.629 181.694 137.871 1.00 71.48  ? 1698 ILE A O     1 
ATOM   1314  C  CB    . ILE A 1 1698 ? 126.466 183.163 140.672 1.00 65.20  ? 1698 ILE A CB    1 
ATOM   1315  C  CG1   . ILE A 1 1698 ? 127.985 183.361 140.684 1.00 59.31  ? 1698 ILE A CG1   1 
ATOM   1316  C  CG2   . ILE A 1 1698 ? 126.018 182.174 141.746 1.00 74.85  ? 1698 ILE A CG2   1 
ATOM   1317  C  CD1   . ILE A 1 1698 ? 128.475 184.439 139.752 1.00 53.95  ? 1698 ILE A CD1   1 
ATOM   1318  N  N     . ASN A 1 1699 ? 126.429 180.346 139.217 1.00 75.68  ? 1699 ASN A N     1 
ATOM   1319  C  CA    . ASN A 1 1699 ? 127.141 179.149 138.787 1.00 74.48  ? 1699 ASN A CA    1 
ATOM   1320  C  C     . ASN A 1 1699 ? 126.941 178.892 137.300 1.00 72.37  ? 1699 ASN A C     1 
ATOM   1321  O  O     . ASN A 1 1699 ? 127.894 178.563 136.583 1.00 73.73  ? 1699 ASN A O     1 
ATOM   1322  C  CB    . ASN A 1 1699 ? 126.664 177.954 139.608 1.00 73.43  ? 1699 ASN A CB    1 
ATOM   1323  C  CG    . ASN A 1 1699 ? 127.252 177.937 141.002 1.00 85.08  ? 1699 ASN A CG    1 
ATOM   1324  O  OD1   . ASN A 1 1699 ? 126.726 177.283 141.900 1.00 92.96  ? 1699 ASN A OD1   1 
ATOM   1325  N  ND2   . ASN A 1 1699 ? 128.347 178.663 141.192 1.00 83.19  ? 1699 ASN A ND2   1 
ATOM   1326  N  N     . GLU A 1 1700 ? 125.706 179.053 136.818 1.00 68.79  ? 1700 GLU A N     1 
ATOM   1327  C  CA    . GLU A 1 1700 ? 125.405 178.761 135.420 1.00 72.18  ? 1700 GLU A CA    1 
ATOM   1328  C  C     . GLU A 1 1700 ? 126.199 179.664 134.485 1.00 69.55  ? 1700 GLU A C     1 
ATOM   1329  O  O     . GLU A 1 1700 ? 126.896 179.183 133.582 1.00 70.89  ? 1700 GLU A O     1 
ATOM   1330  C  CB    . GLU A 1 1700 ? 123.905 178.915 135.168 1.00 85.44  ? 1700 GLU A CB    1 
ATOM   1331  C  CG    . GLU A 1 1700 ? 123.088 177.667 135.455 1.00 99.39  ? 1700 GLU A CG    1 
ATOM   1332  C  CD    . GLU A 1 1700 ? 121.786 177.632 134.678 1.00 104.75 ? 1700 GLU A CD    1 
ATOM   1333  O  OE1   . GLU A 1 1700 ? 121.486 178.619 133.974 1.00 100.18 ? 1700 GLU A OE1   1 
ATOM   1334  O  OE2   . GLU A 1 1700 ? 121.061 176.620 134.773 1.00 103.54 ? 1700 GLU A OE2   1 
ATOM   1335  N  N     . TRP A 1 1701 ? 126.125 180.980 134.696 1.00 65.35  ? 1701 TRP A N     1 
ATOM   1336  C  CA    . TRP A 1 1701 ? 126.807 181.880 133.775 1.00 65.15  ? 1701 TRP A CA    1 
ATOM   1337  C  C     . TRP A 1 1701 ? 128.317 181.845 133.971 1.00 60.68  ? 1701 TRP A C     1 
ATOM   1338  O  O     . TRP A 1 1701 ? 129.059 182.057 133.011 1.00 61.78  ? 1701 TRP A O     1 
ATOM   1339  C  CB    . TRP A 1 1701 ? 126.252 183.304 133.893 1.00 62.21  ? 1701 TRP A CB    1 
ATOM   1340  C  CG    . TRP A 1 1701 ? 126.738 184.121 135.051 1.00 56.70  ? 1701 TRP A CG    1 
ATOM   1341  C  CD1   . TRP A 1 1701 ? 126.111 184.292 136.247 1.00 57.47  ? 1701 TRP A CD1   1 
ATOM   1342  C  CD2   . TRP A 1 1701 ? 127.930 184.914 135.107 1.00 56.20  ? 1701 TRP A CD2   1 
ATOM   1343  N  NE1   . TRP A 1 1701 ? 126.844 185.126 137.053 1.00 52.58  ? 1701 TRP A NE1   1 
ATOM   1344  C  CE2   . TRP A 1 1701 ? 127.967 185.521 136.377 1.00 54.72  ? 1701 TRP A CE2   1 
ATOM   1345  C  CE3   . TRP A 1 1701 ? 128.974 185.160 134.212 1.00 56.07  ? 1701 TRP A CE3   1 
ATOM   1346  C  CZ2   . TRP A 1 1701 ? 129.006 186.359 136.774 1.00 54.67  ? 1701 TRP A CZ2   1 
ATOM   1347  C  CZ3   . TRP A 1 1701 ? 130.005 185.992 134.608 1.00 56.18  ? 1701 TRP A CZ3   1 
ATOM   1348  C  CH2   . TRP A 1 1701 ? 130.014 186.581 135.877 1.00 55.54  ? 1701 TRP A CH2   1 
ATOM   1349  N  N     . LEU A 1 1702 ? 128.798 181.539 135.181 1.00 57.36  ? 1702 LEU A N     1 
ATOM   1350  C  CA    . LEU A 1 1702 ? 130.237 181.352 135.354 1.00 53.84  ? 1702 LEU A CA    1 
ATOM   1351  C  C     . LEU A 1 1702 ? 130.740 180.147 134.563 1.00 61.27  ? 1702 LEU A C     1 
ATOM   1352  O  O     . LEU A 1 1702 ? 131.785 180.221 133.900 1.00 66.57  ? 1702 LEU A O     1 
ATOM   1353  C  CB    . LEU A 1 1702 ? 130.572 181.203 136.837 1.00 55.64  ? 1702 LEU A CB    1 
ATOM   1354  C  CG    . LEU A 1 1702 ? 131.043 182.475 137.542 1.00 58.37  ? 1702 LEU A CG    1 
ATOM   1355  C  CD1   . LEU A 1 1702 ? 131.347 182.200 139.005 1.00 62.33  ? 1702 LEU A CD1   1 
ATOM   1356  C  CD2   . LEU A 1 1702 ? 132.259 183.055 136.839 1.00 58.19  ? 1702 LEU A CD2   1 
ATOM   1357  N  N     . THR A 1 1703 ? 130.006 179.032 134.613 1.00 60.40  ? 1703 THR A N     1 
ATOM   1358  C  CA    . THR A 1 1703 ? 130.393 177.858 133.836 1.00 56.07  ? 1703 THR A CA    1 
ATOM   1359  C  C     . THR A 1 1703 ? 130.321 178.143 132.340 1.00 55.97  ? 1703 THR A C     1 
ATOM   1360  O  O     . THR A 1 1703 ? 131.192 177.707 131.574 1.00 59.92  ? 1703 THR A O     1 
ATOM   1361  C  CB    . THR A 1 1703 ? 129.504 176.670 134.206 1.00 61.93  ? 1703 THR A CB    1 
ATOM   1362  O  OG1   . THR A 1 1703 ? 129.756 176.292 135.566 1.00 63.25  ? 1703 THR A OG1   1 
ATOM   1363  C  CG2   . THR A 1 1703 ? 129.787 175.481 133.299 1.00 63.25  ? 1703 THR A CG2   1 
ATOM   1364  N  N     . LEU A 1 1704 ? 129.291 178.877 131.908 1.00 56.26  ? 1704 LEU A N     1 
ATOM   1365  C  CA    . LEU A 1 1704 ? 129.204 179.267 130.503 1.00 57.50  ? 1704 LEU A CA    1 
ATOM   1366  C  C     . LEU A 1 1704 ? 130.384 180.140 130.092 1.00 53.96  ? 1704 LEU A C     1 
ATOM   1367  O  O     . LEU A 1 1704 ? 130.925 179.978 128.995 1.00 55.59  ? 1704 LEU A O     1 
ATOM   1368  C  CB    . LEU A 1 1704 ? 127.879 179.981 130.225 1.00 63.62  ? 1704 LEU A CB    1 
ATOM   1369  C  CG    . LEU A 1 1704 ? 126.649 179.148 129.841 1.00 63.50  ? 1704 LEU A CG    1 
ATOM   1370  C  CD1   . LEU A 1 1704 ? 126.793 178.645 128.412 1.00 57.62  ? 1704 LEU A CD1   1 
ATOM   1371  C  CD2   . LEU A 1 1704 ? 126.408 177.979 130.782 1.00 61.85  ? 1704 LEU A CD2   1 
ATOM   1372  N  N     . VAL A 1 1705 ? 130.800 181.069 130.957 1.00 51.88  ? 1705 VAL A N     1 
ATOM   1373  C  CA    . VAL A 1 1705 ? 131.953 181.914 130.649 1.00 51.05  ? 1705 VAL A CA    1 
ATOM   1374  C  C     . VAL A 1 1705 ? 133.214 181.072 130.508 1.00 51.02  ? 1705 VAL A C     1 
ATOM   1375  O  O     . VAL A 1 1705 ? 134.011 181.273 129.587 1.00 54.04  ? 1705 VAL A O     1 
ATOM   1376  C  CB    . VAL A 1 1705 ? 132.123 183.014 131.712 1.00 45.90  ? 1705 VAL A CB    1 
ATOM   1377  C  CG1   . VAL A 1 1705 ? 133.434 183.746 131.506 1.00 39.21  ? 1705 VAL A CG1   1 
ATOM   1378  C  CG2   . VAL A 1 1705 ? 130.985 184.008 131.615 1.00 56.47  ? 1705 VAL A CG2   1 
ATOM   1379  N  N     . GLU A 1 1706 ? 133.419 180.120 131.421 1.00 50.92  ? 1706 GLU A N     1 
ATOM   1380  C  CA    . GLU A 1 1706 ? 134.610 179.274 131.336 1.00 46.83  ? 1706 GLU A CA    1 
ATOM   1381  C  C     . GLU A 1 1706 ? 134.612 178.448 130.050 1.00 46.26  ? 1706 GLU A C     1 
ATOM   1382  O  O     . GLU A 1 1706 ? 135.623 178.383 129.330 1.00 50.74  ? 1706 GLU A O     1 
ATOM   1383  C  CB    . GLU A 1 1706 ? 134.695 178.367 132.563 1.00 45.06  ? 1706 GLU A CB    1 
ATOM   1384  C  CG    . GLU A 1 1706 ? 135.826 177.355 132.510 1.00 51.19  ? 1706 GLU A CG    1 
ATOM   1385  C  CD    . GLU A 1 1706 ? 135.642 176.224 133.501 1.00 64.27  ? 1706 GLU A CD    1 
ATOM   1386  O  OE1   . GLU A 1 1706 ? 134.692 175.432 133.329 1.00 74.75  ? 1706 GLU A OE1   1 
ATOM   1387  O  OE2   . GLU A 1 1706 ? 136.445 176.126 134.452 1.00 61.39  ? 1706 GLU A OE2   1 
ATOM   1388  N  N     . LYS A 1 1707 ? 133.476 177.817 129.738 1.00 45.95  ? 1707 LYS A N     1 
ATOM   1389  C  CA    . LYS A 1 1707 ? 133.392 176.999 128.533 1.00 47.06  ? 1707 LYS A CA    1 
ATOM   1390  C  C     . LYS A 1 1707 ? 133.589 177.842 127.280 1.00 51.91  ? 1707 LYS A C     1 
ATOM   1391  O  O     . LYS A 1 1707 ? 134.275 177.421 126.340 1.00 53.72  ? 1707 LYS A O     1 
ATOM   1392  C  CB    . LYS A 1 1707 ? 132.051 176.268 128.484 1.00 52.63  ? 1707 LYS A CB    1 
ATOM   1393  C  CG    . LYS A 1 1707 ? 131.805 175.520 127.185 1.00 58.67  ? 1707 LYS A CG    1 
ATOM   1394  C  CD    . LYS A 1 1707 ? 130.449 174.837 127.183 1.00 71.43  ? 1707 LYS A CD    1 
ATOM   1395  C  CE    . LYS A 1 1707 ? 130.188 174.141 125.858 1.00 82.79  ? 1707 LYS A CE    1 
ATOM   1396  N  NZ    . LYS A 1 1707 ? 130.035 175.113 124.741 1.00 86.58  ? 1707 LYS A NZ    1 
ATOM   1397  N  N     . GLU A 1 1708 ? 132.999 179.039 127.247 1.00 49.57  ? 1708 GLU A N     1 
ATOM   1398  C  CA    . GLU A 1 1708 ? 133.159 179.904 126.086 1.00 43.85  ? 1708 GLU A CA    1 
ATOM   1399  C  C     . GLU A 1 1708 ? 134.579 180.430 125.967 1.00 43.29  ? 1708 GLU A C     1 
ATOM   1400  O  O     . GLU A 1 1708 ? 135.061 180.637 124.853 1.00 45.21  ? 1708 GLU A O     1 
ATOM   1401  C  CB    . GLU A 1 1708 ? 132.165 181.063 126.143 1.00 51.64  ? 1708 GLU A CB    1 
ATOM   1402  C  CG    . GLU A 1 1708 ? 131.889 181.733 124.795 1.00 64.04  ? 1708 GLU A CG    1 
ATOM   1403  C  CD    . GLU A 1 1708 ? 131.566 180.760 123.665 1.00 70.09  ? 1708 GLU A CD    1 
ATOM   1404  O  OE1   . GLU A 1 1708 ? 131.123 179.621 123.931 1.00 68.44  ? 1708 GLU A OE1   1 
ATOM   1405  O  OE2   . GLU A 1 1708 ? 131.761 181.141 122.492 1.00 68.69  ? 1708 GLU A OE2   1 
ATOM   1406  N  N     . MET A 1 1709 ? 135.263 180.654 127.091 1.00 40.25  ? 1709 MET A N     1 
ATOM   1407  C  CA    . MET A 1 1709 ? 136.674 181.019 127.033 1.00 38.24  ? 1709 MET A CA    1 
ATOM   1408  C  C     . MET A 1 1709 ? 137.485 179.913 126.377 1.00 38.11  ? 1709 MET A C     1 
ATOM   1409  O  O     . MET A 1 1709 ? 138.297 180.168 125.478 1.00 41.70  ? 1709 MET A O     1 
ATOM   1410  C  CB    . MET A 1 1709 ? 137.198 181.314 128.439 1.00 35.72  ? 1709 MET A CB    1 
ATOM   1411  C  CG    . MET A 1 1709 ? 138.682 181.029 128.623 1.00 35.14  ? 1709 MET A CG    1 
ATOM   1412  S  SD    . MET A 1 1709 ? 139.184 180.968 130.355 1.00 41.91  ? 1709 MET A SD    1 
ATOM   1413  C  CE    . MET A 1 1709 ? 138.887 179.245 130.737 1.00 31.92  ? 1709 MET A CE    1 
ATOM   1414  N  N     . ARG A 1 1710 ? 137.252 178.666 126.795 1.00 35.62  ? 1710 ARG A N     1 
ATOM   1415  C  CA    . ARG A 1 1710 ? 137.960 177.546 126.180 1.00 31.69  ? 1710 ARG A CA    1 
ATOM   1416  C  C     . ARG A 1 1710 ? 137.652 177.454 124.687 1.00 34.83  ? 1710 ARG A C     1 
ATOM   1417  O  O     . ARG A 1 1710 ? 138.557 177.288 123.857 1.00 36.39  ? 1710 ARG A O     1 
ATOM   1418  C  CB    . ARG A 1 1710 ? 137.592 176.241 126.888 1.00 32.60  ? 1710 ARG A CB    1 
ATOM   1419  C  CG    . ARG A 1 1710 ? 138.294 176.033 128.219 1.00 32.12  ? 1710 ARG A CG    1 
ATOM   1420  C  CD    . ARG A 1 1710 ? 137.728 174.826 128.956 1.00 34.38  ? 1710 ARG A CD    1 
ATOM   1421  N  NE    . ARG A 1 1710 ? 138.718 174.159 129.795 1.00 39.67  ? 1710 ARG A NE    1 
ATOM   1422  C  CZ    . ARG A 1 1710 ? 139.279 174.688 130.875 1.00 45.24  ? 1710 ARG A CZ    1 
ATOM   1423  N  NH1   . ARG A 1 1710 ? 138.948 175.893 131.309 1.00 44.55  ? 1710 ARG A NH1   1 
ATOM   1424  N  NH2   . ARG A 1 1710 ? 140.187 173.984 131.545 1.00 50.64  ? 1710 ARG A NH2   1 
ATOM   1425  N  N     . VAL A 1 1711 ? 136.374 177.588 124.326 1.00 37.97  ? 1711 VAL A N     1 
ATOM   1426  C  CA    . VAL A 1 1711 ? 135.969 177.434 122.932 1.00 37.83  ? 1711 VAL A CA    1 
ATOM   1427  C  C     . VAL A 1 1711 ? 136.555 178.545 122.067 1.00 38.74  ? 1711 VAL A C     1 
ATOM   1428  O  O     . VAL A 1 1711 ? 137.074 178.288 120.973 1.00 43.60  ? 1711 VAL A O     1 
ATOM   1429  C  CB    . VAL A 1 1711 ? 134.434 177.381 122.828 1.00 41.26  ? 1711 VAL A CB    1 
ATOM   1430  C  CG1   . VAL A 1 1711 ? 133.988 177.575 121.388 1.00 46.19  ? 1711 VAL A CG1   1 
ATOM   1431  C  CG2   . VAL A 1 1711 ? 133.914 176.062 123.376 1.00 39.41  ? 1711 VAL A CG2   1 
ATOM   1432  N  N     . THR A 1 1712 ? 136.480 179.796 122.532 1.00 35.07  ? 1712 THR A N     1 
ATOM   1433  C  CA    . THR A 1 1712 ? 137.009 180.901 121.744 1.00 34.77  ? 1712 THR A CA    1 
ATOM   1434  C  C     . THR A 1 1712 ? 138.526 180.837 121.643 1.00 35.78  ? 1712 THR A C     1 
ATOM   1435  O  O     . THR A 1 1712 ? 139.087 181.216 120.610 1.00 41.36  ? 1712 THR A O     1 
ATOM   1436  C  CB    . THR A 1 1712 ? 136.553 182.246 122.321 1.00 36.62  ? 1712 THR A CB    1 
ATOM   1437  O  OG1   . THR A 1 1712 ? 136.825 183.288 121.375 1.00 45.24  ? 1712 THR A OG1   1 
ATOM   1438  C  CG2   . THR A 1 1712 ? 137.263 182.567 123.627 1.00 35.69  ? 1712 THR A CG2   1 
ATOM   1439  N  N     . LEU A 1 1713 ? 139.208 180.339 122.681 1.00 33.53  ? 1713 LEU A N     1 
ATOM   1440  C  CA    . LEU A 1 1713 ? 140.644 180.125 122.560 1.00 30.42  ? 1713 LEU A CA    1 
ATOM   1441  C  C     . LEU A 1 1713 ? 140.946 179.071 121.505 1.00 34.38  ? 1713 LEU A C     1 
ATOM   1442  O  O     . LEU A 1 1713 ? 141.892 179.221 120.723 1.00 34.68  ? 1713 LEU A O     1 
ATOM   1443  C  CB    . LEU A 1 1713 ? 141.237 179.729 123.911 1.00 28.11  ? 1713 LEU A CB    1 
ATOM   1444  C  CG    . LEU A 1 1713 ? 141.654 180.900 124.801 1.00 27.19  ? 1713 LEU A CG    1 
ATOM   1445  C  CD1   . LEU A 1 1713 ? 142.226 180.399 126.114 1.00 27.28  ? 1713 LEU A CD1   1 
ATOM   1446  C  CD2   . LEU A 1 1713 ? 142.653 181.790 124.082 1.00 26.58  ? 1713 LEU A CD2   1 
ATOM   1447  N  N     . ALA A 1 1714 ? 140.142 178.006 121.454 1.00 35.15  ? 1714 ALA A N     1 
ATOM   1448  C  CA    . ALA A 1 1714 ? 140.337 176.989 120.424 1.00 32.75  ? 1714 ALA A CA    1 
ATOM   1449  C  C     . ALA A 1 1714 ? 140.139 177.564 119.024 1.00 39.96  ? 1714 ALA A C     1 
ATOM   1450  O  O     . ALA A 1 1714 ? 140.938 177.302 118.116 1.00 41.87  ? 1714 ALA A O     1 
ATOM   1451  C  CB    . ALA A 1 1714 ? 139.390 175.815 120.661 1.00 32.20  ? 1714 ALA A CB    1 
ATOM   1452  N  N     . LYS A 1 1715 ? 139.079 178.354 118.830 1.00 40.52  ? 1715 LYS A N     1 
ATOM   1453  C  CA    . LYS A 1 1715 ? 138.825 178.939 117.513 1.00 40.44  ? 1715 LYS A CA    1 
ATOM   1454  C  C     . LYS A 1 1715 ? 139.929 179.912 117.112 1.00 41.26  ? 1715 LYS A C     1 
ATOM   1455  O  O     . LYS A 1 1715 ? 140.381 179.916 115.957 1.00 43.98  ? 1715 LYS A O     1 
ATOM   1456  C  CB    . LYS A 1 1715 ? 137.466 179.640 117.492 1.00 39.32  ? 1715 LYS A CB    1 
ATOM   1457  C  CG    . LYS A 1 1715 ? 136.321 178.827 118.066 1.00 38.08  ? 1715 LYS A CG    1 
ATOM   1458  C  CD    . LYS A 1 1715 ? 135.789 177.820 117.063 1.00 45.39  ? 1715 LYS A CD    1 
ATOM   1459  C  CE    . LYS A 1 1715 ? 134.500 177.184 117.559 1.00 55.21  ? 1715 LYS A CE    1 
ATOM   1460  N  NZ    . LYS A 1 1715 ? 133.512 178.205 118.003 1.00 47.47  ? 1715 LYS A NZ    1 
ATOM   1461  N  N     . LEU A 1 1716 ? 140.370 180.753 118.052 1.00 34.93  ? 1716 LEU A N     1 
ATOM   1462  C  CA    . LEU A 1 1716 ? 141.445 181.691 117.758 1.00 32.31  ? 1716 LEU A CA    1 
ATOM   1463  C  C     . LEU A 1 1716 ? 142.737 180.957 117.431 1.00 35.78  ? 1716 LEU A C     1 
ATOM   1464  O  O     . LEU A 1 1716 ? 143.486 181.374 116.540 1.00 37.64  ? 1716 LEU A O     1 
ATOM   1465  C  CB    . LEU A 1 1716 ? 141.644 182.644 118.936 1.00 30.03  ? 1716 LEU A CB    1 
ATOM   1466  C  CG    . LEU A 1 1716 ? 140.607 183.756 119.097 1.00 29.71  ? 1716 LEU A CG    1 
ATOM   1467  C  CD1   . LEU A 1 1716 ? 140.849 184.526 120.384 1.00 28.72  ? 1716 LEU A CD1   1 
ATOM   1468  C  CD2   . LEU A 1 1716 ? 140.632 184.689 117.899 1.00 35.36  ? 1716 LEU A CD2   1 
ATOM   1469  N  N     . LEU A 1 1717 ? 143.017 179.860 118.140 1.00 34.68  ? 1717 LEU A N     1 
ATOM   1470  C  CA    . LEU A 1 1717 ? 144.188 179.055 117.817 1.00 34.48  ? 1717 LEU A CA    1 
ATOM   1471  C  C     . LEU A 1 1717 ? 144.079 178.466 116.418 1.00 35.99  ? 1717 LEU A C     1 
ATOM   1472  O  O     . LEU A 1 1717 ? 145.066 178.425 115.679 1.00 39.08  ? 1717 LEU A O     1 
ATOM   1473  C  CB    . LEU A 1 1717 ? 144.372 177.943 118.849 1.00 31.97  ? 1717 LEU A CB    1 
ATOM   1474  C  CG    . LEU A 1 1717 ? 145.419 176.891 118.474 1.00 28.72  ? 1717 LEU A CG    1 
ATOM   1475  C  CD1   . LEU A 1 1717 ? 146.817 177.488 118.520 1.00 24.35  ? 1717 LEU A CD1   1 
ATOM   1476  C  CD2   . LEU A 1 1717 ? 145.324 175.671 119.373 1.00 26.23  ? 1717 LEU A CD2   1 
ATOM   1477  N  N     . ALA A 1 1718 ? 142.888 177.999 116.039 1.00 35.56  ? 1718 ALA A N     1 
ATOM   1478  C  CA    . ALA A 1 1718 ? 142.706 177.456 114.695 1.00 34.31  ? 1718 ALA A CA    1 
ATOM   1479  C  C     . ALA A 1 1718 ? 142.992 178.513 113.633 1.00 37.18  ? 1718 ALA A C     1 
ATOM   1480  O  O     . ALA A 1 1718 ? 143.709 178.257 112.656 1.00 39.14  ? 1718 ALA A O     1 
ATOM   1481  C  CB    . ALA A 1 1718 ? 141.290 176.902 114.541 1.00 36.20  ? 1718 ALA A CB    1 
ATOM   1482  N  N     . GLU A 1 1719 ? 142.448 179.719 113.819 1.00 39.93  ? 1719 GLU A N     1 
ATOM   1483  C  CA    . GLU A 1 1719 ? 142.696 180.793 112.858 1.00 37.08  ? 1719 GLU A CA    1 
ATOM   1484  C  C     . GLU A 1 1719 ? 144.174 181.172 112.813 1.00 35.55  ? 1719 GLU A C     1 
ATOM   1485  O  O     . GLU A 1 1719 ? 144.738 181.397 111.731 1.00 35.94  ? 1719 GLU A O     1 
ATOM   1486  C  CB    . GLU A 1 1719 ? 141.840 182.013 113.198 1.00 38.67  ? 1719 GLU A CB    1 
ATOM   1487  C  CG    . GLU A 1 1719 ? 140.355 181.721 113.318 1.00 46.18  ? 1719 GLU A CG    1 
ATOM   1488  C  CD    . GLU A 1 1719 ? 139.591 182.854 113.975 1.00 55.32  ? 1719 GLU A CD    1 
ATOM   1489  O  OE1   . GLU A 1 1719 ? 140.198 183.918 114.219 1.00 52.51  ? 1719 GLU A OE1   1 
ATOM   1490  O  OE2   . GLU A 1 1719 ? 138.385 182.681 114.247 1.00 60.26  ? 1719 GLU A OE2   1 
ATOM   1491  N  N     . SER A 1 1720 ? 144.819 181.251 113.979 1.00 33.34  ? 1720 SER A N     1 
ATOM   1492  C  CA    . SER A 1 1720 ? 146.228 181.621 114.024 1.00 33.19  ? 1720 SER A CA    1 
ATOM   1493  C  C     . SER A 1 1720 ? 147.100 180.567 113.354 1.00 37.89  ? 1720 SER A C     1 
ATOM   1494  O  O     . SER A 1 1720 ? 148.083 180.901 112.685 1.00 43.28  ? 1720 SER A O     1 
ATOM   1495  C  CB    . SER A 1 1720 ? 146.663 181.845 115.472 1.00 32.87  ? 1720 SER A CB    1 
ATOM   1496  O  OG    . SER A 1 1720 ? 148.059 182.065 115.555 1.00 36.55  ? 1720 SER A OG    1 
ATOM   1497  N  N     . VAL A 1 1721 ? 146.766 179.286 113.535 1.00 35.62  ? 1721 VAL A N     1 
ATOM   1498  C  CA    . VAL A 1 1721 ? 147.485 178.223 112.837 1.00 31.60  ? 1721 VAL A CA    1 
ATOM   1499  C  C     . VAL A 1 1721 ? 147.285 178.346 111.333 1.00 39.18  ? 1721 VAL A C     1 
ATOM   1500  O  O     . VAL A 1 1721 ? 148.232 178.193 110.551 1.00 43.44  ? 1721 VAL A O     1 
ATOM   1501  C  CB    . VAL A 1 1721 ? 147.050 176.841 113.357 1.00 28.49  ? 1721 VAL A CB    1 
ATOM   1502  C  CG1   . VAL A 1 1721 ? 147.678 175.741 112.522 1.00 35.54  ? 1721 VAL A CG1   1 
ATOM   1503  C  CG2   . VAL A 1 1721 ? 147.460 176.677 114.806 1.00 31.69  ? 1721 VAL A CG2   1 
ATOM   1504  N  N     . THR A 1 1722 ? 146.051 178.627 110.906 1.00 43.68  ? 1722 THR A N     1 
ATOM   1505  C  CA    . THR A 1 1722 ? 145.792 178.821 109.482 1.00 42.52  ? 1722 THR A CA    1 
ATOM   1506  C  C     . THR A 1 1722 ? 146.665 179.932 108.912 1.00 45.35  ? 1722 THR A C     1 
ATOM   1507  O  O     . THR A 1 1722 ? 147.202 179.806 107.805 1.00 48.44  ? 1722 THR A O     1 
ATOM   1508  C  CB    . THR A 1 1722 ? 144.310 179.129 109.258 1.00 37.53  ? 1722 THR A CB    1 
ATOM   1509  O  OG1   . THR A 1 1722 ? 143.534 177.951 109.505 1.00 43.22  ? 1722 THR A OG1   1 
ATOM   1510  C  CG2   . THR A 1 1722 ? 144.065 179.598 107.831 1.00 31.53  ? 1722 THR A CG2   1 
ATOM   1511  N  N     . GLU A 1 1723 ? 146.835 181.022 109.663 1.00 44.17  ? 1723 GLU A N     1 
ATOM   1512  C  CA    . GLU A 1 1723 ? 147.659 182.126 109.173 1.00 43.65  ? 1723 GLU A CA    1 
ATOM   1513  C  C     . GLU A 1 1723 ? 149.146 181.773 109.186 1.00 45.42  ? 1723 GLU A C     1 
ATOM   1514  O  O     . GLU A 1 1723 ? 149.868 182.039 108.216 1.00 49.49  ? 1723 GLU A O     1 
ATOM   1515  C  CB    . GLU A 1 1723 ? 147.394 183.387 109.995 1.00 41.09  ? 1723 GLU A CB    1 
ATOM   1516  C  CG    . GLU A 1 1723 ? 146.045 184.028 109.717 1.00 43.22  ? 1723 GLU A CG    1 
ATOM   1517  C  CD    . GLU A 1 1723 ? 145.825 185.298 110.513 1.00 54.70  ? 1723 GLU A CD    1 
ATOM   1518  O  OE1   . GLU A 1 1723 ? 146.721 186.167 110.506 1.00 56.15  ? 1723 GLU A OE1   1 
ATOM   1519  O  OE2   . GLU A 1 1723 ? 144.754 185.430 111.140 1.00 57.33  ? 1723 GLU A OE2   1 
ATOM   1520  N  N     . VAL A 1 1724 ? 149.628 181.169 110.277 1.00 42.52  ? 1724 VAL A N     1 
ATOM   1521  C  CA    . VAL A 1 1724 ? 151.056 180.892 110.386 1.00 41.85  ? 1724 VAL A CA    1 
ATOM   1522  C  C     . VAL A 1 1724 ? 151.485 179.818 109.394 1.00 48.71  ? 1724 VAL A C     1 
ATOM   1523  O  O     . VAL A 1 1724 ? 152.665 179.755 109.027 1.00 56.44  ? 1724 VAL A O     1 
ATOM   1524  C  CB    . VAL A 1 1724 ? 151.438 180.500 111.828 1.00 37.65  ? 1724 VAL A CB    1 
ATOM   1525  C  CG1   . VAL A 1 1724 ? 150.799 179.185 112.223 1.00 35.10  ? 1724 VAL A CG1   1 
ATOM   1526  C  CG2   . VAL A 1 1724 ? 152.954 180.456 112.007 1.00 39.17  ? 1724 VAL A CG2   1 
ATOM   1527  N  N     . GLU A 1 1725 ? 150.557 178.973 108.935 1.00 51.81  ? 1725 GLU A N     1 
ATOM   1528  C  CA    . GLU A 1 1725 ? 150.880 178.075 107.830 1.00 53.29  ? 1725 GLU A CA    1 
ATOM   1529  C  C     . GLU A 1 1725 ? 151.262 178.865 106.585 1.00 61.69  ? 1725 GLU A C     1 
ATOM   1530  O  O     . GLU A 1 1725 ? 152.206 178.501 105.874 1.00 66.92  ? 1725 GLU A O     1 
ATOM   1531  C  CB    . GLU A 1 1725 ? 149.705 177.143 107.534 1.00 53.87  ? 1725 GLU A CB    1 
ATOM   1532  C  CG    . GLU A 1 1725 ? 149.453 176.090 108.599 1.00 53.02  ? 1725 GLU A CG    1 
ATOM   1533  C  CD    . GLU A 1 1725 ? 148.213 175.265 108.316 1.00 61.28  ? 1725 GLU A CD    1 
ATOM   1534  O  OE1   . GLU A 1 1725 ? 147.659 175.386 107.203 1.00 68.56  ? 1725 GLU A OE1   1 
ATOM   1535  O  OE2   . GLU A 1 1725 ? 147.792 174.497 109.206 1.00 60.66  ? 1725 GLU A OE2   1 
ATOM   1536  N  N     . ILE A 1 1726 ? 150.535 179.949 106.305 1.00 61.23  ? 1726 ILE A N     1 
ATOM   1537  C  CA    . ILE A 1 1726 ? 150.925 180.843 105.220 1.00 57.80  ? 1726 ILE A CA    1 
ATOM   1538  C  C     . ILE A 1 1726 ? 152.261 181.504 105.530 1.00 55.86  ? 1726 ILE A C     1 
ATOM   1539  O  O     . ILE A 1 1726 ? 153.123 181.635 104.652 1.00 58.61  ? 1726 ILE A O     1 
ATOM   1540  C  CB    . ILE A 1 1726 ? 149.823 181.886 104.960 1.00 56.90  ? 1726 ILE A CB    1 
ATOM   1541  C  CG1   . ILE A 1 1726 ? 148.443 181.228 105.010 1.00 53.42  ? 1726 ILE A CG1   1 
ATOM   1542  C  CG2   . ILE A 1 1726 ? 150.045 182.571 103.621 1.00 57.41  ? 1726 ILE A CG2   1 
ATOM   1543  C  CD1   . ILE A 1 1726 ? 148.201 180.227 103.901 1.00 47.82  ? 1726 ILE A CD1   1 
ATOM   1544  N  N     . PHE A 1 1727 ? 152.455 181.939 106.779 1.00 60.60  ? 1727 PHE A N     1 
ATOM   1545  C  CA    . PHE A 1 1727 ? 153.759 182.473 107.169 1.00 65.58  ? 1727 PHE A CA    1 
ATOM   1546  C  C     . PHE A 1 1727 ? 154.850 181.414 107.056 1.00 65.75  ? 1727 PHE A C     1 
ATOM   1547  O  O     . PHE A 1 1727 ? 155.991 181.724 106.695 1.00 64.76  ? 1727 PHE A O     1 
ATOM   1548  C  CB    . PHE A 1 1727 ? 153.711 183.039 108.589 1.00 60.21  ? 1727 PHE A CB    1 
ATOM   1549  C  CG    . PHE A 1 1727 ? 152.920 184.306 108.707 1.00 58.89  ? 1727 PHE A CG    1 
ATOM   1550  C  CD1   . PHE A 1 1727 ? 153.479 185.517 108.340 1.00 60.63  ? 1727 PHE A CD1   1 
ATOM   1551  C  CD2   . PHE A 1 1727 ? 151.625 184.293 109.191 1.00 57.41  ? 1727 PHE A CD2   1 
ATOM   1552  C  CE1   . PHE A 1 1727 ? 152.760 186.688 108.446 1.00 67.93  ? 1727 PHE A CE1   1 
ATOM   1553  C  CE2   . PHE A 1 1727 ? 150.899 185.461 109.298 1.00 63.11  ? 1727 PHE A CE2   1 
ATOM   1554  C  CZ    . PHE A 1 1727 ? 151.468 186.660 108.926 1.00 65.81  ? 1727 PHE A CZ    1 
ATOM   1555  N  N     . GLY A 1 1728 ? 154.522 180.163 107.360 1.00 64.37  ? 1728 GLY A N     1 
ATOM   1556  C  CA    . GLY A 1 1728 ? 155.473 179.083 107.230 1.00 61.46  ? 1728 GLY A CA    1 
ATOM   1557  C  C     . GLY A 1 1728 ? 155.722 178.722 105.777 1.00 69.55  ? 1728 GLY A C     1 
ATOM   1558  O  O     . GLY A 1 1728 ? 155.113 179.257 104.849 1.00 67.89  ? 1728 GLY A O     1 
ATOM   1559  N  N     . LYS A 1 1729 ? 156.642 177.772 105.593 1.00 70.32  ? 1729 LYS A N     1 
ATOM   1560  C  CA    . LYS A 1 1729 ? 157.106 177.295 104.282 1.00 69.85  ? 1729 LYS A CA    1 
ATOM   1561  C  C     . LYS A 1 1729 ? 157.226 178.437 103.273 1.00 75.41  ? 1729 LYS A C     1 
ATOM   1562  O  O     . LYS A 1 1729 ? 156.733 178.368 102.145 1.00 74.22  ? 1729 LYS A O     1 
ATOM   1563  C  CB    . LYS A 1 1729 ? 156.217 176.167 103.740 1.00 69.56  ? 1729 LYS A CB    1 
ATOM   1564  C  CG    . LYS A 1 1729 ? 154.712 176.362 103.863 1.00 70.03  ? 1729 LYS A CG    1 
ATOM   1565  C  CD    . LYS A 1 1729 ? 153.978 175.032 103.908 1.00 69.15  ? 1729 LYS A CD    1 
ATOM   1566  C  CE    . LYS A 1 1729 ? 152.482 175.227 103.727 1.00 76.94  ? 1729 LYS A CE    1 
ATOM   1567  N  NZ    . LYS A 1 1729 ? 151.732 173.946 103.840 1.00 87.29  ? 1729 LYS A NZ    1 
ATOM   1568  N  N     . ALA A 1 1730 ? 157.898 179.506 103.698 1.00 77.21  ? 1730 ALA A N     1 
ATOM   1569  C  CA    . ALA A 1 1730 ? 158.108 180.685 102.870 1.00 73.66  ? 1730 ALA A CA    1 
ATOM   1570  C  C     . ALA A 1 1730 ? 159.584 181.049 102.868 1.00 75.64  ? 1730 ALA A C     1 
ATOM   1571  O  O     . ALA A 1 1730 ? 160.251 180.982 103.905 1.00 73.17  ? 1730 ALA A O     1 
ATOM   1572  C  CB    . ALA A 1 1730 ? 157.275 181.872 103.367 1.00 63.12  ? 1730 ALA A CB    1 
ATOM   1573  N  N     . THR A 1 1731 ? 160.092 181.430 101.692 1.00 78.21  ? 1731 THR A N     1 
ATOM   1574  C  CA    . THR A 1 1731 ? 161.496 181.813 101.581 1.00 78.60  ? 1731 THR A CA    1 
ATOM   1575  C  C     . THR A 1 1731 ? 161.795 183.069 102.390 1.00 75.93  ? 1731 THR A C     1 
ATOM   1576  O  O     . THR A 1 1731 ? 162.826 183.146 103.069 1.00 76.03  ? 1731 THR A O     1 
ATOM   1577  C  CB    . THR A 1 1731 ? 161.871 182.024 100.114 1.00 81.90  ? 1731 THR A CB    1 
ATOM   1578  O  OG1   . THR A 1 1731 ? 161.211 183.193 99.613  1.00 81.20  ? 1731 THR A OG1   1 
ATOM   1579  C  CG2   . THR A 1 1731 ? 161.458 180.819 99.281  1.00 72.71  ? 1731 THR A CG2   1 
ATOM   1580  N  N     . SER A 1 1732 ? 160.910 184.061 102.331 1.00 74.45  ? 1732 SER A N     1 
ATOM   1581  C  CA    . SER A 1 1732 ? 161.076 185.306 103.064 1.00 73.96  ? 1732 SER A CA    1 
ATOM   1582  C  C     . SER A 1 1732 ? 159.762 185.681 103.731 1.00 70.69  ? 1732 SER A C     1 
ATOM   1583  O  O     . SER A 1 1732 ? 158.682 185.310 103.265 1.00 72.95  ? 1732 SER A O     1 
ATOM   1584  C  CB    . SER A 1 1732 ? 161.540 186.445 102.146 1.00 74.47  ? 1732 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 1732 ? 160.539 186.777 101.200 1.00 69.31  ? 1732 SER A OG    1 
ATOM   1586  N  N     . ILE A 1 1733 ? 159.865 186.423 104.830 1.00 69.13  ? 1733 ILE A N     1 
ATOM   1587  C  CA    . ILE A 1 1733 ? 158.708 186.862 105.602 1.00 70.92  ? 1733 ILE A CA    1 
ATOM   1588  C  C     . ILE A 1 1733 ? 158.691 188.382 105.609 1.00 66.04  ? 1733 ILE A C     1 
ATOM   1589  O  O     . ILE A 1 1733 ? 159.685 189.019 105.979 1.00 67.46  ? 1733 ILE A O     1 
ATOM   1590  C  CB    . ILE A 1 1733 ? 158.731 186.310 107.036 1.00 69.25  ? 1733 ILE A CB    1 
ATOM   1591  C  CG1   . ILE A 1 1733 ? 158.564 184.789 107.023 1.00 66.96  ? 1733 ILE A CG1   1 
ATOM   1592  C  CG2   . ILE A 1 1733 ? 157.650 186.969 107.880 1.00 57.58  ? 1733 ILE A CG2   1 
ATOM   1593  C  CD1   . ILE A 1 1733 ? 158.285 184.197 108.383 1.00 56.51  ? 1733 ILE A CD1   1 
ATOM   1594  N  N     . ASP A 1 1734 ? 157.569 188.961 105.199 1.00 61.76  ? 1734 ASP A N     1 
ATOM   1595  C  CA    . ASP A 1 1734 ? 157.396 190.404 105.274 1.00 64.97  ? 1734 ASP A CA    1 
ATOM   1596  C  C     . ASP A 1 1734 ? 157.217 190.808 106.732 1.00 66.71  ? 1734 ASP A C     1 
ATOM   1597  O  O     . ASP A 1 1734 ? 156.305 190.303 107.394 1.00 67.01  ? 1734 ASP A O     1 
ATOM   1598  C  CB    . ASP A 1 1734 ? 156.190 190.840 104.451 1.00 70.25  ? 1734 ASP A CB    1 
ATOM   1599  C  CG    . ASP A 1 1734 ? 156.132 192.341 104.247 1.00 76.94  ? 1734 ASP A CG    1 
ATOM   1600  O  OD1   . ASP A 1 1734 ? 157.196 192.993 104.298 1.00 80.57  ? 1734 ASP A OD1   1 
ATOM   1601  O  OD2   . ASP A 1 1734 ? 155.021 192.869 104.034 1.00 72.24  ? 1734 ASP A OD2   1 
ATOM   1602  N  N     . PRO A 1 1735 ? 158.065 191.686 107.274 1.00 64.38  ? 1735 PRO A N     1 
ATOM   1603  C  CA    . PRO A 1 1735 ? 157.928 192.049 108.694 1.00 62.78  ? 1735 PRO A CA    1 
ATOM   1604  C  C     . PRO A 1 1735 ? 156.581 192.655 109.045 1.00 60.26  ? 1735 PRO A C     1 
ATOM   1605  O  O     . PRO A 1 1735 ? 156.073 192.408 110.145 1.00 55.95  ? 1735 PRO A O     1 
ATOM   1606  C  CB    . PRO A 1 1735 ? 159.071 193.052 108.908 1.00 61.05  ? 1735 PRO A CB    1 
ATOM   1607  C  CG    . PRO A 1 1735 ? 160.062 192.731 107.840 1.00 56.93  ? 1735 PRO A CG    1 
ATOM   1608  C  CD    . PRO A 1 1735 ? 159.252 192.299 106.655 1.00 58.59  ? 1735 PRO A CD    1 
ATOM   1609  N  N     . ASN A 1 1736 ? 155.981 193.433 108.140 1.00 62.10  ? 1736 ASN A N     1 
ATOM   1610  C  CA    . ASN A 1 1736 ? 154.729 194.112 108.459 1.00 62.59  ? 1736 ASN A CA    1 
ATOM   1611  C  C     . ASN A 1 1736 ? 153.614 193.114 108.749 1.00 58.27  ? 1736 ASN A C     1 
ATOM   1612  O  O     . ASN A 1 1736 ? 152.920 193.220 109.766 1.00 57.40  ? 1736 ASN A O     1 
ATOM   1613  C  CB    . ASN A 1 1736 ? 154.335 195.043 107.312 1.00 68.62  ? 1736 ASN A CB    1 
ATOM   1614  C  CG    . ASN A 1 1736 ? 155.531 195.719 106.674 1.00 70.47  ? 1736 ASN A CG    1 
ATOM   1615  O  OD1   . ASN A 1 1736 ? 156.247 196.483 107.323 1.00 66.91  ? 1736 ASN A OD1   1 
ATOM   1616  N  ND2   . ASN A 1 1736 ? 155.756 195.441 105.395 1.00 70.62  ? 1736 ASN A ND2   1 
ATOM   1617  N  N     . THR A 1 1737 ? 153.438 192.123 107.871 1.00 59.78  ? 1737 THR A N     1 
ATOM   1618  C  CA    . THR A 1 1737 ? 152.367 191.154 108.073 1.00 60.78  ? 1737 THR A CA    1 
ATOM   1619  C  C     . THR A 1 1737 ? 152.651 190.234 109.256 1.00 56.99  ? 1737 THR A C     1 
ATOM   1620  O  O     . THR A 1 1737 ? 151.716 189.816 109.948 1.00 53.99  ? 1737 THR A O     1 
ATOM   1621  C  CB    . THR A 1 1737 ? 152.131 190.347 106.791 1.00 59.97  ? 1737 THR A CB    1 
ATOM   1622  O  OG1   . THR A 1 1737 ? 150.989 189.497 106.959 1.00 58.56  ? 1737 THR A OG1   1 
ATOM   1623  C  CG2   . THR A 1 1737 ? 153.348 189.508 106.427 1.00 54.97  ? 1737 THR A CG2   1 
ATOM   1624  N  N     . TYR A 1 1738 ? 153.923 189.921 109.517 1.00 54.95  ? 1738 TYR A N     1 
ATOM   1625  C  CA    . TYR A 1 1738 ? 154.254 189.106 110.682 1.00 45.39  ? 1738 TYR A CA    1 
ATOM   1626  C  C     . TYR A 1 1738 ? 153.925 189.842 111.976 1.00 44.82  ? 1738 TYR A C     1 
ATOM   1627  O  O     . TYR A 1 1738 ? 153.351 189.261 112.905 1.00 47.17  ? 1738 TYR A O     1 
ATOM   1628  C  CB    . TYR A 1 1738 ? 155.728 188.705 110.644 1.00 44.84  ? 1738 TYR A CB    1 
ATOM   1629  C  CG    . TYR A 1 1738 ? 156.049 187.506 111.505 1.00 46.93  ? 1738 TYR A CG    1 
ATOM   1630  C  CD1   . TYR A 1 1738 ? 155.557 186.248 111.186 1.00 52.35  ? 1738 TYR A CD1   1 
ATOM   1631  C  CD2   . TYR A 1 1738 ? 156.841 187.631 112.638 1.00 43.57  ? 1738 TYR A CD2   1 
ATOM   1632  C  CE1   . TYR A 1 1738 ? 155.844 185.149 111.971 1.00 48.70  ? 1738 TYR A CE1   1 
ATOM   1633  C  CE2   . TYR A 1 1738 ? 157.134 186.537 113.427 1.00 36.53  ? 1738 TYR A CE2   1 
ATOM   1634  C  CZ    . TYR A 1 1738 ? 156.633 185.299 113.090 1.00 39.19  ? 1738 TYR A CZ    1 
ATOM   1635  O  OH    . TYR A 1 1738 ? 156.922 184.207 113.874 1.00 42.34  ? 1738 TYR A OH    1 
ATOM   1636  N  N     . ILE A 1 1739 ? 154.277 191.128 112.053 1.00 43.85  ? 1739 ILE A N     1 
ATOM   1637  C  CA    . ILE A 1 1739 ? 153.927 191.915 113.232 1.00 37.64  ? 1739 ILE A CA    1 
ATOM   1638  C  C     . ILE A 1 1739 ? 152.417 192.078 113.345 1.00 40.93  ? 1739 ILE A C     1 
ATOM   1639  O  O     . ILE A 1 1739 ? 151.870 192.082 114.454 1.00 43.10  ? 1739 ILE A O     1 
ATOM   1640  C  CB    . ILE A 1 1739 ? 154.649 193.276 113.204 1.00 43.09  ? 1739 ILE A CB    1 
ATOM   1641  C  CG1   . ILE A 1 1739 ? 156.164 193.077 113.157 1.00 41.13  ? 1739 ILE A CG1   1 
ATOM   1642  C  CG2   . ILE A 1 1739 ? 154.269 194.114 114.412 1.00 46.47  ? 1739 ILE A CG2   1 
ATOM   1643  C  CD1   . ILE A 1 1739 ? 156.705 192.238 114.292 1.00 37.23  ? 1739 ILE A CD1   1 
ATOM   1644  N  N     . THR A 1 1740 ? 151.717 192.209 112.215 1.00 45.50  ? 1740 THR A N     1 
ATOM   1645  C  CA    . THR A 1 1740 ? 150.259 192.278 112.257 1.00 44.51  ? 1740 THR A CA    1 
ATOM   1646  C  C     . THR A 1 1740 ? 149.663 190.999 112.834 1.00 44.33  ? 1740 THR A C     1 
ATOM   1647  O  O     . THR A 1 1740 ? 148.759 191.050 113.676 1.00 46.87  ? 1740 THR A O     1 
ATOM   1648  C  CB    . THR A 1 1740 ? 149.706 192.544 110.857 1.00 45.57  ? 1740 THR A CB    1 
ATOM   1649  O  OG1   . THR A 1 1740 ? 150.104 193.851 110.424 1.00 53.38  ? 1740 THR A OG1   1 
ATOM   1650  C  CG2   . THR A 1 1740 ? 148.187 192.457 110.854 1.00 43.01  ? 1740 THR A CG2   1 
ATOM   1651  N  N     . TRP A 1 1741 ? 150.165 189.842 112.397 1.00 45.16  ? 1741 TRP A N     1 
ATOM   1652  C  CA    . TRP A 1 1741 ? 149.686 188.572 112.934 1.00 38.00  ? 1741 TRP A CA    1 
ATOM   1653  C  C     . TRP A 1 1741 ? 150.000 188.445 114.419 1.00 36.81  ? 1741 TRP A C     1 
ATOM   1654  O  O     . TRP A 1 1741 ? 149.176 187.944 115.192 1.00 42.80  ? 1741 TRP A O     1 
ATOM   1655  C  CB    . TRP A 1 1741 ? 150.298 187.408 112.156 1.00 38.12  ? 1741 TRP A CB    1 
ATOM   1656  C  CG    . TRP A 1 1741 ? 150.119 186.077 112.823 1.00 41.98  ? 1741 TRP A CG    1 
ATOM   1657  C  CD1   . TRP A 1 1741 ? 148.995 185.304 112.817 1.00 43.41  ? 1741 TRP A CD1   1 
ATOM   1658  C  CD2   . TRP A 1 1741 ? 151.094 185.363 113.592 1.00 41.37  ? 1741 TRP A CD2   1 
ATOM   1659  N  NE1   . TRP A 1 1741 ? 149.209 184.153 113.536 1.00 43.80  ? 1741 TRP A NE1   1 
ATOM   1660  C  CE2   . TRP A 1 1741 ? 150.490 184.165 114.022 1.00 41.10  ? 1741 TRP A CE2   1 
ATOM   1661  C  CE3   . TRP A 1 1741 ? 152.417 185.620 113.959 1.00 38.09  ? 1741 TRP A CE3   1 
ATOM   1662  C  CZ2   . TRP A 1 1741 ? 151.164 183.228 114.799 1.00 34.48  ? 1741 TRP A CZ2   1 
ATOM   1663  C  CZ3   . TRP A 1 1741 ? 153.085 184.687 114.731 1.00 34.96  ? 1741 TRP A CZ3   1 
ATOM   1664  C  CH2   . TRP A 1 1741 ? 152.457 183.506 115.143 1.00 32.39  ? 1741 TRP A CH2   1 
ATOM   1665  N  N     . ILE A 1 1742 ? 151.192 188.883 114.833 1.00 33.10  ? 1742 ILE A N     1 
ATOM   1666  C  CA    . ILE A 1 1742 ? 151.558 188.828 116.246 1.00 33.94  ? 1742 ILE A CA    1 
ATOM   1667  C  C     . ILE A 1 1742 ? 150.617 189.693 117.075 1.00 36.51  ? 1742 ILE A C     1 
ATOM   1668  O  O     . ILE A 1 1742 ? 150.143 189.279 118.140 1.00 36.79  ? 1742 ILE A O     1 
ATOM   1669  C  CB    . ILE A 1 1742 ? 153.028 189.248 116.432 1.00 37.07  ? 1742 ILE A CB    1 
ATOM   1670  C  CG1   . ILE A 1 1742 ? 153.965 188.153 115.924 1.00 36.58  ? 1742 ILE A CG1   1 
ATOM   1671  C  CG2   . ILE A 1 1742 ? 153.320 189.564 117.891 1.00 35.26  ? 1742 ILE A CG2   1 
ATOM   1672  C  CD1   . ILE A 1 1742 ? 155.411 188.578 115.859 1.00 39.85  ? 1742 ILE A CD1   1 
ATOM   1673  N  N     . ASP A 1 1743 ? 150.328 190.906 116.597 1.00 37.59  ? 1743 ASP A N     1 
ATOM   1674  C  CA    . ASP A 1 1743 ? 149.432 191.801 117.321 1.00 38.33  ? 1743 ASP A CA    1 
ATOM   1675  C  C     . ASP A 1 1743 ? 148.004 191.273 117.351 1.00 37.97  ? 1743 ASP A C     1 
ATOM   1676  O  O     . ASP A 1 1743 ? 147.282 191.503 118.327 1.00 39.16  ? 1743 ASP A O     1 
ATOM   1677  C  CB    . ASP A 1 1743 ? 149.462 193.193 116.690 1.00 40.29  ? 1743 ASP A CB    1 
ATOM   1678  C  CG    . ASP A 1 1743 ? 150.628 194.028 117.174 1.00 47.81  ? 1743 ASP A CG    1 
ATOM   1679  O  OD1   . ASP A 1 1743 ? 151.170 193.724 118.256 1.00 52.97  ? 1743 ASP A OD1   1 
ATOM   1680  O  OD2   . ASP A 1 1743 ? 151.003 194.990 116.471 1.00 46.27  ? 1743 ASP A OD2   1 
ATOM   1681  N  N     . LYS A 1 1744 ? 147.580 190.577 116.294 1.00 35.26  ? 1744 LYS A N     1 
ATOM   1682  C  CA    . LYS A 1 1744 ? 146.195 190.123 116.208 1.00 32.47  ? 1744 LYS A CA    1 
ATOM   1683  C  C     . LYS A 1 1744 ? 145.862 189.111 117.299 1.00 35.03  ? 1744 LYS A C     1 
ATOM   1684  O  O     . LYS A 1 1744 ? 144.787 189.180 117.907 1.00 36.33  ? 1744 LYS A O     1 
ATOM   1685  C  CB    . LYS A 1 1744 ? 145.928 189.526 114.827 1.00 30.42  ? 1744 LYS A CB    1 
ATOM   1686  C  CG    . LYS A 1 1744 ? 144.530 188.961 114.653 1.00 33.83  ? 1744 LYS A CG    1 
ATOM   1687  C  CD    . LYS A 1 1744 ? 144.208 188.724 113.188 1.00 36.86  ? 1744 LYS A CD    1 
ATOM   1688  C  CE    . LYS A 1 1744 ? 142.873 188.017 113.027 1.00 44.99  ? 1744 LYS A CE    1 
ATOM   1689  N  NZ    . LYS A 1 1744 ? 141.804 188.661 113.838 1.00 45.60  ? 1744 LYS A NZ    1 
ATOM   1690  N  N     . TYR A 1 1745 ? 146.763 188.171 117.566 1.00 39.61  ? 1745 TYR A N     1 
ATOM   1691  C  CA    . TYR A 1 1745 ? 146.472 187.042 118.435 1.00 33.71  ? 1745 TYR A CA    1 
ATOM   1692  C  C     . TYR A 1 1745 ? 147.202 187.170 119.766 1.00 32.65  ? 1745 TYR A C     1 
ATOM   1693  O  O     . TYR A 1 1745 ? 148.152 187.944 119.914 1.00 38.32  ? 1745 TYR A O     1 
ATOM   1694  C  CB    . TYR A 1 1745 ? 146.845 185.724 117.749 1.00 26.15  ? 1745 TYR A CB    1 
ATOM   1695  C  CG    . TYR A 1 1745 ? 145.991 185.435 116.538 1.00 31.21  ? 1745 TYR A CG    1 
ATOM   1696  C  CD1   . TYR A 1 1745 ? 144.688 184.977 116.677 1.00 31.54  ? 1745 TYR A CD1   1 
ATOM   1697  C  CD2   . TYR A 1 1745 ? 146.481 185.639 115.256 1.00 33.28  ? 1745 TYR A CD2   1 
ATOM   1698  C  CE1   . TYR A 1 1745 ? 143.901 184.721 115.572 1.00 35.23  ? 1745 TYR A CE1   1 
ATOM   1699  C  CE2   . TYR A 1 1745 ? 145.702 185.385 114.147 1.00 35.32  ? 1745 TYR A CE2   1 
ATOM   1700  C  CZ    . TYR A 1 1745 ? 144.413 184.926 114.310 1.00 37.99  ? 1745 TYR A CZ    1 
ATOM   1701  O  OH    . TYR A 1 1745 ? 143.634 184.673 113.206 1.00 42.51  ? 1745 TYR A OH    1 
ATOM   1702  N  N     . GLN A 1 1746 ? 146.737 186.389 120.737 1.00 28.23  ? 1746 GLN A N     1 
ATOM   1703  C  CA    . GLN A 1 1746 ? 147.249 186.464 122.096 1.00 27.92  ? 1746 GLN A CA    1 
ATOM   1704  C  C     . GLN A 1 1746 ? 148.663 185.895 122.181 1.00 30.11  ? 1746 GLN A C     1 
ATOM   1705  O  O     . GLN A 1 1746 ? 149.113 185.133 121.321 1.00 33.97  ? 1746 GLN A O     1 
ATOM   1706  C  CB    . GLN A 1 1746 ? 146.326 185.712 123.055 1.00 28.28  ? 1746 GLN A CB    1 
ATOM   1707  C  CG    . GLN A 1 1746 ? 145.057 186.467 123.416 1.00 38.71  ? 1746 GLN A CG    1 
ATOM   1708  C  CD    . GLN A 1 1746 ? 144.014 186.418 122.318 1.00 40.89  ? 1746 GLN A CD    1 
ATOM   1709  O  OE1   . GLN A 1 1746 ? 144.114 185.620 121.387 1.00 37.24  ? 1746 GLN A OE1   1 
ATOM   1710  N  NE2   . GLN A 1 1746 ? 143.008 187.278 122.419 1.00 40.52  ? 1746 GLN A NE2   1 
ATOM   1711  N  N     . ALA A 1 1747 ? 149.369 186.286 123.246 1.00 26.13  ? 1747 ALA A N     1 
ATOM   1712  C  CA    . ALA A 1 1747 ? 150.724 185.790 123.464 1.00 21.74  ? 1747 ALA A CA    1 
ATOM   1713  C  C     . ALA A 1 1747 ? 150.731 184.282 123.677 1.00 27.05  ? 1747 ALA A C     1 
ATOM   1714  O  O     . ALA A 1 1747 ? 151.666 183.591 123.259 1.00 31.58  ? 1747 ALA A O     1 
ATOM   1715  C  CB    . ALA A 1 1747 ? 151.359 186.502 124.657 1.00 21.84  ? 1747 ALA A CB    1 
ATOM   1716  N  N     . GLN A 1 1748 ? 149.696 183.757 124.335 1.00 31.97  ? 1748 GLN A N     1 
ATOM   1717  C  CA    . GLN A 1 1748 ? 149.601 182.317 124.547 1.00 24.51  ? 1748 GLN A CA    1 
ATOM   1718  C  C     . GLN A 1 1748 ? 149.385 181.571 123.236 1.00 20.48  ? 1748 GLN A C     1 
ATOM   1719  O  O     . GLN A 1 1748 ? 149.798 180.413 123.108 1.00 21.28  ? 1748 GLN A O     1 
ATOM   1720  C  CB    . GLN A 1 1748 ? 148.470 182.021 125.535 1.00 19.46  ? 1748 GLN A CB    1 
ATOM   1721  C  CG    . GLN A 1 1748 ? 148.069 180.561 125.648 1.00 17.71  ? 1748 GLN A CG    1 
ATOM   1722  C  CD    . GLN A 1 1748 ? 146.719 180.382 126.311 1.00 21.09  ? 1748 GLN A CD    1 
ATOM   1723  O  OE1   . GLN A 1 1748 ? 146.314 181.190 127.146 1.00 23.69  ? 1748 GLN A OE1   1 
ATOM   1724  N  NE2   . GLN A 1 1748 ? 146.014 179.319 125.942 1.00 24.51  ? 1748 GLN A NE2   1 
ATOM   1725  N  N     . LEU A 1 1749 ? 148.771 182.220 122.249 1.00 21.94  ? 1749 LEU A N     1 
ATOM   1726  C  CA    . LEU A 1 1749 ? 148.402 181.547 121.011 1.00 22.80  ? 1749 LEU A CA    1 
ATOM   1727  C  C     . LEU A 1 1749 ? 149.442 181.692 119.908 1.00 20.18  ? 1749 LEU A C     1 
ATOM   1728  O  O     . LEU A 1 1749 ? 149.562 180.793 119.071 1.00 22.28  ? 1749 LEU A O     1 
ATOM   1729  C  CB    . LEU A 1 1749 ? 147.054 182.070 120.512 1.00 27.01  ? 1749 LEU A CB    1 
ATOM   1730  C  CG    . LEU A 1 1749 ? 145.873 181.810 121.447 1.00 24.94  ? 1749 LEU A CG    1 
ATOM   1731  C  CD1   . LEU A 1 1749 ? 144.607 182.407 120.876 1.00 25.63  ? 1749 LEU A CD1   1 
ATOM   1732  C  CD2   . LEU A 1 1749 ? 145.701 180.320 121.694 1.00 24.55  ? 1749 LEU A CD2   1 
ATOM   1733  N  N     . VAL A 1 1750 ? 150.194 182.794 119.877 1.00 20.40  ? 1750 VAL A N     1 
ATOM   1734  C  CA    . VAL A 1 1750 ? 151.199 182.961 118.830 1.00 22.88  ? 1750 VAL A CA    1 
ATOM   1735  C  C     . VAL A 1 1750 ? 152.306 181.920 118.973 1.00 24.92  ? 1750 VAL A C     1 
ATOM   1736  O  O     . VAL A 1 1750 ? 152.737 181.311 117.985 1.00 27.35  ? 1750 VAL A O     1 
ATOM   1737  C  CB    . VAL A 1 1750 ? 151.756 184.398 118.837 1.00 22.45  ? 1750 VAL A CB    1 
ATOM   1738  C  CG1   . VAL A 1 1750 ? 150.707 185.370 118.323 1.00 29.53  ? 1750 VAL A CG1   1 
ATOM   1739  C  CG2   . VAL A 1 1750 ? 152.209 184.801 120.230 1.00 22.61  ? 1750 VAL A CG2   1 
ATOM   1740  N  N     . VAL A 1 1751 ? 152.773 181.690 120.203 1.00 18.16  ? 1751 VAL A N     1 
ATOM   1741  C  CA    . VAL A 1 1751 ? 153.805 180.685 120.433 1.00 15.25  ? 1751 VAL A CA    1 
ATOM   1742  C  C     . VAL A 1 1751 ? 153.278 179.295 120.104 1.00 18.39  ? 1751 VAL A C     1 
ATOM   1743  O  O     . VAL A 1 1751 ? 153.984 178.473 119.507 1.00 24.84  ? 1751 VAL A O     1 
ATOM   1744  C  CB    . VAL A 1 1751 ? 154.315 180.769 121.883 1.00 12.91  ? 1751 VAL A CB    1 
ATOM   1745  C  CG1   . VAL A 1 1751 ? 155.549 179.902 122.062 1.00 14.20  ? 1751 VAL A CG1   1 
ATOM   1746  C  CG2   . VAL A 1 1751 ? 154.609 182.213 122.257 1.00 16.70  ? 1751 VAL A CG2   1 
ATOM   1747  N  N     . LEU A 1 1752 ? 152.032 179.011 120.489 1.00 15.31  ? 1752 LEU A N     1 
ATOM   1748  C  CA    . LEU A 1 1752 ? 151.438 177.713 120.189 1.00 14.79  ? 1752 LEU A CA    1 
ATOM   1749  C  C     . LEU A 1 1752 ? 151.325 177.490 118.686 1.00 17.66  ? 1752 LEU A C     1 
ATOM   1750  O  O     . LEU A 1 1752 ? 151.612 176.395 118.190 1.00 19.99  ? 1752 LEU A O     1 
ATOM   1751  C  CB    . LEU A 1 1752 ? 150.066 177.607 120.853 1.00 14.96  ? 1752 LEU A CB    1 
ATOM   1752  C  CG    . LEU A 1 1752 ? 149.507 176.206 121.097 1.00 16.61  ? 1752 LEU A CG    1 
ATOM   1753  C  CD1   . LEU A 1 1752 ? 150.487 175.370 121.901 1.00 12.79  ? 1752 LEU A CD1   1 
ATOM   1754  C  CD2   . LEU A 1 1752 ? 148.169 176.300 121.807 1.00 19.74  ? 1752 LEU A CD2   1 
ATOM   1755  N  N     . SER A 1 1753 ? 150.907 178.518 117.945 1.00 17.79  ? 1753 SER A N     1 
ATOM   1756  C  CA    . SER A 1 1753 ? 150.804 178.400 116.495 1.00 16.71  ? 1753 SER A CA    1 
ATOM   1757  C  C     . SER A 1 1753 ? 152.171 178.204 115.857 1.00 18.25  ? 1753 SER A C     1 
ATOM   1758  O  O     . SER A 1 1753 ? 152.314 177.415 114.916 1.00 21.18  ? 1753 SER A O     1 
ATOM   1759  C  CB    . SER A 1 1753 ? 150.115 179.635 115.920 1.00 23.65  ? 1753 SER A CB    1 
ATOM   1760  O  OG    . SER A 1 1753 ? 148.856 179.837 116.533 1.00 27.52  ? 1753 SER A OG    1 
ATOM   1761  N  N     . ALA A 1 1754 ? 153.186 178.921 116.346 1.00 15.83  ? 1754 ALA A N     1 
ATOM   1762  C  CA    . ALA A 1 1754 ? 154.536 178.726 115.828 1.00 15.24  ? 1754 ALA A CA    1 
ATOM   1763  C  C     . ALA A 1 1754 ? 155.015 177.301 116.075 1.00 17.11  ? 1754 ALA A C     1 
ATOM   1764  O  O     . ALA A 1 1754 ? 155.604 176.672 115.186 1.00 21.50  ? 1754 ALA A O     1 
ATOM   1765  C  CB    . ALA A 1 1754 ? 155.494 179.733 116.463 1.00 17.61  ? 1754 ALA A CB    1 
ATOM   1766  N  N     . GLN A 1 1755 ? 154.763 176.773 117.276 1.00 16.94  ? 1755 GLN A N     1 
ATOM   1767  C  CA    . GLN A 1 1755 ? 155.151 175.400 117.581 1.00 14.16  ? 1755 GLN A CA    1 
ATOM   1768  C  C     . GLN A 1 1755 ? 154.420 174.407 116.687 1.00 15.33  ? 1755 GLN A C     1 
ATOM   1769  O  O     . GLN A 1 1755 ? 155.022 173.448 116.192 1.00 18.67  ? 1755 GLN A O     1 
ATOM   1770  C  CB    . GLN A 1 1755 ? 154.882 175.091 119.053 1.00 13.44  ? 1755 GLN A CB    1 
ATOM   1771  C  CG    . GLN A 1 1755 ? 155.735 175.890 120.017 1.00 15.72  ? 1755 GLN A CG    1 
ATOM   1772  C  CD    . GLN A 1 1755 ? 155.372 175.641 121.467 1.00 17.25  ? 1755 GLN A CD    1 
ATOM   1773  O  OE1   . GLN A 1 1755 ? 154.203 175.697 121.845 1.00 19.55  ? 1755 GLN A OE1   1 
ATOM   1774  N  NE2   . GLN A 1 1755 ? 156.377 175.368 122.289 1.00 20.15  ? 1755 GLN A NE2   1 
ATOM   1775  N  N     . ILE A 1 1756 ? 153.121 174.621 116.471 1.00 16.48  ? 1756 ILE A N     1 
ATOM   1776  C  CA    . ILE A 1 1756 ? 152.342 173.718 115.625 1.00 16.32  ? 1756 ILE A CA    1 
ATOM   1777  C  C     . ILE A 1 1756 ? 152.879 173.732 114.200 1.00 20.29  ? 1756 ILE A C     1 
ATOM   1778  O  O     . ILE A 1 1756 ? 153.065 172.679 113.576 1.00 24.26  ? 1756 ILE A O     1 
ATOM   1779  C  CB    . ILE A 1 1756 ? 150.851 174.096 115.669 1.00 15.00  ? 1756 ILE A CB    1 
ATOM   1780  C  CG1   . ILE A 1 1756 ? 150.250 173.755 117.032 1.00 19.78  ? 1756 ILE A CG1   1 
ATOM   1781  C  CG2   . ILE A 1 1756 ? 150.085 173.391 114.562 1.00 19.15  ? 1756 ILE A CG2   1 
ATOM   1782  C  CD1   . ILE A 1 1756 ? 148.885 174.358 117.259 1.00 23.41  ? 1756 ILE A CD1   1 
ATOM   1783  N  N     . ALA A 1 1757 ? 153.137 174.928 113.665 1.00 20.02  ? 1757 ALA A N     1 
ATOM   1784  C  CA    . ALA A 1 1757 ? 153.642 175.037 112.301 1.00 18.72  ? 1757 ALA A CA    1 
ATOM   1785  C  C     . ALA A 1 1757 ? 155.010 174.384 112.163 1.00 19.21  ? 1757 ALA A C     1 
ATOM   1786  O  O     . ALA A 1 1757 ? 155.266 173.664 111.190 1.00 23.29  ? 1757 ALA A O     1 
ATOM   1787  C  CB    . ALA A 1 1757 ? 153.702 176.504 111.878 1.00 21.40  ? 1757 ALA A CB    1 
ATOM   1788  N  N     . TRP A 1 1758 ? 155.903 174.616 113.130 1.00 17.25  ? 1758 TRP A N     1 
ATOM   1789  C  CA    . TRP A 1 1758 ? 157.228 174.010 113.063 1.00 17.46  ? 1758 TRP A CA    1 
ATOM   1790  C  C     . TRP A 1 1758 ? 157.149 172.491 113.157 1.00 20.85  ? 1758 TRP A C     1 
ATOM   1791  O  O     . TRP A 1 1758 ? 157.848 171.783 112.423 1.00 27.01  ? 1758 TRP A O     1 
ATOM   1792  C  CB    . TRP A 1 1758 ? 158.120 174.565 114.172 1.00 15.32  ? 1758 TRP A CB    1 
ATOM   1793  C  CG    . TRP A 1 1758 ? 159.393 173.798 114.337 1.00 16.50  ? 1758 TRP A CG    1 
ATOM   1794  C  CD1   . TRP A 1 1758 ? 160.513 173.895 113.565 1.00 17.77  ? 1758 TRP A CD1   1 
ATOM   1795  C  CD2   . TRP A 1 1758 ? 159.672 172.804 115.328 1.00 17.08  ? 1758 TRP A CD2   1 
ATOM   1796  N  NE1   . TRP A 1 1758 ? 161.476 173.028 114.019 1.00 16.45  ? 1758 TRP A NE1   1 
ATOM   1797  C  CE2   . TRP A 1 1758 ? 160.984 172.346 115.100 1.00 15.64  ? 1758 TRP A CE2   1 
ATOM   1798  C  CE3   . TRP A 1 1758 ? 158.942 172.259 116.388 1.00 16.90  ? 1758 TRP A CE3   1 
ATOM   1799  C  CZ2   . TRP A 1 1758 ? 161.581 171.370 115.893 1.00 15.62  ? 1758 TRP A CZ2   1 
ATOM   1800  C  CZ3   . TRP A 1 1758 ? 159.536 171.290 117.173 1.00 18.61  ? 1758 TRP A CZ3   1 
ATOM   1801  C  CH2   . TRP A 1 1758 ? 160.842 170.856 116.922 1.00 19.27  ? 1758 TRP A CH2   1 
ATOM   1802  N  N     . SER A 1 1759 ? 156.309 171.973 114.057 1.00 21.09  ? 1759 SER A N     1 
ATOM   1803  C  CA    . SER A 1 1759 ? 156.170 170.528 114.190 1.00 18.36  ? 1759 SER A CA    1 
ATOM   1804  C  C     . SER A 1 1759 ? 155.610 169.909 112.918 1.00 23.53  ? 1759 SER A C     1 
ATOM   1805  O  O     . SER A 1 1759 ? 156.073 168.851 112.480 1.00 31.91  ? 1759 SER A O     1 
ATOM   1806  C  CB    . SER A 1 1759 ? 155.282 170.193 115.388 1.00 20.84  ? 1759 SER A CB    1 
ATOM   1807  O  OG    . SER A 1 1759 ? 155.857 170.662 116.594 1.00 26.35  ? 1759 SER A OG    1 
ATOM   1808  N  N     . GLU A 1 1760 ? 154.614 170.556 112.308 1.00 25.05  ? 1760 GLU A N     1 
ATOM   1809  C  CA    . GLU A 1 1760 ? 154.060 170.042 111.060 1.00 26.89  ? 1760 GLU A CA    1 
ATOM   1810  C  C     . GLU A 1 1760 ? 155.098 170.066 109.945 1.00 28.97  ? 1760 GLU A C     1 
ATOM   1811  O  O     . GLU A 1 1760 ? 155.199 169.114 109.161 1.00 32.79  ? 1760 GLU A O     1 
ATOM   1812  C  CB    . GLU A 1 1760 ? 152.823 170.846 110.663 1.00 28.18  ? 1760 GLU A CB    1 
ATOM   1813  C  CG    . GLU A 1 1760 ? 151.602 170.566 111.525 1.00 37.14  ? 1760 GLU A CG    1 
ATOM   1814  C  CD    . GLU A 1 1760 ? 150.357 171.267 111.021 1.00 61.60  ? 1760 GLU A CD    1 
ATOM   1815  O  OE1   . GLU A 1 1760 ? 150.420 172.491 110.777 1.00 58.35  ? 1760 GLU A OE1   1 
ATOM   1816  O  OE2   . GLU A 1 1760 ? 149.315 170.596 110.871 1.00 64.42  ? 1760 GLU A OE2   1 
ATOM   1817  N  N     . ASN A 1 1761 ? 155.885 171.143 109.863 1.00 26.93  ? 1761 ASN A N     1 
ATOM   1818  C  CA    . ASN A 1 1761 ? 156.925 171.222 108.842 1.00 24.81  ? 1761 ASN A CA    1 
ATOM   1819  C  C     . ASN A 1 1761 ? 157.963 170.124 109.027 1.00 27.62  ? 1761 ASN A C     1 
ATOM   1820  O  O     . ASN A 1 1761 ? 158.366 169.471 108.056 1.00 37.46  ? 1761 ASN A O     1 
ATOM   1821  C  CB    . ASN A 1 1761 ? 157.592 172.596 108.877 1.00 22.93  ? 1761 ASN A CB    1 
ATOM   1822  C  CG    . ASN A 1 1761 ? 156.726 173.681 108.272 1.00 30.70  ? 1761 ASN A CG    1 
ATOM   1823  O  OD1   . ASN A 1 1761 ? 155.566 173.448 107.933 1.00 37.63  ? 1761 ASN A OD1   1 
ATOM   1824  N  ND2   . ASN A 1 1761 ? 157.286 174.876 108.133 1.00 35.67  ? 1761 ASN A ND2   1 
ATOM   1825  N  N     . VAL A 1 1762 ? 158.404 169.901 110.267 1.00 24.72  ? 1762 VAL A N     1 
ATOM   1826  C  CA    . VAL A 1 1762 ? 159.407 168.872 110.522 1.00 24.98  ? 1762 VAL A CA    1 
ATOM   1827  C  C     . VAL A 1 1762 ? 158.842 167.487 110.231 1.00 29.62  ? 1762 VAL A C     1 
ATOM   1828  O  O     . VAL A 1 1762 ? 159.529 166.631 109.663 1.00 33.47  ? 1762 VAL A O     1 
ATOM   1829  C  CB    . VAL A 1 1762 ? 159.938 168.980 111.963 1.00 20.97  ? 1762 VAL A CB    1 
ATOM   1830  C  CG1   . VAL A 1 1762 ? 160.877 167.828 112.267 1.00 26.60  ? 1762 VAL A CG1   1 
ATOM   1831  C  CG2   . VAL A 1 1762 ? 160.653 170.303 112.161 1.00 22.12  ? 1762 VAL A CG2   1 
ATOM   1832  N  N     . GLU A 1 1763 ? 157.585 167.243 110.614 1.00 31.26  ? 1763 GLU A N     1 
ATOM   1833  C  CA    . GLU A 1 1763 ? 156.966 165.952 110.335 1.00 31.55  ? 1763 GLU A CA    1 
ATOM   1834  C  C     . GLU A 1 1763 ? 156.867 165.701 108.836 1.00 40.10  ? 1763 GLU A C     1 
ATOM   1835  O  O     . GLU A 1 1763 ? 157.180 164.603 108.362 1.00 48.73  ? 1763 GLU A O     1 
ATOM   1836  C  CB    . GLU A 1 1763 ? 155.583 165.884 110.983 1.00 27.47  ? 1763 GLU A CB    1 
ATOM   1837  C  CG    . GLU A 1 1763 ? 154.954 164.502 110.969 1.00 36.64  ? 1763 GLU A CG    1 
ATOM   1838  C  CD    . GLU A 1 1763 ? 155.272 163.703 112.217 1.00 43.60  ? 1763 GLU A CD    1 
ATOM   1839  O  OE1   . GLU A 1 1763 ? 156.001 164.222 113.087 1.00 40.00  ? 1763 GLU A OE1   1 
ATOM   1840  O  OE2   . GLU A 1 1763 ? 154.791 162.555 112.327 1.00 45.27  ? 1763 GLU A OE2   1 
ATOM   1841  N  N     . THR A 1 1764 ? 156.442 166.711 108.072 1.00 37.97  ? 1764 THR A N     1 
ATOM   1842  C  CA    . THR A 1 1764 ? 156.351 166.555 106.623 1.00 37.82  ? 1764 THR A CA    1 
ATOM   1843  C  C     . THR A 1 1764 ? 157.723 166.314 106.005 1.00 40.88  ? 1764 THR A C     1 
ATOM   1844  O  O     . THR A 1 1764 ? 157.877 165.451 105.132 1.00 48.11  ? 1764 THR A O     1 
ATOM   1845  C  CB    . THR A 1 1764 ? 155.692 167.787 106.003 1.00 38.84  ? 1764 THR A CB    1 
ATOM   1846  O  OG1   . THR A 1 1764 ? 154.380 167.959 106.555 1.00 41.79  ? 1764 THR A OG1   1 
ATOM   1847  C  CG2   . THR A 1 1764 ? 155.582 167.632 104.494 1.00 38.74  ? 1764 THR A CG2   1 
ATOM   1848  N  N     . ALA A 1 1765 ? 158.735 167.064 106.450 1.00 37.24  ? 1765 ALA A N     1 
ATOM   1849  C  CA    . ALA A 1 1765 ? 160.077 166.891 105.904 1.00 39.25  ? 1765 ALA A CA    1 
ATOM   1850  C  C     . ALA A 1 1765 ? 160.626 165.504 106.210 1.00 48.11  ? 1765 ALA A C     1 
ATOM   1851  O  O     . ALA A 1 1765 ? 161.247 164.870 105.348 1.00 57.49  ? 1765 ALA A O     1 
ATOM   1852  C  CB    . ALA A 1 1765 ? 161.009 167.972 106.452 1.00 43.57  ? 1765 ALA A CB    1 
ATOM   1853  N  N     . LEU A 1 1766 ? 160.413 165.015 107.434 1.00 46.98  ? 1766 LEU A N     1 
ATOM   1854  C  CA    . LEU A 1 1766 ? 160.898 163.687 107.796 1.00 47.94  ? 1766 LEU A CA    1 
ATOM   1855  C  C     . LEU A 1 1766 ? 160.141 162.598 107.046 1.00 56.06  ? 1766 LEU A C     1 
ATOM   1856  O  O     . LEU A 1 1766 ? 160.724 161.571 106.681 1.00 63.75  ? 1766 LEU A O     1 
ATOM   1857  C  CB    . LEU A 1 1766 ? 160.788 163.484 109.306 1.00 41.27  ? 1766 LEU A CB    1 
ATOM   1858  C  CG    . LEU A 1 1766 ? 161.813 164.249 110.146 1.00 37.77  ? 1766 LEU A CG    1 
ATOM   1859  C  CD1   . LEU A 1 1766 ? 161.684 163.888 111.615 1.00 33.35  ? 1766 LEU A CD1   1 
ATOM   1860  C  CD2   . LEU A 1 1766 ? 163.223 163.982 109.646 1.00 42.74  ? 1766 LEU A CD2   1 
ATOM   1861  N  N     . SER A 1 1767 ? 158.841 162.798 106.815 1.00 55.12  ? 1767 SER A N     1 
ATOM   1862  C  CA    . SER A 1 1767 ? 158.080 161.843 106.018 1.00 58.66  ? 1767 SER A CA    1 
ATOM   1863  C  C     . SER A 1 1767 ? 158.585 161.804 104.582 1.00 59.71  ? 1767 SER A C     1 
ATOM   1864  O  O     . SER A 1 1767 ? 158.649 160.733 103.967 1.00 66.39  ? 1767 SER A O     1 
ATOM   1865  C  CB    . SER A 1 1767 ? 156.593 162.193 106.058 1.00 55.56  ? 1767 SER A CB    1 
ATOM   1866  O  OG    . SER A 1 1767 ? 156.105 162.184 107.388 1.00 56.24  ? 1767 SER A OG    1 
ATOM   1867  N  N     . SER A 1 1768 ? 158.942 162.965 104.029 1.00 58.30  ? 1768 SER A N     1 
ATOM   1868  C  CA    . SER A 1 1768 ? 159.521 162.999 102.689 1.00 64.12  ? 1768 SER A CA    1 
ATOM   1869  C  C     . SER A 1 1768 ? 160.855 162.263 102.647 1.00 72.18  ? 1768 SER A C     1 
ATOM   1870  O  O     . SER A 1 1768 ? 161.164 161.577 101.666 1.00 79.51  ? 1768 SER A O     1 
ATOM   1871  C  CB    . SER A 1 1768 ? 159.689 164.447 102.227 1.00 61.41  ? 1768 SER A CB    1 
ATOM   1872  O  OG    . SER A 1 1768 ? 160.655 164.544 101.196 1.00 64.07  ? 1768 SER A OG    1 
ATOM   1873  N  N     . MET A 1 1769 ? 161.660 162.395 103.705 1.00 71.21  ? 1769 MET A N     1 
ATOM   1874  C  CA    . MET A 1 1769 ? 162.954 161.723 103.757 1.00 76.74  ? 1769 MET A CA    1 
ATOM   1875  C  C     . MET A 1 1769 ? 162.836 160.248 104.115 1.00 83.62  ? 1769 MET A C     1 
ATOM   1876  O  O     . MET A 1 1769 ? 163.857 159.553 104.154 1.00 90.83  ? 1769 MET A O     1 
ATOM   1877  C  CB    . MET A 1 1769 ? 163.871 162.415 104.765 1.00 75.68  ? 1769 MET A CB    1 
ATOM   1878  C  CG    . MET A 1 1769 ? 164.288 163.818 104.378 1.00 81.79  ? 1769 MET A CG    1 
ATOM   1879  S  SD    . MET A 1 1769 ? 165.297 164.591 105.655 1.00 91.82  ? 1769 MET A SD    1 
ATOM   1880  C  CE    . MET A 1 1769 ? 166.807 163.641 105.504 1.00 88.92  ? 1769 MET A CE    1 
ATOM   1881  N  N     . GLY A 1 1770 ? 161.628 159.757 104.377 1.00 81.04  ? 1770 GLY A N     1 
ATOM   1882  C  CA    . GLY A 1 1770 ? 161.438 158.388 104.816 1.00 89.11  ? 1770 GLY A CA    1 
ATOM   1883  C  C     . GLY A 1 1770 ? 161.877 157.339 103.814 1.00 101.85 ? 1770 GLY A C     1 
ATOM   1884  O  O     . GLY A 1 1770 ? 162.039 156.168 104.169 1.00 103.11 ? 1770 GLY A O     1 
ATOM   1885  N  N     . GLY A 1 1771 ? 162.075 157.744 102.559 1.00 104.47 ? 1771 GLY A N     1 
ATOM   1886  C  CA    . GLY A 1 1771 ? 162.512 156.808 101.539 1.00 111.37 ? 1771 GLY A CA    1 
ATOM   1887  C  C     . GLY A 1 1771 ? 163.936 156.324 101.715 1.00 122.75 ? 1771 GLY A C     1 
ATOM   1888  O  O     . GLY A 1 1771 ? 164.290 155.263 101.188 1.00 128.55 ? 1771 GLY A O     1 
ATOM   1889  N  N     . GLY A 1 1772 ? 164.762 157.074 102.440 1.00 124.89 ? 1772 GLY A N     1 
ATOM   1890  C  CA    . GLY A 1 1772 ? 166.134 156.672 102.680 1.00 127.88 ? 1772 GLY A CA    1 
ATOM   1891  C  C     . GLY A 1 1772 ? 167.092 157.134 101.601 1.00 136.77 ? 1772 GLY A C     1 
ATOM   1892  O  O     . GLY A 1 1772 ? 166.870 156.874 100.414 1.00 143.86 ? 1772 GLY A O     1 
ATOM   1893  N  N     . GLY A 1 1773 ? 168.163 157.816 102.002 1.00 129.36 ? 1773 GLY A N     1 
ATOM   1894  C  CA    . GLY A 1 1773 ? 169.141 158.320 101.058 1.00 130.10 ? 1773 GLY A CA    1 
ATOM   1895  C  C     . GLY A 1 1773 ? 168.560 159.321 100.081 1.00 134.85 ? 1773 GLY A C     1 
ATOM   1896  O  O     . GLY A 1 1773 ? 168.858 159.279 98.884  1.00 133.67 ? 1773 GLY A O     1 
ATOM   1897  N  N     . ASP A 1 1774 ? 167.727 160.226 100.585 1.00 135.19 ? 1774 ASP A N     1 
ATOM   1898  C  CA    . ASP A 1 1774 ? 167.034 161.207 99.767  1.00 131.24 ? 1774 ASP A CA    1 
ATOM   1899  C  C     . ASP A 1 1774 ? 167.502 162.609 100.137 1.00 128.36 ? 1774 ASP A C     1 
ATOM   1900  O  O     . ASP A 1 1774 ? 168.051 162.839 101.218 1.00 120.43 ? 1774 ASP A O     1 
ATOM   1901  C  CB    . ASP A 1 1774 ? 165.511 161.088 99.944  1.00 124.64 ? 1774 ASP A CB    1 
ATOM   1902  C  CG    . ASP A 1 1774 ? 164.738 161.994 99.005  1.00 125.25 ? 1774 ASP A CG    1 
ATOM   1903  O  OD1   . ASP A 1 1774 ? 164.873 161.833 97.774  1.00 130.58 ? 1774 ASP A OD1   1 
ATOM   1904  O  OD2   . ASP A 1 1774 ? 163.994 162.868 99.499  1.00 117.92 ? 1774 ASP A OD2   1 
ATOM   1905  N  N     . ALA A 1 1775 ? 167.290 163.546 99.213  1.00 126.40 ? 1775 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 1775 ? 167.595 164.944 99.482  1.00 117.46 ? 1775 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 1775 ? 166.794 165.430 100.683 1.00 109.73 ? 1775 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 1775 ? 165.633 165.058 100.868 1.00 104.28 ? 1775 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 1775 ? 167.287 165.802 98.254  1.00 108.25 ? 1775 ALA A CB    1 
ATOM   1910  N  N     . ALA A 1 1776 ? 167.428 166.264 101.507 1.00 104.21 ? 1776 ALA A N     1 
ATOM   1911  C  CA    . ALA A 1 1776 ? 166.858 166.644 102.790 1.00 86.51  ? 1776 ALA A CA    1 
ATOM   1912  C  C     . ALA A 1 1776 ? 166.165 167.992 102.685 1.00 78.34  ? 1776 ALA A C     1 
ATOM   1913  O  O     . ALA A 1 1776 ? 166.844 169.013 102.493 1.00 64.85  ? 1776 ALA A O     1 
ATOM   1914  C  CB    . ALA A 1 1776 ? 167.946 166.690 103.860 1.00 68.30  ? 1776 ALA A CB    1 
ATOM   1915  N  N     . PRO A 1 1777 ? 164.836 168.057 102.800 1.00 78.20  ? 1777 PRO A N     1 
ATOM   1916  C  CA    . PRO A 1 1777 ? 164.164 169.350 102.958 1.00 66.86  ? 1777 PRO A CA    1 
ATOM   1917  C  C     . PRO A 1 1777 ? 164.160 169.863 104.388 1.00 62.12  ? 1777 PRO A C     1 
ATOM   1918  O  O     . PRO A 1 1777 ? 163.573 170.919 104.646 1.00 62.60  ? 1777 PRO A O     1 
ATOM   1919  C  CB    . PRO A 1 1777 ? 162.738 169.051 102.478 1.00 57.21  ? 1777 PRO A CB    1 
ATOM   1920  C  CG    . PRO A 1 1777 ? 162.535 167.623 102.826 1.00 62.90  ? 1777 PRO A CG    1 
ATOM   1921  C  CD    . PRO A 1 1777 ? 163.874 166.948 102.671 1.00 71.46  ? 1777 PRO A CD    1 
ATOM   1922  N  N     . LEU A 1 1778 ? 164.788 169.141 105.321 1.00 59.20  ? 1778 LEU A N     1 
ATOM   1923  C  CA    . LEU A 1 1778 ? 164.925 169.642 106.684 1.00 49.21  ? 1778 LEU A CA    1 
ATOM   1924  C  C     . LEU A 1 1778 ? 165.783 170.899 106.725 1.00 49.88  ? 1778 LEU A C     1 
ATOM   1925  O  O     . LEU A 1 1778 ? 165.601 171.750 107.604 1.00 50.70  ? 1778 LEU A O     1 
ATOM   1926  C  CB    . LEU A 1 1778 ? 165.518 168.557 107.582 1.00 46.70  ? 1778 LEU A CB    1 
ATOM   1927  C  CG    . LEU A 1 1778 ? 165.036 168.509 109.033 1.00 43.56  ? 1778 LEU A CG    1 
ATOM   1928  C  CD1   . LEU A 1 1778 ? 163.536 168.289 109.090 1.00 42.33  ? 1778 LEU A CD1   1 
ATOM   1929  C  CD2   . LEU A 1 1778 ? 165.764 167.416 109.797 1.00 36.84  ? 1778 LEU A CD2   1 
ATOM   1930  N  N     . HIS A 1 1779 ? 166.720 171.032 105.783 1.00 46.19  ? 1779 HIS A N     1 
ATOM   1931  C  CA    . HIS A 1 1779 ? 167.482 172.270 105.672 1.00 50.01  ? 1779 HIS A CA    1 
ATOM   1932  C  C     . HIS A 1 1779 ? 166.568 173.442 105.338 1.00 49.92  ? 1779 HIS A C     1 
ATOM   1933  O  O     . HIS A 1 1779 ? 166.799 174.566 105.795 1.00 48.33  ? 1779 HIS A O     1 
ATOM   1934  C  CB    . HIS A 1 1779 ? 168.578 172.122 104.617 1.00 54.80  ? 1779 HIS A CB    1 
ATOM   1935  C  CG    . HIS A 1 1779 ? 169.625 171.112 104.972 1.00 61.61  ? 1779 HIS A CG    1 
ATOM   1936  N  ND1   . HIS A 1 1779 ? 169.687 169.867 104.386 1.00 65.82  ? 1779 HIS A ND1   1 
ATOM   1937  C  CD2   . HIS A 1 1779 ? 170.652 171.164 105.853 1.00 55.46  ? 1779 HIS A CD2   1 
ATOM   1938  C  CE1   . HIS A 1 1779 ? 170.706 169.195 104.890 1.00 60.47  ? 1779 HIS A CE1   1 
ATOM   1939  N  NE2   . HIS A 1 1779 ? 171.308 169.960 105.783 1.00 52.91  ? 1779 HIS A NE2   1 
ATOM   1940  N  N     . SER A 1 1780 ? 165.521 173.198 104.547 1.00 47.92  ? 1780 SER A N     1 
ATOM   1941  C  CA    . SER A 1 1780 ? 164.549 174.251 104.267 1.00 44.41  ? 1780 SER A CA    1 
ATOM   1942  C  C     . SER A 1 1780 ? 163.791 174.654 105.528 1.00 47.37  ? 1780 SER A C     1 
ATOM   1943  O  O     . SER A 1 1780 ? 163.519 175.841 105.742 1.00 56.32  ? 1780 SER A O     1 
ATOM   1944  C  CB    . SER A 1 1780 ? 163.579 173.796 103.178 1.00 42.67  ? 1780 SER A CB    1 
ATOM   1945  O  OG    . SER A 1 1780 ? 162.566 172.963 103.714 1.00 54.35  ? 1780 SER A OG    1 
ATOM   1946  N  N     . VAL A 1 1781 ? 163.443 173.681 106.372 1.00 42.49  ? 1781 VAL A N     1 
ATOM   1947  C  CA    . VAL A 1 1781 ? 162.783 173.991 107.639 1.00 40.18  ? 1781 VAL A CA    1 
ATOM   1948  C  C     . VAL A 1 1781 ? 163.707 174.818 108.526 1.00 44.39  ? 1781 VAL A C     1 
ATOM   1949  O  O     . VAL A 1 1781 ? 163.285 175.795 109.160 1.00 44.62  ? 1781 VAL A O     1 
ATOM   1950  C  CB    . VAL A 1 1781 ? 162.336 172.697 108.342 1.00 34.70  ? 1781 VAL A CB    1 
ATOM   1951  C  CG1   . VAL A 1 1781 ? 161.745 173.008 109.708 1.00 27.46  ? 1781 VAL A CG1   1 
ATOM   1952  C  CG2   . VAL A 1 1781 ? 161.334 171.944 107.482 1.00 40.73  ? 1781 VAL A CG2   1 
ATOM   1953  N  N     . LEU A 1 1782 ? 164.985 174.435 108.581 1.00 44.37  ? 1782 LEU A N     1 
ATOM   1954  C  CA    . LEU A 1 1782 ? 165.948 175.198 109.368 1.00 36.29  ? 1782 LEU A CA    1 
ATOM   1955  C  C     . LEU A 1 1782 ? 166.099 176.615 108.829 1.00 39.51  ? 1782 LEU A C     1 
ATOM   1956  O  O     . LEU A 1 1782 ? 166.196 177.572 109.603 1.00 47.81  ? 1782 LEU A O     1 
ATOM   1957  C  CB    . LEU A 1 1782 ? 167.299 174.483 109.388 1.00 37.96  ? 1782 LEU A CB    1 
ATOM   1958  C  CG    . LEU A 1 1782 ? 168.410 175.185 110.170 1.00 35.54  ? 1782 LEU A CG    1 
ATOM   1959  C  CD1   . LEU A 1 1782 ? 167.969 175.454 111.599 1.00 31.47  ? 1782 LEU A CD1   1 
ATOM   1960  C  CD2   . LEU A 1 1782 ? 169.689 174.364 110.147 1.00 40.68  ? 1782 LEU A CD2   1 
ATOM   1961  N  N     . SER A 1 1783 ? 166.128 176.767 107.503 1.00 33.90  ? 1783 SER A N     1 
ATOM   1962  C  CA    . SER A 1 1783 ? 166.230 178.094 106.906 1.00 35.11  ? 1783 SER A CA    1 
ATOM   1963  C  C     . SER A 1 1783 ? 165.007 178.941 107.231 1.00 39.93  ? 1783 SER A C     1 
ATOM   1964  O  O     . SER A 1 1783 ? 165.128 180.142 107.500 1.00 49.22  ? 1783 SER A O     1 
ATOM   1965  C  CB    . SER A 1 1783 ? 166.414 177.975 105.394 1.00 37.85  ? 1783 SER A CB    1 
ATOM   1966  O  OG    . SER A 1 1783 ? 167.566 177.212 105.079 1.00 46.99  ? 1783 SER A OG    1 
ATOM   1967  N  N     . ASN A 1 1784 ? 163.817 178.336 107.193 1.00 35.52  ? 1784 ASN A N     1 
ATOM   1968  C  CA    . ASN A 1 1784 ? 162.603 179.058 107.561 1.00 37.52  ? 1784 ASN A CA    1 
ATOM   1969  C  C     . ASN A 1 1784 ? 162.675 179.519 109.012 1.00 38.40  ? 1784 ASN A C     1 
ATOM   1970  O  O     . ASN A 1 1784 ? 162.355 180.673 109.327 1.00 40.66  ? 1784 ASN A O     1 
ATOM   1971  C  CB    . ASN A 1 1784 ? 161.385 178.160 107.322 1.00 42.30  ? 1784 ASN A CB    1 
ATOM   1972  C  CG    . ASN A 1 1784 ? 160.059 178.811 107.716 1.00 52.01  ? 1784 ASN A CG    1 
ATOM   1973  O  OD1   . ASN A 1 1784 ? 160.011 179.904 108.277 1.00 48.21  ? 1784 ASN A OD1   1 
ATOM   1974  N  ND2   . ASN A 1 1784 ? 158.967 178.118 107.420 1.00 58.02  ? 1784 ASN A ND2   1 
ATOM   1975  N  N     . VAL A 1 1785 ? 163.116 178.633 109.908 1.00 37.93  ? 1785 VAL A N     1 
ATOM   1976  C  CA    . VAL A 1 1785 ? 163.243 179.003 111.315 1.00 34.62  ? 1785 VAL A CA    1 
ATOM   1977  C  C     . VAL A 1 1785 ? 164.238 180.146 111.477 1.00 36.36  ? 1785 VAL A C     1 
ATOM   1978  O  O     . VAL A 1 1785 ? 163.985 181.111 112.209 1.00 39.71  ? 1785 VAL A O     1 
ATOM   1979  C  CB    . VAL A 1 1785 ? 163.644 177.777 112.157 1.00 29.47  ? 1785 VAL A CB    1 
ATOM   1980  C  CG1   . VAL A 1 1785 ? 164.058 178.203 113.555 1.00 26.73  ? 1785 VAL A CG1   1 
ATOM   1981  C  CG2   . VAL A 1 1785 ? 162.499 176.781 112.220 1.00 29.65  ? 1785 VAL A CG2   1 
ATOM   1982  N  N     . GLU A 1 1786 ? 165.379 180.062 110.787 1.00 33.07  ? 1786 GLU A N     1 
ATOM   1983  C  CA    . GLU A 1 1786 ? 166.405 181.093 110.911 1.00 32.04  ? 1786 GLU A CA    1 
ATOM   1984  C  C     . GLU A 1 1786 ? 165.922 182.438 110.382 1.00 34.94  ? 1786 GLU A C     1 
ATOM   1985  O  O     . GLU A 1 1786 ? 166.181 183.476 110.999 1.00 40.84  ? 1786 GLU A O     1 
ATOM   1986  C  CB    . GLU A 1 1786 ? 167.679 180.663 110.186 1.00 34.13  ? 1786 GLU A CB    1 
ATOM   1987  C  CG    . GLU A 1 1786 ? 168.370 179.456 110.796 1.00 40.65  ? 1786 GLU A CG    1 
ATOM   1988  C  CD    . GLU A 1 1786 ? 169.589 179.835 111.613 1.00 59.53  ? 1786 GLU A CD    1 
ATOM   1989  O  OE1   . GLU A 1 1786 ? 169.603 180.947 112.181 1.00 63.92  ? 1786 GLU A OE1   1 
ATOM   1990  O  OE2   . GLU A 1 1786 ? 170.533 179.022 111.686 1.00 66.77  ? 1786 GLU A OE2   1 
ATOM   1991  N  N     . VAL A 1 1787 ? 165.223 182.450 109.245 1.00 31.19  ? 1787 VAL A N     1 
ATOM   1992  C  CA    . VAL A 1 1787 ? 164.771 183.724 108.692 1.00 33.43  ? 1787 VAL A CA    1 
ATOM   1993  C  C     . VAL A 1 1787 ? 163.670 184.325 109.562 1.00 37.23  ? 1787 VAL A C     1 
ATOM   1994  O  O     . VAL A 1 1787 ? 163.622 185.546 109.768 1.00 41.36  ? 1787 VAL A O     1 
ATOM   1995  C  CB    . VAL A 1 1787 ? 164.334 183.567 107.221 1.00 31.32  ? 1787 VAL A CB    1 
ATOM   1996  C  CG1   . VAL A 1 1787 ? 163.126 182.660 107.086 1.00 33.02  ? 1787 VAL A CG1   1 
ATOM   1997  C  CG2   . VAL A 1 1787 ? 164.054 184.929 106.602 1.00 46.79  ? 1787 VAL A CG2   1 
ATOM   1998  N  N     . THR A 1 1788 ? 162.782 183.486 110.106 1.00 35.34  ? 1788 THR A N     1 
ATOM   1999  C  CA    . THR A 1 1788 ? 161.759 184.004 111.008 1.00 30.05  ? 1788 THR A CA    1 
ATOM   2000  C  C     . THR A 1 1788 ? 162.391 184.573 112.274 1.00 29.20  ? 1788 THR A C     1 
ATOM   2001  O  O     . THR A 1 1788 ? 161.969 185.623 112.776 1.00 33.61  ? 1788 THR A O     1 
ATOM   2002  C  CB    . THR A 1 1788 ? 160.755 182.906 111.356 1.00 30.25  ? 1788 THR A CB    1 
ATOM   2003  O  OG1   . THR A 1 1788 ? 160.197 182.372 110.150 1.00 37.69  ? 1788 THR A OG1   1 
ATOM   2004  C  CG2   . THR A 1 1788 ? 159.624 183.480 112.191 1.00 29.33  ? 1788 THR A CG2   1 
ATOM   2005  N  N     . LEU A 1 1789 ? 163.420 183.900 112.794 1.00 31.12  ? 1789 LEU A N     1 
ATOM   2006  C  CA    . LEU A 1 1789 ? 164.115 184.405 113.973 1.00 28.56  ? 1789 LEU A CA    1 
ATOM   2007  C  C     . LEU A 1 1789 ? 164.857 185.698 113.662 1.00 29.95  ? 1789 LEU A C     1 
ATOM   2008  O  O     . LEU A 1 1789 ? 164.962 186.581 114.518 1.00 36.05  ? 1789 LEU A O     1 
ATOM   2009  C  CB    . LEU A 1 1789 ? 165.074 183.342 114.506 1.00 26.19  ? 1789 LEU A CB    1 
ATOM   2010  C  CG    . LEU A 1 1789 ? 165.816 183.678 115.798 1.00 28.98  ? 1789 LEU A CG    1 
ATOM   2011  C  CD1   . LEU A 1 1789 ? 164.832 183.868 116.938 1.00 22.69  ? 1789 LEU A CD1   1 
ATOM   2012  C  CD2   . LEU A 1 1789 ? 166.813 182.585 116.129 1.00 31.45  ? 1789 LEU A CD2   1 
ATOM   2013  N  N     . ASN A 1 1790 ? 165.389 185.826 112.444 1.00 30.37  ? 1790 ASN A N     1 
ATOM   2014  C  CA    . ASN A 1 1790 ? 166.015 187.080 112.036 1.00 35.59  ? 1790 ASN A CA    1 
ATOM   2015  C  C     . ASN A 1 1790 ? 164.998 188.214 111.999 1.00 39.57  ? 1790 ASN A C     1 
ATOM   2016  O  O     . ASN A 1 1790 ? 165.288 189.336 112.435 1.00 41.40  ? 1790 ASN A O     1 
ATOM   2017  C  CB    . ASN A 1 1790 ? 166.681 186.916 110.670 1.00 39.31  ? 1790 ASN A CB    1 
ATOM   2018  C  CG    . ASN A 1 1790 ? 168.027 186.226 110.757 1.00 51.53  ? 1790 ASN A CG    1 
ATOM   2019  O  OD1   . ASN A 1 1790 ? 168.342 185.577 111.754 1.00 48.67  ? 1790 ASN A OD1   1 
ATOM   2020  N  ND2   . ASN A 1 1790 ? 168.830 186.363 109.709 1.00 52.18  ? 1790 ASN A ND2   1 
ATOM   2021  N  N     . VAL A 1 1791 ? 163.802 187.940 111.475 1.00 38.46  ? 1791 VAL A N     1 
ATOM   2022  C  CA    . VAL A 1 1791 ? 162.742 188.948 111.474 1.00 32.25  ? 1791 VAL A CA    1 
ATOM   2023  C  C     . VAL A 1 1791 ? 162.385 189.342 112.902 1.00 32.64  ? 1791 VAL A C     1 
ATOM   2024  O  O     . VAL A 1 1791 ? 162.204 190.525 113.214 1.00 37.18  ? 1791 VAL A O     1 
ATOM   2025  C  CB    . VAL A 1 1791 ? 161.511 188.440 110.703 1.00 29.75  ? 1791 VAL A CB    1 
ATOM   2026  C  CG1   . VAL A 1 1791 ? 160.401 189.476 110.742 1.00 38.94  ? 1791 VAL A CG1   1 
ATOM   2027  C  CG2   . VAL A 1 1791 ? 161.880 188.125 109.266 1.00 35.82  ? 1791 VAL A CG2   1 
ATOM   2028  N  N     . LEU A 1 1792 ? 162.282 188.353 113.792 1.00 33.20  ? 1792 LEU A N     1 
ATOM   2029  C  CA    . LEU A 1 1792 ? 161.962 188.643 115.189 1.00 28.73  ? 1792 LEU A CA    1 
ATOM   2030  C  C     . LEU A 1 1792 ? 163.057 189.468 115.858 1.00 31.29  ? 1792 LEU A C     1 
ATOM   2031  O  O     . LEU A 1 1792 ? 162.764 190.375 116.647 1.00 39.33  ? 1792 LEU A O     1 
ATOM   2032  C  CB    . LEU A 1 1792 ? 161.729 187.342 115.955 1.00 24.30  ? 1792 LEU A CB    1 
ATOM   2033  C  CG    . LEU A 1 1792 ? 160.472 186.548 115.602 1.00 25.21  ? 1792 LEU A CG    1 
ATOM   2034  C  CD1   . LEU A 1 1792 ? 160.612 185.111 116.063 1.00 23.52  ? 1792 LEU A CD1   1 
ATOM   2035  C  CD2   . LEU A 1 1792 ? 159.248 187.188 116.226 1.00 24.96  ? 1792 LEU A CD2   1 
ATOM   2036  N  N     . ALA A 1 1793 ? 164.324 189.157 115.574 1.00 28.08  ? 1793 ALA A N     1 
ATOM   2037  C  CA    . ALA A 1 1793 ? 165.427 189.927 116.141 1.00 31.46  ? 1793 ALA A CA    1 
ATOM   2038  C  C     . ALA A 1 1793 ? 165.415 191.363 115.634 1.00 40.50  ? 1793 ALA A C     1 
ATOM   2039  O  O     . ALA A 1 1793 ? 165.634 192.305 116.407 1.00 44.60  ? 1793 ALA A O     1 
ATOM   2040  C  CB    . ALA A 1 1793 ? 166.759 189.252 115.819 1.00 32.09  ? 1793 ALA A CB    1 
ATOM   2041  N  N     . ASP A 1 1794 ? 165.157 191.552 114.339 1.00 42.21  ? 1794 ASP A N     1 
ATOM   2042  C  CA    . ASP A 1 1794 ? 165.028 192.905 113.812 1.00 42.50  ? 1794 ASP A CA    1 
ATOM   2043  C  C     . ASP A 1 1794 ? 163.873 193.642 114.478 1.00 42.69  ? 1794 ASP A C     1 
ATOM   2044  O  O     . ASP A 1 1794 ? 163.984 194.834 114.785 1.00 45.48  ? 1794 ASP A O     1 
ATOM   2045  C  CB    . ASP A 1 1794 ? 164.842 192.864 112.295 1.00 48.94  ? 1794 ASP A CB    1 
ATOM   2046  C  CG    . ASP A 1 1794 ? 166.103 192.450 111.564 1.00 58.17  ? 1794 ASP A CG    1 
ATOM   2047  O  OD1   . ASP A 1 1794 ? 167.133 192.223 112.233 1.00 60.86  ? 1794 ASP A OD1   1 
ATOM   2048  O  OD2   . ASP A 1 1794 ? 166.066 192.354 110.319 1.00 57.47  ? 1794 ASP A OD2   1 
ATOM   2049  N  N     . SER A 1 1795 ? 162.762 192.942 114.722 1.00 43.76  ? 1795 SER A N     1 
ATOM   2050  C  CA    . SER A 1 1795 ? 161.616 193.567 115.373 1.00 38.88  ? 1795 SER A CA    1 
ATOM   2051  C  C     . SER A 1 1795 ? 161.939 193.978 116.805 1.00 35.38  ? 1795 SER A C     1 
ATOM   2052  O  O     . SER A 1 1795 ? 161.535 195.058 117.251 1.00 41.02  ? 1795 SER A O     1 
ATOM   2053  C  CB    . SER A 1 1795 ? 160.419 192.618 115.346 1.00 37.85  ? 1795 SER A CB    1 
ATOM   2054  O  OG    . SER A 1 1795 ? 160.101 192.240 114.018 1.00 47.23  ? 1795 SER A OG    1 
ATOM   2055  N  N     . VAL A 1 1796 ? 162.660 193.131 117.547 1.00 34.65  ? 1796 VAL A N     1 
ATOM   2056  C  CA    . VAL A 1 1796 ? 162.984 193.466 118.934 1.00 37.65  ? 1796 VAL A CA    1 
ATOM   2057  C  C     . VAL A 1 1796 ? 164.113 194.476 119.045 1.00 44.91  ? 1796 VAL A C     1 
ATOM   2058  O  O     . VAL A 1 1796 ? 164.293 195.067 120.118 1.00 48.05  ? 1796 VAL A O     1 
ATOM   2059  C  CB    . VAL A 1 1796 ? 163.368 192.236 119.780 1.00 29.17  ? 1796 VAL A CB    1 
ATOM   2060  C  CG1   . VAL A 1 1796 ? 162.211 191.259 119.859 1.00 29.53  ? 1796 VAL A CG1   1 
ATOM   2061  C  CG2   . VAL A 1 1796 ? 164.615 191.567 119.242 1.00 28.69  ? 1796 VAL A CG2   1 
ATOM   2062  N  N     . LEU A 1 1797 ? 164.887 194.687 117.976 1.00 43.60  ? 1797 LEU A N     1 
ATOM   2063  C  CA    . LEU A 1 1797 ? 165.908 195.731 118.014 1.00 39.62  ? 1797 LEU A CA    1 
ATOM   2064  C  C     . LEU A 1 1797 ? 165.287 197.115 118.174 1.00 44.96  ? 1797 LEU A C     1 
ATOM   2065  O  O     . LEU A 1 1797 ? 165.804 197.947 118.929 1.00 52.82  ? 1797 LEU A O     1 
ATOM   2066  C  CB    . LEU A 1 1797 ? 166.775 195.674 116.757 1.00 40.27  ? 1797 LEU A CB    1 
ATOM   2067  C  CG    . LEU A 1 1797 ? 167.877 194.613 116.742 1.00 52.56  ? 1797 LEU A CG    1 
ATOM   2068  C  CD1   . LEU A 1 1797 ? 168.852 194.867 115.604 1.00 60.54  ? 1797 LEU A CD1   1 
ATOM   2069  C  CD2   . LEU A 1 1797 ? 168.607 194.583 118.075 1.00 40.12  ? 1797 LEU A CD2   1 
ATOM   2070  N  N     . MET A 1 1798 ? 164.184 197.382 117.478 1.00 44.66  ? 1798 MET A N     1 
ATOM   2071  C  CA    . MET A 1 1798 ? 163.537 198.683 117.549 1.00 47.24  ? 1798 MET A CA    1 
ATOM   2072  C  C     . MET A 1 1798 ? 162.558 198.736 118.721 1.00 49.45  ? 1798 MET A C     1 
ATOM   2073  O  O     . MET A 1 1798 ? 162.437 197.799 119.515 1.00 52.09  ? 1798 MET A O     1 
ATOM   2074  C  CB    . MET A 1 1798 ? 162.827 199.005 116.235 1.00 46.84  ? 1798 MET A CB    1 
ATOM   2075  C  CG    . MET A 1 1798 ? 162.084 197.837 115.608 1.00 49.15  ? 1798 MET A CG    1 
ATOM   2076  S  SD    . MET A 1 1798 ? 161.647 198.157 113.887 1.00 76.67  ? 1798 MET A SD    1 
ATOM   2077  C  CE    . MET A 1 1798 ? 162.977 197.323 113.027 1.00 50.92  ? 1798 MET A CE    1 
ATOM   2078  N  N     . GLU A 1 1799 ? 161.846 199.856 118.829 1.00 58.64  ? 1799 GLU A N     1 
ATOM   2079  C  CA    . GLU A 1 1799 ? 160.900 200.065 119.917 1.00 59.10  ? 1799 GLU A CA    1 
ATOM   2080  C  C     . GLU A 1 1799 ? 159.555 199.435 119.579 1.00 57.20  ? 1799 GLU A C     1 
ATOM   2081  O  O     . GLU A 1 1799 ? 159.021 199.638 118.484 1.00 58.96  ? 1799 GLU A O     1 
ATOM   2082  C  CB    . GLU A 1 1799 ? 160.727 201.558 120.193 1.00 63.09  ? 1799 GLU A CB    1 
ATOM   2083  C  CG    . GLU A 1 1799 ? 161.847 202.174 121.010 1.00 77.14  ? 1799 GLU A CG    1 
ATOM   2084  C  CD    . GLU A 1 1799 ? 161.346 203.219 121.987 1.00 85.13  ? 1799 GLU A CD    1 
ATOM   2085  O  OE1   . GLU A 1 1799 ? 160.194 203.093 122.454 1.00 81.20  ? 1799 GLU A OE1   1 
ATOM   2086  O  OE2   . GLU A 1 1799 ? 162.102 204.165 122.289 1.00 85.65  ? 1799 GLU A OE2   1 
ATOM   2087  N  N     . GLN A 1 1800 ? 159.012 198.676 120.520 1.00 50.28  ? 1800 GLN A N     1 
ATOM   2088  C  CA    . GLN A 1 1800 ? 157.741 197.987 120.374 1.00 42.07  ? 1800 GLN A CA    1 
ATOM   2089  C  C     . GLN A 1 1800 ? 156.898 198.210 121.618 1.00 42.80  ? 1800 GLN A C     1 
ATOM   2090  O  O     . GLN A 1 1800 ? 157.430 198.499 122.695 1.00 43.52  ? 1800 GLN A O     1 
ATOM   2091  C  CB    . GLN A 1 1800 ? 157.949 196.481 120.151 1.00 40.70  ? 1800 GLN A CB    1 
ATOM   2092  C  CG    . GLN A 1 1800 ? 158.984 196.138 119.090 1.00 43.17  ? 1800 GLN A CG    1 
ATOM   2093  C  CD    . GLN A 1 1800 ? 158.415 196.169 117.686 1.00 47.15  ? 1800 GLN A CD    1 
ATOM   2094  O  OE1   . GLN A 1 1800 ? 157.234 196.449 117.488 1.00 54.90  ? 1800 GLN A OE1   1 
ATOM   2095  N  NE2   . GLN A 1 1800 ? 159.256 195.879 116.701 1.00 46.79  ? 1800 GLN A NE2   1 
ATOM   2096  N  N     . PRO A 1 1801 ? 155.575 198.097 121.502 1.00 45.20  ? 1801 PRO A N     1 
ATOM   2097  C  CA    . PRO A 1 1801 ? 154.733 198.183 122.690 1.00 40.39  ? 1801 PRO A CA    1 
ATOM   2098  C  C     . PRO A 1 1801 ? 155.044 197.049 123.644 1.00 42.21  ? 1801 PRO A C     1 
ATOM   2099  O  O     . PRO A 1 1801 ? 155.494 195.966 123.224 1.00 45.29  ? 1801 PRO A O     1 
ATOM   2100  C  CB    . PRO A 1 1801 ? 153.310 198.072 122.124 1.00 35.83  ? 1801 PRO A CB    1 
ATOM   2101  C  CG    . PRO A 1 1801 ? 153.432 198.491 120.702 1.00 37.84  ? 1801 PRO A CG    1 
ATOM   2102  C  CD    . PRO A 1 1801 ? 154.782 198.024 120.263 1.00 42.40  ? 1801 PRO A CD    1 
ATOM   2103  N  N     . PRO A 1 1802 ? 154.836 197.257 124.950 1.00 39.63  ? 1802 PRO A N     1 
ATOM   2104  C  CA    . PRO A 1 1802 ? 155.236 196.226 125.926 1.00 39.20  ? 1802 PRO A CA    1 
ATOM   2105  C  C     . PRO A 1 1802 ? 154.598 194.867 125.689 1.00 34.04  ? 1802 PRO A C     1 
ATOM   2106  O  O     . PRO A 1 1802 ? 155.274 193.842 125.834 1.00 32.98  ? 1802 PRO A O     1 
ATOM   2107  C  CB    . PRO A 1 1802 ? 154.798 196.832 127.268 1.00 42.24  ? 1802 PRO A CB    1 
ATOM   2108  C  CG    . PRO A 1 1802 ? 154.724 198.303 127.018 1.00 38.65  ? 1802 PRO A CG    1 
ATOM   2109  C  CD    . PRO A 1 1802 ? 154.270 198.450 125.600 1.00 36.23  ? 1802 PRO A CD    1 
ATOM   2110  N  N     . LEU A 1 1803 ? 153.317 194.825 125.315 1.00 33.21  ? 1803 LEU A N     1 
ATOM   2111  C  CA    . LEU A 1 1803 ? 152.678 193.541 125.045 1.00 30.16  ? 1803 LEU A CA    1 
ATOM   2112  C  C     . LEU A 1 1803 ? 153.274 192.881 123.808 1.00 31.82  ? 1803 LEU A C     1 
ATOM   2113  O  O     . LEU A 1 1803 ? 153.589 191.683 123.824 1.00 34.87  ? 1803 LEU A O     1 
ATOM   2114  C  CB    . LEU A 1 1803 ? 151.170 193.728 124.883 1.00 32.76  ? 1803 LEU A CB    1 
ATOM   2115  C  CG    . LEU A 1 1803 ? 150.326 192.459 125.003 1.00 35.18  ? 1803 LEU A CG    1 
ATOM   2116  C  CD1   . LEU A 1 1803 ? 150.250 192.010 126.452 1.00 38.18  ? 1803 LEU A CD1   1 
ATOM   2117  C  CD2   . LEU A 1 1803 ? 148.934 192.683 124.435 1.00 36.03  ? 1803 LEU A CD2   1 
ATOM   2118  N  N     . ARG A 1 1804 ? 153.446 193.649 122.731 1.00 29.67  ? 1804 ARG A N     1 
ATOM   2119  C  CA    . ARG A 1 1804 ? 154.095 193.109 121.544 1.00 28.13  ? 1804 ARG A CA    1 
ATOM   2120  C  C     . ARG A 1 1804 ? 155.546 192.748 121.822 1.00 29.41  ? 1804 ARG A C     1 
ATOM   2121  O  O     . ARG A 1 1804 ? 156.053 191.768 121.267 1.00 36.73  ? 1804 ARG A O     1 
ATOM   2122  C  CB    . ARG A 1 1804 ? 154.005 194.103 120.388 1.00 31.67  ? 1804 ARG A CB    1 
ATOM   2123  C  CG    . ARG A 1 1804 ? 154.318 193.490 119.034 1.00 36.71  ? 1804 ARG A CG    1 
ATOM   2124  C  CD    . ARG A 1 1804 ? 154.683 194.550 118.013 1.00 39.76  ? 1804 ARG A CD    1 
ATOM   2125  N  NE    . ARG A 1 1804 ? 153.576 195.461 117.749 1.00 48.22  ? 1804 ARG A NE    1 
ATOM   2126  C  CZ    . ARG A 1 1804 ? 153.659 196.533 116.973 1.00 48.93  ? 1804 ARG A CZ    1 
ATOM   2127  N  NH1   . ARG A 1 1804 ? 154.789 196.863 116.368 1.00 51.84  ? 1804 ARG A NH1   1 
ATOM   2128  N  NH2   . ARG A 1 1804 ? 152.582 197.292 116.798 1.00 53.31  ? 1804 ARG A NH2   1 
ATOM   2129  N  N     . ARG A 1 1805 ? 156.229 193.518 122.673 1.00 25.83  ? 1805 ARG A N     1 
ATOM   2130  C  CA    . ARG A 1 1805 ? 157.600 193.175 123.037 1.00 25.30  ? 1805 ARG A CA    1 
ATOM   2131  C  C     . ARG A 1 1805 ? 157.659 191.837 123.763 1.00 28.64  ? 1805 ARG A C     1 
ATOM   2132  O  O     . ARG A 1 1805 ? 158.542 191.015 123.493 1.00 30.28  ? 1805 ARG A O     1 
ATOM   2133  C  CB    . ARG A 1 1805 ? 158.209 194.281 123.897 1.00 30.11  ? 1805 ARG A CB    1 
ATOM   2134  C  CG    . ARG A 1 1805 ? 159.714 194.419 123.749 1.00 32.50  ? 1805 ARG A CG    1 
ATOM   2135  C  CD    . ARG A 1 1805 ? 160.334 195.051 124.982 1.00 42.11  ? 1805 ARG A CD    1 
ATOM   2136  N  NE    . ARG A 1 1805 ? 159.923 194.376 126.207 1.00 47.94  ? 1805 ARG A NE    1 
ATOM   2137  C  CZ    . ARG A 1 1805 ? 159.245 194.954 127.189 1.00 50.36  ? 1805 ARG A CZ    1 
ATOM   2138  N  NH1   . ARG A 1 1805 ? 158.884 196.225 127.124 1.00 45.64  ? 1805 ARG A NH1   1 
ATOM   2139  N  NH2   . ARG A 1 1805 ? 158.922 194.240 128.263 1.00 48.06  ? 1805 ARG A NH2   1 
ATOM   2140  N  N     . ARG A 1 1806 ? 156.727 191.599 124.690 1.00 30.36  ? 1806 ARG A N     1 
ATOM   2141  C  CA    . ARG A 1 1806 ? 156.690 190.313 125.381 1.00 24.16  ? 1806 ARG A CA    1 
ATOM   2142  C  C     . ARG A 1 1806 ? 156.361 189.177 124.420 1.00 23.47  ? 1806 ARG A C     1 
ATOM   2143  O  O     . ARG A 1 1806 ? 156.938 188.086 124.516 1.00 28.03  ? 1806 ARG A O     1 
ATOM   2144  C  CB    . ARG A 1 1806 ? 155.681 190.359 126.528 1.00 24.64  ? 1806 ARG A CB    1 
ATOM   2145  C  CG    . ARG A 1 1806 ? 156.058 191.323 127.639 1.00 29.33  ? 1806 ARG A CG    1 
ATOM   2146  C  CD    . ARG A 1 1806 ? 155.138 191.173 128.836 1.00 34.72  ? 1806 ARG A CD    1 
ATOM   2147  N  NE    . ARG A 1 1806 ? 155.455 189.979 129.611 1.00 40.89  ? 1806 ARG A NE    1 
ATOM   2148  C  CZ    . ARG A 1 1806 ? 154.845 189.633 130.736 1.00 43.25  ? 1806 ARG A CZ    1 
ATOM   2149  N  NH1   . ARG A 1 1806 ? 153.877 190.372 131.252 1.00 46.69  ? 1806 ARG A NH1   1 
ATOM   2150  N  NH2   . ARG A 1 1806 ? 155.218 188.520 131.360 1.00 40.36  ? 1806 ARG A NH2   1 
ATOM   2151  N  N     . LYS A 1 1807 ? 155.430 189.411 123.490 1.00 22.31  ? 1807 LYS A N     1 
ATOM   2152  C  CA    . LYS A 1 1807 ? 155.121 188.391 122.491 1.00 19.50  ? 1807 LYS A CA    1 
ATOM   2153  C  C     . LYS A 1 1807 ? 156.345 188.058 121.648 1.00 21.26  ? 1807 LYS A C     1 
ATOM   2154  O  O     . LYS A 1 1807 ? 156.627 186.884 121.380 1.00 24.38  ? 1807 LYS A O     1 
ATOM   2155  C  CB    . LYS A 1 1807 ? 153.972 188.855 121.597 1.00 21.44  ? 1807 LYS A CB    1 
ATOM   2156  C  CG    . LYS A 1 1807 ? 152.634 188.985 122.299 1.00 22.42  ? 1807 LYS A CG    1 
ATOM   2157  C  CD    . LYS A 1 1807 ? 151.545 189.369 121.313 1.00 24.90  ? 1807 LYS A CD    1 
ATOM   2158  C  CE    . LYS A 1 1807 ? 150.222 189.612 122.013 1.00 33.09  ? 1807 LYS A CE    1 
ATOM   2159  N  NZ    . LYS A 1 1807 ? 149.143 189.946 121.045 1.00 31.29  ? 1807 LYS A NZ    1 
ATOM   2160  N  N     . LEU A 1 1808 ? 157.087 189.083 121.224 1.00 21.59  ? 1808 LEU A N     1 
ATOM   2161  C  CA    . LEU A 1 1808 ? 158.294 188.860 120.436 1.00 20.87  ? 1808 LEU A CA    1 
ATOM   2162  C  C     . LEU A 1 1808 ? 159.356 188.126 121.244 1.00 22.13  ? 1808 LEU A C     1 
ATOM   2163  O  O     . LEU A 1 1808 ? 160.064 187.268 120.708 1.00 23.05  ? 1808 LEU A O     1 
ATOM   2164  C  CB    . LEU A 1 1808 ? 158.837 190.192 119.921 1.00 21.04  ? 1808 LEU A CB    1 
ATOM   2165  C  CG    . LEU A 1 1808 ? 157.983 190.966 118.914 1.00 24.91  ? 1808 LEU A CG    1 
ATOM   2166  C  CD1   . LEU A 1 1808 ? 158.354 192.438 118.927 1.00 29.78  ? 1808 LEU A CD1   1 
ATOM   2167  C  CD2   . LEU A 1 1808 ? 158.137 190.390 117.521 1.00 30.27  ? 1808 LEU A CD2   1 
ATOM   2168  N  N     . GLU A 1 1809 ? 159.490 188.456 122.531 1.00 20.93  ? 1809 GLU A N     1 
ATOM   2169  C  CA    . GLU A 1 1809 ? 160.450 187.752 123.377 1.00 18.93  ? 1809 GLU A CA    1 
ATOM   2170  C  C     . GLU A 1 1809 ? 160.095 186.276 123.504 1.00 18.06  ? 1809 GLU A C     1 
ATOM   2171  O  O     . GLU A 1 1809 ? 160.970 185.407 123.403 1.00 20.62  ? 1809 GLU A O     1 
ATOM   2172  C  CB    . GLU A 1 1809 ? 160.515 188.407 124.756 1.00 20.82  ? 1809 GLU A CB    1 
ATOM   2173  C  CG    . GLU A 1 1809 ? 161.239 189.742 124.782 1.00 24.54  ? 1809 GLU A CG    1 
ATOM   2174  C  CD    . GLU A 1 1809 ? 161.216 190.387 126.154 1.00 35.57  ? 1809 GLU A CD    1 
ATOM   2175  O  OE1   . GLU A 1 1809 ? 160.504 189.874 127.041 1.00 35.77  ? 1809 GLU A OE1   1 
ATOM   2176  O  OE2   . GLU A 1 1809 ? 161.909 191.409 126.344 1.00 39.75  ? 1809 GLU A OE2   1 
ATOM   2177  N  N     . HIS A 1 1810 ? 158.812 185.972 123.725 1.00 17.60  ? 1810 HIS A N     1 
ATOM   2178  C  CA    . HIS A 1 1810 ? 158.391 184.576 123.812 1.00 15.96  ? 1810 HIS A CA    1 
ATOM   2179  C  C     . HIS A 1 1810 ? 158.622 183.849 122.494 1.00 17.38  ? 1810 HIS A C     1 
ATOM   2180  O  O     . HIS A 1 1810 ? 159.074 182.696 122.480 1.00 18.35  ? 1810 HIS A O     1 
ATOM   2181  C  CB    . HIS A 1 1810 ? 156.920 184.489 124.219 1.00 15.23  ? 1810 HIS A CB    1 
ATOM   2182  C  CG    . HIS A 1 1810 ? 156.604 185.184 125.506 1.00 20.97  ? 1810 HIS A CG    1 
ATOM   2183  N  ND1   . HIS A 1 1810 ? 157.540 185.373 126.500 1.00 30.08  ? 1810 HIS A ND1   1 
ATOM   2184  C  CD2   . HIS A 1 1810 ? 155.452 185.727 125.965 1.00 19.71  ? 1810 HIS A CD2   1 
ATOM   2185  C  CE1   . HIS A 1 1810 ? 156.980 186.009 127.513 1.00 29.46  ? 1810 HIS A CE1   1 
ATOM   2186  N  NE2   . HIS A 1 1810 ? 155.713 186.235 127.215 1.00 29.35  ? 1810 HIS A NE2   1 
ATOM   2187  N  N     . LEU A 1 1811 ? 158.316 184.507 121.373 1.00 16.57  ? 1811 LEU A N     1 
ATOM   2188  C  CA    . LEU A 1 1811 ? 158.522 183.883 120.071 1.00 14.52  ? 1811 LEU A CA    1 
ATOM   2189  C  C     . LEU A 1 1811 ? 160.000 183.616 119.814 1.00 14.51  ? 1811 LEU A C     1 
ATOM   2190  O  O     . LEU A 1 1811 ? 160.361 182.564 119.280 1.00 18.59  ? 1811 LEU A O     1 
ATOM   2191  C  CB    . LEU A 1 1811 ? 157.931 184.760 118.969 1.00 13.75  ? 1811 LEU A CB    1 
ATOM   2192  C  CG    . LEU A 1 1811 ? 156.512 184.393 118.535 1.00 14.68  ? 1811 LEU A CG    1 
ATOM   2193  C  CD1   . LEU A 1 1811 ? 156.032 185.317 117.431 1.00 21.67  ? 1811 LEU A CD1   1 
ATOM   2194  C  CD2   . LEU A 1 1811 ? 156.448 182.943 118.090 1.00 15.68  ? 1811 LEU A CD2   1 
ATOM   2195  N  N     . ILE A 1 1812 ? 160.868 184.559 120.187 1.00 14.43  ? 1812 ILE A N     1 
ATOM   2196  C  CA    . ILE A 1 1812 ? 162.306 184.356 120.029 1.00 15.08  ? 1812 ILE A CA    1 
ATOM   2197  C  C     . ILE A 1 1812 ? 162.777 183.194 120.890 1.00 15.49  ? 1812 ILE A C     1 
ATOM   2198  O  O     . ILE A 1 1812 ? 163.560 182.346 120.443 1.00 18.56  ? 1812 ILE A O     1 
ATOM   2199  C  CB    . ILE A 1 1812 ? 163.069 185.651 120.365 1.00 15.75  ? 1812 ILE A CB    1 
ATOM   2200  C  CG1   . ILE A 1 1812 ? 162.970 186.646 119.211 1.00 17.00  ? 1812 ILE A CG1   1 
ATOM   2201  C  CG2   . ILE A 1 1812 ? 164.527 185.351 120.672 1.00 19.65  ? 1812 ILE A CG2   1 
ATOM   2202  C  CD1   . ILE A 1 1812 ? 163.763 187.911 119.432 1.00 20.14  ? 1812 ILE A CD1   1 
ATOM   2203  N  N     . THR A 1 1813 ? 162.312 183.136 122.141 1.00 15.86  ? 1813 THR A N     1 
ATOM   2204  C  CA    . THR A 1 1813 ? 162.720 182.055 123.033 1.00 15.12  ? 1813 THR A CA    1 
ATOM   2205  C  C     . THR A 1 1813 ? 162.292 180.700 122.485 1.00 17.12  ? 1813 THR A C     1 
ATOM   2206  O  O     . THR A 1 1813 ? 163.048 179.725 122.560 1.00 17.50  ? 1813 THR A O     1 
ATOM   2207  C  CB    . THR A 1 1813 ? 162.138 182.277 124.429 1.00 15.35  ? 1813 THR A CB    1 
ATOM   2208  O  OG1   . THR A 1 1813 ? 162.484 183.589 124.889 1.00 16.06  ? 1813 THR A OG1   1 
ATOM   2209  C  CG2   . THR A 1 1813 ? 162.684 181.248 125.404 1.00 14.69  ? 1813 THR A CG2   1 
ATOM   2210  N  N     . GLU A 1 1814 ? 161.081 180.619 121.930 1.00 17.42  ? 1814 GLU A N     1 
ATOM   2211  C  CA    . GLU A 1 1814 ? 160.616 179.352 121.373 1.00 15.55  ? 1814 GLU A CA    1 
ATOM   2212  C  C     . GLU A 1 1814 ? 161.371 178.995 120.096 1.00 17.32  ? 1814 GLU A C     1 
ATOM   2213  O  O     . GLU A 1 1814 ? 161.727 177.828 119.880 1.00 23.06  ? 1814 GLU A O     1 
ATOM   2214  C  CB    . GLU A 1 1814 ? 159.112 179.418 121.110 1.00 15.29  ? 1814 GLU A CB    1 
ATOM   2215  C  CG    . GLU A 1 1814 ? 158.579 178.284 120.254 1.00 21.93  ? 1814 GLU A CG    1 
ATOM   2216  C  CD    . GLU A 1 1814 ? 158.845 176.919 120.864 1.00 34.33  ? 1814 GLU A CD    1 
ATOM   2217  O  OE1   . GLU A 1 1814 ? 158.835 176.806 122.108 1.00 35.54  ? 1814 GLU A OE1   1 
ATOM   2218  O  OE2   . GLU A 1 1814 ? 159.060 175.956 120.100 1.00 29.12  ? 1814 GLU A OE2   1 
ATOM   2219  N  N     . LEU A 1 1815 ? 161.635 179.984 119.239 1.00 15.58  ? 1815 LEU A N     1 
ATOM   2220  C  CA    . LEU A 1 1815 ? 162.282 179.703 117.966 1.00 14.45  ? 1815 LEU A CA    1 
ATOM   2221  C  C     . LEU A 1 1815 ? 163.759 179.374 118.116 1.00 17.53  ? 1815 LEU A C     1 
ATOM   2222  O  O     . LEU A 1 1815 ? 164.301 178.657 117.273 1.00 23.63  ? 1815 LEU A O     1 
ATOM   2223  C  CB    . LEU A 1 1815 ? 162.105 180.877 117.007 1.00 16.12  ? 1815 LEU A CB    1 
ATOM   2224  C  CG    . LEU A 1 1815 ? 160.998 180.673 115.972 1.00 16.71  ? 1815 LEU A CG    1 
ATOM   2225  C  CD1   . LEU A 1 1815 ? 159.625 180.670 116.625 1.00 15.98  ? 1815 LEU A CD1   1 
ATOM   2226  C  CD2   . LEU A 1 1815 ? 161.082 181.725 114.891 1.00 23.48  ? 1815 LEU A CD2   1 
ATOM   2227  N  N     . VAL A 1 1816 ? 164.427 179.870 119.159 1.00 16.30  ? 1816 VAL A N     1 
ATOM   2228  C  CA    . VAL A 1 1816 ? 165.796 179.428 119.415 1.00 15.17  ? 1816 VAL A CA    1 
ATOM   2229  C  C     . VAL A 1 1816 ? 165.819 177.935 119.719 1.00 16.72  ? 1816 VAL A C     1 
ATOM   2230  O  O     . VAL A 1 1816 ? 166.667 177.192 119.205 1.00 24.25  ? 1816 VAL A O     1 
ATOM   2231  C  CB    . VAL A 1 1816 ? 166.431 180.251 120.550 1.00 13.77  ? 1816 VAL A CB    1 
ATOM   2232  C  CG1   . VAL A 1 1816 ? 167.789 179.683 120.915 1.00 18.35  ? 1816 VAL A CG1   1 
ATOM   2233  C  CG2   . VAL A 1 1816 ? 166.583 181.699 120.124 1.00 17.42  ? 1816 VAL A CG2   1 
ATOM   2234  N  N     . HIS A 1 1817 ? 164.881 177.469 120.546 1.00 15.83  ? 1817 HIS A N     1 
ATOM   2235  C  CA    . HIS A 1 1817 ? 164.775 176.039 120.816 1.00 16.26  ? 1817 HIS A CA    1 
ATOM   2236  C  C     . HIS A 1 1817 ? 164.429 175.264 119.553 1.00 18.81  ? 1817 HIS A C     1 
ATOM   2237  O  O     . HIS A 1 1817 ? 164.957 174.170 119.323 1.00 24.78  ? 1817 HIS A O     1 
ATOM   2238  C  CB    . HIS A 1 1817 ? 163.733 175.780 121.902 1.00 14.57  ? 1817 HIS A CB    1 
ATOM   2239  C  CG    . HIS A 1 1817 ? 163.510 174.327 122.185 1.00 16.11  ? 1817 HIS A CG    1 
ATOM   2240  N  ND1   . HIS A 1 1817 ? 164.504 173.501 122.662 1.00 16.62  ? 1817 HIS A ND1   1 
ATOM   2241  C  CD2   . HIS A 1 1817 ? 162.407 173.553 122.054 1.00 18.82  ? 1817 HIS A CD2   1 
ATOM   2242  C  CE1   . HIS A 1 1817 ? 164.023 172.280 122.812 1.00 15.61  ? 1817 HIS A CE1   1 
ATOM   2243  N  NE2   . HIS A 1 1817 ? 162.752 172.285 122.452 1.00 19.54  ? 1817 HIS A NE2   1 
ATOM   2244  N  N     . GLN A 1 1818 ? 163.528 175.806 118.729 1.00 17.98  ? 1818 GLN A N     1 
ATOM   2245  C  CA    . GLN A 1 1818 ? 163.183 175.137 117.477 1.00 17.06  ? 1818 GLN A CA    1 
ATOM   2246  C  C     . GLN A 1 1818 ? 164.398 175.008 116.565 1.00 19.48  ? 1818 GLN A C     1 
ATOM   2247  O  O     . GLN A 1 1818 ? 164.625 173.951 115.964 1.00 22.22  ? 1818 GLN A O     1 
ATOM   2248  C  CB    . GLN A 1 1818 ? 162.060 175.893 116.768 1.00 15.43  ? 1818 GLN A CB    1 
ATOM   2249  C  CG    . GLN A 1 1818 ? 160.692 175.682 117.383 1.00 16.35  ? 1818 GLN A CG    1 
ATOM   2250  C  CD    . GLN A 1 1818 ? 159.617 176.512 116.714 1.00 20.46  ? 1818 GLN A CD    1 
ATOM   2251  O  OE1   . GLN A 1 1818 ? 159.877 177.218 115.741 1.00 26.09  ? 1818 GLN A OE1   1 
ATOM   2252  N  NE2   . GLN A 1 1818 ? 158.400 176.433 117.236 1.00 23.36  ? 1818 GLN A NE2   1 
ATOM   2253  N  N     . ARG A 1 1819 ? 165.192 176.075 116.455 1.00 20.66  ? 1819 ARG A N     1 
ATOM   2254  C  CA    . ARG A 1 1819 ? 166.401 176.036 115.640 1.00 19.54  ? 1819 ARG A CA    1 
ATOM   2255  C  C     . ARG A 1 1819 ? 167.402 175.027 116.184 1.00 23.78  ? 1819 ARG A C     1 
ATOM   2256  O  O     . ARG A 1 1819 ? 168.023 174.284 115.416 1.00 31.47  ? 1819 ARG A O     1 
ATOM   2257  C  CB    . ARG A 1 1819 ? 167.029 177.427 115.573 1.00 20.84  ? 1819 ARG A CB    1 
ATOM   2258  C  CG    . ARG A 1 1819 ? 168.257 177.515 114.688 1.00 34.52  ? 1819 ARG A CG    1 
ATOM   2259  C  CD    . ARG A 1 1819 ? 169.021 178.803 114.939 1.00 41.97  ? 1819 ARG A CD    1 
ATOM   2260  N  NE    . ARG A 1 1819 ? 169.510 178.880 116.311 1.00 45.08  ? 1819 ARG A NE    1 
ATOM   2261  C  CZ    . ARG A 1 1819 ? 169.848 180.006 116.925 1.00 48.43  ? 1819 ARG A CZ    1 
ATOM   2262  N  NH1   . ARG A 1 1819 ? 169.777 181.176 116.312 1.00 49.15  ? 1819 ARG A NH1   1 
ATOM   2263  N  NH2   . ARG A 1 1819 ? 170.272 179.955 118.184 1.00 43.51  ? 1819 ARG A NH2   1 
ATOM   2264  N  N     . ASP A 1 1820 ? 167.579 174.992 117.507 1.00 21.64  ? 1820 ASP A N     1 
ATOM   2265  C  CA    . ASP A 1 1820 ? 168.506 174.033 118.100 1.00 23.56  ? 1820 ASP A CA    1 
ATOM   2266  C  C     . ASP A 1 1820 ? 168.056 172.600 117.844 1.00 24.93  ? 1820 ASP A C     1 
ATOM   2267  O  O     . ASP A 1 1820 ? 168.872 171.734 117.506 1.00 29.55  ? 1820 ASP A O     1 
ATOM   2268  C  CB    . ASP A 1 1820 ? 168.643 174.295 119.599 1.00 28.13  ? 1820 ASP A CB    1 
ATOM   2269  C  CG    . ASP A 1 1820 ? 169.321 175.617 119.900 1.00 46.18  ? 1820 ASP A CG    1 
ATOM   2270  O  OD1   . ASP A 1 1820 ? 169.761 176.292 118.945 1.00 41.52  ? 1820 ASP A OD1   1 
ATOM   2271  O  OD2   . ASP A 1 1820 ? 169.413 175.984 121.090 1.00 50.64  ? 1820 ASP A OD2   1 
ATOM   2272  N  N     . VAL A 1 1821 ? 166.756 172.333 117.991 1.00 23.70  ? 1821 VAL A N     1 
ATOM   2273  C  CA    . VAL A 1 1821 ? 166.237 170.988 117.755 1.00 17.83  ? 1821 VAL A CA    1 
ATOM   2274  C  C     . VAL A 1 1821 ? 166.405 170.599 116.293 1.00 22.18  ? 1821 VAL A C     1 
ATOM   2275  O  O     . VAL A 1 1821 ? 166.787 169.467 115.978 1.00 27.44  ? 1821 VAL A O     1 
ATOM   2276  C  CB    . VAL A 1 1821 ? 164.767 170.894 118.203 1.00 13.24  ? 1821 VAL A CB    1 
ATOM   2277  C  CG1   . VAL A 1 1821 ? 164.133 169.615 117.686 1.00 17.33  ? 1821 VAL A CG1   1 
ATOM   2278  C  CG2   . VAL A 1 1821 ? 164.675 170.955 119.715 1.00 15.55  ? 1821 VAL A CG2   1 
ATOM   2279  N  N     . THR A 1 1822 ? 166.120 171.527 115.376 1.00 23.16  ? 1822 THR A N     1 
ATOM   2280  C  CA    . THR A 1 1822 ? 166.274 171.229 113.955 1.00 22.09  ? 1822 THR A CA    1 
ATOM   2281  C  C     . THR A 1 1822 ? 167.734 170.973 113.599 1.00 25.15  ? 1822 THR A C     1 
ATOM   2282  O  O     . THR A 1 1822 ? 168.038 170.073 112.806 1.00 30.64  ? 1822 THR A O     1 
ATOM   2283  C  CB    . THR A 1 1822 ? 165.706 172.372 113.115 1.00 23.57  ? 1822 THR A CB    1 
ATOM   2284  O  OG1   . THR A 1 1822 ? 164.321 172.554 113.432 1.00 23.09  ? 1822 THR A OG1   1 
ATOM   2285  C  CG2   . THR A 1 1822 ? 165.833 172.057 111.636 1.00 29.62  ? 1822 THR A CG2   1 
ATOM   2286  N  N     . ARG A 1 1823 ? 168.653 171.749 114.178 1.00 23.66  ? 1823 ARG A N     1 
ATOM   2287  C  CA    . ARG A 1 1823 ? 170.074 171.522 113.934 1.00 26.38  ? 1823 ARG A CA    1 
ATOM   2288  C  C     . ARG A 1 1823 ? 170.515 170.167 114.473 1.00 32.67  ? 1823 ARG A C     1 
ATOM   2289  O  O     . ARG A 1 1823 ? 171.300 169.461 113.829 1.00 39.89  ? 1823 ARG A O     1 
ATOM   2290  C  CB    . ARG A 1 1823 ? 170.898 172.645 114.562 1.00 26.96  ? 1823 ARG A CB    1 
ATOM   2291  C  CG    . ARG A 1 1823 ? 170.997 173.893 113.703 1.00 30.52  ? 1823 ARG A CG    1 
ATOM   2292  C  CD    . ARG A 1 1823 ? 172.346 174.570 113.869 1.00 41.65  ? 1823 ARG A CD    1 
ATOM   2293  N  NE    . ARG A 1 1823 ? 172.344 175.531 114.964 1.00 44.55  ? 1823 ARG A NE    1 
ATOM   2294  C  CZ    . ARG A 1 1823 ? 172.186 176.839 114.812 1.00 51.45  ? 1823 ARG A CZ    1 
ATOM   2295  N  NH1   . ARG A 1 1823 ? 172.006 177.379 113.618 1.00 47.81  ? 1823 ARG A NH1   1 
ATOM   2296  N  NH2   . ARG A 1 1823 ? 172.209 177.624 115.884 1.00 56.14  ? 1823 ARG A NH2   1 
ATOM   2297  N  N     . SER A 1 1824 ? 170.024 169.791 115.656 1.00 31.38  ? 1824 SER A N     1 
ATOM   2298  C  CA    . SER A 1 1824 ? 170.337 168.473 116.202 1.00 26.48  ? 1824 SER A CA    1 
ATOM   2299  C  C     . SER A 1 1824 ? 169.790 167.365 115.311 1.00 27.63  ? 1824 SER A C     1 
ATOM   2300  O  O     . SER A 1 1824 ? 170.449 166.339 115.107 1.00 32.32  ? 1824 SER A O     1 
ATOM   2301  C  CB    . SER A 1 1824 ? 169.779 168.347 117.619 1.00 29.21  ? 1824 SER A CB    1 
ATOM   2302  O  OG    . SER A 1 1824 ? 169.752 166.994 118.037 1.00 39.79  ? 1824 SER A OG    1 
ATOM   2303  N  N     . LEU A 1 1825 ? 168.579 167.552 114.781 1.00 27.33  ? 1825 LEU A N     1 
ATOM   2304  C  CA    . LEU A 1 1825 ? 167.999 166.567 113.874 1.00 27.66  ? 1825 LEU A CA    1 
ATOM   2305  C  C     . LEU A 1 1825 ? 168.830 166.434 112.605 1.00 30.55  ? 1825 LEU A C     1 
ATOM   2306  O  O     . LEU A 1 1825 ? 169.054 165.322 112.110 1.00 39.90  ? 1825 LEU A O     1 
ATOM   2307  C  CB    . LEU A 1 1825 ? 166.563 166.959 113.525 1.00 26.47  ? 1825 LEU A CB    1 
ATOM   2308  C  CG    . LEU A 1 1825 ? 165.478 166.860 114.601 1.00 24.91  ? 1825 LEU A CG    1 
ATOM   2309  C  CD1   . LEU A 1 1825 ? 164.099 166.922 113.966 1.00 25.47  ? 1825 LEU A CD1   1 
ATOM   2310  C  CD2   . LEU A 1 1825 ? 165.629 165.606 115.441 1.00 26.54  ? 1825 LEU A CD2   1 
ATOM   2311  N  N     . ILE A 1 1826 ? 169.291 167.561 112.060 1.00 29.52  ? 1826 ILE A N     1 
ATOM   2312  C  CA    . ILE A 1 1826 ? 170.057 167.538 110.818 1.00 30.34  ? 1826 ILE A CA    1 
ATOM   2313  C  C     . ILE A 1 1826 ? 171.422 166.896 111.037 1.00 35.86  ? 1826 ILE A C     1 
ATOM   2314  O  O     . ILE A 1 1826 ? 171.898 166.118 110.202 1.00 44.63  ? 1826 ILE A O     1 
ATOM   2315  C  CB    . ILE A 1 1826 ? 170.180 168.962 110.247 1.00 32.55  ? 1826 ILE A CB    1 
ATOM   2316  C  CG1   . ILE A 1 1826 ? 168.844 169.417 109.659 1.00 32.12  ? 1826 ILE A CG1   1 
ATOM   2317  C  CG2   . ILE A 1 1826 ? 171.270 169.030 109.188 1.00 37.44  ? 1826 ILE A CG2   1 
ATOM   2318  C  CD1   . ILE A 1 1826 ? 168.839 170.854 109.199 1.00 35.95  ? 1826 ILE A CD1   1 
ATOM   2319  N  N     . LYS A 1 1827 ? 172.071 167.206 112.163 1.00 33.14  ? 1827 LYS A N     1 
ATOM   2320  C  CA    . LYS A 1 1827 ? 173.409 166.680 112.418 1.00 33.88  ? 1827 LYS A CA    1 
ATOM   2321  C  C     . LYS A 1 1827 ? 173.401 165.159 112.519 1.00 38.69  ? 1827 LYS A C     1 
ATOM   2322  O  O     . LYS A 1 1827 ? 174.308 164.492 112.007 1.00 50.81  ? 1827 LYS A O     1 
ATOM   2323  C  CB    . LYS A 1 1827 ? 173.981 167.300 113.694 1.00 40.03  ? 1827 LYS A CB    1 
ATOM   2324  C  CG    . LYS A 1 1827 ? 175.052 166.459 114.371 1.00 46.67  ? 1827 LYS A CG    1 
ATOM   2325  C  CD    . LYS A 1 1827 ? 175.538 167.103 115.658 1.00 60.61  ? 1827 LYS A CD    1 
ATOM   2326  C  CE    . LYS A 1 1827 ? 176.306 168.384 115.380 1.00 61.05  ? 1827 LYS A CE    1 
ATOM   2327  N  NZ    . LYS A 1 1827 ? 176.419 169.235 116.596 1.00 62.43  ? 1827 LYS A NZ    1 
ATOM   2328  N  N     . SER A 1 1828 ? 172.382 164.593 113.161 1.00 35.85  ? 1828 SER A N     1 
ATOM   2329  C  CA    . SER A 1 1828 ? 172.310 163.153 113.372 1.00 37.40  ? 1828 SER A CA    1 
ATOM   2330  C  C     . SER A 1 1828 ? 171.898 162.382 112.125 1.00 41.15  ? 1828 SER A C     1 
ATOM   2331  O  O     . SER A 1 1828 ? 171.875 161.146 112.169 1.00 49.24  ? 1828 SER A O     1 
ATOM   2332  C  CB    . SER A 1 1828 ? 171.338 162.839 114.513 1.00 40.13  ? 1828 SER A CB    1 
ATOM   2333  O  OG    . SER A 1 1828 ? 171.714 163.511 115.702 1.00 48.99  ? 1828 SER A OG    1 
ATOM   2334  N  N     . LYS A 1 1829 ? 171.571 163.070 111.030 1.00 41.98  ? 1829 LYS A N     1 
ATOM   2335  C  CA    . LYS A 1 1829 ? 171.135 162.439 109.783 1.00 45.62  ? 1829 LYS A CA    1 
ATOM   2336  C  C     . LYS A 1 1829 ? 169.901 161.565 110.020 1.00 54.34  ? 1829 LYS A C     1 
ATOM   2337  O  O     . LYS A 1 1829 ? 169.911 160.349 109.822 1.00 61.64  ? 1829 LYS A O     1 
ATOM   2338  C  CB    . LYS A 1 1829 ? 172.271 161.632 109.144 1.00 52.28  ? 1829 LYS A CB    1 
ATOM   2339  C  CG    . LYS A 1 1829 ? 173.423 162.476 108.627 1.00 55.09  ? 1829 LYS A CG    1 
ATOM   2340  C  CD    . LYS A 1 1829 ? 174.480 161.608 107.965 1.00 61.52  ? 1829 LYS A CD    1 
ATOM   2341  C  CE    . LYS A 1 1829 ? 175.665 162.437 107.503 1.00 67.51  ? 1829 LYS A CE    1 
ATOM   2342  N  NZ    . LYS A 1 1829 ? 175.297 163.351 106.387 1.00 64.61  ? 1829 LYS A NZ    1 
ATOM   2343  N  N     . ILE A 1 1830 ? 168.829 162.218 110.453 1.00 49.84  ? 1830 ILE A N     1 
ATOM   2344  C  CA    . ILE A 1 1830 ? 167.592 161.524 110.789 1.00 49.22  ? 1830 ILE A CA    1 
ATOM   2345  C  C     . ILE A 1 1830 ? 166.644 161.595 109.600 1.00 54.51  ? 1830 ILE A C     1 
ATOM   2346  O  O     . ILE A 1 1830 ? 166.324 162.683 109.107 1.00 61.10  ? 1830 ILE A O     1 
ATOM   2347  C  CB    . ILE A 1 1830 ? 166.960 162.133 112.048 1.00 42.07  ? 1830 ILE A CB    1 
ATOM   2348  C  CG1   . ILE A 1 1830 ? 167.909 161.962 113.232 1.00 44.40  ? 1830 ILE A CG1   1 
ATOM   2349  C  CG2   . ILE A 1 1830 ? 165.614 161.489 112.338 1.00 37.50  ? 1830 ILE A CG2   1 
ATOM   2350  C  CD1   . ILE A 1 1830 ? 167.521 162.758 114.436 1.00 43.20  ? 1830 ILE A CD1   1 
ATOM   2351  N  N     . ASP A 1 1831 ? 166.190 160.430 109.137 1.00 54.73  ? 1831 ASP A N     1 
ATOM   2352  C  CA    . ASP A 1 1831 ? 165.348 160.340 107.956 1.00 60.12  ? 1831 ASP A CA    1 
ATOM   2353  C  C     . ASP A 1 1831 ? 163.972 159.744 108.213 1.00 59.07  ? 1831 ASP A C     1 
ATOM   2354  O  O     . ASP A 1 1831 ? 163.139 159.750 107.299 1.00 65.84  ? 1831 ASP A O     1 
ATOM   2355  C  CB    . ASP A 1 1831 ? 166.053 159.521 106.862 1.00 68.27  ? 1831 ASP A CB    1 
ATOM   2356  C  CG    . ASP A 1 1831 ? 166.356 158.096 107.297 1.00 74.01  ? 1831 ASP A CG    1 
ATOM   2357  O  OD1   . ASP A 1 1831 ? 166.072 157.745 108.462 1.00 72.29  ? 1831 ASP A OD1   1 
ATOM   2358  O  OD2   . ASP A 1 1831 ? 166.883 157.324 106.469 1.00 82.33  ? 1831 ASP A OD2   1 
ATOM   2359  N  N     . ASN A 1 1832 ? 163.704 159.237 109.412 1.00 53.33  ? 1832 ASN A N     1 
ATOM   2360  C  CA    . ASN A 1 1832 ? 162.432 158.608 109.737 1.00 51.63  ? 1832 ASN A CA    1 
ATOM   2361  C  C     . ASN A 1 1832 ? 161.691 159.451 110.764 1.00 50.28  ? 1832 ASN A C     1 
ATOM   2362  O  O     . ASN A 1 1832 ? 162.281 159.889 111.757 1.00 49.87  ? 1832 ASN A O     1 
ATOM   2363  C  CB    . ASN A 1 1832 ? 162.643 157.190 110.271 1.00 51.21  ? 1832 ASN A CB    1 
ATOM   2364  C  CG    . ASN A 1 1832 ? 161.383 156.351 110.207 1.00 54.86  ? 1832 ASN A CG    1 
ATOM   2365  O  OD1   . ASN A 1 1832 ? 160.450 156.666 109.469 1.00 55.51  ? 1832 ASN A OD1   1 
ATOM   2366  N  ND2   . ASN A 1 1832 ? 161.349 155.274 110.983 1.00 54.30  ? 1832 ASN A ND2   1 
ATOM   2367  N  N     . ALA A 1 1833 ? 160.399 159.678 110.520 1.00 44.89  ? 1833 ALA A N     1 
ATOM   2368  C  CA    . ALA A 1 1833 ? 159.573 160.421 111.463 1.00 39.48  ? 1833 ALA A CA    1 
ATOM   2369  C  C     . ALA A 1 1833 ? 159.294 159.643 112.741 1.00 39.83  ? 1833 ALA A C     1 
ATOM   2370  O  O     . ALA A 1 1833 ? 158.855 160.244 113.727 1.00 42.04  ? 1833 ALA A O     1 
ATOM   2371  C  CB    . ALA A 1 1833 ? 158.253 160.821 110.804 1.00 43.28  ? 1833 ALA A CB    1 
ATOM   2372  N  N     . LYS A 1 1834 ? 159.529 158.333 112.749 1.00 41.77  ? 1834 LYS A N     1 
ATOM   2373  C  CA    . LYS A 1 1834 ? 159.337 157.509 113.933 1.00 40.39  ? 1834 LYS A CA    1 
ATOM   2374  C  C     . LYS A 1 1834 ? 160.616 157.313 114.734 1.00 36.96  ? 1834 LYS A C     1 
ATOM   2375  O  O     . LYS A 1 1834 ? 160.604 156.574 115.723 1.00 37.29  ? 1834 LYS A O     1 
ATOM   2376  C  CB    . LYS A 1 1834 ? 158.759 156.145 113.541 1.00 43.74  ? 1834 LYS A CB    1 
ATOM   2377  C  CG    . LYS A 1 1834 ? 157.454 156.226 112.767 1.00 50.95  ? 1834 LYS A CG    1 
ATOM   2378  C  CD    . LYS A 1 1834 ? 156.397 156.999 113.542 1.00 51.96  ? 1834 LYS A CD    1 
ATOM   2379  C  CE    . LYS A 1 1834 ? 155.912 156.218 114.753 1.00 54.78  ? 1834 LYS A CE    1 
ATOM   2380  N  NZ    . LYS A 1 1834 ? 155.784 154.763 114.465 1.00 64.30  ? 1834 LYS A NZ    1 
ATOM   2381  N  N     . SER A 1 1835 ? 161.716 157.944 114.329 1.00 36.91  ? 1835 SER A N     1 
ATOM   2382  C  CA    . SER A 1 1835 ? 162.950 157.863 115.097 1.00 34.45  ? 1835 SER A CA    1 
ATOM   2383  C  C     . SER A 1 1835 ? 162.766 158.530 116.454 1.00 33.25  ? 1835 SER A C     1 
ATOM   2384  O  O     . SER A 1 1835 ? 162.089 159.554 116.574 1.00 37.61  ? 1835 SER A O     1 
ATOM   2385  C  CB    . SER A 1 1835 ? 164.096 158.525 114.335 1.00 39.40  ? 1835 SER A CB    1 
ATOM   2386  O  OG    . SER A 1 1835 ? 165.227 158.701 115.170 1.00 41.97  ? 1835 SER A OG    1 
ATOM   2387  N  N     . PHE A 1 1836 ? 163.375 157.940 117.485 1.00 29.72  ? 1836 PHE A N     1 
ATOM   2388  C  CA    . PHE A 1 1836 ? 163.176 158.445 118.838 1.00 23.55  ? 1836 PHE A CA    1 
ATOM   2389  C  C     . PHE A 1 1836 ? 163.807 159.812 119.057 1.00 22.75  ? 1836 PHE A C     1 
ATOM   2390  O  O     . PHE A 1 1836 ? 163.333 160.563 119.915 1.00 24.38  ? 1836 PHE A O     1 
ATOM   2391  C  CB    . PHE A 1 1836 ? 163.721 157.461 119.870 1.00 23.48  ? 1836 PHE A CB    1 
ATOM   2392  C  CG    . PHE A 1 1836 ? 163.230 157.724 121.263 1.00 21.52  ? 1836 PHE A CG    1 
ATOM   2393  C  CD1   . PHE A 1 1836 ? 161.897 157.537 121.586 1.00 21.60  ? 1836 PHE A CD1   1 
ATOM   2394  C  CD2   . PHE A 1 1836 ? 164.095 158.173 122.244 1.00 18.20  ? 1836 PHE A CD2   1 
ATOM   2395  C  CE1   . PHE A 1 1836 ? 161.440 157.784 122.864 1.00 20.99  ? 1836 PHE A CE1   1 
ATOM   2396  C  CE2   . PHE A 1 1836 ? 163.640 158.422 123.524 1.00 17.17  ? 1836 PHE A CE2   1 
ATOM   2397  C  CZ    . PHE A 1 1836 ? 162.312 158.226 123.834 1.00 20.84  ? 1836 PHE A CZ    1 
ATOM   2398  N  N     . GLU A 1 1837 ? 164.861 160.154 118.313 1.00 26.27  ? 1837 GLU A N     1 
ATOM   2399  C  CA    . GLU A 1 1837 ? 165.443 161.484 118.453 1.00 28.43  ? 1837 GLU A CA    1 
ATOM   2400  C  C     . GLU A 1 1837 ? 164.460 162.568 118.029 1.00 27.07  ? 1837 GLU A C     1 
ATOM   2401  O  O     . GLU A 1 1837 ? 164.578 163.717 118.467 1.00 27.18  ? 1837 GLU A O     1 
ATOM   2402  C  CB    . GLU A 1 1837 ? 166.735 161.583 117.647 1.00 34.84  ? 1837 GLU A CB    1 
ATOM   2403  C  CG    . GLU A 1 1837 ? 167.593 160.331 117.691 1.00 53.36  ? 1837 GLU A CG    1 
ATOM   2404  C  CD    . GLU A 1 1837 ? 169.061 160.623 117.453 1.00 70.52  ? 1837 GLU A CD    1 
ATOM   2405  O  OE1   . GLU A 1 1837 ? 169.407 161.806 117.249 1.00 72.78  ? 1837 GLU A OE1   1 
ATOM   2406  O  OE2   . GLU A 1 1837 ? 169.869 159.671 117.471 1.00 70.37  ? 1837 GLU A OE2   1 
ATOM   2407  N  N     . TRP A 1 1838 ? 163.492 162.223 117.181 1.00 25.74  ? 1838 TRP A N     1 
ATOM   2408  C  CA    . TRP A 1 1838 ? 162.370 163.106 116.892 1.00 20.29  ? 1838 TRP A CA    1 
ATOM   2409  C  C     . TRP A 1 1838 ? 161.163 162.812 117.770 1.00 22.42  ? 1838 TRP A C     1 
ATOM   2410  O  O     . TRP A 1 1838 ? 160.409 163.733 118.102 1.00 28.35  ? 1838 TRP A O     1 
ATOM   2411  C  CB    . TRP A 1 1838 ? 161.974 162.996 115.417 1.00 18.86  ? 1838 TRP A CB    1 
ATOM   2412  C  CG    . TRP A 1 1838 ? 160.685 163.689 115.082 1.00 20.72  ? 1838 TRP A CG    1 
ATOM   2413  C  CD1   . TRP A 1 1838 ? 159.567 163.120 114.546 1.00 23.65  ? 1838 TRP A CD1   1 
ATOM   2414  C  CD2   . TRP A 1 1838 ? 160.377 165.077 115.267 1.00 22.90  ? 1838 TRP A CD2   1 
ATOM   2415  N  NE1   . TRP A 1 1838 ? 158.585 164.065 114.382 1.00 19.74  ? 1838 TRP A NE1   1 
ATOM   2416  C  CE2   . TRP A 1 1838 ? 159.057 165.275 114.817 1.00 18.13  ? 1838 TRP A CE2   1 
ATOM   2417  C  CE3   . TRP A 1 1838 ? 161.090 166.171 115.767 1.00 25.96  ? 1838 TRP A CE3   1 
ATOM   2418  C  CZ2   . TRP A 1 1838 ? 158.435 166.520 114.853 1.00 23.67  ? 1838 TRP A CZ2   1 
ATOM   2419  C  CZ3   . TRP A 1 1838 ? 160.470 167.406 115.802 1.00 21.59  ? 1838 TRP A CZ3   1 
ATOM   2420  C  CH2   . TRP A 1 1838 ? 159.157 167.571 115.348 1.00 24.32  ? 1838 TRP A CH2   1 
ATOM   2421  N  N     . LEU A 1 1839 ? 160.966 161.549 118.157 1.00 20.33  ? 1839 LEU A N     1 
ATOM   2422  C  CA    . LEU A 1 1839 ? 159.844 161.208 119.023 1.00 16.82  ? 1839 LEU A CA    1 
ATOM   2423  C  C     . LEU A 1 1839 ? 160.022 161.768 120.428 1.00 17.64  ? 1839 LEU A C     1 
ATOM   2424  O  O     . LEU A 1 1839 ? 159.036 162.147 121.070 1.00 20.06  ? 1839 LEU A O     1 
ATOM   2425  C  CB    . LEU A 1 1839 ? 159.659 159.692 119.077 1.00 17.41  ? 1839 LEU A CB    1 
ATOM   2426  C  CG    . LEU A 1 1839 ? 159.003 159.036 117.860 1.00 20.26  ? 1839 LEU A CG    1 
ATOM   2427  C  CD1   . LEU A 1 1839 ? 158.623 157.598 118.170 1.00 29.11  ? 1839 LEU A CD1   1 
ATOM   2428  C  CD2   . LEU A 1 1839 ? 157.787 159.827 117.408 1.00 18.66  ? 1839 LEU A CD2   1 
ATOM   2429  N  N     . SER A 1 1840 ? 161.260 161.833 120.923 1.00 18.00  ? 1840 SER A N     1 
ATOM   2430  C  CA    . SER A 1 1840 ? 161.504 162.348 122.265 1.00 13.74  ? 1840 SER A CA    1 
ATOM   2431  C  C     . SER A 1 1840 ? 161.263 163.846 122.379 1.00 14.97  ? 1840 SER A C     1 
ATOM   2432  O  O     . SER A 1 1840 ? 161.170 164.356 123.500 1.00 19.20  ? 1840 SER A O     1 
ATOM   2433  C  CB    . SER A 1 1840 ? 162.934 162.026 122.702 1.00 14.56  ? 1840 SER A CB    1 
ATOM   2434  O  OG    . SER A 1 1840 ? 163.862 162.338 121.679 1.00 19.62  ? 1840 SER A OG    1 
ATOM   2435  N  N     . GLN A 1 1841 ? 161.163 164.558 121.261 1.00 17.36  ? 1841 GLN A N     1 
ATOM   2436  C  CA    . GLN A 1 1841 ? 160.870 165.980 121.293 1.00 18.33  ? 1841 GLN A CA    1 
ATOM   2437  C  C     . GLN A 1 1841 ? 159.374 166.212 121.482 1.00 16.96  ? 1841 GLN A C     1 
ATOM   2438  O  O     . GLN A 1 1841 ? 158.540 165.363 121.156 1.00 19.58  ? 1841 GLN A O     1 
ATOM   2439  C  CB    . GLN A 1 1841 ? 161.342 166.659 120.006 1.00 17.43  ? 1841 GLN A CB    1 
ATOM   2440  C  CG    . GLN A 1 1841 ? 162.766 166.322 119.603 1.00 17.31  ? 1841 GLN A CG    1 
ATOM   2441  C  CD    . GLN A 1 1841 ? 163.794 166.887 120.562 1.00 21.39  ? 1841 GLN A CD    1 
ATOM   2442  O  OE1   . GLN A 1 1841 ? 163.667 168.018 121.031 1.00 23.42  ? 1841 GLN A OE1   1 
ATOM   2443  N  NE2   . GLN A 1 1841 ? 164.821 166.100 120.858 1.00 21.77  ? 1841 GLN A NE2   1 
ATOM   2444  N  N     . MET A 1 1842 ? 159.039 167.380 122.022 1.00 15.50  ? 1842 MET A N     1 
ATOM   2445  C  CA    . MET A 1 1842 ? 157.642 167.775 122.134 1.00 14.65  ? 1842 MET A CA    1 
ATOM   2446  C  C     . MET A 1 1842 ? 157.124 168.188 120.763 1.00 19.95  ? 1842 MET A C     1 
ATOM   2447  O  O     . MET A 1 1842 ? 157.670 169.100 120.134 1.00 25.69  ? 1842 MET A O     1 
ATOM   2448  C  CB    . MET A 1 1842 ? 157.486 168.915 123.136 1.00 14.18  ? 1842 MET A CB    1 
ATOM   2449  C  CG    . MET A 1 1842 ? 156.076 169.063 123.683 1.00 14.56  ? 1842 MET A CG    1 
ATOM   2450  S  SD    . MET A 1 1842 ? 156.011 169.948 125.251 1.00 23.85  ? 1842 MET A SD    1 
ATOM   2451  C  CE    . MET A 1 1842 ? 155.790 168.592 126.398 1.00 16.44  ? 1842 MET A CE    1 
ATOM   2452  N  N     . ARG A 1 1843 ? 156.072 167.519 120.301 1.00 16.87  ? 1843 ARG A N     1 
ATOM   2453  C  CA    . ARG A 1 1843 ? 155.515 167.743 118.976 1.00 15.77  ? 1843 ARG A CA    1 
ATOM   2454  C  C     . ARG A 1 1843 ? 154.041 168.095 119.094 1.00 17.93  ? 1843 ARG A C     1 
ATOM   2455  O  O     . ARG A 1 1843 ? 153.325 167.542 119.934 1.00 17.59  ? 1843 ARG A O     1 
ATOM   2456  C  CB    . ARG A 1 1843 ? 155.696 166.508 118.089 1.00 14.60  ? 1843 ARG A CB    1 
ATOM   2457  C  CG    . ARG A 1 1843 ? 156.994 165.761 118.341 1.00 15.05  ? 1843 ARG A CG    1 
ATOM   2458  C  CD    . ARG A 1 1843 ? 157.073 164.477 117.538 1.00 17.46  ? 1843 ARG A CD    1 
ATOM   2459  N  NE    . ARG A 1 1843 ? 156.055 163.514 117.937 1.00 18.85  ? 1843 ARG A NE    1 
ATOM   2460  C  CZ    . ARG A 1 1843 ? 156.101 162.787 119.045 1.00 16.66  ? 1843 ARG A CZ    1 
ATOM   2461  N  NH1   . ARG A 1 1843 ? 157.102 162.897 119.902 1.00 17.23  ? 1843 ARG A NH1   1 
ATOM   2462  N  NH2   . ARG A 1 1843 ? 155.118 161.929 119.300 1.00 19.26  ? 1843 ARG A NH2   1 
ATOM   2463  N  N     . PHE A 1 1844 ? 153.594 169.020 118.250 1.00 20.03  ? 1844 PHE A N     1 
ATOM   2464  C  CA    . PHE A 1 1844 ? 152.227 169.520 118.271 1.00 17.75  ? 1844 PHE A CA    1 
ATOM   2465  C  C     . PHE A 1 1844 ? 151.547 169.162 116.959 1.00 23.63  ? 1844 PHE A C     1 
ATOM   2466  O  O     . PHE A 1 1844 ? 152.088 169.430 115.881 1.00 27.07  ? 1844 PHE A O     1 
ATOM   2467  C  CB    . PHE A 1 1844 ? 152.197 171.035 118.491 1.00 16.75  ? 1844 PHE A CB    1 
ATOM   2468  C  CG    . PHE A 1 1844 ? 152.867 171.480 119.762 1.00 17.05  ? 1844 PHE A CG    1 
ATOM   2469  C  CD1   . PHE A 1 1844 ? 154.248 171.559 119.844 1.00 14.55  ? 1844 PHE A CD1   1 
ATOM   2470  C  CD2   . PHE A 1 1844 ? 152.116 171.817 120.873 1.00 15.32  ? 1844 PHE A CD2   1 
ATOM   2471  C  CE1   . PHE A 1 1844 ? 154.865 171.965 121.009 1.00 14.51  ? 1844 PHE A CE1   1 
ATOM   2472  C  CE2   . PHE A 1 1844 ? 152.728 172.224 122.042 1.00 14.77  ? 1844 PHE A CE2   1 
ATOM   2473  C  CZ    . PHE A 1 1844 ? 154.104 172.298 122.109 1.00 16.40  ? 1844 PHE A CZ    1 
ATOM   2474  N  N     . TYR A 1 1845 ? 150.365 168.557 117.052 1.00 24.77  ? 1845 TYR A N     1 
ATOM   2475  C  CA    . TYR A 1 1845 ? 149.607 168.133 115.883 1.00 29.05  ? 1845 TYR A CA    1 
ATOM   2476  C  C     . TYR A 1 1845 ? 148.241 168.797 115.905 1.00 29.46  ? 1845 TYR A C     1 
ATOM   2477  O  O     . TYR A 1 1845 ? 147.536 168.743 116.917 1.00 34.09  ? 1845 TYR A O     1 
ATOM   2478  C  CB    . TYR A 1 1845 ? 149.459 166.610 115.844 1.00 24.93  ? 1845 TYR A CB    1 
ATOM   2479  C  CG    . TYR A 1 1845 ? 150.776 165.871 115.826 1.00 26.42  ? 1845 TYR A CG    1 
ATOM   2480  C  CD1   . TYR A 1 1845 ? 151.603 165.916 114.712 1.00 25.37  ? 1845 TYR A CD1   1 
ATOM   2481  C  CD2   . TYR A 1 1845 ? 151.195 165.132 116.923 1.00 26.04  ? 1845 TYR A CD2   1 
ATOM   2482  C  CE1   . TYR A 1 1845 ? 152.809 165.244 114.690 1.00 27.90  ? 1845 TYR A CE1   1 
ATOM   2483  C  CE2   . TYR A 1 1845 ? 152.400 164.456 116.910 1.00 25.21  ? 1845 TYR A CE2   1 
ATOM   2484  C  CZ    . TYR A 1 1845 ? 153.202 164.516 115.791 1.00 28.59  ? 1845 TYR A CZ    1 
ATOM   2485  O  OH    . TYR A 1 1845 ? 154.402 163.846 115.771 1.00 29.67  ? 1845 TYR A OH    1 
ATOM   2486  N  N     . PHE A 1 1846 ? 147.870 169.419 114.790 1.00 30.47  ? 1846 PHE A N     1 
ATOM   2487  C  CA    . PHE A 1 1846 ? 146.589 170.096 114.651 1.00 39.94  ? 1846 PHE A CA    1 
ATOM   2488  C  C     . PHE A 1 1846 ? 145.736 169.363 113.626 1.00 54.03  ? 1846 PHE A C     1 
ATOM   2489  O  O     . PHE A 1 1846 ? 146.192 169.096 112.510 1.00 57.42  ? 1846 PHE A O     1 
ATOM   2490  C  CB    . PHE A 1 1846 ? 146.781 171.555 114.234 1.00 39.70  ? 1846 PHE A CB    1 
ATOM   2491  C  CG    . PHE A 1 1846 ? 145.672 172.461 114.681 1.00 34.97  ? 1846 PHE A CG    1 
ATOM   2492  C  CD1   . PHE A 1 1846 ? 144.813 173.032 113.760 1.00 34.70  ? 1846 PHE A CD1   1 
ATOM   2493  C  CD2   . PHE A 1 1846 ? 145.486 172.736 116.024 1.00 32.96  ? 1846 PHE A CD2   1 
ATOM   2494  C  CE1   . PHE A 1 1846 ? 143.791 173.864 114.169 1.00 37.11  ? 1846 PHE A CE1   1 
ATOM   2495  C  CE2   . PHE A 1 1846 ? 144.466 173.567 116.440 1.00 35.76  ? 1846 PHE A CE2   1 
ATOM   2496  C  CZ    . PHE A 1 1846 ? 143.618 174.131 115.511 1.00 39.14  ? 1846 PHE A CZ    1 
ATOM   2497  N  N     . ASP A 1 1847 ? 144.501 169.043 114.008 1.00 53.41  ? 1847 ASP A N     1 
ATOM   2498  C  CA    . ASP A 1 1847 ? 143.569 168.349 113.126 1.00 55.16  ? 1847 ASP A CA    1 
ATOM   2499  C  C     . ASP A 1 1847 ? 142.380 169.254 112.834 1.00 64.97  ? 1847 ASP A C     1 
ATOM   2500  O  O     . ASP A 1 1847 ? 141.459 169.354 113.660 1.00 66.85  ? 1847 ASP A O     1 
ATOM   2501  C  CB    . ASP A 1 1847 ? 143.103 167.035 113.761 1.00 62.47  ? 1847 ASP A CB    1 
ATOM   2502  C  CG    . ASP A 1 1847 ? 142.161 166.254 112.865 1.00 72.93  ? 1847 ASP A CG    1 
ATOM   2503  O  OD1   . ASP A 1 1847 ? 140.956 166.580 112.834 1.00 72.35  ? 1847 ASP A OD1   1 
ATOM   2504  O  OD2   . ASP A 1 1847 ? 142.626 165.311 112.190 1.00 76.36  ? 1847 ASP A OD2   1 
ATOM   2505  N  N     . PRO A 1 1848 ? 142.351 169.939 111.687 1.00 70.46  ? 1848 PRO A N     1 
ATOM   2506  C  CA    . PRO A 1 1848 ? 141.194 170.791 111.371 1.00 71.44  ? 1848 PRO A CA    1 
ATOM   2507  C  C     . PRO A 1 1848 ? 139.901 170.019 111.179 1.00 74.93  ? 1848 PRO A C     1 
ATOM   2508  O  O     . PRO A 1 1848 ? 138.823 170.620 111.272 1.00 70.18  ? 1848 PRO A O     1 
ATOM   2509  C  CB    . PRO A 1 1848 ? 141.620 171.497 110.076 1.00 67.19  ? 1848 PRO A CB    1 
ATOM   2510  C  CG    . PRO A 1 1848 ? 142.652 170.600 109.478 1.00 61.50  ? 1848 PRO A CG    1 
ATOM   2511  C  CD    . PRO A 1 1848 ? 143.378 169.980 110.633 1.00 66.02  ? 1848 PRO A CD    1 
ATOM   2512  N  N     . LYS A 1 1849 ? 139.968 168.714 110.914 1.00 73.16  ? 1849 LYS A N     1 
ATOM   2513  C  CA    . LYS A 1 1849 ? 138.771 167.914 110.693 1.00 71.51  ? 1849 LYS A CA    1 
ATOM   2514  C  C     . LYS A 1 1849 ? 138.085 167.493 111.986 1.00 72.98  ? 1849 LYS A C     1 
ATOM   2515  O  O     . LYS A 1 1849 ? 136.990 166.925 111.928 1.00 84.70  ? 1849 LYS A O     1 
ATOM   2516  C  CB    . LYS A 1 1849 ? 139.115 166.668 109.873 1.00 73.20  ? 1849 LYS A CB    1 
ATOM   2517  C  CG    . LYS A 1 1849 ? 139.938 166.951 108.627 1.00 74.58  ? 1849 LYS A CG    1 
ATOM   2518  C  CD    . LYS A 1 1849 ? 139.083 167.556 107.527 1.00 74.23  ? 1849 LYS A CD    1 
ATOM   2519  C  CE    . LYS A 1 1849 ? 139.921 168.395 106.578 1.00 71.58  ? 1849 LYS A CE    1 
ATOM   2520  N  NZ    . LYS A 1 1849 ? 140.940 167.574 105.867 1.00 73.01  ? 1849 LYS A NZ    1 
ATOM   2521  N  N     . GLN A 1 1850 ? 138.695 167.750 113.141 1.00 67.09  ? 1850 GLN A N     1 
ATOM   2522  C  CA    . GLN A 1 1850 ? 138.095 167.358 114.408 1.00 67.95  ? 1850 GLN A CA    1 
ATOM   2523  C  C     . GLN A 1 1850 ? 136.881 168.229 114.712 1.00 71.83  ? 1850 GLN A C     1 
ATOM   2524  O  O     . GLN A 1 1850 ? 136.955 169.460 114.653 1.00 64.04  ? 1850 GLN A O     1 
ATOM   2525  C  CB    . GLN A 1 1850 ? 139.121 167.466 115.534 1.00 61.62  ? 1850 GLN A CB    1 
ATOM   2526  C  CG    . GLN A 1 1850 ? 138.634 166.937 116.872 1.00 60.31  ? 1850 GLN A CG    1 
ATOM   2527  C  CD    . GLN A 1 1850 ? 138.578 165.424 116.914 1.00 62.09  ? 1850 GLN A CD    1 
ATOM   2528  O  OE1   . GLN A 1 1850 ? 139.464 164.745 116.396 1.00 60.74  ? 1850 GLN A OE1   1 
ATOM   2529  N  NE2   . GLN A 1 1850 ? 137.533 164.888 117.532 1.00 59.74  ? 1850 GLN A NE2   1 
ATOM   2530  N  N     . THR A 1 1851 ? 135.758 167.582 115.034 1.00 75.32  ? 1851 THR A N     1 
ATOM   2531  C  CA    . THR A 1 1851 ? 134.544 168.326 115.356 1.00 73.23  ? 1851 THR A CA    1 
ATOM   2532  C  C     . THR A 1 1851 ? 134.691 169.084 116.669 1.00 72.79  ? 1851 THR A C     1 
ATOM   2533  O  O     . THR A 1 1851 ? 134.280 170.245 116.771 1.00 76.64  ? 1851 THR A O     1 
ATOM   2534  C  CB    . THR A 1 1851 ? 133.346 167.378 115.418 1.00 73.05  ? 1851 THR A CB    1 
ATOM   2535  O  OG1   . THR A 1 1851 ? 133.527 166.445 116.490 1.00 71.62  ? 1851 THR A OG1   1 
ATOM   2536  C  CG2   . THR A 1 1851 ? 133.203 166.617 114.108 1.00 67.15  ? 1851 THR A CG2   1 
ATOM   2537  N  N     . ASP A 1 1852 ? 135.273 168.447 117.682 1.00 65.17  ? 1852 ASP A N     1 
ATOM   2538  C  CA    . ASP A 1 1852 ? 135.488 169.087 118.974 1.00 63.00  ? 1852 ASP A CA    1 
ATOM   2539  C  C     . ASP A 1 1852 ? 136.696 170.008 118.867 1.00 64.15  ? 1852 ASP A C     1 
ATOM   2540  O  O     . ASP A 1 1852 ? 137.829 169.542 118.706 1.00 64.79  ? 1852 ASP A O     1 
ATOM   2541  C  CB    . ASP A 1 1852 ? 135.686 168.038 120.064 1.00 59.82  ? 1852 ASP A CB    1 
ATOM   2542  C  CG    . ASP A 1 1852 ? 135.381 168.572 121.450 1.00 64.90  ? 1852 ASP A CG    1 
ATOM   2543  O  OD1   . ASP A 1 1852 ? 134.905 169.722 121.554 1.00 66.41  ? 1852 ASP A OD1   1 
ATOM   2544  O  OD2   . ASP A 1 1852 ? 135.616 167.841 122.435 1.00 66.38  ? 1852 ASP A OD2   1 
ATOM   2545  N  N     . VAL A 1 1853 ? 136.457 171.319 118.952 1.00 60.72  ? 1853 VAL A N     1 
ATOM   2546  C  CA    . VAL A 1 1853 ? 137.547 172.284 118.840 1.00 56.84  ? 1853 VAL A CA    1 
ATOM   2547  C  C     . VAL A 1 1853 ? 138.520 172.144 120.002 1.00 59.28  ? 1853 VAL A C     1 
ATOM   2548  O  O     . VAL A 1 1853 ? 139.704 172.480 119.875 1.00 59.68  ? 1853 VAL A O     1 
ATOM   2549  C  CB    . VAL A 1 1853 ? 136.985 173.716 118.739 1.00 54.43  ? 1853 VAL A CB    1 
ATOM   2550  C  CG1   . VAL A 1 1853 ? 136.150 173.865 117.478 1.00 53.74  ? 1853 VAL A CG1   1 
ATOM   2551  C  CG2   . VAL A 1 1853 ? 136.156 174.052 119.967 1.00 51.62  ? 1853 VAL A CG2   1 
ATOM   2552  N  N     . LEU A 1 1854 ? 138.046 171.651 121.149 1.00 52.96  ? 1854 LEU A N     1 
ATOM   2553  C  CA    . LEU A 1 1854 ? 138.934 171.449 122.288 1.00 52.94  ? 1854 LEU A CA    1 
ATOM   2554  C  C     . LEU A 1 1854 ? 139.900 170.295 122.050 1.00 51.34  ? 1854 LEU A C     1 
ATOM   2555  O  O     . LEU A 1 1854 ? 141.017 170.304 122.581 1.00 50.75  ? 1854 LEU A O     1 
ATOM   2556  C  CB    . LEU A 1 1854 ? 138.114 171.205 123.554 1.00 46.37  ? 1854 LEU A CB    1 
ATOM   2557  C  CG    . LEU A 1 1854 ? 137.206 172.351 124.004 1.00 46.07  ? 1854 LEU A CG    1 
ATOM   2558  C  CD1   . LEU A 1 1854 ? 136.741 172.136 125.435 1.00 51.11  ? 1854 LEU A CD1   1 
ATOM   2559  C  CD2   . LEU A 1 1854 ? 137.915 173.689 123.863 1.00 39.97  ? 1854 LEU A CD2   1 
ATOM   2560  N  N     . GLN A 1 1855 ? 139.494 169.302 121.262 1.00 47.79  ? 1855 GLN A N     1 
ATOM   2561  C  CA    . GLN A 1 1855 ? 140.319 168.139 120.967 1.00 47.49  ? 1855 GLN A CA    1 
ATOM   2562  C  C     . GLN A 1 1855 ? 141.106 168.291 119.672 1.00 44.08  ? 1855 GLN A C     1 
ATOM   2563  O  O     . GLN A 1 1855 ? 141.766 167.339 119.245 1.00 41.40  ? 1855 GLN A O     1 
ATOM   2564  C  CB    . GLN A 1 1855 ? 139.449 166.882 120.902 1.00 52.18  ? 1855 GLN A CB    1 
ATOM   2565  C  CG    . GLN A 1 1855 ? 139.030 166.344 122.258 1.00 50.33  ? 1855 GLN A CG    1 
ATOM   2566  C  CD    . GLN A 1 1855 ? 139.159 164.837 122.351 1.00 63.03  ? 1855 GLN A CD    1 
ATOM   2567  O  OE1   . GLN A 1 1855 ? 138.843 164.116 121.405 1.00 67.75  ? 1855 GLN A OE1   1 
ATOM   2568  N  NE2   . GLN A 1 1855 ? 139.626 164.353 123.496 1.00 64.74  ? 1855 GLN A NE2   1 
ATOM   2569  N  N     . GLN A 1 1856 ? 141.043 169.463 119.035 1.00 44.13  ? 1856 GLN A N     1 
ATOM   2570  C  CA    . GLN A 1 1856 ? 141.722 169.654 117.756 1.00 44.73  ? 1856 GLN A CA    1 
ATOM   2571  C  C     . GLN A 1 1856 ? 143.235 169.543 117.900 1.00 41.55  ? 1856 GLN A C     1 
ATOM   2572  O  O     . GLN A 1 1856 ? 143.901 168.940 117.052 1.00 40.35  ? 1856 GLN A O     1 
ATOM   2573  C  CB    . GLN A 1 1856 ? 141.339 171.007 117.158 1.00 46.44  ? 1856 GLN A CB    1 
ATOM   2574  C  CG    . GLN A 1 1856 ? 140.138 170.957 116.232 1.00 51.71  ? 1856 GLN A CG    1 
ATOM   2575  C  CD    . GLN A 1 1856 ? 140.015 172.200 115.377 1.00 58.79  ? 1856 GLN A CD    1 
ATOM   2576  O  OE1   . GLN A 1 1856 ? 140.027 172.126 114.149 1.00 59.44  ? 1856 GLN A OE1   1 
ATOM   2577  N  NE2   . GLN A 1 1856 ? 139.896 173.354 116.023 1.00 54.00  ? 1856 GLN A NE2   1 
ATOM   2578  N  N     . LEU A 1 1857 ? 143.794 170.114 118.963 1.00 38.02  ? 1857 LEU A N     1 
ATOM   2579  C  CA    . LEU A 1 1857 ? 145.235 170.130 119.174 1.00 28.25  ? 1857 LEU A CA    1 
ATOM   2580  C  C     . LEU A 1 1857 ? 145.640 168.990 120.098 1.00 29.83  ? 1857 LEU A C     1 
ATOM   2581  O  O     . LEU A 1 1857 ? 145.049 168.810 121.168 1.00 33.54  ? 1857 LEU A O     1 
ATOM   2582  C  CB    . LEU A 1 1857 ? 145.687 171.467 119.761 1.00 22.94  ? 1857 LEU A CB    1 
ATOM   2583  C  CG    . LEU A 1 1857 ? 147.139 171.522 120.240 1.00 17.31  ? 1857 LEU A CG    1 
ATOM   2584  C  CD1   . LEU A 1 1857 ? 148.094 171.290 119.082 1.00 19.39  ? 1857 LEU A CD1   1 
ATOM   2585  C  CD2   . LEU A 1 1857 ? 147.430 172.846 120.919 1.00 16.95  ? 1857 LEU A CD2   1 
ATOM   2586  N  N     . SER A 1 1858 ? 146.646 168.227 119.680 1.00 25.12  ? 1858 SER A N     1 
ATOM   2587  C  CA    . SER A 1 1858 ? 147.211 167.146 120.474 1.00 19.26  ? 1858 SER A CA    1 
ATOM   2588  C  C     . SER A 1 1858 ? 148.697 167.403 120.669 1.00 20.36  ? 1858 SER A C     1 
ATOM   2589  O  O     . SER A 1 1858 ? 149.420 167.650 119.698 1.00 26.25  ? 1858 SER A O     1 
ATOM   2590  C  CB    . SER A 1 1858 ? 146.989 165.790 119.798 1.00 24.03  ? 1858 SER A CB    1 
ATOM   2591  O  OG    . SER A 1 1858 ? 147.644 164.752 120.506 1.00 30.79  ? 1858 SER A OG    1 
ATOM   2592  N  N     . ILE A 1 1859 ? 149.148 167.345 121.918 1.00 16.37  ? 1859 ILE A N     1 
ATOM   2593  C  CA    . ILE A 1 1859 ? 150.547 167.552 122.269 1.00 14.96  ? 1859 ILE A CA    1 
ATOM   2594  C  C     . ILE A 1 1859 ? 151.141 166.208 122.662 1.00 21.39  ? 1859 ILE A C     1 
ATOM   2595  O  O     . ILE A 1 1859 ? 150.650 165.550 123.587 1.00 29.31  ? 1859 ILE A O     1 
ATOM   2596  C  CB    . ILE A 1 1859 ? 150.702 168.579 123.404 1.00 14.05  ? 1859 ILE A CB    1 
ATOM   2597  C  CG1   . ILE A 1 1859 ? 149.945 169.864 123.066 1.00 14.84  ? 1859 ILE A CG1   1 
ATOM   2598  C  CG2   . ILE A 1 1859 ? 152.170 168.874 123.663 1.00 14.57  ? 1859 ILE A CG2   1 
ATOM   2599  C  CD1   . ILE A 1 1859 ? 149.920 170.867 124.191 1.00 16.72  ? 1859 ILE A CD1   1 
ATOM   2600  N  N     . GLN A 1 1860 ? 152.195 165.802 121.958 1.00 18.28  ? 1860 GLN A N     1 
ATOM   2601  C  CA    . GLN A 1 1860 ? 152.829 164.510 122.163 1.00 15.28  ? 1860 GLN A CA    1 
ATOM   2602  C  C     . GLN A 1 1860 ? 154.309 164.703 122.442 1.00 17.50  ? 1860 GLN A C     1 
ATOM   2603  O  O     . GLN A 1 1860 ? 154.943 165.606 121.888 1.00 23.72  ? 1860 GLN A O     1 
ATOM   2604  C  CB    . GLN A 1 1860 ? 152.651 163.600 120.941 1.00 15.43  ? 1860 GLN A CB    1 
ATOM   2605  C  CG    . GLN A 1 1860 ? 151.242 163.575 120.381 1.00 21.02  ? 1860 GLN A CG    1 
ATOM   2606  C  CD    . GLN A 1 1860 ? 150.990 162.376 119.489 1.00 35.26  ? 1860 GLN A CD    1 
ATOM   2607  O  OE1   . GLN A 1 1860 ? 151.858 161.521 119.315 1.00 35.36  ? 1860 GLN A OE1   1 
ATOM   2608  N  NE2   . GLN A 1 1860 ? 149.794 162.308 118.917 1.00 41.45  ? 1860 GLN A NE2   1 
ATOM   2609  N  N     . MET A 1 1861 ? 154.855 163.853 123.305 1.00 17.46  ? 1861 MET A N     1 
ATOM   2610  C  CA    . MET A 1 1861 ? 156.287 163.836 123.579 1.00 14.62  ? 1861 MET A CA    1 
ATOM   2611  C  C     . MET A 1 1861 ? 156.636 162.429 124.039 1.00 21.06  ? 1861 MET A C     1 
ATOM   2612  O  O     . MET A 1 1861 ? 156.113 161.961 125.055 1.00 27.40  ? 1861 MET A O     1 
ATOM   2613  C  CB    . MET A 1 1861 ? 156.670 164.887 124.621 1.00 14.78  ? 1861 MET A CB    1 
ATOM   2614  C  CG    . MET A 1 1861 ? 158.161 164.980 124.881 1.00 17.90  ? 1861 MET A CG    1 
ATOM   2615  S  SD    . MET A 1 1861 ? 158.602 166.290 126.037 1.00 26.14  ? 1861 MET A SD    1 
ATOM   2616  C  CE    . MET A 1 1861 ? 160.369 166.038 126.176 1.00 14.34  ? 1861 MET A CE    1 
ATOM   2617  N  N     . ALA A 1 1862 ? 157.499 161.754 123.275 1.00 20.43  ? 1862 ALA A N     1 
ATOM   2618  C  CA    . ALA A 1 1862 ? 157.808 160.330 123.446 1.00 20.77  ? 1862 ALA A CA    1 
ATOM   2619  C  C     . ALA A 1 1862 ? 156.512 159.558 123.228 1.00 26.33  ? 1862 ALA A C     1 
ATOM   2620  O  O     . ALA A 1 1862 ? 155.885 159.734 122.168 1.00 28.27  ? 1862 ALA A O     1 
ATOM   2621  C  CB    . ALA A 1 1862 ? 158.507 160.104 124.789 1.00 18.26  ? 1862 ALA A CB    1 
ATOM   2622  N  N     . ASN A 1 1863 ? 156.070 158.718 124.161 1.00 25.83  ? 1863 ASN A N     1 
ATOM   2623  C  CA    . ASN A 1 1863 ? 154.841 157.953 124.000 1.00 28.93  ? 1863 ASN A CA    1 
ATOM   2624  C  C     . ASN A 1 1863 ? 153.659 158.581 124.726 1.00 33.03  ? 1863 ASN A C     1 
ATOM   2625  O  O     . ASN A 1 1863 ? 152.585 157.974 124.778 1.00 39.89  ? 1863 ASN A O     1 
ATOM   2626  C  CB    . ASN A 1 1863 ? 155.043 156.516 124.484 1.00 33.03  ? 1863 ASN A CB    1 
ATOM   2627  C  CG    . ASN A 1 1863 ? 155.048 156.405 125.994 1.00 41.47  ? 1863 ASN A CG    1 
ATOM   2628  O  OD1   . ASN A 1 1863 ? 155.879 157.011 126.670 1.00 36.58  ? 1863 ASN A OD1   1 
ATOM   2629  N  ND2   . ASN A 1 1863 ? 154.115 155.630 126.532 1.00 48.36  ? 1863 ASN A ND2   1 
ATOM   2630  N  N     . ALA A 1 1864 ? 153.827 159.777 125.281 1.00 29.88  ? 1864 ALA A N     1 
ATOM   2631  C  CA    . ALA A 1 1864 ? 152.777 160.451 126.033 1.00 25.81  ? 1864 ALA A CA    1 
ATOM   2632  C  C     . ALA A 1 1864 ? 152.032 161.418 125.125 1.00 25.57  ? 1864 ALA A C     1 
ATOM   2633  O  O     . ALA A 1 1864 ? 152.654 162.183 124.382 1.00 29.37  ? 1864 ALA A O     1 
ATOM   2634  C  CB    . ALA A 1 1864 ? 153.361 161.196 127.234 1.00 21.92  ? 1864 ALA A CB    1 
ATOM   2635  N  N     . LYS A 1 1865 ? 150.704 161.379 125.185 1.00 25.31  ? 1865 LYS A N     1 
ATOM   2636  C  CA    . LYS A 1 1865 ? 149.848 162.248 124.389 1.00 21.12  ? 1865 LYS A CA    1 
ATOM   2637  C  C     . LYS A 1 1865 ? 148.959 163.060 125.318 1.00 23.13  ? 1865 LYS A C     1 
ATOM   2638  O  O     . LYS A 1 1865 ? 148.338 162.505 126.230 1.00 30.50  ? 1865 LYS A O     1 
ATOM   2639  C  CB    . LYS A 1 1865 ? 148.995 161.437 123.410 1.00 27.07  ? 1865 LYS A CB    1 
ATOM   2640  C  CG    . LYS A 1 1865 ? 149.802 160.615 122.421 1.00 32.76  ? 1865 LYS A CG    1 
ATOM   2641  C  CD    . LYS A 1 1865 ? 148.908 159.714 121.588 1.00 32.56  ? 1865 LYS A CD    1 
ATOM   2642  C  CE    . LYS A 1 1865 ? 149.730 158.762 120.735 1.00 33.70  ? 1865 LYS A CE    1 
ATOM   2643  N  NZ    . LYS A 1 1865 ? 150.790 158.078 121.527 1.00 32.51  ? 1865 LYS A NZ    1 
ATOM   2644  N  N     . PHE A 1 1866 ? 148.899 164.368 125.085 1.00 20.61  ? 1866 PHE A N     1 
ATOM   2645  C  CA    . PHE A 1 1866 ? 148.119 165.274 125.913 1.00 19.20  ? 1866 PHE A CA    1 
ATOM   2646  C  C     . PHE A 1 1866 ? 147.220 166.133 125.036 1.00 21.01  ? 1866 PHE A C     1 
ATOM   2647  O  O     . PHE A 1 1866 ? 147.472 166.324 123.844 1.00 27.61  ? 1866 PHE A O     1 
ATOM   2648  C  CB    . PHE A 1 1866 ? 149.016 166.179 126.769 1.00 15.21  ? 1866 PHE A CB    1 
ATOM   2649  C  CG    . PHE A 1 1866 ? 149.995 165.431 127.624 1.00 16.30  ? 1866 PHE A CG    1 
ATOM   2650  C  CD1   . PHE A 1 1866 ? 149.622 164.950 128.867 1.00 14.14  ? 1866 PHE A CD1   1 
ATOM   2651  C  CD2   . PHE A 1 1866 ? 151.290 165.214 127.189 1.00 18.34  ? 1866 PHE A CD2   1 
ATOM   2652  C  CE1   . PHE A 1 1866 ? 150.521 164.263 129.657 1.00 17.64  ? 1866 PHE A CE1   1 
ATOM   2653  C  CE2   . PHE A 1 1866 ? 152.193 164.528 127.974 1.00 16.68  ? 1866 PHE A CE2   1 
ATOM   2654  C  CZ    . PHE A 1 1866 ? 151.808 164.052 129.210 1.00 17.56  ? 1866 PHE A CZ    1 
ATOM   2655  N  N     . ASN A 1 1867 ? 146.159 166.647 125.649 1.00 21.81  ? 1867 ASN A N     1 
ATOM   2656  C  CA    . ASN A 1 1867 ? 145.247 167.585 125.012 1.00 24.30  ? 1867 ASN A CA    1 
ATOM   2657  C  C     . ASN A 1 1867 ? 145.425 168.953 125.651 1.00 27.16  ? 1867 ASN A C     1 
ATOM   2658  O  O     . ASN A 1 1867 ? 145.531 169.058 126.878 1.00 32.53  ? 1867 ASN A O     1 
ATOM   2659  C  CB    . ASN A 1 1867 ? 143.795 167.122 125.149 1.00 27.14  ? 1867 ASN A CB    1 
ATOM   2660  C  CG    . ASN A 1 1867 ? 143.312 166.349 123.940 1.00 45.60  ? 1867 ASN A CG    1 
ATOM   2661  O  OD1   . ASN A 1 1867 ? 144.109 165.790 123.187 1.00 46.38  ? 1867 ASN A OD1   1 
ATOM   2662  N  ND2   . ASN A 1 1867 ? 142.000 166.314 123.747 1.00 48.95  ? 1867 ASN A ND2   1 
ATOM   2663  N  N     . TYR A 1 1868 ? 145.471 169.993 124.823 1.00 20.25  ? 1868 TYR A N     1 
ATOM   2664  C  CA    . TYR A 1 1868 ? 145.598 171.347 125.344 1.00 16.82  ? 1868 TYR A CA    1 
ATOM   2665  C  C     . TYR A 1 1868 ? 144.375 171.703 126.178 1.00 20.12  ? 1868 TYR A C     1 
ATOM   2666  O  O     . TYR A 1 1868 ? 143.235 171.540 125.733 1.00 26.87  ? 1868 TYR A O     1 
ATOM   2667  C  CB    . TYR A 1 1868 ? 145.768 172.342 124.195 1.00 18.56  ? 1868 TYR A CB    1 
ATOM   2668  C  CG    . TYR A 1 1868 ? 146.460 173.627 124.590 1.00 16.32  ? 1868 TYR A CG    1 
ATOM   2669  C  CD1   . TYR A 1 1868 ? 147.827 173.659 124.822 1.00 15.66  ? 1868 TYR A CD1   1 
ATOM   2670  C  CD2   . TYR A 1 1868 ? 145.747 174.809 124.727 1.00 16.46  ? 1868 TYR A CD2   1 
ATOM   2671  C  CE1   . TYR A 1 1868 ? 148.464 174.830 125.181 1.00 15.29  ? 1868 TYR A CE1   1 
ATOM   2672  C  CE2   . TYR A 1 1868 ? 146.376 175.985 125.086 1.00 15.49  ? 1868 TYR A CE2   1 
ATOM   2673  C  CZ    . TYR A 1 1868 ? 147.734 175.989 125.312 1.00 16.31  ? 1868 TYR A CZ    1 
ATOM   2674  O  OH    . TYR A 1 1868 ? 148.367 177.157 125.670 1.00 20.87  ? 1868 TYR A OH    1 
ATOM   2675  N  N     . GLY A 1 1869 ? 144.615 172.190 127.396 1.00 18.04  ? 1869 GLY A N     1 
ATOM   2676  C  CA    . GLY A 1 1869 ? 143.520 172.548 128.279 1.00 19.04  ? 1869 GLY A CA    1 
ATOM   2677  C  C     . GLY A 1 1869 ? 142.791 173.809 127.874 1.00 22.75  ? 1869 GLY A C     1 
ATOM   2678  O  O     . GLY A 1 1869 ? 141.648 174.014 128.297 1.00 28.56  ? 1869 GLY A O     1 
ATOM   2679  N  N     . PHE A 1 1870 ? 143.429 174.659 127.067 1.00 22.54  ? 1870 PHE A N     1 
ATOM   2680  C  CA    . PHE A 1 1870 ? 142.834 175.900 126.571 1.00 23.99  ? 1870 PHE A CA    1 
ATOM   2681  C  C     . PHE A 1 1870 ? 142.394 176.815 127.709 1.00 25.61  ? 1870 PHE A C     1 
ATOM   2682  O  O     . PHE A 1 1870 ? 141.403 177.539 127.593 1.00 31.67  ? 1870 PHE A O     1 
ATOM   2683  C  CB    . PHE A 1 1870 ? 141.666 175.618 125.624 1.00 23.84  ? 1870 PHE A CB    1 
ATOM   2684  C  CG    . PHE A 1 1870 ? 142.097 175.206 124.248 1.00 22.30  ? 1870 PHE A CG    1 
ATOM   2685  C  CD1   . PHE A 1 1870 ? 142.757 176.097 123.422 1.00 21.89  ? 1870 PHE A CD1   1 
ATOM   2686  C  CD2   . PHE A 1 1870 ? 141.849 173.927 123.784 1.00 24.53  ? 1870 PHE A CD2   1 
ATOM   2687  C  CE1   . PHE A 1 1870 ? 143.160 175.721 122.159 1.00 25.48  ? 1870 PHE A CE1   1 
ATOM   2688  C  CE2   . PHE A 1 1870 ? 142.248 173.545 122.519 1.00 26.75  ? 1870 PHE A CE2   1 
ATOM   2689  C  CZ    . PHE A 1 1870 ? 142.904 174.443 121.706 1.00 26.57  ? 1870 PHE A CZ    1 
ATOM   2690  N  N     . GLU A 1 1871 ? 143.128 176.787 128.816 1.00 25.75  ? 1871 GLU A N     1 
ATOM   2691  C  CA    . GLU A 1 1871 ? 142.907 177.709 129.919 1.00 23.32  ? 1871 GLU A CA    1 
ATOM   2692  C  C     . GLU A 1 1871 ? 143.665 178.999 129.638 1.00 28.56  ? 1871 GLU A C     1 
ATOM   2693  O  O     . GLU A 1 1871 ? 144.865 178.966 129.347 1.00 31.36  ? 1871 GLU A O     1 
ATOM   2694  C  CB    . GLU A 1 1871 ? 143.368 177.091 131.240 1.00 21.90  ? 1871 GLU A CB    1 
ATOM   2695  C  CG    . GLU A 1 1871 ? 143.598 178.093 132.355 1.00 28.04  ? 1871 GLU A CG    1 
ATOM   2696  C  CD    . GLU A 1 1871 ? 142.334 178.411 133.126 1.00 41.98  ? 1871 GLU A CD    1 
ATOM   2697  O  OE1   . GLU A 1 1871 ? 142.220 179.541 133.644 1.00 43.52  ? 1871 GLU A OE1   1 
ATOM   2698  O  OE2   . GLU A 1 1871 ? 141.454 177.530 133.217 1.00 44.11  ? 1871 GLU A OE2   1 
ATOM   2699  N  N     . TYR A 1 1872 ? 142.963 180.128 129.712 1.00 29.21  ? 1872 TYR A N     1 
ATOM   2700  C  CA    . TYR A 1 1872 ? 143.571 181.416 129.391 1.00 24.40  ? 1872 TYR A CA    1 
ATOM   2701  C  C     . TYR A 1 1872 ? 144.668 181.725 130.399 1.00 27.28  ? 1872 TYR A C     1 
ATOM   2702  O  O     . TYR A 1 1872 ? 144.395 181.953 131.581 1.00 31.28  ? 1872 TYR A O     1 
ATOM   2703  C  CB    . TYR A 1 1872 ? 142.520 182.519 129.371 1.00 26.99  ? 1872 TYR A CB    1 
ATOM   2704  C  CG    . TYR A 1 1872 ? 143.090 183.865 128.988 1.00 29.66  ? 1872 TYR A CG    1 
ATOM   2705  C  CD1   . TYR A 1 1872 ? 143.735 184.043 127.773 1.00 29.75  ? 1872 TYR A CD1   1 
ATOM   2706  C  CD2   . TYR A 1 1872 ? 142.983 184.956 129.839 1.00 29.68  ? 1872 TYR A CD2   1 
ATOM   2707  C  CE1   . TYR A 1 1872 ? 144.264 185.267 127.419 1.00 30.07  ? 1872 TYR A CE1   1 
ATOM   2708  C  CE2   . TYR A 1 1872 ? 143.505 186.186 129.490 1.00 30.54  ? 1872 TYR A CE2   1 
ATOM   2709  C  CZ    . TYR A 1 1872 ? 144.143 186.335 128.278 1.00 34.25  ? 1872 TYR A CZ    1 
ATOM   2710  O  OH    . TYR A 1 1872 ? 144.666 187.556 127.923 1.00 44.88  ? 1872 TYR A OH    1 
ATOM   2711  N  N     . LEU A 1 1873 ? 145.911 181.732 129.928 1.00 25.34  ? 1873 LEU A N     1 
ATOM   2712  C  CA    . LEU A 1 1873 ? 147.076 181.926 130.776 1.00 25.42  ? 1873 LEU A CA    1 
ATOM   2713  C  C     . LEU A 1 1873 ? 147.557 183.370 130.806 1.00 29.01  ? 1873 LEU A C     1 
ATOM   2714  O  O     . LEU A 1 1873 ? 148.471 183.686 131.573 1.00 38.93  ? 1873 LEU A O     1 
ATOM   2715  C  CB    . LEU A 1 1873 ? 148.212 181.017 130.301 1.00 24.93  ? 1873 LEU A CB    1 
ATOM   2716  C  CG    . LEU A 1 1873 ? 147.939 179.518 130.419 1.00 22.42  ? 1873 LEU A CG    1 
ATOM   2717  C  CD1   . LEU A 1 1873 ? 149.045 178.729 129.755 1.00 18.60  ? 1873 LEU A CD1   1 
ATOM   2718  C  CD2   . LEU A 1 1873 ? 147.790 179.110 131.875 1.00 21.93  ? 1873 LEU A CD2   1 
ATOM   2719  N  N     . GLY A 1 1874 ? 146.962 184.250 130.004 1.00 31.56  ? 1874 GLY A N     1 
ATOM   2720  C  CA    . GLY A 1 1874 ? 147.460 185.612 129.930 1.00 31.21  ? 1874 GLY A CA    1 
ATOM   2721  C  C     . GLY A 1 1874 ? 148.827 185.653 129.276 1.00 35.98  ? 1874 GLY A C     1 
ATOM   2722  O  O     . GLY A 1 1874 ? 149.130 184.881 128.359 1.00 34.86  ? 1874 GLY A O     1 
ATOM   2723  N  N     . VAL A 1 1875 ? 149.670 186.567 129.751 1.00 36.65  ? 1875 VAL A N     1 
ATOM   2724  C  CA    . VAL A 1 1875 ? 151.035 186.681 129.252 1.00 33.54  ? 1875 VAL A CA    1 
ATOM   2725  C  C     . VAL A 1 1875 ? 152.003 186.250 130.345 1.00 33.26  ? 1875 VAL A C     1 
ATOM   2726  O  O     . VAL A 1 1875 ? 152.385 187.051 131.204 1.00 36.38  ? 1875 VAL A O     1 
ATOM   2727  C  CB    . VAL A 1 1875 ? 151.340 188.112 128.775 1.00 32.14  ? 1875 VAL A CB    1 
ATOM   2728  C  CG1   . VAL A 1 1875 ? 152.701 188.166 128.101 1.00 28.06  ? 1875 VAL A CG1   1 
ATOM   2729  C  CG2   . VAL A 1 1875 ? 150.254 188.596 127.831 1.00 36.01  ? 1875 VAL A CG2   1 
ATOM   2730  N  N     . GLN A 1 1876 ? 152.401 184.983 130.320 1.00 35.42  ? 1876 GLN A N     1 
ATOM   2731  C  CA    . GLN A 1 1876 ? 153.342 184.450 131.291 1.00 35.98  ? 1876 GLN A CA    1 
ATOM   2732  C  C     . GLN A 1 1876 ? 154.768 184.545 130.761 1.00 36.74  ? 1876 GLN A C     1 
ATOM   2733  O  O     . GLN A 1 1876 ? 155.009 184.605 129.553 1.00 33.91  ? 1876 GLN A O     1 
ATOM   2734  C  CB    . GLN A 1 1876 ? 153.006 182.997 131.629 1.00 34.76  ? 1876 GLN A CB    1 
ATOM   2735  C  CG    . GLN A 1 1876 ? 151.528 182.737 131.854 1.00 31.46  ? 1876 GLN A CG    1 
ATOM   2736  C  CD    . GLN A 1 1876 ? 151.135 182.844 133.314 1.00 32.88  ? 1876 GLN A CD    1 
ATOM   2737  O  OE1   . GLN A 1 1876 ? 151.975 183.093 134.178 1.00 42.46  ? 1876 GLN A OE1   1 
ATOM   2738  N  NE2   . GLN A 1 1876 ? 149.852 182.655 133.596 1.00 32.48  ? 1876 GLN A NE2   1 
ATOM   2739  N  N     . ASP A 1 1877 ? 155.721 184.558 131.690 1.00 37.04  ? 1877 ASP A N     1 
ATOM   2740  C  CA    . ASP A 1 1877 ? 157.135 184.631 131.340 1.00 39.55  ? 1877 ASP A CA    1 
ATOM   2741  C  C     . ASP A 1 1877 ? 157.610 183.246 130.920 1.00 33.02  ? 1877 ASP A C     1 
ATOM   2742  O  O     . ASP A 1 1877 ? 157.704 182.335 131.749 1.00 28.03  ? 1877 ASP A O     1 
ATOM   2743  C  CB    . ASP A 1 1877 ? 157.950 185.161 132.515 1.00 47.71  ? 1877 ASP A CB    1 
ATOM   2744  C  CG    . ASP A 1 1877 ? 159.148 185.978 132.071 1.00 64.75  ? 1877 ASP A CG    1 
ATOM   2745  O  OD1   . ASP A 1 1877 ? 160.068 186.182 132.891 1.00 66.00  ? 1877 ASP A OD1   1 
ATOM   2746  O  OD2   . ASP A 1 1877 ? 159.170 186.416 130.901 1.00 59.86  ? 1877 ASP A OD2   1 
ATOM   2747  N  N     . LYS A 1 1878 ? 157.920 183.094 129.630 1.00 32.87  ? 1878 LYS A N     1 
ATOM   2748  C  CA    . LYS A 1 1878 ? 158.417 181.791 129.118 1.00 27.76  ? 1878 LYS A CA    1 
ATOM   2749  C  C     . LYS A 1 1878 ? 159.825 181.525 129.673 1.00 24.29  ? 1878 LYS A C     1 
ATOM   2750  O  O     . LYS A 1 1878 ? 160.573 182.503 129.885 1.00 25.17  ? 1878 LYS A O     1 
ATOM   2751  C  CB    . LYS A 1 1878 ? 158.446 181.779 127.586 1.00 23.52  ? 1878 LYS A CB    1 
ATOM   2752  C  CG    . LYS A 1 1878 ? 157.085 181.761 126.908 1.00 23.83  ? 1878 LYS A CG    1 
ATOM   2753  C  CD    . LYS A 1 1878 ? 157.189 181.262 125.473 1.00 26.16  ? 1878 LYS A CD    1 
ATOM   2754  C  CE    . LYS A 1 1878 ? 157.880 179.936 125.418 1.00 27.57  ? 1878 LYS A CE    1 
ATOM   2755  N  NZ    . LYS A 1 1878 ? 158.066 179.466 124.044 1.00 26.84  ? 1878 LYS A NZ    1 
ATOM   2756  N  N     . LEU A 1 1879 ? 160.165 180.252 129.896 1.00 19.84  ? 1879 LEU A N     1 
ATOM   2757  C  CA    . LEU A 1 1879 ? 161.519 179.890 130.391 1.00 14.98  ? 1879 LEU A CA    1 
ATOM   2758  C  C     . LEU A 1 1879 ? 162.332 179.305 129.226 1.00 17.59  ? 1879 LEU A C     1 
ATOM   2759  O  O     . LEU A 1 1879 ? 161.747 178.554 128.416 1.00 19.77  ? 1879 LEU A O     1 
ATOM   2760  C  CB    . LEU A 1 1879 ? 161.412 178.902 131.552 1.00 12.51  ? 1879 LEU A CB    1 
ATOM   2761  C  CG    . LEU A 1 1879 ? 161.369 179.508 132.958 1.00 12.40  ? 1879 LEU A CG    1 
ATOM   2762  C  CD1   . LEU A 1 1879 ? 160.216 180.484 133.113 1.00 16.39  ? 1879 LEU A CD1   1 
ATOM   2763  C  CD2   . LEU A 1 1879 ? 161.289 178.413 134.008 1.00 10.87  ? 1879 LEU A CD2   1 
ATOM   2764  N  N     . VAL A 1 1880 ? 163.622 179.641 129.148 1.00 18.32  ? 1880 VAL A N     1 
ATOM   2765  C  CA    . VAL A 1 1880 ? 164.500 179.085 128.074 1.00 15.15  ? 1880 VAL A CA    1 
ATOM   2766  C  C     . VAL A 1 1880 ? 164.432 177.551 128.148 1.00 17.64  ? 1880 VAL A C     1 
ATOM   2767  O  O     . VAL A 1 1880 ? 164.625 177.005 129.256 1.00 17.85  ? 1880 VAL A O     1 
ATOM   2768  C  CB    . VAL A 1 1880 ? 165.946 179.596 128.218 1.00 12.15  ? 1880 VAL A CB    1 
ATOM   2769  C  CG1   . VAL A 1 1880 ? 166.862 179.019 127.146 1.00 13.67  ? 1880 VAL A CG1   1 
ATOM   2770  C  CG2   . VAL A 1 1880 ? 166.011 181.118 128.220 1.00 10.70  ? 1880 VAL A CG2   1 
ATOM   2771  N  N     . GLN A 1 1881 ? 164.170 176.888 127.018 1.00 17.16  ? 1881 GLN A N     1 
ATOM   2772  C  CA    . GLN A 1 1881 ? 164.025 175.408 127.014 1.00 18.33  ? 1881 GLN A CA    1 
ATOM   2773  C  C     . GLN A 1 1881 ? 165.424 174.772 127.040 1.00 22.61  ? 1881 GLN A C     1 
ATOM   2774  O  O     . GLN A 1 1881 ? 165.862 174.257 125.989 1.00 27.02  ? 1881 GLN A O     1 
ATOM   2775  C  CB    . GLN A 1 1881 ? 163.209 174.964 125.799 1.00 19.89  ? 1881 GLN A CB    1 
ATOM   2776  C  CG    . GLN A 1 1881 ? 162.831 173.487 125.808 1.00 23.20  ? 1881 GLN A CG    1 
ATOM   2777  C  CD    . GLN A 1 1881 ? 161.857 173.118 126.905 1.00 22.56  ? 1881 GLN A CD    1 
ATOM   2778  O  OE1   . GLN A 1 1881 ? 161.369 173.973 127.653 1.00 23.04  ? 1881 GLN A OE1   1 
ATOM   2779  N  NE2   . GLN A 1 1881 ? 161.551 171.832 127.002 1.00 21.16  ? 1881 GLN A NE2   1 
ATOM   2780  N  N     . THR A 1 1882 ? 166.092 174.814 128.196 1.00 19.28  ? 1882 THR A N     1 
ATOM   2781  C  CA    . THR A 1 1882 ? 167.452 174.246 128.321 1.00 18.36  ? 1882 THR A CA    1 
ATOM   2782  C  C     . THR A 1 1882 ? 167.365 172.736 128.295 1.00 20.87  ? 1882 THR A C     1 
ATOM   2783  O  O     . THR A 1 1882 ? 166.286 172.199 128.624 1.00 24.03  ? 1882 THR A O     1 
ATOM   2784  C  CB    . THR A 1 1882 ? 168.094 174.749 129.613 1.00 18.17  ? 1882 THR A CB    1 
ATOM   2785  O  OG1   . THR A 1 1882 ? 167.300 174.200 130.659 1.00 18.26  ? 1882 THR A OG1   1 
ATOM   2786  C  CG2   . THR A 1 1882 ? 168.108 176.264 129.703 1.00 17.87  ? 1882 THR A CG2   1 
ATOM   2787  N  N     . PRO A 1 1883 ? 168.447 172.013 127.933 1.00 19.69  ? 1883 PRO A N     1 
ATOM   2788  C  CA    . PRO A 1 1883 ? 168.434 170.558 127.971 1.00 19.42  ? 1883 PRO A CA    1 
ATOM   2789  C  C     . PRO A 1 1883 ? 167.880 170.033 129.289 1.00 17.85  ? 1883 PRO A C     1 
ATOM   2790  O  O     . PRO A 1 1883 ? 167.156 169.018 129.278 1.00 17.49  ? 1883 PRO A O     1 
ATOM   2791  C  CB    . PRO A 1 1883 ? 169.919 170.219 127.790 1.00 16.28  ? 1883 PRO A CB    1 
ATOM   2792  C  CG    . PRO A 1 1883 ? 170.444 171.349 126.938 1.00 17.06  ? 1883 PRO A CG    1 
ATOM   2793  C  CD    . PRO A 1 1883 ? 169.693 172.572 127.436 1.00 19.92  ? 1883 PRO A CD    1 
ATOM   2794  N  N     . LEU A 1 1884 ? 168.211 170.699 130.400 1.00 17.15  ? 1884 LEU A N     1 
ATOM   2795  C  CA    . LEU A 1 1884 ? 167.676 170.290 131.725 1.00 15.09  ? 1884 LEU A CA    1 
ATOM   2796  C  C     . LEU A 1 1884 ? 166.145 170.409 131.696 1.00 14.11  ? 1884 LEU A C     1 
ATOM   2797  O  O     . LEU A 1 1884 ? 165.470 169.470 132.171 1.00 16.78  ? 1884 LEU A O     1 
ATOM   2798  C  CB    . LEU A 1 1884 ? 168.286 171.147 132.833 1.00 19.74  ? 1884 LEU A CB    1 
ATOM   2799  C  CG    . LEU A 1 1884 ? 167.778 170.869 134.251 1.00 18.10  ? 1884 LEU A CG    1 
ATOM   2800  C  CD1   . LEU A 1 1884 ? 167.965 169.407 134.618 1.00 18.49  ? 1884 LEU A CD1   1 
ATOM   2801  C  CD2   . LEU A 1 1884 ? 168.469 171.765 135.264 1.00 15.44  ? 1884 LEU A CD2   1 
ATOM   2802  N  N     . THR A 1 1885 ? 165.623 171.513 131.155 1.00 15.51  ? 1885 THR A N     1 
ATOM   2803  C  CA    . THR A 1 1885 ? 164.158 171.679 131.035 1.00 14.42  ? 1885 THR A CA    1 
ATOM   2804  C  C     . THR A 1 1885 ? 163.633 170.578 130.143 1.00 17.12  ? 1885 THR A C     1 
ATOM   2805  O  O     . THR A 1 1885 ? 162.567 170.013 130.466 1.00 20.44  ? 1885 THR A O     1 
ATOM   2806  C  CB    . THR A 1 1885 ? 163.837 173.063 130.474 1.00 16.57  ? 1885 THR A CB    1 
ATOM   2807  O  OG1   . THR A 1 1885 ? 164.591 173.976 131.264 1.00 23.58  ? 1885 THR A OG1   1 
ATOM   2808  C  CG2   . THR A 1 1885 ? 162.359 173.394 130.560 1.00 14.62  ? 1885 THR A CG2   1 
ATOM   2809  N  N     . ASP A 1 1886 ? 164.352 170.275 129.059 1.00 15.64  ? 1886 ASP A N     1 
ATOM   2810  C  CA    . ASP A 1 1886 ? 163.952 169.161 128.156 1.00 12.25  ? 1886 ASP A CA    1 
ATOM   2811  C  C     . ASP A 1 1886 ? 163.858 167.875 128.981 1.00 15.76  ? 1886 ASP A C     1 
ATOM   2812  O  O     . ASP A 1 1886 ? 162.765 167.270 129.011 1.00 17.86  ? 1886 ASP A O     1 
ATOM   2813  C  CB    . ASP A 1 1886 ? 164.912 169.025 126.986 1.00 18.71  ? 1886 ASP A CB    1 
ATOM   2814  C  CG    . ASP A 1 1886 ? 165.216 170.316 126.240 1.00 31.88  ? 1886 ASP A CG    1 
ATOM   2815  O  OD1   . ASP A 1 1886 ? 164.664 171.362 126.634 1.00 31.55  ? 1886 ASP A OD1   1 
ATOM   2816  O  OD2   . ASP A 1 1886 ? 166.006 170.263 125.274 1.00 33.57  ? 1886 ASP A OD2   1 
ATOM   2817  N  N     . ARG A 1 1887 ? 164.959 167.477 129.628 1.00 17.30  ? 1887 ARG A N     1 
ATOM   2818  C  CA    . ARG A 1 1887 ? 164.933 166.286 130.472 1.00 11.44  ? 1887 ARG A CA    1 
ATOM   2819  C  C     . ARG A 1 1887 ? 163.779 166.345 131.463 1.00 12.75  ? 1887 ARG A C     1 
ATOM   2820  O  O     . ARG A 1 1887 ? 163.116 165.332 131.719 1.00 17.35  ? 1887 ARG A O     1 
ATOM   2821  C  CB    . ARG A 1 1887 ? 166.264 166.137 131.206 1.00 11.11  ? 1887 ARG A CB    1 
ATOM   2822  C  CG    . ARG A 1 1887 ? 166.383 164.869 132.031 1.00 14.02  ? 1887 ARG A CG    1 
ATOM   2823  C  CD    . ARG A 1 1887 ? 167.787 164.296 131.956 1.00 17.13  ? 1887 ARG A CD    1 
ATOM   2824  N  NE    . ARG A 1 1887 ? 168.159 163.603 133.182 1.00 21.50  ? 1887 ARG A NE    1 
ATOM   2825  C  CZ    . ARG A 1 1887 ? 169.330 163.016 133.385 1.00 24.44  ? 1887 ARG A CZ    1 
ATOM   2826  N  NH1   . ARG A 1 1887 ? 170.273 163.016 132.458 1.00 29.47  ? 1887 ARG A NH1   1 
ATOM   2827  N  NH2   . ARG A 1 1887 ? 169.561 162.413 134.548 1.00 21.72  ? 1887 ARG A NH2   1 
ATOM   2828  N  N     . CYS A 1 1888 ? 163.530 167.524 132.036 1.00 11.92  ? 1888 CYS A N     1 
ATOM   2829  C  CA    . CYS A 1 1888 ? 162.409 167.684 132.955 1.00 10.92  ? 1888 CYS A CA    1 
ATOM   2830  C  C     . CYS A 1 1888 ? 161.087 167.421 132.250 1.00 14.22  ? 1888 CYS A C     1 
ATOM   2831  O  O     . CYS A 1 1888 ? 160.218 166.722 132.780 1.00 18.49  ? 1888 CYS A O     1 
ATOM   2832  C  CB    . CYS A 1 1888 ? 162.427 169.083 133.569 1.00 14.07  ? 1888 CYS A CB    1 
ATOM   2833  S  SG    . CYS A 1 1888 ? 160.883 169.549 134.382 1.00 30.45  ? 1888 CYS A SG    1 
ATOM   2834  N  N     . TYR A 1 1889 ? 160.924 167.966 131.044 1.00 15.91  ? 1889 TYR A N     1 
ATOM   2835  C  CA    . TYR A 1 1889 ? 159.704 167.735 130.279 1.00 12.17  ? 1889 TYR A CA    1 
ATOM   2836  C  C     . TYR A 1 1889 ? 159.513 166.252 130.002 1.00 11.99  ? 1889 TYR A C     1 
ATOM   2837  O  O     . TYR A 1 1889 ? 158.420 165.709 130.195 1.00 15.48  ? 1889 TYR A O     1 
ATOM   2838  C  CB    . TYR A 1 1889 ? 159.752 168.522 128.969 1.00 10.88  ? 1889 TYR A CB    1 
ATOM   2839  C  CG    . TYR A 1 1889 ? 159.257 169.947 129.068 1.00 12.43  ? 1889 TYR A CG    1 
ATOM   2840  C  CD1   . TYR A 1 1889 ? 159.554 170.733 130.173 1.00 14.03  ? 1889 TYR A CD1   1 
ATOM   2841  C  CD2   . TYR A 1 1889 ? 158.506 170.510 128.047 1.00 13.66  ? 1889 TYR A CD2   1 
ATOM   2842  C  CE1   . TYR A 1 1889 ? 159.106 172.038 130.260 1.00 14.42  ? 1889 TYR A CE1   1 
ATOM   2843  C  CE2   . TYR A 1 1889 ? 158.055 171.810 128.126 1.00 16.28  ? 1889 TYR A CE2   1 
ATOM   2844  C  CZ    . TYR A 1 1889 ? 158.358 172.570 129.233 1.00 17.21  ? 1889 TYR A CZ    1 
ATOM   2845  O  OH    . TYR A 1 1889 ? 157.910 173.868 129.313 1.00 20.68  ? 1889 TYR A OH    1 
ATOM   2846  N  N     . LEU A 1 1890 ? 160.577 165.575 129.566 1.00 11.88  ? 1890 LEU A N     1 
ATOM   2847  C  CA    . LEU A 1 1890 ? 160.479 164.152 129.257 1.00 11.81  ? 1890 LEU A CA    1 
ATOM   2848  C  C     . LEU A 1 1890 ? 160.092 163.345 130.490 1.00 13.01  ? 1890 LEU A C     1 
ATOM   2849  O  O     . LEU A 1 1890 ? 159.154 162.539 130.448 1.00 16.27  ? 1890 LEU A O     1 
ATOM   2850  C  CB    . LEU A 1 1890 ? 161.803 163.652 128.679 1.00 12.43  ? 1890 LEU A CB    1 
ATOM   2851  C  CG    . LEU A 1 1890 ? 161.820 162.199 128.206 1.00 11.60  ? 1890 LEU A CG    1 
ATOM   2852  C  CD1   . LEU A 1 1890 ? 160.980 162.042 126.950 1.00 10.81  ? 1890 LEU A CD1   1 
ATOM   2853  C  CD2   . LEU A 1 1890 ? 163.244 161.725 127.965 1.00 13.85  ? 1890 LEU A CD2   1 
ATOM   2854  N  N     . THR A 1 1891 ? 160.801 163.554 131.603 1.00 13.23  ? 1891 THR A N     1 
ATOM   2855  C  CA    . THR A 1 1891 ? 160.523 162.781 132.810 1.00 12.06  ? 1891 THR A CA    1 
ATOM   2856  C  C     . THR A 1 1891 ? 159.119 163.050 133.333 1.00 13.28  ? 1891 THR A C     1 
ATOM   2857  O  O     . THR A 1 1891 ? 158.398 162.117 133.712 1.00 18.16  ? 1891 THR A O     1 
ATOM   2858  C  CB    . THR A 1 1891 ? 161.561 163.092 133.888 1.00 12.42  ? 1891 THR A CB    1 
ATOM   2859  O  OG1   . THR A 1 1891 ? 162.878 162.914 133.352 1.00 13.25  ? 1891 THR A OG1   1 
ATOM   2860  C  CG2   . THR A 1 1891 ? 161.377 162.170 135.081 1.00 14.18  ? 1891 THR A CG2   1 
ATOM   2861  N  N     . MET A 1 1892 ? 158.700 164.317 133.347 1.00 12.52  ? 1892 MET A N     1 
ATOM   2862  C  CA    . MET A 1 1892 ? 157.400 164.646 133.916 1.00 12.61  ? 1892 MET A CA    1 
ATOM   2863  C  C     . MET A 1 1892 ? 156.265 164.159 133.023 1.00 12.74  ? 1892 MET A C     1 
ATOM   2864  O  O     . MET A 1 1892 ? 155.228 163.712 133.523 1.00 19.77  ? 1892 MET A O     1 
ATOM   2865  C  CB    . MET A 1 1892 ? 157.301 166.151 134.154 1.00 11.94  ? 1892 MET A CB    1 
ATOM   2866  C  CG    . MET A 1 1892 ? 158.277 166.695 135.193 1.00 13.36  ? 1892 MET A CG    1 
ATOM   2867  S  SD    . MET A 1 1892 ? 158.084 166.022 136.852 1.00 38.60  ? 1892 MET A SD    1 
ATOM   2868  C  CE    . MET A 1 1892 ? 159.437 164.851 136.912 1.00 11.13  ? 1892 MET A CE    1 
ATOM   2869  N  N     . THR A 1 1893 ? 156.441 164.220 131.699 1.00 10.63  ? 1893 THR A N     1 
ATOM   2870  C  CA    . THR A 1 1893 ? 155.417 163.692 130.803 1.00 11.32  ? 1893 THR A CA    1 
ATOM   2871  C  C     . THR A 1 1893 ? 155.343 162.173 130.885 1.00 14.16  ? 1893 THR A C     1 
ATOM   2872  O  O     . THR A 1 1893 ? 154.254 161.595 130.793 1.00 19.02  ? 1893 THR A O     1 
ATOM   2873  C  CB    . THR A 1 1893 ? 155.685 164.140 129.366 1.00 14.70  ? 1893 THR A CB    1 
ATOM   2874  O  OG1   . THR A 1 1893 ? 157.061 163.916 129.038 1.00 22.50  ? 1893 THR A OG1   1 
ATOM   2875  C  CG2   . THR A 1 1893 ? 155.359 165.617 129.196 1.00 12.19  ? 1893 THR A CG2   1 
ATOM   2876  N  N     . GLN A 1 1894 ? 156.489 161.506 131.056 1.00 13.90  ? 1894 GLN A N     1 
ATOM   2877  C  CA    . GLN A 1 1894 ? 156.471 160.062 131.260 1.00 12.77  ? 1894 GLN A CA    1 
ATOM   2878  C  C     . GLN A 1 1894 ? 155.750 159.703 132.552 1.00 15.25  ? 1894 GLN A C     1 
ATOM   2879  O  O     . GLN A 1 1894 ? 155.012 158.713 132.606 1.00 21.76  ? 1894 GLN A O     1 
ATOM   2880  C  CB    . GLN A 1 1894 ? 157.897 159.514 131.268 1.00 12.34  ? 1894 GLN A CB    1 
ATOM   2881  C  CG    . GLN A 1 1894 ? 158.530 159.417 129.893 1.00 13.98  ? 1894 GLN A CG    1 
ATOM   2882  C  CD    . GLN A 1 1894 ? 157.665 158.658 128.911 1.00 21.09  ? 1894 GLN A CD    1 
ATOM   2883  O  OE1   . GLN A 1 1894 ? 157.435 157.460 129.066 1.00 25.76  ? 1894 GLN A OE1   1 
ATOM   2884  N  NE2   . GLN A 1 1894 ? 157.176 159.354 127.892 1.00 21.48  ? 1894 GLN A NE2   1 
ATOM   2885  N  N     . ALA A 1 1895 ? 155.962 160.493 133.607 1.00 13.88  ? 1895 ALA A N     1 
ATOM   2886  C  CA    . ALA A 1 1895 ? 155.218 160.283 134.846 1.00 12.86  ? 1895 ALA A CA    1 
ATOM   2887  C  C     . ALA A 1 1895 ? 153.724 160.500 134.636 1.00 15.06  ? 1895 ALA A C     1 
ATOM   2888  O  O     . ALA A 1 1895 ? 152.901 159.722 135.131 1.00 22.08  ? 1895 ALA A O     1 
ATOM   2889  C  CB    . ALA A 1 1895 ? 155.745 161.214 135.937 1.00 10.37  ? 1895 ALA A CB    1 
ATOM   2890  N  N     . LEU A 1 1896 ? 153.358 161.551 133.899 1.00 13.30  ? 1896 LEU A N     1 
ATOM   2891  C  CA    . LEU A 1 1896 ? 151.949 161.846 133.660 1.00 13.62  ? 1896 LEU A CA    1 
ATOM   2892  C  C     . LEU A 1 1896 ? 151.268 160.729 132.881 1.00 18.55  ? 1896 LEU A C     1 
ATOM   2893  O  O     . LEU A 1 1896 ? 150.126 160.363 133.179 1.00 24.75  ? 1896 LEU A O     1 
ATOM   2894  C  CB    . LEU A 1 1896 ? 151.811 163.171 132.912 1.00 13.56  ? 1896 LEU A CB    1 
ATOM   2895  C  CG    . LEU A 1 1896 ? 152.120 164.445 133.695 1.00 13.10  ? 1896 LEU A CG    1 
ATOM   2896  C  CD1   . LEU A 1 1896 ? 152.321 165.612 132.747 1.00 11.49  ? 1896 LEU A CD1   1 
ATOM   2897  C  CD2   . LEU A 1 1896 ? 151.007 164.735 134.677 1.00 13.92  ? 1896 LEU A CD2   1 
ATOM   2898  N  N     . GLU A 1 1897 ? 151.949 160.184 131.871 1.00 18.74  ? 1897 GLU A N     1 
ATOM   2899  C  CA    . GLU A 1 1897 ? 151.348 159.124 131.067 1.00 24.52  ? 1897 GLU A CA    1 
ATOM   2900  C  C     . GLU A 1 1897 ? 151.094 157.875 131.902 1.00 27.40  ? 1897 GLU A C     1 
ATOM   2901  O  O     . GLU A 1 1897 ? 150.069 157.205 131.734 1.00 35.46  ? 1897 GLU A O     1 
ATOM   2902  C  CB    . GLU A 1 1897 ? 152.237 158.800 129.867 1.00 27.74  ? 1897 GLU A CB    1 
ATOM   2903  C  CG    . GLU A 1 1897 ? 151.679 157.712 128.960 1.00 36.33  ? 1897 GLU A CG    1 
ATOM   2904  C  CD    . GLU A 1 1897 ? 150.540 158.199 128.081 1.00 49.75  ? 1897 GLU A CD    1 
ATOM   2905  O  OE1   . GLU A 1 1897 ? 150.219 159.406 128.122 1.00 48.80  ? 1897 GLU A OE1   1 
ATOM   2906  O  OE2   . GLU A 1 1897 ? 149.961 157.371 127.347 1.00 53.63  ? 1897 GLU A OE2   1 
ATOM   2907  N  N     . ALA A 1 1898 ? 152.011 157.548 132.808 1.00 21.49  ? 1898 ALA A N     1 
ATOM   2908  C  CA    . ALA A 1 1898 ? 151.846 156.405 133.695 1.00 20.85  ? 1898 ALA A CA    1 
ATOM   2909  C  C     . ALA A 1 1898 ? 150.965 156.716 134.901 1.00 21.98  ? 1898 ALA A C     1 
ATOM   2910  O  O     . ALA A 1 1898 ? 150.882 155.891 135.817 1.00 24.74  ? 1898 ALA A O     1 
ATOM   2911  C  CB    . ALA A 1 1898 ? 153.213 155.896 134.156 1.00 20.67  ? 1898 ALA A CB    1 
ATOM   2912  N  N     . ARG A 1 1899 ? 150.321 157.885 134.913 1.00 21.69  ? 1899 ARG A N     1 
ATOM   2913  C  CA    . ARG A 1 1899 ? 149.330 158.251 135.928 1.00 20.35  ? 1899 ARG A CA    1 
ATOM   2914  C  C     . ARG A 1 1899 ? 149.921 158.259 137.337 1.00 18.31  ? 1899 ARG A C     1 
ATOM   2915  O  O     . ARG A 1 1899 ? 149.309 157.771 138.288 1.00 26.03  ? 1899 ARG A O     1 
ATOM   2916  C  CB    . ARG A 1 1899 ? 148.107 157.333 135.861 1.00 27.07  ? 1899 ARG A CB    1 
ATOM   2917  C  CG    . ARG A 1 1899 ? 147.335 157.412 134.553 1.00 32.11  ? 1899 ARG A CG    1 
ATOM   2918  C  CD    . ARG A 1 1899 ? 147.185 158.852 134.081 1.00 35.37  ? 1899 ARG A CD    1 
ATOM   2919  N  NE    . ARG A 1 1899 ? 146.340 158.974 132.898 1.00 44.82  ? 1899 ARG A NE    1 
ATOM   2920  C  CZ    . ARG A 1 1899 ? 146.648 158.508 131.694 1.00 49.29  ? 1899 ARG A CZ    1 
ATOM   2921  N  NH1   . ARG A 1 1899 ? 147.797 157.895 131.460 1.00 43.36  ? 1899 ARG A NH1   1 
ATOM   2922  N  NH2   . ARG A 1 1899 ? 145.785 158.671 130.696 1.00 54.79  ? 1899 ARG A NH2   1 
ATOM   2923  N  N     . LEU A 1 1900 ? 151.121 158.819 137.475 1.00 14.92  ? 1900 LEU A N     1 
ATOM   2924  C  CA    . LEU A 1 1900 ? 151.681 159.089 138.791 1.00 16.46  ? 1900 LEU A CA    1 
ATOM   2925  C  C     . LEU A 1 1900 ? 152.426 160.413 138.724 1.00 15.23  ? 1900 LEU A C     1 
ATOM   2926  O  O     . LEU A 1 1900 ? 152.913 160.804 137.661 1.00 17.89  ? 1900 LEU A O     1 
ATOM   2927  C  CB    . LEU A 1 1900 ? 152.610 157.967 139.276 1.00 14.74  ? 1900 LEU A CB    1 
ATOM   2928  C  CG    . LEU A 1 1900 ? 154.018 157.809 138.702 1.00 12.58  ? 1900 LEU A CG    1 
ATOM   2929  C  CD1   . LEU A 1 1900 ? 154.836 156.890 139.593 1.00 14.65  ? 1900 LEU A CD1   1 
ATOM   2930  C  CD2   . LEU A 1 1900 ? 153.985 157.273 137.293 1.00 17.63  ? 1900 LEU A CD2   1 
ATOM   2931  N  N     . GLY A 1 1901 ? 152.511 161.095 139.860 1.00 14.19  ? 1901 GLY A N     1 
ATOM   2932  C  CA    . GLY A 1 1901 ? 153.058 162.434 139.883 1.00 12.94  ? 1901 GLY A CA    1 
ATOM   2933  C  C     . GLY A 1 1901 ? 154.550 162.473 139.613 1.00 14.94  ? 1901 GLY A C     1 
ATOM   2934  O  O     . GLY A 1 1901 ? 155.244 161.458 139.565 1.00 22.39  ? 1901 GLY A O     1 
ATOM   2935  N  N     . GLY A 1 1902 ? 155.044 163.689 139.417 1.00 8.38   ? 1902 GLY A N     1 
ATOM   2936  C  CA    . GLY A 1 1902 ? 156.462 163.940 139.203 1.00 9.50   ? 1902 GLY A CA    1 
ATOM   2937  C  C     . GLY A 1 1902 ? 157.043 164.698 140.384 1.00 10.47  ? 1902 GLY A C     1 
ATOM   2938  O  O     . GLY A 1 1902 ? 156.396 165.592 140.935 1.00 11.05  ? 1902 GLY A O     1 
ATOM   2939  N  N     . SER A 1 1903 ? 158.265 164.336 140.766 1.00 10.46  ? 1903 SER A N     1 
ATOM   2940  C  CA    . SER A 1 1903 ? 158.924 164.893 141.947 1.00 7.71   ? 1903 SER A CA    1 
ATOM   2941  C  C     . SER A 1 1903 ? 160.336 165.346 141.601 1.00 10.14  ? 1903 SER A C     1 
ATOM   2942  O  O     . SER A 1 1903 ? 161.318 164.688 141.962 1.00 11.91  ? 1903 SER A O     1 
ATOM   2943  C  CB    . SER A 1 1903 ? 158.948 163.873 143.084 1.00 11.62  ? 1903 SER A CB    1 
ATOM   2944  O  OG    . SER A 1 1903 ? 159.894 164.237 144.073 1.00 21.30  ? 1903 SER A OG    1 
ATOM   2945  N  N     . PRO A 1 1904 ? 160.477 166.471 140.900 1.00 12.72  ? 1904 PRO A N     1 
ATOM   2946  C  CA    . PRO A 1 1904 ? 161.818 167.026 140.682 1.00 11.59  ? 1904 PRO A CA    1 
ATOM   2947  C  C     . PRO A 1 1904 ? 162.444 167.462 141.998 1.00 10.88  ? 1904 PRO A C     1 
ATOM   2948  O  O     . PRO A 1 1904 ? 161.768 167.992 142.882 1.00 12.99  ? 1904 PRO A O     1 
ATOM   2949  C  CB    . PRO A 1 1904 ? 161.566 168.219 139.753 1.00 9.27   ? 1904 PRO A CB    1 
ATOM   2950  C  CG    . PRO A 1 1904 ? 160.147 168.587 139.980 1.00 9.04   ? 1904 PRO A CG    1 
ATOM   2951  C  CD    . PRO A 1 1904 ? 159.422 167.322 140.324 1.00 11.33  ? 1904 PRO A CD    1 
ATOM   2952  N  N     . PHE A 1 1905 ? 163.749 167.234 142.122 1.00 11.08  ? 1905 PHE A N     1 
ATOM   2953  C  CA    . PHE A 1 1905 ? 164.471 167.579 143.337 1.00 11.75  ? 1905 PHE A CA    1 
ATOM   2954  C  C     . PHE A 1 1905 ? 165.821 168.176 142.968 1.00 12.89  ? 1905 PHE A C     1 
ATOM   2955  O  O     . PHE A 1 1905 ? 166.267 168.106 141.820 1.00 17.41  ? 1905 PHE A O     1 
ATOM   2956  C  CB    . PHE A 1 1905 ? 164.653 166.364 144.260 1.00 11.73  ? 1905 PHE A CB    1 
ATOM   2957  C  CG    . PHE A 1 1905 ? 165.443 165.240 143.648 1.00 10.79  ? 1905 PHE A CG    1 
ATOM   2958  C  CD1   . PHE A 1 1905 ? 166.820 165.185 143.791 1.00 12.14  ? 1905 PHE A CD1   1 
ATOM   2959  C  CD2   . PHE A 1 1905 ? 164.809 164.228 142.950 1.00 12.86  ? 1905 PHE A CD2   1 
ATOM   2960  C  CE1   . PHE A 1 1905 ? 167.549 164.154 143.235 1.00 11.97  ? 1905 PHE A CE1   1 
ATOM   2961  C  CE2   . PHE A 1 1905 ? 165.535 163.193 142.392 1.00 14.53  ? 1905 PHE A CE2   1 
ATOM   2962  C  CZ    . PHE A 1 1905 ? 166.906 163.157 142.536 1.00 13.17  ? 1905 PHE A CZ    1 
ATOM   2963  N  N     . GLY A 1 1906 ? 166.486 168.765 143.964 1.00 13.30  ? 1906 GLY A N     1 
ATOM   2964  C  CA    . GLY A 1 1906 ? 167.810 169.370 143.723 1.00 15.66  ? 1906 GLY A CA    1 
ATOM   2965  C  C     . GLY A 1 1906 ? 167.990 170.629 144.548 1.00 20.25  ? 1906 GLY A C     1 
ATOM   2966  O  O     . GLY A 1 1906 ? 167.099 170.932 145.368 1.00 27.12  ? 1906 GLY A O     1 
ATOM   2967  N  N     . PRO A 1 1907 ? 169.094 171.385 144.371 1.00 14.71  ? 1907 PRO A N     1 
ATOM   2968  C  CA    . PRO A 1 1907 ? 169.278 172.638 145.088 1.00 16.14  ? 1907 PRO A CA    1 
ATOM   2969  C  C     . PRO A 1 1907 ? 168.311 173.700 144.587 1.00 19.56  ? 1907 PRO A C     1 
ATOM   2970  O  O     . PRO A 1 1907 ? 167.688 173.505 143.524 1.00 24.39  ? 1907 PRO A O     1 
ATOM   2971  C  CB    . PRO A 1 1907 ? 170.741 172.990 144.786 1.00 18.77  ? 1907 PRO A CB    1 
ATOM   2972  C  CG    . PRO A 1 1907 ? 171.002 172.342 143.446 1.00 18.36  ? 1907 PRO A CG    1 
ATOM   2973  C  CD    . PRO A 1 1907 ? 170.193 171.057 143.479 1.00 16.58  ? 1907 PRO A CD    1 
ATOM   2974  N  N     . ALA A 1 1908 ? 168.175 174.796 145.339 1.00 18.36  ? 1908 ALA A N     1 
ATOM   2975  C  CA    . ALA A 1 1908 ? 167.268 175.896 144.934 1.00 17.53  ? 1908 ALA A CA    1 
ATOM   2976  C  C     . ALA A 1 1908 ? 167.874 176.659 143.754 1.00 19.17  ? 1908 ALA A C     1 
ATOM   2977  O  O     . ALA A 1 1908 ? 169.112 176.617 143.585 1.00 26.29  ? 1908 ALA A O     1 
ATOM   2978  C  CB    . ALA A 1 1908 ? 167.014 176.810 146.112 1.00 22.55  ? 1908 ALA A CB    1 
ATOM   2979  N  N     . GLY A 1 1909 ? 167.032 177.330 142.963 1.00 19.43  ? 1909 GLY A N     1 
ATOM   2980  C  CA    . GLY A 1 1909 ? 167.523 178.122 141.818 1.00 16.56  ? 1909 GLY A CA    1 
ATOM   2981  C  C     . GLY A 1 1909 ? 167.756 177.253 140.598 1.00 18.55  ? 1909 GLY A C     1 
ATOM   2982  O  O     . GLY A 1 1909 ? 168.275 177.780 139.592 1.00 23.56  ? 1909 GLY A O     1 
ATOM   2983  N  N     . THR A 1 1910 ? 167.386 175.972 140.675 1.00 17.69  ? 1910 THR A N     1 
ATOM   2984  C  CA    . THR A 1 1910 ? 167.566 175.044 139.535 1.00 14.99  ? 1910 THR A CA    1 
ATOM   2985  C  C     . THR A 1 1910 ? 166.344 175.106 138.641 1.00 12.58  ? 1910 THR A C     1 
ATOM   2986  O  O     . THR A 1 1910 ? 166.333 174.394 137.614 1.00 15.52  ? 1910 THR A O     1 
ATOM   2987  C  CB    . THR A 1 1910 ? 167.834 173.633 140.055 1.00 12.67  ? 1910 THR A CB    1 
ATOM   2988  O  OG1   . THR A 1 1910 ? 166.778 173.360 140.969 1.00 16.12  ? 1910 THR A OG1   1 
ATOM   2989  C  CG2   . THR A 1 1910 ? 169.172 173.530 140.763 1.00 15.02  ? 1910 THR A CG2   1 
ATOM   2990  N  N     . GLY A 1 1911 ? 165.348 175.918 139.006 1.00 12.12  ? 1911 GLY A N     1 
ATOM   2991  C  CA    . GLY A 1 1911 ? 164.160 176.104 138.148 1.00 11.90  ? 1911 GLY A CA    1 
ATOM   2992  C  C     . GLY A 1 1911 ? 163.204 174.929 138.216 1.00 12.71  ? 1911 GLY A C     1 
ATOM   2993  O  O     . GLY A 1 1911 ? 162.407 174.768 137.272 1.00 15.32  ? 1911 GLY A O     1 
ATOM   2994  N  N     . LYS A 1 1912 ? 163.266 174.142 139.294 1.00 12.15  ? 1912 LYS A N     1 
ATOM   2995  C  CA    . LYS A 1 1912 ? 162.387 172.951 139.433 1.00 9.46   ? 1912 LYS A CA    1 
ATOM   2996  C  C     . LYS A 1 1912 ? 160.917 173.397 139.396 1.00 12.26  ? 1912 LYS A C     1 
ATOM   2997  O  O     . LYS A 1 1912 ? 160.155 172.849 138.570 1.00 17.76  ? 1912 LYS A O     1 
ATOM   2998  C  CB    . LYS A 1 1912 ? 162.700 172.213 140.739 1.00 10.27  ? 1912 LYS A CB    1 
ATOM   2999  C  CG    . LYS A 1 1912 ? 164.120 171.678 140.848 1.00 11.85  ? 1912 LYS A CG    1 
ATOM   3000  C  CD    . LYS A 1 1912 ? 164.447 171.156 142.240 1.00 13.23  ? 1912 LYS A CD    1 
ATOM   3001  C  CE    . LYS A 1 1912 ? 164.316 172.225 143.278 1.00 15.65  ? 1912 LYS A CE    1 
ATOM   3002  N  NZ    . LYS A 1 1912 ? 164.577 171.708 144.624 1.00 29.11  ? 1912 LYS A NZ    1 
ATOM   3003  N  N     . THR A 1 1913 ? 160.544 174.365 140.237 1.00 11.98  ? 1913 THR A N     1 
ATOM   3004  C  CA    . THR A 1 1913 ? 159.139 174.829 140.299 1.00 9.85   ? 1913 THR A CA    1 
ATOM   3005  C  C     . THR A 1 1913 ? 158.769 175.495 138.991 1.00 11.57  ? 1913 THR A C     1 
ATOM   3006  O  O     . THR A 1 1913 ? 157.681 175.186 138.458 1.00 11.53  ? 1913 THR A O     1 
ATOM   3007  C  CB    . THR A 1 1913 ? 158.964 175.780 141.481 1.00 14.00  ? 1913 THR A CB    1 
ATOM   3008  O  OG1   . THR A 1 1913 ? 159.265 175.000 142.634 1.00 24.93  ? 1913 THR A OG1   1 
ATOM   3009  C  CG2   . THR A 1 1913 ? 157.553 176.332 141.574 1.00 18.55  ? 1913 THR A CG2   1 
ATOM   3010  N  N     . GLU A 1 1914 ? 159.636 176.376 138.486 1.00 14.02  ? 1914 GLU A N     1 
ATOM   3011  C  CA    . GLU A 1 1914 ? 159.357 177.096 137.216 1.00 12.54  ? 1914 GLU A CA    1 
ATOM   3012  C  C     . GLU A 1 1914 ? 159.200 176.067 136.087 1.00 12.17  ? 1914 GLU A C     1 
ATOM   3013  O  O     . GLU A 1 1914 ? 158.251 176.206 135.286 1.00 13.92  ? 1914 GLU A O     1 
ATOM   3014  C  CB    . GLU A 1 1914 ? 160.478 178.089 136.904 1.00 15.77  ? 1914 GLU A CB    1 
ATOM   3015  C  CG    . GLU A 1 1914 ? 160.585 179.222 137.920 1.00 26.19  ? 1914 GLU A CG    1 
ATOM   3016  C  CD    . GLU A 1 1914 ? 159.370 180.131 137.963 1.00 36.23  ? 1914 GLU A CD    1 
ATOM   3017  O  OE1   . GLU A 1 1914 ? 158.742 180.230 139.038 1.00 34.65  ? 1914 GLU A OE1   1 
ATOM   3018  O  OE2   . GLU A 1 1914 ? 159.053 180.741 136.920 1.00 35.98  ? 1914 GLU A OE2   1 
ATOM   3019  N  N     . SER A 1 1915 ? 160.091 175.072 136.037 1.00 10.80  ? 1915 SER A N     1 
ATOM   3020  C  CA    . SER A 1 1915 ? 160.010 174.018 134.994 1.00 7.03   ? 1915 SER A CA    1 
ATOM   3021  C  C     . SER A 1 1915 ? 158.628 173.356 135.048 1.00 7.16   ? 1915 SER A C     1 
ATOM   3022  O  O     . SER A 1 1915 ? 158.044 173.115 133.969 1.00 11.22  ? 1915 SER A O     1 
ATOM   3023  C  CB    . SER A 1 1915 ? 161.110 173.003 135.154 1.00 9.82   ? 1915 SER A CB    1 
ATOM   3024  O  OG    . SER A 1 1915 ? 162.384 173.603 134.965 1.00 13.12  ? 1915 SER A OG    1 
ATOM   3025  N  N     . VAL A 1 1916 ? 158.127 173.084 136.257 1.00 7.27   ? 1916 VAL A N     1 
ATOM   3026  C  CA    . VAL A 1 1916 ? 156.808 172.468 136.395 1.00 8.09   ? 1916 VAL A CA    1 
ATOM   3027  C  C     . VAL A 1 1916 ? 155.724 173.411 135.888 1.00 7.67   ? 1916 VAL A C     1 
ATOM   3028  O  O     . VAL A 1 1916 ? 154.812 173.001 135.156 1.00 6.76   ? 1916 VAL A O     1 
ATOM   3029  C  CB    . VAL A 1 1916 ? 156.563 172.052 137.858 1.00 6.23   ? 1916 VAL A CB    1 
ATOM   3030  C  CG1   . VAL A 1 1916 ? 155.114 171.641 138.057 1.00 6.46   ? 1916 VAL A CG1   1 
ATOM   3031  C  CG2   . VAL A 1 1916 ? 157.497 170.921 138.249 1.00 7.05   ? 1916 VAL A CG2   1 
ATOM   3032  N  N     . LYS A 1 1917 ? 155.810 174.691 136.260 1.00 10.89  ? 1917 LYS A N     1 
ATOM   3033  C  CA    . LYS A 1 1917 ? 154.832 175.669 135.793 1.00 7.86   ? 1917 LYS A CA    1 
ATOM   3034  C  C     . LYS A 1 1917 ? 154.884 175.833 134.279 1.00 8.96   ? 1917 LYS A C     1 
ATOM   3035  O  O     . LYS A 1 1917 ? 153.842 175.957 133.628 1.00 12.71  ? 1917 LYS A O     1 
ATOM   3036  C  CB    . LYS A 1 1917 ? 155.063 177.013 136.482 1.00 10.72  ? 1917 LYS A CB    1 
ATOM   3037  C  CG    . LYS A 1 1917 ? 154.690 177.034 137.952 1.00 15.11  ? 1917 LYS A CG    1 
ATOM   3038  C  CD    . LYS A 1 1917 ? 154.282 178.429 138.391 1.00 19.92  ? 1917 LYS A CD    1 
ATOM   3039  C  CE    . LYS A 1 1917 ? 155.331 179.458 138.010 1.00 22.01  ? 1917 LYS A CE    1 
ATOM   3040  N  NZ    . LYS A 1 1917 ? 154.935 180.832 138.425 1.00 25.20  ? 1917 LYS A NZ    1 
ATOM   3041  N  N     . ALA A 1 1918 ? 156.088 175.848 133.703 1.00 9.92   ? 1918 ALA A N     1 
ATOM   3042  C  CA    . ALA A 1 1918 ? 156.225 175.991 132.258 1.00 6.76   ? 1918 ALA A CA    1 
ATOM   3043  C  C     . ALA A 1 1918 ? 155.639 174.793 131.525 1.00 7.51   ? 1918 ALA A C     1 
ATOM   3044  O  O     . ALA A 1 1918 ? 154.996 174.953 130.482 1.00 10.96  ? 1918 ALA A O     1 
ATOM   3045  C  CB    . ALA A 1 1918 ? 157.695 176.181 131.887 1.00 8.79   ? 1918 ALA A CB    1 
ATOM   3046  N  N     . LEU A 1 1919 ? 155.859 173.583 132.046 1.00 7.79   ? 1919 LEU A N     1 
ATOM   3047  C  CA    . LEU A 1 1919 ? 155.251 172.406 131.434 1.00 7.91   ? 1919 LEU A CA    1 
ATOM   3048  C  C     . LEU A 1 1919 ? 153.733 172.456 131.542 1.00 8.71   ? 1919 LEU A C     1 
ATOM   3049  O  O     . LEU A 1 1919 ? 153.024 172.107 130.591 1.00 12.00  ? 1919 LEU A O     1 
ATOM   3050  C  CB    . LEU A 1 1919 ? 155.789 171.131 132.078 1.00 9.61   ? 1919 LEU A CB    1 
ATOM   3051  C  CG    . LEU A 1 1919 ? 155.135 169.851 131.554 1.00 8.76   ? 1919 LEU A CG    1 
ATOM   3052  C  CD1   . LEU A 1 1919 ? 155.398 169.682 130.066 1.00 9.51   ? 1919 LEU A CD1   1 
ATOM   3053  C  CD2   . LEU A 1 1919 ? 155.619 168.645 132.324 1.00 10.49  ? 1919 LEU A CD2   1 
ATOM   3054  N  N     . GLY A 1 1920 ? 153.215 172.884 132.695 1.00 10.57  ? 1920 GLY A N     1 
ATOM   3055  C  CA    . GLY A 1 1920 ? 151.773 173.007 132.841 1.00 8.88   ? 1920 GLY A CA    1 
ATOM   3056  C  C     . GLY A 1 1920 ? 151.176 174.032 131.897 1.00 11.21  ? 1920 GLY A C     1 
ATOM   3057  O  O     . GLY A 1 1920 ? 150.075 173.844 131.375 1.00 13.28  ? 1920 GLY A O     1 
ATOM   3058  N  N     . HIS A 1 1921 ? 151.894 175.133 131.668 1.00 11.37  ? 1921 HIS A N     1 
ATOM   3059  C  CA    . HIS A 1 1921 ? 151.412 176.158 130.749 1.00 10.30  ? 1921 HIS A CA    1 
ATOM   3060  C  C     . HIS A 1 1921 ? 151.546 175.721 129.297 1.00 11.65  ? 1921 HIS A C     1 
ATOM   3061  O  O     . HIS A 1 1921 ? 150.762 176.157 128.446 1.00 15.76  ? 1921 HIS A O     1 
ATOM   3062  C  CB    . HIS A 1 1921 ? 152.166 177.467 130.984 1.00 11.26  ? 1921 HIS A CB    1 
ATOM   3063  C  CG    . HIS A 1 1921 ? 151.968 178.040 132.353 1.00 16.54  ? 1921 HIS A CG    1 
ATOM   3064  N  ND1   . HIS A 1 1921 ? 150.919 177.674 133.168 1.00 19.18  ? 1921 HIS A ND1   1 
ATOM   3065  C  CD2   . HIS A 1 1921 ? 152.686 178.952 133.050 1.00 17.67  ? 1921 HIS A CD2   1 
ATOM   3066  C  CE1   . HIS A 1 1921 ? 150.998 178.336 134.308 1.00 19.51  ? 1921 HIS A CE1   1 
ATOM   3067  N  NE2   . HIS A 1 1921 ? 152.062 179.118 134.262 1.00 20.15  ? 1921 HIS A NE2   1 
ATOM   3068  N  N     . GLN A 1 1922 ? 152.530 174.873 128.993 1.00 11.17  ? 1922 GLN A N     1 
ATOM   3069  C  CA    . GLN A 1 1922 ? 152.686 174.371 127.632 1.00 10.81  ? 1922 GLN A CA    1 
ATOM   3070  C  C     . GLN A 1 1922 ? 151.505 173.504 127.220 1.00 13.46  ? 1922 GLN A C     1 
ATOM   3071  O  O     . GLN A 1 1922 ? 151.124 173.495 126.044 1.00 15.78  ? 1922 GLN A O     1 
ATOM   3072  C  CB    . GLN A 1 1922 ? 153.994 173.589 127.510 1.00 11.19  ? 1922 GLN A CB    1 
ATOM   3073  C  CG    . GLN A 1 1922 ? 154.254 173.018 126.129 1.00 15.00  ? 1922 GLN A CG    1 
ATOM   3074  C  CD    . GLN A 1 1922 ? 154.561 174.091 125.105 1.00 25.38  ? 1922 GLN A CD    1 
ATOM   3075  O  OE1   . GLN A 1 1922 ? 155.705 174.523 124.966 1.00 36.72  ? 1922 GLN A OE1   1 
ATOM   3076  N  NE2   . GLN A 1 1922 ? 153.539 174.528 124.381 1.00 19.32  ? 1922 GLN A NE2   1 
ATOM   3077  N  N     . LEU A 1 1923 ? 150.918 172.776 128.165 1.00 15.04  ? 1923 LEU A N     1 
ATOM   3078  C  CA    . LEU A 1 1923 ? 149.734 171.967 127.915 1.00 11.83  ? 1923 LEU A CA    1 
ATOM   3079  C  C     . LEU A 1 1923 ? 148.442 172.734 128.165 1.00 14.49  ? 1923 LEU A C     1 
ATOM   3080  O  O     . LEU A 1 1923 ? 147.361 172.141 128.101 1.00 20.02  ? 1923 LEU A O     1 
ATOM   3081  C  CB    . LEU A 1 1923 ? 149.768 170.704 128.779 1.00 9.83   ? 1923 LEU A CB    1 
ATOM   3082  C  CG    . LEU A 1 1923 ? 151.085 169.927 128.785 1.00 9.59   ? 1923 LEU A CG    1 
ATOM   3083  C  CD1   . LEU A 1 1923 ? 151.025 168.778 129.776 1.00 9.62   ? 1923 LEU A CD1   1 
ATOM   3084  C  CD2   . LEU A 1 1923 ? 151.416 169.419 127.392 1.00 10.64  ? 1923 LEU A CD2   1 
ATOM   3085  N  N     . GLY A 1 1924 ? 148.532 174.030 128.450 1.00 12.93  ? 1924 GLY A N     1 
ATOM   3086  C  CA    . GLY A 1 1924 ? 147.351 174.830 128.711 1.00 13.36  ? 1924 GLY A CA    1 
ATOM   3087  C  C     . GLY A 1 1924 ? 146.611 174.454 129.973 1.00 15.92  ? 1924 GLY A C     1 
ATOM   3088  O  O     . GLY A 1 1924 ? 145.380 174.540 130.010 1.00 22.98  ? 1924 GLY A O     1 
ATOM   3089  N  N     . ARG A 1 1925 ? 147.328 174.046 131.012 1.00 15.48  ? 1925 ARG A N     1 
ATOM   3090  C  CA    . ARG A 1 1925 ? 146.724 173.619 132.264 1.00 15.34  ? 1925 ARG A CA    1 
ATOM   3091  C  C     . ARG A 1 1925 ? 146.689 174.766 133.266 1.00 17.96  ? 1925 ARG A C     1 
ATOM   3092  O  O     . ARG A 1 1925 ? 147.424 175.750 133.152 1.00 22.80  ? 1925 ARG A O     1 
ATOM   3093  C  CB    . ARG A 1 1925 ? 147.490 172.434 132.858 1.00 11.25  ? 1925 ARG A CB    1 
ATOM   3094  C  CG    . ARG A 1 1925 ? 147.518 171.202 131.973 1.00 12.45  ? 1925 ARG A CG    1 
ATOM   3095  C  CD    . ARG A 1 1925 ? 146.129 170.618 131.790 1.00 16.25  ? 1925 ARG A CD    1 
ATOM   3096  N  NE    . ARG A 1 1925 ? 146.179 169.242 131.313 1.00 18.33  ? 1925 ARG A NE    1 
ATOM   3097  C  CZ    . ARG A 1 1925 ? 146.340 168.894 130.044 1.00 18.87  ? 1925 ARG A CZ    1 
ATOM   3098  N  NH1   . ARG A 1 1925 ? 146.463 169.801 129.089 1.00 17.44  ? 1925 ARG A NH1   1 
ATOM   3099  N  NH2   . ARG A 1 1925 ? 146.378 167.604 129.725 1.00 20.65  ? 1925 ARG A NH2   1 
ATOM   3100  N  N     . PHE A 1 1926 ? 145.814 174.622 134.257 1.00 18.49  ? 1926 PHE A N     1 
ATOM   3101  C  CA    . PHE A 1 1926 ? 145.716 175.569 135.365 1.00 16.41  ? 1926 PHE A CA    1 
ATOM   3102  C  C     . PHE A 1 1926 ? 146.622 175.052 136.475 1.00 15.97  ? 1926 PHE A C     1 
ATOM   3103  O  O     . PHE A 1 1926 ? 146.288 174.090 137.169 1.00 18.23  ? 1926 PHE A O     1 
ATOM   3104  C  CB    . PHE A 1 1926 ? 144.268 175.710 135.821 1.00 19.03  ? 1926 PHE A CB    1 
ATOM   3105  C  CG    . PHE A 1 1926 ? 144.065 176.702 136.936 1.00 20.72  ? 1926 PHE A CG    1 
ATOM   3106  C  CD1   . PHE A 1 1926 ? 144.988 177.706 137.177 1.00 23.43  ? 1926 PHE A CD1   1 
ATOM   3107  C  CD2   . PHE A 1 1926 ? 142.940 176.631 137.740 1.00 24.91  ? 1926 PHE A CD2   1 
ATOM   3108  C  CE1   . PHE A 1 1926 ? 144.796 178.613 138.201 1.00 24.46  ? 1926 PHE A CE1   1 
ATOM   3109  C  CE2   . PHE A 1 1926 ? 142.742 177.535 138.763 1.00 27.34  ? 1926 PHE A CE2   1 
ATOM   3110  C  CZ    . PHE A 1 1926 ? 143.671 178.527 138.994 1.00 26.02  ? 1926 PHE A CZ    1 
ATOM   3111  N  N     . VAL A 1 1927 ? 147.779 175.683 136.638 1.00 13.89  ? 1927 VAL A N     1 
ATOM   3112  C  CA    . VAL A 1 1927 ? 148.767 175.251 137.620 1.00 12.08  ? 1927 VAL A CA    1 
ATOM   3113  C  C     . VAL A 1 1927 ? 148.635 176.118 138.864 1.00 14.95  ? 1927 VAL A C     1 
ATOM   3114  O  O     . VAL A 1 1927 ? 148.774 177.344 138.795 1.00 25.30  ? 1927 VAL A O     1 
ATOM   3115  C  CB    . VAL A 1 1927 ? 150.189 175.325 137.046 1.00 10.50  ? 1927 VAL A CB    1 
ATOM   3116  C  CG1   . VAL A 1 1927 ? 151.182 174.703 138.014 1.00 8.59   ? 1927 VAL A CG1   1 
ATOM   3117  C  CG2   . VAL A 1 1927 ? 150.249 174.632 135.699 1.00 11.03  ? 1927 VAL A CG2   1 
ATOM   3118  N  N     . LEU A 1 1928 ? 148.367 175.483 140.000 1.00 10.77  ? 1928 LEU A N     1 
ATOM   3119  C  CA    . LEU A 1 1928 ? 148.330 176.152 141.292 1.00 10.67  ? 1928 LEU A CA    1 
ATOM   3120  C  C     . LEU A 1 1928 ? 149.560 175.752 142.091 1.00 11.51  ? 1928 LEU A C     1 
ATOM   3121  O  O     . LEU A 1 1928 ? 149.884 174.564 142.188 1.00 14.70  ? 1928 LEU A O     1 
ATOM   3122  C  CB    . LEU A 1 1928 ? 147.058 175.805 142.066 1.00 11.61  ? 1928 LEU A CB    1 
ATOM   3123  C  CG    . LEU A 1 1928 ? 145.748 176.369 141.517 1.00 15.26  ? 1928 LEU A CG    1 
ATOM   3124  C  CD1   . LEU A 1 1928 ? 145.076 175.372 140.597 1.00 20.02  ? 1928 LEU A CD1   1 
ATOM   3125  C  CD2   . LEU A 1 1928 ? 144.823 176.762 142.655 1.00 18.75  ? 1928 LEU A CD2   1 
ATOM   3126  N  N     . VAL A 1 1929 ? 150.237 176.742 142.661 1.00 11.97  ? 1929 VAL A N     1 
ATOM   3127  C  CA    . VAL A 1 1929 ? 151.470 176.529 143.407 1.00 12.00  ? 1929 VAL A CA    1 
ATOM   3128  C  C     . VAL A 1 1929 ? 151.171 176.718 144.886 1.00 16.04  ? 1929 VAL A C     1 
ATOM   3129  O  O     . VAL A 1 1929 ? 150.631 177.753 145.293 1.00 23.75  ? 1929 VAL A O     1 
ATOM   3130  C  CB    . VAL A 1 1929 ? 152.577 177.485 142.940 1.00 13.71  ? 1929 VAL A CB    1 
ATOM   3131  C  CG1   . VAL A 1 1929 ? 153.797 177.352 143.830 1.00 16.22  ? 1929 VAL A CG1   1 
ATOM   3132  C  CG2   . VAL A 1 1929 ? 152.936 177.201 141.495 1.00 14.53  ? 1929 VAL A CG2   1 
ATOM   3133  N  N     . PHE A 1 1930 ? 151.517 175.717 145.689 1.00 13.23  ? 1930 PHE A N     1 
ATOM   3134  C  CA    . PHE A 1 1930 ? 151.335 175.762 147.132 1.00 15.80  ? 1930 PHE A CA    1 
ATOM   3135  C  C     . PHE A 1 1930 ? 152.694 175.655 147.806 1.00 18.04  ? 1930 PHE A C     1 
ATOM   3136  O  O     . PHE A 1 1930 ? 153.466 174.738 147.508 1.00 24.37  ? 1930 PHE A O     1 
ATOM   3137  C  CB    . PHE A 1 1930 ? 150.419 174.633 147.611 1.00 13.56  ? 1930 PHE A CB    1 
ATOM   3138  C  CG    . PHE A 1 1930 ? 149.054 174.652 146.988 1.00 14.14  ? 1930 PHE A CG    1 
ATOM   3139  C  CD1   . PHE A 1 1930 ? 148.039 175.413 147.539 1.00 14.82  ? 1930 PHE A CD1   1 
ATOM   3140  C  CD2   . PHE A 1 1930 ? 148.785 173.902 145.856 1.00 13.88  ? 1930 PHE A CD2   1 
ATOM   3141  C  CE1   . PHE A 1 1930 ? 146.781 175.431 146.969 1.00 16.93  ? 1930 PHE A CE1   1 
ATOM   3142  C  CE2   . PHE A 1 1930 ? 147.529 173.916 145.282 1.00 12.58  ? 1930 PHE A CE2   1 
ATOM   3143  C  CZ    . PHE A 1 1930 ? 146.527 174.681 145.839 1.00 13.43  ? 1930 PHE A CZ    1 
ATOM   3144  N  N     . ASN A 1 1931 ? 152.983 176.589 148.707 1.00 17.27  ? 1931 ASN A N     1 
ATOM   3145  C  CA    . ASN A 1 1931 ? 154.208 176.545 149.502 1.00 19.19  ? 1931 ASN A CA    1 
ATOM   3146  C  C     . ASN A 1 1931 ? 153.897 175.764 150.771 1.00 23.55  ? 1931 ASN A C     1 
ATOM   3147  O  O     . ASN A 1 1931 ? 153.416 176.322 151.759 1.00 28.72  ? 1931 ASN A O     1 
ATOM   3148  C  CB    . ASN A 1 1931 ? 154.713 177.948 149.810 1.00 22.17  ? 1931 ASN A CB    1 
ATOM   3149  C  CG    . ASN A 1 1931 ? 156.109 177.945 150.394 1.00 22.80  ? 1931 ASN A CG    1 
ATOM   3150  O  OD1   . ASN A 1 1931 ? 157.094 177.806 149.671 1.00 30.58  ? 1931 ASN A OD1   1 
ATOM   3151  N  ND2   . ASN A 1 1931 ? 156.202 178.093 151.709 1.00 22.39  ? 1931 ASN A ND2   1 
ATOM   3152  N  N     . CYS A 1 1932 ? 154.172 174.464 150.739 1.00 19.65  ? 1932 CYS A N     1 
ATOM   3153  C  CA    . CYS A 1 1932 ? 153.785 173.585 151.832 1.00 21.21  ? 1932 CYS A CA    1 
ATOM   3154  C  C     . CYS A 1 1932 ? 154.623 173.849 153.076 1.00 24.39  ? 1932 CYS A C     1 
ATOM   3155  O  O     . CYS A 1 1932 ? 155.833 174.079 152.996 1.00 29.00  ? 1932 CYS A O     1 
ATOM   3156  C  CB    . CYS A 1 1932 ? 153.925 172.127 151.405 1.00 21.10  ? 1932 CYS A CB    1 
ATOM   3157  S  SG    . CYS A 1 1932 ? 152.693 171.579 150.205 1.00 35.11  ? 1932 CYS A SG    1 
ATOM   3158  N  N     . ASP A 1 1933 ? 153.966 173.816 154.234 1.00 24.56  ? 1933 ASP A N     1 
ATOM   3159  C  CA    . ASP A 1 1933 ? 154.632 173.916 155.523 1.00 23.54  ? 1933 ASP A CA    1 
ATOM   3160  C  C     . ASP A 1 1933 ? 154.045 172.855 156.446 1.00 26.12  ? 1933 ASP A C     1 
ATOM   3161  O  O     . ASP A 1 1933 ? 153.181 172.068 156.048 1.00 29.01  ? 1933 ASP A O     1 
ATOM   3162  C  CB    . ASP A 1 1933 ? 154.503 175.326 156.113 1.00 26.86  ? 1933 ASP A CB    1 
ATOM   3163  C  CG    . ASP A 1 1933 ? 153.086 175.665 156.516 1.00 33.37  ? 1933 ASP A CG    1 
ATOM   3164  O  OD1   . ASP A 1 1933 ? 152.303 176.097 155.646 1.00 39.04  ? 1933 ASP A OD1   1 
ATOM   3165  O  OD2   . ASP A 1 1933 ? 152.760 175.513 157.710 1.00 37.29  ? 1933 ASP A OD2   1 
ATOM   3166  N  N     . GLU A 1 1934 ? 154.523 172.833 157.692 1.00 28.15  ? 1934 GLU A N     1 
ATOM   3167  C  CA    . GLU A 1 1934 ? 154.125 171.781 158.622 1.00 31.17  ? 1934 GLU A CA    1 
ATOM   3168  C  C     . GLU A 1 1934 ? 152.647 171.845 158.988 1.00 33.45  ? 1934 GLU A C     1 
ATOM   3169  O  O     . GLU A 1 1934 ? 152.098 170.846 159.466 1.00 36.45  ? 1934 GLU A O     1 
ATOM   3170  C  CB    . GLU A 1 1934 ? 154.981 171.845 159.888 1.00 30.84  ? 1934 GLU A CB    1 
ATOM   3171  C  CG    . GLU A 1 1934 ? 154.686 173.032 160.784 1.00 36.67  ? 1934 GLU A CG    1 
ATOM   3172  C  CD    . GLU A 1 1934 ? 155.608 174.205 160.518 1.00 42.62  ? 1934 GLU A CD    1 
ATOM   3173  O  OE1   . GLU A 1 1934 ? 155.459 175.244 161.194 1.00 44.35  ? 1934 GLU A OE1   1 
ATOM   3174  O  OE2   . GLU A 1 1934 ? 156.481 174.088 159.633 1.00 40.99  ? 1934 GLU A OE2   1 
ATOM   3175  N  N     . THR A 1 1935 ? 151.989 172.984 158.778 1.00 29.59  ? 1935 THR A N     1 
ATOM   3176  C  CA    . THR A 1 1935 ? 150.570 173.105 159.087 1.00 25.67  ? 1935 THR A CA    1 
ATOM   3177  C  C     . THR A 1 1935 ? 149.673 172.532 157.998 1.00 29.61  ? 1935 THR A C     1 
ATOM   3178  O  O     . THR A 1 1935 ? 148.453 172.487 158.186 1.00 31.72  ? 1935 THR A O     1 
ATOM   3179  C  CB    . THR A 1 1935 ? 150.201 174.570 159.336 1.00 26.12  ? 1935 THR A CB    1 
ATOM   3180  O  OG1   . THR A 1 1935 ? 150.433 175.333 158.146 1.00 31.17  ? 1935 THR A OG1   1 
ATOM   3181  C  CG2   . THR A 1 1935 ? 151.034 175.141 160.471 1.00 34.20  ? 1935 THR A CG2   1 
ATOM   3182  N  N     . PHE A 1 1936 ? 150.238 172.099 156.870 1.00 29.65  ? 1936 PHE A N     1 
ATOM   3183  C  CA    . PHE A 1 1936 ? 149.470 171.425 155.824 1.00 28.78  ? 1936 PHE A CA    1 
ATOM   3184  C  C     . PHE A 1 1936 ? 149.166 170.010 156.306 1.00 32.75  ? 1936 PHE A C     1 
ATOM   3185  O  O     . PHE A 1 1936 ? 149.851 169.039 155.977 1.00 34.65  ? 1936 PHE A O     1 
ATOM   3186  C  CB    . PHE A 1 1936 ? 150.234 171.418 154.506 1.00 24.54  ? 1936 PHE A CB    1 
ATOM   3187  C  CG    . PHE A 1 1936 ? 150.060 172.668 153.693 1.00 26.22  ? 1936 PHE A CG    1 
ATOM   3188  C  CD1   . PHE A 1 1936 ? 150.574 173.875 154.132 1.00 25.11  ? 1936 PHE A CD1   1 
ATOM   3189  C  CD2   . PHE A 1 1936 ? 149.389 172.633 152.483 1.00 25.70  ? 1936 PHE A CD2   1 
ATOM   3190  C  CE1   . PHE A 1 1936 ? 150.417 175.024 153.382 1.00 23.26  ? 1936 PHE A CE1   1 
ATOM   3191  C  CE2   . PHE A 1 1936 ? 149.229 173.778 151.730 1.00 23.19  ? 1936 PHE A CE2   1 
ATOM   3192  C  CZ    . PHE A 1 1936 ? 149.744 174.975 152.180 1.00 23.25  ? 1936 PHE A CZ    1 
ATOM   3193  N  N     . ASP A 1 1937 ? 148.113 169.898 157.108 1.00 29.05  ? 1937 ASP A N     1 
ATOM   3194  C  CA    . ASP A 1 1937 ? 147.767 168.628 157.730 1.00 26.37  ? 1937 ASP A CA    1 
ATOM   3195  C  C     . ASP A 1 1937 ? 147.012 167.749 156.734 1.00 31.33  ? 1937 ASP A C     1 
ATOM   3196  O  O     . ASP A 1 1937 ? 146.909 168.057 155.543 1.00 31.14  ? 1937 ASP A O     1 
ATOM   3197  C  CB    . ASP A 1 1937 ? 146.968 168.867 159.009 1.00 28.57  ? 1937 ASP A CB    1 
ATOM   3198  C  CG    . ASP A 1 1937 ? 145.628 169.518 158.747 1.00 38.62  ? 1937 ASP A CG    1 
ATOM   3199  O  OD1   . ASP A 1 1937 ? 145.603 170.609 158.140 1.00 42.77  ? 1937 ASP A OD1   1 
ATOM   3200  O  OD2   . ASP A 1 1937 ? 144.597 168.940 159.149 1.00 41.09  ? 1937 ASP A OD2   1 
ATOM   3201  N  N     . PHE A 1 1938 ? 146.483 166.625 157.223 1.00 33.22  ? 1938 PHE A N     1 
ATOM   3202  C  CA    . PHE A 1 1938 ? 145.766 165.695 156.357 1.00 26.06  ? 1938 PHE A CA    1 
ATOM   3203  C  C     . PHE A 1 1938 ? 144.510 166.331 155.773 1.00 26.40  ? 1938 PHE A C     1 
ATOM   3204  O  O     . PHE A 1 1938 ? 144.228 166.181 154.578 1.00 24.21  ? 1938 PHE A O     1 
ATOM   3205  C  CB    . PHE A 1 1938 ? 145.417 164.429 157.141 1.00 25.69  ? 1938 PHE A CB    1 
ATOM   3206  C  CG    . PHE A 1 1938 ? 144.590 163.439 156.372 1.00 26.97  ? 1938 PHE A CG    1 
ATOM   3207  C  CD1   . PHE A 1 1938 ? 145.183 162.570 155.474 1.00 27.17  ? 1938 PHE A CD1   1 
ATOM   3208  C  CD2   . PHE A 1 1938 ? 143.220 163.367 156.558 1.00 31.76  ? 1938 PHE A CD2   1 
ATOM   3209  C  CE1   . PHE A 1 1938 ? 144.427 161.654 154.772 1.00 28.81  ? 1938 PHE A CE1   1 
ATOM   3210  C  CE2   . PHE A 1 1938 ? 142.457 162.454 155.857 1.00 30.10  ? 1938 PHE A CE2   1 
ATOM   3211  C  CZ    . PHE A 1 1938 ? 143.062 161.597 154.962 1.00 31.70  ? 1938 PHE A CZ    1 
ATOM   3212  N  N     . GLN A 1 1939 ? 143.750 167.057 156.596 1.00 27.20  ? 1939 GLN A N     1 
ATOM   3213  C  CA    . GLN A 1 1939 ? 142.471 167.595 156.144 1.00 24.31  ? 1939 GLN A CA    1 
ATOM   3214  C  C     . GLN A 1 1939 ? 142.657 168.717 155.129 1.00 27.49  ? 1939 GLN A C     1 
ATOM   3215  O  O     . GLN A 1 1939 ? 141.955 168.762 154.113 1.00 30.54  ? 1939 GLN A O     1 
ATOM   3216  C  CB    . GLN A 1 1939 ? 141.658 168.083 157.341 1.00 30.64  ? 1939 GLN A CB    1 
ATOM   3217  C  CG    . GLN A 1 1939 ? 141.409 167.017 158.392 1.00 36.66  ? 1939 GLN A CG    1 
ATOM   3218  C  CD    . GLN A 1 1939 ? 140.113 166.268 158.161 1.00 50.53  ? 1939 GLN A CD    1 
ATOM   3219  O  OE1   . GLN A 1 1939 ? 140.104 165.044 158.034 1.00 48.21  ? 1939 GLN A OE1   1 
ATOM   3220  N  NE2   . GLN A 1 1939 ? 139.008 167.002 158.104 1.00 55.36  ? 1939 GLN A NE2   1 
ATOM   3221  N  N     . ALA A 1 1940 ? 143.587 169.638 155.390 1.00 25.79  ? 1940 ALA A N     1 
ATOM   3222  C  CA    . ALA A 1 1940 ? 143.819 170.736 154.456 1.00 19.35  ? 1940 ALA A CA    1 
ATOM   3223  C  C     . ALA A 1 1940 ? 144.349 170.226 153.123 1.00 18.48  ? 1940 ALA A C     1 
ATOM   3224  O  O     . ALA A 1 1940 ? 143.912 170.675 152.054 1.00 25.66  ? 1940 ALA A O     1 
ATOM   3225  C  CB    . ALA A 1 1940 ? 144.789 171.745 155.069 1.00 23.96  ? 1940 ALA A CB    1 
ATOM   3226  N  N     . MET A 1 1941 ? 145.290 169.282 153.166 1.00 19.13  ? 1941 MET A N     1 
ATOM   3227  C  CA    . MET A 1 1941 ? 145.828 168.719 151.934 1.00 18.11  ? 1941 MET A CA    1 
ATOM   3228  C  C     . MET A 1 1941 ? 144.754 167.945 151.180 1.00 16.50  ? 1941 MET A C     1 
ATOM   3229  O  O     . MET A 1 1941 ? 144.702 167.984 149.945 1.00 16.53  ? 1941 MET A O     1 
ATOM   3230  C  CB    . MET A 1 1941 ? 147.027 167.826 152.254 1.00 16.47  ? 1941 MET A CB    1 
ATOM   3231  C  CG    . MET A 1 1941 ? 148.353 168.576 152.301 1.00 17.45  ? 1941 MET A CG    1 
ATOM   3232  S  SD    . MET A 1 1941 ? 149.016 169.048 150.695 1.00 33.33  ? 1941 MET A SD    1 
ATOM   3233  C  CE    . MET A 1 1941 ? 148.984 167.478 149.847 1.00 16.61  ? 1941 MET A CE    1 
ATOM   3234  N  N     . GLY A 1 1942 ? 143.877 167.247 151.907 1.00 17.83  ? 1942 GLY A N     1 
ATOM   3235  C  CA    . GLY A 1 1942 ? 142.772 166.561 151.259 1.00 18.08  ? 1942 GLY A CA    1 
ATOM   3236  C  C     . GLY A 1 1942 ? 141.790 167.515 150.605 1.00 18.79  ? 1942 GLY A C     1 
ATOM   3237  O  O     . GLY A 1 1942 ? 141.262 167.232 149.530 1.00 24.14  ? 1942 GLY A O     1 
ATOM   3238  N  N     . ARG A 1 1943 ? 141.522 168.651 151.252 1.00 17.36  ? 1943 ARG A N     1 
ATOM   3239  C  CA    . ARG A 1 1943 ? 140.655 169.660 150.648 1.00 16.85  ? 1943 ARG A CA    1 
ATOM   3240  C  C     . ARG A 1 1943 ? 141.284 170.243 149.387 1.00 19.18  ? 1943 ARG A C     1 
ATOM   3241  O  O     . ARG A 1 1943 ? 140.594 170.468 148.382 1.00 26.17  ? 1943 ARG A O     1 
ATOM   3242  C  CB    . ARG A 1 1943 ? 140.354 170.761 151.663 1.00 20.55  ? 1943 ARG A CB    1 
ATOM   3243  C  CG    . ARG A 1 1943 ? 138.966 171.364 151.543 1.00 29.95  ? 1943 ARG A CG    1 
ATOM   3244  C  CD    . ARG A 1 1943 ? 138.838 172.611 152.403 1.00 42.32  ? 1943 ARG A CD    1 
ATOM   3245  N  NE    . ARG A 1 1943 ? 139.202 173.822 151.678 1.00 45.65  ? 1943 ARG A NE    1 
ATOM   3246  C  CZ    . ARG A 1 1943 ? 138.347 174.571 150.996 1.00 54.23  ? 1943 ARG A CZ    1 
ATOM   3247  N  NH1   . ARG A 1 1943 ? 137.062 174.265 150.927 1.00 56.00  ? 1943 ARG A NH1   1 
ATOM   3248  N  NH2   . ARG A 1 1943 ? 138.792 175.656 150.368 1.00 55.05  ? 1943 ARG A NH2   1 
ATOM   3249  N  N     . ILE A 1 1944 ? 142.595 170.493 149.422 1.00 16.78  ? 1944 ILE A N     1 
ATOM   3250  C  CA    . ILE A 1 1944 ? 143.298 170.957 148.227 1.00 13.64  ? 1944 ILE A CA    1 
ATOM   3251  C  C     . ILE A 1 1944 ? 143.197 169.920 147.115 1.00 15.25  ? 1944 ILE A C     1 
ATOM   3252  O  O     . ILE A 1 1944 ? 142.972 170.257 145.945 1.00 15.86  ? 1944 ILE A O     1 
ATOM   3253  C  CB    . ILE A 1 1944 ? 144.763 171.288 148.566 1.00 11.41  ? 1944 ILE A CB    1 
ATOM   3254  C  CG1   . ILE A 1 1944 ? 144.837 172.523 149.464 1.00 14.77  ? 1944 ILE A CG1   1 
ATOM   3255  C  CG2   . ILE A 1 1944 ? 145.572 171.501 147.299 1.00 11.31  ? 1944 ILE A CG2   1 
ATOM   3256  C  CD1   . ILE A 1 1944 ? 146.207 172.766 150.052 1.00 13.35  ? 1944 ILE A CD1   1 
ATOM   3257  N  N     . PHE A 1 1945 ? 143.362 168.641 147.465 1.00 16.08  ? 1945 PHE A N     1 
ATOM   3258  C  CA    . PHE A 1 1945 ? 143.225 167.574 146.479 1.00 14.71  ? 1945 PHE A CA    1 
ATOM   3259  C  C     . PHE A 1 1945 ? 141.814 167.517 145.910 1.00 15.51  ? 1945 PHE A C     1 
ATOM   3260  O  O     . PHE A 1 1945 ? 141.634 167.260 144.717 1.00 16.86  ? 1945 PHE A O     1 
ATOM   3261  C  CB    . PHE A 1 1945 ? 143.603 166.230 147.100 1.00 14.52  ? 1945 PHE A CB    1 
ATOM   3262  C  CG    . PHE A 1 1945 ? 145.080 165.989 147.169 1.00 13.75  ? 1945 PHE A CG    1 
ATOM   3263  C  CD1   . PHE A 1 1945 ? 145.929 166.563 146.240 1.00 12.78  ? 1945 PHE A CD1   1 
ATOM   3264  C  CD2   . PHE A 1 1945 ? 145.619 165.179 148.153 1.00 15.86  ? 1945 PHE A CD2   1 
ATOM   3265  C  CE1   . PHE A 1 1945 ? 147.288 166.341 146.295 1.00 15.26  ? 1945 PHE A CE1   1 
ATOM   3266  C  CE2   . PHE A 1 1945 ? 146.978 164.953 148.212 1.00 14.07  ? 1945 PHE A CE2   1 
ATOM   3267  C  CZ    . PHE A 1 1945 ? 147.813 165.533 147.280 1.00 14.19  ? 1945 PHE A CZ    1 
ATOM   3268  N  N     . VAL A 1 1946 ? 140.801 167.730 146.750 1.00 18.60  ? 1946 VAL A N     1 
ATOM   3269  C  CA    . VAL A 1 1946 ? 139.420 167.742 146.273 1.00 17.38  ? 1946 VAL A CA    1 
ATOM   3270  C  C     . VAL A 1 1946 ? 139.224 168.862 145.260 1.00 20.80  ? 1946 VAL A C     1 
ATOM   3271  O  O     . VAL A 1 1946 ? 138.616 168.673 144.197 1.00 26.14  ? 1946 VAL A O     1 
ATOM   3272  C  CB    . VAL A 1 1946 ? 138.446 167.879 147.457 1.00 14.57  ? 1946 VAL A CB    1 
ATOM   3273  C  CG1   . VAL A 1 1946 ? 137.077 168.332 146.976 1.00 22.45  ? 1946 VAL A CG1   1 
ATOM   3274  C  CG2   . VAL A 1 1946 ? 138.343 166.570 148.217 1.00 18.14  ? 1946 VAL A CG2   1 
ATOM   3275  N  N     . GLY A 1 1947 ? 139.742 170.050 145.580 1.00 21.40  ? 1947 GLY A N     1 
ATOM   3276  C  CA    . GLY A 1 1947 ? 139.637 171.163 144.650 1.00 23.68  ? 1947 GLY A CA    1 
ATOM   3277  C  C     . GLY A 1 1947 ? 140.323 170.878 143.327 1.00 22.18  ? 1947 GLY A C     1 
ATOM   3278  O  O     . GLY A 1 1947 ? 139.768 171.136 142.256 1.00 22.94  ? 1947 GLY A O     1 
ATOM   3279  N  N     . LEU A 1 1948 ? 141.538 170.325 143.386 1.00 21.73  ? 1948 LEU A N     1 
ATOM   3280  C  CA    . LEU A 1 1948 ? 142.265 170.005 142.161 1.00 17.09  ? 1948 LEU A CA    1 
ATOM   3281  C  C     . LEU A 1 1948 ? 141.548 168.930 141.352 1.00 18.70  ? 1948 LEU A C     1 
ATOM   3282  O  O     . LEU A 1 1948 ? 141.494 169.004 140.119 1.00 19.72  ? 1948 LEU A O     1 
ATOM   3283  C  CB    . LEU A 1 1948 ? 143.690 169.563 142.493 1.00 16.61  ? 1948 LEU A CB    1 
ATOM   3284  C  CG    . LEU A 1 1948 ? 144.594 170.597 143.165 1.00 15.51  ? 1948 LEU A CG    1 
ATOM   3285  C  CD1   . LEU A 1 1948 ? 145.942 169.985 143.500 1.00 14.94  ? 1948 LEU A CD1   1 
ATOM   3286  C  CD2   . LEU A 1 1948 ? 144.762 171.822 142.282 1.00 13.45  ? 1948 LEU A CD2   1 
ATOM   3287  N  N     . CYS A 1 1949 ? 141.001 167.916 142.028 1.00 22.11  ? 1949 CYS A N     1 
ATOM   3288  C  CA    . CYS A 1 1949 ? 140.289 166.849 141.335 1.00 19.69  ? 1949 CYS A CA    1 
ATOM   3289  C  C     . CYS A 1 1949 ? 139.057 167.380 140.618 1.00 24.94  ? 1949 CYS A C     1 
ATOM   3290  O  O     . CYS A 1 1949 ? 138.806 167.030 139.459 1.00 30.82  ? 1949 CYS A O     1 
ATOM   3291  C  CB    . CYS A 1 1949 ? 139.884 165.756 142.326 1.00 22.40  ? 1949 CYS A CB    1 
ATOM   3292  S  SG    . CYS A 1 1949 ? 141.221 164.694 142.908 1.00 30.18  ? 1949 CYS A SG    1 
ATOM   3293  N  N     . GLN A 1 1950 ? 138.274 168.228 141.289 1.00 27.04  ? 1950 GLN A N     1 
ATOM   3294  C  CA    . GLN A 1 1950 ? 137.036 168.698 140.677 1.00 28.13  ? 1950 GLN A CA    1 
ATOM   3295  C  C     . GLN A 1 1950 ? 137.305 169.726 139.585 1.00 28.05  ? 1950 GLN A C     1 
ATOM   3296  O  O     . GLN A 1 1950 ? 136.640 169.717 138.543 1.00 30.01  ? 1950 GLN A O     1 
ATOM   3297  C  CB    . GLN A 1 1950 ? 136.099 169.265 141.742 1.00 34.24  ? 1950 GLN A CB    1 
ATOM   3298  C  CG    . GLN A 1 1950 ? 135.551 168.206 142.682 1.00 36.03  ? 1950 GLN A CG    1 
ATOM   3299  C  CD    . GLN A 1 1950 ? 134.105 168.449 143.060 1.00 59.16  ? 1950 GLN A CD    1 
ATOM   3300  O  OE1   . GLN A 1 1950 ? 133.190 167.978 142.385 1.00 57.99  ? 1950 GLN A OE1   1 
ATOM   3301  N  NE2   . GLN A 1 1950 ? 133.889 169.180 144.146 1.00 66.62  ? 1950 GLN A NE2   1 
ATOM   3302  N  N     . VAL A 1 1951 ? 138.272 170.621 139.799 1.00 27.41  ? 1951 VAL A N     1 
ATOM   3303  C  CA    . VAL A 1 1951 ? 138.588 171.613 138.775 1.00 24.29  ? 1951 VAL A CA    1 
ATOM   3304  C  C     . VAL A 1 1951 ? 139.263 170.956 137.578 1.00 24.28  ? 1951 VAL A C     1 
ATOM   3305  O  O     . VAL A 1 1951 ? 138.923 171.238 136.423 1.00 27.85  ? 1951 VAL A O     1 
ATOM   3306  C  CB    . VAL A 1 1951 ? 139.456 172.737 139.367 1.00 23.72  ? 1951 VAL A CB    1 
ATOM   3307  C  CG1   . VAL A 1 1951 ? 139.955 173.658 138.266 1.00 22.69  ? 1951 VAL A CG1   1 
ATOM   3308  C  CG2   . VAL A 1 1951 ? 138.668 173.522 140.393 1.00 34.46  ? 1951 VAL A CG2   1 
ATOM   3309  N  N     . GLY A 1 1952 ? 140.218 170.066 137.830 1.00 25.09  ? 1952 GLY A N     1 
ATOM   3310  C  CA    . GLY A 1 1952 ? 141.022 169.502 136.765 1.00 22.61  ? 1952 GLY A CA    1 
ATOM   3311  C  C     . GLY A 1 1952 ? 142.284 170.310 136.559 1.00 28.58  ? 1952 GLY A C     1 
ATOM   3312  O  O     . GLY A 1 1952 ? 142.647 170.647 135.428 1.00 33.74  ? 1952 GLY A O     1 
ATOM   3313  N  N     . ALA A 1 1953 ? 142.958 170.627 137.657 1.00 23.08  ? 1953 ALA A N     1 
ATOM   3314  C  CA    . ALA A 1 1953 ? 144.103 171.521 137.664 1.00 14.73  ? 1953 ALA A CA    1 
ATOM   3315  C  C     . ALA A 1 1953 ? 145.350 170.788 138.141 1.00 16.40  ? 1953 ALA A C     1 
ATOM   3316  O  O     . ALA A 1 1953 ? 145.293 169.660 138.636 1.00 21.00  ? 1953 ALA A O     1 
ATOM   3317  C  CB    . ALA A 1 1953 ? 143.823 172.738 138.551 1.00 13.63  ? 1953 ALA A CB    1 
ATOM   3318  N  N     . TRP A 1 1954 ? 146.490 171.454 137.984 1.00 12.67  ? 1954 TRP A N     1 
ATOM   3319  C  CA    . TRP A 1 1954 ? 147.782 170.917 138.389 1.00 9.35   ? 1954 TRP A CA    1 
ATOM   3320  C  C     . TRP A 1 1954 ? 148.172 171.493 139.742 1.00 10.72  ? 1954 TRP A C     1 
ATOM   3321  O  O     . TRP A 1 1954 ? 148.041 172.700 139.970 1.00 16.36  ? 1954 TRP A O     1 
ATOM   3322  C  CB    . TRP A 1 1954 ? 148.860 171.243 137.356 1.00 9.62   ? 1954 TRP A CB    1 
ATOM   3323  C  CG    . TRP A 1 1954 ? 148.840 170.356 136.154 1.00 9.95   ? 1954 TRP A CG    1 
ATOM   3324  C  CD1   . TRP A 1 1954 ? 147.764 169.700 135.637 1.00 14.66  ? 1954 TRP A CD1   1 
ATOM   3325  C  CD2   . TRP A 1 1954 ? 149.952 170.027 135.316 1.00 7.85   ? 1954 TRP A CD2   1 
ATOM   3326  N  NE1   . TRP A 1 1954 ? 148.136 168.982 134.527 1.00 15.93  ? 1954 TRP A NE1   1 
ATOM   3327  C  CE2   . TRP A 1 1954 ? 149.476 169.167 134.309 1.00 11.90  ? 1954 TRP A CE2   1 
ATOM   3328  C  CE3   . TRP A 1 1954 ? 151.306 170.377 135.320 1.00 8.00   ? 1954 TRP A CE3   1 
ATOM   3329  C  CZ2   . TRP A 1 1954 ? 150.304 168.652 133.316 1.00 11.65  ? 1954 TRP A CZ2   1 
ATOM   3330  C  CZ3   . TRP A 1 1954 ? 152.125 169.864 134.334 1.00 8.96   ? 1954 TRP A CZ3   1 
ATOM   3331  C  CH2   . TRP A 1 1954 ? 151.622 169.012 133.346 1.00 10.59  ? 1954 TRP A CH2   1 
ATOM   3332  N  N     . GLY A 1 1955 ? 148.648 170.631 140.635 1.00 9.02   ? 1955 GLY A N     1 
ATOM   3333  C  CA    . GLY A 1 1955 ? 149.099 171.077 141.936 1.00 8.50   ? 1955 GLY A CA    1 
ATOM   3334  C  C     . GLY A 1 1955 ? 150.593 170.932 142.122 1.00 10.18  ? 1955 GLY A C     1 
ATOM   3335  O  O     . GLY A 1 1955 ? 151.105 169.814 142.231 1.00 14.43  ? 1955 GLY A O     1 
ATOM   3336  N  N     . CYS A 1 1956 ? 151.307 172.054 142.156 1.00 7.97   ? 1956 CYS A N     1 
ATOM   3337  C  CA    . CYS A 1 1956 ? 152.752 172.065 142.371 1.00 8.71   ? 1956 CYS A CA    1 
ATOM   3338  C  C     . CYS A 1 1956 ? 153.001 172.384 143.840 1.00 12.18  ? 1956 CYS A C     1 
ATOM   3339  O  O     . CYS A 1 1956 ? 153.007 173.550 144.241 1.00 19.72  ? 1956 CYS A O     1 
ATOM   3340  C  CB    . CYS A 1 1956 ? 153.433 173.074 141.453 1.00 10.80  ? 1956 CYS A CB    1 
ATOM   3341  S  SG    . CYS A 1 1956 ? 155.237 173.014 141.493 1.00 27.01  ? 1956 CYS A SG    1 
ATOM   3342  N  N     . PHE A 1 1957 ? 153.206 171.343 144.642 1.00 10.54  ? 1957 PHE A N     1 
ATOM   3343  C  CA    . PHE A 1 1957 ? 153.406 171.495 146.081 1.00 11.65  ? 1957 PHE A CA    1 
ATOM   3344  C  C     . PHE A 1 1957 ? 154.893 171.684 146.346 1.00 15.29  ? 1957 PHE A C     1 
ATOM   3345  O  O     . PHE A 1 1957 ? 155.642 170.714 146.481 1.00 16.45  ? 1957 PHE A O     1 
ATOM   3346  C  CB    . PHE A 1 1957 ? 152.846 170.291 146.830 1.00 10.17  ? 1957 PHE A CB    1 
ATOM   3347  C  CG    . PHE A 1 1957 ? 151.368 170.099 146.643 1.00 12.43  ? 1957 PHE A CG    1 
ATOM   3348  C  CD1   . PHE A 1 1957 ? 150.880 169.322 145.607 1.00 11.91  ? 1957 PHE A CD1   1 
ATOM   3349  C  CD2   . PHE A 1 1957 ? 150.467 170.704 147.501 1.00 13.04  ? 1957 PHE A CD2   1 
ATOM   3350  C  CE1   . PHE A 1 1957 ? 149.521 169.150 145.433 1.00 11.84  ? 1957 PHE A CE1   1 
ATOM   3351  C  CE2   . PHE A 1 1957 ? 149.108 170.535 147.332 1.00 10.90  ? 1957 PHE A CE2   1 
ATOM   3352  C  CZ    . PHE A 1 1957 ? 148.635 169.757 146.297 1.00 10.10  ? 1957 PHE A CZ    1 
ATOM   3353  N  N     . ASP A 1 1958 ? 155.322 172.941 146.418 1.00 16.19  ? 1958 ASP A N     1 
ATOM   3354  C  CA    . ASP A 1 1958 ? 156.721 173.240 146.684 1.00 16.05  ? 1958 ASP A CA    1 
ATOM   3355  C  C     . ASP A 1 1958 ? 157.068 172.921 148.131 1.00 23.35  ? 1958 ASP A C     1 
ATOM   3356  O  O     . ASP A 1 1958 ? 156.248 173.102 149.037 1.00 27.28  ? 1958 ASP A O     1 
ATOM   3357  C  CB    . ASP A 1 1958 ? 157.018 174.708 146.390 1.00 20.05  ? 1958 ASP A CB    1 
ATOM   3358  C  CG    . ASP A 1 1958 ? 156.948 175.030 144.914 1.00 30.32  ? 1958 ASP A CG    1 
ATOM   3359  O  OD1   . ASP A 1 1958 ? 157.218 174.129 144.093 1.00 29.38  ? 1958 ASP A OD1   1 
ATOM   3360  O  OD2   . ASP A 1 1958 ? 156.628 176.188 144.576 1.00 33.71  ? 1958 ASP A OD2   1 
ATOM   3361  N  N     . GLU A 1 1959 ? 158.297 172.453 148.343 1.00 25.21  ? 1959 GLU A N     1 
ATOM   3362  C  CA    . GLU A 1 1959 ? 158.794 172.102 149.671 1.00 25.50  ? 1959 GLU A CA    1 
ATOM   3363  C  C     . GLU A 1 1959 ? 157.858 171.111 150.358 1.00 24.65  ? 1959 GLU A C     1 
ATOM   3364  O  O     . GLU A 1 1959 ? 157.478 171.271 151.519 1.00 25.72  ? 1959 GLU A O     1 
ATOM   3365  C  CB    . GLU A 1 1959 ? 158.999 173.354 150.524 1.00 28.10  ? 1959 GLU A CB    1 
ATOM   3366  C  CG    . GLU A 1 1959 ? 160.166 174.219 150.081 1.00 39.74  ? 1959 GLU A CG    1 
ATOM   3367  C  CD    . GLU A 1 1959 ? 161.389 173.401 149.711 1.00 52.28  ? 1959 GLU A CD    1 
ATOM   3368  O  OE1   . GLU A 1 1959 ? 161.915 172.684 150.588 1.00 45.20  ? 1959 GLU A OE1   1 
ATOM   3369  O  OE2   . GLU A 1 1959 ? 161.822 173.474 148.542 1.00 51.08  ? 1959 GLU A OE2   1 
ATOM   3370  N  N     . PHE A 1 1960 ? 157.483 170.070 149.614 1.00 19.67  ? 1960 PHE A N     1 
ATOM   3371  C  CA    . PHE A 1 1960 ? 156.556 169.063 150.114 1.00 17.09  ? 1960 PHE A CA    1 
ATOM   3372  C  C     . PHE A 1 1960 ? 157.146 168.234 151.248 1.00 21.49  ? 1960 PHE A C     1 
ATOM   3373  O  O     . PHE A 1 1960 ? 156.399 167.516 151.919 1.00 29.09  ? 1960 PHE A O     1 
ATOM   3374  C  CB    . PHE A 1 1960 ? 156.114 168.161 148.960 1.00 17.52  ? 1960 PHE A CB    1 
ATOM   3375  C  CG    . PHE A 1 1960 ? 154.966 167.253 149.295 1.00 16.39  ? 1960 PHE A CG    1 
ATOM   3376  C  CD1   . PHE A 1 1960 ? 153.665 167.727 149.275 1.00 17.09  ? 1960 PHE A CD1   1 
ATOM   3377  C  CD2   . PHE A 1 1960 ? 155.181 165.917 149.589 1.00 15.59  ? 1960 PHE A CD2   1 
ATOM   3378  C  CE1   . PHE A 1 1960 ? 152.604 166.896 149.571 1.00 19.27  ? 1960 PHE A CE1   1 
ATOM   3379  C  CE2   . PHE A 1 1960 ? 154.122 165.080 149.881 1.00 20.79  ? 1960 PHE A CE2   1 
ATOM   3380  C  CZ    . PHE A 1 1960 ? 152.833 165.570 149.874 1.00 23.57  ? 1960 PHE A CZ    1 
ATOM   3381  N  N     . ASN A 1 1961 ? 158.451 168.319 151.483 1.00 21.82  ? 1961 ASN A N     1 
ATOM   3382  C  CA    . ASN A 1 1961 ? 159.075 167.647 152.612 1.00 19.27  ? 1961 ASN A CA    1 
ATOM   3383  C  C     . ASN A 1 1961 ? 159.084 168.500 153.875 1.00 21.64  ? 1961 ASN A C     1 
ATOM   3384  O  O     . ASN A 1 1961 ? 159.649 168.075 154.887 1.00 25.71  ? 1961 ASN A O     1 
ATOM   3385  C  CB    . ASN A 1 1961 ? 160.502 167.220 152.251 1.00 18.55  ? 1961 ASN A CB    1 
ATOM   3386  C  CG    . ASN A 1 1961 ? 161.334 168.362 151.710 1.00 25.98  ? 1961 ASN A CG    1 
ATOM   3387  O  OD1   . ASN A 1 1961 ? 160.809 169.423 151.377 1.00 30.33  ? 1961 ASN A OD1   1 
ATOM   3388  N  ND2   . ASN A 1 1961 ? 162.639 168.144 151.606 1.00 26.14  ? 1961 ASN A ND2   1 
ATOM   3389  N  N     . ARG A 1 1962 ? 158.479 169.690 153.840 1.00 20.52  ? 1962 ARG A N     1 
ATOM   3390  C  CA    . ARG A 1 1962 ? 158.286 170.472 155.055 1.00 19.33  ? 1962 ARG A CA    1 
ATOM   3391  C  C     . ARG A 1 1962 ? 157.112 169.971 155.882 1.00 22.65  ? 1962 ARG A C     1 
ATOM   3392  O  O     . ARG A 1 1962 ? 156.985 170.356 157.050 1.00 29.12  ? 1962 ARG A O     1 
ATOM   3393  C  CB    . ARG A 1 1962 ? 158.092 171.952 154.713 1.00 16.30  ? 1962 ARG A CB    1 
ATOM   3394  C  CG    . ARG A 1 1962 ? 159.324 172.589 154.100 1.00 19.41  ? 1962 ARG A CG    1 
ATOM   3395  C  CD    . ARG A 1 1962 ? 159.227 174.103 153.971 1.00 21.37  ? 1962 ARG A CD    1 
ATOM   3396  N  NE    . ARG A 1 1962 ? 159.122 174.781 155.257 1.00 23.35  ? 1962 ARG A NE    1 
ATOM   3397  C  CZ    . ARG A 1 1962 ? 158.183 175.667 155.558 1.00 22.03  ? 1962 ARG A CZ    1 
ATOM   3398  N  NH1   . ARG A 1 1962 ? 157.273 176.034 154.672 1.00 24.13  ? 1962 ARG A NH1   1 
ATOM   3399  N  NH2   . ARG A 1 1962 ? 158.167 176.209 156.772 1.00 16.94  ? 1962 ARG A NH2   1 
ATOM   3400  N  N     . LEU A 1 1963 ? 156.258 169.130 155.307 1.00 19.28  ? 1963 LEU A N     1 
ATOM   3401  C  CA    . LEU A 1 1963 ? 155.210 168.474 156.071 1.00 19.75  ? 1963 LEU A CA    1 
ATOM   3402  C  C     . LEU A 1 1963 ? 155.816 167.488 157.064 1.00 26.49  ? 1963 LEU A C     1 
ATOM   3403  O  O     . LEU A 1 1963 ? 156.929 166.985 156.885 1.00 30.34  ? 1963 LEU A O     1 
ATOM   3404  C  CB    . LEU A 1 1963 ? 154.243 167.736 155.146 1.00 15.05  ? 1963 LEU A CB    1 
ATOM   3405  C  CG    . LEU A 1 1963 ? 153.226 168.532 154.330 1.00 18.05  ? 1963 LEU A CG    1 
ATOM   3406  C  CD1   . LEU A 1 1963 ? 153.830 168.996 153.028 1.00 21.10  ? 1963 LEU A CD1   1 
ATOM   3407  C  CD2   . LEU A 1 1963 ? 152.003 167.673 154.062 1.00 20.05  ? 1963 LEU A CD2   1 
ATOM   3408  N  N     . GLU A 1 1964 ? 155.068 167.218 158.128 1.00 27.98  ? 1964 GLU A N     1 
ATOM   3409  C  CA    . GLU A 1 1964 ? 155.476 166.193 159.074 1.00 26.39  ? 1964 GLU A CA    1 
ATOM   3410  C  C     . GLU A 1 1964 ? 155.428 164.821 158.411 1.00 24.47  ? 1964 GLU A C     1 
ATOM   3411  O  O     . GLU A 1 1964 ? 154.640 164.578 157.493 1.00 25.54  ? 1964 GLU A O     1 
ATOM   3412  C  CB    . GLU A 1 1964 ? 154.577 166.218 160.309 1.00 32.94  ? 1964 GLU A CB    1 
ATOM   3413  C  CG    . GLU A 1 1964 ? 154.185 167.615 160.757 1.00 41.60  ? 1964 GLU A CG    1 
ATOM   3414  C  CD    . GLU A 1 1964 ? 153.861 167.683 162.234 1.00 58.54  ? 1964 GLU A CD    1 
ATOM   3415  O  OE1   . GLU A 1 1964 ? 154.080 168.751 162.844 1.00 50.26  ? 1964 GLU A OE1   1 
ATOM   3416  O  OE2   . GLU A 1 1964 ? 153.387 166.669 162.787 1.00 58.76  ? 1964 GLU A OE2   1 
ATOM   3417  N  N     . GLU A 1 1965 ? 156.292 163.920 158.884 1.00 21.65  ? 1965 GLU A N     1 
ATOM   3418  C  CA    . GLU A 1 1965 ? 156.370 162.588 158.292 1.00 21.37  ? 1965 GLU A CA    1 
ATOM   3419  C  C     . GLU A 1 1965 ? 155.046 161.846 158.424 1.00 21.36  ? 1965 GLU A C     1 
ATOM   3420  O  O     . GLU A 1 1965 ? 154.629 161.133 157.503 1.00 26.25  ? 1965 GLU A O     1 
ATOM   3421  C  CB    . GLU A 1 1965 ? 157.502 161.792 158.942 1.00 22.12  ? 1965 GLU A CB    1 
ATOM   3422  C  CG    . GLU A 1 1965 ? 158.887 162.334 158.639 1.00 30.67  ? 1965 GLU A CG    1 
ATOM   3423  C  CD    . GLU A 1 1965 ? 159.979 161.586 159.375 1.00 40.56  ? 1965 GLU A CD    1 
ATOM   3424  O  OE1   . GLU A 1 1965 ? 159.651 160.664 160.151 1.00 47.68  ? 1965 GLU A OE1   1 
ATOM   3425  O  OE2   . GLU A 1 1965 ? 161.166 161.921 159.180 1.00 37.20  ? 1965 GLU A OE2   1 
ATOM   3426  N  N     . ARG A 1 1966 ? 154.372 162.001 159.565 1.00 16.40  ? 1966 ARG A N     1 
ATOM   3427  C  CA    . ARG A 1 1966 ? 153.058 161.394 159.736 1.00 17.50  ? 1966 ARG A CA    1 
ATOM   3428  C  C     . ARG A 1 1966 ? 152.052 161.971 158.744 1.00 22.65  ? 1966 ARG A C     1 
ATOM   3429  O  O     . ARG A 1 1966 ? 151.242 161.233 158.167 1.00 24.98  ? 1966 ARG A O     1 
ATOM   3430  C  CB    . ARG A 1 1966 ? 152.594 161.572 161.184 1.00 21.81  ? 1966 ARG A CB    1 
ATOM   3431  C  CG    . ARG A 1 1966 ? 152.399 163.013 161.634 1.00 33.65  ? 1966 ARG A CG    1 
ATOM   3432  C  CD    . ARG A 1 1966 ? 152.500 163.133 163.149 1.00 43.36  ? 1966 ARG A CD    1 
ATOM   3433  N  NE    . ARG A 1 1966 ? 151.863 164.340 163.664 1.00 51.95  ? 1966 ARG A NE    1 
ATOM   3434  C  CZ    . ARG A 1 1966 ? 150.552 164.531 163.730 1.00 53.96  ? 1966 ARG A CZ    1 
ATOM   3435  N  NH1   . ARG A 1 1966 ? 149.697 163.588 163.371 1.00 44.84  ? 1966 ARG A NH1   1 
ATOM   3436  N  NH2   . ARG A 1 1966 ? 150.087 165.692 164.182 1.00 57.68  ? 1966 ARG A NH2   1 
ATOM   3437  N  N     . MET A 1 1967 ? 152.107 163.284 158.509 1.00 23.45  ? 1967 MET A N     1 
ATOM   3438  C  CA    . MET A 1 1967 ? 151.241 163.892 157.504 1.00 17.85  ? 1967 MET A CA    1 
ATOM   3439  C  C     . MET A 1 1967 ? 151.602 163.424 156.101 1.00 18.66  ? 1967 MET A C     1 
ATOM   3440  O  O     . MET A 1 1967 ? 150.717 163.243 155.260 1.00 23.60  ? 1967 MET A O     1 
ATOM   3441  C  CB    . MET A 1 1967 ? 151.304 165.414 157.602 1.00 21.70  ? 1967 MET A CB    1 
ATOM   3442  C  CG    . MET A 1 1967 ? 150.738 165.978 158.895 1.00 33.41  ? 1967 MET A CG    1 
ATOM   3443  S  SD    . MET A 1 1967 ? 148.984 165.600 159.099 1.00 44.15  ? 1967 MET A SD    1 
ATOM   3444  C  CE    . MET A 1 1967 ? 149.034 164.256 160.277 1.00 28.90  ? 1967 MET A CE    1 
ATOM   3445  N  N     . LEU A 1 1968 ? 152.893 163.226 155.826 1.00 17.71  ? 1968 LEU A N     1 
ATOM   3446  C  CA    . LEU A 1 1968 ? 153.296 162.691 154.528 1.00 15.45  ? 1968 LEU A CA    1 
ATOM   3447  C  C     . LEU A 1 1968 ? 152.710 161.301 154.311 1.00 17.31  ? 1968 LEU A C     1 
ATOM   3448  O  O     . LEU A 1 1968 ? 152.152 161.002 153.246 1.00 21.13  ? 1968 LEU A O     1 
ATOM   3449  C  CB    . LEU A 1 1968 ? 154.821 162.651 154.430 1.00 15.13  ? 1968 LEU A CB    1 
ATOM   3450  C  CG    . LEU A 1 1968 ? 155.561 163.989 154.410 1.00 15.24  ? 1968 LEU A CG    1 
ATOM   3451  C  CD1   . LEU A 1 1968 ? 157.051 163.783 154.624 1.00 17.43  ? 1968 LEU A CD1   1 
ATOM   3452  C  CD2   . LEU A 1 1968 ? 155.303 164.719 153.111 1.00 14.16  ? 1968 LEU A CD2   1 
ATOM   3453  N  N     . SER A 1 1969 ? 152.815 160.441 155.327 1.00 17.70  ? 1969 SER A N     1 
ATOM   3454  C  CA    . SER A 1 1969 ? 152.254 159.099 155.227 1.00 18.42  ? 1969 SER A CA    1 
ATOM   3455  C  C     . SER A 1 1969 ? 150.745 159.146 155.033 1.00 17.53  ? 1969 SER A C     1 
ATOM   3456  O  O     . SER A 1 1969 ? 150.195 158.411 154.206 1.00 20.99  ? 1969 SER A O     1 
ATOM   3457  C  CB    . SER A 1 1969 ? 152.612 158.288 156.472 1.00 18.01  ? 1969 SER A CB    1 
ATOM   3458  O  OG    . SER A 1 1969 ? 152.134 156.959 156.372 1.00 26.66  ? 1969 SER A OG    1 
ATOM   3459  N  N     . ALA A 1 1970 ? 150.058 160.016 155.778 1.00 16.58  ? 1970 ALA A N     1 
ATOM   3460  C  CA    . ALA A 1 1970 ? 148.608 160.121 155.644 1.00 17.95  ? 1970 ALA A CA    1 
ATOM   3461  C  C     . ALA A 1 1970 ? 148.206 160.619 154.259 1.00 20.59  ? 1970 ALA A C     1 
ATOM   3462  O  O     . ALA A 1 1970 ? 147.237 160.123 153.673 1.00 23.63  ? 1970 ALA A O     1 
ATOM   3463  C  CB    . ALA A 1 1970 ? 148.050 161.039 156.730 1.00 20.32  ? 1970 ALA A CB    1 
ATOM   3464  N  N     . VAL A 1 1971 ? 148.936 161.599 153.721 1.00 21.14  ? 1971 VAL A N     1 
ATOM   3465  C  CA    . VAL A 1 1971 ? 148.615 162.159 152.411 1.00 16.61  ? 1971 VAL A CA    1 
ATOM   3466  C  C     . VAL A 1 1971 ? 148.905 161.153 151.303 1.00 18.60  ? 1971 VAL A C     1 
ATOM   3467  O  O     . VAL A 1 1971 ? 148.271 161.190 150.235 1.00 23.60  ? 1971 VAL A O     1 
ATOM   3468  C  CB    . VAL A 1 1971 ? 149.385 163.482 152.219 1.00 14.65  ? 1971 VAL A CB    1 
ATOM   3469  C  CG1   . VAL A 1 1971 ? 149.449 163.889 150.755 1.00 18.18  ? 1971 VAL A CG1   1 
ATOM   3470  C  CG2   . VAL A 1 1971 ? 148.746 164.585 153.049 1.00 19.36  ? 1971 VAL A CG2   1 
ATOM   3471  N  N     . SER A 1 1972 ? 149.865 160.248 151.528 1.00 18.02  ? 1972 SER A N     1 
ATOM   3472  C  CA    . SER A 1 1972 ? 150.145 159.208 150.542 1.00 16.57  ? 1972 SER A CA    1 
ATOM   3473  C  C     . SER A 1 1972 ? 148.900 158.397 150.206 1.00 18.54  ? 1972 SER A C     1 
ATOM   3474  O  O     . SER A 1 1972 ? 148.725 157.983 149.055 1.00 24.72  ? 1972 SER A O     1 
ATOM   3475  C  CB    . SER A 1 1972 ? 151.253 158.286 151.049 1.00 16.33  ? 1972 SER A CB    1 
ATOM   3476  O  OG    . SER A 1 1972 ? 150.828 157.553 152.184 1.00 22.00  ? 1972 SER A OG    1 
ATOM   3477  N  N     . GLN A 1 1973 ? 148.021 158.173 151.186 1.00 18.90  ? 1973 GLN A N     1 
ATOM   3478  C  CA    . GLN A 1 1973 ? 146.789 157.433 150.928 1.00 21.22  ? 1973 GLN A CA    1 
ATOM   3479  C  C     . GLN A 1 1973 ? 145.908 158.162 149.919 1.00 20.60  ? 1973 GLN A C     1 
ATOM   3480  O  O     . GLN A 1 1973 ? 145.422 157.562 148.952 1.00 25.30  ? 1973 GLN A O     1 
ATOM   3481  C  CB    . GLN A 1 1973 ? 146.032 157.212 152.238 1.00 26.85  ? 1973 GLN A CB    1 
ATOM   3482  C  CG    . GLN A 1 1973 ? 145.219 155.931 152.285 1.00 34.44  ? 1973 GLN A CG    1 
ATOM   3483  C  CD    . GLN A 1 1973 ? 144.581 155.700 153.640 1.00 43.44  ? 1973 GLN A CD    1 
ATOM   3484  O  OE1   . GLN A 1 1973 ? 144.781 156.478 154.574 1.00 39.93  ? 1973 GLN A OE1   1 
ATOM   3485  N  NE2   . GLN A 1 1973 ? 143.805 154.629 153.755 1.00 41.08  ? 1973 GLN A NE2   1 
ATOM   3486  N  N     . GLN A 1 1974 ? 145.689 159.462 150.133 1.00 19.16  ? 1974 GLN A N     1 
ATOM   3487  C  CA    . GLN A 1 1974 ? 144.863 160.237 149.212 1.00 17.83  ? 1974 GLN A CA    1 
ATOM   3488  C  C     . GLN A 1 1974 ? 145.491 160.294 147.828 1.00 20.94  ? 1974 GLN A C     1 
ATOM   3489  O  O     . GLN A 1 1974 ? 144.789 160.194 146.814 1.00 25.06  ? 1974 GLN A O     1 
ATOM   3490  C  CB    . GLN A 1 1974 ? 144.647 161.647 149.759 1.00 14.68  ? 1974 GLN A CB    1 
ATOM   3491  C  CG    . GLN A 1 1974 ? 144.283 161.691 151.229 1.00 21.33  ? 1974 GLN A CG    1 
ATOM   3492  C  CD    . GLN A 1 1974 ? 144.196 163.105 151.764 1.00 20.69  ? 1974 GLN A CD    1 
ATOM   3493  O  OE1   . GLN A 1 1974 ? 143.177 163.507 152.324 1.00 24.99  ? 1974 GLN A OE1   1 
ATOM   3494  N  NE2   . GLN A 1 1974 ? 145.269 163.868 151.595 1.00 19.50  ? 1974 GLN A NE2   1 
ATOM   3495  N  N     . VAL A 1 1975 ? 146.815 160.456 147.765 1.00 20.40  ? 1975 VAL A N     1 
ATOM   3496  C  CA    . VAL A 1 1975 ? 147.491 160.486 146.470 1.00 15.59  ? 1975 VAL A CA    1 
ATOM   3497  C  C     . VAL A 1 1975 ? 147.306 159.158 145.746 1.00 17.96  ? 1975 VAL A C     1 
ATOM   3498  O  O     . VAL A 1 1975 ? 147.056 159.123 144.534 1.00 20.11  ? 1975 VAL A O     1 
ATOM   3499  C  CB    . VAL A 1 1975 ? 148.980 160.836 146.646 1.00 12.24  ? 1975 VAL A CB    1 
ATOM   3500  C  CG1   . VAL A 1 1975 ? 149.684 160.842 145.301 1.00 16.09  ? 1975 VAL A CG1   1 
ATOM   3501  C  CG2   . VAL A 1 1975 ? 149.128 162.185 147.321 1.00 10.70  ? 1975 VAL A CG2   1 
ATOM   3502  N  N     . GLN A 1 1976 ? 147.419 158.046 146.477 1.00 19.82  ? 1976 GLN A N     1 
ATOM   3503  C  CA    . GLN A 1 1976 ? 147.244 156.733 145.866 1.00 22.30  ? 1976 GLN A CA    1 
ATOM   3504  C  C     . GLN A 1 1976 ? 145.821 156.539 145.357 1.00 24.81  ? 1976 GLN A C     1 
ATOM   3505  O  O     . GLN A 1 1976 ? 145.617 155.997 144.265 1.00 29.79  ? 1976 GLN A O     1 
ATOM   3506  C  CB    . GLN A 1 1976 ? 147.611 155.640 146.869 1.00 23.66  ? 1976 GLN A CB    1 
ATOM   3507  C  CG    . GLN A 1 1976 ? 147.392 154.227 146.362 1.00 33.23  ? 1976 GLN A CG    1 
ATOM   3508  C  CD    . GLN A 1 1976 ? 148.275 153.217 147.065 1.00 41.57  ? 1976 GLN A CD    1 
ATOM   3509  O  OE1   . GLN A 1 1976 ? 149.219 153.583 147.765 1.00 40.67  ? 1976 GLN A OE1   1 
ATOM   3510  N  NE2   . GLN A 1 1976 ? 147.974 151.937 146.881 1.00 44.15  ? 1976 GLN A NE2   1 
ATOM   3511  N  N     . CYS A 1 1977 ? 144.822 156.970 146.133 1.00 21.94  ? 1977 CYS A N     1 
ATOM   3512  C  CA    . CYS A 1 1977 ? 143.439 156.853 145.670 1.00 22.71  ? 1977 CYS A CA    1 
ATOM   3513  C  C     . CYS A 1 1977 ? 143.195 157.696 144.423 1.00 24.52  ? 1977 CYS A C     1 
ATOM   3514  O  O     . CYS A 1 1977 ? 142.532 157.245 143.479 1.00 29.22  ? 1977 CYS A O     1 
ATOM   3515  C  CB    . CYS A 1 1977 ? 142.458 157.242 146.778 1.00 28.64  ? 1977 CYS A CB    1 
ATOM   3516  S  SG    . CYS A 1 1977 ? 142.714 156.414 148.361 1.00 56.50  ? 1977 CYS A SG    1 
ATOM   3517  N  N     . ILE A 1 1978 ? 143.724 158.922 144.396 1.00 26.27  ? 1978 ILE A N     1 
ATOM   3518  C  CA    . ILE A 1 1978 ? 143.551 159.775 143.222 1.00 23.81  ? 1978 ILE A CA    1 
ATOM   3519  C  C     . ILE A 1 1978 ? 144.219 159.152 142.003 1.00 22.10  ? 1978 ILE A C     1 
ATOM   3520  O  O     . ILE A 1 1978 ? 143.662 159.161 140.897 1.00 26.18  ? 1978 ILE A O     1 
ATOM   3521  C  CB    . ILE A 1 1978 ? 144.089 161.190 143.501 1.00 18.47  ? 1978 ILE A CB    1 
ATOM   3522  C  CG1   . ILE A 1 1978 ? 143.274 161.865 144.604 1.00 17.18  ? 1978 ILE A CG1   1 
ATOM   3523  C  CG2   . ILE A 1 1978 ? 144.069 162.023 142.237 1.00 15.68  ? 1978 ILE A CG2   1 
ATOM   3524  C  CD1   . ILE A 1 1978 ? 143.880 163.154 145.102 1.00 14.47  ? 1978 ILE A CD1   1 
ATOM   3525  N  N     . GLN A 1 1979 ? 145.424 158.606 142.179 1.00 20.00  ? 1979 GLN A N     1 
ATOM   3526  C  CA    . GLN A 1 1979 ? 146.123 157.991 141.056 1.00 17.17  ? 1979 GLN A CA    1 
ATOM   3527  C  C     . GLN A 1 1979 ? 145.401 156.739 140.570 1.00 27.70  ? 1979 GLN A C     1 
ATOM   3528  O  O     . GLN A 1 1979 ? 145.365 156.470 139.365 1.00 34.05  ? 1979 GLN A O     1 
ATOM   3529  C  CB    . GLN A 1 1979 ? 147.564 157.675 141.448 1.00 17.15  ? 1979 GLN A CB    1 
ATOM   3530  C  CG    . GLN A 1 1979 ? 148.452 158.905 141.522 1.00 16.45  ? 1979 GLN A CG    1 
ATOM   3531  C  CD    . GLN A 1 1979 ? 149.862 158.583 141.964 1.00 18.86  ? 1979 GLN A CD    1 
ATOM   3532  O  OE1   . GLN A 1 1979 ? 150.227 157.417 142.107 1.00 23.41  ? 1979 GLN A OE1   1 
ATOM   3533  N  NE2   . GLN A 1 1979 ? 150.664 159.618 142.185 1.00 13.01  ? 1979 GLN A NE2   1 
ATOM   3534  N  N     . GLU A 1 1980 ? 144.821 155.962 141.488 1.00 31.58  ? 1980 GLU A N     1 
ATOM   3535  C  CA    . GLU A 1 1980 ? 144.032 154.802 141.080 1.00 31.20  ? 1980 GLU A CA    1 
ATOM   3536  C  C     . GLU A 1 1980 ? 142.797 155.227 140.296 1.00 31.37  ? 1980 GLU A C     1 
ATOM   3537  O  O     . GLU A 1 1980 ? 142.427 154.582 139.306 1.00 36.49  ? 1980 GLU A O     1 
ATOM   3538  C  CB    . GLU A 1 1980 ? 143.634 153.978 142.304 1.00 34.88  ? 1980 GLU A CB    1 
ATOM   3539  C  CG    . GLU A 1 1980 ? 144.714 153.025 142.788 1.00 43.58  ? 1980 GLU A CG    1 
ATOM   3540  C  CD    . GLU A 1 1980 ? 144.415 152.451 144.159 1.00 58.15  ? 1980 GLU A CD    1 
ATOM   3541  O  OE1   . GLU A 1 1980 ? 143.408 152.865 144.772 1.00 52.31  ? 1980 GLU A OE1   1 
ATOM   3542  O  OE2   . GLU A 1 1980 ? 145.186 151.586 144.624 1.00 63.44  ? 1980 GLU A OE2   1 
ATOM   3543  N  N     . ALA A 1 1981 ? 142.141 156.306 140.729 1.00 31.26  ? 1981 ALA A N     1 
ATOM   3544  C  CA    . ALA A 1 1981 ? 141.000 156.823 139.979 1.00 34.99  ? 1981 ALA A CA    1 
ATOM   3545  C  C     . ALA A 1 1981 ? 141.419 157.279 138.587 1.00 37.98  ? 1981 ALA A C     1 
ATOM   3546  O  O     . ALA A 1 1981 ? 140.721 157.017 137.602 1.00 49.77  ? 1981 ALA A O     1 
ATOM   3547  C  CB    . ALA A 1 1981 ? 140.342 157.969 140.746 1.00 35.06  ? 1981 ALA A CB    1 
ATOM   3548  N  N     . LEU A 1 1982 ? 142.566 157.953 138.484 1.00 35.32  ? 1982 LEU A N     1 
ATOM   3549  C  CA    . LEU A 1 1982 ? 143.064 158.368 137.175 1.00 30.73  ? 1982 LEU A CA    1 
ATOM   3550  C  C     . LEU A 1 1982 ? 143.370 157.162 136.294 1.00 39.21  ? 1982 LEU A C     1 
ATOM   3551  O  O     . LEU A 1 1982 ? 143.077 157.168 135.092 1.00 47.32  ? 1982 LEU A O     1 
ATOM   3552  C  CB    . LEU A 1 1982 ? 144.309 159.240 137.340 1.00 26.71  ? 1982 LEU A CB    1 
ATOM   3553  C  CG    . LEU A 1 1982 ? 144.080 160.692 137.760 1.00 23.11  ? 1982 LEU A CG    1 
ATOM   3554  C  CD1   . LEU A 1 1982 ? 145.408 161.407 137.947 1.00 22.54  ? 1982 LEU A CD1   1 
ATOM   3555  C  CD2   . LEU A 1 1982 ? 143.219 161.414 136.737 1.00 27.22  ? 1982 LEU A CD2   1 
ATOM   3556  N  N     . ARG A 1 1983 ? 143.968 156.119 136.875 1.00 41.18  ? 1983 ARG A N     1 
ATOM   3557  C  CA    . ARG A 1 1983 ? 144.294 154.921 136.108 1.00 42.49  ? 1983 ARG A CA    1 
ATOM   3558  C  C     . ARG A 1 1983 ? 143.036 154.229 135.600 1.00 49.26  ? 1983 ARG A C     1 
ATOM   3559  O  O     . ARG A 1 1983 ? 142.983 153.791 134.445 1.00 54.69  ? 1983 ARG A O     1 
ATOM   3560  C  CB    . ARG A 1 1983 ? 145.126 153.966 136.962 1.00 37.49  ? 1983 ARG A CB    1 
ATOM   3561  C  CG    . ARG A 1 1983 ? 146.624 154.107 136.765 1.00 32.26  ? 1983 ARG A CG    1 
ATOM   3562  C  CD    . ARG A 1 1983 ? 147.378 152.967 137.428 1.00 38.14  ? 1983 ARG A CD    1 
ATOM   3563  N  NE    . ARG A 1 1983 ? 147.879 153.335 138.747 1.00 35.93  ? 1983 ARG A NE    1 
ATOM   3564  C  CZ    . ARG A 1 1983 ? 148.895 154.160 138.965 1.00 33.88  ? 1983 ARG A CZ    1 
ATOM   3565  N  NH1   . ARG A 1 1983 ? 149.561 154.717 137.967 1.00 27.65  ? 1983 ARG A NH1   1 
ATOM   3566  N  NH2   . ARG A 1 1983 ? 149.255 154.429 140.216 1.00 33.03  ? 1983 ARG A NH2   1 
ATOM   3567  N  N     . GLU A 1 1984 ? 142.010 154.117 136.448 1.00 52.50  ? 1984 GLU A N     1 
ATOM   3568  C  CA    . GLU A 1 1984 ? 140.760 153.512 135.996 1.00 56.67  ? 1984 GLU A CA    1 
ATOM   3569  C  C     . GLU A 1 1984 ? 140.042 154.408 134.993 1.00 57.70  ? 1984 GLU A C     1 
ATOM   3570  O  O     . GLU A 1 1984 ? 139.262 153.915 134.171 1.00 70.78  ? 1984 GLU A O     1 
ATOM   3571  C  CB    . GLU A 1 1984 ? 139.858 153.194 137.191 1.00 56.67  ? 1984 GLU A CB    1 
ATOM   3572  C  CG    . GLU A 1 1984 ? 139.049 154.365 137.719 1.00 58.06  ? 1984 GLU A CG    1 
ATOM   3573  C  CD    . GLU A 1 1984 ? 137.948 153.932 138.667 1.00 67.12  ? 1984 GLU A CD    1 
ATOM   3574  O  OE1   . GLU A 1 1984 ? 138.264 153.313 139.704 1.00 63.73  ? 1984 GLU A OE1   1 
ATOM   3575  O  OE2   . GLU A 1 1984 ? 136.766 154.209 138.375 1.00 70.68  ? 1984 GLU A OE2   1 
ATOM   3576  N  N     . HIS A 1 1985 ? 140.290 155.719 135.046 1.00 55.76  ? 1985 HIS A N     1 
ATOM   3577  C  CA    . HIS A 1 1985 ? 139.792 156.614 134.008 1.00 63.07  ? 1985 HIS A CA    1 
ATOM   3578  C  C     . HIS A 1 1985 ? 140.495 156.376 132.679 1.00 69.29  ? 1985 HIS A C     1 
ATOM   3579  O  O     . HIS A 1 1985 ? 139.864 156.465 131.619 1.00 70.03  ? 1985 HIS A O     1 
ATOM   3580  C  CB    . HIS A 1 1985 ? 139.970 158.068 134.445 1.00 61.79  ? 1985 HIS A CB    1 
ATOM   3581  C  CG    . HIS A 1 1985 ? 139.367 159.063 133.504 1.00 64.13  ? 1985 HIS A CG    1 
ATOM   3582  N  ND1   . HIS A 1 1985 ? 138.093 159.563 133.663 1.00 73.44  ? 1985 HIS A ND1   1 
ATOM   3583  C  CD2   . HIS A 1 1985 ? 139.866 159.652 132.391 1.00 65.42  ? 1985 HIS A CD2   1 
ATOM   3584  C  CE1   . HIS A 1 1985 ? 137.832 160.417 132.690 1.00 72.46  ? 1985 HIS A CE1   1 
ATOM   3585  N  NE2   . HIS A 1 1985 ? 138.891 160.488 131.904 1.00 70.55  ? 1985 HIS A NE2   1 
ATOM   3586  N  N     . SER A 1 1986 ? 141.794 156.077 132.713 1.00 73.22  ? 1986 SER A N     1 
ATOM   3587  C  CA    . SER A 1 1986 ? 142.577 155.902 131.496 1.00 71.70  ? 1986 SER A CA    1 
ATOM   3588  C  C     . SER A 1 1986 ? 142.294 154.589 130.777 1.00 77.75  ? 1986 SER A C     1 
ATOM   3589  O  O     . SER A 1 1986 ? 142.714 154.435 129.625 1.00 79.27  ? 1986 SER A O     1 
ATOM   3590  C  CB    . SER A 1 1986 ? 144.071 155.989 131.818 1.00 63.66  ? 1986 SER A CB    1 
ATOM   3591  O  OG    . SER A 1 1986 ? 144.581 154.728 132.211 1.00 70.00  ? 1986 SER A OG    1 
ATOM   3592  N  N     . ASN A 1 1987 ? 141.609 153.648 131.416 1.00 82.15  ? 1987 ASN A N     1 
ATOM   3593  C  CA    . ASN A 1 1987 ? 141.329 152.367 130.775 1.00 90.20  ? 1987 ASN A CA    1 
ATOM   3594  C  C     . ASN A 1 1987 ? 140.371 152.565 129.604 1.00 100.75 ? 1987 ASN A C     1 
ATOM   3595  O  O     . ASN A 1 1987 ? 139.375 153.286 129.739 1.00 97.23  ? 1987 ASN A O     1 
ATOM   3596  C  CB    . ASN A 1 1987 ? 140.739 151.382 131.782 1.00 93.90  ? 1987 ASN A CB    1 
ATOM   3597  C  CG    . ASN A 1 1987 ? 141.732 150.984 132.857 1.00 89.16  ? 1987 ASN A CG    1 
ATOM   3598  O  OD1   . ASN A 1 1987 ? 142.944 151.070 132.661 1.00 84.87  ? 1987 ASN A OD1   1 
ATOM   3599  N  ND2   . ASN A 1 1987 ? 141.221 150.542 134.000 1.00 85.88  ? 1987 ASN A ND2   1 
ATOM   3600  N  N     . PRO A 1 1988 ? 140.636 151.955 128.446 1.00 111.67 ? 1988 PRO A N     1 
ATOM   3601  C  CA    . PRO A 1 1988 ? 139.733 152.135 127.297 1.00 110.95 ? 1988 PRO A CA    1 
ATOM   3602  C  C     . PRO A 1 1988 ? 138.342 151.568 127.514 1.00 115.61 ? 1988 PRO A C     1 
ATOM   3603  O  O     . PRO A 1 1988 ? 137.407 151.985 126.818 1.00 109.79 ? 1988 PRO A O     1 
ATOM   3604  C  CB    . PRO A 1 1988 ? 140.463 151.406 126.160 1.00 106.03 ? 1988 PRO A CB    1 
ATOM   3605  C  CG    . PRO A 1 1988 ? 141.340 150.414 126.848 1.00 105.35 ? 1988 PRO A CG    1 
ATOM   3606  C  CD    . PRO A 1 1988 ? 141.764 151.060 128.135 1.00 104.57 ? 1988 PRO A CD    1 
ATOM   3607  N  N     . ASN A 1 1989 ? 138.172 150.630 128.449 1.00 121.79 ? 1989 ASN A N     1 
ATOM   3608  C  CA    . ASN A 1 1989 ? 136.849 150.066 128.698 1.00 119.34 ? 1989 ASN A CA    1 
ATOM   3609  C  C     . ASN A 1 1989 ? 135.889 151.109 129.255 1.00 119.71 ? 1989 ASN A C     1 
ATOM   3610  O  O     . ASN A 1 1989 ? 134.681 151.034 129.001 1.00 115.55 ? 1989 ASN A O     1 
ATOM   3611  C  CB    . ASN A 1 1989 ? 136.955 148.876 129.652 1.00 113.86 ? 1989 ASN A CB    1 
ATOM   3612  C  CG    . ASN A 1 1989 ? 137.939 149.119 130.779 1.00 110.37 ? 1989 ASN A CG    1 
ATOM   3613  O  OD1   . ASN A 1 1989 ? 137.748 150.011 131.605 1.00 109.52 ? 1989 ASN A OD1   1 
ATOM   3614  N  ND2   . ASN A 1 1989 ? 139.001 148.323 130.818 1.00 104.01 ? 1989 ASN A ND2   1 
ATOM   3615  N  N     . TYR A 1 1990 ? 136.399 152.076 130.012 1.00 119.06 ? 1990 TYR A N     1 
ATOM   3616  C  CA    . TYR A 1 1990 ? 135.556 153.141 130.537 1.00 122.30 ? 1990 TYR A CA    1 
ATOM   3617  C  C     . TYR A 1 1990 ? 135.078 154.050 129.412 1.00 124.90 ? 1990 TYR A C     1 
ATOM   3618  O  O     . TYR A 1 1990 ? 135.823 154.357 128.478 1.00 123.24 ? 1990 TYR A O     1 
ATOM   3619  C  CB    . TYR A 1 1990 ? 136.319 153.954 131.584 1.00 115.50 ? 1990 TYR A CB    1 
ATOM   3620  C  CG    . TYR A 1 1990 ? 135.689 155.291 131.906 1.00 114.12 ? 1990 TYR A CG    1 
ATOM   3621  C  CD1   . TYR A 1 1990 ? 134.565 155.373 132.718 1.00 116.02 ? 1990 TYR A CD1   1 
ATOM   3622  C  CD2   . TYR A 1 1990 ? 136.219 156.472 131.401 1.00 104.28 ? 1990 TYR A CD2   1 
ATOM   3623  C  CE1   . TYR A 1 1990 ? 133.986 156.593 133.016 1.00 117.42 ? 1990 TYR A CE1   1 
ATOM   3624  C  CE2   . TYR A 1 1990 ? 135.646 157.696 131.693 1.00 104.79 ? 1990 TYR A CE2   1 
ATOM   3625  C  CZ    . TYR A 1 1990 ? 134.531 157.750 132.501 1.00 114.31 ? 1990 TYR A CZ    1 
ATOM   3626  O  OH    . TYR A 1 1990 ? 133.957 158.966 132.795 1.00 108.57 ? 1990 TYR A OH    1 
ATOM   3627  N  N     . ASP A 1 1991 ? 133.823 154.481 129.508 1.00 129.38 ? 1991 ASP A N     1 
ATOM   3628  C  CA    . ASP A 1 1991 ? 133.229 155.410 128.559 1.00 131.94 ? 1991 ASP A CA    1 
ATOM   3629  C  C     . ASP A 1 1991 ? 132.686 156.616 129.311 1.00 131.93 ? 1991 ASP A C     1 
ATOM   3630  O  O     . ASP A 1 1991 ? 132.170 156.483 130.425 1.00 131.61 ? 1991 ASP A O     1 
ATOM   3631  C  CB    . ASP A 1 1991 ? 132.111 154.743 127.749 1.00 136.91 ? 1991 ASP A CB    1 
ATOM   3632  C  CG    . ASP A 1 1991 ? 131.104 154.026 128.626 1.00 138.22 ? 1991 ASP A CG    1 
ATOM   3633  O  OD1   . ASP A 1 1991 ? 131.515 153.130 129.393 1.00 134.64 ? 1991 ASP A OD1   1 
ATOM   3634  O  OD2   . ASP A 1 1991 ? 129.903 154.358 128.548 1.00 140.75 ? 1991 ASP A OD2   1 
ATOM   3635  N  N     . LYS A 1 1992 ? 132.807 157.796 128.696 1.00 130.96 ? 1992 LYS A N     1 
ATOM   3636  C  CA    . LYS A 1 1992 ? 132.371 159.022 129.356 1.00 132.99 ? 1992 LYS A CA    1 
ATOM   3637  C  C     . LYS A 1 1992 ? 130.871 159.020 129.620 1.00 137.41 ? 1992 LYS A C     1 
ATOM   3638  O  O     . LYS A 1 1992 ? 130.403 159.697 130.543 1.00 131.57 ? 1992 LYS A O     1 
ATOM   3639  C  CB    . LYS A 1 1992 ? 132.764 160.238 128.515 1.00 120.86 ? 1992 LYS A CB    1 
ATOM   3640  C  CG    . LYS A 1 1992 ? 134.261 160.373 128.289 1.00 115.03 ? 1992 LYS A CG    1 
ATOM   3641  C  CD    . LYS A 1 1992 ? 134.607 161.698 127.631 1.00 110.56 ? 1992 LYS A CD    1 
ATOM   3642  C  CE    . LYS A 1 1992 ? 133.846 161.887 126.329 1.00 111.13 ? 1992 LYS A CE    1 
ATOM   3643  N  NZ    . LYS A 1 1992 ? 134.127 163.212 125.710 1.00 112.99 ? 1992 LYS A NZ    1 
ATOM   3644  N  N     . THR A 1 1993 ? 130.102 158.271 128.829 1.00 142.71 ? 1993 THR A N     1 
ATOM   3645  C  CA    . THR A 1 1993 ? 128.667 158.153 129.051 1.00 143.74 ? 1993 THR A CA    1 
ATOM   3646  C  C     . THR A 1 1993 ? 128.322 157.288 130.256 1.00 142.96 ? 1993 THR A C     1 
ATOM   3647  O  O     . THR A 1 1993 ? 127.162 157.284 130.681 1.00 143.51 ? 1993 THR A O     1 
ATOM   3648  C  CB    . THR A 1 1993 ? 127.984 157.585 127.804 1.00 144.21 ? 1993 THR A CB    1 
ATOM   3649  O  OG1   . THR A 1 1993 ? 128.557 156.312 127.481 1.00 144.33 ? 1993 THR A OG1   1 
ATOM   3650  C  CG2   . THR A 1 1993 ? 128.160 158.529 126.624 1.00 136.18 ? 1993 THR A CG2   1 
ATOM   3651  N  N     . SER A 1 1994 ? 129.290 156.562 130.810 1.00 140.48 ? 1994 SER A N     1 
ATOM   3652  C  CA    . SER A 1 1994 ? 129.056 155.727 131.980 1.00 139.30 ? 1994 SER A CA    1 
ATOM   3653  C  C     . SER A 1 1994 ? 129.147 156.585 133.242 1.00 137.30 ? 1994 SER A C     1 
ATOM   3654  O  O     . SER A 1 1994 ? 129.157 157.818 133.187 1.00 135.30 ? 1994 SER A O     1 
ATOM   3655  C  CB    . SER A 1 1994 ? 130.040 154.560 132.004 1.00 131.61 ? 1994 SER A CB    1 
ATOM   3656  O  OG    . SER A 1 1994 ? 131.379 155.022 132.026 1.00 127.71 ? 1994 SER A OG    1 
ATOM   3657  N  N     . ALA A 1 1995 ? 129.204 155.933 134.399 1.00 135.01 ? 1995 ALA A N     1 
ATOM   3658  C  CA    . ALA A 1 1995 ? 129.282 156.661 135.656 1.00 124.87 ? 1995 ALA A CA    1 
ATOM   3659  C  C     . ALA A 1 1995 ? 130.594 157.438 135.733 1.00 121.95 ? 1995 ALA A C     1 
ATOM   3660  O  O     . ALA A 1 1995 ? 131.646 156.924 135.333 1.00 118.40 ? 1995 ALA A O     1 
ATOM   3661  C  CB    . ALA A 1 1995 ? 129.170 155.700 136.840 1.00 119.34 ? 1995 ALA A CB    1 
ATOM   3662  N  N     . PRO A 1 1996 ? 130.570 158.674 136.225 1.00 116.19 ? 1996 PRO A N     1 
ATOM   3663  C  CA    . PRO A 1 1996 ? 131.804 159.457 136.335 1.00 103.50 ? 1996 PRO A CA    1 
ATOM   3664  C  C     . PRO A 1 1996 ? 132.807 158.816 137.279 1.00 91.29  ? 1996 PRO A C     1 
ATOM   3665  O  O     . PRO A 1 1996 ? 132.452 158.146 138.251 1.00 87.36  ? 1996 PRO A O     1 
ATOM   3666  C  CB    . PRO A 1 1996 ? 131.318 160.803 136.887 1.00 94.51  ? 1996 PRO A CB    1 
ATOM   3667  C  CG    . PRO A 1 1996 ? 129.883 160.880 136.488 1.00 97.26  ? 1996 PRO A CG    1 
ATOM   3668  C  CD    . PRO A 1 1996 ? 129.376 159.470 136.555 1.00 109.58 ? 1996 PRO A CD    1 
ATOM   3669  N  N     . ILE A 1 1997 ? 134.085 159.034 136.973 1.00 84.80  ? 1997 ILE A N     1 
ATOM   3670  C  CA    . ILE A 1 1997 ? 135.161 158.483 137.788 1.00 74.19  ? 1997 ILE A CA    1 
ATOM   3671  C  C     . ILE A 1 1997 ? 135.262 159.286 139.078 1.00 65.90  ? 1997 ILE A C     1 
ATOM   3672  O  O     . ILE A 1 1997 ? 135.483 160.502 139.053 1.00 62.46  ? 1997 ILE A O     1 
ATOM   3673  C  CB    . ILE A 1 1997 ? 136.488 158.491 137.022 1.00 66.22  ? 1997 ILE A CB    1 
ATOM   3674  C  CG1   . ILE A 1 1997 ? 136.363 157.675 135.734 1.00 73.80  ? 1997 ILE A CG1   1 
ATOM   3675  C  CG2   . ILE A 1 1997 ? 137.608 157.951 137.895 1.00 61.59  ? 1997 ILE A CG2   1 
ATOM   3676  C  CD1   . ILE A 1 1997 ? 136.018 156.223 135.961 1.00 74.93  ? 1997 ILE A CD1   1 
ATOM   3677  N  N     . THR A 1 1998 ? 135.105 158.608 140.212 1.00 64.66  ? 1998 THR A N     1 
ATOM   3678  C  CA    . THR A 1 1998 ? 135.127 159.248 141.518 1.00 56.49  ? 1998 THR A CA    1 
ATOM   3679  C  C     . THR A 1 1998 ? 136.096 158.516 142.435 1.00 53.40  ? 1998 THR A C     1 
ATOM   3680  O  O     . THR A 1 1998 ? 136.372 157.327 142.254 1.00 61.78  ? 1998 THR A O     1 
ATOM   3681  C  CB    . THR A 1 1998 ? 133.732 159.276 142.163 1.00 60.80  ? 1998 THR A CB    1 
ATOM   3682  O  OG1   . THR A 1 1998 ? 133.235 157.939 142.292 1.00 68.00  ? 1998 THR A OG1   1 
ATOM   3683  C  CG2   . THR A 1 1998 ? 132.766 160.095 141.320 1.00 55.29  ? 1998 THR A CG2   1 
ATOM   3684  N  N     . CYS A 1 1999 ? 136.611 159.244 143.424 1.00 45.40  ? 1999 CYS A N     1 
ATOM   3685  C  CA    . CYS A 1 1999 ? 137.537 158.688 144.398 1.00 46.70  ? 1999 CYS A CA    1 
ATOM   3686  C  C     . CYS A 1 1999 ? 137.126 159.140 145.792 1.00 50.53  ? 1999 CYS A C     1 
ATOM   3687  O  O     . CYS A 1 1999 ? 136.475 160.173 145.966 1.00 52.16  ? 1999 CYS A O     1 
ATOM   3688  C  CB    . CYS A 1 1999 ? 138.985 159.104 144.106 1.00 42.95  ? 1999 CYS A CB    1 
ATOM   3689  S  SG    . CYS A 1 1999 ? 139.395 160.793 144.598 1.00 51.02  ? 1999 CYS A SG    1 
ATOM   3690  N  N     . GLU A 1 2000 ? 137.515 158.348 146.788 1.00 52.77  ? 2000 GLU A N     1 
ATOM   3691  C  CA    . GLU A 1 2000 ? 137.183 158.635 148.182 1.00 50.82  ? 2000 GLU A CA    1 
ATOM   3692  C  C     . GLU A 1 2000 ? 138.190 159.636 148.731 1.00 52.35  ? 2000 GLU A C     1 
ATOM   3693  O  O     . GLU A 1 2000 ? 139.315 159.276 149.087 1.00 53.15  ? 2000 GLU A O     1 
ATOM   3694  C  CB    . GLU A 1 2000 ? 137.172 157.354 149.007 1.00 55.16  ? 2000 GLU A CB    1 
ATOM   3695  C  CG    . GLU A 1 2000 ? 136.410 157.470 150.317 1.00 63.80  ? 2000 GLU A CG    1 
ATOM   3696  C  CD    . GLU A 1 2000 ? 134.931 157.177 150.160 1.00 72.19  ? 2000 GLU A CD    1 
ATOM   3697  O  OE1   . GLU A 1 2000 ? 134.590 156.131 149.569 1.00 76.56  ? 2000 GLU A OE1   1 
ATOM   3698  O  OE2   . GLU A 1 2000 ? 134.109 157.993 150.627 1.00 71.87  ? 2000 GLU A OE2   1 
ATOM   3699  N  N     . LEU A 1 2001 ? 137.787 160.902 148.801 1.00 48.16  ? 2001 LEU A N     1 
ATOM   3700  C  CA    . LEU A 1 2001 ? 138.611 161.969 149.354 1.00 38.13  ? 2001 LEU A CA    1 
ATOM   3701  C  C     . LEU A 1 2001 ? 137.865 162.601 150.519 1.00 42.70  ? 2001 LEU A C     1 
ATOM   3702  O  O     . LEU A 1 2001 ? 136.762 163.129 150.337 1.00 51.37  ? 2001 LEU A O     1 
ATOM   3703  C  CB    . LEU A 1 2001 ? 138.941 163.018 148.289 1.00 34.17  ? 2001 LEU A CB    1 
ATOM   3704  C  CG    . LEU A 1 2001 ? 140.290 162.887 147.582 1.00 27.39  ? 2001 LEU A CG    1 
ATOM   3705  C  CD1   . LEU A 1 2001 ? 140.393 163.888 146.445 1.00 23.41  ? 2001 LEU A CD1   1 
ATOM   3706  C  CD2   . LEU A 1 2001 ? 141.432 163.073 148.566 1.00 24.65  ? 2001 LEU A CD2   1 
ATOM   3707  N  N     . LEU A 1 2002 ? 138.469 162.549 151.707 1.00 38.28  ? 2002 LEU A N     1 
ATOM   3708  C  CA    . LEU A 1 2002 ? 137.859 163.072 152.930 1.00 41.55  ? 2002 LEU A CA    1 
ATOM   3709  C  C     . LEU A 1 2002 ? 136.480 162.460 153.165 1.00 49.14  ? 2002 LEU A C     1 
ATOM   3710  O  O     . LEU A 1 2002 ? 135.521 163.150 153.520 1.00 54.61  ? 2002 LEU A O     1 
ATOM   3711  C  CB    . LEU A 1 2002 ? 137.784 164.600 152.899 1.00 42.35  ? 2002 LEU A CB    1 
ATOM   3712  C  CG    . LEU A 1 2002 ? 139.113 165.347 153.025 1.00 34.09  ? 2002 LEU A CG    1 
ATOM   3713  C  CD1   . LEU A 1 2002 ? 138.873 166.818 153.316 1.00 35.39  ? 2002 LEU A CD1   1 
ATOM   3714  C  CD2   . LEU A 1 2002 ? 139.986 164.721 154.100 1.00 31.47  ? 2002 LEU A CD2   1 
ATOM   3715  N  N     . ASN A 1 2003 ? 136.385 161.144 152.957 1.00 50.70  ? 2003 ASN A N     1 
ATOM   3716  C  CA    . ASN A 1 2003 ? 135.152 160.384 153.172 1.00 53.61  ? 2003 ASN A CA    1 
ATOM   3717  C  C     . ASN A 1 2003 ? 134.004 160.913 152.315 1.00 56.77  ? 2003 ASN A C     1 
ATOM   3718  O  O     . ASN A 1 2003 ? 132.847 160.935 152.739 1.00 58.91  ? 2003 ASN A O     1 
ATOM   3719  C  CB    . ASN A 1 2003 ? 134.762 160.368 154.652 1.00 52.42  ? 2003 ASN A CB    1 
ATOM   3720  C  CG    . ASN A 1 2003 ? 135.277 159.142 155.377 1.00 51.50  ? 2003 ASN A CG    1 
ATOM   3721  O  OD1   . ASN A 1 2003 ? 135.032 158.011 154.958 1.00 52.15  ? 2003 ASN A OD1   1 
ATOM   3722  N  ND2   . ASN A 1 2003 ? 135.997 159.359 156.471 1.00 51.95  ? 2003 ASN A ND2   1 
ATOM   3723  N  N     . LYS A 1 2004 ? 134.325 161.342 151.096 1.00 52.28  ? 2004 LYS A N     1 
ATOM   3724  C  CA    . LYS A 1 2004 ? 133.325 161.791 150.140 1.00 51.28  ? 2004 LYS A CA    1 
ATOM   3725  C  C     . LYS A 1 2004 ? 133.709 161.310 148.749 1.00 57.23  ? 2004 LYS A C     1 
ATOM   3726  O  O     . LYS A 1 2004 ? 134.881 161.047 148.468 1.00 58.61  ? 2004 LYS A O     1 
ATOM   3727  C  CB    . LYS A 1 2004 ? 133.175 163.320 150.133 1.00 51.43  ? 2004 LYS A CB    1 
ATOM   3728  C  CG    . LYS A 1 2004 ? 132.598 163.907 151.410 1.00 61.56  ? 2004 LYS A CG    1 
ATOM   3729  C  CD    . LYS A 1 2004 ? 132.331 165.394 151.253 1.00 75.90  ? 2004 LYS A CD    1 
ATOM   3730  C  CE    . LYS A 1 2004 ? 133.625 166.192 151.262 1.00 76.11  ? 2004 LYS A CE    1 
ATOM   3731  N  NZ    . LYS A 1 2004 ? 133.373 167.659 151.219 1.00 79.62  ? 2004 LYS A NZ    1 
ATOM   3732  N  N     . GLN A 1 2005 ? 132.707 161.200 147.880 1.00 57.03  ? 2005 GLN A N     1 
ATOM   3733  C  CA    . GLN A 1 2005 ? 132.922 160.815 146.489 1.00 55.02  ? 2005 GLN A CA    1 
ATOM   3734  C  C     . GLN A 1 2005 ? 133.219 162.073 145.683 1.00 54.63  ? 2005 GLN A C     1 
ATOM   3735  O  O     . GLN A 1 2005 ? 132.338 162.915 145.483 1.00 57.86  ? 2005 GLN A O     1 
ATOM   3736  C  CB    . GLN A 1 2005 ? 131.706 160.078 145.936 1.00 53.79  ? 2005 GLN A CB    1 
ATOM   3737  C  CG    . GLN A 1 2005 ? 131.488 158.705 146.546 1.00 60.37  ? 2005 GLN A CG    1 
ATOM   3738  C  CD    . GLN A 1 2005 ? 132.670 157.781 146.331 1.00 60.10  ? 2005 GLN A CD    1 
ATOM   3739  O  OE1   . GLN A 1 2005 ? 133.063 157.512 145.197 1.00 59.58  ? 2005 GLN A OE1   1 
ATOM   3740  N  NE2   . GLN A 1 2005 ? 133.244 157.291 147.423 1.00 55.26  ? 2005 GLN A NE2   1 
ATOM   3741  N  N     . VAL A 1 2006 ? 134.459 162.199 145.221 1.00 51.61  ? 2006 VAL A N     1 
ATOM   3742  C  CA    . VAL A 1 2006 ? 134.921 163.372 144.489 1.00 43.82  ? 2006 VAL A CA    1 
ATOM   3743  C  C     . VAL A 1 2006 ? 135.267 162.938 143.074 1.00 46.17  ? 2006 VAL A C     1 
ATOM   3744  O  O     . VAL A 1 2006 ? 136.099 162.042 142.880 1.00 53.20  ? 2006 VAL A O     1 
ATOM   3745  C  CB    . VAL A 1 2006 ? 136.131 164.028 145.170 1.00 35.10  ? 2006 VAL A CB    1 
ATOM   3746  C  CG1   . VAL A 1 2006 ? 136.659 165.172 144.325 1.00 34.23  ? 2006 VAL A CG1   1 
ATOM   3747  C  CG2   . VAL A 1 2006 ? 135.754 164.515 146.559 1.00 44.22  ? 2006 VAL A CG2   1 
ATOM   3748  N  N     . LYS A 1 2007 ? 134.633 163.569 142.089 1.00 44.91  ? 2007 LYS A N     1 
ATOM   3749  C  CA    . LYS A 1 2007 ? 134.945 163.276 140.697 1.00 42.94  ? 2007 LYS A CA    1 
ATOM   3750  C  C     . LYS A 1 2007 ? 136.363 163.735 140.379 1.00 38.81  ? 2007 LYS A C     1 
ATOM   3751  O  O     . LYS A 1 2007 ? 136.823 164.767 140.879 1.00 40.51  ? 2007 LYS A O     1 
ATOM   3752  C  CB    . LYS A 1 2007 ? 133.927 163.943 139.769 1.00 40.24  ? 2007 LYS A CB    1 
ATOM   3753  C  CG    . LYS A 1 2007 ? 134.210 165.397 139.430 1.00 45.66  ? 2007 LYS A CG    1 
ATOM   3754  C  CD    . LYS A 1 2007 ? 133.431 165.840 138.202 1.00 47.79  ? 2007 LYS A CD    1 
ATOM   3755  C  CE    . LYS A 1 2007 ? 133.913 167.191 137.700 1.00 53.32  ? 2007 LYS A CE    1 
ATOM   3756  N  NZ    . LYS A 1 2007 ? 135.335 167.146 137.262 1.00 51.05  ? 2007 LYS A NZ    1 
ATOM   3757  N  N     . VAL A 1 2008 ? 137.069 162.949 139.574 1.00 39.19  ? 2008 VAL A N     1 
ATOM   3758  C  CA    . VAL A 1 2008 ? 138.464 163.210 139.238 1.00 35.26  ? 2008 VAL A CA    1 
ATOM   3759  C  C     . VAL A 1 2008 ? 138.534 163.516 137.750 1.00 37.92  ? 2008 VAL A C     1 
ATOM   3760  O  O     . VAL A 1 2008 ? 138.222 162.659 136.913 1.00 51.71  ? 2008 VAL A O     1 
ATOM   3761  C  CB    . VAL A 1 2008 ? 139.369 162.027 139.605 1.00 32.08  ? 2008 VAL A CB    1 
ATOM   3762  C  CG1   . VAL A 1 2008 ? 140.829 162.403 139.422 1.00 28.82  ? 2008 VAL A CG1   1 
ATOM   3763  C  CG2   . VAL A 1 2008 ? 139.104 161.579 141.032 1.00 31.05  ? 2008 VAL A CG2   1 
ATOM   3764  N  N     . SER A 1 2009 ? 138.941 164.735 137.417 1.00 30.86  ? 2009 SER A N     1 
ATOM   3765  C  CA    . SER A 1 2009 ? 139.130 165.093 136.021 1.00 32.12  ? 2009 SER A CA    1 
ATOM   3766  C  C     . SER A 1 2009 ? 140.424 164.473 135.497 1.00 39.42  ? 2009 SER A C     1 
ATOM   3767  O  O     . SER A 1 2009 ? 141.415 164.393 136.229 1.00 42.35  ? 2009 SER A O     1 
ATOM   3768  C  CB    . SER A 1 2009 ? 139.167 166.610 135.856 1.00 31.46  ? 2009 SER A CB    1 
ATOM   3769  O  OG    . SER A 1 2009 ? 139.510 166.973 134.531 1.00 39.14  ? 2009 SER A OG    1 
ATOM   3770  N  N     . PRO A 1 2010 ? 140.445 164.021 134.241 1.00 38.11  ? 2010 PRO A N     1 
ATOM   3771  C  CA    . PRO A 1 2010 ? 141.672 163.412 133.702 1.00 35.78  ? 2010 PRO A CA    1 
ATOM   3772  C  C     . PRO A 1 2010 ? 142.843 164.374 133.600 1.00 35.20  ? 2010 PRO A C     1 
ATOM   3773  O  O     . PRO A 1 2010 ? 143.990 163.919 133.515 1.00 35.68  ? 2010 PRO A O     1 
ATOM   3774  C  CB    . PRO A 1 2010 ? 141.238 162.913 132.317 1.00 41.58  ? 2010 PRO A CB    1 
ATOM   3775  C  CG    . PRO A 1 2010 ? 140.029 163.725 131.978 1.00 36.35  ? 2010 PRO A CG    1 
ATOM   3776  C  CD    . PRO A 1 2010 ? 139.333 163.979 133.277 1.00 37.23  ? 2010 PRO A CD    1 
ATOM   3777  N  N     . ASP A 1 2011 ? 142.597 165.681 133.605 1.00 31.01  ? 2011 ASP A N     1 
ATOM   3778  C  CA    . ASP A 1 2011 ? 143.647 166.674 133.424 1.00 25.35  ? 2011 ASP A CA    1 
ATOM   3779  C  C     . ASP A 1 2011 ? 144.407 166.987 134.706 1.00 28.04  ? 2011 ASP A C     1 
ATOM   3780  O  O     . ASP A 1 2011 ? 145.378 167.748 134.661 1.00 26.25  ? 2011 ASP A O     1 
ATOM   3781  C  CB    . ASP A 1 2011 ? 143.054 167.968 132.857 1.00 27.71  ? 2011 ASP A CB    1 
ATOM   3782  C  CG    . ASP A 1 2011 ? 142.557 167.808 131.435 1.00 43.83  ? 2011 ASP A CG    1 
ATOM   3783  O  OD1   . ASP A 1 2011 ? 143.107 166.960 130.703 1.00 49.05  ? 2011 ASP A OD1   1 
ATOM   3784  O  OD2   . ASP A 1 2011 ? 141.618 168.534 131.049 1.00 56.65  ? 2011 ASP A OD2   1 
ATOM   3785  N  N     . MET A 1 2012 ? 143.994 166.428 135.840 1.00 28.65  ? 2012 MET A N     1 
ATOM   3786  C  CA    . MET A 1 2012 ? 144.637 166.748 137.105 1.00 21.11  ? 2012 MET A CA    1 
ATOM   3787  C  C     . MET A 1 2012 ? 146.025 166.119 137.185 1.00 20.49  ? 2012 MET A C     1 
ATOM   3788  O  O     . MET A 1 2012 ? 146.269 165.024 136.672 1.00 20.94  ? 2012 MET A O     1 
ATOM   3789  C  CB    . MET A 1 2012 ? 143.782 166.265 138.276 1.00 18.52  ? 2012 MET A CB    1 
ATOM   3790  C  CG    . MET A 1 2012 ? 144.458 166.411 139.625 1.00 23.27  ? 2012 MET A CG    1 
ATOM   3791  S  SD    . MET A 1 2012 ? 143.874 165.241 140.852 1.00 48.94  ? 2012 MET A SD    1 
ATOM   3792  C  CE    . MET A 1 2012 ? 144.694 165.860 142.318 1.00 26.53  ? 2012 MET A CE    1 
ATOM   3793  N  N     . ALA A 1 2013 ? 146.941 166.831 137.838 1.00 15.30  ? 2013 ALA A N     1 
ATOM   3794  C  CA    . ALA A 1 2013 ? 148.285 166.331 138.071 1.00 9.91   ? 2013 ALA A CA    1 
ATOM   3795  C  C     . ALA A 1 2013 ? 148.761 166.804 139.436 1.00 9.52   ? 2013 ALA A C     1 
ATOM   3796  O  O     . ALA A 1 2013 ? 148.323 167.844 139.935 1.00 13.29  ? 2013 ALA A O     1 
ATOM   3797  C  CB    . ALA A 1 2013 ? 149.251 166.797 136.980 1.00 9.77   ? 2013 ALA A CB    1 
ATOM   3798  N  N     . ILE A 1 2014 ? 149.660 166.029 140.035 1.00 6.76   ? 2014 ILE A N     1 
ATOM   3799  C  CA    . ILE A 1 2014 ? 150.254 166.355 141.326 1.00 8.82   ? 2014 ILE A CA    1 
ATOM   3800  C  C     . ILE A 1 2014 ? 151.764 166.392 141.151 1.00 9.09   ? 2014 ILE A C     1 
ATOM   3801  O  O     . ILE A 1 2014 ? 152.374 165.389 140.760 1.00 12.14  ? 2014 ILE A O     1 
ATOM   3802  C  CB    . ILE A 1 2014 ? 149.857 165.345 142.414 1.00 10.40  ? 2014 ILE A CB    1 
ATOM   3803  C  CG1   . ILE A 1 2014 ? 148.335 165.250 142.529 1.00 15.96  ? 2014 ILE A CG1   1 
ATOM   3804  C  CG2   . ILE A 1 2014 ? 150.469 165.734 143.751 1.00 9.00   ? 2014 ILE A CG2   1 
ATOM   3805  C  CD1   . ILE A 1 2014 ? 147.863 164.152 143.455 1.00 16.62  ? 2014 ILE A CD1   1 
ATOM   3806  N  N     . PHE A 1 2015 ? 152.366 167.542 141.439 1.00 5.41   ? 2015 PHE A N     1 
ATOM   3807  C  CA    . PHE A 1 2015 ? 153.809 167.713 141.385 1.00 6.77   ? 2015 PHE A CA    1 
ATOM   3808  C  C     . PHE A 1 2015 ? 154.307 168.198 142.737 1.00 9.76   ? 2015 PHE A C     1 
ATOM   3809  O  O     . PHE A 1 2015 ? 153.698 169.078 143.353 1.00 14.94  ? 2015 PHE A O     1 
ATOM   3810  C  CB    . PHE A 1 2015 ? 154.219 168.707 140.293 1.00 8.50   ? 2015 PHE A CB    1 
ATOM   3811  C  CG    . PHE A 1 2015 ? 154.034 168.188 138.897 1.00 6.86   ? 2015 PHE A CG    1 
ATOM   3812  C  CD1   . PHE A 1 2015 ? 152.772 168.087 138.342 1.00 5.32   ? 2015 PHE A CD1   1 
ATOM   3813  C  CD2   . PHE A 1 2015 ? 155.124 167.800 138.140 1.00 6.46   ? 2015 PHE A CD2   1 
ATOM   3814  C  CE1   . PHE A 1 2015 ? 152.603 167.611 137.059 1.00 8.26   ? 2015 PHE A CE1   1 
ATOM   3815  C  CE2   . PHE A 1 2015 ? 154.957 167.323 136.857 1.00 9.00   ? 2015 PHE A CE2   1 
ATOM   3816  C  CZ    . PHE A 1 2015 ? 153.696 167.228 136.317 1.00 9.81   ? 2015 PHE A CZ    1 
ATOM   3817  N  N     . ILE A 1 2016 ? 155.413 167.621 143.198 1.00 7.88   ? 2016 ILE A N     1 
ATOM   3818  C  CA    . ILE A 1 2016 ? 156.016 167.981 144.476 1.00 10.03  ? 2016 ILE A CA    1 
ATOM   3819  C  C     . ILE A 1 2016 ? 157.482 168.312 144.214 1.00 12.88  ? 2016 ILE A C     1 
ATOM   3820  O  O     . ILE A 1 2016 ? 158.229 167.488 143.674 1.00 17.76  ? 2016 ILE A O     1 
ATOM   3821  C  CB    . ILE A 1 2016 ? 155.863 166.876 145.531 1.00 8.85   ? 2016 ILE A CB    1 
ATOM   3822  C  CG1   . ILE A 1 2016 ? 156.407 165.539 145.026 1.00 9.73   ? 2016 ILE A CG1   1 
ATOM   3823  C  CG2   . ILE A 1 2016 ? 154.403 166.717 145.916 1.00 11.12  ? 2016 ILE A CG2   1 
ATOM   3824  C  CD1   . ILE A 1 2016 ? 156.541 164.490 146.105 1.00 11.35  ? 2016 ILE A CD1   1 
ATOM   3825  N  N     . THR A 1 2017 ? 157.884 169.538 144.558 1.00 14.89  ? 2017 THR A N     1 
ATOM   3826  C  CA    . THR A 1 2017 ? 159.295 169.943 144.386 1.00 15.75  ? 2017 THR A CA    1 
ATOM   3827  C  C     . THR A 1 2017 ? 159.876 170.187 145.759 1.00 21.26  ? 2017 THR A C     1 
ATOM   3828  O  O     . THR A 1 2017 ? 159.216 170.885 146.557 1.00 26.38  ? 2017 THR A O     1 
ATOM   3829  C  CB    . THR A 1 2017 ? 159.376 171.187 143.504 1.00 17.94  ? 2017 THR A CB    1 
ATOM   3830  O  OG1   . THR A 1 2017 ? 158.812 172.234 144.288 1.00 29.55  ? 2017 THR A OG1   1 
ATOM   3831  C  CG2   . THR A 1 2017 ? 158.604 171.033 142.206 1.00 12.09  ? 2017 THR A CG2   1 
ATOM   3832  N  N     . MET A 1 2018 ? 161.056 169.630 146.045 1.00 18.46  ? 2018 MET A N     1 
ATOM   3833  C  CA    . MET A 1 2018 ? 161.625 169.755 147.412 1.00 23.49  ? 2018 MET A CA    1 
ATOM   3834  C  C     . MET A 1 2018 ? 163.159 169.739 147.348 1.00 23.85  ? 2018 MET A C     1 
ATOM   3835  O  O     . MET A 1 2018 ? 163.706 169.206 146.358 1.00 21.10  ? 2018 MET A O     1 
ATOM   3836  C  CB    . MET A 1 2018 ? 161.145 168.601 148.298 1.00 25.94  ? 2018 MET A CB    1 
ATOM   3837  C  CG    . MET A 1 2018 ? 161.501 167.229 147.761 1.00 24.59  ? 2018 MET A CG    1 
ATOM   3838  S  SD    . MET A 1 2018 ? 160.721 165.899 148.696 1.00 19.35  ? 2018 MET A SD    1 
ATOM   3839  C  CE    . MET A 1 2018 ? 158.989 166.326 148.468 1.00 21.54  ? 2018 MET A CE    1 
ATOM   3840  N  N     . ASN A 1 2019 ? 163.818 170.307 148.363 1.00 30.23  ? 2019 ASN A N     1 
ATOM   3841  C  CA    . ASN A 1 2019 ? 165.306 170.285 148.423 1.00 29.18  ? 2019 ASN A CA    1 
ATOM   3842  C  C     . ASN A 1 2019 ? 165.731 169.163 149.375 1.00 33.63  ? 2019 ASN A C     1 
ATOM   3843  O  O     . ASN A 1 2019 ? 165.734 169.393 150.605 1.00 36.16  ? 2019 ASN A O     1 
ATOM   3844  C  CB    . ASN A 1 2019 ? 165.869 171.642 148.829 1.00 32.12  ? 2019 ASN A CB    1 
ATOM   3845  C  CG    . ASN A 1 2019 ? 167.375 171.634 148.946 1.00 32.00  ? 2019 ASN A CG    1 
ATOM   3846  O  OD1   . ASN A 1 2019 ? 167.934 170.919 149.785 1.00 33.70  ? 2019 ASN A OD1   1 
ATOM   3847  N  ND2   . ASN A 1 2019 ? 168.047 172.430 148.128 1.00 29.91  ? 2019 ASN A ND2   1 
ATOM   3848  N  N     . PRO A 1 2020 ? 166.083 167.963 148.865 1.00 36.01  ? 2020 PRO A N     1 
ATOM   3849  C  CA    . PRO A 1 2020 ? 166.438 166.846 149.729 1.00 36.33  ? 2020 PRO A CA    1 
ATOM   3850  C  C     . PRO A 1 2020 ? 167.659 167.194 150.562 1.00 40.54  ? 2020 PRO A C     1 
ATOM   3851  O  O     . PRO A 1 2020 ? 167.782 166.697 151.700 1.00 39.09  ? 2020 PRO A O     1 
ATOM   3852  C  CB    . PRO A 1 2020 ? 166.716 165.705 148.739 1.00 37.97  ? 2020 PRO A CB    1 
ATOM   3853  C  CG    . PRO A 1 2020 ? 166.010 166.132 147.472 1.00 32.98  ? 2020 PRO A CG    1 
ATOM   3854  C  CD    . PRO A 1 2020 ? 166.146 167.643 147.451 1.00 33.02  ? 2020 PRO A CD    1 
ATOM   3855  N  N     . GLY A 1 2021 ? 168.540 168.039 150.019 1.00 45.05  ? 2021 GLY A N     1 
ATOM   3856  C  CA    . GLY A 1 2021 ? 169.778 168.407 150.732 1.00 46.18  ? 2021 GLY A CA    1 
ATOM   3857  C  C     . GLY A 1 2021 ? 169.476 168.916 152.126 1.00 44.80  ? 2021 GLY A C     1 
ATOM   3858  O  O     . GLY A 1 2021 ? 170.387 168.840 152.976 1.00 49.09  ? 2021 GLY A O     1 
ATOM   3859  N  N     A TYR A 1 2022 ? 168.413 169.716 152.255 0.52 40.81  ? 2022 TYR A N     1 
ATOM   3860  N  N     B TYR A 1 2022 ? 168.402 169.700 152.259 0.48 40.80  ? 2022 TYR A N     1 
ATOM   3861  C  CA    A TYR A 1 2022 ? 168.021 170.260 153.585 0.52 41.14  ? 2022 TYR A CA    1 
ATOM   3862  C  CA    B TYR A 1 2022 ? 168.024 170.262 153.584 0.48 41.13  ? 2022 TYR A CA    1 
ATOM   3863  C  C     A TYR A 1 2022 ? 167.756 169.092 154.532 0.52 44.76  ? 2022 TYR A C     1 
ATOM   3864  C  C     B TYR A 1 2022 ? 167.747 169.102 154.539 0.48 44.75  ? 2022 TYR A C     1 
ATOM   3865  O  O     A TYR A 1 2022 ? 166.637 168.539 154.458 0.52 44.82  ? 2022 TYR A O     1 
ATOM   3866  O  O     B TYR A 1 2022 ? 166.610 168.586 154.489 0.48 44.81  ? 2022 TYR A O     1 
ATOM   3867  C  CB    A TYR A 1 2022 ? 166.799 171.175 153.463 0.52 39.20  ? 2022 TYR A CB    1 
ATOM   3868  C  CB    B TYR A 1 2022 ? 166.844 171.216 153.375 0.48 39.39  ? 2022 TYR A CB    1 
ATOM   3869  C  CG    A TYR A 1 2022 ? 166.989 172.383 152.556 0.52 37.00  ? 2022 TYR A CG    1 
ATOM   3870  C  CG    B TYR A 1 2022 ? 166.458 172.051 154.589 0.48 41.47  ? 2022 TYR A CG    1 
ATOM   3871  C  CD1   A TYR A 1 2022 ? 168.249 172.926 152.339 0.52 37.41  ? 2022 TYR A CD1   1 
ATOM   3872  C  CD1   B TYR A 1 2022 ? 166.549 171.535 155.875 0.48 41.21  ? 2022 TYR A CD1   1 
ATOM   3873  C  CD2   A TYR A 1 2022 ? 165.905 172.988 151.932 0.52 35.96  ? 2022 TYR A CD2   1 
ATOM   3874  C  CD2   B TYR A 1 2022 ? 166.020 173.362 154.448 0.48 39.26  ? 2022 TYR A CD2   1 
ATOM   3875  C  CE1   A TYR A 1 2022 ? 168.427 174.027 151.517 0.52 37.59  ? 2022 TYR A CE1   1 
ATOM   3876  C  CE1   B TYR A 1 2022 ? 166.203 172.290 156.982 0.48 40.00  ? 2022 TYR A CE1   1 
ATOM   3877  C  CE2   A TYR A 1 2022 ? 166.071 174.091 151.110 0.52 35.04  ? 2022 TYR A CE2   1 
ATOM   3878  C  CE2   B TYR A 1 2022 ? 165.673 174.129 155.547 0.48 37.34  ? 2022 TYR A CE2   1 
ATOM   3879  C  CZ    A TYR A 1 2022 ? 167.335 174.611 150.902 0.52 34.81  ? 2022 TYR A CZ    1 
ATOM   3880  C  CZ    B TYR A 1 2022 ? 165.764 173.590 156.818 0.48 36.49  ? 2022 TYR A CZ    1 
ATOM   3881  O  OH    A TYR A 1 2022 ? 167.507 175.697 150.093 0.52 30.48  ? 2022 TYR A OH    1 
ATOM   3882  O  OH    B TYR A 1 2022 ? 165.424 174.331 157.911 0.48 34.90  ? 2022 TYR A OH    1 
ATOM   3883  N  N     . ALA A 1 2023 ? 168.567 168.978 155.588 1.00 47.28  ? 2023 ALA A N     1 
ATOM   3884  C  CA    . ALA A 1 2023 ? 168.401 167.866 156.559 1.00 51.28  ? 2023 ALA A CA    1 
ATOM   3885  C  C     . ALA A 1 2023 ? 167.114 168.045 157.368 1.00 54.14  ? 2023 ALA A C     1 
ATOM   3886  O  O     . ALA A 1 2023 ? 166.367 167.055 157.530 1.00 58.57  ? 2023 ALA A O     1 
ATOM   3887  C  CB    . ALA A 1 2023 ? 169.611 167.792 157.463 1.00 48.12  ? 2023 ALA A CB    1 
ATOM   3888  N  N     . GLY A 1 2024 ? 166.857 169.263 157.853 1.00 51.08  ? 2024 GLY A N     1 
ATOM   3889  C  CA    . GLY A 1 2024 ? 165.670 169.509 158.696 1.00 51.69  ? 2024 GLY A CA    1 
ATOM   3890  C  C     . GLY A 1 2024 ? 164.401 169.056 158.001 1.00 48.59  ? 2024 GLY A C     1 
ATOM   3891  O  O     . GLY A 1 2024 ? 163.482 168.585 158.702 1.00 43.42  ? 2024 GLY A O     1 
ATOM   3892  N  N     . ARG A 1 2025 ? 164.352 169.183 156.673 1.00 48.57  ? 2025 ARG A N     1 
ATOM   3893  C  CA    . ARG A 1 2025 ? 163.158 168.762 155.896 1.00 41.11  ? 2025 ARG A CA    1 
ATOM   3894  C  C     . ARG A 1 2025 ? 162.802 167.311 156.258 1.00 34.59  ? 2025 ARG A C     1 
ATOM   3895  O  O     . ARG A 1 2025 ? 163.729 166.476 156.335 1.00 31.62  ? 2025 ARG A O     1 
ATOM   3896  C  CB    . ARG A 1 2025 ? 163.448 168.903 154.399 1.00 39.44  ? 2025 ARG A CB    1 
ATOM   3897  C  CG    . ARG A 1 2025 ? 163.576 170.340 153.919 1.00 35.86  ? 2025 ARG A CG    1 
ATOM   3898  C  CD    . ARG A 1 2025 ? 162.218 170.960 153.644 1.00 33.21  ? 2025 ARG A CD    1 
ATOM   3899  N  NE    . ARG A 1 2025 ? 162.314 172.347 153.178 1.00 38.01  ? 2025 ARG A NE    1 
ATOM   3900  C  CZ    . ARG A 1 2025 ? 162.777 173.355 153.903 1.00 42.37  ? 2025 ARG A CZ    1 
ATOM   3901  N  NH1   . ARG A 1 2025 ? 162.799 173.264 155.221 1.00 44.12  ? 2025 ARG A NH1   1 
ATOM   3902  N  NH2   . ARG A 1 2025 ? 163.199 174.457 153.309 1.00 38.15  ? 2025 ARG A NH2   1 
ATOM   3903  N  N     . SER A 1 2026 ? 161.512 167.030 156.468 1.00 29.96  ? 2026 SER A N     1 
ATOM   3904  C  CA    . SER A 1 2026 ? 161.066 165.661 156.840 1.00 25.62  ? 2026 SER A CA    1 
ATOM   3905  C  C     . SER A 1 2026 ? 161.349 164.685 155.690 1.00 26.43  ? 2026 SER A C     1 
ATOM   3906  O  O     . SER A 1 2026 ? 161.270 165.113 154.518 1.00 33.10  ? 2026 SER A O     1 
ATOM   3907  C  CB    . SER A 1 2026 ? 159.607 165.648 157.213 1.00 24.10  ? 2026 SER A CB    1 
ATOM   3908  O  OG    . SER A 1 2026 ? 159.343 166.560 158.270 1.00 33.06  ? 2026 SER A OG    1 
ATOM   3909  N  N     . ASN A 1 2027 ? 161.659 163.428 156.016 1.00 29.31  ? 2027 ASN A N     1 
ATOM   3910  C  CA    . ASN A 1 2027 ? 161.925 162.400 154.971 1.00 30.52  ? 2027 ASN A CA    1 
ATOM   3911  C  C     . ASN A 1 2027 ? 160.592 161.816 154.495 1.00 27.98  ? 2027 ASN A C     1 
ATOM   3912  O  O     . ASN A 1 2027 ? 159.673 161.683 155.332 1.00 29.97  ? 2027 ASN A O     1 
ATOM   3913  C  CB    . ASN A 1 2027 ? 162.870 161.318 155.482 1.00 32.24  ? 2027 ASN A CB    1 
ATOM   3914  C  CG    . ASN A 1 2027 ? 164.145 161.901 156.042 1.00 44.26  ? 2027 ASN A CG    1 
ATOM   3915  O  OD1   . ASN A 1 2027 ? 164.453 161.704 157.223 1.00 51.79  ? 2027 ASN A OD1   1 
ATOM   3916  N  ND2   . ASN A 1 2027 ? 164.894 162.620 155.219 1.00 42.07  ? 2027 ASN A ND2   1 
ATOM   3917  N  N     . LEU A 1 2028 ? 160.492 161.481 153.205 1.00 26.22  ? 2028 LEU A N     1 
ATOM   3918  C  CA    . LEU A 1 2028 ? 159.253 160.937 152.669 1.00 22.43  ? 2028 LEU A CA    1 
ATOM   3919  C  C     . LEU A 1 2028 ? 159.200 159.426 152.883 1.00 26.63  ? 2028 LEU A C     1 
ATOM   3920  O  O     . LEU A 1 2028 ? 160.219 158.743 152.747 1.00 30.59  ? 2028 LEU A O     1 
ATOM   3921  C  CB    . LEU A 1 2028 ? 159.128 161.253 151.180 1.00 17.54  ? 2028 LEU A CB    1 
ATOM   3922  C  CG    . LEU A 1 2028 ? 158.390 162.534 150.790 1.00 17.37  ? 2028 LEU A CG    1 
ATOM   3923  C  CD1   . LEU A 1 2028 ? 159.226 163.762 151.111 1.00 15.53  ? 2028 LEU A CD1   1 
ATOM   3924  C  CD2   . LEU A 1 2028 ? 158.021 162.505 149.317 1.00 16.84  ? 2028 LEU A CD2   1 
ATOM   3925  N  N     . PRO A 1 2029 ? 158.035 158.882 153.223 1.00 27.61  ? 2029 PRO A N     1 
ATOM   3926  C  CA    . PRO A 1 2029 ? 157.904 157.427 153.334 1.00 25.48  ? 2029 PRO A CA    1 
ATOM   3927  C  C     . PRO A 1 2029 ? 158.052 156.753 151.978 1.00 26.24  ? 2029 PRO A C     1 
ATOM   3928  O  O     . PRO A 1 2029 ? 157.823 157.349 150.923 1.00 26.80  ? 2029 PRO A O     1 
ATOM   3929  C  CB    . PRO A 1 2029 ? 156.493 157.234 153.901 1.00 21.88  ? 2029 PRO A CB    1 
ATOM   3930  C  CG    . PRO A 1 2029 ? 155.773 158.498 153.579 1.00 21.61  ? 2029 PRO A CG    1 
ATOM   3931  C  CD    . PRO A 1 2029 ? 156.803 159.582 153.623 1.00 23.52  ? 2029 PRO A CD    1 
ATOM   3932  N  N     . ASP A 1 2030 ? 158.454 155.481 152.024 1.00 27.07  ? 2030 ASP A N     1 
ATOM   3933  C  CA    . ASP A 1 2030 ? 158.709 154.737 150.794 1.00 26.63  ? 2030 ASP A CA    1 
ATOM   3934  C  C     . ASP A 1 2030 ? 157.441 154.571 149.965 1.00 25.68  ? 2030 ASP A C     1 
ATOM   3935  O  O     . ASP A 1 2030 ? 157.491 154.626 148.731 1.00 31.21  ? 2030 ASP A O     1 
ATOM   3936  C  CB    . ASP A 1 2030 ? 159.319 153.375 151.122 1.00 39.97  ? 2030 ASP A CB    1 
ATOM   3937  C  CG    . ASP A 1 2030 ? 160.600 153.489 151.925 1.00 56.68  ? 2030 ASP A CG    1 
ATOM   3938  O  OD1   . ASP A 1 2030 ? 160.700 152.834 152.984 1.00 60.59  ? 2030 ASP A OD1   1 
ATOM   3939  O  OD2   . ASP A 1 2030 ? 161.507 154.233 151.498 1.00 55.15  ? 2030 ASP A OD2   1 
ATOM   3940  N  N     . ASN A 1 2031 ? 156.297 154.359 150.620 1.00 26.40  ? 2031 ASN A N     1 
ATOM   3941  C  CA    . ASN A 1 2031 ? 155.046 154.217 149.882 1.00 23.73  ? 2031 ASN A CA    1 
ATOM   3942  C  C     . ASN A 1 2031 ? 154.651 155.513 149.187 1.00 22.28  ? 2031 ASN A C     1 
ATOM   3943  O  O     . ASN A 1 2031 ? 154.055 155.477 148.105 1.00 24.95  ? 2031 ASN A O     1 
ATOM   3944  C  CB    . ASN A 1 2031 ? 153.930 153.753 150.817 1.00 20.53  ? 2031 ASN A CB    1 
ATOM   3945  C  CG    . ASN A 1 2031 ? 153.848 154.578 152.083 1.00 25.63  ? 2031 ASN A CG    1 
ATOM   3946  O  OD1   . ASN A 1 2031 ? 154.766 154.571 152.902 1.00 33.00  ? 2031 ASN A OD1   1 
ATOM   3947  N  ND2   . ASN A 1 2031 ? 152.744 155.295 152.252 1.00 23.74  ? 2031 ASN A ND2   1 
ATOM   3948  N  N     . LEU A 1 2032 ? 154.964 156.662 149.789 1.00 19.67  ? 2032 LEU A N     1 
ATOM   3949  C  CA    . LEU A 1 2032 ? 154.686 157.940 149.142 1.00 17.53  ? 2032 LEU A CA    1 
ATOM   3950  C  C     . LEU A 1 2032 ? 155.688 158.233 148.032 1.00 15.63  ? 2032 LEU A C     1 
ATOM   3951  O  O     . LEU A 1 2032 ? 155.322 158.801 146.997 1.00 15.09  ? 2032 LEU A O     1 
ATOM   3952  C  CB    . LEU A 1 2032 ? 154.693 159.064 150.178 1.00 17.51  ? 2032 LEU A CB    1 
ATOM   3953  C  CG    . LEU A 1 2032 ? 154.557 160.495 149.656 1.00 12.78  ? 2032 LEU A CG    1 
ATOM   3954  C  CD1   . LEU A 1 2032 ? 153.204 160.702 148.999 1.00 17.33  ? 2032 LEU A CD1   1 
ATOM   3955  C  CD2   . LEU A 1 2032 ? 154.761 161.490 150.785 1.00 14.42  ? 2032 LEU A CD2   1 
ATOM   3956  N  N     . LYS A 1 2033 ? 156.952 157.855 148.229 1.00 16.16  ? 2033 LYS A N     1 
ATOM   3957  C  CA    . LYS A 1 2033 ? 157.970 158.112 147.216 1.00 13.20  ? 2033 LYS A CA    1 
ATOM   3958  C  C     . LYS A 1 2033 ? 157.708 157.308 145.949 1.00 15.22  ? 2033 LYS A C     1 
ATOM   3959  O  O     . LYS A 1 2033 ? 157.969 157.787 144.839 1.00 22.27  ? 2033 LYS A O     1 
ATOM   3960  C  CB    . LYS A 1 2033 ? 159.357 157.799 147.776 1.00 13.72  ? 2033 LYS A CB    1 
ATOM   3961  C  CG    . LYS A 1 2033 ? 160.000 158.961 148.508 1.00 16.33  ? 2033 LYS A CG    1 
ATOM   3962  C  CD    . LYS A 1 2033 ? 161.481 158.724 148.743 1.00 22.93  ? 2033 LYS A CD    1 
ATOM   3963  C  CE    . LYS A 1 2033 ? 161.709 157.777 149.908 1.00 31.79  ? 2033 LYS A CE    1 
ATOM   3964  N  NZ    . LYS A 1 2033 ? 163.109 157.838 150.409 1.00 34.17  ? 2033 LYS A NZ    1 
ATOM   3965  N  N     . LYS A 1 2034 ? 157.195 156.085 146.092 1.00 16.26  ? 2034 LYS A N     1 
ATOM   3966  C  CA    . LYS A 1 2034 ? 156.901 155.250 144.935 1.00 16.07  ? 2034 LYS A CA    1 
ATOM   3967  C  C     . LYS A 1 2034 ? 155.736 155.776 144.107 1.00 15.52  ? 2034 LYS A C     1 
ATOM   3968  O  O     . LYS A 1 2034 ? 155.548 155.317 142.975 1.00 18.60  ? 2034 LYS A O     1 
ATOM   3969  C  CB    . LYS A 1 2034 ? 156.615 153.816 145.385 1.00 20.08  ? 2034 LYS A CB    1 
ATOM   3970  C  CG    . LYS A 1 2034 ? 155.147 153.520 145.639 1.00 23.93  ? 2034 LYS A CG    1 
ATOM   3971  C  CD    . LYS A 1 2034 ? 154.967 152.172 146.314 1.00 32.36  ? 2034 LYS A CD    1 
ATOM   3972  C  CE    . LYS A 1 2034 ? 153.497 151.836 146.486 1.00 43.37  ? 2034 LYS A CE    1 
ATOM   3973  N  NZ    . LYS A 1 2034 ? 152.834 151.585 145.177 1.00 51.74  ? 2034 LYS A NZ    1 
ATOM   3974  N  N     . LEU A 1 2035 ? 154.958 156.719 144.635 1.00 14.32  ? 2035 LEU A N     1 
ATOM   3975  C  CA    . LEU A 1 2035 ? 153.854 157.315 143.896 1.00 12.85  ? 2035 LEU A CA    1 
ATOM   3976  C  C     . LEU A 1 2035 ? 154.292 158.468 143.003 1.00 13.33  ? 2035 LEU A C     1 
ATOM   3977  O  O     . LEU A 1 2035 ? 153.458 159.018 142.276 1.00 13.76  ? 2035 LEU A O     1 
ATOM   3978  C  CB    . LEU A 1 2035 ? 152.774 157.810 144.864 1.00 13.72  ? 2035 LEU A CB    1 
ATOM   3979  C  CG    . LEU A 1 2035 ? 152.027 156.742 145.663 1.00 18.33  ? 2035 LEU A CG    1 
ATOM   3980  C  CD1   . LEU A 1 2035 ? 151.048 157.387 146.629 1.00 15.13  ? 2035 LEU A CD1   1 
ATOM   3981  C  CD2   . LEU A 1 2035 ? 151.313 155.776 144.734 1.00 22.38  ? 2035 LEU A CD2   1 
ATOM   3982  N  N     . PHE A 1 2036 ? 155.567 158.845 143.040 1.00 14.67  ? 2036 PHE A N     1 
ATOM   3983  C  CA    . PHE A 1 2036 ? 156.086 159.947 142.247 1.00 11.19  ? 2036 PHE A CA    1 
ATOM   3984  C  C     . PHE A 1 2036 ? 157.308 159.489 141.466 1.00 11.44  ? 2036 PHE A C     1 
ATOM   3985  O  O     . PHE A 1 2036 ? 158.017 158.566 141.876 1.00 15.49  ? 2036 PHE A O     1 
ATOM   3986  C  CB    . PHE A 1 2036 ? 156.457 161.151 143.126 1.00 10.46  ? 2036 PHE A CB    1 
ATOM   3987  C  CG    . PHE A 1 2036 ? 155.279 161.808 143.784 1.00 10.73  ? 2036 PHE A CG    1 
ATOM   3988  C  CD1   . PHE A 1 2036 ? 154.841 161.389 145.028 1.00 11.01  ? 2036 PHE A CD1   1 
ATOM   3989  C  CD2   . PHE A 1 2036 ? 154.610 162.846 143.159 1.00 9.82   ? 2036 PHE A CD2   1 
ATOM   3990  C  CE1   . PHE A 1 2036 ? 153.759 161.992 145.635 1.00 10.24  ? 2036 PHE A CE1   1 
ATOM   3991  C  CE2   . PHE A 1 2036 ? 153.527 163.452 143.761 1.00 9.43   ? 2036 PHE A CE2   1 
ATOM   3992  C  CZ    . PHE A 1 2036 ? 153.101 163.024 145.000 1.00 9.59   ? 2036 PHE A CZ    1 
ATOM   3993  N  N     . ARG A 1 2037 ? 157.546 160.143 140.333 1.00 10.20  ? 2037 ARG A N     1 
ATOM   3994  C  CA    . ARG A 1 2037 ? 158.720 159.889 139.507 1.00 10.61  ? 2037 ARG A CA    1 
ATOM   3995  C  C     . ARG A 1 2037 ? 159.724 161.008 139.757 1.00 12.13  ? 2037 ARG A C     1 
ATOM   3996  O  O     . ARG A 1 2037 ? 159.512 162.148 139.332 1.00 14.14  ? 2037 ARG A O     1 
ATOM   3997  C  CB    . ARG A 1 2037 ? 158.342 159.804 138.031 1.00 13.00  ? 2037 ARG A CB    1 
ATOM   3998  C  CG    . ARG A 1 2037 ? 157.982 158.404 137.564 1.00 16.56  ? 2037 ARG A CG    1 
ATOM   3999  C  CD    . ARG A 1 2037 ? 159.219 157.621 137.161 1.00 18.07  ? 2037 ARG A CD    1 
ATOM   4000  N  NE    . ARG A 1 2037 ? 159.597 157.874 135.776 1.00 25.03  ? 2037 ARG A NE    1 
ATOM   4001  C  CZ    . ARG A 1 2037 ? 158.986 157.349 134.723 1.00 29.24  ? 2037 ARG A CZ    1 
ATOM   4002  N  NH1   . ARG A 1 2037 ? 157.959 156.526 134.858 1.00 26.19  ? 2037 ARG A NH1   1 
ATOM   4003  N  NH2   . ARG A 1 2037 ? 159.417 157.657 133.504 1.00 26.98  ? 2037 ARG A NH2   1 
ATOM   4004  N  N     . SER A 1 2038 ? 160.815 160.680 140.443 1.00 13.88  ? 2038 SER A N     1 
ATOM   4005  C  CA    . SER A 1 2038 ? 161.785 161.688 140.839 1.00 14.87  ? 2038 SER A CA    1 
ATOM   4006  C  C     . SER A 1 2038 ? 162.639 162.123 139.652 1.00 14.53  ? 2038 SER A C     1 
ATOM   4007  O  O     . SER A 1 2038 ? 162.730 161.441 138.628 1.00 19.25  ? 2038 SER A O     1 
ATOM   4008  C  CB    . SER A 1 2038 ? 162.679 161.158 141.960 1.00 17.29  ? 2038 SER A CB    1 
ATOM   4009  O  OG    . SER A 1 2038 ? 163.452 160.057 141.518 1.00 20.85  ? 2038 SER A OG    1 
ATOM   4010  N  N     . LEU A 1 2039 ? 163.269 163.286 139.803 1.00 12.07  ? 2039 LEU A N     1 
ATOM   4011  C  CA    . LEU A 1 2039 ? 164.178 163.807 138.790 1.00 13.89  ? 2039 LEU A CA    1 
ATOM   4012  C  C     . LEU A 1 2039 ? 165.156 164.768 139.445 1.00 14.47  ? 2039 LEU A C     1 
ATOM   4013  O  O     . LEU A 1 2039 ? 164.745 165.642 140.213 1.00 15.62  ? 2039 LEU A O     1 
ATOM   4014  C  CB    . LEU A 1 2039 ? 163.419 164.517 137.673 1.00 11.20  ? 2039 LEU A CB    1 
ATOM   4015  C  CG    . LEU A 1 2039 ? 164.338 165.047 136.576 1.00 12.35  ? 2039 LEU A CG    1 
ATOM   4016  C  CD1   . LEU A 1 2039 ? 165.054 163.914 135.860 1.00 14.52  ? 2039 LEU A CD1   1 
ATOM   4017  C  CD2   . LEU A 1 2039 ? 163.548 165.878 135.615 1.00 13.82  ? 2039 LEU A CD2   1 
ATOM   4018  N  N     . ALA A 1 2040 ? 166.437 164.619 139.125 1.00 13.43  ? 2040 ALA A N     1 
ATOM   4019  C  CA    . ALA A 1 2040 ? 167.480 165.461 139.693 1.00 13.17  ? 2040 ALA A CA    1 
ATOM   4020  C  C     . ALA A 1 2040 ? 167.680 166.691 138.815 1.00 19.50  ? 2040 ALA A C     1 
ATOM   4021  O  O     . ALA A 1 2040 ? 168.145 166.579 137.675 1.00 29.06  ? 2040 ALA A O     1 
ATOM   4022  C  CB    . ALA A 1 2040 ? 168.786 164.682 139.831 1.00 16.23  ? 2040 ALA A CB    1 
ATOM   4023  N  N     . MET A 1 2041 ? 167.329 167.858 139.347 1.00 16.49  ? 2041 MET A N     1 
ATOM   4024  C  CA    . MET A 1 2041 ? 167.580 169.143 138.700 1.00 16.76  ? 2041 MET A CA    1 
ATOM   4025  C  C     . MET A 1 2041 ? 168.575 169.895 139.580 1.00 18.73  ? 2041 MET A C     1 
ATOM   4026  O  O     . MET A 1 2041 ? 168.199 170.643 140.482 1.00 24.29  ? 2041 MET A O     1 
ATOM   4027  C  CB    . MET A 1 2041 ? 166.282 169.930 138.505 1.00 14.78  ? 2041 MET A CB    1 
ATOM   4028  C  CG    . MET A 1 2041 ? 165.155 169.127 137.883 1.00 18.10  ? 2041 MET A CG    1 
ATOM   4029  S  SD    . MET A 1 2041 ? 163.816 170.165 137.270 1.00 29.81  ? 2041 MET A SD    1 
ATOM   4030  C  CE    . MET A 1 2041 ? 164.736 171.398 136.354 1.00 15.26  ? 2041 MET A CE    1 
ATOM   4031  N  N     . THR A 1 2042 ? 169.862 169.680 139.313 1.00 19.22  ? 2042 THR A N     1 
ATOM   4032  C  CA    . THR A 1 2042 ? 170.925 170.206 140.161 1.00 23.39  ? 2042 THR A CA    1 
ATOM   4033  C  C     . THR A 1 2042 ? 171.779 171.264 139.478 1.00 27.01  ? 2042 THR A C     1 
ATOM   4034  O  O     . THR A 1 2042 ? 172.226 172.208 140.136 1.00 29.34  ? 2042 THR A O     1 
ATOM   4035  C  CB    . THR A 1 2042 ? 171.827 169.065 140.642 1.00 24.54  ? 2042 THR A CB    1 
ATOM   4036  O  OG1   . THR A 1 2042 ? 172.396 168.394 139.511 1.00 26.66  ? 2042 THR A OG1   1 
ATOM   4037  C  CG2   . THR A 1 2042 ? 171.026 168.067 141.464 1.00 20.90  ? 2042 THR A CG2   1 
ATOM   4038  N  N     . LYS A 1 2043 ? 172.021 171.134 138.177 1.00 23.90  ? 2043 LYS A N     1 
ATOM   4039  C  CA    . LYS A 1 2043 ? 172.893 172.056 137.448 1.00 20.51  ? 2043 LYS A CA    1 
ATOM   4040  C  C     . LYS A 1 2043 ? 172.143 172.661 136.271 1.00 21.91  ? 2043 LYS A C     1 
ATOM   4041  O  O     . LYS A 1 2043 ? 172.151 172.088 135.166 1.00 29.41  ? 2043 LYS A O     1 
ATOM   4042  C  CB    . LYS A 1 2043 ? 174.154 171.341 136.967 1.00 26.23  ? 2043 LYS A CB    1 
ATOM   4043  C  CG    . LYS A 1 2043 ? 174.938 170.655 138.072 1.00 33.94  ? 2043 LYS A CG    1 
ATOM   4044  C  CD    . LYS A 1 2043 ? 176.091 171.522 138.550 1.00 42.98  ? 2043 LYS A CD    1 
ATOM   4045  C  CE    . LYS A 1 2043 ? 176.420 171.249 140.008 1.00 44.85  ? 2043 LYS A CE    1 
ATOM   4046  N  NZ    . LYS A 1 2043 ? 177.322 172.288 140.577 1.00 52.86  ? 2043 LYS A NZ    1 
ATOM   4047  N  N     . PRO A 1 2044 ? 171.482 173.801 136.449 1.00 20.26  ? 2044 PRO A N     1 
ATOM   4048  C  CA    . PRO A 1 2044 ? 170.830 174.456 135.312 1.00 19.45  ? 2044 PRO A CA    1 
ATOM   4049  C  C     . PRO A 1 2044 ? 171.850 174.965 134.308 1.00 21.48  ? 2044 PRO A C     1 
ATOM   4050  O  O     . PRO A 1 2044 ? 172.978 175.322 134.655 1.00 27.74  ? 2044 PRO A O     1 
ATOM   4051  C  CB    . PRO A 1 2044 ? 170.061 175.610 135.964 1.00 15.89  ? 2044 PRO A CB    1 
ATOM   4052  C  CG    . PRO A 1 2044 ? 170.846 175.920 137.190 1.00 16.60  ? 2044 PRO A CG    1 
ATOM   4053  C  CD    . PRO A 1 2044 ? 171.364 174.595 137.684 1.00 20.78  ? 2044 PRO A CD    1 
ATOM   4054  N  N     . ASP A 1 2045 ? 171.438 174.993 133.043 1.00 21.14  ? 2045 ASP A N     1 
ATOM   4055  C  CA    . ASP A 1 2045 ? 172.306 175.430 131.951 1.00 27.26  ? 2045 ASP A CA    1 
ATOM   4056  C  C     . ASP A 1 2045 ? 172.267 176.951 131.897 1.00 24.83  ? 2045 ASP A C     1 
ATOM   4057  O  O     . ASP A 1 2045 ? 171.516 177.552 131.129 1.00 27.31  ? 2045 ASP A O     1 
ATOM   4058  C  CB    . ASP A 1 2045 ? 171.866 174.801 130.636 1.00 34.19  ? 2045 ASP A CB    1 
ATOM   4059  C  CG    . ASP A 1 2045 ? 172.110 173.306 130.600 1.00 47.60  ? 2045 ASP A CG    1 
ATOM   4060  O  OD1   . ASP A 1 2045 ? 173.058 172.842 131.267 1.00 52.91  ? 2045 ASP A OD1   1 
ATOM   4061  O  OD2   . ASP A 1 2045 ? 171.351 172.591 129.914 1.00 43.29  ? 2045 ASP A OD2   1 
ATOM   4062  N  N     . ARG A 1 2046 ? 173.102 177.580 132.728 1.00 22.07  ? 2046 ARG A N     1 
ATOM   4063  C  CA    . ARG A 1 2046 ? 173.050 179.030 132.890 1.00 19.97  ? 2046 ARG A CA    1 
ATOM   4064  C  C     . ARG A 1 2046 ? 173.477 179.758 131.621 1.00 22.03  ? 2046 ARG A C     1 
ATOM   4065  O  O     . ARG A 1 2046 ? 172.928 180.817 131.295 1.00 21.73  ? 2046 ARG A O     1 
ATOM   4066  C  CB    . ARG A 1 2046 ? 173.925 179.453 134.068 1.00 19.75  ? 2046 ARG A CB    1 
ATOM   4067  C  CG    . ARG A 1 2046 ? 173.568 178.773 135.375 1.00 20.00  ? 2046 ARG A CG    1 
ATOM   4068  C  CD    . ARG A 1 2046 ? 174.080 179.564 136.564 1.00 21.40  ? 2046 ARG A CD    1 
ATOM   4069  N  NE    . ARG A 1 2046 ? 173.965 178.810 137.807 1.00 32.49  ? 2046 ARG A NE    1 
ATOM   4070  C  CZ    . ARG A 1 2046 ? 174.776 178.953 138.846 1.00 39.41  ? 2046 ARG A CZ    1 
ATOM   4071  N  NH1   . ARG A 1 2046 ? 175.777 179.818 138.827 1.00 37.69  ? 2046 ARG A NH1   1 
ATOM   4072  N  NH2   . ARG A 1 2046 ? 174.578 178.210 139.931 1.00 39.86  ? 2046 ARG A NH2   1 
ATOM   4073  N  N     . GLN A 1 2047 ? 174.467 179.220 130.904 1.00 22.61  ? 2047 GLN A N     1 
ATOM   4074  C  CA    . GLN A 1 2047 ? 174.981 179.907 129.723 1.00 22.13  ? 2047 GLN A CA    1 
ATOM   4075  C  C     . GLN A 1 2047 ? 173.906 180.039 128.652 1.00 21.24  ? 2047 GLN A C     1 
ATOM   4076  O  O     . GLN A 1 2047 ? 173.737 181.108 128.055 1.00 26.53  ? 2047 GLN A O     1 
ATOM   4077  C  CB    . GLN A 1 2047 ? 176.202 179.168 129.175 1.00 26.15  ? 2047 GLN A CB    1 
ATOM   4078  C  CG    . GLN A 1 2047 ? 177.000 179.965 128.157 1.00 29.43  ? 2047 GLN A CG    1 
ATOM   4079  C  CD    . GLN A 1 2047 ? 176.621 179.633 126.727 1.00 45.17  ? 2047 GLN A CD    1 
ATOM   4080  O  OE1   . GLN A 1 2047 ? 176.393 178.473 126.386 1.00 51.18  ? 2047 GLN A OE1   1 
ATOM   4081  N  NE2   . GLN A 1 2047 ? 176.552 180.655 125.882 1.00 41.45  ? 2047 GLN A NE2   1 
ATOM   4082  N  N     . LEU A 1 2048 ? 173.157 178.956 128.425 1.00 20.83  ? 2048 LEU A N     1 
ATOM   4083  C  CA    . LEU A 1 2048 ? 172.071 178.978 127.409 1.00 18.68  ? 2048 LEU A CA    1 
ATOM   4084  C  C     . LEU A 1 2048 ? 171.023 180.033 127.802 1.00 18.91  ? 2048 LEU A C     1 
ATOM   4085  O  O     . LEU A 1 2048 ? 170.685 180.877 126.946 1.00 21.37  ? 2048 LEU A O     1 
ATOM   4086  C  CB    . LEU A 1 2048 ? 171.446 177.590 127.283 1.00 20.81  ? 2048 LEU A CB    1 
ATOM   4087  C  CG    . LEU A 1 2048 ? 170.269 177.471 126.309 1.00 20.45  ? 2048 LEU A CG    1 
ATOM   4088  C  CD1   . LEU A 1 2048 ? 170.670 177.960 124.929 1.00 22.32  ? 2048 LEU A CD1   1 
ATOM   4089  C  CD2   . LEU A 1 2048 ? 169.763 176.041 126.243 1.00 25.01  ? 2048 LEU A CD2   1 
ATOM   4090  N  N     . ILE A 1 2049 ? 170.538 179.986 129.047 1.00 18.11  ? 2049 ILE A N     1 
ATOM   4091  C  CA    . ILE A 1 2049 ? 169.479 180.938 129.500 1.00 12.71  ? 2049 ILE A CA    1 
ATOM   4092  C  C     . ILE A 1 2049 ? 169.985 182.372 129.288 1.00 14.82  ? 2049 ILE A C     1 
ATOM   4093  O  O     . ILE A 1 2049 ? 169.242 183.179 128.690 1.00 16.49  ? 2049 ILE A O     1 
ATOM   4094  C  CB    . ILE A 1 2049 ? 169.113 180.686 130.974 1.00 13.24  ? 2049 ILE A CB    1 
ATOM   4095  C  CG1   . ILE A 1 2049 ? 168.639 179.251 131.201 1.00 13.39  ? 2049 ILE A CG1   1 
ATOM   4096  C  CG2   . ILE A 1 2049 ? 168.085 181.706 131.463 1.00 14.80  ? 2049 ILE A CG2   1 
ATOM   4097  C  CD1   . ILE A 1 2049 ? 168.339 178.924 132.652 1.00 11.58  ? 2049 ILE A CD1   1 
ATOM   4098  N  N     . ALA A 1 2050 ? 171.204 182.665 129.750 1.00 15.94  ? 2050 ALA A N     1 
ATOM   4099  C  CA    . ALA A 1 2050 ? 171.779 184.022 129.594 1.00 14.69  ? 2050 ALA A CA    1 
ATOM   4100  C  C     . ALA A 1 2050 ? 171.801 184.398 128.113 1.00 16.86  ? 2050 ALA A C     1 
ATOM   4101  O  O     . ALA A 1 2050 ? 171.379 185.524 127.771 1.00 21.13  ? 2050 ALA A O     1 
ATOM   4102  C  CB    . ALA A 1 2050 ? 173.165 184.063 130.195 1.00 16.58  ? 2050 ALA A CB    1 
ATOM   4103  N  N     . GLN A 1 2051 ? 172.268 183.482 127.260 1.00 17.16  ? 2051 GLN A N     1 
ATOM   4104  C  CA    . GLN A 1 2051 ? 172.366 183.771 125.834 1.00 18.13  ? 2051 GLN A CA    1 
ATOM   4105  C  C     . GLN A 1 2051 ? 170.994 184.046 125.233 1.00 16.73  ? 2051 GLN A C     1 
ATOM   4106  O  O     . GLN A 1 2051 ? 170.800 185.046 124.533 1.00 18.57  ? 2051 GLN A O     1 
ATOM   4107  C  CB    . GLN A 1 2051 ? 173.044 182.603 125.118 1.00 23.41  ? 2051 GLN A CB    1 
ATOM   4108  C  CG    . GLN A 1 2051 ? 173.289 182.825 123.638 1.00 32.08  ? 2051 GLN A CG    1 
ATOM   4109  C  CD    . GLN A 1 2051 ? 174.008 181.657 122.993 1.00 48.93  ? 2051 GLN A CD    1 
ATOM   4110  O  OE1   . GLN A 1 2051 ? 175.111 181.293 123.398 1.00 57.35  ? 2051 GLN A OE1   1 
ATOM   4111  N  NE2   . GLN A 1 2051 ? 173.384 181.063 121.983 1.00 56.40  ? 2051 GLN A NE2   1 
ATOM   4112  N  N     . VAL A 1 2052 ? 170.022 183.175 125.514 1.00 17.52  ? 2052 VAL A N     1 
ATOM   4113  C  CA    . VAL A 1 2052 ? 168.694 183.334 124.929 1.00 13.96  ? 2052 VAL A CA    1 
ATOM   4114  C  C     . VAL A 1 2052 ? 167.998 184.564 125.499 1.00 16.58  ? 2052 VAL A C     1 
ATOM   4115  O  O     . VAL A 1 2052 ? 167.308 185.291 124.774 1.00 19.66  ? 2052 VAL A O     1 
ATOM   4116  C  CB    . VAL A 1 2052 ? 167.863 182.057 125.138 1.00 12.46  ? 2052 VAL A CB    1 
ATOM   4117  C  CG1   . VAL A 1 2052 ? 166.434 182.265 124.664 1.00 14.80  ? 2052 VAL A CG1   1 
ATOM   4118  C  CG2   . VAL A 1 2052 ? 168.499 180.892 124.401 1.00 12.31  ? 2052 VAL A CG2   1 
ATOM   4119  N  N     . MET A 1 2053 ? 168.163 184.823 126.799 1.00 15.97  ? 2053 MET A N     1 
ATOM   4120  C  CA    . MET A 1 2053 ? 167.533 185.992 127.400 1.00 16.31  ? 2053 MET A CA    1 
ATOM   4121  C  C     . MET A 1 2053 ? 168.090 187.284 126.818 1.00 20.85  ? 2053 MET A C     1 
ATOM   4122  O  O     . MET A 1 2053 ? 167.335 188.220 126.534 1.00 29.01  ? 2053 MET A O     1 
ATOM   4123  C  CB    . MET A 1 2053 ? 167.716 185.966 128.915 1.00 16.35  ? 2053 MET A CB    1 
ATOM   4124  C  CG    . MET A 1 2053 ? 166.622 185.224 129.652 1.00 18.78  ? 2053 MET A CG    1 
ATOM   4125  S  SD    . MET A 1 2053 ? 166.636 185.594 131.411 1.00 40.73  ? 2053 MET A SD    1 
ATOM   4126  C  CE    . MET A 1 2053 ? 165.600 187.053 131.441 1.00 24.92  ? 2053 MET A CE    1 
ATOM   4127  N  N     . LEU A 1 2054 ? 169.410 187.357 126.636 1.00 17.49  ? 2054 LEU A N     1 
ATOM   4128  C  CA    . LEU A 1 2054 ? 170.000 188.558 126.058 1.00 18.67  ? 2054 LEU A CA    1 
ATOM   4129  C  C     . LEU A 1 2054 ? 169.631 188.702 124.587 1.00 21.53  ? 2054 LEU A C     1 
ATOM   4130  O  O     . LEU A 1 2054 ? 169.407 189.817 124.104 1.00 28.03  ? 2054 LEU A O     1 
ATOM   4131  C  CB    . LEU A 1 2054 ? 171.516 188.535 126.243 1.00 20.64  ? 2054 LEU A CB    1 
ATOM   4132  C  CG    . LEU A 1 2054 ? 171.986 188.747 127.683 1.00 16.60  ? 2054 LEU A CG    1 
ATOM   4133  C  CD1   . LEU A 1 2054 ? 173.493 188.626 127.783 1.00 18.47  ? 2054 LEU A CD1   1 
ATOM   4134  C  CD2   . LEU A 1 2054 ? 171.519 190.095 128.208 1.00 18.63  ? 2054 LEU A CD2   1 
ATOM   4135  N  N     . TYR A 1 2055 ? 169.557 187.585 123.857 1.00 20.88  ? 2055 TYR A N     1 
ATOM   4136  C  CA    . TYR A 1 2055 ? 169.163 187.644 122.454 1.00 20.91  ? 2055 TYR A CA    1 
ATOM   4137  C  C     . TYR A 1 2055 ? 167.724 188.122 122.302 1.00 19.27  ? 2055 TYR A C     1 
ATOM   4138  O  O     . TYR A 1 2055 ? 167.414 188.909 121.400 1.00 21.48  ? 2055 TYR A O     1 
ATOM   4139  C  CB    . TYR A 1 2055 ? 169.346 186.273 121.805 1.00 20.25  ? 2055 TYR A CB    1 
ATOM   4140  C  CG    . TYR A 1 2055 ? 169.192 186.273 120.303 1.00 22.61  ? 2055 TYR A CG    1 
ATOM   4141  C  CD1   . TYR A 1 2055 ? 169.958 187.114 119.508 1.00 22.34  ? 2055 TYR A CD1   1 
ATOM   4142  C  CD2   . TYR A 1 2055 ? 168.282 185.431 119.679 1.00 22.26  ? 2055 TYR A CD2   1 
ATOM   4143  C  CE1   . TYR A 1 2055 ? 169.821 187.117 118.133 1.00 27.21  ? 2055 TYR A CE1   1 
ATOM   4144  C  CE2   . TYR A 1 2055 ? 168.138 185.427 118.306 1.00 23.19  ? 2055 TYR A CE2   1 
ATOM   4145  C  CZ    . TYR A 1 2055 ? 168.910 186.272 117.538 1.00 28.27  ? 2055 TYR A CZ    1 
ATOM   4146  O  OH    . TYR A 1 2055 ? 168.770 186.271 116.170 1.00 32.46  ? 2055 TYR A OH    1 
ATOM   4147  N  N     . SER A 1 2056 ? 166.828 187.656 123.176 1.00 19.21  ? 2056 SER A N     1 
ATOM   4148  C  CA    . SER A 1 2056 ? 165.424 188.033 123.083 1.00 20.36  ? 2056 SER A CA    1 
ATOM   4149  C  C     . SER A 1 2056 ? 165.175 189.471 123.515 1.00 22.72  ? 2056 SER A C     1 
ATOM   4150  O  O     . SER A 1 2056 ? 164.125 190.030 123.184 1.00 24.44  ? 2056 SER A O     1 
ATOM   4151  C  CB    . SER A 1 2056 ? 164.569 187.085 123.926 1.00 19.93  ? 2056 SER A CB    1 
ATOM   4152  O  OG    . SER A 1 2056 ? 164.940 187.143 125.292 1.00 21.69  ? 2056 SER A OG    1 
ATOM   4153  N  N     . GLN A 1 2057 ? 166.108 190.080 124.242 1.00 24.22  ? 2057 GLN A N     1 
ATOM   4154  C  CA    . GLN A 1 2057 ? 165.969 191.461 124.682 1.00 26.26  ? 2057 GLN A CA    1 
ATOM   4155  C  C     . GLN A 1 2057 ? 166.556 192.459 123.694 1.00 28.71  ? 2057 GLN A C     1 
ATOM   4156  O  O     . GLN A 1 2057 ? 166.476 193.667 123.937 1.00 35.30  ? 2057 GLN A O     1 
ATOM   4157  C  CB    . GLN A 1 2057 ? 166.628 191.647 126.052 1.00 25.20  ? 2057 GLN A CB    1 
ATOM   4158  C  CG    . GLN A 1 2057 ? 165.814 191.099 127.212 1.00 25.63  ? 2057 GLN A CG    1 
ATOM   4159  C  CD    . GLN A 1 2057 ? 166.632 190.952 128.478 1.00 36.00  ? 2057 GLN A CD    1 
ATOM   4160  O  OE1   . GLN A 1 2057 ? 167.834 191.215 128.488 1.00 34.75  ? 2057 GLN A OE1   1 
ATOM   4161  N  NE2   . GLN A 1 2057 ? 165.983 190.528 129.556 1.00 34.28  ? 2057 GLN A NE2   1 
ATOM   4162  N  N     . GLY A 1 2058 ? 167.133 191.991 122.591 1.00 25.97  ? 2058 GLY A N     1 
ATOM   4163  C  CA    . GLY A 1 2058 ? 167.725 192.871 121.607 1.00 27.71  ? 2058 GLY A CA    1 
ATOM   4164  C  C     . GLY A 1 2058 ? 169.201 193.138 121.783 1.00 34.53  ? 2058 GLY A C     1 
ATOM   4165  O  O     . GLY A 1 2058 ? 169.735 194.031 121.114 1.00 44.08  ? 2058 GLY A O     1 
ATOM   4166  N  N     . PHE A 1 2059 ? 169.879 192.398 122.657 1.00 30.74  ? 2059 PHE A N     1 
ATOM   4167  C  CA    . PHE A 1 2059 ? 171.305 192.594 122.894 1.00 31.57  ? 2059 PHE A CA    1 
ATOM   4168  C  C     . PHE A 1 2059 ? 172.091 191.956 121.756 1.00 39.43  ? 2059 PHE A C     1 
ATOM   4169  O  O     . PHE A 1 2059 ? 172.135 190.728 121.634 1.00 42.96  ? 2059 PHE A O     1 
ATOM   4170  C  CB    . PHE A 1 2059 ? 171.715 191.990 124.234 1.00 27.29  ? 2059 PHE A CB    1 
ATOM   4171  C  CG    . PHE A 1 2059 ? 171.517 192.909 125.403 1.00 30.99  ? 2059 PHE A CG    1 
ATOM   4172  C  CD1   . PHE A 1 2059 ? 170.262 193.084 125.959 1.00 32.65  ? 2059 PHE A CD1   1 
ATOM   4173  C  CD2   . PHE A 1 2059 ? 172.589 193.590 125.954 1.00 32.45  ? 2059 PHE A CD2   1 
ATOM   4174  C  CE1   . PHE A 1 2059 ? 170.078 193.925 127.038 1.00 34.81  ? 2059 PHE A CE1   1 
ATOM   4175  C  CE2   . PHE A 1 2059 ? 172.411 194.434 127.032 1.00 32.81  ? 2059 PHE A CE2   1 
ATOM   4176  C  CZ    . PHE A 1 2059 ? 171.154 194.601 127.574 1.00 33.01  ? 2059 PHE A CZ    1 
ATOM   4177  N  N     . ARG A 1 2060 ? 172.710 192.784 120.918 1.00 42.64  ? 2060 ARG A N     1 
ATOM   4178  C  CA    . ARG A 1 2060 ? 173.626 192.263 119.915 1.00 44.29  ? 2060 ARG A CA    1 
ATOM   4179  C  C     . ARG A 1 2060 ? 174.860 191.681 120.595 1.00 49.24  ? 2060 ARG A C     1 
ATOM   4180  O  O     . ARG A 1 2060 ? 175.243 192.095 121.692 1.00 50.07  ? 2060 ARG A O     1 
ATOM   4181  C  CB    . ARG A 1 2060 ? 174.030 193.360 118.931 1.00 54.92  ? 2060 ARG A CB    1 
ATOM   4182  C  CG    . ARG A 1 2060 ? 172.889 193.874 118.068 1.00 62.45  ? 2060 ARG A CG    1 
ATOM   4183  C  CD    . ARG A 1 2060 ? 173.123 195.250 117.408 1.00 78.02  ? 2060 ARG A CD    1 
ATOM   4184  N  NE    . ARG A 1 2060 ? 174.380 195.400 116.677 1.00 91.55  ? 2060 ARG A NE    1 
ATOM   4185  C  CZ    . ARG A 1 2060 ? 175.564 195.660 117.218 1.00 91.77  ? 2060 ARG A CZ    1 
ATOM   4186  N  NH1   . ARG A 1 2060 ? 175.698 195.914 118.509 1.00 81.11  ? 2060 ARG A NH1   1 
ATOM   4187  N  NH2   . ARG A 1 2060 ? 176.639 195.697 116.435 1.00 86.12  ? 2060 ARG A NH2   1 
ATOM   4188  N  N     . THR A 1 2061 ? 175.484 190.710 119.926 1.00 53.04  ? 2061 THR A N     1 
ATOM   4189  C  CA    . THR A 1 2061 ? 176.607 189.957 120.491 1.00 57.28  ? 2061 THR A CA    1 
ATOM   4190  C  C     . THR A 1 2061 ? 176.227 189.354 121.841 1.00 49.00  ? 2061 THR A C     1 
ATOM   4191  O  O     . THR A 1 2061 ? 176.991 189.401 122.808 1.00 47.14  ? 2061 THR A O     1 
ATOM   4192  C  CB    . THR A 1 2061 ? 177.866 190.823 120.615 1.00 61.38  ? 2061 THR A CB    1 
ATOM   4193  O  OG1   . THR A 1 2061 ? 177.619 191.923 121.500 1.00 49.17  ? 2061 THR A OG1   1 
ATOM   4194  C  CG2   . THR A 1 2061 ? 178.280 191.359 119.253 1.00 59.03  ? 2061 THR A CG2   1 
ATOM   4195  N  N     . ALA A 1 2062 ? 175.020 188.786 121.905 1.00 44.19  ? 2062 ALA A N     1 
ATOM   4196  C  CA    . ALA A 1 2062 ? 174.524 188.221 123.155 1.00 37.06  ? 2062 ALA A CA    1 
ATOM   4197  C  C     . ALA A 1 2062 ? 175.332 187.005 123.589 1.00 43.01  ? 2062 ALA A C     1 
ATOM   4198  O  O     . ALA A 1 2062 ? 175.469 186.754 124.792 1.00 44.50  ? 2062 ALA A O     1 
ATOM   4199  C  CB    . ALA A 1 2062 ? 173.049 187.852 123.014 1.00 29.21  ? 2062 ALA A CB    1 
ATOM   4200  N  N     . GLU A 1 2063 ? 175.863 186.238 122.634 1.00 43.29  ? 2063 GLU A N     1 
ATOM   4201  C  CA    . GLU A 1 2063 ? 176.663 185.070 122.988 1.00 43.31  ? 2063 GLU A CA    1 
ATOM   4202  C  C     . GLU A 1 2063 ? 177.935 185.473 123.726 1.00 45.92  ? 2063 GLU A C     1 
ATOM   4203  O  O     . GLU A 1 2063 ? 178.322 184.828 124.708 1.00 48.59  ? 2063 GLU A O     1 
ATOM   4204  C  CB    . GLU A 1 2063 ? 176.982 184.253 121.733 1.00 53.96  ? 2063 GLU A CB    1 
ATOM   4205  C  CG    . GLU A 1 2063 ? 177.846 184.965 120.701 1.00 69.27  ? 2063 GLU A CG    1 
ATOM   4206  C  CD    . GLU A 1 2063 ? 178.073 184.135 119.453 1.00 96.29  ? 2063 GLU A CD    1 
ATOM   4207  O  OE1   . GLU A 1 2063 ? 177.537 183.009 119.380 1.00 98.26  ? 2063 GLU A OE1   1 
ATOM   4208  O  OE2   . GLU A 1 2063 ? 178.786 184.609 118.544 1.00 99.13  ? 2063 GLU A OE2   1 
ATOM   4209  N  N     . VAL A 1 2064 ? 178.590 186.548 123.278 1.00 43.17  ? 2064 VAL A N     1 
ATOM   4210  C  CA    . VAL A 1 2064 ? 179.792 187.026 123.956 1.00 42.01  ? 2064 VAL A CA    1 
ATOM   4211  C  C     . VAL A 1 2064 ? 179.453 187.497 125.363 1.00 42.94  ? 2064 VAL A C     1 
ATOM   4212  O  O     . VAL A 1 2064 ? 180.167 187.194 126.328 1.00 47.13  ? 2064 VAL A O     1 
ATOM   4213  C  CB    . VAL A 1 2064 ? 180.461 188.140 123.129 1.00 38.53  ? 2064 VAL A CB    1 
ATOM   4214  C  CG1   . VAL A 1 2064 ? 181.553 188.823 123.936 1.00 40.51  ? 2064 VAL A CG1   1 
ATOM   4215  C  CG2   . VAL A 1 2064 ? 181.021 187.574 121.834 1.00 43.42  ? 2064 VAL A CG2   1 
ATOM   4216  N  N     . LEU A 1 2065 ? 178.349 188.234 125.505 1.00 38.79  ? 2065 LEU A N     1 
ATOM   4217  C  CA    . LEU A 1 2065 ? 177.949 188.721 126.820 1.00 33.36  ? 2065 LEU A CA    1 
ATOM   4218  C  C     . LEU A 1 2065 ? 177.638 187.568 127.766 1.00 34.67  ? 2065 LEU A C     1 
ATOM   4219  O  O     . LEU A 1 2065 ? 178.006 187.611 128.943 1.00 39.63  ? 2065 LEU A O     1 
ATOM   4220  C  CB    . LEU A 1 2065 ? 176.746 189.654 126.690 1.00 31.67  ? 2065 LEU A CB    1 
ATOM   4221  C  CG    . LEU A 1 2065 ? 177.011 191.018 126.051 1.00 33.69  ? 2065 LEU A CG    1 
ATOM   4222  C  CD1   . LEU A 1 2065 ? 175.789 191.912 126.175 1.00 35.82  ? 2065 LEU A CD1   1 
ATOM   4223  C  CD2   . LEU A 1 2065 ? 178.226 191.677 126.681 1.00 36.15  ? 2065 LEU A CD2   1 
ATOM   4224  N  N     . ALA A 1 2066 ? 176.964 186.528 127.272 1.00 33.09  ? 2066 ALA A N     1 
ATOM   4225  C  CA    . ALA A 1 2066 ? 176.653 185.378 128.118 1.00 35.54  ? 2066 ALA A CA    1 
ATOM   4226  C  C     . ALA A 1 2066 ? 177.919 184.626 128.518 1.00 39.45  ? 2066 ALA A C     1 
ATOM   4227  O  O     . ALA A 1 2066 ? 178.105 184.278 129.694 1.00 44.56  ? 2066 ALA A O     1 
ATOM   4228  C  CB    . ALA A 1 2066 ? 175.678 184.448 127.399 1.00 29.07  ? 2066 ALA A CB    1 
ATOM   4229  N  N     . ASN A 1 2067 ? 178.800 184.360 127.548 1.00 38.36  ? 2067 ASN A N     1 
ATOM   4230  C  CA    . ASN A 1 2067 ? 180.054 183.670 127.822 1.00 43.41  ? 2067 ASN A CA    1 
ATOM   4231  C  C     . ASN A 1 2067 ? 181.001 184.496 128.679 1.00 48.70  ? 2067 ASN A C     1 
ATOM   4232  O  O     . ASN A 1 2067 ? 181.982 183.948 129.191 1.00 53.63  ? 2067 ASN A O     1 
ATOM   4233  C  CB    . ASN A 1 2067 ? 180.747 183.292 126.511 1.00 47.43  ? 2067 ASN A CB    1 
ATOM   4234  C  CG    . ASN A 1 2067 ? 180.016 182.198 125.759 1.00 49.60  ? 2067 ASN A CG    1 
ATOM   4235  O  OD1   . ASN A 1 2067 ? 179.697 182.345 124.580 1.00 51.78  ? 2067 ASN A OD1   1 
ATOM   4236  N  ND2   . ASN A 1 2067 ? 179.748 181.090 126.440 1.00 44.53  ? 2067 ASN A ND2   1 
ATOM   4237  N  N     . LYS A 1 2068 ? 180.752 185.796 128.819 1.00 41.89  ? 2068 LYS A N     1 
ATOM   4238  C  CA    . LYS A 1 2068 ? 181.519 186.606 129.756 1.00 36.66  ? 2068 LYS A CA    1 
ATOM   4239  C  C     . LYS A 1 2068 ? 180.857 186.688 131.127 1.00 39.15  ? 2068 LYS A C     1 
ATOM   4240  O  O     . LYS A 1 2068 ? 181.554 186.755 132.144 1.00 43.45  ? 2068 LYS A O     1 
ATOM   4241  C  CB    . LYS A 1 2068 ? 181.716 188.015 129.192 1.00 34.32  ? 2068 LYS A CB    1 
ATOM   4242  C  CG    . LYS A 1 2068 ? 182.799 188.118 128.132 1.00 37.99  ? 2068 LYS A CG    1 
ATOM   4243  C  CD    . LYS A 1 2068 ? 182.930 189.541 127.618 1.00 42.06  ? 2068 LYS A CD    1 
ATOM   4244  C  CE    . LYS A 1 2068 ? 184.241 189.743 126.879 1.00 47.16  ? 2068 LYS A CE    1 
ATOM   4245  N  NZ    . LYS A 1 2068 ? 185.413 189.404 127.732 1.00 45.47  ? 2068 LYS A NZ    1 
ATOM   4246  N  N     . ILE A 1 2069 ? 179.527 186.667 131.179 1.00 36.97  ? 2069 ILE A N     1 
ATOM   4247  C  CA    . ILE A 1 2069 ? 178.831 186.931 132.432 1.00 33.27  ? 2069 ILE A CA    1 
ATOM   4248  C  C     . ILE A 1 2069 ? 178.607 185.669 133.264 1.00 35.21  ? 2069 ILE A C     1 
ATOM   4249  O  O     . ILE A 1 2069 ? 178.528 185.754 134.493 1.00 38.44  ? 2069 ILE A O     1 
ATOM   4250  C  CB    . ILE A 1 2069 ? 177.500 187.656 132.153 1.00 29.16  ? 2069 ILE A CB    1 
ATOM   4251  C  CG1   . ILE A 1 2069 ? 177.003 188.366 133.413 1.00 35.03  ? 2069 ILE A CG1   1 
ATOM   4252  C  CG2   . ILE A 1 2069 ? 176.445 186.690 131.635 1.00 29.93  ? 2069 ILE A CG2   1 
ATOM   4253  C  CD1   . ILE A 1 2069 ? 177.938 189.442 133.915 1.00 30.58  ? 2069 ILE A CD1   1 
ATOM   4254  N  N     . VAL A 1 2070 ? 178.507 184.498 132.640 1.00 35.49  ? 2070 VAL A N     1 
ATOM   4255  C  CA    . VAL A 1 2070 ? 178.323 183.274 133.422 1.00 35.32  ? 2070 VAL A CA    1 
ATOM   4256  C  C     . VAL A 1 2070 ? 179.629 182.911 134.130 1.00 38.19  ? 2070 VAL A C     1 
ATOM   4257  O  O     . VAL A 1 2070 ? 179.617 182.675 135.352 1.00 35.86  ? 2070 VAL A O     1 
ATOM   4258  C  CB    . VAL A 1 2070 ? 177.799 182.121 132.549 1.00 30.41  ? 2070 VAL A CB    1 
ATOM   4259  C  CG1   . VAL A 1 2070 ? 177.752 180.830 133.349 1.00 30.56  ? 2070 VAL A CG1   1 
ATOM   4260  C  CG2   . VAL A 1 2070 ? 176.425 182.461 131.999 1.00 26.96  ? 2070 VAL A CG2   1 
ATOM   4261  N  N     . PRO A 1 2071 ? 180.775 182.853 133.435 1.00 38.49  ? 2071 PRO A N     1 
ATOM   4262  C  CA    . PRO A 1 2071 ? 182.035 182.654 134.166 1.00 37.50  ? 2071 PRO A CA    1 
ATOM   4263  C  C     . PRO A 1 2071 ? 182.308 183.740 135.184 1.00 38.93  ? 2071 PRO A C     1 
ATOM   4264  O  O     . PRO A 1 2071 ? 182.917 183.457 136.219 1.00 45.84  ? 2071 PRO A O     1 
ATOM   4265  C  CB    . PRO A 1 2071 ? 183.091 182.642 133.052 1.00 37.55  ? 2071 PRO A CB    1 
ATOM   4266  C  CG    . PRO A 1 2071 ? 182.351 182.216 131.850 1.00 41.15  ? 2071 PRO A CG    1 
ATOM   4267  C  CD    . PRO A 1 2071 ? 181.013 182.869 131.980 1.00 36.37  ? 2071 PRO A CD    1 
ATOM   4268  N  N     . PHE A 1 2072 ? 181.879 184.978 134.925 1.00 32.07  ? 2072 PHE A N     1 
ATOM   4269  C  CA    . PHE A 1 2072 ? 182.050 186.040 135.911 1.00 29.51  ? 2072 PHE A CA    1 
ATOM   4270  C  C     . PHE A 1 2072 ? 181.296 185.723 137.196 1.00 32.07  ? 2072 PHE A C     1 
ATOM   4271  O  O     . PHE A 1 2072 ? 181.813 185.937 138.299 1.00 36.61  ? 2072 PHE A O     1 
ATOM   4272  C  CB    . PHE A 1 2072 ? 181.585 187.374 135.332 1.00 32.69  ? 2072 PHE A CB    1 
ATOM   4273  C  CG    . PHE A 1 2072 ? 181.350 188.434 136.367 1.00 34.73  ? 2072 PHE A CG    1 
ATOM   4274  C  CD1   . PHE A 1 2072 ? 182.416 189.075 136.974 1.00 36.57  ? 2072 PHE A CD1   1 
ATOM   4275  C  CD2   . PHE A 1 2072 ? 180.064 188.788 136.734 1.00 32.64  ? 2072 PHE A CD2   1 
ATOM   4276  C  CE1   . PHE A 1 2072 ? 182.202 190.051 137.927 1.00 33.21  ? 2072 PHE A CE1   1 
ATOM   4277  C  CE2   . PHE A 1 2072 ? 179.843 189.761 137.686 1.00 33.98  ? 2072 PHE A CE2   1 
ATOM   4278  C  CZ    . PHE A 1 2072 ? 180.913 190.395 138.282 1.00 33.22  ? 2072 PHE A CZ    1 
ATOM   4279  N  N     . PHE A 1 2073 ? 180.068 185.214 137.074 1.00 35.47  ? 2073 PHE A N     1 
ATOM   4280  C  CA    . PHE A 1 2073 ? 179.325 184.796 138.258 1.00 33.34  ? 2073 PHE A CA    1 
ATOM   4281  C  C     . PHE A 1 2073 ? 180.015 183.632 138.955 1.00 35.34  ? 2073 PHE A C     1 
ATOM   4282  O  O     . PHE A 1 2073 ? 180.027 183.560 140.191 1.00 39.40  ? 2073 PHE A O     1 
ATOM   4283  C  CB    . PHE A 1 2073 ? 177.893 184.425 137.877 1.00 32.04  ? 2073 PHE A CB    1 
ATOM   4284  C  CG    . PHE A 1 2073 ? 176.918 185.556 138.025 1.00 26.51  ? 2073 PHE A CG    1 
ATOM   4285  C  CD1   . PHE A 1 2073 ? 176.839 186.549 137.066 1.00 26.13  ? 2073 PHE A CD1   1 
ATOM   4286  C  CD2   . PHE A 1 2073 ? 176.086 185.628 139.128 1.00 27.91  ? 2073 PHE A CD2   1 
ATOM   4287  C  CE1   . PHE A 1 2073 ? 175.945 187.591 137.202 1.00 27.41  ? 2073 PHE A CE1   1 
ATOM   4288  C  CE2   . PHE A 1 2073 ? 175.191 186.667 139.269 1.00 27.65  ? 2073 PHE A CE2   1 
ATOM   4289  C  CZ    . PHE A 1 2073 ? 175.121 187.649 138.305 1.00 29.04  ? 2073 PHE A CZ    1 
ATOM   4290  N  N     . LYS A 1 2074 ? 180.597 182.711 138.182 1.00 37.49  ? 2074 LYS A N     1 
ATOM   4291  C  CA    . LYS A 1 2074 ? 181.349 181.620 138.798 1.00 36.80  ? 2074 LYS A CA    1 
ATOM   4292  C  C     . LYS A 1 2074 ? 182.530 182.151 139.608 1.00 41.34  ? 2074 LYS A C     1 
ATOM   4293  O  O     . LYS A 1 2074 ? 182.775 181.699 140.734 1.00 44.71  ? 2074 LYS A O     1 
ATOM   4294  C  CB    . LYS A 1 2074 ? 181.825 180.642 137.724 1.00 37.59  ? 2074 LYS A CB    1 
ATOM   4295  C  CG    . LYS A 1 2074 ? 182.523 179.408 138.267 1.00 47.88  ? 2074 LYS A CG    1 
ATOM   4296  C  CD    . LYS A 1 2074 ? 182.101 178.163 137.504 1.00 51.42  ? 2074 LYS A CD    1 
ATOM   4297  C  CE    . LYS A 1 2074 ? 182.445 176.896 138.270 1.00 54.88  ? 2074 LYS A CE    1 
ATOM   4298  N  NZ    . LYS A 1 2074 ? 183.914 176.733 138.447 1.00 60.76  ? 2074 LYS A NZ    1 
ATOM   4299  N  N     . LEU A 1 2075 ? 183.263 183.121 139.056 1.00 39.64  ? 2075 LEU A N     1 
ATOM   4300  C  CA    . LEU A 1 2075 ? 184.385 183.711 139.784 1.00 33.97  ? 2075 LEU A CA    1 
ATOM   4301  C  C     . LEU A 1 2075 ? 183.915 184.466 141.019 1.00 37.52  ? 2075 LEU A C     1 
ATOM   4302  O  O     . LEU A 1 2075 ? 184.592 184.458 142.050 1.00 43.25  ? 2075 LEU A O     1 
ATOM   4303  C  CB    . LEU A 1 2075 ? 185.193 184.645 138.887 1.00 31.34  ? 2075 LEU A CB    1 
ATOM   4304  C  CG    . LEU A 1 2075 ? 185.509 184.269 137.447 1.00 40.69  ? 2075 LEU A CG    1 
ATOM   4305  C  CD1   . LEU A 1 2075 ? 186.294 185.390 136.804 1.00 37.78  ? 2075 LEU A CD1   1 
ATOM   4306  C  CD2   . LEU A 1 2075 ? 186.280 182.962 137.405 1.00 46.71  ? 2075 LEU A CD2   1 
ATOM   4307  N  N     . CYS A 1 2076 ? 182.777 185.153 140.928 1.00 38.99  ? 2076 CYS A N     1 
ATOM   4308  C  CA    . CYS A 1 2076 ? 182.245 185.825 142.110 1.00 32.98  ? 2076 CYS A CA    1 
ATOM   4309  C  C     . CYS A 1 2076 ? 181.896 184.818 143.197 1.00 34.35  ? 2076 CYS A C     1 
ATOM   4310  O  O     . CYS A 1 2076 ? 182.138 185.064 144.385 1.00 36.88  ? 2076 CYS A O     1 
ATOM   4311  C  CB    . CYS A 1 2076 ? 181.025 186.665 141.741 1.00 29.10  ? 2076 CYS A CB    1 
ATOM   4312  S  SG    . CYS A 1 2076 ? 181.400 188.065 140.678 1.00 44.41  ? 2076 CYS A SG    1 
ATOM   4313  N  N     . ASP A 1 2077 ? 181.323 183.678 142.809 1.00 35.82  ? 2077 ASP A N     1 
ATOM   4314  C  CA    . ASP A 1 2077 ? 181.016 182.635 143.783 1.00 37.68  ? 2077 ASP A CA    1 
ATOM   4315  C  C     . ASP A 1 2077 ? 182.285 182.072 144.413 1.00 44.11  ? 2077 ASP A C     1 
ATOM   4316  O  O     . ASP A 1 2077 ? 182.326 181.813 145.622 1.00 49.78  ? 2077 ASP A O     1 
ATOM   4317  C  CB    . ASP A 1 2077 ? 180.209 181.522 143.116 1.00 42.48  ? 2077 ASP A CB    1 
ATOM   4318  C  CG    . ASP A 1 2077 ? 179.371 180.734 144.103 1.00 52.79  ? 2077 ASP A CG    1 
ATOM   4319  O  OD1   . ASP A 1 2077 ? 179.706 180.730 145.305 1.00 58.50  ? 2077 ASP A OD1   1 
ATOM   4320  O  OD2   . ASP A 1 2077 ? 178.374 180.116 143.674 1.00 52.60  ? 2077 ASP A OD2   1 
ATOM   4321  N  N     . GLU A 1 2078 ? 183.332 181.879 143.611 1.00 50.38  ? 2078 GLU A N     1 
ATOM   4322  C  CA    . GLU A 1 2078 ? 184.505 181.144 144.078 1.00 49.20  ? 2078 GLU A CA    1 
ATOM   4323  C  C     . GLU A 1 2078 ? 185.497 182.049 144.804 1.00 46.00  ? 2078 GLU A C     1 
ATOM   4324  O  O     . GLU A 1 2078 ? 185.837 181.813 145.968 1.00 50.13  ? 2078 GLU A O     1 
ATOM   4325  C  CB    . GLU A 1 2078 ? 185.181 180.459 142.889 1.00 47.58  ? 2078 GLU A CB    1 
ATOM   4326  C  CG    . GLU A 1 2078 ? 184.309 179.416 142.215 1.00 56.01  ? 2078 GLU A CG    1 
ATOM   4327  C  CD    . GLU A 1 2078 ? 185.085 178.518 141.280 1.00 69.71  ? 2078 GLU A CD    1 
ATOM   4328  O  OE1   . GLU A 1 2078 ? 185.926 179.035 140.516 1.00 72.63  ? 2078 GLU A OE1   1 
ATOM   4329  O  OE2   . GLU A 1 2078 ? 184.830 177.299 141.289 1.00 73.49  ? 2078 GLU A OE2   1 
ATOM   4330  N  N     . GLN A 1 2079 ? 185.971 183.093 144.123 1.00 44.67  ? 2079 GLN A N     1 
ATOM   4331  C  CA    . GLN A 1 2079 ? 187.096 183.890 144.597 1.00 47.70  ? 2079 GLN A CA    1 
ATOM   4332  C  C     . GLN A 1 2079 ? 186.720 184.790 145.770 1.00 53.05  ? 2079 GLN A C     1 
ATOM   4333  O  O     . GLN A 1 2079 ? 187.533 184.997 146.677 1.00 62.08  ? 2079 GLN A O     1 
ATOM   4334  C  CB    . GLN A 1 2079 ? 187.648 184.725 143.441 1.00 41.41  ? 2079 GLN A CB    1 
ATOM   4335  C  CG    . GLN A 1 2079 ? 189.123 185.049 143.541 1.00 56.81  ? 2079 GLN A CG    1 
ATOM   4336  C  CD    . GLN A 1 2079 ? 189.673 185.609 142.245 1.00 71.95  ? 2079 GLN A CD    1 
ATOM   4337  O  OE1   . GLN A 1 2079 ? 189.717 186.823 142.051 1.00 88.58  ? 2079 GLN A OE1   1 
ATOM   4338  N  NE2   . GLN A 1 2079 ? 190.091 184.724 141.348 1.00 64.58  ? 2079 GLN A NE2   1 
ATOM   4339  N  N     . LEU A 1 2080 ? 185.508 185.341 145.769 1.00 51.39  ? 2080 LEU A N     1 
ATOM   4340  C  CA    . LEU A 1 2080 ? 185.103 186.253 146.829 1.00 44.49  ? 2080 LEU A CA    1 
ATOM   4341  C  C     . LEU A 1 2080 ? 184.989 185.522 148.162 1.00 49.79  ? 2080 LEU A C     1 
ATOM   4342  O  O     . LEU A 1 2080 ? 184.811 184.302 148.217 1.00 53.16  ? 2080 LEU A O     1 
ATOM   4343  C  CB    . LEU A 1 2080 ? 183.773 186.924 146.485 1.00 39.78  ? 2080 LEU A CB    1 
ATOM   4344  C  CG    . LEU A 1 2080 ? 183.770 187.908 145.313 1.00 40.73  ? 2080 LEU A CG    1 
ATOM   4345  C  CD1   . LEU A 1 2080 ? 182.529 188.784 145.357 1.00 35.13  ? 2080 LEU A CD1   1 
ATOM   4346  C  CD2   . LEU A 1 2080 ? 185.027 188.761 145.319 1.00 37.68  ? 2080 LEU A CD2   1 
ATOM   4347  N  N     . SER A 1 2081 ? 185.100 186.287 149.246 1.00 45.39  ? 2081 SER A N     1 
ATOM   4348  C  CA    . SER A 1 2081 ? 185.065 185.710 150.582 1.00 45.51  ? 2081 SER A CA    1 
ATOM   4349  C  C     . SER A 1 2081 ? 183.703 185.086 150.864 1.00 44.18  ? 2081 SER A C     1 
ATOM   4350  O  O     . SER A 1 2081 ? 182.672 185.525 150.348 1.00 50.25  ? 2081 SER A O     1 
ATOM   4351  C  CB    . SER A 1 2081 ? 185.381 186.776 151.630 1.00 42.81  ? 2081 SER A CB    1 
ATOM   4352  O  OG    . SER A 1 2081 ? 184.452 187.844 151.566 1.00 44.36  ? 2081 SER A OG    1 
ATOM   4353  N  N     . SER A 1 2082 ? 183.708 184.048 151.695 1.00 37.68  ? 2082 SER A N     1 
ATOM   4354  C  CA    . SER A 1 2082 ? 182.493 183.303 152.007 1.00 38.64  ? 2082 SER A CA    1 
ATOM   4355  C  C     . SER A 1 2082 ? 181.678 184.079 153.034 1.00 40.55  ? 2082 SER A C     1 
ATOM   4356  O  O     . SER A 1 2082 ? 182.105 184.245 154.182 1.00 46.86  ? 2082 SER A O     1 
ATOM   4357  C  CB    . SER A 1 2082 ? 182.841 181.909 152.522 1.00 47.49  ? 2082 SER A CB    1 
ATOM   4358  O  OG    . SER A 1 2082 ? 181.673 181.183 152.858 1.00 51.00  ? 2082 SER A OG    1 
ATOM   4359  N  N     . GLN A 1 2083 ? 180.506 184.556 152.623 1.00 38.51  ? 2083 GLN A N     1 
ATOM   4360  C  CA    . GLN A 1 2083 ? 179.585 185.255 153.505 1.00 32.40  ? 2083 GLN A CA    1 
ATOM   4361  C  C     . GLN A 1 2083 ? 178.214 184.603 153.419 1.00 28.89  ? 2083 GLN A C     1 
ATOM   4362  O  O     . GLN A 1 2083 ? 177.832 184.057 152.381 1.00 30.15  ? 2083 GLN A O     1 
ATOM   4363  C  CB    . GLN A 1 2083 ? 179.485 186.745 153.156 1.00 28.40  ? 2083 GLN A CB    1 
ATOM   4364  C  CG    . GLN A 1 2083 ? 180.823 187.465 153.128 1.00 36.43  ? 2083 GLN A CG    1 
ATOM   4365  C  CD    . GLN A 1 2083 ? 181.299 187.864 154.509 1.00 47.17  ? 2083 GLN A CD    1 
ATOM   4366  O  OE1   . GLN A 1 2083 ? 180.505 187.978 155.443 1.00 47.25  ? 2083 GLN A OE1   1 
ATOM   4367  N  NE2   . GLN A 1 2083 ? 182.602 188.077 154.647 1.00 54.36  ? 2083 GLN A NE2   1 
ATOM   4368  N  N     . SER A 1 2084 ? 177.475 184.665 154.528 1.00 29.54  ? 2084 SER A N     1 
ATOM   4369  C  CA    . SER A 1 2084 ? 176.188 183.984 154.606 1.00 28.47  ? 2084 SER A CA    1 
ATOM   4370  C  C     . SER A 1 2084 ? 175.118 184.641 153.745 1.00 28.16  ? 2084 SER A C     1 
ATOM   4371  O  O     . SER A 1 2084 ? 174.106 183.999 153.445 1.00 35.55  ? 2084 SER A O     1 
ATOM   4372  C  CB    . SER A 1 2084 ? 175.716 183.922 156.059 1.00 27.96  ? 2084 SER A CB    1 
ATOM   4373  O  OG    . SER A 1 2084 ? 175.636 185.219 156.625 1.00 35.79  ? 2084 SER A OG    1 
ATOM   4374  N  N     . HIS A 1 2085 ? 175.310 185.896 153.342 1.00 23.09  ? 2085 HIS A N     1 
ATOM   4375  C  CA    . HIS A 1 2085 ? 174.321 186.614 152.549 1.00 21.66  ? 2085 HIS A CA    1 
ATOM   4376  C  C     . HIS A 1 2085 ? 174.690 186.697 151.073 1.00 26.28  ? 2085 HIS A C     1 
ATOM   4377  O  O     . HIS A 1 2085 ? 173.973 187.345 150.304 1.00 31.97  ? 2085 HIS A O     1 
ATOM   4378  C  CB    . HIS A 1 2085 ? 174.108 188.020 153.116 1.00 20.09  ? 2085 HIS A CB    1 
ATOM   4379  C  CG    . HIS A 1 2085 ? 175.334 188.878 153.088 1.00 20.05  ? 2085 HIS A CG    1 
ATOM   4380  N  ND1   . HIS A 1 2085 ? 176.379 188.714 153.971 1.00 24.99  ? 2085 HIS A ND1   1 
ATOM   4381  C  CD2   . HIS A 1 2085 ? 175.678 189.913 152.286 1.00 19.81  ? 2085 HIS A CD2   1 
ATOM   4382  C  CE1   . HIS A 1 2085 ? 177.316 189.608 153.712 1.00 26.03  ? 2085 HIS A CE1   1 
ATOM   4383  N  NE2   . HIS A 1 2085 ? 176.915 190.348 152.695 1.00 22.31  ? 2085 HIS A NE2   1 
ATOM   4384  N  N     . TYR A 1 2086 ? 175.781 186.060 150.658 1.00 23.64  ? 2086 TYR A N     1 
ATOM   4385  C  CA    . TYR A 1 2086 ? 176.172 186.038 149.255 1.00 22.68  ? 2086 TYR A CA    1 
ATOM   4386  C  C     . TYR A 1 2086 ? 175.387 184.970 148.507 1.00 30.89  ? 2086 TYR A C     1 
ATOM   4387  O  O     . TYR A 1 2086 ? 175.245 183.841 148.988 1.00 34.85  ? 2086 TYR A O     1 
ATOM   4388  C  CB    . TYR A 1 2086 ? 177.672 185.782 149.103 1.00 24.14  ? 2086 TYR A CB    1 
ATOM   4389  C  CG    . TYR A 1 2086 ? 178.542 186.986 149.373 1.00 26.38  ? 2086 TYR A CG    1 
ATOM   4390  C  CD1   . TYR A 1 2086 ? 177.987 188.247 149.535 1.00 24.22  ? 2086 TYR A CD1   1 
ATOM   4391  C  CD2   . TYR A 1 2086 ? 179.923 186.865 149.442 1.00 28.18  ? 2086 TYR A CD2   1 
ATOM   4392  C  CE1   . TYR A 1 2086 ? 178.782 189.350 149.774 1.00 27.23  ? 2086 TYR A CE1   1 
ATOM   4393  C  CE2   . TYR A 1 2086 ? 180.725 187.962 149.678 1.00 29.10  ? 2086 TYR A CE2   1 
ATOM   4394  C  CZ    . TYR A 1 2086 ? 180.149 189.201 149.844 1.00 31.17  ? 2086 TYR A CZ    1 
ATOM   4395  O  OH    . TYR A 1 2086 ? 180.946 190.297 150.080 1.00 39.36  ? 2086 TYR A OH    1 
ATOM   4396  N  N     . ASP A 1 2087 ? 174.880 185.332 147.331 1.00 32.69  ? 2087 ASP A N     1 
ATOM   4397  C  CA    . ASP A 1 2087 ? 174.203 184.391 146.447 1.00 28.72  ? 2087 ASP A CA    1 
ATOM   4398  C  C     . ASP A 1 2087 ? 174.547 184.752 145.012 1.00 29.76  ? 2087 ASP A C     1 
ATOM   4399  O  O     . ASP A 1 2087 ? 174.193 185.837 144.542 1.00 32.28  ? 2087 ASP A O     1 
ATOM   4400  C  CB    . ASP A 1 2087 ? 172.688 184.412 146.657 1.00 31.01  ? 2087 ASP A CB    1 
ATOM   4401  C  CG    . ASP A 1 2087 ? 171.950 183.583 145.626 1.00 39.37  ? 2087 ASP A CG    1 
ATOM   4402  O  OD1   . ASP A 1 2087 ? 172.094 182.343 145.647 1.00 36.09  ? 2087 ASP A OD1   1 
ATOM   4403  O  OD2   . ASP A 1 2087 ? 171.230 184.170 144.791 1.00 39.98  ? 2087 ASP A OD2   1 
ATOM   4404  N  N     . PHE A 1 2088 ? 175.232 183.846 144.323 1.00 30.84  ? 2088 PHE A N     1 
ATOM   4405  C  CA    . PHE A 1 2088 ? 175.633 184.033 142.935 1.00 29.30  ? 2088 PHE A CA    1 
ATOM   4406  C  C     . PHE A 1 2088 ? 175.093 182.904 142.074 1.00 32.87  ? 2088 PHE A C     1 
ATOM   4407  O  O     . PHE A 1 2088 ? 175.777 182.386 141.187 1.00 41.20  ? 2088 PHE A O     1 
ATOM   4408  C  CB    . PHE A 1 2088 ? 177.152 184.133 142.819 1.00 28.67  ? 2088 PHE A CB    1 
ATOM   4409  C  CG    . PHE A 1 2088 ? 177.750 185.227 143.656 1.00 30.90  ? 2088 PHE A CG    1 
ATOM   4410  C  CD1   . PHE A 1 2088 ? 177.537 186.557 143.337 1.00 29.98  ? 2088 PHE A CD1   1 
ATOM   4411  C  CD2   . PHE A 1 2088 ? 178.512 184.927 144.772 1.00 30.55  ? 2088 PHE A CD2   1 
ATOM   4412  C  CE1   . PHE A 1 2088 ? 178.083 187.565 144.107 1.00 28.02  ? 2088 PHE A CE1   1 
ATOM   4413  C  CE2   . PHE A 1 2088 ? 179.059 185.930 145.546 1.00 28.58  ? 2088 PHE A CE2   1 
ATOM   4414  C  CZ    . PHE A 1 2088 ? 178.844 187.251 145.213 1.00 27.35  ? 2088 PHE A CZ    1 
ATOM   4415  N  N     . GLY A 1 2089 ? 173.832 182.531 142.318 1.00 27.60  ? 2089 GLY A N     1 
ATOM   4416  C  CA    . GLY A 1 2089 ? 173.219 181.417 141.568 1.00 24.30  ? 2089 GLY A CA    1 
ATOM   4417  C  C     . GLY A 1 2089 ? 172.450 181.898 140.353 1.00 25.17  ? 2089 GLY A C     1 
ATOM   4418  O  O     . GLY A 1 2089 ? 172.719 183.028 139.893 1.00 27.72  ? 2089 GLY A O     1 
ATOM   4419  N  N     . LEU A 1 2090 ? 171.527 181.074 139.847 1.00 21.63  ? 2090 LEU A N     1 
ATOM   4420  C  CA    . LEU A 1 2090 ? 170.749 181.427 138.629 1.00 16.86  ? 2090 LEU A CA    1 
ATOM   4421  C  C     . LEU A 1 2090 ? 169.861 182.650 138.910 1.00 18.32  ? 2090 LEU A C     1 
ATOM   4422  O  O     . LEU A 1 2090 ? 169.748 183.511 138.015 1.00 23.87  ? 2090 LEU A O     1 
ATOM   4423  C  CB    . LEU A 1 2090 ? 169.918 180.230 138.171 1.00 17.34  ? 2090 LEU A CB    1 
ATOM   4424  C  CG    . LEU A 1 2090 ? 169.040 180.458 136.937 1.00 15.50  ? 2090 LEU A CG    1 
ATOM   4425  C  CD1   . LEU A 1 2090 ? 169.878 180.920 135.757 1.00 16.89  ? 2090 LEU A CD1   1 
ATOM   4426  C  CD2   . LEU A 1 2090 ? 168.274 179.195 136.585 1.00 14.88  ? 2090 LEU A CD2   1 
ATOM   4427  N  N     . ARG A 1 2091 ? 169.255 182.715 140.099 1.00 17.72  ? 2091 ARG A N     1 
ATOM   4428  C  CA    . ARG A 1 2091 ? 168.338 183.839 140.426 1.00 17.25  ? 2091 ARG A CA    1 
ATOM   4429  C  C     . ARG A 1 2091 ? 169.100 185.167 140.295 1.00 24.07  ? 2091 ARG A C     1 
ATOM   4430  O  O     . ARG A 1 2091 ? 168.532 186.122 139.722 1.00 30.37  ? 2091 ARG A O     1 
ATOM   4431  C  CB    . ARG A 1 2091 ? 167.752 183.688 141.835 1.00 16.52  ? 2091 ARG A CB    1 
ATOM   4432  C  CG    . ARG A 1 2091 ? 166.659 182.636 141.950 1.00 21.87  ? 2091 ARG A CG    1 
ATOM   4433  C  CD    . ARG A 1 2091 ? 165.938 182.719 143.285 1.00 20.17  ? 2091 ARG A CD    1 
ATOM   4434  N  NE    . ARG A 1 2091 ? 164.761 181.844 143.339 1.00 25.39  ? 2091 ARG A NE    1 
ATOM   4435  C  CZ    . ARG A 1 2091 ? 164.587 180.870 144.221 1.00 24.25  ? 2091 ARG A CZ    1 
ATOM   4436  N  NH1   . ARG A 1 2091 ? 165.501 180.647 145.149 1.00 24.58  ? 2091 ARG A NH1   1 
ATOM   4437  N  NH2   . ARG A 1 2091 ? 163.500 180.122 144.173 1.00 21.88  ? 2091 ARG A NH2   1 
ATOM   4438  N  N     . ALA A 1 2092 ? 170.337 185.218 140.800 1.00 21.98  ? 2092 ALA A N     1 
ATOM   4439  C  CA    . ALA A 1 2092 ? 171.149 186.455 140.719 1.00 20.46  ? 2092 ALA A CA    1 
ATOM   4440  C  C     . ALA A 1 2092 ? 171.387 186.815 139.251 1.00 21.02  ? 2092 ALA A C     1 
ATOM   4441  O  O     . ALA A 1 2092 ? 171.174 187.987 138.874 1.00 25.65  ? 2092 ALA A O     1 
ATOM   4442  C  CB    . ALA A 1 2092 ? 172.451 186.264 141.462 1.00 28.64  ? 2092 ALA A CB    1 
ATOM   4443  N  N     . LEU A 1 2093 ? 171.802 185.835 138.445 1.00 18.81  ? 2093 LEU A N     1 
ATOM   4444  C  CA    . LEU A 1 2093 ? 172.042 186.081 136.999 1.00 18.41  ? 2093 LEU A CA    1 
ATOM   4445  C  C     . LEU A 1 2093 ? 170.718 186.495 136.340 1.00 20.44  ? 2093 LEU A C     1 
ATOM   4446  O  O     . LEU A 1 2093 ? 170.734 187.433 135.515 1.00 25.75  ? 2093 LEU A O     1 
ATOM   4447  C  CB    . LEU A 1 2093 ? 172.626 184.830 136.346 1.00 19.31  ? 2093 LEU A CB    1 
ATOM   4448  C  CG    . LEU A 1 2093 ? 172.914 184.933 134.845 1.00 23.64  ? 2093 LEU A CG    1 
ATOM   4449  C  CD1   . LEU A 1 2093 ? 173.889 186.063 134.561 1.00 25.88  ? 2093 LEU A CD1   1 
ATOM   4450  C  CD2   . LEU A 1 2093 ? 173.447 183.617 134.304 1.00 25.59  ? 2093 LEU A CD2   1 
ATOM   4451  N  N     . LYS A 1 2094 ? 169.620 185.827 136.702 1.00 21.53  ? 2094 LYS A N     1 
ATOM   4452  C  CA    . LYS A 1 2094 ? 168.293 186.142 136.114 1.00 20.93  ? 2094 LYS A CA    1 
ATOM   4453  C  C     . LYS A 1 2094 ? 167.955 187.610 136.409 1.00 21.39  ? 2094 LYS A C     1 
ATOM   4454  O  O     . LYS A 1 2094 ? 167.543 188.324 135.469 1.00 25.82  ? 2094 LYS A O     1 
ATOM   4455  C  CB    . LYS A 1 2094 ? 167.239 185.199 136.703 1.00 20.04  ? 2094 LYS A CB    1 
ATOM   4456  C  CG    . LYS A 1 2094 ? 165.852 185.293 136.086 1.00 25.60  ? 2094 LYS A CG    1 
ATOM   4457  C  CD    . LYS A 1 2094 ? 165.806 184.785 134.650 1.00 24.36  ? 2094 LYS A CD    1 
ATOM   4458  C  CE    . LYS A 1 2094 ? 164.430 184.856 134.067 1.00 30.21  ? 2094 LYS A CE    1 
ATOM   4459  N  NZ    . LYS A 1 2094 ? 163.475 184.055 134.836 1.00 26.14  ? 2094 LYS A NZ    1 
ATOM   4460  N  N     . SER A 1 2095 ? 168.136 188.039 137.662 1.00 19.28  ? 2095 SER A N     1 
ATOM   4461  C  CA    . SER A 1 2095 ? 167.861 189.449 138.040 1.00 21.85  ? 2095 SER A CA    1 
ATOM   4462  C  C     . SER A 1 2095 ? 168.810 190.373 137.267 1.00 22.47  ? 2095 SER A C     1 
ATOM   4463  O  O     . SER A 1 2095 ? 168.362 191.453 136.828 1.00 23.93  ? 2095 SER A O     1 
ATOM   4464  C  CB    . SER A 1 2095 ? 167.994 189.651 139.526 1.00 26.16  ? 2095 SER A CB    1 
ATOM   4465  O  OG    . SER A 1 2095 ? 169.321 189.383 139.958 1.00 25.24  ? 2095 SER A OG    1 
ATOM   4466  N  N     . VAL A 1 2096 ? 170.070 189.960 137.112 1.00 21.60  ? 2096 VAL A N     1 
ATOM   4467  C  CA    . VAL A 1 2096 ? 171.033 190.764 136.365 1.00 19.85  ? 2096 VAL A CA    1 
ATOM   4468  C  C     . VAL A 1 2096 ? 170.597 190.907 134.912 1.00 22.21  ? 2096 VAL A C     1 
ATOM   4469  O  O     . VAL A 1 2096 ? 170.696 191.988 134.325 1.00 28.23  ? 2096 VAL A O     1 
ATOM   4470  C  CB    . VAL A 1 2096 ? 172.443 190.157 136.483 1.00 21.60  ? 2096 VAL A CB    1 
ATOM   4471  C  CG1   . VAL A 1 2096 ? 173.360 190.714 135.407 1.00 22.63  ? 2096 VAL A CG1   1 
ATOM   4472  C  CG2   . VAL A 1 2096 ? 173.017 190.434 137.860 1.00 25.42  ? 2096 VAL A CG2   1 
ATOM   4473  N  N     . LEU A 1 2097 ? 170.098 189.825 134.312 1.00 21.43  ? 2097 LEU A N     1 
ATOM   4474  C  CA    . LEU A 1 2097 ? 169.682 189.884 132.912 1.00 19.22  ? 2097 LEU A CA    1 
ATOM   4475  C  C     . LEU A 1 2097 ? 168.451 190.766 132.724 1.00 21.83  ? 2097 LEU A C     1 
ATOM   4476  O  O     . LEU A 1 2097 ? 168.390 191.563 131.776 1.00 26.74  ? 2097 LEU A O     1 
ATOM   4477  C  CB    . LEU A 1 2097 ? 169.420 188.475 132.381 1.00 16.80  ? 2097 LEU A CB    1 
ATOM   4478  C  CG    . LEU A 1 2097 ? 170.622 187.531 132.374 1.00 16.19  ? 2097 LEU A CG    1 
ATOM   4479  C  CD1   . LEU A 1 2097 ? 170.181 186.104 132.108 1.00 16.62  ? 2097 LEU A CD1   1 
ATOM   4480  C  CD2   . LEU A 1 2097 ? 171.656 187.978 131.354 1.00 20.13  ? 2097 LEU A CD2   1 
ATOM   4481  N  N     . VAL A 1 2098 ? 167.455 190.641 133.605 1.00 21.27  ? 2098 VAL A N     1 
ATOM   4482  C  CA    . VAL A 1 2098 ? 166.271 191.486 133.465 1.00 21.96  ? 2098 VAL A CA    1 
ATOM   4483  C  C     . VAL A 1 2098 ? 166.625 192.947 133.730 1.00 27.16  ? 2098 VAL A C     1 
ATOM   4484  O  O     . VAL A 1 2098 ? 166.099 193.858 133.075 1.00 35.75  ? 2098 VAL A O     1 
ATOM   4485  C  CB    . VAL A 1 2098 ? 165.124 190.990 134.369 1.00 20.51  ? 2098 VAL A CB    1 
ATOM   4486  C  CG1   . VAL A 1 2098 ? 164.783 189.543 134.046 1.00 20.23  ? 2098 VAL A CG1   1 
ATOM   4487  C  CG2   . VAL A 1 2098 ? 165.463 191.143 135.839 1.00 23.88  ? 2098 VAL A CG2   1 
ATOM   4488  N  N     . SER A 1 2099 ? 167.543 193.196 134.669 1.00 22.61  ? 2099 SER A N     1 
ATOM   4489  C  CA    . SER A 1 2099 ? 168.010 194.556 134.902 1.00 24.23  ? 2099 SER A CA    1 
ATOM   4490  C  C     . SER A 1 2099 ? 168.772 195.089 133.697 1.00 27.92  ? 2099 SER A C     1 
ATOM   4491  O  O     . SER A 1 2099 ? 168.684 196.277 133.382 1.00 33.48  ? 2099 SER A O     1 
ATOM   4492  C  CB    . SER A 1 2099 ? 168.882 194.605 136.156 1.00 27.34  ? 2099 SER A CB    1 
ATOM   4493  O  OG    . SER A 1 2099 ? 169.564 195.843 136.254 1.00 39.81  ? 2099 SER A OG    1 
ATOM   4494  N  N     . ALA A 1 2100 ? 169.532 194.228 133.016 1.00 24.87  ? 2100 ALA A N     1 
ATOM   4495  C  CA    . ALA A 1 2100 ? 170.230 194.649 131.806 1.00 23.59  ? 2100 ALA A CA    1 
ATOM   4496  C  C     . ALA A 1 2100 ? 169.245 195.036 130.714 1.00 25.58  ? 2100 ALA A C     1 
ATOM   4497  O  O     . ALA A 1 2100 ? 169.436 196.043 130.024 1.00 33.95  ? 2100 ALA A O     1 
ATOM   4498  C  CB    . ALA A 1 2100 ? 171.162 193.539 131.323 1.00 20.56  ? 2100 ALA A CB    1 
ATOM   4499  N  N     . GLY A 1 2101 ? 168.183 194.248 130.546 1.00 23.49  ? 2101 GLY A N     1 
ATOM   4500  C  CA    . GLY A 1 2101 ? 167.157 194.614 129.581 1.00 27.37  ? 2101 GLY A CA    1 
ATOM   4501  C  C     . GLY A 1 2101 ? 166.503 195.943 129.913 1.00 34.01  ? 2101 GLY A C     1 
ATOM   4502  O  O     . GLY A 1 2101 ? 166.328 196.805 129.042 1.00 40.38  ? 2101 GLY A O     1 
ATOM   4503  N  N     . ASN A 1 2102 ? 166.150 196.134 131.188 1.00 33.04  ? 2102 ASN A N     1 
ATOM   4504  C  CA    . ASN A 1 2102 ? 165.537 197.392 131.604 1.00 31.71  ? 2102 ASN A CA    1 
ATOM   4505  C  C     . ASN A 1 2102 ? 166.484 198.569 131.398 1.00 33.69  ? 2102 ASN A C     1 
ATOM   4506  O  O     . ASN A 1 2102 ? 166.068 199.634 130.927 1.00 42.32  ? 2102 ASN A O     1 
ATOM   4507  C  CB    . ASN A 1 2102 ? 165.102 197.305 133.066 1.00 34.04  ? 2102 ASN A CB    1 
ATOM   4508  C  CG    . ASN A 1 2102 ? 163.877 196.435 133.258 1.00 42.47  ? 2102 ASN A CG    1 
ATOM   4509  O  OD1   . ASN A 1 2102 ? 163.200 196.076 132.296 1.00 43.53  ? 2102 ASN A OD1   1 
ATOM   4510  N  ND2   . ASN A 1 2102 ? 163.586 196.091 134.507 1.00 41.97  ? 2102 ASN A ND2   1 
ATOM   4511  N  N     . VAL A 1 2103 ? 167.761 198.396 131.746 1.00 31.72  ? 2103 VAL A N     1 
ATOM   4512  C  CA    . VAL A 1 2103 ? 168.738 199.470 131.604 1.00 34.24  ? 2103 VAL A CA    1 
ATOM   4513  C  C     . VAL A 1 2103 ? 168.939 199.815 130.136 1.00 41.86  ? 2103 VAL A C     1 
ATOM   4514  O  O     . VAL A 1 2103 ? 169.063 200.990 129.773 1.00 48.46  ? 2103 VAL A O     1 
ATOM   4515  C  CB    . VAL A 1 2103 ? 170.063 199.079 132.287 1.00 27.09  ? 2103 VAL A CB    1 
ATOM   4516  C  CG1   . VAL A 1 2103 ? 171.202 199.959 131.799 1.00 32.55  ? 2103 VAL A CG1   1 
ATOM   4517  C  CG2   . VAL A 1 2103 ? 169.928 199.180 133.797 1.00 34.83  ? 2103 VAL A CG2   1 
ATOM   4518  N  N     . LYS A 1 2104 ? 168.977 198.801 129.268 1.00 40.01  ? 2104 LYS A N     1 
ATOM   4519  C  CA    . LYS A 1 2104 ? 169.091 199.069 127.840 1.00 36.30  ? 2104 LYS A CA    1 
ATOM   4520  C  C     . LYS A 1 2104 ? 167.885 199.844 127.330 1.00 41.19  ? 2104 LYS A C     1 
ATOM   4521  O  O     . LYS A 1 2104 ? 168.032 200.780 126.535 1.00 50.27  ? 2104 LYS A O     1 
ATOM   4522  C  CB    . LYS A 1 2104 ? 169.254 197.763 127.065 1.00 33.95  ? 2104 LYS A CB    1 
ATOM   4523  C  CG    . LYS A 1 2104 ? 169.726 197.964 125.636 1.00 38.70  ? 2104 LYS A CG    1 
ATOM   4524  C  CD    . LYS A 1 2104 ? 169.767 196.658 124.865 1.00 36.02  ? 2104 LYS A CD    1 
ATOM   4525  C  CE    . LYS A 1 2104 ? 168.372 196.211 124.471 1.00 37.37  ? 2104 LYS A CE    1 
ATOM   4526  N  NZ    . LYS A 1 2104 ? 167.732 197.164 123.522 1.00 42.10  ? 2104 LYS A NZ    1 
ATOM   4527  N  N     . ARG A 1 2105 ? 166.681 199.476 127.779 1.00 39.05  ? 2105 ARG A N     1 
ATOM   4528  C  CA    . ARG A 1 2105 ? 165.492 200.213 127.354 1.00 41.83  ? 2105 ARG A CA    1 
ATOM   4529  C  C     . ARG A 1 2105 ? 165.535 201.663 127.827 1.00 50.74  ? 2105 ARG A C     1 
ATOM   4530  O  O     . ARG A 1 2105 ? 165.210 202.585 127.065 1.00 60.93  ? 2105 ARG A O     1 
ATOM   4531  C  CB    . ARG A 1 2105 ? 164.231 199.514 127.861 1.00 40.68  ? 2105 ARG A CB    1 
ATOM   4532  C  CG    . ARG A 1 2105 ? 163.709 198.438 126.922 1.00 37.25  ? 2105 ARG A CG    1 
ATOM   4533  C  CD    . ARG A 1 2105 ? 162.350 197.921 127.363 1.00 43.43  ? 2105 ARG A CD    1 
ATOM   4534  N  NE    . ARG A 1 2105 ? 162.450 197.027 128.511 1.00 42.27  ? 2105 ARG A NE    1 
ATOM   4535  C  CZ    . ARG A 1 2105 ? 162.823 195.757 128.442 1.00 46.05  ? 2105 ARG A CZ    1 
ATOM   4536  N  NH1   . ARG A 1 2105 ? 163.138 195.190 127.288 1.00 46.81  ? 2105 ARG A NH1   1 
ATOM   4537  N  NH2   . ARG A 1 2105 ? 162.880 195.036 129.558 1.00 48.74  ? 2105 ARG A NH2   1 
ATOM   4538  N  N     . GLU A 1 2106 ? 165.941 201.889 129.081 1.00 52.35  ? 2106 GLU A N     1 
ATOM   4539  C  CA    . GLU A 1 2106 ? 166.031 203.256 129.589 1.00 54.40  ? 2106 GLU A CA    1 
ATOM   4540  C  C     . GLU A 1 2106 ? 167.093 204.057 128.846 1.00 55.04  ? 2106 GLU A C     1 
ATOM   4541  O  O     . GLU A 1 2106 ? 166.908 205.250 128.584 1.00 62.21  ? 2106 GLU A O     1 
ATOM   4542  C  CB    . GLU A 1 2106 ? 166.314 203.260 131.094 1.00 49.65  ? 2106 GLU A CB    1 
ATOM   4543  C  CG    . GLU A 1 2106 ? 165.386 202.403 131.961 1.00 52.60  ? 2106 GLU A CG    1 
ATOM   4544  C  CD    . GLU A 1 2106 ? 163.928 202.404 131.518 1.00 63.22  ? 2106 GLU A CD    1 
ATOM   4545  O  OE1   . GLU A 1 2106 ? 163.263 201.361 131.689 1.00 70.36  ? 2106 GLU A OE1   1 
ATOM   4546  O  OE2   . GLU A 1 2106 ? 163.425 203.451 131.055 1.00 66.21  ? 2106 GLU A OE2   1 
ATOM   4547  N  N     . ARG A 1 2107 ? 168.220 203.425 128.511 1.00 47.39  ? 2107 ARG A N     1 
ATOM   4548  C  CA    . ARG A 1 2107 ? 169.255 204.118 127.750 1.00 50.38  ? 2107 ARG A CA    1 
ATOM   4549  C  C     . ARG A 1 2107 ? 168.766 204.473 126.351 1.00 55.70  ? 2107 ARG A C     1 
ATOM   4550  O  O     . ARG A 1 2107 ? 169.071 205.556 125.838 1.00 65.00  ? 2107 ARG A O     1 
ATOM   4551  C  CB    . ARG A 1 2107 ? 170.519 203.263 127.681 1.00 49.33  ? 2107 ARG A CB    1 
ATOM   4552  C  CG    . ARG A 1 2107 ? 171.741 204.011 127.179 1.00 57.21  ? 2107 ARG A CG    1 
ATOM   4553  C  CD    . ARG A 1 2107 ? 173.022 203.402 127.722 1.00 62.92  ? 2107 ARG A CD    1 
ATOM   4554  N  NE    . ARG A 1 2107 ? 172.984 203.260 129.173 1.00 56.49  ? 2107 ARG A NE    1 
ATOM   4555  C  CZ    . ARG A 1 2107 ? 174.052 203.072 129.935 1.00 55.47  ? 2107 ARG A CZ    1 
ATOM   4556  N  NH1   . ARG A 1 2107 ? 175.267 203.003 129.418 1.00 59.55  ? 2107 ARG A NH1   1 
ATOM   4557  N  NH2   . ARG A 1 2107 ? 173.897 202.952 131.251 1.00 50.44  ? 2107 ARG A NH2   1 
ATOM   4558  N  N     . ILE A 1 2108 ? 168.009 203.572 125.719 1.00 53.74  ? 2108 ILE A N     1 
ATOM   4559  C  CA    . ILE A 1 2108 ? 167.425 203.874 124.415 1.00 55.91  ? 2108 ILE A CA    1 
ATOM   4560  C  C     . ILE A 1 2108 ? 166.488 205.070 124.523 1.00 57.85  ? 2108 ILE A C     1 
ATOM   4561  O  O     . ILE A 1 2108 ? 166.511 205.981 123.686 1.00 64.66  ? 2108 ILE A O     1 
ATOM   4562  C  CB    . ILE A 1 2108 ? 166.700 202.639 123.849 1.00 57.26  ? 2108 ILE A CB    1 
ATOM   4563  C  CG1   . ILE A 1 2108 ? 167.698 201.521 123.537 1.00 54.40  ? 2108 ILE A CG1   1 
ATOM   4564  C  CG2   . ILE A 1 2108 ? 165.898 203.009 122.609 1.00 62.84  ? 2108 ILE A CG2   1 
ATOM   4565  C  CD1   . ILE A 1 2108 ? 168.478 201.727 122.263 1.00 62.54  ? 2108 ILE A CD1   1 
ATOM   4566  N  N     . GLN A 1 2109 ? 165.650 205.086 125.563 1.00 57.34  ? 2109 GLN A N     1 
ATOM   4567  C  CA    . GLN A 1 2109 ? 164.731 206.206 125.755 1.00 61.82  ? 2109 GLN A CA    1 
ATOM   4568  C  C     . GLN A 1 2109 ? 165.484 207.511 125.992 1.00 69.78  ? 2109 GLN A C     1 
ATOM   4569  O  O     . GLN A 1 2109 ? 165.097 208.566 125.472 1.00 74.08  ? 2109 GLN A O     1 
ATOM   4570  C  CB    . GLN A 1 2109 ? 163.784 205.913 126.918 1.00 62.35  ? 2109 GLN A CB    1 
ATOM   4571  C  CG    . GLN A 1 2109 ? 162.372 206.436 126.716 1.00 63.54  ? 2109 GLN A CG    1 
ATOM   4572  C  CD    . GLN A 1 2109 ? 161.576 205.600 125.734 1.00 72.69  ? 2109 GLN A CD    1 
ATOM   4573  O  OE1   . GLN A 1 2109 ? 161.920 204.451 125.457 1.00 79.85  ? 2109 GLN A OE1   1 
ATOM   4574  N  NE2   . GLN A 1 2109 ? 160.504 206.174 125.201 1.00 71.79  ? 2109 GLN A NE2   1 
ATOM   4575  N  N     . LYS A 1 2110 ? 166.558 207.462 126.785 1.00 66.79  ? 2110 LYS A N     1 
ATOM   4576  C  CA    . LYS A 1 2110 ? 167.341 208.663 127.057 1.00 65.29  ? 2110 LYS A CA    1 
ATOM   4577  C  C     . LYS A 1 2110 ? 168.014 209.186 125.795 1.00 69.57  ? 2110 LYS A C     1 
ATOM   4578  O  O     . LYS A 1 2110 ? 168.039 210.398 125.552 1.00 74.09  ? 2110 LYS A O     1 
ATOM   4579  C  CB    . LYS A 1 2110 ? 168.381 208.375 128.140 1.00 65.90  ? 2110 LYS A CB    1 
ATOM   4580  C  CG    . LYS A 1 2110 ? 169.016 209.619 128.739 1.00 71.15  ? 2110 LYS A CG    1 
ATOM   4581  C  CD    . LYS A 1 2110 ? 170.365 209.303 129.364 1.00 72.89  ? 2110 LYS A CD    1 
ATOM   4582  C  CE    . LYS A 1 2110 ? 171.341 208.768 128.328 1.00 74.21  ? 2110 LYS A CE    1 
ATOM   4583  N  NZ    . LYS A 1 2110 ? 172.423 207.960 128.952 1.00 73.85  ? 2110 LYS A NZ    1 
ATOM   4584  N  N     . ILE A 1 2111 ? 168.572 208.288 124.980 1.00 70.41  ? 2111 ILE A N     1 
ATOM   4585  C  CA    . ILE A 1 2111 ? 169.176 208.709 123.720 1.00 72.71  ? 2111 ILE A CA    1 
ATOM   4586  C  C     . ILE A 1 2111 ? 168.119 209.304 122.797 1.00 77.14  ? 2111 ILE A C     1 
ATOM   4587  O  O     . ILE A 1 2111 ? 168.366 210.303 122.109 1.00 84.03  ? 2111 ILE A O     1 
ATOM   4588  C  CB    . ILE A 1 2111 ? 169.913 207.530 123.060 1.00 72.90  ? 2111 ILE A CB    1 
ATOM   4589  C  CG1   . ILE A 1 2111 ? 171.126 207.124 123.899 1.00 71.62  ? 2111 ILE A CG1   1 
ATOM   4590  C  CG2   . ILE A 1 2111 ? 170.348 207.887 121.646 1.00 70.23  ? 2111 ILE A CG2   1 
ATOM   4591  C  CD1   . ILE A 1 2111 ? 171.915 205.975 123.313 1.00 74.37  ? 2111 ILE A CD1   1 
ATOM   4592  N  N     . LYS A 1 2112 ? 166.925 208.706 122.770 1.00 78.16  ? 2112 LYS A N     1 
ATOM   4593  C  CA    . LYS A 1 2112 ? 165.844 209.239 121.949 1.00 78.93  ? 2112 LYS A CA    1 
ATOM   4594  C  C     . LYS A 1 2112 ? 165.460 210.646 122.389 1.00 83.69  ? 2112 LYS A C     1 
ATOM   4595  O  O     . LYS A 1 2112 ? 165.276 211.540 121.557 1.00 89.57  ? 2112 LYS A O     1 
ATOM   4596  C  CB    . LYS A 1 2112 ? 164.633 208.307 122.008 1.00 80.65  ? 2112 LYS A CB    1 
ATOM   4597  C  CG    . LYS A 1 2112 ? 164.549 207.318 120.858 1.00 85.60  ? 2112 LYS A CG    1 
ATOM   4598  C  CD    . LYS A 1 2112 ? 163.124 206.826 120.665 1.00 91.34  ? 2112 LYS A CD    1 
ATOM   4599  C  CE    . LYS A 1 2112 ? 162.926 206.225 119.283 1.00 102.98 ? 2112 LYS A CE    1 
ATOM   4600  N  NZ    . LYS A 1 2112 ? 161.496 206.245 118.868 1.00 93.21  ? 2112 LYS A NZ    1 
ATOM   4601  N  N     . ARG A 1 2113 ? 165.342 210.867 123.701 1.00 84.85  ? 2113 ARG A N     1 
ATOM   4602  C  CA    . ARG A 1 2113 ? 164.968 212.196 124.176 1.00 86.72  ? 2113 ARG A CA    1 
ATOM   4603  C  C     . ARG A 1 2113 ? 166.087 213.210 123.949 1.00 94.20  ? 2113 ARG A C     1 
ATOM   4604  O  O     . ARG A 1 2113 ? 165.809 214.386 123.683 1.00 99.43  ? 2113 ARG A O     1 
ATOM   4605  C  CB    . ARG A 1 2113 ? 164.562 212.145 125.653 1.00 77.09  ? 2113 ARG A CB    1 
ATOM   4606  C  CG    . ARG A 1 2113 ? 165.703 212.219 126.654 1.00 80.05  ? 2113 ARG A CG    1 
ATOM   4607  C  CD    . ARG A 1 2113 ? 165.198 212.628 128.030 1.00 77.94  ? 2113 ARG A CD    1 
ATOM   4608  N  NE    . ARG A 1 2113 ? 166.139 212.280 129.088 1.00 79.19  ? 2113 ARG A NE    1 
ATOM   4609  C  CZ    . ARG A 1 2113 ? 165.937 211.324 129.985 1.00 78.44  ? 2113 ARG A CZ    1 
ATOM   4610  N  NH1   . ARG A 1 2113 ? 164.835 210.591 129.978 1.00 76.80  ? 2113 ARG A NH1   1 
ATOM   4611  N  NH2   . ARG A 1 2113 ? 166.863 211.098 130.912 1.00 76.46  ? 2113 ARG A NH2   1 
ATOM   4612  N  N     . GLU A 1 2114 ? 167.349 212.779 124.036 1.00 95.42  ? 2114 GLU A N     1 
ATOM   4613  C  CA    . GLU A 1 2114 ? 168.460 213.677 123.738 1.00 94.63  ? 2114 GLU A CA    1 
ATOM   4614  C  C     . GLU A 1 2114 ? 168.449 214.082 122.269 1.00 99.95  ? 2114 GLU A C     1 
ATOM   4615  O  O     . GLU A 1 2114 ? 168.652 215.254 121.932 1.00 104.24 ? 2114 GLU A O     1 
ATOM   4616  C  CB    . GLU A 1 2114 ? 169.787 213.013 124.115 1.00 93.89  ? 2114 GLU A CB    1 
ATOM   4617  C  CG    . GLU A 1 2114 ? 171.037 213.813 123.752 1.00 104.35 ? 2114 GLU A CG    1 
ATOM   4618  C  CD    . GLU A 1 2114 ? 171.501 213.583 122.324 1.00 109.34 ? 2114 GLU A CD    1 
ATOM   4619  O  OE1   . GLU A 1 2114 ? 171.317 212.459 121.811 1.00 101.73 ? 2114 GLU A OE1   1 
ATOM   4620  O  OE2   . GLU A 1 2114 ? 172.045 214.528 121.715 1.00 114.29 ? 2114 GLU A OE2   1 
ATOM   4621  N  N     . LYS A 1 2115 ? 168.219 213.117 121.375 1.00 100.02 ? 2115 LYS A N     1 
ATOM   4622  C  CA    . LYS A 1 2115 ? 168.102 213.429 119.957 1.00 101.55 ? 2115 LYS A CA    1 
ATOM   4623  C  C     . LYS A 1 2115 ? 166.858 214.255 119.655 1.00 101.65 ? 2115 LYS A C     1 
ATOM   4624  O  O     . LYS A 1 2115 ? 166.829 214.968 118.648 1.00 108.89 ? 2115 LYS A O     1 
ATOM   4625  C  CB    . LYS A 1 2115 ? 168.088 212.140 119.135 1.00 99.23  ? 2115 LYS A CB    1 
ATOM   4626  C  CG    . LYS A 1 2115 ? 169.447 211.471 119.010 1.00 94.86  ? 2115 LYS A CG    1 
ATOM   4627  C  CD    . LYS A 1 2115 ? 169.529 210.610 117.762 1.00 91.53  ? 2115 LYS A CD    1 
ATOM   4628  C  CE    . LYS A 1 2115 ? 170.811 209.793 117.736 1.00 82.46  ? 2115 LYS A CE    1 
ATOM   4629  N  NZ    . LYS A 1 2115 ? 171.973 210.563 118.261 1.00 85.23  ? 2115 LYS A NZ    1 
ATOM   4630  N  N     . GLU A 1 2116 ? 165.828 214.157 120.497 1.00 98.12  ? 2116 GLU A N     1 
ATOM   4631  C  CA    . GLU A 1 2116 ? 164.648 214.996 120.326 1.00 105.21 ? 2116 GLU A CA    1 
ATOM   4632  C  C     . GLU A 1 2116 ? 164.936 216.442 120.713 1.00 109.91 ? 2116 GLU A C     1 
ATOM   4633  O  O     . GLU A 1 2116 ? 164.555 217.371 119.990 1.00 110.66 ? 2116 GLU A O     1 
ATOM   4634  C  CB    . GLU A 1 2116 ? 163.490 214.438 121.153 1.00 105.22 ? 2116 GLU A CB    1 
ATOM   4635  C  CG    . GLU A 1 2116 ? 162.291 215.362 121.260 1.00 109.33 ? 2116 GLU A CG    1 
ATOM   4636  C  CD    . GLU A 1 2116 ? 161.245 214.842 122.226 1.00 116.44 ? 2116 GLU A CD    1 
ATOM   4637  O  OE1   . GLU A 1 2116 ? 160.600 213.819 121.912 1.00 123.66 ? 2116 GLU A OE1   1 
ATOM   4638  O  OE2   . GLU A 1 2116 ? 161.068 215.454 123.300 1.00 119.58 ? 2116 GLU A OE2   1 
ATOM   4639  N  N     . GLU A 1 2117 ? 165.611 216.655 121.846 1.00 110.56 ? 2117 GLU A N     1 
ATOM   4640  C  CA    . GLU A 1 2117 ? 165.900 218.018 122.281 1.00 109.88 ? 2117 GLU A CA    1 
ATOM   4641  C  C     . GLU A 1 2117 ? 167.013 218.664 121.466 1.00 112.46 ? 2117 GLU A C     1 
ATOM   4642  O  O     . GLU A 1 2117 ? 167.105 219.896 121.436 1.00 110.41 ? 2117 GLU A O     1 
ATOM   4643  C  CB    . GLU A 1 2117 ? 166.251 218.038 123.772 1.00 105.33 ? 2117 GLU A CB    1 
ATOM   4644  C  CG    . GLU A 1 2117 ? 167.486 217.234 124.159 1.00 110.70 ? 2117 GLU A CG    1 
ATOM   4645  C  CD    . GLU A 1 2117 ? 168.774 218.030 124.039 1.00 110.07 ? 2117 GLU A CD    1 
ATOM   4646  O  OE1   . GLU A 1 2117 ? 168.705 219.277 124.020 1.00 111.12 ? 2117 GLU A OE1   1 
ATOM   4647  O  OE2   . GLU A 1 2117 ? 169.854 217.409 123.966 1.00 106.67 ? 2117 GLU A OE2   1 
ATOM   4648  N  N     . ARG A 1 2118 ? 167.857 217.868 120.810 1.00 112.48 ? 2118 ARG A N     1 
ATOM   4649  C  CA    . ARG A 1 2118 ? 168.934 218.378 119.967 1.00 111.01 ? 2118 ARG A CA    1 
ATOM   4650  C  C     . ARG A 1 2118 ? 168.817 217.721 118.599 1.00 116.79 ? 2118 ARG A C     1 
ATOM   4651  O  O     . ARG A 1 2118 ? 169.085 216.524 118.457 1.00 119.95 ? 2118 ARG A O     1 
ATOM   4652  C  CB    . ARG A 1 2118 ? 170.304 218.104 120.588 1.00 111.31 ? 2118 ARG A CB    1 
ATOM   4653  C  CG    . ARG A 1 2118 ? 171.464 218.261 119.618 1.00 113.31 ? 2118 ARG A CG    1 
ATOM   4654  C  CD    . ARG A 1 2118 ? 172.690 217.499 120.088 1.00 115.32 ? 2118 ARG A CD    1 
ATOM   4655  N  NE    . ARG A 1 2118 ? 173.567 217.148 118.978 1.00 126.40 ? 2118 ARG A NE    1 
ATOM   4656  C  CZ    . ARG A 1 2118 ? 173.753 215.914 118.530 1.00 122.94 ? 2118 ARG A CZ    1 
ATOM   4657  N  NH1   . ARG A 1 2118 ? 173.135 214.880 119.078 1.00 122.45 ? 2118 ARG A NH1   1 
ATOM   4658  N  NH2   . ARG A 1 2118 ? 174.578 215.712 117.507 1.00 113.21 ? 2118 ARG A NH2   1 
ATOM   4659  N  N     . GLY A 1 2119 ? 168.425 218.499 117.596 1.00 114.94 ? 2119 GLY A N     1 
ATOM   4660  C  CA    . GLY A 1 2119 ? 168.230 217.965 116.266 1.00 122.07 ? 2119 GLY A CA    1 
ATOM   4661  C  C     . GLY A 1 2119 ? 166.895 217.259 116.119 1.00 123.92 ? 2119 GLY A C     1 
ATOM   4662  O  O     . GLY A 1 2119 ? 166.054 217.239 117.023 1.00 117.53 ? 2119 GLY A O     1 
ATOM   4663  N  N     . GLU A 1 2120 ? 166.704 216.665 114.937 1.00 125.47 ? 2120 GLU A N     1 
ATOM   4664  C  CA    . GLU A 1 2120 ? 165.454 215.976 114.637 1.00 128.90 ? 2120 GLU A CA    1 
ATOM   4665  C  C     . GLU A 1 2120 ? 165.656 214.659 113.896 1.00 134.96 ? 2120 GLU A C     1 
ATOM   4666  O  O     . GLU A 1 2120 ? 164.687 214.131 113.334 1.00 136.96 ? 2120 GLU A O     1 
ATOM   4667  C  CB    . GLU A 1 2120 ? 164.522 216.885 113.822 1.00 130.06 ? 2120 GLU A CB    1 
ATOM   4668  C  CG    . GLU A 1 2120 ? 163.934 218.045 114.611 1.00 126.57 ? 2120 GLU A CG    1 
ATOM   4669  C  CD    . GLU A 1 2120 ? 163.008 218.909 113.778 1.00 116.63 ? 2120 GLU A CD    1 
ATOM   4670  O  OE1   . GLU A 1 2120 ? 161.954 218.402 113.341 1.00 121.77 ? 2120 GLU A OE1   1 
ATOM   4671  O  OE2   . GLU A 1 2120 ? 163.333 220.095 113.562 1.00 103.51 ? 2120 GLU A OE2   1 
ATOM   4672  N  N     . ALA A 1 2121 ? 166.868 214.110 113.871 1.00 134.86 ? 2121 ALA A N     1 
ATOM   4673  C  CA    . ALA A 1 2121 ? 167.149 212.859 113.179 1.00 129.80 ? 2121 ALA A CA    1 
ATOM   4674  C  C     . ALA A 1 2121 ? 167.226 211.728 114.197 1.00 126.97 ? 2121 ALA A C     1 
ATOM   4675  O  O     . ALA A 1 2121 ? 168.030 211.785 115.133 1.00 126.88 ? 2121 ALA A O     1 
ATOM   4676  C  CB    . ALA A 1 2121 ? 168.450 212.956 112.382 1.00 124.91 ? 2121 ALA A CB    1 
ATOM   4677  N  N     . VAL A 1 2122 ? 166.391 210.707 114.013 1.00 124.17 ? 2122 VAL A N     1 
ATOM   4678  C  CA    . VAL A 1 2122 ? 166.337 209.555 114.905 1.00 122.58 ? 2122 VAL A CA    1 
ATOM   4679  C  C     . VAL A 1 2122 ? 166.357 208.288 114.060 1.00 119.86 ? 2122 VAL A C     1 
ATOM   4680  O  O     . VAL A 1 2122 ? 165.586 208.163 113.103 1.00 115.29 ? 2122 VAL A O     1 
ATOM   4681  C  CB    . VAL A 1 2122 ? 165.085 209.590 115.805 1.00 115.14 ? 2122 VAL A CB    1 
ATOM   4682  C  CG1   . VAL A 1 2122 ? 164.762 208.200 116.336 1.00 105.83 ? 2122 VAL A CG1   1 
ATOM   4683  C  CG2   . VAL A 1 2122 ? 165.284 210.570 116.950 1.00 111.62 ? 2122 VAL A CG2   1 
ATOM   4684  N  N     . ASP A 1 2123 ? 167.240 207.354 114.412 1.00 118.77 ? 2123 ASP A N     1 
ATOM   4685  C  CA    . ASP A 1 2123 ? 167.327 206.062 113.734 1.00 117.21 ? 2123 ASP A CA    1 
ATOM   4686  C  C     . ASP A 1 2123 ? 167.550 204.992 114.793 1.00 112.96 ? 2123 ASP A C     1 
ATOM   4687  O  O     . ASP A 1 2123 ? 168.592 204.980 115.454 1.00 109.57 ? 2123 ASP A O     1 
ATOM   4688  C  CB    . ASP A 1 2123 ? 168.453 206.051 112.699 1.00 116.13 ? 2123 ASP A CB    1 
ATOM   4689  C  CG    . ASP A 1 2123 ? 168.429 204.811 111.820 1.00 119.05 ? 2123 ASP A CG    1 
ATOM   4690  O  OD1   . ASP A 1 2123 ? 167.558 203.940 112.029 1.00 115.96 ? 2123 ASP A OD1   1 
ATOM   4691  O  OD2   . ASP A 1 2123 ? 169.283 204.709 110.915 1.00 122.39 ? 2123 ASP A OD2   1 
ATOM   4692  N  N     . GLU A 1 2124 ? 166.574 204.094 114.949 1.00 111.82 ? 2124 GLU A N     1 
ATOM   4693  C  CA    . GLU A 1 2124 ? 166.691 203.040 115.953 1.00 104.74 ? 2124 GLU A CA    1 
ATOM   4694  C  C     . GLU A 1 2124 ? 167.844 202.095 115.636 1.00 108.10 ? 2124 GLU A C     1 
ATOM   4695  O  O     . GLU A 1 2124 ? 168.543 201.634 116.546 1.00 105.54 ? 2124 GLU A O     1 
ATOM   4696  C  CB    . GLU A 1 2124 ? 165.377 202.265 116.059 1.00 95.09  ? 2124 GLU A CB    1 
ATOM   4697  C  CG    . GLU A 1 2124 ? 164.215 203.070 116.626 1.00 97.87  ? 2124 GLU A CG    1 
ATOM   4698  C  CD    . GLU A 1 2124 ? 163.525 203.924 115.579 1.00 113.49 ? 2124 GLU A CD    1 
ATOM   4699  O  OE1   . GLU A 1 2124 ? 163.909 203.844 114.394 1.00 114.47 ? 2124 GLU A OE1   1 
ATOM   4700  O  OE2   . GLU A 1 2124 ? 162.597 204.676 115.944 1.00 115.86 ? 2124 GLU A OE2   1 
ATOM   4701  N  N     . GLY A 1 2125 ? 168.054 201.792 114.353 1.00 111.67 ? 2125 GLY A N     1 
ATOM   4702  C  CA    . GLY A 1 2125 ? 169.135 200.894 113.983 1.00 107.09 ? 2125 GLY A CA    1 
ATOM   4703  C  C     . GLY A 1 2125 ? 170.504 201.441 114.339 1.00 106.28 ? 2125 GLY A C     1 
ATOM   4704  O  O     . GLY A 1 2125 ? 171.349 200.723 114.878 1.00 101.17 ? 2125 GLY A O     1 
ATOM   4705  N  N     . GLU A 1 2126 ? 170.743 202.721 114.042 1.00 113.76 ? 2126 GLU A N     1 
ATOM   4706  C  CA    . GLU A 1 2126 ? 172.022 203.331 114.392 1.00 108.66 ? 2126 GLU A CA    1 
ATOM   4707  C  C     . GLU A 1 2126 ? 172.210 203.401 115.901 1.00 99.09  ? 2126 GLU A C     1 
ATOM   4708  O  O     . GLU A 1 2126 ? 173.307 203.142 116.408 1.00 100.04 ? 2126 GLU A O     1 
ATOM   4709  C  CB    . GLU A 1 2126 ? 172.133 204.724 113.772 1.00 113.49 ? 2126 GLU A CB    1 
ATOM   4710  C  CG    . GLU A 1 2126 ? 172.212 204.720 112.256 1.00 123.47 ? 2126 GLU A CG    1 
ATOM   4711  C  CD    . GLU A 1 2126 ? 173.492 204.088 111.745 1.00 132.02 ? 2126 GLU A CD    1 
ATOM   4712  O  OE1   . GLU A 1 2126 ? 174.527 204.194 112.436 1.00 128.84 ? 2126 GLU A OE1   1 
ATOM   4713  O  OE2   . GLU A 1 2126 ? 173.464 203.483 110.653 1.00 143.87 ? 2126 GLU A OE2   1 
ATOM   4714  N  N     . ILE A 1 2127 ? 171.151 203.750 116.637 1.00 94.89  ? 2127 ILE A N     1 
ATOM   4715  C  CA    . ILE A 1 2127 ? 171.248 203.826 118.092 1.00 95.98  ? 2127 ILE A CA    1 
ATOM   4716  C  C     . ILE A 1 2127 ? 171.586 202.461 118.676 1.00 93.95  ? 2127 ILE A C     1 
ATOM   4717  O  O     . ILE A 1 2127 ? 172.423 202.344 119.579 1.00 92.00  ? 2127 ILE A O     1 
ATOM   4718  C  CB    . ILE A 1 2127 ? 169.945 204.392 118.688 1.00 89.84  ? 2127 ILE A CB    1 
ATOM   4719  C  CG1   . ILE A 1 2127 ? 169.751 205.848 118.265 1.00 95.54  ? 2127 ILE A CG1   1 
ATOM   4720  C  CG2   . ILE A 1 2127 ? 169.961 204.292 120.202 1.00 81.13  ? 2127 ILE A CG2   1 
ATOM   4721  C  CD1   . ILE A 1 2127 ? 168.416 206.428 118.677 1.00 87.58  ? 2127 ILE A CD1   1 
ATOM   4722  N  N     . ALA A 1 2128 ? 170.947 201.406 118.166 1.00 93.06  ? 2128 ALA A N     1 
ATOM   4723  C  CA    . ALA A 1 2128 ? 171.249 200.061 118.643 1.00 88.73  ? 2128 ALA A CA    1 
ATOM   4724  C  C     . ALA A 1 2128 ? 172.646 199.613 118.232 1.00 85.45  ? 2128 ALA A C     1 
ATOM   4725  O  O     . ALA A 1 2128 ? 173.288 198.849 118.961 1.00 83.34  ? 2128 ALA A O     1 
ATOM   4726  C  CB    . ALA A 1 2128 ? 170.202 199.073 118.128 1.00 82.83  ? 2128 ALA A CB    1 
ATOM   4727  N  N     . GLU A 1 2129 ? 173.128 200.064 117.071 1.00 88.57  ? 2129 GLU A N     1 
ATOM   4728  C  CA    . GLU A 1 2129 ? 174.428 199.613 116.584 1.00 87.30  ? 2129 GLU A CA    1 
ATOM   4729  C  C     . GLU A 1 2129 ? 175.563 200.112 117.472 1.00 90.37  ? 2129 GLU A C     1 
ATOM   4730  O  O     . GLU A 1 2129 ? 176.408 199.325 117.913 1.00 93.97  ? 2129 GLU A O     1 
ATOM   4731  C  CB    . GLU A 1 2129 ? 174.633 200.072 115.140 1.00 92.30  ? 2129 GLU A CB    1 
ATOM   4732  C  CG    . GLU A 1 2129 ? 175.819 199.427 114.440 1.00 96.10  ? 2129 GLU A CG    1 
ATOM   4733  C  CD    . GLU A 1 2129 ? 175.467 198.106 113.780 1.00 106.47 ? 2129 GLU A CD    1 
ATOM   4734  O  OE1   . GLU A 1 2129 ? 174.577 197.396 114.293 1.00 102.33 ? 2129 GLU A OE1   1 
ATOM   4735  O  OE2   . GLU A 1 2129 ? 176.081 197.778 112.743 1.00 108.97 ? 2129 GLU A OE2   1 
ATOM   4736  N  N     . ASN A 1 2130 ? 175.601 201.412 117.745 1.00 89.37  ? 2130 ASN A N     1 
ATOM   4737  C  CA    . ASN A 1 2130 ? 176.649 201.988 118.590 1.00 87.46  ? 2130 ASN A CA    1 
ATOM   4738  C  C     . ASN A 1 2130 ? 176.176 202.078 120.039 1.00 84.67  ? 2130 ASN A C     1 
ATOM   4739  O  O     . ASN A 1 2130 ? 176.234 203.124 120.686 1.00 86.97  ? 2130 ASN A O     1 
ATOM   4740  C  CB    . ASN A 1 2130 ? 177.074 203.354 118.055 1.00 84.15  ? 2130 ASN A CB    1 
ATOM   4741  C  CG    . ASN A 1 2130 ? 175.896 204.261 117.754 1.00 90.73  ? 2130 ASN A CG    1 
ATOM   4742  O  OD1   . ASN A 1 2130 ? 174.851 204.177 118.399 1.00 93.44  ? 2130 ASN A OD1   1 
ATOM   4743  N  ND2   . ASN A 1 2130 ? 176.061 205.135 116.769 1.00 87.30  ? 2130 ASN A ND2   1 
ATOM   4744  N  N     . LEU A 1 2131 ? 175.702 200.944 120.547 1.00 80.74  ? 2131 LEU A N     1 
ATOM   4745  C  CA    . LEU A 1 2131 ? 175.156 200.878 121.890 1.00 74.73  ? 2131 LEU A CA    1 
ATOM   4746  C  C     . LEU A 1 2131 ? 176.079 200.072 122.788 1.00 74.39  ? 2131 LEU A C     1 
ATOM   4747  O  O     . LEU A 1 2131 ? 176.308 198.883 122.527 1.00 76.56  ? 2131 LEU A O     1 
ATOM   4748  C  CB    . LEU A 1 2131 ? 173.759 200.250 121.873 1.00 76.81  ? 2131 LEU A CB    1 
ATOM   4749  C  CG    . LEU A 1 2131 ? 173.008 200.194 123.202 1.00 66.95  ? 2131 LEU A CG    1 
ATOM   4750  C  CD1   . LEU A 1 2131 ? 172.741 201.596 123.722 1.00 63.94  ? 2131 LEU A CD1   1 
ATOM   4751  C  CD2   . LEU A 1 2131 ? 171.709 199.433 123.031 1.00 67.82  ? 2131 LEU A CD2   1 
ATOM   4752  N  N     . PRO A 1 2132 ? 176.623 200.675 123.842 1.00 72.01  ? 2132 PRO A N     1 
ATOM   4753  C  CA    . PRO A 1 2132 ? 177.563 199.981 124.750 1.00 66.85  ? 2132 PRO A CA    1 
ATOM   4754  C  C     . PRO A 1 2132 ? 176.865 198.989 125.679 1.00 57.68  ? 2132 PRO A C     1 
ATOM   4755  O  O     . PRO A 1 2132 ? 176.501 199.273 126.819 1.00 55.86  ? 2132 PRO A O     1 
ATOM   4756  C  CB    . PRO A 1 2132 ? 178.202 201.140 125.517 1.00 60.49  ? 2132 PRO A CB    1 
ATOM   4757  C  CG    . PRO A 1 2132 ? 177.157 202.201 125.520 1.00 57.64  ? 2132 PRO A CG    1 
ATOM   4758  C  CD    . PRO A 1 2132 ? 176.395 202.076 124.237 1.00 64.05  ? 2132 PRO A CD    1 
ATOM   4759  N  N     . GLU A 1 2133 ? 176.662 197.777 125.159 1.00 51.88  ? 2133 GLU A N     1 
ATOM   4760  C  CA    . GLU A 1 2133 ? 175.951 196.749 125.913 1.00 44.98  ? 2133 GLU A CA    1 
ATOM   4761  C  C     . GLU A 1 2133 ? 176.773 196.252 127.097 1.00 45.17  ? 2133 GLU A C     1 
ATOM   4762  O  O     . GLU A 1 2133 ? 176.213 195.862 128.130 1.00 53.03  ? 2133 GLU A O     1 
ATOM   4763  C  CB    . GLU A 1 2133 ? 175.587 195.592 124.986 1.00 44.18  ? 2133 GLU A CB    1 
ATOM   4764  C  CG    . GLU A 1 2133 ? 174.429 195.894 124.053 1.00 47.20  ? 2133 GLU A CG    1 
ATOM   4765  C  CD    . GLU A 1 2133 ? 174.594 195.242 122.696 1.00 53.38  ? 2133 GLU A CD    1 
ATOM   4766  O  OE1   . GLU A 1 2133 ? 175.719 194.799 122.384 1.00 57.55  ? 2133 GLU A OE1   1 
ATOM   4767  O  OE2   . GLU A 1 2133 ? 173.601 195.174 121.941 1.00 54.85  ? 2133 GLU A OE2   1 
ATOM   4768  N  N     . GLN A 1 2134 ? 178.102 196.247 126.963 1.00 41.18  ? 2134 GLN A N     1 
ATOM   4769  C  CA    . GLN A 1 2134 ? 178.948 195.748 128.042 1.00 41.14  ? 2134 GLN A CA    1 
ATOM   4770  C  C     . GLN A 1 2134 ? 178.820 196.606 129.293 1.00 42.65  ? 2134 GLN A C     1 
ATOM   4771  O  O     . GLN A 1 2134 ? 178.732 196.078 130.410 1.00 44.75  ? 2134 GLN A O     1 
ATOM   4772  C  CB    . GLN A 1 2134 ? 180.405 195.677 127.585 1.00 43.96  ? 2134 GLN A CB    1 
ATOM   4773  C  CG    . GLN A 1 2134 ? 180.716 194.479 126.704 1.00 48.90  ? 2134 GLN A CG    1 
ATOM   4774  C  CD    . GLN A 1 2134 ? 182.190 194.126 126.699 1.00 60.54  ? 2134 GLN A CD    1 
ATOM   4775  O  OE1   . GLN A 1 2134 ? 182.996 194.771 127.367 1.00 64.20  ? 2134 GLN A OE1   1 
ATOM   4776  N  NE2   . GLN A 1 2134 ? 182.548 193.092 125.947 1.00 59.18  ? 2134 GLN A NE2   1 
ATOM   4777  N  N     . GLU A 1 2135 ? 178.800 197.933 129.137 1.00 41.02  ? 2135 GLU A N     1 
ATOM   4778  C  CA    . GLU A 1 2135 ? 178.656 198.777 130.317 1.00 39.19  ? 2135 GLU A CA    1 
ATOM   4779  C  C     . GLU A 1 2135 ? 177.248 198.676 130.882 1.00 39.76  ? 2135 GLU A C     1 
ATOM   4780  O  O     . GLU A 1 2135 ? 177.045 198.867 132.081 1.00 45.29  ? 2135 GLU A O     1 
ATOM   4781  C  CB    . GLU A 1 2135 ? 179.005 200.235 130.015 1.00 47.35  ? 2135 GLU A CB    1 
ATOM   4782  C  CG    . GLU A 1 2135 ? 178.011 200.994 129.163 1.00 57.93  ? 2135 GLU A CG    1 
ATOM   4783  C  CD    . GLU A 1 2135 ? 178.434 202.437 128.956 1.00 69.18  ? 2135 GLU A CD    1 
ATOM   4784  O  OE1   . GLU A 1 2135 ? 179.533 202.804 129.422 1.00 69.14  ? 2135 GLU A OE1   1 
ATOM   4785  O  OE2   . GLU A 1 2135 ? 177.657 203.214 128.366 1.00 67.88  ? 2135 GLU A OE2   1 
ATOM   4786  N  N     . ILE A 1 2136 ? 176.264 198.355 130.039 1.00 37.77  ? 2136 ILE A N     1 
ATOM   4787  C  CA    . ILE A 1 2136 ? 174.913 198.107 130.539 1.00 37.01  ? 2136 ILE A CA    1 
ATOM   4788  C  C     . ILE A 1 2136 ? 174.897 196.874 131.436 1.00 32.70  ? 2136 ILE A C     1 
ATOM   4789  O  O     . ILE A 1 2136 ? 174.317 196.884 132.533 1.00 37.50  ? 2136 ILE A O     1 
ATOM   4790  C  CB    . ILE A 1 2136 ? 173.930 197.965 129.361 1.00 37.57  ? 2136 ILE A CB    1 
ATOM   4791  C  CG1   . ILE A 1 2136 ? 173.633 199.333 128.746 1.00 37.49  ? 2136 ILE A CG1   1 
ATOM   4792  C  CG2   . ILE A 1 2136 ? 172.650 197.277 129.805 1.00 37.86  ? 2136 ILE A CG2   1 
ATOM   4793  C  CD1   . ILE A 1 2136 ? 173.013 199.261 127.370 1.00 41.05  ? 2136 ILE A CD1   1 
ATOM   4794  N  N     . LEU A 1 2137 ? 175.540 195.794 130.986 1.00 33.02  ? 2137 LEU A N     1 
ATOM   4795  C  CA    . LEU A 1 2137 ? 175.601 194.580 131.792 1.00 33.40  ? 2137 LEU A CA    1 
ATOM   4796  C  C     . LEU A 1 2137 ? 176.372 194.817 133.087 1.00 34.43  ? 2137 LEU A C     1 
ATOM   4797  O  O     . LEU A 1 2137 ? 175.964 194.350 134.159 1.00 38.20  ? 2137 LEU A O     1 
ATOM   4798  C  CB    . LEU A 1 2137 ? 176.232 193.450 130.978 1.00 32.87  ? 2137 LEU A CB    1 
ATOM   4799  C  CG    . LEU A 1 2137 ? 176.289 192.059 131.608 1.00 36.48  ? 2137 LEU A CG    1 
ATOM   4800  C  CD1   . LEU A 1 2137 ? 174.887 191.539 131.869 1.00 42.02  ? 2137 LEU A CD1   1 
ATOM   4801  C  CD2   . LEU A 1 2137 ? 177.053 191.108 130.706 1.00 32.90  ? 2137 LEU A CD2   1 
ATOM   4802  N  N     . ILE A 1 2138 ? 177.483 195.555 133.009 1.00 33.42  ? 2138 ILE A N     1 
ATOM   4803  C  CA    . ILE A 1 2138 ? 178.247 195.874 134.213 1.00 34.32  ? 2138 ILE A CA    1 
ATOM   4804  C  C     . ILE A 1 2138 ? 177.433 196.759 135.150 1.00 35.08  ? 2138 ILE A C     1 
ATOM   4805  O  O     . ILE A 1 2138 ? 177.502 196.616 136.376 1.00 37.46  ? 2138 ILE A O     1 
ATOM   4806  C  CB    . ILE A 1 2138 ? 179.592 196.522 133.841 1.00 36.59  ? 2138 ILE A CB    1 
ATOM   4807  C  CG1   . ILE A 1 2138 ? 180.570 195.462 133.345 1.00 38.89  ? 2138 ILE A CG1   1 
ATOM   4808  C  CG2   . ILE A 1 2138 ? 180.187 197.272 135.022 1.00 37.13  ? 2138 ILE A CG2   1 
ATOM   4809  C  CD1   . ILE A 1 2138 ? 181.924 196.017 133.024 1.00 50.14  ? 2138 ILE A CD1   1 
ATOM   4810  N  N     . GLN A 1 2139 ? 176.652 197.687 134.593 1.00 32.04  ? 2139 GLN A N     1 
ATOM   4811  C  CA    . GLN A 1 2139 ? 175.798 198.533 135.414 1.00 33.89  ? 2139 GLN A CA    1 
ATOM   4812  C  C     . GLN A 1 2139 ? 174.777 197.702 136.169 1.00 33.80  ? 2139 GLN A C     1 
ATOM   4813  O  O     . GLN A 1 2139 ? 174.557 197.917 137.364 1.00 40.82  ? 2139 GLN A O     1 
ATOM   4814  C  CB    . GLN A 1 2139 ? 175.100 199.574 134.538 1.00 34.42  ? 2139 GLN A CB    1 
ATOM   4815  C  CG    . GLN A 1 2139 ? 173.948 200.293 135.219 1.00 40.37  ? 2139 GLN A CG    1 
ATOM   4816  C  CD    . GLN A 1 2139 ? 173.331 201.364 134.343 1.00 42.55  ? 2139 GLN A CD    1 
ATOM   4817  O  OE1   . GLN A 1 2139 ? 173.972 201.875 133.425 1.00 41.99  ? 2139 GLN A OE1   1 
ATOM   4818  N  NE2   . GLN A 1 2139 ? 172.082 201.714 134.625 1.00 42.63  ? 2139 GLN A NE2   1 
ATOM   4819  N  N     . SER A 1 2140 ? 174.146 196.742 135.491 1.00 31.58  ? 2140 SER A N     1 
ATOM   4820  C  CA    . SER A 1 2140 ? 173.200 195.867 136.178 1.00 28.93  ? 2140 SER A CA    1 
ATOM   4821  C  C     . SER A 1 2140 ? 173.893 195.048 137.261 1.00 28.58  ? 2140 SER A C     1 
ATOM   4822  O  O     . SER A 1 2140 ? 173.371 194.904 138.376 1.00 32.97  ? 2140 SER A O     1 
ATOM   4823  C  CB    . SER A 1 2140 ? 172.506 194.955 135.172 1.00 26.50  ? 2140 SER A CB    1 
ATOM   4824  O  OG    . SER A 1 2140 ? 171.874 195.725 134.171 1.00 30.48  ? 2140 SER A OG    1 
ATOM   4825  N  N     . VAL A 1 2141 ? 175.079 194.518 136.954 1.00 27.61  ? 2141 VAL A N     1 
ATOM   4826  C  CA    . VAL A 1 2141 ? 175.831 193.744 137.938 1.00 26.39  ? 2141 VAL A CA    1 
ATOM   4827  C  C     . VAL A 1 2141 ? 176.122 194.589 139.172 1.00 33.07  ? 2141 VAL A C     1 
ATOM   4828  O  O     . VAL A 1 2141 ? 175.973 194.128 140.309 1.00 41.20  ? 2141 VAL A O     1 
ATOM   4829  C  CB    . VAL A 1 2141 ? 177.124 193.196 137.307 1.00 24.30  ? 2141 VAL A CB    1 
ATOM   4830  C  CG1   . VAL A 1 2141 ? 178.105 192.769 138.385 1.00 25.52  ? 2141 VAL A CG1   1 
ATOM   4831  C  CG2   . VAL A 1 2141 ? 176.811 192.037 136.376 1.00 28.26  ? 2141 VAL A CG2   1 
ATOM   4832  N  N     . CYS A 1 2142 ? 176.526 195.844 138.967 1.00 31.98  ? 2142 CYS A N     1 
ATOM   4833  C  CA    . CYS A 1 2142 ? 176.852 196.711 140.093 1.00 29.52  ? 2142 CYS A CA    1 
ATOM   4834  C  C     . CYS A 1 2142 ? 175.609 197.127 140.871 1.00 27.71  ? 2142 CYS A C     1 
ATOM   4835  O  O     . CYS A 1 2142 ? 175.657 197.227 142.100 1.00 33.49  ? 2142 CYS A O     1 
ATOM   4836  C  CB    . CYS A 1 2142 ? 177.611 197.941 139.603 1.00 35.40  ? 2142 CYS A CB    1 
ATOM   4837  S  SG    . CYS A 1 2142 ? 179.260 197.581 138.959 1.00 49.51  ? 2142 CYS A SG    1 
ATOM   4838  N  N     . GLU A 1 2143 ? 174.493 197.377 140.186 1.00 25.43  ? 2143 GLU A N     1 
ATOM   4839  C  CA    . GLU A 1 2143 ? 173.259 197.666 140.905 1.00 28.10  ? 2143 GLU A CA    1 
ATOM   4840  C  C     . GLU A 1 2143 ? 172.737 196.456 141.665 1.00 30.05  ? 2143 GLU A C     1 
ATOM   4841  O  O     . GLU A 1 2143 ? 171.927 196.625 142.581 1.00 36.27  ? 2143 GLU A O     1 
ATOM   4842  C  CB    . GLU A 1 2143 ? 172.173 198.181 139.954 1.00 32.71  ? 2143 GLU A CB    1 
ATOM   4843  C  CG    . GLU A 1 2143 ? 172.596 199.340 139.070 1.00 46.47  ? 2143 GLU A CG    1 
ATOM   4844  C  CD    . GLU A 1 2143 ? 171.424 200.180 138.601 1.00 63.39  ? 2143 GLU A CD    1 
ATOM   4845  O  OE1   . GLU A 1 2143 ? 170.628 199.681 137.778 1.00 66.15  ? 2143 GLU A OE1   1 
ATOM   4846  O  OE2   . GLU A 1 2143 ? 171.306 201.341 139.043 1.00 58.44  ? 2143 GLU A OE2   1 
ATOM   4847  N  N     . THR A 1 2144 ? 173.172 195.246 141.316 1.00 26.73  ? 2144 THR A N     1 
ATOM   4848  C  CA    . THR A 1 2144 ? 172.689 194.061 142.013 1.00 26.13  ? 2144 THR A CA    1 
ATOM   4849  C  C     . THR A 1 2144 ? 173.738 193.417 142.911 1.00 26.50  ? 2144 THR A C     1 
ATOM   4850  O  O     . THR A 1 2144 ? 173.465 193.166 144.088 1.00 30.06  ? 2144 THR A O     1 
ATOM   4851  C  CB    . THR A 1 2144 ? 172.157 193.040 140.998 1.00 26.00  ? 2144 THR A CB    1 
ATOM   4852  O  OG1   . THR A 1 2144 ? 171.416 193.729 139.985 1.00 26.49  ? 2144 THR A OG1   1 
ATOM   4853  C  CG2   . THR A 1 2144 ? 171.216 192.067 141.688 1.00 31.30  ? 2144 THR A CG2   1 
ATOM   4854  N  N     . MET A 1 2145 ? 174.942 193.146 142.395 1.00 27.12  ? 2145 MET A N     1 
ATOM   4855  C  CA    . MET A 1 2145 ? 175.979 192.502 143.203 1.00 26.06  ? 2145 MET A CA    1 
ATOM   4856  C  C     . MET A 1 2145 ? 176.592 193.437 144.242 1.00 22.49  ? 2145 MET A C     1 
ATOM   4857  O  O     . MET A 1 2145 ? 176.830 193.023 145.381 1.00 26.45  ? 2145 MET A O     1 
ATOM   4858  C  CB    . MET A 1 2145 ? 177.091 191.945 142.308 1.00 32.35  ? 2145 MET A CB    1 
ATOM   4859  C  CG    . MET A 1 2145 ? 176.752 190.735 141.439 1.00 37.53  ? 2145 MET A CG    1 
ATOM   4860  S  SD    . MET A 1 2145 ? 175.613 189.544 142.177 1.00 61.70  ? 2145 MET A SD    1 
ATOM   4861  C  CE    . MET A 1 2145 ? 174.060 190.027 141.436 1.00 30.06  ? 2145 MET A CE    1 
ATOM   4862  N  N     . VAL A 1 2146 ? 176.880 194.687 143.868 1.00 20.89  ? 2146 VAL A N     1 
ATOM   4863  C  CA    . VAL A 1 2146 ? 177.681 195.556 144.738 1.00 23.88  ? 2146 VAL A CA    1 
ATOM   4864  C  C     . VAL A 1 2146 ? 177.033 195.812 146.096 1.00 25.76  ? 2146 VAL A C     1 
ATOM   4865  O  O     . VAL A 1 2146 ? 177.743 195.747 147.113 1.00 28.11  ? 2146 VAL A O     1 
ATOM   4866  C  CB    . VAL A 1 2146 ? 178.037 196.860 143.998 1.00 20.97  ? 2146 VAL A CB    1 
ATOM   4867  C  CG1   . VAL A 1 2146 ? 178.403 197.958 144.985 1.00 18.51  ? 2146 VAL A CG1   1 
ATOM   4868  C  CG2   . VAL A 1 2146 ? 179.175 196.617 143.017 1.00 23.95  ? 2146 VAL A CG2   1 
ATOM   4869  N  N     . PRO A 1 2147 ? 175.728 196.110 146.199 1.00 22.65  ? 2147 PRO A N     1 
ATOM   4870  C  CA    . PRO A 1 2147 ? 175.176 196.472 147.519 1.00 17.10  ? 2147 PRO A CA    1 
ATOM   4871  C  C     . PRO A 1 2147 ? 175.383 195.427 148.604 1.00 18.18  ? 2147 PRO A C     1 
ATOM   4872  O  O     . PRO A 1 2147 ? 175.519 195.797 149.777 1.00 21.78  ? 2147 PRO A O     1 
ATOM   4873  C  CB    . PRO A 1 2147 ? 173.686 196.680 147.223 1.00 13.29  ? 2147 PRO A CB    1 
ATOM   4874  C  CG    . PRO A 1 2147 ? 173.654 197.114 145.819 1.00 19.67  ? 2147 PRO A CG    1 
ATOM   4875  C  CD    . PRO A 1 2147 ? 174.731 196.327 145.133 1.00 25.27  ? 2147 PRO A CD    1 
ATOM   4876  N  N     . LYS A 1 2148 ? 175.412 194.142 148.264 1.00 15.67  ? 2148 LYS A N     1 
ATOM   4877  C  CA    . LYS A 1 2148 ? 175.587 193.097 149.265 1.00 14.04  ? 2148 LYS A CA    1 
ATOM   4878  C  C     . LYS A 1 2148 ? 177.047 192.836 149.608 1.00 17.19  ? 2148 LYS A C     1 
ATOM   4879  O  O     . LYS A 1 2148 ? 177.320 192.063 150.532 1.00 21.53  ? 2148 LYS A O     1 
ATOM   4880  C  CB    . LYS A 1 2148 ? 174.938 191.793 148.793 1.00 18.61  ? 2148 LYS A CB    1 
ATOM   4881  C  CG    . LYS A 1 2148 ? 175.597 191.163 147.582 1.00 18.34  ? 2148 LYS A CG    1 
ATOM   4882  C  CD    . LYS A 1 2148 ? 174.863 189.906 147.151 1.00 21.38  ? 2148 LYS A CD    1 
ATOM   4883  C  CE    . LYS A 1 2148 ? 175.526 189.265 145.947 1.00 28.52  ? 2148 LYS A CE    1 
ATOM   4884  N  NZ    . LYS A 1 2148 ? 174.805 188.040 145.507 1.00 33.41  ? 2148 LYS A NZ    1 
ATOM   4885  N  N     . LEU A 1 2149 ? 177.984 193.453 148.896 1.00 19.88  ? 2149 LEU A N     1 
ATOM   4886  C  CA    . LEU A 1 2149 ? 179.400 193.193 149.114 1.00 23.66  ? 2149 LEU A CA    1 
ATOM   4887  C  C     . LEU A 1 2149 ? 179.877 193.801 150.425 1.00 26.05  ? 2149 LEU A C     1 
ATOM   4888  O  O     . LEU A 1 2149 ? 179.441 194.885 150.822 1.00 27.49  ? 2149 LEU A O     1 
ATOM   4889  C  CB    . LEU A 1 2149 ? 180.231 193.758 147.964 1.00 27.82  ? 2149 LEU A CB    1 
ATOM   4890  C  CG    . LEU A 1 2149 ? 180.067 193.146 146.576 1.00 21.97  ? 2149 LEU A CG    1 
ATOM   4891  C  CD1   . LEU A 1 2149 ? 180.976 193.872 145.603 1.00 26.19  ? 2149 LEU A CD1   1 
ATOM   4892  C  CD2   . LEU A 1 2149 ? 180.378 191.660 146.604 1.00 17.51  ? 2149 LEU A CD2   1 
ATOM   4893  N  N     . VAL A 1 2150 ? 180.783 193.092 151.095 1.00 27.80  ? 2150 VAL A N     1 
ATOM   4894  C  CA    . VAL A 1 2150 ? 181.496 193.640 152.242 1.00 28.98  ? 2150 VAL A CA    1 
ATOM   4895  C  C     . VAL A 1 2150 ? 182.554 194.603 151.719 1.00 34.64  ? 2150 VAL A C     1 
ATOM   4896  O  O     . VAL A 1 2150 ? 182.824 194.646 150.514 1.00 38.38  ? 2150 VAL A O     1 
ATOM   4897  C  CB    . VAL A 1 2150 ? 182.122 192.531 153.106 1.00 30.80  ? 2150 VAL A CB    1 
ATOM   4898  C  CG1   . VAL A 1 2150 ? 181.037 191.660 153.718 1.00 30.36  ? 2150 VAL A CG1   1 
ATOM   4899  C  CG2   . VAL A 1 2150 ? 183.073 191.693 152.279 1.00 34.43  ? 2150 VAL A CG2   1 
ATOM   4900  N  N     . ALA A 1 2151 ? 183.153 195.386 152.619 1.00 34.55  ? 2151 ALA A N     1 
ATOM   4901  C  CA    . ALA A 1 2151 ? 184.108 196.405 152.194 1.00 36.20  ? 2151 ALA A CA    1 
ATOM   4902  C  C     . ALA A 1 2151 ? 185.325 195.787 151.517 1.00 38.12  ? 2151 ALA A C     1 
ATOM   4903  O  O     . ALA A 1 2151 ? 185.854 196.343 150.547 1.00 34.14  ? 2151 ALA A O     1 
ATOM   4904  C  CB    . ALA A 1 2151 ? 184.534 197.254 153.391 1.00 35.15  ? 2151 ALA A CB    1 
ATOM   4905  N  N     . GLU A 1 2152 ? 185.787 194.638 152.013 1.00 41.35  ? 2152 GLU A N     1 
ATOM   4906  C  CA    . GLU A 1 2152 ? 186.988 194.011 151.474 1.00 42.85  ? 2152 GLU A CA    1 
ATOM   4907  C  C     . GLU A 1 2152 ? 186.767 193.356 150.116 1.00 47.77  ? 2152 GLU A C     1 
ATOM   4908  O  O     . GLU A 1 2152 ? 187.750 193.007 149.455 1.00 53.87  ? 2152 GLU A O     1 
ATOM   4909  C  CB    . GLU A 1 2152 ? 187.519 192.970 152.462 1.00 50.00  ? 2152 GLU A CB    1 
ATOM   4910  C  CG    . GLU A 1 2152 ? 186.666 191.717 152.557 1.00 52.36  ? 2152 GLU A CG    1 
ATOM   4911  C  CD    . GLU A 1 2152 ? 186.799 191.017 153.895 1.00 68.19  ? 2152 GLU A CD    1 
ATOM   4912  O  OE1   . GLU A 1 2152 ? 186.678 191.695 154.938 1.00 76.82  ? 2152 GLU A OE1   1 
ATOM   4913  O  OE2   . GLU A 1 2152 ? 187.021 189.789 153.905 1.00 73.47  ? 2152 GLU A OE2   1 
ATOM   4914  N  N     . ASP A 1 2153 ? 185.517 193.182 149.683 1.00 43.75  ? 2153 ASP A N     1 
ATOM   4915  C  CA    . ASP A 1 2153 ? 185.231 192.475 148.441 1.00 35.87  ? 2153 ASP A CA    1 
ATOM   4916  C  C     . ASP A 1 2153 ? 184.926 193.394 147.266 1.00 34.93  ? 2153 ASP A C     1 
ATOM   4917  O  O     . ASP A 1 2153 ? 184.971 192.934 146.120 1.00 36.70  ? 2153 ASP A O     1 
ATOM   4918  C  CB    . ASP A 1 2153 ? 184.054 191.512 148.636 1.00 30.77  ? 2153 ASP A CB    1 
ATOM   4919  C  CG    . ASP A 1 2153 ? 184.450 190.253 149.379 1.00 42.72  ? 2153 ASP A CG    1 
ATOM   4920  O  OD1   . ASP A 1 2153 ? 185.664 189.986 149.491 1.00 48.84  ? 2153 ASP A OD1   1 
ATOM   4921  O  OD2   . ASP A 1 2153 ? 183.548 189.528 149.848 1.00 43.57  ? 2153 ASP A OD2   1 
ATOM   4922  N  N     . ILE A 1 2154 ? 184.608 194.666 147.515 1.00 36.98  ? 2154 ILE A N     1 
ATOM   4923  C  CA    . ILE A 1 2154 ? 184.307 195.582 146.412 1.00 37.03  ? 2154 ILE A CA    1 
ATOM   4924  C  C     . ILE A 1 2154 ? 185.500 195.769 145.481 1.00 41.15  ? 2154 ILE A C     1 
ATOM   4925  O  O     . ILE A 1 2154 ? 185.322 195.655 144.256 1.00 46.56  ? 2154 ILE A O     1 
ATOM   4926  C  CB    . ILE A 1 2154 ? 183.765 196.913 146.963 1.00 38.01  ? 2154 ILE A CB    1 
ATOM   4927  C  CG1   . ILE A 1 2154 ? 182.448 196.685 147.706 1.00 36.80  ? 2154 ILE A CG1   1 
ATOM   4928  C  CG2   . ILE A 1 2154 ? 183.577 197.920 145.841 1.00 37.16  ? 2154 ILE A CG2   1 
ATOM   4929  C  CD1   . ILE A 1 2154 ? 181.979 197.884 148.495 1.00 40.31  ? 2154 ILE A CD1   1 
ATOM   4930  N  N     . PRO A 1 2155 ? 186.719 196.058 145.966 1.00 44.07  ? 2155 PRO A N     1 
ATOM   4931  C  CA    . PRO A 1 2155 ? 187.859 196.107 145.034 1.00 40.47  ? 2155 PRO A CA    1 
ATOM   4932  C  C     . PRO A 1 2155 ? 188.085 194.796 144.305 1.00 41.61  ? 2155 PRO A C     1 
ATOM   4933  O  O     . PRO A 1 2155 ? 188.448 194.804 143.123 1.00 43.98  ? 2155 PRO A O     1 
ATOM   4934  C  CB    . PRO A 1 2155 ? 189.041 196.466 145.946 1.00 37.22  ? 2155 PRO A CB    1 
ATOM   4935  C  CG    . PRO A 1 2155 ? 188.425 197.137 147.115 1.00 37.26  ? 2155 PRO A CG    1 
ATOM   4936  C  CD    . PRO A 1 2155 ? 187.132 196.420 147.334 1.00 41.20  ? 2155 PRO A CD    1 
ATOM   4937  N  N     . LEU A 1 2156 ? 187.865 193.662 144.976 1.00 37.49  ? 2156 LEU A N     1 
ATOM   4938  C  CA    . LEU A 1 2156 ? 188.021 192.374 144.310 1.00 35.55  ? 2156 LEU A CA    1 
ATOM   4939  C  C     . LEU A 1 2156 ? 187.013 192.208 143.180 1.00 42.08  ? 2156 LEU A C     1 
ATOM   4940  O  O     . LEU A 1 2156 ? 187.378 191.804 142.071 1.00 51.43  ? 2156 LEU A O     1 
ATOM   4941  C  CB    . LEU A 1 2156 ? 187.885 191.235 145.321 1.00 37.72  ? 2156 LEU A CB    1 
ATOM   4942  C  CG    . LEU A 1 2156 ? 188.749 191.320 146.580 1.00 46.87  ? 2156 LEU A CG    1 
ATOM   4943  C  CD1   . LEU A 1 2156 ? 188.652 190.029 147.378 1.00 45.30  ? 2156 LEU A CD1   1 
ATOM   4944  C  CD2   . LEU A 1 2156 ? 190.195 191.622 146.222 1.00 47.71  ? 2156 LEU A CD2   1 
ATOM   4945  N  N     . LEU A 1 2157 ? 185.741 192.523 143.434 1.00 41.80  ? 2157 LEU A N     1 
ATOM   4946  C  CA    . LEU A 1 2157 ? 184.734 192.358 142.391 1.00 38.10  ? 2157 LEU A CA    1 
ATOM   4947  C  C     . LEU A 1 2157 ? 184.966 193.334 141.245 1.00 36.59  ? 2157 LEU A C     1 
ATOM   4948  O  O     . LEU A 1 2157 ? 184.705 193.005 140.083 1.00 44.93  ? 2157 LEU A O     1 
ATOM   4949  C  CB    . LEU A 1 2157 ? 183.328 192.508 142.978 1.00 37.86  ? 2157 LEU A CB    1 
ATOM   4950  C  CG    . LEU A 1 2157 ? 182.141 192.182 142.060 1.00 40.29  ? 2157 LEU A CG    1 
ATOM   4951  C  CD1   . LEU A 1 2157 ? 180.978 191.631 142.862 1.00 40.94  ? 2157 LEU A CD1   1 
ATOM   4952  C  CD2   . LEU A 1 2157 ? 181.682 193.411 141.287 1.00 35.00  ? 2157 LEU A CD2   1 
ATOM   4953  N  N     . PHE A 1 2158 ? 185.471 194.532 141.542 1.00 34.64  ? 2158 PHE A N     1 
ATOM   4954  C  CA    . PHE A 1 2158 ? 185.802 195.447 140.455 1.00 38.17  ? 2158 PHE A CA    1 
ATOM   4955  C  C     . PHE A 1 2158 ? 187.014 194.964 139.664 1.00 43.08  ? 2158 PHE A C     1 
ATOM   4956  O  O     . PHE A 1 2158 ? 187.084 195.179 138.449 1.00 45.00  ? 2158 PHE A O     1 
ATOM   4957  C  CB    . PHE A 1 2158 ? 186.022 196.857 140.998 1.00 40.86  ? 2158 PHE A CB    1 
ATOM   4958  C  CG    . PHE A 1 2158 ? 184.760 197.670 141.076 1.00 39.19  ? 2158 PHE A CG    1 
ATOM   4959  C  CD1   . PHE A 1 2158 ? 184.325 198.404 139.986 1.00 40.82  ? 2158 PHE A CD1   1 
ATOM   4960  C  CD2   . PHE A 1 2158 ? 184.000 197.685 142.233 1.00 38.76  ? 2158 PHE A CD2   1 
ATOM   4961  C  CE1   . PHE A 1 2158 ? 183.162 199.145 140.052 1.00 42.56  ? 2158 PHE A CE1   1 
ATOM   4962  C  CE2   . PHE A 1 2158 ? 182.835 198.424 142.305 1.00 38.33  ? 2158 PHE A CE2   1 
ATOM   4963  C  CZ    . PHE A 1 2158 ? 182.416 199.155 141.213 1.00 40.76  ? 2158 PHE A CZ    1 
ATOM   4964  N  N     . SER A 1 2159 ? 187.965 194.295 140.322 1.00 43.03  ? 2159 SER A N     1 
ATOM   4965  C  CA    . SER A 1 2159 ? 189.063 193.668 139.592 1.00 44.67  ? 2159 SER A CA    1 
ATOM   4966  C  C     . SER A 1 2159 ? 188.553 192.558 138.681 1.00 49.47  ? 2159 SER A C     1 
ATOM   4967  O  O     . SER A 1 2159 ? 189.021 192.407 137.547 1.00 57.02  ? 2159 SER A O     1 
ATOM   4968  C  CB    . SER A 1 2159 ? 190.103 193.124 140.571 1.00 44.55  ? 2159 SER A CB    1 
ATOM   4969  O  OG    . SER A 1 2159 ? 190.659 194.167 141.351 1.00 53.84  ? 2159 SER A OG    1 
ATOM   4970  N  N     . LEU A 1 2160 ? 187.597 191.764 139.167 1.00 45.03  ? 2160 LEU A N     1 
ATOM   4971  C  CA    . LEU A 1 2160 ? 186.970 190.751 138.318 1.00 41.48  ? 2160 LEU A CA    1 
ATOM   4972  C  C     . LEU A 1 2160 ? 186.240 191.383 137.137 1.00 43.14  ? 2160 LEU A C     1 
ATOM   4973  O  O     . LEU A 1 2160 ? 186.293 190.860 136.019 1.00 51.96  ? 2160 LEU A O     1 
ATOM   4974  C  CB    . LEU A 1 2160 ? 186.017 189.878 139.136 1.00 35.29  ? 2160 LEU A CB    1 
ATOM   4975  C  CG    . LEU A 1 2160 ? 186.571 188.656 139.877 1.00 39.10  ? 2160 LEU A CG    1 
ATOM   4976  C  CD1   . LEU A 1 2160 ? 187.469 189.000 141.038 1.00 47.28  ? 2160 LEU A CD1   1 
ATOM   4977  C  CD2   . LEU A 1 2160 ? 185.401 187.825 140.371 1.00 41.95  ? 2160 LEU A CD2   1 
ATOM   4978  N  N     . LEU A 1 2161 ? 185.545 192.499 137.365 1.00 35.40  ? 2161 LEU A N     1 
ATOM   4979  C  CA    . LEU A 1 2161 ? 184.898 193.201 136.258 1.00 34.90  ? 2161 LEU A CA    1 
ATOM   4980  C  C     . LEU A 1 2161 ? 185.920 193.692 135.241 1.00 42.89  ? 2161 LEU A C     1 
ATOM   4981  O  O     . LEU A 1 2161 ? 185.693 193.603 134.028 1.00 47.77  ? 2161 LEU A O     1 
ATOM   4982  C  CB    . LEU A 1 2161 ? 184.065 194.371 136.780 1.00 39.19  ? 2161 LEU A CB    1 
ATOM   4983  C  CG    . LEU A 1 2161 ? 182.804 194.052 137.580 1.00 39.61  ? 2161 LEU A CG    1 
ATOM   4984  C  CD1   . LEU A 1 2161 ? 182.204 195.327 138.141 1.00 41.52  ? 2161 LEU A CD1   1 
ATOM   4985  C  CD2   . LEU A 1 2161 ? 181.801 193.348 136.688 1.00 35.75  ? 2161 LEU A CD2   1 
ATOM   4986  N  N     . SER A 1 2162 ? 187.048 194.222 135.716 1.00 48.05  ? 2162 SER A N     1 
ATOM   4987  C  CA    . SER A 1 2162 ? 188.091 194.685 134.807 1.00 46.04  ? 2162 SER A CA    1 
ATOM   4988  C  C     . SER A 1 2162 ? 188.688 193.530 134.011 1.00 47.34  ? 2162 SER A C     1 
ATOM   4989  O  O     . SER A 1 2162 ? 188.986 193.677 132.820 1.00 54.84  ? 2162 SER A O     1 
ATOM   4990  C  CB    . SER A 1 2162 ? 189.181 195.417 135.588 1.00 48.96  ? 2162 SER A CB    1 
ATOM   4991  O  OG    . SER A 1 2162 ? 188.671 196.592 136.193 1.00 58.49  ? 2162 SER A OG    1 
ATOM   4992  N  N     . ASP A 1 2163 ? 188.881 192.377 134.653 1.00 48.74  ? 2163 ASP A N     1 
ATOM   4993  C  CA    . ASP A 1 2163 ? 189.455 191.229 133.956 1.00 54.04  ? 2163 ASP A CA    1 
ATOM   4994  C  C     . ASP A 1 2163 ? 188.489 190.666 132.920 1.00 47.61  ? 2163 ASP A C     1 
ATOM   4995  O  O     . ASP A 1 2163 ? 188.867 190.429 131.767 1.00 55.11  ? 2163 ASP A O     1 
ATOM   4996  C  CB    . ASP A 1 2163 ? 189.854 190.149 134.963 1.00 56.83  ? 2163 ASP A CB    1 
ATOM   4997  C  CG    . ASP A 1 2163 ? 191.004 190.576 135.853 1.00 68.22  ? 2163 ASP A CG    1 
ATOM   4998  O  OD1   . ASP A 1 2163 ? 191.639 189.694 136.469 1.00 76.43  ? 2163 ASP A OD1   1 
ATOM   4999  O  OD2   . ASP A 1 2163 ? 191.278 191.792 135.932 1.00 71.59  ? 2163 ASP A OD2   1 
ATOM   5000  N  N     . VAL A 1 2164 ? 187.233 190.440 133.314 1.00 42.41  ? 2164 VAL A N     1 
ATOM   5001  C  CA    . VAL A 1 2164 ? 186.268 189.830 132.404 1.00 43.20  ? 2164 VAL A CA    1 
ATOM   5002  C  C     . VAL A 1 2164 ? 185.840 190.815 131.323 1.00 43.05  ? 2164 VAL A C     1 
ATOM   5003  O  O     . VAL A 1 2164 ? 185.737 190.456 130.144 1.00 47.33  ? 2164 VAL A O     1 
ATOM   5004  C  CB    . VAL A 1 2164 ? 185.061 189.290 133.190 1.00 41.51  ? 2164 VAL A CB    1 
ATOM   5005  C  CG1   . VAL A 1 2164 ? 184.072 188.642 132.246 1.00 35.45  ? 2164 VAL A CG1   1 
ATOM   5006  C  CG2   . VAL A 1 2164 ? 185.521 188.292 134.241 1.00 45.50  ? 2164 VAL A CG2   1 
ATOM   5007  N  N     . PHE A 1 2165 ? 185.585 192.069 131.700 1.00 43.92  ? 2165 PHE A N     1 
ATOM   5008  C  CA    . PHE A 1 2165 ? 185.164 193.115 130.768 1.00 45.21  ? 2165 PHE A CA    1 
ATOM   5009  C  C     . PHE A 1 2165 ? 186.224 194.207 130.777 1.00 50.38  ? 2165 PHE A C     1 
ATOM   5010  O  O     . PHE A 1 2165 ? 186.099 195.202 131.509 1.00 54.84  ? 2165 PHE A O     1 
ATOM   5011  C  CB    . PHE A 1 2165 ? 183.796 193.681 131.145 1.00 41.31  ? 2165 PHE A CB    1 
ATOM   5012  C  CG    . PHE A 1 2165 ? 182.712 192.646 131.257 1.00 43.88  ? 2165 PHE A CG    1 
ATOM   5013  C  CD1   . PHE A 1 2165 ? 181.965 192.283 130.149 1.00 47.10  ? 2165 PHE A CD1   1 
ATOM   5014  C  CD2   . PHE A 1 2165 ? 182.430 192.047 132.474 1.00 44.23  ? 2165 PHE A CD2   1 
ATOM   5015  C  CE1   . PHE A 1 2165 ? 180.963 191.337 130.251 1.00 43.46  ? 2165 PHE A CE1   1 
ATOM   5016  C  CE2   . PHE A 1 2165 ? 181.430 191.100 132.581 1.00 41.67  ? 2165 PHE A CE2   1 
ATOM   5017  C  CZ    . PHE A 1 2165 ? 180.696 190.745 131.468 1.00 39.95  ? 2165 PHE A CZ    1 
ATOM   5018  N  N     . PRO A 1 2166 ? 187.282 194.069 129.982 1.00 49.72  ? 2166 PRO A N     1 
ATOM   5019  C  CA    . PRO A 1 2166 ? 188.369 195.053 130.020 1.00 53.13  ? 2166 PRO A CA    1 
ATOM   5020  C  C     . PRO A 1 2166 ? 188.015 196.336 129.286 1.00 50.25  ? 2166 PRO A C     1 
ATOM   5021  O  O     . PRO A 1 2166 ? 187.303 196.328 128.278 1.00 54.70  ? 2166 PRO A O     1 
ATOM   5022  C  CB    . PRO A 1 2166 ? 189.526 194.322 129.329 1.00 60.23  ? 2166 PRO A CB    1 
ATOM   5023  C  CG    . PRO A 1 2166 ? 188.859 193.364 128.404 1.00 57.37  ? 2166 PRO A CG    1 
ATOM   5024  C  CD    . PRO A 1 2166 ? 187.559 192.963 129.049 1.00 47.14  ? 2166 PRO A CD    1 
ATOM   5025  N  N     . GLY A 1 2167 ? 188.524 197.450 129.810 1.00 52.55  ? 2167 GLY A N     1 
ATOM   5026  C  CA    . GLY A 1 2167 ? 188.430 198.732 129.146 1.00 65.53  ? 2167 GLY A CA    1 
ATOM   5027  C  C     . GLY A 1 2167 ? 187.100 199.442 129.261 1.00 64.06  ? 2167 GLY A C     1 
ATOM   5028  O  O     . GLY A 1 2167 ? 186.913 200.474 128.604 1.00 66.27  ? 2167 GLY A O     1 
ATOM   5029  N  N     . VAL A 1 2168 ? 186.171 198.936 130.066 1.00 60.09  ? 2168 VAL A N     1 
ATOM   5030  C  CA    . VAL A 1 2168 ? 184.847 199.529 130.216 1.00 61.05  ? 2168 VAL A CA    1 
ATOM   5031  C  C     . VAL A 1 2168 ? 184.573 199.743 131.700 1.00 63.13  ? 2168 VAL A C     1 
ATOM   5032  O  O     . VAL A 1 2168 ? 184.903 198.889 132.530 1.00 61.37  ? 2168 VAL A O     1 
ATOM   5033  C  CB    . VAL A 1 2168 ? 183.761 198.663 129.549 1.00 58.82  ? 2168 VAL A CB    1 
ATOM   5034  C  CG1   . VAL A 1 2168 ? 183.635 197.315 130.233 1.00 50.87  ? 2168 VAL A CG1   1 
ATOM   5035  C  CG2   . VAL A 1 2168 ? 182.430 199.391 129.547 1.00 57.39  ? 2168 VAL A CG2   1 
ATOM   5036  N  N     . GLN A 1 2169 ? 183.997 200.897 132.030 1.00 68.11  ? 2169 GLN A N     1 
ATOM   5037  C  CA    . GLN A 1 2169 ? 183.765 201.306 133.406 1.00 70.60  ? 2169 GLN A CA    1 
ATOM   5038  C  C     . GLN A 1 2169 ? 182.311 201.718 133.599 1.00 67.94  ? 2169 GLN A C     1 
ATOM   5039  O  O     . GLN A 1 2169 ? 181.614 202.084 132.650 1.00 69.44  ? 2169 GLN A O     1 
ATOM   5040  C  CB    . GLN A 1 2169 ? 184.689 202.466 133.803 1.00 78.51  ? 2169 GLN A CB    1 
ATOM   5041  C  CG    . GLN A 1 2169 ? 186.169 202.123 133.777 1.00 84.22  ? 2169 GLN A CG    1 
ATOM   5042  C  CD    . GLN A 1 2169 ? 187.048 203.325 134.060 1.00 89.81  ? 2169 GLN A CD    1 
ATOM   5043  O  OE1   . GLN A 1 2169 ? 187.901 203.689 133.249 1.00 86.11  ? 2169 GLN A OE1   1 
ATOM   5044  N  NE2   . GLN A 1 2169 ? 186.844 203.950 135.213 1.00 92.15  ? 2169 GLN A NE2   1 
ATOM   5045  N  N     . TYR A 1 2170 ? 181.862 201.654 134.851 1.00 65.04  ? 2170 TYR A N     1 
ATOM   5046  C  CA    . TYR A 1 2170 ? 180.506 202.027 135.229 1.00 65.10  ? 2170 TYR A CA    1 
ATOM   5047  C  C     . TYR A 1 2170 ? 180.555 203.152 136.251 1.00 66.45  ? 2170 TYR A C     1 
ATOM   5048  O  O     . TYR A 1 2170 ? 181.281 203.060 137.246 1.00 67.16  ? 2170 TYR A O     1 
ATOM   5049  C  CB    . TYR A 1 2170 ? 179.743 200.831 135.804 1.00 64.71  ? 2170 TYR A CB    1 
ATOM   5050  C  CG    . TYR A 1 2170 ? 178.567 201.219 136.673 1.00 61.67  ? 2170 TYR A CG    1 
ATOM   5051  C  CD1   . TYR A 1 2170 ? 177.448 201.834 136.128 1.00 59.44  ? 2170 TYR A CD1   1 
ATOM   5052  C  CD2   . TYR A 1 2170 ? 178.579 200.976 138.039 1.00 57.53  ? 2170 TYR A CD2   1 
ATOM   5053  C  CE1   . TYR A 1 2170 ? 176.373 202.192 136.919 1.00 59.05  ? 2170 TYR A CE1   1 
ATOM   5054  C  CE2   . TYR A 1 2170 ? 177.508 201.331 138.838 1.00 58.49  ? 2170 TYR A CE2   1 
ATOM   5055  C  CZ    . TYR A 1 2170 ? 176.408 201.937 138.273 1.00 63.43  ? 2170 TYR A CZ    1 
ATOM   5056  O  OH    . TYR A 1 2170 ? 175.340 202.290 139.065 1.00 67.75  ? 2170 TYR A OH    1 
ATOM   5057  N  N     . HIS A 1 2171 ? 179.782 204.206 136.005 1.00 68.37  ? 2171 HIS A N     1 
ATOM   5058  C  CA    . HIS A 1 2171 ? 179.651 205.325 136.928 1.00 64.42  ? 2171 HIS A CA    1 
ATOM   5059  C  C     . HIS A 1 2171 ? 178.220 205.382 137.440 1.00 66.67  ? 2171 HIS A C     1 
ATOM   5060  O  O     . HIS A 1 2171 ? 177.275 205.425 136.645 1.00 68.49  ? 2171 HIS A O     1 
ATOM   5061  C  CB    . HIS A 1 2171 ? 180.030 206.647 136.253 1.00 67.34  ? 2171 HIS A CB    1 
ATOM   5062  C  CG    . HIS A 1 2171 ? 181.473 206.736 135.868 1.00 81.81  ? 2171 HIS A CG    1 
ATOM   5063  N  ND1   . HIS A 1 2171 ? 181.948 206.295 134.651 1.00 81.82  ? 2171 HIS A ND1   1 
ATOM   5064  C  CD2   . HIS A 1 2171 ? 182.548 207.212 136.540 1.00 81.79  ? 2171 HIS A CD2   1 
ATOM   5065  C  CE1   . HIS A 1 2171 ? 183.252 206.497 134.590 1.00 77.41  ? 2171 HIS A CE1   1 
ATOM   5066  N  NE2   . HIS A 1 2171 ? 183.641 207.052 135.723 1.00 79.85  ? 2171 HIS A NE2   1 
ATOM   5067  N  N     . ARG A 1 2172 ? 178.066 205.378 138.761 1.00 67.42  ? 2172 ARG A N     1 
ATOM   5068  C  CA    . ARG A 1 2172 ? 176.742 205.423 139.362 1.00 63.40  ? 2172 ARG A CA    1 
ATOM   5069  C  C     . ARG A 1 2172 ? 176.060 206.753 139.065 1.00 64.72  ? 2172 ARG A C     1 
ATOM   5070  O  O     . ARG A 1 2172 ? 176.691 207.813 139.047 1.00 68.31  ? 2172 ARG A O     1 
ATOM   5071  C  CB    . ARG A 1 2172 ? 176.835 205.207 140.872 1.00 65.64  ? 2172 ARG A CB    1 
ATOM   5072  C  CG    . ARG A 1 2172 ? 177.961 205.978 141.541 1.00 79.12  ? 2172 ARG A CG    1 
ATOM   5073  C  CD    . ARG A 1 2172 ? 178.336 205.360 142.878 1.00 90.62  ? 2172 ARG A CD    1 
ATOM   5074  N  NE    . ARG A 1 2172 ? 179.008 204.075 142.717 1.00 106.14 ? 2172 ARG A NE    1 
ATOM   5075  C  CZ    . ARG A 1 2172 ? 180.293 203.933 142.423 1.00 107.57 ? 2172 ARG A CZ    1 
ATOM   5076  N  NH1   . ARG A 1 2172 ? 181.084 204.980 142.253 1.00 110.53 ? 2172 ARG A NH1   1 
ATOM   5077  N  NH2   . ARG A 1 2172 ? 180.798 202.709 142.296 1.00 90.76  ? 2172 ARG A NH2   1 
ATOM   5078  N  N     . GLY A 1 2173 ? 174.754 206.686 138.823 1.00 63.30  ? 2173 GLY A N     1 
ATOM   5079  C  CA    . GLY A 1 2173 ? 174.000 207.891 138.530 1.00 65.19  ? 2173 GLY A CA    1 
ATOM   5080  C  C     . GLY A 1 2173 ? 173.920 208.807 139.739 1.00 71.55  ? 2173 GLY A C     1 
ATOM   5081  O  O     . GLY A 1 2173 ? 173.809 208.359 140.882 1.00 75.28  ? 2173 GLY A O     1 
ATOM   5082  N  N     . GLU A 1 2174 ? 173.979 210.110 139.477 1.00 71.70  ? 2174 GLU A N     1 
ATOM   5083  C  CA    . GLU A 1 2174 ? 173.890 211.129 140.522 1.00 72.15  ? 2174 GLU A CA    1 
ATOM   5084  C  C     . GLU A 1 2174 ? 172.413 211.465 140.727 1.00 70.32  ? 2174 GLU A C     1 
ATOM   5085  O  O     . GLU A 1 2174 ? 171.792 212.181 139.941 1.00 73.65  ? 2174 GLU A O     1 
ATOM   5086  C  CB    . GLU A 1 2174 ? 174.755 212.342 140.169 1.00 68.67  ? 2174 GLU A CB    1 
ATOM   5087  C  CG    . GLU A 1 2174 ? 174.349 213.137 138.930 1.00 79.07  ? 2174 GLU A CG    1 
ATOM   5088  C  CD    . GLU A 1 2174 ? 174.907 212.550 137.646 1.00 89.35  ? 2174 GLU A CD    1 
ATOM   5089  O  OE1   . GLU A 1 2174 ? 175.352 211.383 137.665 1.00 84.67  ? 2174 GLU A OE1   1 
ATOM   5090  O  OE2   . GLU A 1 2174 ? 174.897 213.256 136.616 1.00 92.43  ? 2174 GLU A OE2   1 
ATOM   5091  N  N     . MET A 1 2175 ? 171.838 210.903 141.790 1.00 58.34  ? 2175 MET A N     1 
ATOM   5092  C  CA    . MET A 1 2175 ? 170.417 211.072 142.090 1.00 54.23  ? 2175 MET A CA    1 
ATOM   5093  C  C     . MET A 1 2175 ? 170.230 212.292 142.993 1.00 46.46  ? 2175 MET A C     1 
ATOM   5094  O  O     . MET A 1 2175 ? 169.860 212.200 144.165 1.00 48.28  ? 2175 MET A O     1 
ATOM   5095  C  CB    . MET A 1 2175 ? 169.857 209.805 142.721 1.00 52.44  ? 2175 MET A CB    1 
ATOM   5096  C  CG    . MET A 1 2175 ? 169.838 208.616 141.773 1.00 55.11  ? 2175 MET A CG    1 
ATOM   5097  S  SD    . MET A 1 2175 ? 169.123 207.129 142.495 1.00 81.06  ? 2175 MET A SD    1 
ATOM   5098  C  CE    . MET A 1 2175 ? 170.442 206.622 143.594 1.00 42.53  ? 2175 MET A CE    1 
ATOM   5099  N  N     . THR A 1 2176 ? 170.486 213.465 142.408 1.00 44.59  ? 2176 THR A N     1 
ATOM   5100  C  CA    . THR A 1 2176 ? 170.396 214.711 143.163 1.00 42.45  ? 2176 THR A CA    1 
ATOM   5101  C  C     . THR A 1 2176 ? 168.974 214.967 143.646 1.00 47.12  ? 2176 THR A C     1 
ATOM   5102  O  O     . THR A 1 2176 ? 168.770 215.514 144.737 1.00 52.06  ? 2176 THR A O     1 
ATOM   5103  C  CB    . THR A 1 2176 ? 170.886 215.880 142.308 1.00 49.32  ? 2176 THR A CB    1 
ATOM   5104  O  OG1   . THR A 1 2176 ? 169.932 216.149 141.273 1.00 50.33  ? 2176 THR A OG1   1 
ATOM   5105  C  CG2   . THR A 1 2176 ? 172.230 215.550 141.678 1.00 54.98  ? 2176 THR A CG2   1 
ATOM   5106  N  N     . ALA A 1 2177 ? 167.977 214.582 142.845 1.00 45.07  ? 2177 ALA A N     1 
ATOM   5107  C  CA    . ALA A 1 2177 ? 166.587 214.774 143.247 1.00 43.77  ? 2177 ALA A CA    1 
ATOM   5108  C  C     . ALA A 1 2177 ? 166.271 214.001 144.520 1.00 43.04  ? 2177 ALA A C     1 
ATOM   5109  O  O     . ALA A 1 2177 ? 165.577 214.509 145.408 1.00 42.41  ? 2177 ALA A O     1 
ATOM   5110  C  CB    . ALA A 1 2177 ? 165.650 214.355 142.116 1.00 42.63  ? 2177 ALA A CB    1 
ATOM   5111  N  N     . LEU A 1 2178 ? 166.763 212.766 144.625 1.00 42.37  ? 2178 LEU A N     1 
ATOM   5112  C  CA    . LEU A 1 2178 ? 166.609 212.015 145.864 1.00 34.05  ? 2178 LEU A CA    1 
ATOM   5113  C  C     . LEU A 1 2178 ? 167.585 212.479 146.936 1.00 33.43  ? 2178 LEU A C     1 
ATOM   5114  O  O     . LEU A 1 2178 ? 167.275 212.386 148.128 1.00 35.15  ? 2178 LEU A O     1 
ATOM   5115  C  CB    . LEU A 1 2178 ? 166.791 210.519 145.604 1.00 31.69  ? 2178 LEU A CB    1 
ATOM   5116  C  CG    . LEU A 1 2178 ? 166.443 209.600 146.777 1.00 28.76  ? 2178 LEU A CG    1 
ATOM   5117  C  CD1   . LEU A 1 2178 ? 164.967 209.707 147.128 1.00 26.44  ? 2178 LEU A CD1   1 
ATOM   5118  C  CD2   . LEU A 1 2178 ? 166.822 208.163 146.471 1.00 26.94  ? 2178 LEU A CD2   1 
ATOM   5119  N  N     . ARG A 1 2179 ? 168.759 212.976 146.540 1.00 36.57  ? 2179 ARG A N     1 
ATOM   5120  C  CA    . ARG A 1 2179 ? 169.756 213.382 147.525 1.00 30.16  ? 2179 ARG A CA    1 
ATOM   5121  C  C     . ARG A 1 2179 ? 169.303 214.609 148.308 1.00 34.70  ? 2179 ARG A C     1 
ATOM   5122  O  O     . ARG A 1 2179 ? 169.563 214.709 149.511 1.00 39.43  ? 2179 ARG A O     1 
ATOM   5123  C  CB    . ARG A 1 2179 ? 171.100 213.639 146.843 1.00 30.95  ? 2179 ARG A CB    1 
ATOM   5124  C  CG    . ARG A 1 2179 ? 171.889 212.371 146.549 1.00 30.84  ? 2179 ARG A CG    1 
ATOM   5125  C  CD    . ARG A 1 2179 ? 173.375 212.652 146.413 1.00 35.57  ? 2179 ARG A CD    1 
ATOM   5126  N  NE    . ARG A 1 2179 ? 174.125 211.452 146.061 1.00 36.95  ? 2179 ARG A NE    1 
ATOM   5127  C  CZ    . ARG A 1 2179 ? 175.020 210.869 146.847 1.00 42.20  ? 2179 ARG A CZ    1 
ATOM   5128  N  NH1   . ARG A 1 2179 ? 175.294 211.341 148.052 1.00 42.21  ? 2179 ARG A NH1   1 
ATOM   5129  N  NH2   . ARG A 1 2179 ? 175.653 209.783 146.414 1.00 39.10  ? 2179 ARG A NH2   1 
ATOM   5130  N  N     . GLU A 1 2180 ? 168.623 215.553 147.652 1.00 33.79  ? 2180 GLU A N     1 
ATOM   5131  C  CA    . GLU A 1 2180 ? 168.112 216.712 148.380 1.00 37.96  ? 2180 GLU A CA    1 
ATOM   5132  C  C     . GLU A 1 2180 ? 167.025 216.309 149.373 1.00 35.66  ? 2180 GLU A C     1 
ATOM   5133  O  O     . GLU A 1 2180 ? 166.965 216.840 150.490 1.00 40.70  ? 2180 GLU A O     1 
ATOM   5134  C  CB    . GLU A 1 2180 ? 167.601 217.773 147.401 1.00 49.23  ? 2180 GLU A CB    1 
ATOM   5135  C  CG    . GLU A 1 2180 ? 166.398 217.360 146.571 1.00 59.17  ? 2180 GLU A CG    1 
ATOM   5136  C  CD    . GLU A 1 2180 ? 165.972 218.433 145.588 1.00 74.81  ? 2180 GLU A CD    1 
ATOM   5137  O  OE1   . GLU A 1 2180 ? 166.630 219.493 145.541 1.00 79.96  ? 2180 GLU A OE1   1 
ATOM   5138  O  OE2   . GLU A 1 2180 ? 164.980 218.214 144.862 1.00 76.96  ? 2180 GLU A OE2   1 
ATOM   5139  N  N     . GLU A 1 2181 ? 166.162 215.365 148.989 1.00 29.70  ? 2181 GLU A N     1 
ATOM   5140  C  CA    . GLU A 1 2181 ? 165.151 214.867 149.916 1.00 26.67  ? 2181 GLU A CA    1 
ATOM   5141  C  C     . GLU A 1 2181 ? 165.795 214.140 151.089 1.00 27.27  ? 2181 GLU A C     1 
ATOM   5142  O  O     . GLU A 1 2181 ? 165.349 214.276 152.235 1.00 28.41  ? 2181 GLU A O     1 
ATOM   5143  C  CB    . GLU A 1 2181 ? 164.174 213.949 149.182 1.00 29.15  ? 2181 GLU A CB    1 
ATOM   5144  C  CG    . GLU A 1 2181 ? 163.262 214.670 148.205 1.00 33.66  ? 2181 GLU A CG    1 
ATOM   5145  C  CD    . GLU A 1 2181 ? 162.661 215.932 148.788 1.00 44.49  ? 2181 GLU A CD    1 
ATOM   5146  O  OE1   . GLU A 1 2181 ? 162.069 215.860 149.886 1.00 48.01  ? 2181 GLU A OE1   1 
ATOM   5147  O  OE2   . GLU A 1 2181 ? 162.779 216.998 148.148 1.00 51.88  ? 2181 GLU A OE2   1 
ATOM   5148  N  N     . LEU A 1 2182 ? 166.841 213.355 150.818 1.00 28.20  ? 2182 LEU A N     1 
ATOM   5149  C  CA    . LEU A 1 2182 ? 167.577 212.703 151.896 1.00 23.88  ? 2182 LEU A CA    1 
ATOM   5150  C  C     . LEU A 1 2182 ? 168.193 213.733 152.831 1.00 27.87  ? 2182 LEU A C     1 
ATOM   5151  O  O     . LEU A 1 2182 ? 168.171 213.562 154.054 1.00 37.19  ? 2182 LEU A O     1 
ATOM   5152  C  CB    . LEU A 1 2182 ? 168.661 211.791 151.320 1.00 24.13  ? 2182 LEU A CB    1 
ATOM   5153  C  CG    . LEU A 1 2182 ? 168.220 210.533 150.571 1.00 21.83  ? 2182 LEU A CG    1 
ATOM   5154  C  CD1   . LEU A 1 2182 ? 169.431 209.754 150.086 1.00 23.79  ? 2182 LEU A CD1   1 
ATOM   5155  C  CD2   . LEU A 1 2182 ? 167.339 209.660 151.443 1.00 16.78  ? 2182 LEU A CD2   1 
ATOM   5156  N  N     . LYS A 1 2183 ? 168.751 214.808 152.270 1.00 28.74  ? 2183 LYS A N     1 
ATOM   5157  C  CA    . LYS A 1 2183 ? 169.285 215.893 153.086 1.00 31.32  ? 2183 LYS A CA    1 
ATOM   5158  C  C     . LYS A 1 2183 ? 168.212 216.468 153.999 1.00 31.03  ? 2183 LYS A C     1 
ATOM   5159  O  O     . LYS A 1 2183 ? 168.424 216.620 155.208 1.00 37.00  ? 2183 LYS A O     1 
ATOM   5160  C  CB    . LYS A 1 2183 ? 169.856 216.989 152.187 1.00 34.81  ? 2183 LYS A CB    1 
ATOM   5161  C  CG    . LYS A 1 2183 ? 171.322 216.829 151.848 1.00 38.84  ? 2183 LYS A CG    1 
ATOM   5162  C  CD    . LYS A 1 2183 ? 171.918 218.144 151.374 1.00 48.65  ? 2183 LYS A CD    1 
ATOM   5163  C  CE    . LYS A 1 2183 ? 172.051 219.134 152.518 1.00 57.97  ? 2183 LYS A CE    1 
ATOM   5164  N  NZ    . LYS A 1 2183 ? 172.995 218.651 153.563 1.00 58.26  ? 2183 LYS A NZ    1 
ATOM   5165  N  N     . LYS A 1 2184 ? 167.050 216.798 153.431 1.00 28.44  ? 2184 LYS A N     1 
ATOM   5166  C  CA    . LYS A 1 2184 ? 165.975 217.382 154.228 1.00 27.41  ? 2184 LYS A CA    1 
ATOM   5167  C  C     . LYS A 1 2184 ? 165.545 216.438 155.345 1.00 28.47  ? 2184 LYS A C     1 
ATOM   5168  O  O     . LYS A 1 2184 ? 165.418 216.846 156.507 1.00 35.84  ? 2184 LYS A O     1 
ATOM   5169  C  CB    . LYS A 1 2184 ? 164.785 217.730 153.334 1.00 32.09  ? 2184 LYS A CB    1 
ATOM   5170  C  CG    . LYS A 1 2184 ? 165.025 218.902 152.398 1.00 41.53  ? 2184 LYS A CG    1 
ATOM   5171  C  CD    . LYS A 1 2184 ? 163.802 219.173 151.537 1.00 43.08  ? 2184 LYS A CD    1 
ATOM   5172  C  CE    . LYS A 1 2184 ? 163.993 220.411 150.677 1.00 45.62  ? 2184 LYS A CE    1 
ATOM   5173  N  NZ    . LYS A 1 2184 ? 165.146 220.268 149.746 1.00 45.64  ? 2184 LYS A NZ    1 
ATOM   5174  N  N     . VAL A 1 2185 ? 165.340 215.161 155.014 1.00 25.27  ? 2185 VAL A N     1 
ATOM   5175  C  CA    . VAL A 1 2185 ? 164.880 214.199 156.012 1.00 24.56  ? 2185 VAL A CA    1 
ATOM   5176  C  C     . VAL A 1 2185 ? 165.924 214.025 157.109 1.00 28.57  ? 2185 VAL A C     1 
ATOM   5177  O  O     . VAL A 1 2185 ? 165.588 213.926 158.295 1.00 34.28  ? 2185 VAL A O     1 
ATOM   5178  C  CB    . VAL A 1 2185 ? 164.528 212.858 155.340 1.00 21.79  ? 2185 VAL A CB    1 
ATOM   5179  C  CG1   . VAL A 1 2185 ? 164.224 211.800 156.386 1.00 21.99  ? 2185 VAL A CG1   1 
ATOM   5180  C  CG2   . VAL A 1 2185 ? 163.343 213.034 154.407 1.00 23.14  ? 2185 VAL A CG2   1 
ATOM   5181  N  N     . CYS A 1 2186 ? 167.206 213.995 156.735 1.00 26.90  ? 2186 CYS A N     1 
ATOM   5182  C  CA    . CYS A 1 2186 ? 168.263 213.857 157.730 1.00 23.23  ? 2186 CYS A CA    1 
ATOM   5183  C  C     . CYS A 1 2186 ? 168.315 215.065 158.655 1.00 28.74  ? 2186 CYS A C     1 
ATOM   5184  O  O     . CYS A 1 2186 ? 168.528 214.918 159.865 1.00 35.39  ? 2186 CYS A O     1 
ATOM   5185  C  CB    . CYS A 1 2186 ? 169.610 213.650 157.038 1.00 28.48  ? 2186 CYS A CB    1 
ATOM   5186  S  SG    . CYS A 1 2186 ? 169.824 212.011 156.310 1.00 38.18  ? 2186 CYS A SG    1 
ATOM   5187  N  N     . GLN A 1 2187 ? 168.133 216.272 158.109 1.00 28.59  ? 2187 GLN A N     1 
ATOM   5188  C  CA    . GLN A 1 2187 ? 168.106 217.454 158.968 1.00 32.74  ? 2187 GLN A CA    1 
ATOM   5189  C  C     . GLN A 1 2187 ? 166.916 217.424 159.918 1.00 34.30  ? 2187 GLN A C     1 
ATOM   5190  O  O     . GLN A 1 2187 ? 167.048 217.774 161.096 1.00 37.21  ? 2187 GLN A O     1 
ATOM   5191  C  CB    . GLN A 1 2187 ? 168.094 218.742 158.138 1.00 37.55  ? 2187 GLN A CB    1 
ATOM   5192  C  CG    . GLN A 1 2187 ? 169.155 218.863 157.042 1.00 46.81  ? 2187 GLN A CG    1 
ATOM   5193  C  CD    . GLN A 1 2187 ? 170.432 218.082 157.321 1.00 49.25  ? 2187 GLN A CD    1 
ATOM   5194  O  OE1   . GLN A 1 2187 ? 171.032 218.200 158.391 1.00 51.31  ? 2187 GLN A OE1   1 
ATOM   5195  N  NE2   . GLN A 1 2187 ? 170.851 217.276 156.352 1.00 40.29  ? 2187 GLN A NE2   1 
ATOM   5196  N  N     . GLU A 1 2188 ? 165.743 217.009 159.432 1.00 34.66  ? 2188 GLU A N     1 
ATOM   5197  C  CA    . GLU A 1 2188 ? 164.586 216.947 160.319 1.00 33.93  ? 2188 GLU A CA    1 
ATOM   5198  C  C     . GLU A 1 2188 ? 164.658 215.784 161.301 1.00 32.36  ? 2188 GLU A C     1 
ATOM   5199  O  O     . GLU A 1 2188 ? 163.987 215.825 162.338 1.00 37.04  ? 2188 GLU A O     1 
ATOM   5200  C  CB    . GLU A 1 2188 ? 163.286 216.866 159.514 1.00 29.99  ? 2188 GLU A CB    1 
ATOM   5201  C  CG    . GLU A 1 2188 ? 163.201 217.843 158.353 1.00 39.62  ? 2188 GLU A CG    1 
ATOM   5202  C  CD    . GLU A 1 2188 ? 162.982 219.279 158.796 1.00 57.06  ? 2188 GLU A CD    1 
ATOM   5203  O  OE1   . GLU A 1 2188 ? 162.771 219.513 160.005 1.00 61.04  ? 2188 GLU A OE1   1 
ATOM   5204  O  OE2   . GLU A 1 2188 ? 163.025 220.178 157.931 1.00 59.30  ? 2188 GLU A OE2   1 
ATOM   5205  N  N     . MET A 1 2189 ? 165.450 214.754 161.008 1.00 28.56  ? 2189 MET A N     1 
ATOM   5206  C  CA    . MET A 1 2189 ? 165.593 213.604 161.892 1.00 25.19  ? 2189 MET A CA    1 
ATOM   5207  C  C     . MET A 1 2189 ? 166.884 213.637 162.701 1.00 27.05  ? 2189 MET A C     1 
ATOM   5208  O  O     . MET A 1 2189 ? 167.247 212.624 163.306 1.00 30.50  ? 2189 MET A O     1 
ATOM   5209  C  CB    . MET A 1 2189 ? 165.515 212.305 161.089 1.00 24.21  ? 2189 MET A CB    1 
ATOM   5210  C  CG    . MET A 1 2189 ? 164.122 211.973 160.583 1.00 26.45  ? 2189 MET A CG    1 
ATOM   5211  S  SD    . MET A 1 2189 ? 164.042 210.377 159.750 1.00 38.18  ? 2189 MET A SD    1 
ATOM   5212  C  CE    . MET A 1 2189 ? 163.939 209.265 161.150 1.00 28.44  ? 2189 MET A CE    1 
ATOM   5213  N  N     . TYR A 1 2190 ? 167.585 214.773 162.717 1.00 25.49  ? 2190 TYR A N     1 
ATOM   5214  C  CA    . TYR A 1 2190 ? 168.826 214.941 163.476 1.00 23.42  ? 2190 TYR A CA    1 
ATOM   5215  C  C     . TYR A 1 2190 ? 169.895 213.938 163.051 1.00 25.06  ? 2190 TYR A C     1 
ATOM   5216  O  O     . TYR A 1 2190 ? 170.719 213.512 163.864 1.00 31.89  ? 2190 TYR A O     1 
ATOM   5217  C  CB    . TYR A 1 2190 ? 168.577 214.843 164.984 1.00 22.39  ? 2190 TYR A CB    1 
ATOM   5218  C  CG    . TYR A 1 2190 ? 167.482 215.754 165.483 1.00 28.36  ? 2190 TYR A CG    1 
ATOM   5219  C  CD1   . TYR A 1 2190 ? 167.579 217.131 165.341 1.00 30.71  ? 2190 TYR A CD1   1 
ATOM   5220  C  CD2   . TYR A 1 2190 ? 166.350 215.237 166.098 1.00 28.31  ? 2190 TYR A CD2   1 
ATOM   5221  C  CE1   . TYR A 1 2190 ? 166.579 217.966 165.795 1.00 32.20  ? 2190 TYR A CE1   1 
ATOM   5222  C  CE2   . TYR A 1 2190 ? 165.346 216.064 166.556 1.00 28.95  ? 2190 TYR A CE2   1 
ATOM   5223  C  CZ    . TYR A 1 2190 ? 165.465 217.428 166.403 1.00 33.07  ? 2190 TYR A CZ    1 
ATOM   5224  O  OH    . TYR A 1 2190 ? 164.466 218.256 166.858 1.00 44.30  ? 2190 TYR A OH    1 
ATOM   5225  N  N     . LEU A 1 2191 ? 169.893 213.555 161.780 1.00 22.70  ? 2191 LEU A N     1 
ATOM   5226  C  CA    . LEU A 1 2191 ? 170.862 212.611 161.249 1.00 21.59  ? 2191 LEU A CA    1 
ATOM   5227  C  C     . LEU A 1 2191 ? 171.922 213.337 160.429 1.00 25.40  ? 2191 LEU A C     1 
ATOM   5228  O  O     . LEU A 1 2191 ? 171.722 214.459 159.959 1.00 33.39  ? 2191 LEU A O     1 
ATOM   5229  C  CB    . LEU A 1 2191 ? 170.171 211.546 160.394 1.00 22.16  ? 2191 LEU A CB    1 
ATOM   5230  C  CG    . LEU A 1 2191 ? 169.116 210.692 161.099 1.00 19.75  ? 2191 LEU A CG    1 
ATOM   5231  C  CD1   . LEU A 1 2191 ? 168.760 209.485 160.255 1.00 16.03  ? 2191 LEU A CD1   1 
ATOM   5232  C  CD2   . LEU A 1 2191 ? 169.599 210.259 162.473 1.00 24.29  ? 2191 LEU A CD2   1 
ATOM   5233  N  N     . THR A 1 2192 ? 173.062 212.675 160.263 1.00 26.15  ? 2192 THR A N     1 
ATOM   5234  C  CA    . THR A 1 2192 ? 174.203 213.234 159.552 1.00 28.24  ? 2192 THR A CA    1 
ATOM   5235  C  C     . THR A 1 2192 ? 174.172 212.785 158.098 1.00 34.65  ? 2192 THR A C     1 
ATOM   5236  O  O     . THR A 1 2192 ? 174.073 211.587 157.814 1.00 35.77  ? 2192 THR A O     1 
ATOM   5237  C  CB    . THR A 1 2192 ? 175.517 212.807 160.207 1.00 27.01  ? 2192 THR A CB    1 
ATOM   5238  O  OG1   . THR A 1 2192 ? 175.628 213.415 161.500 1.00 32.95  ? 2192 THR A OG1   1 
ATOM   5239  C  CG2   . THR A 1 2192 ? 176.702 213.227 159.354 1.00 27.06  ? 2192 THR A CG2   1 
ATOM   5240  N  N     . TYR A 1 2193 ? 174.255 213.747 157.184 1.00 42.40  ? 2193 TYR A N     1 
ATOM   5241  C  CA    . TYR A 1 2193 ? 174.278 213.482 155.754 1.00 40.76  ? 2193 TYR A CA    1 
ATOM   5242  C  C     . TYR A 1 2193 ? 175.643 213.861 155.198 1.00 43.68  ? 2193 TYR A C     1 
ATOM   5243  O  O     . TYR A 1 2193 ? 176.225 214.877 155.593 1.00 50.95  ? 2193 TYR A O     1 
ATOM   5244  C  CB    . TYR A 1 2193 ? 173.160 214.256 155.038 1.00 34.23  ? 2193 TYR A CB    1 
ATOM   5245  C  CG    . TYR A 1 2193 ? 173.160 214.159 153.522 1.00 42.78  ? 2193 TYR A CG    1 
ATOM   5246  C  CD1   . TYR A 1 2193 ? 172.198 213.410 152.860 1.00 41.90  ? 2193 TYR A CD1   1 
ATOM   5247  C  CD2   . TYR A 1 2193 ? 174.084 214.860 152.750 1.00 44.43  ? 2193 TYR A CD2   1 
ATOM   5248  C  CE1   . TYR A 1 2193 ? 172.181 213.324 151.482 1.00 39.83  ? 2193 TYR A CE1   1 
ATOM   5249  C  CE2   . TYR A 1 2193 ? 174.075 214.777 151.374 1.00 43.81  ? 2193 TYR A CE2   1 
ATOM   5250  C  CZ    . TYR A 1 2193 ? 173.120 214.012 150.745 1.00 43.08  ? 2193 TYR A CZ    1 
ATOM   5251  O  OH    . TYR A 1 2193 ? 173.107 213.935 149.373 1.00 52.03  ? 2193 TYR A OH    1 
ATOM   5252  N  N     . GLY A 1 2194 ? 176.146 213.046 154.284 1.00 37.54  ? 2194 GLY A N     1 
ATOM   5253  C  CA    . GLY A 1 2194 ? 177.418 213.323 153.642 1.00 41.34  ? 2194 GLY A CA    1 
ATOM   5254  C  C     . GLY A 1 2194 ? 177.422 212.803 152.224 1.00 45.49  ? 2194 GLY A C     1 
ATOM   5255  O  O     . GLY A 1 2194 ? 176.711 211.849 151.891 1.00 44.20  ? 2194 GLY A O     1 
ATOM   5256  N  N     . ASP A 1 2195 ? 178.227 213.441 151.381 1.00 52.25  ? 2195 ASP A N     1 
ATOM   5257  C  CA    . ASP A 1 2195 ? 178.365 213.064 149.982 1.00 56.25  ? 2195 ASP A CA    1 
ATOM   5258  C  C     . ASP A 1 2195 ? 179.796 212.616 149.718 1.00 55.54  ? 2195 ASP A C     1 
ATOM   5259  O  O     . ASP A 1 2195 ? 180.743 213.362 149.989 1.00 58.56  ? 2195 ASP A O     1 
ATOM   5260  C  CB    . ASP A 1 2195 ? 177.997 214.229 149.060 1.00 56.09  ? 2195 ASP A CB    1 
ATOM   5261  C  CG    . ASP A 1 2195 ? 176.500 214.424 148.937 1.00 55.48  ? 2195 ASP A CG    1 
ATOM   5262  O  OD1   . ASP A 1 2195 ? 175.761 213.419 148.991 1.00 50.65  ? 2195 ASP A OD1   1 
ATOM   5263  O  OD2   . ASP A 1 2195 ? 176.060 215.583 148.786 1.00 54.41  ? 2195 ASP A OD2   1 
ATOM   5264  N  N     . GLY A 1 2196 ? 179.948 211.407 149.188 1.00 53.01  ? 2196 GLY A N     1 
ATOM   5265  C  CA    . GLY A 1 2196 ? 181.263 210.890 148.867 1.00 57.68  ? 2196 GLY A CA    1 
ATOM   5266  C  C     . GLY A 1 2196 ? 182.078 210.500 150.082 1.00 59.18  ? 2196 GLY A C     1 
ATOM   5267  O  O     . GLY A 1 2196 ? 181.719 209.567 150.806 1.00 60.67  ? 2196 GLY A O     1 
ATOM   5268  N  N     . GLU A 1 2197 ? 183.181 211.210 150.317 1.00 60.86  ? 2197 GLU A N     1 
ATOM   5269  C  CA    . GLU A 1 2197 ? 184.090 210.910 151.414 1.00 59.95  ? 2197 GLU A CA    1 
ATOM   5270  C  C     . GLU A 1 2197 ? 183.817 211.746 152.657 1.00 60.46  ? 2197 GLU A C     1 
ATOM   5271  O  O     . GLU A 1 2197 ? 184.574 211.657 153.628 1.00 59.70  ? 2197 GLU A O     1 
ATOM   5272  C  CB    . GLU A 1 2197 ? 185.540 211.103 150.964 1.00 58.04  ? 2197 GLU A CB    1 
ATOM   5273  C  CG    . GLU A 1 2197 ? 186.013 210.093 149.930 1.00 62.95  ? 2197 GLU A CG    1 
ATOM   5274  C  CD    . GLU A 1 2197 ? 186.551 208.820 150.554 1.00 70.77  ? 2197 GLU A CD    1 
ATOM   5275  O  OE1   . GLU A 1 2197 ? 185.853 208.227 151.404 1.00 68.98  ? 2197 GLU A OE1   1 
ATOM   5276  O  OE2   . GLU A 1 2197 ? 187.674 208.410 150.195 1.00 73.72  ? 2197 GLU A OE2   1 
ATOM   5277  N  N     . GLU A 1 2198 ? 182.761 212.556 152.650 1.00 54.97  ? 2198 GLU A N     1 
ATOM   5278  C  CA    . GLU A 1 2198 ? 182.408 213.340 153.823 1.00 46.29  ? 2198 GLU A CA    1 
ATOM   5279  C  C     . GLU A 1 2198 ? 181.889 212.423 154.930 1.00 43.31  ? 2198 GLU A C     1 
ATOM   5280  O  O     . GLU A 1 2198 ? 181.714 211.215 154.751 1.00 40.45  ? 2198 GLU A O     1 
ATOM   5281  C  CB    . GLU A 1 2198 ? 181.368 214.399 153.463 1.00 44.71  ? 2198 GLU A CB    1 
ATOM   5282  C  CG    . GLU A 1 2198 ? 181.773 215.311 152.319 1.00 54.24  ? 2198 GLU A CG    1 
ATOM   5283  C  CD    . GLU A 1 2198 ? 180.631 216.191 151.846 1.00 61.71  ? 2198 GLU A CD    1 
ATOM   5284  O  OE1   . GLU A 1 2198 ? 179.632 216.319 152.584 1.00 60.88  ? 2198 GLU A OE1   1 
ATOM   5285  O  OE2   . GLU A 1 2198 ? 180.733 216.754 150.736 1.00 63.25  ? 2198 GLU A OE2   1 
ATOM   5286  N  N     . VAL A 1 2199 ? 181.640 213.014 156.099 1.00 48.23  ? 2199 VAL A N     1 
ATOM   5287  C  CA    . VAL A 1 2199 ? 181.095 212.255 157.216 1.00 40.87  ? 2199 VAL A CA    1 
ATOM   5288  C  C     . VAL A 1 2199 ? 179.661 211.860 156.898 1.00 37.90  ? 2199 VAL A C     1 
ATOM   5289  O  O     . VAL A 1 2199 ? 178.825 212.708 156.561 1.00 38.59  ? 2199 VAL A O     1 
ATOM   5290  C  CB    . VAL A 1 2199 ? 181.177 213.071 158.514 1.00 37.05  ? 2199 VAL A CB    1 
ATOM   5291  C  CG1   . VAL A 1 2199 ? 180.541 212.306 159.663 1.00 30.00  ? 2199 VAL A CG1   1 
ATOM   5292  C  CG2   . VAL A 1 2199 ? 182.624 213.415 158.832 1.00 39.24  ? 2199 VAL A CG2   1 
ATOM   5293  N  N     . GLY A 1 2200 ? 179.369 210.566 157.004 1.00 33.88  ? 2200 GLY A N     1 
ATOM   5294  C  CA    . GLY A 1 2200 ? 178.061 210.058 156.653 1.00 30.55  ? 2200 GLY A CA    1 
ATOM   5295  C  C     . GLY A 1 2200 ? 177.863 209.749 155.189 1.00 31.60  ? 2200 GLY A C     1 
ATOM   5296  O  O     . GLY A 1 2200 ? 176.739 209.428 154.788 1.00 35.53  ? 2200 GLY A O     1 
ATOM   5297  N  N     . GLY A 1 2201 ? 178.916 209.839 154.374 1.00 32.10  ? 2201 GLY A N     1 
ATOM   5298  C  CA    . GLY A 1 2201 ? 178.769 209.548 152.958 1.00 28.68  ? 2201 GLY A CA    1 
ATOM   5299  C  C     . GLY A 1 2201 ? 178.442 208.092 152.685 1.00 28.36  ? 2201 GLY A C     1 
ATOM   5300  O  O     . GLY A 1 2201 ? 177.585 207.786 151.852 1.00 30.25  ? 2201 GLY A O     1 
ATOM   5301  N  N     . MET A 1 2202 ? 179.115 207.176 153.387 1.00 28.43  ? 2202 MET A N     1 
ATOM   5302  C  CA    . MET A 1 2202 ? 178.880 205.751 153.173 1.00 26.32  ? 2202 MET A CA    1 
ATOM   5303  C  C     . MET A 1 2202 ? 177.447 205.370 153.518 1.00 20.53  ? 2202 MET A C     1 
ATOM   5304  O  O     . MET A 1 2202 ? 176.842 204.522 152.851 1.00 22.90  ? 2202 MET A O     1 
ATOM   5305  C  CB    . MET A 1 2202 ? 179.867 204.929 154.002 1.00 29.51  ? 2202 MET A CB    1 
ATOM   5306  C  CG    . MET A 1 2202 ? 181.314 205.068 153.565 1.00 43.01  ? 2202 MET A CG    1 
ATOM   5307  S  SD    . MET A 1 2202 ? 182.448 204.149 154.624 1.00 81.94  ? 2202 MET A SD    1 
ATOM   5308  C  CE    . MET A 1 2202 ? 182.041 202.464 154.173 1.00 51.68  ? 2202 MET A CE    1 
ATOM   5309  N  N     . TRP A 1 2203 ? 176.886 205.985 154.560 1.00 18.05  ? 2203 TRP A N     1 
ATOM   5310  C  CA    . TRP A 1 2203 ? 175.500 205.708 154.921 1.00 18.02  ? 2203 TRP A CA    1 
ATOM   5311  C  C     . TRP A 1 2203 ? 174.544 206.158 153.822 1.00 18.65  ? 2203 TRP A C     1 
ATOM   5312  O  O     . TRP A 1 2203 ? 173.564 205.468 153.520 1.00 21.72  ? 2203 TRP A O     1 
ATOM   5313  C  CB    . TRP A 1 2203 ? 175.166 206.387 156.249 1.00 18.93  ? 2203 TRP A CB    1 
ATOM   5314  C  CG    . TRP A 1 2203 ? 173.797 206.081 156.753 1.00 13.66  ? 2203 TRP A CG    1 
ATOM   5315  C  CD1   . TRP A 1 2203 ? 173.370 204.908 157.301 1.00 10.51  ? 2203 TRP A CD1   1 
ATOM   5316  C  CD2   . TRP A 1 2203 ? 172.670 206.962 156.762 1.00 13.47  ? 2203 TRP A CD2   1 
ATOM   5317  N  NE1   . TRP A 1 2203 ? 172.045 205.004 157.648 1.00 10.26  ? 2203 TRP A NE1   1 
ATOM   5318  C  CE2   . TRP A 1 2203 ? 171.592 206.256 157.327 1.00 10.75  ? 2203 TRP A CE2   1 
ATOM   5319  C  CE3   . TRP A 1 2203 ? 172.468 208.280 156.344 1.00 15.16  ? 2203 TRP A CE3   1 
ATOM   5320  C  CZ2   . TRP A 1 2203 ? 170.332 206.823 157.488 1.00 12.67  ? 2203 TRP A CZ2   1 
ATOM   5321  C  CZ3   . TRP A 1 2203 ? 171.218 208.840 156.503 1.00 14.48  ? 2203 TRP A CZ3   1 
ATOM   5322  C  CH2   . TRP A 1 2203 ? 170.165 208.114 157.070 1.00 14.26  ? 2203 TRP A CH2   1 
ATOM   5323  N  N     . VAL A 1 2204 ? 174.816 207.309 153.206 1.00 17.68  ? 2204 VAL A N     1 
ATOM   5324  C  CA    . VAL A 1 2204 ? 173.973 207.780 152.111 1.00 15.37  ? 2204 VAL A CA    1 
ATOM   5325  C  C     . VAL A 1 2204 ? 174.119 206.875 150.893 1.00 17.89  ? 2204 VAL A C     1 
ATOM   5326  O  O     . VAL A 1 2204 ? 173.144 206.612 150.178 1.00 22.08  ? 2204 VAL A O     1 
ATOM   5327  C  CB    . VAL A 1 2204 ? 174.301 209.247 151.779 1.00 20.87  ? 2204 VAL A CB    1 
ATOM   5328  C  CG1   . VAL A 1 2204 ? 173.440 209.739 150.628 1.00 26.98  ? 2204 VAL A CG1   1 
ATOM   5329  C  CG2   . VAL A 1 2204 ? 174.097 210.120 153.005 1.00 25.56  ? 2204 VAL A CG2   1 
ATOM   5330  N  N     . GLU A 1 2205 ? 175.335 206.383 150.634 1.00 18.63  ? 2205 GLU A N     1 
ATOM   5331  C  CA    . GLU A 1 2205 ? 175.514 205.409 149.560 1.00 17.31  ? 2205 GLU A CA    1 
ATOM   5332  C  C     . GLU A 1 2205 ? 174.707 204.147 149.830 1.00 16.92  ? 2205 GLU A C     1 
ATOM   5333  O  O     . GLU A 1 2205 ? 174.093 203.585 148.915 1.00 21.62  ? 2205 GLU A O     1 
ATOM   5334  C  CB    . GLU A 1 2205 ? 176.994 205.066 149.388 1.00 22.99  ? 2205 GLU A CB    1 
ATOM   5335  C  CG    . GLU A 1 2205 ? 177.911 206.262 149.208 1.00 37.00  ? 2205 GLU A CG    1 
ATOM   5336  C  CD    . GLU A 1 2205 ? 178.036 206.694 147.763 1.00 58.53  ? 2205 GLU A CD    1 
ATOM   5337  O  OE1   . GLU A 1 2205 ? 177.774 205.864 146.867 1.00 67.02  ? 2205 GLU A OE1   1 
ATOM   5338  O  OE2   . GLU A 1 2205 ? 178.398 207.865 147.521 1.00 55.16  ? 2205 GLU A OE2   1 
ATOM   5339  N  N     . LYS A 1 2206 ? 174.697 203.686 151.082 1.00 17.31  ? 2206 LYS A N     1 
ATOM   5340  C  CA    . LYS A 1 2206 ? 173.901 202.515 151.437 1.00 12.32  ? 2206 LYS A CA    1 
ATOM   5341  C  C     . LYS A 1 2206 ? 172.412 202.785 151.259 1.00 12.73  ? 2206 LYS A C     1 
ATOM   5342  O  O     . LYS A 1 2206 ? 171.664 201.906 150.819 1.00 15.82  ? 2206 LYS A O     1 
ATOM   5343  C  CB    . LYS A 1 2206 ? 174.204 202.091 152.873 1.00 10.26  ? 2206 LYS A CB    1 
ATOM   5344  C  CG    . LYS A 1 2206 ? 175.474 201.273 153.016 1.00 10.60  ? 2206 LYS A CG    1 
ATOM   5345  C  CD    . LYS A 1 2206 ? 175.354 199.948 152.286 1.00 9.75   ? 2206 LYS A CD    1 
ATOM   5346  C  CE    . LYS A 1 2206 ? 176.693 199.509 151.721 1.00 13.66  ? 2206 LYS A CE    1 
ATOM   5347  N  NZ    . LYS A 1 2206 ? 176.593 198.193 151.032 1.00 11.42  ? 2206 LYS A NZ    1 
ATOM   5348  N  N     . VAL A 1 2207 ? 171.963 203.994 151.601 1.00 13.64  ? 2207 VAL A N     1 
ATOM   5349  C  CA    . VAL A 1 2207 ? 170.559 204.352 151.407 1.00 12.00  ? 2207 VAL A CA    1 
ATOM   5350  C  C     . VAL A 1 2207 ? 170.199 204.328 149.926 1.00 13.23  ? 2207 VAL A C     1 
ATOM   5351  O  O     . VAL A 1 2207 ? 169.139 203.822 149.534 1.00 17.04  ? 2207 VAL A O     1 
ATOM   5352  C  CB    . VAL A 1 2207 ? 170.266 205.726 152.040 1.00 10.71  ? 2207 VAL A CB    1 
ATOM   5353  C  CG1   . VAL A 1 2207 ? 168.906 206.240 151.596 1.00 10.87  ? 2207 VAL A CG1   1 
ATOM   5354  C  CG2   . VAL A 1 2207 ? 170.331 205.637 153.553 1.00 10.71  ? 2207 VAL A CG2   1 
ATOM   5355  N  N     . LEU A 1 2208 ? 171.073 204.876 149.079 1.00 12.92  ? 2208 LEU A N     1 
ATOM   5356  C  CA    . LEU A 1 2208 ? 170.814 204.865 147.641 1.00 13.05  ? 2208 LEU A CA    1 
ATOM   5357  C  C     . LEU A 1 2208 ? 170.808 203.443 147.087 1.00 14.30  ? 2208 LEU A C     1 
ATOM   5358  O  O     . LEU A 1 2208 ? 169.985 203.107 146.226 1.00 21.57  ? 2208 LEU A O     1 
ATOM   5359  C  CB    . LEU A 1 2208 ? 171.849 205.724 146.915 1.00 14.99  ? 2208 LEU A CB    1 
ATOM   5360  C  CG    . LEU A 1 2208 ? 171.839 207.214 147.261 1.00 18.16  ? 2208 LEU A CG    1 
ATOM   5361  C  CD1   . LEU A 1 2208 ? 172.854 207.967 146.419 1.00 23.54  ? 2208 LEU A CD1   1 
ATOM   5362  C  CD2   . LEU A 1 2208 ? 170.451 207.804 147.086 1.00 16.85  ? 2208 LEU A CD2   1 
ATOM   5363  N  N     . GLN A 1 2209 ? 171.721 202.595 147.566 1.00 11.68  ? 2209 GLN A N     1 
ATOM   5364  C  CA    . GLN A 1 2209 ? 171.724 201.197 147.148 1.00 12.14  ? 2209 GLN A CA    1 
ATOM   5365  C  C     . GLN A 1 2209 ? 170.444 200.493 147.578 1.00 14.25  ? 2209 GLN A C     1 
ATOM   5366  O  O     . GLN A 1 2209 ? 169.892 199.675 146.832 1.00 20.91  ? 2209 GLN A O     1 
ATOM   5367  C  CB    . GLN A 1 2209 ? 172.949 200.483 147.717 1.00 10.78  ? 2209 GLN A CB    1 
ATOM   5368  C  CG    . GLN A 1 2209 ? 174.267 200.948 147.124 1.00 11.69  ? 2209 GLN A CG    1 
ATOM   5369  C  CD    . GLN A 1 2209 ? 175.464 200.359 147.838 1.00 12.10  ? 2209 GLN A CD    1 
ATOM   5370  O  OE1   . GLN A 1 2209 ? 175.318 199.561 148.763 1.00 14.95  ? 2209 GLN A OE1   1 
ATOM   5371  N  NE2   . GLN A 1 2209 ? 176.659 200.749 147.412 1.00 13.80  ? 2209 GLN A NE2   1 
ATOM   5372  N  N     . LEU A 1 2210 ? 169.960 200.796 148.785 1.00 13.93  ? 2210 LEU A N     1 
ATOM   5373  C  CA    . LEU A 1 2210 ? 168.693 200.238 149.243 1.00 12.65  ? 2210 LEU A CA    1 
ATOM   5374  C  C     . LEU A 1 2210 ? 167.545 200.694 148.355 1.00 13.54  ? 2210 LEU A C     1 
ATOM   5375  O  O     . LEU A 1 2210 ? 166.641 199.910 148.045 1.00 17.87  ? 2210 LEU A O     1 
ATOM   5376  C  CB    . LEU A 1 2210 ? 168.444 200.641 150.697 1.00 12.26  ? 2210 LEU A CB    1 
ATOM   5377  C  CG    . LEU A 1 2210 ? 167.110 200.228 151.320 1.00 15.62  ? 2210 LEU A CG    1 
ATOM   5378  C  CD1   . LEU A 1 2210 ? 167.051 198.723 151.508 1.00 19.92  ? 2210 LEU A CD1   1 
ATOM   5379  C  CD2   . LEU A 1 2210 ? 166.897 200.945 152.641 1.00 10.83  ? 2210 LEU A CD2   1 
ATOM   5380  N  N     . TYR A 1 2211 ? 167.565 201.961 147.936 1.00 13.25  ? 2211 TYR A N     1 
ATOM   5381  C  CA    . TYR A 1 2211 ? 166.549 202.452 147.008 1.00 14.50  ? 2211 TYR A CA    1 
ATOM   5382  C  C     . TYR A 1 2211 ? 166.596 201.694 145.688 1.00 19.24  ? 2211 TYR A C     1 
ATOM   5383  O  O     . TYR A 1 2211 ? 165.553 201.326 145.134 1.00 24.87  ? 2211 TYR A O     1 
ATOM   5384  C  CB    . TYR A 1 2211 ? 166.738 203.948 146.765 1.00 16.39  ? 2211 TYR A CB    1 
ATOM   5385  C  CG    . TYR A 1 2211 ? 165.852 204.509 145.676 1.00 22.98  ? 2211 TYR A CG    1 
ATOM   5386  C  CD1   . TYR A 1 2211 ? 164.477 204.318 145.705 1.00 23.59  ? 2211 TYR A CD1   1 
ATOM   5387  C  CD2   . TYR A 1 2211 ? 166.391 205.224 144.616 1.00 26.30  ? 2211 TYR A CD2   1 
ATOM   5388  C  CE1   . TYR A 1 2211 ? 163.665 204.828 144.713 1.00 27.38  ? 2211 TYR A CE1   1 
ATOM   5389  C  CE2   . TYR A 1 2211 ? 165.586 205.738 143.619 1.00 30.14  ? 2211 TYR A CE2   1 
ATOM   5390  C  CZ    . TYR A 1 2211 ? 164.224 205.538 143.672 1.00 33.30  ? 2211 TYR A CZ    1 
ATOM   5391  O  OH    . TYR A 1 2211 ? 163.418 206.048 142.681 1.00 47.66  ? 2211 TYR A OH    1 
ATOM   5392  N  N     . GLN A 1 2212 ? 167.800 201.455 145.167 1.00 18.13  ? 2212 GLN A N     1 
ATOM   5393  C  CA    . GLN A 1 2212 ? 167.933 200.721 143.911 1.00 17.00  ? 2212 GLN A CA    1 
ATOM   5394  C  C     . GLN A 1 2212 ? 167.406 199.296 144.049 1.00 18.77  ? 2212 GLN A C     1 
ATOM   5395  O  O     . GLN A 1 2212 ? 166.694 198.793 143.169 1.00 24.36  ? 2212 GLN A O     1 
ATOM   5396  C  CB    . GLN A 1 2212 ? 169.394 200.717 143.462 1.00 21.81  ? 2212 GLN A CB    1 
ATOM   5397  C  CG    . GLN A 1 2212 ? 169.946 202.099 143.155 1.00 27.99  ? 2212 GLN A CG    1 
ATOM   5398  C  CD    . GLN A 1 2212 ? 171.342 202.054 142.570 1.00 43.55  ? 2212 GLN A CD    1 
ATOM   5399  O  OE1   . GLN A 1 2212 ? 171.599 202.613 141.505 1.00 49.68  ? 2212 GLN A OE1   1 
ATOM   5400  N  NE2   . GLN A 1 2212 ? 172.254 201.385 143.265 1.00 35.72  ? 2212 GLN A NE2   1 
ATOM   5401  N  N     . ILE A 1 2213 ? 167.745 198.629 145.156 1.00 18.13  ? 2213 ILE A N     1 
ATOM   5402  C  CA    . ILE A 1 2213 ? 167.280 197.260 145.371 1.00 16.78  ? 2213 ILE A CA    1 
ATOM   5403  C  C     . ILE A 1 2213 ? 165.764 197.230 145.527 1.00 15.77  ? 2213 ILE A C     1 
ATOM   5404  O  O     . ILE A 1 2213 ? 165.095 196.302 145.057 1.00 17.68  ? 2213 ILE A O     1 
ATOM   5405  C  CB    . ILE A 1 2213 ? 167.994 196.633 146.583 1.00 15.26  ? 2213 ILE A CB    1 
ATOM   5406  C  CG1   . ILE A 1 2213 ? 169.505 196.602 146.353 1.00 15.65  ? 2213 ILE A CG1   1 
ATOM   5407  C  CG2   . ILE A 1 2213 ? 167.489 195.223 146.832 1.00 17.93  ? 2213 ILE A CG2   1 
ATOM   5408  C  CD1   . ILE A 1 2213 ? 169.945 195.596 145.314 1.00 18.78  ? 2213 ILE A CD1   1 
ATOM   5409  N  N     . THR A 1 2214 ? 165.198 198.245 146.185 1.00 16.73  ? 2214 THR A N     1 
ATOM   5410  C  CA    . THR A 1 2214 ? 163.745 198.363 146.260 1.00 16.15  ? 2214 THR A CA    1 
ATOM   5411  C  C     . THR A 1 2214 ? 163.140 198.515 144.871 1.00 20.26  ? 2214 THR A C     1 
ATOM   5412  O  O     . THR A 1 2214 ? 162.099 197.921 144.567 1.00 25.64  ? 2214 THR A O     1 
ATOM   5413  C  CB    . THR A 1 2214 ? 163.362 199.552 147.145 1.00 16.61  ? 2214 THR A CB    1 
ATOM   5414  O  OG1   . THR A 1 2214 ? 163.582 199.222 148.521 1.00 18.27  ? 2214 THR A OG1   1 
ATOM   5415  C  CG2   . THR A 1 2214 ? 161.900 199.927 146.951 1.00 18.85  ? 2214 THR A CG2   1 
ATOM   5416  N  N     . GLN A 1 2215 ? 163.787 199.306 144.013 1.00 24.58  ? 2215 GLN A N     1 
ATOM   5417  C  CA    . GLN A 1 2215 ? 163.294 199.484 142.652 1.00 25.43  ? 2215 GLN A CA    1 
ATOM   5418  C  C     . GLN A 1 2215 ? 163.313 198.173 141.874 1.00 25.82  ? 2215 GLN A C     1 
ATOM   5419  O  O     . GLN A 1 2215 ? 162.376 197.875 141.125 1.00 30.12  ? 2215 GLN A O     1 
ATOM   5420  C  CB    . GLN A 1 2215 ? 164.122 200.545 141.926 1.00 25.22  ? 2215 GLN A CB    1 
ATOM   5421  C  CG    . GLN A 1 2215 ? 163.886 201.976 142.391 1.00 30.75  ? 2215 GLN A CG    1 
ATOM   5422  C  CD    . GLN A 1 2215 ? 162.448 202.431 142.214 1.00 44.65  ? 2215 GLN A CD    1 
ATOM   5423  O  OE1   . GLN A 1 2215 ? 161.564 202.068 142.991 1.00 48.68  ? 2215 GLN A OE1   1 
ATOM   5424  N  NE2   . GLN A 1 2215 ? 162.208 203.231 141.182 1.00 49.25  ? 2215 GLN A NE2   1 
ATOM   5425  N  N     . ILE A 1 2216 ? 164.371 197.373 142.037 1.00 23.40  ? 2216 ILE A N     1 
ATOM   5426  C  CA    . ILE A 1 2216 ? 164.545 196.181 141.207 1.00 19.89  ? 2216 ILE A CA    1 
ATOM   5427  C  C     . ILE A 1 2216 ? 164.084 194.890 141.878 1.00 22.40  ? 2216 ILE A C     1 
ATOM   5428  O  O     . ILE A 1 2216 ? 164.091 193.836 141.222 1.00 25.44  ? 2216 ILE A O     1 
ATOM   5429  C  CB    . ILE A 1 2216 ? 166.012 196.027 140.751 1.00 21.44  ? 2216 ILE A CB    1 
ATOM   5430  C  CG1   . ILE A 1 2216 ? 166.886 195.537 141.906 1.00 22.23  ? 2216 ILE A CG1   1 
ATOM   5431  C  CG2   . ILE A 1 2216 ? 166.537 197.340 140.192 1.00 25.38  ? 2216 ILE A CG2   1 
ATOM   5432  C  CD1   . ILE A 1 2216 ? 168.365 195.525 141.587 1.00 23.05  ? 2216 ILE A CD1   1 
ATOM   5433  N  N     . ASN A 1 2217 ? 163.685 194.929 143.148 1.00 24.22  ? 2217 ASN A N     1 
ATOM   5434  C  CA    . ASN A 1 2217 ? 163.238 193.734 143.852 1.00 19.53  ? 2217 ASN A CA    1 
ATOM   5435  C  C     . ASN A 1 2217 ? 161.986 194.032 144.664 1.00 17.44  ? 2217 ASN A C     1 
ATOM   5436  O  O     . ASN A 1 2217 ? 161.735 195.175 145.053 1.00 26.90  ? 2217 ASN A O     1 
ATOM   5437  C  CB    . ASN A 1 2217 ? 164.324 193.182 144.789 1.00 17.01  ? 2217 ASN A CB    1 
ATOM   5438  C  CG    . ASN A 1 2217 ? 165.548 192.695 144.043 1.00 27.81  ? 2217 ASN A CG    1 
ATOM   5439  O  OD1   . ASN A 1 2217 ? 166.634 193.257 144.177 1.00 33.55  ? 2217 ASN A OD1   1 
ATOM   5440  N  ND2   . ASN A 1 2217 ? 165.380 191.639 143.257 1.00 36.34  ? 2217 ASN A ND2   1 
ATOM   5441  N  N     . HIS A 1 2218 ? 161.200 192.985 144.915 1.00 15.74  ? 2218 HIS A N     1 
ATOM   5442  C  CA    . HIS A 1 2218 ? 160.076 193.058 145.837 1.00 18.02  ? 2218 HIS A CA    1 
ATOM   5443  C  C     . HIS A 1 2218 ? 160.364 192.366 147.161 1.00 16.32  ? 2218 HIS A C     1 
ATOM   5444  O  O     . HIS A 1 2218 ? 159.494 192.343 148.037 1.00 14.55  ? 2218 HIS A O     1 
ATOM   5445  C  CB    . HIS A 1 2218 ? 158.815 192.463 145.197 1.00 18.45  ? 2218 HIS A CB    1 
ATOM   5446  C  CG    . HIS A 1 2218 ? 158.882 190.983 144.979 1.00 17.49  ? 2218 HIS A CG    1 
ATOM   5447  N  ND1   . HIS A 1 2218 ? 159.662 190.410 143.999 1.00 20.68  ? 2218 HIS A ND1   1 
ATOM   5448  C  CD2   . HIS A 1 2218 ? 158.258 189.961 145.610 1.00 16.60  ? 2218 HIS A CD2   1 
ATOM   5449  C  CE1   . HIS A 1 2218 ? 159.520 189.097 144.038 1.00 22.58  ? 2218 HIS A CE1   1 
ATOM   5450  N  NE2   . HIS A 1 2218 ? 158.673 188.799 145.007 1.00 19.93  ? 2218 HIS A NE2   1 
ATOM   5451  N  N     . GLY A 1 2219 ? 161.558 191.801 147.325 1.00 20.00  ? 2219 GLY A N     1 
ATOM   5452  C  CA    . GLY A 1 2219 ? 161.985 191.229 148.585 1.00 15.33  ? 2219 GLY A CA    1 
ATOM   5453  C  C     . GLY A 1 2219 ? 163.387 191.682 148.937 1.00 17.82  ? 2219 GLY A C     1 
ATOM   5454  O  O     . GLY A 1 2219 ? 164.329 191.437 148.179 1.00 26.03  ? 2219 GLY A O     1 
ATOM   5455  N  N     . LEU A 1 2220 ? 163.541 192.343 150.080 1.00 16.44  ? 2220 LEU A N     1 
ATOM   5456  C  CA    . LEU A 1 2220 ? 164.797 192.973 150.454 1.00 14.73  ? 2220 LEU A CA    1 
ATOM   5457  C  C     . LEU A 1 2220 ? 165.271 192.466 151.808 1.00 15.03  ? 2220 LEU A C     1 
ATOM   5458  O  O     . LEU A 1 2220 ? 164.468 192.093 152.667 1.00 17.30  ? 2220 LEU A O     1 
ATOM   5459  C  CB    . LEU A 1 2220 ? 164.656 194.497 150.511 1.00 13.30  ? 2220 LEU A CB    1 
ATOM   5460  C  CG    . LEU A 1 2220 ? 164.459 195.234 149.189 1.00 19.34  ? 2220 LEU A CG    1 
ATOM   5461  C  CD1   . LEU A 1 2220 ? 162.981 195.436 148.900 1.00 19.55  ? 2220 LEU A CD1   1 
ATOM   5462  C  CD2   . LEU A 1 2220 ? 165.183 196.562 149.237 1.00 23.95  ? 2220 LEU A CD2   1 
ATOM   5463  N  N     . MET A 1 2221 ? 166.589 192.459 151.988 1.00 11.97  ? 2221 MET A N     1 
ATOM   5464  C  CA    . MET A 1 2221 ? 167.196 192.156 153.276 1.00 11.33  ? 2221 MET A CA    1 
ATOM   5465  C  C     . MET A 1 2221 ? 168.298 193.164 153.553 1.00 14.26  ? 2221 MET A C     1 
ATOM   5466  O  O     . MET A 1 2221 ? 169.192 193.352 152.724 1.00 16.52  ? 2221 MET A O     1 
ATOM   5467  C  CB    . MET A 1 2221 ? 167.761 190.731 153.314 1.00 12.08  ? 2221 MET A CB    1 
ATOM   5468  C  CG    . MET A 1 2221 ? 166.845 189.726 153.989 1.00 15.40  ? 2221 MET A CG    1 
ATOM   5469  S  SD    . MET A 1 2221 ? 167.441 188.028 153.925 1.00 35.88  ? 2221 MET A SD    1 
ATOM   5470  C  CE    . MET A 1 2221 ? 166.029 187.148 154.586 1.00 24.35  ? 2221 MET A CE    1 
ATOM   5471  N  N     . MET A 1 2222 ? 168.228 193.810 154.713 1.00 14.52  ? 2222 MET A N     1 
ATOM   5472  C  CA    . MET A 1 2222 ? 169.268 194.722 155.182 1.00 11.71  ? 2222 MET A CA    1 
ATOM   5473  C  C     . MET A 1 2222 ? 170.079 193.973 156.233 1.00 13.52  ? 2222 MET A C     1 
ATOM   5474  O  O     . MET A 1 2222 ? 169.657 193.852 157.386 1.00 17.59  ? 2222 MET A O     1 
ATOM   5475  C  CB    . MET A 1 2222 ? 168.666 196.007 155.740 1.00 9.87   ? 2222 MET A CB    1 
ATOM   5476  C  CG    . MET A 1 2222 ? 167.799 196.767 154.753 1.00 10.14  ? 2222 MET A CG    1 
ATOM   5477  S  SD    . MET A 1 2222 ? 166.761 198.004 155.551 1.00 24.47  ? 2222 MET A SD    1 
ATOM   5478  C  CE    . MET A 1 2222 ? 165.188 197.149 155.584 1.00 14.17  ? 2222 MET A CE    1 
ATOM   5479  N  N     . VAL A 1 2223 ? 171.240 193.473 155.830 1.00 13.71  ? 2223 VAL A N     1 
ATOM   5480  C  CA    . VAL A 1 2223 ? 172.077 192.631 156.676 1.00 12.81  ? 2223 VAL A CA    1 
ATOM   5481  C  C     . VAL A 1 2223 ? 173.250 193.454 157.183 1.00 13.99  ? 2223 VAL A C     1 
ATOM   5482  O  O     . VAL A 1 2223 ? 173.889 194.187 156.418 1.00 22.67  ? 2223 VAL A O     1 
ATOM   5483  C  CB    . VAL A 1 2223 ? 172.564 191.388 155.906 1.00 12.91  ? 2223 VAL A CB    1 
ATOM   5484  C  CG1   . VAL A 1 2223 ? 173.487 190.549 156.773 1.00 18.31  ? 2223 VAL A CG1   1 
ATOM   5485  C  CG2   . VAL A 1 2223 ? 171.382 190.571 155.421 1.00 14.77  ? 2223 VAL A CG2   1 
ATOM   5486  N  N     . GLY A 1 2224 ? 173.531 193.342 158.477 1.00 11.41  ? 2224 GLY A N     1 
ATOM   5487  C  CA    . GLY A 1 2224 ? 174.646 194.036 159.072 1.00 14.21  ? 2224 GLY A CA    1 
ATOM   5488  C  C     . GLY A 1 2224 ? 174.572 194.030 160.582 1.00 16.14  ? 2224 GLY A C     1 
ATOM   5489  O  O     . GLY A 1 2224 ? 173.493 193.921 161.170 1.00 18.12  ? 2224 GLY A O     1 
ATOM   5490  N  N     . PRO A 1 2225 ? 175.724 194.161 161.241 1.00 17.34  ? 2225 PRO A N     1 
ATOM   5491  C  CA    . PRO A 1 2225 ? 175.752 194.091 162.706 1.00 17.40  ? 2225 PRO A CA    1 
ATOM   5492  C  C     . PRO A 1 2225 ? 174.855 195.142 163.342 1.00 18.55  ? 2225 PRO A C     1 
ATOM   5493  O  O     . PRO A 1 2225 ? 174.449 196.120 162.712 1.00 20.61  ? 2225 PRO A O     1 
ATOM   5494  C  CB    . PRO A 1 2225 ? 177.227 194.338 163.048 1.00 19.29  ? 2225 PRO A CB    1 
ATOM   5495  C  CG    . PRO A 1 2225 ? 177.969 193.988 161.802 1.00 18.27  ? 2225 PRO A CG    1 
ATOM   5496  C  CD    . PRO A 1 2225 ? 177.065 194.370 160.672 1.00 16.72  ? 2225 PRO A CD    1 
ATOM   5497  N  N     . SER A 1 2226 ? 174.538 194.915 164.615 1.00 18.45  ? 2226 SER A N     1 
ATOM   5498  C  CA    . SER A 1 2226 ? 173.657 195.819 165.339 1.00 17.00  ? 2226 SER A CA    1 
ATOM   5499  C  C     . SER A 1 2226 ? 174.233 197.228 165.355 1.00 17.25  ? 2226 SER A C     1 
ATOM   5500  O  O     . SER A 1 2226 ? 175.434 197.427 165.557 1.00 21.02  ? 2226 SER A O     1 
ATOM   5501  C  CB    . SER A 1 2226 ? 173.443 195.321 166.768 1.00 16.54  ? 2226 SER A CB    1 
ATOM   5502  O  OG    . SER A 1 2226 ? 172.631 196.220 167.502 1.00 19.56  ? 2226 SER A OG    1 
ATOM   5503  N  N     . GLY A 1 2227 ? 173.364 198.209 165.143 1.00 11.74  ? 2227 GLY A N     1 
ATOM   5504  C  CA    . GLY A 1 2227 ? 173.798 199.590 165.070 1.00 11.85  ? 2227 GLY A CA    1 
ATOM   5505  C  C     . GLY A 1 2227 ? 174.633 199.936 163.858 1.00 15.93  ? 2227 GLY A C     1 
ATOM   5506  O  O     . GLY A 1 2227 ? 175.647 200.634 163.987 1.00 23.44  ? 2227 GLY A O     1 
ATOM   5507  N  N     . SER A 1 2228 ? 174.239 199.456 162.681 1.00 17.36  ? 2228 SER A N     1 
ATOM   5508  C  CA    . SER A 1 2228 ? 174.879 199.837 161.433 1.00 13.98  ? 2228 SER A CA    1 
ATOM   5509  C  C     . SER A 1 2228 ? 174.058 200.838 160.634 1.00 12.27  ? 2228 SER A C     1 
ATOM   5510  O  O     . SER A 1 2228 ? 174.450 201.189 159.516 1.00 16.87  ? 2228 SER A O     1 
ATOM   5511  C  CB    . SER A 1 2228 ? 175.158 198.594 160.582 1.00 12.93  ? 2228 SER A CB    1 
ATOM   5512  O  OG    . SER A 1 2228 ? 174.031 197.738 160.549 1.00 16.68  ? 2228 SER A OG    1 
ATOM   5513  N  N     . GLY A 1 2229 ? 172.937 201.308 161.173 1.00 10.93  ? 2229 GLY A N     1 
ATOM   5514  C  CA    . GLY A 1 2229 ? 172.140 202.319 160.511 1.00 11.01  ? 2229 GLY A CA    1 
ATOM   5515  C  C     . GLY A 1 2229 ? 171.065 201.808 159.581 1.00 12.37  ? 2229 GLY A C     1 
ATOM   5516  O  O     . GLY A 1 2229 ? 170.562 202.584 158.764 1.00 15.76  ? 2229 GLY A O     1 
ATOM   5517  N  N     . LYS A 1 2230 ? 170.688 200.531 159.681 1.00 10.56  ? 2230 LYS A N     1 
ATOM   5518  C  CA    . LYS A 1 2230 ? 169.722 199.961 158.744 1.00 8.94   ? 2230 LYS A CA    1 
ATOM   5519  C  C     . LYS A 1 2230 ? 168.335 200.565 158.933 1.00 11.52  ? 2230 LYS A C     1 
ATOM   5520  O  O     . LYS A 1 2230 ? 167.685 200.979 157.962 1.00 15.17  ? 2230 LYS A O     1 
ATOM   5521  C  CB    . LYS A 1 2230 ? 169.669 198.443 158.916 1.00 9.16   ? 2230 LYS A CB    1 
ATOM   5522  C  CG    . LYS A 1 2230 ? 171.017 197.759 158.810 1.00 9.94   ? 2230 LYS A CG    1 
ATOM   5523  C  CD    . LYS A 1 2230 ? 170.964 196.345 159.358 1.00 11.83  ? 2230 LYS A CD    1 
ATOM   5524  C  CE    . LYS A 1 2230 ? 170.629 196.342 160.837 1.00 11.79  ? 2230 LYS A CE    1 
ATOM   5525  N  NZ    . LYS A 1 2230 ? 170.648 194.969 161.408 1.00 16.04  ? 2230 LYS A NZ    1 
ATOM   5526  N  N     . SER A 1 2231 ? 167.861 200.615 160.181 1.00 11.44  ? 2231 SER A N     1 
ATOM   5527  C  CA    . SER A 1 2231 ? 166.516 201.115 160.446 1.00 11.82  ? 2231 SER A CA    1 
ATOM   5528  C  C     . SER A 1 2231 ? 166.393 202.580 160.056 1.00 13.15  ? 2231 SER A C     1 
ATOM   5529  O  O     . SER A 1 2231 ? 165.422 202.984 159.403 1.00 14.15  ? 2231 SER A O     1 
ATOM   5530  C  CB    . SER A 1 2231 ? 166.164 200.915 161.920 1.00 16.36  ? 2231 SER A CB    1 
ATOM   5531  O  OG    . SER A 1 2231 ? 165.005 201.649 162.272 1.00 28.36  ? 2231 SER A OG    1 
ATOM   5532  N  N     . MET A 1 2232 ? 167.383 203.390 160.435 1.00 11.77  ? 2232 MET A N     1 
ATOM   5533  C  CA    . MET A 1 2232 ? 167.390 204.788 160.021 1.00 11.08  ? 2232 MET A CA    1 
ATOM   5534  C  C     . MET A 1 2232 ? 167.495 204.905 158.509 1.00 11.41  ? 2232 MET A C     1 
ATOM   5535  O  O     . MET A 1 2232 ? 166.873 205.786 157.906 1.00 13.36  ? 2232 MET A O     1 
ATOM   5536  C  CB    . MET A 1 2232 ? 168.533 205.538 160.702 1.00 10.89  ? 2232 MET A CB    1 
ATOM   5537  C  CG    . MET A 1 2232 ? 168.327 205.761 162.189 1.00 20.39  ? 2232 MET A CG    1 
ATOM   5538  S  SD    . MET A 1 2232 ? 166.666 206.341 162.580 1.00 37.82  ? 2232 MET A SD    1 
ATOM   5539  C  CE    . MET A 1 2232 ? 166.184 205.160 163.836 1.00 24.18  ? 2232 MET A CE    1 
ATOM   5540  N  N     . ALA A 1 2233 ? 168.269 204.019 157.877 1.00 10.99  ? 2233 ALA A N     1 
ATOM   5541  C  CA    . ALA A 1 2233 ? 168.399 204.056 156.424 1.00 9.29   ? 2233 ALA A CA    1 
ATOM   5542  C  C     . ALA A 1 2233 ? 167.046 203.890 155.748 1.00 8.10   ? 2233 ALA A C     1 
ATOM   5543  O  O     . ALA A 1 2233 ? 166.649 204.721 154.922 1.00 12.46  ? 2233 ALA A O     1 
ATOM   5544  C  CB    . ALA A 1 2233 ? 169.369 202.975 155.948 1.00 8.19   ? 2233 ALA A CB    1 
ATOM   5545  N  N     . TRP A 1 2234 ? 166.304 202.840 156.106 1.00 7.79   ? 2234 TRP A N     1 
ATOM   5546  C  CA    . TRP A 1 2234 ? 165.042 202.626 155.404 1.00 7.57   ? 2234 TRP A CA    1 
ATOM   5547  C  C     . TRP A 1 2234 ? 163.965 203.612 155.844 1.00 9.37   ? 2234 TRP A C     1 
ATOM   5548  O  O     . TRP A 1 2234 ? 163.102 203.967 155.035 1.00 12.84  ? 2234 TRP A O     1 
ATOM   5549  C  CB    . TRP A 1 2234 ? 164.566 201.174 155.549 1.00 9.35   ? 2234 TRP A CB    1 
ATOM   5550  C  CG    . TRP A 1 2234 ? 164.049 200.753 156.890 1.00 8.16   ? 2234 TRP A CG    1 
ATOM   5551  C  CD1   . TRP A 1 2234 ? 164.714 200.021 157.825 1.00 9.72   ? 2234 TRP A CD1   1 
ATOM   5552  C  CD2   . TRP A 1 2234 ? 162.739 200.988 157.423 1.00 9.94   ? 2234 TRP A CD2   1 
ATOM   5553  N  NE1   . TRP A 1 2234 ? 163.913 199.806 158.918 1.00 10.59  ? 2234 TRP A NE1   1 
ATOM   5554  C  CE2   . TRP A 1 2234 ? 162.694 200.390 158.696 1.00 10.42  ? 2234 TRP A CE2   1 
ATOM   5555  C  CE3   . TRP A 1 2234 ? 161.606 201.657 156.952 1.00 11.11  ? 2234 TRP A CE3   1 
ATOM   5556  C  CZ2   . TRP A 1 2234 ? 161.563 200.441 159.504 1.00 13.62  ? 2234 TRP A CZ2   1 
ATOM   5557  C  CZ3   . TRP A 1 2234 ? 160.486 201.708 157.756 1.00 11.46  ? 2234 TRP A CZ3   1 
ATOM   5558  C  CH2   . TRP A 1 2234 ? 160.471 201.103 159.017 1.00 13.17  ? 2234 TRP A CH2   1 
ATOM   5559  N  N     . ARG A 1 2235 ? 164.009 204.103 157.087 1.00 12.04  ? 2235 ARG A N     1 
ATOM   5560  C  CA    . ARG A 1 2235 ? 163.056 205.129 157.501 1.00 9.14   ? 2235 ARG A CA    1 
ATOM   5561  C  C     . ARG A 1 2235 ? 163.272 206.426 156.726 1.00 13.68  ? 2235 ARG A C     1 
ATOM   5562  O  O     . ARG A 1 2235 ? 162.315 207.037 156.227 1.00 17.97  ? 2235 ARG A O     1 
ATOM   5563  C  CB    . ARG A 1 2235 ? 163.178 205.372 159.005 1.00 11.21  ? 2235 ARG A CB    1 
ATOM   5564  C  CG    . ARG A 1 2235 ? 162.402 204.384 159.856 1.00 14.85  ? 2235 ARG A CG    1 
ATOM   5565  C  CD    . ARG A 1 2235 ? 162.270 204.873 161.286 1.00 28.43  ? 2235 ARG A CD    1 
ATOM   5566  N  NE    . ARG A 1 2235 ? 162.472 203.793 162.245 1.00 32.96  ? 2235 ARG A NE    1 
ATOM   5567  C  CZ    . ARG A 1 2235 ? 161.529 202.938 162.616 1.00 39.76  ? 2235 ARG A CZ    1 
ATOM   5568  N  NH1   . ARG A 1 2235 ? 160.298 203.017 162.139 1.00 33.51  ? 2235 ARG A NH1   1 
ATOM   5569  N  NH2   . ARG A 1 2235 ? 161.829 201.980 163.489 1.00 34.43  ? 2235 ARG A NH2   1 
ATOM   5570  N  N     . VAL A 1 2236 ? 164.530 206.859 156.612 1.00 13.28  ? 2236 VAL A N     1 
ATOM   5571  C  CA    . VAL A 1 2236 ? 164.846 208.067 155.860 1.00 11.88  ? 2236 VAL A CA    1 
ATOM   5572  C  C     . VAL A 1 2236 ? 164.512 207.874 154.389 1.00 14.13  ? 2236 VAL A C     1 
ATOM   5573  O  O     . VAL A 1 2236 ? 164.018 208.793 153.726 1.00 16.74  ? 2236 VAL A O     1 
ATOM   5574  C  CB    . VAL A 1 2236 ? 166.324 208.447 156.067 1.00 11.26  ? 2236 VAL A CB    1 
ATOM   5575  C  CG1   . VAL A 1 2236 ? 166.786 209.433 155.010 1.00 16.23  ? 2236 VAL A CG1   1 
ATOM   5576  C  CG2   . VAL A 1 2236 ? 166.526 209.025 157.454 1.00 15.73  ? 2236 VAL A CG2   1 
ATOM   5577  N  N     . LEU A 1 2237 ? 164.766 206.677 153.854 1.00 12.51  ? 2237 LEU A N     1 
ATOM   5578  C  CA    . LEU A 1 2237 ? 164.412 206.406 152.466 1.00 10.95  ? 2237 LEU A CA    1 
ATOM   5579  C  C     . LEU A 1 2237 ? 162.907 206.502 152.251 1.00 11.73  ? 2237 LEU A C     1 
ATOM   5580  O  O     . LEU A 1 2237 ? 162.453 207.074 151.256 1.00 19.56  ? 2237 LEU A O     1 
ATOM   5581  C  CB    . LEU A 1 2237 ? 164.925 205.029 152.051 1.00 11.24  ? 2237 LEU A CB    1 
ATOM   5582  C  CG    . LEU A 1 2237 ? 164.736 204.693 150.573 1.00 10.80  ? 2237 LEU A CG    1 
ATOM   5583  C  CD1   . LEU A 1 2237 ? 165.540 205.649 149.711 1.00 10.96  ? 2237 LEU A CD1   1 
ATOM   5584  C  CD2   . LEU A 1 2237 ? 165.126 203.253 150.297 1.00 11.99  ? 2237 LEU A CD2   1 
ATOM   5585  N  N     . LEU A 1 2238 ? 162.117 205.950 153.176 1.00 11.37  ? 2238 LEU A N     1 
ATOM   5586  C  CA    . LEU A 1 2238 ? 160.665 206.024 153.053 1.00 10.53  ? 2238 LEU A CA    1 
ATOM   5587  C  C     . LEU A 1 2238 ? 160.185 207.470 153.094 1.00 15.48  ? 2238 LEU A C     1 
ATOM   5588  O  O     . LEU A 1 2238 ? 159.354 207.884 152.277 1.00 22.41  ? 2238 LEU A O     1 
ATOM   5589  C  CB    . LEU A 1 2238 ? 160.006 205.204 154.162 1.00 11.54  ? 2238 LEU A CB    1 
ATOM   5590  C  CG    . LEU A 1 2238 ? 158.516 204.896 154.013 1.00 14.34  ? 2238 LEU A CG    1 
ATOM   5591  C  CD1   . LEU A 1 2238 ? 158.250 204.108 152.742 1.00 18.07  ? 2238 LEU A CD1   1 
ATOM   5592  C  CD2   . LEU A 1 2238 ? 158.004 204.143 155.229 1.00 13.11  ? 2238 LEU A CD2   1 
ATOM   5593  N  N     . LYS A 1 2239 ? 160.710 208.260 154.035 1.00 17.08  ? 2239 LYS A N     1 
ATOM   5594  C  CA    . LYS A 1 2239 ? 160.297 209.659 154.127 1.00 15.80  ? 2239 LYS A CA    1 
ATOM   5595  C  C     . LYS A 1 2239 ? 160.697 210.441 152.880 1.00 17.38  ? 2239 LYS A C     1 
ATOM   5596  O  O     . LYS A 1 2239 ? 159.911 211.246 152.360 1.00 21.95  ? 2239 LYS A O     1 
ATOM   5597  C  CB    . LYS A 1 2239 ? 160.890 210.304 155.378 1.00 17.95  ? 2239 LYS A CB    1 
ATOM   5598  C  CG    . LYS A 1 2239 ? 160.357 209.739 156.683 1.00 23.52  ? 2239 LYS A CG    1 
ATOM   5599  C  CD    . LYS A 1 2239 ? 160.609 210.694 157.836 1.00 28.09  ? 2239 LYS A CD    1 
ATOM   5600  C  CE    . LYS A 1 2239 ? 160.149 210.103 159.158 1.00 29.68  ? 2239 LYS A CE    1 
ATOM   5601  N  NZ    . LYS A 1 2239 ? 160.114 211.126 160.239 1.00 32.55  ? 2239 LYS A NZ    1 
ATOM   5602  N  N     . ALA A 1 2240 ? 161.918 210.219 152.386 1.00 16.80  ? 2240 ALA A N     1 
ATOM   5603  C  CA    . ALA A 1 2240 ? 162.381 210.926 151.198 1.00 16.47  ? 2240 ALA A CA    1 
ATOM   5604  C  C     . ALA A 1 2240 ? 161.558 210.550 149.975 1.00 21.23  ? 2240 ALA A C     1 
ATOM   5605  O  O     . ALA A 1 2240 ? 161.219 211.413 149.161 1.00 29.18  ? 2240 ALA A O     1 
ATOM   5606  C  CB    . ALA A 1 2240 ? 163.861 210.636 150.959 1.00 14.61  ? 2240 ALA A CB    1 
ATOM   5607  N  N     . LEU A 1 2241 ? 161.230 209.265 149.826 1.00 21.67  ? 2241 LEU A N     1 
ATOM   5608  C  CA    . LEU A 1 2241 ? 160.391 208.844 148.710 1.00 18.61  ? 2241 LEU A CA    1 
ATOM   5609  C  C     . LEU A 1 2241 ? 158.999 209.451 148.813 1.00 22.12  ? 2241 LEU A C     1 
ATOM   5610  O  O     . LEU A 1 2241 ? 158.417 209.860 147.802 1.00 30.19  ? 2241 LEU A O     1 
ATOM   5611  C  CB    . LEU A 1 2241 ? 160.314 207.319 148.657 1.00 17.50  ? 2241 LEU A CB    1 
ATOM   5612  C  CG    . LEU A 1 2241 ? 161.584 206.597 148.202 1.00 16.83  ? 2241 LEU A CG    1 
ATOM   5613  C  CD1   . LEU A 1 2241 ? 161.329 205.108 148.041 1.00 15.46  ? 2241 LEU A CD1   1 
ATOM   5614  C  CD2   . LEU A 1 2241 ? 162.110 207.199 146.910 1.00 24.65  ? 2241 LEU A CD2   1 
ATOM   5615  N  N     . GLU A 1 2242 ? 158.452 209.522 150.029 1.00 23.08  ? 2242 GLU A N     1 
ATOM   5616  C  CA    . GLU A 1 2242 ? 157.142 210.138 150.217 1.00 25.90  ? 2242 GLU A CA    1 
ATOM   5617  C  C     . GLU A 1 2242 ? 157.161 211.605 149.807 1.00 28.82  ? 2242 GLU A C     1 
ATOM   5618  O  O     . GLU A 1 2242 ? 156.251 212.081 149.120 1.00 35.31  ? 2242 GLU A O     1 
ATOM   5619  C  CB    . GLU A 1 2242 ? 156.701 209.991 151.674 1.00 28.75  ? 2242 GLU A CB    1 
ATOM   5620  C  CG    . GLU A 1 2242 ? 155.613 210.965 152.093 1.00 35.52  ? 2242 GLU A CG    1 
ATOM   5621  C  CD    . GLU A 1 2242 ? 155.151 210.744 153.519 1.00 54.80  ? 2242 GLU A CD    1 
ATOM   5622  O  OE1   . GLU A 1 2242 ? 155.014 209.572 153.926 1.00 54.76  ? 2242 GLU A OE1   1 
ATOM   5623  O  OE2   . GLU A 1 2242 ? 154.926 211.743 154.233 1.00 71.33  ? 2242 GLU A OE2   1 
ATOM   5624  N  N     . ARG A 1 2243 ? 158.197 212.339 150.218 1.00 31.35  ? 2243 ARG A N     1 
ATOM   5625  C  CA    . ARG A 1 2243 ? 158.270 213.755 149.876 1.00 30.38  ? 2243 ARG A CA    1 
ATOM   5626  C  C     . ARG A 1 2243 ? 158.662 214.003 148.423 1.00 31.81  ? 2243 ARG A C     1 
ATOM   5627  O  O     . ARG A 1 2243 ? 158.360 215.077 147.893 1.00 34.51  ? 2243 ARG A O     1 
ATOM   5628  C  CB    . ARG A 1 2243 ? 159.251 214.481 150.799 1.00 25.83  ? 2243 ARG A CB    1 
ATOM   5629  C  CG    . ARG A 1 2243 ? 158.924 214.358 152.275 1.00 30.64  ? 2243 ARG A CG    1 
ATOM   5630  C  CD    . ARG A 1 2243 ? 160.176 214.463 153.125 1.00 39.97  ? 2243 ARG A CD    1 
ATOM   5631  N  NE    . ARG A 1 2243 ? 160.452 215.842 153.510 1.00 44.92  ? 2243 ARG A NE    1 
ATOM   5632  C  CZ    . ARG A 1 2243 ? 160.342 216.310 154.746 1.00 48.29  ? 2243 ARG A CZ    1 
ATOM   5633  N  NH1   . ARG A 1 2243 ? 159.962 215.535 155.748 1.00 47.52  ? 2243 ARG A NH1   1 
ATOM   5634  N  NH2   . ARG A 1 2243 ? 160.618 217.590 154.981 1.00 51.46  ? 2243 ARG A NH2   1 
ATOM   5635  N  N     . LEU A 1 2244 ? 159.318 213.046 147.770 1.00 33.00  ? 2244 LEU A N     1 
ATOM   5636  C  CA    . LEU A 1 2244 ? 159.780 213.234 146.400 1.00 31.25  ? 2244 LEU A CA    1 
ATOM   5637  C  C     . LEU A 1 2244 ? 158.735 212.810 145.374 1.00 35.90  ? 2244 LEU A C     1 
ATOM   5638  O  O     . LEU A 1 2244 ? 158.355 213.605 144.509 1.00 45.48  ? 2244 LEU A O     1 
ATOM   5639  C  CB    . LEU A 1 2244 ? 161.083 212.458 146.182 1.00 27.84  ? 2244 LEU A CB    1 
ATOM   5640  C  CG    . LEU A 1 2244 ? 161.595 212.338 144.747 1.00 31.65  ? 2244 LEU A CG    1 
ATOM   5641  C  CD1   . LEU A 1 2244 ? 162.388 213.573 144.356 1.00 33.45  ? 2244 LEU A CD1   1 
ATOM   5642  C  CD2   . LEU A 1 2244 ? 162.441 211.084 144.588 1.00 30.78  ? 2244 LEU A CD2   1 
ATOM   5643  N  N     . GLU A 1 2245 ? 158.264 211.567 145.453 1.00 37.11  ? 2245 GLU A N     1 
ATOM   5644  C  CA    . GLU A 1 2245 ? 157.293 211.056 144.497 1.00 40.40  ? 2245 GLU A CA    1 
ATOM   5645  C  C     . GLU A 1 2245 ? 155.859 211.437 144.837 1.00 37.65  ? 2245 GLU A C     1 
ATOM   5646  O  O     . GLU A 1 2245 ? 154.972 211.257 143.997 1.00 37.41  ? 2245 GLU A O     1 
ATOM   5647  C  CB    . GLU A 1 2245 ? 157.400 209.531 144.400 1.00 40.52  ? 2245 GLU A CB    1 
ATOM   5648  C  CG    . GLU A 1 2245 ? 158.774 209.027 143.997 1.00 43.57  ? 2245 GLU A CG    1 
ATOM   5649  C  CD    . GLU A 1 2245 ? 158.870 207.516 144.028 1.00 56.13  ? 2245 GLU A CD    1 
ATOM   5650  O  OE1   . GLU A 1 2245 ? 157.885 206.866 144.438 1.00 54.63  ? 2245 GLU A OE1   1 
ATOM   5651  O  OE2   . GLU A 1 2245 ? 159.928 206.977 143.641 1.00 58.22  ? 2245 GLU A OE2   1 
ATOM   5652  N  N     . GLY A 1 2246 ? 155.611 211.957 146.037 1.00 35.81  ? 2246 GLY A N     1 
ATOM   5653  C  CA    . GLY A 1 2246 ? 154.269 212.296 146.454 1.00 36.64  ? 2246 GLY A CA    1 
ATOM   5654  C  C     . GLY A 1 2246 ? 153.427 211.126 146.909 1.00 39.78  ? 2246 GLY A C     1 
ATOM   5655  O  O     . GLY A 1 2246 ? 152.247 211.322 147.226 1.00 43.07  ? 2246 GLY A O     1 
ATOM   5656  N  N     . VAL A 1 2247 ? 153.988 209.922 146.953 1.00 37.64  ? 2247 VAL A N     1 
ATOM   5657  C  CA    . VAL A 1 2247 ? 153.253 208.729 147.355 1.00 37.41  ? 2247 VAL A CA    1 
ATOM   5658  C  C     . VAL A 1 2247 ? 153.495 208.493 148.839 1.00 42.96  ? 2247 VAL A C     1 
ATOM   5659  O  O     . VAL A 1 2247 ? 154.639 208.305 149.267 1.00 42.40  ? 2247 VAL A O     1 
ATOM   5660  C  CB    . VAL A 1 2247 ? 153.679 207.509 146.526 1.00 33.79  ? 2247 VAL A CB    1 
ATOM   5661  C  CG1   . VAL A 1 2247 ? 152.985 206.256 147.031 1.00 34.04  ? 2247 VAL A CG1   1 
ATOM   5662  C  CG2   . VAL A 1 2247 ? 153.376 207.737 145.054 1.00 37.08  ? 2247 VAL A CG2   1 
ATOM   5663  N  N     . GLU A 1 2248 ? 152.419 208.505 149.623 1.00 43.90  ? 2248 GLU A N     1 
ATOM   5664  C  CA    . GLU A 1 2248 ? 152.539 208.299 151.060 1.00 41.32  ? 2248 GLU A CA    1 
ATOM   5665  C  C     . GLU A 1 2248 ? 153.080 206.906 151.357 1.00 36.30  ? 2248 GLU A C     1 
ATOM   5666  O  O     . GLU A 1 2248 ? 152.640 205.912 150.774 1.00 34.54  ? 2248 GLU A O     1 
ATOM   5667  C  CB    . GLU A 1 2248 ? 151.182 208.495 151.736 1.00 44.89  ? 2248 GLU A CB    1 
ATOM   5668  C  CG    . GLU A 1 2248 ? 151.167 208.155 153.217 1.00 54.37  ? 2248 GLU A CG    1 
ATOM   5669  C  CD    . GLU A 1 2248 ? 149.793 208.309 153.837 1.00 62.61  ? 2248 GLU A CD    1 
ATOM   5670  O  OE1   . GLU A 1 2248 ? 148.884 208.824 153.152 1.00 65.12  ? 2248 GLU A OE1   1 
ATOM   5671  O  OE2   . GLU A 1 2248 ? 149.620 207.914 155.009 1.00 61.06  ? 2248 GLU A OE2   1 
ATOM   5672  N  N     . GLY A 1 2249 ? 154.045 206.839 152.272 1.00 34.34  ? 2249 GLY A N     1 
ATOM   5673  C  CA    . GLY A 1 2249 ? 154.663 205.583 152.651 1.00 29.68  ? 2249 GLY A CA    1 
ATOM   5674  C  C     . GLY A 1 2249 ? 154.181 205.128 154.016 1.00 28.97  ? 2249 GLY A C     1 
ATOM   5675  O  O     . GLY A 1 2249 ? 154.165 205.905 154.974 1.00 34.30  ? 2249 GLY A O     1 
ATOM   5676  N  N     . VAL A 1 2250 ? 153.789 203.859 154.091 1.00 21.63  ? 2250 VAL A N     1 
ATOM   5677  C  CA    . VAL A 1 2250 ? 153.344 203.231 155.329 1.00 21.75  ? 2250 VAL A CA    1 
ATOM   5678  C  C     . VAL A 1 2250 ? 154.222 202.016 155.582 1.00 20.64  ? 2250 VAL A C     1 
ATOM   5679  O  O     . VAL A 1 2250 ? 154.428 201.195 154.682 1.00 24.84  ? 2250 VAL A O     1 
ATOM   5680  C  CB    . VAL A 1 2250 ? 151.859 202.829 155.266 1.00 20.89  ? 2250 VAL A CB    1 
ATOM   5681  C  CG1   . VAL A 1 2250 ? 151.370 202.397 156.639 1.00 19.50  ? 2250 VAL A CG1   1 
ATOM   5682  C  CG2   . VAL A 1 2250 ? 151.018 203.978 154.736 1.00 30.01  ? 2250 VAL A CG2   1 
ATOM   5683  N  N     . ALA A 1 2251 ? 154.739 201.904 156.802 1.00 16.56  ? 2251 ALA A N     1 
ATOM   5684  C  CA    . ALA A 1 2251 ? 155.627 200.815 157.184 1.00 12.00  ? 2251 ALA A CA    1 
ATOM   5685  C  C     . ALA A 1 2251 ? 154.984 200.000 158.294 1.00 15.47  ? 2251 ALA A C     1 
ATOM   5686  O  O     . ALA A 1 2251 ? 154.489 200.562 159.277 1.00 21.28  ? 2251 ALA A O     1 
ATOM   5687  C  CB    . ALA A 1 2251 ? 156.988 201.348 157.638 1.00 12.06  ? 2251 ALA A CB    1 
ATOM   5688  N  N     . HIS A 1 2252 ? 154.992 198.680 158.135 1.00 13.16  ? 2252 HIS A N     1 
ATOM   5689  C  CA    . HIS A 1 2252 ? 154.465 197.751 159.131 1.00 12.95  ? 2252 HIS A CA    1 
ATOM   5690  C  C     . HIS A 1 2252 ? 155.631 196.917 159.649 1.00 12.49  ? 2252 HIS A C     1 
ATOM   5691  O  O     . HIS A 1 2252 ? 156.004 195.910 159.041 1.00 14.57  ? 2252 HIS A O     1 
ATOM   5692  C  CB    . HIS A 1 2252 ? 153.370 196.872 158.535 1.00 12.44  ? 2252 HIS A CB    1 
ATOM   5693  C  CG    . HIS A 1 2252 ? 152.301 197.638 157.822 1.00 17.50  ? 2252 HIS A CG    1 
ATOM   5694  N  ND1   . HIS A 1 2252 ? 151.158 198.084 158.451 1.00 18.35  ? 2252 HIS A ND1   1 
ATOM   5695  C  CD2   . HIS A 1 2252 ? 152.199 198.037 156.532 1.00 18.64  ? 2252 HIS A CD2   1 
ATOM   5696  C  CE1   . HIS A 1 2252 ? 150.400 198.725 157.580 1.00 19.08  ? 2252 HIS A CE1   1 
ATOM   5697  N  NE2   . HIS A 1 2252 ? 151.009 198.711 156.408 1.00 19.39  ? 2252 HIS A NE2   1 
ATOM   5698  N  N     . ILE A 1 2253 ? 156.202 197.337 160.772 1.00 13.04  ? 2253 ILE A N     1 
ATOM   5699  C  CA    . ILE A 1 2253 ? 157.331 196.630 161.364 1.00 12.32  ? 2253 ILE A CA    1 
ATOM   5700  C  C     . ILE A 1 2253 ? 156.807 195.468 162.196 1.00 12.67  ? 2253 ILE A C     1 
ATOM   5701  O  O     . ILE A 1 2253 ? 155.975 195.654 163.093 1.00 15.81  ? 2253 ILE A O     1 
ATOM   5702  C  CB    . ILE A 1 2253 ? 158.187 197.582 162.212 1.00 12.85  ? 2253 ILE A CB    1 
ATOM   5703  C  CG1   . ILE A 1 2253 ? 158.449 198.879 161.447 1.00 13.56  ? 2253 ILE A CG1   1 
ATOM   5704  C  CG2   . ILE A 1 2253 ? 159.497 196.918 162.596 1.00 15.65  ? 2253 ILE A CG2   1 
ATOM   5705  C  CD1   . ILE A 1 2253 ? 158.817 200.041 162.333 1.00 18.16  ? 2253 ILE A CD1   1 
ATOM   5706  N  N     . ILE A 1 2254 ? 157.293 194.266 161.900 1.00 12.00  ? 2254 ILE A N     1 
ATOM   5707  C  CA    . ILE A 1 2254 ? 156.852 193.045 162.561 1.00 11.63  ? 2254 ILE A CA    1 
ATOM   5708  C  C     . ILE A 1 2254 ? 158.077 192.318 163.095 1.00 14.69  ? 2254 ILE A C     1 
ATOM   5709  O  O     . ILE A 1 2254 ? 159.069 192.157 162.376 1.00 14.82  ? 2254 ILE A O     1 
ATOM   5710  C  CB    . ILE A 1 2254 ? 156.058 192.134 161.605 1.00 10.97  ? 2254 ILE A CB    1 
ATOM   5711  C  CG1   . ILE A 1 2254 ? 154.786 192.836 161.127 1.00 11.18  ? 2254 ILE A CG1   1 
ATOM   5712  C  CG2   . ILE A 1 2254 ? 155.725 190.811 162.274 1.00 14.11  ? 2254 ILE A CG2   1 
ATOM   5713  C  CD1   . ILE A 1 2254 ? 154.125 192.161 159.949 1.00 12.76  ? 2254 ILE A CD1   1 
ATOM   5714  N  N     . ASP A 1 2255 ? 158.013 191.889 164.357 1.00 17.72  ? 2255 ASP A N     1 
ATOM   5715  C  CA    . ASP A 1 2255 ? 159.044 191.038 164.931 1.00 15.04  ? 2255 ASP A CA    1 
ATOM   5716  C  C     . ASP A 1 2255 ? 158.620 189.589 164.741 1.00 17.73  ? 2255 ASP A C     1 
ATOM   5717  O  O     . ASP A 1 2255 ? 157.772 189.092 165.498 1.00 17.81  ? 2255 ASP A O     1 
ATOM   5718  C  CB    . ASP A 1 2255 ? 159.254 191.351 166.414 1.00 17.70  ? 2255 ASP A CB    1 
ATOM   5719  C  CG    . ASP A 1 2255 ? 160.653 191.011 166.889 1.00 23.05  ? 2255 ASP A CG    1 
ATOM   5720  O  OD1   . ASP A 1 2255 ? 161.133 189.899 166.584 1.00 20.74  ? 2255 ASP A OD1   1 
ATOM   5721  O  OD2   . ASP A 1 2255 ? 161.274 191.855 167.568 1.00 23.38  ? 2255 ASP A OD2   1 
ATOM   5722  N  N     . PRO A 1 2256 ? 159.159 188.878 163.749 1.00 15.24  ? 2256 PRO A N     1 
ATOM   5723  C  CA    . PRO A 1 2256 ? 158.661 187.523 163.459 1.00 13.34  ? 2256 PRO A CA    1 
ATOM   5724  C  C     . PRO A 1 2256 ? 158.856 186.534 164.594 1.00 16.61  ? 2256 PRO A C     1 
ATOM   5725  O  O     . PRO A 1 2256 ? 158.020 185.638 164.768 1.00 16.38  ? 2256 PRO A O     1 
ATOM   5726  C  CB    . PRO A 1 2256 ? 159.469 187.121 162.219 1.00 11.51  ? 2256 PRO A CB    1 
ATOM   5727  C  CG    . PRO A 1 2256 ? 160.715 187.934 162.311 1.00 10.66  ? 2256 PRO A CG    1 
ATOM   5728  C  CD    . PRO A 1 2256 ? 160.302 189.244 162.897 1.00 11.95  ? 2256 PRO A CD    1 
ATOM   5729  N  N     . LYS A 1 2257 ? 159.931 186.662 165.369 1.00 17.93  ? 2257 LYS A N     1 
ATOM   5730  C  CA    . LYS A 1 2257 ? 160.237 185.698 166.416 1.00 14.68  ? 2257 LYS A CA    1 
ATOM   5731  C  C     . LYS A 1 2257 ? 159.743 186.120 167.793 1.00 16.34  ? 2257 LYS A C     1 
ATOM   5732  O  O     . LYS A 1 2257 ? 159.877 185.342 168.743 1.00 20.60  ? 2257 LYS A O     1 
ATOM   5733  C  CB    . LYS A 1 2257 ? 161.746 185.437 166.467 1.00 17.08  ? 2257 LYS A CB    1 
ATOM   5734  C  CG    . LYS A 1 2257 ? 162.331 185.031 165.126 1.00 16.70  ? 2257 LYS A CG    1 
ATOM   5735  C  CD    . LYS A 1 2257 ? 162.265 183.528 164.926 1.00 13.46  ? 2257 LYS A CD    1 
ATOM   5736  C  CE    . LYS A 1 2257 ? 163.464 182.839 165.545 1.00 18.84  ? 2257 LYS A CE    1 
ATOM   5737  N  NZ    . LYS A 1 2257 ? 163.321 181.359 165.544 1.00 29.52  ? 2257 LYS A NZ    1 
ATOM   5738  N  N     . ALA A 1 2258 ? 159.180 187.321 167.929 1.00 14.27  ? 2258 ALA A N     1 
ATOM   5739  C  CA    . ALA A 1 2258 ? 158.559 187.711 169.187 1.00 14.17  ? 2258 ALA A CA    1 
ATOM   5740  C  C     . ALA A 1 2258 ? 157.224 187.019 169.415 1.00 20.21  ? 2258 ALA A C     1 
ATOM   5741  O  O     . ALA A 1 2258 ? 156.692 187.085 170.528 1.00 25.04  ? 2258 ALA A O     1 
ATOM   5742  C  CB    . ALA A 1 2258 ? 158.368 189.227 169.236 1.00 14.37  ? 2258 ALA A CB    1 
ATOM   5743  N  N     . ILE A 1 2259 ? 156.674 186.364 168.392 1.00 23.75  ? 2259 ILE A N     1 
ATOM   5744  C  CA    . ILE A 1 2259 ? 155.411 185.649 168.485 1.00 21.01  ? 2259 ILE A CA    1 
ATOM   5745  C  C     . ILE A 1 2259 ? 155.587 184.277 167.850 1.00 24.94  ? 2259 ILE A C     1 
ATOM   5746  O  O     . ILE A 1 2259 ? 156.535 184.027 167.104 1.00 28.23  ? 2259 ILE A O     1 
ATOM   5747  C  CB    . ILE A 1 2259 ? 154.255 186.409 167.804 1.00 15.71  ? 2259 ILE A CB    1 
ATOM   5748  C  CG1   . ILE A 1 2259 ? 154.645 186.793 166.376 1.00 13.21  ? 2259 ILE A CG1   1 
ATOM   5749  C  CG2   . ILE A 1 2259 ? 153.880 187.641 168.608 1.00 21.57  ? 2259 ILE A CG2   1 
ATOM   5750  C  CD1   . ILE A 1 2259 ? 153.625 187.658 165.676 1.00 19.44  ? 2259 ILE A CD1   1 
ATOM   5751  N  N     . SER A 1 2260 ? 154.653 183.383 168.159 1.00 28.05  ? 2260 SER A N     1 
ATOM   5752  C  CA    . SER A 1 2260 ? 154.672 182.058 167.563 1.00 26.92  ? 2260 SER A CA    1 
ATOM   5753  C  C     . SER A 1 2260 ? 154.301 182.134 166.084 1.00 26.12  ? 2260 SER A C     1 
ATOM   5754  O  O     . SER A 1 2260 ? 153.686 183.097 165.617 1.00 29.09  ? 2260 SER A O     1 
ATOM   5755  C  CB    . SER A 1 2260 ? 153.716 181.122 168.301 1.00 30.79  ? 2260 SER A CB    1 
ATOM   5756  O  OG    . SER A 1 2260 ? 152.367 181.477 168.060 1.00 31.38  ? 2260 SER A OG    1 
ATOM   5757  N  N     . LYS A 1 2261 ? 154.695 181.096 165.342 1.00 24.71  ? 2261 LYS A N     1 
ATOM   5758  C  CA    . LYS A 1 2261 ? 154.404 181.052 163.912 1.00 20.64  ? 2261 LYS A CA    1 
ATOM   5759  C  C     . LYS A 1 2261 ? 152.905 181.055 163.644 1.00 22.19  ? 2261 LYS A C     1 
ATOM   5760  O  O     . LYS A 1 2261 ? 152.455 181.607 162.632 1.00 23.12  ? 2261 LYS A O     1 
ATOM   5761  C  CB    . LYS A 1 2261 ? 155.056 179.819 163.287 1.00 17.05  ? 2261 LYS A CB    1 
ATOM   5762  C  CG    . LYS A 1 2261 ? 154.964 179.763 161.775 1.00 19.98  ? 2261 LYS A CG    1 
ATOM   5763  C  CD    . LYS A 1 2261 ? 155.822 178.641 161.220 1.00 24.84  ? 2261 LYS A CD    1 
ATOM   5764  C  CE    . LYS A 1 2261 ? 155.337 178.204 159.851 1.00 31.48  ? 2261 LYS A CE    1 
ATOM   5765  N  NZ    . LYS A 1 2261 ? 156.249 177.198 159.240 1.00 36.40  ? 2261 LYS A NZ    1 
ATOM   5766  N  N     . ASP A 1 2262 ? 152.118 180.446 164.535 1.00 24.69  ? 2262 ASP A N     1 
ATOM   5767  C  CA    . ASP A 1 2262 ? 150.667 180.480 164.387 1.00 24.80  ? 2262 ASP A CA    1 
ATOM   5768  C  C     . ASP A 1 2262 ? 150.137 181.903 164.502 1.00 26.14  ? 2262 ASP A C     1 
ATOM   5769  O  O     . ASP A 1 2262 ? 149.214 182.290 163.777 1.00 32.42  ? 2262 ASP A O     1 
ATOM   5770  C  CB    . ASP A 1 2262 ? 150.013 179.575 165.431 1.00 30.16  ? 2262 ASP A CB    1 
ATOM   5771  C  CG    . ASP A 1 2262 ? 150.717 178.241 165.567 1.00 44.09  ? 2262 ASP A CG    1 
ATOM   5772  O  OD1   . ASP A 1 2262 ? 150.628 177.422 164.629 1.00 48.40  ? 2262 ASP A OD1   1 
ATOM   5773  O  OD2   . ASP A 1 2262 ? 151.362 178.012 166.612 1.00 48.76  ? 2262 ASP A OD2   1 
ATOM   5774  N  N     . HIS A 1 2263 ? 150.702 182.695 165.413 1.00 21.92  ? 2263 HIS A N     1 
ATOM   5775  C  CA    . HIS A 1 2263 ? 150.306 184.093 165.528 1.00 20.68  ? 2263 HIS A CA    1 
ATOM   5776  C  C     . HIS A 1 2263 ? 150.869 184.946 164.401 1.00 21.38  ? 2263 HIS A C     1 
ATOM   5777  O  O     . HIS A 1 2263 ? 150.331 186.025 164.129 1.00 22.20  ? 2263 HIS A O     1 
ATOM   5778  C  CB    . HIS A 1 2263 ? 150.749 184.656 166.878 1.00 24.15  ? 2263 HIS A CB    1 
ATOM   5779  C  CG    . HIS A 1 2263 ? 150.007 184.083 168.044 1.00 31.18  ? 2263 HIS A CG    1 
ATOM   5780  N  ND1   . HIS A 1 2263 ? 148.645 183.872 168.029 1.00 31.96  ? 2263 HIS A ND1   1 
ATOM   5781  C  CD2   . HIS A 1 2263 ? 150.437 183.675 169.261 1.00 34.30  ? 2263 HIS A CD2   1 
ATOM   5782  C  CE1   . HIS A 1 2263 ? 148.269 183.359 169.186 1.00 30.41  ? 2263 HIS A CE1   1 
ATOM   5783  N  NE2   . HIS A 1 2263 ? 149.337 183.229 169.952 1.00 38.36  ? 2263 HIS A NE2   1 
ATOM   5784  N  N     . LEU A 1 2264 ? 151.936 184.491 163.741 1.00 22.56  ? 2264 LEU A N     1 
ATOM   5785  C  CA    . LEU A 1 2264 ? 152.542 185.276 162.672 1.00 18.94  ? 2264 LEU A CA    1 
ATOM   5786  C  C     . LEU A 1 2264 ? 151.825 185.074 161.344 1.00 18.70  ? 2264 LEU A C     1 
ATOM   5787  O  O     . LEU A 1 2264 ? 151.568 186.043 160.622 1.00 20.41  ? 2264 LEU A O     1 
ATOM   5788  C  CB    . LEU A 1 2264 ? 154.023 184.919 162.536 1.00 16.97  ? 2264 LEU A CB    1 
ATOM   5789  C  CG    . LEU A 1 2264 ? 154.767 185.514 161.339 1.00 14.51  ? 2264 LEU A CG    1 
ATOM   5790  C  CD1   . LEU A 1 2264 ? 154.776 187.032 161.408 1.00 14.87  ? 2264 LEU A CD1   1 
ATOM   5791  C  CD2   . LEU A 1 2264 ? 156.183 184.970 161.266 1.00 13.29  ? 2264 LEU A CD2   1 
ATOM   5792  N  N     . TYR A 1 2265 ? 151.492 183.829 161.003 1.00 17.43  ? 2265 TYR A N     1 
ATOM   5793  C  CA    . TYR A 1 2265 ? 150.866 183.525 159.723 1.00 15.08  ? 2265 TYR A CA    1 
ATOM   5794  C  C     . TYR A 1 2265 ? 149.395 183.166 159.826 1.00 17.87  ? 2265 TYR A C     1 
ATOM   5795  O  O     . TYR A 1 2265 ? 148.649 183.404 158.875 1.00 19.67  ? 2265 TYR A O     1 
ATOM   5796  C  CB    . TYR A 1 2265 ? 151.604 182.372 159.031 1.00 14.05  ? 2265 TYR A CB    1 
ATOM   5797  C  CG    . TYR A 1 2265 ? 152.963 182.759 158.504 1.00 15.97  ? 2265 TYR A CG    1 
ATOM   5798  C  CD1   . TYR A 1 2265 ? 153.094 183.697 157.490 1.00 15.91  ? 2265 TYR A CD1   1 
ATOM   5799  C  CD2   . TYR A 1 2265 ? 154.115 182.192 159.025 1.00 17.62  ? 2265 TYR A CD2   1 
ATOM   5800  C  CE1   . TYR A 1 2265 ? 154.334 184.055 157.009 1.00 15.67  ? 2265 TYR A CE1   1 
ATOM   5801  C  CE2   . TYR A 1 2265 ? 155.358 182.543 158.551 1.00 18.51  ? 2265 TYR A CE2   1 
ATOM   5802  C  CZ    . TYR A 1 2265 ? 155.462 183.475 157.543 1.00 18.94  ? 2265 TYR A CZ    1 
ATOM   5803  O  OH    . TYR A 1 2265 ? 156.703 183.826 157.069 1.00 22.68  ? 2265 TYR A OH    1 
ATOM   5804  N  N     . GLY A 1 2266 ? 148.960 182.604 160.948 1.00 20.41  ? 2266 GLY A N     1 
ATOM   5805  C  CA    . GLY A 1 2266 ? 147.584 182.179 161.092 1.00 22.39  ? 2266 GLY A CA    1 
ATOM   5806  C  C     . GLY A 1 2266 ? 147.476 180.717 161.467 1.00 26.95  ? 2266 GLY A C     1 
ATOM   5807  O  O     . GLY A 1 2266 ? 148.438 179.959 161.312 1.00 26.86  ? 2266 GLY A O     1 
ATOM   5808  N  N     . THR A 1 2267 ? 146.313 180.307 161.962 1.00 30.60  ? 2267 THR A N     1 
ATOM   5809  C  CA    . THR A 1 2267 ? 146.085 178.929 162.365 1.00 34.18  ? 2267 THR A CA    1 
ATOM   5810  C  C     . THR A 1 2267 ? 144.745 178.453 161.825 1.00 35.87  ? 2267 THR A C     1 
ATOM   5811  O  O     . THR A 1 2267 ? 143.832 179.249 161.587 1.00 32.88  ? 2267 THR A O     1 
ATOM   5812  C  CB    . THR A 1 2267 ? 146.125 178.772 163.895 1.00 40.24  ? 2267 THR A CB    1 
ATOM   5813  O  OG1   . THR A 1 2267 ? 146.065 177.382 164.237 1.00 46.23  ? 2267 THR A OG1   1 
ATOM   5814  C  CG2   . THR A 1 2267 ? 144.962 179.504 164.547 1.00 41.68  ? 2267 THR A CG2   1 
ATOM   5815  N  N     . LEU A 1 2268 ? 144.643 177.143 161.622 1.00 40.28  ? 2268 LEU A N     1 
ATOM   5816  C  CA    . LEU A 1 2268 ? 143.433 176.510 161.118 1.00 42.85  ? 2268 LEU A CA    1 
ATOM   5817  C  C     . LEU A 1 2268 ? 142.864 175.606 162.200 1.00 48.05  ? 2268 LEU A C     1 
ATOM   5818  O  O     . LEU A 1 2268 ? 143.578 174.754 162.741 1.00 49.71  ? 2268 LEU A O     1 
ATOM   5819  C  CB    . LEU A 1 2268 ? 143.723 175.710 159.845 1.00 41.37  ? 2268 LEU A CB    1 
ATOM   5820  C  CG    . LEU A 1 2268 ? 142.523 175.302 158.990 1.00 44.05  ? 2268 LEU A CG    1 
ATOM   5821  C  CD1   . LEU A 1 2268 ? 141.687 176.516 158.628 1.00 41.94  ? 2268 LEU A CD1   1 
ATOM   5822  C  CD2   . LEU A 1 2268 ? 142.991 174.584 157.737 1.00 38.29  ? 2268 LEU A CD2   1 
ATOM   5823  N  N     . ASP A 1 2269 ? 141.591 175.793 162.513 1.00 51.23  ? 2269 ASP A N     1 
ATOM   5824  C  CA    . ASP A 1 2269 ? 140.953 175.013 163.567 1.00 57.45  ? 2269 ASP A CA    1 
ATOM   5825  C  C     . ASP A 1 2269 ? 140.808 173.564 163.124 1.00 67.00  ? 2269 ASP A C     1 
ATOM   5826  O  O     . ASP A 1 2269 ? 140.193 173.304 162.082 1.00 70.00  ? 2269 ASP A O     1 
ATOM   5827  C  CB    . ASP A 1 2269 ? 139.589 175.604 163.908 1.00 63.92  ? 2269 ASP A CB    1 
ATOM   5828  C  CG    . ASP A 1 2269 ? 139.258 175.495 165.382 1.00 75.32  ? 2269 ASP A CG    1 
ATOM   5829  O  OD1   . ASP A 1 2269 ? 140.128 175.047 166.158 1.00 77.71  ? 2269 ASP A OD1   1 
ATOM   5830  O  OD2   . ASP A 1 2269 ? 138.126 175.856 165.766 1.00 82.32  ? 2269 ASP A OD2   1 
ATOM   5831  N  N     . PRO A 1 2270 ? 141.356 172.596 163.863 1.00 66.13  ? 2270 PRO A N     1 
ATOM   5832  C  CA    . PRO A 1 2270 ? 141.192 171.190 163.463 1.00 66.17  ? 2270 PRO A CA    1 
ATOM   5833  C  C     . PRO A 1 2270 ? 139.756 170.699 163.526 1.00 72.61  ? 2270 PRO A C     1 
ATOM   5834  O  O     . PRO A 1 2270 ? 139.431 169.706 162.864 1.00 67.70  ? 2270 PRO A O     1 
ATOM   5835  C  CB    . PRO A 1 2270 ? 142.085 170.434 164.457 1.00 60.58  ? 2270 PRO A CB    1 
ATOM   5836  C  CG    . PRO A 1 2270 ? 142.177 171.336 165.641 1.00 55.16  ? 2270 PRO A CG    1 
ATOM   5837  C  CD    . PRO A 1 2270 ? 142.144 172.735 165.099 1.00 59.80  ? 2270 PRO A CD    1 
ATOM   5838  N  N     . ASN A 1 2271 ? 138.888 171.358 164.294 1.00 73.59  ? 2271 ASN A N     1 
ATOM   5839  C  CA    . ASN A 1 2271 ? 137.513 170.898 164.466 1.00 71.34  ? 2271 ASN A CA    1 
ATOM   5840  C  C     . ASN A 1 2271 ? 136.557 171.581 163.491 1.00 70.58  ? 2271 ASN A C     1 
ATOM   5841  O  O     . ASN A 1 2271 ? 135.892 170.913 162.693 1.00 75.36  ? 2271 ASN A O     1 
ATOM   5842  C  CB    . ASN A 1 2271 ? 137.063 171.133 165.913 1.00 80.07  ? 2271 ASN A CB    1 
ATOM   5843  C  CG    . ASN A 1 2271 ? 138.128 170.752 166.922 1.00 79.57  ? 2271 ASN A CG    1 
ATOM   5844  O  OD1   . ASN A 1 2271 ? 138.440 171.520 167.832 1.00 78.27  ? 2271 ASN A OD1   1 
ATOM   5845  N  ND2   . ASN A 1 2271 ? 138.691 169.559 166.767 1.00 72.44  ? 2271 ASN A ND2   1 
ATOM   5846  N  N     . THR A 1 2272 ? 136.478 172.908 163.545 1.00 67.25  ? 2272 THR A N     1 
ATOM   5847  C  CA    . THR A 1 2272 ? 135.544 173.665 162.723 1.00 67.71  ? 2272 THR A CA    1 
ATOM   5848  C  C     . THR A 1 2272 ? 136.130 174.089 161.383 1.00 65.25  ? 2272 THR A C     1 
ATOM   5849  O  O     . THR A 1 2272 ? 135.397 174.637 160.553 1.00 66.77  ? 2272 THR A O     1 
ATOM   5850  C  CB    . THR A 1 2272 ? 135.060 174.907 163.480 1.00 71.58  ? 2272 THR A CB    1 
ATOM   5851  O  OG1   . THR A 1 2272 ? 136.176 175.756 163.775 1.00 71.88  ? 2272 THR A OG1   1 
ATOM   5852  C  CG2   . THR A 1 2272 ? 134.378 174.506 164.779 1.00 70.89  ? 2272 THR A CG2   1 
ATOM   5853  N  N     . ARG A 1 2273 ? 137.421 173.841 161.152 1.00 63.10  ? 2273 ARG A N     1 
ATOM   5854  C  CA    . ARG A 1 2273 ? 138.098 174.233 159.914 1.00 61.22  ? 2273 ARG A CA    1 
ATOM   5855  C  C     . ARG A 1 2273 ? 137.911 175.721 159.626 1.00 65.34  ? 2273 ARG A C     1 
ATOM   5856  O  O     . ARG A 1 2273 ? 137.655 176.132 158.493 1.00 67.99  ? 2273 ARG A O     1 
ATOM   5857  C  CB    . ARG A 1 2273 ? 137.630 173.381 158.732 1.00 60.49  ? 2273 ARG A CB    1 
ATOM   5858  C  CG    . ARG A 1 2273 ? 137.424 171.910 159.065 1.00 67.18  ? 2273 ARG A CG    1 
ATOM   5859  C  CD    . ARG A 1 2273 ? 138.711 171.261 159.552 1.00 62.76  ? 2273 ARG A CD    1 
ATOM   5860  N  NE    . ARG A 1 2273 ? 139.822 171.479 158.635 1.00 53.85  ? 2273 ARG A NE    1 
ATOM   5861  C  CZ    . ARG A 1 2273 ? 141.081 171.156 158.895 1.00 48.53  ? 2273 ARG A CZ    1 
ATOM   5862  N  NH1   . ARG A 1 2273 ? 141.429 170.601 160.045 1.00 49.65  ? 2273 ARG A NH1   1 
ATOM   5863  N  NH2   . ARG A 1 2273 ? 142.016 171.394 157.980 1.00 40.12  ? 2273 ARG A NH2   1 
ATOM   5864  N  N     . GLU A 1 2274 ? 138.041 176.535 160.669 1.00 64.26  ? 2274 GLU A N     1 
ATOM   5865  C  CA    . GLU A 1 2274 ? 137.921 177.982 160.560 1.00 58.21  ? 2274 GLU A CA    1 
ATOM   5866  C  C     . GLU A 1 2274 ? 139.310 178.604 160.580 1.00 52.41  ? 2274 GLU A C     1 
ATOM   5867  O  O     . GLU A 1 2274 ? 140.136 178.262 161.433 1.00 52.12  ? 2274 GLU A O     1 
ATOM   5868  C  CB    . GLU A 1 2274 ? 137.068 178.548 161.696 1.00 63.45  ? 2274 GLU A CB    1 
ATOM   5869  C  CG    . GLU A 1 2274 ? 136.474 179.918 161.406 1.00 76.31  ? 2274 GLU A CG    1 
ATOM   5870  C  CD    . GLU A 1 2274 ? 135.462 179.890 160.276 1.00 91.99  ? 2274 GLU A CD    1 
ATOM   5871  O  OE1   . GLU A 1 2274 ? 135.864 180.085 159.109 1.00 77.98  ? 2274 GLU A OE1   1 
ATOM   5872  O  OE2   . GLU A 1 2274 ? 134.264 179.673 160.555 1.00 103.46 ? 2274 GLU A OE2   1 
ATOM   5873  N  N     . TRP A 1 2275 ? 139.562 179.513 159.644 1.00 49.79  ? 2275 TRP A N     1 
ATOM   5874  C  CA    . TRP A 1 2275 ? 140.875 180.126 159.491 1.00 36.07  ? 2275 TRP A CA    1 
ATOM   5875  C  C     . TRP A 1 2275 ? 140.917 181.449 160.245 1.00 35.18  ? 2275 TRP A C     1 
ATOM   5876  O  O     . TRP A 1 2275 ? 140.099 182.340 159.994 1.00 39.09  ? 2275 TRP A O     1 
ATOM   5877  C  CB    . TRP A 1 2275 ? 141.200 180.340 158.014 1.00 31.65  ? 2275 TRP A CB    1 
ATOM   5878  C  CG    . TRP A 1 2275 ? 142.445 181.140 157.792 1.00 30.81  ? 2275 TRP A CG    1 
ATOM   5879  C  CD1   . TRP A 1 2275 ? 142.523 182.458 157.455 1.00 28.62  ? 2275 TRP A CD1   1 
ATOM   5880  C  CD2   . TRP A 1 2275 ? 143.794 180.673 157.903 1.00 32.06  ? 2275 TRP A CD2   1 
ATOM   5881  N  NE1   . TRP A 1 2275 ? 143.837 182.841 157.344 1.00 29.94  ? 2275 TRP A NE1   1 
ATOM   5882  C  CE2   . TRP A 1 2275 ? 144.637 181.763 157.615 1.00 27.00  ? 2275 TRP A CE2   1 
ATOM   5883  C  CE3   . TRP A 1 2275 ? 144.371 179.439 158.216 1.00 28.25  ? 2275 TRP A CE3   1 
ATOM   5884  C  CZ2   . TRP A 1 2275 ? 146.025 181.657 157.631 1.00 21.81  ? 2275 TRP A CZ2   1 
ATOM   5885  C  CZ3   . TRP A 1 2275 ? 145.747 179.336 158.230 1.00 23.78  ? 2275 TRP A CZ3   1 
ATOM   5886  C  CH2   . TRP A 1 2275 ? 146.559 180.437 157.940 1.00 21.78  ? 2275 TRP A CH2   1 
ATOM   5887  N  N     . THR A 1 2276 ? 141.870 181.573 161.164 1.00 35.45  ? 2276 THR A N     1 
ATOM   5888  C  CA    . THR A 1 2276 ? 142.117 182.808 161.896 1.00 32.54  ? 2276 THR A CA    1 
ATOM   5889  C  C     . THR A 1 2276 ? 143.406 183.423 161.370 1.00 31.34  ? 2276 THR A C     1 
ATOM   5890  O  O     . THR A 1 2276 ? 144.460 182.781 161.403 1.00 31.69  ? 2276 THR A O     1 
ATOM   5891  C  CB    . THR A 1 2276 ? 142.216 182.552 163.399 1.00 34.81  ? 2276 THR A CB    1 
ATOM   5892  O  OG1   . THR A 1 2276 ? 140.988 181.983 163.871 1.00 46.95  ? 2276 THR A OG1   1 
ATOM   5893  C  CG2   . THR A 1 2276 ? 142.484 183.850 164.143 1.00 35.23  ? 2276 THR A CG2   1 
ATOM   5894  N  N     . ASP A 1 2277 ? 143.318 184.658 160.885 1.00 26.93  ? 2277 ASP A N     1 
ATOM   5895  C  CA    . ASP A 1 2277 ? 144.467 185.304 160.266 1.00 21.10  ? 2277 ASP A CA    1 
ATOM   5896  C  C     . ASP A 1 2277 ? 145.559 185.579 161.292 1.00 26.48  ? 2277 ASP A C     1 
ATOM   5897  O  O     . ASP A 1 2277 ? 145.281 185.909 162.448 1.00 36.59  ? 2277 ASP A O     1 
ATOM   5898  C  CB    . ASP A 1 2277 ? 144.044 186.610 159.596 1.00 22.56  ? 2277 ASP A CB    1 
ATOM   5899  C  CG    . ASP A 1 2277 ? 143.657 186.421 158.145 1.00 31.35  ? 2277 ASP A CG    1 
ATOM   5900  O  OD1   . ASP A 1 2277 ? 144.106 185.430 157.533 1.00 32.18  ? 2277 ASP A OD1   1 
ATOM   5901  O  OD2   . ASP A 1 2277 ? 142.906 187.265 157.615 1.00 38.48  ? 2277 ASP A OD2   1 
ATOM   5902  N  N     . GLY A 1 2278 ? 146.808 185.437 160.860 1.00 23.11  ? 2278 GLY A N     1 
ATOM   5903  C  CA    . GLY A 1 2278 ? 147.947 185.801 161.672 1.00 19.84  ? 2278 GLY A CA    1 
ATOM   5904  C  C     . GLY A 1 2278 ? 148.229 187.286 161.582 1.00 20.06  ? 2278 GLY A C     1 
ATOM   5905  O  O     . GLY A 1 2278 ? 147.382 188.092 161.198 1.00 22.63  ? 2278 GLY A O     1 
ATOM   5906  N  N     . LEU A 1 2279 ? 149.456 187.653 161.949 1.00 20.62  ? 2279 LEU A N     1 
ATOM   5907  C  CA    . LEU A 1 2279 ? 149.848 189.059 161.903 1.00 19.37  ? 2279 LEU A CA    1 
ATOM   5908  C  C     . LEU A 1 2279 ? 150.188 189.486 160.479 1.00 20.16  ? 2279 LEU A C     1 
ATOM   5909  O  O     . LEU A 1 2279 ? 149.570 190.405 159.923 1.00 23.31  ? 2279 LEU A O     1 
ATOM   5910  C  CB    . LEU A 1 2279 ? 151.028 189.300 162.845 1.00 15.76  ? 2279 LEU A CB    1 
ATOM   5911  C  CG    . LEU A 1 2279 ? 151.535 190.736 162.965 1.00 16.60  ? 2279 LEU A CG    1 
ATOM   5912  C  CD1   . LEU A 1 2279 ? 150.381 191.692 163.206 1.00 23.10  ? 2279 LEU A CD1   1 
ATOM   5913  C  CD2   . LEU A 1 2279 ? 152.553 190.833 164.084 1.00 19.08  ? 2279 LEU A CD2   1 
ATOM   5914  N  N     . PHE A 1 2280 ? 151.175 188.823 159.871 1.00 19.01  ? 2280 PHE A N     1 
ATOM   5915  C  CA    . PHE A 1 2280 ? 151.558 189.149 158.501 1.00 15.22  ? 2280 PHE A CA    1 
ATOM   5916  C  C     . PHE A 1 2280 ? 150.409 188.900 157.535 1.00 18.32  ? 2280 PHE A C     1 
ATOM   5917  O  O     . PHE A 1 2280 ? 150.191 189.684 156.603 1.00 23.15  ? 2280 PHE A O     1 
ATOM   5918  C  CB    . PHE A 1 2280 ? 152.786 188.338 158.090 1.00 14.01  ? 2280 PHE A CB    1 
ATOM   5919  C  CG    . PHE A 1 2280 ? 153.092 188.408 156.622 1.00 16.06  ? 2280 PHE A CG    1 
ATOM   5920  C  CD1   . PHE A 1 2280 ? 153.640 189.552 156.068 1.00 14.29  ? 2280 PHE A CD1   1 
ATOM   5921  C  CD2   . PHE A 1 2280 ? 152.824 187.332 155.793 1.00 17.31  ? 2280 PHE A CD2   1 
ATOM   5922  C  CE1   . PHE A 1 2280 ? 153.919 189.619 154.718 1.00 12.25  ? 2280 PHE A CE1   1 
ATOM   5923  C  CE2   . PHE A 1 2280 ? 153.099 187.395 154.443 1.00 15.27  ? 2280 PHE A CE2   1 
ATOM   5924  C  CZ    . PHE A 1 2280 ? 153.649 188.539 153.905 1.00 12.95  ? 2280 PHE A CZ    1 
ATOM   5925  N  N     . THR A 1 2281 ? 149.671 187.806 157.733 1.00 14.45  ? 2281 THR A N     1 
ATOM   5926  C  CA    . THR A 1 2281 ? 148.532 187.519 156.869 1.00 13.44  ? 2281 THR A CA    1 
ATOM   5927  C  C     . THR A 1 2281 ? 147.471 188.605 156.979 1.00 22.41  ? 2281 THR A C     1 
ATOM   5928  O  O     . THR A 1 2281 ? 146.912 189.038 155.966 1.00 25.81  ? 2281 THR A O     1 
ATOM   5929  C  CB    . THR A 1 2281 ? 147.937 186.154 157.212 1.00 17.61  ? 2281 THR A CB    1 
ATOM   5930  O  OG1   . THR A 1 2281 ? 148.993 185.205 157.403 1.00 20.64  ? 2281 THR A OG1   1 
ATOM   5931  C  CG2   . THR A 1 2281 ? 147.032 185.675 156.092 1.00 19.34  ? 2281 THR A CG2   1 
ATOM   5932  N  N     . HIS A 1 2282 ? 147.181 189.060 158.201 1.00 22.43  ? 2282 HIS A N     1 
ATOM   5933  C  CA    . HIS A 1 2282 ? 146.203 190.129 158.378 1.00 22.83  ? 2282 HIS A CA    1 
ATOM   5934  C  C     . HIS A 1 2282 ? 146.666 191.416 157.712 1.00 23.34  ? 2282 HIS A C     1 
ATOM   5935  O  O     . HIS A 1 2282 ? 145.874 192.099 157.052 1.00 27.72  ? 2282 HIS A O     1 
ATOM   5936  C  CB    . HIS A 1 2282 ? 145.936 190.364 159.864 1.00 25.02  ? 2282 HIS A CB    1 
ATOM   5937  C  CG    . HIS A 1 2282 ? 145.239 191.655 160.161 1.00 32.34  ? 2282 HIS A CG    1 
ATOM   5938  N  ND1   . HIS A 1 2282 ? 143.869 191.794 160.094 1.00 43.82  ? 2282 HIS A ND1   1 
ATOM   5939  C  CD2   . HIS A 1 2282 ? 145.721 192.863 160.536 1.00 32.30  ? 2282 HIS A CD2   1 
ATOM   5940  C  CE1   . HIS A 1 2282 ? 143.539 193.033 160.410 1.00 41.78  ? 2282 HIS A CE1   1 
ATOM   5941  N  NE2   . HIS A 1 2282 ? 144.644 193.703 160.682 1.00 38.00  ? 2282 HIS A NE2   1 
ATOM   5942  N  N     . VAL A 1 2283 ? 147.945 191.764 157.868 1.00 22.19  ? 2283 VAL A N     1 
ATOM   5943  C  CA    . VAL A 1 2283 ? 148.459 192.989 157.259 1.00 19.06  ? 2283 VAL A CA    1 
ATOM   5944  C  C     . VAL A 1 2283 ? 148.357 192.910 155.739 1.00 23.89  ? 2283 VAL A C     1 
ATOM   5945  O  O     . VAL A 1 2283 ? 147.883 193.844 155.076 1.00 29.37  ? 2283 VAL A O     1 
ATOM   5946  C  CB    . VAL A 1 2283 ? 149.905 193.249 157.716 1.00 15.25  ? 2283 VAL A CB    1 
ATOM   5947  C  CG1   . VAL A 1 2283 ? 150.573 194.277 156.819 1.00 17.05  ? 2283 VAL A CG1   1 
ATOM   5948  C  CG2   . VAL A 1 2283 ? 149.928 193.704 159.166 1.00 18.45  ? 2283 VAL A CG2   1 
ATOM   5949  N  N     . LEU A 1 2284 ? 148.787 191.783 155.166 1.00 22.96  ? 2284 LEU A N     1 
ATOM   5950  C  CA    . LEU A 1 2284 ? 148.754 191.627 153.716 1.00 18.63  ? 2284 LEU A CA    1 
ATOM   5951  C  C     . LEU A 1 2284 ? 147.325 191.635 153.189 1.00 21.91  ? 2284 LEU A C     1 
ATOM   5952  O  O     . LEU A 1 2284 ? 147.048 192.244 152.151 1.00 28.09  ? 2284 LEU A O     1 
ATOM   5953  C  CB    . LEU A 1 2284 ? 149.473 190.342 153.310 1.00 17.03  ? 2284 LEU A CB    1 
ATOM   5954  C  CG    . LEU A 1 2284 ? 149.765 190.180 151.818 1.00 18.33  ? 2284 LEU A CG    1 
ATOM   5955  C  CD1   . LEU A 1 2284 ? 150.651 191.311 151.323 1.00 15.14  ? 2284 LEU A CD1   1 
ATOM   5956  C  CD2   . LEU A 1 2284 ? 150.410 188.832 151.543 1.00 17.05  ? 2284 LEU A CD2   1 
ATOM   5957  N  N     . ARG A 1 2285 ? 146.403 190.968 153.887 1.00 21.20  ? 2285 ARG A N     1 
ATOM   5958  C  CA    . ARG A 1 2285 ? 145.012 190.952 153.450 1.00 24.57  ? 2285 ARG A CA    1 
ATOM   5959  C  C     . ARG A 1 2285 ? 144.386 192.337 153.543 1.00 28.12  ? 2285 ARG A C     1 
ATOM   5960  O  O     . ARG A 1 2285 ? 143.607 192.730 152.668 1.00 33.88  ? 2285 ARG A O     1 
ATOM   5961  C  CB    . ARG A 1 2285 ? 144.217 189.943 154.276 1.00 26.09  ? 2285 ARG A CB    1 
ATOM   5962  C  CG    . ARG A 1 2285 ? 142.790 189.741 153.804 1.00 29.07  ? 2285 ARG A CG    1 
ATOM   5963  C  CD    . ARG A 1 2285 ? 141.988 188.948 154.819 1.00 32.87  ? 2285 ARG A CD    1 
ATOM   5964  N  NE    . ARG A 1 2285 ? 142.686 187.736 155.230 1.00 29.42  ? 2285 ARG A NE    1 
ATOM   5965  C  CZ    . ARG A 1 2285 ? 142.730 186.619 154.517 1.00 25.85  ? 2285 ARG A CZ    1 
ATOM   5966  N  NH1   . ARG A 1 2285 ? 142.124 186.524 153.345 1.00 31.14  ? 2285 ARG A NH1   1 
ATOM   5967  N  NH2   . ARG A 1 2285 ? 143.400 185.573 154.990 1.00 24.32  ? 2285 ARG A NH2   1 
ATOM   5968  N  N     . LYS A 1 2286 ? 144.708 193.088 154.599 1.00 26.92  ? 2286 LYS A N     1 
ATOM   5969  C  CA    . LYS A 1 2286 ? 144.202 194.450 154.720 1.00 26.63  ? 2286 LYS A CA    1 
ATOM   5970  C  C     . LYS A 1 2286 ? 144.716 195.326 153.586 1.00 33.69  ? 2286 LYS A C     1 
ATOM   5971  O  O     . LYS A 1 2286 ? 143.970 196.146 153.037 1.00 43.02  ? 2286 LYS A O     1 
ATOM   5972  C  CB    . LYS A 1 2286 ? 144.593 195.032 156.079 1.00 31.73  ? 2286 LYS A CB    1 
ATOM   5973  C  CG    . LYS A 1 2286 ? 144.733 196.544 156.102 1.00 49.08  ? 2286 LYS A CG    1 
ATOM   5974  C  CD    . LYS A 1 2286 ? 145.004 197.049 157.510 1.00 55.96  ? 2286 LYS A CD    1 
ATOM   5975  C  CE    . LYS A 1 2286 ? 143.835 196.759 158.435 1.00 62.41  ? 2286 LYS A CE    1 
ATOM   5976  N  NZ    . LYS A 1 2286 ? 142.573 197.378 157.945 1.00 70.43  ? 2286 LYS A NZ    1 
ATOM   5977  N  N     . ILE A 1 2287 ? 145.990 195.167 153.219 1.00 33.48  ? 2287 ILE A N     1 
ATOM   5978  C  CA    . ILE A 1 2287 ? 146.529 195.922 152.090 1.00 30.14  ? 2287 ILE A CA    1 
ATOM   5979  C  C     . ILE A 1 2287 ? 145.838 195.517 150.792 1.00 29.99  ? 2287 ILE A C     1 
ATOM   5980  O  O     . ILE A 1 2287 ? 145.489 196.368 149.965 1.00 37.03  ? 2287 ILE A O     1 
ATOM   5981  C  CB    . ILE A 1 2287 ? 148.055 195.738 152.000 1.00 25.51  ? 2287 ILE A CB    1 
ATOM   5982  C  CG1   . ILE A 1 2287 ? 148.737 196.311 153.243 1.00 25.83  ? 2287 ILE A CG1   1 
ATOM   5983  C  CG2   . ILE A 1 2287 ? 148.596 196.406 150.750 1.00 26.50  ? 2287 ILE A CG2   1 
ATOM   5984  C  CD1   . ILE A 1 2287 ? 150.229 196.071 153.285 1.00 22.12  ? 2287 ILE A CD1   1 
ATOM   5985  N  N     . ILE A 1 2288 ? 145.631 194.212 150.592 1.00 29.46  ? 2288 ILE A N     1 
ATOM   5986  C  CA    . ILE A 1 2288 ? 145.051 193.722 149.342 1.00 30.56  ? 2288 ILE A CA    1 
ATOM   5987  C  C     . ILE A 1 2288 ? 143.615 194.206 149.182 1.00 36.29  ? 2288 ILE A C     1 
ATOM   5988  O  O     . ILE A 1 2288 ? 143.212 194.648 148.099 1.00 41.99  ? 2288 ILE A O     1 
ATOM   5989  C  CB    . ILE A 1 2288 ? 145.140 192.186 149.281 1.00 25.64  ? 2288 ILE A CB    1 
ATOM   5990  C  CG1   . ILE A 1 2288 ? 146.587 191.743 149.061 1.00 20.44  ? 2288 ILE A CG1   1 
ATOM   5991  C  CG2   . ILE A 1 2288 ? 144.247 191.637 148.181 1.00 29.82  ? 2288 ILE A CG2   1 
ATOM   5992  C  CD1   . ILE A 1 2288 ? 146.795 190.259 149.228 1.00 15.00  ? 2288 ILE A CD1   1 
ATOM   5993  N  N     . ASP A 1 2289 ? 142.819 194.127 150.252 1.00 39.41  ? 2289 ASP A N     1 
ATOM   5994  C  CA    . ASP A 1 2289 ? 141.415 194.517 150.162 1.00 44.04  ? 2289 ASP A CA    1 
ATOM   5995  C  C     . ASP A 1 2289 ? 141.271 195.993 149.815 1.00 49.41  ? 2289 ASP A C     1 
ATOM   5996  O  O     . ASP A 1 2289 ? 140.378 196.373 149.047 1.00 53.66  ? 2289 ASP A O     1 
ATOM   5997  C  CB    . ASP A 1 2289 ? 140.694 194.200 151.471 1.00 44.64  ? 2289 ASP A CB    1 
ATOM   5998  C  CG    . ASP A 1 2289 ? 140.706 192.720 151.799 1.00 51.65  ? 2289 ASP A CG    1 
ATOM   5999  O  OD1   . ASP A 1 2289 ? 141.266 191.938 151.002 1.00 47.67  ? 2289 ASP A OD1   1 
ATOM   6000  O  OD2   . ASP A 1 2289 ? 140.157 192.339 152.854 1.00 48.96  ? 2289 ASP A OD2   1 
ATOM   6001  N  N     . SER A 1 2290 ? 142.136 196.838 150.377 1.00 46.27  ? 2290 SER A N     1 
ATOM   6002  C  CA    . SER A 1 2290 ? 142.168 198.271 150.085 1.00 44.35  ? 2290 SER A CA    1 
ATOM   6003  C  C     . SER A 1 2290 ? 140.832 198.936 150.419 1.00 55.18  ? 2290 SER A C     1 
ATOM   6004  O  O     . SER A 1 2290 ? 140.200 199.589 149.586 1.00 59.12  ? 2290 SER A O     1 
ATOM   6005  C  CB    . SER A 1 2290 ? 142.563 198.527 148.628 1.00 42.14  ? 2290 SER A CB    1 
ATOM   6006  O  OG    . SER A 1 2290 ? 142.737 199.911 148.383 1.00 51.58  ? 2290 SER A OG    1 
ATOM   6007  N  N     . VAL A 1 2291 ? 140.407 198.752 151.669 1.00 61.48  ? 2291 VAL A N     1 
ATOM   6008  C  CA    . VAL A 1 2291 ? 139.211 199.435 152.148 1.00 58.34  ? 2291 VAL A CA    1 
ATOM   6009  C  C     . VAL A 1 2291 ? 139.461 200.934 152.247 1.00 59.51  ? 2291 VAL A C     1 
ATOM   6010  O  O     . VAL A 1 2291 ? 138.588 201.748 151.921 1.00 62.07  ? 2291 VAL A O     1 
ATOM   6011  C  CB    . VAL A 1 2291 ? 138.764 198.840 153.496 1.00 59.34  ? 2291 VAL A CB    1 
ATOM   6012  C  CG1   . VAL A 1 2291 ? 137.595 199.624 154.067 1.00 69.05  ? 2291 VAL A CG1   1 
ATOM   6013  C  CG2   . VAL A 1 2291 ? 138.396 197.374 153.330 1.00 65.26  ? 2291 VAL A CG2   1 
ATOM   6014  N  N     . ARG A 1 2292 ? 140.656 201.323 152.682 1.00 58.47  ? 2292 ARG A N     1 
ATOM   6015  C  CA    . ARG A 1 2292 ? 141.026 202.720 152.871 1.00 57.73  ? 2292 ARG A CA    1 
ATOM   6016  C  C     . ARG A 1 2292 ? 142.164 203.120 151.938 1.00 56.15  ? 2292 ARG A C     1 
ATOM   6017  O  O     . ARG A 1 2292 ? 143.028 203.926 152.290 1.00 53.94  ? 2292 ARG A O     1 
ATOM   6018  C  CB    . ARG A 1 2292 ? 141.397 202.984 154.328 1.00 58.82  ? 2292 ARG A CB    1 
ATOM   6019  C  CG    . ARG A 1 2292 ? 140.555 202.194 155.316 1.00 67.97  ? 2292 ARG A CG    1 
ATOM   6020  C  CD    . ARG A 1 2292 ? 140.785 202.647 156.750 1.00 82.05  ? 2292 ARG A CD    1 
ATOM   6021  N  NE    . ARG A 1 2292 ? 139.790 202.100 157.667 1.00 92.83  ? 2292 ARG A NE    1 
ATOM   6022  C  CZ    . ARG A 1 2292 ? 139.681 200.818 157.992 1.00 90.55  ? 2292 ARG A CZ    1 
ATOM   6023  N  NH1   . ARG A 1 2292 ? 140.511 199.907 157.510 1.00 85.69  ? 2292 ARG A NH1   1 
ATOM   6024  N  NH2   . ARG A 1 2292 ? 138.717 200.441 158.827 1.00 89.59  ? 2292 ARG A NH2   1 
ATOM   6025  N  N     . GLY A 1 2293 ? 142.172 202.559 150.733 1.00 51.93  ? 2293 GLY A N     1 
ATOM   6026  C  CA    . GLY A 1 2293 ? 143.147 202.949 149.724 1.00 48.17  ? 2293 GLY A CA    1 
ATOM   6027  C  C     . GLY A 1 2293 ? 144.583 202.607 150.055 1.00 46.57  ? 2293 GLY A C     1 
ATOM   6028  O  O     . GLY A 1 2293 ? 145.475 203.444 149.868 1.00 42.66  ? 2293 GLY A O     1 
ATOM   6029  N  N     . GLU A 1 2294 ? 144.832 201.391 150.545 1.00 46.11  ? 2294 GLU A N     1 
ATOM   6030  C  CA    . GLU A 1 2294 ? 146.197 200.969 150.835 1.00 40.03  ? 2294 GLU A CA    1 
ATOM   6031  C  C     . GLU A 1 2294 ? 146.998 200.624 149.586 1.00 39.05  ? 2294 GLU A C     1 
ATOM   6032  O  O     . GLU A 1 2294 ? 148.229 200.558 149.661 1.00 41.14  ? 2294 GLU A O     1 
ATOM   6033  C  CB    . GLU A 1 2294 ? 146.197 199.771 151.790 1.00 40.14  ? 2294 GLU A CB    1 
ATOM   6034  C  CG    . GLU A 1 2294 ? 145.771 200.095 153.217 1.00 49.35  ? 2294 GLU A CG    1 
ATOM   6035  C  CD    . GLU A 1 2294 ? 144.269 200.111 153.403 1.00 57.93  ? 2294 GLU A CD    1 
ATOM   6036  O  OE1   . GLU A 1 2294 ? 143.546 199.815 152.433 1.00 56.07  ? 2294 GLU A OE1   1 
ATOM   6037  O  OE2   . GLU A 1 2294 ? 143.812 200.415 154.525 1.00 65.56  ? 2294 GLU A OE2   1 
ATOM   6038  N  N     . LEU A 1 2295 ? 146.343 200.402 148.445 1.00 38.59  ? 2295 LEU A N     1 
ATOM   6039  C  CA    . LEU A 1 2295 ? 147.080 200.130 147.217 1.00 34.79  ? 2295 LEU A CA    1 
ATOM   6040  C  C     . LEU A 1 2295 ? 147.660 201.386 146.581 1.00 33.17  ? 2295 LEU A C     1 
ATOM   6041  O  O     . LEU A 1 2295 ? 148.528 201.274 145.709 1.00 32.10  ? 2295 LEU A O     1 
ATOM   6042  C  CB    . LEU A 1 2295 ? 146.193 199.414 146.194 1.00 38.13  ? 2295 LEU A CB    1 
ATOM   6043  C  CG    . LEU A 1 2295 ? 145.638 198.035 146.554 1.00 37.97  ? 2295 LEU A CG    1 
ATOM   6044  C  CD1   . LEU A 1 2295 ? 144.390 197.738 145.738 1.00 40.25  ? 2295 LEU A CD1   1 
ATOM   6045  C  CD2   . LEU A 1 2295 ? 146.689 196.960 146.343 1.00 32.18  ? 2295 LEU A CD2   1 
ATOM   6046  N  N     . GLN A 1 2296 ? 147.207 202.569 146.988 1.00 36.59  ? 2296 GLN A N     1 
ATOM   6047  C  CA    . GLN A 1 2296 ? 147.749 203.823 146.486 1.00 37.08  ? 2296 GLN A CA    1 
ATOM   6048  C  C     . GLN A 1 2296 ? 148.907 204.341 147.327 1.00 34.99  ? 2296 GLN A C     1 
ATOM   6049  O  O     . GLN A 1 2296 ? 149.443 205.412 147.028 1.00 36.18  ? 2296 GLN A O     1 
ATOM   6050  C  CB    . GLN A 1 2296 ? 146.648 204.888 146.415 1.00 39.95  ? 2296 GLN A CB    1 
ATOM   6051  C  CG    . GLN A 1 2296 ? 145.702 204.736 145.233 1.00 41.68  ? 2296 GLN A CG    1 
ATOM   6052  C  CD    . GLN A 1 2296 ? 144.725 203.590 145.406 1.00 42.61  ? 2296 GLN A CD    1 
ATOM   6053  O  OE1   . GLN A 1 2296 ? 144.732 202.631 144.635 1.00 41.54  ? 2296 GLN A OE1   1 
ATOM   6054  N  NE2   . GLN A 1 2296 ? 143.875 203.684 146.422 1.00 42.38  ? 2296 GLN A NE2   1 
ATOM   6055  N  N     . LYS A 1 2297 ? 149.302 203.610 148.365 1.00 32.34  ? 2297 LYS A N     1 
ATOM   6056  C  CA    . LYS A 1 2297 ? 150.394 203.998 149.240 1.00 28.42  ? 2297 LYS A CA    1 
ATOM   6057  C  C     . LYS A 1 2297 ? 151.540 203.004 149.116 1.00 27.18  ? 2297 LYS A C     1 
ATOM   6058  O  O     . LYS A 1 2297 ? 151.330 201.818 148.847 1.00 32.21  ? 2297 LYS A O     1 
ATOM   6059  C  CB    . LYS A 1 2297 ? 149.936 204.070 150.700 1.00 31.30  ? 2297 LYS A CB    1 
ATOM   6060  C  CG    . LYS A 1 2297 ? 148.610 204.776 150.909 1.00 39.42  ? 2297 LYS A CG    1 
ATOM   6061  C  CD    . LYS A 1 2297 ? 148.481 205.277 152.337 1.00 40.80  ? 2297 LYS A CD    1 
ATOM   6062  C  CE    . LYS A 1 2297 ? 147.030 205.535 152.703 1.00 53.87  ? 2297 LYS A CE    1 
ATOM   6063  N  NZ    . LYS A 1 2297 ? 146.478 204.452 153.563 1.00 58.65  ? 2297 LYS A NZ    1 
ATOM   6064  N  N     . ARG A 1 2298 ? 152.758 203.499 149.315 1.00 24.98  ? 2298 ARG A N     1 
ATOM   6065  C  CA    . ARG A 1 2298 ? 153.942 202.648 149.311 1.00 20.65  ? 2298 ARG A CA    1 
ATOM   6066  C  C     . ARG A 1 2298 ? 153.997 201.899 150.637 1.00 22.51  ? 2298 ARG A C     1 
ATOM   6067  O  O     . ARG A 1 2298 ? 154.304 202.487 151.679 1.00 29.13  ? 2298 ARG A O     1 
ATOM   6068  C  CB    . ARG A 1 2298 ? 155.198 203.486 149.088 1.00 18.61  ? 2298 ARG A CB    1 
ATOM   6069  C  CG    . ARG A 1 2298 ? 156.499 202.769 149.399 1.00 18.34  ? 2298 ARG A CG    1 
ATOM   6070  C  CD    . ARG A 1 2298 ? 157.694 203.658 149.099 1.00 20.23  ? 2298 ARG A CD    1 
ATOM   6071  N  NE    . ARG A 1 2298 ? 157.955 203.758 147.668 1.00 19.81  ? 2298 ARG A NE    1 
ATOM   6072  C  CZ    . ARG A 1 2298 ? 157.617 204.796 146.916 1.00 22.12  ? 2298 ARG A CZ    1 
ATOM   6073  N  NH1   . ARG A 1 2298 ? 156.996 205.846 147.427 1.00 23.29  ? 2298 ARG A NH1   1 
ATOM   6074  N  NH2   . ARG A 1 2298 ? 157.908 204.779 145.619 1.00 27.13  ? 2298 ARG A NH2   1 
ATOM   6075  N  N     . GLN A 1 2299 ? 153.692 200.606 150.603 1.00 17.94  ? 2299 GLN A N     1 
ATOM   6076  C  CA    . GLN A 1 2299 ? 153.611 199.788 151.805 1.00 14.54  ? 2299 GLN A CA    1 
ATOM   6077  C  C     . GLN A 1 2299 ? 154.863 198.933 151.933 1.00 14.76  ? 2299 GLN A C     1 
ATOM   6078  O  O     . GLN A 1 2299 ? 155.214 198.193 151.008 1.00 19.13  ? 2299 GLN A O     1 
ATOM   6079  C  CB    . GLN A 1 2299 ? 152.365 198.902 151.775 1.00 18.29  ? 2299 GLN A CB    1 
ATOM   6080  C  CG    . GLN A 1 2299 ? 151.093 199.646 151.410 1.00 22.81  ? 2299 GLN A CG    1 
ATOM   6081  C  CD    . GLN A 1 2299 ? 150.379 200.206 152.623 1.00 28.38  ? 2299 GLN A CD    1 
ATOM   6082  O  OE1   . GLN A 1 2299 ? 150.826 200.032 153.756 1.00 27.58  ? 2299 GLN A OE1   1 
ATOM   6083  N  NE2   . GLN A 1 2299 ? 149.266 200.890 152.390 1.00 32.63  ? 2299 GLN A NE2   1 
ATOM   6084  N  N     . TRP A 1 2300 ? 155.531 199.037 153.079 1.00 14.43  ? 2300 TRP A N     1 
ATOM   6085  C  CA    . TRP A 1 2300 ? 156.752 198.291 153.362 1.00 11.80  ? 2300 TRP A CA    1 
ATOM   6086  C  C     . TRP A 1 2300 ? 156.515 197.443 154.604 1.00 12.75  ? 2300 TRP A C     1 
ATOM   6087  O  O     . TRP A 1 2300 ? 156.323 197.981 155.700 1.00 22.54  ? 2300 TRP A O     1 
ATOM   6088  C  CB    . TRP A 1 2300 ? 157.937 199.235 153.562 1.00 12.36  ? 2300 TRP A CB    1 
ATOM   6089  C  CG    . TRP A 1 2300 ? 158.500 199.779 152.288 1.00 12.73  ? 2300 TRP A CG    1 
ATOM   6090  C  CD1   . TRP A 1 2300 ? 158.027 199.570 151.027 1.00 13.34  ? 2300 TRP A CD1   1 
ATOM   6091  C  CD2   . TRP A 1 2300 ? 159.642 200.632 152.151 1.00 14.28  ? 2300 TRP A CD2   1 
ATOM   6092  N  NE1   . TRP A 1 2300 ? 158.805 200.235 150.112 1.00 13.43  ? 2300 TRP A NE1   1 
ATOM   6093  C  CE2   . TRP A 1 2300 ? 159.804 200.896 150.777 1.00 15.73  ? 2300 TRP A CE2   1 
ATOM   6094  C  CE3   . TRP A 1 2300 ? 160.545 201.196 153.057 1.00 12.10  ? 2300 TRP A CE3   1 
ATOM   6095  C  CZ2   . TRP A 1 2300 ? 160.831 201.699 150.288 1.00 14.75  ? 2300 TRP A CZ2   1 
ATOM   6096  C  CZ3   . TRP A 1 2300 ? 161.563 201.993 152.569 1.00 12.58  ? 2300 TRP A CZ3   1 
ATOM   6097  C  CH2   . TRP A 1 2300 ? 161.698 202.237 151.198 1.00 12.94  ? 2300 TRP A CH2   1 
ATOM   6098  N  N     . ILE A 1 2301 ? 156.530 196.126 154.437 1.00 8.28   ? 2301 ILE A N     1 
ATOM   6099  C  CA    . ILE A 1 2301 ? 156.373 195.189 155.542 1.00 9.80   ? 2301 ILE A CA    1 
ATOM   6100  C  C     . ILE A 1 2301 ? 157.769 194.768 155.978 1.00 9.95   ? 2301 ILE A C     1 
ATOM   6101  O  O     . ILE A 1 2301 ? 158.418 193.951 155.316 1.00 13.65  ? 2301 ILE A O     1 
ATOM   6102  C  CB    . ILE A 1 2301 ? 155.517 193.981 155.144 1.00 10.10  ? 2301 ILE A CB    1 
ATOM   6103  C  CG1   . ILE A 1 2301 ? 154.140 194.443 154.665 1.00 11.08  ? 2301 ILE A CG1   1 
ATOM   6104  C  CG2   . ILE A 1 2301 ? 155.381 193.018 156.313 1.00 10.04  ? 2301 ILE A CG2   1 
ATOM   6105  C  CD1   . ILE A 1 2301 ? 153.226 193.313 154.251 1.00 11.05  ? 2301 ILE A CD1   1 
ATOM   6106  N  N     . VAL A 1 2302 ? 158.235 195.324 157.093 1.00 10.56  ? 2302 VAL A N     1 
ATOM   6107  C  CA    . VAL A 1 2302 ? 159.594 195.114 157.575 1.00 11.04  ? 2302 VAL A CA    1 
ATOM   6108  C  C     . VAL A 1 2302 ? 159.576 194.038 158.649 1.00 11.44  ? 2302 VAL A C     1 
ATOM   6109  O  O     . VAL A 1 2302 ? 158.797 194.117 159.608 1.00 15.37  ? 2302 VAL A O     1 
ATOM   6110  C  CB    . VAL A 1 2302 ? 160.202 196.419 158.114 1.00 9.59   ? 2302 VAL A CB    1 
ATOM   6111  C  CG1   . VAL A 1 2302 ? 161.701 196.263 158.309 1.00 11.16  ? 2302 VAL A CG1   1 
ATOM   6112  C  CG2   . VAL A 1 2302 ? 159.899 197.572 157.173 1.00 9.83   ? 2302 VAL A CG2   1 
ATOM   6113  N  N     . PHE A 1 2303 ? 160.431 193.030 158.490 1.00 9.23   ? 2303 PHE A N     1 
ATOM   6114  C  CA    . PHE A 1 2303 ? 160.566 191.942 159.457 1.00 8.73   ? 2303 PHE A CA    1 
ATOM   6115  C  C     . PHE A 1 2303 ? 161.818 192.213 160.284 1.00 12.58  ? 2303 PHE A C     1 
ATOM   6116  O  O     . PHE A 1 2303 ? 162.897 191.691 160.005 1.00 14.07  ? 2303 PHE A O     1 
ATOM   6117  C  CB    . PHE A 1 2303 ? 160.633 190.593 158.751 1.00 10.07  ? 2303 PHE A CB    1 
ATOM   6118  C  CG    . PHE A 1 2303 ? 159.302 190.096 158.268 1.00 9.49   ? 2303 PHE A CG    1 
ATOM   6119  C  CD1   . PHE A 1 2303 ? 158.342 189.662 159.165 1.00 11.35  ? 2303 PHE A CD1   1 
ATOM   6120  C  CD2   . PHE A 1 2303 ? 159.010 190.064 156.915 1.00 8.59   ? 2303 PHE A CD2   1 
ATOM   6121  C  CE1   . PHE A 1 2303 ? 157.118 189.204 158.724 1.00 11.65  ? 2303 PHE A CE1   1 
ATOM   6122  C  CE2   . PHE A 1 2303 ? 157.787 189.607 156.468 1.00 10.43  ? 2303 PHE A CE2   1 
ATOM   6123  C  CZ    . PHE A 1 2303 ? 156.840 189.176 157.374 1.00 11.57  ? 2303 PHE A CZ    1 
ATOM   6124  N  N     . ASP A 1 2304 ? 161.665 193.042 161.317 1.00 15.79  ? 2304 ASP A N     1 
ATOM   6125  C  CA    . ASP A 1 2304 ? 162.782 193.439 162.175 1.00 15.68  ? 2304 ASP A CA    1 
ATOM   6126  C  C     . ASP A 1 2304 ? 162.962 192.377 163.256 1.00 17.06  ? 2304 ASP A C     1 
ATOM   6127  O  O     . ASP A 1 2304 ? 162.497 192.506 164.390 1.00 25.71  ? 2304 ASP A O     1 
ATOM   6128  C  CB    . ASP A 1 2304 ? 162.534 194.821 162.768 1.00 17.37  ? 2304 ASP A CB    1 
ATOM   6129  C  CG    . ASP A 1 2304 ? 163.790 195.449 163.343 1.00 23.64  ? 2304 ASP A CG    1 
ATOM   6130  O  OD1   . ASP A 1 2304 ? 164.666 194.711 163.839 1.00 22.34  ? 2304 ASP A OD1   1 
ATOM   6131  O  OD2   . ASP A 1 2304 ? 163.900 196.692 163.298 1.00 29.89  ? 2304 ASP A OD2   1 
ATOM   6132  N  N     . GLY A 1 2305 ? 163.654 191.308 162.887 1.00 12.46  ? 2305 GLY A N     1 
ATOM   6133  C  CA    . GLY A 1 2305 ? 163.901 190.226 163.822 1.00 15.64  ? 2305 GLY A CA    1 
ATOM   6134  C  C     . GLY A 1 2305 ? 164.746 189.153 163.175 1.00 21.72  ? 2305 GLY A C     1 
ATOM   6135  O  O     . GLY A 1 2305 ? 165.132 189.251 162.006 1.00 25.22  ? 2305 GLY A O     1 
ATOM   6136  N  N     . ASP A 1 2306 ? 165.027 188.117 163.960 1.00 23.94  ? 2306 ASP A N     1 
ATOM   6137  C  CA    . ASP A 1 2306 ? 165.859 187.020 163.488 1.00 18.06  ? 2306 ASP A CA    1 
ATOM   6138  C  C     . ASP A 1 2306 ? 165.124 186.194 162.438 1.00 17.76  ? 2306 ASP A C     1 
ATOM   6139  O  O     . ASP A 1 2306 ? 163.897 186.070 162.457 1.00 22.73  ? 2306 ASP A O     1 
ATOM   6140  C  CB    . ASP A 1 2306 ? 166.278 186.128 164.655 1.00 21.84  ? 2306 ASP A CB    1 
ATOM   6141  C  CG    . ASP A 1 2306 ? 166.789 186.922 165.841 1.00 32.17  ? 2306 ASP A CG    1 
ATOM   6142  O  OD1   . ASP A 1 2306 ? 167.385 187.998 165.627 1.00 46.82  ? 2306 ASP A OD1   1 
ATOM   6143  O  OD2   . ASP A 1 2306 ? 166.594 186.471 166.988 1.00 22.92  ? 2306 ASP A OD2   1 
ATOM   6144  N  N     . VAL A 1 2307 ? 165.893 185.626 161.514 1.00 18.03  ? 2307 VAL A N     1 
ATOM   6145  C  CA    . VAL A 1 2307 ? 165.365 184.799 160.436 1.00 19.16  ? 2307 VAL A CA    1 
ATOM   6146  C  C     . VAL A 1 2307 ? 165.801 183.361 160.664 1.00 23.01  ? 2307 VAL A C     1 
ATOM   6147  O  O     . VAL A 1 2307 ? 166.999 183.079 160.781 1.00 26.75  ? 2307 VAL A O     1 
ATOM   6148  C  CB    . VAL A 1 2307 ? 165.830 185.295 159.054 1.00 14.61  ? 2307 VAL A CB    1 
ATOM   6149  C  CG1   . VAL A 1 2307 ? 165.415 184.314 157.979 1.00 16.55  ? 2307 VAL A CG1   1 
ATOM   6150  C  CG2   . VAL A 1 2307 ? 165.235 186.654 158.763 1.00 14.53  ? 2307 VAL A CG2   1 
ATOM   6151  N  N     . ASP A 1 2308 ? 164.831 182.460 160.727 1.00 22.65  ? 2308 ASP A N     1 
ATOM   6152  C  CA    . ASP A 1 2308 ? 165.077 181.030 160.795 1.00 21.40  ? 2308 ASP A CA    1 
ATOM   6153  C  C     . ASP A 1 2308 ? 164.220 180.343 159.744 1.00 23.56  ? 2308 ASP A C     1 
ATOM   6154  O  O     . ASP A 1 2308 ? 163.208 180.897 159.302 1.00 25.97  ? 2308 ASP A O     1 
ATOM   6155  C  CB    . ASP A 1 2308 ? 164.830 180.478 162.213 1.00 23.57  ? 2308 ASP A CB    1 
ATOM   6156  C  CG    . ASP A 1 2308 ? 163.351 180.264 162.561 1.00 31.80  ? 2308 ASP A CG    1 
ATOM   6157  O  OD1   . ASP A 1 2308 ? 162.439 180.596 161.783 1.00 30.37  ? 2308 ASP A OD1   1 
ATOM   6158  O  OD2   . ASP A 1 2308 ? 163.097 179.739 163.664 1.00 38.68  ? 2308 ASP A OD2   1 
ATOM   6159  N  N     . PRO A 1 2309 ? 164.612 179.147 159.302 1.00 22.15  ? 2309 PRO A N     1 
ATOM   6160  C  CA    . PRO A 1 2309 ? 163.889 178.502 158.196 1.00 24.26  ? 2309 PRO A CA    1 
ATOM   6161  C  C     . PRO A 1 2309 ? 162.544 177.914 158.595 1.00 25.60  ? 2309 PRO A C     1 
ATOM   6162  O  O     . PRO A 1 2309 ? 161.969 177.119 157.847 1.00 33.52  ? 2309 PRO A O     1 
ATOM   6163  C  CB    . PRO A 1 2309 ? 164.861 177.406 157.742 1.00 27.30  ? 2309 PRO A CB    1 
ATOM   6164  C  CG    . PRO A 1 2309 ? 165.690 177.130 158.940 1.00 28.81  ? 2309 PRO A CG    1 
ATOM   6165  C  CD    . PRO A 1 2309 ? 165.869 178.448 159.614 1.00 22.28  ? 2309 PRO A CD    1 
ATOM   6166  N  N     . GLU A 1 2310 ? 162.034 178.278 159.770 1.00 24.34  ? 2310 GLU A N     1 
ATOM   6167  C  CA    . GLU A 1 2310 ? 160.701 177.842 160.165 1.00 24.04  ? 2310 GLU A CA    1 
ATOM   6168  C  C     . GLU A 1 2310 ? 159.623 178.816 159.703 1.00 25.40  ? 2310 GLU A C     1 
ATOM   6169  O  O     . GLU A 1 2310 ? 158.560 178.393 159.240 1.00 27.85  ? 2310 GLU A O     1 
ATOM   6170  C  CB    . GLU A 1 2310 ? 160.632 177.655 161.683 1.00 29.44  ? 2310 GLU A CB    1 
ATOM   6171  C  CG    . GLU A 1 2310 ? 161.702 176.737 162.237 1.00 39.27  ? 2310 GLU A CG    1 
ATOM   6172  C  CD    . GLU A 1 2310 ? 161.382 175.272 162.022 1.00 54.46  ? 2310 GLU A CD    1 
ATOM   6173  O  OE1   . GLU A 1 2310 ? 160.251 174.854 162.348 1.00 60.00  ? 2310 GLU A OE1   1 
ATOM   6174  O  OE2   . GLU A 1 2310 ? 162.262 174.537 161.527 1.00 52.17  ? 2310 GLU A OE2   1 
ATOM   6175  N  N     . TRP A 1 2311 ? 159.879 180.119 159.820 1.00 23.83  ? 2311 TRP A N     1 
ATOM   6176  C  CA    . TRP A 1 2311 ? 158.896 181.122 159.438 1.00 17.22  ? 2311 TRP A CA    1 
ATOM   6177  C  C     . TRP A 1 2311 ? 159.192 181.787 158.101 1.00 17.50  ? 2311 TRP A C     1 
ATOM   6178  O  O     . TRP A 1 2311 ? 158.253 182.228 157.430 1.00 19.79  ? 2311 TRP A O     1 
ATOM   6179  C  CB    . TRP A 1 2311 ? 158.781 182.201 160.527 1.00 14.46  ? 2311 TRP A CB    1 
ATOM   6180  C  CG    . TRP A 1 2311 ? 159.930 183.168 160.569 1.00 15.51  ? 2311 TRP A CG    1 
ATOM   6181  C  CD1   . TRP A 1 2311 ? 161.035 183.089 161.361 1.00 15.03  ? 2311 TRP A CD1   1 
ATOM   6182  C  CD2   . TRP A 1 2311 ? 160.073 184.370 159.802 1.00 14.47  ? 2311 TRP A CD2   1 
ATOM   6183  N  NE1   . TRP A 1 2311 ? 161.866 184.156 161.126 1.00 11.84  ? 2311 TRP A NE1   1 
ATOM   6184  C  CE2   . TRP A 1 2311 ? 161.297 184.958 160.173 1.00 12.70  ? 2311 TRP A CE2   1 
ATOM   6185  C  CE3   . TRP A 1 2311 ? 159.289 185.002 158.832 1.00 11.55  ? 2311 TRP A CE3   1 
ATOM   6186  C  CZ2   . TRP A 1 2311 ? 161.756 186.144 159.609 1.00 12.68  ? 2311 TRP A CZ2   1 
ATOM   6187  C  CZ3   . TRP A 1 2311 ? 159.745 186.179 158.275 1.00 10.22  ? 2311 TRP A CZ3   1 
ATOM   6188  C  CH2   . TRP A 1 2311 ? 160.965 186.739 158.667 1.00 12.00  ? 2311 TRP A CH2   1 
ATOM   6189  N  N     . VAL A 1 2312 ? 160.459 181.869 157.691 1.00 18.25  ? 2312 VAL A N     1 
ATOM   6190  C  CA    . VAL A 1 2312 ? 160.777 182.577 156.455 1.00 14.30  ? 2312 VAL A CA    1 
ATOM   6191  C  C     . VAL A 1 2312 ? 160.504 181.721 155.224 1.00 19.50  ? 2312 VAL A C     1 
ATOM   6192  O  O     . VAL A 1 2312 ? 160.247 182.267 154.143 1.00 22.13  ? 2312 VAL A O     1 
ATOM   6193  C  CB    . VAL A 1 2312 ? 162.239 183.058 156.458 1.00 11.42  ? 2312 VAL A CB    1 
ATOM   6194  C  CG1   . VAL A 1 2312 ? 163.200 181.883 156.367 1.00 19.22  ? 2312 VAL A CG1   1 
ATOM   6195  C  CG2   . VAL A 1 2312 ? 162.484 184.066 155.344 1.00 15.48  ? 2312 VAL A CG2   1 
ATOM   6196  N  N     . GLU A 1 2313 ? 160.534 180.393 155.356 1.00 19.40  ? 2313 GLU A N     1 
ATOM   6197  C  CA    . GLU A 1 2313 ? 160.244 179.524 154.223 1.00 17.91  ? 2313 GLU A CA    1 
ATOM   6198  C  C     . GLU A 1 2313 ? 158.780 179.568 153.813 1.00 20.94  ? 2313 GLU A C     1 
ATOM   6199  O  O     . GLU A 1 2313 ? 158.455 179.178 152.686 1.00 30.07  ? 2313 GLU A O     1 
ATOM   6200  C  CB    . GLU A 1 2313 ? 160.651 178.085 154.540 1.00 21.28  ? 2313 GLU A CB    1 
ATOM   6201  C  CG    . GLU A 1 2313 ? 162.128 177.913 154.851 1.00 27.28  ? 2313 GLU A CG    1 
ATOM   6202  C  CD    . GLU A 1 2313 ? 163.000 177.973 153.615 1.00 41.98  ? 2313 GLU A CD    1 
ATOM   6203  O  OE1   . GLU A 1 2313 ? 162.818 177.127 152.715 1.00 47.32  ? 2313 GLU A OE1   1 
ATOM   6204  O  OE2   . GLU A 1 2313 ? 163.872 178.864 153.545 1.00 46.56  ? 2313 GLU A OE2   1 
ATOM   6205  N  N     . ASN A 1 2314 ? 157.890 180.026 154.696 1.00 17.17  ? 2314 ASN A N     1 
ATOM   6206  C  CA    . ASN A 1 2314 ? 156.509 180.265 154.297 1.00 17.58  ? 2314 ASN A CA    1 
ATOM   6207  C  C     . ASN A 1 2314 ? 156.393 181.441 153.339 1.00 23.38  ? 2314 ASN A C     1 
ATOM   6208  O  O     . ASN A 1 2314 ? 155.374 181.572 152.654 1.00 32.22  ? 2314 ASN A O     1 
ATOM   6209  C  CB    . ASN A 1 2314 ? 155.635 180.504 155.527 1.00 17.70  ? 2314 ASN A CB    1 
ATOM   6210  C  CG    . ASN A 1 2314 ? 155.535 179.282 156.414 1.00 23.86  ? 2314 ASN A CG    1 
ATOM   6211  O  OD1   . ASN A 1 2314 ? 156.543 178.758 156.883 1.00 26.80  ? 2314 ASN A OD1   1 
ATOM   6212  N  ND2   . ASN A 1 2314 ? 154.312 178.823 156.651 1.00 27.74  ? 2314 ASN A ND2   1 
ATOM   6213  N  N     . LEU A 1 2315 ? 157.413 182.295 153.279 1.00 19.32  ? 2315 LEU A N     1 
ATOM   6214  C  CA    . LEU A 1 2315 ? 157.460 183.413 152.351 1.00 17.01  ? 2315 LEU A CA    1 
ATOM   6215  C  C     . LEU A 1 2315 ? 158.167 183.060 151.051 1.00 19.86  ? 2315 LEU A C     1 
ATOM   6216  O  O     . LEU A 1 2315 ? 158.434 183.955 150.244 1.00 29.09  ? 2315 LEU A O     1 
ATOM   6217  C  CB    . LEU A 1 2315 ? 158.148 184.614 153.001 1.00 15.60  ? 2315 LEU A CB    1 
ATOM   6218  C  CG    . LEU A 1 2315 ? 157.501 185.171 154.268 1.00 13.64  ? 2315 LEU A CG    1 
ATOM   6219  C  CD1   . LEU A 1 2315 ? 158.312 186.332 154.817 1.00 12.80  ? 2315 LEU A CD1   1 
ATOM   6220  C  CD2   . LEU A 1 2315 ? 156.073 185.593 153.989 1.00 14.70  ? 2315 LEU A CD2   1 
ATOM   6221  N  N     . ASN A 1 2316 ? 158.488 181.782 150.838 1.00 17.84  ? 2316 ASN A N     1 
ATOM   6222  C  CA    . ASN A 1 2316 ? 159.197 181.390 149.624 1.00 18.10  ? 2316 ASN A CA    1 
ATOM   6223  C  C     . ASN A 1 2316 ? 158.394 181.748 148.380 1.00 19.28  ? 2316 ASN A C     1 
ATOM   6224  O  O     . ASN A 1 2316 ? 158.906 182.402 147.467 1.00 22.84  ? 2316 ASN A O     1 
ATOM   6225  C  CB    . ASN A 1 2316 ? 159.503 179.893 149.656 1.00 17.73  ? 2316 ASN A CB    1 
ATOM   6226  C  CG    . ASN A 1 2316 ? 160.849 179.587 150.278 1.00 25.13  ? 2316 ASN A CG    1 
ATOM   6227  O  OD1   . ASN A 1 2316 ? 161.540 180.482 150.763 1.00 31.20  ? 2316 ASN A OD1   1 
ATOM   6228  N  ND2   . ASN A 1 2316 ? 161.229 178.316 150.267 1.00 23.33  ? 2316 ASN A ND2   1 
ATOM   6229  N  N     . SER A 1 2317 ? 157.122 181.348 148.338 1.00 20.31  ? 2317 SER A N     1 
ATOM   6230  C  CA    . SER A 1 2317 ? 156.282 181.698 147.199 1.00 19.21  ? 2317 SER A CA    1 
ATOM   6231  C  C     . SER A 1 2317 ? 156.035 183.197 147.107 1.00 18.49  ? 2317 SER A C     1 
ATOM   6232  O  O     . SER A 1 2317 ? 155.740 183.699 146.017 1.00 23.22  ? 2317 SER A O     1 
ATOM   6233  C  CB    . SER A 1 2317 ? 154.949 180.953 147.278 1.00 20.46  ? 2317 SER A CB    1 
ATOM   6234  O  OG    . SER A 1 2317 ? 154.347 181.118 148.549 1.00 26.32  ? 2317 SER A OG    1 
ATOM   6235  N  N     . VAL A 1 2318 ? 156.141 183.919 148.223 1.00 16.86  ? 2318 VAL A N     1 
ATOM   6236  C  CA    . VAL A 1 2318 ? 155.973 185.368 148.192 1.00 15.31  ? 2318 VAL A CA    1 
ATOM   6237  C  C     . VAL A 1 2318 ? 157.158 186.032 147.502 1.00 17.81  ? 2318 VAL A C     1 
ATOM   6238  O  O     . VAL A 1 2318 ? 156.992 186.995 146.743 1.00 19.71  ? 2318 VAL A O     1 
ATOM   6239  C  CB    . VAL A 1 2318 ? 155.771 185.911 149.618 1.00 13.38  ? 2318 VAL A CB    1 
ATOM   6240  C  CG1   . VAL A 1 2318 ? 155.353 187.370 149.576 1.00 15.70  ? 2318 VAL A CG1   1 
ATOM   6241  C  CG2   . VAL A 1 2318 ? 154.740 185.078 150.361 1.00 18.45  ? 2318 VAL A CG2   1 
ATOM   6242  N  N     . LEU A 1 2319 ? 158.368 185.567 147.829 1.00 19.63  ? 2319 LEU A N     1 
ATOM   6243  C  CA    . LEU A 1 2319 ? 159.595 186.203 147.281 1.00 20.07  ? 2319 LEU A CA    1 
ATOM   6244  C  C     . LEU A 1 2319 ? 159.840 185.712 145.848 1.00 21.52  ? 2319 LEU A C     1 
ATOM   6245  O  O     . LEU A 1 2319 ? 160.543 186.416 145.093 1.00 24.65  ? 2319 LEU A O     1 
ATOM   6246  C  CB    . LEU A 1 2319 ? 160.764 185.867 148.204 1.00 20.55  ? 2319 LEU A CB    1 
ATOM   6247  C  CG    . LEU A 1 2319 ? 160.554 186.187 149.687 1.00 18.21  ? 2319 LEU A CG    1 
ATOM   6248  C  CD1   . LEU A 1 2319 ? 161.647 185.570 150.540 1.00 16.53  ? 2319 LEU A CD1   1 
ATOM   6249  C  CD2   . LEU A 1 2319 ? 160.476 187.687 149.915 1.00 17.11  ? 2319 LEU A CD2   1 
ATOM   6250  N  N     . ASP A 1 2320 ? 159.282 184.552 145.495 1.00 21.03  ? 2320 ASP A N     1 
ATOM   6251  C  CA    . ASP A 1 2320 ? 159.426 184.019 144.113 1.00 23.57  ? 2320 ASP A CA    1 
ATOM   6252  C  C     . ASP A 1 2320 ? 158.557 184.852 143.166 1.00 31.00  ? 2320 ASP A C     1 
ATOM   6253  O  O     . ASP A 1 2320 ? 157.754 185.672 143.663 1.00 30.92  ? 2320 ASP A O     1 
ATOM   6254  C  CB    . ASP A 1 2320 ? 159.091 182.537 144.055 1.00 25.59  ? 2320 ASP A CB    1 
ATOM   6255  C  CG    . ASP A 1 2320 ? 160.119 181.617 144.696 1.00 36.33  ? 2320 ASP A CG    1 
ATOM   6256  O  OD1   . ASP A 1 2320 ? 161.158 182.133 145.155 1.00 38.98  ? 2320 ASP A OD1   1 
ATOM   6257  O  OD2   . ASP A 1 2320 ? 159.868 180.394 144.736 1.00 38.33  ? 2320 ASP A OD2   1 
ATOM   6258  N  N     . ASP A 1 2321 ? 158.708 184.643 141.856 1.00 38.74  ? 2321 ASP A N     1 
ATOM   6259  C  CA    . ASP A 1 2321 ? 157.876 185.375 140.862 1.00 38.68  ? 2321 ASP A CA    1 
ATOM   6260  C  C     . ASP A 1 2321 ? 156.402 185.159 141.214 1.00 32.80  ? 2321 ASP A C     1 
ATOM   6261  O  O     . ASP A 1 2321 ? 155.585 186.062 140.930 1.00 37.02  ? 2321 ASP A O     1 
ATOM   6262  C  CB    . ASP A 1 2321 ? 158.201 184.934 139.444 1.00 51.92  ? 2321 ASP A CB    1 
ATOM   6263  C  CG    . ASP A 1 2321 ? 159.674 184.988 139.066 1.00 56.70  ? 2321 ASP A CG    1 
ATOM   6264  O  OD1   . ASP A 1 2321 ? 160.485 185.395 139.924 1.00 54.00  ? 2321 ASP A OD1   1 
ATOM   6265  O  OD2   . ASP A 1 2321 ? 159.999 184.618 137.918 1.00 55.92  ? 2321 ASP A OD2   1 
ATOM   6266  N  N     . ASN A 1 2322 ? 156.081 184.006 141.808 1.00 26.30  ? 2322 ASN A N     1 
ATOM   6267  C  CA    . ASN A 1 2322 ? 154.680 183.699 142.207 1.00 25.28  ? 2322 ASN A CA    1 
ATOM   6268  C  C     . ASN A 1 2322 ? 154.077 184.905 142.933 1.00 25.50  ? 2322 ASN A C     1 
ATOM   6269  O  O     . ASN A 1 2322 ? 152.848 185.104 142.819 1.00 25.44  ? 2322 ASN A O     1 
ATOM   6270  C  CB    . ASN A 1 2322 ? 154.615 182.446 143.071 1.00 24.24  ? 2322 ASN A CB    1 
ATOM   6271  C  CG    . ASN A 1 2322 ? 155.371 181.293 142.456 1.00 32.12  ? 2322 ASN A CG    1 
ATOM   6272  O  OD1   . ASN A 1 2322 ? 155.052 180.864 141.341 1.00 34.73  ? 2322 ASN A OD1   1 
ATOM   6273  N  ND2   . ASN A 1 2322 ? 156.373 180.784 143.157 1.00 27.05  ? 2322 ASN A ND2   1 
ATOM   6274  N  N     . LYS A 1 2323 ? 154.903 185.678 143.645 1.00 22.38  ? 2323 LYS A N     1 
ATOM   6275  C  CA    . LYS A 1 2323 ? 154.388 186.809 144.419 1.00 21.15  ? 2323 LYS A CA    1 
ATOM   6276  C  C     . LYS A 1 2323 ? 153.077 186.442 145.110 1.00 20.76  ? 2323 LYS A C     1 
ATOM   6277  O  O     . LYS A 1 2323 ? 152.120 187.217 145.124 1.00 26.14  ? 2323 LYS A O     1 
ATOM   6278  C  CB    . LYS A 1 2323 ? 154.215 188.051 143.542 1.00 19.68  ? 2323 LYS A CB    1 
ATOM   6279  C  CG    . LYS A 1 2323 ? 155.481 188.869 143.371 1.00 21.22  ? 2323 LYS A CG    1 
ATOM   6280  C  CD    . LYS A 1 2323 ? 155.259 190.038 142.428 1.00 24.21  ? 2323 LYS A CD    1 
ATOM   6281  C  CE    . LYS A 1 2323 ? 155.598 189.664 140.996 1.00 33.21  ? 2323 LYS A CE    1 
ATOM   6282  N  NZ    . LYS A 1 2323 ? 157.057 189.430 140.812 1.00 32.30  ? 2323 LYS A NZ    1 
ATOM   6283  N  N     . LEU A 1 2324 ? 153.037 185.244 145.686 1.00 18.88  ? 2324 LEU A N     1 
ATOM   6284  C  CA    . LEU A 1 2324 ? 151.817 184.664 146.222 1.00 18.27  ? 2324 LEU A CA    1 
ATOM   6285  C  C     . LEU A 1 2324 ? 152.065 184.126 147.622 1.00 19.52  ? 2324 LEU A C     1 
ATOM   6286  O  O     . LEU A 1 2324 ? 153.111 183.530 147.891 1.00 25.90  ? 2324 LEU A O     1 
ATOM   6287  C  CB    . LEU A 1 2324 ? 151.313 183.539 145.315 1.00 17.47  ? 2324 LEU A CB    1 
ATOM   6288  C  CG    . LEU A 1 2324 ? 149.830 183.186 145.351 1.00 17.75  ? 2324 LEU A CG    1 
ATOM   6289  C  CD1   . LEU A 1 2324 ? 149.026 184.160 144.513 1.00 20.74  ? 2324 LEU A CD1   1 
ATOM   6290  C  CD2   . LEU A 1 2324 ? 149.644 181.771 144.853 1.00 18.16  ? 2324 LEU A CD2   1 
ATOM   6291  N  N     . LEU A 1 2325 ? 151.098 184.338 148.510 1.00 15.49  ? 2325 LEU A N     1 
ATOM   6292  C  CA    . LEU A 1 2325 ? 151.123 183.782 149.859 1.00 14.06  ? 2325 LEU A CA    1 
ATOM   6293  C  C     . LEU A 1 2325 ? 150.052 182.702 149.936 1.00 19.68  ? 2325 LEU A C     1 
ATOM   6294  O  O     . LEU A 1 2325 ? 148.854 183.004 149.900 1.00 20.27  ? 2325 LEU A O     1 
ATOM   6295  C  CB    . LEU A 1 2325 ? 150.892 184.866 150.909 1.00 16.15  ? 2325 LEU A CB    1 
ATOM   6296  C  CG    . LEU A 1 2325 ? 150.735 184.382 152.352 1.00 15.63  ? 2325 LEU A CG    1 
ATOM   6297  C  CD1   . LEU A 1 2325 ? 152.064 183.895 152.904 1.00 16.86  ? 2325 LEU A CD1   1 
ATOM   6298  C  CD2   . LEU A 1 2325 ? 150.161 185.482 153.229 1.00 13.69  ? 2325 LEU A CD2   1 
ATOM   6299  N  N     . THR A 1 2326 ? 150.481 181.449 150.044 1.00 25.64  ? 2326 THR A N     1 
ATOM   6300  C  CA    . THR A 1 2326 ? 149.574 180.310 150.072 1.00 21.30  ? 2326 THR A CA    1 
ATOM   6301  C  C     . THR A 1 2326 ? 149.395 179.833 151.506 1.00 21.57  ? 2326 THR A C     1 
ATOM   6302  O  O     . THR A 1 2326 ? 150.377 179.532 152.194 1.00 24.42  ? 2326 THR A O     1 
ATOM   6303  C  CB    . THR A 1 2326 ? 150.099 179.169 149.200 1.00 19.07  ? 2326 THR A CB    1 
ATOM   6304  O  OG1   . THR A 1 2326 ? 151.141 178.474 149.895 1.00 27.25  ? 2326 THR A OG1   1 
ATOM   6305  C  CG2   . THR A 1 2326 ? 150.649 179.713 147.892 1.00 14.97  ? 2326 THR A CG2   1 
ATOM   6306  N  N     . LEU A 1 2327 ? 148.150 179.765 151.947 1.00 20.13  ? 2327 LEU A N     1 
ATOM   6307  C  CA    . LEU A 1 2327 ? 147.791 179.331 153.285 1.00 20.49  ? 2327 LEU A CA    1 
ATOM   6308  C  C     . LEU A 1 2327 ? 147.303 177.890 153.263 1.00 25.09  ? 2327 LEU A C     1 
ATOM   6309  O  O     . LEU A 1 2327 ? 146.867 177.387 152.224 1.00 26.79  ? 2327 LEU A O     1 
ATOM   6310  C  CB    . LEU A 1 2327 ? 146.706 180.244 153.863 1.00 20.20  ? 2327 LEU A CB    1 
ATOM   6311  C  CG    . LEU A 1 2327 ? 146.991 181.745 153.815 1.00 15.67  ? 2327 LEU A CG    1 
ATOM   6312  C  CD1   . LEU A 1 2327 ? 145.738 182.535 154.150 1.00 21.90  ? 2327 LEU A CD1   1 
ATOM   6313  C  CD2   . LEU A 1 2327 ? 148.128 182.108 154.755 1.00 14.86  ? 2327 LEU A CD2   1 
ATOM   6314  N  N     . PRO A 1 2328 ? 147.376 177.187 154.398 1.00 23.98  ? 2328 PRO A N     1 
ATOM   6315  C  CA    . PRO A 1 2328 ? 146.923 175.785 154.415 1.00 20.94  ? 2328 PRO A CA    1 
ATOM   6316  C  C     . PRO A 1 2328 ? 145.464 175.606 154.036 1.00 20.52  ? 2328 PRO A C     1 
ATOM   6317  O  O     . PRO A 1 2328 ? 145.097 174.542 153.522 1.00 22.65  ? 2328 PRO A O     1 
ATOM   6318  C  CB    . PRO A 1 2328 ? 147.188 175.346 155.864 1.00 23.31  ? 2328 PRO A CB    1 
ATOM   6319  C  CG    . PRO A 1 2328 ? 147.399 176.610 156.635 1.00 23.87  ? 2328 PRO A CG    1 
ATOM   6320  C  CD    . PRO A 1 2328 ? 147.999 177.576 155.673 1.00 22.79  ? 2328 PRO A CD    1 
ATOM   6321  N  N     . ASN A 1 2329 ? 144.619 176.611 154.260 1.00 24.12  ? 2329 ASN A N     1 
ATOM   6322  C  CA    . ASN A 1 2329 ? 143.201 176.512 153.938 1.00 27.28  ? 2329 ASN A CA    1 
ATOM   6323  C  C     . ASN A 1 2329 ? 142.912 176.701 152.451 1.00 30.72  ? 2329 ASN A C     1 
ATOM   6324  O  O     . ASN A 1 2329 ? 141.751 176.915 152.080 1.00 31.55  ? 2329 ASN A O     1 
ATOM   6325  C  CB    . ASN A 1 2329 ? 142.401 177.526 154.762 1.00 27.48  ? 2329 ASN A CB    1 
ATOM   6326  C  CG    . ASN A 1 2329 ? 142.543 178.942 154.243 1.00 30.05  ? 2329 ASN A CG    1 
ATOM   6327  O  OD1   . ASN A 1 2329 ? 143.642 179.389 153.920 1.00 27.78  ? 2329 ASN A OD1   1 
ATOM   6328  N  ND2   . ASN A 1 2329 ? 141.428 179.656 154.162 1.00 40.18  ? 2329 ASN A ND2   1 
ATOM   6329  N  N     . GLY A 1 2330 ? 143.930 176.625 151.596 1.00 30.22  ? 2330 GLY A N     1 
ATOM   6330  C  CA    . GLY A 1 2330 ? 143.750 176.773 150.169 1.00 30.01  ? 2330 GLY A CA    1 
ATOM   6331  C  C     . GLY A 1 2330 ? 143.669 178.199 149.674 1.00 32.57  ? 2330 GLY A C     1 
ATOM   6332  O  O     . GLY A 1 2330 ? 143.483 178.408 148.469 1.00 38.62  ? 2330 GLY A O     1 
ATOM   6333  N  N     . GLU A 1 2331 ? 143.801 179.183 150.557 1.00 28.87  ? 2331 GLU A N     1 
ATOM   6334  C  CA    . GLU A 1 2331 ? 143.713 180.580 150.161 1.00 28.88  ? 2331 GLU A CA    1 
ATOM   6335  C  C     . GLU A 1 2331 ? 145.064 181.079 149.667 1.00 27.99  ? 2331 GLU A C     1 
ATOM   6336  O  O     . GLU A 1 2331 ? 146.109 180.766 150.245 1.00 30.22  ? 2331 GLU A O     1 
ATOM   6337  C  CB    . GLU A 1 2331 ? 143.233 181.433 151.333 1.00 35.16  ? 2331 GLU A CB    1 
ATOM   6338  C  CG    . GLU A 1 2331 ? 142.476 182.678 150.923 1.00 45.40  ? 2331 GLU A CG    1 
ATOM   6339  C  CD    . GLU A 1 2331 ? 142.265 183.635 152.075 1.00 52.34  ? 2331 GLU A CD    1 
ATOM   6340  O  OE1   . GLU A 1 2331 ? 141.487 183.301 152.993 1.00 53.67  ? 2331 GLU A OE1   1 
ATOM   6341  O  OE2   . GLU A 1 2331 ? 142.878 184.723 152.063 1.00 55.23  ? 2331 GLU A OE2   1 
ATOM   6342  N  N     . ARG A 1 2332 ? 145.038 181.859 148.588 1.00 26.34  ? 2332 ARG A N     1 
ATOM   6343  C  CA    . ARG A 1 2332 ? 146.247 182.394 147.973 1.00 23.45  ? 2332 ARG A CA    1 
ATOM   6344  C  C     . ARG A 1 2332 ? 146.116 183.904 147.860 1.00 26.20  ? 2332 ARG A C     1 
ATOM   6345  O  O     . ARG A 1 2332 ? 145.164 184.401 147.250 1.00 33.99  ? 2332 ARG A O     1 
ATOM   6346  C  CB    . ARG A 1 2332 ? 146.486 181.768 146.597 1.00 23.79  ? 2332 ARG A CB    1 
ATOM   6347  C  CG    . ARG A 1 2332 ? 146.421 180.249 146.590 1.00 27.34  ? 2332 ARG A CG    1 
ATOM   6348  C  CD    . ARG A 1 2332 ? 145.785 179.722 145.314 1.00 26.32  ? 2332 ARG A CD    1 
ATOM   6349  N  NE    . ARG A 1 2332 ? 146.675 179.832 144.164 1.00 25.57  ? 2332 ARG A NE    1 
ATOM   6350  C  CZ    . ARG A 1 2332 ? 147.747 179.076 143.968 1.00 24.12  ? 2332 ARG A CZ    1 
ATOM   6351  N  NH1   . ARG A 1 2332 ? 148.096 178.132 144.827 1.00 18.02  ? 2332 ARG A NH1   1 
ATOM   6352  N  NH2   . ARG A 1 2332 ? 148.488 179.272 142.881 1.00 20.93  ? 2332 ARG A NH2   1 
ATOM   6353  N  N     . LEU A 1 2333 ? 147.070 184.629 148.437 1.00 20.74  ? 2333 LEU A N     1 
ATOM   6354  C  CA    . LEU A 1 2333 ? 147.076 186.086 148.425 1.00 18.08  ? 2333 LEU A CA    1 
ATOM   6355  C  C     . LEU A 1 2333 ? 148.223 186.570 147.549 1.00 18.88  ? 2333 LEU A C     1 
ATOM   6356  O  O     . LEU A 1 2333 ? 149.382 186.219 147.790 1.00 24.63  ? 2333 LEU A O     1 
ATOM   6357  C  CB    . LEU A 1 2333 ? 147.211 186.646 149.841 1.00 18.60  ? 2333 LEU A CB    1 
ATOM   6358  C  CG    . LEU A 1 2333 ? 146.091 186.314 150.828 1.00 18.82  ? 2333 LEU A CG    1 
ATOM   6359  C  CD1   . LEU A 1 2333 ? 146.484 185.140 151.705 1.00 19.39  ? 2333 LEU A CD1   1 
ATOM   6360  C  CD2   . LEU A 1 2333 ? 145.753 187.527 151.675 1.00 21.80  ? 2333 LEU A CD2   1 
ATOM   6361  N  N     . SER A 1 2334 ? 147.898 187.377 146.542 1.00 19.31  ? 2334 SER A N     1 
ATOM   6362  C  CA    . SER A 1 2334 ? 148.907 187.908 145.636 1.00 19.86  ? 2334 SER A CA    1 
ATOM   6363  C  C     . SER A 1 2334 ? 149.522 189.171 146.221 1.00 20.20  ? 2334 SER A C     1 
ATOM   6364  O  O     . SER A 1 2334 ? 148.807 190.059 146.695 1.00 29.07  ? 2334 SER A O     1 
ATOM   6365  C  CB    . SER A 1 2334 ? 148.292 188.205 144.269 1.00 24.06  ? 2334 SER A CB    1 
ATOM   6366  O  OG    . SER A 1 2334 ? 147.774 187.030 143.672 1.00 39.32  ? 2334 SER A OG    1 
ATOM   6367  N  N     . LEU A 1 2335 ? 150.844 189.253 146.185 1.00 18.03  ? 2335 LEU A N     1 
ATOM   6368  C  CA    . LEU A 1 2335 ? 151.534 190.436 146.681 1.00 15.57  ? 2335 LEU A CA    1 
ATOM   6369  C  C     . LEU A 1 2335 ? 151.275 191.611 145.747 1.00 19.64  ? 2335 LEU A C     1 
ATOM   6370  O  O     . LEU A 1 2335 ? 151.567 191.513 144.549 1.00 25.14  ? 2335 LEU A O     1 
ATOM   6371  C  CB    . LEU A 1 2335 ? 153.031 190.169 146.799 1.00 14.53  ? 2335 LEU A CB    1 
ATOM   6372  C  CG    . LEU A 1 2335 ? 153.838 191.158 147.643 1.00 15.74  ? 2335 LEU A CG    1 
ATOM   6373  C  CD1   . LEU A 1 2335 ? 153.642 190.887 149.124 1.00 15.96  ? 2335 LEU A CD1   1 
ATOM   6374  C  CD2   . LEU A 1 2335 ? 155.311 191.098 147.276 1.00 16.38  ? 2335 LEU A CD2   1 
ATOM   6375  N  N     . PRO A 1 2336 ? 150.725 192.724 146.237 1.00 16.43  ? 2336 PRO A N     1 
ATOM   6376  C  CA    . PRO A 1 2336 ? 150.489 193.866 145.358 1.00 14.80  ? 2336 PRO A CA    1 
ATOM   6377  C  C     . PRO A 1 2336 ? 151.801 194.461 144.882 1.00 17.11  ? 2336 PRO A C     1 
ATOM   6378  O  O     . PRO A 1 2336 ? 152.835 194.347 145.563 1.00 18.13  ? 2336 PRO A O     1 
ATOM   6379  C  CB    . PRO A 1 2336 ? 149.717 194.851 146.256 1.00 16.36  ? 2336 PRO A CB    1 
ATOM   6380  C  CG    . PRO A 1 2336 ? 149.160 194.011 147.358 1.00 17.73  ? 2336 PRO A CG    1 
ATOM   6381  C  CD    . PRO A 1 2336 ? 150.177 192.941 147.586 1.00 18.25  ? 2336 PRO A CD    1 
ATOM   6382  N  N     . PRO A 1 2337 ? 151.812 195.100 143.708 1.00 18.10  ? 2337 PRO A N     1 
ATOM   6383  C  CA    . PRO A 1 2337 ? 153.072 195.656 143.186 1.00 19.22  ? 2337 PRO A CA    1 
ATOM   6384  C  C     . PRO A 1 2337 ? 153.662 196.764 144.042 1.00 16.60  ? 2337 PRO A C     1 
ATOM   6385  O  O     . PRO A 1 2337 ? 154.859 197.047 143.912 1.00 17.70  ? 2337 PRO A O     1 
ATOM   6386  C  CB    . PRO A 1 2337 ? 152.679 196.176 141.796 1.00 18.14  ? 2337 PRO A CB    1 
ATOM   6387  C  CG    . PRO A 1 2337 ? 151.204 196.384 141.869 1.00 19.32  ? 2337 PRO A CG    1 
ATOM   6388  C  CD    . PRO A 1 2337 ? 150.682 195.327 142.792 1.00 17.61  ? 2337 PRO A CD    1 
ATOM   6389  N  N     . ASN A 1 2338 ? 152.873 197.400 144.904 1.00 17.03  ? 2338 ASN A N     1 
ATOM   6390  C  CA    . ASN A 1 2338 ? 153.360 198.481 145.750 1.00 19.80  ? 2338 ASN A CA    1 
ATOM   6391  C  C     . ASN A 1 2338 ? 153.892 197.998 147.093 1.00 18.03  ? 2338 ASN A C     1 
ATOM   6392  O  O     . ASN A 1 2338 ? 154.374 198.817 147.881 1.00 17.96  ? 2338 ASN A O     1 
ATOM   6393  C  CB    . ASN A 1 2338 ? 152.251 199.511 145.982 1.00 20.34  ? 2338 ASN A CB    1 
ATOM   6394  C  CG    . ASN A 1 2338 ? 151.135 198.977 146.857 1.00 21.43  ? 2338 ASN A CG    1 
ATOM   6395  O  OD1   . ASN A 1 2338 ? 150.532 197.950 146.554 1.00 24.42  ? 2338 ASN A OD1   1 
ATOM   6396  N  ND2   . ASN A 1 2338 ? 150.857 199.674 147.951 1.00 21.75  ? 2338 ASN A ND2   1 
ATOM   6397  N  N     . VAL A 1 2339 ? 153.822 196.699 147.371 1.00 16.70  ? 2339 VAL A N     1 
ATOM   6398  C  CA    . VAL A 1 2339 ? 154.228 196.142 148.657 1.00 14.09  ? 2339 VAL A CA    1 
ATOM   6399  C  C     . VAL A 1 2339 ? 155.621 195.548 148.522 1.00 16.32  ? 2339 VAL A C     1 
ATOM   6400  O  O     . VAL A 1 2339 ? 155.888 194.770 147.597 1.00 19.48  ? 2339 VAL A O     1 
ATOM   6401  C  CB    . VAL A 1 2339 ? 153.225 195.085 149.147 1.00 11.51  ? 2339 VAL A CB    1 
ATOM   6402  C  CG1   . VAL A 1 2339 ? 153.699 194.467 150.451 1.00 12.59  ? 2339 VAL A CG1   1 
ATOM   6403  C  CG2   . VAL A 1 2339 ? 151.854 195.706 149.319 1.00 13.86  ? 2339 VAL A CG2   1 
ATOM   6404  N  N     . ARG A 1 2340 ? 156.510 195.915 149.442 1.00 14.03  ? 2340 ARG A N     1 
ATOM   6405  C  CA    . ARG A 1 2340 ? 157.859 195.375 149.509 1.00 12.99  ? 2340 ARG A CA    1 
ATOM   6406  C  C     . ARG A 1 2340 ? 158.030 194.631 150.824 1.00 12.85  ? 2340 ARG A C     1 
ATOM   6407  O  O     . ARG A 1 2340 ? 157.727 195.174 151.891 1.00 18.22  ? 2340 ARG A O     1 
ATOM   6408  C  CB    . ARG A 1 2340 ? 158.908 196.483 149.391 1.00 14.42  ? 2340 ARG A CB    1 
ATOM   6409  C  CG    . ARG A 1 2340 ? 158.844 197.272 148.097 1.00 18.63  ? 2340 ARG A CG    1 
ATOM   6410  C  CD    . ARG A 1 2340 ? 159.453 196.488 146.949 1.00 14.94  ? 2340 ARG A CD    1 
ATOM   6411  N  NE    . ARG A 1 2340 ? 159.493 197.261 145.714 1.00 17.50  ? 2340 ARG A NE    1 
ATOM   6412  C  CZ    . ARG A 1 2340 ? 158.447 197.475 144.928 1.00 20.17  ? 2340 ARG A CZ    1 
ATOM   6413  N  NH1   . ARG A 1 2340 ? 157.254 196.981 145.214 1.00 20.38  ? 2340 ARG A NH1   1 
ATOM   6414  N  NH2   . ARG A 1 2340 ? 158.603 198.202 143.825 1.00 29.93  ? 2340 ARG A NH2   1 
ATOM   6415  N  N     . ILE A 1 2341 ? 158.512 193.395 150.747 1.00 11.12  ? 2341 ILE A N     1 
ATOM   6416  C  CA    . ILE A 1 2341 ? 158.784 192.590 151.933 1.00 10.84  ? 2341 ILE A CA    1 
ATOM   6417  C  C     . ILE A 1 2341 ? 160.258 192.761 152.276 1.00 12.65  ? 2341 ILE A C     1 
ATOM   6418  O  O     . ILE A 1 2341 ? 161.134 192.283 151.551 1.00 17.62  ? 2341 ILE A O     1 
ATOM   6419  C  CB    . ILE A 1 2341 ? 158.429 191.116 151.710 1.00 11.43  ? 2341 ILE A CB    1 
ATOM   6420  C  CG1   . ILE A 1 2341 ? 156.990 190.985 151.206 1.00 10.50  ? 2341 ILE A CG1   1 
ATOM   6421  C  CG2   . ILE A 1 2341 ? 158.619 190.325 152.992 1.00 9.88   ? 2341 ILE A CG2   1 
ATOM   6422  C  CD1   . ILE A 1 2341 ? 155.948 191.373 152.228 1.00 12.23  ? 2341 ILE A CD1   1 
ATOM   6423  N  N     . MET A 1 2342 ? 160.534 193.441 153.384 1.00 11.07  ? 2342 MET A N     1 
ATOM   6424  C  CA    . MET A 1 2342 ? 161.893 193.751 153.802 1.00 10.99  ? 2342 MET A CA    1 
ATOM   6425  C  C     . MET A 1 2342 ? 162.202 193.056 155.119 1.00 8.42   ? 2342 MET A C     1 
ATOM   6426  O  O     . MET A 1 2342 ? 161.332 192.934 155.987 1.00 11.81  ? 2342 MET A O     1 
ATOM   6427  C  CB    . MET A 1 2342 ? 162.092 195.262 153.952 1.00 12.28  ? 2342 MET A CB    1 
ATOM   6428  C  CG    . MET A 1 2342 ? 161.345 196.090 152.923 1.00 14.32  ? 2342 MET A CG    1 
ATOM   6429  S  SD    . MET A 1 2342 ? 161.682 197.852 153.077 1.00 36.76  ? 2342 MET A SD    1 
ATOM   6430  C  CE    . MET A 1 2342 ? 163.128 198.011 152.034 1.00 20.53  ? 2342 MET A CE    1 
ATOM   6431  N  N     . PHE A 1 2343 ? 163.440 192.594 155.259 1.00 7.89   ? 2343 PHE A N     1 
ATOM   6432  C  CA    . PHE A 1 2343 ? 163.926 191.998 156.495 1.00 8.27   ? 2343 PHE A CA    1 
ATOM   6433  C  C     . PHE A 1 2343 ? 165.109 192.812 156.995 1.00 12.12  ? 2343 PHE A C     1 
ATOM   6434  O  O     . PHE A 1 2343 ? 166.069 193.038 156.252 1.00 15.92  ? 2343 PHE A O     1 
ATOM   6435  C  CB    . PHE A 1 2343 ? 164.347 190.536 156.298 1.00 9.80   ? 2343 PHE A CB    1 
ATOM   6436  C  CG    . PHE A 1 2343 ? 163.330 189.690 155.576 1.00 11.20  ? 2343 PHE A CG    1 
ATOM   6437  C  CD1   . PHE A 1 2343 ? 163.223 189.731 154.196 1.00 12.86  ? 2343 PHE A CD1   1 
ATOM   6438  C  CD2   . PHE A 1 2343 ? 162.496 188.840 156.279 1.00 11.03  ? 2343 PHE A CD2   1 
ATOM   6439  C  CE1   . PHE A 1 2343 ? 162.296 188.953 153.534 1.00 10.76  ? 2343 PHE A CE1   1 
ATOM   6440  C  CE2   . PHE A 1 2343 ? 161.567 188.058 155.619 1.00 9.52   ? 2343 PHE A CE2   1 
ATOM   6441  C  CZ    . PHE A 1 2343 ? 161.467 188.116 154.247 1.00 10.24  ? 2343 PHE A CZ    1 
ATOM   6442  N  N     . GLU A 1 2344 ? 165.039 193.251 158.247 1.00 12.14  ? 2344 GLU A N     1 
ATOM   6443  C  CA    . GLU A 1 2344 ? 166.131 193.972 158.896 1.00 11.22  ? 2344 GLU A CA    1 
ATOM   6444  C  C     . GLU A 1 2344 ? 166.758 193.020 159.908 1.00 13.38  ? 2344 GLU A C     1 
ATOM   6445  O  O     . GLU A 1 2344 ? 166.222 192.822 161.002 1.00 17.45  ? 2344 GLU A O     1 
ATOM   6446  C  CB    . GLU A 1 2344 ? 165.633 195.251 159.558 1.00 10.86  ? 2344 GLU A CB    1 
ATOM   6447  C  CG    . GLU A 1 2344 ? 166.741 196.133 160.105 1.00 12.34  ? 2344 GLU A CG    1 
ATOM   6448  C  CD    . GLU A 1 2344 ? 166.209 197.308 160.897 1.00 17.42  ? 2344 GLU A CD    1 
ATOM   6449  O  OE1   . GLU A 1 2344 ? 165.333 198.028 160.375 1.00 21.71  ? 2344 GLU A OE1   1 
ATOM   6450  O  OE2   . GLU A 1 2344 ? 166.668 197.514 162.040 1.00 15.98  ? 2344 GLU A OE2   1 
ATOM   6451  N  N     . VAL A 1 2345 ? 167.893 192.434 159.541 1.00 10.64  ? 2345 VAL A N     1 
ATOM   6452  C  CA    . VAL A 1 2345 ? 168.525 191.388 160.332 1.00 12.08  ? 2345 VAL A CA    1 
ATOM   6453  C  C     . VAL A 1 2345 ? 169.975 191.762 160.592 1.00 16.35  ? 2345 VAL A C     1 
ATOM   6454  O  O     . VAL A 1 2345 ? 170.570 192.568 159.870 1.00 21.32  ? 2345 VAL A O     1 
ATOM   6455  C  CB    . VAL A 1 2345 ? 168.439 190.017 159.631 1.00 13.95  ? 2345 VAL A CB    1 
ATOM   6456  C  CG1   . VAL A 1 2345 ? 166.994 189.623 159.432 1.00 16.31  ? 2345 VAL A CG1   1 
ATOM   6457  C  CG2   . VAL A 1 2345 ? 169.166 190.058 158.300 1.00 15.78  ? 2345 VAL A CG2   1 
ATOM   6458  N  N     . GLN A 1 2346 ? 170.543 191.169 161.641 1.00 15.75  ? 2346 GLN A N     1 
ATOM   6459  C  CA    . GLN A 1 2346 ? 171.949 191.375 161.954 1.00 17.13  ? 2346 GLN A CA    1 
ATOM   6460  C  C     . GLN A 1 2346 ? 172.845 190.270 161.414 1.00 23.24  ? 2346 GLN A C     1 
ATOM   6461  O  O     . GLN A 1 2346 ? 174.057 190.479 161.291 1.00 27.40  ? 2346 GLN A O     1 
ATOM   6462  C  CB    . GLN A 1 2346 ? 172.147 191.501 163.467 1.00 18.11  ? 2346 GLN A CB    1 
ATOM   6463  C  CG    . GLN A 1 2346 ? 171.747 190.273 164.261 1.00 26.06  ? 2346 GLN A CG    1 
ATOM   6464  C  CD    . GLN A 1 2346 ? 172.280 190.305 165.680 1.00 39.18  ? 2346 GLN A CD    1 
ATOM   6465  O  OE1   . GLN A 1 2346 ? 173.153 191.108 166.009 1.00 32.95  ? 2346 GLN A OE1   1 
ATOM   6466  N  NE2   . GLN A 1 2346 ? 171.753 189.433 166.530 1.00 41.87  ? 2346 GLN A NE2   1 
ATOM   6467  N  N     . ASP A 1 2347 ? 172.281 189.110 161.088 1.00 22.91  ? 2347 ASP A N     1 
ATOM   6468  C  CA    . ASP A 1 2347 ? 173.050 188.016 160.513 1.00 21.50  ? 2347 ASP A CA    1 
ATOM   6469  C  C     . ASP A 1 2347 ? 172.094 187.061 159.815 1.00 26.96  ? 2347 ASP A C     1 
ATOM   6470  O  O     . ASP A 1 2347 ? 170.885 187.076 160.056 1.00 30.09  ? 2347 ASP A O     1 
ATOM   6471  C  CB    . ASP A 1 2347 ? 173.880 187.288 161.580 1.00 24.86  ? 2347 ASP A CB    1 
ATOM   6472  C  CG    . ASP A 1 2347 ? 173.022 186.648 162.659 1.00 37.49  ? 2347 ASP A CG    1 
ATOM   6473  O  OD1   . ASP A 1 2347 ? 172.305 185.669 162.365 1.00 44.97  ? 2347 ASP A OD1   1 
ATOM   6474  O  OD2   . ASP A 1 2347 ? 173.068 187.127 163.812 1.00 33.23  ? 2347 ASP A OD2   1 
ATOM   6475  N  N     . LEU A 1 2348 ? 172.659 186.229 158.940 1.00 27.93  ? 2348 LEU A N     1 
ATOM   6476  C  CA    . LEU A 1 2348 ? 171.904 185.196 158.241 1.00 26.09  ? 2348 LEU A CA    1 
ATOM   6477  C  C     . LEU A 1 2348 ? 172.561 183.833 158.417 1.00 31.85  ? 2348 LEU A C     1 
ATOM   6478  O  O     . LEU A 1 2348 ? 172.557 183.011 157.497 1.00 38.24  ? 2348 LEU A O     1 
ATOM   6479  C  CB    . LEU A 1 2348 ? 171.758 185.529 156.757 1.00 24.57  ? 2348 LEU A CB    1 
ATOM   6480  C  CG    . LEU A 1 2348 ? 170.820 186.677 156.381 1.00 21.02  ? 2348 LEU A CG    1 
ATOM   6481  C  CD1   . LEU A 1 2348 ? 170.959 187.005 154.904 1.00 20.83  ? 2348 LEU A CD1   1 
ATOM   6482  C  CD2   . LEU A 1 2348 ? 169.379 186.344 156.726 1.00 23.31  ? 2348 LEU A CD2   1 
ATOM   6483  N  N     . LYS A 1 2349 ? 173.131 183.580 159.596 1.00 30.64  ? 2349 LYS A N     1 
ATOM   6484  C  CA    . LYS A 1 2349 ? 173.842 182.332 159.844 1.00 29.48  ? 2349 LYS A CA    1 
ATOM   6485  C  C     . LYS A 1 2349 ? 172.914 181.129 159.934 1.00 31.68  ? 2349 LYS A C     1 
ATOM   6486  O  O     . LYS A 1 2349 ? 173.393 179.993 159.839 1.00 36.32  ? 2349 LYS A O     1 
ATOM   6487  C  CB    . LYS A 1 2349 ? 174.668 182.449 161.125 1.00 28.52  ? 2349 LYS A CB    1 
ATOM   6488  C  CG    . LYS A 1 2349 ? 173.843 182.484 162.399 1.00 29.41  ? 2349 LYS A CG    1 
ATOM   6489  C  CD    . LYS A 1 2349 ? 174.703 182.838 163.602 1.00 32.76  ? 2349 LYS A CD    1 
ATOM   6490  C  CE    . LYS A 1 2349 ? 175.889 181.898 163.732 1.00 37.48  ? 2349 LYS A CE    1 
ATOM   6491  N  NZ    . LYS A 1 2349 ? 175.465 180.495 163.991 1.00 37.26  ? 2349 LYS A NZ    1 
ATOM   6492  N  N     . TYR A 1 2350 ? 171.612 181.343 160.112 1.00 30.30  ? 2350 TYR A N     1 
ATOM   6493  C  CA    . TYR A 1 2350 ? 170.645 180.257 160.154 1.00 27.30  ? 2350 TYR A CA    1 
ATOM   6494  C  C     . TYR A 1 2350 ? 169.683 180.270 158.976 1.00 30.68  ? 2350 TYR A C     1 
ATOM   6495  O  O     . TYR A 1 2350 ? 168.882 179.338 158.841 1.00 32.39  ? 2350 TYR A O     1 
ATOM   6496  C  CB    . TYR A 1 2350 ? 169.854 180.300 161.468 1.00 25.50  ? 2350 TYR A CB    1 
ATOM   6497  C  CG    . TYR A 1 2350 ? 170.701 180.008 162.684 1.00 29.20  ? 2350 TYR A CG    1 
ATOM   6498  C  CD1   . TYR A 1 2350 ? 171.369 178.798 162.811 1.00 28.94  ? 2350 TYR A CD1   1 
ATOM   6499  C  CD2   . TYR A 1 2350 ? 170.846 180.945 163.696 1.00 29.37  ? 2350 TYR A CD2   1 
ATOM   6500  C  CE1   . TYR A 1 2350 ? 172.149 178.526 163.917 1.00 30.17  ? 2350 TYR A CE1   1 
ATOM   6501  C  CE2   . TYR A 1 2350 ? 171.626 180.681 164.806 1.00 25.77  ? 2350 TYR A CE2   1 
ATOM   6502  C  CZ    . TYR A 1 2350 ? 172.273 179.470 164.911 1.00 29.62  ? 2350 TYR A CZ    1 
ATOM   6503  O  OH    . TYR A 1 2350 ? 173.050 179.203 166.013 1.00 36.65  ? 2350 TYR A OH    1 
ATOM   6504  N  N     . ALA A 1 2351 ? 169.736 181.289 158.124 1.00 28.56  ? 2351 ALA A N     1 
ATOM   6505  C  CA    . ALA A 1 2351 ? 168.896 181.326 156.937 1.00 24.19  ? 2351 ALA A CA    1 
ATOM   6506  C  C     . ALA A 1 2351 ? 169.502 180.464 155.839 1.00 25.09  ? 2351 ALA A C     1 
ATOM   6507  O  O     . ALA A 1 2351 ? 170.711 180.503 155.594 1.00 24.45  ? 2351 ALA A O     1 
ATOM   6508  C  CB    . ALA A 1 2351 ? 168.724 182.762 156.444 1.00 20.41  ? 2351 ALA A CB    1 
ATOM   6509  N  N     . THR A 1 2352 ? 168.654 179.684 155.179 1.00 26.20  ? 2352 THR A N     1 
ATOM   6510  C  CA    . THR A 1 2352 ? 169.110 178.783 154.136 1.00 22.92  ? 2352 THR A CA    1 
ATOM   6511  C  C     . THR A 1 2352 ? 169.275 179.529 152.815 1.00 23.97  ? 2352 THR A C     1 
ATOM   6512  O  O     . THR A 1 2352 ? 168.827 180.665 152.647 1.00 23.40  ? 2352 THR A O     1 
ATOM   6513  C  CB    . THR A 1 2352 ? 168.136 177.620 153.971 1.00 24.23  ? 2352 THR A CB    1 
ATOM   6514  O  OG1   . THR A 1 2352 ? 166.831 178.127 153.664 1.00 28.03  ? 2352 THR A OG1   1 
ATOM   6515  C  CG2   . THR A 1 2352 ? 168.067 176.811 155.251 1.00 27.53  ? 2352 THR A CG2   1 
ATOM   6516  N  N     . LEU A 1 2353 ? 169.933 178.864 151.862 1.00 27.47  ? 2353 LEU A N     1 
ATOM   6517  C  CA    . LEU A 1 2353 ? 170.137 179.458 150.546 1.00 25.29  ? 2353 LEU A CA    1 
ATOM   6518  C  C     . LEU A 1 2353 ? 168.827 179.647 149.793 1.00 21.59  ? 2353 LEU A C     1 
ATOM   6519  O  O     . LEU A 1 2353 ? 168.790 180.402 148.816 1.00 22.13  ? 2353 LEU A O     1 
ATOM   6520  C  CB    . LEU A 1 2353 ? 171.095 178.594 149.724 1.00 28.38  ? 2353 LEU A CB    1 
ATOM   6521  C  CG    . LEU A 1 2353 ? 171.814 179.274 148.557 1.00 31.70  ? 2353 LEU A CG    1 
ATOM   6522  C  CD1   . LEU A 1 2353 ? 172.317 180.651 148.961 1.00 31.12  ? 2353 LEU A CD1   1 
ATOM   6523  C  CD2   . LEU A 1 2353 ? 172.959 178.408 148.058 1.00 33.10  ? 2353 LEU A CD2   1 
ATOM   6524  N  N     . ALA A 1 2354 ? 167.756 178.975 150.222 1.00 20.72  ? 2354 ALA A N     1 
ATOM   6525  C  CA    . ALA A 1 2354 ? 166.461 179.163 149.579 1.00 21.81  ? 2354 ALA A CA    1 
ATOM   6526  C  C     . ALA A 1 2354 ? 165.964 180.593 149.744 1.00 26.17  ? 2354 ALA A C     1 
ATOM   6527  O  O     . ALA A 1 2354 ? 165.465 181.196 148.788 1.00 31.40  ? 2354 ALA A O     1 
ATOM   6528  C  CB    . ALA A 1 2354 ? 165.444 178.173 150.145 1.00 24.48  ? 2354 ALA A CB    1 
ATOM   6529  N  N     . THR A 1 2355 ? 166.098 181.157 150.944 1.00 26.08  ? 2355 THR A N     1 
ATOM   6530  C  CA    . THR A 1 2355 ? 165.618 182.510 151.201 1.00 24.15  ? 2355 THR A CA    1 
ATOM   6531  C  C     . THR A 1 2355 ? 166.668 183.573 150.900 1.00 20.63  ? 2355 THR A C     1 
ATOM   6532  O  O     . THR A 1 2355 ? 166.316 184.726 150.630 1.00 25.84  ? 2355 THR A O     1 
ATOM   6533  C  CB    . THR A 1 2355 ? 165.143 182.640 152.652 1.00 28.45  ? 2355 THR A CB    1 
ATOM   6534  O  OG1   . THR A 1 2355 ? 164.542 183.927 152.844 1.00 32.76  ? 2355 THR A OG1   1 
ATOM   6535  C  CG2   . THR A 1 2355 ? 166.302 182.475 153.621 1.00 25.03  ? 2355 THR A CG2   1 
ATOM   6536  N  N     . VAL A 1 2356 ? 167.952 183.213 150.946 1.00 19.40  ? 2356 VAL A N     1 
ATOM   6537  C  CA    . VAL A 1 2356 ? 168.999 184.170 150.598 1.00 22.22  ? 2356 VAL A CA    1 
ATOM   6538  C  C     . VAL A 1 2356 ? 168.945 184.500 149.112 1.00 24.18  ? 2356 VAL A C     1 
ATOM   6539  O  O     . VAL A 1 2356 ? 169.128 185.655 148.708 1.00 26.16  ? 2356 VAL A O     1 
ATOM   6540  C  CB    . VAL A 1 2356 ? 170.380 183.628 151.013 1.00 21.60  ? 2356 VAL A CB    1 
ATOM   6541  C  CG1   . VAL A 1 2356 ? 171.482 184.570 150.559 1.00 18.82  ? 2356 VAL A CG1   1 
ATOM   6542  C  CG2   . VAL A 1 2356 ? 170.440 183.436 152.517 1.00 19.71  ? 2356 VAL A CG2   1 
ATOM   6543  N  N     . SER A 1 2357 ? 168.673 183.480 148.294 1.00 19.10  ? 2357 SER A N     1 
ATOM   6544  C  CA    . SER A 1 2357 ? 168.619 183.678 146.821 1.00 18.01  ? 2357 SER A CA    1 
ATOM   6545  C  C     . SER A 1 2357 ? 167.315 184.382 146.424 1.00 20.02  ? 2357 SER A C     1 
ATOM   6546  O  O     . SER A 1 2357 ? 167.216 184.813 145.255 1.00 21.77  ? 2357 SER A O     1 
ATOM   6547  C  CB    . SER A 1 2357 ? 168.757 182.361 146.106 1.00 19.44  ? 2357 SER A CB    1 
ATOM   6548  O  OG    . SER A 1 2357 ? 167.728 181.464 146.502 1.00 20.19  ? 2357 SER A OG    1 
ATOM   6549  N  N     . ARG A 1 2358 ? 166.362 184.502 147.352 1.00 19.95  ? 2358 ARG A N     1 
ATOM   6550  C  CA    . ARG A 1 2358 ? 165.039 185.092 147.017 1.00 18.66  ? 2358 ARG A CA    1 
ATOM   6551  C  C     . ARG A 1 2358 ? 164.962 186.561 147.462 1.00 20.69  ? 2358 ARG A C     1 
ATOM   6552  O  O     . ARG A 1 2358 ? 163.846 187.122 147.410 1.00 23.91  ? 2358 ARG A O     1 
ATOM   6553  C  CB    . ARG A 1 2358 ? 163.914 184.329 147.722 1.00 18.30  ? 2358 ARG A CB    1 
ATOM   6554  C  CG    . ARG A 1 2358 ? 163.520 182.968 147.169 1.00 19.28  ? 2358 ARG A CG    1 
ATOM   6555  C  CD    . ARG A 1 2358 ? 162.446 182.356 148.058 1.00 21.00  ? 2358 ARG A CD    1 
ATOM   6556  N  NE    . ARG A 1 2358 ? 161.787 181.183 147.475 1.00 22.09  ? 2358 ARG A NE    1 
ATOM   6557  C  CZ    . ARG A 1 2358 ? 162.385 180.044 147.151 1.00 26.17  ? 2358 ARG A CZ    1 
ATOM   6558  N  NH1   . ARG A 1 2358 ? 163.643 179.832 147.493 1.00 27.00  ? 2358 ARG A NH1   1 
ATOM   6559  N  NH2   . ARG A 1 2358 ? 161.718 179.116 146.490 1.00 29.07  ? 2358 ARG A NH2   1 
ATOM   6560  N  N     . CYS A 1 2359 ? 166.079 187.161 147.885 1.00 19.34  ? 2359 CYS A N     1 
ATOM   6561  C  CA    . CYS A 1 2359 ? 166.004 188.546 148.425 1.00 17.61  ? 2359 CYS A CA    1 
ATOM   6562  C  C     . CYS A 1 2359 ? 167.252 189.367 148.075 1.00 19.95  ? 2359 CYS A C     1 
ATOM   6563  O  O     . CYS A 1 2359 ? 168.371 188.866 148.319 1.00 21.47  ? 2359 CYS A O     1 
ATOM   6564  C  CB    . CYS A 1 2359 ? 165.872 188.527 149.943 1.00 17.31  ? 2359 CYS A CB    1 
ATOM   6565  S  SG    . CYS A 1 2359 ? 164.376 187.695 150.538 1.00 27.79  ? 2359 CYS A SG    1 
ATOM   6566  N  N     . GLY A 1 2360 ? 167.069 190.576 147.533 1.00 17.94  ? 2360 GLY A N     1 
ATOM   6567  C  CA    . GLY A 1 2360 ? 168.195 191.458 147.277 1.00 14.27  ? 2360 GLY A CA    1 
ATOM   6568  C  C     . GLY A 1 2360 ? 168.789 191.938 148.588 1.00 13.32  ? 2360 GLY A C     1 
ATOM   6569  O  O     . GLY A 1 2360 ? 168.065 192.357 149.498 1.00 15.71  ? 2360 GLY A O     1 
ATOM   6570  N  N     . MET A 1 2361 ? 170.113 191.880 148.693 1.00 15.21  ? 2361 MET A N     1 
ATOM   6571  C  CA    . MET A 1 2361 ? 170.808 192.128 149.946 1.00 12.96  ? 2361 MET A CA    1 
ATOM   6572  C  C     . MET A 1 2361 ? 171.522 193.471 149.913 1.00 12.74  ? 2361 MET A C     1 
ATOM   6573  O  O     . MET A 1 2361 ? 172.165 193.823 148.920 1.00 16.99  ? 2361 MET A O     1 
ATOM   6574  C  CB    . MET A 1 2361 ? 171.825 191.022 150.237 1.00 12.65  ? 2361 MET A CB    1 
ATOM   6575  C  CG    . MET A 1 2361 ? 171.257 189.623 150.176 1.00 15.97  ? 2361 MET A CG    1 
ATOM   6576  S  SD    . MET A 1 2361 ? 170.549 189.104 151.744 1.00 22.22  ? 2361 MET A SD    1 
ATOM   6577  C  CE    . MET A 1 2361 ? 169.601 187.689 151.208 1.00 22.36  ? 2361 MET A CE    1 
ATOM   6578  N  N     . VAL A 1 2362 ? 171.398 194.218 151.007 1.00 12.29  ? 2362 VAL A N     1 
ATOM   6579  C  CA    . VAL A 1 2362 ? 172.201 195.407 151.262 1.00 13.20  ? 2362 VAL A CA    1 
ATOM   6580  C  C     . VAL A 1 2362 ? 172.980 195.152 152.543 1.00 12.65  ? 2362 VAL A C     1 
ATOM   6581  O  O     . VAL A 1 2362 ? 172.383 194.878 153.592 1.00 13.82  ? 2362 VAL A O     1 
ATOM   6582  C  CB    . VAL A 1 2362 ? 171.339 196.673 151.382 1.00 10.29  ? 2362 VAL A CB    1 
ATOM   6583  C  CG1   . VAL A 1 2362 ? 172.212 197.915 151.316 1.00 9.15   ? 2362 VAL A CG1   1 
ATOM   6584  C  CG2   . VAL A 1 2362 ? 170.281 196.702 150.293 1.00 12.01  ? 2362 VAL A CG2   1 
ATOM   6585  N  N     . TRP A 1 2363 ? 174.304 195.237 152.462 1.00 10.91  ? 2363 TRP A N     1 
ATOM   6586  C  CA    . TRP A 1 2363 ? 175.175 194.922 153.587 1.00 11.51  ? 2363 TRP A CA    1 
ATOM   6587  C  C     . TRP A 1 2363 ? 175.570 196.210 154.298 1.00 14.90  ? 2363 TRP A C     1 
ATOM   6588  O  O     . TRP A 1 2363 ? 176.264 197.054 153.722 1.00 17.44  ? 2363 TRP A O     1 
ATOM   6589  C  CB    . TRP A 1 2363 ? 176.417 194.162 153.124 1.00 14.88  ? 2363 TRP A CB    1 
ATOM   6590  C  CG    . TRP A 1 2363 ? 177.482 194.077 154.171 1.00 18.66  ? 2363 TRP A CG    1 
ATOM   6591  C  CD1   . TRP A 1 2363 ? 178.645 194.788 154.217 1.00 18.56  ? 2363 TRP A CD1   1 
ATOM   6592  C  CD2   . TRP A 1 2363 ? 177.478 193.241 155.334 1.00 18.50  ? 2363 TRP A CD2   1 
ATOM   6593  N  NE1   . TRP A 1 2363 ? 179.368 194.443 155.332 1.00 19.74  ? 2363 TRP A NE1   1 
ATOM   6594  C  CE2   . TRP A 1 2363 ? 178.672 193.495 156.035 1.00 18.12  ? 2363 TRP A CE2   1 
ATOM   6595  C  CE3   . TRP A 1 2363 ? 176.581 192.301 155.850 1.00 16.79  ? 2363 TRP A CE3   1 
ATOM   6596  C  CZ2   . TRP A 1 2363 ? 178.993 192.843 157.223 1.00 17.48  ? 2363 TRP A CZ2   1 
ATOM   6597  C  CZ3   . TRP A 1 2363 ? 176.901 191.655 157.029 1.00 16.01  ? 2363 TRP A CZ3   1 
ATOM   6598  C  CH2   . TRP A 1 2363 ? 178.097 191.929 157.702 1.00 17.10  ? 2363 TRP A CH2   1 
ATOM   6599  N  N     . PHE A 1 2364 ? 175.134 196.351 155.547 1.00 13.28  ? 2364 PHE A N     1 
ATOM   6600  C  CA    . PHE A 1 2364 ? 175.443 197.520 156.369 1.00 11.69  ? 2364 PHE A CA    1 
ATOM   6601  C  C     . PHE A 1 2364 ? 176.566 197.139 157.328 1.00 16.44  ? 2364 PHE A C     1 
ATOM   6602  O  O     . PHE A 1 2364 ? 176.328 196.590 158.403 1.00 22.00  ? 2364 PHE A O     1 
ATOM   6603  C  CB    . PHE A 1 2364 ? 174.210 197.996 157.127 1.00 9.83   ? 2364 PHE A CB    1 
ATOM   6604  C  CG    . PHE A 1 2364 ? 173.209 198.724 156.278 1.00 7.69   ? 2364 PHE A CG    1 
ATOM   6605  C  CD1   . PHE A 1 2364 ? 172.313 198.028 155.488 1.00 9.74   ? 2364 PHE A CD1   1 
ATOM   6606  C  CD2   . PHE A 1 2364 ? 173.153 200.106 156.288 1.00 7.89   ? 2364 PHE A CD2   1 
ATOM   6607  C  CE1   . PHE A 1 2364 ? 171.386 198.698 154.714 1.00 10.57  ? 2364 PHE A CE1   1 
ATOM   6608  C  CE2   . PHE A 1 2364 ? 172.229 200.781 155.516 1.00 8.71   ? 2364 PHE A CE2   1 
ATOM   6609  C  CZ    . PHE A 1 2364 ? 171.344 200.076 154.728 1.00 10.95  ? 2364 PHE A CZ    1 
ATOM   6610  N  N     . SER A 1 2365 ? 177.801 197.434 156.937 1.00 17.13  ? 2365 SER A N     1 
ATOM   6611  C  CA    . SER A 1 2365 ? 178.918 197.225 157.843 1.00 19.15  ? 2365 SER A CA    1 
ATOM   6612  C  C     . SER A 1 2365 ? 178.882 198.258 158.966 1.00 25.88  ? 2365 SER A C     1 
ATOM   6613  O  O     . SER A 1 2365 ? 178.265 199.319 158.851 1.00 31.63  ? 2365 SER A O     1 
ATOM   6614  C  CB    . SER A 1 2365 ? 180.246 197.304 157.092 1.00 25.50  ? 2365 SER A CB    1 
ATOM   6615  O  OG    . SER A 1 2365 ? 180.335 198.499 156.336 1.00 36.13  ? 2365 SER A OG    1 
ATOM   6616  N  N     . GLU A 1 2366 ? 179.549 197.929 160.075 1.00 28.82  ? 2366 GLU A N     1 
ATOM   6617  C  CA    . GLU A 1 2366 ? 179.607 198.861 161.195 1.00 33.11  ? 2366 GLU A CA    1 
ATOM   6618  C  C     . GLU A 1 2366 ? 180.385 200.124 160.854 1.00 27.55  ? 2366 GLU A C     1 
ATOM   6619  O  O     . GLU A 1 2366 ? 180.149 201.167 161.473 1.00 26.19  ? 2366 GLU A O     1 
ATOM   6620  C  CB    . GLU A 1 2366 ? 180.220 198.184 162.420 1.00 43.97  ? 2366 GLU A CB    1 
ATOM   6621  C  CG    . GLU A 1 2366 ? 179.205 197.483 163.306 1.00 46.13  ? 2366 GLU A CG    1 
ATOM   6622  C  CD    . GLU A 1 2366 ? 179.666 197.372 164.745 1.00 58.75  ? 2366 GLU A CD    1 
ATOM   6623  O  OE1   . GLU A 1 2366 ? 178.832 197.561 165.655 1.00 52.80  ? 2366 GLU A OE1   1 
ATOM   6624  O  OE2   . GLU A 1 2366 ? 180.864 197.097 164.966 1.00 74.80  ? 2366 GLU A OE2   1 
ATOM   6625  N  N     . ASP A 1 2367 ? 181.303 200.055 159.888 1.00 28.78  ? 2367 ASP A N     1 
ATOM   6626  C  CA    . ASP A 1 2367 ? 182.023 201.246 159.455 1.00 29.23  ? 2367 ASP A CA    1 
ATOM   6627  C  C     . ASP A 1 2367 ? 181.128 202.220 158.701 1.00 29.94  ? 2367 ASP A C     1 
ATOM   6628  O  O     . ASP A 1 2367 ? 181.503 203.386 158.539 1.00 33.60  ? 2367 ASP A O     1 
ATOM   6629  C  CB    . ASP A 1 2367 ? 183.215 200.850 158.583 1.00 37.48  ? 2367 ASP A CB    1 
ATOM   6630  C  CG    . ASP A 1 2367 ? 184.016 199.708 159.177 1.00 44.40  ? 2367 ASP A CG    1 
ATOM   6631  O  OD1   . ASP A 1 2367 ? 184.793 199.954 160.123 1.00 40.78  ? 2367 ASP A OD1   1 
ATOM   6632  O  OD2   . ASP A 1 2367 ? 183.870 198.564 158.698 1.00 47.72  ? 2367 ASP A OD2   1 
ATOM   6633  N  N     . VAL A 1 2368 ? 179.964 201.768 158.231 1.00 33.16  ? 2368 VAL A N     1 
ATOM   6634  C  CA    . VAL A 1 2368 ? 179.025 202.666 157.563 1.00 26.65  ? 2368 VAL A CA    1 
ATOM   6635  C  C     . VAL A 1 2368 ? 178.541 203.737 158.532 1.00 23.67  ? 2368 VAL A C     1 
ATOM   6636  O  O     . VAL A 1 2368 ? 178.488 204.927 158.200 1.00 23.62  ? 2368 VAL A O     1 
ATOM   6637  C  CB    . VAL A 1 2368 ? 177.853 201.865 156.967 1.00 18.28  ? 2368 VAL A CB    1 
ATOM   6638  C  CG1   . VAL A 1 2368 ? 176.646 202.759 156.745 1.00 18.04  ? 2368 VAL A CG1   1 
ATOM   6639  C  CG2   . VAL A 1 2368 ? 178.273 201.197 155.668 1.00 20.61  ? 2368 VAL A CG2   1 
ATOM   6640  N  N     . LEU A 1 2369 ? 178.190 203.330 159.749 1.00 22.75  ? 2369 LEU A N     1 
ATOM   6641  C  CA    . LEU A 1 2369 ? 177.755 204.246 160.800 1.00 22.36  ? 2369 LEU A CA    1 
ATOM   6642  C  C     . LEU A 1 2369 ? 178.956 204.549 161.688 1.00 24.01  ? 2369 LEU A C     1 
ATOM   6643  O  O     . LEU A 1 2369 ? 179.254 203.804 162.625 1.00 30.47  ? 2369 LEU A O     1 
ATOM   6644  C  CB    . LEU A 1 2369 ? 176.608 203.645 161.604 1.00 18.86  ? 2369 LEU A CB    1 
ATOM   6645  C  CG    . LEU A 1 2369 ? 176.020 204.523 162.709 1.00 19.12  ? 2369 LEU A CG    1 
ATOM   6646  C  CD1   . LEU A 1 2369 ? 175.387 205.770 162.130 1.00 21.32  ? 2369 LEU A CD1   1 
ATOM   6647  C  CD2   . LEU A 1 2369 ? 175.014 203.746 163.533 1.00 18.48  ? 2369 LEU A CD2   1 
ATOM   6648  N  N     . SER A 1 2370 ? 179.649 205.643 161.390 1.00 19.29  ? 2370 SER A N     1 
ATOM   6649  C  CA    . SER A 1 2370 ? 180.793 206.041 162.192 1.00 18.60  ? 2370 SER A CA    1 
ATOM   6650  C  C     . SER A 1 2370 ? 180.333 206.643 163.517 1.00 22.15  ? 2370 SER A C     1 
ATOM   6651  O  O     . SER A 1 2370 ? 179.204 207.119 163.658 1.00 24.33  ? 2370 SER A O     1 
ATOM   6652  C  CB    . SER A 1 2370 ? 181.667 207.037 161.430 1.00 24.39  ? 2370 SER A CB    1 
ATOM   6653  O  OG    . SER A 1 2370 ? 180.908 208.141 160.974 1.00 29.98  ? 2370 SER A OG    1 
ATOM   6654  N  N     . THR A 1 2371 ? 181.235 206.609 164.500 1.00 27.07  ? 2371 THR A N     1 
ATOM   6655  C  CA    . THR A 1 2371 ? 180.916 207.131 165.825 1.00 22.17  ? 2371 THR A CA    1 
ATOM   6656  C  C     . THR A 1 2371 ? 180.702 208.641 165.794 1.00 23.48  ? 2371 THR A C     1 
ATOM   6657  O  O     . THR A 1 2371 ? 179.931 209.177 166.601 1.00 26.03  ? 2371 THR A O     1 
ATOM   6658  C  CB    . THR A 1 2371 ? 182.032 206.758 166.804 1.00 20.10  ? 2371 THR A CB    1 
ATOM   6659  O  OG1   . THR A 1 2371 ? 182.178 205.334 166.837 1.00 24.12  ? 2371 THR A OG1   1 
ATOM   6660  C  CG2   . THR A 1 2371 ? 181.704 207.236 168.203 1.00 20.44  ? 2371 THR A CG2   1 
ATOM   6661  N  N     . ASP A 1 2372 ? 181.360 209.336 164.862 1.00 24.14  ? 2372 ASP A N     1 
ATOM   6662  C  CA    . ASP A 1 2372 ? 181.174 210.778 164.737 1.00 25.64  ? 2372 ASP A CA    1 
ATOM   6663  C  C     . ASP A 1 2372 ? 179.727 211.119 164.409 1.00 25.86  ? 2372 ASP A C     1 
ATOM   6664  O  O     . ASP A 1 2372 ? 179.184 212.108 164.915 1.00 27.75  ? 2372 ASP A O     1 
ATOM   6665  C  CB    . ASP A 1 2372 ? 182.109 211.334 163.663 1.00 37.37  ? 2372 ASP A CB    1 
ATOM   6666  C  CG    . ASP A 1 2372 ? 183.566 211.277 164.072 1.00 64.60  ? 2372 ASP A CG    1 
ATOM   6667  O  OD1   . ASP A 1 2372 ? 183.848 211.349 165.287 1.00 71.46  ? 2372 ASP A OD1   1 
ATOM   6668  O  OD2   . ASP A 1 2372 ? 184.430 211.158 163.178 1.00 69.37  ? 2372 ASP A OD2   1 
ATOM   6669  N  N     . MET A 1 2373 ? 179.088 210.316 163.556 1.00 22.98  ? 2373 MET A N     1 
ATOM   6670  C  CA    . MET A 1 2373 ? 177.689 210.557 163.219 1.00 19.87  ? 2373 MET A CA    1 
ATOM   6671  C  C     . MET A 1 2373 ? 176.793 210.382 164.438 1.00 22.43  ? 2373 MET A C     1 
ATOM   6672  O  O     . MET A 1 2373 ? 175.845 211.150 164.636 1.00 30.64  ? 2373 MET A O     1 
ATOM   6673  C  CB    . MET A 1 2373 ? 177.261 209.622 162.089 1.00 19.28  ? 2373 MET A CB    1 
ATOM   6674  C  CG    . MET A 1 2373 ? 178.151 209.720 160.862 1.00 23.69  ? 2373 MET A CG    1 
ATOM   6675  S  SD    . MET A 1 2373 ? 177.965 208.345 159.715 1.00 32.56  ? 2373 MET A SD    1 
ATOM   6676  C  CE    . MET A 1 2373 ? 176.185 208.205 159.635 1.00 21.57  ? 2373 MET A CE    1 
ATOM   6677  N  N     . ILE A 1 2374 ? 177.081 209.380 165.271 1.00 21.71  ? 2374 ILE A N     1 
ATOM   6678  C  CA    . ILE A 1 2374 ? 176.306 209.178 166.493 1.00 18.68  ? 2374 ILE A CA    1 
ATOM   6679  C  C     . ILE A 1 2374 ? 176.488 210.357 167.440 1.00 20.13  ? 2374 ILE A C     1 
ATOM   6680  O  O     . ILE A 1 2374 ? 175.526 210.830 168.061 1.00 24.11  ? 2374 ILE A O     1 
ATOM   6681  C  CB    . ILE A 1 2374 ? 176.701 207.850 167.163 1.00 17.89  ? 2374 ILE A CB    1 
ATOM   6682  C  CG1   . ILE A 1 2374 ? 176.749 206.727 166.127 1.00 21.51  ? 2374 ILE A CG1   1 
ATOM   6683  C  CG2   . ILE A 1 2374 ? 175.722 207.506 168.272 1.00 19.39  ? 2374 ILE A CG2   1 
ATOM   6684  C  CD1   . ILE A 1 2374 ? 177.281 205.422 166.668 1.00 20.08  ? 2374 ILE A CD1   1 
ATOM   6685  N  N     . PHE A 1 2375 ? 177.725 210.843 167.575 1.00 21.39  ? 2375 PHE A N     1 
ATOM   6686  C  CA    . PHE A 1 2375 ? 177.972 212.009 168.419 1.00 18.20  ? 2375 PHE A CA    1 
ATOM   6687  C  C     . PHE A 1 2375 ? 177.220 213.230 167.906 1.00 19.72  ? 2375 PHE A C     1 
ATOM   6688  O  O     . PHE A 1 2375 ? 176.634 213.984 168.693 1.00 23.58  ? 2375 PHE A O     1 
ATOM   6689  C  CB    . PHE A 1 2375 ? 179.470 212.302 168.491 1.00 20.41  ? 2375 PHE A CB    1 
ATOM   6690  C  CG    . PHE A 1 2375 ? 180.246 211.309 169.304 1.00 19.92  ? 2375 PHE A CG    1 
ATOM   6691  C  CD1   . PHE A 1 2375 ? 179.601 210.455 170.181 1.00 17.55  ? 2375 PHE A CD1   1 
ATOM   6692  C  CD2   . PHE A 1 2375 ? 181.623 211.236 169.196 1.00 26.59  ? 2375 PHE A CD2   1 
ATOM   6693  C  CE1   . PHE A 1 2375 ? 180.314 209.545 170.931 1.00 17.82  ? 2375 PHE A CE1   1 
ATOM   6694  C  CE2   . PHE A 1 2375 ? 182.342 210.327 169.944 1.00 29.59  ? 2375 PHE A CE2   1 
ATOM   6695  C  CZ    . PHE A 1 2375 ? 181.687 209.482 170.813 1.00 23.89  ? 2375 PHE A CZ    1 
ATOM   6696  N  N     . ASN A 1 2376 ? 177.234 213.445 166.588 1.00 19.14  ? 2376 ASN A N     1 
ATOM   6697  C  CA    . ASN A 1 2376 ? 176.511 214.574 166.013 1.00 19.57  ? 2376 ASN A CA    1 
ATOM   6698  C  C     . ASN A 1 2376 ? 175.014 214.449 166.252 1.00 22.47  ? 2376 ASN A C     1 
ATOM   6699  O  O     . ASN A 1 2376 ? 174.345 215.438 166.572 1.00 25.45  ? 2376 ASN A O     1 
ATOM   6700  C  CB    . ASN A 1 2376 ? 176.805 214.682 164.517 1.00 21.77  ? 2376 ASN A CB    1 
ATOM   6701  C  CG    . ASN A 1 2376 ? 178.272 214.917 164.227 1.00 35.01  ? 2376 ASN A CG    1 
ATOM   6702  O  OD1   . ASN A 1 2376 ? 179.078 215.087 165.142 1.00 43.21  ? 2376 ASN A OD1   1 
ATOM   6703  N  ND2   . ASN A 1 2376 ? 178.629 214.925 162.948 1.00 31.84  ? 2376 ASN A ND2   1 
ATOM   6704  N  N     . ASN A 1 2377 ? 174.468 213.240 166.098 1.00 20.17  ? 2377 ASN A N     1 
ATOM   6705  C  CA    . ASN A 1 2377 ? 173.047 213.029 166.354 1.00 20.49  ? 2377 ASN A CA    1 
ATOM   6706  C  C     . ASN A 1 2377 ? 172.698 213.332 167.805 1.00 24.55  ? 2377 ASN A C     1 
ATOM   6707  O  O     . ASN A 1 2377 ? 171.702 214.012 168.084 1.00 28.54  ? 2377 ASN A O     1 
ATOM   6708  C  CB    . ASN A 1 2377 ? 172.660 211.594 165.996 1.00 18.51  ? 2377 ASN A CB    1 
ATOM   6709  C  CG    . ASN A 1 2377 ? 171.234 211.260 166.382 1.00 22.49  ? 2377 ASN A CG    1 
ATOM   6710  O  OD1   . ASN A 1 2377 ? 170.994 210.384 167.212 1.00 27.28  ? 2377 ASN A OD1   1 
ATOM   6711  N  ND2   . ASN A 1 2377 ? 170.279 211.955 165.778 1.00 23.47  ? 2377 ASN A ND2   1 
ATOM   6712  N  N     . PHE A 1 2378 ? 173.513 212.844 168.744 1.00 23.02  ? 2378 PHE A N     1 
ATOM   6713  C  CA    . PHE A 1 2378 ? 173.249 213.100 170.157 1.00 19.40  ? 2378 PHE A CA    1 
ATOM   6714  C  C     . PHE A 1 2378 ? 173.319 214.588 170.472 1.00 20.46  ? 2378 PHE A C     1 
ATOM   6715  O  O     . PHE A 1 2378 ? 172.455 215.124 171.178 1.00 23.69  ? 2378 PHE A O     1 
ATOM   6716  C  CB    . PHE A 1 2378 ? 174.237 212.325 171.027 1.00 17.63  ? 2378 PHE A CB    1 
ATOM   6717  C  CG    . PHE A 1 2378 ? 174.341 212.845 172.434 1.00 20.67  ? 2378 PHE A CG    1 
ATOM   6718  C  CD1   . PHE A 1 2378 ? 173.242 212.830 173.278 1.00 18.61  ? 2378 PHE A CD1   1 
ATOM   6719  C  CD2   . PHE A 1 2378 ? 175.537 213.356 172.911 1.00 18.73  ? 2378 PHE A CD2   1 
ATOM   6720  C  CE1   . PHE A 1 2378 ? 173.336 213.308 174.569 1.00 17.37  ? 2378 PHE A CE1   1 
ATOM   6721  C  CE2   . PHE A 1 2378 ? 175.636 213.835 174.201 1.00 17.24  ? 2378 PHE A CE2   1 
ATOM   6722  C  CZ    . PHE A 1 2378 ? 174.534 213.812 175.031 1.00 19.03  ? 2378 PHE A CZ    1 
ATOM   6723  N  N     . LEU A 1 2379 ? 174.341 215.276 169.955 1.00 19.66  ? 2379 LEU A N     1 
ATOM   6724  C  CA    . LEU A 1 2379 ? 174.485 216.700 170.236 1.00 20.76  ? 2379 LEU A CA    1 
ATOM   6725  C  C     . LEU A 1 2379 ? 173.346 217.505 169.622 1.00 26.12  ? 2379 LEU A C     1 
ATOM   6726  O  O     . LEU A 1 2379 ? 172.842 218.446 170.245 1.00 34.86  ? 2379 LEU A O     1 
ATOM   6727  C  CB    . LEU A 1 2379 ? 175.839 217.199 169.733 1.00 21.89  ? 2379 LEU A CB    1 
ATOM   6728  C  CG    . LEU A 1 2379 ? 177.050 216.695 170.520 1.00 18.28  ? 2379 LEU A CG    1 
ATOM   6729  C  CD1   . LEU A 1 2379 ? 178.348 217.136 169.864 1.00 23.58  ? 2379 LEU A CD1   1 
ATOM   6730  C  CD2   . LEU A 1 2379 ? 176.988 217.166 171.964 1.00 19.28  ? 2379 LEU A CD2   1 
ATOM   6731  N  N     . ALA A 1 2380 ? 172.923 217.152 168.405 1.00 21.84  ? 2380 ALA A N     1 
ATOM   6732  C  CA    . ALA A 1 2380 ? 171.804 217.850 167.781 1.00 24.07  ? 2380 ALA A CA    1 
ATOM   6733  C  C     . ALA A 1 2380 ? 170.513 217.632 168.558 1.00 25.63  ? 2380 ALA A C     1 
ATOM   6734  O  O     . ALA A 1 2380 ? 169.739 218.575 168.770 1.00 32.11  ? 2380 ALA A O     1 
ATOM   6735  C  CB    . ALA A 1 2380 ? 171.645 217.393 166.332 1.00 22.90  ? 2380 ALA A CB    1 
ATOM   6736  N  N     . ARG A 1 2381 ? 170.262 216.394 168.995 1.00 22.59  ? 2381 ARG A N     1 
ATOM   6737  C  CA    . ARG A 1 2381 ? 169.063 216.124 169.782 1.00 23.91  ? 2381 ARG A CA    1 
ATOM   6738  C  C     . ARG A 1 2381 ? 169.089 216.885 171.101 1.00 28.57  ? 2381 ARG A C     1 
ATOM   6739  O  O     . ARG A 1 2381 ? 168.058 217.400 171.549 1.00 36.69  ? 2381 ARG A O     1 
ATOM   6740  C  CB    . ARG A 1 2381 ? 168.919 214.623 170.028 1.00 23.60  ? 2381 ARG A CB    1 
ATOM   6741  C  CG    . ARG A 1 2381 ? 168.582 213.821 168.784 1.00 24.85  ? 2381 ARG A CG    1 
ATOM   6742  C  CD    . ARG A 1 2381 ? 168.449 212.342 169.101 1.00 24.80  ? 2381 ARG A CD    1 
ATOM   6743  N  NE    . ARG A 1 2381 ? 167.346 212.080 170.018 1.00 27.29  ? 2381 ARG A NE    1 
ATOM   6744  C  CZ    . ARG A 1 2381 ? 166.082 211.932 169.645 1.00 26.74  ? 2381 ARG A CZ    1 
ATOM   6745  N  NH1   . ARG A 1 2381 ? 165.722 212.013 168.375 1.00 28.30  ? 2381 ARG A NH1   1 
ATOM   6746  N  NH2   . ARG A 1 2381 ? 165.156 211.699 170.571 1.00 24.91  ? 2381 ARG A NH2   1 
ATOM   6747  N  N     . LEU A 1 2382 ? 170.258 216.961 171.742 1.00 23.97  ? 2382 LEU A N     1 
ATOM   6748  C  CA    . LEU A 1 2382 ? 170.367 217.724 172.981 1.00 24.52  ? 2382 LEU A CA    1 
ATOM   6749  C  C     . LEU A 1 2382 ? 170.128 219.210 172.742 1.00 31.36  ? 2382 LEU A C     1 
ATOM   6750  O  O     . LEU A 1 2382 ? 169.441 219.869 173.531 1.00 41.55  ? 2382 LEU A O     1 
ATOM   6751  C  CB    . LEU A 1 2382 ? 171.735 217.497 173.621 1.00 23.73  ? 2382 LEU A CB    1 
ATOM   6752  C  CG    . LEU A 1 2382 ? 171.870 217.969 175.069 1.00 27.85  ? 2382 LEU A CG    1 
ATOM   6753  C  CD1   . LEU A 1 2382 ? 171.030 217.106 175.995 1.00 31.71  ? 2382 LEU A CD1   1 
ATOM   6754  C  CD2   . LEU A 1 2382 ? 173.323 217.956 175.497 1.00 29.18  ? 2382 LEU A CD2   1 
ATOM   6755  N  N     . ARG A 1 2383 ? 170.686 219.757 171.659 1.00 28.71  ? 2383 ARG A N     1 
ATOM   6756  C  CA    . ARG A 1 2383 ? 170.526 221.178 171.375 1.00 26.48  ? 2383 ARG A CA    1 
ATOM   6757  C  C     . ARG A 1 2383 ? 169.126 221.525 170.890 1.00 31.73  ? 2383 ARG A C     1 
ATOM   6758  O  O     . ARG A 1 2383 ? 168.748 222.700 170.929 1.00 39.19  ? 2383 ARG A O     1 
ATOM   6759  C  CB    . ARG A 1 2383 ? 171.552 221.630 170.334 1.00 23.70  ? 2383 ARG A CB    1 
ATOM   6760  C  CG    . ARG A 1 2383 ? 172.981 221.680 170.841 1.00 27.23  ? 2383 ARG A CG    1 
ATOM   6761  C  CD    . ARG A 1 2383 ? 173.944 222.054 169.726 1.00 33.43  ? 2383 ARG A CD    1 
ATOM   6762  N  NE    . ARG A 1 2383 ? 175.274 222.374 170.232 1.00 41.69  ? 2383 ARG A NE    1 
ATOM   6763  C  CZ    . ARG A 1 2383 ? 176.393 221.801 169.812 1.00 44.90  ? 2383 ARG A CZ    1 
ATOM   6764  N  NH1   . ARG A 1 2383 ? 176.382 220.867 168.876 1.00 38.31  ? 2383 ARG A NH1   1 
ATOM   6765  N  NH2   . ARG A 1 2383 ? 177.553 222.176 170.344 1.00 38.83  ? 2383 ARG A NH2   1 
ATOM   6766  N  N     . SER A 1 2384 ? 168.349 220.542 170.434 1.00 33.61  ? 2384 SER A N     1 
ATOM   6767  C  CA    . SER A 1 2384 ? 167.022 220.803 169.894 1.00 35.07  ? 2384 SER A CA    1 
ATOM   6768  C  C     . SER A 1 2384 ? 165.908 220.297 170.803 1.00 36.16  ? 2384 SER A C     1 
ATOM   6769  O  O     . SER A 1 2384 ? 165.029 221.071 171.191 1.00 48.45  ? 2384 SER A O     1 
ATOM   6770  C  CB    . SER A 1 2384 ? 166.895 220.177 168.499 1.00 36.78  ? 2384 SER A CB    1 
ATOM   6771  O  OG    . SER A 1 2384 ? 165.772 220.697 167.809 1.00 45.94  ? 2384 SER A OG    1 
ATOM   6772  N  N     . ILE A 1 2385 ? 165.920 219.016 171.156 1.00 36.57  ? 2385 ILE A N     1 
ATOM   6773  C  CA    . ILE A 1 2385 ? 164.822 218.413 171.909 1.00 41.42  ? 2385 ILE A CA    1 
ATOM   6774  C  C     . ILE A 1 2385 ? 164.941 218.767 173.387 1.00 45.53  ? 2385 ILE A C     1 
ATOM   6775  O  O     . ILE A 1 2385 ? 165.975 218.488 174.010 1.00 46.74  ? 2385 ILE A O     1 
ATOM   6776  C  CB    . ILE A 1 2385 ? 164.787 216.890 171.713 1.00 38.97  ? 2385 ILE A CB    1 
ATOM   6777  C  CG1   . ILE A 1 2385 ? 164.660 216.549 170.228 1.00 36.17  ? 2385 ILE A CG1   1 
ATOM   6778  C  CG2   . ILE A 1 2385 ? 163.641 216.280 172.502 1.00 37.64  ? 2385 ILE A CG2   1 
ATOM   6779  C  CD1   . ILE A 1 2385 ? 164.573 215.068 169.949 1.00 28.83  ? 2385 ILE A CD1   1 
ATOM   6780  N  N     . PRO A 1 2386 ? 163.920 219.380 173.985 1.00 47.46  ? 2386 PRO A N     1 
ATOM   6781  C  CA    . PRO A 1 2386 ? 163.966 219.647 175.428 1.00 50.47  ? 2386 PRO A CA    1 
ATOM   6782  C  C     . PRO A 1 2386 ? 163.839 218.360 176.228 1.00 53.09  ? 2386 PRO A C     1 
ATOM   6783  O  O     . PRO A 1 2386 ? 163.089 217.451 175.864 1.00 59.02  ? 2386 PRO A O     1 
ATOM   6784  C  CB    . PRO A 1 2386 ? 162.766 220.575 175.663 1.00 51.53  ? 2386 PRO A CB    1 
ATOM   6785  C  CG    . PRO A 1 2386 ? 162.285 220.980 174.293 1.00 51.67  ? 2386 PRO A CG    1 
ATOM   6786  C  CD    . PRO A 1 2386 ? 162.680 219.877 173.372 1.00 45.97  ? 2386 PRO A CD    1 
ATOM   6787  N  N     . LEU A 1 2387 ? 164.583 218.292 177.334 1.00 48.62  ? 2387 LEU A N     1 
ATOM   6788  C  CA    . LEU A 1 2387 ? 164.572 217.088 178.158 1.00 48.08  ? 2387 LEU A CA    1 
ATOM   6789  C  C     . LEU A 1 2387 ? 163.310 216.989 179.006 1.00 60.96  ? 2387 LEU A C     1 
ATOM   6790  O  O     . LEU A 1 2387 ? 162.802 215.886 179.237 1.00 66.81  ? 2387 LEU A O     1 
ATOM   6791  C  CB    . LEU A 1 2387 ? 165.813 217.049 179.051 1.00 47.26  ? 2387 LEU A CB    1 
ATOM   6792  C  CG    . LEU A 1 2387 ? 167.086 216.499 178.409 1.00 45.39  ? 2387 LEU A CG    1 
ATOM   6793  C  CD1   . LEU A 1 2387 ? 168.221 216.472 179.416 1.00 43.16  ? 2387 LEU A CD1   1 
ATOM   6794  C  CD2   . LEU A 1 2387 ? 166.841 215.113 177.836 1.00 42.62  ? 2387 LEU A CD2   1 
ATOM   6795  N  N     . ASP A 1 2388 ? 162.795 218.125 179.486 1.00 65.12  ? 2388 ASP A N     1 
ATOM   6796  C  CA    . ASP A 1 2388 ? 161.619 218.090 180.351 1.00 67.30  ? 2388 ASP A CA    1 
ATOM   6797  C  C     . ASP A 1 2388 ? 160.385 217.599 179.600 1.00 66.10  ? 2388 ASP A C     1 
ATOM   6798  O  O     . ASP A 1 2388 ? 159.664 216.720 180.087 1.00 66.68  ? 2388 ASP A O     1 
ATOM   6799  C  CB    . ASP A 1 2388 ? 161.382 219.470 180.971 1.00 65.81  ? 2388 ASP A CB    1 
ATOM   6800  C  CG    . ASP A 1 2388 ? 161.152 220.557 179.933 1.00 69.94  ? 2388 ASP A CG    1 
ATOM   6801  O  OD1   . ASP A 1 2388 ? 161.224 220.264 178.721 1.00 73.69  ? 2388 ASP A OD1   1 
ATOM   6802  O  OD2   . ASP A 1 2388 ? 160.896 221.712 180.333 1.00 74.67  ? 2388 ASP A OD2   1 
ATOM   6803  N  N     . GLU A 1 2389 ? 160.133 218.143 178.413 1.00 62.52  ? 2389 GLU A N     1 
ATOM   6804  C  CA    . GLU A 1 2389 ? 159.020 217.702 177.577 1.00 61.99  ? 2389 GLU A CA    1 
ATOM   6805  C  C     . GLU A 1 2389 ? 159.406 217.745 176.103 1.00 62.79  ? 2389 GLU A C     1 
ATOM   6806  O  O     . GLU A 1 2389 ? 159.825 218.783 175.590 0.00 61.68  ? 2389 GLU A O     1 
ATOM   6807  C  CB    . GLU A 1 2389 ? 157.776 218.565 177.816 1.00 68.27  ? 2389 GLU A CB    1 
ATOM   6808  C  CG    . GLU A 1 2389 ? 157.146 218.412 179.193 1.00 77.38  ? 2389 GLU A CG    1 
ATOM   6809  C  CD    . GLU A 1 2389 ? 156.545 217.036 179.408 1.00 78.11  ? 2389 GLU A CD    1 
ATOM   6810  O  OE1   . GLU A 1 2389 ? 156.067 216.434 178.423 1.00 77.87  ? 2389 GLU A OE1   1 
ATOM   6811  O  OE2   . GLU A 1 2389 ? 156.550 216.555 180.560 1.00 73.54  ? 2389 GLU A OE2   1 
ATOM   6812  N  N     . SER A 1 2410 ? 163.091 228.269 176.610 1.00 68.61  ? 2410 SER A N     1 
ATOM   6813  C  CA    . SER A 1 2410 ? 163.022 227.275 177.675 1.00 68.70  ? 2410 SER A CA    1 
ATOM   6814  C  C     . SER A 1 2410 ? 164.339 227.202 178.440 1.00 67.06  ? 2410 SER A C     1 
ATOM   6815  O  O     . SER A 1 2410 ? 165.395 226.990 177.842 1.00 65.19  ? 2410 SER A O     1 
ATOM   6816  C  CB    . SER A 1 2410 ? 162.669 225.901 177.103 1.00 62.47  ? 2410 SER A CB    1 
ATOM   6817  O  OG    . SER A 1 2410 ? 162.654 224.914 178.120 1.00 65.74  ? 2410 SER A OG    1 
ATOM   6818  N  N     . PRO A 1 2411 ? 164.278 227.394 179.761 1.00 62.58  ? 2411 PRO A N     1 
ATOM   6819  C  CA    . PRO A 1 2411 ? 165.509 227.298 180.565 1.00 61.58  ? 2411 PRO A CA    1 
ATOM   6820  C  C     . PRO A 1 2411 ? 166.178 225.938 180.476 1.00 59.25  ? 2411 PRO A C     1 
ATOM   6821  O  O     . PRO A 1 2411 ? 167.413 225.857 180.444 1.00 60.45  ? 2411 PRO A O     1 
ATOM   6822  C  CB    . PRO A 1 2411 ? 165.020 227.605 181.988 1.00 62.56  ? 2411 PRO A CB    1 
ATOM   6823  C  CG    . PRO A 1 2411 ? 163.562 227.273 181.969 1.00 63.42  ? 2411 PRO A CG    1 
ATOM   6824  C  CD    . PRO A 1 2411 ? 163.085 227.623 180.593 1.00 58.58  ? 2411 PRO A CD    1 
ATOM   6825  N  N     . MET A 1 2412 ? 165.390 224.861 180.427 1.00 58.89  ? 2412 MET A N     1 
ATOM   6826  C  CA    . MET A 1 2412 ? 165.968 223.530 180.276 1.00 54.03  ? 2412 MET A CA    1 
ATOM   6827  C  C     . MET A 1 2412 ? 166.664 223.387 178.929 1.00 52.89  ? 2412 MET A C     1 
ATOM   6828  O  O     . MET A 1 2412 ? 167.741 222.787 178.838 1.00 53.75  ? 2412 MET A O     1 
ATOM   6829  C  CB    . MET A 1 2412 ? 164.883 222.466 180.442 1.00 55.05  ? 2412 MET A CB    1 
ATOM   6830  C  CG    . MET A 1 2412 ? 165.334 221.057 180.100 1.00 59.20  ? 2412 MET A CG    1 
ATOM   6831  S  SD    . MET A 1 2412 ? 166.381 220.330 181.375 1.00 66.83  ? 2412 MET A SD    1 
ATOM   6832  C  CE    . MET A 1 2412 ? 165.147 219.603 182.448 1.00 56.57  ? 2412 MET A CE    1 
ATOM   6833  N  N     . LEU A 1 2413 ? 166.064 223.937 177.870 1.00 53.06  ? 2413 LEU A N     1 
ATOM   6834  C  CA    . LEU A 1 2413 ? 166.699 223.895 176.558 1.00 51.98  ? 2413 LEU A CA    1 
ATOM   6835  C  C     . LEU A 1 2413 ? 167.986 224.712 176.543 1.00 50.99  ? 2413 LEU A C     1 
ATOM   6836  O  O     . LEU A 1 2413 ? 168.972 224.321 175.907 1.00 52.50  ? 2413 LEU A O     1 
ATOM   6837  C  CB    . LEU A 1 2413 ? 165.725 224.392 175.490 1.00 57.63  ? 2413 LEU A CB    1 
ATOM   6838  C  CG    . LEU A 1 2413 ? 166.203 224.352 174.039 1.00 57.40  ? 2413 LEU A CG    1 
ATOM   6839  C  CD1   . LEU A 1 2413 ? 166.479 222.922 173.612 1.00 47.40  ? 2413 LEU A CD1   1 
ATOM   6840  C  CD2   . LEU A 1 2413 ? 165.172 224.993 173.125 1.00 60.06  ? 2413 LEU A CD2   1 
ATOM   6841  N  N     . GLN A 1 2414 ? 167.996 225.853 177.239 1.00 52.20  ? 2414 GLN A N     1 
ATOM   6842  C  CA    . GLN A 1 2414 ? 169.218 226.644 177.348 1.00 53.98  ? 2414 GLN A CA    1 
ATOM   6843  C  C     . GLN A 1 2414 ? 170.310 225.873 178.080 1.00 52.55  ? 2414 GLN A C     1 
ATOM   6844  O  O     . GLN A 1 2414 ? 171.481 225.902 177.677 1.00 52.23  ? 2414 GLN A O     1 
ATOM   6845  C  CB    . GLN A 1 2414 ? 168.924 227.964 178.060 1.00 52.01  ? 2414 GLN A CB    1 
ATOM   6846  C  CG    . GLN A 1 2414 ? 170.097 228.931 178.096 1.00 56.53  ? 2414 GLN A CG    1 
ATOM   6847  C  CD    . GLN A 1 2414 ? 170.668 229.209 176.721 1.00 66.13  ? 2414 GLN A CD    1 
ATOM   6848  O  OE1   . GLN A 1 2414 ? 169.931 229.473 175.771 1.00 77.21  ? 2414 GLN A OE1   1 
ATOM   6849  N  NE2   . GLN A 1 2414 ? 171.990 229.153 176.607 1.00 61.14  ? 2414 GLN A NE2   1 
ATOM   6850  N  N     . ILE A 1 2415 ? 169.945 225.179 179.160 1.00 50.03  ? 2415 ILE A N     1 
ATOM   6851  C  CA    . ILE A 1 2415 ? 170.913 224.359 179.885 1.00 48.47  ? 2415 ILE A CA    1 
ATOM   6852  C  C     . ILE A 1 2415 ? 171.448 223.251 178.988 1.00 51.84  ? 2415 ILE A C     1 
ATOM   6853  O  O     . ILE A 1 2415 ? 172.650 222.957 178.985 1.00 51.92  ? 2415 ILE A O     1 
ATOM   6854  C  CB    . ILE A 1 2415 ? 170.276 223.793 181.168 1.00 45.64  ? 2415 ILE A CB    1 
ATOM   6855  C  CG1   . ILE A 1 2415 ? 170.019 224.915 182.174 1.00 50.25  ? 2415 ILE A CG1   1 
ATOM   6856  C  CG2   . ILE A 1 2415 ? 171.159 222.716 181.777 1.00 43.34  ? 2415 ILE A CG2   1 
ATOM   6857  C  CD1   . ILE A 1 2415 ? 169.120 224.509 183.316 1.00 46.41  ? 2415 ILE A CD1   1 
ATOM   6858  N  N     . GLN A 1 2416 ? 170.562 222.617 178.217 1.00 50.28  ? 2416 GLN A N     1 
ATOM   6859  C  CA    . GLN A 1 2416 ? 170.987 221.569 177.295 1.00 40.00  ? 2416 GLN A CA    1 
ATOM   6860  C  C     . GLN A 1 2416 ? 171.960 222.110 176.255 1.00 44.52  ? 2416 GLN A C     1 
ATOM   6861  O  O     . GLN A 1 2416 ? 172.968 221.466 175.943 1.00 43.51  ? 2416 GLN A O     1 
ATOM   6862  C  CB    . GLN A 1 2416 ? 169.771 220.954 176.605 1.00 33.22  ? 2416 GLN A CB    1 
ATOM   6863  C  CG    . GLN A 1 2416 ? 168.932 220.057 177.487 1.00 37.61  ? 2416 GLN A CG    1 
ATOM   6864  C  CD    . GLN A 1 2416 ? 167.650 219.629 176.808 1.00 40.32  ? 2416 GLN A CD    1 
ATOM   6865  O  OE1   . GLN A 1 2416 ? 166.577 219.661 177.407 1.00 52.77  ? 2416 GLN A OE1   1 
ATOM   6866  N  NE2   . GLN A 1 2416 ? 167.754 219.227 175.548 1.00 35.15  ? 2416 GLN A NE2   1 
ATOM   6867  N  N     . ARG A 1 2417 ? 171.667 223.288 175.701 1.00 45.04  ? 2417 ARG A N     1 
ATOM   6868  C  CA    . ARG A 1 2417 ? 172.551 223.878 174.700 1.00 40.90  ? 2417 ARG A CA    1 
ATOM   6869  C  C     . ARG A 1 2417 ? 173.910 224.222 175.295 1.00 44.52  ? 2417 ARG A C     1 
ATOM   6870  O  O     . ARG A 1 2417 ? 174.948 223.978 174.668 1.00 48.72  ? 2417 ARG A O     1 
ATOM   6871  C  CB    . ARG A 1 2417 ? 171.900 225.120 174.094 1.00 36.86  ? 2417 ARG A CB    1 
ATOM   6872  C  CG    . ARG A 1 2417 ? 170.718 224.817 173.193 1.00 40.58  ? 2417 ARG A CG    1 
ATOM   6873  C  CD    . ARG A 1 2417 ? 170.316 226.034 172.381 1.00 46.59  ? 2417 ARG A CD    1 
ATOM   6874  N  NE    . ARG A 1 2417 ? 169.305 225.708 171.383 1.00 48.18  ? 2417 ARG A NE    1 
ATOM   6875  C  CZ    . ARG A 1 2417 ? 168.071 226.192 171.386 1.00 48.44  ? 2417 ARG A CZ    1 
ATOM   6876  N  NH1   . ARG A 1 2417 ? 167.664 227.041 172.315 1.00 51.19  ? 2417 ARG A NH1   1 
ATOM   6877  N  NH2   . ARG A 1 2417 ? 167.224 225.816 170.432 1.00 46.37  ? 2417 ARG A NH2   1 
ATOM   6878  N  N     . ASP A 1 2418 ? 173.924 224.787 176.505 1.00 41.71  ? 2418 ASP A N     1 
ATOM   6879  C  CA    . ASP A 1 2418 ? 175.193 225.100 177.155 1.00 42.74  ? 2418 ASP A CA    1 
ATOM   6880  C  C     . ASP A 1 2418 ? 176.000 223.835 177.424 1.00 44.34  ? 2418 ASP A C     1 
ATOM   6881  O  O     . ASP A 1 2418 ? 177.216 223.802 177.190 1.00 44.59  ? 2418 ASP A O     1 
ATOM   6882  C  CB    . ASP A 1 2418 ? 174.942 225.864 178.453 1.00 45.79  ? 2418 ASP A CB    1 
ATOM   6883  C  CG    . ASP A 1 2418 ? 174.836 227.360 178.238 1.00 60.19  ? 2418 ASP A CG    1 
ATOM   6884  O  OD1   . ASP A 1 2418 ? 175.591 227.896 177.401 1.00 61.22  ? 2418 ASP A OD1   1 
ATOM   6885  O  OD2   . ASP A 1 2418 ? 173.999 228.000 178.908 1.00 67.93  ? 2418 ASP A OD2   1 
ATOM   6886  N  N     . ALA A 1 2419 ? 175.339 222.779 177.904 1.00 39.69  ? 2419 ALA A N     1 
ATOM   6887  C  CA    . ALA A 1 2419 ? 176.038 221.522 178.150 1.00 35.39  ? 2419 ALA A CA    1 
ATOM   6888  C  C     . ALA A 1 2419 ? 176.597 220.940 176.859 1.00 40.85  ? 2419 ALA A C     1 
ATOM   6889  O  O     . ALA A 1 2419 ? 177.741 220.474 176.825 1.00 41.82  ? 2419 ALA A O     1 
ATOM   6890  C  CB    . ALA A 1 2419 ? 175.100 220.525 178.829 1.00 32.47  ? 2419 ALA A CB    1 
ATOM   6891  N  N     . ALA A 1 2420 ? 175.808 220.970 175.782 1.00 40.04  ? 2420 ALA A N     1 
ATOM   6892  C  CA    . ALA A 1 2420 ? 176.280 220.455 174.501 1.00 35.88  ? 2420 ALA A CA    1 
ATOM   6893  C  C     . ALA A 1 2420 ? 177.473 221.252 173.996 1.00 37.21  ? 2420 ALA A C     1 
ATOM   6894  O  O     . ALA A 1 2420 ? 178.407 220.688 173.413 1.00 38.65  ? 2420 ALA A O     1 
ATOM   6895  C  CB    . ALA A 1 2420 ? 175.147 220.475 173.477 1.00 31.33  ? 2420 ALA A CB    1 
ATOM   6896  N  N     . THR A 1 2421 ? 177.457 222.570 174.204 1.00 39.30  ? 2421 THR A N     1 
ATOM   6897  C  CA    . THR A 1 2421 ? 178.613 223.386 173.851 1.00 39.09  ? 2421 THR A CA    1 
ATOM   6898  C  C     . THR A 1 2421 ? 179.835 222.988 174.668 1.00 38.21  ? 2421 THR A C     1 
ATOM   6899  O  O     . THR A 1 2421 ? 180.956 222.949 174.146 1.00 38.37  ? 2421 THR A O     1 
ATOM   6900  C  CB    . THR A 1 2421 ? 178.292 224.868 174.054 1.00 40.20  ? 2421 THR A CB    1 
ATOM   6901  O  OG1   . THR A 1 2421 ? 177.079 225.194 173.365 1.00 47.64  ? 2421 THR A OG1   1 
ATOM   6902  C  CG2   . THR A 1 2421 ? 179.419 225.736 173.518 1.00 43.77  ? 2421 THR A CG2   1 
ATOM   6903  N  N     . ILE A 1 2422 ? 179.640 222.690 175.955 1.00 38.87  ? 2422 ILE A N     1 
ATOM   6904  C  CA    . ILE A 1 2422 ? 180.776 222.346 176.808 1.00 39.14  ? 2422 ILE A CA    1 
ATOM   6905  C  C     . ILE A 1 2422 ? 181.375 220.999 176.408 1.00 42.48  ? 2422 ILE A C     1 
ATOM   6906  O  O     . ILE A 1 2422 ? 182.601 220.850 176.345 1.00 46.49  ? 2422 ILE A O     1 
ATOM   6907  C  CB    . ILE A 1 2422 ? 180.367 222.368 178.292 1.00 34.77  ? 2422 ILE A CB    1 
ATOM   6908  C  CG1   . ILE A 1 2422 ? 179.947 223.778 178.704 1.00 36.50  ? 2422 ILE A CG1   1 
ATOM   6909  C  CG2   . ILE A 1 2422 ? 181.521 221.910 179.165 1.00 33.86  ? 2422 ILE A CG2   1 
ATOM   6910  C  CD1   . ILE A 1 2422 ? 179.119 223.820 179.961 1.00 37.46  ? 2422 ILE A CD1   1 
ATOM   6911  N  N     . MET A 1 2423 ? 180.536 220.000 176.134 1.00 38.57  ? 2423 MET A N     1 
ATOM   6912  C  CA    . MET A 1 2423 ? 181.038 218.681 175.759 1.00 35.14  ? 2423 MET A CA    1 
ATOM   6913  C  C     . MET A 1 2423 ? 181.359 218.554 174.276 1.00 38.03  ? 2423 MET A C     1 
ATOM   6914  O  O     . MET A 1 2423 ? 181.795 217.481 173.847 1.00 38.18  ? 2423 MET A O     1 
ATOM   6915  C  CB    . MET A 1 2423 ? 180.046 217.576 176.145 1.00 28.86  ? 2423 MET A CB    1 
ATOM   6916  C  CG    . MET A 1 2423 ? 179.182 217.876 177.342 1.00 34.78  ? 2423 MET A CG    1 
ATOM   6917  S  SD    . MET A 1 2423 ? 177.958 216.592 177.647 1.00 46.16  ? 2423 MET A SD    1 
ATOM   6918  C  CE    . MET A 1 2423 ? 176.679 217.070 176.492 1.00 20.57  ? 2423 MET A CE    1 
ATOM   6919  N  N     . GLN A 1 2424 ? 181.148 219.605 173.487 1.00 40.64  ? 2424 GLN A N     1 
ATOM   6920  C  CA    . GLN A 1 2424 ? 181.476 219.533 172.066 1.00 35.92  ? 2424 GLN A CA    1 
ATOM   6921  C  C     . GLN A 1 2424 ? 182.940 219.196 171.795 1.00 35.42  ? 2424 GLN A C     1 
ATOM   6922  O  O     . GLN A 1 2424 ? 183.191 218.348 170.921 1.00 36.45  ? 2424 GLN A O     1 
ATOM   6923  C  CB    . GLN A 1 2424 ? 181.079 220.844 171.375 1.00 42.64  ? 2424 GLN A CB    1 
ATOM   6924  C  CG    . GLN A 1 2424 ? 181.476 220.916 169.911 1.00 44.13  ? 2424 GLN A CG    1 
ATOM   6925  C  CD    . GLN A 1 2424 ? 180.706 219.935 169.052 1.00 48.76  ? 2424 GLN A CD    1 
ATOM   6926  O  OE1   . GLN A 1 2424 ? 179.511 220.108 168.812 1.00 48.22  ? 2424 GLN A OE1   1 
ATOM   6927  N  NE2   . GLN A 1 2424 ? 181.388 218.897 168.583 1.00 49.34  ? 2424 GLN A NE2   1 
ATOM   6928  N  N     . PRO A 1 2425 ? 183.933 219.795 172.466 1.00 37.33  ? 2425 PRO A N     1 
ATOM   6929  C  CA    . PRO A 1 2425 ? 185.326 219.394 172.197 1.00 38.99  ? 2425 PRO A CA    1 
ATOM   6930  C  C     . PRO A 1 2425 ? 185.613 217.932 172.492 1.00 40.40  ? 2425 PRO A C     1 
ATOM   6931  O  O     . PRO A 1 2425 ? 186.492 217.344 171.850 1.00 41.81  ? 2425 PRO A O     1 
ATOM   6932  C  CB    . PRO A 1 2425 ? 186.139 220.320 173.112 1.00 36.06  ? 2425 PRO A CB    1 
ATOM   6933  C  CG    . PRO A 1 2425 ? 185.268 221.497 173.324 1.00 40.87  ? 2425 PRO A CG    1 
ATOM   6934  C  CD    . PRO A 1 2425 ? 183.877 220.952 173.380 1.00 35.68  ? 2425 PRO A CD    1 
ATOM   6935  N  N     . TYR A 1 2426 ? 184.907 217.326 173.445 1.00 41.37  ? 2426 TYR A N     1 
ATOM   6936  C  CA    . TYR A 1 2426 ? 185.170 215.948 173.836 1.00 37.85  ? 2426 TYR A CA    1 
ATOM   6937  C  C     . TYR A 1 2426 ? 184.451 214.922 172.970 1.00 40.89  ? 2426 TYR A C     1 
ATOM   6938  O  O     . TYR A 1 2426 ? 184.768 213.732 173.062 1.00 44.05  ? 2426 TYR A O     1 
ATOM   6939  C  CB    . TYR A 1 2426 ? 184.777 215.733 175.301 1.00 31.00  ? 2426 TYR A CB    1 
ATOM   6940  C  CG    . TYR A 1 2426 ? 185.524 216.620 176.269 1.00 36.23  ? 2426 TYR A CG    1 
ATOM   6941  C  CD1   . TYR A 1 2426 ? 186.905 216.544 176.384 1.00 38.92  ? 2426 TYR A CD1   1 
ATOM   6942  C  CD2   . TYR A 1 2426 ? 184.850 217.535 177.066 1.00 31.99  ? 2426 TYR A CD2   1 
ATOM   6943  C  CE1   . TYR A 1 2426 ? 187.593 217.351 177.265 1.00 39.79  ? 2426 TYR A CE1   1 
ATOM   6944  C  CE2   . TYR A 1 2426 ? 185.531 218.347 177.951 1.00 35.74  ? 2426 TYR A CE2   1 
ATOM   6945  C  CZ    . TYR A 1 2426 ? 186.902 218.250 178.045 1.00 43.91  ? 2426 TYR A CZ    1 
ATOM   6946  O  OH    . TYR A 1 2426 ? 187.590 219.055 178.924 1.00 55.29  ? 2426 TYR A OH    1 
ATOM   6947  N  N     . PHE A 1 2427 ? 183.507 215.343 172.133 1.00 37.61  ? 2427 PHE A N     1 
ATOM   6948  C  CA    . PHE A 1 2427 ? 182.726 214.434 171.302 1.00 30.17  ? 2427 PHE A CA    1 
ATOM   6949  C  C     . PHE A 1 2427 ? 183.119 214.536 169.831 1.00 40.87  ? 2427 PHE A C     1 
ATOM   6950  O  O     . PHE A 1 2427 ? 182.281 214.421 168.936 1.00 51.29  ? 2427 PHE A O     1 
ATOM   6951  C  CB    . PHE A 1 2427 ? 181.232 214.690 171.476 1.00 27.21  ? 2427 PHE A CB    1 
ATOM   6952  C  CG    . PHE A 1 2427 ? 180.643 214.016 172.680 1.00 22.81  ? 2427 PHE A CG    1 
ATOM   6953  C  CD1   . PHE A 1 2427 ? 180.545 212.638 172.737 1.00 23.51  ? 2427 PHE A CD1   1 
ATOM   6954  C  CD2   . PHE A 1 2427 ? 180.193 214.759 173.757 1.00 26.14  ? 2427 PHE A CD2   1 
ATOM   6955  C  CE1   . PHE A 1 2427 ? 180.006 212.012 173.842 1.00 21.24  ? 2427 PHE A CE1   1 
ATOM   6956  C  CE2   . PHE A 1 2427 ? 179.653 214.139 174.865 1.00 26.50  ? 2427 PHE A CE2   1 
ATOM   6957  C  CZ    . PHE A 1 2427 ? 179.561 212.764 174.907 1.00 23.25  ? 2427 PHE A CZ    1 
ATOM   6958  N  N     . THR A 1 2428 ? 184.402 214.754 169.571 1.00 43.91  ? 2428 THR A N     1 
ATOM   6959  C  CA    . THR A 1 2428 ? 184.946 214.779 168.223 1.00 50.74  ? 2428 THR A CA    1 
ATOM   6960  C  C     . THR A 1 2428 ? 185.781 213.529 167.980 1.00 53.62  ? 2428 THR A C     1 
ATOM   6961  O  O     . THR A 1 2428 ? 186.099 212.774 168.902 1.00 56.75  ? 2428 THR A O     1 
ATOM   6962  C  CB    . THR A 1 2428 ? 185.794 216.036 167.996 1.00 48.60  ? 2428 THR A CB    1 
ATOM   6963  O  OG1   . THR A 1 2428 ? 187.007 215.940 168.754 1.00 43.93  ? 2428 THR A OG1   1 
ATOM   6964  C  CG2   . THR A 1 2428 ? 185.031 217.279 168.422 1.00 44.22  ? 2428 THR A CG2   1 
ATOM   6965  N  N     . SER A 1 2429 ? 186.129 213.313 166.713 1.00 55.62  ? 2429 SER A N     1 
ATOM   6966  C  CA    . SER A 1 2429 ? 187.013 212.210 166.369 1.00 56.56  ? 2429 SER A CA    1 
ATOM   6967  C  C     . SER A 1 2429 ? 188.374 212.412 167.023 1.00 61.96  ? 2429 SER A C     1 
ATOM   6968  O  O     . SER A 1 2429 ? 188.877 213.536 167.110 1.00 61.39  ? 2429 SER A O     1 
ATOM   6969  C  CB    . SER A 1 2429 ? 187.162 212.099 164.852 1.00 56.43  ? 2429 SER A CB    1 
ATOM   6970  O  OG    . SER A 1 2429 ? 187.871 210.925 164.496 1.00 55.96  ? 2429 SER A OG    1 
ATOM   6971  N  N     . ASN A 1 2430 ? 188.964 211.310 167.489 1.00 61.02  ? 2430 ASN A N     1 
ATOM   6972  C  CA    . ASN A 1 2430 ? 190.198 211.345 168.278 1.00 66.25  ? 2430 ASN A CA    1 
ATOM   6973  C  C     . ASN A 1 2430 ? 190.015 212.213 169.522 1.00 65.12  ? 2430 ASN A C     1 
ATOM   6974  O  O     . ASN A 1 2430 ? 190.918 212.942 169.938 1.00 68.94  ? 2430 ASN A O     1 
ATOM   6975  C  CB    . ASN A 1 2430 ? 191.385 211.824 167.436 1.00 73.63  ? 2430 ASN A CB    1 
ATOM   6976  C  CG    . ASN A 1 2430 ? 192.728 211.486 168.063 1.00 83.01  ? 2430 ASN A CG    1 
ATOM   6977  O  OD1   . ASN A 1 2430 ? 192.804 211.066 169.218 1.00 82.17  ? 2430 ASN A OD1   1 
ATOM   6978  N  ND2   . ASN A 1 2430 ? 193.799 211.673 167.299 1.00 82.62  ? 2430 ASN A ND2   1 
ATOM   6979  N  N     . GLY A 1 2431 ? 188.822 212.147 170.113 1.00 53.29  ? 2431 GLY A N     1 
ATOM   6980  C  CA    . GLY A 1 2431 ? 188.523 212.846 171.341 1.00 45.47  ? 2431 GLY A CA    1 
ATOM   6981  C  C     . GLY A 1 2431 ? 188.620 211.937 172.553 1.00 46.53  ? 2431 GLY A C     1 
ATOM   6982  O  O     . GLY A 1 2431 ? 189.008 210.770 172.469 1.00 51.16  ? 2431 GLY A O     1 
ATOM   6983  N  N     . LEU A 1 2432 ? 188.255 212.497 173.708 1.00 41.60  ? 2432 LEU A N     1 
ATOM   6984  C  CA    . LEU A 1 2432 ? 188.293 211.723 174.945 1.00 34.96  ? 2432 LEU A CA    1 
ATOM   6985  C  C     . LEU A 1 2432 ? 187.338 210.538 174.879 1.00 35.17  ? 2432 LEU A C     1 
ATOM   6986  O  O     . LEU A 1 2432 ? 187.706 209.407 175.222 1.00 39.99  ? 2432 LEU A O     1 
ATOM   6987  C  CB    . LEU A 1 2432 ? 187.955 212.621 176.135 1.00 38.16  ? 2432 LEU A CB    1 
ATOM   6988  C  CG    . LEU A 1 2432 ? 187.568 211.912 177.434 1.00 36.36  ? 2432 LEU A CG    1 
ATOM   6989  C  CD1   . LEU A 1 2432 ? 188.771 211.211 178.045 1.00 36.09  ? 2432 LEU A CD1   1 
ATOM   6990  C  CD2   . LEU A 1 2432 ? 186.954 212.893 178.420 1.00 30.48  ? 2432 LEU A CD2   1 
ATOM   6991  N  N     . VAL A 1 2433 ? 186.107 210.777 174.423 1.00 33.66  ? 2433 VAL A N     1 
ATOM   6992  C  CA    . VAL A 1 2433 ? 185.108 209.714 174.377 1.00 29.26  ? 2433 VAL A CA    1 
ATOM   6993  C  C     . VAL A 1 2433 ? 185.525 208.631 173.390 1.00 31.89  ? 2433 VAL A C     1 
ATOM   6994  O  O     . VAL A 1 2433 ? 185.422 207.434 173.681 1.00 32.93  ? 2433 VAL A O     1 
ATOM   6995  C  CB    . VAL A 1 2433 ? 183.725 210.290 174.028 1.00 21.81  ? 2433 VAL A CB    1 
ATOM   6996  C  CG1   . VAL A 1 2433 ? 182.664 209.211 174.141 1.00 19.92  ? 2433 VAL A CG1   1 
ATOM   6997  C  CG2   . VAL A 1 2433 ? 183.397 211.465 174.930 1.00 26.21  ? 2433 VAL A CG2   1 
ATOM   6998  N  N     . THR A 1 2434 ? 185.998 209.032 172.208 1.00 33.42  ? 2434 THR A N     1 
ATOM   6999  C  CA    . THR A 1 2434 ? 186.375 208.055 171.191 1.00 32.93  ? 2434 THR A CA    1 
ATOM   7000  C  C     . THR A 1 2434 ? 187.576 207.224 171.631 1.00 34.67  ? 2434 THR A C     1 
ATOM   7001  O  O     . THR A 1 2434 ? 187.589 206.000 171.452 1.00 39.16  ? 2434 THR A O     1 
ATOM   7002  C  CB    . THR A 1 2434 ? 186.669 208.761 169.868 1.00 38.71  ? 2434 THR A CB    1 
ATOM   7003  O  OG1   . THR A 1 2434 ? 185.551 209.580 169.505 1.00 39.25  ? 2434 THR A OG1   1 
ATOM   7004  C  CG2   . THR A 1 2434 ? 186.922 207.744 168.767 1.00 34.66  ? 2434 THR A CG2   1 
ATOM   7005  N  N     . LYS A 1 2435 ? 188.594 207.868 172.206 1.00 34.29  ? 2435 LYS A N     1 
ATOM   7006  C  CA    . LYS A 1 2435 ? 189.761 207.128 172.676 1.00 35.87  ? 2435 LYS A CA    1 
ATOM   7007  C  C     . LYS A 1 2435 ? 189.397 206.191 173.820 1.00 37.94  ? 2435 LYS A C     1 
ATOM   7008  O  O     . LYS A 1 2435 ? 189.874 205.050 173.874 1.00 40.70  ? 2435 LYS A O     1 
ATOM   7009  C  CB    . LYS A 1 2435 ? 190.864 208.099 173.099 1.00 37.03  ? 2435 LYS A CB    1 
ATOM   7010  C  CG    . LYS A 1 2435 ? 191.472 208.879 171.943 1.00 49.44  ? 2435 LYS A CG    1 
ATOM   7011  C  CD    . LYS A 1 2435 ? 192.228 210.104 172.432 1.00 51.37  ? 2435 LYS A CD    1 
ATOM   7012  C  CE    . LYS A 1 2435 ? 193.619 209.741 172.919 1.00 54.58  ? 2435 LYS A CE    1 
ATOM   7013  N  NZ    . LYS A 1 2435 ? 194.405 210.952 173.288 1.00 59.55  ? 2435 LYS A NZ    1 
ATOM   7014  N  N     . ALA A 1 2436 ? 188.550 206.652 174.744 1.00 36.54  ? 2436 ALA A N     1 
ATOM   7015  C  CA    . ALA A 1 2436 ? 188.110 205.786 175.833 1.00 28.16  ? 2436 ALA A CA    1 
ATOM   7016  C  C     . ALA A 1 2436 ? 187.320 204.595 175.305 1.00 29.92  ? 2436 ALA A C     1 
ATOM   7017  O  O     . ALA A 1 2436 ? 187.482 203.470 175.790 1.00 37.11  ? 2436 ALA A O     1 
ATOM   7018  C  CB    . ALA A 1 2436 ? 187.278 206.585 176.835 1.00 27.03  ? 2436 ALA A CB    1 
ATOM   7019  N  N     . LEU A 1 2437 ? 186.454 204.825 174.313 1.00 29.44  ? 2437 LEU A N     1 
ATOM   7020  C  CA    . LEU A 1 2437 ? 185.682 203.734 173.729 1.00 25.04  ? 2437 LEU A CA    1 
ATOM   7021  C  C     . LEU A 1 2437 ? 186.590 202.736 173.024 1.00 29.58  ? 2437 LEU A C     1 
ATOM   7022  O  O     . LEU A 1 2437 ? 186.366 201.522 173.097 1.00 32.90  ? 2437 LEU A O     1 
ATOM   7023  C  CB    . LEU A 1 2437 ? 184.638 204.294 172.764 1.00 22.61  ? 2437 LEU A CB    1 
ATOM   7024  C  CG    . LEU A 1 2437 ? 183.648 203.305 172.149 1.00 29.37  ? 2437 LEU A CG    1 
ATOM   7025  C  CD1   . LEU A 1 2437 ? 182.706 202.758 173.208 1.00 28.91  ? 2437 LEU A CD1   1 
ATOM   7026  C  CD2   . LEU A 1 2437 ? 182.866 203.968 171.028 1.00 27.16  ? 2437 LEU A CD2   1 
ATOM   7027  N  N     . GLU A 1 2438 ? 187.618 203.230 172.333 1.00 32.28  ? 2438 GLU A N     1 
ATOM   7028  C  CA    . GLU A 1 2438 ? 188.583 202.332 171.707 1.00 36.74  ? 2438 GLU A CA    1 
ATOM   7029  C  C     . GLU A 1 2438 ? 189.321 201.506 172.752 1.00 36.54  ? 2438 GLU A C     1 
ATOM   7030  O  O     . GLU A 1 2438 ? 189.548 200.306 172.559 1.00 34.42  ? 2438 GLU A O     1 
ATOM   7031  C  CB    . GLU A 1 2438 ? 189.570 203.132 170.857 1.00 43.70  ? 2438 GLU A CB    1 
ATOM   7032  C  CG    . GLU A 1 2438 ? 190.587 202.277 170.120 1.00 54.76  ? 2438 GLU A CG    1 
ATOM   7033  C  CD    . GLU A 1 2438 ? 191.876 203.020 169.835 1.00 66.97  ? 2438 GLU A CD    1 
ATOM   7034  O  OE1   . GLU A 1 2438 ? 191.863 204.269 169.860 1.00 70.97  ? 2438 GLU A OE1   1 
ATOM   7035  O  OE2   . GLU A 1 2438 ? 192.904 202.356 169.586 1.00 71.16  ? 2438 GLU A OE2   1 
ATOM   7036  N  N     . HIS A 1 2439 ? 189.707 202.131 173.867 1.00 36.69  ? 2439 HIS A N     1 
ATOM   7037  C  CA    . HIS A 1 2439 ? 190.405 201.397 174.917 1.00 35.53  ? 2439 HIS A CA    1 
ATOM   7038  C  C     . HIS A 1 2439 ? 189.475 200.431 175.639 1.00 35.83  ? 2439 HIS A C     1 
ATOM   7039  O  O     . HIS A 1 2439 ? 189.880 199.315 175.985 1.00 40.36  ? 2439 HIS A O     1 
ATOM   7040  C  CB    . HIS A 1 2439 ? 191.035 202.368 175.912 1.00 33.69  ? 2439 HIS A CB    1 
ATOM   7041  C  CG    . HIS A 1 2439 ? 191.884 201.700 176.949 1.00 38.22  ? 2439 HIS A CG    1 
ATOM   7042  N  ND1   . HIS A 1 2439 ? 193.161 201.252 176.689 1.00 42.47  ? 2439 HIS A ND1   1 
ATOM   7043  C  CD2   . HIS A 1 2439 ? 191.637 201.401 178.246 1.00 42.07  ? 2439 HIS A CD2   1 
ATOM   7044  C  CE1   . HIS A 1 2439 ? 193.666 200.708 177.781 1.00 45.61  ? 2439 HIS A CE1   1 
ATOM   7045  N  NE2   . HIS A 1 2439 ? 192.761 200.785 178.741 1.00 48.53  ? 2439 HIS A NE2   1 
ATOM   7046  N  N     . ALA A 1 2440 ? 188.229 200.844 175.885 1.00 35.26  ? 2440 ALA A N     1 
ATOM   7047  C  CA    . ALA A 1 2440 ? 187.299 199.998 176.628 1.00 29.24  ? 2440 ALA A CA    1 
ATOM   7048  C  C     . ALA A 1 2440 ? 187.004 198.698 175.893 1.00 34.35  ? 2440 ALA A C     1 
ATOM   7049  O  O     . ALA A 1 2440 ? 186.669 197.691 176.526 1.00 41.83  ? 2440 ALA A O     1 
ATOM   7050  C  CB    . ALA A 1 2440 ? 186.001 200.757 176.903 1.00 22.13  ? 2440 ALA A CB    1 
ATOM   7051  N  N     . PHE A 1 2441 ? 187.120 198.697 174.564 1.00 35.55  ? 2441 PHE A N     1 
ATOM   7052  C  CA    . PHE A 1 2441 ? 186.892 197.477 173.801 1.00 34.02  ? 2441 PHE A CA    1 
ATOM   7053  C  C     . PHE A 1 2441 ? 188.002 196.455 174.008 1.00 34.75  ? 2441 PHE A C     1 
ATOM   7054  O  O     . PHE A 1 2441 ? 187.770 195.257 173.810 1.00 34.16  ? 2441 PHE A O     1 
ATOM   7055  C  CB    . PHE A 1 2441 ? 186.750 197.808 172.315 1.00 38.28  ? 2441 PHE A CB    1 
ATOM   7056  C  CG    . PHE A 1 2441 ? 185.335 198.074 171.889 1.00 39.96  ? 2441 PHE A CG    1 
ATOM   7057  C  CD1   . PHE A 1 2441 ? 184.373 197.083 171.978 1.00 40.52  ? 2441 PHE A CD1   1 
ATOM   7058  C  CD2   . PHE A 1 2441 ? 184.966 199.317 171.406 1.00 36.41  ? 2441 PHE A CD2   1 
ATOM   7059  C  CE1   . PHE A 1 2441 ? 183.070 197.328 171.589 1.00 38.65  ? 2441 PHE A CE1   1 
ATOM   7060  C  CE2   . PHE A 1 2441 ? 183.665 199.568 171.016 1.00 35.37  ? 2441 PHE A CE2   1 
ATOM   7061  C  CZ    . PHE A 1 2441 ? 182.716 198.572 171.107 1.00 38.52  ? 2441 PHE A CZ    1 
ATOM   7062  N  N     . GLN A 1 2442 ? 189.198 196.896 174.400 1.00 37.85  ? 2442 GLN A N     1 
ATOM   7063  C  CA    . GLN A 1 2442 ? 190.286 195.969 174.685 1.00 41.37  ? 2442 GLN A CA    1 
ATOM   7064  C  C     . GLN A 1 2442 ? 190.085 195.224 175.997 1.00 39.24  ? 2442 GLN A C     1 
ATOM   7065  O  O     . GLN A 1 2442 ? 190.648 194.138 176.171 1.00 37.67  ? 2442 GLN A O     1 
ATOM   7066  C  CB    . GLN A 1 2442 ? 191.622 196.714 174.718 1.00 37.84  ? 2442 GLN A CB    1 
ATOM   7067  C  CG    . GLN A 1 2442 ? 191.767 197.773 173.639 1.00 42.08  ? 2442 GLN A CG    1 
ATOM   7068  C  CD    . GLN A 1 2442 ? 191.788 197.181 172.244 1.00 51.30  ? 2442 GLN A CD    1 
ATOM   7069  O  OE1   . GLN A 1 2442 ? 192.527 196.236 171.970 1.00 51.39  ? 2442 GLN A OE1   1 
ATOM   7070  N  NE2   . GLN A 1 2442 ? 190.972 197.734 171.354 1.00 48.50  ? 2442 GLN A NE2   1 
ATOM   7071  N  N     . LEU A 1 2443 ? 189.301 195.781 176.914 1.00 37.78  ? 2443 LEU A N     1 
ATOM   7072  C  CA    . LEU A 1 2443 ? 188.993 195.126 178.173 1.00 37.58  ? 2443 LEU A CA    1 
ATOM   7073  C  C     . LEU A 1 2443 ? 187.955 194.026 177.955 1.00 47.05  ? 2443 LEU A C     1 
ATOM   7074  O  O     . LEU A 1 2443 ? 187.240 194.000 176.950 1.00 50.64  ? 2443 LEU A O     1 
ATOM   7075  C  CB    . LEU A 1 2443 ? 188.480 196.147 179.187 1.00 32.88  ? 2443 LEU A CB    1 
ATOM   7076  C  CG    . LEU A 1 2443 ? 189.330 197.402 179.403 1.00 38.82  ? 2443 LEU A CG    1 
ATOM   7077  C  CD1   . LEU A 1 2443 ? 188.676 198.327 180.418 1.00 31.59  ? 2443 LEU A CD1   1 
ATOM   7078  C  CD2   . LEU A 1 2443 ? 190.742 197.039 179.835 1.00 41.76  ? 2443 LEU A CD2   1 
ATOM   7079  N  N     . GLU A 1 2444 ? 187.874 193.105 178.911 1.00 47.62  ? 2444 GLU A N     1 
ATOM   7080  C  CA    . GLU A 1 2444 ? 186.813 192.108 178.920 1.00 50.26  ? 2444 GLU A CA    1 
ATOM   7081  C  C     . GLU A 1 2444 ? 185.746 192.506 179.931 1.00 43.67  ? 2444 GLU A C     1 
ATOM   7082  O  O     . GLU A 1 2444 ? 186.051 193.045 180.999 1.00 35.54  ? 2444 GLU A O     1 
ATOM   7083  C  CB    . GLU A 1 2444 ? 187.338 190.698 179.223 1.00 52.97  ? 2444 GLU A CB    1 
ATOM   7084  C  CG    . GLU A 1 2444 ? 187.579 190.379 180.692 1.00 51.94  ? 2444 GLU A CG    1 
ATOM   7085  C  CD    . GLU A 1 2444 ? 189.023 190.564 181.100 1.00 60.41  ? 2444 GLU A CD    1 
ATOM   7086  O  OE1   . GLU A 1 2444 ? 189.375 190.183 182.236 1.00 67.69  ? 2444 GLU A OE1   1 
ATOM   7087  O  OE2   . GLU A 1 2444 ? 189.819 191.045 180.266 1.00 56.79  ? 2444 GLU A OE2   1 
ATOM   7088  N  N     . HIS A 1 2445 ? 184.492 192.257 179.571 1.00 38.03  ? 2445 HIS A N     1 
ATOM   7089  C  CA    . HIS A 1 2445 ? 183.343 192.638 180.372 1.00 26.76  ? 2445 HIS A CA    1 
ATOM   7090  C  C     . HIS A 1 2445 ? 182.512 191.404 180.692 1.00 26.37  ? 2445 HIS A C     1 
ATOM   7091  O  O     . HIS A 1 2445 ? 182.700 190.334 180.108 1.00 30.59  ? 2445 HIS A O     1 
ATOM   7092  C  CB    . HIS A 1 2445 ? 182.484 193.678 179.642 1.00 25.02  ? 2445 HIS A CB    1 
ATOM   7093  C  CG    . HIS A 1 2445 ? 183.262 194.844 179.119 1.00 31.43  ? 2445 HIS A CG    1 
ATOM   7094  N  ND1   . HIS A 1 2445 ? 183.517 195.969 179.875 1.00 30.98  ? 2445 HIS A ND1   1 
ATOM   7095  C  CD2   . HIS A 1 2445 ? 183.852 195.057 177.919 1.00 31.81  ? 2445 HIS A CD2   1 
ATOM   7096  C  CE1   . HIS A 1 2445 ? 184.224 196.826 179.160 1.00 30.74  ? 2445 HIS A CE1   1 
ATOM   7097  N  NE2   . HIS A 1 2445 ? 184.441 196.296 177.970 1.00 34.59  ? 2445 HIS A NE2   1 
ATOM   7098  N  N     . ILE A 1 2446 ? 181.585 191.563 181.641 1.00 26.50  ? 2446 ILE A N     1 
ATOM   7099  C  CA    . ILE A 1 2446 ? 180.697 190.463 181.994 1.00 24.99  ? 2446 ILE A CA    1 
ATOM   7100  C  C     . ILE A 1 2446 ? 179.782 190.092 180.835 1.00 28.52  ? 2446 ILE A C     1 
ATOM   7101  O  O     . ILE A 1 2446 ? 179.261 188.972 180.794 1.00 34.16  ? 2446 ILE A O     1 
ATOM   7102  C  CB    . ILE A 1 2446 ? 179.883 190.811 183.255 1.00 22.49  ? 2446 ILE A CB    1 
ATOM   7103  C  CG1   . ILE A 1 2446 ? 179.493 189.536 184.002 1.00 25.07  ? 2446 ILE A CG1   1 
ATOM   7104  C  CG2   . ILE A 1 2446 ? 178.652 191.631 182.900 1.00 18.15  ? 2446 ILE A CG2   1 
ATOM   7105  C  CD1   . ILE A 1 2446 ? 180.676 188.693 184.421 1.00 28.60  ? 2446 ILE A CD1   1 
ATOM   7106  N  N     . MET A 1 2447 ? 179.576 191.004 179.887 1.00 24.80  ? 2447 MET A N     1 
ATOM   7107  C  CA    . MET A 1 2447 ? 178.811 190.729 178.682 1.00 23.98  ? 2447 MET A CA    1 
ATOM   7108  C  C     . MET A 1 2447 ? 179.553 191.316 177.491 1.00 33.39  ? 2447 MET A C     1 
ATOM   7109  O  O     . MET A 1 2447 ? 180.401 192.199 177.639 1.00 36.68  ? 2447 MET A O     1 
ATOM   7110  C  CB    . MET A 1 2447 ? 177.391 191.300 178.765 1.00 22.26  ? 2447 MET A CB    1 
ATOM   7111  C  CG    . MET A 1 2447 ? 176.476 190.537 179.704 1.00 26.80  ? 2447 MET A CG    1 
ATOM   7112  S  SD    . MET A 1 2447 ? 174.779 191.137 179.664 1.00 40.82  ? 2447 MET A SD    1 
ATOM   7113  C  CE    . MET A 1 2447 ? 173.947 189.824 180.550 1.00 20.13  ? 2447 MET A CE    1 
ATOM   7114  N  N     . ASP A 1 2448 ? 179.235 190.802 176.305 1.00 34.55  ? 2448 ASP A N     1 
ATOM   7115  C  CA    . ASP A 1 2448 ? 179.876 191.283 175.089 1.00 30.83  ? 2448 ASP A CA    1 
ATOM   7116  C  C     . ASP A 1 2448 ? 179.626 192.775 174.916 1.00 32.32  ? 2448 ASP A C     1 
ATOM   7117  O  O     . ASP A 1 2448 ? 178.487 193.241 175.000 1.00 39.90  ? 2448 ASP A O     1 
ATOM   7118  C  CB    . ASP A 1 2448 ? 179.353 190.513 173.877 1.00 36.08  ? 2448 ASP A CB    1 
ATOM   7119  C  CG    . ASP A 1 2448 ? 179.723 189.045 173.916 1.00 47.21  ? 2448 ASP A CG    1 
ATOM   7120  O  OD1   . ASP A 1 2448 ? 180.021 188.535 175.017 1.00 53.41  ? 2448 ASP A OD1   1 
ATOM   7121  O  OD2   . ASP A 1 2448 ? 179.715 188.400 172.847 1.00 44.22  ? 2448 ASP A OD2   1 
ATOM   7122  N  N     . LEU A 1 2449 ? 180.698 193.524 174.675 1.00 31.48  ? 2449 LEU A N     1 
ATOM   7123  C  CA    . LEU A 1 2449 ? 180.597 194.972 174.589 1.00 33.09  ? 2449 LEU A CA    1 
ATOM   7124  C  C     . LEU A 1 2449 ? 180.213 195.408 173.182 1.00 35.81  ? 2449 LEU A C     1 
ATOM   7125  O  O     . LEU A 1 2449 ? 180.771 194.930 172.190 1.00 40.55  ? 2449 LEU A O     1 
ATOM   7126  C  CB    . LEU A 1 2449 ? 181.915 195.631 174.994 1.00 31.13  ? 2449 LEU A CB    1 
ATOM   7127  C  CG    . LEU A 1 2449 ? 181.793 197.099 175.407 1.00 25.83  ? 2449 LEU A CG    1 
ATOM   7128  C  CD1   . LEU A 1 2449 ? 181.293 197.209 176.838 1.00 29.74  ? 2449 LEU A CD1   1 
ATOM   7129  C  CD2   . LEU A 1 2449 ? 183.116 197.827 175.241 1.00 29.66  ? 2449 LEU A CD2   1 
ATOM   7130  N  N     . THR A 1 2450 ? 179.251 196.322 173.107 1.00 30.11  ? 2450 THR A N     1 
ATOM   7131  C  CA    . THR A 1 2450 ? 178.835 196.930 171.855 1.00 26.98  ? 2450 THR A CA    1 
ATOM   7132  C  C     . THR A 1 2450 ? 178.943 198.441 171.987 1.00 25.63  ? 2450 THR A C     1 
ATOM   7133  O  O     . THR A 1 2450 ? 178.813 198.994 173.082 1.00 28.31  ? 2450 THR A O     1 
ATOM   7134  C  CB    . THR A 1 2450 ? 177.400 196.535 171.474 1.00 35.08  ? 2450 THR A CB    1 
ATOM   7135  O  OG1   . THR A 1 2450 ? 176.493 196.986 172.487 1.00 36.53  ? 2450 THR A OG1   1 
ATOM   7136  C  CG2   . THR A 1 2450 ? 177.283 195.026 171.328 1.00 31.06  ? 2450 THR A CG2   1 
ATOM   7137  N  N     . ARG A 1 2451 ? 179.197 199.102 170.856 1.00 25.59  ? 2451 ARG A N     1 
ATOM   7138  C  CA    . ARG A 1 2451 ? 179.412 200.545 170.876 1.00 21.10  ? 2451 ARG A CA    1 
ATOM   7139  C  C     . ARG A 1 2451 ? 178.170 201.290 171.349 1.00 17.25  ? 2451 ARG A C     1 
ATOM   7140  O  O     . ARG A 1 2451 ? 178.262 202.200 172.184 1.00 20.38  ? 2451 ARG A O     1 
ATOM   7141  C  CB    . ARG A 1 2451 ? 179.833 201.026 169.488 1.00 22.01  ? 2451 ARG A CB    1 
ATOM   7142  C  CG    . ARG A 1 2451 ? 179.757 202.528 169.291 1.00 19.50  ? 2451 ARG A CG    1 
ATOM   7143  C  CD    . ARG A 1 2451 ? 180.035 202.898 167.843 1.00 26.51  ? 2451 ARG A CD    1 
ATOM   7144  N  NE    . ARG A 1 2451 ? 179.118 202.233 166.926 1.00 28.57  ? 2451 ARG A NE    1 
ATOM   7145  C  CZ    . ARG A 1 2451 ? 179.173 202.335 165.605 1.00 23.46  ? 2451 ARG A CZ    1 
ATOM   7146  N  NH1   . ARG A 1 2451 ? 180.097 203.069 165.007 1.00 21.65  ? 2451 ARG A NH1   1 
ATOM   7147  N  NH2   . ARG A 1 2451 ? 178.281 201.683 164.865 1.00 24.08  ? 2451 ARG A NH2   1 
ATOM   7148  N  N     . LEU A 1 2452 ? 176.994 200.911 170.843 1.00 17.26  ? 2452 LEU A N     1 
ATOM   7149  C  CA    . LEU A 1 2452 ? 175.801 201.691 171.149 1.00 16.50  ? 2452 LEU A CA    1 
ATOM   7150  C  C     . LEU A 1 2452 ? 175.301 201.469 172.567 1.00 18.14  ? 2452 LEU A C     1 
ATOM   7151  O  O     . LEU A 1 2452 ? 174.637 202.349 173.114 1.00 22.69  ? 2452 LEU A O     1 
ATOM   7152  C  CB    . LEU A 1 2452 ? 174.684 201.404 170.150 1.00 13.31  ? 2452 LEU A CB    1 
ATOM   7153  C  CG    . LEU A 1 2452 ? 174.927 201.950 168.748 1.00 11.82  ? 2452 LEU A CG    1 
ATOM   7154  C  CD1   . LEU A 1 2452 ? 173.795 201.539 167.852 1.00 15.09  ? 2452 LEU A CD1   1 
ATOM   7155  C  CD2   . LEU A 1 2452 ? 175.051 203.460 168.792 1.00 12.95  ? 2452 LEU A CD2   1 
ATOM   7156  N  N     . ARG A 1 2453 ? 175.604 200.331 173.192 1.00 16.00  ? 2453 ARG A N     1 
ATOM   7157  C  CA    . ARG A 1 2453 ? 175.231 200.176 174.595 1.00 15.78  ? 2453 ARG A CA    1 
ATOM   7158  C  C     . ARG A 1 2453 ? 175.949 201.207 175.457 1.00 19.11  ? 2453 ARG A C     1 
ATOM   7159  O  O     . ARG A 1 2453 ? 175.321 201.931 176.243 1.00 26.21  ? 2453 ARG A O     1 
ATOM   7160  C  CB    . ARG A 1 2453 ? 175.534 198.758 175.080 1.00 13.26  ? 2453 ARG A CB    1 
ATOM   7161  C  CG    . ARG A 1 2453 ? 175.373 198.597 176.584 1.00 13.94  ? 2453 ARG A CG    1 
ATOM   7162  C  CD    . ARG A 1 2453 ? 175.342 197.140 177.014 1.00 15.32  ? 2453 ARG A CD    1 
ATOM   7163  N  NE    . ARG A 1 2453 ? 176.546 196.411 176.637 1.00 20.47  ? 2453 ARG A NE    1 
ATOM   7164  C  CZ    . ARG A 1 2453 ? 177.425 195.931 177.505 1.00 24.72  ? 2453 ARG A CZ    1 
ATOM   7165  N  NH1   . ARG A 1 2453 ? 177.278 196.108 178.807 1.00 22.96  ? 2453 ARG A NH1   1 
ATOM   7166  N  NH2   . ARG A 1 2453 ? 178.478 195.255 177.056 1.00 29.27  ? 2453 ARG A NH2   1 
ATOM   7167  N  N     . CYS A 1 2454 ? 177.270 201.311 175.292 1.00 14.96  ? 2454 CYS A N     1 
ATOM   7168  C  CA    . CYS A 1 2454 ? 178.039 202.310 176.025 1.00 13.80  ? 2454 CYS A CA    1 
ATOM   7169  C  C     . CYS A 1 2454 ? 177.612 203.722 175.647 1.00 17.10  ? 2454 CYS A C     1 
ATOM   7170  O  O     . CYS A 1 2454 ? 177.497 204.595 176.515 1.00 23.93  ? 2454 CYS A O     1 
ATOM   7171  C  CB    . CYS A 1 2454 ? 179.532 202.117 175.762 1.00 14.09  ? 2454 CYS A CB    1 
ATOM   7172  S  SG    . CYS A 1 2454 ? 180.072 200.396 175.764 1.00 38.54  ? 2454 CYS A SG    1 
ATOM   7173  N  N     . LEU A 1 2455 ? 177.381 203.969 174.355 1.00 13.37  ? 2455 LEU A N     1 
ATOM   7174  C  CA    . LEU A 1 2455 ? 177.001 205.311 173.926 1.00 11.61  ? 2455 LEU A CA    1 
ATOM   7175  C  C     . LEU A 1 2455 ? 175.644 205.720 174.492 1.00 14.98  ? 2455 LEU A C     1 
ATOM   7176  O  O     . LEU A 1 2455 ? 175.475 206.858 174.939 1.00 25.31  ? 2455 LEU A O     1 
ATOM   7177  C  CB    . LEU A 1 2455 ? 177.005 205.397 172.401 1.00 15.29  ? 2455 LEU A CB    1 
ATOM   7178  C  CG    . LEU A 1 2455 ? 178.391 205.401 171.751 1.00 14.21  ? 2455 LEU A CG    1 
ATOM   7179  C  CD1   . LEU A 1 2455 ? 178.328 205.968 170.343 1.00 15.61  ? 2455 LEU A CD1   1 
ATOM   7180  C  CD2   . LEU A 1 2455 ? 179.389 206.177 172.598 1.00 13.91  ? 2455 LEU A CD2   1 
ATOM   7181  N  N     . GLY A 1 2456 ? 174.668 204.810 174.487 1.00 11.90  ? 2456 GLY A N     1 
ATOM   7182  C  CA    . GLY A 1 2456 ? 173.373 205.123 175.064 1.00 14.96  ? 2456 GLY A CA    1 
ATOM   7183  C  C     . GLY A 1 2456 ? 173.440 205.314 176.565 1.00 19.47  ? 2456 GLY A C     1 
ATOM   7184  O  O     . GLY A 1 2456 ? 172.769 206.190 177.117 1.00 28.80  ? 2456 GLY A O     1 
ATOM   7185  N  N     . SER A 1 2457 ? 174.250 204.500 177.248 1.00 15.01  ? 2457 SER A N     1 
ATOM   7186  C  CA    . SER A 1 2457 ? 174.470 204.712 178.674 1.00 12.98  ? 2457 SER A CA    1 
ATOM   7187  C  C     . SER A 1 2457 ? 175.024 206.107 178.930 1.00 16.85  ? 2457 SER A C     1 
ATOM   7188  O  O     . SER A 1 2457 ? 174.529 206.840 179.795 1.00 22.60  ? 2457 SER A O     1 
ATOM   7189  C  CB    . SER A 1 2457 ? 175.425 203.650 179.215 1.00 12.90  ? 2457 SER A CB    1 
ATOM   7190  O  OG    . SER A 1 2457 ? 174.881 202.352 179.072 1.00 15.44  ? 2457 SER A OG    1 
ATOM   7191  N  N     . LEU A 1 2458 ? 176.046 206.496 178.164 1.00 15.22  ? 2458 LEU A N     1 
ATOM   7192  C  CA    . LEU A 1 2458 ? 176.664 207.805 178.342 1.00 15.17  ? 2458 LEU A CA    1 
ATOM   7193  C  C     . LEU A 1 2458 ? 175.678 208.929 178.051 1.00 18.98  ? 2458 LEU A C     1 
ATOM   7194  O  O     . LEU A 1 2458 ? 175.641 209.933 178.771 1.00 24.02  ? 2458 LEU A O     1 
ATOM   7195  C  CB    . LEU A 1 2458 ? 177.897 207.917 177.445 1.00 15.05  ? 2458 LEU A CB    1 
ATOM   7196  C  CG    . LEU A 1 2458 ? 178.543 209.290 177.274 1.00 20.93  ? 2458 LEU A CG    1 
ATOM   7197  C  CD1   . LEU A 1 2458 ? 179.115 209.781 178.590 1.00 20.30  ? 2458 LEU A CD1   1 
ATOM   7198  C  CD2   . LEU A 1 2458 ? 179.623 209.228 176.211 1.00 21.23  ? 2458 LEU A CD2   1 
ATOM   7199  N  N     . PHE A 1 2459 ? 174.869 208.779 177.000 1.00 9.66   ? 2459 PHE A N     1 
ATOM   7200  C  CA    . PHE A 1 2459 ? 173.900 209.816 176.660 1.00 16.62  ? 2459 PHE A CA    1 
ATOM   7201  C  C     . PHE A 1 2459 ? 172.833 209.952 177.740 1.00 22.28  ? 2459 PHE A C     1 
ATOM   7202  O  O     . PHE A 1 2459 ? 172.429 211.070 178.083 1.00 31.03  ? 2459 PHE A O     1 
ATOM   7203  C  CB    . PHE A 1 2459 ? 173.260 209.518 175.304 1.00 15.23  ? 2459 PHE A CB    1 
ATOM   7204  C  CG    . PHE A 1 2459 ? 174.242 209.459 174.165 1.00 15.89  ? 2459 PHE A CG    1 
ATOM   7205  C  CD1   . PHE A 1 2459 ? 175.474 210.086 174.255 1.00 16.43  ? 2459 PHE A CD1   1 
ATOM   7206  C  CD2   . PHE A 1 2459 ? 173.930 208.775 173.002 1.00 14.68  ? 2459 PHE A CD2   1 
ATOM   7207  C  CE1   . PHE A 1 2459 ? 176.376 210.028 173.210 1.00 15.39  ? 2459 PHE A CE1   1 
ATOM   7208  C  CE2   . PHE A 1 2459 ? 174.828 208.716 171.954 1.00 11.74  ? 2459 PHE A CE2   1 
ATOM   7209  C  CZ    . PHE A 1 2459 ? 176.052 209.344 172.059 1.00 12.77  ? 2459 PHE A CZ    1 
ATOM   7210  N  N     . SER A 1 2460 ? 172.363 208.828 178.287 1.00 17.76  ? 2460 SER A N     1 
ATOM   7211  C  CA    . SER A 1 2460 ? 171.398 208.888 179.380 1.00 19.49  ? 2460 SER A CA    1 
ATOM   7212  C  C     . SER A 1 2460 ? 172.001 209.562 180.607 1.00 23.21  ? 2460 SER A C     1 
ATOM   7213  O  O     . SER A 1 2460 ? 171.338 210.367 181.274 1.00 27.31  ? 2460 SER A O     1 
ATOM   7214  C  CB    . SER A 1 2460 ? 170.906 207.483 179.723 1.00 23.09  ? 2460 SER A CB    1 
ATOM   7215  O  OG    . SER A 1 2460 ? 169.721 207.534 180.497 1.00 36.85  ? 2460 SER A OG    1 
ATOM   7216  N  N     . MET A 1 2461 ? 173.261 209.250 180.918 1.00 20.96  ? 2461 MET A N     1 
ATOM   7217  C  CA    . MET A 1 2461 ? 173.908 209.885 182.063 1.00 19.86  ? 2461 MET A CA    1 
ATOM   7218  C  C     . MET A 1 2461 ? 174.090 211.384 181.841 1.00 23.17  ? 2461 MET A C     1 
ATOM   7219  O  O     . MET A 1 2461 ? 173.953 212.177 182.778 1.00 26.81  ? 2461 MET A O     1 
ATOM   7220  C  CB    . MET A 1 2461 ? 175.246 209.205 182.351 1.00 19.02  ? 2461 MET A CB    1 
ATOM   7221  C  CG    . MET A 1 2461 ? 175.121 207.719 182.646 1.00 17.66  ? 2461 MET A CG    1 
ATOM   7222  S  SD    . MET A 1 2461 ? 176.500 207.042 183.582 1.00 19.92  ? 2461 MET A SD    1 
ATOM   7223  C  CE    . MET A 1 2461 ? 176.550 208.187 184.951 1.00 23.48  ? 2461 MET A CE    1 
ATOM   7224  N  N     . LEU A 1 2462 ? 174.395 211.795 180.608 1.00 20.92  ? 2462 LEU A N     1 
ATOM   7225  C  CA    . LEU A 1 2462 ? 174.527 213.222 180.323 1.00 20.66  ? 2462 LEU A CA    1 
ATOM   7226  C  C     . LEU A 1 2462 ? 173.179 213.933 180.406 1.00 22.28  ? 2462 LEU A C     1 
ATOM   7227  O  O     . LEU A 1 2462 ? 173.102 215.083 180.859 1.00 30.30  ? 2462 LEU A O     1 
ATOM   7228  C  CB    . LEU A 1 2462 ? 175.166 213.425 178.951 1.00 15.68  ? 2462 LEU A CB    1 
ATOM   7229  C  CG    . LEU A 1 2462 ? 176.614 212.941 178.853 1.00 15.26  ? 2462 LEU A CG    1 
ATOM   7230  C  CD1   . LEU A 1 2462 ? 177.134 213.072 177.434 1.00 16.49  ? 2462 LEU A CD1   1 
ATOM   7231  C  CD2   . LEU A 1 2462 ? 177.501 213.698 179.830 1.00 17.87  ? 2462 LEU A CD2   1 
ATOM   7232  N  N     . HIS A 1 2463 ? 172.107 213.268 179.970 1.00 21.72  ? 2463 HIS A N     1 
ATOM   7233  C  CA    . HIS A 1 2463 ? 170.772 213.825 180.163 1.00 25.03  ? 2463 HIS A CA    1 
ATOM   7234  C  C     . HIS A 1 2463 ? 170.458 213.977 181.646 1.00 28.26  ? 2463 HIS A C     1 
ATOM   7235  O  O     . HIS A 1 2463 ? 169.850 214.970 182.066 1.00 29.84  ? 2463 HIS A O     1 
ATOM   7236  C  CB    . HIS A 1 2463 ? 169.728 212.944 179.479 1.00 28.31  ? 2463 HIS A CB    1 
ATOM   7237  C  CG    . HIS A 1 2463 ? 169.861 212.896 177.989 1.00 31.77  ? 2463 HIS A CG    1 
ATOM   7238  N  ND1   . HIS A 1 2463 ? 169.174 211.991 177.210 1.00 37.74  ? 2463 HIS A ND1   1 
ATOM   7239  C  CD2   . HIS A 1 2463 ? 170.603 213.640 177.136 1.00 30.15  ? 2463 HIS A CD2   1 
ATOM   7240  C  CE1   . HIS A 1 2463 ? 169.486 212.180 175.940 1.00 37.76  ? 2463 HIS A CE1   1 
ATOM   7241  N  NE2   . HIS A 1 2463 ? 170.351 213.175 175.868 1.00 35.95  ? 2463 HIS A NE2   1 
ATOM   7242  N  N     . GLN A 1 2464 ? 170.870 212.999 182.456 1.00 33.18  ? 2464 GLN A N     1 
ATOM   7243  C  CA    . GLN A 1 2464 ? 170.712 213.119 183.902 1.00 29.25  ? 2464 GLN A CA    1 
ATOM   7244  C  C     . GLN A 1 2464 ? 171.512 214.292 184.455 1.00 30.67  ? 2464 GLN A C     1 
ATOM   7245  O  O     . GLN A 1 2464 ? 171.059 214.982 185.372 1.00 39.10  ? 2464 GLN A O     1 
ATOM   7246  C  CB    . GLN A 1 2464 ? 171.121 211.818 184.590 1.00 27.49  ? 2464 GLN A CB    1 
ATOM   7247  C  CG    . GLN A 1 2464 ? 170.843 211.801 186.083 1.00 35.40  ? 2464 GLN A CG    1 
ATOM   7248  C  CD    . GLN A 1 2464 ? 169.445 212.275 186.422 1.00 42.97  ? 2464 GLN A CD    1 
ATOM   7249  O  OE1   . GLN A 1 2464 ? 168.465 211.831 185.829 1.00 43.42  ? 2464 GLN A OE1   1 
ATOM   7250  N  NE2   . GLN A 1 2464 ? 169.347 213.185 187.385 1.00 38.89  ? 2464 GLN A NE2   1 
ATOM   7251  N  N     . ALA A 1 2465 ? 172.714 214.520 183.923 1.00 29.43  ? 2465 ALA A N     1 
ATOM   7252  C  CA    . ALA A 1 2465 ? 173.506 215.669 184.354 1.00 29.30  ? 2465 ALA A CA    1 
ATOM   7253  C  C     . ALA A 1 2465 ? 172.799 216.980 184.030 1.00 32.89  ? 2465 ALA A C     1 
ATOM   7254  O  O     . ALA A 1 2465 ? 172.775 217.906 184.851 1.00 37.82  ? 2465 ALA A O     1 
ATOM   7255  C  CB    . ALA A 1 2465 ? 174.885 215.635 183.699 1.00 22.78  ? 2465 ALA A CB    1 
ATOM   7256  N  N     . CYS A 1 2466 ? 172.223 217.077 182.831 1.00 31.64  ? 2466 CYS A N     1 
ATOM   7257  C  CA    . CYS A 1 2466 ? 171.472 218.276 182.469 1.00 29.51  ? 2466 CYS A CA    1 
ATOM   7258  C  C     . CYS A 1 2466 ? 170.266 218.464 183.383 1.00 31.74  ? 2466 CYS A C     1 
ATOM   7259  O  O     . CYS A 1 2466 ? 169.958 219.588 183.801 1.00 36.76  ? 2466 CYS A O     1 
ATOM   7260  C  CB    . CYS A 1 2466 ? 171.036 218.202 181.007 1.00 28.05  ? 2466 CYS A CB    1 
ATOM   7261  S  SG    . CYS A 1 2466 ? 172.401 218.195 179.823 1.00 49.09  ? 2466 CYS A SG    1 
ATOM   7262  N  N     . ARG A 1 2467 ? 169.573 217.370 183.707 1.00 33.01  ? 2467 ARG A N     1 
ATOM   7263  C  CA    . ARG A 1 2467 ? 168.442 217.457 184.626 1.00 32.60  ? 2467 ARG A CA    1 
ATOM   7264  C  C     . ARG A 1 2467 ? 168.890 217.887 186.018 1.00 34.01  ? 2467 ARG A C     1 
ATOM   7265  O  O     . ARG A 1 2467 ? 168.174 218.615 186.710 1.00 37.15  ? 2467 ARG A O     1 
ATOM   7266  C  CB    . ARG A 1 2467 ? 167.707 216.118 184.684 1.00 31.67  ? 2467 ARG A CB    1 
ATOM   7267  C  CG    . ARG A 1 2467 ? 166.853 215.831 183.461 1.00 33.95  ? 2467 ARG A CG    1 
ATOM   7268  C  CD    . ARG A 1 2467 ? 166.193 214.467 183.554 1.00 43.59  ? 2467 ARG A CD    1 
ATOM   7269  N  NE    . ARG A 1 2467 ? 165.639 214.041 182.274 1.00 50.76  ? 2467 ARG A NE    1 
ATOM   7270  C  CZ    . ARG A 1 2467 ? 164.440 214.388 181.826 1.00 57.31  ? 2467 ARG A CZ    1 
ATOM   7271  N  NH1   . ARG A 1 2467 ? 163.638 215.169 182.532 1.00 52.35  ? 2467 ARG A NH1   1 
ATOM   7272  N  NH2   . ARG A 1 2467 ? 164.036 213.941 180.641 1.00 61.69  ? 2467 ARG A NH2   1 
ATOM   7273  N  N     . ASN A 1 2468 ? 170.069 217.434 186.449 1.00 31.33  ? 2468 ASN A N     1 
ATOM   7274  C  CA    . ASN A 1 2468 ? 170.609 217.862 187.737 1.00 29.25  ? 2468 ASN A CA    1 
ATOM   7275  C  C     . ASN A 1 2468 ? 170.923 219.352 187.734 1.00 36.43  ? 2468 ASN A C     1 
ATOM   7276  O  O     . ASN A 1 2468 ? 170.679 220.049 188.726 1.00 44.33  ? 2468 ASN A O     1 
ATOM   7277  C  CB    . ASN A 1 2468 ? 171.861 217.053 188.076 1.00 26.18  ? 2468 ASN A CB    1 
ATOM   7278  C  CG    . ASN A 1 2468 ? 171.558 215.592 188.333 1.00 34.88  ? 2468 ASN A CG    1 
ATOM   7279  O  OD1   . ASN A 1 2468 ? 170.398 215.181 188.362 1.00 40.89  ? 2468 ASN A OD1   1 
ATOM   7280  N  ND2   . ASN A 1 2468 ? 172.604 214.796 188.520 1.00 35.56  ? 2468 ASN A ND2   1 
ATOM   7281  N  N     . VAL A 1 2469 ? 171.478 219.855 186.630 1.00 38.55  ? 2469 VAL A N     1 
ATOM   7282  C  CA    . VAL A 1 2469 ? 171.721 221.292 186.514 1.00 36.33  ? 2469 VAL A CA    1 
ATOM   7283  C  C     . VAL A 1 2469 ? 170.406 222.060 186.584 1.00 39.20  ? 2469 VAL A C     1 
ATOM   7284  O  O     . VAL A 1 2469 ? 170.307 223.100 187.249 1.00 41.91  ? 2469 VAL A O     1 
ATOM   7285  C  CB    . VAL A 1 2469 ? 172.493 221.606 185.219 1.00 34.47  ? 2469 VAL A CB    1 
ATOM   7286  C  CG1   . VAL A 1 2469 ? 172.687 223.104 185.072 1.00 37.41  ? 2469 VAL A CG1   1 
ATOM   7287  C  CG2   . VAL A 1 2469 ? 173.839 220.901 185.221 1.00 34.55  ? 2469 VAL A CG2   1 
ATOM   7288  N  N     . ALA A 1 2470 ? 169.373 221.556 185.903 1.00 40.04  ? 2470 ALA A N     1 
ATOM   7289  C  CA    . ALA A 1 2470 ? 168.063 222.201 185.962 1.00 38.23  ? 2470 ALA A CA    1 
ATOM   7290  C  C     . ALA A 1 2470 ? 167.497 222.179 187.378 1.00 45.58  ? 2470 ALA A C     1 
ATOM   7291  O  O     . ALA A 1 2470 ? 166.880 223.153 187.824 1.00 50.09  ? 2470 ALA A O     1 
ATOM   7292  C  CB    . ALA A 1 2470 ? 167.100 221.526 184.986 1.00 35.13  ? 2470 ALA A CB    1 
ATOM   7293  N  N     . GLN A 1 2471 ? 167.687 221.070 188.094 1.00 46.96  ? 2471 GLN A N     1 
ATOM   7294  C  CA    . GLN A 1 2471 ? 167.219 220.976 189.474 1.00 45.16  ? 2471 GLN A CA    1 
ATOM   7295  C  C     . GLN A 1 2471 ? 167.942 221.973 190.371 1.00 45.65  ? 2471 GLN A C     1 
ATOM   7296  O  O     . GLN A 1 2471 ? 167.325 222.598 191.242 1.00 51.15  ? 2471 GLN A O     1 
ATOM   7297  C  CB    . GLN A 1 2471 ? 167.406 219.549 189.990 1.00 44.67  ? 2471 GLN A CB    1 
ATOM   7298  C  CG    . GLN A 1 2471 ? 167.144 219.378 191.476 1.00 51.18  ? 2471 GLN A CG    1 
ATOM   7299  C  CD    . GLN A 1 2471 ? 165.666 219.396 191.811 1.00 55.14  ? 2471 GLN A CD    1 
ATOM   7300  O  OE1   . GLN A 1 2471 ? 164.888 218.605 191.279 1.00 56.97  ? 2471 GLN A OE1   1 
ATOM   7301  N  NE2   . GLN A 1 2471 ? 165.270 220.303 192.695 1.00 55.39  ? 2471 GLN A NE2   1 
ATOM   7302  N  N     . TYR A 1 2472 ? 169.256 222.124 190.183 1.00 44.73  ? 2472 TYR A N     1 
ATOM   7303  C  CA    . TYR A 1 2472 ? 170.001 223.129 190.937 1.00 44.95  ? 2472 TYR A CA    1 
ATOM   7304  C  C     . TYR A 1 2472 ? 169.484 224.529 190.635 1.00 50.00  ? 2472 TYR A C     1 
ATOM   7305  O  O     . TYR A 1 2472 ? 169.332 225.352 191.546 1.00 56.81  ? 2472 TYR A O     1 
ATOM   7306  C  CB    . TYR A 1 2472 ? 171.500 223.013 190.635 1.00 47.76  ? 2472 TYR A CB    1 
ATOM   7307  C  CG    . TYR A 1 2472 ? 172.405 224.003 191.360 1.00 47.91  ? 2472 TYR A CG    1 
ATOM   7308  C  CD1   . TYR A 1 2472 ? 172.394 225.360 191.050 1.00 52.23  ? 2472 TYR A CD1   1 
ATOM   7309  C  CD2   . TYR A 1 2472 ? 173.260 223.578 192.367 1.00 54.65  ? 2472 TYR A CD2   1 
ATOM   7310  C  CE1   . TYR A 1 2472 ? 173.213 226.254 191.711 1.00 57.67  ? 2472 TYR A CE1   1 
ATOM   7311  C  CE2   . TYR A 1 2472 ? 174.084 224.467 193.034 1.00 56.81  ? 2472 TYR A CE2   1 
ATOM   7312  C  CZ    . TYR A 1 2472 ? 174.055 225.803 192.702 1.00 57.55  ? 2472 TYR A CZ    1 
ATOM   7313  O  OH    . TYR A 1 2472 ? 174.870 226.692 193.363 1.00 59.86  ? 2472 TYR A OH    1 
ATOM   7314  N  N     . ASN A 1 2473 ? 169.212 224.819 189.361 1.00 49.64  ? 2473 ASN A N     1 
ATOM   7315  C  CA    . ASN A 1 2473 ? 168.673 226.129 189.009 1.00 48.45  ? 2473 ASN A CA    1 
ATOM   7316  C  C     . ASN A 1 2473 ? 167.313 226.357 189.657 1.00 49.68  ? 2473 ASN A C     1 
ATOM   7317  O  O     . ASN A 1 2473 ? 167.010 227.467 190.111 1.00 53.52  ? 2473 ASN A O     1 
ATOM   7318  C  CB    . ASN A 1 2473 ? 168.577 226.272 187.491 1.00 49.14  ? 2473 ASN A CB    1 
ATOM   7319  C  CG    . ASN A 1 2473 ? 169.862 226.782 186.873 1.00 56.72  ? 2473 ASN A CG    1 
ATOM   7320  O  OD1   . ASN A 1 2473 ? 170.825 227.086 187.577 1.00 59.40  ? 2473 ASN A OD1   1 
ATOM   7321  N  ND2   . ASN A 1 2473 ? 169.883 226.886 185.550 1.00 56.41  ? 2473 ASN A ND2   1 
ATOM   7322  N  N     . ALA A 1 2474 ? 166.477 225.318 189.704 1.00 52.66  ? 2474 ALA A N     1 
ATOM   7323  C  CA    . ALA A 1 2474 ? 165.168 225.446 190.337 1.00 54.87  ? 2474 ALA A CA    1 
ATOM   7324  C  C     . ALA A 1 2474 ? 165.283 225.655 191.842 1.00 58.15  ? 2474 ALA A C     1 
ATOM   7325  O  O     . ALA A 1 2474 ? 164.517 226.438 192.416 1.00 61.89  ? 2474 ALA A O     1 
ATOM   7326  C  CB    . ALA A 1 2474 ? 164.315 224.214 190.037 1.00 55.02  ? 2474 ALA A CB    1 
ATOM   7327  N  N     . ASN A 1 2475 ? 166.223 224.970 192.498 1.00 57.03  ? 2475 ASN A N     1 
ATOM   7328  C  CA    . ASN A 1 2475 ? 166.386 225.108 193.941 1.00 55.02  ? 2475 ASN A CA    1 
ATOM   7329  C  C     . ASN A 1 2475 ? 167.065 226.409 194.342 1.00 57.26  ? 2475 ASN A C     1 
ATOM   7330  O  O     . ASN A 1 2475 ? 166.985 226.797 195.512 1.00 65.27  ? 2475 ASN A O     1 
ATOM   7331  C  CB    . ASN A 1 2475 ? 167.177 223.924 194.502 1.00 53.08  ? 2475 ASN A CB    1 
ATOM   7332  C  CG    . ASN A 1 2475 ? 166.341 222.665 194.608 1.00 62.09  ? 2475 ASN A CG    1 
ATOM   7333  O  OD1   . ASN A 1 2475 ? 165.549 222.358 193.718 1.00 61.30  ? 2475 ASN A OD1   1 
ATOM   7334  N  ND2   . ASN A 1 2475 ? 166.514 221.928 195.699 1.00 61.29  ? 2475 ASN A ND2   1 
ATOM   7335  N  N     . HIS A 1 2476 ? 167.731 227.089 193.409 1.00 56.48  ? 2476 HIS A N     1 
ATOM   7336  C  CA    . HIS A 1 2476 ? 168.395 228.364 193.671 1.00 61.53  ? 2476 HIS A CA    1 
ATOM   7337  C  C     . HIS A 1 2476 ? 167.938 229.391 192.640 1.00 72.08  ? 2476 HIS A C     1 
ATOM   7338  O  O     . HIS A 1 2476 ? 168.709 229.777 191.750 1.00 76.40  ? 2476 HIS A O     1 
ATOM   7339  C  CB    . HIS A 1 2476 ? 169.914 228.211 193.647 1.00 62.46  ? 2476 HIS A CB    1 
ATOM   7340  C  CG    . HIS A 1 2476 ? 170.450 227.330 194.732 1.00 63.88  ? 2476 HIS A CG    1 
ATOM   7341  N  ND1   . HIS A 1 2476 ? 170.539 227.738 196.045 1.00 74.39  ? 2476 HIS A ND1   1 
ATOM   7342  C  CD2   . HIS A 1 2476 ? 170.928 226.064 194.698 1.00 60.36  ? 2476 HIS A CD2   1 
ATOM   7343  C  CE1   . HIS A 1 2476 ? 171.046 226.760 196.774 1.00 74.49  ? 2476 HIS A CE1   1 
ATOM   7344  N  NE2   . HIS A 1 2476 ? 171.291 225.733 195.980 1.00 64.04  ? 2476 HIS A NE2   1 
ATOM   7345  N  N     . PRO A 1 2477 ? 166.684 229.845 192.722 1.00 74.69  ? 2477 PRO A N     1 
ATOM   7346  C  CA    . PRO A 1 2477 ? 166.218 230.865 191.768 1.00 75.11  ? 2477 PRO A CA    1 
ATOM   7347  C  C     . PRO A 1 2477 ? 166.990 232.169 191.852 1.00 77.74  ? 2477 PRO A C     1 
ATOM   7348  O  O     . PRO A 1 2477 ? 167.182 232.834 190.827 1.00 73.59  ? 2477 PRO A O     1 
ATOM   7349  C  CB    . PRO A 1 2477 ? 164.742 231.058 192.151 1.00 68.95  ? 2477 PRO A CB    1 
ATOM   7350  C  CG    . PRO A 1 2477 ? 164.388 229.863 192.990 1.00 61.09  ? 2477 PRO A CG    1 
ATOM   7351  C  CD    . PRO A 1 2477 ? 165.645 229.494 193.702 1.00 66.56  ? 2477 PRO A CD    1 
ATOM   7352  N  N     . ASP A 1 2478 ? 167.439 232.554 193.049 1.00 78.22  ? 2478 ASP A N     1 
ATOM   7353  C  CA    . ASP A 1 2478 ? 168.163 233.809 193.211 1.00 82.06  ? 2478 ASP A CA    1 
ATOM   7354  C  C     . ASP A 1 2478 ? 169.540 233.728 192.559 1.00 85.56  ? 2478 ASP A C     1 
ATOM   7355  O  O     . ASP A 1 2478 ? 169.938 234.644 191.830 1.00 87.70  ? 2478 ASP A O     1 
ATOM   7356  C  CB    . ASP A 1 2478 ? 168.275 234.145 194.703 1.00 76.43  ? 2478 ASP A CB    1 
ATOM   7357  C  CG    . ASP A 1 2478 ? 168.992 235.466 194.978 1.00 85.95  ? 2478 ASP A CG    1 
ATOM   7358  O  OD1   . ASP A 1 2478 ? 169.574 236.081 194.060 1.00 94.00  ? 2478 ASP A OD1   1 
ATOM   7359  O  OD2   . ASP A 1 2478 ? 168.966 235.896 196.149 1.00 86.83  ? 2478 ASP A OD2   1 
ATOM   7360  N  N     . PHE A 1 2479 ? 170.266 232.628 192.791 1.00 83.29  ? 2479 PHE A N     1 
ATOM   7361  C  CA    . PHE A 1 2479 ? 171.616 232.415 192.266 1.00 83.00  ? 2479 PHE A CA    1 
ATOM   7362  C  C     . PHE A 1 2479 ? 171.598 231.232 191.302 1.00 80.73  ? 2479 PHE A C     1 
ATOM   7363  O  O     . PHE A 1 2479 ? 171.866 230.086 191.699 1.00 76.67  ? 2479 PHE A O     1 
ATOM   7364  C  CB    . PHE A 1 2479 ? 172.624 232.181 193.392 1.00 86.27  ? 2479 PHE A CB    1 
ATOM   7365  C  CG    . PHE A 1 2479 ? 172.921 233.405 194.219 1.00 92.14  ? 2479 PHE A CG    1 
ATOM   7366  C  CD1   . PHE A 1 2479 ? 172.378 234.642 193.898 1.00 92.43  ? 2479 PHE A CD1   1 
ATOM   7367  C  CD2   . PHE A 1 2479 ? 173.756 233.315 195.318 1.00 91.23  ? 2479 PHE A CD2   1 
ATOM   7368  C  CE1   . PHE A 1 2479 ? 172.661 235.760 194.664 1.00 87.32  ? 2479 PHE A CE1   1 
ATOM   7369  C  CE2   . PHE A 1 2479 ? 174.042 234.427 196.084 1.00 88.73  ? 2479 PHE A CE2   1 
ATOM   7370  C  CZ    . PHE A 1 2479 ? 173.494 235.650 195.758 1.00 87.15  ? 2479 PHE A CZ    1 
ATOM   7371  N  N     . PRO A 1 2480 ? 171.293 231.469 190.027 1.00 78.36  ? 2480 PRO A N     1 
ATOM   7372  C  CA    . PRO A 1 2480 ? 171.362 230.389 189.041 1.00 66.53  ? 2480 PRO A CA    1 
ATOM   7373  C  C     . PRO A 1 2480 ? 172.803 230.006 188.747 1.00 68.89  ? 2480 PRO A C     1 
ATOM   7374  O  O     . PRO A 1 2480 ? 173.743 230.782 188.940 1.00 77.62  ? 2480 PRO A O     1 
ATOM   7375  C  CB    . PRO A 1 2480 ? 170.680 230.984 187.806 1.00 67.75  ? 2480 PRO A CB    1 
ATOM   7376  C  CG    . PRO A 1 2480 ? 170.879 232.429 187.945 1.00 80.81  ? 2480 PRO A CG    1 
ATOM   7377  C  CD    . PRO A 1 2480 ? 170.842 232.731 189.420 1.00 80.59  ? 2480 PRO A CD    1 
ATOM   7378  N  N     . MET A 1 2481 ? 172.963 228.779 188.269 1.00 61.74  ? 2481 MET A N     1 
ATOM   7379  C  CA    . MET A 1 2481 ? 174.288 228.194 188.125 1.00 64.40  ? 2481 MET A CA    1 
ATOM   7380  C  C     . MET A 1 2481 ? 175.047 228.869 186.983 1.00 64.75  ? 2481 MET A C     1 
ATOM   7381  O  O     . MET A 1 2481 ? 174.524 229.023 185.874 1.00 60.63  ? 2481 MET A O     1 
ATOM   7382  C  CB    . MET A 1 2481 ? 174.147 226.688 187.905 1.00 57.61  ? 2481 MET A CB    1 
ATOM   7383  C  CG    . MET A 1 2481 ? 175.434 225.886 187.825 1.00 57.00  ? 2481 MET A CG    1 
ATOM   7384  S  SD    . MET A 1 2481 ? 175.022 224.130 187.670 1.00 71.44  ? 2481 MET A SD    1 
ATOM   7385  C  CE    . MET A 1 2481 ? 176.632 223.380 187.490 1.00 52.73  ? 2481 MET A CE    1 
ATOM   7386  N  N     . GLN A 1 2482 ? 176.286 229.264 187.256 1.00 68.55  ? 2482 GLN A N     1 
ATOM   7387  C  CA    . GLN A 1 2482 ? 177.061 230.097 186.350 1.00 70.82  ? 2482 GLN A CA    1 
ATOM   7388  C  C     . GLN A 1 2482 ? 177.831 229.235 185.343 1.00 65.70  ? 2482 GLN A C     1 
ATOM   7389  O  O     . GLN A 1 2482 ? 178.007 228.027 185.518 1.00 68.53  ? 2482 GLN A O     1 
ATOM   7390  C  CB    . GLN A 1 2482 ? 177.997 231.002 187.158 1.00 72.86  ? 2482 GLN A CB    1 
ATOM   7391  C  CG    . GLN A 1 2482 ? 178.767 232.035 186.357 1.00 77.45  ? 2482 GLN A CG    1 
ATOM   7392  C  CD    . GLN A 1 2482 ? 179.611 232.933 187.236 1.00 90.15  ? 2482 GLN A CD    1 
ATOM   7393  O  OE1   . GLN A 1 2482 ? 179.651 232.770 188.457 1.00 97.22  ? 2482 GLN A OE1   1 
ATOM   7394  N  NE2   . GLN A 1 2482 ? 180.293 233.889 186.618 1.00 92.15  ? 2482 GLN A NE2   1 
ATOM   7395  N  N     . ILE A 1 2483 ? 178.287 229.881 184.267 1.00 56.00  ? 2483 ILE A N     1 
ATOM   7396  C  CA    . ILE A 1 2483 ? 178.903 229.160 183.157 1.00 58.93  ? 2483 ILE A CA    1 
ATOM   7397  C  C     . ILE A 1 2483 ? 180.220 228.500 183.563 1.00 64.23  ? 2483 ILE A C     1 
ATOM   7398  O  O     . ILE A 1 2483 ? 180.578 227.448 183.023 1.00 62.91  ? 2483 ILE A O     1 
ATOM   7399  C  CB    . ILE A 1 2483 ? 179.087 230.104 181.954 1.00 65.02  ? 2483 ILE A CB    1 
ATOM   7400  C  CG1   . ILE A 1 2483 ? 179.226 229.299 180.660 1.00 61.58  ? 2483 ILE A CG1   1 
ATOM   7401  C  CG2   . ILE A 1 2483 ? 180.285 231.017 182.153 1.00 63.21  ? 2483 ILE A CG2   1 
ATOM   7402  C  CD1   . ILE A 1 2483 ? 178.007 228.466 180.320 1.00 47.13  ? 2483 ILE A CD1   1 
ATOM   7403  N  N     . GLU A 1 2484 ? 180.967 229.087 184.504 1.00 65.54  ? 2484 GLU A N     1 
ATOM   7404  C  CA    . GLU A 1 2484 ? 182.204 228.447 184.947 1.00 65.50  ? 2484 GLU A CA    1 
ATOM   7405  C  C     . GLU A 1 2484 ? 181.905 227.210 185.790 1.00 63.29  ? 2484 GLU A C     1 
ATOM   7406  O  O     . GLU A 1 2484 ? 182.515 226.147 185.597 1.00 60.16  ? 2484 GLU A O     1 
ATOM   7407  C  CB    . GLU A 1 2484 ? 183.076 229.449 185.713 1.00 68.56  ? 2484 GLU A CB    1 
ATOM   7408  C  CG    . GLU A 1 2484 ? 182.435 230.029 186.960 1.00 76.76  ? 2484 GLU A CG    1 
ATOM   7409  C  CD    . GLU A 1 2484 ? 183.447 230.495 187.982 1.00 92.90  ? 2484 GLU A CD    1 
ATOM   7410  O  OE1   . GLU A 1 2484 ? 184.615 230.722 187.604 1.00 101.36 ? 2484 GLU A OE1   1 
ATOM   7411  O  OE2   . GLU A 1 2484 ? 183.072 230.629 189.165 1.00 92.89  ? 2484 GLU A OE2   1 
ATOM   7412  N  N     . GLN A 1 2485 ? 180.950 227.326 186.716 1.00 62.18  ? 2485 GLN A N     1 
ATOM   7413  C  CA    . GLN A 1 2485 ? 180.514 226.169 187.487 1.00 55.88  ? 2485 GLN A CA    1 
ATOM   7414  C  C     . GLN A 1 2485 ? 179.905 225.109 186.582 1.00 52.30  ? 2485 GLN A C     1 
ATOM   7415  O  O     . GLN A 1 2485 ? 180.156 223.912 186.759 1.00 52.22  ? 2485 GLN A O     1 
ATOM   7416  C  CB    . GLN A 1 2485 ? 179.507 226.606 188.549 1.00 56.18  ? 2485 GLN A CB    1 
ATOM   7417  C  CG    . GLN A 1 2485 ? 179.352 225.622 189.688 1.00 56.82  ? 2485 GLN A CG    1 
ATOM   7418  C  CD    . GLN A 1 2485 ? 178.103 225.874 190.513 1.00 58.75  ? 2485 GLN A CD    1 
ATOM   7419  O  OE1   . GLN A 1 2485 ? 177.444 224.938 190.970 1.00 55.12  ? 2485 GLN A OE1   1 
ATOM   7420  N  NE2   . GLN A 1 2485 ? 177.764 227.146 190.699 1.00 64.13  ? 2485 GLN A NE2   1 
ATOM   7421  N  N     . LEU A 1 2486 ? 179.103 225.536 185.602 1.00 50.82  ? 2486 LEU A N     1 
ATOM   7422  C  CA    . LEU A 1 2486 ? 178.520 224.600 184.650 1.00 43.57  ? 2486 LEU A CA    1 
ATOM   7423  C  C     . LEU A 1 2486 ? 179.598 223.874 183.855 1.00 42.27  ? 2486 LEU A C     1 
ATOM   7424  O  O     . LEU A 1 2486 ? 179.504 222.663 183.647 1.00 45.52  ? 2486 LEU A O     1 
ATOM   7425  C  CB    . LEU A 1 2486 ? 177.554 225.333 183.716 1.00 44.32  ? 2486 LEU A CB    1 
ATOM   7426  C  CG    . LEU A 1 2486 ? 176.816 224.466 182.695 1.00 37.22  ? 2486 LEU A CG    1 
ATOM   7427  C  CD1   . LEU A 1 2486 ? 176.087 223.324 183.398 1.00 34.06  ? 2486 LEU A CD1   1 
ATOM   7428  C  CD2   . LEU A 1 2486 ? 175.824 225.309 181.894 1.00 41.96  ? 2486 LEU A CD2   1 
ATOM   7429  N  N     . GLU A 1 2487 ? 180.632 224.592 183.408 1.00 43.82  ? 2487 GLU A N     1 
ATOM   7430  C  CA    . GLU A 1 2487 ? 181.714 223.959 182.662 1.00 45.23  ? 2487 GLU A CA    1 
ATOM   7431  C  C     . GLU A 1 2487 ? 182.440 222.929 183.517 1.00 44.72  ? 2487 GLU A C     1 
ATOM   7432  O  O     . GLU A 1 2487 ? 182.670 221.795 183.077 1.00 43.78  ? 2487 GLU A O     1 
ATOM   7433  C  CB    . GLU A 1 2487 ? 182.691 225.025 182.159 1.00 50.30  ? 2487 GLU A CB    1 
ATOM   7434  C  CG    . GLU A 1 2487 ? 183.942 224.459 181.510 1.00 57.47  ? 2487 GLU A CG    1 
ATOM   7435  C  CD    . GLU A 1 2487 ? 185.124 225.410 181.601 1.00 74.16  ? 2487 GLU A CD    1 
ATOM   7436  O  OE1   . GLU A 1 2487 ? 185.653 225.596 182.719 1.00 74.46  ? 2487 GLU A OE1   1 
ATOM   7437  O  OE2   . GLU A 1 2487 ? 185.524 225.976 180.564 1.00 86.71  ? 2487 GLU A OE2   1 
ATOM   7438  N  N     . ARG A 1 2488 ? 182.806 223.305 184.748 1.00 46.20  ? 2488 ARG A N     1 
ATOM   7439  C  CA    . ARG A 1 2488 ? 183.501 222.364 185.626 1.00 43.26  ? 2488 ARG A CA    1 
ATOM   7440  C  C     . ARG A 1 2488 ? 182.649 221.128 185.891 1.00 41.66  ? 2488 ARG A C     1 
ATOM   7441  O  O     . ARG A 1 2488 ? 183.120 219.987 185.754 1.00 42.79  ? 2488 ARG A O     1 
ATOM   7442  C  CB    . ARG A 1 2488 ? 183.875 223.045 186.944 1.00 44.17  ? 2488 ARG A CB    1 
ATOM   7443  C  CG    . ARG A 1 2488 ? 184.911 224.144 186.809 1.00 52.80  ? 2488 ARG A CG    1 
ATOM   7444  C  CD    . ARG A 1 2488 ? 185.374 224.619 188.173 1.00 54.91  ? 2488 ARG A CD    1 
ATOM   7445  N  NE    . ARG A 1 2488 ? 184.293 224.587 189.150 1.00 57.68  ? 2488 ARG A NE    1 
ATOM   7446  C  CZ    . ARG A 1 2488 ? 183.823 225.650 189.786 1.00 60.35  ? 2488 ARG A CZ    1 
ATOM   7447  N  NH1   . ARG A 1 2488 ? 184.319 226.858 189.573 1.00 64.20  ? 2488 ARG A NH1   1 
ATOM   7448  N  NH2   . ARG A 1 2488 ? 182.833 225.498 190.660 1.00 50.08  ? 2488 ARG A NH2   1 
ATOM   7449  N  N     . TYR A 1 2489 ? 181.379 221.338 186.252 1.00 37.34  ? 2489 TYR A N     1 
ATOM   7450  C  CA    . TYR A 1 2489 ? 180.491 220.223 186.553 1.00 31.62  ? 2489 TYR A CA    1 
ATOM   7451  C  C     . TYR A 1 2489 ? 180.301 219.326 185.341 1.00 32.20  ? 2489 TYR A C     1 
ATOM   7452  O  O     . TYR A 1 2489 ? 180.311 218.099 185.466 1.00 33.98  ? 2489 TYR A O     1 
ATOM   7453  C  CB    . TYR A 1 2489 ? 179.139 220.740 187.046 1.00 31.54  ? 2489 TYR A CB    1 
ATOM   7454  C  CG    . TYR A 1 2489 ? 178.117 219.647 187.268 1.00 32.47  ? 2489 TYR A CG    1 
ATOM   7455  C  CD1   . TYR A 1 2489 ? 178.223 218.782 188.348 1.00 32.44  ? 2489 TYR A CD1   1 
ATOM   7456  C  CD2   . TYR A 1 2489 ? 177.057 219.469 186.390 1.00 31.29  ? 2489 TYR A CD2   1 
ATOM   7457  C  CE1   . TYR A 1 2489 ? 177.296 217.778 188.552 1.00 29.74  ? 2489 TYR A CE1   1 
ATOM   7458  C  CE2   . TYR A 1 2489 ? 176.127 218.466 186.586 1.00 32.05  ? 2489 TYR A CE2   1 
ATOM   7459  C  CZ    . TYR A 1 2489 ? 176.252 217.625 187.668 1.00 30.85  ? 2489 TYR A CZ    1 
ATOM   7460  O  OH    . TYR A 1 2489 ? 175.326 216.627 187.866 1.00 33.56  ? 2489 TYR A OH    1 
ATOM   7461  N  N     . ILE A 1 2490 ? 180.131 219.917 184.157 1.00 34.32  ? 2490 ILE A N     1 
ATOM   7462  C  CA    . ILE A 1 2490 ? 179.852 219.120 182.971 1.00 29.57  ? 2490 ILE A CA    1 
ATOM   7463  C  C     . ILE A 1 2490 ? 181.075 218.309 182.567 1.00 28.76  ? 2490 ILE A C     1 
ATOM   7464  O  O     . ILE A 1 2490 ? 180.956 217.135 182.207 1.00 32.16  ? 2490 ILE A O     1 
ATOM   7465  C  CB    . ILE A 1 2490 ? 179.349 220.019 181.828 1.00 28.83  ? 2490 ILE A CB    1 
ATOM   7466  C  CG1   . ILE A 1 2490 ? 177.893 220.414 182.074 1.00 28.56  ? 2490 ILE A CG1   1 
ATOM   7467  C  CG2   . ILE A 1 2490 ? 179.462 219.307 180.503 1.00 28.01  ? 2490 ILE A CG2   1 
ATOM   7468  C  CD1   . ILE A 1 2490 ? 176.966 219.234 182.262 1.00 27.11  ? 2490 ILE A CD1   1 
ATOM   7469  N  N     . GLN A 1 2491 ? 182.270 218.902 182.635 1.00 28.47  ? 2491 GLN A N     1 
ATOM   7470  C  CA    . GLN A 1 2491 ? 183.477 218.143 182.312 1.00 28.32  ? 2491 GLN A CA    1 
ATOM   7471  C  C     . GLN A 1 2491 ? 183.678 216.985 183.286 1.00 30.16  ? 2491 GLN A C     1 
ATOM   7472  O  O     . GLN A 1 2491 ? 183.939 215.841 182.876 1.00 31.70  ? 2491 GLN A O     1 
ATOM   7473  C  CB    . GLN A 1 2491 ? 184.695 219.067 182.316 1.00 29.96  ? 2491 GLN A CB    1 
ATOM   7474  C  CG    . GLN A 1 2491 ? 184.619 220.210 181.320 1.00 34.85  ? 2491 GLN A CG    1 
ATOM   7475  C  CD    . GLN A 1 2491 ? 185.986 220.712 180.903 1.00 46.69  ? 2491 GLN A CD    1 
ATOM   7476  O  OE1   . GLN A 1 2491 ? 186.215 221.028 179.735 1.00 53.39  ? 2491 GLN A OE1   1 
ATOM   7477  N  NE2   . GLN A 1 2491 ? 186.905 220.791 181.859 1.00 49.13  ? 2491 GLN A NE2   1 
ATOM   7478  N  N     . ARG A 1 2492 ? 183.547 217.261 184.589 1.00 28.44  ? 2492 ARG A N     1 
ATOM   7479  C  CA    . ARG A 1 2492 ? 183.750 216.207 185.577 1.00 24.18  ? 2492 ARG A CA    1 
ATOM   7480  C  C     . ARG A 1 2492 ? 182.703 215.108 185.442 1.00 25.24  ? 2492 ARG A C     1 
ATOM   7481  O  O     . ARG A 1 2492 ? 183.030 213.916 185.522 1.00 27.05  ? 2492 ARG A O     1 
ATOM   7482  C  CB    . ARG A 1 2492 ? 183.739 216.806 186.982 1.00 26.53  ? 2492 ARG A CB    1 
ATOM   7483  C  CG    . ARG A 1 2492 ? 185.016 217.549 187.331 1.00 29.57  ? 2492 ARG A CG    1 
ATOM   7484  C  CD    . ARG A 1 2492 ? 184.777 218.613 188.386 1.00 35.35  ? 2492 ARG A CD    1 
ATOM   7485  N  NE    . ARG A 1 2492 ? 186.027 219.142 188.920 1.00 43.49  ? 2492 ARG A NE    1 
ATOM   7486  C  CZ    . ARG A 1 2492 ? 186.815 219.998 188.285 1.00 46.84  ? 2492 ARG A CZ    1 
ATOM   7487  N  NH1   . ARG A 1 2492 ? 186.513 220.454 187.080 1.00 50.77  ? 2492 ARG A NH1   1 
ATOM   7488  N  NH2   . ARG A 1 2492 ? 187.933 220.410 188.874 1.00 49.57  ? 2492 ARG A NH2   1 
ATOM   7489  N  N     . TYR A 1 2493 ? 181.441 215.482 185.219 1.00 23.05  ? 2493 TYR A N     1 
ATOM   7490  C  CA    . TYR A 1 2493 ? 180.397 214.481 185.055 1.00 18.65  ? 2493 TYR A CA    1 
ATOM   7491  C  C     . TYR A 1 2493 ? 180.553 213.717 183.751 1.00 20.15  ? 2493 TYR A C     1 
ATOM   7492  O  O     . TYR A 1 2493 ? 180.166 212.552 183.678 1.00 25.89  ? 2493 TYR A O     1 
ATOM   7493  C  CB    . TYR A 1 2493 ? 179.015 215.129 185.119 1.00 20.20  ? 2493 TYR A CB    1 
ATOM   7494  C  CG    . TYR A 1 2493 ? 177.916 214.150 185.466 1.00 22.14  ? 2493 TYR A CG    1 
ATOM   7495  C  CD1   . TYR A 1 2493 ? 177.325 213.365 184.487 1.00 19.53  ? 2493 TYR A CD1   1 
ATOM   7496  C  CD2   . TYR A 1 2493 ? 177.471 214.011 186.772 1.00 24.68  ? 2493 TYR A CD2   1 
ATOM   7497  C  CE1   . TYR A 1 2493 ? 176.324 212.469 184.799 1.00 19.46  ? 2493 TYR A CE1   1 
ATOM   7498  C  CE2   . TYR A 1 2493 ? 176.468 213.118 187.093 1.00 26.81  ? 2493 TYR A CE2   1 
ATOM   7499  C  CZ    . TYR A 1 2493 ? 175.899 212.350 186.103 1.00 26.59  ? 2493 TYR A CZ    1 
ATOM   7500  O  OH    . TYR A 1 2493 ? 174.899 211.459 186.418 1.00 32.17  ? 2493 TYR A OH    1 
ATOM   7501  N  N     . LEU A 1 2494 ? 181.104 214.345 182.711 1.00 22.79  ? 2494 LEU A N     1 
ATOM   7502  C  CA    . LEU A 1 2494 ? 181.381 213.611 181.483 1.00 19.15  ? 2494 LEU A CA    1 
ATOM   7503  C  C     . LEU A 1 2494 ? 182.434 212.540 181.719 1.00 19.70  ? 2494 LEU A C     1 
ATOM   7504  O  O     . LEU A 1 2494 ? 182.286 211.405 181.253 1.00 20.50  ? 2494 LEU A O     1 
ATOM   7505  C  CB    . LEU A 1 2494 ? 181.823 214.573 180.382 1.00 17.70  ? 2494 LEU A CB    1 
ATOM   7506  C  CG    . LEU A 1 2494 ? 182.138 213.940 179.027 1.00 21.40  ? 2494 LEU A CG    1 
ATOM   7507  C  CD1   . LEU A 1 2494 ? 180.970 213.097 178.544 1.00 22.16  ? 2494 LEU A CD1   1 
ATOM   7508  C  CD2   . LEU A 1 2494 ? 182.478 215.013 178.012 1.00 30.48  ? 2494 LEU A CD2   1 
ATOM   7509  N  N     . VAL A 1 2495 ? 183.496 212.876 182.456 1.00 22.38  ? 2495 VAL A N     1 
ATOM   7510  C  CA    . VAL A 1 2495 ? 184.495 211.862 182.797 1.00 19.78  ? 2495 VAL A CA    1 
ATOM   7511  C  C     . VAL A 1 2495 ? 183.863 210.747 183.628 1.00 19.75  ? 2495 VAL A C     1 
ATOM   7512  O  O     . VAL A 1 2495 ? 184.083 209.552 183.375 1.00 22.13  ? 2495 VAL A O     1 
ATOM   7513  C  CB    . VAL A 1 2495 ? 185.686 212.509 183.529 1.00 21.94  ? 2495 VAL A CB    1 
ATOM   7514  C  CG1   . VAL A 1 2495 ? 186.605 211.441 184.098 1.00 21.38  ? 2495 VAL A CG1   1 
ATOM   7515  C  CG2   . VAL A 1 2495 ? 186.447 213.427 182.588 1.00 30.83  ? 2495 VAL A CG2   1 
ATOM   7516  N  N     . TYR A 1 2496 ? 183.055 211.124 184.622 1.00 21.11  ? 2496 TYR A N     1 
ATOM   7517  C  CA    . TYR A 1 2496 ? 182.403 210.148 185.491 1.00 20.35  ? 2496 TYR A CA    1 
ATOM   7518  C  C     . TYR A 1 2496 ? 181.470 209.230 184.703 1.00 20.48  ? 2496 TYR A C     1 
ATOM   7519  O  O     . TYR A 1 2496 ? 181.463 208.009 184.907 1.00 25.39  ? 2496 TYR A O     1 
ATOM   7520  C  CB    . TYR A 1 2496 ? 181.657 210.904 186.596 1.00 19.90  ? 2496 TYR A CB    1 
ATOM   7521  C  CG    . TYR A 1 2496 ? 180.577 210.150 187.339 1.00 20.40  ? 2496 TYR A CG    1 
ATOM   7522  C  CD1   . TYR A 1 2496 ? 179.257 210.186 186.911 1.00 21.40  ? 2496 TYR A CD1   1 
ATOM   7523  C  CD2   . TYR A 1 2496 ? 180.868 209.445 188.498 1.00 24.02  ? 2496 TYR A CD2   1 
ATOM   7524  C  CE1   . TYR A 1 2496 ? 178.266 209.517 187.597 1.00 22.13  ? 2496 TYR A CE1   1 
ATOM   7525  C  CE2   . TYR A 1 2496 ? 179.880 208.774 189.192 1.00 26.01  ? 2496 TYR A CE2   1 
ATOM   7526  C  CZ    . TYR A 1 2496 ? 178.582 208.811 188.735 1.00 25.42  ? 2496 TYR A CZ    1 
ATOM   7527  O  OH    . TYR A 1 2496 ? 177.592 208.144 189.419 1.00 26.91  ? 2496 TYR A OH    1 
ATOM   7528  N  N     . ALA A 1 2497 ? 180.689 209.801 183.785 1.00 17.29  ? 2497 ALA A N     1 
ATOM   7529  C  CA    . ALA A 1 2497 ? 179.756 209.018 182.985 1.00 13.46  ? 2497 ALA A CA    1 
ATOM   7530  C  C     . ALA A 1 2497 ? 180.487 208.117 182.003 1.00 17.39  ? 2497 ALA A C     1 
ATOM   7531  O  O     . ALA A 1 2497 ? 180.052 206.989 181.753 1.00 21.00  ? 2497 ALA A O     1 
ATOM   7532  C  CB    . ALA A 1 2497 ? 178.794 209.947 182.247 1.00 16.90  ? 2497 ALA A CB    1 
ATOM   7533  N  N     . ILE A 1 2498 ? 181.596 208.592 181.431 1.00 18.77  ? 2498 ILE A N     1 
ATOM   7534  C  CA    . ILE A 1 2498 ? 182.398 207.733 180.566 1.00 17.44  ? 2498 ILE A CA    1 
ATOM   7535  C  C     . ILE A 1 2498 ? 182.903 206.531 181.348 1.00 17.12  ? 2498 ILE A C     1 
ATOM   7536  O  O     . ILE A 1 2498 ? 182.822 205.386 180.882 1.00 17.80  ? 2498 ILE A O     1 
ATOM   7537  C  CB    . ILE A 1 2498 ? 183.560 208.531 179.945 1.00 16.13  ? 2498 ILE A CB    1 
ATOM   7538  C  CG1   . ILE A 1 2498 ? 183.049 209.446 178.834 1.00 19.73  ? 2498 ILE A CG1   1 
ATOM   7539  C  CG2   . ILE A 1 2498 ? 184.628 207.593 179.404 1.00 14.79  ? 2498 ILE A CG2   1 
ATOM   7540  C  CD1   . ILE A 1 2498 ? 184.100 210.388 178.307 1.00 24.03  ? 2498 ILE A CD1   1 
ATOM   7541  N  N     . LEU A 1 2499 ? 183.406 206.768 182.562 1.00 20.28  ? 2499 LEU A N     1 
ATOM   7542  C  CA    . LEU A 1 2499 ? 183.901 205.664 183.378 1.00 19.88  ? 2499 LEU A CA    1 
ATOM   7543  C  C     . LEU A 1 2499 ? 182.792 204.680 183.728 1.00 16.83  ? 2499 LEU A C     1 
ATOM   7544  O  O     . LEU A 1 2499 ? 182.994 203.461 183.671 1.00 18.01  ? 2499 LEU A O     1 
ATOM   7545  C  CB    . LEU A 1 2499 ? 184.557 206.198 184.649 1.00 21.78  ? 2499 LEU A CB    1 
ATOM   7546  C  CG    . LEU A 1 2499 ? 186.081 206.250 184.598 1.00 27.34  ? 2499 LEU A CG    1 
ATOM   7547  C  CD1   . LEU A 1 2499 ? 186.625 206.911 185.841 1.00 33.86  ? 2499 LEU A CD1   1 
ATOM   7548  C  CD2   . LEU A 1 2499 ? 186.647 204.850 184.442 1.00 29.75  ? 2499 LEU A CD2   1 
ATOM   7549  N  N     . TRP A 1 2500 ? 181.613 205.184 184.096 1.00 16.46  ? 2500 TRP A N     1 
ATOM   7550  C  CA    . TRP A 1 2500 ? 180.546 204.292 184.536 1.00 16.03  ? 2500 TRP A CA    1 
ATOM   7551  C  C     . TRP A 1 2500 ? 179.762 203.665 183.391 1.00 17.02  ? 2500 TRP A C     1 
ATOM   7552  O  O     . TRP A 1 2500 ? 179.008 202.716 183.632 1.00 22.83  ? 2500 TRP A O     1 
ATOM   7553  C  CB    . TRP A 1 2500 ? 179.584 205.029 185.467 1.00 14.69  ? 2500 TRP A CB    1 
ATOM   7554  C  CG    . TRP A 1 2500 ? 179.981 204.931 186.903 1.00 16.88  ? 2500 TRP A CG    1 
ATOM   7555  C  CD1   . TRP A 1 2500 ? 180.381 205.949 187.711 1.00 17.54  ? 2500 TRP A CD1   1 
ATOM   7556  C  CD2   . TRP A 1 2500 ? 180.032 203.740 187.699 1.00 20.10  ? 2500 TRP A CD2   1 
ATOM   7557  N  NE1   . TRP A 1 2500 ? 180.669 205.472 188.967 1.00 25.17  ? 2500 TRP A NE1   1 
ATOM   7558  C  CE2   . TRP A 1 2500 ? 180.463 204.118 188.985 1.00 22.22  ? 2500 TRP A CE2   1 
ATOM   7559  C  CE3   . TRP A 1 2500 ? 179.752 202.394 187.450 1.00 16.85  ? 2500 TRP A CE3   1 
ATOM   7560  C  CZ2   . TRP A 1 2500 ? 180.623 203.198 190.018 1.00 18.83  ? 2500 TRP A CZ2   1 
ATOM   7561  C  CZ3   . TRP A 1 2500 ? 179.909 201.483 188.477 1.00 18.67  ? 2500 TRP A CZ3   1 
ATOM   7562  C  CH2   . TRP A 1 2500 ? 180.340 201.889 189.745 1.00 19.40  ? 2500 TRP A CH2   1 
ATOM   7563  N  N     . SER A 1 2501 ? 179.912 204.158 182.165 1.00 16.84  ? 2501 SER A N     1 
ATOM   7564  C  CA    . SER A 1 2501 ? 179.241 203.576 181.012 1.00 13.38  ? 2501 SER A CA    1 
ATOM   7565  C  C     . SER A 1 2501 ? 180.131 202.626 180.228 1.00 19.53  ? 2501 SER A C     1 
ATOM   7566  O  O     . SER A 1 2501 ? 179.648 201.616 179.709 1.00 23.86  ? 2501 SER A O     1 
ATOM   7567  C  CB    . SER A 1 2501 ? 178.741 204.682 180.079 1.00 12.35  ? 2501 SER A CB    1 
ATOM   7568  O  OG    . SER A 1 2501 ? 177.897 205.586 180.768 1.00 20.24  ? 2501 SER A OG    1 
ATOM   7569  N  N     . LEU A 1 2502 ? 181.425 202.928 180.129 1.00 18.88  ? 2502 LEU A N     1 
ATOM   7570  C  CA    . LEU A 1 2502 ? 182.339 202.109 179.349 1.00 16.00  ? 2502 LEU A CA    1 
ATOM   7571  C  C     . LEU A 1 2502 ? 182.970 200.984 180.157 1.00 19.77  ? 2502 LEU A C     1 
ATOM   7572  O  O     . LEU A 1 2502 ? 183.634 200.122 179.572 1.00 31.21  ? 2502 LEU A O     1 
ATOM   7573  C  CB    . LEU A 1 2502 ? 183.430 202.995 178.745 1.00 16.69  ? 2502 LEU A CB    1 
ATOM   7574  C  CG    . LEU A 1 2502 ? 183.074 203.797 177.489 1.00 14.25  ? 2502 LEU A CG    1 
ATOM   7575  C  CD1   . LEU A 1 2502 ? 182.088 204.919 177.767 1.00 17.16  ? 2502 LEU A CD1   1 
ATOM   7576  C  CD2   . LEU A 1 2502 ? 184.337 204.371 176.913 1.00 17.41  ? 2502 LEU A CD2   1 
ATOM   7577  N  N     . SER A 1 2503 ? 182.779 200.967 181.480 1.00 18.82  ? 2503 SER A N     1 
ATOM   7578  C  CA    . SER A 1 2503 ? 183.320 199.897 182.309 1.00 19.60  ? 2503 SER A CA    1 
ATOM   7579  C  C     . SER A 1 2503 ? 182.338 199.452 183.388 1.00 21.10  ? 2503 SER A C     1 
ATOM   7580  O  O     . SER A 1 2503 ? 182.760 198.860 184.388 1.00 25.63  ? 2503 SER A O     1 
ATOM   7581  C  CB    . SER A 1 2503 ? 184.637 200.325 182.962 1.00 24.63  ? 2503 SER A CB    1 
ATOM   7582  O  OG    . SER A 1 2503 ? 184.408 201.266 183.996 1.00 30.71  ? 2503 SER A OG    1 
ATOM   7583  N  N     . GLY A 1 2504 ? 181.044 199.725 183.215 1.00 17.81  ? 2504 GLY A N     1 
ATOM   7584  C  CA    . GLY A 1 2504 ? 180.070 199.334 184.219 1.00 16.19  ? 2504 GLY A CA    1 
ATOM   7585  C  C     . GLY A 1 2504 ? 179.928 197.834 184.371 1.00 20.45  ? 2504 GLY A C     1 
ATOM   7586  O  O     . GLY A 1 2504 ? 179.683 197.341 185.476 1.00 26.87  ? 2504 GLY A O     1 
ATOM   7587  N  N     . ASP A 1 2505 ? 180.082 197.088 183.276 1.00 17.68  ? 2505 ASP A N     1 
ATOM   7588  C  CA    . ASP A 1 2505 ? 179.911 195.641 183.274 1.00 16.39  ? 2505 ASP A CA    1 
ATOM   7589  C  C     . ASP A 1 2505 ? 181.237 194.898 183.397 1.00 21.32  ? 2505 ASP A C     1 
ATOM   7590  O  O     . ASP A 1 2505 ? 181.389 193.805 182.842 1.00 28.99  ? 2505 ASP A O     1 
ATOM   7591  C  CB    . ASP A 1 2505 ? 179.173 195.200 182.011 1.00 17.41  ? 2505 ASP A CB    1 
ATOM   7592  C  CG    . ASP A 1 2505 ? 179.820 195.726 180.747 1.00 23.97  ? 2505 ASP A CG    1 
ATOM   7593  O  OD1   . ASP A 1 2505 ? 180.603 196.694 180.839 1.00 23.99  ? 2505 ASP A OD1   1 
ATOM   7594  O  OD2   . ASP A 1 2505 ? 179.546 195.172 179.662 1.00 29.38  ? 2505 ASP A OD2   1 
ATOM   7595  N  N     . SER A 1 2506 ? 182.199 195.468 184.117 1.00 19.97  ? 2506 SER A N     1 
ATOM   7596  C  CA    . SER A 1 2506 ? 183.504 194.854 184.302 1.00 24.68  ? 2506 SER A CA    1 
ATOM   7597  C  C     . SER A 1 2506 ? 183.886 194.901 185.774 1.00 26.91  ? 2506 SER A C     1 
ATOM   7598  O  O     . SER A 1 2506 ? 183.305 195.647 186.566 1.00 26.75  ? 2506 SER A O     1 
ATOM   7599  C  CB    . SER A 1 2506 ? 184.578 195.547 183.453 1.00 27.38  ? 2506 SER A CB    1 
ATOM   7600  O  OG    . SER A 1 2506 ? 184.449 196.956 183.519 1.00 27.84  ? 2506 SER A OG    1 
ATOM   7601  N  N     . ARG A 1 2507 ? 184.876 194.086 186.133 1.00 30.12  ? 2507 ARG A N     1 
ATOM   7602  C  CA    . ARG A 1 2507 ? 185.325 194.004 187.512 1.00 30.84  ? 2507 ARG A CA    1 
ATOM   7603  C  C     . ARG A 1 2507 ? 186.001 195.307 187.937 1.00 35.12  ? 2507 ARG A C     1 
ATOM   7604  O  O     . ARG A 1 2507 ? 186.265 196.201 187.127 1.00 41.41  ? 2507 ARG A O     1 
ATOM   7605  C  CB    . ARG A 1 2507 ? 186.284 192.828 187.694 1.00 33.34  ? 2507 ARG A CB    1 
ATOM   7606  C  CG    . ARG A 1 2507 ? 185.740 191.501 187.195 1.00 39.48  ? 2507 ARG A CG    1 
ATOM   7607  C  CD    . ARG A 1 2507 ? 186.744 190.380 187.407 1.00 54.46  ? 2507 ARG A CD    1 
ATOM   7608  N  NE    . ARG A 1 2507 ? 188.101 190.790 187.069 1.00 59.13  ? 2507 ARG A NE    1 
ATOM   7609  C  CZ    . ARG A 1 2507 ? 188.608 190.767 185.844 1.00 54.79  ? 2507 ARG A CZ    1 
ATOM   7610  N  NH1   . ARG A 1 2507 ? 187.895 190.357 184.808 1.00 55.20  ? 2507 ARG A NH1   1 
ATOM   7611  N  NH2   . ARG A 1 2507 ? 189.862 191.166 185.654 1.00 48.07  ? 2507 ARG A NH2   1 
ATOM   7612  N  N     . LEU A 1 2508 ? 186.281 195.407 189.239 1.00 31.85  ? 2508 LEU A N     1 
ATOM   7613  C  CA    . LEU A 1 2508 ? 186.904 196.615 189.771 1.00 34.54  ? 2508 LEU A CA    1 
ATOM   7614  C  C     . LEU A 1 2508 ? 188.303 196.824 189.208 1.00 38.68  ? 2508 LEU A C     1 
ATOM   7615  O  O     . LEU A 1 2508 ? 188.740 197.969 189.043 1.00 42.33  ? 2508 LEU A O     1 
ATOM   7616  C  CB    . LEU A 1 2508 ? 186.952 196.562 191.299 1.00 37.22  ? 2508 LEU A CB    1 
ATOM   7617  C  CG    . LEU A 1 2508 ? 185.675 196.898 192.077 1.00 37.93  ? 2508 LEU A CG    1 
ATOM   7618  C  CD1   . LEU A 1 2508 ? 184.630 195.796 191.960 1.00 41.63  ? 2508 LEU A CD1   1 
ATOM   7619  C  CD2   . LEU A 1 2508 ? 186.003 197.177 193.536 1.00 35.84  ? 2508 LEU A CD2   1 
ATOM   7620  N  N     . LYS A 1 2509 ? 189.018 195.737 188.905 1.00 37.61  ? 2509 LYS A N     1 
ATOM   7621  C  CA    . LYS A 1 2509 ? 190.351 195.869 188.326 1.00 36.60  ? 2509 LYS A CA    1 
ATOM   7622  C  C     . LYS A 1 2509 ? 190.301 196.598 186.989 1.00 42.91  ? 2509 LYS A C     1 
ATOM   7623  O  O     . LYS A 1 2509 ? 191.093 197.515 186.742 1.00 47.93  ? 2509 LYS A O     1 
ATOM   7624  C  CB    . LYS A 1 2509 ? 190.989 194.490 188.159 1.00 37.92  ? 2509 LYS A CB    1 
ATOM   7625  C  CG    . LYS A 1 2509 ? 192.192 194.479 187.230 1.00 50.89  ? 2509 LYS A CG    1 
ATOM   7626  C  CD    . LYS A 1 2509 ? 192.444 193.091 186.660 1.00 63.54  ? 2509 LYS A CD    1 
ATOM   7627  C  CE    . LYS A 1 2509 ? 193.786 193.021 185.946 1.00 65.01  ? 2509 LYS A CE    1 
ATOM   7628  N  NZ    . LYS A 1 2509 ? 193.756 192.090 184.782 1.00 52.04  ? 2509 LYS A NZ    1 
ATOM   7629  N  N     . MET A 1 2510 ? 189.359 196.226 186.122 1.00 40.28  ? 2510 MET A N     1 
ATOM   7630  C  CA    . MET A 1 2510 ? 189.291 196.864 184.813 1.00 36.03  ? 2510 MET A CA    1 
ATOM   7631  C  C     . MET A 1 2510 ? 188.656 198.245 184.878 1.00 35.21  ? 2510 MET A C     1 
ATOM   7632  O  O     . MET A 1 2510 ? 188.971 199.102 184.046 1.00 39.29  ? 2510 MET A O     1 
ATOM   7633  C  CB    . MET A 1 2510 ? 188.548 195.964 183.832 1.00 27.75  ? 2510 MET A CB    1 
ATOM   7634  C  CG    . MET A 1 2510 ? 188.881 194.504 184.030 1.00 39.88  ? 2510 MET A CG    1 
ATOM   7635  S  SD    . MET A 1 2510 ? 190.403 194.089 183.164 1.00 59.52  ? 2510 MET A SD    1 
ATOM   7636  C  CE    . MET A 1 2510 ? 189.793 193.842 181.510 1.00 48.68  ? 2510 MET A CE    1 
ATOM   7637  N  N     . ARG A 1 2511 ? 187.783 198.492 185.857 1.00 31.82  ? 2511 ARG A N     1 
ATOM   7638  C  CA    . ARG A 1 2511 ? 187.344 199.860 186.104 1.00 30.09  ? 2511 ARG A CA    1 
ATOM   7639  C  C     . ARG A 1 2511 ? 188.528 200.743 186.479 1.00 34.07  ? 2511 ARG A C     1 
ATOM   7640  O  O     . ARG A 1 2511 ? 188.656 201.871 185.986 1.00 36.47  ? 2511 ARG A O     1 
ATOM   7641  C  CB    . ARG A 1 2511 ? 186.284 199.885 187.205 1.00 30.39  ? 2511 ARG A CB    1 
ATOM   7642  C  CG    . ARG A 1 2511 ? 184.976 199.211 186.830 1.00 25.14  ? 2511 ARG A CG    1 
ATOM   7643  C  CD    . ARG A 1 2511 ? 184.033 199.145 188.020 1.00 22.20  ? 2511 ARG A CD    1 
ATOM   7644  N  NE    . ARG A 1 2511 ? 182.785 198.466 187.693 1.00 21.06  ? 2511 ARG A NE    1 
ATOM   7645  C  CZ    . ARG A 1 2511 ? 181.793 198.271 188.550 1.00 20.82  ? 2511 ARG A CZ    1 
ATOM   7646  N  NH1   . ARG A 1 2511 ? 181.868 198.693 189.801 1.00 23.14  ? 2511 ARG A NH1   1 
ATOM   7647  N  NH2   . ARG A 1 2511 ? 180.696 197.642 188.141 1.00 18.68  ? 2511 ARG A NH2   1 
ATOM   7648  N  N     . ALA A 1 2512 ? 189.415 200.233 187.336 1.00 36.15  ? 2512 ALA A N     1 
ATOM   7649  C  CA    . ALA A 1 2512 ? 190.626 200.971 187.678 1.00 39.08  ? 2512 ALA A CA    1 
ATOM   7650  C  C     . ALA A 1 2512 ? 191.524 201.157 186.461 1.00 43.26  ? 2512 ALA A C     1 
ATOM   7651  O  O     . ALA A 1 2512 ? 192.138 202.215 186.293 1.00 50.73  ? 2512 ALA A O     1 
ATOM   7652  C  CB    . ALA A 1 2512 ? 191.378 200.253 188.798 1.00 37.59  ? 2512 ALA A CB    1 
ATOM   7653  N  N     . GLU A 1 2513 ? 191.624 200.134 185.610 1.00 38.37  ? 2513 GLU A N     1 
ATOM   7654  C  CA    . GLU A 1 2513 ? 192.441 200.248 184.403 1.00 39.41  ? 2513 GLU A CA    1 
ATOM   7655  C  C     . GLU A 1 2513 ? 191.909 201.337 183.475 1.00 38.52  ? 2513 GLU A C     1 
ATOM   7656  O  O     . GLU A 1 2513 ? 192.678 202.147 182.942 1.00 44.17  ? 2513 GLU A O     1 
ATOM   7657  C  CB    . GLU A 1 2513 ? 192.494 198.905 183.674 1.00 41.26  ? 2513 GLU A CB    1 
ATOM   7658  C  CG    . GLU A 1 2513 ? 193.232 197.812 184.426 1.00 57.59  ? 2513 GLU A CG    1 
ATOM   7659  C  CD    . GLU A 1 2513 ? 193.928 196.836 183.499 1.00 67.17  ? 2513 GLU A CD    1 
ATOM   7660  O  OE1   . GLU A 1 2513 ? 193.275 196.346 182.553 1.00 61.54  ? 2513 GLU A OE1   1 
ATOM   7661  O  OE2   . GLU A 1 2513 ? 195.126 196.558 183.715 1.00 77.29  ? 2513 GLU A OE2   1 
ATOM   7662  N  N     . LEU A 1 2514 ? 190.591 201.366 183.266 1.00 36.44  ? 2514 LEU A N     1 
ATOM   7663  C  CA    . LEU A 1 2514 ? 190.003 202.402 182.423 1.00 34.11  ? 2514 LEU A CA    1 
ATOM   7664  C  C     . LEU A 1 2514 ? 190.173 203.781 183.046 1.00 33.66  ? 2514 LEU A C     1 
ATOM   7665  O  O     . LEU A 1 2514 ? 190.427 204.760 182.336 1.00 37.64  ? 2514 LEU A O     1 
ATOM   7666  C  CB    . LEU A 1 2514 ? 188.526 202.109 182.164 1.00 31.22  ? 2514 LEU A CB    1 
ATOM   7667  C  CG    . LEU A 1 2514 ? 187.876 203.044 181.140 1.00 29.57  ? 2514 LEU A CG    1 
ATOM   7668  C  CD1   . LEU A 1 2514 ? 188.446 202.795 179.753 1.00 31.82  ? 2514 LEU A CD1   1 
ATOM   7669  C  CD2   . LEU A 1 2514 ? 186.366 202.895 181.133 1.00 22.46  ? 2514 LEU A CD2   1 
ATOM   7670  N  N     . GLY A 1 2515 ? 190.032 203.879 184.370 1.00 32.60  ? 2515 GLY A N     1 
ATOM   7671  C  CA    . GLY A 1 2515 ? 190.279 205.149 185.032 1.00 34.79  ? 2515 GLY A CA    1 
ATOM   7672  C  C     . GLY A 1 2515 ? 191.709 205.625 184.861 1.00 41.30  ? 2515 GLY A C     1 
ATOM   7673  O  O     . GLY A 1 2515 ? 191.956 206.811 184.635 1.00 47.56  ? 2515 GLY A O     1 
ATOM   7674  N  N     . GLU A 1 2516 ? 192.669 204.703 184.964 1.00 39.26  ? 2516 GLU A N     1 
ATOM   7675  C  CA    . GLU A 1 2516 ? 194.070 205.060 184.764 1.00 42.29  ? 2516 GLU A CA    1 
ATOM   7676  C  C     . GLU A 1 2516 ? 194.326 205.516 183.334 1.00 45.49  ? 2516 GLU A C     1 
ATOM   7677  O  O     . GLU A 1 2516 ? 195.044 206.496 183.105 1.00 54.46  ? 2516 GLU A O     1 
ATOM   7678  C  CB    . GLU A 1 2516 ? 194.967 203.874 185.117 1.00 42.63  ? 2516 GLU A CB    1 
ATOM   7679  C  CG    . GLU A 1 2516 ? 195.030 203.564 186.602 1.00 48.40  ? 2516 GLU A CG    1 
ATOM   7680  C  CD    . GLU A 1 2516 ? 195.293 202.097 186.879 1.00 58.16  ? 2516 GLU A CD    1 
ATOM   7681  O  OE1   . GLU A 1 2516 ? 195.802 201.402 185.974 1.00 57.92  ? 2516 GLU A OE1   1 
ATOM   7682  O  OE2   . GLU A 1 2516 ? 194.987 201.638 187.999 1.00 58.45  ? 2516 GLU A OE2   1 
ATOM   7683  N  N     . TYR A 1 2517 ? 193.746 204.817 182.354 1.00 40.09  ? 2517 TYR A N     1 
ATOM   7684  C  CA    . TYR A 1 2517 ? 193.914 205.232 180.965 1.00 39.65  ? 2517 TYR A CA    1 
ATOM   7685  C  C     . TYR A 1 2517 ? 193.311 206.613 180.727 1.00 41.90  ? 2517 TYR A C     1 
ATOM   7686  O  O     . TYR A 1 2517 ? 193.916 207.458 180.052 1.00 52.69  ? 2517 TYR A O     1 
ATOM   7687  C  CB    . TYR A 1 2517 ? 193.286 204.204 180.025 1.00 39.02  ? 2517 TYR A CB    1 
ATOM   7688  C  CG    . TYR A 1 2517 ? 193.366 204.591 178.565 1.00 45.17  ? 2517 TYR A CG    1 
ATOM   7689  C  CD1   . TYR A 1 2517 ? 194.544 204.430 177.850 1.00 48.59  ? 2517 TYR A CD1   1 
ATOM   7690  C  CD2   . TYR A 1 2517 ? 192.266 205.119 177.904 1.00 41.41  ? 2517 TYR A CD2   1 
ATOM   7691  C  CE1   . TYR A 1 2517 ? 194.626 204.782 176.518 1.00 47.56  ? 2517 TYR A CE1   1 
ATOM   7692  C  CE2   . TYR A 1 2517 ? 192.340 205.474 176.571 1.00 43.07  ? 2517 TYR A CE2   1 
ATOM   7693  C  CZ    . TYR A 1 2517 ? 193.521 205.304 175.884 1.00 46.22  ? 2517 TYR A CZ    1 
ATOM   7694  O  OH    . TYR A 1 2517 ? 193.597 205.656 174.556 1.00 46.70  ? 2517 TYR A OH    1 
ATOM   7695  N  N     . ILE A 1 2518 ? 192.123 206.862 181.283 1.00 38.85  ? 2518 ILE A N     1 
ATOM   7696  C  CA    . ILE A 1 2518 ? 191.497 208.173 181.145 1.00 37.32  ? 2518 ILE A CA    1 
ATOM   7697  C  C     . ILE A 1 2518 ? 192.377 209.245 181.771 1.00 42.15  ? 2518 ILE A C     1 
ATOM   7698  O  O     . ILE A 1 2518 ? 192.623 210.296 181.167 1.00 49.64  ? 2518 ILE A O     1 
ATOM   7699  C  CB    . ILE A 1 2518 ? 190.088 208.160 181.765 1.00 34.07  ? 2518 ILE A CB    1 
ATOM   7700  C  CG1   . ILE A 1 2518 ? 189.103 207.457 180.831 1.00 38.83  ? 2518 ILE A CG1   1 
ATOM   7701  C  CG2   . ILE A 1 2518 ? 189.619 209.574 182.068 1.00 32.37  ? 2518 ILE A CG2   1 
ATOM   7702  C  CD1   . ILE A 1 2518 ? 187.712 207.328 181.403 1.00 30.98  ? 2518 ILE A CD1   1 
ATOM   7703  N  N     . ARG A 1 2519 ? 192.890 208.984 182.977 1.00 44.14  ? 2519 ARG A N     1 
ATOM   7704  C  CA    . ARG A 1 2519 ? 193.793 209.929 183.627 1.00 48.40  ? 2519 ARG A CA    1 
ATOM   7705  C  C     . ARG A 1 2519 ? 195.024 210.190 182.770 1.00 51.23  ? 2519 ARG A C     1 
ATOM   7706  O  O     . ARG A 1 2519 ? 195.551 211.308 182.749 1.00 53.88  ? 2519 ARG A O     1 
ATOM   7707  C  CB    . ARG A 1 2519 ? 194.199 209.397 185.001 1.00 46.11  ? 2519 ARG A CB    1 
ATOM   7708  C  CG    . ARG A 1 2519 ? 194.957 210.392 185.863 1.00 50.66  ? 2519 ARG A CG    1 
ATOM   7709  C  CD    . ARG A 1 2519 ? 195.408 209.755 187.168 1.00 52.67  ? 2519 ARG A CD    1 
ATOM   7710  N  NE    . ARG A 1 2519 ? 194.315 209.611 188.123 1.00 52.21  ? 2519 ARG A NE    1 
ATOM   7711  C  CZ    . ARG A 1 2519 ? 193.858 210.589 188.894 1.00 51.13  ? 2519 ARG A CZ    1 
ATOM   7712  N  NH1   . ARG A 1 2519 ? 194.373 211.806 188.845 1.00 49.71  ? 2519 ARG A NH1   1 
ATOM   7713  N  NH2   . ARG A 1 2519 ? 192.861 210.337 189.737 1.00 51.58  ? 2519 ARG A NH2   1 
ATOM   7714  N  N     . ARG A 1 2520 ? 195.498 209.165 182.061 1.00 49.66  ? 2520 ARG A N     1 
ATOM   7715  C  CA    . ARG A 1 2520 ? 196.629 209.353 181.160 1.00 49.41  ? 2520 ARG A CA    1 
ATOM   7716  C  C     . ARG A 1 2520 ? 196.268 210.263 179.991 1.00 51.22  ? 2520 ARG A C     1 
ATOM   7717  O  O     . ARG A 1 2520 ? 197.073 211.111 179.591 1.00 55.64  ? 2520 ARG A O     1 
ATOM   7718  C  CB    . ARG A 1 2520 ? 197.126 208.002 180.645 1.00 49.99  ? 2520 ARG A CB    1 
ATOM   7719  C  CG    . ARG A 1 2520 ? 197.930 207.204 181.656 1.00 56.84  ? 2520 ARG A CG    1 
ATOM   7720  C  CD    . ARG A 1 2520 ? 199.027 206.341 181.019 1.00 68.23  ? 2520 ARG A CD    1 
ATOM   7721  N  NE    . ARG A 1 2520 ? 198.526 205.204 180.251 1.00 75.36  ? 2520 ARG A NE    1 
ATOM   7722  C  CZ    . ARG A 1 2520 ? 198.153 205.246 178.978 1.00 74.87  ? 2520 ARG A CZ    1 
ATOM   7723  N  NH1   . ARG A 1 2520 ? 198.263 206.351 178.258 1.00 69.40  ? 2520 ARG A NH1   1 
ATOM   7724  N  NH2   . ARG A 1 2520 ? 197.679 204.144 178.405 1.00 69.11  ? 2520 ARG A NH2   1 
ATOM   7725  N  N     . ILE A 1 2521 ? 195.068 210.107 179.429 1.00 50.57  ? 2521 ILE A N     1 
ATOM   7726  C  CA    . ILE A 1 2521 ? 194.733 210.811 178.194 1.00 49.84  ? 2521 ILE A CA    1 
ATOM   7727  C  C     . ILE A 1 2521 ? 193.954 212.111 178.396 1.00 51.67  ? 2521 ILE A C     1 
ATOM   7728  O  O     . ILE A 1 2521 ? 194.036 213.000 177.536 1.00 57.43  ? 2521 ILE A O     1 
ATOM   7729  C  CB    . ILE A 1 2521 ? 193.955 209.895 177.224 1.00 49.81  ? 2521 ILE A CB    1 
ATOM   7730  C  CG1   . ILE A 1 2521 ? 192.491 209.775 177.653 1.00 49.04  ? 2521 ILE A CG1   1 
ATOM   7731  C  CG2   . ILE A 1 2521 ? 194.621 208.532 177.124 1.00 54.75  ? 2521 ILE A CG2   1 
ATOM   7732  C  CD1   . ILE A 1 2521 ? 191.679 208.828 176.811 1.00 45.92  ? 2521 ILE A CD1   1 
ATOM   7733  N  N     . THR A 1 2522 ? 193.208 212.252 179.489 1.00 52.63  ? 2522 THR A N     1 
ATOM   7734  C  CA    . THR A 1 2522 ? 192.297 213.383 179.577 1.00 56.14  ? 2522 THR A CA    1 
ATOM   7735  C  C     . THR A 1 2522 ? 193.030 214.650 180.010 1.00 60.40  ? 2522 THR A C     1 
ATOM   7736  O  O     . THR A 1 2522 ? 194.149 214.613 180.529 1.00 61.53  ? 2522 THR A O     1 
ATOM   7737  C  CB    . THR A 1 2522 ? 191.154 213.103 180.553 1.00 54.43  ? 2522 THR A CB    1 
ATOM   7738  O  OG1   . THR A 1 2522 ? 190.166 214.133 180.433 1.00 50.31  ? 2522 THR A OG1   1 
ATOM   7739  C  CG2   . THR A 1 2522 ? 191.667 213.107 181.981 1.00 53.13  ? 2522 THR A CG2   1 
ATOM   7740  N  N     . THR A 1 2523 ? 192.373 215.786 179.780 1.00 62.12  ? 2523 THR A N     1 
ATOM   7741  C  CA    . THR A 1 2523 ? 192.833 217.076 180.270 1.00 62.65  ? 2523 THR A CA    1 
ATOM   7742  C  C     . THR A 1 2523 ? 191.903 217.660 181.324 1.00 61.07  ? 2523 THR A C     1 
ATOM   7743  O  O     . THR A 1 2523 ? 192.206 218.725 181.876 1.00 62.64  ? 2523 THR A O     1 
ATOM   7744  C  CB    . THR A 1 2523 ? 192.984 218.069 179.110 1.00 67.89  ? 2523 THR A CB    1 
ATOM   7745  O  OG1   . THR A 1 2523 ? 193.738 219.207 179.545 1.00 77.44  ? 2523 THR A OG1   1 
ATOM   7746  C  CG2   . THR A 1 2523 ? 191.619 218.526 178.616 1.00 59.42  ? 2523 THR A CG2   1 
ATOM   7747  N  N     . VAL A 1 2524 ? 190.784 217.000 181.610 1.00 57.89  ? 2524 VAL A N     1 
ATOM   7748  C  CA    . VAL A 1 2524 ? 189.865 217.462 182.656 1.00 56.76  ? 2524 VAL A CA    1 
ATOM   7749  C  C     . VAL A 1 2524 ? 190.554 217.352 184.009 1.00 58.09  ? 2524 VAL A C     1 
ATOM   7750  O  O     . VAL A 1 2524 ? 191.301 216.380 184.244 1.00 58.27  ? 2524 VAL A O     1 
ATOM   7751  C  CB    . VAL A 1 2524 ? 188.567 216.635 182.629 1.00 46.25  ? 2524 VAL A CB    1 
ATOM   7752  C  CG1   . VAL A 1 2524 ? 187.543 217.191 183.603 1.00 43.42  ? 2524 VAL A CG1   1 
ATOM   7753  C  CG2   . VAL A 1 2524 ? 187.998 216.592 181.218 1.00 41.96  ? 2524 VAL A CG2   1 
ATOM   7754  N  N     . PRO A 1 2525 ? 190.376 218.309 184.921 1.00 54.82  ? 2525 PRO A N     1 
ATOM   7755  C  CA    . PRO A 1 2525 ? 190.939 218.149 186.267 1.00 52.17  ? 2525 PRO A CA    1 
ATOM   7756  C  C     . PRO A 1 2525 ? 190.390 216.902 186.942 1.00 56.87  ? 2525 PRO A C     1 
ATOM   7757  O  O     . PRO A 1 2525 ? 189.213 216.564 186.807 1.00 58.41  ? 2525 PRO A O     1 
ATOM   7758  C  CB    . PRO A 1 2525 ? 190.500 219.427 186.989 1.00 49.35  ? 2525 PRO A CB    1 
ATOM   7759  C  CG    . PRO A 1 2525 ? 190.297 220.420 185.900 1.00 51.88  ? 2525 PRO A CG    1 
ATOM   7760  C  CD    . PRO A 1 2525 ? 189.781 219.642 184.726 1.00 55.33  ? 2525 PRO A CD    1 
ATOM   7761  N  N     . LEU A 1 2526 ? 191.258 216.219 187.673 1.00 52.27  ? 2526 LEU A N     1 
ATOM   7762  C  CA    . LEU A 1 2526 ? 190.979 214.913 188.242 1.00 48.02  ? 2526 LEU A CA    1 
ATOM   7763  C  C     . LEU A 1 2526 ? 191.389 214.892 189.705 1.00 55.45  ? 2526 LEU A C     1 
ATOM   7764  O  O     . LEU A 1 2526 ? 192.216 215.703 190.136 1.00 62.15  ? 2526 LEU A O     1 
ATOM   7765  C  CB    . LEU A 1 2526 ? 191.730 213.823 187.463 1.00 44.81  ? 2526 LEU A CB    1 
ATOM   7766  C  CG    . LEU A 1 2526 ? 191.147 213.511 186.084 1.00 46.62  ? 2526 LEU A CG    1 
ATOM   7767  C  CD1   . LEU A 1 2526 ? 191.783 212.270 185.505 1.00 45.02  ? 2526 LEU A CD1   1 
ATOM   7768  C  CD2   . LEU A 1 2526 ? 189.635 213.349 186.159 1.00 42.48  ? 2526 LEU A CD2   1 
ATOM   7769  N  N     . PRO A 1 2527 ? 190.812 213.992 190.502 1.00 51.99  ? 2527 PRO A N     1 
ATOM   7770  C  CA    . PRO A 1 2527 ? 191.207 213.903 191.913 1.00 52.42  ? 2527 PRO A CA    1 
ATOM   7771  C  C     . PRO A 1 2527 ? 192.688 213.585 192.057 1.00 63.65  ? 2527 PRO A C     1 
ATOM   7772  O  O     . PRO A 1 2527 ? 193.261 212.826 191.273 1.00 66.41  ? 2527 PRO A O     1 
ATOM   7773  C  CB    . PRO A 1 2527 ? 190.332 212.768 192.455 1.00 47.41  ? 2527 PRO A CB    1 
ATOM   7774  C  CG    . PRO A 1 2527 ? 189.153 212.735 191.546 1.00 44.20  ? 2527 PRO A CG    1 
ATOM   7775  C  CD    . PRO A 1 2527 ? 189.670 213.115 190.191 1.00 42.78  ? 2527 PRO A CD    1 
ATOM   7776  N  N     . THR A 1 2528 ? 193.307 214.178 193.080 1.00 64.31  ? 2528 THR A N     1 
ATOM   7777  C  CA    . THR A 1 2528 ? 194.731 214.011 193.344 1.00 65.62  ? 2528 THR A CA    1 
ATOM   7778  C  C     . THR A 1 2528 ? 195.020 212.846 194.282 1.00 76.54  ? 2528 THR A C     1 
ATOM   7779  O  O     . THR A 1 2528 ? 196.040 212.857 194.984 1.00 80.78  ? 2528 THR A O     1 
ATOM   7780  C  CB    . THR A 1 2528 ? 195.316 215.305 193.911 1.00 72.03  ? 2528 THR A CB    1 
ATOM   7781  O  OG1   . THR A 1 2528 ? 194.686 215.608 195.162 1.00 74.37  ? 2528 THR A OG1   1 
ATOM   7782  C  CG2   . THR A 1 2528 ? 195.093 216.459 192.945 1.00 69.92  ? 2528 THR A CG2   1 
ATOM   7783  N  N     . ALA A 1 2529 ? 194.150 211.847 194.316 1.00 80.39  ? 2529 ALA A N     1 
ATOM   7784  C  CA    . ALA A 1 2529 ? 194.362 210.704 195.191 1.00 82.89  ? 2529 ALA A CA    1 
ATOM   7785  C  C     . ALA A 1 2529 ? 195.523 209.861 194.673 1.00 89.20  ? 2529 ALA A C     1 
ATOM   7786  O  O     . ALA A 1 2529 ? 195.510 209.449 193.507 1.00 87.54  ? 2529 ALA A O     1 
ATOM   7787  C  CB    . ALA A 1 2529 ? 193.094 209.863 195.283 1.00 71.65  ? 2529 ALA A CB    1 
ATOM   7788  N  N     . PRO A 1 2530 ? 196.542 209.597 195.494 1.00 89.04  ? 2530 PRO A N     1 
ATOM   7789  C  CA    . PRO A 1 2530 ? 197.690 208.814 195.008 1.00 90.99  ? 2530 PRO A CA    1 
ATOM   7790  C  C     . PRO A 1 2530 ? 197.340 207.397 194.587 1.00 90.33  ? 2530 PRO A C     1 
ATOM   7791  O  O     . PRO A 1 2530 ? 197.962 206.870 193.656 1.00 91.39  ? 2530 PRO A O     1 
ATOM   7792  C  CB    . PRO A 1 2530 ? 198.651 208.824 196.206 1.00 92.79  ? 2530 PRO A CB    1 
ATOM   7793  C  CG    . PRO A 1 2530 ? 197.787 209.098 197.391 1.00 93.54  ? 2530 PRO A CG    1 
ATOM   7794  C  CD    . PRO A 1 2530 ? 196.691 209.994 196.904 1.00 86.09  ? 2530 PRO A CD    1 
ATOM   7795  N  N     . ASN A 1 2531 ? 196.366 206.760 195.236 1.00 83.86  ? 2531 ASN A N     1 
ATOM   7796  C  CA    . ASN A 1 2531 ? 196.075 205.360 194.953 1.00 86.54  ? 2531 ASN A CA    1 
ATOM   7797  C  C     . ASN A 1 2531 ? 194.595 205.124 194.682 1.00 75.84  ? 2531 ASN A C     1 
ATOM   7798  O  O     . ASN A 1 2531 ? 194.233 204.162 193.996 1.00 70.04  ? 2531 ASN A O     1 
ATOM   7799  C  CB    . ASN A 1 2531 ? 196.538 204.477 196.115 1.00 98.44  ? 2531 ASN A CB    1 
ATOM   7800  C  CG    . ASN A 1 2531 ? 198.047 204.397 196.222 1.00 97.59  ? 2531 ASN A CG    1 
ATOM   7801  O  OD1   . ASN A 1 2531 ? 198.747 204.283 195.216 1.00 91.83  ? 2531 ASN A OD1   1 
ATOM   7802  N  ND2   . ASN A 1 2531 ? 198.558 204.456 197.446 1.00 99.36  ? 2531 ASN A ND2   1 
ATOM   7803  N  N     . ILE A 1 2532 ? 193.737 205.983 195.214 1.00 73.00  ? 2532 ILE A N     1 
ATOM   7804  C  CA    . ILE A 1 2532 ? 192.291 205.783 195.061 1.00 64.88  ? 2532 ILE A CA    1 
ATOM   7805  C  C     . ILE A 1 2532 ? 191.904 206.006 193.602 1.00 59.39  ? 2532 ILE A C     1 
ATOM   7806  O  O     . ILE A 1 2532 ? 192.251 207.052 193.025 1.00 58.13  ? 2532 ILE A O     1 
ATOM   7807  C  CB    . ILE A 1 2532 ? 191.521 206.726 195.984 1.00 59.71  ? 2532 ILE A CB    1 
ATOM   7808  C  CG1   . ILE A 1 2532 ? 191.840 206.418 197.447 1.00 61.67  ? 2532 ILE A CG1   1 
ATOM   7809  C  CG2   . ILE A 1 2532 ? 190.028 206.614 195.734 1.00 54.51  ? 2532 ILE A CG2   1 
ATOM   7810  C  CD1   . ILE A 1 2532 ? 191.327 207.462 198.410 1.00 58.53  ? 2532 ILE A CD1   1 
ATOM   7811  N  N     . PRO A 1 2533 ? 191.201 205.071 192.969 1.00 51.62  ? 2533 PRO A N     1 
ATOM   7812  C  CA    . PRO A 1 2533 ? 190.814 205.262 191.569 1.00 45.32  ? 2533 PRO A CA    1 
ATOM   7813  C  C     . PRO A 1 2533 ? 189.717 206.306 191.428 1.00 45.40  ? 2533 PRO A C     1 
ATOM   7814  O  O     . PRO A 1 2533 ? 189.028 206.668 192.385 1.00 51.32  ? 2533 PRO A O     1 
ATOM   7815  C  CB    . PRO A 1 2533 ? 190.319 203.877 191.143 1.00 41.36  ? 2533 PRO A CB    1 
ATOM   7816  C  CG    . PRO A 1 2533 ? 189.857 203.247 192.407 1.00 40.33  ? 2533 PRO A CG    1 
ATOM   7817  C  CD    . PRO A 1 2533 ? 190.754 203.770 193.495 1.00 50.28  ? 2533 PRO A CD    1 
ATOM   7818  N  N     . ILE A 1 2534 ? 189.575 206.799 190.196 1.00 41.87  ? 2534 ILE A N     1 
ATOM   7819  C  CA    . ILE A 1 2534 ? 188.566 207.811 189.905 1.00 37.59  ? 2534 ILE A CA    1 
ATOM   7820  C  C     . ILE A 1 2534 ? 187.170 207.232 190.090 1.00 34.81  ? 2534 ILE A C     1 
ATOM   7821  O  O     . ILE A 1 2534 ? 186.221 207.959 190.411 1.00 38.72  ? 2534 ILE A O     1 
ATOM   7822  C  CB    . ILE A 1 2534 ? 188.769 208.352 188.479 1.00 34.25  ? 2534 ILE A CB    1 
ATOM   7823  C  CG1   . ILE A 1 2534 ? 190.135 209.023 188.355 1.00 41.70  ? 2534 ILE A CG1   1 
ATOM   7824  C  CG2   . ILE A 1 2534 ? 187.702 209.381 188.146 1.00 33.29  ? 2534 ILE A CG2   1 
ATOM   7825  C  CD1   . ILE A 1 2534 ? 190.523 209.340 186.929 1.00 41.85  ? 2534 ILE A CD1   1 
ATOM   7826  N  N     . ILE A 1 2535 ? 187.024 205.915 189.914 1.00 33.74  ? 2535 ILE A N     1 
ATOM   7827  C  CA    . ILE A 1 2535 ? 185.724 205.266 190.016 1.00 33.30  ? 2535 ILE A CA    1 
ATOM   7828  C  C     . ILE A 1 2535 ? 185.147 205.397 191.420 1.00 33.77  ? 2535 ILE A C     1 
ATOM   7829  O  O     . ILE A 1 2535 ? 183.938 205.232 191.613 1.00 32.90  ? 2535 ILE A O     1 
ATOM   7830  C  CB    . ILE A 1 2535 ? 185.849 203.785 189.590 1.00 32.76  ? 2535 ILE A CB    1 
ATOM   7831  C  CG1   . ILE A 1 2535 ? 184.473 203.162 189.360 1.00 32.49  ? 2535 ILE A CG1   1 
ATOM   7832  C  CG2   . ILE A 1 2535 ? 186.641 202.989 190.618 1.00 32.74  ? 2535 ILE A CG2   1 
ATOM   7833  C  CD1   . ILE A 1 2535 ? 183.738 203.760 188.186 1.00 26.45  ? 2535 ILE A CD1   1 
ATOM   7834  N  N     . ASP A 1 2536 ? 185.984 205.715 192.405 1.00 34.17  ? 2536 ASP A N     1 
ATOM   7835  C  CA    . ASP A 1 2536 ? 185.555 205.885 193.786 1.00 32.64  ? 2536 ASP A CA    1 
ATOM   7836  C  C     . ASP A 1 2536 ? 185.104 207.306 194.096 1.00 36.11  ? 2536 ASP A C     1 
ATOM   7837  O  O     . ASP A 1 2536 ? 184.767 207.594 195.249 1.00 39.96  ? 2536 ASP A O     1 
ATOM   7838  C  CB    . ASP A 1 2536 ? 186.686 205.491 194.740 1.00 35.62  ? 2536 ASP A CB    1 
ATOM   7839  C  CG    . ASP A 1 2536 ? 186.970 204.003 194.724 1.00 50.19  ? 2536 ASP A CG    1 
ATOM   7840  O  OD1   . ASP A 1 2536 ? 186.342 203.287 193.917 1.00 49.43  ? 2536 ASP A OD1   1 
ATOM   7841  O  OD2   . ASP A 1 2536 ? 187.819 203.548 195.519 1.00 55.96  ? 2536 ASP A OD2   1 
ATOM   7842  N  N     . TYR A 1 2537 ? 185.093 208.196 193.108 1.00 35.34  ? 2537 TYR A N     1 
ATOM   7843  C  CA    . TYR A 1 2537 ? 184.698 209.582 193.297 1.00 29.01  ? 2537 TYR A CA    1 
ATOM   7844  C  C     . TYR A 1 2537 ? 183.417 209.874 192.529 1.00 27.93  ? 2537 TYR A C     1 
ATOM   7845  O  O     . TYR A 1 2537 ? 183.183 209.325 191.448 1.00 38.48  ? 2537 TYR A O     1 
ATOM   7846  C  CB    . TYR A 1 2537 ? 185.795 210.545 192.829 1.00 30.05  ? 2537 TYR A CB    1 
ATOM   7847  C  CG    . TYR A 1 2537 ? 186.959 210.681 193.781 1.00 33.95  ? 2537 TYR A CG    1 
ATOM   7848  C  CD1   . TYR A 1 2537 ? 187.970 209.731 193.812 1.00 33.20  ? 2537 TYR A CD1   1 
ATOM   7849  C  CD2   . TYR A 1 2537 ? 187.052 211.765 194.641 1.00 37.80  ? 2537 TYR A CD2   1 
ATOM   7850  C  CE1   . TYR A 1 2537 ? 189.037 209.855 194.678 1.00 39.17  ? 2537 TYR A CE1   1 
ATOM   7851  C  CE2   . TYR A 1 2537 ? 188.115 211.897 195.510 1.00 41.23  ? 2537 TYR A CE2   1 
ATOM   7852  C  CZ    . TYR A 1 2537 ? 189.104 210.939 195.525 1.00 42.19  ? 2537 TYR A CZ    1 
ATOM   7853  O  OH    . TYR A 1 2537 ? 190.165 211.068 196.390 1.00 53.55  ? 2537 TYR A OH    1 
ATOM   7854  N  N     . GLU A 1 2538 ? 182.591 210.745 193.096 1.00 25.82  ? 2538 GLU A N     1 
ATOM   7855  C  CA    . GLU A 1 2538 ? 181.426 211.282 192.411 1.00 31.31  ? 2538 GLU A CA    1 
ATOM   7856  C  C     . GLU A 1 2538 ? 181.715 212.707 191.962 1.00 36.78  ? 2538 GLU A C     1 
ATOM   7857  O  O     . GLU A 1 2538 ? 182.799 213.250 192.187 1.00 40.60  ? 2538 GLU A O     1 
ATOM   7858  C  CB    . GLU A 1 2538 ? 180.187 211.261 193.312 1.00 29.09  ? 2538 GLU A CB    1 
ATOM   7859  C  CG    . GLU A 1 2538 ? 180.284 212.202 194.496 1.00 32.63  ? 2538 GLU A CG    1 
ATOM   7860  C  CD    . GLU A 1 2538 ? 179.049 212.176 195.370 1.00 42.65  ? 2538 GLU A CD    1 
ATOM   7861  O  OE1   . GLU A 1 2538 ? 178.113 211.414 195.055 1.00 42.43  ? 2538 GLU A OE1   1 
ATOM   7862  O  OE2   . GLU A 1 2538 ? 179.014 212.921 196.371 1.00 53.42  ? 2538 GLU A OE2   1 
ATOM   7863  N  N     . VAL A 1 2539 ? 180.723 213.316 191.326 1.00 34.12  ? 2539 VAL A N     1 
ATOM   7864  C  CA    . VAL A 1 2539 ? 180.811 214.698 190.877 1.00 31.63  ? 2539 VAL A CA    1 
ATOM   7865  C  C     . VAL A 1 2539 ? 179.702 215.470 191.577 1.00 33.89  ? 2539 VAL A C     1 
ATOM   7866  O  O     . VAL A 1 2539 ? 178.518 215.297 191.264 1.00 36.69  ? 2539 VAL A O     1 
ATOM   7867  C  CB    . VAL A 1 2539 ? 180.697 214.812 189.352 1.00 30.91  ? 2539 VAL A CB    1 
ATOM   7868  C  CG1   . VAL A 1 2539 ? 180.553 216.266 188.937 1.00 26.53  ? 2539 VAL A CG1   1 
ATOM   7869  C  CG2   . VAL A 1 2539 ? 181.900 214.174 188.687 1.00 33.37  ? 2539 VAL A CG2   1 
ATOM   7870  N  N     . SER A 1 2540 ? 180.081 216.314 192.531 1.00 31.95  ? 2540 SER A N     1 
ATOM   7871  C  CA    . SER A 1 2540 ? 179.101 217.123 193.236 1.00 31.43  ? 2540 SER A CA    1 
ATOM   7872  C  C     . SER A 1 2540 ? 178.531 218.189 192.307 1.00 34.88  ? 2540 SER A C     1 
ATOM   7873  O  O     . SER A 1 2540 ? 179.174 218.629 191.350 1.00 37.63  ? 2540 SER A O     1 
ATOM   7874  C  CB    . SER A 1 2540 ? 179.727 217.773 194.468 1.00 35.95  ? 2540 SER A CB    1 
ATOM   7875  O  OG    . SER A 1 2540 ? 180.977 218.360 194.153 1.00 41.93  ? 2540 SER A OG    1 
ATOM   7876  N  N     . ILE A 1 2541 ? 177.297 218.606 192.603 1.00 36.11  ? 2541 ILE A N     1 
ATOM   7877  C  CA    . ILE A 1 2541 ? 176.627 219.589 191.762 1.00 36.94  ? 2541 ILE A CA    1 
ATOM   7878  C  C     . ILE A 1 2541 ? 177.352 220.929 191.791 1.00 38.43  ? 2541 ILE A C     1 
ATOM   7879  O  O     . ILE A 1 2541 ? 177.211 221.729 190.859 1.00 44.24  ? 2541 ILE A O     1 
ATOM   7880  C  CB    . ILE A 1 2541 ? 175.154 219.732 192.190 1.00 41.33  ? 2541 ILE A CB    1 
ATOM   7881  C  CG1   . ILE A 1 2541 ? 174.376 220.587 191.188 1.00 37.83  ? 2541 ILE A CG1   1 
ATOM   7882  C  CG2   . ILE A 1 2541 ? 175.056 220.327 193.586 1.00 43.86  ? 2541 ILE A CG2   1 
ATOM   7883  C  CD1   . ILE A 1 2541 ? 174.474 220.098 189.761 1.00 38.61  ? 2541 ILE A CD1   1 
ATOM   7884  N  N     . SER A 1 2542 ? 178.148 221.190 192.831 1.00 37.42  ? 2542 SER A N     1 
ATOM   7885  C  CA    . SER A 1 2542 ? 178.957 222.401 192.882 1.00 37.61  ? 2542 SER A CA    1 
ATOM   7886  C  C     . SER A 1 2542 ? 180.089 222.395 191.864 1.00 42.14  ? 2542 SER A C     1 
ATOM   7887  O  O     . SER A 1 2542 ? 180.715 223.439 191.656 1.00 51.60  ? 2542 SER A O     1 
ATOM   7888  C  CB    . SER A 1 2542 ? 179.529 222.592 194.287 1.00 40.45  ? 2542 SER A CB    1 
ATOM   7889  O  OG    . SER A 1 2542 ? 180.608 221.704 194.523 1.00 44.70  ? 2542 SER A OG    1 
ATOM   7890  N  N     . GLY A 1 2543 ? 180.371 221.256 191.236 1.00 37.74  ? 2543 GLY A N     1 
ATOM   7891  C  CA    . GLY A 1 2543 ? 181.382 221.198 190.202 1.00 37.67  ? 2543 GLY A CA    1 
ATOM   7892  C  C     . GLY A 1 2543 ? 182.753 220.756 190.655 1.00 44.25  ? 2543 GLY A C     1 
ATOM   7893  O  O     . GLY A 1 2543 ? 183.753 221.186 190.070 1.00 55.72  ? 2543 GLY A O     1 
ATOM   7894  N  N     . GLU A 1 2544 ? 182.838 219.912 191.681 1.00 40.08  ? 2544 GLU A N     1 
ATOM   7895  C  CA    . GLU A 1 2544 ? 184.118 219.430 192.175 1.00 40.64  ? 2544 GLU A CA    1 
ATOM   7896  C  C     . GLU A 1 2544 ? 184.011 217.950 192.512 1.00 38.29  ? 2544 GLU A C     1 
ATOM   7897  O  O     . GLU A 1 2544 ? 182.932 217.445 192.831 1.00 43.91  ? 2544 GLU A O     1 
ATOM   7898  C  CB    . GLU A 1 2544 ? 184.584 220.219 193.406 1.00 46.65  ? 2544 GLU A CB    1 
ATOM   7899  C  CG    . GLU A 1 2544 ? 183.622 220.163 194.582 1.00 54.02  ? 2544 GLU A CG    1 
ATOM   7900  C  CD    . GLU A 1 2544 ? 184.250 220.650 195.873 1.00 70.35  ? 2544 GLU A CD    1 
ATOM   7901  O  OE1   . GLU A 1 2544 ? 184.166 221.864 196.156 1.00 78.99  ? 2544 GLU A OE1   1 
ATOM   7902  O  OE2   . GLU A 1 2544 ? 184.826 219.819 196.605 1.00 71.72  ? 2544 GLU A OE2   1 
ATOM   7903  N  N     . TRP A 1 2545 ? 185.146 217.261 192.434 1.00 38.24  ? 2545 TRP A N     1 
ATOM   7904  C  CA    . TRP A 1 2545 ? 185.193 215.845 192.772 1.00 36.67  ? 2545 TRP A CA    1 
ATOM   7905  C  C     . TRP A 1 2545 ? 185.063 215.657 194.278 1.00 43.46  ? 2545 TRP A C     1 
ATOM   7906  O  O     . TRP A 1 2545 ? 185.735 216.336 195.060 1.00 50.61  ? 2545 TRP A O     1 
ATOM   7907  C  CB    . TRP A 1 2545 ? 186.499 215.224 192.280 1.00 37.05  ? 2545 TRP A CB    1 
ATOM   7908  C  CG    . TRP A 1 2545 ? 186.611 215.104 190.792 1.00 36.38  ? 2545 TRP A CG    1 
ATOM   7909  C  CD1   . TRP A 1 2545 ? 187.325 215.912 189.958 1.00 37.07  ? 2545 TRP A CD1   1 
ATOM   7910  C  CD2   . TRP A 1 2545 ? 186.015 214.099 189.962 1.00 36.65  ? 2545 TRP A CD2   1 
ATOM   7911  N  NE1   . TRP A 1 2545 ? 187.200 215.483 188.660 1.00 37.77  ? 2545 TRP A NE1   1 
ATOM   7912  C  CE2   . TRP A 1 2545 ? 186.401 214.371 188.636 1.00 36.68  ? 2545 TRP A CE2   1 
ATOM   7913  C  CE3   . TRP A 1 2545 ? 185.188 213.001 190.212 1.00 35.10  ? 2545 TRP A CE3   1 
ATOM   7914  C  CZ2   . TRP A 1 2545 ? 185.988 213.585 187.563 1.00 34.48  ? 2545 TRP A CZ2   1 
ATOM   7915  C  CZ3   . TRP A 1 2545 ? 184.779 212.222 189.146 1.00 27.56  ? 2545 TRP A CZ3   1 
ATOM   7916  C  CH2   . TRP A 1 2545 ? 185.179 212.517 187.839 1.00 29.45  ? 2545 TRP A CH2   1 
ATOM   7917  N  N     . SER A 1 2546 ? 184.198 214.730 194.684 1.00 41.79  ? 2546 SER A N     1 
ATOM   7918  C  CA    . SER A 1 2546 ? 184.059 214.366 196.082 1.00 40.92  ? 2546 SER A CA    1 
ATOM   7919  C  C     . SER A 1 2546 ? 184.049 212.849 196.213 1.00 39.02  ? 2546 SER A C     1 
ATOM   7920  O  O     . SER A 1 2546 ? 183.429 212.158 195.395 1.00 44.95  ? 2546 SER A O     1 
ATOM   7921  C  CB    . SER A 1 2546 ? 182.777 214.955 196.688 1.00 40.01  ? 2546 SER A CB    1 
ATOM   7922  O  OG    . SER A 1 2546 ? 181.658 214.714 195.856 1.00 40.97  ? 2546 SER A OG    1 
ATOM   7923  N  N     . PRO A 1 2547 ? 184.728 212.303 197.219 1.00 36.35  ? 2547 PRO A N     1 
ATOM   7924  C  CA    . PRO A 1 2547 ? 184.786 210.846 197.360 1.00 37.45  ? 2547 PRO A CA    1 
ATOM   7925  C  C     . PRO A 1 2547 ? 183.429 210.252 197.697 1.00 37.73  ? 2547 PRO A C     1 
ATOM   7926  O  O     . PRO A 1 2547 ? 182.584 210.884 198.337 1.00 39.75  ? 2547 PRO A O     1 
ATOM   7927  C  CB    . PRO A 1 2547 ? 185.781 210.639 198.508 1.00 35.30  ? 2547 PRO A CB    1 
ATOM   7928  C  CG    . PRO A 1 2547 ? 185.746 211.916 199.273 1.00 33.41  ? 2547 PRO A CG    1 
ATOM   7929  C  CD    . PRO A 1 2547 ? 185.503 212.995 198.262 1.00 33.91  ? 2547 PRO A CD    1 
ATOM   7930  N  N     . TRP A 1 2548 ? 183.226 209.012 197.248 1.00 34.38  ? 2548 TRP A N     1 
ATOM   7931  C  CA    . TRP A 1 2548 ? 182.011 208.283 197.590 1.00 33.44  ? 2548 TRP A CA    1 
ATOM   7932  C  C     . TRP A 1 2548 ? 181.989 207.855 199.050 1.00 37.46  ? 2548 TRP A C     1 
ATOM   7933  O  O     . TRP A 1 2548 ? 180.917 207.525 199.569 1.00 38.20  ? 2548 TRP A O     1 
ATOM   7934  C  CB    . TRP A 1 2548 ? 181.861 207.058 196.687 1.00 29.96  ? 2548 TRP A CB    1 
ATOM   7935  C  CG    . TRP A 1 2548 ? 181.088 207.320 195.435 1.00 27.26  ? 2548 TRP A CG    1 
ATOM   7936  C  CD1   . TRP A 1 2548 ? 181.534 207.189 194.154 1.00 27.54  ? 2548 TRP A CD1   1 
ATOM   7937  C  CD2   . TRP A 1 2548 ? 179.723 207.744 195.343 1.00 26.38  ? 2548 TRP A CD2   1 
ATOM   7938  N  NE1   . TRP A 1 2548 ? 180.535 207.512 193.269 1.00 25.99  ? 2548 TRP A NE1   1 
ATOM   7939  C  CE2   . TRP A 1 2548 ? 179.412 207.856 193.975 1.00 24.43  ? 2548 TRP A CE2   1 
ATOM   7940  C  CE3   . TRP A 1 2548 ? 178.735 208.043 196.286 1.00 28.89  ? 2548 TRP A CE3   1 
ATOM   7941  C  CZ2   . TRP A 1 2548 ? 178.157 208.254 193.527 1.00 22.62  ? 2548 TRP A CZ2   1 
ATOM   7942  C  CZ3   . TRP A 1 2548 ? 177.491 208.437 195.839 1.00 30.59  ? 2548 TRP A CZ3   1 
ATOM   7943  C  CH2   . TRP A 1 2548 ? 177.213 208.540 194.473 1.00 26.68  ? 2548 TRP A CH2   1 
ATOM   7944  N  N     . GLN A 1 2549 ? 183.144 207.850 199.720 1.00 40.49  ? 2549 GLN A N     1 
ATOM   7945  C  CA    . GLN A 1 2549 ? 183.190 207.481 201.129 1.00 38.93  ? 2549 GLN A CA    1 
ATOM   7946  C  C     . GLN A 1 2549 ? 182.436 208.469 202.008 1.00 37.37  ? 2549 GLN A C     1 
ATOM   7947  O  O     . GLN A 1 2549 ? 181.978 208.092 203.092 1.00 42.39  ? 2549 GLN A O     1 
ATOM   7948  C  CB    . GLN A 1 2549 ? 184.643 207.370 201.594 1.00 38.11  ? 2549 GLN A CB    1 
ATOM   7949  C  CG    . GLN A 1 2549 ? 184.842 206.465 202.797 1.00 49.34  ? 2549 GLN A CG    1 
ATOM   7950  C  CD    . GLN A 1 2549 ? 184.670 204.998 202.455 1.00 61.47  ? 2549 GLN A CD    1 
ATOM   7951  O  OE1   . GLN A 1 2549 ? 183.799 204.320 203.000 1.00 63.06  ? 2549 GLN A OE1   1 
ATOM   7952  N  NE2   . GLN A 1 2549 ? 185.502 204.501 201.548 1.00 62.00  ? 2549 GLN A NE2   1 
ATOM   7953  N  N     . ALA A 1 2550 ? 182.298 209.722 201.570 1.00 32.67  ? 2550 ALA A N     1 
ATOM   7954  C  CA    . ALA A 1 2550 ? 181.515 210.692 202.324 1.00 35.44  ? 2550 ALA A CA    1 
ATOM   7955  C  C     . ALA A 1 2550 ? 180.035 210.336 202.355 1.00 38.78  ? 2550 ALA A C     1 
ATOM   7956  O  O     . ALA A 1 2550 ? 179.321 210.781 203.260 1.00 43.77  ? 2550 ALA A O     1 
ATOM   7957  C  CB    . ALA A 1 2550 ? 181.702 212.092 201.739 1.00 42.29  ? 2550 ALA A CB    1 
ATOM   7958  N  N     . LYS A 1 2551 ? 179.563 209.549 201.392 1.00 38.45  ? 2551 LYS A N     1 
ATOM   7959  C  CA    . LYS A 1 2551 ? 178.186 209.080 201.365 1.00 35.82  ? 2551 LYS A CA    1 
ATOM   7960  C  C     . LYS A 1 2551 ? 178.005 207.751 202.084 1.00 39.52  ? 2551 LYS A C     1 
ATOM   7961  O  O     . LYS A 1 2551 ? 176.892 207.216 202.095 1.00 43.33  ? 2551 LYS A O     1 
ATOM   7962  C  CB    . LYS A 1 2551 ? 177.700 208.948 199.917 1.00 34.49  ? 2551 LYS A CB    1 
ATOM   7963  C  CG    . LYS A 1 2551 ? 177.773 210.235 199.114 1.00 36.51  ? 2551 LYS A CG    1 
ATOM   7964  C  CD    . LYS A 1 2551 ? 176.799 211.270 199.645 1.00 41.79  ? 2551 LYS A CD    1 
ATOM   7965  C  CE    . LYS A 1 2551 ? 176.675 212.450 198.697 1.00 44.61  ? 2551 LYS A CE    1 
ATOM   7966  N  NZ    . LYS A 1 2551 ? 175.974 212.077 197.438 1.00 45.23  ? 2551 LYS A NZ    1 
ATOM   7967  N  N     . VAL A 1 2552 ? 179.062 207.209 202.679 1.00 39.97  ? 2552 VAL A N     1 
ATOM   7968  C  CA    . VAL A 1 2552 ? 178.993 205.921 203.362 1.00 36.98  ? 2552 VAL A CA    1 
ATOM   7969  C  C     . VAL A 1 2552 ? 179.198 206.155 204.855 1.00 42.40  ? 2552 VAL A C     1 
ATOM   7970  O  O     . VAL A 1 2552 ? 180.341 206.302 205.311 1.00 48.85  ? 2552 VAL A O     1 
ATOM   7971  C  CB    . VAL A 1 2552 ? 180.032 204.937 202.799 1.00 33.39  ? 2552 VAL A CB    1 
ATOM   7972  C  CG1   . VAL A 1 2552 ? 180.116 203.685 203.662 1.00 36.21  ? 2552 VAL A CG1   1 
ATOM   7973  C  CG2   . VAL A 1 2552 ? 179.699 204.582 201.362 1.00 32.73  ? 2552 VAL A CG2   1 
ATOM   7974  N  N     . PRO A 1 2553 ? 178.130 206.224 205.643 1.00 41.08  ? 2553 PRO A N     1 
ATOM   7975  C  CA    . PRO A 1 2553 ? 178.276 206.365 207.092 1.00 50.20  ? 2553 PRO A CA    1 
ATOM   7976  C  C     . PRO A 1 2553 ? 178.242 205.027 207.811 1.00 57.40  ? 2553 PRO A C     1 
ATOM   7977  O  O     . PRO A 1 2553 ? 177.602 204.066 207.380 1.00 59.61  ? 2553 PRO A O     1 
ATOM   7978  C  CB    . PRO A 1 2553 ? 177.059 207.220 207.469 1.00 52.25  ? 2553 PRO A CB    1 
ATOM   7979  C  CG    . PRO A 1 2553 ? 176.012 206.816 206.471 1.00 47.02  ? 2553 PRO A CG    1 
ATOM   7980  C  CD    . PRO A 1 2553 ? 176.723 206.335 205.220 1.00 43.26  ? 2553 PRO A CD    1 
ATOM   7981  N  N     . GLN A 1 2554 ? 178.955 204.977 208.932 1.00 55.32  ? 2554 GLN A N     1 
ATOM   7982  C  CA    . GLN A 1 2554 ? 178.912 203.817 209.818 1.00 57.87  ? 2554 GLN A CA    1 
ATOM   7983  C  C     . GLN A 1 2554 ? 177.699 203.970 210.726 1.00 63.57  ? 2554 GLN A C     1 
ATOM   7984  O  O     . GLN A 1 2554 ? 177.739 204.696 211.721 1.00 71.43  ? 2554 GLN A O     1 
ATOM   7985  C  CB    . GLN A 1 2554 ? 180.200 203.701 210.623 1.00 57.18  ? 2554 GLN A CB    1 
ATOM   7986  C  CG    . GLN A 1 2554 ? 180.364 202.370 211.338 1.00 66.10  ? 2554 GLN A CG    1 
ATOM   7987  C  CD    . GLN A 1 2554 ? 181.813 201.936 211.442 1.00 74.31  ? 2554 GLN A CD    1 
ATOM   7988  O  OE1   . GLN A 1 2554 ? 182.446 201.601 210.442 1.00 78.75  ? 2554 GLN A OE1   1 
ATOM   7989  N  NE2   . GLN A 1 2554 ? 182.345 201.938 212.659 1.00 64.96  ? 2554 GLN A NE2   1 
ATOM   7990  N  N     . ILE A 1 2555 ? 176.614 203.285 210.386 1.00 61.29  ? 2555 ILE A N     1 
ATOM   7991  C  CA    . ILE A 1 2555 ? 175.368 203.412 211.109 1.00 61.42  ? 2555 ILE A CA    1 
ATOM   7992  C  C     . ILE A 1 2555 ? 175.227 202.246 212.079 1.00 62.90  ? 2555 ILE A C     1 
ATOM   7993  O  O     . ILE A 1 2555 ? 175.949 201.255 212.008 1.00 59.01  ? 2555 ILE A O     1 
ATOM   7994  C  CB    . ILE A 1 2555 ? 174.151 203.487 210.157 1.00 62.44  ? 2555 ILE A CB    1 
ATOM   7995  C  CG1   . ILE A 1 2555 ? 174.164 202.313 209.177 1.00 55.64  ? 2555 ILE A CG1   1 
ATOM   7996  C  CG2   . ILE A 1 2555 ? 174.141 204.809 209.407 1.00 59.09  ? 2555 ILE A CG2   1 
ATOM   7997  C  CD1   . ILE A 1 2555 ? 173.011 202.331 208.202 1.00 48.44  ? 2555 ILE A CD1   1 
ATOM   7998  N  N     . GLU A 1 2556 ? 174.280 202.369 213.005 1.00 63.21  ? 2556 GLU A N     1 
ATOM   7999  C  CA    . GLU A 1 2556 ? 173.946 201.311 213.954 1.00 60.24  ? 2556 GLU A CA    1 
ATOM   8000  C  C     . GLU A 1 2556 ? 172.486 200.941 213.717 1.00 62.73  ? 2556 GLU A C     1 
ATOM   8001  O  O     . GLU A 1 2556 ? 171.579 201.644 214.175 1.00 64.57  ? 2556 GLU A O     1 
ATOM   8002  C  CB    . GLU A 1 2556 ? 174.185 201.766 215.394 1.00 56.93  ? 2556 GLU A CB    1 
ATOM   8003  C  CG    . GLU A 1 2556 ? 175.537 202.440 215.663 1.00 58.25  ? 2556 GLU A CG    1 
ATOM   8004  C  CD    . GLU A 1 2556 ? 176.745 201.512 215.546 1.00 68.57  ? 2556 GLU A CD    1 
ATOM   8005  O  OE1   . GLU A 1 2556 ? 176.717 200.540 214.763 1.00 65.90  ? 2556 GLU A OE1   1 
ATOM   8006  O  OE2   . GLU A 1 2556 ? 177.742 201.767 216.253 1.00 72.04  ? 2556 GLU A OE2   1 
ATOM   8007  N  N     . VAL A 1 2557 ? 172.258 199.843 212.994 1.00 61.72  ? 2557 VAL A N     1 
ATOM   8008  C  CA    . VAL A 1 2557 ? 170.895 199.416 212.707 1.00 59.29  ? 2557 VAL A CA    1 
ATOM   8009  C  C     . VAL A 1 2557 ? 170.221 198.951 213.992 1.00 59.75  ? 2557 VAL A C     1 
ATOM   8010  O  O     . VAL A 1 2557 ? 170.872 198.467 214.928 1.00 57.66  ? 2557 VAL A O     1 
ATOM   8011  C  CB    . VAL A 1 2557 ? 170.879 198.312 211.633 1.00 49.98  ? 2557 VAL A CB    1 
ATOM   8012  C  CG1   . VAL A 1 2557 ? 171.457 198.837 210.329 1.00 53.66  ? 2557 VAL A CG1   1 
ATOM   8013  C  CG2   . VAL A 1 2557 ? 171.653 197.096 212.102 1.00 46.40  ? 2557 VAL A CG2   1 
ATOM   8014  N  N     . GLU A 1 2558 ? 168.902 199.115 214.045 1.00 65.00  ? 2558 GLU A N     1 
ATOM   8015  C  CA    . GLU A 1 2558 ? 168.152 198.782 215.246 1.00 67.74  ? 2558 GLU A CA    1 
ATOM   8016  C  C     . GLU A 1 2558 ? 168.180 197.279 215.504 1.00 68.39  ? 2558 GLU A C     1 
ATOM   8017  O  O     . GLU A 1 2558 ? 168.343 196.470 214.586 1.00 72.72  ? 2558 GLU A O     1 
ATOM   8018  C  CB    . GLU A 1 2558 ? 166.711 199.276 215.129 1.00 69.91  ? 2558 GLU A CB    1 
ATOM   8019  C  CG    . GLU A 1 2558 ? 166.601 200.776 214.901 1.00 76.10  ? 2558 GLU A CG    1 
ATOM   8020  C  CD    . GLU A 1 2558 ? 165.170 201.275 214.948 1.00 83.62  ? 2558 GLU A CD    1 
ATOM   8021  O  OE1   . GLU A 1 2558 ? 164.349 200.812 214.130 1.00 79.81  ? 2558 GLU A OE1   1 
ATOM   8022  O  OE2   . GLU A 1 2558 ? 164.868 202.135 215.802 1.00 90.31  ? 2558 GLU A OE2   1 
ATOM   8023  N  N     . THR A 1 2559 ? 168.027 196.914 216.779 1.00 63.32  ? 2559 THR A N     1 
ATOM   8024  C  CA    . THR A 1 2559 ? 168.156 195.516 217.178 1.00 58.16  ? 2559 THR A CA    1 
ATOM   8025  C  C     . THR A 1 2559 ? 167.105 194.641 216.504 1.00 58.62  ? 2559 THR A C     1 
ATOM   8026  O  O     . THR A 1 2559 ? 167.414 193.540 216.033 1.00 63.09  ? 2559 THR A O     1 
ATOM   8027  C  CB    . THR A 1 2559 ? 168.057 195.396 218.699 1.00 64.41  ? 2559 THR A CB    1 
ATOM   8028  O  OG1   . THR A 1 2559 ? 169.099 196.167 219.308 1.00 70.95  ? 2559 THR A OG1   1 
ATOM   8029  C  CG2   . THR A 1 2559 ? 168.195 193.946 219.128 1.00 56.63  ? 2559 THR A CG2   1 
ATOM   8030  N  N     . HIS A 1 2560 ? 165.859 195.111 216.443 1.00 58.02  ? 2560 HIS A N     1 
ATOM   8031  C  CA    . HIS A 1 2560 ? 164.805 194.326 215.811 1.00 61.63  ? 2560 HIS A CA    1 
ATOM   8032  C  C     . HIS A 1 2560 ? 164.927 194.287 214.294 1.00 64.32  ? 2560 HIS A C     1 
ATOM   8033  O  O     . HIS A 1 2560 ? 164.226 193.494 213.656 1.00 66.33  ? 2560 HIS A O     1 
ATOM   8034  C  CB    . HIS A 1 2560 ? 163.431 194.872 216.208 1.00 59.51  ? 2560 HIS A CB    1 
ATOM   8035  C  CG    . HIS A 1 2560 ? 163.204 196.294 215.803 1.00 71.91  ? 2560 HIS A CG    1 
ATOM   8036  N  ND1   . HIS A 1 2560 ? 162.523 196.642 214.657 1.00 76.10  ? 2560 HIS A ND1   1 
ATOM   8037  C  CD2   . HIS A 1 2560 ? 163.566 197.458 216.394 1.00 73.69  ? 2560 HIS A CD2   1 
ATOM   8038  C  CE1   . HIS A 1 2560 ? 162.475 197.959 214.558 1.00 77.90  ? 2560 HIS A CE1   1 
ATOM   8039  N  NE2   . HIS A 1 2560 ? 163.101 198.478 215.599 1.00 78.72  ? 2560 HIS A NE2   1 
ATOM   8040  N  N     . LYS A 1 2561 ? 165.792 195.113 213.705 1.00 63.50  ? 2561 LYS A N     1 
ATOM   8041  C  CA    . LYS A 1 2561 ? 166.003 195.146 212.263 1.00 60.10  ? 2561 LYS A CA    1 
ATOM   8042  C  C     . LYS A 1 2561 ? 167.317 194.489 211.855 1.00 56.13  ? 2561 LYS A C     1 
ATOM   8043  O  O     . LYS A 1 2561 ? 167.954 194.920 210.888 1.00 56.94  ? 2561 LYS A O     1 
ATOM   8044  C  CB    . LYS A 1 2561 ? 165.950 196.587 211.755 1.00 58.36  ? 2561 LYS A CB    1 
ATOM   8045  C  CG    . LYS A 1 2561 ? 164.583 197.235 211.872 1.00 66.43  ? 2561 LYS A CG    1 
ATOM   8046  C  CD    . LYS A 1 2561 ? 164.666 198.740 211.677 1.00 73.89  ? 2561 LYS A CD    1 
ATOM   8047  C  CE    . LYS A 1 2561 ? 165.154 199.096 210.283 1.00 69.22  ? 2561 LYS A CE    1 
ATOM   8048  N  NZ    . LYS A 1 2561 ? 165.254 200.569 210.089 1.00 65.20  ? 2561 LYS A NZ    1 
ATOM   8049  N  N     . VAL A 1 2562 ? 167.737 193.453 212.575 1.00 53.34  ? 2562 VAL A N     1 
ATOM   8050  C  CA    . VAL A 1 2562 ? 168.996 192.775 212.283 1.00 46.34  ? 2562 VAL A CA    1 
ATOM   8051  C  C     . VAL A 1 2562 ? 168.774 191.795 211.138 1.00 48.55  ? 2562 VAL A C     1 
ATOM   8052  O  O     . VAL A 1 2562 ? 167.897 190.928 211.212 1.00 50.72  ? 2562 VAL A O     1 
ATOM   8053  C  CB    . VAL A 1 2562 ? 169.540 192.061 213.528 1.00 41.08  ? 2562 VAL A CB    1 
ATOM   8054  C  CG1   . VAL A 1 2562 ? 170.523 190.975 213.133 1.00 35.97  ? 2562 VAL A CG1   1 
ATOM   8055  C  CG2   . VAL A 1 2562 ? 170.201 193.060 214.461 1.00 43.99  ? 2562 VAL A CG2   1 
ATOM   8056  N  N     . ALA A 1 2563 ? 169.567 191.940 210.074 1.00 46.68  ? 2563 ALA A N     1 
ATOM   8057  C  CA    . ALA A 1 2563 ? 169.518 191.061 208.904 1.00 42.28  ? 2563 ALA A CA    1 
ATOM   8058  C  C     . ALA A 1 2563 ? 168.134 191.038 208.259 1.00 51.37  ? 2563 ALA A C     1 
ATOM   8059  O  O     . ALA A 1 2563 ? 167.723 190.028 207.683 1.00 48.11  ? 2563 ALA A O     1 
ATOM   8060  C  CB    . ALA A 1 2563 ? 169.967 189.640 209.255 1.00 35.37  ? 2563 ALA A CB    1 
ATOM   8061  N  N     . ALA A 1 2564 ? 167.406 192.146 208.351 1.00 54.10  ? 2564 ALA A N     1 
ATOM   8062  C  CA    . ALA A 1 2564 ? 166.121 192.248 207.684 1.00 53.90  ? 2564 ALA A CA    1 
ATOM   8063  C  C     . ALA A 1 2564 ? 166.320 192.453 206.182 1.00 59.72  ? 2564 ALA A C     1 
ATOM   8064  O  O     . ALA A 1 2564 ? 167.325 193.030 205.757 1.00 60.90  ? 2564 ALA A O     1 
ATOM   8065  C  CB    . ALA A 1 2564 ? 165.310 193.403 208.262 1.00 52.20  ? 2564 ALA A CB    1 
ATOM   8066  N  N     . PRO A 1 2565 ? 165.385 191.974 205.358 1.00 57.76  ? 2565 PRO A N     1 
ATOM   8067  C  CA    . PRO A 1 2565 ? 165.520 192.187 203.906 1.00 59.18  ? 2565 PRO A CA    1 
ATOM   8068  C  C     . PRO A 1 2565 ? 165.542 193.652 203.510 1.00 59.15  ? 2565 PRO A C     1 
ATOM   8069  O  O     . PRO A 1 2565 ? 166.223 194.015 202.543 1.00 56.62  ? 2565 PRO A O     1 
ATOM   8070  C  CB    . PRO A 1 2565 ? 164.295 191.460 203.330 1.00 55.75  ? 2565 PRO A CB    1 
ATOM   8071  C  CG    . PRO A 1 2565 ? 163.330 191.368 204.469 1.00 60.14  ? 2565 PRO A CG    1 
ATOM   8072  C  CD    . PRO A 1 2565 ? 164.173 191.208 205.694 1.00 57.77  ? 2565 PRO A CD    1 
ATOM   8073  N  N     . ASP A 1 2566 ? 164.822 194.494 204.254 1.00 58.86  ? 2566 ASP A N     1 
ATOM   8074  C  CA    . ASP A 1 2566 ? 164.784 195.950 203.943 1.00 55.25  ? 2566 ASP A CA    1 
ATOM   8075  C  C     . ASP A 1 2566 ? 166.108 196.594 204.369 1.00 53.48  ? 2566 ASP A C     1 
ATOM   8076  O  O     . ASP A 1 2566 ? 166.600 197.475 203.631 1.00 52.75  ? 2566 ASP A O     1 
ATOM   8077  C  CB    . ASP A 1 2566 ? 163.583 196.623 204.587 1.00 60.51  ? 2566 ASP A CB    1 
ATOM   8078  C  CG    . ASP A 1 2566 ? 163.340 198.069 204.177 1.00 65.07  ? 2566 ASP A CG    1 
ATOM   8079  O  OD1   . ASP A 1 2566 ? 164.113 198.582 203.341 1.00 66.89  ? 2566 ASP A OD1   1 
ATOM   8080  O  OD2   . ASP A 1 2566 ? 162.378 198.671 204.699 1.00 72.03  ? 2566 ASP A OD2   1 
ATOM   8081  N  N     . VAL A 1 2567 ? 166.667 196.167 205.505 1.00 49.85  ? 2567 VAL A N     1 
ATOM   8082  C  CA    . VAL A 1 2567 ? 167.916 196.794 206.036 1.00 43.30  ? 2567 VAL A CA    1 
ATOM   8083  C  C     . VAL A 1 2567 ? 169.067 196.587 205.038 1.00 41.22  ? 2567 VAL A C     1 
ATOM   8084  O  O     . VAL A 1 2567 ? 169.264 195.434 204.597 1.00 42.16  ? 2567 VAL A O     1 
ATOM   8085  C  CB    . VAL A 1 2567 ? 168.266 196.219 207.421 1.00 38.52  ? 2567 VAL A CB    1 
ATOM   8086  C  CG1   . VAL A 1 2567 ? 169.631 196.692 207.905 1.00 35.31  ? 2567 VAL A CG1   1 
ATOM   8087  C  CG2   . VAL A 1 2567 ? 167.187 196.538 208.447 1.00 46.25  ? 2567 VAL A CG2   1 
ATOM   8088  N  N     . VAL A 1 2568 ? 169.793 197.660 204.708 1.00 37.00  ? 2568 VAL A N     1 
ATOM   8089  C  CA    . VAL A 1 2568 ? 170.966 197.556 203.786 1.00 29.63  ? 2568 VAL A CA    1 
ATOM   8090  C  C     . VAL A 1 2568 ? 172.127 198.365 204.388 1.00 29.33  ? 2568 VAL A C     1 
ATOM   8091  O  O     . VAL A 1 2568 ? 171.994 199.604 204.479 1.00 34.62  ? 2568 VAL A O     1 
ATOM   8092  C  CB    . VAL A 1 2568 ? 170.630 198.051 202.367 1.00 28.15  ? 2568 VAL A CB    1 
ATOM   8093  C  CG1   . VAL A 1 2568 ? 171.846 198.001 201.450 1.00 25.91  ? 2568 VAL A CG1   1 
ATOM   8094  C  CG2   . VAL A 1 2568 ? 169.462 197.285 201.758 1.00 35.53  ? 2568 VAL A CG2   1 
ATOM   8095  N  N     . VAL A 1 2569 ? 173.214 197.692 204.775 1.00 26.22  ? 2569 VAL A N     1 
ATOM   8096  C  CA    . VAL A 1 2569 ? 174.408 198.403 205.326 1.00 23.93  ? 2569 VAL A CA    1 
ATOM   8097  C  C     . VAL A 1 2569 ? 175.031 199.241 204.199 1.00 28.16  ? 2569 VAL A C     1 
ATOM   8098  O  O     . VAL A 1 2569 ? 175.281 198.677 203.113 1.00 29.96  ? 2569 VAL A O     1 
ATOM   8099  C  CB    . VAL A 1 2569 ? 175.430 197.421 205.928 1.00 19.90  ? 2569 VAL A CB    1 
ATOM   8100  C  CG1   . VAL A 1 2569 ? 176.761 198.098 206.232 1.00 23.68  ? 2569 VAL A CG1   1 
ATOM   8101  C  CG2   . VAL A 1 2569 ? 174.882 196.721 207.166 1.00 22.42  ? 2569 VAL A CG2   1 
ATOM   8102  N  N     . PRO A 1 2570 ? 175.291 200.551 204.404 1.00 27.33  ? 2570 PRO A N     1 
ATOM   8103  C  CA    . PRO A 1 2570 ? 175.818 201.391 203.337 1.00 27.69  ? 2570 PRO A CA    1 
ATOM   8104  C  C     . PRO A 1 2570 ? 177.279 201.084 203.047 1.00 31.07  ? 2570 PRO A C     1 
ATOM   8105  O  O     . PRO A 1 2570 ? 178.103 201.131 203.980 1.00 37.71  ? 2570 PRO A O     1 
ATOM   8106  C  CB    . PRO A 1 2570 ? 175.619 202.805 203.900 1.00 31.92  ? 2570 PRO A CB    1 
ATOM   8107  C  CG    . PRO A 1 2570 ? 175.707 202.618 205.396 1.00 29.33  ? 2570 PRO A CG    1 
ATOM   8108  C  CD    . PRO A 1 2570 ? 175.087 201.256 205.657 1.00 27.67  ? 2570 PRO A CD    1 
ATOM   8109  N  N     . THR A 1 2571 ? 177.595 200.780 201.785 1.00 23.89  ? 2571 THR A N     1 
ATOM   8110  C  CA    . THR A 1 2571 ? 178.989 200.473 201.393 1.00 26.20  ? 2571 THR A CA    1 
ATOM   8111  C  C     . THR A 1 2571 ? 179.323 201.241 200.132 1.00 29.88  ? 2571 THR A C     1 
ATOM   8112  O  O     . THR A 1 2571 ? 178.380 201.698 199.452 1.00 33.09  ? 2571 THR A O     1 
ATOM   8113  C  CB    . THR A 1 2571 ? 179.150 198.966 201.197 1.00 25.51  ? 2571 THR A CB    1 
ATOM   8114  O  OG1   . THR A 1 2571 ? 178.346 198.647 200.066 1.00 33.35  ? 2571 THR A OG1   1 
ATOM   8115  C  CG2   . THR A 1 2571 ? 178.694 198.168 202.405 1.00 21.50  ? 2571 THR A CG2   1 
ATOM   8116  N  N     . LEU A 1 2572 ? 180.615 201.375 199.817 1.00 30.70  ? 2572 LEU A N     1 
ATOM   8117  C  CA    . LEU A 1 2572 ? 181.046 202.139 198.617 1.00 27.64  ? 2572 LEU A CA    1 
ATOM   8118  C  C     . LEU A 1 2572 ? 180.326 201.580 197.381 1.00 26.75  ? 2572 LEU A C     1 
ATOM   8119  O  O     . LEU A 1 2572 ? 179.778 202.384 196.600 1.00 29.54  ? 2572 LEU A O     1 
ATOM   8120  C  CB    . LEU A 1 2572 ? 182.562 202.034 198.469 1.00 28.16  ? 2572 LEU A CB    1 
ATOM   8121  C  CG    . LEU A 1 2572 ? 183.173 202.768 197.271 1.00 30.51  ? 2572 LEU A CG    1 
ATOM   8122  C  CD1   . LEU A 1 2572 ? 183.230 204.258 197.541 1.00 39.19  ? 2572 LEU A CD1   1 
ATOM   8123  C  CD2   . LEU A 1 2572 ? 184.555 202.228 196.950 1.00 33.20  ? 2572 LEU A CD2   1 
ATOM   8124  N  N     . ASP A 1 2573 ? 180.323 200.255 197.223 1.00 24.54  ? 2573 ASP A N     1 
ATOM   8125  C  CA    . ASP A 1 2573 ? 179.677 199.622 196.041 1.00 25.13  ? 2573 ASP A CA    1 
ATOM   8126  C  C     . ASP A 1 2573 ? 178.181 199.942 196.054 1.00 23.02  ? 2573 ASP A C     1 
ATOM   8127  O  O     . ASP A 1 2573 ? 177.636 200.273 194.980 1.00 26.52  ? 2573 ASP A O     1 
ATOM   8128  C  CB    . ASP A 1 2573 ? 179.940 198.125 196.007 1.00 30.32  ? 2573 ASP A CB    1 
ATOM   8129  C  CG    . ASP A 1 2573 ? 181.402 197.718 196.124 1.00 42.36  ? 2573 ASP A CG    1 
ATOM   8130  O  OD1   . ASP A 1 2573 ? 182.193 198.120 195.246 1.00 46.80  ? 2573 ASP A OD1   1 
ATOM   8131  O  OD2   . ASP A 1 2573 ? 181.736 197.006 197.094 1.00 49.46  ? 2573 ASP A OD2   1 
ATOM   8132  N  N     . THR A 1 2574 ? 177.546 199.853 197.225 1.00 21.44  ? 2574 THR A N     1 
ATOM   8133  C  CA    . THR A 1 2574 ? 176.092 200.105 197.328 1.00 22.25  ? 2574 THR A CA    1 
ATOM   8134  C  C     . THR A 1 2574 ? 175.803 201.538 196.940 1.00 23.75  ? 2574 THR A C     1 
ATOM   8135  O  O     . THR A 1 2574 ? 174.849 201.753 196.164 1.00 25.43  ? 2574 THR A O     1 
ATOM   8136  C  CB    . THR A 1 2574 ? 175.623 199.801 198.749 1.00 27.55  ? 2574 THR A CB    1 
ATOM   8137  O  OG1   . THR A 1 2574 ? 175.850 198.407 198.927 1.00 34.15  ? 2574 THR A OG1   1 
ATOM   8138  C  CG2   . THR A 1 2574 ? 174.153 200.115 198.958 1.00 26.67  ? 2574 THR A CG2   1 
ATOM   8139  N  N     . VAL A 1 2575 ? 176.595 202.490 197.441 1.00 24.15  ? 2575 VAL A N     1 
ATOM   8140  C  CA    . VAL A 1 2575 ? 176.320 203.935 197.174 1.00 20.44  ? 2575 VAL A CA    1 
ATOM   8141  C  C     . VAL A 1 2575 ? 176.622 204.243 195.697 1.00 19.74  ? 2575 VAL A C     1 
ATOM   8142  O  O     . VAL A 1 2575 ? 175.928 205.111 195.126 1.00 23.32  ? 2575 VAL A O     1 
ATOM   8143  C  CB    . VAL A 1 2575 ? 177.104 204.870 198.116 1.00 19.61  ? 2575 VAL A CB    1 
ATOM   8144  C  CG1   . VAL A 1 2575 ? 176.761 204.615 199.579 1.00 24.03  ? 2575 VAL A CG1   1 
ATOM   8145  C  CG2   . VAL A 1 2575 ? 178.608 204.789 197.889 1.00 22.59  ? 2575 VAL A CG2   1 
ATOM   8146  N  N     . ARG A 1 2576 ? 177.607 203.559 195.106 1.00 18.29  ? 2576 ARG A N     1 
ATOM   8147  C  CA    . ARG A 1 2576 ? 177.922 203.784 193.697 1.00 16.74  ? 2576 ARG A CA    1 
ATOM   8148  C  C     . ARG A 1 2576 ? 176.858 203.171 192.793 1.00 19.49  ? 2576 ARG A C     1 
ATOM   8149  O  O     . ARG A 1 2576 ? 176.357 203.826 191.867 1.00 22.10  ? 2576 ARG A O     1 
ATOM   8150  C  CB    . ARG A 1 2576 ? 179.299 203.209 193.368 1.00 15.69  ? 2576 ARG A CB    1 
ATOM   8151  C  CG    . ARG A 1 2576 ? 180.459 203.974 193.971 1.00 21.62  ? 2576 ARG A CG    1 
ATOM   8152  C  CD    . ARG A 1 2576 ? 181.789 203.436 193.475 1.00 25.38  ? 2576 ARG A CD    1 
ATOM   8153  N  NE    . ARG A 1 2576 ? 181.793 201.981 193.397 1.00 26.17  ? 2576 ARG A NE    1 
ATOM   8154  C  CZ    . ARG A 1 2576 ? 182.885 201.231 193.451 1.00 29.98  ? 2576 ARG A CZ    1 
ATOM   8155  N  NH1   . ARG A 1 2576 ? 184.087 201.768 193.578 1.00 27.32  ? 2576 ARG A NH1   1 
ATOM   8156  N  NH2   . ARG A 1 2576 ? 182.767 199.908 193.374 1.00 35.56  ? 2576 ARG A NH2   1 
ATOM   8157  N  N     . HIS A 1 2577 ? 176.489 201.916 193.057 1.00 18.86  ? 2577 HIS A N     1 
ATOM   8158  C  CA    . HIS A 1 2577 ? 175.487 201.253 192.235 1.00 14.78  ? 2577 HIS A CA    1 
ATOM   8159  C  C     . HIS A 1 2577 ? 174.110 201.873 192.416 1.00 16.49  ? 2577 HIS A C     1 
ATOM   8160  O  O     . HIS A 1 2577 ? 173.341 201.942 191.455 1.00 19.23  ? 2577 HIS A O     1 
ATOM   8161  C  CB    . HIS A 1 2577 ? 175.454 199.759 192.554 1.00 15.11  ? 2577 HIS A CB    1 
ATOM   8162  C  CG    . HIS A 1 2577 ? 176.718 199.041 192.199 1.00 18.46  ? 2577 HIS A CG    1 
ATOM   8163  N  ND1   . HIS A 1 2577 ? 177.029 197.792 192.691 1.00 23.54  ? 2577 HIS A ND1   1 
ATOM   8164  C  CD2   . HIS A 1 2577 ? 177.750 199.397 191.398 1.00 18.69  ? 2577 HIS A CD2   1 
ATOM   8165  C  CE1   . HIS A 1 2577 ? 178.198 197.410 192.209 1.00 23.61  ? 2577 HIS A CE1   1 
ATOM   8166  N  NE2   . HIS A 1 2577 ? 178.657 198.366 191.421 1.00 18.66  ? 2577 HIS A NE2   1 
ATOM   8167  N  N     . GLU A 1 2578 ? 173.778 202.332 193.626 1.00 18.00  ? 2578 GLU A N     1 
ATOM   8168  C  CA    . GLU A 1 2578 ? 172.502 203.010 193.826 1.00 16.05  ? 2578 GLU A CA    1 
ATOM   8169  C  C     . GLU A 1 2578 ? 172.431 204.296 193.017 1.00 19.85  ? 2578 GLU A C     1 
ATOM   8170  O  O     . GLU A 1 2578 ? 171.406 204.586 192.389 1.00 25.93  ? 2578 GLU A O     1 
ATOM   8171  C  CB    . GLU A 1 2578 ? 172.287 203.300 195.311 1.00 18.00  ? 2578 GLU A CB    1 
ATOM   8172  C  CG    . GLU A 1 2578 ? 171.763 202.120 196.107 1.00 24.61  ? 2578 GLU A CG    1 
ATOM   8173  C  CD    . GLU A 1 2578 ? 171.563 202.454 197.571 1.00 35.14  ? 2578 GLU A CD    1 
ATOM   8174  O  OE1   . GLU A 1 2578 ? 171.556 203.656 197.912 1.00 39.70  ? 2578 GLU A OE1   1 
ATOM   8175  O  OE2   . GLU A 1 2578 ? 171.418 201.516 198.382 1.00 35.85  ? 2578 GLU A OE2   1 
ATOM   8176  N  N     . ALA A 1 2579 ? 173.512 205.081 193.016 1.00 18.84  ? 2579 ALA A N     1 
ATOM   8177  C  CA    . ALA A 1 2579 ? 173.530 206.303 192.218 1.00 16.46  ? 2579 ALA A CA    1 
ATOM   8178  C  C     . ALA A 1 2579 ? 173.419 205.993 190.731 1.00 18.35  ? 2579 ALA A C     1 
ATOM   8179  O  O     . ALA A 1 2579 ? 172.675 206.664 190.004 1.00 21.70  ? 2579 ALA A O     1 
ATOM   8180  C  CB    . ALA A 1 2579 ? 174.800 207.100 192.504 1.00 15.70  ? 2579 ALA A CB    1 
ATOM   8181  N  N     . LEU A 1 2580 ? 174.149 204.978 190.261 1.00 19.19  ? 2580 LEU A N     1 
ATOM   8182  C  CA    . LEU A 1 2580 ? 174.082 204.618 188.847 1.00 14.95  ? 2580 LEU A CA    1 
ATOM   8183  C  C     . LEU A 1 2580 ? 172.684 204.146 188.458 1.00 16.10  ? 2580 LEU A C     1 
ATOM   8184  O  O     . LEU A 1 2580 ? 172.164 204.519 187.398 1.00 19.04  ? 2580 LEU A O     1 
ATOM   8185  C  CB    . LEU A 1 2580 ? 175.120 203.543 188.535 1.00 16.54  ? 2580 LEU A CB    1 
ATOM   8186  C  CG    . LEU A 1 2580 ? 175.374 203.245 187.058 1.00 18.67  ? 2580 LEU A CG    1 
ATOM   8187  C  CD1   . LEU A 1 2580 ? 175.980 204.454 186.367 1.00 18.89  ? 2580 LEU A CD1   1 
ATOM   8188  C  CD2   . LEU A 1 2580 ? 176.277 202.035 186.916 1.00 17.06  ? 2580 LEU A CD2   1 
ATOM   8189  N  N     . LEU A 1 2581 ? 172.060 203.325 189.305 1.00 15.76  ? 2581 LEU A N     1 
ATOM   8190  C  CA    . LEU A 1 2581 ? 170.716 202.838 189.017 1.00 14.41  ? 2581 LEU A CA    1 
ATOM   8191  C  C     . LEU A 1 2581 ? 169.699 203.968 189.043 1.00 15.47  ? 2581 LEU A C     1 
ATOM   8192  O  O     . LEU A 1 2581 ? 168.778 203.989 188.223 1.00 22.59  ? 2581 LEU A O     1 
ATOM   8193  C  CB    . LEU A 1 2581 ? 170.326 201.739 190.005 1.00 13.31  ? 2581 LEU A CB    1 
ATOM   8194  C  CG    . LEU A 1 2581 ? 171.068 200.409 189.865 1.00 11.65  ? 2581 LEU A CG    1 
ATOM   8195  C  CD1   . LEU A 1 2581 ? 170.460 199.361 190.778 1.00 17.67  ? 2581 LEU A CD1   1 
ATOM   8196  C  CD2   . LEU A 1 2581 ? 171.057 199.936 188.422 1.00 14.19  ? 2581 LEU A CD2   1 
ATOM   8197  N  N     . TYR A 1 2582 ? 169.838 204.913 189.976 1.00 15.36  ? 2582 TYR A N     1 
ATOM   8198  C  CA    . TYR A 1 2582 ? 168.949 206.070 189.978 1.00 17.65  ? 2582 TYR A CA    1 
ATOM   8199  C  C     . TYR A 1 2582 ? 169.114 206.884 188.702 1.00 23.31  ? 2582 TYR A C     1 
ATOM   8200  O  O     . TYR A 1 2582 ? 168.125 207.320 188.100 1.00 27.31  ? 2582 TYR A O     1 
ATOM   8201  C  CB    . TYR A 1 2582 ? 169.212 206.936 191.212 1.00 19.25  ? 2582 TYR A CB    1 
ATOM   8202  C  CG    . TYR A 1 2582 ? 168.371 208.195 191.284 1.00 30.18  ? 2582 TYR A CG    1 
ATOM   8203  C  CD1   . TYR A 1 2582 ? 168.777 209.366 190.655 1.00 32.92  ? 2582 TYR A CD1   1 
ATOM   8204  C  CD2   . TYR A 1 2582 ? 167.171 208.210 191.980 1.00 34.15  ? 2582 TYR A CD2   1 
ATOM   8205  C  CE1   . TYR A 1 2582 ? 168.011 210.514 190.717 1.00 36.34  ? 2582 TYR A CE1   1 
ATOM   8206  C  CE2   . TYR A 1 2582 ? 166.400 209.354 192.049 1.00 37.79  ? 2582 TYR A CE2   1 
ATOM   8207  C  CZ    . TYR A 1 2582 ? 166.824 210.502 191.416 1.00 40.49  ? 2582 TYR A CZ    1 
ATOM   8208  O  OH    . TYR A 1 2582 ? 166.059 211.644 191.481 1.00 47.00  ? 2582 TYR A OH    1 
ATOM   8209  N  N     . THR A 1 2583 ? 170.361 207.092 188.270 1.00 24.04  ? 2583 THR A N     1 
ATOM   8210  C  CA    . THR A 1 2583 ? 170.606 207.842 187.043 1.00 21.31  ? 2583 THR A CA    1 
ATOM   8211  C  C     . THR A 1 2583 ? 169.969 207.156 185.842 1.00 22.42  ? 2583 THR A C     1 
ATOM   8212  O  O     . THR A 1 2583 ? 169.323 207.810 185.015 1.00 25.99  ? 2583 THR A O     1 
ATOM   8213  C  CB    . THR A 1 2583 ? 172.110 208.016 186.828 1.00 20.94  ? 2583 THR A CB    1 
ATOM   8214  O  OG1   . THR A 1 2583 ? 172.614 209.007 187.732 1.00 30.54  ? 2583 THR A OG1   1 
ATOM   8215  C  CG2   . THR A 1 2583 ? 172.405 208.445 185.399 1.00 20.84  ? 2583 THR A CG2   1 
ATOM   8216  N  N     . TRP A 1 2584 ? 170.120 205.835 185.739 1.00 25.69  ? 2584 TRP A N     1 
ATOM   8217  C  CA    . TRP A 1 2584 ? 169.564 205.123 184.593 1.00 21.82  ? 2584 TRP A CA    1 
ATOM   8218  C  C     . TRP A 1 2584 ? 168.046 204.987 184.665 1.00 23.82  ? 2584 TRP A C     1 
ATOM   8219  O  O     . TRP A 1 2584 ? 167.385 204.947 183.622 1.00 28.51  ? 2584 TRP A O     1 
ATOM   8220  C  CB    . TRP A 1 2584 ? 170.207 203.744 184.461 1.00 16.51  ? 2584 TRP A CB    1 
ATOM   8221  C  CG    . TRP A 1 2584 ? 171.575 203.776 183.860 1.00 15.93  ? 2584 TRP A CG    1 
ATOM   8222  C  CD1   . TRP A 1 2584 ? 172.107 204.768 183.091 1.00 16.26  ? 2584 TRP A CD1   1 
ATOM   8223  C  CD2   . TRP A 1 2584 ? 172.581 202.764 183.964 1.00 18.40  ? 2584 TRP A CD2   1 
ATOM   8224  N  NE1   . TRP A 1 2584 ? 173.386 204.441 182.717 1.00 17.39  ? 2584 TRP A NE1   1 
ATOM   8225  C  CE2   . TRP A 1 2584 ? 173.701 203.214 183.239 1.00 17.82  ? 2584 TRP A CE2   1 
ATOM   8226  C  CE3   . TRP A 1 2584 ? 172.646 201.522 184.602 1.00 18.91  ? 2584 TRP A CE3   1 
ATOM   8227  C  CZ2   . TRP A 1 2584 ? 174.872 202.468 183.134 1.00 17.84  ? 2584 TRP A CZ2   1 
ATOM   8228  C  CZ3   . TRP A 1 2584 ? 173.808 200.782 184.497 1.00 20.49  ? 2584 TRP A CZ3   1 
ATOM   8229  C  CH2   . TRP A 1 2584 ? 174.906 201.257 183.768 1.00 19.91  ? 2584 TRP A CH2   1 
ATOM   8230  N  N     . LEU A 1 2585 ? 167.476 204.909 185.870 1.00 22.48  ? 2585 LEU A N     1 
ATOM   8231  C  CA    . LEU A 1 2585 ? 166.033 204.768 186.015 1.00 22.37  ? 2585 LEU A CA    1 
ATOM   8232  C  C     . LEU A 1 2585 ? 165.308 206.098 185.875 1.00 31.33  ? 2585 LEU A C     1 
ATOM   8233  O  O     . LEU A 1 2585 ? 164.108 206.114 185.584 1.00 36.29  ? 2585 LEU A O     1 
ATOM   8234  C  CB    . LEU A 1 2585 ? 165.699 204.140 187.370 1.00 20.29  ? 2585 LEU A CB    1 
ATOM   8235  C  CG    . LEU A 1 2585 ? 165.921 202.637 187.541 1.00 18.06  ? 2585 LEU A CG    1 
ATOM   8236  C  CD1   . LEU A 1 2585 ? 165.980 202.271 189.016 1.00 13.31  ? 2585 LEU A CD1   1 
ATOM   8237  C  CD2   . LEU A 1 2585 ? 164.833 201.847 186.839 1.00 23.00  ? 2585 LEU A CD2   1 
ATOM   8238  N  N     . ALA A 1 2586 ? 166.009 207.216 186.085 1.00 30.04  ? 2586 ALA A N     1 
ATOM   8239  C  CA    . ALA A 1 2586 ? 165.364 208.519 185.974 1.00 30.39  ? 2586 ALA A CA    1 
ATOM   8240  C  C     . ALA A 1 2586 ? 164.860 208.782 184.560 1.00 33.04  ? 2586 ALA A C     1 
ATOM   8241  O  O     . ALA A 1 2586 ? 163.771 209.340 184.386 1.00 37.94  ? 2586 ALA A O     1 
ATOM   8242  C  CB    . ALA A 1 2586 ? 166.326 209.620 186.412 1.00 34.97  ? 2586 ALA A CB    1 
ATOM   8243  N  N     . GLU A 1 2587 ? 165.628 208.394 183.545 1.00 24.45  ? 2587 GLU A N     1 
ATOM   8244  C  CA    . GLU A 1 2587 ? 165.192 208.517 182.161 1.00 31.33  ? 2587 GLU A CA    1 
ATOM   8245  C  C     . GLU A 1 2587 ? 164.350 207.337 181.700 1.00 33.52  ? 2587 GLU A C     1 
ATOM   8246  O  O     . GLU A 1 2587 ? 164.031 207.253 180.509 1.00 42.57  ? 2587 GLU A O     1 
ATOM   8247  C  CB    . GLU A 1 2587 ? 166.397 208.676 181.225 1.00 39.50  ? 2587 GLU A CB    1 
ATOM   8248  C  CG    . GLU A 1 2587 ? 167.117 210.008 181.348 1.00 50.12  ? 2587 GLU A CG    1 
ATOM   8249  C  CD    . GLU A 1 2587 ? 168.171 210.003 182.432 1.00 46.63  ? 2587 GLU A CD    1 
ATOM   8250  O  OE1   . GLU A 1 2587 ? 168.879 208.984 182.565 1.00 40.42  ? 2587 GLU A OE1   1 
ATOM   8251  O  OE2   . GLU A 1 2587 ? 168.290 211.016 183.150 1.00 42.04  ? 2587 GLU A OE2   1 
ATOM   8252  N  N     . HIS A 1 2588 ? 163.997 206.423 182.608 1.00 28.16  ? 2588 HIS A N     1 
ATOM   8253  C  CA    . HIS A 1 2588 ? 163.163 205.263 182.294 1.00 25.28  ? 2588 HIS A CA    1 
ATOM   8254  C  C     . HIS A 1 2588 ? 163.817 204.367 181.248 1.00 24.94  ? 2588 HIS A C     1 
ATOM   8255  O  O     . HIS A 1 2588 ? 163.135 203.663 180.499 1.00 24.73  ? 2588 HIS A O     1 
ATOM   8256  C  CB    . HIS A 1 2588 ? 161.765 205.692 181.843 1.00 25.46  ? 2588 HIS A CB    1 
ATOM   8257  C  CG    . HIS A 1 2588 ? 161.191 206.811 182.654 1.00 27.70  ? 2588 HIS A CG    1 
ATOM   8258  N  ND1   . HIS A 1 2588 ? 161.125 206.775 184.030 1.00 29.07  ? 2588 HIS A ND1   1 
ATOM   8259  C  CD2   . HIS A 1 2588 ? 160.670 208.005 182.284 1.00 30.06  ? 2588 HIS A CD2   1 
ATOM   8260  C  CE1   . HIS A 1 2588 ? 160.579 207.893 184.473 1.00 28.80  ? 2588 HIS A CE1   1 
ATOM   8261  N  NE2   . HIS A 1 2588 ? 160.295 208.657 183.433 1.00 30.69  ? 2588 HIS A NE2   1 
ATOM   8262  N  N     . LYS A 1 2589 ? 165.140 204.393 181.191 1.00 25.02  ? 2589 LYS A N     1 
ATOM   8263  C  CA    . LYS A 1 2589 ? 165.883 203.551 180.264 1.00 22.68  ? 2589 LYS A CA    1 
ATOM   8264  C  C     . LYS A 1 2589 ? 165.966 202.130 180.810 1.00 21.77  ? 2589 LYS A C     1 
ATOM   8265  O  O     . LYS A 1 2589 ? 166.334 201.943 181.974 1.00 22.92  ? 2589 LYS A O     1 
ATOM   8266  C  CB    . LYS A 1 2589 ? 167.285 204.113 180.043 1.00 24.70  ? 2589 LYS A CB    1 
ATOM   8267  C  CG    . LYS A 1 2589 ? 168.169 203.271 179.142 1.00 27.04  ? 2589 LYS A CG    1 
ATOM   8268  C  CD    . LYS A 1 2589 ? 168.389 203.949 177.800 1.00 23.01  ? 2589 LYS A CD    1 
ATOM   8269  C  CE    . LYS A 1 2589 ? 169.637 203.422 177.113 1.00 24.02  ? 2589 LYS A CE    1 
ATOM   8270  N  NZ    . LYS A 1 2589 ? 169.689 203.813 175.678 1.00 33.49  ? 2589 LYS A NZ    1 
ATOM   8271  N  N     . PRO A 1 2590 ? 165.617 201.116 180.019 1.00 21.29  ? 2590 PRO A N     1 
ATOM   8272  C  CA    . PRO A 1 2590 ? 165.746 199.735 180.499 1.00 18.91  ? 2590 PRO A CA    1 
ATOM   8273  C  C     . PRO A 1 2590 ? 167.195 199.411 180.827 1.00 16.68  ? 2590 PRO A C     1 
ATOM   8274  O  O     . PRO A 1 2590 ? 168.118 199.855 180.145 1.00 18.76  ? 2590 PRO A O     1 
ATOM   8275  C  CB    . PRO A 1 2590 ? 165.231 198.901 179.322 1.00 15.81  ? 2590 PRO A CB    1 
ATOM   8276  C  CG    . PRO A 1 2590 ? 165.419 199.778 178.133 1.00 17.35  ? 2590 PRO A CG    1 
ATOM   8277  C  CD    . PRO A 1 2590 ? 165.176 201.175 178.617 1.00 19.89  ? 2590 PRO A CD    1 
ATOM   8278  N  N     . LEU A 1 2591 ? 167.387 198.627 181.884 1.00 13.64  ? 2591 LEU A N     1 
ATOM   8279  C  CA    . LEU A 1 2591 ? 168.717 198.348 182.401 1.00 11.24  ? 2591 LEU A CA    1 
ATOM   8280  C  C     . LEU A 1 2591 ? 168.773 196.922 182.928 1.00 10.89  ? 2591 LEU A C     1 
ATOM   8281  O  O     . LEU A 1 2591 ? 167.751 196.323 183.271 1.00 13.10  ? 2591 LEU A O     1 
ATOM   8282  C  CB    . LEU A 1 2591 ? 169.105 199.369 183.484 1.00 12.62  ? 2591 LEU A CB    1 
ATOM   8283  C  CG    . LEU A 1 2591 ? 168.221 199.494 184.731 1.00 14.36  ? 2591 LEU A CG    1 
ATOM   8284  C  CD1   . LEU A 1 2591 ? 168.589 198.494 185.802 1.00 11.51  ? 2591 LEU A CD1   1 
ATOM   8285  C  CD2   . LEU A 1 2591 ? 168.270 200.902 185.288 1.00 18.20  ? 2591 LEU A CD2   1 
ATOM   8286  N  N     . VAL A 1 2592 ? 169.988 196.381 182.986 1.00 11.22  ? 2592 VAL A N     1 
ATOM   8287  C  CA    . VAL A 1 2592 ? 170.226 195.001 183.390 1.00 10.51  ? 2592 VAL A CA    1 
ATOM   8288  C  C     . VAL A 1 2592 ? 171.327 194.981 184.440 1.00 9.34   ? 2592 VAL A C     1 
ATOM   8289  O  O     . VAL A 1 2592 ? 172.369 195.622 184.264 1.00 11.05  ? 2592 VAL A O     1 
ATOM   8290  C  CB    . VAL A 1 2592 ? 170.608 194.117 182.185 1.00 10.30  ? 2592 VAL A CB    1 
ATOM   8291  C  CG1   . VAL A 1 2592 ? 171.240 192.815 182.649 1.00 9.32   ? 2592 VAL A CG1   1 
ATOM   8292  C  CG2   . VAL A 1 2592 ? 169.390 193.841 181.322 1.00 11.70  ? 2592 VAL A CG2   1 
ATOM   8293  N  N     . LEU A 1 2593 ? 171.094 194.256 185.533 1.00 9.94   ? 2593 LEU A N     1 
ATOM   8294  C  CA    . LEU A 1 2593 ? 172.113 194.019 186.548 1.00 9.80   ? 2593 LEU A CA    1 
ATOM   8295  C  C     . LEU A 1 2593 ? 172.674 192.617 186.354 1.00 10.68  ? 2593 LEU A C     1 
ATOM   8296  O  O     . LEU A 1 2593 ? 171.919 191.639 186.338 1.00 14.45  ? 2593 LEU A O     1 
ATOM   8297  C  CB    . LEU A 1 2593 ? 171.552 194.168 187.964 1.00 8.28   ? 2593 LEU A CB    1 
ATOM   8298  C  CG    . LEU A 1 2593 ? 171.307 195.569 188.528 1.00 8.69   ? 2593 LEU A CG    1 
ATOM   8299  C  CD1   . LEU A 1 2593 ? 170.075 196.187 187.916 1.00 9.00   ? 2593 LEU A CD1   1 
ATOM   8300  C  CD2   . LEU A 1 2593 ? 171.197 195.546 190.040 1.00 9.78   ? 2593 LEU A CD2   1 
ATOM   8301  N  N     . CYS A 1 2594 ? 173.990 192.521 186.209 1.00 9.48   ? 2594 CYS A N     1 
ATOM   8302  C  CA    . CYS A 1 2594 ? 174.665 191.246 186.033 1.00 10.39  ? 2594 CYS A CA    1 
ATOM   8303  C  C     . CYS A 1 2594 ? 175.582 190.977 187.218 1.00 14.62  ? 2594 CYS A C     1 
ATOM   8304  O  O     . CYS A 1 2594 ? 176.148 191.900 187.808 1.00 19.10  ? 2594 CYS A O     1 
ATOM   8305  C  CB    . CYS A 1 2594 ? 175.472 191.223 184.732 1.00 13.03  ? 2594 CYS A CB    1 
ATOM   8306  S  SG    . CYS A 1 2594 ? 175.762 189.570 184.063 1.00 23.70  ? 2594 CYS A SG    1 
ATOM   8307  N  N     . GLY A 1 2595 ? 175.728 189.700 187.576 1.00 14.60  ? 2595 GLY A N     1 
ATOM   8308  C  CA    . GLY A 1 2595 ? 176.642 189.350 188.679 1.00 17.22  ? 2595 GLY A CA    1 
ATOM   8309  C  C     . GLY A 1 2595 ? 176.299 188.012 189.297 1.00 21.82  ? 2595 GLY A C     1 
ATOM   8310  O  O     . GLY A 1 2595 ? 175.274 187.417 188.905 1.00 24.66  ? 2595 GLY A O     1 
ATOM   8311  N  N     . PRO A 1 2596 ? 177.108 187.512 190.256 1.00 23.66  ? 2596 PRO A N     1 
ATOM   8312  C  CA    . PRO A 1 2596 ? 176.863 186.215 190.865 1.00 20.27  ? 2596 PRO A CA    1 
ATOM   8313  C  C     . PRO A 1 2596 ? 175.571 186.246 191.670 1.00 21.87  ? 2596 PRO A C     1 
ATOM   8314  O  O     . PRO A 1 2596 ? 175.164 187.326 192.137 1.00 24.13  ? 2596 PRO A O     1 
ATOM   8315  C  CB    . PRO A 1 2596 ? 178.097 186.000 191.753 1.00 17.22  ? 2596 PRO A CB    1 
ATOM   8316  C  CG    . PRO A 1 2596 ? 179.110 187.003 191.248 1.00 19.55  ? 2596 PRO A CG    1 
ATOM   8317  C  CD    . PRO A 1 2596 ? 178.282 188.183 190.780 1.00 20.30  ? 2596 PRO A CD    1 
ATOM   8318  N  N     . PRO A 1 2597 ? 174.893 185.094 191.863 1.00 20.59  ? 2597 PRO A N     1 
ATOM   8319  C  CA    . PRO A 1 2597 ? 173.681 185.054 192.667 1.00 21.36  ? 2597 PRO A CA    1 
ATOM   8320  C  C     . PRO A 1 2597 ? 173.958 185.455 194.109 1.00 20.26  ? 2597 PRO A C     1 
ATOM   8321  O  O     . PRO A 1 2597 ? 174.921 184.941 194.703 1.00 23.22  ? 2597 PRO A O     1 
ATOM   8322  C  CB    . PRO A 1 2597 ? 173.239 183.588 192.545 1.00 20.88  ? 2597 PRO A CB    1 
ATOM   8323  C  CG    . PRO A 1 2597 ? 174.514 182.847 192.219 1.00 20.78  ? 2597 PRO A CG    1 
ATOM   8324  C  CD    . PRO A 1 2597 ? 175.274 183.803 191.319 1.00 21.34  ? 2597 PRO A CD    1 
ATOM   8325  N  N     . GLY A 1 2598 ? 173.130 186.344 194.665 1.00 18.06  ? 2598 GLY A N     1 
ATOM   8326  C  CA    . GLY A 1 2598 ? 173.322 186.805 196.053 1.00 17.80  ? 2598 GLY A CA    1 
ATOM   8327  C  C     . GLY A 1 2598 ? 174.285 187.973 196.118 1.00 21.33  ? 2598 GLY A C     1 
ATOM   8328  O  O     . GLY A 1 2598 ? 174.618 188.399 197.242 1.00 24.62  ? 2598 GLY A O     1 
ATOM   8329  N  N     . SER A 1 2599 ? 174.717 188.478 194.959 1.00 20.70  ? 2599 SER A N     1 
ATOM   8330  C  CA    . SER A 1 2599 ? 175.659 189.627 194.911 1.00 18.61  ? 2599 SER A CA    1 
ATOM   8331  C  C     . SER A 1 2599 ? 174.996 190.874 195.511 1.00 18.27  ? 2599 SER A C     1 
ATOM   8332  O  O     . SER A 1 2599 ? 175.726 191.714 196.080 1.00 19.13  ? 2599 SER A O     1 
ATOM   8333  C  CB    . SER A 1 2599 ? 176.131 189.879 193.505 1.00 17.74  ? 2599 SER A CB    1 
ATOM   8334  O  OG    . SER A 1 2599 ? 175.033 190.114 192.635 1.00 21.21  ? 2599 SER A OG    1 
ATOM   8335  N  N     . GLY A 1 2600 ? 173.670 190.986 195.390 1.00 17.43  ? 2600 GLY A N     1 
ATOM   8336  C  CA    . GLY A 1 2600 ? 172.945 192.153 195.930 1.00 17.46  ? 2600 GLY A CA    1 
ATOM   8337  C  C     . GLY A 1 2600 ? 172.282 192.952 194.827 1.00 16.00  ? 2600 GLY A C     1 
ATOM   8338  O  O     . GLY A 1 2600 ? 171.941 194.125 195.075 1.00 16.97  ? 2600 GLY A O     1 
ATOM   8339  N  N     . LYS A 1 2601 ? 172.103 192.346 193.651 1.00 17.84  ? 2601 LYS A N     1 
ATOM   8340  C  CA    . LYS A 1 2601 ? 171.508 193.064 192.493 1.00 14.27  ? 2601 LYS A CA    1 
ATOM   8341  C  C     . LYS A 1 2601 ? 170.082 193.517 192.845 1.00 13.74  ? 2601 LYS A C     1 
ATOM   8342  O  O     . LYS A 1 2601 ? 169.783 194.718 192.672 1.00 20.15  ? 2601 LYS A O     1 
ATOM   8343  C  CB    . LYS A 1 2601 ? 171.533 192.158 191.257 1.00 12.59  ? 2601 LYS A CB    1 
ATOM   8344  C  CG    . LYS A 1 2601 ? 172.927 191.780 190.776 1.00 11.36  ? 2601 LYS A CG    1 
ATOM   8345  C  CD    . LYS A 1 2601 ? 172.938 190.872 189.552 1.00 13.76  ? 2601 LYS A CD    1 
ATOM   8346  C  CE    . LYS A 1 2601 ? 172.426 189.498 189.846 1.00 18.83  ? 2601 LYS A CE    1 
ATOM   8347  N  NZ    . LYS A 1 2601 ? 173.274 188.804 190.817 1.00 20.08  ? 2601 LYS A NZ    1 
ATOM   8348  N  N     . THR A 1 2602 ? 169.245 192.598 193.334 1.00 13.45  ? 2602 THR A N     1 
ATOM   8349  C  CA    . THR A 1 2602 ? 167.848 192.939 193.684 1.00 14.80  ? 2602 THR A CA    1 
ATOM   8350  C  C     . THR A 1 2602 ? 167.855 193.928 194.829 1.00 17.07  ? 2602 THR A C     1 
ATOM   8351  O  O     . THR A 1 2602 ? 167.062 194.894 194.780 1.00 19.67  ? 2602 THR A O     1 
ATOM   8352  C  CB    . THR A 1 2602 ? 167.080 191.669 194.041 1.00 18.95  ? 2602 THR A CB    1 
ATOM   8353  O  OG1   . THR A 1 2602 ? 167.195 190.830 192.896 1.00 27.45  ? 2602 THR A OG1   1 
ATOM   8354  C  CG2   . THR A 1 2602 ? 165.618 191.942 194.346 1.00 21.86  ? 2602 THR A CG2   1 
ATOM   8355  N  N     . MET A 1 2603 ? 168.718 193.705 195.823 1.00 17.02  ? 2603 MET A N     1 
ATOM   8356  C  CA    . MET A 1 2603 ? 168.815 194.622 196.987 1.00 15.78  ? 2603 MET A CA    1 
ATOM   8357  C  C     . MET A 1 2603 ? 169.200 196.023 196.491 1.00 15.32  ? 2603 MET A C     1 
ATOM   8358  O  O     . MET A 1 2603 ? 168.579 197.006 196.947 1.00 20.40  ? 2603 MET A O     1 
ATOM   8359  C  CB    . MET A 1 2603 ? 169.880 194.130 197.973 1.00 16.47  ? 2603 MET A CB    1 
ATOM   8360  C  CG    . MET A 1 2603 ? 170.179 195.105 199.094 1.00 22.18  ? 2603 MET A CG    1 
ATOM   8361  S  SD    . MET A 1 2603 ? 171.590 194.581 200.088 1.00 26.43  ? 2603 MET A SD    1 
ATOM   8362  C  CE    . MET A 1 2603 ? 172.856 194.481 198.815 1.00 20.78  ? 2603 MET A CE    1 
ATOM   8363  N  N     . THR A 1 2604 ? 170.182 196.102 195.589 1.00 16.41  ? 2604 THR A N     1 
ATOM   8364  C  CA    . THR A 1 2604 ? 170.634 197.407 195.063 1.00 15.69  ? 2604 THR A CA    1 
ATOM   8365  C  C     . THR A 1 2604 ? 169.490 198.055 194.315 1.00 17.74  ? 2604 THR A C     1 
ATOM   8366  O  O     . THR A 1 2604 ? 169.307 199.281 194.468 1.00 20.42  ? 2604 THR A O     1 
ATOM   8367  C  CB    . THR A 1 2604 ? 171.854 197.214 194.165 1.00 16.07  ? 2604 THR A CB    1 
ATOM   8368  O  OG1   . THR A 1 2604 ? 172.834 196.594 194.991 1.00 20.91  ? 2604 THR A OG1   1 
ATOM   8369  C  CG2   . THR A 1 2604 ? 172.389 198.527 193.625 1.00 17.36  ? 2604 THR A CG2   1 
ATOM   8370  N  N     . LEU A 1 2605 ? 168.741 197.270 193.536 1.00 15.55  ? 2605 LEU A N     1 
ATOM   8371  C  CA    . LEU A 1 2605 ? 167.665 197.847 192.737 1.00 14.18  ? 2605 LEU A CA    1 
ATOM   8372  C  C     . LEU A 1 2605 ? 166.535 198.364 193.618 1.00 17.74  ? 2605 LEU A C     1 
ATOM   8373  O  O     . LEU A 1 2605 ? 166.005 199.455 193.383 1.00 25.13  ? 2605 LEU A O     1 
ATOM   8374  C  CB    . LEU A 1 2605 ? 167.133 196.819 191.742 1.00 12.98  ? 2605 LEU A CB    1 
ATOM   8375  C  CG    . LEU A 1 2605 ? 165.821 197.224 191.069 1.00 17.14  ? 2605 LEU A CG    1 
ATOM   8376  C  CD1   . LEU A 1 2605 ? 166.075 198.242 189.969 1.00 17.26  ? 2605 LEU A CD1   1 
ATOM   8377  C  CD2   . LEU A 1 2605 ? 165.089 196.012 190.530 1.00 20.97  ? 2605 LEU A CD2   1 
ATOM   8378  N  N     . PHE A 1 2606 ? 166.155 197.596 194.642 1.00 18.84  ? 2606 PHE A N     1 
ATOM   8379  C  CA    . PHE A 1 2606 ? 165.051 198.013 195.500 1.00 17.70  ? 2606 PHE A CA    1 
ATOM   8380  C  C     . PHE A 1 2606 ? 165.437 199.208 196.362 1.00 20.29  ? 2606 PHE A C     1 
ATOM   8381  O  O     . PHE A 1 2606 ? 164.600 200.074 196.640 1.00 25.58  ? 2606 PHE A O     1 
ATOM   8382  C  CB    . PHE A 1 2606 ? 164.582 196.844 196.365 1.00 18.45  ? 2606 PHE A CB    1 
ATOM   8383  C  CG    . PHE A 1 2606 ? 163.687 195.872 195.643 1.00 22.95  ? 2606 PHE A CG    1 
ATOM   8384  C  CD1   . PHE A 1 2606 ? 163.813 195.666 194.279 1.00 22.87  ? 2606 PHE A CD1   1 
ATOM   8385  C  CD2   . PHE A 1 2606 ? 162.715 195.167 196.331 1.00 33.87  ? 2606 PHE A CD2   1 
ATOM   8386  C  CE1   . PHE A 1 2606 ? 162.990 194.776 193.617 1.00 21.53  ? 2606 PHE A CE1   1 
ATOM   8387  C  CE2   . PHE A 1 2606 ? 161.889 194.275 195.675 1.00 36.97  ? 2606 PHE A CE2   1 
ATOM   8388  C  CZ    . PHE A 1 2606 ? 162.027 194.080 194.316 1.00 28.14  ? 2606 PHE A CZ    1 
ATOM   8389  N  N     . SER A 1 2607 ? 166.698 199.277 196.797 1.00 18.92  ? 2607 SER A N     1 
ATOM   8390  C  CA    . SER A 1 2607 ? 167.150 200.449 197.538 1.00 19.20  ? 2607 SER A CA    1 
ATOM   8391  C  C     . SER A 1 2607 ? 167.204 201.678 196.639 1.00 21.86  ? 2607 SER A C     1 
ATOM   8392  O  O     . SER A 1 2607 ? 166.911 202.794 197.085 1.00 27.62  ? 2607 SER A O     1 
ATOM   8393  C  CB    . SER A 1 2607 ? 168.513 200.178 198.170 1.00 24.26  ? 2607 SER A CB    1 
ATOM   8394  O  OG    . SER A 1 2607 ? 169.510 200.004 197.179 1.00 22.93  ? 2607 SER A OG    1 
ATOM   8395  N  N     . ALA A 1 2608 ? 167.583 201.496 195.372 1.00 21.26  ? 2608 ALA A N     1 
ATOM   8396  C  CA    . ALA A 1 2608 ? 167.562 202.607 194.428 1.00 18.57  ? 2608 ALA A CA    1 
ATOM   8397  C  C     . ALA A 1 2608 ? 166.134 203.026 194.100 1.00 19.49  ? 2608 ALA A C     1 
ATOM   8398  O  O     . ALA A 1 2608 ? 165.855 204.217 193.924 1.00 24.93  ? 2608 ALA A O     1 
ATOM   8399  C  CB    . ALA A 1 2608 ? 168.317 202.229 193.154 1.00 16.27  ? 2608 ALA A CB    1 
ATOM   8400  N  N     . LEU A 1 2609 ? 165.217 202.059 194.010 1.00 18.73  ? 2609 LEU A N     1 
ATOM   8401  C  CA    . LEU A 1 2609 ? 163.828 202.381 193.702 1.00 19.64  ? 2609 LEU A CA    1 
ATOM   8402  C  C     . LEU A 1 2609 ? 163.136 203.076 194.866 1.00 26.92  ? 2609 LEU A C     1 
ATOM   8403  O  O     . LEU A 1 2609 ? 162.133 203.770 194.662 1.00 38.65  ? 2609 LEU A O     1 
ATOM   8404  C  CB    . LEU A 1 2609 ? 163.068 201.113 193.317 1.00 16.89  ? 2609 LEU A CB    1 
ATOM   8405  C  CG    . LEU A 1 2609 ? 163.129 200.708 191.844 1.00 16.63  ? 2609 LEU A CG    1 
ATOM   8406  C  CD1   . LEU A 1 2609 ? 162.464 199.359 191.632 1.00 12.17  ? 2609 LEU A CD1   1 
ATOM   8407  C  CD2   . LEU A 1 2609 ? 162.483 201.771 190.973 1.00 19.63  ? 2609 LEU A CD2   1 
ATOM   8408  N  N     . ARG A 1 2610 ? 163.646 202.901 196.088 1.00 24.54  ? 2610 ARG A N     1 
ATOM   8409  C  CA    . ARG A 1 2610 ? 163.039 203.558 197.241 1.00 27.03  ? 2610 ARG A CA    1 
ATOM   8410  C  C     . ARG A 1 2610 ? 163.206 205.070 197.177 1.00 31.87  ? 2610 ARG A C     1 
ATOM   8411  O  O     . ARG A 1 2610 ? 162.386 205.808 197.734 1.00 34.54  ? 2610 ARG A O     1 
ATOM   8412  C  CB    . ARG A 1 2610 ? 163.638 203.004 198.533 1.00 28.82  ? 2610 ARG A CB    1 
ATOM   8413  C  CG    . ARG A 1 2610 ? 162.975 201.722 199.009 1.00 34.25  ? 2610 ARG A CG    1 
ATOM   8414  C  CD    . ARG A 1 2610 ? 163.309 201.421 200.460 1.00 34.52  ? 2610 ARG A CD    1 
ATOM   8415  N  NE    . ARG A 1 2610 ? 164.439 200.507 200.578 1.00 40.71  ? 2610 ARG A NE    1 
ATOM   8416  C  CZ    . ARG A 1 2610 ? 164.368 199.197 200.380 1.00 40.73  ? 2610 ARG A CZ    1 
ATOM   8417  N  NH1   . ARG A 1 2610 ? 163.229 198.607 200.058 1.00 37.72  ? 2610 ARG A NH1   1 
ATOM   8418  N  NH2   . ARG A 1 2610 ? 165.468 198.461 200.512 1.00 36.13  ? 2610 ARG A NH2   1 
ATOM   8419  N  N     . ALA A 1 2611 ? 164.254 205.548 196.506 1.00 31.91  ? 2611 ALA A N     1 
ATOM   8420  C  CA    . ALA A 1 2611 ? 164.442 206.977 196.298 1.00 34.28  ? 2611 ALA A CA    1 
ATOM   8421  C  C     . ALA A 1 2611 ? 163.500 207.547 195.246 1.00 38.96  ? 2611 ALA A C     1 
ATOM   8422  O  O     . ALA A 1 2611 ? 163.450 208.770 195.080 1.00 42.19  ? 2611 ALA A O     1 
ATOM   8423  C  CB    . ALA A 1 2611 ? 165.891 207.267 195.901 1.00 27.74  ? 2611 ALA A CB    1 
ATOM   8424  N  N     . LEU A 1 2612 ? 162.764 206.695 194.534 1.00 37.09  ? 2612 LEU A N     1 
ATOM   8425  C  CA    . LEU A 1 2612 ? 161.802 207.127 193.527 1.00 35.59  ? 2612 LEU A CA    1 
ATOM   8426  C  C     . LEU A 1 2612 ? 160.401 206.737 193.981 1.00 44.03  ? 2612 LEU A C     1 
ATOM   8427  O  O     . LEU A 1 2612 ? 160.001 205.573 193.827 1.00 43.75  ? 2612 LEU A O     1 
ATOM   8428  C  CB    . LEU A 1 2612 ? 162.126 206.496 192.170 1.00 29.89  ? 2612 LEU A CB    1 
ATOM   8429  C  CG    . LEU A 1 2612 ? 163.450 206.939 191.541 1.00 29.42  ? 2612 LEU A CG    1 
ATOM   8430  C  CD1   . LEU A 1 2612 ? 164.023 205.850 190.650 1.00 26.40  ? 2612 LEU A CD1   1 
ATOM   8431  C  CD2   . LEU A 1 2612 ? 163.258 208.225 190.756 1.00 35.90  ? 2612 LEU A CD2   1 
ATOM   8432  N  N     . PRO A 1 2613 ? 159.618 207.663 194.543 1.00 50.13  ? 2613 PRO A N     1 
ATOM   8433  C  CA    . PRO A 1 2613 ? 158.311 207.289 195.099 1.00 48.64  ? 2613 PRO A CA    1 
ATOM   8434  C  C     . PRO A 1 2613 ? 157.197 207.189 194.070 1.00 49.41  ? 2613 PRO A C     1 
ATOM   8435  O  O     . PRO A 1 2613 ? 156.135 206.639 194.391 1.00 49.38  ? 2613 PRO A O     1 
ATOM   8436  C  CB    . PRO A 1 2613 ? 158.024 208.413 196.106 1.00 48.07  ? 2613 PRO A CB    1 
ATOM   8437  C  CG    . PRO A 1 2613 ? 158.931 209.557 195.721 1.00 46.20  ? 2613 PRO A CG    1 
ATOM   8438  C  CD    . PRO A 1 2613 ? 159.876 209.108 194.643 1.00 44.50  ? 2613 PRO A CD    1 
ATOM   8439  N  N     . ASP A 1 2614 ? 157.397 207.696 192.857 1.00 48.45  ? 2614 ASP A N     1 
ATOM   8440  C  CA    . ASP A 1 2614 ? 156.407 207.598 191.796 1.00 48.19  ? 2614 ASP A CA    1 
ATOM   8441  C  C     . ASP A 1 2614 ? 156.583 206.345 190.950 1.00 46.82  ? 2614 ASP A C     1 
ATOM   8442  O  O     . ASP A 1 2614 ? 156.115 206.312 189.807 1.00 46.99  ? 2614 ASP A O     1 
ATOM   8443  C  CB    . ASP A 1 2614 ? 156.468 208.838 190.899 1.00 51.67  ? 2614 ASP A CB    1 
ATOM   8444  C  CG    . ASP A 1 2614 ? 155.586 209.964 191.400 1.00 64.25  ? 2614 ASP A CG    1 
ATOM   8445  O  OD1   . ASP A 1 2614 ? 154.348 209.806 191.378 1.00 67.96  ? 2614 ASP A OD1   1 
ATOM   8446  O  OD2   . ASP A 1 2614 ? 156.132 211.010 191.811 1.00 67.26  ? 2614 ASP A OD2   1 
ATOM   8447  N  N     . MET A 1 2615 ? 157.241 205.319 191.482 1.00 47.22  ? 2615 MET A N     1 
ATOM   8448  C  CA    . MET A 1 2615 ? 157.633 204.148 190.713 1.00 37.78  ? 2615 MET A CA    1 
ATOM   8449  C  C     . MET A 1 2615 ? 157.249 202.893 191.482 1.00 42.24  ? 2615 MET A C     1 
ATOM   8450  O  O     . MET A 1 2615 ? 157.676 202.709 192.626 1.00 48.57  ? 2615 MET A O     1 
ATOM   8451  C  CB    . MET A 1 2615 ? 159.138 204.171 190.447 1.00 32.13  ? 2615 MET A CB    1 
ATOM   8452  C  CG    . MET A 1 2615 ? 159.511 204.733 189.093 1.00 30.33  ? 2615 MET A CG    1 
ATOM   8453  S  SD    . MET A 1 2615 ? 161.274 204.611 188.760 1.00 56.53  ? 2615 MET A SD    1 
ATOM   8454  C  CE    . MET A 1 2615 ? 161.392 205.589 187.268 1.00 33.56  ? 2615 MET A CE    1 
ATOM   8455  N  N     . GLU A 1 2616 ? 156.452 202.033 190.855 1.00 39.32  ? 2616 GLU A N     1 
ATOM   8456  C  CA    . GLU A 1 2616 ? 156.045 200.767 191.448 1.00 38.50  ? 2616 GLU A CA    1 
ATOM   8457  C  C     . GLU A 1 2616 ? 156.655 199.614 190.663 1.00 31.00  ? 2616 GLU A C     1 
ATOM   8458  O  O     . GLU A 1 2616 ? 156.651 199.617 189.427 1.00 34.94  ? 2616 GLU A O     1 
ATOM   8459  C  CB    . GLU A 1 2616 ? 154.517 200.642 191.494 1.00 36.76  ? 2616 GLU A CB    1 
ATOM   8460  C  CG    . GLU A 1 2616 ? 153.827 200.688 190.142 1.00 46.09  ? 2616 GLU A CG    1 
ATOM   8461  C  CD    . GLU A 1 2616 ? 152.476 199.999 190.157 1.00 61.57  ? 2616 GLU A CD    1 
ATOM   8462  O  OE1   . GLU A 1 2616 ? 151.533 200.526 189.530 1.00 64.57  ? 2616 GLU A OE1   1 
ATOM   8463  O  OE2   . GLU A 1 2616 ? 152.357 198.931 190.793 1.00 60.66  ? 2616 GLU A OE2   1 
ATOM   8464  N  N     . VAL A 1 2617 ? 157.192 198.635 191.386 1.00 24.41  ? 2617 VAL A N     1 
ATOM   8465  C  CA    . VAL A 1 2617 ? 157.913 197.516 190.793 1.00 20.42  ? 2617 VAL A CA    1 
ATOM   8466  C  C     . VAL A 1 2617 ? 157.037 196.272 190.851 1.00 26.98  ? 2617 VAL A C     1 
ATOM   8467  O  O     . VAL A 1 2617 ? 156.259 196.086 191.795 1.00 34.28  ? 2617 VAL A O     1 
ATOM   8468  C  CB    . VAL A 1 2617 ? 159.267 197.282 191.496 1.00 16.83  ? 2617 VAL A CB    1 
ATOM   8469  C  CG1   . VAL A 1 2617 ? 159.069 196.731 192.901 1.00 24.36  ? 2617 VAL A CG1   1 
ATOM   8470  C  CG2   . VAL A 1 2617 ? 160.146 196.354 190.670 1.00 19.63  ? 2617 VAL A CG2   1 
ATOM   8471  N  N     . VAL A 1 2618 ? 157.145 195.436 189.821 1.00 22.58  ? 2618 VAL A N     1 
ATOM   8472  C  CA    . VAL A 1 2618 ? 156.450 194.158 189.751 1.00 22.29  ? 2618 VAL A CA    1 
ATOM   8473  C  C     . VAL A 1 2618 ? 157.482 193.082 189.447 1.00 21.43  ? 2618 VAL A C     1 
ATOM   8474  O  O     . VAL A 1 2618 ? 158.227 193.191 188.466 1.00 23.79  ? 2618 VAL A O     1 
ATOM   8475  C  CB    . VAL A 1 2618 ? 155.337 194.173 188.688 1.00 21.57  ? 2618 VAL A CB    1 
ATOM   8476  C  CG1   . VAL A 1 2618 ? 154.949 192.757 188.302 1.00 19.72  ? 2618 VAL A CG1   1 
ATOM   8477  C  CG2   . VAL A 1 2618 ? 154.133 194.939 189.200 1.00 25.24  ? 2618 VAL A CG2   1 
ATOM   8478  N  N     . GLY A 1 2619 ? 157.525 192.048 190.285 1.00 19.54  ? 2619 GLY A N     1 
ATOM   8479  C  CA    . GLY A 1 2619 ? 158.561 191.036 190.166 1.00 16.40  ? 2619 GLY A CA    1 
ATOM   8480  C  C     . GLY A 1 2619 ? 158.178 189.938 189.192 1.00 19.81  ? 2619 GLY A C     1 
ATOM   8481  O  O     . GLY A 1 2619 ? 157.095 189.352 189.290 1.00 26.15  ? 2619 GLY A O     1 
ATOM   8482  N  N     . LEU A 1 2620 ? 159.072 189.659 188.246 1.00 20.16  ? 2620 LEU A N     1 
ATOM   8483  C  CA    . LEU A 1 2620 ? 158.929 188.543 187.322 1.00 19.56  ? 2620 LEU A CA    1 
ATOM   8484  C  C     . LEU A 1 2620 ? 160.173 187.677 187.419 1.00 21.63  ? 2620 LEU A C     1 
ATOM   8485  O  O     . LEU A 1 2620 ? 161.294 188.194 187.420 1.00 28.75  ? 2620 LEU A O     1 
ATOM   8486  C  CB    . LEU A 1 2620 ? 158.730 189.016 185.876 1.00 18.06  ? 2620 LEU A CB    1 
ATOM   8487  C  CG    . LEU A 1 2620 ? 157.354 189.522 185.436 1.00 20.80  ? 2620 LEU A CG    1 
ATOM   8488  C  CD1   . LEU A 1 2620 ? 157.052 190.891 186.017 1.00 20.82  ? 2620 LEU A CD1   1 
ATOM   8489  C  CD2   . LEU A 1 2620 ? 157.258 189.551 183.920 1.00 24.51  ? 2620 LEU A CD2   1 
ATOM   8490  N  N     . ASN A 1 2621 ? 159.977 186.365 187.504 1.00 19.39  ? 2621 ASN A N     1 
ATOM   8491  C  CA    . ASN A 1 2621 ? 161.074 185.407 187.596 1.00 19.80  ? 2621 ASN A CA    1 
ATOM   8492  C  C     . ASN A 1 2621 ? 161.029 184.508 186.370 1.00 21.22  ? 2621 ASN A C     1 
ATOM   8493  O  O     . ASN A 1 2621 ? 160.143 183.656 186.249 1.00 27.97  ? 2621 ASN A O     1 
ATOM   8494  C  CB    . ASN A 1 2621 ? 160.981 184.594 188.884 1.00 23.56  ? 2621 ASN A CB    1 
ATOM   8495  C  CG    . ASN A 1 2621 ? 160.886 185.471 190.113 1.00 29.09  ? 2621 ASN A CG    1 
ATOM   8496  O  OD1   . ASN A 1 2621 ? 159.801 185.898 190.499 1.00 30.07  ? 2621 ASN A OD1   1 
ATOM   8497  N  ND2   . ASN A 1 2621 ? 162.021 185.724 190.750 1.00 32.42  ? 2621 ASN A ND2   1 
ATOM   8498  N  N     . PHE A 1 2622 ? 161.983 184.699 185.465 1.00 21.20  ? 2622 PHE A N     1 
ATOM   8499  C  CA    . PHE A 1 2622 ? 162.031 183.920 184.240 1.00 20.44  ? 2622 PHE A CA    1 
ATOM   8500  C  C     . PHE A 1 2622 ? 162.681 182.566 184.494 1.00 21.52  ? 2622 PHE A C     1 
ATOM   8501  O  O     . PHE A 1 2622 ? 163.539 182.415 185.368 1.00 26.44  ? 2622 PHE A O     1 
ATOM   8502  C  CB    . PHE A 1 2622 ? 162.809 184.662 183.152 1.00 16.55  ? 2622 PHE A CB    1 
ATOM   8503  C  CG    . PHE A 1 2622 ? 162.101 185.867 182.593 1.00 12.49  ? 2622 PHE A CG    1 
ATOM   8504  C  CD1   . PHE A 1 2622 ? 160.914 186.323 183.141 1.00 17.29  ? 2622 PHE A CD1   1 
ATOM   8505  C  CD2   . PHE A 1 2622 ? 162.638 186.551 181.515 1.00 11.20  ? 2622 PHE A CD2   1 
ATOM   8506  C  CE1   . PHE A 1 2622 ? 160.276 187.431 182.620 1.00 16.98  ? 2622 PHE A CE1   1 
ATOM   8507  C  CE2   . PHE A 1 2622 ? 162.005 187.658 180.992 1.00 12.14  ? 2622 PHE A CE2   1 
ATOM   8508  C  CZ    . PHE A 1 2622 ? 160.822 188.099 181.545 1.00 14.52  ? 2622 PHE A CZ    1 
ATOM   8509  N  N     . SER A 1 2623 ? 162.259 181.574 183.716 1.00 18.78  ? 2623 SER A N     1 
ATOM   8510  C  CA    . SER A 1 2623 ? 162.853 180.247 183.722 1.00 18.14  ? 2623 SER A CA    1 
ATOM   8511  C  C     . SER A 1 2623 ? 163.100 179.823 182.280 1.00 18.63  ? 2623 SER A C     1 
ATOM   8512  O  O     . SER A 1 2623 ? 162.872 180.588 181.339 1.00 24.22  ? 2623 SER A O     1 
ATOM   8513  C  CB    . SER A 1 2623 ? 161.961 179.238 184.455 1.00 23.64  ? 2623 SER A CB    1 
ATOM   8514  O  OG    . SER A 1 2623 ? 160.700 179.113 183.823 1.00 29.05  ? 2623 SER A OG    1 
ATOM   8515  N  N     . SER A 1 2624 ? 163.573 178.588 182.103 1.00 17.09  ? 2624 SER A N     1 
ATOM   8516  C  CA    . SER A 1 2624 ? 163.858 178.092 180.762 1.00 18.90  ? 2624 SER A CA    1 
ATOM   8517  C  C     . SER A 1 2624 ? 162.601 177.960 179.911 1.00 24.67  ? 2624 SER A C     1 
ATOM   8518  O  O     . SER A 1 2624 ? 162.703 177.915 178.681 1.00 31.81  ? 2624 SER A O     1 
ATOM   8519  C  CB    . SER A 1 2624 ? 164.575 176.745 180.840 1.00 26.50  ? 2624 SER A CB    1 
ATOM   8520  O  OG    . SER A 1 2624 ? 163.690 175.720 181.253 1.00 38.33  ? 2624 SER A OG    1 
ATOM   8521  N  N     . ALA A 1 2625 ? 161.425 177.903 180.532 1.00 22.67  ? 2625 ALA A N     1 
ATOM   8522  C  CA    . ALA A 1 2625 ? 160.161 177.782 179.820 1.00 24.56  ? 2625 ALA A CA    1 
ATOM   8523  C  C     . ALA A 1 2625 ? 159.417 179.106 179.715 1.00 23.08  ? 2625 ALA A C     1 
ATOM   8524  O  O     . ALA A 1 2625 ? 158.224 179.110 179.396 1.00 29.25  ? 2625 ALA A O     1 
ATOM   8525  C  CB    . ALA A 1 2625 ? 159.273 176.738 180.497 1.00 29.58  ? 2625 ALA A CB    1 
ATOM   8526  N  N     . THR A 1 2626 ? 160.089 180.223 179.977 1.00 21.48  ? 2626 THR A N     1 
ATOM   8527  C  CA    . THR A 1 2626 ? 159.424 181.519 179.969 1.00 18.96  ? 2626 THR A CA    1 
ATOM   8528  C  C     . THR A 1 2626 ? 159.082 181.939 178.545 1.00 24.62  ? 2626 THR A C     1 
ATOM   8529  O  O     . THR A 1 2626 ? 159.905 181.818 177.632 1.00 30.00  ? 2626 THR A O     1 
ATOM   8530  C  CB    . THR A 1 2626 ? 160.309 182.571 180.634 1.00 14.02  ? 2626 THR A CB    1 
ATOM   8531  O  OG1   . THR A 1 2626 ? 160.598 182.167 181.977 1.00 17.97  ? 2626 THR A OG1   1 
ATOM   8532  C  CG2   . THR A 1 2626 ? 159.609 183.920 180.661 1.00 14.81  ? 2626 THR A CG2   1 
ATOM   8533  N  N     . THR A 1 2627 ? 157.867 182.432 178.363 1.00 26.78  ? 2627 THR A N     1 
ATOM   8534  C  CA    . THR A 1 2627 ? 157.350 182.925 177.098 1.00 24.17  ? 2627 THR A CA    1 
ATOM   8535  C  C     . THR A 1 2627 ? 156.753 184.304 177.325 1.00 24.43  ? 2627 THR A C     1 
ATOM   8536  O  O     . THR A 1 2627 ? 156.457 184.677 178.465 1.00 27.29  ? 2627 THR A O     1 
ATOM   8537  C  CB    . THR A 1 2627 ? 156.286 181.976 176.524 1.00 29.40  ? 2627 THR A CB    1 
ATOM   8538  O  OG1   . THR A 1 2627 ? 155.389 181.572 177.565 1.00 33.64  ? 2627 THR A OG1   1 
ATOM   8539  C  CG2   . THR A 1 2627 ? 156.942 180.746 175.916 1.00 30.16  ? 2627 THR A CG2   1 
ATOM   8540  N  N     . PRO A 1 2628 ? 156.577 185.101 176.257 1.00 21.31  ? 2628 PRO A N     1 
ATOM   8541  C  CA    . PRO A 1 2628 ? 155.946 186.421 176.415 1.00 19.54  ? 2628 PRO A CA    1 
ATOM   8542  C  C     . PRO A 1 2628 ? 154.568 186.375 177.062 1.00 25.08  ? 2628 PRO A C     1 
ATOM   8543  O  O     . PRO A 1 2628 ? 154.018 187.417 177.432 1.00 24.31  ? 2628 PRO A O     1 
ATOM   8544  C  CB    . PRO A 1 2628 ? 155.862 186.939 174.974 1.00 16.71  ? 2628 PRO A CB    1 
ATOM   8545  C  CG    . PRO A 1 2628 ? 156.982 186.270 174.275 1.00 18.56  ? 2628 PRO A CG    1 
ATOM   8546  C  CD    . PRO A 1 2628 ? 157.129 184.914 174.903 1.00 21.06  ? 2628 PRO A CD    1 
ATOM   8547  N  N     . GLU A 1 2629 ? 154.000 185.174 177.199 1.00 28.78  ? 2629 GLU A N     1 
ATOM   8548  C  CA    . GLU A 1 2629 ? 152.707 185.037 177.860 1.00 27.35  ? 2629 GLU A CA    1 
ATOM   8549  C  C     . GLU A 1 2629 ? 152.769 185.471 179.318 1.00 24.01  ? 2629 GLU A C     1 
ATOM   8550  O  O     . GLU A 1 2629 ? 151.786 185.997 179.845 1.00 30.89  ? 2629 GLU A O     1 
ATOM   8551  C  CB    . GLU A 1 2629 ? 152.211 183.595 177.752 1.00 33.68  ? 2629 GLU A CB    1 
ATOM   8552  C  CG    . GLU A 1 2629 ? 152.326 183.001 176.354 1.00 49.20  ? 2629 GLU A CG    1 
ATOM   8553  C  CD    . GLU A 1 2629 ? 151.321 183.585 175.375 1.00 65.77  ? 2629 GLU A CD    1 
ATOM   8554  O  OE1   . GLU A 1 2629 ? 150.432 184.351 175.804 1.00 61.00  ? 2629 GLU A OE1   1 
ATOM   8555  O  OE2   . GLU A 1 2629 ? 151.423 183.278 174.168 1.00 69.70  ? 2629 GLU A OE2   1 
ATOM   8556  N  N     . LEU A 1 2630 ? 153.904 185.260 179.987 1.00 21.72  ? 2630 LEU A N     1 
ATOM   8557  C  CA    . LEU A 1 2630 ? 154.052 185.738 181.359 1.00 23.66  ? 2630 LEU A CA    1 
ATOM   8558  C  C     . LEU A 1 2630 ? 153.982 187.260 181.417 1.00 26.49  ? 2630 LEU A C     1 
ATOM   8559  O  O     . LEU A 1 2630 ? 153.315 187.836 182.288 1.00 31.40  ? 2630 LEU A O     1 
ATOM   8560  C  CB    . LEU A 1 2630 ? 155.368 185.230 181.948 1.00 23.78  ? 2630 LEU A CB    1 
ATOM   8561  C  CG    . LEU A 1 2630 ? 155.677 185.608 183.397 1.00 20.44  ? 2630 LEU A CG    1 
ATOM   8562  C  CD1   . LEU A 1 2630 ? 154.949 184.682 184.356 1.00 34.83  ? 2630 LEU A CD1   1 
ATOM   8563  C  CD2   . LEU A 1 2630 ? 157.175 185.571 183.648 1.00 12.20  ? 2630 LEU A CD2   1 
ATOM   8564  N  N     . LEU A 1 2631 ? 154.661 187.929 180.483 1.00 23.30  ? 2631 LEU A N     1 
ATOM   8565  C  CA    . LEU A 1 2631 ? 154.589 189.385 180.414 1.00 19.31  ? 2631 LEU A CA    1 
ATOM   8566  C  C     . LEU A 1 2631 ? 153.174 189.848 180.095 1.00 21.62  ? 2631 LEU A C     1 
ATOM   8567  O  O     . LEU A 1 2631 ? 152.712 190.863 180.626 1.00 25.58  ? 2631 LEU A O     1 
ATOM   8568  C  CB    . LEU A 1 2631 ? 155.572 189.912 179.370 1.00 19.52  ? 2631 LEU A CB    1 
ATOM   8569  C  CG    . LEU A 1 2631 ? 157.055 189.878 179.739 1.00 17.53  ? 2631 LEU A CG    1 
ATOM   8570  C  CD1   . LEU A 1 2631 ? 157.905 189.752 178.489 1.00 18.41  ? 2631 LEU A CD1   1 
ATOM   8571  C  CD2   . LEU A 1 2631 ? 157.440 191.115 180.524 1.00 15.15  ? 2631 LEU A CD2   1 
ATOM   8572  N  N     . LEU A 1 2632 ? 152.475 189.123 179.220 1.00 20.38  ? 2632 LEU A N     1 
ATOM   8573  C  CA    . LEU A 1 2632 ? 151.099 189.486 178.896 1.00 19.53  ? 2632 LEU A CA    1 
ATOM   8574  C  C     . LEU A 1 2632 ? 150.182 189.325 180.104 1.00 22.43  ? 2632 LEU A C     1 
ATOM   8575  O  O     . LEU A 1 2632 ? 149.288 190.149 180.324 1.00 28.04  ? 2632 LEU A O     1 
ATOM   8576  C  CB    . LEU A 1 2632 ? 150.599 188.651 177.719 1.00 24.75  ? 2632 LEU A CB    1 
ATOM   8577  C  CG    . LEU A 1 2632 ? 151.320 188.897 176.392 1.00 19.81  ? 2632 LEU A CG    1 
ATOM   8578  C  CD1   . LEU A 1 2632 ? 150.738 188.029 175.290 1.00 24.58  ? 2632 LEU A CD1   1 
ATOM   8579  C  CD2   . LEU A 1 2632 ? 151.261 190.368 176.011 1.00 18.32  ? 2632 LEU A CD2   1 
ATOM   8580  N  N     . LYS A 1 2633 ? 150.383 188.268 180.895 1.00 21.99  ? 2633 LYS A N     1 
ATOM   8581  C  CA    . LYS A 1 2633 ? 149.615 188.103 182.125 1.00 23.89  ? 2633 LYS A CA    1 
ATOM   8582  C  C     . LYS A 1 2633 ? 149.895 189.235 183.103 1.00 28.31  ? 2633 LYS A C     1 
ATOM   8583  O  O     . LYS A 1 2633 ? 148.974 189.758 183.744 1.00 34.11  ? 2633 LYS A O     1 
ATOM   8584  C  CB    . LYS A 1 2633 ? 149.931 186.755 182.774 1.00 27.01  ? 2633 LYS A CB    1 
ATOM   8585  C  CG    . LYS A 1 2633 ? 149.521 185.543 181.959 1.00 27.99  ? 2633 LYS A CG    1 
ATOM   8586  C  CD    . LYS A 1 2633 ? 149.904 184.257 182.673 1.00 38.56  ? 2633 LYS A CD    1 
ATOM   8587  C  CE    . LYS A 1 2633 ? 150.310 183.173 181.689 1.00 47.09  ? 2633 LYS A CE    1 
ATOM   8588  N  NZ    . LYS A 1 2633 ? 151.452 182.364 182.197 1.00 46.27  ? 2633 LYS A NZ    1 
ATOM   8589  N  N     . THR A 1 2634 ? 151.167 189.622 183.237 1.00 27.00  ? 2634 THR A N     1 
ATOM   8590  C  CA    . THR A 1 2634 ? 151.508 190.744 184.107 1.00 23.52  ? 2634 THR A CA    1 
ATOM   8591  C  C     . THR A 1 2634 ? 150.845 192.032 183.629 1.00 20.66  ? 2634 THR A C     1 
ATOM   8592  O  O     . THR A 1 2634 ? 150.318 192.807 184.437 1.00 25.98  ? 2634 THR A O     1 
ATOM   8593  C  CB    . THR A 1 2634 ? 153.027 190.913 184.172 1.00 26.28  ? 2634 THR A CB    1 
ATOM   8594  O  OG1   . THR A 1 2634 ? 153.609 189.763 184.797 1.00 30.64  ? 2634 THR A OG1   1 
ATOM   8595  C  CG2   . THR A 1 2634 ? 153.396 192.155 184.968 1.00 28.81  ? 2634 THR A CG2   1 
ATOM   8596  N  N     . PHE A 1 2635 ? 150.856 192.270 182.316 1.00 20.47  ? 2635 PHE A N     1 
ATOM   8597  C  CA    . PHE A 1 2635 ? 150.204 193.452 181.762 1.00 21.85  ? 2635 PHE A CA    1 
ATOM   8598  C  C     . PHE A 1 2635 ? 148.705 193.431 182.025 1.00 27.35  ? 2635 PHE A C     1 
ATOM   8599  O  O     . PHE A 1 2635 ? 148.113 194.457 182.374 1.00 29.85  ? 2635 PHE A O     1 
ATOM   8600  C  CB    . PHE A 1 2635 ? 150.474 193.544 180.260 1.00 24.30  ? 2635 PHE A CB    1 
ATOM   8601  C  CG    . PHE A 1 2635 ? 151.892 193.894 179.916 1.00 19.96  ? 2635 PHE A CG    1 
ATOM   8602  C  CD1   . PHE A 1 2635 ? 152.691 194.575 180.816 1.00 19.50  ? 2635 PHE A CD1   1 
ATOM   8603  C  CD2   . PHE A 1 2635 ? 152.426 193.540 178.689 1.00 16.77  ? 2635 PHE A CD2   1 
ATOM   8604  C  CE1   . PHE A 1 2635 ? 153.994 194.898 180.498 1.00 18.86  ? 2635 PHE A CE1   1 
ATOM   8605  C  CE2   . PHE A 1 2635 ? 153.728 193.859 178.366 1.00 15.92  ? 2635 PHE A CE2   1 
ATOM   8606  C  CZ    . PHE A 1 2635 ? 154.514 194.539 179.272 1.00 17.71  ? 2635 PHE A CZ    1 
ATOM   8607  N  N     . ASP A 1 2636 ? 148.071 192.270 181.851 1.00 27.09  ? 2636 ASP A N     1 
ATOM   8608  C  CA    . ASP A 1 2636 ? 146.635 192.169 182.084 1.00 31.30  ? 2636 ASP A CA    1 
ATOM   8609  C  C     . ASP A 1 2636 ? 146.295 192.409 183.549 1.00 33.07  ? 2636 ASP A C     1 
ATOM   8610  O  O     . ASP A 1 2636 ? 145.283 193.048 183.860 1.00 34.76  ? 2636 ASP A O     1 
ATOM   8611  C  CB    . ASP A 1 2636 ? 146.126 190.802 181.629 1.00 31.80  ? 2636 ASP A CB    1 
ATOM   8612  C  CG    . ASP A 1 2636 ? 145.754 190.779 180.160 1.00 54.43  ? 2636 ASP A CG    1 
ATOM   8613  O  OD1   . ASP A 1 2636 ? 146.381 190.013 179.399 1.00 53.90  ? 2636 ASP A OD1   1 
ATOM   8614  O  OD2   . ASP A 1 2636 ? 144.835 191.527 179.766 1.00 62.25  ? 2636 ASP A OD2   1 
ATOM   8615  N  N     . HIS A 1 2637 ? 147.125 191.904 184.463 1.00 28.85  ? 2637 HIS A N     1 
ATOM   8616  C  CA    . HIS A 1 2637 ? 146.836 192.063 185.884 1.00 24.50  ? 2637 HIS A CA    1 
ATOM   8617  C  C     . HIS A 1 2637 ? 147.068 193.497 186.346 1.00 21.63  ? 2637 HIS A C     1 
ATOM   8618  O  O     . HIS A 1 2637 ? 146.256 194.058 187.090 1.00 24.58  ? 2637 HIS A O     1 
ATOM   8619  C  CB    . HIS A 1 2637 ? 147.682 191.091 186.706 1.00 30.98  ? 2637 HIS A CB    1 
ATOM   8620  C  CG    . HIS A 1 2637 ? 147.348 191.088 188.166 1.00 38.29  ? 2637 HIS A CG    1 
ATOM   8621  N  ND1   . HIS A 1 2637 ? 147.770 192.077 189.028 1.00 34.52  ? 2637 HIS A ND1   1 
ATOM   8622  C  CD2   . HIS A 1 2637 ? 146.627 190.220 188.913 1.00 46.37  ? 2637 HIS A CD2   1 
ATOM   8623  C  CE1   . HIS A 1 2637 ? 147.325 191.817 190.244 1.00 38.47  ? 2637 HIS A CE1   1 
ATOM   8624  N  NE2   . HIS A 1 2637 ? 146.629 190.696 190.202 1.00 46.00  ? 2637 HIS A NE2   1 
ATOM   8625  N  N     . TYR A 1 2638 ? 148.172 194.111 185.916 1.00 24.23  ? 2638 TYR A N     1 
ATOM   8626  C  CA    . TYR A 1 2638 ? 148.573 195.403 186.457 1.00 23.91  ? 2638 TYR A CA    1 
ATOM   8627  C  C     . TYR A 1 2638 ? 148.224 196.586 185.564 1.00 25.95  ? 2638 TYR A C     1 
ATOM   8628  O  O     . TYR A 1 2638 ? 148.101 197.705 186.074 1.00 28.34  ? 2638 TYR A O     1 
ATOM   8629  C  CB    . TYR A 1 2638 ? 150.082 195.417 186.731 1.00 21.71  ? 2638 TYR A CB    1 
ATOM   8630  C  CG    . TYR A 1 2638 ? 150.481 194.641 187.964 1.00 21.34  ? 2638 TYR A CG    1 
ATOM   8631  C  CD1   . TYR A 1 2638 ? 150.410 195.218 189.224 1.00 22.62  ? 2638 TYR A CD1   1 
ATOM   8632  C  CD2   . TYR A 1 2638 ? 150.927 193.330 187.869 1.00 23.92  ? 2638 TYR A CD2   1 
ATOM   8633  C  CE1   . TYR A 1 2638 ? 150.772 194.513 190.354 1.00 26.85  ? 2638 TYR A CE1   1 
ATOM   8634  C  CE2   . TYR A 1 2638 ? 151.292 192.617 188.994 1.00 27.81  ? 2638 TYR A CE2   1 
ATOM   8635  C  CZ    . TYR A 1 2638 ? 151.213 193.213 190.233 1.00 32.43  ? 2638 TYR A CZ    1 
ATOM   8636  O  OH    . TYR A 1 2638 ? 151.575 192.507 191.357 1.00 41.65  ? 2638 TYR A OH    1 
ATOM   8637  N  N     . CYS A 1 2639 ? 148.065 196.379 184.264 1.00 27.60  ? 2639 CYS A N     1 
ATOM   8638  C  CA    . CYS A 1 2639 ? 147.772 197.454 183.327 1.00 29.64  ? 2639 CYS A CA    1 
ATOM   8639  C  C     . CYS A 1 2639 ? 146.414 197.215 182.675 1.00 36.87  ? 2639 CYS A C     1 
ATOM   8640  O  O     . CYS A 1 2639 ? 145.749 196.205 182.918 1.00 38.91  ? 2639 CYS A O     1 
ATOM   8641  C  CB    . CYS A 1 2639 ? 148.873 197.568 182.269 1.00 29.93  ? 2639 CYS A CB    1 
ATOM   8642  S  SG    . CYS A 1 2639 ? 150.550 197.460 182.921 1.00 34.01  ? 2639 CYS A SG    1 
ATOM   8643  N  N     . GLU A 1 2640 ? 146.005 198.164 181.836 1.00 37.21  ? 2640 GLU A N     1 
ATOM   8644  C  CA    . GLU A 1 2640 ? 144.750 198.067 181.107 1.00 36.71  ? 2640 GLU A CA    1 
ATOM   8645  C  C     . GLU A 1 2640 ? 144.923 198.679 179.725 1.00 38.28  ? 2640 GLU A C     1 
ATOM   8646  O  O     . GLU A 1 2640 ? 145.739 199.583 179.527 1.00 37.26  ? 2640 GLU A O     1 
ATOM   8647  C  CB    . GLU A 1 2640 ? 143.605 198.761 181.857 1.00 39.68  ? 2640 GLU A CB    1 
ATOM   8648  C  CG    . GLU A 1 2640 ? 143.767 200.266 181.987 1.00 49.46  ? 2640 GLU A CG    1 
ATOM   8649  C  CD    . GLU A 1 2640 ? 142.653 200.903 182.794 1.00 61.36  ? 2640 GLU A CD    1 
ATOM   8650  O  OE1   . GLU A 1 2640 ? 141.768 200.165 183.275 1.00 57.48  ? 2640 GLU A OE1   1 
ATOM   8651  O  OE2   . GLU A 1 2640 ? 142.662 202.142 182.948 1.00 77.04  ? 2640 GLU A OE2   1 
ATOM   8652  N  N     . TYR A 1 2641 ? 144.147 198.175 178.771 1.00 38.23  ? 2641 TYR A N     1 
ATOM   8653  C  CA    . TYR A 1 2641 ? 144.186 198.646 177.394 1.00 36.02  ? 2641 TYR A CA    1 
ATOM   8654  C  C     . TYR A 1 2641 ? 143.085 199.675 177.176 1.00 43.91  ? 2641 TYR A C     1 
ATOM   8655  O  O     . TYR A 1 2641 ? 141.926 199.436 177.529 1.00 55.64  ? 2641 TYR A O     1 
ATOM   8656  C  CB    . TYR A 1 2641 ? 144.016 197.487 176.409 1.00 38.44  ? 2641 TYR A CB    1 
ATOM   8657  C  CG    . TYR A 1 2641 ? 145.090 196.424 176.486 1.00 37.78  ? 2641 TYR A CG    1 
ATOM   8658  C  CD1   . TYR A 1 2641 ? 145.065 195.451 177.476 1.00 42.70  ? 2641 TYR A CD1   1 
ATOM   8659  C  CD2   . TYR A 1 2641 ? 146.123 196.386 175.559 1.00 32.79  ? 2641 TYR A CD2   1 
ATOM   8660  C  CE1   . TYR A 1 2641 ? 146.041 194.476 177.545 1.00 40.79  ? 2641 TYR A CE1   1 
ATOM   8661  C  CE2   . TYR A 1 2641 ? 147.103 195.414 175.620 1.00 31.36  ? 2641 TYR A CE2   1 
ATOM   8662  C  CZ    . TYR A 1 2641 ? 147.057 194.463 176.615 1.00 35.62  ? 2641 TYR A CZ    1 
ATOM   8663  O  OH    . TYR A 1 2641 ? 148.031 193.493 176.680 1.00 33.32  ? 2641 TYR A OH    1 
ATOM   8664  N  N     . ARG A 1 2642 ? 143.450 200.815 176.594 1.00 36.51  ? 2642 ARG A N     1 
ATOM   8665  C  CA    . ARG A 1 2642 ? 142.492 201.855 176.253 1.00 43.73  ? 2642 ARG A CA    1 
ATOM   8666  C  C     . ARG A 1 2642 ? 142.709 202.286 174.810 1.00 45.42  ? 2642 ARG A C     1 
ATOM   8667  O  O     . ARG A 1 2642 ? 143.826 202.231 174.290 1.00 47.59  ? 2642 ARG A O     1 
ATOM   8668  C  CB    . ARG A 1 2642 ? 142.603 203.067 177.192 1.00 42.05  ? 2642 ARG A CB    1 
ATOM   8669  C  CG    . ARG A 1 2642 ? 143.859 203.901 177.007 1.00 45.40  ? 2642 ARG A CG    1 
ATOM   8670  C  CD    . ARG A 1 2642 ? 143.757 205.211 177.772 1.00 50.03  ? 2642 ARG A CD    1 
ATOM   8671  N  NE    . ARG A 1 2642 ? 144.998 205.974 177.729 1.00 52.95  ? 2642 ARG A NE    1 
ATOM   8672  C  CZ    . ARG A 1 2642 ? 146.020 205.791 178.552 1.00 54.22  ? 2642 ARG A CZ    1 
ATOM   8673  N  NH1   . ARG A 1 2642 ? 145.986 204.871 179.502 1.00 54.29  ? 2642 ARG A NH1   1 
ATOM   8674  N  NH2   . ARG A 1 2642 ? 147.104 206.551 178.421 1.00 52.07  ? 2642 ARG A NH2   1 
ATOM   8675  N  N     . ARG A 1 2643 ? 141.624 202.707 174.165 1.00 48.75  ? 2643 ARG A N     1 
ATOM   8676  C  CA    . ARG A 1 2643 ? 141.647 203.087 172.753 1.00 53.39  ? 2643 ARG A CA    1 
ATOM   8677  C  C     . ARG A 1 2643 ? 141.735 204.606 172.657 1.00 55.41  ? 2643 ARG A C     1 
ATOM   8678  O  O     . ARG A 1 2643 ? 140.724 205.308 172.638 1.00 61.47  ? 2643 ARG A O     1 
ATOM   8679  C  CB    . ARG A 1 2643 ? 140.418 202.555 172.026 1.00 64.16  ? 2643 ARG A CB    1 
ATOM   8680  C  CG    . ARG A 1 2643 ? 140.351 201.040 171.928 1.00 62.52  ? 2643 ARG A CG    1 
ATOM   8681  C  CD    . ARG A 1 2643 ? 139.126 200.477 171.170 1.00 68.36  ? 2643 ARG A CD    1 
ATOM   8682  N  NE    . ARG A 1 2643 ? 138.729 201.197 169.961 1.00 79.16  ? 2643 ARG A NE    1 
ATOM   8683  C  CZ    . ARG A 1 2643 ? 138.007 202.312 169.928 1.00 80.77  ? 2643 ARG A CZ    1 
ATOM   8684  N  NH1   . ARG A 1 2643 ? 137.494 202.840 171.027 1.00 70.24  ? 2643 ARG A NH1   1 
ATOM   8685  N  NH2   . ARG A 1 2643 ? 137.773 202.896 168.756 1.00 77.48  ? 2643 ARG A NH2   1 
ATOM   8686  N  N     . THR A 1 2644 ? 142.960 205.112 172.598 1.00 51.46  ? 2644 THR A N     1 
ATOM   8687  C  CA    . THR A 1 2644 ? 143.181 206.519 172.317 1.00 59.75  ? 2644 THR A CA    1 
ATOM   8688  C  C     . THR A 1 2644 ? 142.934 206.798 170.838 1.00 66.63  ? 2644 THR A C     1 
ATOM   8689  O  O     . THR A 1 2644 ? 142.955 205.881 170.013 1.00 68.93  ? 2644 THR A O     1 
ATOM   8690  C  CB    . THR A 1 2644 ? 144.603 206.914 172.703 1.00 57.30  ? 2644 THR A CB    1 
ATOM   8691  O  OG1   . THR A 1 2644 ? 145.518 206.450 171.702 1.00 65.80  ? 2644 THR A OG1   1 
ATOM   8692  C  CG2   . THR A 1 2644 ? 144.975 206.309 174.047 1.00 50.66  ? 2644 THR A CG2   1 
ATOM   8693  N  N     . PRO A 1 2645 ? 142.672 208.058 170.474 1.00 66.76  ? 2645 PRO A N     1 
ATOM   8694  C  CA    . PRO A 1 2645 ? 142.491 208.374 169.048 1.00 66.92  ? 2645 PRO A CA    1 
ATOM   8695  C  C     . PRO A 1 2645 ? 143.688 208.002 168.190 1.00 66.89  ? 2645 PRO A C     1 
ATOM   8696  O  O     . PRO A 1 2645 ? 143.510 207.633 167.023 1.00 67.16  ? 2645 PRO A O     1 
ATOM   8697  C  CB    . PRO A 1 2645 ? 142.249 209.889 169.056 1.00 68.94  ? 2645 PRO A CB    1 
ATOM   8698  C  CG    . PRO A 1 2645 ? 141.676 210.166 170.400 1.00 71.33  ? 2645 PRO A CG    1 
ATOM   8699  C  CD    . PRO A 1 2645 ? 142.349 209.207 171.339 1.00 67.96  ? 2645 PRO A CD    1 
ATOM   8700  N  N     . ASN A 1 2646 ? 144.903 208.088 168.731 1.00 64.91  ? 2646 ASN A N     1 
ATOM   8701  C  CA    . ASN A 1 2646 ? 146.093 207.678 167.998 1.00 62.70  ? 2646 ASN A CA    1 
ATOM   8702  C  C     . ASN A 1 2646 ? 146.266 206.166 167.941 1.00 63.88  ? 2646 ASN A C     1 
ATOM   8703  O  O     . ASN A 1 2646 ? 147.027 205.679 167.098 1.00 64.74  ? 2646 ASN A O     1 
ATOM   8704  C  CB    . ASN A 1 2646 ? 147.339 208.311 168.622 1.00 61.80  ? 2646 ASN A CB    1 
ATOM   8705  C  CG    . ASN A 1 2646 ? 147.762 209.582 167.915 1.00 72.52  ? 2646 ASN A CG    1 
ATOM   8706  O  OD1   . ASN A 1 2646 ? 147.770 209.649 166.686 1.00 70.82  ? 2646 ASN A OD1   1 
ATOM   8707  N  ND2   . ASN A 1 2646 ? 148.118 210.600 168.689 1.00 78.51  ? 2646 ASN A ND2   1 
ATOM   8708  N  N     . GLY A 1 2647 ? 145.588 205.417 168.808 1.00 55.51  ? 2647 GLY A N     1 
ATOM   8709  C  CA    . GLY A 1 2647 ? 145.706 203.972 168.816 1.00 43.88  ? 2647 GLY A CA    1 
ATOM   8710  C  C     . GLY A 1 2647 ? 145.595 203.372 170.202 1.00 42.44  ? 2647 GLY A C     1 
ATOM   8711  O  O     . GLY A 1 2647 ? 145.428 204.097 171.187 1.00 52.78  ? 2647 GLY A O     1 
ATOM   8712  N  N     . VAL A 1 2648 ? 145.687 202.045 170.291 1.00 37.06  ? 2648 VAL A N     1 
ATOM   8713  C  CA    . VAL A 1 2648 ? 145.582 201.369 171.578 1.00 33.34  ? 2648 VAL A CA    1 
ATOM   8714  C  C     . VAL A 1 2648 ? 146.838 201.635 172.396 1.00 29.61  ? 2648 VAL A C     1 
ATOM   8715  O  O     . VAL A 1 2648 ? 147.964 201.499 171.899 1.00 30.48  ? 2648 VAL A O     1 
ATOM   8716  C  CB    . VAL A 1 2648 ? 145.353 199.863 171.377 1.00 29.48  ? 2648 VAL A CB    1 
ATOM   8717  C  CG1   . VAL A 1 2648 ? 145.405 199.132 172.708 1.00 30.85  ? 2648 VAL A CG1   1 
ATOM   8718  C  CG2   . VAL A 1 2648 ? 144.021 199.621 170.687 1.00 39.45  ? 2648 VAL A CG2   1 
ATOM   8719  N  N     . VAL A 1 2649 ? 146.650 202.019 173.656 1.00 30.29  ? 2649 VAL A N     1 
ATOM   8720  C  CA    . VAL A 1 2649 ? 147.747 202.335 174.563 1.00 28.73  ? 2649 VAL A CA    1 
ATOM   8721  C  C     . VAL A 1 2649 ? 147.601 201.482 175.815 1.00 26.84  ? 2649 VAL A C     1 
ATOM   8722  O  O     . VAL A 1 2649 ? 146.520 201.428 176.411 1.00 36.10  ? 2649 VAL A O     1 
ATOM   8723  C  CB    . VAL A 1 2649 ? 147.772 203.832 174.926 1.00 32.02  ? 2649 VAL A CB    1 
ATOM   8724  C  CG1   . VAL A 1 2649 ? 148.653 204.073 176.138 1.00 33.06  ? 2649 VAL A CG1   1 
ATOM   8725  C  CG2   . VAL A 1 2649 ? 148.255 204.655 173.744 1.00 36.55  ? 2649 VAL A CG2   1 
ATOM   8726  N  N     . LEU A 1 2650 ? 148.685 200.817 176.209 1.00 23.18  ? 2650 LEU A N     1 
ATOM   8727  C  CA    . LEU A 1 2650 ? 148.717 200.013 177.424 1.00 27.07  ? 2650 LEU A CA    1 
ATOM   8728  C  C     . LEU A 1 2650 ? 149.447 200.793 178.510 1.00 34.95  ? 2650 LEU A C     1 
ATOM   8729  O  O     . LEU A 1 2650 ? 150.631 201.113 178.361 1.00 36.98  ? 2650 LEU A O     1 
ATOM   8730  C  CB    . LEU A 1 2650 ? 149.401 198.670 177.173 1.00 21.88  ? 2650 LEU A CB    1 
ATOM   8731  C  CG    . LEU A 1 2650 ? 149.499 197.722 178.369 1.00 21.89  ? 2650 LEU A CG    1 
ATOM   8732  C  CD1   . LEU A 1 2650 ? 148.130 197.174 178.724 1.00 27.06  ? 2650 LEU A CD1   1 
ATOM   8733  C  CD2   . LEU A 1 2650 ? 150.469 196.592 178.077 1.00 19.74  ? 2650 LEU A CD2   1 
ATOM   8734  N  N     . ALA A 1 2651 ? 148.742 201.093 179.595 1.00 32.07  ? 2651 ALA A N     1 
ATOM   8735  C  CA    . ALA A 1 2651 ? 149.281 201.875 180.695 1.00 27.30  ? 2651 ALA A CA    1 
ATOM   8736  C  C     . ALA A 1 2651 ? 148.831 201.263 182.012 1.00 35.51  ? 2651 ALA A C     1 
ATOM   8737  O  O     . ALA A 1 2651 ? 147.790 200.599 182.066 1.00 36.98  ? 2651 ALA A O     1 
ATOM   8738  C  CB    . ALA A 1 2651 ? 148.824 203.341 180.618 1.00 31.36  ? 2651 ALA A CB    1 
ATOM   8739  N  N     . PRO A 1 2652 ? 149.595 201.466 183.087 1.00 36.04  ? 2652 PRO A N     1 
ATOM   8740  C  CA    . PRO A 1 2652 ? 149.194 200.916 184.387 1.00 34.51  ? 2652 PRO A CA    1 
ATOM   8741  C  C     . PRO A 1 2652 ? 147.887 201.522 184.875 1.00 40.60  ? 2652 PRO A C     1 
ATOM   8742  O  O     . PRO A 1 2652 ? 147.527 202.648 184.526 1.00 40.64  ? 2652 PRO A O     1 
ATOM   8743  C  CB    . PRO A 1 2652 ? 150.360 201.292 185.309 1.00 28.39  ? 2652 PRO A CB    1 
ATOM   8744  C  CG    . PRO A 1 2652 ? 151.512 201.516 184.396 1.00 25.90  ? 2652 PRO A CG    1 
ATOM   8745  C  CD    . PRO A 1 2652 ? 150.931 202.081 183.140 1.00 31.55  ? 2652 PRO A CD    1 
ATOM   8746  N  N     . VAL A 1 2653 ? 147.166 200.744 185.686 1.00 43.31  ? 2653 VAL A N     1 
ATOM   8747  C  CA    . VAL A 1 2653 ? 145.911 201.223 186.259 1.00 46.81  ? 2653 VAL A CA    1 
ATOM   8748  C  C     . VAL A 1 2653 ? 146.162 202.426 187.159 1.00 53.64  ? 2653 VAL A C     1 
ATOM   8749  O  O     . VAL A 1 2653 ? 145.395 203.397 187.151 1.00 55.09  ? 2653 VAL A O     1 
ATOM   8750  C  CB    . VAL A 1 2653 ? 145.199 200.087 187.016 1.00 44.53  ? 2653 VAL A CB    1 
ATOM   8751  C  CG1   . VAL A 1 2653 ? 143.855 200.561 187.541 1.00 54.03  ? 2653 VAL A CG1   1 
ATOM   8752  C  CG2   . VAL A 1 2653 ? 145.024 198.878 186.112 1.00 37.99  ? 2653 VAL A CG2   1 
ATOM   8753  N  N     . GLN A 1 2654 ? 147.232 202.382 187.951 1.00 53.30  ? 2654 GLN A N     1 
ATOM   8754  C  CA    . GLN A 1 2654 ? 147.595 203.501 188.811 1.00 50.30  ? 2654 GLN A CA    1 
ATOM   8755  C  C     . GLN A 1 2654 ? 148.003 204.711 187.980 1.00 44.38  ? 2654 GLN A C     1 
ATOM   8756  O  O     . GLN A 1 2654 ? 149.007 204.668 187.262 1.00 44.64  ? 2654 GLN A O     1 
ATOM   8757  C  CB    . GLN A 1 2654 ? 148.729 203.103 189.758 1.00 54.15  ? 2654 GLN A CB    1 
ATOM   8758  C  CG    . GLN A 1 2654 ? 148.288 202.248 190.932 1.00 58.48  ? 2654 GLN A CG    1 
ATOM   8759  C  CD    . GLN A 1 2654 ? 149.236 202.345 192.110 1.00 68.49  ? 2654 GLN A CD    1 
ATOM   8760  O  OE1   . GLN A 1 2654 ? 149.742 203.422 192.428 1.00 66.33  ? 2654 GLN A OE1   1 
ATOM   8761  N  NE2   . GLN A 1 2654 ? 149.484 201.217 192.766 1.00 72.94  ? 2654 GLN A NE2   1 
ATOM   8762  N  N     . LEU A 1 2655 ? 147.232 205.792 188.069 1.00 42.42  ? 2655 LEU A N     1 
ATOM   8763  C  CA    . LEU A 1 2655 ? 147.552 207.002 187.323 1.00 46.54  ? 2655 LEU A CA    1 
ATOM   8764  C  C     . LEU A 1 2655 ? 148.760 207.700 187.937 1.00 47.51  ? 2655 LEU A C     1 
ATOM   8765  O  O     . LEU A 1 2655 ? 148.872 207.812 189.161 1.00 48.78  ? 2655 LEU A O     1 
ATOM   8766  C  CB    . LEU A 1 2655 ? 146.354 207.952 187.299 1.00 48.74  ? 2655 LEU A CB    1 
ATOM   8767  C  CG    . LEU A 1 2655 ? 145.264 207.753 186.239 1.00 57.95  ? 2655 LEU A CG    1 
ATOM   8768  C  CD1   . LEU A 1 2655 ? 145.832 207.952 184.840 1.00 52.02  ? 2655 LEU A CD1   1 
ATOM   8769  C  CD2   . LEU A 1 2655 ? 144.573 206.402 186.361 1.00 55.83  ? 2655 LEU A CD2   1 
ATOM   8770  N  N     . GLY A 1 2656 ? 149.666 208.169 187.081 1.00 43.74  ? 2656 GLY A N     1 
ATOM   8771  C  CA    . GLY A 1 2656 ? 150.822 208.916 187.523 1.00 40.37  ? 2656 GLY A CA    1 
ATOM   8772  C  C     . GLY A 1 2656 ? 151.976 208.088 188.043 1.00 43.25  ? 2656 GLY A C     1 
ATOM   8773  O  O     . GLY A 1 2656 ? 152.975 208.665 188.489 1.00 43.47  ? 2656 GLY A O     1 
ATOM   8774  N  N     . LYS A 1 2657 ? 151.878 206.763 188.001 1.00 44.29  ? 2657 LYS A N     1 
ATOM   8775  C  CA    . LYS A 1 2657 ? 152.928 205.880 188.487 1.00 42.38  ? 2657 LYS A CA    1 
ATOM   8776  C  C     . LYS A 1 2657 ? 153.547 205.115 187.327 1.00 36.58  ? 2657 LYS A C     1 
ATOM   8777  O  O     . LYS A 1 2657 ? 152.848 204.705 186.396 1.00 37.66  ? 2657 LYS A O     1 
ATOM   8778  C  CB    . LYS A 1 2657 ? 152.384 204.896 189.527 1.00 42.18  ? 2657 LYS A CB    1 
ATOM   8779  C  CG    . LYS A 1 2657 ? 151.758 205.559 190.741 1.00 47.19  ? 2657 LYS A CG    1 
ATOM   8780  C  CD    . LYS A 1 2657 ? 152.785 205.756 191.843 1.00 52.30  ? 2657 LYS A CD    1 
ATOM   8781  C  CE    . LYS A 1 2657 ? 152.149 206.334 193.095 1.00 64.08  ? 2657 LYS A CE    1 
ATOM   8782  N  NZ    . LYS A 1 2657 ? 152.969 207.433 193.674 1.00 60.34  ? 2657 LYS A NZ    1 
ATOM   8783  N  N     . TRP A 1 2658 ? 154.861 204.928 187.390 1.00 32.73  ? 2658 TRP A N     1 
ATOM   8784  C  CA    . TRP A 1 2658 ? 155.599 204.175 186.386 1.00 25.67  ? 2658 TRP A CA    1 
ATOM   8785  C  C     . TRP A 1 2658 ? 155.761 202.736 186.854 1.00 27.49  ? 2658 TRP A C     1 
ATOM   8786  O  O     . TRP A 1 2658 ? 156.246 202.490 187.963 1.00 35.81  ? 2658 TRP A O     1 
ATOM   8787  C  CB    . TRP A 1 2658 ? 156.968 204.806 186.128 1.00 25.18  ? 2658 TRP A CB    1 
ATOM   8788  C  CG    . TRP A 1 2658 ? 156.936 205.893 185.103 1.00 28.85  ? 2658 TRP A CG    1 
ATOM   8789  C  CD1   . TRP A 1 2658 ? 156.508 207.175 185.281 1.00 29.17  ? 2658 TRP A CD1   1 
ATOM   8790  C  CD2   . TRP A 1 2658 ? 157.345 205.792 183.735 1.00 28.47  ? 2658 TRP A CD2   1 
ATOM   8791  N  NE1   . TRP A 1 2658 ? 156.626 207.880 184.109 1.00 27.81  ? 2658 TRP A NE1   1 
ATOM   8792  C  CE2   . TRP A 1 2658 ? 157.138 207.054 183.144 1.00 26.98  ? 2658 TRP A CE2   1 
ATOM   8793  C  CE3   . TRP A 1 2658 ? 157.868 204.759 182.952 1.00 23.88  ? 2658 TRP A CE3   1 
ATOM   8794  C  CZ2   . TRP A 1 2658 ? 157.434 207.309 181.808 1.00 25.06  ? 2658 TRP A CZ2   1 
ATOM   8795  C  CZ3   . TRP A 1 2658 ? 158.161 205.014 181.627 1.00 25.23  ? 2658 TRP A CZ3   1 
ATOM   8796  C  CH2   . TRP A 1 2658 ? 157.944 206.279 181.068 1.00 24.37  ? 2658 TRP A CH2   1 
ATOM   8797  N  N     . LEU A 1 2659 ? 155.354 201.793 186.011 1.00 23.13  ? 2659 LEU A N     1 
ATOM   8798  C  CA    . LEU A 1 2659 ? 155.458 200.375 186.327 1.00 20.40  ? 2659 LEU A CA    1 
ATOM   8799  C  C     . LEU A 1 2659 ? 156.836 199.873 185.915 1.00 20.23  ? 2659 LEU A C     1 
ATOM   8800  O  O     . LEU A 1 2659 ? 157.223 199.993 184.748 1.00 27.71  ? 2659 LEU A O     1 
ATOM   8801  C  CB    . LEU A 1 2659 ? 154.362 199.578 185.623 1.00 21.66  ? 2659 LEU A CB    1 
ATOM   8802  C  CG    . LEU A 1 2659 ? 154.190 198.133 186.092 1.00 22.78  ? 2659 LEU A CG    1 
ATOM   8803  C  CD1   . LEU A 1 2659 ? 153.577 198.095 187.478 1.00 29.17  ? 2659 LEU A CD1   1 
ATOM   8804  C  CD2   . LEU A 1 2659 ? 153.342 197.345 185.112 1.00 17.50  ? 2659 LEU A CD2   1 
ATOM   8805  N  N     . VAL A 1 2660 ? 157.570 199.313 186.870 1.00 16.48  ? 2660 VAL A N     1 
ATOM   8806  C  CA    . VAL A 1 2660 ? 158.900 198.770 186.632 1.00 14.75  ? 2660 VAL A CA    1 
ATOM   8807  C  C     . VAL A 1 2660 ? 158.785 197.254 186.675 1.00 17.55  ? 2660 VAL A C     1 
ATOM   8808  O  O     . VAL A 1 2660 ? 158.474 196.675 187.724 1.00 25.41  ? 2660 VAL A O     1 
ATOM   8809  C  CB    . VAL A 1 2660 ? 159.918 199.280 187.660 1.00 14.34  ? 2660 VAL A CB    1 
ATOM   8810  C  CG1   . VAL A 1 2660 ? 161.289 198.693 187.381 1.00 12.91  ? 2660 VAL A CG1   1 
ATOM   8811  C  CG2   . VAL A 1 2660 ? 159.970 200.799 187.645 1.00 19.43  ? 2660 VAL A CG2   1 
ATOM   8812  N  N     . LEU A 1 2661 ? 159.030 196.606 185.540 1.00 17.36  ? 2661 LEU A N     1 
ATOM   8813  C  CA    . LEU A 1 2661 ? 158.979 195.151 185.453 1.00 16.47  ? 2661 LEU A CA    1 
ATOM   8814  C  C     . LEU A 1 2661 ? 160.374 194.606 185.728 1.00 16.88  ? 2661 LEU A C     1 
ATOM   8815  O  O     . LEU A 1 2661 ? 161.306 194.842 184.952 1.00 20.72  ? 2661 LEU A O     1 
ATOM   8816  C  CB    . LEU A 1 2661 ? 158.471 194.699 184.086 1.00 16.46  ? 2661 LEU A CB    1 
ATOM   8817  C  CG    . LEU A 1 2661 ? 156.963 194.767 183.833 1.00 16.35  ? 2661 LEU A CG    1 
ATOM   8818  C  CD1   . LEU A 1 2661 ? 156.484 196.199 183.649 1.00 20.59  ? 2661 LEU A CD1   1 
ATOM   8819  C  CD2   . LEU A 1 2661 ? 156.591 193.919 182.634 1.00 15.80  ? 2661 LEU A CD2   1 
ATOM   8820  N  N     . PHE A 1 2662 ? 160.518 193.879 186.831 1.00 14.79  ? 2662 PHE A N     1 
ATOM   8821  C  CA    . PHE A 1 2662 ? 161.804 193.326 187.245 1.00 15.25  ? 2662 PHE A CA    1 
ATOM   8822  C  C     . PHE A 1 2662 ? 161.853 191.861 186.829 1.00 21.01  ? 2662 PHE A C     1 
ATOM   8823  O  O     . PHE A 1 2662 ? 161.233 191.003 187.461 1.00 29.35  ? 2662 PHE A O     1 
ATOM   8824  C  CB    . PHE A 1 2662 ? 162.006 193.491 188.747 1.00 13.74  ? 2662 PHE A CB    1 
ATOM   8825  C  CG    . PHE A 1 2662 ? 163.325 192.973 189.239 1.00 18.57  ? 2662 PHE A CG    1 
ATOM   8826  C  CD1   . PHE A 1 2662 ? 164.488 193.225 188.531 1.00 18.58  ? 2662 PHE A CD1   1 
ATOM   8827  C  CD2   . PHE A 1 2662 ? 163.405 192.240 190.410 1.00 22.47  ? 2662 PHE A CD2   1 
ATOM   8828  C  CE1   . PHE A 1 2662 ? 165.704 192.753 188.980 1.00 16.59  ? 2662 PHE A CE1   1 
ATOM   8829  C  CE2   . PHE A 1 2662 ? 164.620 191.766 190.864 1.00 21.88  ? 2662 PHE A CE2   1 
ATOM   8830  C  CZ    . PHE A 1 2662 ? 165.771 192.023 190.147 1.00 17.50  ? 2662 PHE A CZ    1 
ATOM   8831  N  N     . CYS A 1 2663 ? 162.592 191.579 185.759 1.00 18.01  ? 2663 CYS A N     1 
ATOM   8832  C  CA    . CYS A 1 2663 ? 162.816 190.213 185.299 1.00 18.57  ? 2663 CYS A CA    1 
ATOM   8833  C  C     . CYS A 1 2663 ? 164.008 189.650 186.063 1.00 21.38  ? 2663 CYS A C     1 
ATOM   8834  O  O     . CYS A 1 2663 ? 165.144 190.093 185.870 1.00 25.61  ? 2663 CYS A O     1 
ATOM   8835  C  CB    . CYS A 1 2663 ? 163.051 190.185 183.791 1.00 25.03  ? 2663 CYS A CB    1 
ATOM   8836  S  SG    . CYS A 1 2663 ? 161.923 191.240 182.851 1.00 37.73  ? 2663 CYS A SG    1 
ATOM   8837  N  N     . ASP A 1 2664 ? 163.746 188.670 186.932 1.00 23.18  ? 2664 ASP A N     1 
ATOM   8838  C  CA    . ASP A 1 2664 ? 164.755 188.243 187.896 1.00 24.78  ? 2664 ASP A CA    1 
ATOM   8839  C  C     . ASP A 1 2664 ? 165.914 187.513 187.229 1.00 28.36  ? 2664 ASP A C     1 
ATOM   8840  O  O     . ASP A 1 2664 ? 167.074 187.714 187.604 1.00 39.94  ? 2664 ASP A O     1 
ATOM   8841  C  CB    . ASP A 1 2664 ? 164.116 187.360 188.964 1.00 32.70  ? 2664 ASP A CB    1 
ATOM   8842  C  CG    . ASP A 1 2664 ? 165.005 187.177 190.176 1.00 44.99  ? 2664 ASP A CG    1 
ATOM   8843  O  OD1   . ASP A 1 2664 ? 165.964 187.961 190.336 1.00 39.65  ? 2664 ASP A OD1   1 
ATOM   8844  O  OD2   . ASP A 1 2664 ? 164.745 186.248 190.969 1.00 53.33  ? 2664 ASP A OD2   1 
ATOM   8845  N  N     . GLU A 1 2665 ? 165.626 186.639 186.261 1.00 19.58  ? 2665 GLU A N     1 
ATOM   8846  C  CA    . GLU A 1 2665 ? 166.656 185.864 185.563 1.00 20.30  ? 2665 GLU A CA    1 
ATOM   8847  C  C     . GLU A 1 2665 ? 166.402 185.994 184.064 1.00 22.50  ? 2665 GLU A C     1 
ATOM   8848  O  O     . GLU A 1 2665 ? 165.785 185.124 183.449 1.00 27.43  ? 2665 GLU A O     1 
ATOM   8849  C  CB    . GLU A 1 2665 ? 166.642 184.413 186.018 1.00 25.78  ? 2665 GLU A CB    1 
ATOM   8850  C  CG    . GLU A 1 2665 ? 166.839 184.214 187.511 1.00 36.91  ? 2665 GLU A CG    1 
ATOM   8851  C  CD    . GLU A 1 2665 ? 168.290 183.990 187.882 1.00 43.55  ? 2665 GLU A CD    1 
ATOM   8852  O  OE1   . GLU A 1 2665 ? 169.135 183.921 186.965 1.00 37.61  ? 2665 GLU A OE1   1 
ATOM   8853  O  OE2   . GLU A 1 2665 ? 168.587 183.882 189.090 1.00 46.92  ? 2665 GLU A OE2   1 
ATOM   8854  N  N     . ILE A 1 2666 ? 166.923 187.067 183.468 1.00 20.12  ? 2666 ILE A N     1 
ATOM   8855  C  CA    . ILE A 1 2666 ? 166.521 187.429 182.114 1.00 16.67  ? 2666 ILE A CA    1 
ATOM   8856  C  C     . ILE A 1 2666 ? 167.139 186.526 181.049 1.00 16.24  ? 2666 ILE A C     1 
ATOM   8857  O  O     . ILE A 1 2666 ? 166.614 186.458 179.930 1.00 20.19  ? 2666 ILE A O     1 
ATOM   8858  C  CB    . ILE A 1 2666 ? 166.862 188.908 181.857 1.00 13.93  ? 2666 ILE A CB    1 
ATOM   8859  C  CG1   . ILE A 1 2666 ? 166.180 189.416 180.586 1.00 19.35  ? 2666 ILE A CG1   1 
ATOM   8860  C  CG2   . ILE A 1 2666 ? 168.365 189.104 181.766 1.00 13.58  ? 2666 ILE A CG2   1 
ATOM   8861  C  CD1   . ILE A 1 2666 ? 166.198 190.919 180.449 1.00 23.14  ? 2666 ILE A CD1   1 
ATOM   8862  N  N     . ASN A 1 2667 ? 168.218 185.808 181.359 1.00 16.86  ? 2667 ASN A N     1 
ATOM   8863  C  CA    . ASN A 1 2667 ? 168.927 185.023 180.356 1.00 15.54  ? 2667 ASN A CA    1 
ATOM   8864  C  C     . ASN A 1 2667 ? 168.723 183.517 180.502 1.00 19.45  ? 2667 ASN A C     1 
ATOM   8865  O  O     . ASN A 1 2667 ? 169.410 182.746 179.825 1.00 21.56  ? 2667 ASN A O     1 
ATOM   8866  C  CB    . ASN A 1 2667 ? 170.421 185.358 180.385 1.00 14.96  ? 2667 ASN A CB    1 
ATOM   8867  C  CG    . ASN A 1 2667 ? 171.034 185.188 181.758 1.00 20.89  ? 2667 ASN A CG    1 
ATOM   8868  O  OD1   . ASN A 1 2667 ? 170.360 184.798 182.711 1.00 31.06  ? 2667 ASN A OD1   1 
ATOM   8869  N  ND2   . ASN A 1 2667 ? 172.323 185.486 181.869 1.00 17.24  ? 2667 ASN A ND2   1 
ATOM   8870  N  N     . LEU A 1 2668 ? 167.803 183.078 181.361 1.00 20.49  ? 2668 LEU A N     1 
ATOM   8871  C  CA    . LEU A 1 2668 ? 167.432 181.665 181.423 1.00 18.55  ? 2668 LEU A CA    1 
ATOM   8872  C  C     . LEU A 1 2668 ? 166.546 181.166 180.280 1.00 20.40  ? 2668 LEU A C     1 
ATOM   8873  O  O     . LEU A 1 2668 ? 166.702 180.005 179.882 1.00 22.84  ? 2668 LEU A O     1 
ATOM   8874  C  CB    . LEU A 1 2668 ? 166.734 181.330 182.743 1.00 17.41  ? 2668 LEU A CB    1 
ATOM   8875  C  CG    . LEU A 1 2668 ? 167.554 181.318 184.026 1.00 21.55  ? 2668 LEU A CG    1 
ATOM   8876  C  CD1   . LEU A 1 2668 ? 166.645 181.055 185.205 1.00 31.29  ? 2668 LEU A CD1   1 
ATOM   8877  C  CD2   . LEU A 1 2668 ? 168.609 180.239 183.932 1.00 21.52  ? 2668 LEU A CD2   1 
ATOM   8878  N  N     . PRO A 1 2669 ? 165.602 181.956 179.748 1.00 15.31  ? 2669 PRO A N     1 
ATOM   8879  C  CA    . PRO A 1 2669 ? 164.671 181.406 178.753 1.00 15.36  ? 2669 PRO A CA    1 
ATOM   8880  C  C     . PRO A 1 2669 ? 165.385 180.704 177.607 1.00 18.86  ? 2669 PRO A C     1 
ATOM   8881  O  O     . PRO A 1 2669 ? 166.412 181.168 177.107 1.00 21.27  ? 2669 PRO A O     1 
ATOM   8882  C  CB    . PRO A 1 2669 ? 163.910 182.642 178.270 1.00 16.27  ? 2669 PRO A CB    1 
ATOM   8883  C  CG    . PRO A 1 2669 ? 163.873 183.508 179.456 1.00 15.42  ? 2669 PRO A CG    1 
ATOM   8884  C  CD    . PRO A 1 2669 ? 165.197 183.322 180.138 1.00 15.50  ? 2669 PRO A CD    1 
ATOM   8885  N  N     . ASP A 1 2670 ? 164.827 179.564 177.208 1.00 21.87  ? 2670 ASP A N     1 
ATOM   8886  C  CA    . ASP A 1 2670 ? 165.510 178.657 176.297 1.00 20.06  ? 2670 ASP A CA    1 
ATOM   8887  C  C     . ASP A 1 2670 ? 165.742 179.301 174.939 1.00 22.02  ? 2670 ASP A C     1 
ATOM   8888  O  O     . ASP A 1 2670 ? 164.853 179.944 174.373 1.00 27.25  ? 2670 ASP A O     1 
ATOM   8889  C  CB    . ASP A 1 2670 ? 164.698 177.373 176.128 1.00 25.80  ? 2670 ASP A CB    1 
ATOM   8890  C  CG    . ASP A 1 2670 ? 165.057 176.316 177.151 1.00 36.19  ? 2670 ASP A CG    1 
ATOM   8891  O  OD1   . ASP A 1 2670 ? 166.188 176.359 177.681 1.00 37.65  ? 2670 ASP A OD1   1 
ATOM   8892  O  OD2   . ASP A 1 2670 ? 164.209 175.442 177.426 1.00 35.55  ? 2670 ASP A OD2   1 
ATOM   8893  N  N     . MET A 1 2671 ? 166.951 179.122 174.418 1.00 22.54  ? 2671 MET A N     1 
ATOM   8894  C  CA    . MET A 1 2671 ? 167.264 179.473 173.043 1.00 22.24  ? 2671 MET A CA    1 
ATOM   8895  C  C     . MET A 1 2671 ? 166.864 178.312 172.144 1.00 24.77  ? 2671 MET A C     1 
ATOM   8896  O  O     . MET A 1 2671 ? 167.272 177.170 172.380 1.00 29.75  ? 2671 MET A O     1 
ATOM   8897  C  CB    . MET A 1 2671 ? 168.754 179.777 172.884 1.00 19.65  ? 2671 MET A CB    1 
ATOM   8898  C  CG    . MET A 1 2671 ? 169.123 181.237 173.068 1.00 19.52  ? 2671 MET A CG    1 
ATOM   8899  S  SD    . MET A 1 2671 ? 170.656 181.669 172.228 1.00 46.96  ? 2671 MET A SD    1 
ATOM   8900  C  CE    . MET A 1 2671 ? 170.542 183.455 172.211 1.00 32.86  ? 2671 MET A CE    1 
ATOM   8901  N  N     . ASP A 1 2672 ? 166.066 178.601 171.122 1.00 21.93  ? 2672 ASP A N     1 
ATOM   8902  C  CA    . ASP A 1 2672 ? 165.649 177.561 170.196 1.00 27.09  ? 2672 ASP A CA    1 
ATOM   8903  C  C     . ASP A 1 2672 ? 166.841 177.092 169.359 1.00 29.42  ? 2672 ASP A C     1 
ATOM   8904  O  O     . ASP A 1 2672 ? 167.977 177.542 169.529 1.00 31.80  ? 2672 ASP A O     1 
ATOM   8905  C  CB    . ASP A 1 2672 ? 164.470 178.050 169.349 1.00 30.28  ? 2672 ASP A CB    1 
ATOM   8906  C  CG    . ASP A 1 2672 ? 164.836 179.177 168.382 1.00 31.53  ? 2672 ASP A CG    1 
ATOM   8907  O  OD1   . ASP A 1 2672 ? 165.997 179.287 167.943 1.00 33.58  ? 2672 ASP A OD1   1 
ATOM   8908  O  OD2   . ASP A 1 2672 ? 163.927 179.967 168.050 1.00 34.13  ? 2672 ASP A OD2   1 
ATOM   8909  N  N     . LYS A 1 2673 ? 166.571 176.161 168.440 1.00 25.24  ? 2673 LYS A N     1 
ATOM   8910  C  CA    . LYS A 1 2673 ? 167.634 175.589 167.620 1.00 26.69  ? 2673 LYS A CA    1 
ATOM   8911  C  C     . LYS A 1 2673 ? 168.360 176.651 166.803 1.00 28.01  ? 2673 LYS A C     1 
ATOM   8912  O  O     . LYS A 1 2673 ? 169.520 176.450 166.428 1.00 32.20  ? 2673 LYS A O     1 
ATOM   8913  C  CB    . LYS A 1 2673 ? 167.047 174.507 166.707 1.00 29.11  ? 2673 LYS A CB    1 
ATOM   8914  C  CG    . LYS A 1 2673 ? 168.016 173.911 165.697 1.00 33.94  ? 2673 LYS A CG    1 
ATOM   8915  C  CD    . LYS A 1 2673 ? 167.420 172.693 165.012 1.00 37.74  ? 2673 LYS A CD    1 
ATOM   8916  C  CE    . LYS A 1 2673 ? 167.208 172.941 163.528 1.00 45.04  ? 2673 LYS A CE    1 
ATOM   8917  N  NZ    . LYS A 1 2673 ? 167.068 171.668 162.768 1.00 54.95  ? 2673 LYS A NZ    1 
ATOM   8918  N  N     . TYR A 1 2674 ? 167.717 177.791 166.553 1.00 28.18  ? 2674 TYR A N     1 
ATOM   8919  C  CA    . TYR A 1 2674 ? 168.283 178.865 165.751 1.00 28.09  ? 2674 TYR A CA    1 
ATOM   8920  C  C     . TYR A 1 2674 ? 168.739 180.050 166.597 1.00 29.12  ? 2674 TYR A C     1 
ATOM   8921  O  O     . TYR A 1 2674 ? 168.823 181.172 166.088 1.00 32.07  ? 2674 TYR A O     1 
ATOM   8922  C  CB    . TYR A 1 2674 ? 167.265 179.308 164.703 1.00 27.87  ? 2674 TYR A CB    1 
ATOM   8923  C  CG    . TYR A 1 2674 ? 166.669 178.142 163.950 1.00 29.47  ? 2674 TYR A CG    1 
ATOM   8924  C  CD1   . TYR A 1 2674 ? 167.392 177.480 162.968 1.00 30.94  ? 2674 TYR A CD1   1 
ATOM   8925  C  CD2   . TYR A 1 2674 ? 165.394 177.681 164.246 1.00 28.01  ? 2674 TYR A CD2   1 
ATOM   8926  C  CE1   . TYR A 1 2674 ? 166.854 176.407 162.287 1.00 31.68  ? 2674 TYR A CE1   1 
ATOM   8927  C  CE2   . TYR A 1 2674 ? 164.850 176.610 163.572 1.00 28.01  ? 2674 TYR A CE2   1 
ATOM   8928  C  CZ    . TYR A 1 2674 ? 165.581 175.977 162.593 1.00 32.42  ? 2674 TYR A CZ    1 
ATOM   8929  O  OH    . TYR A 1 2674 ? 165.038 174.908 161.919 1.00 38.31  ? 2674 TYR A OH    1 
ATOM   8930  N  N     . GLY A 1 2675 ? 169.020 179.824 167.879 1.00 28.78  ? 2675 GLY A N     1 
ATOM   8931  C  CA    . GLY A 1 2675 ? 169.612 180.839 168.731 1.00 26.27  ? 2675 GLY A CA    1 
ATOM   8932  C  C     . GLY A 1 2675 ? 168.765 182.071 168.974 1.00 24.55  ? 2675 GLY A C     1 
ATOM   8933  O  O     . GLY A 1 2675 ? 169.265 183.196 168.875 1.00 30.04  ? 2675 GLY A O     1 
ATOM   8934  N  N     . THR A 1 2676 ? 167.487 181.882 169.292 1.00 20.44  ? 2676 THR A N     1 
ATOM   8935  C  CA    . THR A 1 2676 ? 166.587 182.998 169.550 1.00 20.92  ? 2676 THR A CA    1 
ATOM   8936  C  C     . THR A 1 2676 ? 165.765 182.721 170.798 1.00 25.51  ? 2676 THR A C     1 
ATOM   8937  O  O     . THR A 1 2676 ? 165.243 181.615 170.967 1.00 35.02  ? 2676 THR A O     1 
ATOM   8938  C  CB    . THR A 1 2676 ? 165.658 183.247 168.356 1.00 27.75  ? 2676 THR A CB    1 
ATOM   8939  O  OG1   . THR A 1 2676 ? 166.438 183.554 167.194 1.00 38.35  ? 2676 THR A OG1   1 
ATOM   8940  C  CG2   . THR A 1 2676 ? 164.708 184.402 168.643 1.00 21.60  ? 2676 THR A CG2   1 
ATOM   8941  N  N     . GLN A 1 2677 ? 165.657 183.723 171.666 1.00 23.67  ? 2677 GLN A N     1 
ATOM   8942  C  CA    . GLN A 1 2677 ? 164.763 183.683 172.815 1.00 17.17  ? 2677 GLN A CA    1 
ATOM   8943  C  C     . GLN A 1 2677 ? 163.543 184.541 172.501 1.00 17.34  ? 2677 GLN A C     1 
ATOM   8944  O  O     . GLN A 1 2677 ? 163.679 185.736 172.218 1.00 21.80  ? 2677 GLN A O     1 
ATOM   8945  C  CB    . GLN A 1 2677 ? 165.465 184.182 174.077 1.00 12.35  ? 2677 GLN A CB    1 
ATOM   8946  C  CG    . GLN A 1 2677 ? 166.524 183.238 174.614 1.00 17.08  ? 2677 GLN A CG    1 
ATOM   8947  C  CD    . GLN A 1 2677 ? 167.652 183.966 175.318 1.00 20.46  ? 2677 GLN A CD    1 
ATOM   8948  O  OE1   . GLN A 1 2677 ? 168.319 184.817 174.730 1.00 24.55  ? 2677 GLN A OE1   1 
ATOM   8949  N  NE2   . GLN A 1 2677 ? 167.872 183.634 176.583 1.00 16.49  ? 2677 GLN A NE2   1 
ATOM   8950  N  N     . ARG A 1 2678 ? 162.358 183.929 172.542 1.00 14.63  ? 2678 ARG A N     1 
ATOM   8951  C  CA    . ARG A 1 2678 ? 161.146 184.640 172.147 1.00 13.75  ? 2678 ARG A CA    1 
ATOM   8952  C  C     . ARG A 1 2678 ? 160.847 185.805 173.083 1.00 16.16  ? 2678 ARG A C     1 
ATOM   8953  O  O     . ARG A 1 2678 ? 160.473 186.891 172.628 1.00 19.21  ? 2678 ARG A O     1 
ATOM   8954  C  CB    . ARG A 1 2678 ? 159.963 183.675 172.096 1.00 16.05  ? 2678 ARG A CB    1 
ATOM   8955  C  CG    . ARG A 1 2678 ? 158.671 184.311 171.612 1.00 18.44  ? 2678 ARG A CG    1 
ATOM   8956  C  CD    . ARG A 1 2678 ? 157.533 183.307 171.581 1.00 27.00  ? 2678 ARG A CD    1 
ATOM   8957  N  NE    . ARG A 1 2678 ? 157.809 182.197 170.679 1.00 31.97  ? 2678 ARG A NE    1 
ATOM   8958  C  CZ    . ARG A 1 2678 ? 157.045 181.120 170.561 1.00 37.53  ? 2678 ARG A CZ    1 
ATOM   8959  N  NH1   . ARG A 1 2678 ? 155.940 180.976 171.274 1.00 37.47  ? 2678 ARG A NH1   1 
ATOM   8960  N  NH2   . ARG A 1 2678 ? 157.398 180.164 169.707 1.00 38.78  ? 2678 ARG A NH2   1 
ATOM   8961  N  N     . VAL A 1 2679 ? 161.003 185.599 174.392 1.00 15.90  ? 2679 VAL A N     1 
ATOM   8962  C  CA    . VAL A 1 2679 ? 160.720 186.668 175.345 1.00 12.36  ? 2679 VAL A CA    1 
ATOM   8963  C  C     . VAL A 1 2679 ? 161.746 187.791 175.226 1.00 13.50  ? 2679 VAL A C     1 
ATOM   8964  O  O     . VAL A 1 2679 ? 161.407 188.969 175.388 1.00 15.47  ? 2679 VAL A O     1 
ATOM   8965  C  CB    . VAL A 1 2679 ? 160.652 186.099 176.774 1.00 12.05  ? 2679 VAL A CB    1 
ATOM   8966  C  CG1   . VAL A 1 2679 ? 161.929 185.365 177.114 1.00 13.42  ? 2679 VAL A CG1   1 
ATOM   8967  C  CG2   . VAL A 1 2679 ? 160.380 187.202 177.781 1.00 11.45  ? 2679 VAL A CG2   1 
ATOM   8968  N  N     . ILE A 1 2680 ? 163.007 187.457 174.947 1.00 13.55  ? 2680 ILE A N     1 
ATOM   8969  C  CA    . ILE A 1 2680 ? 164.022 188.491 174.769 1.00 10.99  ? 2680 ILE A CA    1 
ATOM   8970  C  C     . ILE A 1 2680 ? 163.714 189.333 173.537 1.00 12.92  ? 2680 ILE A C     1 
ATOM   8971  O  O     . ILE A 1 2680 ? 163.831 190.564 173.565 1.00 14.69  ? 2680 ILE A O     1 
ATOM   8972  C  CB    . ILE A 1 2680 ? 165.422 187.857 174.694 1.00 13.27  ? 2680 ILE A CB    1 
ATOM   8973  C  CG1   . ILE A 1 2680 ? 165.784 187.223 176.037 1.00 15.26  ? 2680 ILE A CG1   1 
ATOM   8974  C  CG2   . ILE A 1 2680 ? 166.460 188.895 174.302 1.00 12.87  ? 2680 ILE A CG2   1 
ATOM   8975  C  CD1   . ILE A 1 2680 ? 165.652 188.164 177.207 1.00 10.83  ? 2680 ILE A CD1   1 
ATOM   8976  N  N     . SER A 1 2681 ? 163.307 188.688 172.441 1.00 13.74  ? 2681 SER A N     1 
ATOM   8977  C  CA    . SER A 1 2681 ? 162.894 189.431 171.255 1.00 11.59  ? 2681 SER A CA    1 
ATOM   8978  C  C     . SER A 1 2681 ? 161.661 190.277 171.541 1.00 13.97  ? 2681 SER A C     1 
ATOM   8979  O  O     . SER A 1 2681 ? 161.535 191.397 171.035 1.00 18.76  ? 2681 SER A O     1 
ATOM   8980  C  CB    . SER A 1 2681 ? 162.630 188.468 170.098 1.00 11.42  ? 2681 SER A CB    1 
ATOM   8981  O  OG    . SER A 1 2681 ? 163.829 187.856 169.658 1.00 16.15  ? 2681 SER A OG    1 
ATOM   8982  N  N     . PHE A 1 2682 ? 160.741 189.756 172.354 1.00 12.62  ? 2682 PHE A N     1 
ATOM   8983  C  CA    . PHE A 1 2682 ? 159.559 190.518 172.746 1.00 11.55  ? 2682 PHE A CA    1 
ATOM   8984  C  C     . PHE A 1 2682 ? 159.948 191.790 173.490 1.00 14.33  ? 2682 PHE A C     1 
ATOM   8985  O  O     . PHE A 1 2682 ? 159.464 192.885 173.176 1.00 20.10  ? 2682 PHE A O     1 
ATOM   8986  C  CB    . PHE A 1 2682 ? 158.657 189.636 173.611 1.00 10.50  ? 2682 PHE A CB    1 
ATOM   8987  C  CG    . PHE A 1 2682 ? 157.270 190.173 173.801 1.00 13.06  ? 2682 PHE A CG    1 
ATOM   8988  C  CD1   . PHE A 1 2682 ? 156.463 190.443 172.712 1.00 17.50  ? 2682 PHE A CD1   1 
ATOM   8989  C  CD2   . PHE A 1 2682 ? 156.767 190.387 175.072 1.00 12.98  ? 2682 PHE A CD2   1 
ATOM   8990  C  CE1   . PHE A 1 2682 ? 155.184 190.927 172.887 1.00 16.40  ? 2682 PHE A CE1   1 
ATOM   8991  C  CE2   . PHE A 1 2682 ? 155.488 190.870 175.253 1.00 13.37  ? 2682 PHE A CE2   1 
ATOM   8992  C  CZ    . PHE A 1 2682 ? 154.697 191.143 174.159 1.00 14.88  ? 2682 PHE A CZ    1 
ATOM   8993  N  N     . ILE A 1 2683 ? 160.834 191.661 174.480 1.00 11.19  ? 2683 ILE A N     1 
ATOM   8994  C  CA    . ILE A 1 2683 ? 161.268 192.819 175.254 1.00 10.70  ? 2683 ILE A CA    1 
ATOM   8995  C  C     . ILE A 1 2683 ? 162.026 193.800 174.368 1.00 13.68  ? 2683 ILE A C     1 
ATOM   8996  O  O     . ILE A 1 2683 ? 161.873 195.020 174.499 1.00 19.48  ? 2683 ILE A O     1 
ATOM   8997  C  CB    . ILE A 1 2683 ? 162.111 192.374 176.462 1.00 10.73  ? 2683 ILE A CB    1 
ATOM   8998  C  CG1   . ILE A 1 2683 ? 161.293 191.461 177.375 1.00 11.48  ? 2683 ILE A CG1   1 
ATOM   8999  C  CG2   . ILE A 1 2683 ? 162.607 193.581 177.240 1.00 9.75   ? 2683 ILE A CG2   1 
ATOM   9000  C  CD1   . ILE A 1 2683 ? 162.081 190.890 178.531 1.00 10.35  ? 2683 ILE A CD1   1 
ATOM   9001  N  N     . ARG A 1 2684 ? 162.851 193.289 173.451 1.00 10.86  ? 2684 ARG A N     1 
ATOM   9002  C  CA    . ARG A 1 2684 ? 163.554 194.170 172.525 1.00 11.37  ? 2684 ARG A CA    1 
ATOM   9003  C  C     . ARG A 1 2684 ? 162.573 194.928 171.641 1.00 14.65  ? 2684 ARG A C     1 
ATOM   9004  O  O     . ARG A 1 2684 ? 162.792 196.101 171.322 1.00 17.77  ? 2684 ARG A O     1 
ATOM   9005  C  CB    . ARG A 1 2684 ? 164.538 193.363 171.678 1.00 10.44  ? 2684 ARG A CB    1 
ATOM   9006  C  CG    . ARG A 1 2684 ? 165.283 194.179 170.634 1.00 12.44  ? 2684 ARG A CG    1 
ATOM   9007  C  CD    . ARG A 1 2684 ? 165.420 193.417 169.328 1.00 16.74  ? 2684 ARG A CD    1 
ATOM   9008  N  NE    . ARG A 1 2684 ? 165.839 194.282 168.232 1.00 20.43  ? 2684 ARG A NE    1 
ATOM   9009  C  CZ    . ARG A 1 2684 ? 165.018 194.795 167.326 1.00 25.47  ? 2684 ARG A CZ    1 
ATOM   9010  N  NH1   . ARG A 1 2684 ? 163.719 194.548 167.352 1.00 26.35  ? 2684 ARG A NH1   1 
ATOM   9011  N  NH2   . ARG A 1 2684 ? 165.513 195.575 166.370 1.00 22.72  ? 2684 ARG A NH2   1 
ATOM   9012  N  N     . GLN A 1 2685 ? 161.484 194.272 171.234 1.00 14.07  ? 2685 GLN A N     1 
ATOM   9013  C  CA    . GLN A 1 2685 ? 160.466 194.946 170.435 1.00 13.59  ? 2685 GLN A CA    1 
ATOM   9014  C  C     . GLN A 1 2685 ? 159.782 196.053 171.226 1.00 15.15  ? 2685 GLN A C     1 
ATOM   9015  O  O     . GLN A 1 2685 ? 159.618 197.172 170.725 1.00 19.39  ? 2685 GLN A O     1 
ATOM   9016  C  CB    . GLN A 1 2685 ? 159.437 193.935 169.934 1.00 14.30  ? 2685 GLN A CB    1 
ATOM   9017  C  CG    . GLN A 1 2685 ? 158.210 194.568 169.302 1.00 17.26  ? 2685 GLN A CG    1 
ATOM   9018  C  CD    . GLN A 1 2685 ? 157.246 193.543 168.745 1.00 22.19  ? 2685 GLN A CD    1 
ATOM   9019  O  OE1   . GLN A 1 2685 ? 156.770 192.666 169.465 1.00 21.90  ? 2685 GLN A OE1   1 
ATOM   9020  N  NE2   . GLN A 1 2685 ? 156.951 193.650 167.456 1.00 21.19  ? 2685 GLN A NE2   1 
ATOM   9021  N  N     . MET A 1 2686 ? 159.374 195.764 172.463 1.00 16.51  ? 2686 MET A N     1 
ATOM   9022  C  CA    . MET A 1 2686 ? 158.713 196.789 173.267 1.00 14.94  ? 2686 MET A CA    1 
ATOM   9023  C  C     . MET A 1 2686 ? 159.665 197.854 173.798 1.00 13.52  ? 2686 MET A C     1 
ATOM   9024  O  O     . MET A 1 2686 ? 159.193 198.875 174.310 1.00 15.38  ? 2686 MET A O     1 
ATOM   9025  C  CB    . MET A 1 2686 ? 157.939 196.167 174.434 1.00 12.82  ? 2686 MET A CB    1 
ATOM   9026  C  CG    . MET A 1 2686 ? 157.408 194.779 174.172 1.00 16.26  ? 2686 MET A CG    1 
ATOM   9027  S  SD    . MET A 1 2686 ? 156.382 194.148 175.510 1.00 40.90  ? 2686 MET A SD    1 
ATOM   9028  C  CE    . MET A 1 2686 ? 157.620 193.815 176.758 1.00 17.87  ? 2686 MET A CE    1 
ATOM   9029  N  N     . VAL A 1 2687 ? 160.974 197.653 173.698 1.00 15.65  ? 2687 VAL A N     1 
ATOM   9030  C  CA    . VAL A 1 2687 ? 161.922 198.702 174.066 1.00 17.56  ? 2687 VAL A CA    1 
ATOM   9031  C  C     . VAL A 1 2687 ? 162.280 199.573 172.869 1.00 19.99  ? 2687 VAL A C     1 
ATOM   9032  O  O     . VAL A 1 2687 ? 162.221 200.803 172.943 1.00 23.75  ? 2687 VAL A O     1 
ATOM   9033  C  CB    . VAL A 1 2687 ? 163.180 198.080 174.708 1.00 14.48  ? 2687 VAL A CB    1 
ATOM   9034  C  CG1   . VAL A 1 2687 ? 164.297 199.099 174.755 1.00 16.70  ? 2687 VAL A CG1   1 
ATOM   9035  C  CG2   . VAL A 1 2687 ? 162.867 197.580 176.108 1.00 12.02  ? 2687 VAL A CG2   1 
ATOM   9036  N  N     . GLU A 1 2688 ? 162.656 198.952 171.748 1.00 17.91  ? 2688 GLU A N     1 
ATOM   9037  C  CA    . GLU A 1 2688 ? 163.021 199.715 170.559 1.00 18.60  ? 2688 GLU A CA    1 
ATOM   9038  C  C     . GLU A 1 2688 ? 161.817 200.443 169.973 1.00 20.62  ? 2688 GLU A C     1 
ATOM   9039  O  O     . GLU A 1 2688 ? 161.878 201.650 169.707 1.00 23.88  ? 2688 GLU A O     1 
ATOM   9040  C  CB    . GLU A 1 2688 ? 163.643 198.789 169.514 1.00 17.18  ? 2688 GLU A CB    1 
ATOM   9041  C  CG    . GLU A 1 2688 ? 164.070 199.498 168.240 1.00 23.11  ? 2688 GLU A CG    1 
ATOM   9042  C  CD    . GLU A 1 2688 ? 165.313 198.892 167.622 1.00 35.48  ? 2688 GLU A CD    1 
ATOM   9043  O  OE1   . GLU A 1 2688 ? 165.738 197.809 168.074 1.00 32.36  ? 2688 GLU A OE1   1 
ATOM   9044  O  OE2   . GLU A 1 2688 ? 165.865 199.500 166.681 1.00 35.29  ? 2688 GLU A OE2   1 
ATOM   9045  N  N     . HIS A 1 2689 ? 160.715 199.728 169.763 1.00 17.49  ? 2689 HIS A N     1 
ATOM   9046  C  CA    . HIS A 1 2689 ? 159.536 200.285 169.115 1.00 17.15  ? 2689 HIS A CA    1 
ATOM   9047  C  C     . HIS A 1 2689 ? 158.486 200.775 170.101 1.00 19.96  ? 2689 HIS A C     1 
ATOM   9048  O  O     . HIS A 1 2689 ? 157.444 201.281 169.672 1.00 25.65  ? 2689 HIS A O     1 
ATOM   9049  C  CB    . HIS A 1 2689 ? 158.920 199.247 168.172 1.00 16.24  ? 2689 HIS A CB    1 
ATOM   9050  C  CG    . HIS A 1 2689 ? 159.878 198.724 167.148 1.00 25.00  ? 2689 HIS A CG    1 
ATOM   9051  N  ND1   . HIS A 1 2689 ? 160.289 197.409 167.115 1.00 28.32  ? 2689 HIS A ND1   1 
ATOM   9052  C  CD2   . HIS A 1 2689 ? 160.513 199.342 166.124 1.00 23.62  ? 2689 HIS A CD2   1 
ATOM   9053  C  CE1   . HIS A 1 2689 ? 161.133 197.238 166.113 1.00 24.50  ? 2689 HIS A CE1   1 
ATOM   9054  N  NE2   . HIS A 1 2689 ? 161.286 198.395 165.496 1.00 25.08  ? 2689 HIS A NE2   1 
ATOM   9055  N  N     . GLY A 1 2690 ? 158.733 200.644 171.400 1.00 19.16  ? 2690 GLY A N     1 
ATOM   9056  C  CA    . GLY A 1 2690 ? 157.803 201.148 172.399 1.00 17.65  ? 2690 GLY A CA    1 
ATOM   9057  C  C     . GLY A 1 2690 ? 156.431 200.512 172.353 1.00 17.14  ? 2690 GLY A C     1 
ATOM   9058  O  O     . GLY A 1 2690 ? 155.421 201.209 172.513 1.00 24.18  ? 2690 GLY A O     1 
ATOM   9059  N  N     . GLY A 1 2691 ? 156.368 199.206 172.139 1.00 14.02  ? 2691 GLY A N     1 
ATOM   9060  C  CA    . GLY A 1 2691 ? 155.093 198.522 172.106 1.00 15.25  ? 2691 GLY A CA    1 
ATOM   9061  C  C     . GLY A 1 2691 ? 155.229 197.151 171.484 1.00 19.48  ? 2691 GLY A C     1 
ATOM   9062  O  O     . GLY A 1 2691 ? 156.320 196.714 171.106 1.00 24.86  ? 2691 GLY A O     1 
ATOM   9063  N  N     . PHE A 1 2692 ? 154.087 196.478 171.379 1.00 21.44  ? 2692 PHE A N     1 
ATOM   9064  C  CA    . PHE A 1 2692 ? 154.033 195.128 170.834 1.00 17.93  ? 2692 PHE A CA    1 
ATOM   9065  C  C     . PHE A 1 2692 ? 152.749 194.983 170.026 1.00 16.31  ? 2692 PHE A C     1 
ATOM   9066  O  O     . PHE A 1 2692 ? 152.012 195.951 169.818 1.00 17.87  ? 2692 PHE A O     1 
ATOM   9067  C  CB    . PHE A 1 2692 ? 154.133 194.087 171.957 1.00 18.00  ? 2692 PHE A CB    1 
ATOM   9068  C  CG    . PHE A 1 2692 ? 153.000 194.143 172.943 1.00 18.57  ? 2692 PHE A CG    1 
ATOM   9069  C  CD1   . PHE A 1 2692 ? 153.017 195.047 173.991 1.00 18.38  ? 2692 PHE A CD1   1 
ATOM   9070  C  CD2   . PHE A 1 2692 ? 151.919 193.285 172.825 1.00 19.08  ? 2692 PHE A CD2   1 
ATOM   9071  C  CE1   . PHE A 1 2692 ? 151.977 195.098 174.898 1.00 21.43  ? 2692 PHE A CE1   1 
ATOM   9072  C  CE2   . PHE A 1 2692 ? 150.876 193.332 173.729 1.00 18.88  ? 2692 PHE A CE2   1 
ATOM   9073  C  CZ    . PHE A 1 2692 ? 150.906 194.239 174.766 1.00 20.32  ? 2692 PHE A CZ    1 
ATOM   9074  N  N     . TYR A 1 2693 ? 152.482 193.763 169.569 1.00 17.89  ? 2693 TYR A N     1 
ATOM   9075  C  CA    . TYR A 1 2693 ? 151.295 193.448 168.787 1.00 17.18  ? 2693 TYR A CA    1 
ATOM   9076  C  C     . TYR A 1 2693 ? 150.368 192.565 169.610 1.00 20.22  ? 2693 TYR A C     1 
ATOM   9077  O  O     . TYR A 1 2693 ? 150.800 191.545 170.158 1.00 24.60  ? 2693 TYR A O     1 
ATOM   9078  C  CB    . TYR A 1 2693 ? 151.667 192.741 167.482 1.00 14.32  ? 2693 TYR A CB    1 
ATOM   9079  C  CG    . TYR A 1 2693 ? 151.865 193.671 166.308 1.00 15.53  ? 2693 TYR A CG    1 
ATOM   9080  C  CD1   . TYR A 1 2693 ? 150.786 194.314 165.718 1.00 17.02  ? 2693 TYR A CD1   1 
ATOM   9081  C  CD2   . TYR A 1 2693 ? 153.130 193.902 165.785 1.00 16.07  ? 2693 TYR A CD2   1 
ATOM   9082  C  CE1   . TYR A 1 2693 ? 150.962 195.164 164.644 1.00 18.06  ? 2693 TYR A CE1   1 
ATOM   9083  C  CE2   . TYR A 1 2693 ? 153.315 194.748 164.710 1.00 16.05  ? 2693 TYR A CE2   1 
ATOM   9084  C  CZ    . TYR A 1 2693 ? 152.227 195.377 164.144 1.00 17.71  ? 2693 TYR A CZ    1 
ATOM   9085  O  OH    . TYR A 1 2693 ? 152.406 196.222 163.074 1.00 15.92  ? 2693 TYR A OH    1 
ATOM   9086  N  N     . ARG A 1 2694 ? 149.100 192.958 169.695 1.00 21.75  ? 2694 ARG A N     1 
ATOM   9087  C  CA    . ARG A 1 2694 ? 148.095 192.165 170.395 1.00 25.32  ? 2694 ARG A CA    1 
ATOM   9088  C  C     . ARG A 1 2694 ? 147.579 191.091 169.446 1.00 27.87  ? 2694 ARG A C     1 
ATOM   9089  O  O     . ARG A 1 2694 ? 146.911 191.398 168.454 1.00 31.93  ? 2694 ARG A O     1 
ATOM   9090  C  CB    . ARG A 1 2694 ? 146.963 193.058 170.894 1.00 26.19  ? 2694 ARG A CB    1 
ATOM   9091  C  CG    . ARG A 1 2694 ? 146.027 192.383 171.880 1.00 28.65  ? 2694 ARG A CG    1 
ATOM   9092  C  CD    . ARG A 1 2694 ? 145.108 193.395 172.541 1.00 37.23  ? 2694 ARG A CD    1 
ATOM   9093  N  NE    . ARG A 1 2694 ? 144.385 194.200 171.564 1.00 36.77  ? 2694 ARG A NE    1 
ATOM   9094  C  CZ    . ARG A 1 2694 ? 143.554 195.185 171.874 1.00 39.24  ? 2694 ARG A CZ    1 
ATOM   9095  N  NH1   . ARG A 1 2694 ? 143.315 195.518 173.131 1.00 33.75  ? 2694 ARG A NH1   1 
ATOM   9096  N  NH2   . ARG A 1 2694 ? 142.946 195.853 170.897 1.00 41.81  ? 2694 ARG A NH2   1 
ATOM   9097  N  N     . THR A 1 2695 ? 147.884 189.829 169.750 1.00 28.66  ? 2695 THR A N     1 
ATOM   9098  C  CA    . THR A 1 2695 ? 147.545 188.729 168.856 1.00 29.59  ? 2695 THR A CA    1 
ATOM   9099  C  C     . THR A 1 2695 ? 146.049 188.453 168.784 1.00 32.03  ? 2695 THR A C     1 
ATOM   9100  O  O     . THR A 1 2695 ? 145.620 187.708 167.896 1.00 34.76  ? 2695 THR A O     1 
ATOM   9101  C  CB    . THR A 1 2695 ? 148.279 187.458 169.287 1.00 32.95  ? 2695 THR A CB    1 
ATOM   9102  O  OG1   . THR A 1 2695 ? 147.939 187.146 170.643 1.00 37.50  ? 2695 THR A OG1   1 
ATOM   9103  C  CG2   . THR A 1 2695 ? 149.783 187.652 169.178 1.00 28.03  ? 2695 THR A CG2   1 
ATOM   9104  N  N     . SER A 1 2696 ? 145.251 189.018 169.692 1.00 33.36  ? 2696 SER A N     1 
ATOM   9105  C  CA    . SER A 1 2696 ? 143.809 188.797 169.642 1.00 33.85  ? 2696 SER A CA    1 
ATOM   9106  C  C     . SER A 1 2696 ? 143.193 189.427 168.398 1.00 30.81  ? 2696 SER A C     1 
ATOM   9107  O  O     . SER A 1 2696 ? 142.301 188.840 167.776 1.00 29.98  ? 2696 SER A O     1 
ATOM   9108  C  CB    . SER A 1 2696 ? 143.149 189.346 170.906 1.00 33.53  ? 2696 SER A CB    1 
ATOM   9109  O  OG    . SER A 1 2696 ? 143.263 190.756 170.972 1.00 36.67  ? 2696 SER A OG    1 
ATOM   9110  N  N     . ASP A 1 2697 ? 143.656 190.621 168.018 1.00 28.48  ? 2697 ASP A N     1 
ATOM   9111  C  CA    . ASP A 1 2697 ? 143.108 191.328 166.868 1.00 28.15  ? 2697 ASP A CA    1 
ATOM   9112  C  C     . ASP A 1 2697 ? 144.184 191.925 165.968 1.00 30.85  ? 2697 ASP A C     1 
ATOM   9113  O  O     . ASP A 1 2697 ? 143.859 192.751 165.107 1.00 33.18  ? 2697 ASP A O     1 
ATOM   9114  C  CB    . ASP A 1 2697 ? 142.148 192.432 167.326 1.00 32.79  ? 2697 ASP A CB    1 
ATOM   9115  C  CG    . ASP A 1 2697 ? 142.754 193.325 168.389 1.00 38.16  ? 2697 ASP A CG    1 
ATOM   9116  O  OD1   . ASP A 1 2697 ? 143.805 192.954 168.951 1.00 34.53  ? 2697 ASP A OD1   1 
ATOM   9117  O  OD2   . ASP A 1 2697 ? 142.178 194.399 168.664 1.00 48.56  ? 2697 ASP A OD2   1 
ATOM   9118  N  N     . GLN A 1 2698 ? 145.448 191.529 166.142 1.00 30.09  ? 2698 GLN A N     1 
ATOM   9119  C  CA    . GLN A 1 2698 ? 146.561 192.040 165.338 1.00 26.00  ? 2698 GLN A CA    1 
ATOM   9120  C  C     . GLN A 1 2698 ? 146.636 193.564 165.393 1.00 28.43  ? 2698 GLN A C     1 
ATOM   9121  O  O     . GLN A 1 2698 ? 146.883 194.229 164.385 1.00 32.96  ? 2698 GLN A O     1 
ATOM   9122  C  CB    . GLN A 1 2698 ? 146.472 191.554 163.889 1.00 27.69  ? 2698 GLN A CB    1 
ATOM   9123  C  CG    . GLN A 1 2698 ? 146.826 190.089 163.686 1.00 25.75  ? 2698 GLN A CG    1 
ATOM   9124  C  CD    . GLN A 1 2698 ? 145.785 189.143 164.248 1.00 29.91  ? 2698 GLN A CD    1 
ATOM   9125  O  OE1   . GLN A 1 2698 ? 146.077 188.335 165.129 1.00 35.11  ? 2698 GLN A OE1   1 
ATOM   9126  N  NE2   . GLN A 1 2698 ? 144.563 189.236 163.738 1.00 29.71  ? 2698 GLN A NE2   1 
ATOM   9127  N  N     . THR A 1 2699 ? 146.423 194.121 166.580 1.00 26.46  ? 2699 THR A N     1 
ATOM   9128  C  CA    . THR A 1 2699 ? 146.421 195.563 166.783 1.00 27.75  ? 2699 THR A CA    1 
ATOM   9129  C  C     . THR A 1 2699 ? 147.688 195.977 167.519 1.00 24.05  ? 2699 THR A C     1 
ATOM   9130  O  O     . THR A 1 2699 ? 148.032 195.391 168.551 1.00 26.25  ? 2699 THR A O     1 
ATOM   9131  C  CB    . THR A 1 2699 ? 145.185 196.000 167.573 1.00 32.33  ? 2699 THR A CB    1 
ATOM   9132  O  OG1   . THR A 1 2699 ? 144.014 195.823 166.767 1.00 37.49  ? 2699 THR A OG1   1 
ATOM   9133  C  CG2   . THR A 1 2699 ? 145.296 197.461 167.976 1.00 28.14  ? 2699 THR A CG2   1 
ATOM   9134  N  N     . TRP A 1 2700 ? 148.379 196.981 166.984 1.00 21.55  ? 2700 TRP A N     1 
ATOM   9135  C  CA    . TRP A 1 2700 ? 149.580 197.490 167.630 1.00 19.67  ? 2700 TRP A CA    1 
ATOM   9136  C  C     . TRP A 1 2700 ? 149.213 198.206 168.923 1.00 20.16  ? 2700 TRP A C     1 
ATOM   9137  O  O     . TRP A 1 2700 ? 148.354 199.092 168.933 1.00 23.01  ? 2700 TRP A O     1 
ATOM   9138  C  CB    . TRP A 1 2700 ? 150.326 198.435 166.689 1.00 16.49  ? 2700 TRP A CB    1 
ATOM   9139  C  CG    . TRP A 1 2700 ? 151.549 199.055 167.293 1.00 15.15  ? 2700 TRP A CG    1 
ATOM   9140  C  CD1   . TRP A 1 2700 ? 151.667 200.321 167.787 1.00 17.52  ? 2700 TRP A CD1   1 
ATOM   9141  C  CD2   . TRP A 1 2700 ? 152.831 198.439 167.461 1.00 16.05  ? 2700 TRP A CD2   1 
ATOM   9142  N  NE1   . TRP A 1 2700 ? 152.941 200.530 168.255 1.00 19.05  ? 2700 TRP A NE1   1 
ATOM   9143  C  CE2   . TRP A 1 2700 ? 153.675 199.390 168.066 1.00 18.72  ? 2700 TRP A CE2   1 
ATOM   9144  C  CE3   . TRP A 1 2700 ? 153.347 197.175 167.161 1.00 17.43  ? 2700 TRP A CE3   1 
ATOM   9145  C  CZ2   . TRP A 1 2700 ? 155.005 199.117 168.376 1.00 19.51  ? 2700 TRP A CZ2   1 
ATOM   9146  C  CZ3   . TRP A 1 2700 ? 154.667 196.907 167.468 1.00 15.91  ? 2700 TRP A CZ3   1 
ATOM   9147  C  CH2   . TRP A 1 2700 ? 155.481 197.873 168.069 1.00 16.87  ? 2700 TRP A CH2   1 
ATOM   9148  N  N     . VAL A 1 2701 ? 149.867 197.820 170.014 1.00 19.66  ? 2701 VAL A N     1 
ATOM   9149  C  CA    . VAL A 1 2701 ? 149.618 198.385 171.335 1.00 20.37  ? 2701 VAL A CA    1 
ATOM   9150  C  C     . VAL A 1 2701 ? 150.880 199.113 171.774 1.00 18.99  ? 2701 VAL A C     1 
ATOM   9151  O  O     . VAL A 1 2701 ? 151.972 198.532 171.769 1.00 24.02  ? 2701 VAL A O     1 
ATOM   9152  C  CB    . VAL A 1 2701 ? 149.224 197.302 172.350 1.00 20.67  ? 2701 VAL A CB    1 
ATOM   9153  C  CG1   . VAL A 1 2701 ? 148.864 197.932 173.680 1.00 26.26  ? 2701 VAL A CG1   1 
ATOM   9154  C  CG2   . VAL A 1 2701 ? 148.068 196.473 171.817 1.00 23.81  ? 2701 VAL A CG2   1 
ATOM   9155  N  N     . LYS A 1 2702 ? 150.733 200.378 172.156 1.00 16.96  ? 2702 LYS A N     1 
ATOM   9156  C  CA    . LYS A 1 2702 ? 151.861 201.219 172.534 1.00 21.78  ? 2702 LYS A CA    1 
ATOM   9157  C  C     . LYS A 1 2702 ? 151.968 201.271 174.053 1.00 27.43  ? 2702 LYS A C     1 
ATOM   9158  O  O     . LYS A 1 2702 ? 151.003 201.629 174.736 1.00 32.58  ? 2702 LYS A O     1 
ATOM   9159  C  CB    . LYS A 1 2702 ? 151.707 202.627 171.960 1.00 24.84  ? 2702 LYS A CB    1 
ATOM   9160  C  CG    . LYS A 1 2702 ? 152.903 203.528 172.211 1.00 30.40  ? 2702 LYS A CG    1 
ATOM   9161  C  CD    . LYS A 1 2702 ? 152.707 204.896 171.582 1.00 38.89  ? 2702 LYS A CD    1 
ATOM   9162  C  CE    . LYS A 1 2702 ? 151.830 205.781 172.452 1.00 44.99  ? 2702 LYS A CE    1 
ATOM   9163  N  NZ    . LYS A 1 2702 ? 152.546 206.242 173.673 1.00 44.08  ? 2702 LYS A NZ    1 
ATOM   9164  N  N     . LEU A 1 2703 ? 153.138 200.914 174.574 1.00 26.99  ? 2703 LEU A N     1 
ATOM   9165  C  CA    . LEU A 1 2703 ? 153.367 200.965 176.010 1.00 22.81  ? 2703 LEU A CA    1 
ATOM   9166  C  C     . LEU A 1 2703 ? 153.438 202.408 176.491 1.00 28.93  ? 2703 LEU A C     1 
ATOM   9167  O  O     . LEU A 1 2703 ? 153.964 203.285 175.802 1.00 37.05  ? 2703 LEU A O     1 
ATOM   9168  C  CB    . LEU A 1 2703 ? 154.657 200.231 176.372 1.00 21.22  ? 2703 LEU A CB    1 
ATOM   9169  C  CG    . LEU A 1 2703 ? 154.722 198.735 176.065 1.00 21.10  ? 2703 LEU A CG    1 
ATOM   9170  C  CD1   . LEU A 1 2703 ? 155.853 198.088 176.842 1.00 21.69  ? 2703 LEU A CD1   1 
ATOM   9171  C  CD2   . LEU A 1 2703 ? 153.399 198.062 176.383 1.00 23.71  ? 2703 LEU A CD2   1 
ATOM   9172  N  N     . GLU A 1 2704 ? 152.903 202.650 177.685 1.00 27.30  ? 2704 GLU A N     1 
ATOM   9173  C  CA    . GLU A 1 2704 ? 152.958 203.964 178.310 1.00 28.74  ? 2704 GLU A CA    1 
ATOM   9174  C  C     . GLU A 1 2704 ? 153.174 203.786 179.803 1.00 29.60  ? 2704 GLU A C     1 
ATOM   9175  O  O     . GLU A 1 2704 ? 152.485 202.983 180.438 1.00 35.23  ? 2704 GLU A O     1 
ATOM   9176  C  CB    . GLU A 1 2704 ? 151.676 204.761 178.048 1.00 31.66  ? 2704 GLU A CB    1 
ATOM   9177  C  CG    . GLU A 1 2704 ? 151.665 206.141 178.681 1.00 41.86  ? 2704 GLU A CG    1 
ATOM   9178  C  CD    . GLU A 1 2704 ? 150.268 206.717 178.801 1.00 56.12  ? 2704 GLU A CD    1 
ATOM   9179  O  OE1   . GLU A 1 2704 ? 149.565 206.794 177.771 1.00 62.69  ? 2704 GLU A OE1   1 
ATOM   9180  O  OE2   . GLU A 1 2704 ? 149.872 207.093 179.924 1.00 51.05  ? 2704 GLU A OE2   1 
ATOM   9181  N  N     . ARG A 1 2705 ? 154.132 204.535 180.354 1.00 23.90  ? 2705 ARG A N     1 
ATOM   9182  C  CA    . ARG A 1 2705 ? 154.474 204.469 181.776 1.00 21.87  ? 2705 ARG A CA    1 
ATOM   9183  C  C     . ARG A 1 2705 ? 154.858 203.050 182.191 1.00 23.10  ? 2705 ARG A C     1 
ATOM   9184  O  O     . ARG A 1 2705 ? 154.520 202.589 183.283 1.00 25.16  ? 2705 ARG A O     1 
ATOM   9185  C  CB    . ARG A 1 2705 ? 153.333 205.002 182.646 1.00 25.64  ? 2705 ARG A CB    1 
ATOM   9186  C  CG    . ARG A 1 2705 ? 153.281 206.517 182.734 1.00 25.97  ? 2705 ARG A CG    1 
ATOM   9187  C  CD    . ARG A 1 2705 ? 152.140 206.986 183.621 1.00 30.19  ? 2705 ARG A CD    1 
ATOM   9188  N  NE    . ARG A 1 2705 ? 150.837 206.608 183.089 1.00 36.26  ? 2705 ARG A NE    1 
ATOM   9189  C  CZ    . ARG A 1 2705 ? 149.962 205.840 183.723 1.00 35.65  ? 2705 ARG A CZ    1 
ATOM   9190  N  NH1   . ARG A 1 2705 ? 150.221 205.340 184.920 1.00 34.34  ? 2705 ARG A NH1   1 
ATOM   9191  N  NH2   . ARG A 1 2705 ? 148.797 205.567 183.143 1.00 37.13  ? 2705 ARG A NH2   1 
ATOM   9192  N  N     . ILE A 1 2706 ? 155.571 202.350 181.312 1.00 24.05  ? 2706 ILE A N     1 
ATOM   9193  C  CA    . ILE A 1 2706 ? 156.042 200.995 181.575 1.00 23.45  ? 2706 ILE A CA    1 
ATOM   9194  C  C     . ILE A 1 2706 ? 157.511 200.913 181.188 1.00 23.16  ? 2706 ILE A C     1 
ATOM   9195  O  O     . ILE A 1 2706 ? 157.890 201.321 180.085 1.00 23.73  ? 2706 ILE A O     1 
ATOM   9196  C  CB    . ILE A 1 2706 ? 155.222 199.940 180.806 1.00 21.36  ? 2706 ILE A CB    1 
ATOM   9197  C  CG1   . ILE A 1 2706 ? 153.824 199.804 181.407 1.00 17.96  ? 2706 ILE A CG1   1 
ATOM   9198  C  CG2   . ILE A 1 2706 ? 155.933 198.596 180.814 1.00 20.68  ? 2706 ILE A CG2   1 
ATOM   9199  C  CD1   . ILE A 1 2706 ? 152.865 199.028 180.538 1.00 19.13  ? 2706 ILE A CD1   1 
ATOM   9200  N  N     . GLN A 1 2707 ? 158.338 200.390 182.092 1.00 19.66  ? 2707 GLN A N     1 
ATOM   9201  C  CA    . GLN A 1 2707 ? 159.752 200.182 181.822 1.00 19.06  ? 2707 GLN A CA    1 
ATOM   9202  C  C     . GLN A 1 2707 ? 160.165 198.825 182.372 1.00 18.59  ? 2707 GLN A C     1 
ATOM   9203  O  O     . GLN A 1 2707 ? 159.392 198.143 183.049 1.00 22.10  ? 2707 GLN A O     1 
ATOM   9204  C  CB    . GLN A 1 2707 ? 160.613 201.295 182.425 1.00 19.77  ? 2707 GLN A CB    1 
ATOM   9205  C  CG    . GLN A 1 2707 ? 160.453 201.457 183.917 1.00 19.48  ? 2707 GLN A CG    1 
ATOM   9206  C  CD    . GLN A 1 2707 ? 161.457 202.424 184.492 1.00 22.32  ? 2707 GLN A CD    1 
ATOM   9207  O  OE1   . GLN A 1 2707 ? 161.089 203.433 185.086 1.00 21.01  ? 2707 GLN A OE1   1 
ATOM   9208  N  NE2   . GLN A 1 2707 ? 162.737 202.127 184.312 1.00 29.17  ? 2707 GLN A NE2   1 
ATOM   9209  N  N     . PHE A 1 2708 ? 161.402 198.436 182.076 1.00 16.81  ? 2708 PHE A N     1 
ATOM   9210  C  CA    . PHE A 1 2708 ? 161.890 197.104 182.397 1.00 16.37  ? 2708 PHE A CA    1 
ATOM   9211  C  C     . PHE A 1 2708 ? 163.245 197.184 183.080 1.00 17.80  ? 2708 PHE A C     1 
ATOM   9212  O  O     . PHE A 1 2708 ? 164.087 198.012 182.722 1.00 20.77  ? 2708 PHE A O     1 
ATOM   9213  C  CB    . PHE A 1 2708 ? 161.996 196.241 181.135 1.00 13.10  ? 2708 PHE A CB    1 
ATOM   9214  C  CG    . PHE A 1 2708 ? 160.810 196.360 180.226 1.00 17.24  ? 2708 PHE A CG    1 
ATOM   9215  C  CD1   . PHE A 1 2708 ? 159.701 195.553 180.404 1.00 16.44  ? 2708 PHE A CD1   1 
ATOM   9216  C  CD2   . PHE A 1 2708 ? 160.802 197.286 179.196 1.00 18.73  ? 2708 PHE A CD2   1 
ATOM   9217  C  CE1   . PHE A 1 2708 ? 158.608 195.667 179.572 1.00 15.98  ? 2708 PHE A CE1   1 
ATOM   9218  C  CE2   . PHE A 1 2708 ? 159.713 197.403 178.361 1.00 17.79  ? 2708 PHE A CE2   1 
ATOM   9219  C  CZ    . PHE A 1 2708 ? 158.615 196.594 178.549 1.00 18.32  ? 2708 PHE A CZ    1 
ATOM   9220  N  N     . VAL A 1 2709 ? 163.444 196.318 184.070 1.00 14.72  ? 2709 VAL A N     1 
ATOM   9221  C  CA    . VAL A 1 2709 ? 164.728 196.139 184.734 1.00 12.33  ? 2709 VAL A CA    1 
ATOM   9222  C  C     . VAL A 1 2709 ? 165.034 194.650 184.754 1.00 14.07  ? 2709 VAL A C     1 
ATOM   9223  O  O     . VAL A 1 2709 ? 164.189 193.845 185.160 1.00 20.14  ? 2709 VAL A O     1 
ATOM   9224  C  CB    . VAL A 1 2709 ? 164.726 196.714 186.163 1.00 13.06  ? 2709 VAL A CB    1 
ATOM   9225  C  CG1   . VAL A 1 2709 ? 165.949 196.237 186.925 1.00 13.59  ? 2709 VAL A CG1   1 
ATOM   9226  C  CG2   . VAL A 1 2709 ? 164.686 198.230 186.119 1.00 15.08  ? 2709 VAL A CG2   1 
ATOM   9227  N  N     . GLY A 1 2710 ? 166.232 194.283 184.313 1.00 13.43  ? 2710 GLY A N     1 
ATOM   9228  C  CA    . GLY A 1 2710 ? 166.632 192.893 184.216 1.00 14.25  ? 2710 GLY A CA    1 
ATOM   9229  C  C     . GLY A 1 2710 ? 167.731 192.555 185.204 1.00 13.85  ? 2710 GLY A C     1 
ATOM   9230  O  O     . GLY A 1 2710 ? 168.557 193.401 185.551 1.00 18.96  ? 2710 GLY A O     1 
ATOM   9231  N  N     . ALA A 1 2711 ? 167.724 191.310 185.667 1.00 11.70  ? 2711 ALA A N     1 
ATOM   9232  C  CA    . ALA A 1 2711 ? 168.794 190.765 186.485 1.00 9.82   ? 2711 ALA A CA    1 
ATOM   9233  C  C     . ALA A 1 2711 ? 169.164 189.395 185.940 1.00 15.78  ? 2711 ALA A C     1 
ATOM   9234  O  O     . ALA A 1 2711 ? 168.318 188.684 185.392 1.00 24.65  ? 2711 ALA A O     1 
ATOM   9235  C  CB    . ALA A 1 2711 ? 168.392 190.660 187.960 1.00 10.13  ? 2711 ALA A CB    1 
ATOM   9236  N  N     . CYS A 1 2712 ? 170.436 189.034 186.081 1.00 14.34  ? 2712 CYS A N     1 
ATOM   9237  C  CA    . CYS A 1 2712 ? 170.897 187.768 185.529 1.00 15.66  ? 2712 CYS A CA    1 
ATOM   9238  C  C     . CYS A 1 2712 ? 172.274 187.442 186.078 1.00 17.06  ? 2712 CYS A C     1 
ATOM   9239  O  O     . CYS A 1 2712 ? 173.036 188.336 186.456 1.00 19.22  ? 2712 CYS A O     1 
ATOM   9240  C  CB    . CYS A 1 2712 ? 170.944 187.813 183.997 1.00 15.92  ? 2712 CYS A CB    1 
ATOM   9241  S  SG    . CYS A 1 2712 ? 171.763 189.272 183.324 1.00 16.20  ? 2712 CYS A SG    1 
ATOM   9242  N  N     . ASN A 1 2713 ? 172.576 186.150 186.119 1.00 17.12  ? 2713 ASN A N     1 
ATOM   9243  C  CA    . ASN A 1 2713 ? 173.923 185.677 186.367 1.00 16.79  ? 2713 ASN A CA    1 
ATOM   9244  C  C     . ASN A 1 2713 ? 174.767 185.853 185.108 1.00 20.12  ? 2713 ASN A C     1 
ATOM   9245  O  O     . ASN A 1 2713 ? 174.227 186.039 184.014 1.00 23.32  ? 2713 ASN A O     1 
ATOM   9246  C  CB    . ASN A 1 2713 ? 173.891 184.214 186.797 1.00 19.40  ? 2713 ASN A CB    1 
ATOM   9247  C  CG    . ASN A 1 2713 ? 173.145 184.009 188.099 1.00 23.95  ? 2713 ASN A CG    1 
ATOM   9248  O  OD1   . ASN A 1 2713 ? 172.667 184.963 188.710 1.00 25.31  ? 2713 ASN A OD1   1 
ATOM   9249  N  ND2   . ASN A 1 2713 ? 173.044 182.759 188.532 1.00 27.29  ? 2713 ASN A ND2   1 
ATOM   9250  N  N     . PRO A 1 2714 ? 176.093 185.826 185.234 1.00 19.46  ? 2714 PRO A N     1 
ATOM   9251  C  CA    . PRO A 1 2714 ? 176.934 185.972 184.051 1.00 19.50  ? 2714 PRO A CA    1 
ATOM   9252  C  C     . PRO A 1 2714 ? 176.627 184.891 183.038 1.00 21.66  ? 2714 PRO A C     1 
ATOM   9253  O  O     . PRO A 1 2714 ? 176.297 183.746 183.402 1.00 25.50  ? 2714 PRO A O     1 
ATOM   9254  C  CB    . PRO A 1 2714 ? 178.356 185.831 184.613 1.00 21.16  ? 2714 PRO A CB    1 
ATOM   9255  C  CG    . PRO A 1 2714 ? 178.242 186.292 186.014 1.00 20.24  ? 2714 PRO A CG    1 
ATOM   9256  C  CD    . PRO A 1 2714 ? 176.886 185.847 186.477 1.00 20.42  ? 2714 PRO A CD    1 
ATOM   9257  N  N     . PRO A 1 2715 ? 176.708 185.211 181.743 1.00 21.55  ? 2715 PRO A N     1 
ATOM   9258  C  CA    . PRO A 1 2715 ? 176.339 184.223 180.716 1.00 18.67  ? 2715 PRO A CA    1 
ATOM   9259  C  C     . PRO A 1 2715 ? 177.212 182.982 180.718 1.00 21.09  ? 2715 PRO A C     1 
ATOM   9260  O  O     . PRO A 1 2715 ? 176.800 181.955 180.165 1.00 23.60  ? 2715 PRO A O     1 
ATOM   9261  C  CB    . PRO A 1 2715 ? 176.484 185.008 179.404 1.00 19.98  ? 2715 PRO A CB    1 
ATOM   9262  C  CG    . PRO A 1 2715 ? 177.415 186.128 179.729 1.00 23.55  ? 2715 PRO A CG    1 
ATOM   9263  C  CD    . PRO A 1 2715 ? 177.143 186.489 181.157 1.00 19.42  ? 2715 PRO A CD    1 
ATOM   9264  N  N     . THR A 1 2716 ? 178.403 183.040 181.315 1.00 24.46  ? 2716 THR A N     1 
ATOM   9265  C  CA    . THR A 1 2716 ? 179.249 181.857 181.406 1.00 25.08  ? 2716 THR A CA    1 
ATOM   9266  C  C     . THR A 1 2716 ? 178.708 180.834 182.397 1.00 29.45  ? 2716 THR A C     1 
ATOM   9267  O  O     . THR A 1 2716 ? 179.135 179.675 182.364 1.00 35.35  ? 2716 THR A O     1 
ATOM   9268  C  CB    . THR A 1 2716 ? 180.671 182.254 181.800 1.00 30.27  ? 2716 THR A CB    1 
ATOM   9269  O  OG1   . THR A 1 2716 ? 180.662 182.821 183.116 1.00 29.57  ? 2716 THR A OG1   1 
ATOM   9270  C  CG2   . THR A 1 2716 ? 181.228 183.273 180.819 1.00 25.35  ? 2716 THR A CG2   1 
ATOM   9271  N  N     . ASP A 1 2717 ? 177.790 181.233 183.273 1.00 25.17  ? 2717 ASP A N     1 
ATOM   9272  C  CA    . ASP A 1 2717 ? 177.216 180.303 184.231 1.00 25.74  ? 2717 ASP A CA    1 
ATOM   9273  C  C     . ASP A 1 2717 ? 176.371 179.254 183.510 1.00 27.78  ? 2717 ASP A C     1 
ATOM   9274  O  O     . ASP A 1 2717 ? 175.789 179.531 182.458 1.00 28.73  ? 2717 ASP A O     1 
ATOM   9275  C  CB    . ASP A 1 2717 ? 176.361 181.049 185.251 1.00 25.34  ? 2717 ASP A CB    1 
ATOM   9276  C  CG    . ASP A 1 2717 ? 177.190 181.725 186.323 1.00 36.91  ? 2717 ASP A CG    1 
ATOM   9277  O  OD1   . ASP A 1 2717 ? 178.429 181.779 186.173 1.00 32.89  ? 2717 ASP A OD1   1 
ATOM   9278  O  OD2   . ASP A 1 2717 ? 176.604 182.204 187.316 1.00 42.90  ? 2717 ASP A OD2   1 
ATOM   9279  N  N     . PRO A 1 2718 ? 176.302 178.035 184.047 1.00 27.29  ? 2718 PRO A N     1 
ATOM   9280  C  CA    . PRO A 1 2718 ? 175.506 176.988 183.393 1.00 24.34  ? 2718 PRO A CA    1 
ATOM   9281  C  C     . PRO A 1 2718 ? 174.037 177.374 183.311 1.00 24.37  ? 2718 PRO A C     1 
ATOM   9282  O  O     . PRO A 1 2718 ? 173.469 177.938 184.247 1.00 29.99  ? 2718 PRO A O     1 
ATOM   9283  C  CB    . PRO A 1 2718 ? 175.719 175.764 184.291 1.00 22.90  ? 2718 PRO A CB    1 
ATOM   9284  C  CG    . PRO A 1 2718 ? 176.194 176.313 185.595 1.00 25.62  ? 2718 PRO A CG    1 
ATOM   9285  C  CD    . PRO A 1 2718 ? 176.975 177.542 185.259 1.00 26.87  ? 2718 PRO A CD    1 
ATOM   9286  N  N     . GLY A 1 2719 ? 173.423 177.058 182.173 1.00 22.83  ? 2719 GLY A N     1 
ATOM   9287  C  CA    . GLY A 1 2719 ? 172.033 177.378 181.940 1.00 22.39  ? 2719 GLY A CA    1 
ATOM   9288  C  C     . GLY A 1 2719 ? 171.761 178.807 181.528 1.00 24.11  ? 2719 GLY A C     1 
ATOM   9289  O  O     . GLY A 1 2719 ? 170.593 179.165 181.333 1.00 30.03  ? 2719 GLY A O     1 
ATOM   9290  N  N     . ARG A 1 2720 ? 172.793 179.633 181.386 1.00 21.67  ? 2720 ARG A N     1 
ATOM   9291  C  CA    . ARG A 1 2720 ? 172.646 181.037 181.030 1.00 19.43  ? 2720 ARG A CA    1 
ATOM   9292  C  C     . ARG A 1 2720 ? 173.095 181.246 179.592 1.00 20.34  ? 2720 ARG A C     1 
ATOM   9293  O  O     . ARG A 1 2720 ? 174.209 180.860 179.223 1.00 22.40  ? 2720 ARG A O     1 
ATOM   9294  C  CB    . ARG A 1 2720 ? 173.457 181.928 181.973 1.00 20.19  ? 2720 ARG A CB    1 
ATOM   9295  C  CG    . ARG A 1 2720 ? 173.248 181.615 183.443 1.00 21.19  ? 2720 ARG A CG    1 
ATOM   9296  C  CD    . ARG A 1 2720 ? 171.790 181.771 183.823 1.00 23.64  ? 2720 ARG A CD    1 
ATOM   9297  N  NE    . ARG A 1 2720 ? 171.581 181.732 185.265 1.00 27.99  ? 2720 ARG A NE    1 
ATOM   9298  C  CZ    . ARG A 1 2720 ? 171.498 180.617 185.978 1.00 25.61  ? 2720 ARG A CZ    1 
ATOM   9299  N  NH1   . ARG A 1 2720 ? 171.614 179.426 185.416 1.00 25.46  ? 2720 ARG A NH1   1 
ATOM   9300  N  NH2   . ARG A 1 2720 ? 171.288 180.699 187.289 1.00 26.39  ? 2720 ARG A NH2   1 
ATOM   9301  N  N     . LYS A 1 2721 ? 172.230 181.855 178.788 1.00 20.88  ? 2721 LYS A N     1 
ATOM   9302  C  CA    . LYS A 1 2721 ? 172.569 182.127 177.400 1.00 21.55  ? 2721 LYS A CA    1 
ATOM   9303  C  C     . LYS A 1 2721 ? 172.920 183.596 177.216 1.00 24.30  ? 2721 LYS A C     1 
ATOM   9304  O  O     . LYS A 1 2721 ? 172.320 184.463 177.862 1.00 23.71  ? 2721 LYS A O     1 
ATOM   9305  C  CB    . LYS A 1 2721 ? 171.403 181.768 176.477 1.00 19.90  ? 2721 LYS A CB    1 
ATOM   9306  C  CG    . LYS A 1 2721 ? 171.395 180.321 176.013 1.00 20.57  ? 2721 LYS A CG    1 
ATOM   9307  C  CD    . LYS A 1 2721 ? 170.812 179.403 177.075 1.00 19.82  ? 2721 LYS A CD    1 
ATOM   9308  C  CE    . LYS A 1 2721 ? 169.422 179.853 177.490 1.00 19.69  ? 2721 LYS A CE    1 
ATOM   9309  N  NZ    . LYS A 1 2721 ? 168.832 178.953 178.518 1.00 21.05  ? 2721 LYS A NZ    1 
ATOM   9310  N  N     . PRO A 1 2722 ? 173.892 183.908 176.360 1.00 22.98  ? 2722 PRO A N     1 
ATOM   9311  C  CA    . PRO A 1 2722 ? 174.215 185.316 176.103 1.00 20.61  ? 2722 PRO A CA    1 
ATOM   9312  C  C     . PRO A 1 2722 ? 173.041 186.042 175.467 1.00 22.49  ? 2722 PRO A C     1 
ATOM   9313  O  O     . PRO A 1 2722 ? 172.316 185.486 174.639 1.00 23.96  ? 2722 PRO A O     1 
ATOM   9314  C  CB    . PRO A 1 2722 ? 175.413 185.239 175.149 1.00 20.41  ? 2722 PRO A CB    1 
ATOM   9315  C  CG    . PRO A 1 2722 ? 175.305 183.895 174.513 1.00 20.64  ? 2722 PRO A CG    1 
ATOM   9316  C  CD    . PRO A 1 2722 ? 174.718 182.992 175.556 1.00 22.99  ? 2722 PRO A CD    1 
ATOM   9317  N  N     . LEU A 1 2723 ? 172.859 187.297 175.864 1.00 21.57  ? 2723 LEU A N     1 
ATOM   9318  C  CA    . LEU A 1 2723 ? 171.768 188.101 175.338 1.00 18.40  ? 2723 LEU A CA    1 
ATOM   9319  C  C     . LEU A 1 2723 ? 172.112 188.623 173.948 1.00 19.20  ? 2723 LEU A C     1 
ATOM   9320  O  O     . LEU A 1 2723 ? 173.281 188.829 173.609 1.00 24.60  ? 2723 LEU A O     1 
ATOM   9321  C  CB    . LEU A 1 2723 ? 171.455 189.264 176.278 1.00 17.52  ? 2723 LEU A CB    1 
ATOM   9322  C  CG    . LEU A 1 2723 ? 170.775 188.879 177.594 1.00 12.45  ? 2723 LEU A CG    1 
ATOM   9323  C  CD1   . LEU A 1 2723 ? 170.800 190.037 178.577 1.00 12.02  ? 2723 LEU A CD1   1 
ATOM   9324  C  CD2   . LEU A 1 2723 ? 169.351 188.414 177.346 1.00 12.08  ? 2723 LEU A CD2   1 
ATOM   9325  N  N     . SER A 1 2724 ? 171.075 188.831 173.142 1.00 15.89  ? 2724 SER A N     1 
ATOM   9326  C  CA    . SER A 1 2724 ? 171.264 189.286 171.772 1.00 15.56  ? 2724 SER A CA    1 
ATOM   9327  C  C     . SER A 1 2724 ? 171.894 190.673 171.747 1.00 17.85  ? 2724 SER A C     1 
ATOM   9328  O  O     . SER A 1 2724 ? 171.595 191.525 172.588 1.00 21.53  ? 2724 SER A O     1 
ATOM   9329  C  CB    . SER A 1 2724 ? 169.928 189.303 171.031 1.00 19.27  ? 2724 SER A CB    1 
ATOM   9330  O  OG    . SER A 1 2724 ? 170.077 189.818 169.720 1.00 26.04  ? 2724 SER A OG    1 
ATOM   9331  N  N     . HIS A 1 2725 ? 172.779 190.893 170.772 1.00 19.47  ? 2725 HIS A N     1 
ATOM   9332  C  CA    . HIS A 1 2725 ? 173.419 192.197 170.638 1.00 15.92  ? 2725 HIS A CA    1 
ATOM   9333  C  C     . HIS A 1 2725 ? 172.414 193.281 170.274 1.00 14.12  ? 2725 HIS A C     1 
ATOM   9334  O  O     . HIS A 1 2725 ? 172.622 194.453 170.605 1.00 16.93  ? 2725 HIS A O     1 
ATOM   9335  C  CB    . HIS A 1 2725 ? 174.533 192.133 169.595 1.00 22.79  ? 2725 HIS A CB    1 
ATOM   9336  C  CG    . HIS A 1 2725 ? 175.788 191.488 170.093 1.00 30.32  ? 2725 HIS A CG    1 
ATOM   9337  N  ND1   . HIS A 1 2725 ? 176.920 191.364 169.318 1.00 37.98  ? 2725 HIS A ND1   1 
ATOM   9338  C  CD2   . HIS A 1 2725 ? 176.089 190.931 171.290 1.00 30.95  ? 2725 HIS A CD2   1 
ATOM   9339  C  CE1   . HIS A 1 2725 ? 177.864 190.759 170.015 1.00 42.06  ? 2725 HIS A CE1   1 
ATOM   9340  N  NE2   . HIS A 1 2725 ? 177.385 190.485 171.215 1.00 37.22  ? 2725 HIS A NE2   1 
ATOM   9341  N  N     . ARG A 1 2726 ? 171.327 192.915 169.592 1.00 16.38  ? 2726 ARG A N     1 
ATOM   9342  C  CA    . ARG A 1 2726 ? 170.271 193.877 169.306 1.00 14.09  ? 2726 ARG A CA    1 
ATOM   9343  C  C     . ARG A 1 2726 ? 169.469 194.228 170.551 1.00 15.12  ? 2726 ARG A C     1 
ATOM   9344  O  O     . ARG A 1 2726 ? 168.830 195.284 170.585 1.00 18.38  ? 2726 ARG A O     1 
ATOM   9345  C  CB    . ARG A 1 2726 ? 169.345 193.332 168.219 1.00 13.82  ? 2726 ARG A CB    1 
ATOM   9346  C  CG    . ARG A 1 2726 ? 170.075 192.820 166.989 1.00 17.11  ? 2726 ARG A CG    1 
ATOM   9347  C  CD    . ARG A 1 2726 ? 169.105 192.407 165.897 1.00 21.68  ? 2726 ARG A CD    1 
ATOM   9348  N  NE    . ARG A 1 2726 ? 168.623 193.549 165.130 1.00 15.23  ? 2726 ARG A NE    1 
ATOM   9349  C  CZ    . ARG A 1 2726 ? 167.774 193.464 164.115 1.00 15.84  ? 2726 ARG A CZ    1 
ATOM   9350  N  NH1   . ARG A 1 2726 ? 167.288 192.301 163.718 1.00 20.49  ? 2726 ARG A NH1   1 
ATOM   9351  N  NH2   . ARG A 1 2726 ? 167.404 194.574 163.484 1.00 16.13  ? 2726 ARG A NH2   1 
ATOM   9352  N  N     . PHE A 1 2727 ? 169.489 193.367 171.568 1.00 13.49  ? 2727 PHE A N     1 
ATOM   9353  C  CA    . PHE A 1 2727 ? 168.837 193.650 172.841 1.00 10.45  ? 2727 PHE A CA    1 
ATOM   9354  C  C     . PHE A 1 2727 ? 169.751 194.409 173.793 1.00 11.74  ? 2727 PHE A C     1 
ATOM   9355  O  O     . PHE A 1 2727 ? 169.305 195.349 174.460 1.00 15.15  ? 2727 PHE A O     1 
ATOM   9356  C  CB    . PHE A 1 2727 ? 168.373 192.347 173.496 1.00 11.70  ? 2727 PHE A CB    1 
ATOM   9357  C  CG    . PHE A 1 2727 ? 167.842 192.524 174.889 1.00 12.47  ? 2727 PHE A CG    1 
ATOM   9358  C  CD1   . PHE A 1 2727 ? 166.596 193.087 175.103 1.00 12.58  ? 2727 PHE A CD1   1 
ATOM   9359  C  CD2   . PHE A 1 2727 ? 168.590 192.130 175.985 1.00 13.18  ? 2727 PHE A CD2   1 
ATOM   9360  C  CE1   . PHE A 1 2727 ? 166.107 193.252 176.382 1.00 10.41  ? 2727 PHE A CE1   1 
ATOM   9361  C  CE2   . PHE A 1 2727 ? 168.105 192.294 177.266 1.00 13.44  ? 2727 PHE A CE2   1 
ATOM   9362  C  CZ    . PHE A 1 2727 ? 166.862 192.855 177.465 1.00 10.67  ? 2727 PHE A CZ    1 
ATOM   9363  N  N     . LEU A 1 2728 ? 171.025 194.019 173.867 1.00 13.70  ? 2728 LEU A N     1 
ATOM   9364  C  CA    . LEU A 1 2728 ? 171.973 194.702 174.738 1.00 12.21  ? 2728 LEU A CA    1 
ATOM   9365  C  C     . LEU A 1 2728 ? 172.245 196.131 174.291 1.00 12.81  ? 2728 LEU A C     1 
ATOM   9366  O  O     . LEU A 1 2728 ? 172.782 196.921 175.074 1.00 18.31  ? 2728 LEU A O     1 
ATOM   9367  C  CB    . LEU A 1 2728 ? 173.286 193.921 174.802 1.00 14.76  ? 2728 LEU A CB    1 
ATOM   9368  C  CG    . LEU A 1 2728 ? 173.270 192.631 175.621 1.00 14.68  ? 2728 LEU A CG    1 
ATOM   9369  C  CD1   . LEU A 1 2728 ? 174.668 192.048 175.721 1.00 22.74  ? 2728 LEU A CD1   1 
ATOM   9370  C  CD2   . LEU A 1 2728 ? 172.694 192.887 177.003 1.00 12.85  ? 2728 LEU A CD2   1 
ATOM   9371  N  N     . ARG A 1 2729 ? 171.892 196.477 173.052 1.00 12.54  ? 2729 ARG A N     1 
ATOM   9372  C  CA    . ARG A 1 2729 ? 172.127 197.830 172.562 1.00 11.78  ? 2729 ARG A CA    1 
ATOM   9373  C  C     . ARG A 1 2729 ? 171.341 198.862 173.360 1.00 11.63  ? 2729 ARG A C     1 
ATOM   9374  O  O     . ARG A 1 2729 ? 171.840 199.966 173.609 1.00 14.85  ? 2729 ARG A O     1 
ATOM   9375  C  CB    . ARG A 1 2729 ? 171.772 197.908 171.075 1.00 10.56  ? 2729 ARG A CB    1 
ATOM   9376  C  CG    . ARG A 1 2729 ? 171.525 199.309 170.549 1.00 12.85  ? 2729 ARG A CG    1 
ATOM   9377  C  CD    . ARG A 1 2729 ? 171.094 199.274 169.093 1.00 12.62  ? 2729 ARG A CD    1 
ATOM   9378  N  NE    . ARG A 1 2729 ? 170.705 200.593 168.609 1.00 11.83  ? 2729 ARG A NE    1 
ATOM   9379  C  CZ    . ARG A 1 2729 ? 169.535 200.871 168.054 1.00 13.41  ? 2729 ARG A CZ    1 
ATOM   9380  N  NH1   . ARG A 1 2729 ? 168.611 199.940 167.884 1.00 17.21  ? 2729 ARG A NH1   1 
ATOM   9381  N  NH2   . ARG A 1 2729 ? 169.284 202.115 167.658 1.00 14.62  ? 2729 ARG A NH2   1 
ATOM   9382  N  N     . HIS A 1 2730 ? 170.124 198.524 173.783 1.00 11.44  ? 2730 HIS A N     1 
ATOM   9383  C  CA    . HIS A 1 2730 ? 169.271 199.458 174.503 1.00 15.32  ? 2730 HIS A CA    1 
ATOM   9384  C  C     . HIS A 1 2730 ? 169.380 199.345 176.018 1.00 16.56  ? 2730 HIS A C     1 
ATOM   9385  O  O     . HIS A 1 2730 ? 168.933 200.257 176.720 1.00 21.46  ? 2730 HIS A O     1 
ATOM   9386  C  CB    . HIS A 1 2730 ? 167.805 199.264 174.098 1.00 16.28  ? 2730 HIS A CB    1 
ATOM   9387  C  CG    . HIS A 1 2730 ? 167.589 199.166 172.620 1.00 14.61  ? 2730 HIS A CG    1 
ATOM   9388  N  ND1   . HIS A 1 2730 ? 167.822 198.009 171.909 1.00 16.26  ? 2730 HIS A ND1   1 
ATOM   9389  C  CD2   . HIS A 1 2730 ? 167.158 200.080 171.720 1.00 13.70  ? 2730 HIS A CD2   1 
ATOM   9390  C  CE1   . HIS A 1 2730 ? 167.544 198.215 170.634 1.00 16.14  ? 2730 HIS A CE1   1 
ATOM   9391  N  NE2   . HIS A 1 2730 ? 167.139 199.464 170.493 1.00 15.90  ? 2730 HIS A NE2   1 
ATOM   9392  N  N     . VAL A 1 2731 ? 169.948 198.263 176.541 1.00 12.60  ? 2731 VAL A N     1 
ATOM   9393  C  CA    . VAL A 1 2731 ? 169.999 198.070 177.989 1.00 11.82  ? 2731 VAL A CA    1 
ATOM   9394  C  C     . VAL A 1 2731 ? 171.433 198.184 178.500 1.00 15.00  ? 2731 VAL A C     1 
ATOM   9395  O  O     . VAL A 1 2731 ? 172.295 197.365 178.150 1.00 15.19  ? 2731 VAL A O     1 
ATOM   9396  C  CB    . VAL A 1 2731 ? 169.344 196.736 178.392 1.00 10.38  ? 2731 VAL A CB    1 
ATOM   9397  C  CG1   . VAL A 1 2731 ? 167.875 196.748 178.021 1.00 13.18  ? 2731 VAL A CG1   1 
ATOM   9398  C  CG2   . VAL A 1 2731 ? 170.015 195.554 177.713 1.00 14.95  ? 2731 VAL A CG2   1 
ATOM   9399  N  N     . PRO A 1 2732 ? 171.745 199.210 179.290 1.00 14.65  ? 2732 PRO A N     1 
ATOM   9400  C  CA    . PRO A 1 2732 ? 173.025 199.224 180.005 1.00 12.89  ? 2732 PRO A CA    1 
ATOM   9401  C  C     . PRO A 1 2732 ? 173.123 198.060 180.978 1.00 15.79  ? 2732 PRO A C     1 
ATOM   9402  O  O     . PRO A 1 2732 ? 172.131 197.628 181.570 1.00 18.48  ? 2732 PRO A O     1 
ATOM   9403  C  CB    . PRO A 1 2732 ? 173.009 200.568 180.744 1.00 10.66  ? 2732 PRO A CB    1 
ATOM   9404  C  CG    . PRO A 1 2732 ? 171.588 201.043 180.685 1.00 12.15  ? 2732 PRO A CG    1 
ATOM   9405  C  CD    . PRO A 1 2732 ? 171.032 200.489 179.420 1.00 12.88  ? 2732 PRO A CD    1 
ATOM   9406  N  N     . VAL A 1 2733 ? 174.341 197.552 181.141 1.00 15.66  ? 2733 VAL A N     1 
ATOM   9407  C  CA    . VAL A 1 2733 ? 174.620 196.431 182.028 1.00 10.60  ? 2733 VAL A CA    1 
ATOM   9408  C  C     . VAL A 1 2733 ? 175.595 196.897 183.098 1.00 14.54  ? 2733 VAL A C     1 
ATOM   9409  O  O     . VAL A 1 2733 ? 176.660 197.439 182.781 1.00 19.12  ? 2733 VAL A O     1 
ATOM   9410  C  CB    . VAL A 1 2733 ? 175.189 195.224 181.260 1.00 10.39  ? 2733 VAL A CB    1 
ATOM   9411  C  CG1   . VAL A 1 2733 ? 175.546 194.103 182.221 1.00 11.91  ? 2733 VAL A CG1   1 
ATOM   9412  C  CG2   . VAL A 1 2733 ? 174.194 194.743 180.218 1.00 14.19  ? 2733 VAL A CG2   1 
ATOM   9413  N  N     . VAL A 1 2734 ? 175.230 196.689 184.360 1.00 14.44  ? 2734 VAL A N     1 
ATOM   9414  C  CA    . VAL A 1 2734 ? 176.090 196.984 185.497 1.00 13.23  ? 2734 VAL A CA    1 
ATOM   9415  C  C     . VAL A 1 2734 ? 176.427 195.673 186.191 1.00 12.92  ? 2734 VAL A C     1 
ATOM   9416  O  O     . VAL A 1 2734 ? 175.561 194.809 186.368 1.00 11.36  ? 2734 VAL A O     1 
ATOM   9417  C  CB    . VAL A 1 2734 ? 175.437 197.990 186.471 1.00 12.94  ? 2734 VAL A CB    1 
ATOM   9418  C  CG1   . VAL A 1 2734 ? 174.157 197.427 187.069 1.00 11.61  ? 2734 VAL A CG1   1 
ATOM   9419  C  CG2   . VAL A 1 2734 ? 176.414 198.380 187.569 1.00 14.93  ? 2734 VAL A CG2   1 
ATOM   9420  N  N     . TYR A 1 2735 ? 177.697 195.511 186.554 1.00 15.01  ? 2735 TYR A N     1 
ATOM   9421  C  CA    . TYR A 1 2735 ? 178.189 194.277 187.153 1.00 14.47  ? 2735 TYR A CA    1 
ATOM   9422  C  C     . TYR A 1 2735 ? 178.206 194.437 188.668 1.00 18.54  ? 2735 TYR A C     1 
ATOM   9423  O  O     . TYR A 1 2735 ? 179.054 195.148 189.216 1.00 21.08  ? 2735 TYR A O     1 
ATOM   9424  C  CB    . TYR A 1 2735 ? 179.577 193.930 186.621 1.00 15.62  ? 2735 TYR A CB    1 
ATOM   9425  C  CG    . TYR A 1 2735 ? 180.107 192.609 187.126 1.00 19.02  ? 2735 TYR A CG    1 
ATOM   9426  C  CD1   . TYR A 1 2735 ? 179.331 191.461 187.066 1.00 17.14  ? 2735 TYR A CD1   1 
ATOM   9427  C  CD2   . TYR A 1 2735 ? 181.384 192.507 187.659 1.00 24.86  ? 2735 TYR A CD2   1 
ATOM   9428  C  CE1   . TYR A 1 2735 ? 179.808 190.251 187.525 1.00 20.35  ? 2735 TYR A CE1   1 
ATOM   9429  C  CE2   . TYR A 1 2735 ? 181.871 191.300 188.119 1.00 27.26  ? 2735 TYR A CE2   1 
ATOM   9430  C  CZ    . TYR A 1 2735 ? 181.079 190.175 188.050 1.00 31.47  ? 2735 TYR A CZ    1 
ATOM   9431  O  OH    . TYR A 1 2735 ? 181.558 188.970 188.507 1.00 40.26  ? 2735 TYR A OH    1 
ATOM   9432  N  N     . VAL A 1 2736 ? 177.268 193.775 189.341 1.00 18.37  ? 2736 VAL A N     1 
ATOM   9433  C  CA    . VAL A 1 2736 ? 177.213 193.759 190.798 1.00 16.09  ? 2736 VAL A CA    1 
ATOM   9434  C  C     . VAL A 1 2736 ? 177.932 192.493 191.252 1.00 19.43  ? 2736 VAL A C     1 
ATOM   9435  O  O     . VAL A 1 2736 ? 177.376 191.395 191.203 1.00 23.66  ? 2736 VAL A O     1 
ATOM   9436  C  CB    . VAL A 1 2736 ? 175.774 193.814 191.313 1.00 13.23  ? 2736 VAL A CB    1 
ATOM   9437  C  CG1   . VAL A 1 2736 ? 175.759 193.868 192.831 1.00 16.49  ? 2736 VAL A CG1   1 
ATOM   9438  C  CG2   . VAL A 1 2736 ? 175.046 195.012 190.725 1.00 13.95  ? 2736 VAL A CG2   1 
ATOM   9439  N  N     . ASP A 1 2737 ? 179.175 192.647 191.692 1.00 17.73  ? 2737 ASP A N     1 
ATOM   9440  C  CA    . ASP A 1 2737 ? 179.992 191.518 192.102 1.00 19.21  ? 2737 ASP A CA    1 
ATOM   9441  C  C     . ASP A 1 2737 ? 179.807 191.232 193.590 1.00 22.35  ? 2737 ASP A C     1 
ATOM   9442  O  O     . ASP A 1 2737 ? 179.178 191.995 194.326 1.00 27.51  ? 2737 ASP A O     1 
ATOM   9443  C  CB    . ASP A 1 2737 ? 181.464 191.784 191.784 1.00 24.82  ? 2737 ASP A CB    1 
ATOM   9444  C  CG    . ASP A 1 2737 ? 182.275 190.509 191.660 1.00 30.78  ? 2737 ASP A CG    1 
ATOM   9445  O  OD1   . ASP A 1 2737 ? 181.706 189.417 191.871 1.00 27.55  ? 2737 ASP A OD1   1 
ATOM   9446  O  OD2   . ASP A 1 2737 ? 183.482 190.597 191.352 1.00 35.96  ? 2737 ASP A OD2   1 
ATOM   9447  N  N     . TYR A 1 2738 ? 180.355 190.101 194.043 1.00 22.20  ? 2738 TYR A N     1 
ATOM   9448  C  CA    . TYR A 1 2738 ? 180.224 189.714 195.475 1.00 19.80  ? 2738 TYR A CA    1 
ATOM   9449  C  C     . TYR A 1 2738 ? 180.987 190.711 196.342 1.00 23.02  ? 2738 TYR A C     1 
ATOM   9450  O  O     . TYR A 1 2738 ? 182.089 191.147 195.946 1.00 24.89  ? 2738 TYR A O     1 
ATOM   9451  C  CB    . TYR A 1 2738 ? 180.761 188.298 195.700 1.00 16.99  ? 2738 TYR A CB    1 
ATOM   9452  C  CG    . TYR A 1 2738 ? 179.788 187.162 195.412 1.00 18.14  ? 2738 TYR A CG    1 
ATOM   9453  C  CD1   . TYR A 1 2738 ? 178.419 187.321 195.586 1.00 18.39  ? 2738 TYR A CD1   1 
ATOM   9454  C  CD2   . TYR A 1 2738 ? 180.248 185.925 194.979 1.00 19.29  ? 2738 TYR A CD2   1 
ATOM   9455  C  CE1   . TYR A 1 2738 ? 177.536 186.285 195.330 1.00 20.11  ? 2738 TYR A CE1   1 
ATOM   9456  C  CE2   . TYR A 1 2738 ? 179.376 184.882 194.720 1.00 18.14  ? 2738 TYR A CE2   1 
ATOM   9457  C  CZ    . TYR A 1 2738 ? 178.016 185.062 194.897 1.00 20.29  ? 2738 TYR A CZ    1 
ATOM   9458  O  OH    . TYR A 1 2738 ? 177.165 184.028 194.638 1.00 22.72  ? 2738 TYR A OH    1 
ATOM   9459  N  N     . PRO A 1 2739 ? 180.459 191.097 197.524 1.00 22.19  ? 2739 PRO A N     1 
ATOM   9460  C  CA    . PRO A 1 2739 ? 181.186 191.982 198.423 1.00 21.55  ? 2739 PRO A CA    1 
ATOM   9461  C  C     . PRO A 1 2739 ? 182.514 191.360 198.833 1.00 25.30  ? 2739 PRO A C     1 
ATOM   9462  O  O     . PRO A 1 2739 ? 182.545 190.152 199.140 1.00 24.06  ? 2739 PRO A O     1 
ATOM   9463  C  CB    . PRO A 1 2739 ? 180.226 192.142 199.611 1.00 18.99  ? 2739 PRO A CB    1 
ATOM   9464  C  CG    . PRO A 1 2739 ? 178.869 191.802 199.039 1.00 16.82  ? 2739 PRO A CG    1 
ATOM   9465  C  CD    . PRO A 1 2739 ? 179.147 190.717 198.015 1.00 18.41  ? 2739 PRO A CD    1 
ATOM   9466  N  N     . GLY A 1 2740 ? 183.585 192.160 198.844 1.00 30.16  ? 2740 GLY A N     1 
ATOM   9467  C  CA    . GLY A 1 2740 ? 184.922 191.654 199.219 1.00 31.23  ? 2740 GLY A CA    1 
ATOM   9468  C  C     . GLY A 1 2740 ? 184.991 191.325 200.698 1.00 33.02  ? 2740 GLY A C     1 
ATOM   9469  O  O     . GLY A 1 2740 ? 184.026 191.647 201.421 1.00 32.43  ? 2740 GLY A O     1 
ATOM   9470  N  N     . PRO A 1 2741 ? 186.084 190.705 201.198 1.00 34.79  ? 2741 PRO A N     1 
ATOM   9471  C  CA    . PRO A 1 2741 ? 186.224 190.430 202.636 1.00 28.59  ? 2741 PRO A CA    1 
ATOM   9472  C  C     . PRO A 1 2741 ? 186.070 191.669 203.498 1.00 30.84  ? 2741 PRO A C     1 
ATOM   9473  O  O     . PRO A 1 2741 ? 185.501 191.582 204.592 1.00 29.92  ? 2741 PRO A O     1 
ATOM   9474  C  CB    . PRO A 1 2741 ? 187.634 189.834 202.742 1.00 29.31  ? 2741 PRO A CB    1 
ATOM   9475  C  CG    . PRO A 1 2741 ? 187.908 189.276 201.385 1.00 29.60  ? 2741 PRO A CG    1 
ATOM   9476  C  CD    . PRO A 1 2741 ? 187.234 190.210 200.423 1.00 31.89  ? 2741 PRO A CD    1 
ATOM   9477  N  N     . ALA A 1 2742 ? 186.546 192.826 203.032 1.00 30.92  ? 2742 ALA A N     1 
ATOM   9478  C  CA    . ALA A 1 2742 ? 186.384 194.057 203.798 1.00 24.55  ? 2742 ALA A CA    1 
ATOM   9479  C  C     . ALA A 1 2742 ? 184.924 194.495 203.840 1.00 25.76  ? 2742 ALA A C     1 
ATOM   9480  O  O     . ALA A 1 2742 ? 184.410 194.876 204.898 1.00 30.50  ? 2742 ALA A O     1 
ATOM   9481  C  CB    . ALA A 1 2742 ? 187.262 195.160 203.208 1.00 27.37  ? 2742 ALA A CB    1 
ATOM   9482  N  N     . SER A 1 2743 ? 184.239 194.453 202.694 1.00 26.48  ? 2743 SER A N     1 
ATOM   9483  C  CA    . SER A 1 2743 ? 182.831 194.838 202.659 1.00 23.36  ? 2743 SER A CA    1 
ATOM   9484  C  C     . SER A 1 2743 ? 181.974 193.879 203.477 1.00 26.70  ? 2743 SER A C     1 
ATOM   9485  O  O     . SER A 1 2743 ? 181.081 194.311 204.218 1.00 29.51  ? 2743 SER A O     1 
ATOM   9486  C  CB    . SER A 1 2743 ? 182.338 194.897 201.214 1.00 24.57  ? 2743 SER A CB    1 
ATOM   9487  O  OG    . SER A 1 2743 ? 183.116 195.798 200.447 1.00 37.11  ? 2743 SER A OG    1 
ATOM   9488  N  N     . LEU A 1 2744 ? 182.227 192.574 203.348 1.00 28.30  ? 2744 LEU A N     1 
ATOM   9489  C  CA    . LEU A 1 2744 ? 181.509 191.596 204.157 1.00 22.93  ? 2744 LEU A CA    1 
ATOM   9490  C  C     . LEU A 1 2744 ? 181.771 191.825 205.638 1.00 24.17  ? 2744 LEU A C     1 
ATOM   9491  O  O     . LEU A 1 2744 ? 180.846 191.772 206.458 1.00 25.27  ? 2744 LEU A O     1 
ATOM   9492  C  CB    . LEU A 1 2744 ? 181.922 190.180 203.758 1.00 18.82  ? 2744 LEU A CB    1 
ATOM   9493  C  CG    . LEU A 1 2744 ? 181.439 189.653 202.407 1.00 23.73  ? 2744 LEU A CG    1 
ATOM   9494  C  CD1   . LEU A 1 2744 ? 182.047 188.290 202.130 1.00 24.41  ? 2744 LEU A CD1   1 
ATOM   9495  C  CD2   . LEU A 1 2744 ? 179.924 189.584 202.363 1.00 25.46  ? 2744 LEU A CD2   1 
ATOM   9496  N  N     . THR A 1 2745 ? 183.031 192.088 205.994 1.00 27.26  ? 2745 THR A N     1 
ATOM   9497  C  CA    . THR A 1 2745 ? 183.372 192.361 207.383 1.00 24.48  ? 2745 THR A CA    1 
ATOM   9498  C  C     . THR A 1 2745 ? 182.606 193.568 207.900 1.00 23.55  ? 2745 THR A C     1 
ATOM   9499  O  O     . THR A 1 2745 ? 182.026 193.523 208.984 1.00 29.27  ? 2745 THR A O     1 
ATOM   9500  C  CB    . THR A 1 2745 ? 184.880 192.580 207.523 1.00 25.24  ? 2745 THR A CB    1 
ATOM   9501  O  OG1   . THR A 1 2745 ? 185.576 191.395 207.117 1.00 29.52  ? 2745 THR A OG1   1 
ATOM   9502  C  CG2   . THR A 1 2745 ? 185.240 192.905 208.964 1.00 25.35  ? 2745 THR A CG2   1 
ATOM   9503  N  N     . GLN A 1 2746 ? 182.515 194.614 207.075 1.00 23.79  ? 2746 GLN A N     1 
ATOM   9504  C  CA    . GLN A 1 2746 ? 181.763 195.836 207.464 1.00 25.24  ? 2746 GLN A CA    1 
ATOM   9505  C  C     . GLN A 1 2746 ? 180.260 195.536 207.582 1.00 27.10  ? 2746 GLN A C     1 
ATOM   9506  O  O     . GLN A 1 2746 ? 179.684 195.836 208.650 1.00 31.41  ? 2746 GLN A O     1 
ATOM   9507  C  CB    . GLN A 1 2746 ? 181.968 196.924 206.411 1.00 27.32  ? 2746 GLN A CB    1 
ATOM   9508  C  CG    . GLN A 1 2746 ? 180.960 198.066 206.498 1.00 35.43  ? 2746 GLN A CG    1 
ATOM   9509  C  CD    . GLN A 1 2746 ? 180.903 198.908 205.242 1.00 48.19  ? 2746 GLN A CD    1 
ATOM   9510  O  OE1   . GLN A 1 2746 ? 181.612 198.656 204.262 1.00 51.27  ? 2746 GLN A OE1   1 
ATOM   9511  N  NE2   . GLN A 1 2746 ? 180.049 199.921 205.259 1.00 45.44  ? 2746 GLN A NE2   1 
ATOM   9512  N  N     . ILE A 1 2747 ? 179.650 194.972 206.535 1.00 25.48  ? 2747 ILE A N     1 
ATOM   9513  C  CA    . ILE A 1 2747 ? 178.171 194.741 206.530 1.00 22.03  ? 2747 ILE A CA    1 
ATOM   9514  C  C     . ILE A 1 2747 ? 177.763 193.840 207.706 1.00 25.44  ? 2747 ILE A C     1 
ATOM   9515  O  O     . ILE A 1 2747 ? 176.938 194.290 208.535 1.00 31.09  ? 2747 ILE A O     1 
ATOM   9516  C  CB    . ILE A 1 2747 ? 177.736 194.124 205.188 1.00 17.28  ? 2747 ILE A CB    1 
ATOM   9517  C  CG1   . ILE A 1 2747 ? 178.140 195.003 204.007 1.00 19.87  ? 2747 ILE A CG1   1 
ATOM   9518  C  CG2   . ILE A 1 2747 ? 176.237 193.823 205.183 1.00 18.50  ? 2747 ILE A CG2   1 
ATOM   9519  C  CD1   . ILE A 1 2747 ? 178.127 194.283 202.671 1.00 14.06  ? 2747 ILE A CD1   1 
ATOM   9520  N  N     . TYR A 1 2748 ? 178.320 192.630 207.785 1.00 22.58  ? 2748 TYR A N     1 
ATOM   9521  C  CA    . TYR A 1 2748 ? 177.887 191.667 208.838 1.00 20.81  ? 2748 TYR A CA    1 
ATOM   9522  C  C     . TYR A 1 2748 ? 178.474 192.082 210.186 1.00 23.13  ? 2748 TYR A C     1 
ATOM   9523  O  O     . TYR A 1 2748 ? 177.915 191.682 211.229 1.00 29.31  ? 2748 TYR A O     1 
ATOM   9524  C  CB    . TYR A 1 2748 ? 178.220 190.255 208.345 1.00 20.63  ? 2748 TYR A CB    1 
ATOM   9525  C  CG    . TYR A 1 2748 ? 177.462 189.937 207.064 1.00 21.98  ? 2748 TYR A CG    1 
ATOM   9526  C  CD1   . TYR A 1 2748 ? 176.169 189.430 207.105 1.00 21.18  ? 2748 TYR A CD1   1 
ATOM   9527  C  CD2   . TYR A 1 2748 ? 178.025 190.176 205.816 1.00 23.47  ? 2748 TYR A CD2   1 
ATOM   9528  C  CE1   . TYR A 1 2748 ? 175.464 189.156 205.945 1.00 18.01  ? 2748 TYR A CE1   1 
ATOM   9529  C  CE2   . TYR A 1 2748 ? 177.331 189.903 204.649 1.00 22.45  ? 2748 TYR A CE2   1 
ATOM   9530  C  CZ    . TYR A 1 2748 ? 176.048 189.391 204.714 1.00 21.01  ? 2748 TYR A CZ    1 
ATOM   9531  O  OH    . TYR A 1 2748 ? 175.359 189.121 203.568 1.00 24.11  ? 2748 TYR A OH    1 
ATOM   9532  N  N     . GLY A 1 2749 ? 179.558 192.862 210.178 1.00 20.82  ? 2749 GLY A N     1 
ATOM   9533  C  CA    . GLY A 1 2749 ? 180.095 193.379 211.450 1.00 21.37  ? 2749 GLY A CA    1 
ATOM   9534  C  C     . GLY A 1 2749 ? 179.065 194.274 212.106 1.00 26.94  ? 2749 GLY A C     1 
ATOM   9535  O  O     . GLY A 1 2749 ? 178.875 194.158 213.335 1.00 35.26  ? 2749 GLY A O     1 
ATOM   9536  N  N     . THR A 1 2750 ? 178.405 195.125 211.314 1.00 26.10  ? 2750 THR A N     1 
ATOM   9537  C  CA    . THR A 1 2750 ? 177.345 196.006 211.848 1.00 26.45  ? 2750 THR A CA    1 
ATOM   9538  C  C     . THR A 1 2750 ? 176.201 195.147 212.336 1.00 25.92  ? 2750 THR A C     1 
ATOM   9539  O  O     . THR A 1 2750 ? 175.668 195.437 213.429 1.00 32.60  ? 2750 THR A O     1 
ATOM   9540  C  CB    . THR A 1 2750 ? 176.890 196.974 210.758 1.00 26.86  ? 2750 THR A CB    1 
ATOM   9541  O  OG1   . THR A 1 2750 ? 178.047 197.737 210.432 1.00 36.75  ? 2750 THR A OG1   1 
ATOM   9542  C  CG2   . THR A 1 2750 ? 175.773 197.890 211.224 1.00 31.92  ? 2750 THR A CG2   1 
ATOM   9543  N  N     . PHE A 1 2751 ? 175.835 194.123 211.561 1.00 23.50  ? 2751 PHE A N     1 
ATOM   9544  C  CA    . PHE A 1 2751 ? 174.702 193.235 211.939 1.00 24.80  ? 2751 PHE A CA    1 
ATOM   9545  C  C     . PHE A 1 2751 ? 175.016 192.570 213.277 1.00 27.16  ? 2751 PHE A C     1 
ATOM   9546  O  O     . PHE A 1 2751 ? 174.114 192.479 214.135 1.00 29.11  ? 2751 PHE A O     1 
ATOM   9547  C  CB    . PHE A 1 2751 ? 174.457 192.201 210.836 1.00 23.81  ? 2751 PHE A CB    1 
ATOM   9548  C  CG    . PHE A 1 2751 ? 173.839 192.759 209.561 1.00 25.34  ? 2751 PHE A CG    1 
ATOM   9549  C  CD1   . PHE A 1 2751 ? 172.960 193.834 209.606 1.00 25.25  ? 2751 PHE A CD1   1 
ATOM   9550  C  CD2   . PHE A 1 2751 ? 174.140 192.206 208.322 1.00 26.15  ? 2751 PHE A CD2   1 
ATOM   9551  C  CE1   . PHE A 1 2751 ? 172.397 194.338 208.444 1.00 27.04  ? 2751 PHE A CE1   1 
ATOM   9552  C  CE2   . PHE A 1 2751 ? 173.575 192.715 207.163 1.00 28.35  ? 2751 PHE A CE2   1 
ATOM   9553  C  CZ    . PHE A 1 2751 ? 172.706 193.779 207.226 1.00 28.69  ? 2751 PHE A CZ    1 
ATOM   9554  N  N     . ASN A 1 2752 ? 176.263 192.127 213.455 1.00 29.48  ? 2752 ASN A N     1 
ATOM   9555  C  CA    . ASN A 1 2752 ? 176.658 191.424 214.708 1.00 24.45  ? 2752 ASN A CA    1 
ATOM   9556  C  C     . ASN A 1 2752 ? 176.603 192.408 215.882 1.00 31.82  ? 2752 ASN A C     1 
ATOM   9557  O  O     . ASN A 1 2752 ? 176.074 192.025 216.946 1.00 42.45  ? 2752 ASN A O     1 
ATOM   9558  C  CB    . ASN A 1 2752 ? 178.021 190.753 214.571 1.00 21.44  ? 2752 ASN A CB    1 
ATOM   9559  C  CG    . ASN A 1 2752 ? 177.988 189.594 213.603 1.00 24.81  ? 2752 ASN A CG    1 
ATOM   9560  O  OD1   . ASN A 1 2752 ? 179.008 188.929 213.395 1.00 29.89  ? 2752 ASN A OD1   1 
ATOM   9561  N  ND2   . ASN A 1 2752 ? 176.832 189.330 213.011 1.00 23.72  ? 2752 ASN A ND2   1 
ATOM   9562  N  N     . ARG A 1 2753 ? 177.125 193.624 215.697 1.00 30.81  ? 2753 ARG A N     1 
ATOM   9563  C  CA    . ARG A 1 2753 ? 177.102 194.615 216.766 1.00 28.98  ? 2753 ARG A CA    1 
ATOM   9564  C  C     . ARG A 1 2753 ? 175.673 194.945 217.169 1.00 33.84  ? 2753 ARG A C     1 
ATOM   9565  O  O     . ARG A 1 2753 ? 175.362 195.062 218.360 1.00 41.02  ? 2753 ARG A O     1 
ATOM   9566  C  CB    . ARG A 1 2753 ? 177.842 195.878 216.325 1.00 30.89  ? 2753 ARG A CB    1 
ATOM   9567  C  CG    . ARG A 1 2753 ? 179.352 195.797 216.451 1.00 36.46  ? 2753 ARG A CG    1 
ATOM   9568  C  CD    . ARG A 1 2753 ? 179.978 197.180 216.405 1.00 41.58  ? 2753 ARG A CD    1 
ATOM   9569  N  NE    . ARG A 1 2753 ? 179.207 198.097 215.573 1.00 37.94  ? 2753 ARG A NE    1 
ATOM   9570  C  CZ    . ARG A 1 2753 ? 179.449 198.332 214.291 1.00 39.30  ? 2753 ARG A CZ    1 
ATOM   9571  N  NH1   . ARG A 1 2753 ? 180.444 197.737 213.654 1.00 33.27  ? 2753 ARG A NH1   1 
ATOM   9572  N  NH2   . ARG A 1 2753 ? 178.673 199.187 213.631 1.00 43.64  ? 2753 ARG A NH2   1 
ATOM   9573  N  N     . ALA A 1 2754 ? 174.785 195.104 216.185 1.00 32.96  ? 2754 ALA A N     1 
ATOM   9574  C  CA    . ALA A 1 2754 ? 173.376 195.308 216.508 1.00 39.47  ? 2754 ALA A CA    1 
ATOM   9575  C  C     . ALA A 1 2754 ? 172.773 194.062 217.147 1.00 43.18  ? 2754 ALA A C     1 
ATOM   9576  O  O     . ALA A 1 2754 ? 171.909 194.160 218.025 1.00 50.71  ? 2754 ALA A O     1 
ATOM   9577  C  CB    . ALA A 1 2754 ? 172.599 195.699 215.253 1.00 46.01  ? 2754 ALA A CB    1 
ATOM   9578  N  N     . MET A 1 2755 ? 173.216 192.881 216.711 1.00 43.21  ? 2755 MET A N     1 
ATOM   9579  C  CA    . MET A 1 2755 ? 172.694 191.626 217.242 1.00 39.56  ? 2755 MET A CA    1 
ATOM   9580  C  C     . MET A 1 2755 ? 173.152 191.390 218.674 1.00 43.31  ? 2755 MET A C     1 
ATOM   9581  O  O     . MET A 1 2755 ? 172.347 191.026 219.538 1.00 50.64  ? 2755 MET A O     1 
ATOM   9582  C  CB    . MET A 1 2755 ? 173.133 190.469 216.346 1.00 30.89  ? 2755 MET A CB    1 
ATOM   9583  C  CG    . MET A 1 2755 ? 172.621 189.102 216.762 1.00 25.36  ? 2755 MET A CG    1 
ATOM   9584  S  SD    . MET A 1 2755 ? 173.189 187.830 215.620 1.00 40.78  ? 2755 MET A SD    1 
ATOM   9585  C  CE    . MET A 1 2755 ? 174.928 187.767 216.053 1.00 28.95  ? 2755 MET A CE    1 
ATOM   9586  N  N     . LEU A 1 2756 ? 174.441 191.594 218.945 1.00 42.55  ? 2756 LEU A N     1 
ATOM   9587  C  CA    . LEU A 1 2756 ? 174.997 191.279 220.253 1.00 39.88  ? 2756 LEU A CA    1 
ATOM   9588  C  C     . LEU A 1 2756 ? 174.641 192.314 221.310 1.00 45.38  ? 2756 LEU A C     1 
ATOM   9589  O  O     . LEU A 1 2756 ? 174.969 192.112 222.483 1.00 55.21  ? 2756 LEU A O     1 
ATOM   9590  C  CB    . LEU A 1 2756 ? 176.514 191.128 220.145 1.00 39.55  ? 2756 LEU A CB    1 
ATOM   9591  C  CG    . LEU A 1 2756 ? 176.955 189.824 219.474 1.00 36.02  ? 2756 LEU A CG    1 
ATOM   9592  C  CD1   . LEU A 1 2756 ? 178.446 189.598 219.630 1.00 42.52  ? 2756 LEU A CD1   1 
ATOM   9593  C  CD2   . LEU A 1 2756 ? 176.174 188.648 220.038 1.00 35.53  ? 2756 LEU A CD2   1 
ATOM   9594  N  N     . ARG A 1 2757 ? 173.989 193.414 220.927 1.00 46.19  ? 2757 ARG A N     1 
ATOM   9595  C  CA    . ARG A 1 2757 ? 173.505 194.374 221.910 1.00 51.63  ? 2757 ARG A CA    1 
ATOM   9596  C  C     . ARG A 1 2757 ? 172.390 193.798 222.772 1.00 54.02  ? 2757 ARG A C     1 
ATOM   9597  O  O     . ARG A 1 2757 ? 172.068 194.374 223.817 1.00 56.74  ? 2757 ARG A O     1 
ATOM   9598  C  CB    . ARG A 1 2757 ? 173.022 195.643 221.205 1.00 54.11  ? 2757 ARG A CB    1 
ATOM   9599  C  CG    . ARG A 1 2757 ? 174.098 196.700 221.028 1.00 55.59  ? 2757 ARG A CG    1 
ATOM   9600  C  CD    . ARG A 1 2757 ? 173.494 198.087 220.899 1.00 60.16  ? 2757 ARG A CD    1 
ATOM   9601  N  NE    . ARG A 1 2757 ? 172.480 198.141 219.853 1.00 63.46  ? 2757 ARG A NE    1 
ATOM   9602  C  CZ    . ARG A 1 2757 ? 172.647 198.733 218.679 1.00 68.23  ? 2757 ARG A CZ    1 
ATOM   9603  N  NH1   . ARG A 1 2757 ? 173.783 199.334 218.363 1.00 63.22  ? 2757 ARG A NH1   1 
ATOM   9604  N  NH2   . ARG A 1 2757 ? 171.650 198.721 217.798 1.00 67.14  ? 2757 ARG A NH2   1 
ATOM   9605  N  N     . LEU A 1 2758 ? 171.788 192.681 222.353 1.00 49.92  ? 2758 LEU A N     1 
ATOM   9606  C  CA    . LEU A 1 2758 ? 170.778 192.025 223.178 1.00 55.01  ? 2758 LEU A CA    1 
ATOM   9607  C  C     . LEU A 1 2758 ? 171.377 191.520 224.484 1.00 56.50  ? 2758 LEU A C     1 
ATOM   9608  O  O     . LEU A 1 2758 ? 170.763 191.649 225.549 1.00 56.66  ? 2758 LEU A O     1 
ATOM   9609  C  CB    . LEU A 1 2758 ? 170.138 190.872 222.404 1.00 50.84  ? 2758 LEU A CB    1 
ATOM   9610  C  CG    . LEU A 1 2758 ? 169.026 191.232 221.419 1.00 56.31  ? 2758 LEU A CG    1 
ATOM   9611  C  CD1   . LEU A 1 2758 ? 168.758 190.077 220.468 1.00 49.18  ? 2758 LEU A CD1   1 
ATOM   9612  C  CD2   . LEU A 1 2758 ? 167.758 191.626 222.159 1.00 51.29  ? 2758 LEU A CD2   1 
ATOM   9613  N  N     . ILE A 1 2759 ? 172.572 190.943 224.421 1.00 55.38  ? 2759 ILE A N     1 
ATOM   9614  C  CA    . ILE A 1 2759 ? 173.270 190.413 225.586 1.00 57.97  ? 2759 ILE A CA    1 
ATOM   9615  C  C     . ILE A 1 2759 ? 174.478 191.312 225.846 1.00 59.99  ? 2759 ILE A C     1 
ATOM   9616  O  O     . ILE A 1 2759 ? 175.462 191.259 225.093 1.00 58.48  ? 2759 ILE A O     1 
ATOM   9617  C  CB    . ILE A 1 2759 ? 173.690 188.953 225.376 1.00 55.39  ? 2759 ILE A CB    1 
ATOM   9618  C  CG1   . ILE A 1 2759 ? 172.463 188.041 225.421 1.00 54.48  ? 2759 ILE A CG1   1 
ATOM   9619  C  CG2   . ILE A 1 2759 ? 174.685 188.523 226.441 1.00 61.33  ? 2759 ILE A CG2   1 
ATOM   9620  C  CD1   . ILE A 1 2759 ? 172.537 186.873 224.466 1.00 48.05  ? 2759 ILE A CD1   1 
ATOM   9621  N  N     . PRO A 1 2760 ? 174.444 192.161 226.877 1.00 60.97  ? 2760 PRO A N     1 
ATOM   9622  C  CA    . PRO A 1 2760 ? 175.568 193.085 227.105 1.00 63.96  ? 2760 PRO A CA    1 
ATOM   9623  C  C     . PRO A 1 2760 ? 176.897 192.392 227.352 1.00 65.93  ? 2760 PRO A C     1 
ATOM   9624  O  O     . PRO A 1 2760 ? 177.944 192.937 226.980 1.00 65.77  ? 2760 PRO A O     1 
ATOM   9625  C  CB    . PRO A 1 2760 ? 175.121 193.894 228.331 1.00 65.40  ? 2760 PRO A CB    1 
ATOM   9626  C  CG    . PRO A 1 2760 ? 173.645 193.712 228.416 1.00 60.60  ? 2760 PRO A CG    1 
ATOM   9627  C  CD    . PRO A 1 2760 ? 173.325 192.386 227.807 1.00 60.73  ? 2760 PRO A CD    1 
ATOM   9628  N  N     . SER A 1 2761 ? 176.893 191.209 227.970 1.00 63.13  ? 2761 SER A N     1 
ATOM   9629  C  CA    . SER A 1 2761 ? 178.147 190.529 228.271 1.00 66.26  ? 2761 SER A CA    1 
ATOM   9630  C  C     . SER A 1 2761 ? 178.831 189.982 227.024 1.00 67.07  ? 2761 SER A C     1 
ATOM   9631  O  O     . SER A 1 2761 ? 180.015 189.635 227.085 1.00 59.91  ? 2761 SER A O     1 
ATOM   9632  C  CB    . SER A 1 2761 ? 177.906 189.396 229.270 1.00 72.83  ? 2761 SER A CB    1 
ATOM   9633  O  OG    . SER A 1 2761 ? 176.955 188.470 228.776 1.00 64.92  ? 2761 SER A OG    1 
ATOM   9634  N  N     . LEU A 1 2762 ? 178.119 189.894 225.902 1.00 67.36  ? 2762 LEU A N     1 
ATOM   9635  C  CA    . LEU A 1 2762 ? 178.679 189.376 224.662 1.00 60.44  ? 2762 LEU A CA    1 
ATOM   9636  C  C     . LEU A 1 2762 ? 179.038 190.468 223.663 1.00 62.06  ? 2762 LEU A C     1 
ATOM   9637  O  O     . LEU A 1 2762 ? 179.470 190.148 222.552 1.00 58.73  ? 2762 LEU A O     1 
ATOM   9638  C  CB    . LEU A 1 2762 ? 177.700 188.392 224.013 1.00 56.02  ? 2762 LEU A CB    1 
ATOM   9639  C  CG    . LEU A 1 2762 ? 177.587 187.009 224.655 1.00 56.88  ? 2762 LEU A CG    1 
ATOM   9640  C  CD1   . LEU A 1 2762 ? 176.498 186.193 223.978 1.00 50.25  ? 2762 LEU A CD1   1 
ATOM   9641  C  CD2   . LEU A 1 2762 ? 178.920 186.281 224.597 1.00 53.17  ? 2762 LEU A CD2   1 
ATOM   9642  N  N     . ARG A 1 2763 ? 178.883 191.743 224.028 1.00 60.85  ? 2763 ARG A N     1 
ATOM   9643  C  CA    . ARG A 1 2763 ? 179.144 192.825 223.083 1.00 55.30  ? 2763 ARG A CA    1 
ATOM   9644  C  C     . ARG A 1 2763 ? 180.605 192.898 222.660 1.00 61.06  ? 2763 ARG A C     1 
ATOM   9645  O  O     . ARG A 1 2763 ? 180.909 193.507 221.629 1.00 69.73  ? 2763 ARG A O     1 
ATOM   9646  C  CB    . ARG A 1 2763 ? 178.716 194.167 223.679 1.00 54.46  ? 2763 ARG A CB    1 
ATOM   9647  C  CG    . ARG A 1 2763 ? 177.251 194.507 223.462 1.00 60.71  ? 2763 ARG A CG    1 
ATOM   9648  C  CD    . ARG A 1 2763 ? 176.714 195.385 224.580 1.00 68.56  ? 2763 ARG A CD    1 
ATOM   9649  N  NE    . ARG A 1 2763 ? 177.261 196.735 224.528 1.00 75.48  ? 2763 ARG A NE    1 
ATOM   9650  C  CZ    . ARG A 1 2763 ? 178.129 197.225 225.402 1.00 75.90  ? 2763 ARG A CZ    1 
ATOM   9651  N  NH1   . ARG A 1 2763 ? 178.572 196.500 226.416 1.00 69.41  ? 2763 ARG A NH1   1 
ATOM   9652  N  NH2   . ARG A 1 2763 ? 178.563 198.474 225.257 1.00 72.99  ? 2763 ARG A NH2   1 
ATOM   9653  N  N     . THR A 1 2764 ? 181.515 192.296 223.425 1.00 57.98  ? 2764 THR A N     1 
ATOM   9654  C  CA    . THR A 1 2764 ? 182.933 192.345 223.094 1.00 56.25  ? 2764 THR A CA    1 
ATOM   9655  C  C     . THR A 1 2764 ? 183.355 191.270 222.102 1.00 52.81  ? 2764 THR A C     1 
ATOM   9656  O  O     . THR A 1 2764 ? 184.512 191.274 221.669 1.00 53.67  ? 2764 THR A O     1 
ATOM   9657  C  CB    . THR A 1 2764 ? 183.776 192.219 224.365 1.00 58.77  ? 2764 THR A CB    1 
ATOM   9658  O  OG1   . THR A 1 2764 ? 185.167 192.265 224.023 1.00 68.43  ? 2764 THR A OG1   1 
ATOM   9659  C  CG2   . THR A 1 2764 ? 183.477 190.907 225.073 1.00 53.53  ? 2764 THR A CG2   1 
ATOM   9660  N  N     . TYR A 1 2765 ? 182.459 190.356 221.734 1.00 46.98  ? 2765 TYR A N     1 
ATOM   9661  C  CA    . TYR A 1 2765 ? 182.785 189.269 220.821 1.00 49.35  ? 2765 TYR A CA    1 
ATOM   9662  C  C     . TYR A 1 2765 ? 182.262 189.501 219.410 1.00 44.59  ? 2765 TYR A C     1 
ATOM   9663  O  O     . TYR A 1 2765 ? 182.283 188.573 218.596 1.00 41.15  ? 2765 TYR A O     1 
ATOM   9664  C  CB    . TYR A 1 2765 ? 182.245 187.943 221.362 1.00 51.75  ? 2765 TYR A CB    1 
ATOM   9665  C  CG    . TYR A 1 2765 ? 182.919 187.483 222.633 1.00 49.92  ? 2765 TYR A CG    1 
ATOM   9666  C  CD1   . TYR A 1 2765 ? 184.174 186.892 222.600 1.00 44.88  ? 2765 TYR A CD1   1 
ATOM   9667  C  CD2   . TYR A 1 2765 ? 182.299 187.634 223.865 1.00 50.96  ? 2765 TYR A CD2   1 
ATOM   9668  C  CE1   . TYR A 1 2765 ? 184.795 186.469 223.758 1.00 48.49  ? 2765 TYR A CE1   1 
ATOM   9669  C  CE2   . TYR A 1 2765 ? 182.912 187.214 225.029 1.00 54.21  ? 2765 TYR A CE2   1 
ATOM   9670  C  CZ    . TYR A 1 2765 ? 184.159 186.632 224.970 1.00 54.18  ? 2765 TYR A CZ    1 
ATOM   9671  O  OH    . TYR A 1 2765 ? 184.774 186.212 226.126 1.00 52.08  ? 2765 TYR A OH    1 
ATOM   9672  N  N     . ALA A 1 2766 ? 181.790 190.711 219.101 1.00 42.12  ? 2766 ALA A N     1 
ATOM   9673  C  CA    . ALA A 1 2766 ? 181.260 190.976 217.767 1.00 40.00  ? 2766 ALA A CA    1 
ATOM   9674  C  C     . ALA A 1 2766 ? 182.345 190.864 216.703 1.00 36.92  ? 2766 ALA A C     1 
ATOM   9675  O  O     . ALA A 1 2766 ? 182.128 190.260 215.647 1.00 33.48  ? 2766 ALA A O     1 
ATOM   9676  C  CB    . ALA A 1 2766 ? 180.608 192.357 217.728 1.00 36.59  ? 2766 ALA A CB    1 
ATOM   9677  N  N     . GLU A 1 2767 ? 183.521 191.448 216.962 1.00 38.63  ? 2767 GLU A N     1 
ATOM   9678  C  CA    . GLU A 1 2767 ? 184.594 191.402 215.969 1.00 39.34  ? 2767 GLU A CA    1 
ATOM   9679  C  C     . GLU A 1 2767 ? 185.092 189.984 215.707 1.00 41.57  ? 2767 GLU A C     1 
ATOM   9680  O  O     . GLU A 1 2767 ? 185.174 189.593 214.528 1.00 40.26  ? 2767 GLU A O     1 
ATOM   9681  C  CB    . GLU A 1 2767 ? 185.730 192.339 216.391 1.00 42.49  ? 2767 GLU A CB    1 
ATOM   9682  C  CG    . GLU A 1 2767 ? 186.872 192.427 215.393 1.00 55.45  ? 2767 GLU A CG    1 
ATOM   9683  C  CD    . GLU A 1 2767 ? 187.947 193.405 215.825 1.00 70.81  ? 2767 GLU A CD    1 
ATOM   9684  O  OE1   . GLU A 1 2767 ? 187.807 194.000 216.914 1.00 73.42  ? 2767 GLU A OE1   1 
ATOM   9685  O  OE2   . GLU A 1 2767 ? 188.932 193.577 215.077 1.00 77.61  ? 2767 GLU A OE2   1 
ATOM   9686  N  N     . PRO A 1 2768 ? 185.457 189.177 216.714 1.00 41.88  ? 2768 PRO A N     1 
ATOM   9687  C  CA    . PRO A 1 2768 ? 185.874 187.799 216.406 1.00 35.59  ? 2768 PRO A CA    1 
ATOM   9688  C  C     . PRO A 1 2768 ? 184.772 186.958 215.792 1.00 34.59  ? 2768 PRO A C     1 
ATOM   9689  O  O     . PRO A 1 2768 ? 185.059 186.121 214.929 1.00 35.30  ? 2768 PRO A O     1 
ATOM   9690  C  CB    . PRO A 1 2768 ? 186.314 187.251 217.770 1.00 33.10  ? 2768 PRO A CB    1 
ATOM   9691  C  CG    . PRO A 1 2768 ? 185.577 188.065 218.756 1.00 39.53  ? 2768 PRO A CG    1 
ATOM   9692  C  CD    . PRO A 1 2768 ? 185.507 189.439 218.165 1.00 40.56  ? 2768 PRO A CD    1 
ATOM   9693  N  N     . LEU A 1 2769 ? 183.517 187.158 216.202 1.00 32.16  ? 2769 LEU A N     1 
ATOM   9694  C  CA    . LEU A 1 2769 ? 182.421 186.405 215.602 1.00 27.05  ? 2769 LEU A CA    1 
ATOM   9695  C  C     . LEU A 1 2769 ? 182.267 186.744 214.126 1.00 27.93  ? 2769 LEU A C     1 
ATOM   9696  O  O     . LEU A 1 2769 ? 182.115 185.847 213.288 1.00 30.41  ? 2769 LEU A O     1 
ATOM   9697  C  CB    . LEU A 1 2769 ? 181.119 186.678 216.354 1.00 25.07  ? 2769 LEU A CB    1 
ATOM   9698  C  CG    . LEU A 1 2769 ? 179.863 185.966 215.849 1.00 26.33  ? 2769 LEU A CG    1 
ATOM   9699  C  CD1   . LEU A 1 2769 ? 179.790 184.554 216.403 1.00 25.82  ? 2769 LEU A CD1   1 
ATOM   9700  C  CD2   . LEU A 1 2769 ? 178.618 186.754 216.221 1.00 27.48  ? 2769 LEU A CD2   1 
ATOM   9701  N  N     . THR A 1 2770 ? 182.312 188.035 213.788 1.00 28.97  ? 2770 THR A N     1 
ATOM   9702  C  CA    . THR A 1 2770 ? 182.223 188.438 212.389 1.00 26.32  ? 2770 THR A CA    1 
ATOM   9703  C  C     . THR A 1 2770 ? 183.402 187.904 211.588 1.00 29.19  ? 2770 THR A C     1 
ATOM   9704  O  O     . THR A 1 2770 ? 183.234 187.448 210.450 1.00 29.79  ? 2770 THR A O     1 
ATOM   9705  C  CB    . THR A 1 2770 ? 182.151 189.961 212.285 1.00 25.53  ? 2770 THR A CB    1 
ATOM   9706  O  OG1   . THR A 1 2770 ? 181.021 190.439 213.025 1.00 28.80  ? 2770 THR A OG1   1 
ATOM   9707  C  CG2   . THR A 1 2770 ? 182.017 190.390 210.833 1.00 24.21  ? 2770 THR A CG2   1 
ATOM   9708  N  N     . ALA A 1 2771 ? 184.605 187.954 212.166 1.00 28.37  ? 2771 ALA A N     1 
ATOM   9709  C  CA    . ALA A 1 2771 ? 185.775 187.426 211.473 1.00 27.43  ? 2771 ALA A CA    1 
ATOM   9710  C  C     . ALA A 1 2771 ? 185.631 185.933 211.209 1.00 28.13  ? 2771 ALA A C     1 
ATOM   9711  O  O     . ALA A 1 2771 ? 185.943 185.457 210.111 1.00 31.60  ? 2771 ALA A O     1 
ATOM   9712  C  CB    . ALA A 1 2771 ? 187.038 187.710 212.285 1.00 28.46  ? 2771 ALA A CB    1 
ATOM   9713  N  N     . ALA A 1 2772 ? 185.153 185.180 212.203 1.00 27.12  ? 2772 ALA A N     1 
ATOM   9714  C  CA    . ALA A 1 2772 ? 184.952 183.747 212.021 1.00 22.56  ? 2772 ALA A CA    1 
ATOM   9715  C  C     . ALA A 1 2772 ? 183.905 183.467 210.952 1.00 23.80  ? 2772 ALA A C     1 
ATOM   9716  O  O     . ALA A 1 2772 ? 184.094 182.585 210.104 1.00 28.29  ? 2772 ALA A O     1 
ATOM   9717  C  CB    . ALA A 1 2772 ? 184.550 183.103 213.348 1.00 21.00  ? 2772 ALA A CB    1 
ATOM   9718  N  N     . MET A 1 2773 ? 182.794 184.207 210.976 1.00 22.90  ? 2773 MET A N     1 
ATOM   9719  C  CA    . MET A 1 2773 ? 181.751 184.015 209.974 1.00 20.88  ? 2773 MET A CA    1 
ATOM   9720  C  C     . MET A 1 2773 ? 182.290 184.271 208.573 1.00 25.42  ? 2773 MET A C     1 
ATOM   9721  O  O     . MET A 1 2773 ? 182.093 183.459 207.660 1.00 30.47  ? 2773 MET A O     1 
ATOM   9722  C  CB    . MET A 1 2773 ? 180.562 184.931 210.272 1.00 17.98  ? 2773 MET A CB    1 
ATOM   9723  C  CG    . MET A 1 2773 ? 179.848 184.614 211.577 1.00 22.69  ? 2773 MET A CG    1 
ATOM   9724  S  SD    . MET A 1 2773 ? 178.223 185.378 211.759 1.00 29.65  ? 2773 MET A SD    1 
ATOM   9725  C  CE    . MET A 1 2773 ? 177.666 185.426 210.061 1.00 20.07  ? 2773 MET A CE    1 
ATOM   9726  N  N     . VAL A 1 2774 ? 183.001 185.387 208.394 1.00 26.66  ? 2774 VAL A N     1 
ATOM   9727  C  CA    . VAL A 1 2774 ? 183.530 185.738 207.078 1.00 24.77  ? 2774 VAL A CA    1 
ATOM   9728  C  C     . VAL A 1 2774 ? 184.543 184.702 206.612 1.00 28.05  ? 2774 VAL A C     1 
ATOM   9729  O  O     . VAL A 1 2774 ? 184.514 184.263 205.454 1.00 29.64  ? 2774 VAL A O     1 
ATOM   9730  C  CB    . VAL A 1 2774 ? 184.138 187.152 207.110 1.00 21.99  ? 2774 VAL A CB    1 
ATOM   9731  C  CG1   . VAL A 1 2774 ? 184.961 187.410 205.858 1.00 21.25  ? 2774 VAL A CG1   1 
ATOM   9732  C  CG2   . VAL A 1 2774 ? 183.043 188.193 207.250 1.00 24.48  ? 2774 VAL A CG2   1 
ATOM   9733  N  N     . GLU A 1 2775 ? 185.449 184.287 207.501 1.00 26.63  ? 2775 GLU A N     1 
ATOM   9734  C  CA    . GLU A 1 2775 ? 186.479 183.330 207.112 1.00 24.98  ? 2775 GLU A CA    1 
ATOM   9735  C  C     . GLU A 1 2775 ? 185.867 181.993 206.719 1.00 24.54  ? 2775 GLU A C     1 
ATOM   9736  O  O     . GLU A 1 2775 ? 186.211 181.425 205.674 1.00 31.36  ? 2775 GLU A O     1 
ATOM   9737  C  CB    . GLU A 1 2775 ? 187.485 183.148 208.248 1.00 32.55  ? 2775 GLU A CB    1 
ATOM   9738  C  CG    . GLU A 1 2775 ? 188.286 181.858 208.154 1.00 40.02  ? 2775 GLU A CG    1 
ATOM   9739  C  CD    . GLU A 1 2775 ? 189.547 181.885 208.994 1.00 52.71  ? 2775 GLU A CD    1 
ATOM   9740  O  OE1   . GLU A 1 2775 ? 189.492 182.376 210.140 1.00 50.82  ? 2775 GLU A OE1   1 
ATOM   9741  O  OE2   . GLU A 1 2775 ? 190.595 181.415 208.505 1.00 63.43  ? 2775 GLU A OE2   1 
ATOM   9742  N  N     . PHE A 1 2776 ? 184.952 181.472 207.542 1.00 22.73  ? 2776 PHE A N     1 
ATOM   9743  C  CA    . PHE A 1 2776 ? 184.346 180.186 207.220 1.00 25.67  ? 2776 PHE A CA    1 
ATOM   9744  C  C     . PHE A 1 2776 ? 183.526 180.268 205.941 1.00 27.14  ? 2776 PHE A C     1 
ATOM   9745  O  O     . PHE A 1 2776 ? 183.544 179.335 205.132 1.00 26.56  ? 2776 PHE A O     1 
ATOM   9746  C  CB    . PHE A 1 2776 ? 183.478 179.685 208.370 1.00 23.09  ? 2776 PHE A CB    1 
ATOM   9747  C  CG    . PHE A 1 2776 ? 182.819 178.370 208.082 1.00 25.00  ? 2776 PHE A CG    1 
ATOM   9748  C  CD1   . PHE A 1 2776 ? 183.579 177.226 207.910 1.00 27.70  ? 2776 PHE A CD1   1 
ATOM   9749  C  CD2   . PHE A 1 2776 ? 181.445 178.280 207.954 1.00 25.89  ? 2776 PHE A CD2   1 
ATOM   9750  C  CE1   . PHE A 1 2776 ? 182.980 176.016 207.631 1.00 28.06  ? 2776 PHE A CE1   1 
ATOM   9751  C  CE2   . PHE A 1 2776 ? 180.841 177.071 207.676 1.00 23.49  ? 2776 PHE A CE2   1 
ATOM   9752  C  CZ    . PHE A 1 2776 ? 181.609 175.939 207.511 1.00 24.32  ? 2776 PHE A CZ    1 
ATOM   9753  N  N     . TYR A 1 2777 ? 182.803 181.373 205.736 1.00 25.34  ? 2777 TYR A N     1 
ATOM   9754  C  CA    . TYR A 1 2777 ? 182.041 181.525 204.503 1.00 21.43  ? 2777 TYR A CA    1 
ATOM   9755  C  C     . TYR A 1 2777 ? 182.963 181.550 203.291 1.00 25.80  ? 2777 TYR A C     1 
ATOM   9756  O  O     . TYR A 1 2777 ? 182.659 180.942 202.259 1.00 31.57  ? 2777 TYR A O     1 
ATOM   9757  C  CB    . TYR A 1 2777 ? 181.191 182.794 204.567 1.00 22.91  ? 2777 TYR A CB    1 
ATOM   9758  C  CG    . TYR A 1 2777 ? 180.799 183.347 203.217 1.00 27.80  ? 2777 TYR A CG    1 
ATOM   9759  C  CD1   . TYR A 1 2777 ? 179.780 182.765 202.477 1.00 25.42  ? 2777 TYR A CD1   1 
ATOM   9760  C  CD2   . TYR A 1 2777 ? 181.442 184.456 202.685 1.00 26.27  ? 2777 TYR A CD2   1 
ATOM   9761  C  CE1   . TYR A 1 2777 ? 179.416 183.267 201.244 1.00 24.75  ? 2777 TYR A CE1   1 
ATOM   9762  C  CE2   . TYR A 1 2777 ? 181.085 184.964 201.452 1.00 25.01  ? 2777 TYR A CE2   1 
ATOM   9763  C  CZ    . TYR A 1 2777 ? 180.071 184.367 200.737 1.00 27.13  ? 2777 TYR A CZ    1 
ATOM   9764  O  OH    . TYR A 1 2777 ? 179.713 184.872 199.508 1.00 28.47  ? 2777 TYR A OH    1 
ATOM   9765  N  N     . THR A 1 2778 ? 184.105 182.235 203.404 1.00 27.83  ? 2778 THR A N     1 
ATOM   9766  C  CA    . THR A 1 2778 ? 185.044 182.297 202.287 1.00 27.45  ? 2778 THR A CA    1 
ATOM   9767  C  C     . THR A 1 2778 ? 185.629 180.926 201.969 1.00 28.13  ? 2778 THR A C     1 
ATOM   9768  O  O     . THR A 1 2778 ? 185.700 180.530 200.797 1.00 31.70  ? 2778 THR A O     1 
ATOM   9769  C  CB    . THR A 1 2778 ? 186.158 183.296 202.596 1.00 29.20  ? 2778 THR A CB    1 
ATOM   9770  O  OG1   . THR A 1 2778 ? 185.592 184.595 202.812 1.00 28.35  ? 2778 THR A OG1   1 
ATOM   9771  C  CG2   . THR A 1 2778 ? 187.145 183.367 201.442 1.00 38.46  ? 2778 THR A CG2   1 
ATOM   9772  N  N     . MET A 1 2779 ? 186.056 180.183 202.995 1.00 27.17  ? 2779 MET A N     1 
ATOM   9773  C  CA    . MET A 1 2779 ? 186.616 178.857 202.736 1.00 30.20  ? 2779 MET A CA    1 
ATOM   9774  C  C     . MET A 1 2779 ? 185.557 177.899 202.204 1.00 30.09  ? 2779 MET A C     1 
ATOM   9775  O  O     . MET A 1 2779 ? 185.857 177.046 201.362 1.00 34.66  ? 2779 MET A O     1 
ATOM   9776  C  CB    . MET A 1 2779 ? 187.283 178.276 203.985 1.00 29.02  ? 2779 MET A CB    1 
ATOM   9777  C  CG    . MET A 1 2779 ? 188.069 179.262 204.820 1.00 35.25  ? 2779 MET A CG    1 
ATOM   9778  S  SD    . MET A 1 2779 ? 188.944 178.464 206.179 1.00 62.20  ? 2779 MET A SD    1 
ATOM   9779  C  CE    . MET A 1 2779 ? 187.696 177.319 206.760 1.00 38.10  ? 2779 MET A CE    1 
ATOM   9780  N  N     . SER A 1 2780 ? 184.316 178.012 202.683 1.00 25.00  ? 2780 SER A N     1 
ATOM   9781  C  CA    . SER A 1 2780 ? 183.250 177.170 202.152 1.00 24.28  ? 2780 SER A CA    1 
ATOM   9782  C  C     . SER A 1 2780 ? 182.957 177.504 200.695 1.00 26.08  ? 2780 SER A C     1 
ATOM   9783  O  O     . SER A 1 2780 ? 182.714 176.604 199.883 1.00 28.45  ? 2780 SER A O     1 
ATOM   9784  C  CB    . SER A 1 2780 ? 181.991 177.317 203.003 1.00 25.70  ? 2780 SER A CB    1 
ATOM   9785  O  OG    . SER A 1 2780 ? 182.238 176.944 204.347 1.00 34.46  ? 2780 SER A OG    1 
ATOM   9786  N  N     . GLN A 1 2781 ? 182.969 178.793 200.348 1.00 28.18  ? 2781 GLN A N     1 
ATOM   9787  C  CA    . GLN A 1 2781 ? 182.743 179.193 198.964 1.00 26.17  ? 2781 GLN A CA    1 
ATOM   9788  C  C     . GLN A 1 2781 ? 183.857 178.693 198.053 1.00 31.86  ? 2781 GLN A C     1 
ATOM   9789  O  O     . GLN A 1 2781 ? 183.595 178.231 196.936 1.00 32.94  ? 2781 GLN A O     1 
ATOM   9790  C  CB    . GLN A 1 2781 ? 182.622 180.714 198.875 1.00 22.07  ? 2781 GLN A CB    1 
ATOM   9791  C  CG    . GLN A 1 2781 ? 182.126 181.219 197.537 1.00 25.34  ? 2781 GLN A CG    1 
ATOM   9792  C  CD    . GLN A 1 2781 ? 181.849 182.706 197.547 1.00 27.95  ? 2781 GLN A CD    1 
ATOM   9793  O  OE1   . GLN A 1 2781 ? 182.072 183.384 198.549 1.00 29.61  ? 2781 GLN A OE1   1 
ATOM   9794  N  NE2   . GLN A 1 2781 ? 181.361 183.223 196.429 1.00 28.80  ? 2781 GLN A NE2   1 
ATOM   9795  N  N     . GLU A 1 2782 ? 185.108 178.783 198.509 1.00 32.77  ? 2782 GLU A N     1 
ATOM   9796  C  CA    . GLU A 1 2782 ? 186.221 178.326 197.681 1.00 35.04  ? 2782 GLU A CA    1 
ATOM   9797  C  C     . GLU A 1 2782 ? 186.239 176.806 197.557 1.00 37.09  ? 2782 GLU A C     1 
ATOM   9798  O  O     . GLU A 1 2782 ? 186.518 176.269 196.478 1.00 36.58  ? 2782 GLU A O     1 
ATOM   9799  C  CB    . GLU A 1 2782 ? 187.546 178.830 198.253 1.00 35.89  ? 2782 GLU A CB    1 
ATOM   9800  C  CG    . GLU A 1 2782 ? 187.759 180.326 198.104 1.00 49.00  ? 2782 GLU A CG    1 
ATOM   9801  C  CD    . GLU A 1 2782 ? 188.882 180.842 198.980 1.00 61.97  ? 2782 GLU A CD    1 
ATOM   9802  O  OE1   . GLU A 1 2782 ? 189.095 182.072 199.013 1.00 59.45  ? 2782 GLU A OE1   1 
ATOM   9803  O  OE2   . GLU A 1 2782 ? 189.554 180.017 199.635 1.00 65.68  ? 2782 GLU A OE2   1 
ATOM   9804  N  N     . ARG A 1 2783 ? 185.947 176.097 198.649 1.00 36.38  ? 2783 ARG A N     1 
ATOM   9805  C  CA    . ARG A 1 2783 ? 186.050 174.642 198.651 1.00 31.46  ? 2783 ARG A CA    1 
ATOM   9806  C  C     . ARG A 1 2783 ? 184.953 174.003 197.807 1.00 38.09  ? 2783 ARG A C     1 
ATOM   9807  O  O     . ARG A 1 2783 ? 185.225 173.124 196.981 1.00 43.32  ? 2783 ARG A O     1 
ATOM   9808  C  CB    . ARG A 1 2783 ? 185.998 174.125 200.089 1.00 27.11  ? 2783 ARG A CB    1 
ATOM   9809  C  CG    . ARG A 1 2783 ? 185.795 172.628 200.219 1.00 34.36  ? 2783 ARG A CG    1 
ATOM   9810  C  CD    . ARG A 1 2783 ? 187.029 171.858 199.784 1.00 39.84  ? 2783 ARG A CD    1 
ATOM   9811  N  NE    . ARG A 1 2783 ? 187.020 170.490 200.288 1.00 48.45  ? 2783 ARG A NE    1 
ATOM   9812  C  CZ    . ARG A 1 2783 ? 186.282 169.508 199.787 1.00 55.65  ? 2783 ARG A CZ    1 
ATOM   9813  N  NH1   . ARG A 1 2783 ? 185.478 169.704 198.755 1.00 47.01  ? 2783 ARG A NH1   1 
ATOM   9814  N  NH2   . ARG A 1 2783 ? 186.352 168.299 200.337 1.00 59.42  ? 2783 ARG A NH2   1 
ATOM   9815  N  N     . PHE A 1 2784 ? 183.707 174.432 197.997 1.00 35.72  ? 2784 PHE A N     1 
ATOM   9816  C  CA    . PHE A 1 2784 ? 182.564 173.868 197.287 1.00 28.75  ? 2784 PHE A CA    1 
ATOM   9817  C  C     . PHE A 1 2784 ? 182.131 174.845 196.201 1.00 32.44  ? 2784 PHE A C     1 
ATOM   9818  O  O     . PHE A 1 2784 ? 181.485 175.857 196.488 1.00 35.92  ? 2784 PHE A O     1 
ATOM   9819  C  CB    . PHE A 1 2784 ? 181.414 173.573 198.247 1.00 29.42  ? 2784 PHE A CB    1 
ATOM   9820  C  CG    . PHE A 1 2784 ? 181.821 172.791 199.461 1.00 29.01  ? 2784 PHE A CG    1 
ATOM   9821  C  CD1   . PHE A 1 2784 ? 182.308 171.502 199.338 1.00 28.93  ? 2784 PHE A CD1   1 
ATOM   9822  C  CD2   . PHE A 1 2784 ? 181.713 173.343 200.725 1.00 28.60  ? 2784 PHE A CD2   1 
ATOM   9823  C  CE1   . PHE A 1 2784 ? 182.682 170.781 200.452 1.00 30.37  ? 2784 PHE A CE1   1 
ATOM   9824  C  CE2   . PHE A 1 2784 ? 182.085 172.625 201.842 1.00 27.59  ? 2784 PHE A CE2   1 
ATOM   9825  C  CZ    . PHE A 1 2784 ? 182.570 171.342 201.705 1.00 31.19  ? 2784 PHE A CZ    1 
ATOM   9826  N  N     . THR A 1 2785 ? 182.484 174.537 194.959 1.00 35.43  ? 2785 THR A N     1 
ATOM   9827  C  CA    . THR A 1 2785 ? 182.111 175.341 193.806 1.00 39.82  ? 2785 THR A CA    1 
ATOM   9828  C  C     . THR A 1 2785 ? 181.002 174.647 193.027 1.00 34.71  ? 2785 THR A C     1 
ATOM   9829  O  O     . THR A 1 2785 ? 180.652 173.493 193.286 1.00 36.42  ? 2785 THR A O     1 
ATOM   9830  C  CB    . THR A 1 2785 ? 183.323 175.591 192.900 1.00 46.39  ? 2785 THR A CB    1 
ATOM   9831  O  OG1   . THR A 1 2785 ? 183.766 174.350 192.339 1.00 51.71  ? 2785 THR A OG1   1 
ATOM   9832  C  CG2   . THR A 1 2785 ? 184.459 176.217 193.693 1.00 42.79  ? 2785 THR A CG2   1 
ATOM   9833  N  N     . GLN A 1 2786 ? 180.446 175.373 192.056 1.00 36.42  ? 2786 GLN A N     1 
ATOM   9834  C  CA    . GLN A 1 2786 ? 179.392 174.815 191.218 1.00 39.68  ? 2786 GLN A CA    1 
ATOM   9835  C  C     . GLN A 1 2786 ? 179.898 173.722 190.287 1.00 45.91  ? 2786 GLN A C     1 
ATOM   9836  O  O     . GLN A 1 2786 ? 179.079 173.026 189.677 1.00 44.52  ? 2786 GLN A O     1 
ATOM   9837  C  CB    . GLN A 1 2786 ? 178.729 175.924 190.401 1.00 40.89  ? 2786 GLN A CB    1 
ATOM   9838  C  CG    . GLN A 1 2786 ? 177.239 175.726 190.189 1.00 40.61  ? 2786 GLN A CG    1 
ATOM   9839  C  CD    . GLN A 1 2786 ? 176.592 176.895 189.477 1.00 54.25  ? 2786 GLN A CD    1 
ATOM   9840  O  OE1   . GLN A 1 2786 ? 177.275 177.799 188.997 1.00 64.60  ? 2786 GLN A OE1   1 
ATOM   9841  N  NE2   . GLN A 1 2786 ? 175.266 176.884 189.405 1.00 50.50  ? 2786 GLN A NE2   1 
ATOM   9842  N  N     . ASP A 1 2787 ? 181.217 173.562 190.156 1.00 50.11  ? 2787 ASP A N     1 
ATOM   9843  C  CA    . ASP A 1 2787 ? 181.756 172.481 189.338 1.00 44.74  ? 2787 ASP A CA    1 
ATOM   9844  C  C     . ASP A 1 2787 ? 181.406 171.120 189.926 1.00 47.47  ? 2787 ASP A C     1 
ATOM   9845  O  O     . ASP A 1 2787 ? 181.098 170.177 189.188 1.00 51.99  ? 2787 ASP A O     1 
ATOM   9846  C  CB    . ASP A 1 2787 ? 183.271 172.633 189.202 1.00 55.45  ? 2787 ASP A CB    1 
ATOM   9847  C  CG    . ASP A 1 2787 ? 183.662 173.834 188.365 1.00 80.30  ? 2787 ASP A CG    1 
ATOM   9848  O  OD1   . ASP A 1 2787 ? 182.882 174.216 187.468 1.00 86.48  ? 2787 ASP A OD1   1 
ATOM   9849  O  OD2   . ASP A 1 2787 ? 184.751 174.398 188.604 1.00 86.00  ? 2787 ASP A OD2   1 
ATOM   9850  N  N     . THR A 1 2788 ? 181.453 170.998 191.254 1.00 49.20  ? 2788 THR A N     1 
ATOM   9851  C  CA    . THR A 1 2788 ? 181.136 169.728 191.899 1.00 44.97  ? 2788 THR A CA    1 
ATOM   9852  C  C     . THR A 1 2788 ? 179.654 169.400 191.760 1.00 39.96  ? 2788 THR A C     1 
ATOM   9853  O  O     . THR A 1 2788 ? 179.282 168.385 191.160 1.00 42.12  ? 2788 THR A O     1 
ATOM   9854  C  CB    . THR A 1 2788 ? 181.543 169.772 193.373 1.00 41.40  ? 2788 THR A CB    1 
ATOM   9855  O  OG1   . THR A 1 2788 ? 182.853 170.339 193.493 1.00 43.32  ? 2788 THR A OG1   1 
ATOM   9856  C  CG2   . THR A 1 2788 ? 181.547 168.372 193.966 1.00 45.00  ? 2788 THR A CG2   1 
ATOM   9857  N  N     . GLN A 1 2789 ? 178.793 170.249 192.310 1.00 34.43  ? 2789 GLN A N     1 
ATOM   9858  C  CA    . GLN A 1 2789 ? 177.354 170.069 192.229 1.00 32.40  ? 2789 GLN A CA    1 
ATOM   9859  C  C     . GLN A 1 2789 ? 176.690 171.376 191.824 1.00 36.29  ? 2789 GLN A C     1 
ATOM   9860  O  O     . GLN A 1 2789 ? 177.189 172.458 192.150 1.00 38.15  ? 2789 GLN A O     1 
ATOM   9861  C  CB    . GLN A 1 2789 ? 176.775 169.591 193.569 1.00 31.59  ? 2789 GLN A CB    1 
ATOM   9862  C  CG    . GLN A 1 2789 ? 177.412 168.318 194.103 1.00 34.79  ? 2789 GLN A CG    1 
ATOM   9863  C  CD    . GLN A 1 2789 ? 176.793 167.066 193.516 1.00 35.79  ? 2789 GLN A CD    1 
ATOM   9864  O  OE1   . GLN A 1 2789 ? 175.689 167.102 192.974 1.00 34.86  ? 2789 GLN A OE1   1 
ATOM   9865  N  NE2   . GLN A 1 2789 ? 177.504 165.950 193.621 1.00 41.43  ? 2789 GLN A NE2   1 
ATOM   9866  N  N     . PRO A 1 2790 ? 175.568 171.306 191.104 1.00 37.22  ? 2790 PRO A N     1 
ATOM   9867  C  CA    . PRO A 1 2790 ? 174.898 172.544 190.671 1.00 37.64  ? 2790 PRO A CA    1 
ATOM   9868  C  C     . PRO A 1 2790 ? 174.425 173.420 191.817 1.00 34.44  ? 2790 PRO A C     1 
ATOM   9869  O  O     . PRO A 1 2790 ? 174.399 174.649 191.672 1.00 38.94  ? 2790 PRO A O     1 
ATOM   9870  C  CB    . PRO A 1 2790 ? 173.721 172.029 189.831 1.00 41.32  ? 2790 PRO A CB    1 
ATOM   9871  C  CG    . PRO A 1 2790 ? 173.513 170.619 190.281 1.00 40.62  ? 2790 PRO A CG    1 
ATOM   9872  C  CD    . PRO A 1 2790 ? 174.876 170.103 190.612 1.00 37.20  ? 2790 PRO A CD    1 
ATOM   9873  N  N     . HIS A 1 2791 ? 174.050 172.834 192.951 1.00 32.10  ? 2791 HIS A N     1 
ATOM   9874  C  CA    . HIS A 1 2791 ? 173.486 173.590 194.061 1.00 29.74  ? 2791 HIS A CA    1 
ATOM   9875  C  C     . HIS A 1 2791 ? 174.540 174.113 195.028 1.00 30.19  ? 2791 HIS A C     1 
ATOM   9876  O  O     . HIS A 1 2791 ? 174.179 174.720 196.041 1.00 34.00  ? 2791 HIS A O     1 
ATOM   9877  C  CB    . HIS A 1 2791 ? 172.471 172.732 194.823 1.00 28.68  ? 2791 HIS A CB    1 
ATOM   9878  C  CG    . HIS A 1 2791 ? 173.057 171.497 195.432 1.00 28.31  ? 2791 HIS A CG    1 
ATOM   9879  N  ND1   . HIS A 1 2791 ? 173.346 170.369 194.696 1.00 32.06  ? 2791 HIS A ND1   1 
ATOM   9880  C  CD2   . HIS A 1 2791 ? 173.405 171.212 196.709 1.00 23.47  ? 2791 HIS A CD2   1 
ATOM   9881  C  CE1   . HIS A 1 2791 ? 173.848 169.443 195.493 1.00 28.87  ? 2791 HIS A CE1   1 
ATOM   9882  N  NE2   . HIS A 1 2791 ? 173.894 169.929 196.720 1.00 25.07  ? 2791 HIS A NE2   1 
ATOM   9883  N  N     . TYR A 1 2792 ? 175.825 173.897 194.747 1.00 28.77  ? 2792 TYR A N     1 
ATOM   9884  C  CA    . TYR A 1 2792 ? 176.901 174.377 195.615 1.00 25.68  ? 2792 TYR A CA    1 
ATOM   9885  C  C     . TYR A 1 2792 ? 177.163 175.856 195.324 1.00 30.70  ? 2792 TYR A C     1 
ATOM   9886  O  O     . TYR A 1 2792 ? 178.212 176.258 194.818 1.00 37.88  ? 2792 TYR A O     1 
ATOM   9887  C  CB    . TYR A 1 2792 ? 178.159 173.541 195.425 1.00 28.08  ? 2792 TYR A CB    1 
ATOM   9888  C  CG    . TYR A 1 2792 ? 178.124 172.195 196.112 1.00 26.93  ? 2792 TYR A CG    1 
ATOM   9889  C  CD1   . TYR A 1 2792 ? 177.026 171.803 196.863 1.00 26.19  ? 2792 TYR A CD1   1 
ATOM   9890  C  CD2   . TYR A 1 2792 ? 179.194 171.318 196.011 1.00 31.83  ? 2792 TYR A CD2   1 
ATOM   9891  C  CE1   . TYR A 1 2792 ? 176.994 170.574 197.491 1.00 27.16  ? 2792 TYR A CE1   1 
ATOM   9892  C  CE2   . TYR A 1 2792 ? 179.171 170.089 196.635 1.00 29.92  ? 2792 TYR A CE2   1 
ATOM   9893  C  CZ    . TYR A 1 2792 ? 178.069 169.721 197.373 1.00 28.67  ? 2792 TYR A CZ    1 
ATOM   9894  O  OH    . TYR A 1 2792 ? 178.043 168.496 197.997 1.00 36.56  ? 2792 TYR A OH    1 
ATOM   9895  N  N     . ILE A 1 2793 ? 176.172 176.675 195.662 1.00 27.72  ? 2793 ILE A N     1 
ATOM   9896  C  CA    . ILE A 1 2793 ? 176.234 178.120 195.472 1.00 25.28  ? 2793 ILE A CA    1 
ATOM   9897  C  C     . ILE A 1 2793 ? 176.196 178.774 196.845 1.00 27.20  ? 2793 ILE A C     1 
ATOM   9898  O  O     . ILE A 1 2793 ? 175.215 178.626 197.585 1.00 30.04  ? 2793 ILE A O     1 
ATOM   9899  C  CB    . ILE A 1 2793 ? 175.086 178.626 194.588 1.00 28.00  ? 2793 ILE A CB    1 
ATOM   9900  C  CG1   . ILE A 1 2793 ? 175.252 178.119 193.155 1.00 29.98  ? 2793 ILE A CG1   1 
ATOM   9901  C  CG2   . ILE A 1 2793 ? 175.022 180.145 194.616 1.00 32.06  ? 2793 ILE A CG2   1 
ATOM   9902  C  CD1   . ILE A 1 2793 ? 173.968 178.118 192.357 1.00 34.44  ? 2793 ILE A CD1   1 
ATOM   9903  N  N     . TYR A 1 2794 ? 177.259 179.498 197.185 1.00 22.55  ? 2794 TYR A N     1 
ATOM   9904  C  CA    . TYR A 1 2794 ? 177.359 180.206 198.453 1.00 22.31  ? 2794 TYR A CA    1 
ATOM   9905  C  C     . TYR A 1 2794 ? 177.476 181.697 198.178 1.00 25.58  ? 2794 TYR A C     1 
ATOM   9906  O  O     . TYR A 1 2794 ? 178.296 182.119 197.356 1.00 27.85  ? 2794 TYR A O     1 
ATOM   9907  C  CB    . TYR A 1 2794 ? 178.552 179.706 199.269 1.00 23.63  ? 2794 TYR A CB    1 
ATOM   9908  C  CG    . TYR A 1 2794 ? 178.420 178.261 199.690 1.00 26.38  ? 2794 TYR A CG    1 
ATOM   9909  C  CD1   . TYR A 1 2794 ? 177.532 177.887 200.689 1.00 26.05  ? 2794 TYR A CD1   1 
ATOM   9910  C  CD2   . TYR A 1 2794 ? 179.177 177.268 199.084 1.00 27.03  ? 2794 TYR A CD2   1 
ATOM   9911  C  CE1   . TYR A 1 2794 ? 177.403 176.568 201.073 1.00 26.77  ? 2794 TYR A CE1   1 
ATOM   9912  C  CE2   . TYR A 1 2794 ? 179.056 175.946 199.463 1.00 25.88  ? 2794 TYR A CE2   1 
ATOM   9913  C  CZ    . TYR A 1 2794 ? 178.168 175.602 200.458 1.00 27.86  ? 2794 TYR A CZ    1 
ATOM   9914  O  OH    . TYR A 1 2794 ? 178.045 174.286 200.839 1.00 31.90  ? 2794 TYR A OH    1 
ATOM   9915  N  N     . SER A 1 2795 ? 176.643 182.492 198.855 1.00 23.32  ? 2795 SER A N     1 
ATOM   9916  C  CA    . SER A 1 2795 ? 176.621 183.956 198.600 1.00 18.72  ? 2795 SER A CA    1 
ATOM   9917  C  C     . SER A 1 2795 ? 176.461 184.717 199.922 1.00 21.26  ? 2795 SER A C     1 
ATOM   9918  O  O     . SER A 1 2795 ? 176.276 184.056 200.966 1.00 28.12  ? 2795 SER A O     1 
ATOM   9919  C  CB    . SER A 1 2795 ? 175.513 184.297 197.644 1.00 20.13  ? 2795 SER A CB    1 
ATOM   9920  O  OG    . SER A 1 2795 ? 174.252 183.918 198.176 1.00 20.87  ? 2795 SER A OG    1 
ATOM   9921  N  N     . PRO A 1 2796 ? 176.518 186.068 199.933 1.00 19.30  ? 2796 PRO A N     1 
ATOM   9922  C  CA    . PRO A 1 2796 ? 176.287 186.824 201.156 1.00 17.58  ? 2796 PRO A CA    1 
ATOM   9923  C  C     . PRO A 1 2796 ? 174.928 186.479 201.745 1.00 20.12  ? 2796 PRO A C     1 
ATOM   9924  O  O     . PRO A 1 2796 ? 174.703 186.738 202.942 1.00 25.45  ? 2796 PRO A O     1 
ATOM   9925  C  CB    . PRO A 1 2796 ? 176.364 188.281 200.684 1.00 16.17  ? 2796 PRO A CB    1 
ATOM   9926  C  CG    . PRO A 1 2796 ? 177.233 188.219 199.451 1.00 17.78  ? 2796 PRO A CG    1 
ATOM   9927  C  CD    . PRO A 1 2796 ? 176.854 186.905 198.793 1.00 17.93  ? 2796 PRO A CD    1 
ATOM   9928  N  N     . ARG A 1 2797 ? 174.037 185.915 200.925 1.00 19.40  ? 2797 ARG A N     1 
ATOM   9929  C  CA    . ARG A 1 2797 ? 172.692 185.508 201.411 1.00 18.85  ? 2797 ARG A CA    1 
ATOM   9930  C  C     . ARG A 1 2797 ? 172.855 184.479 202.540 1.00 21.90  ? 2797 ARG A C     1 
ATOM   9931  O  O     . ARG A 1 2797 ? 172.082 184.547 203.519 1.00 25.56  ? 2797 ARG A O     1 
ATOM   9932  C  CB    . ARG A 1 2797 ? 171.860 184.956 200.249 1.00 20.50  ? 2797 ARG A CB    1 
ATOM   9933  C  CG    . ARG A 1 2797 ? 171.521 186.018 199.213 1.00 26.73  ? 2797 ARG A CG    1 
ATOM   9934  C  CD    . ARG A 1 2797 ? 170.726 185.468 198.042 1.00 24.13  ? 2797 ARG A CD    1 
ATOM   9935  N  NE    . ARG A 1 2797 ? 171.484 184.472 197.277 1.00 30.83  ? 2797 ARG A NE    1 
ATOM   9936  C  CZ    . ARG A 1 2797 ? 171.042 183.873 196.180 1.00 43.44  ? 2797 ARG A CZ    1 
ATOM   9937  N  NH1   . ARG A 1 2797 ? 169.867 184.204 195.675 1.00 45.82  ? 2797 ARG A NH1   1 
ATOM   9938  N  NH2   . ARG A 1 2797 ? 171.778 182.949 195.589 1.00 45.74  ? 2797 ARG A NH2   1 
ATOM   9939  N  N     . GLU A 1 2798 ? 173.825 183.569 202.407 1.00 21.11  ? 2798 GLU A N     1 
ATOM   9940  C  CA    . GLU A 1 2798 ? 174.084 182.564 203.470 1.00 18.05  ? 2798 GLU A CA    1 
ATOM   9941  C  C     . GLU A 1 2798 ? 174.460 183.301 204.762 1.00 18.45  ? 2798 GLU A C     1 
ATOM   9942  O  O     . GLU A 1 2798 ? 173.919 182.942 205.829 1.00 26.49  ? 2798 GLU A O     1 
ATOM   9943  C  CB    . GLU A 1 2798 ? 175.214 181.621 203.058 1.00 17.05  ? 2798 GLU A CB    1 
ATOM   9944  C  CG    . GLU A 1 2798 ? 175.158 181.204 201.591 1.00 26.63  ? 2798 GLU A CG    1 
ATOM   9945  C  CD    . GLU A 1 2798 ? 173.978 180.334 201.200 1.00 38.66  ? 2798 GLU A CD    1 
ATOM   9946  O  OE1   . GLU A 1 2798 ? 173.156 180.003 202.080 1.00 46.27  ? 2798 GLU A OE1   1 
ATOM   9947  O  OE2   . GLU A 1 2798 ? 173.883 179.986 200.004 1.00 32.87  ? 2798 GLU A OE2   1 
ATOM   9948  N  N     . MET A 1 2799 ? 175.341 184.300 204.660 1.00 16.72  ? 2799 MET A N     1 
ATOM   9949  C  CA    . MET A 1 2799 ? 175.780 185.070 205.853 1.00 16.94  ? 2799 MET A CA    1 
ATOM   9950  C  C     . MET A 1 2799 ? 174.577 185.822 206.447 1.00 16.38  ? 2799 MET A C     1 
ATOM   9951  O  O     . MET A 1 2799 ? 174.478 185.890 207.689 1.00 21.12  ? 2799 MET A O     1 
ATOM   9952  C  CB    . MET A 1 2799 ? 176.887 186.063 205.485 1.00 15.43  ? 2799 MET A CB    1 
ATOM   9953  C  CG    . MET A 1 2799 ? 178.094 185.419 204.834 1.00 24.25  ? 2799 MET A CG    1 
ATOM   9954  S  SD    . MET A 1 2799 ? 179.481 186.561 204.685 1.00 43.25  ? 2799 MET A SD    1 
ATOM   9955  C  CE    . MET A 1 2799 ? 179.762 186.949 206.418 1.00 26.41  ? 2799 MET A CE    1 
ATOM   9956  N  N     . THR A 1 2800 ? 173.704 186.362 205.592 1.00 15.22  ? 2800 THR A N     1 
ATOM   9957  C  CA    . THR A 1 2800 ? 172.502 187.070 206.081 1.00 14.87  ? 2800 THR A CA    1 
ATOM   9958  C  C     . THR A 1 2800 ? 171.659 186.095 206.872 1.00 19.77  ? 2800 THR A C     1 
ATOM   9959  O  O     . THR A 1 2800 ? 171.238 186.454 207.993 1.00 24.49  ? 2800 THR A O     1 
ATOM   9960  C  CB    . THR A 1 2800 ? 171.732 187.658 204.901 1.00 16.29  ? 2800 THR A CB    1 
ATOM   9961  O  OG1   . THR A 1 2800 ? 172.655 188.525 204.250 1.00 21.13  ? 2800 THR A OG1   1 
ATOM   9962  C  CG2   . THR A 1 2800 ? 170.504 188.435 205.338 1.00 19.24  ? 2800 THR A CG2   1 
ATOM   9963  N  N     . ARG A 1 2801 ? 171.427 184.899 206.323 1.00 20.87  ? 2801 ARG A N     1 
ATOM   9964  C  CA    . ARG A 1 2801 ? 170.669 183.854 207.057 1.00 16.60  ? 2801 ARG A CA    1 
ATOM   9965  C  C     . ARG A 1 2801 ? 171.394 183.564 208.376 1.00 19.19  ? 2801 ARG A C     1 
ATOM   9966  O  O     . ARG A 1 2801 ? 170.723 183.541 209.430 1.00 25.77  ? 2801 ARG A O     1 
ATOM   9967  C  CB    . ARG A 1 2801 ? 170.572 182.576 206.219 1.00 17.28  ? 2801 ARG A CB    1 
ATOM   9968  C  CG    . ARG A 1 2801 ? 169.585 182.637 205.063 1.00 31.34  ? 2801 ARG A CG    1 
ATOM   9969  C  CD    . ARG A 1 2801 ? 169.632 181.358 204.243 1.00 47.88  ? 2801 ARG A CD    1 
ATOM   9970  N  NE    . ARG A 1 2801 ? 168.343 181.036 203.620 1.00 68.12  ? 2801 ARG A NE    1 
ATOM   9971  C  CZ    . ARG A 1 2801 ? 167.228 180.764 204.287 1.00 60.85  ? 2801 ARG A CZ    1 
ATOM   9972  N  NH1   . ARG A 1 2801 ? 167.263 180.584 205.595 1.00 48.30  ? 2801 ARG A NH1   1 
ATOM   9973  N  NH2   . ARG A 1 2801 ? 166.080 180.665 203.641 1.00 52.37  ? 2801 ARG A NH2   1 
ATOM   9974  N  N     . TRP A 1 2802 ? 172.710 183.355 208.313 1.00 16.01  ? 2802 TRP A N     1 
ATOM   9975  C  CA    . TRP A 1 2802 ? 173.493 183.096 209.517 1.00 13.69  ? 2802 TRP A CA    1 
ATOM   9976  C  C     . TRP A 1 2802 ? 173.188 184.120 210.601 1.00 18.60  ? 2802 TRP A C     1 
ATOM   9977  O  O     . TRP A 1 2802 ? 172.874 183.765 211.746 1.00 26.45  ? 2802 TRP A O     1 
ATOM   9978  C  CB    . TRP A 1 2802 ? 174.978 183.124 209.158 1.00 12.32  ? 2802 TRP A CB    1 
ATOM   9979  C  CG    . TRP A 1 2802 ? 175.861 182.313 210.031 1.00 14.33  ? 2802 TRP A CG    1 
ATOM   9980  C  CD1   . TRP A 1 2802 ? 175.600 181.888 211.297 1.00 14.95  ? 2802 TRP A CD1   1 
ATOM   9981  C  CD2   . TRP A 1 2802 ? 177.170 181.837 209.708 1.00 15.33  ? 2802 TRP A CD2   1 
ATOM   9982  N  NE1   . TRP A 1 2802 ? 176.664 181.167 211.782 1.00 13.89  ? 2802 TRP A NE1   1 
ATOM   9983  C  CE2   . TRP A 1 2802 ? 177.642 181.123 210.823 1.00 13.71  ? 2802 TRP A CE2   1 
ATOM   9984  C  CE3   . TRP A 1 2802 ? 177.988 181.944 208.579 1.00 17.84  ? 2802 TRP A CE3   1 
ATOM   9985  C  CZ2   . TRP A 1 2802 ? 178.893 180.519 210.844 1.00 14.11  ? 2802 TRP A CZ2   1 
ATOM   9986  C  CZ3   . TRP A 1 2802 ? 179.230 181.343 208.603 1.00 17.82  ? 2802 TRP A CZ3   1 
ATOM   9987  C  CH2   . TRP A 1 2802 ? 179.671 180.639 209.728 1.00 14.57  ? 2802 TRP A CH2   1 
ATOM   9988  N  N     . VAL A 1 2803 ? 173.278 185.403 210.249 1.00 18.37  ? 2803 VAL A N     1 
ATOM   9989  C  CA    . VAL A 1 2803 ? 173.032 186.464 211.222 1.00 18.72  ? 2803 VAL A CA    1 
ATOM   9990  C  C     . VAL A 1 2803 ? 171.595 186.403 211.724 1.00 20.65  ? 2803 VAL A C     1 
ATOM   9991  O  O     . VAL A 1 2803 ? 171.336 186.556 212.924 1.00 23.10  ? 2803 VAL A O     1 
ATOM   9992  C  CB    . VAL A 1 2803 ? 173.366 187.838 210.613 1.00 18.85  ? 2803 VAL A CB    1 
ATOM   9993  C  CG1   . VAL A 1 2803 ? 173.088 188.940 211.614 1.00 17.10  ? 2803 VAL A CG1   1 
ATOM   9994  C  CG2   . VAL A 1 2803 ? 174.818 187.880 210.171 1.00 19.17  ? 2803 VAL A CG2   1 
ATOM   9995  N  N     . ARG A 1 2804 ? 170.641 186.174 210.818 1.00 20.10  ? 2804 ARG A N     1 
ATOM   9996  C  CA    . ARG A 1 2804 ? 169.237 186.104 211.213 1.00 22.62  ? 2804 ARG A CA    1 
ATOM   9997  C  C     . ARG A 1 2804 ? 168.984 184.942 212.166 1.00 28.43  ? 2804 ARG A C     1 
ATOM   9998  O  O     . ARG A 1 2804 ? 168.256 185.089 213.154 1.00 34.54  ? 2804 ARG A O     1 
ATOM   9999  C  CB    . ARG A 1 2804 ? 168.353 185.982 209.973 1.00 25.87  ? 2804 ARG A CB    1 
ATOM   10000 C  CG    . ARG A 1 2804 ? 166.914 186.415 210.187 1.00 34.26  ? 2804 ARG A CG    1 
ATOM   10001 C  CD    . ARG A 1 2804 ? 166.832 187.885 210.561 1.00 46.18  ? 2804 ARG A CD    1 
ATOM   10002 N  NE    . ARG A 1 2804 ? 165.462 188.307 210.824 1.00 58.14  ? 2804 ARG A NE    1 
ATOM   10003 C  CZ    . ARG A 1 2804 ? 165.127 189.302 211.635 1.00 60.19  ? 2804 ARG A CZ    1 
ATOM   10004 N  NH1   . ARG A 1 2804 ? 166.043 190.005 212.281 1.00 51.73  ? 2804 ARG A NH1   1 
ATOM   10005 N  NH2   . ARG A 1 2804 ? 163.842 189.601 211.799 1.00 62.73  ? 2804 ARG A NH2   1 
ATOM   10006 N  N     . GLY A 1 2805 ? 169.573 183.779 211.888 1.00 23.36  ? 2805 GLY A N     1 
ATOM   10007 C  CA    . GLY A 1 2805 ? 169.383 182.636 212.764 1.00 20.18  ? 2805 GLY A CA    1 
ATOM   10008 C  C     . GLY A 1 2805 ? 170.000 182.839 214.133 1.00 24.44  ? 2805 GLY A C     1 
ATOM   10009 O  O     . GLY A 1 2805 ? 169.395 182.494 215.153 1.00 32.89  ? 2805 GLY A O     1 
ATOM   10010 N  N     . ILE A 1 2806 ? 171.209 183.405 214.180 1.00 20.55  ? 2806 ILE A N     1 
ATOM   10011 C  CA    . ILE A 1 2806 ? 171.833 183.667 215.475 1.00 17.51  ? 2806 ILE A CA    1 
ATOM   10012 C  C     . ILE A 1 2806 ? 171.026 184.699 216.254 1.00 23.08  ? 2806 ILE A C     1 
ATOM   10013 O  O     . ILE A 1 2806 ? 170.862 184.587 217.474 1.00 27.98  ? 2806 ILE A O     1 
ATOM   10014 C  CB    . ILE A 1 2806 ? 173.298 184.105 215.297 1.00 18.04  ? 2806 ILE A CB    1 
ATOM   10015 C  CG1   . ILE A 1 2806 ? 174.088 183.040 214.537 1.00 18.84  ? 2806 ILE A CG1   1 
ATOM   10016 C  CG2   . ILE A 1 2806 ? 173.944 184.345 216.650 1.00 19.95  ? 2806 ILE A CG2   1 
ATOM   10017 C  CD1   . ILE A 1 2806 ? 175.572 183.324 214.461 1.00 17.59  ? 2806 ILE A CD1   1 
ATOM   10018 N  N     . PHE A 1 2807 ? 170.504 185.717 215.563 1.00 25.13  ? 2807 PHE A N     1 
ATOM   10019 C  CA    . PHE A 1 2807 ? 169.670 186.716 216.224 1.00 24.11  ? 2807 PHE A CA    1 
ATOM   10020 C  C     . PHE A 1 2807 ? 168.390 186.097 216.772 1.00 29.41  ? 2807 PHE A C     1 
ATOM   10021 O  O     . PHE A 1 2807 ? 167.973 186.407 217.894 1.00 39.80  ? 2807 PHE A O     1 
ATOM   10022 C  CB    . PHE A 1 2807 ? 169.348 187.849 215.249 1.00 28.01  ? 2807 PHE A CB    1 
ATOM   10023 C  CG    . PHE A 1 2807 ? 168.215 188.731 215.693 1.00 35.01  ? 2807 PHE A CG    1 
ATOM   10024 C  CD1   . PHE A 1 2807 ? 168.397 189.663 216.700 1.00 36.08  ? 2807 PHE A CD1   1 
ATOM   10025 C  CD2   . PHE A 1 2807 ? 166.968 188.630 215.099 1.00 38.32  ? 2807 PHE A CD2   1 
ATOM   10026 C  CE1   . PHE A 1 2807 ? 167.358 190.476 217.108 1.00 40.76  ? 2807 PHE A CE1   1 
ATOM   10027 C  CE2   . PHE A 1 2807 ? 165.924 189.440 215.503 1.00 41.09  ? 2807 PHE A CE2   1 
ATOM   10028 C  CZ    . PHE A 1 2807 ? 166.120 190.364 216.508 1.00 42.00  ? 2807 PHE A CZ    1 
ATOM   10029 N  N     . GLU A 1 2808 ? 167.751 185.218 215.994 1.00 28.91  ? 2808 GLU A N     1 
ATOM   10030 C  CA    . GLU A 1 2808 ? 166.520 184.583 216.451 1.00 31.37  ? 2808 GLU A CA    1 
ATOM   10031 C  C     . GLU A 1 2808 ? 166.775 183.644 217.621 1.00 36.35  ? 2808 GLU A C     1 
ATOM   10032 O  O     . GLU A 1 2808 ? 165.923 183.514 218.507 1.00 45.83  ? 2808 GLU A O     1 
ATOM   10033 C  CB    . GLU A 1 2808 ? 165.857 183.829 215.299 1.00 32.52  ? 2808 GLU A CB    1 
ATOM   10034 C  CG    . GLU A 1 2808 ? 164.871 184.666 214.501 1.00 40.31  ? 2808 GLU A CG    1 
ATOM   10035 C  CD    . GLU A 1 2808 ? 164.843 184.291 213.034 1.00 51.98  ? 2808 GLU A CD    1 
ATOM   10036 O  OE1   . GLU A 1 2808 ? 165.106 183.113 212.714 1.00 49.33  ? 2808 GLU A OE1   1 
ATOM   10037 O  OE2   . GLU A 1 2808 ? 164.559 185.176 212.200 1.00 51.79  ? 2808 GLU A OE2   1 
ATOM   10038 N  N     . ALA A 1 2809 ? 167.929 182.976 217.638 1.00 33.43  ? 2809 ALA A N     1 
ATOM   10039 C  CA    . ALA A 1 2809 ? 168.271 182.131 218.777 1.00 31.13  ? 2809 ALA A CA    1 
ATOM   10040 C  C     . ALA A 1 2809 ? 168.586 182.966 220.013 1.00 35.30  ? 2809 ALA A C     1 
ATOM   10041 O  O     . ALA A 1 2809 ? 168.232 182.583 221.134 1.00 44.49  ? 2809 ALA A O     1 
ATOM   10042 C  CB    . ALA A 1 2809 ? 169.449 181.226 218.423 1.00 24.19  ? 2809 ALA A CB    1 
ATOM   10043 N  N     . LEU A 1 2810 ? 169.249 184.111 219.830 1.00 34.42  ? 2810 LEU A N     1 
ATOM   10044 C  CA    . LEU A 1 2810 ? 169.666 184.941 220.953 1.00 30.94  ? 2810 LEU A CA    1 
ATOM   10045 C  C     . LEU A 1 2810 ? 168.561 185.851 221.472 1.00 40.80  ? 2810 LEU A C     1 
ATOM   10046 O  O     . LEU A 1 2810 ? 168.702 186.405 222.567 1.00 50.59  ? 2810 LEU A O     1 
ATOM   10047 C  CB    . LEU A 1 2810 ? 170.866 185.804 220.555 1.00 29.45  ? 2810 LEU A CB    1 
ATOM   10048 C  CG    . LEU A 1 2810 ? 172.261 185.343 220.975 1.00 31.51  ? 2810 LEU A CG    1 
ATOM   10049 C  CD1   . LEU A 1 2810 ? 172.660 184.092 220.220 1.00 31.51  ? 2810 LEU A CD1   1 
ATOM   10050 C  CD2   . LEU A 1 2810 ? 173.275 186.451 220.752 1.00 35.73  ? 2810 LEU A CD2   1 
ATOM   10051 N  N     . ARG A 1 2811 ? 167.478 186.026 220.715 1.00 39.60  ? 2811 ARG A N     1 
ATOM   10052 C  CA    . ARG A 1 2811 ? 166.456 187.000 221.097 1.00 42.63  ? 2811 ARG A CA    1 
ATOM   10053 C  C     . ARG A 1 2811 ? 165.792 186.697 222.436 1.00 51.27  ? 2811 ARG A C     1 
ATOM   10054 O  O     . ARG A 1 2811 ? 165.728 187.605 223.282 1.00 53.73  ? 2811 ARG A O     1 
ATOM   10055 C  CB    . ARG A 1 2811 ? 165.420 187.122 219.974 1.00 43.04  ? 2811 ARG A CB    1 
ATOM   10056 C  CG    . ARG A 1 2811 ? 164.304 188.108 220.273 1.00 55.73  ? 2811 ARG A CG    1 
ATOM   10057 C  CD    . ARG A 1 2811 ? 164.098 189.079 219.122 1.00 59.17  ? 2811 ARG A CD    1 
ATOM   10058 N  NE    . ARG A 1 2811 ? 163.555 188.424 217.937 1.00 67.90  ? 2811 ARG A NE    1 
ATOM   10059 C  CZ    . ARG A 1 2811 ? 162.293 188.039 217.804 1.00 73.66  ? 2811 ARG A CZ    1 
ATOM   10060 N  NH1   . ARG A 1 2811 ? 161.406 188.230 218.766 1.00 78.75  ? 2811 ARG A NH1   1 
ATOM   10061 N  NH2   . ARG A 1 2811 ? 161.911 187.448 216.675 1.00 66.37  ? 2811 ARG A NH2   1 
ATOM   10062 N  N     . PRO A 1 2812 ? 165.287 185.485 222.709 1.00 54.84  ? 2812 PRO A N     1 
ATOM   10063 C  CA    . PRO A 1 2812 ? 164.586 185.273 223.984 1.00 56.34  ? 2812 PRO A CA    1 
ATOM   10064 C  C     . PRO A 1 2812 ? 165.503 185.090 225.181 1.00 53.30  ? 2812 PRO A C     1 
ATOM   10065 O  O     . PRO A 1 2812 ? 165.031 185.221 226.318 1.00 58.46  ? 2812 PRO A O     1 
ATOM   10066 C  CB    . PRO A 1 2812 ? 163.766 184.002 223.726 1.00 58.43  ? 2812 PRO A CB    1 
ATOM   10067 C  CG    . PRO A 1 2812 ? 164.576 183.249 222.745 1.00 52.48  ? 2812 PRO A CG    1 
ATOM   10068 C  CD    . PRO A 1 2812 ? 165.253 184.271 221.869 1.00 51.43  ? 2812 PRO A CD    1 
ATOM   10069 N  N     . LEU A 1 2813 ? 166.783 184.797 224.971 1.00 50.50  ? 2813 LEU A N     1 
ATOM   10070 C  CA    . LEU A 1 2813 ? 167.683 184.532 226.086 1.00 58.37  ? 2813 LEU A CA    1 
ATOM   10071 C  C     . LEU A 1 2813 ? 168.024 185.824 226.820 1.00 69.13  ? 2813 LEU A C     1 
ATOM   10072 O  O     . LEU A 1 2813 ? 168.409 186.820 226.201 1.00 68.42  ? 2813 LEU A O     1 
ATOM   10073 C  CB    . LEU A 1 2813 ? 168.958 183.857 225.586 1.00 54.55  ? 2813 LEU A CB    1 
ATOM   10074 C  CG    . LEU A 1 2813 ? 168.775 182.677 224.631 1.00 50.64  ? 2813 LEU A CG    1 
ATOM   10075 C  CD1   . LEU A 1 2813 ? 170.121 182.081 224.255 1.00 49.30  ? 2813 LEU A CD1   1 
ATOM   10076 C  CD2   . LEU A 1 2813 ? 167.872 181.620 225.247 1.00 59.35  ? 2813 LEU A CD2   1 
ATOM   10077 N  N     . GLU A 1 2814 ? 167.880 185.804 228.147 1.00 70.84  ? 2814 GLU A N     1 
ATOM   10078 C  CA    . GLU A 1 2814 ? 168.254 186.960 228.954 1.00 76.07  ? 2814 GLU A CA    1 
ATOM   10079 C  C     . GLU A 1 2814 ? 169.768 187.088 229.074 1.00 75.99  ? 2814 GLU A C     1 
ATOM   10080 O  O     . GLU A 1 2814 ? 170.312 188.193 228.965 1.00 72.69  ? 2814 GLU A O     1 
ATOM   10081 C  CB    . GLU A 1 2814 ? 167.617 186.861 230.341 1.00 76.31  ? 2814 GLU A CB    1 
ATOM   10082 C  CG    . GLU A 1 2814 ? 166.191 186.308 230.366 1.00 72.73  ? 2814 GLU A CG    1 
ATOM   10083 C  CD    . GLU A 1 2814 ? 165.157 187.221 229.717 1.00 80.78  ? 2814 GLU A CD    1 
ATOM   10084 O  OE1   . GLU A 1 2814 ? 163.952 186.917 229.840 1.00 85.20  ? 2814 GLU A OE1   1 
ATOM   10085 O  OE2   . GLU A 1 2814 ? 165.528 188.246 229.108 1.00 79.65  ? 2814 GLU A OE2   1 
ATOM   10086 N  N     . THR A 1 2815 ? 170.458 185.973 229.296 1.00 71.57  ? 2815 THR A N     1 
ATOM   10087 C  CA    . THR A 1 2815 ? 171.911 185.963 229.366 1.00 70.44  ? 2815 THR A CA    1 
ATOM   10088 C  C     . THR A 1 2815 ? 172.419 184.716 228.661 1.00 67.61  ? 2815 THR A C     1 
ATOM   10089 O  O     . THR A 1 2815 ? 171.703 183.720 228.525 1.00 71.26  ? 2815 THR A O     1 
ATOM   10090 C  CB    . THR A 1 2815 ? 172.414 186.012 230.815 1.00 76.75  ? 2815 THR A CB    1 
ATOM   10091 O  OG1   . THR A 1 2815 ? 173.821 186.286 230.825 1.00 81.01  ? 2815 THR A OG1   1 
ATOM   10092 C  CG2   . THR A 1 2815 ? 172.152 184.689 231.523 1.00 65.44  ? 2815 THR A CG2   1 
ATOM   10093 N  N     . LEU A 1 2816 ? 173.665 184.783 228.204 1.00 58.91  ? 2816 LEU A N     1 
ATOM   10094 C  CA    . LEU A 1 2816 ? 174.239 183.668 227.467 1.00 51.77  ? 2816 LEU A CA    1 
ATOM   10095 C  C     . LEU A 1 2816 ? 175.760 183.759 227.489 1.00 51.08  ? 2816 LEU A C     1 
ATOM   10096 O  O     . LEU A 1 2816 ? 176.327 184.784 227.090 1.00 57.30  ? 2816 LEU A O     1 
ATOM   10097 C  CB    . LEU A 1 2816 ? 173.718 183.664 226.028 1.00 50.46  ? 2816 LEU A CB    1 
ATOM   10098 C  CG    . LEU A 1 2816 ? 174.468 182.822 224.997 1.00 49.41  ? 2816 LEU A CG    1 
ATOM   10099 C  CD1   . LEU A 1 2816 ? 174.365 181.356 225.365 1.00 46.23  ? 2816 LEU A CD1   1 
ATOM   10100 C  CD2   . LEU A 1 2816 ? 173.924 183.066 223.600 1.00 45.44  ? 2816 LEU A CD2   1 
ATOM   10101 N  N     . PRO A 1 2817 ? 176.453 182.719 227.947 1.00 50.91  ? 2817 PRO A N     1 
ATOM   10102 C  CA    . PRO A 1 2817 ? 177.920 182.745 227.937 1.00 49.32  ? 2817 PRO A CA    1 
ATOM   10103 C  C     . PRO A 1 2817 ? 178.464 182.673 226.518 1.00 51.35  ? 2817 PRO A C     1 
ATOM   10104 O  O     . PRO A 1 2817 ? 177.741 182.446 225.546 1.00 56.42  ? 2817 PRO A O     1 
ATOM   10105 C  CB    . PRO A 1 2817 ? 178.306 181.505 228.749 1.00 54.26  ? 2817 PRO A CB    1 
ATOM   10106 C  CG    . PRO A 1 2817 ? 177.115 180.609 228.663 1.00 54.83  ? 2817 PRO A CG    1 
ATOM   10107 C  CD    . PRO A 1 2817 ? 175.925 181.520 228.617 1.00 52.02  ? 2817 PRO A CD    1 
ATOM   10108 N  N     . VAL A 1 2818 ? 179.779 182.878 226.412 1.00 49.39  ? 2818 VAL A N     1 
ATOM   10109 C  CA    . VAL A 1 2818 ? 180.434 182.848 225.107 1.00 48.83  ? 2818 VAL A CA    1 
ATOM   10110 C  C     . VAL A 1 2818 ? 180.355 181.458 224.490 1.00 47.51  ? 2818 VAL A C     1 
ATOM   10111 O  O     . VAL A 1 2818 ? 180.236 181.320 223.266 1.00 46.45  ? 2818 VAL A O     1 
ATOM   10112 C  CB    . VAL A 1 2818 ? 181.891 183.345 225.227 1.00 45.19  ? 2818 VAL A CB    1 
ATOM   10113 C  CG1   . VAL A 1 2818 ? 182.718 182.414 226.104 1.00 46.92  ? 2818 VAL A CG1   1 
ATOM   10114 C  CG2   . VAL A 1 2818 ? 182.521 183.487 223.850 1.00 44.87  ? 2818 VAL A CG2   1 
ATOM   10115 N  N     . GLU A 1 2819 ? 180.414 180.410 225.315 1.00 47.33  ? 2819 GLU A N     1 
ATOM   10116 C  CA    . GLU A 1 2819 ? 180.378 179.049 224.791 1.00 45.22  ? 2819 GLU A CA    1 
ATOM   10117 C  C     . GLU A 1 2819 ? 179.044 178.745 224.122 1.00 42.19  ? 2819 GLU A C     1 
ATOM   10118 O  O     . GLU A 1 2819 ? 179.002 178.093 223.073 1.00 39.92  ? 2819 GLU A O     1 
ATOM   10119 C  CB    . GLU A 1 2819 ? 180.658 178.054 225.913 1.00 53.57  ? 2819 GLU A CB    1 
ATOM   10120 C  CG    . GLU A 1 2819 ? 182.094 178.074 226.391 1.00 60.57  ? 2819 GLU A CG    1 
ATOM   10121 C  CD    . GLU A 1 2819 ? 182.310 179.018 227.555 1.00 67.99  ? 2819 GLU A CD    1 
ATOM   10122 O  OE1   . GLU A 1 2819 ? 181.309 179.491 228.131 1.00 68.04  ? 2819 GLU A OE1   1 
ATOM   10123 O  OE2   . GLU A 1 2819 ? 183.482 179.288 227.893 1.00 67.07  ? 2819 GLU A OE2   1 
ATOM   10124 N  N     . GLY A 1 2820 ? 177.942 179.208 224.712 1.00 43.25  ? 2820 GLY A N     1 
ATOM   10125 C  CA    . GLY A 1 2820 ? 176.649 179.029 224.074 1.00 39.62  ? 2820 GLY A CA    1 
ATOM   10126 C  C     . GLY A 1 2820 ? 176.536 179.794 222.769 1.00 35.03  ? 2820 GLY A C     1 
ATOM   10127 O  O     . GLY A 1 2820 ? 175.921 179.318 221.810 1.00 38.09  ? 2820 GLY A O     1 
ATOM   10128 N  N     . LEU A 1 2821 ? 177.125 180.991 222.714 1.00 31.64  ? 2821 LEU A N     1 
ATOM   10129 C  CA    . LEU A 1 2821 ? 177.152 181.742 221.464 1.00 33.12  ? 2821 LEU A CA    1 
ATOM   10130 C  C     . LEU A 1 2821 ? 177.935 180.994 220.393 1.00 29.94  ? 2821 LEU A C     1 
ATOM   10131 O  O     . LEU A 1 2821 ? 177.522 180.948 219.229 1.00 28.94  ? 2821 LEU A O     1 
ATOM   10132 C  CB    . LEU A 1 2821 ? 177.748 183.130 221.698 1.00 36.73  ? 2821 LEU A CB    1 
ATOM   10133 C  CG    . LEU A 1 2821 ? 178.107 183.944 220.453 1.00 32.21  ? 2821 LEU A CG    1 
ATOM   10134 C  CD1   . LEU A 1 2821 ? 176.874 184.620 219.879 1.00 26.98  ? 2821 LEU A CD1   1 
ATOM   10135 C  CD2   . LEU A 1 2821 ? 179.183 184.969 220.774 1.00 33.56  ? 2821 LEU A CD2   1 
ATOM   10136 N  N     . ILE A 1 2822 ? 179.065 180.392 220.771 1.00 30.40  ? 2822 ILE A N     1 
ATOM   10137 C  CA    . ILE A 1 2822 ? 179.839 179.598 219.820 1.00 27.82  ? 2822 ILE A CA    1 
ATOM   10138 C  C     . ILE A 1 2822 ? 179.042 178.383 219.367 1.00 28.73  ? 2822 ILE A C     1 
ATOM   10139 O  O     . ILE A 1 2822 ? 179.097 177.986 218.197 1.00 31.88  ? 2822 ILE A O     1 
ATOM   10140 C  CB    . ILE A 1 2822 ? 181.191 179.192 220.435 1.00 30.20  ? 2822 ILE A CB    1 
ATOM   10141 C  CG1   . ILE A 1 2822 ? 181.984 180.435 220.824 1.00 33.90  ? 2822 ILE A CG1   1 
ATOM   10142 C  CG2   . ILE A 1 2822 ? 181.991 178.339 219.462 1.00 27.15  ? 2822 ILE A CG2   1 
ATOM   10143 C  CD1   . ILE A 1 2822 ? 182.295 181.324 219.657 1.00 40.83  ? 2822 ILE A CD1   1 
ATOM   10144 N  N     . ARG A 1 2823 ? 178.300 177.765 220.288 1.00 28.33  ? 2823 ARG A N     1 
ATOM   10145 C  CA    . ARG A 1 2823 ? 177.476 176.618 219.923 1.00 22.63  ? 2823 ARG A CA    1 
ATOM   10146 C  C     . ARG A 1 2823 ? 176.393 177.011 218.925 1.00 23.54  ? 2823 ARG A C     1 
ATOM   10147 O  O     . ARG A 1 2823 ? 176.143 176.289 217.954 1.00 25.01  ? 2823 ARG A O     1 
ATOM   10148 C  CB    . ARG A 1 2823 ? 176.859 175.998 221.177 1.00 25.51  ? 2823 ARG A CB    1 
ATOM   10149 C  CG    . ARG A 1 2823 ? 175.864 174.888 220.895 1.00 31.44  ? 2823 ARG A CG    1 
ATOM   10150 C  CD    . ARG A 1 2823 ? 175.833 173.871 222.021 1.00 35.57  ? 2823 ARG A CD    1 
ATOM   10151 N  NE    . ARG A 1 2823 ? 176.767 172.777 221.788 1.00 38.78  ? 2823 ARG A NE    1 
ATOM   10152 C  CZ    . ARG A 1 2823 ? 176.405 171.536 221.494 1.00 40.26  ? 2823 ARG A CZ    1 
ATOM   10153 N  NH1   . ARG A 1 2823 ? 175.132 171.192 221.399 1.00 41.28  ? 2823 ARG A NH1   1 
ATOM   10154 N  NH2   . ARG A 1 2823 ? 177.344 170.618 221.288 1.00 43.93  ? 2823 ARG A NH2   1 
ATOM   10155 N  N     . ILE A 1 2824 ? 175.745 178.157 219.144 1.00 25.70  ? 2824 ILE A N     1 
ATOM   10156 C  CA    . ILE A 1 2824 ? 174.734 178.636 218.202 1.00 21.03  ? 2824 ILE A CA    1 
ATOM   10157 C  C     . ILE A 1 2824 ? 175.368 178.957 216.854 1.00 20.40  ? 2824 ILE A C     1 
ATOM   10158 O  O     . ILE A 1 2824 ? 174.799 178.660 215.795 1.00 24.54  ? 2824 ILE A O     1 
ATOM   10159 C  CB    . ILE A 1 2824 ? 173.993 179.853 218.783 1.00 18.87  ? 2824 ILE A CB    1 
ATOM   10160 C  CG1   . ILE A 1 2824 ? 173.260 179.466 220.067 1.00 28.86  ? 2824 ILE A CG1   1 
ATOM   10161 C  CG2   . ILE A 1 2824 ? 173.018 180.420 217.766 1.00 19.77  ? 2824 ILE A CG2   1 
ATOM   10162 C  CD1   . ILE A 1 2824 ? 172.373 180.550 220.624 1.00 32.35  ? 2824 ILE A CD1   1 
ATOM   10163 N  N     . TRP A 1 2825 ? 176.551 179.574 216.872 1.00 21.36  ? 2825 TRP A N     1 
ATOM   10164 C  CA    . TRP A 1 2825 ? 177.261 179.889 215.637 1.00 16.27  ? 2825 TRP A CA    1 
ATOM   10165 C  C     . TRP A 1 2825 ? 177.574 178.622 214.850 1.00 17.19  ? 2825 TRP A C     1 
ATOM   10166 O  O     . TRP A 1 2825 ? 177.356 178.559 213.634 1.00 18.97  ? 2825 TRP A O     1 
ATOM   10167 C  CB    . TRP A 1 2825 ? 178.538 180.660 215.979 1.00 15.38  ? 2825 TRP A CB    1 
ATOM   10168 C  CG    . TRP A 1 2825 ? 179.487 180.883 214.843 1.00 16.30  ? 2825 TRP A CG    1 
ATOM   10169 C  CD1   . TRP A 1 2825 ? 179.527 181.960 214.010 1.00 17.78  ? 2825 TRP A CD1   1 
ATOM   10170 C  CD2   . TRP A 1 2825 ? 180.557 180.021 214.436 1.00 15.89  ? 2825 TRP A CD2   1 
ATOM   10171 N  NE1   . TRP A 1 2825 ? 180.546 181.819 213.102 1.00 17.38  ? 2825 TRP A NE1   1 
ATOM   10172 C  CE2   . TRP A 1 2825 ? 181.192 180.635 213.340 1.00 17.38  ? 2825 TRP A CE2   1 
ATOM   10173 C  CE3   . TRP A 1 2825 ? 181.033 178.786 214.885 1.00 16.96  ? 2825 TRP A CE3   1 
ATOM   10174 C  CZ2   . TRP A 1 2825 ? 182.278 180.057 212.687 1.00 17.87  ? 2825 TRP A CZ2   1 
ATOM   10175 C  CZ3   . TRP A 1 2825 ? 182.111 178.215 214.236 1.00 19.86  ? 2825 TRP A CZ3   1 
ATOM   10176 C  CH2   . TRP A 1 2825 ? 182.721 178.850 213.149 1.00 20.79  ? 2825 TRP A CH2   1 
ATOM   10177 N  N     . ALA A 1 2826 ? 178.065 177.590 215.539 1.00 18.29  ? 2826 ALA A N     1 
ATOM   10178 C  CA    . ALA A 1 2826 ? 178.378 176.327 214.878 1.00 15.26  ? 2826 ALA A CA    1 
ATOM   10179 C  C     . ALA A 1 2826 ? 177.119 175.640 214.365 1.00 16.76  ? 2826 ALA A C     1 
ATOM   10180 O  O     . ALA A 1 2826 ? 177.129 175.046 213.282 1.00 21.80  ? 2826 ALA A O     1 
ATOM   10181 C  CB    . ALA A 1 2826 ? 179.141 175.410 215.832 1.00 15.08  ? 2826 ALA A CB    1 
ATOM   10182 N  N     . HIS A 1 2827 ? 176.028 175.700 215.132 1.00 15.64  ? 2827 HIS A N     1 
ATOM   10183 C  CA    . HIS A 1 2827 ? 174.775 175.099 214.686 1.00 17.52  ? 2827 HIS A CA    1 
ATOM   10184 C  C     . HIS A 1 2827 ? 174.265 175.766 213.416 1.00 19.33  ? 2827 HIS A C     1 
ATOM   10185 O  O     . HIS A 1 2827 ? 173.838 175.086 212.476 1.00 19.20  ? 2827 HIS A O     1 
ATOM   10186 C  CB    . HIS A 1 2827 ? 173.728 175.189 215.795 1.00 19.68  ? 2827 HIS A CB    1 
ATOM   10187 C  CG    . HIS A 1 2827 ? 172.366 174.729 215.380 1.00 21.10  ? 2827 HIS A CG    1 
ATOM   10188 N  ND1   . HIS A 1 2827 ? 172.074 173.408 215.121 1.00 23.07  ? 2827 HIS A ND1   1 
ATOM   10189 C  CD2   . HIS A 1 2827 ? 171.216 175.415 215.182 1.00 21.35  ? 2827 HIS A CD2   1 
ATOM   10190 C  CE1   . HIS A 1 2827 ? 170.802 173.299 214.780 1.00 22.29  ? 2827 HIS A CE1   1 
ATOM   10191 N  NE2   . HIS A 1 2827 ? 170.259 174.503 214.809 1.00 24.31  ? 2827 HIS A NE2   1 
ATOM   10192 N  N     . GLU A 1 2828 ? 174.301 177.099 213.371 1.00 20.33  ? 2828 GLU A N     1 
ATOM   10193 C  CA    . GLU A 1 2828 ? 173.874 177.806 212.169 1.00 15.66  ? 2828 GLU A CA    1 
ATOM   10194 C  C     . GLU A 1 2828 ? 174.799 177.508 210.995 1.00 16.44  ? 2828 GLU A C     1 
ATOM   10195 O  O     . GLU A 1 2828 ? 174.335 177.334 209.861 1.00 21.19  ? 2828 GLU A O     1 
ATOM   10196 C  CB    . GLU A 1 2828 ? 173.805 179.307 212.439 1.00 15.31  ? 2828 GLU A CB    1 
ATOM   10197 C  CG    . GLU A 1 2828 ? 172.744 179.708 213.449 1.00 20.01  ? 2828 GLU A CG    1 
ATOM   10198 C  CD    . GLU A 1 2828 ? 171.388 179.104 213.143 1.00 32.15  ? 2828 GLU A CD    1 
ATOM   10199 O  OE1   . GLU A 1 2828 ? 170.957 179.162 211.973 1.00 33.35  ? 2828 GLU A OE1   1 
ATOM   10200 O  OE2   . GLU A 1 2828 ? 170.752 178.570 214.076 1.00 38.91  ? 2828 GLU A OE2   1 
ATOM   10201 N  N     . ALA A 1 2829 ? 176.109 177.436 211.248 1.00 15.09  ? 2829 ALA A N     1 
ATOM   10202 C  CA    . ALA A 1 2829 ? 177.046 177.082 210.187 1.00 13.34  ? 2829 ALA A CA    1 
ATOM   10203 C  C     . ALA A 1 2829 ? 176.735 175.704 209.621 1.00 15.84  ? 2829 ALA A C     1 
ATOM   10204 O  O     . ALA A 1 2829 ? 176.753 175.507 208.401 1.00 19.61  ? 2829 ALA A O     1 
ATOM   10205 C  CB    . ALA A 1 2829 ? 178.479 177.129 210.714 1.00 12.78  ? 2829 ALA A CB    1 
ATOM   10206 N  N     . LEU A 1 2830 ? 176.447 174.739 210.496 1.00 17.18  ? 2830 LEU A N     1 
ATOM   10207 C  CA    . LEU A 1 2830 ? 176.078 173.406 210.035 1.00 15.29  ? 2830 LEU A CA    1 
ATOM   10208 C  C     . LEU A 1 2830 ? 174.802 173.447 209.208 1.00 17.31  ? 2830 LEU A C     1 
ATOM   10209 O  O     . LEU A 1 2830 ? 174.769 172.941 208.080 1.00 20.37  ? 2830 LEU A O     1 
ATOM   10210 C  CB    . LEU A 1 2830 ? 175.908 172.470 211.231 1.00 17.87  ? 2830 LEU A CB    1 
ATOM   10211 C  CG    . LEU A 1 2830 ? 177.188 172.066 211.959 1.00 17.82  ? 2830 LEU A CG    1 
ATOM   10212 C  CD1   . LEU A 1 2830 ? 176.865 171.364 213.266 1.00 15.62  ? 2830 LEU A CD1   1 
ATOM   10213 C  CD2   . LEU A 1 2830 ? 178.029 171.183 211.066 1.00 24.93  ? 2830 LEU A CD2   1 
ATOM   10214 N  N     . ARG A 1 2831 ? 173.752 174.080 209.738 1.00 17.44  ? 2831 ARG A N     1 
ATOM   10215 C  CA    . ARG A 1 2831 ? 172.467 174.107 209.051 1.00 19.49  ? 2831 ARG A CA    1 
ATOM   10216 C  C     . ARG A 1 2831 ? 172.526 174.853 207.726 1.00 16.38  ? 2831 ARG A C     1 
ATOM   10217 O  O     . ARG A 1 2831 ? 171.678 174.615 206.860 1.00 21.13  ? 2831 ARG A O     1 
ATOM   10218 C  CB    . ARG A 1 2831 ? 171.400 174.733 209.949 1.00 20.26  ? 2831 ARG A CB    1 
ATOM   10219 C  CG    . ARG A 1 2831 ? 171.130 173.963 211.233 1.00 21.33  ? 2831 ARG A CG    1 
ATOM   10220 C  CD    . ARG A 1 2831 ? 170.281 172.724 210.988 1.00 19.86  ? 2831 ARG A CD    1 
ATOM   10221 N  NE    . ARG A 1 2831 ? 171.083 171.578 210.575 1.00 19.51  ? 2831 ARG A NE    1 
ATOM   10222 C  CZ    . ARG A 1 2831 ? 171.873 170.883 211.381 1.00 26.84  ? 2831 ARG A CZ    1 
ATOM   10223 N  NH1   . ARG A 1 2831 ? 171.986 171.179 212.665 1.00 23.69  ? 2831 ARG A NH1   1 
ATOM   10224 N  NH2   . ARG A 1 2831 ? 172.568 169.862 210.886 1.00 34.13  ? 2831 ARG A NH2   1 
ATOM   10225 N  N     . LEU A 1 2832 ? 173.496 175.746 207.545 1.00 13.08  ? 2832 LEU A N     1 
ATOM   10226 C  CA    . LEU A 1 2832 ? 173.600 176.501 206.302 1.00 12.55  ? 2832 LEU A CA    1 
ATOM   10227 C  C     . LEU A 1 2832 ? 174.547 175.879 205.285 1.00 16.08  ? 2832 LEU A C     1 
ATOM   10228 O  O     . LEU A 1 2832 ? 174.274 175.939 204.083 1.00 22.06  ? 2832 LEU A O     1 
ATOM   10229 C  CB    . LEU A 1 2832 ? 174.050 177.934 206.590 1.00 14.12  ? 2832 LEU A CB    1 
ATOM   10230 C  CG    . LEU A 1 2832 ? 173.003 178.836 207.236 1.00 15.25  ? 2832 LEU A CG    1 
ATOM   10231 C  CD1   . LEU A 1 2832 ? 173.619 180.177 207.535 1.00 16.04  ? 2832 LEU A CD1   1 
ATOM   10232 C  CD2   . LEU A 1 2832 ? 171.791 178.989 206.334 1.00 20.32  ? 2832 LEU A CD2   1 
ATOM   10233 N  N     . PHE A 1 2833 ? 175.655 175.282 205.726 1.00 17.42  ? 2833 PHE A N     1 
ATOM   10234 C  CA    . PHE A 1 2833 ? 176.683 174.831 204.799 1.00 16.51  ? 2833 PHE A CA    1 
ATOM   10235 C  C     . PHE A 1 2833 ? 176.759 173.318 204.646 1.00 22.27  ? 2833 PHE A C     1 
ATOM   10236 O  O     . PHE A 1 2833 ? 177.257 172.846 203.619 1.00 31.71  ? 2833 PHE A O     1 
ATOM   10237 C  CB    . PHE A 1 2833 ? 178.054 175.358 205.241 1.00 16.49  ? 2833 PHE A CB    1 
ATOM   10238 C  CG    . PHE A 1 2833 ? 178.162 176.858 205.222 1.00 17.88  ? 2833 PHE A CG    1 
ATOM   10239 C  CD1   . PHE A 1 2833 ? 177.787 177.609 206.322 1.00 14.38  ? 2833 PHE A CD1   1 
ATOM   10240 C  CD2   . PHE A 1 2833 ? 178.644 177.516 204.104 1.00 20.75  ? 2833 PHE A CD2   1 
ATOM   10241 C  CE1   . PHE A 1 2833 ? 177.886 178.986 206.306 1.00 13.43  ? 2833 PHE A CE1   1 
ATOM   10242 C  CE2   . PHE A 1 2833 ? 178.747 178.893 204.082 1.00 19.46  ? 2833 PHE A CE2   1 
ATOM   10243 C  CZ    . PHE A 1 2833 ? 178.367 179.628 205.185 1.00 17.42  ? 2833 PHE A CZ    1 
ATOM   10244 N  N     . GLN A 1 2834 ? 176.282 172.546 205.624 1.00 19.52  ? 2834 GLN A N     1 
ATOM   10245 C  CA    . GLN A 1 2834 ? 176.421 171.097 205.583 1.00 19.41  ? 2834 GLN A CA    1 
ATOM   10246 C  C     . GLN A 1 2834 ? 175.156 170.378 205.135 1.00 24.69  ? 2834 GLN A C     1 
ATOM   10247 O  O     . GLN A 1 2834 ? 175.236 169.211 204.737 1.00 30.32  ? 2834 GLN A O     1 
ATOM   10248 C  CB    . GLN A 1 2834 ? 176.838 170.572 206.962 1.00 21.23  ? 2834 GLN A CB    1 
ATOM   10249 C  CG    . GLN A 1 2834 ? 177.555 169.234 206.934 1.00 25.78  ? 2834 GLN A CG    1 
ATOM   10250 C  CD    . GLN A 1 2834 ? 177.679 168.615 208.310 1.00 32.79  ? 2834 GLN A CD    1 
ATOM   10251 O  OE1   . GLN A 1 2834 ? 176.689 168.458 209.024 1.00 39.23  ? 2834 GLN A OE1   1 
ATOM   10252 N  NE2   . GLN A 1 2834 ? 178.899 168.260 208.692 1.00 36.05  ? 2834 GLN A NE2   1 
ATOM   10253 N  N     . ASP A 1 2835 ? 173.999 171.040 205.190 1.00 24.11  ? 2835 ASP A N     1 
ATOM   10254 C  CA    . ASP A 1 2835 ? 172.748 170.382 204.827 1.00 20.31  ? 2835 ASP A CA    1 
ATOM   10255 C  C     . ASP A 1 2835 ? 172.720 170.004 203.351 1.00 20.03  ? 2835 ASP A C     1 
ATOM   10256 O  O     . ASP A 1 2835 ? 172.255 168.917 202.990 1.00 26.91  ? 2835 ASP A O     1 
ATOM   10257 C  CB    . ASP A 1 2835 ? 171.565 171.286 205.170 1.00 24.34  ? 2835 ASP A CB    1 
ATOM   10258 C  CG    . ASP A 1 2835 ? 171.302 171.357 206.658 1.00 33.59  ? 2835 ASP A CG    1 
ATOM   10259 O  OD1   . ASP A 1 2835 ? 172.276 171.296 207.437 1.00 35.63  ? 2835 ASP A OD1   1 
ATOM   10260 O  OD2   . ASP A 1 2835 ? 170.124 171.482 207.049 1.00 35.90  ? 2835 ASP A OD2   1 
ATOM   10261 N  N     . ARG A 1 2836 ? 173.210 170.888 202.482 1.00 20.97  ? 2836 ARG A N     1 
ATOM   10262 C  CA    . ARG A 1 2836 ? 173.134 170.665 201.044 1.00 19.99  ? 2836 ARG A CA    1 
ATOM   10263 C  C     . ARG A 1 2836 ? 174.252 169.778 200.511 1.00 25.72  ? 2836 ARG A C     1 
ATOM   10264 O  O     . ARG A 1 2836 ? 174.222 169.423 199.328 1.00 29.36  ? 2836 ARG A O     1 
ATOM   10265 C  CB    . ARG A 1 2836 ? 173.153 172.007 200.307 1.00 19.12  ? 2836 ARG A CB    1 
ATOM   10266 C  CG    . ARG A 1 2836 ? 174.543 172.590 200.117 1.00 24.10  ? 2836 ARG A CG    1 
ATOM   10267 C  CD    . ARG A 1 2836 ? 174.484 173.954 199.455 1.00 26.58  ? 2836 ARG A CD    1 
ATOM   10268 N  NE    . ARG A 1 2836 ? 174.168 175.011 200.408 1.00 28.28  ? 2836 ARG A NE    1 
ATOM   10269 C  CZ    . ARG A 1 2836 ? 173.942 176.275 200.078 1.00 29.26  ? 2836 ARG A CZ    1 
ATOM   10270 N  NH1   . ARG A 1 2836 ? 173.985 176.679 198.819 1.00 29.11  ? 2836 ARG A NH1   1 
ATOM   10271 N  NH2   . ARG A 1 2836 ? 173.667 177.156 201.035 1.00 28.35  ? 2836 ARG A NH2   1 
ATOM   10272 N  N     . LEU A 1 2837 ? 175.226 169.414 201.339 1.00 25.47  ? 2837 LEU A N     1 
ATOM   10273 C  CA    . LEU A 1 2837 ? 176.350 168.618 200.870 1.00 23.57  ? 2837 LEU A CA    1 
ATOM   10274 C  C     . LEU A 1 2837 ? 175.912 167.196 200.537 1.00 26.49  ? 2837 LEU A C     1 
ATOM   10275 O  O     . LEU A 1 2837 ? 175.005 166.636 201.158 1.00 32.95  ? 2837 LEU A O     1 
ATOM   10276 C  CB    . LEU A 1 2837 ? 177.459 168.592 201.920 1.00 24.98  ? 2837 LEU A CB    1 
ATOM   10277 C  CG    . LEU A 1 2837 ? 178.060 169.955 202.257 1.00 19.93  ? 2837 LEU A CG    1 
ATOM   10278 C  CD1   . LEU A 1 2837 ? 179.260 169.794 203.169 1.00 24.92  ? 2837 LEU A CD1   1 
ATOM   10279 C  CD2   . LEU A 1 2837 ? 178.440 170.702 200.991 1.00 18.11  ? 2837 LEU A CD2   1 
ATOM   10280 N  N     . VAL A 1 2838 ? 176.574 166.611 199.540 1.00 25.81  ? 2838 VAL A N     1 
ATOM   10281 C  CA    . VAL A 1 2838 ? 176.215 165.289 199.040 1.00 26.95  ? 2838 VAL A CA    1 
ATOM   10282 C  C     . VAL A 1 2838 ? 177.103 164.226 199.673 1.00 33.63  ? 2838 VAL A C     1 
ATOM   10283 O  O     . VAL A 1 2838 ? 176.617 163.330 200.371 1.00 35.37  ? 2838 VAL A O     1 
ATOM   10284 C  CB    . VAL A 1 2838 ? 176.312 165.236 197.505 1.00 23.17  ? 2838 VAL A CB    1 
ATOM   10285 C  CG1   . VAL A 1 2838 ? 175.827 163.893 196.988 1.00 24.57  ? 2838 VAL A CG1   1 
ATOM   10286 C  CG2   . VAL A 1 2838 ? 175.518 166.372 196.884 1.00 22.71  ? 2838 VAL A CG2   1 
ATOM   10287 N  N     . GLU A 1 2839 ? 178.408 164.317 199.435 1.00 36.53  ? 2839 GLU A N     1 
ATOM   10288 C  CA    . GLU A 1 2839 ? 179.335 163.298 199.899 1.00 38.28  ? 2839 GLU A CA    1 
ATOM   10289 C  C     . GLU A 1 2839 ? 179.640 163.474 201.385 1.00 41.61  ? 2839 GLU A C     1 
ATOM   10290 O  O     . GLU A 1 2839 ? 179.555 164.572 201.941 1.00 44.63  ? 2839 GLU A O     1 
ATOM   10291 C  CB    . GLU A 1 2839 ? 180.630 163.342 199.086 1.00 40.38  ? 2839 GLU A CB    1 
ATOM   10292 C  CG    . GLU A 1 2839 ? 180.422 163.492 197.583 1.00 39.40  ? 2839 GLU A CG    1 
ATOM   10293 C  CD    . GLU A 1 2839 ? 179.944 162.215 196.910 1.00 48.23  ? 2839 GLU A CD    1 
ATOM   10294 O  OE1   . GLU A 1 2839 ? 179.719 161.207 197.612 1.00 50.01  ? 2839 GLU A OE1   1 
ATOM   10295 O  OE2   . GLU A 1 2839 ? 179.790 162.222 195.670 1.00 51.43  ? 2839 GLU A OE2   1 
ATOM   10296 N  N     . ASP A 1 2840 ? 180.003 162.362 202.027 1.00 44.87  ? 2840 ASP A N     1 
ATOM   10297 C  CA    . ASP A 1 2840 ? 180.316 162.381 203.451 1.00 48.80  ? 2840 ASP A CA    1 
ATOM   10298 C  C     . ASP A 1 2840 ? 181.643 163.073 203.739 1.00 51.00  ? 2840 ASP A C     1 
ATOM   10299 O  O     . ASP A 1 2840 ? 181.803 163.677 204.808 1.00 52.02  ? 2840 ASP A O     1 
ATOM   10300 C  CB    . ASP A 1 2840 ? 180.337 160.953 203.998 1.00 58.98  ? 2840 ASP A CB    1 
ATOM   10301 C  CG    . ASP A 1 2840 ? 180.519 160.906 205.500 1.00 77.61  ? 2840 ASP A CG    1 
ATOM   10302 O  OD1   . ASP A 1 2840 ? 179.555 161.219 206.229 1.00 79.05  ? 2840 ASP A OD1   1 
ATOM   10303 O  OD2   . ASP A 1 2840 ? 181.630 160.561 205.952 1.00 83.91  ? 2840 ASP A OD2   1 
ATOM   10304 N  N     . GLU A 1 2841 ? 182.600 162.994 202.811 1.00 47.36  ? 2841 GLU A N     1 
ATOM   10305 C  CA    . GLU A 1 2841 ? 183.875 163.675 203.005 1.00 49.90  ? 2841 GLU A CA    1 
ATOM   10306 C  C     . GLU A 1 2841 ? 183.685 165.184 203.076 1.00 53.77  ? 2841 GLU A C     1 
ATOM   10307 O  O     . GLU A 1 2841 ? 184.365 165.868 203.849 1.00 55.20  ? 2841 GLU A O     1 
ATOM   10308 C  CB    . GLU A 1 2841 ? 184.844 163.303 201.882 1.00 52.67  ? 2841 GLU A CB    1 
ATOM   10309 C  CG    . GLU A 1 2841 ? 186.169 164.048 201.926 1.00 62.53  ? 2841 GLU A CG    1 
ATOM   10310 C  CD    . GLU A 1 2841 ? 186.990 163.853 200.668 1.00 70.44  ? 2841 GLU A CD    1 
ATOM   10311 O  OE1   . GLU A 1 2841 ? 187.351 162.696 200.366 1.00 73.84  ? 2841 GLU A OE1   1 
ATOM   10312 O  OE2   . GLU A 1 2841 ? 187.277 164.856 199.981 1.00 68.17  ? 2841 GLU A OE2   1 
ATOM   10313 N  N     . GLU A 1 2842 ? 182.760 165.722 202.277 1.00 46.36  ? 2842 GLU A N     1 
ATOM   10314 C  CA    . GLU A 1 2842 ? 182.467 167.150 202.336 1.00 37.94  ? 2842 GLU A CA    1 
ATOM   10315 C  C     . GLU A 1 2842 ? 181.909 167.546 203.699 1.00 40.43  ? 2842 GLU A C     1 
ATOM   10316 O  O     . GLU A 1 2842 ? 182.289 168.582 204.258 1.00 47.49  ? 2842 GLU A O     1 
ATOM   10317 C  CB    . GLU A 1 2842 ? 181.490 167.524 201.223 1.00 29.22  ? 2842 GLU A CB    1 
ATOM   10318 C  CG    . GLU A 1 2842 ? 182.047 167.323 199.824 1.00 35.94  ? 2842 GLU A CG    1 
ATOM   10319 C  CD    . GLU A 1 2842 ? 180.963 167.266 198.766 1.00 40.70  ? 2842 GLU A CD    1 
ATOM   10320 O  OE1   . GLU A 1 2842 ? 179.771 167.313 199.132 1.00 41.27  ? 2842 GLU A OE1   1 
ATOM   10321 O  OE2   . GLU A 1 2842 ? 181.304 167.174 197.568 1.00 45.32  ? 2842 GLU A OE2   1 
ATOM   10322 N  N     . ARG A 1 2843 ? 181.005 166.733 204.251 1.00 31.00  ? 2843 ARG A N     1 
ATOM   10323 C  CA    . ARG A 1 2843 ? 180.457 167.020 205.574 1.00 30.77  ? 2843 ARG A CA    1 
ATOM   10324 C  C     . ARG A 1 2843 ? 181.534 166.932 206.649 1.00 39.84  ? 2843 ARG A C     1 
ATOM   10325 O  O     . ARG A 1 2843 ? 181.554 167.743 207.585 1.00 42.85  ? 2843 ARG A O     1 
ATOM   10326 C  CB    . ARG A 1 2843 ? 179.309 166.059 205.878 1.00 34.65  ? 2843 ARG A CB    1 
ATOM   10327 C  CG    . ARG A 1 2843 ? 178.333 165.888 204.726 1.00 31.90  ? 2843 ARG A CG    1 
ATOM   10328 C  CD    . ARG A 1 2843 ? 176.950 165.499 205.216 1.00 35.48  ? 2843 ARG A CD    1 
ATOM   10329 N  NE    . ARG A 1 2843 ? 176.082 165.091 204.118 1.00 45.03  ? 2843 ARG A NE    1 
ATOM   10330 C  CZ    . ARG A 1 2843 ? 175.986 163.851 203.658 1.00 50.21  ? 2843 ARG A CZ    1 
ATOM   10331 N  NH1   . ARG A 1 2843 ? 176.692 162.863 204.182 1.00 51.68  ? 2843 ARG A NH1   1 
ATOM   10332 N  NH2   . ARG A 1 2843 ? 175.161 163.596 202.646 1.00 39.64  ? 2843 ARG A NH2   1 
ATOM   10333 N  N     . ARG A 1 2844 ? 182.431 165.950 206.537 1.00 40.57  ? 2844 ARG A N     1 
ATOM   10334 C  CA    . ARG A 1 2844 ? 183.538 165.846 207.482 1.00 44.70  ? 2844 ARG A CA    1 
ATOM   10335 C  C     . ARG A 1 2844 ? 184.444 167.069 207.402 1.00 47.51  ? 2844 ARG A C     1 
ATOM   10336 O  O     . ARG A 1 2844 ? 184.882 167.599 208.431 1.00 53.83  ? 2844 ARG A O     1 
ATOM   10337 C  CB    . ARG A 1 2844 ? 184.330 164.567 207.210 1.00 55.92  ? 2844 ARG A CB    1 
ATOM   10338 C  CG    . ARG A 1 2844 ? 185.707 164.521 207.853 1.00 63.64  ? 2844 ARG A CG    1 
ATOM   10339 C  CD    . ARG A 1 2844 ? 186.287 163.102 207.965 1.00 71.86  ? 2844 ARG A CD    1 
ATOM   10340 N  NE    . ARG A 1 2844 ? 186.052 162.257 206.796 1.00 75.79  ? 2844 ARG A NE    1 
ATOM   10341 C  CZ    . ARG A 1 2844 ? 184.998 161.468 206.626 1.00 69.93  ? 2844 ARG A CZ    1 
ATOM   10342 N  NH1   . ARG A 1 2844 ? 184.056 161.363 207.549 1.00 61.01  ? 2844 ARG A NH1   1 
ATOM   10343 N  NH2   . ARG A 1 2844 ? 184.890 160.763 205.504 1.00 72.22  ? 2844 ARG A NH2   1 
ATOM   10344 N  N     . TRP A 1 2845 ? 184.731 167.530 206.181 1.00 40.64  ? 2845 TRP A N     1 
ATOM   10345 C  CA    . TRP A 1 2845 ? 185.521 168.744 206.002 1.00 40.52  ? 2845 TRP A CA    1 
ATOM   10346 C  C     . TRP A 1 2845 ? 184.831 169.942 206.636 1.00 37.47  ? 2845 TRP A C     1 
ATOM   10347 O  O     . TRP A 1 2845 ? 185.478 170.764 207.295 1.00 43.42  ? 2845 TRP A O     1 
ATOM   10348 C  CB    . TRP A 1 2845 ? 185.762 168.988 204.511 1.00 39.97  ? 2845 TRP A CB    1 
ATOM   10349 C  CG    . TRP A 1 2845 ? 186.552 170.227 204.193 1.00 43.97  ? 2845 TRP A CG    1 
ATOM   10350 C  CD1   . TRP A 1 2845 ? 187.891 170.302 203.943 1.00 46.32  ? 2845 TRP A CD1   1 
ATOM   10351 C  CD2   . TRP A 1 2845 ? 186.046 171.564 204.069 1.00 44.09  ? 2845 TRP A CD2   1 
ATOM   10352 N  NE1   . TRP A 1 2845 ? 188.252 171.601 203.682 1.00 46.46  ? 2845 TRP A NE1   1 
ATOM   10353 C  CE2   . TRP A 1 2845 ? 187.138 172.395 203.749 1.00 44.51  ? 2845 TRP A CE2   1 
ATOM   10354 C  CE3   . TRP A 1 2845 ? 184.779 172.139 204.200 1.00 38.82  ? 2845 TRP A CE3   1 
ATOM   10355 C  CZ2   . TRP A 1 2845 ? 187.002 173.769 203.567 1.00 40.70  ? 2845 TRP A CZ2   1 
ATOM   10356 C  CZ3   . TRP A 1 2845 ? 184.646 173.503 204.016 1.00 32.08  ? 2845 TRP A CZ3   1 
ATOM   10357 C  CH2   . TRP A 1 2845 ? 185.750 174.301 203.702 1.00 34.03  ? 2845 TRP A CH2   1 
ATOM   10358 N  N     . THR A 1 2846 ? 183.515 170.057 206.443 1.00 33.22  ? 2846 THR A N     1 
ATOM   10359 C  CA    . THR A 1 2846 ? 182.772 171.166 207.032 1.00 34.08  ? 2846 THR A CA    1 
ATOM   10360 C  C     . THR A 1 2846 ? 182.846 171.134 208.553 1.00 35.87  ? 2846 THR A C     1 
ATOM   10361 O  O     . THR A 1 2846 ? 183.075 172.167 209.191 1.00 41.13  ? 2846 THR A O     1 
ATOM   10362 C  CB    . THR A 1 2846 ? 181.317 171.133 206.562 1.00 33.54  ? 2846 THR A CB    1 
ATOM   10363 O  OG1   . THR A 1 2846 ? 181.270 171.327 205.144 1.00 32.45  ? 2846 THR A OG1   1 
ATOM   10364 C  CG2   . THR A 1 2846 ? 180.509 172.226 207.241 1.00 27.67  ? 2846 THR A CG2   1 
ATOM   10365 N  N     . ASP A 1 2847 ? 182.672 169.953 209.151 1.00 35.44  ? 2847 ASP A N     1 
ATOM   10366 C  CA    . ASP A 1 2847 ? 182.758 169.834 210.606 1.00 38.82  ? 2847 ASP A CA    1 
ATOM   10367 C  C     . ASP A 1 2847 ? 184.142 170.235 211.107 1.00 41.93  ? 2847 ASP A C     1 
ATOM   10368 O  O     . ASP A 1 2847 ? 184.278 171.051 212.034 1.00 43.56  ? 2847 ASP A O     1 
ATOM   10369 C  CB    . ASP A 1 2847 ? 182.439 168.399 211.030 1.00 48.38  ? 2847 ASP A CB    1 
ATOM   10370 C  CG    . ASP A 1 2847 ? 180.956 168.156 211.202 1.00 56.84  ? 2847 ASP A CG    1 
ATOM   10371 O  OD1   . ASP A 1 2847 ? 180.160 168.954 210.671 1.00 50.57  ? 2847 ASP A OD1   1 
ATOM   10372 O  OD2   . ASP A 1 2847 ? 180.586 167.165 211.867 1.00 64.39  ? 2847 ASP A OD2   1 
ATOM   10373 N  N     . GLU A 1 2848 ? 185.185 169.671 210.492 1.00 42.32  ? 2848 GLU A N     1 
ATOM   10374 C  CA    . GLU A 1 2848 ? 186.547 169.932 210.941 1.00 43.00  ? 2848 GLU A CA    1 
ATOM   10375 C  C     . GLU A 1 2848 ? 186.902 171.405 210.800 1.00 44.23  ? 2848 GLU A C     1 
ATOM   10376 O  O     . GLU A 1 2848 ? 187.531 171.986 211.691 1.00 49.21  ? 2848 GLU A O     1 
ATOM   10377 C  CB    . GLU A 1 2848 ? 187.531 169.064 210.156 1.00 48.41  ? 2848 GLU A CB    1 
ATOM   10378 C  CG    . GLU A 1 2848 ? 187.402 167.576 210.440 1.00 58.32  ? 2848 GLU A CG    1 
ATOM   10379 C  CD    . GLU A 1 2848 ? 188.374 166.741 209.631 1.00 77.22  ? 2848 GLU A CD    1 
ATOM   10380 O  OE1   . GLU A 1 2848 ? 189.063 167.308 208.757 1.00 75.88  ? 2848 GLU A OE1   1 
ATOM   10381 O  OE2   . GLU A 1 2848 ? 188.447 165.517 209.869 1.00 80.56  ? 2848 GLU A OE2   1 
ATOM   10382 N  N     . ASN A 1 2849 ? 186.495 172.035 209.698 1.00 36.34  ? 2849 ASN A N     1 
ATOM   10383 C  CA    . ASN A 1 2849 ? 186.836 173.435 209.494 1.00 34.00  ? 2849 ASN A CA    1 
ATOM   10384 C  C     . ASN A 1 2849 ? 185.987 174.370 210.345 1.00 32.84  ? 2849 ASN A C     1 
ATOM   10385 O  O     . ASN A 1 2849 ? 186.463 175.444 210.723 1.00 38.67  ? 2849 ASN A O     1 
ATOM   10386 C  CB    . ASN A 1 2849 ? 186.726 173.788 208.014 1.00 39.27  ? 2849 ASN A CB    1 
ATOM   10387 C  CG    . ASN A 1 2849 ? 187.991 173.455 207.252 1.00 46.66  ? 2849 ASN A CG    1 
ATOM   10388 O  OD1   . ASN A 1 2849 ? 188.031 172.501 206.480 1.00 44.95  ? 2849 ASN A OD1   1 
ATOM   10389 N  ND2   . ASN A 1 2849 ? 189.038 174.241 207.473 1.00 53.97  ? 2849 ASN A ND2   1 
ATOM   10390 N  N     . ILE A 1 2850 ? 184.752 173.986 210.679 1.00 31.64  ? 2850 ILE A N     1 
ATOM   10391 C  CA    . ILE A 1 2850 ? 183.991 174.751 211.663 1.00 32.04  ? 2850 ILE A CA    1 
ATOM   10392 C  C     . ILE A 1 2850 ? 184.724 174.752 212.995 1.00 35.60  ? 2850 ILE A C     1 
ATOM   10393 O  O     . ILE A 1 2850 ? 184.894 175.799 213.635 1.00 36.97  ? 2850 ILE A O     1 
ATOM   10394 C  CB    . ILE A 1 2850 ? 182.567 174.185 211.806 1.00 31.89  ? 2850 ILE A CB    1 
ATOM   10395 C  CG1   . ILE A 1 2850 ? 181.675 174.689 210.675 1.00 28.64  ? 2850 ILE A CG1   1 
ATOM   10396 C  CG2   . ILE A 1 2850 ? 181.969 174.562 213.153 1.00 25.45  ? 2850 ILE A CG2   1 
ATOM   10397 C  CD1   . ILE A 1 2850 ? 180.371 173.943 210.553 1.00 24.62  ? 2850 ILE A CD1   1 
ATOM   10398 N  N     . ASP A 1 2851 ? 185.193 173.575 213.419 1.00 40.44  ? 2851 ASP A N     1 
ATOM   10399 C  CA    . ASP A 1 2851 ? 185.963 173.502 214.658 1.00 41.75  ? 2851 ASP A CA    1 
ATOM   10400 C  C     . ASP A 1 2851 ? 187.239 174.334 214.566 1.00 41.10  ? 2851 ASP A C     1 
ATOM   10401 O  O     . ASP A 1 2851 ? 187.588 175.061 215.505 1.00 41.72  ? 2851 ASP A O     1 
ATOM   10402 C  CB    . ASP A 1 2851 ? 186.292 172.047 214.985 1.00 50.12  ? 2851 ASP A CB    1 
ATOM   10403 C  CG    . ASP A 1 2851 ? 185.109 171.300 215.567 1.00 60.05  ? 2851 ASP A CG    1 
ATOM   10404 O  OD1   . ASP A 1 2851 ? 183.978 171.823 215.486 1.00 58.01  ? 2851 ASP A OD1   1 
ATOM   10405 O  OD2   . ASP A 1 2851 ? 185.310 170.191 216.105 1.00 64.69  ? 2851 ASP A OD2   1 
ATOM   10406 N  N     . THR A 1 2852 ? 187.942 174.245 213.435 1.00 38.41  ? 2852 THR A N     1 
ATOM   10407 C  CA    . THR A 1 2852 ? 189.196 174.975 213.269 1.00 35.26  ? 2852 THR A CA    1 
ATOM   10408 C  C     . THR A 1 2852 ? 188.973 176.481 213.343 1.00 38.49  ? 2852 THR A C     1 
ATOM   10409 O  O     . THR A 1 2852 ? 189.718 177.196 214.022 1.00 41.67  ? 2852 THR A O     1 
ATOM   10410 C  CB    . THR A 1 2852 ? 189.848 174.593 211.940 1.00 34.24  ? 2852 THR A CB    1 
ATOM   10411 O  OG1   . THR A 1 2852 ? 190.117 173.186 211.924 1.00 36.41  ? 2852 THR A OG1   1 
ATOM   10412 C  CG2   . THR A 1 2852 ? 191.149 175.355 211.743 1.00 42.31  ? 2852 THR A CG2   1 
ATOM   10413 N  N     . VAL A 1 2853 ? 187.947 176.980 212.652 1.00 36.72  ? 2853 VAL A N     1 
ATOM   10414 C  CA    . VAL A 1 2853 ? 187.649 178.408 212.673 1.00 33.82  ? 2853 VAL A CA    1 
ATOM   10415 C  C     . VAL A 1 2853 ? 187.253 178.852 214.075 1.00 33.86  ? 2853 VAL A C     1 
ATOM   10416 O  O     . VAL A 1 2853 ? 187.697 179.904 214.559 1.00 35.48  ? 2853 VAL A O     1 
ATOM   10417 C  CB    . VAL A 1 2853 ? 186.553 178.733 211.641 1.00 29.43  ? 2853 VAL A CB    1 
ATOM   10418 C  CG1   . VAL A 1 2853 ? 185.969 180.108 211.896 1.00 32.80  ? 2853 VAL A CG1   1 
ATOM   10419 C  CG2   . VAL A 1 2853 ? 187.113 178.644 210.232 1.00 28.17  ? 2853 VAL A CG2   1 
ATOM   10420 N  N     . ALA A 1 2854 ? 186.420 178.057 214.754 1.00 32.08  ? 2854 ALA A N     1 
ATOM   10421 C  CA    . ALA A 1 2854 ? 185.987 178.424 216.097 1.00 30.53  ? 2854 ALA A CA    1 
ATOM   10422 C  C     . ALA A 1 2854 ? 187.165 178.499 217.059 1.00 38.53  ? 2854 ALA A C     1 
ATOM   10423 O  O     . ALA A 1 2854 ? 187.222 179.394 217.909 1.00 41.27  ? 2854 ALA A O     1 
ATOM   10424 C  CB    . ALA A 1 2854 ? 184.940 177.433 216.598 1.00 37.53  ? 2854 ALA A CB    1 
ATOM   10425 N  N     . LEU A 1 2855 ? 188.121 177.572 216.944 1.00 45.64  ? 2855 LEU A N     1 
ATOM   10426 C  CA    . LEU A 1 2855 ? 189.288 177.657 217.819 1.00 47.15  ? 2855 LEU A CA    1 
ATOM   10427 C  C     . LEU A 1 2855 ? 190.229 178.783 217.413 1.00 45.19  ? 2855 LEU A C     1 
ATOM   10428 O  O     . LEU A 1 2855 ? 190.878 179.383 218.277 1.00 49.62  ? 2855 LEU A O     1 
ATOM   10429 C  CB    . LEU A 1 2855 ? 190.061 176.339 217.856 1.00 51.17  ? 2855 LEU A CB    1 
ATOM   10430 C  CG    . LEU A 1 2855 ? 189.557 175.264 218.821 1.00 57.30  ? 2855 LEU A CG    1 
ATOM   10431 C  CD1   . LEU A 1 2855 ? 189.668 175.791 220.246 1.00 58.95  ? 2855 LEU A CD1   1 
ATOM   10432 C  CD2   . LEU A 1 2855 ? 188.161 174.771 218.516 1.00 52.58  ? 2855 LEU A CD2   1 
ATOM   10433 N  N     . LYS A 1 2856 ? 190.329 179.079 216.116 1.00 39.77  ? 2856 LYS A N     1 
ATOM   10434 C  CA    . LYS A 1 2856 ? 191.238 180.130 215.673 1.00 42.34  ? 2856 LYS A CA    1 
ATOM   10435 C  C     . LYS A 1 2856 ? 190.764 181.499 216.141 1.00 43.35  ? 2856 LYS A C     1 
ATOM   10436 O  O     . LYS A 1 2856 ? 191.562 182.311 216.625 1.00 43.69  ? 2856 LYS A O     1 
ATOM   10437 C  CB    . LYS A 1 2856 ? 191.376 180.097 214.151 1.00 38.71  ? 2856 LYS A CB    1 
ATOM   10438 C  CG    . LYS A 1 2856 ? 192.027 181.335 213.565 1.00 40.21  ? 2856 LYS A CG    1 
ATOM   10439 C  CD    . LYS A 1 2856 ? 192.169 181.226 212.057 1.00 49.99  ? 2856 LYS A CD    1 
ATOM   10440 C  CE    . LYS A 1 2856 ? 192.872 182.448 211.487 1.00 55.37  ? 2856 LYS A CE    1 
ATOM   10441 N  NZ    . LYS A 1 2856 ? 193.022 182.376 210.007 1.00 44.46  ? 2856 LYS A NZ    1 
ATOM   10442 N  N     . HIS A 1 2857 ? 189.468 181.775 216.010 1.00 41.35  ? 2857 HIS A N     1 
ATOM   10443 C  CA    . HIS A 1 2857 ? 188.952 183.093 216.354 1.00 35.65  ? 2857 HIS A CA    1 
ATOM   10444 C  C     . HIS A 1 2857 ? 188.485 183.205 217.800 1.00 37.76  ? 2857 HIS A C     1 
ATOM   10445 O  O     . HIS A 1 2857 ? 188.220 184.321 218.260 1.00 38.00  ? 2857 HIS A O     1 
ATOM   10446 C  CB    . HIS A 1 2857 ? 187.810 183.470 215.407 1.00 32.46  ? 2857 HIS A CB    1 
ATOM   10447 C  CG    . HIS A 1 2857 ? 188.264 183.755 214.010 1.00 32.84  ? 2857 HIS A CG    1 
ATOM   10448 N  ND1   . HIS A 1 2857 ? 188.840 184.953 213.645 1.00 35.34  ? 2857 HIS A ND1   1 
ATOM   10449 C  CD2   . HIS A 1 2857 ? 188.242 182.993 212.892 1.00 35.03  ? 2857 HIS A CD2   1 
ATOM   10450 C  CE1   . HIS A 1 2857 ? 189.147 184.919 212.361 1.00 39.17  ? 2857 HIS A CE1   1 
ATOM   10451 N  NE2   . HIS A 1 2857 ? 188.793 183.741 211.880 1.00 37.07  ? 2857 HIS A NE2   1 
ATOM   10452 N  N     . PHE A 1 2858 ? 188.376 182.093 218.524 1.00 42.10  ? 2858 PHE A N     1 
ATOM   10453 C  CA    . PHE A 1 2858 ? 188.000 182.092 219.938 1.00 45.16  ? 2858 PHE A CA    1 
ATOM   10454 C  C     . PHE A 1 2858 ? 188.960 181.173 220.681 1.00 51.71  ? 2858 PHE A C     1 
ATOM   10455 O  O     . PHE A 1 2858 ? 188.654 179.998 220.924 1.00 58.77  ? 2858 PHE A O     1 
ATOM   10456 C  CB    . PHE A 1 2858 ? 186.546 181.660 220.126 1.00 39.58  ? 2858 PHE A CB    1 
ATOM   10457 C  CG    . PHE A 1 2858 ? 185.550 182.620 219.541 1.00 37.81  ? 2858 PHE A CG    1 
ATOM   10458 C  CD1   . PHE A 1 2858 ? 185.216 182.561 218.198 1.00 34.87  ? 2858 PHE A CD1   1 
ATOM   10459 C  CD2   . PHE A 1 2858 ? 184.950 183.584 220.333 1.00 38.15  ? 2858 PHE A CD2   1 
ATOM   10460 C  CE1   . PHE A 1 2858 ? 184.302 183.443 217.657 1.00 32.52  ? 2858 PHE A CE1   1 
ATOM   10461 C  CE2   . PHE A 1 2858 ? 184.035 184.468 219.798 1.00 40.81  ? 2858 PHE A CE2   1 
ATOM   10462 C  CZ    . PHE A 1 2858 ? 183.710 184.397 218.459 1.00 39.29  ? 2858 PHE A CZ    1 
ATOM   10463 N  N     . PRO A 1 2859 ? 190.138 181.677 221.058 1.00 53.36  ? 2859 PRO A N     1 
ATOM   10464 C  CA    . PRO A 1 2859 ? 191.153 180.777 221.628 1.00 58.80  ? 2859 PRO A CA    1 
ATOM   10465 C  C     . PRO A 1 2859 ? 190.917 180.422 223.086 1.00 60.98  ? 2859 PRO A C     1 
ATOM   10466 O  O     . PRO A 1 2859 ? 191.174 179.279 223.483 1.00 59.67  ? 2859 PRO A O     1 
ATOM   10467 C  CB    . PRO A 1 2859 ? 192.460 181.562 221.433 1.00 61.75  ? 2859 PRO A CB    1 
ATOM   10468 C  CG    . PRO A 1 2859 ? 192.046 183.001 221.123 1.00 60.37  ? 2859 PRO A CG    1 
ATOM   10469 C  CD    . PRO A 1 2859 ? 190.547 183.087 221.142 1.00 53.95  ? 2859 PRO A CD    1 
ATOM   10470 N  N     . ASN A 1 2860 ? 190.438 181.359 223.899 1.00 60.35  ? 2860 ASN A N     1 
ATOM   10471 C  CA    . ASN A 1 2860 ? 190.309 181.140 225.340 1.00 62.14  ? 2860 ASN A CA    1 
ATOM   10472 C  C     . ASN A 1 2860 ? 188.899 180.673 225.702 1.00 63.01  ? 2860 ASN A C     1 
ATOM   10473 O  O     . ASN A 1 2860 ? 188.193 181.287 226.502 1.00 68.32  ? 2860 ASN A O     1 
ATOM   10474 C  CB    . ASN A 1 2860 ? 190.686 182.408 226.102 1.00 71.02  ? 2860 ASN A CB    1 
ATOM   10475 C  CG    . ASN A 1 2860 ? 191.972 183.032 225.595 1.00 76.99  ? 2860 ASN A CG    1 
ATOM   10476 O  OD1   . ASN A 1 2860 ? 192.952 182.335 225.334 1.00 71.96  ? 2860 ASN A OD1   1 
ATOM   10477 N  ND2   . ASN A 1 2860 ? 191.974 184.352 225.456 1.00 81.89  ? 2860 ASN A ND2   1 
ATOM   10478 N  N     . ILE A 1 2861 ? 188.492 179.558 225.095 1.00 61.70  ? 2861 ILE A N     1 
ATOM   10479 C  CA    . ILE A 1 2861 ? 187.244 178.888 225.432 1.00 65.84  ? 2861 ILE A CA    1 
ATOM   10480 C  C     . ILE A 1 2861 ? 187.514 177.394 225.529 1.00 71.79  ? 2861 ILE A C     1 
ATOM   10481 O  O     . ILE A 1 2861 ? 188.489 176.877 224.978 1.00 72.40  ? 2861 ILE A O     1 
ATOM   10482 C  CB    . ILE A 1 2861 ? 186.119 179.161 224.406 1.00 60.53  ? 2861 ILE A CB    1 
ATOM   10483 C  CG1   . ILE A 1 2861 ? 186.509 178.624 223.028 1.00 58.95  ? 2861 ILE A CG1   1 
ATOM   10484 C  CG2   . ILE A 1 2861 ? 185.788 180.646 224.341 1.00 64.96  ? 2861 ILE A CG2   1 
ATOM   10485 C  CD1   . ILE A 1 2861 ? 185.377 178.637 222.028 1.00 49.80  ? 2861 ILE A CD1   1 
ATOM   10486 N  N     . ASP A 1 2862 ? 186.633 176.696 226.241 1.00 74.40  ? 2862 ASP A N     1 
ATOM   10487 C  CA    . ASP A 1 2862 ? 186.706 175.245 226.321 1.00 74.71  ? 2862 ASP A CA    1 
ATOM   10488 C  C     . ASP A 1 2862 ? 186.001 174.620 225.122 1.00 69.93  ? 2862 ASP A C     1 
ATOM   10489 O  O     . ASP A 1 2862 ? 185.048 175.184 224.577 1.00 69.41  ? 2862 ASP A O     1 
ATOM   10490 C  CB    . ASP A 1 2862 ? 186.118 174.731 227.641 1.00 74.43  ? 2862 ASP A CB    1 
ATOM   10491 C  CG    . ASP A 1 2862 ? 184.660 175.104 227.832 1.00 77.28  ? 2862 ASP A CG    1 
ATOM   10492 O  OD1   . ASP A 1 2862 ? 184.098 175.818 226.981 1.00 81.91  ? 2862 ASP A OD1   1 
ATOM   10493 O  OD2   . ASP A 1 2862 ? 184.070 174.677 228.846 1.00 77.31  ? 2862 ASP A OD2   1 
ATOM   10494 N  N     . ARG A 1 2863 ? 186.496 173.457 224.701 1.00 68.82  ? 2863 ARG A N     1 
ATOM   10495 C  CA    . ARG A 1 2863 ? 186.063 172.879 223.434 1.00 65.73  ? 2863 ARG A CA    1 
ATOM   10496 C  C     . ARG A 1 2863 ? 184.777 172.075 223.592 1.00 69.44  ? 2863 ARG A C     1 
ATOM   10497 O  O     . ARG A 1 2863 ? 183.847 172.217 222.788 1.00 67.39  ? 2863 ARG A O     1 
ATOM   10498 C  CB    . ARG A 1 2863 ? 187.170 171.985 222.872 1.00 69.24  ? 2863 ARG A CB    1 
ATOM   10499 C  CG    . ARG A 1 2863 ? 188.103 172.643 221.865 1.00 61.04  ? 2863 ARG A CG    1 
ATOM   10500 C  CD    . ARG A 1 2863 ? 189.387 171.822 221.758 1.00 65.51  ? 2863 ARG A CD    1 
ATOM   10501 N  NE    . ARG A 1 2863 ? 190.305 172.077 222.864 1.00 71.29  ? 2863 ARG A NE    1 
ATOM   10502 C  CZ    . ARG A 1 2863 ? 191.245 173.011 222.871 1.00 64.81  ? 2863 ARG A CZ    1 
ATOM   10503 N  NH1   . ARG A 1 2863 ? 191.486 173.760 221.809 1.00 63.51  ? 2863 ARG A NH1   1 
ATOM   10504 N  NH2   . ARG A 1 2863 ? 191.976 173.187 223.968 1.00 62.42  ? 2863 ARG A NH2   1 
ATOM   10505 N  N     . GLU A 1 2864 ? 184.705 171.241 224.633 1.00 71.45  ? 2864 GLU A N     1 
ATOM   10506 C  CA    . GLU A 1 2864 ? 183.658 170.227 224.715 1.00 69.47  ? 2864 GLU A CA    1 
ATOM   10507 C  C     . GLU A 1 2864 ? 182.287 170.842 224.965 1.00 64.25  ? 2864 GLU A C     1 
ATOM   10508 O  O     . GLU A 1 2864 ? 181.309 170.476 224.301 1.00 62.93  ? 2864 GLU A O     1 
ATOM   10509 C  CB    . GLU A 1 2864 ? 183.998 169.218 225.812 1.00 64.31  ? 2864 GLU A CB    1 
ATOM   10510 C  CG    . GLU A 1 2864 ? 185.044 168.189 225.410 1.00 68.31  ? 2864 GLU A CG    1 
ATOM   10511 C  CD    . GLU A 1 2864 ? 184.951 167.796 223.949 1.00 71.89  ? 2864 GLU A CD    1 
ATOM   10512 O  OE1   . GLU A 1 2864 ? 185.931 168.022 223.210 1.00 72.28  ? 2864 GLU A OE1   1 
ATOM   10513 O  OE2   . GLU A 1 2864 ? 183.903 167.249 223.542 1.00 67.99  ? 2864 GLU A OE2   1 
ATOM   10514 N  N     . LYS A 1 2865 ? 182.189 171.768 225.921 1.00 60.75  ? 2865 LYS A N     1 
ATOM   10515 C  CA    . LYS A 1 2865 ? 180.885 172.326 226.271 1.00 63.61  ? 2865 LYS A CA    1 
ATOM   10516 C  C     . LYS A 1 2865 ? 180.275 173.089 225.102 1.00 60.99  ? 2865 LYS A C     1 
ATOM   10517 O  O     . LYS A 1 2865 ? 179.075 172.965 224.830 1.00 61.05  ? 2865 LYS A O     1 
ATOM   10518 C  CB    . LYS A 1 2865 ? 181.011 173.233 227.496 1.00 66.88  ? 2865 LYS A CB    1 
ATOM   10519 C  CG    . LYS A 1 2865 ? 179.934 174.305 227.584 1.00 63.87  ? 2865 LYS A CG    1 
ATOM   10520 C  CD    . LYS A 1 2865 ? 180.370 175.467 228.460 1.00 71.17  ? 2865 LYS A CD    1 
ATOM   10521 C  CE    . LYS A 1 2865 ? 180.214 175.136 229.934 1.00 78.63  ? 2865 LYS A CE    1 
ATOM   10522 N  NZ    . LYS A 1 2865 ? 180.093 176.368 230.761 1.00 84.59  ? 2865 LYS A NZ    1 
ATOM   10523 N  N     . ALA A 1 2866 ? 181.085 173.872 224.395 1.00 60.87  ? 2866 ALA A N     1 
ATOM   10524 C  CA    . ALA A 1 2866 ? 180.588 174.682 223.294 1.00 57.21  ? 2866 ALA A CA    1 
ATOM   10525 C  C     . ALA A 1 2866 ? 180.396 173.899 222.003 1.00 52.75  ? 2866 ALA A C     1 
ATOM   10526 O  O     . ALA A 1 2866 ? 179.529 174.266 221.201 1.00 50.88  ? 2866 ALA A O     1 
ATOM   10527 C  CB    . ALA A 1 2866 ? 181.537 175.856 223.032 1.00 52.24  ? 2866 ALA A CB    1 
ATOM   10528 N  N     . MET A 1 2867 ? 181.173 172.838 221.773 1.00 52.98  ? 2867 MET A N     1 
ATOM   10529 C  CA    . MET A 1 2867 ? 181.197 172.193 220.465 1.00 51.80  ? 2867 MET A CA    1 
ATOM   10530 C  C     . MET A 1 2867 ? 181.203 170.672 220.561 1.00 61.20  ? 2867 MET A C     1 
ATOM   10531 O  O     . MET A 1 2867 ? 181.961 170.006 219.850 1.00 59.82  ? 2867 MET A O     1 
ATOM   10532 C  CB    . MET A 1 2867 ? 182.394 172.683 219.658 1.00 52.48  ? 2867 MET A CB    1 
ATOM   10533 C  CG    . MET A 1 2867 ? 182.291 174.143 219.280 1.00 60.97  ? 2867 MET A CG    1 
ATOM   10534 S  SD    . MET A 1 2867 ? 183.694 174.671 218.306 1.00 70.02  ? 2867 MET A SD    1 
ATOM   10535 C  CE    . MET A 1 2867 ? 184.912 174.737 219.612 1.00 68.92  ? 2867 MET A CE    1 
ATOM   10536 N  N     . SER A 1 2868 ? 180.375 170.106 221.433 1.00 62.89  ? 2868 SER A N     1 
ATOM   10537 C  CA    . SER A 1 2868 ? 180.113 168.677 221.367 1.00 55.73  ? 2868 SER A CA    1 
ATOM   10538 C  C     . SER A 1 2868 ? 179.413 168.358 220.052 1.00 56.45  ? 2868 SER A C     1 
ATOM   10539 O  O     . SER A 1 2868 ? 178.533 169.099 219.610 1.00 58.91  ? 2868 SER A O     1 
ATOM   10540 C  CB    . SER A 1 2868 ? 179.258 168.232 222.552 1.00 57.51  ? 2868 SER A CB    1 
ATOM   10541 O  OG    . SER A 1 2868 ? 179.930 168.458 223.778 1.00 54.71  ? 2868 SER A OG    1 
ATOM   10542 N  N     . ARG A 1 2869 ? 179.813 167.249 219.428 1.00 56.12  ? 2869 ARG A N     1 
ATOM   10543 C  CA    . ARG A 1 2869 ? 179.373 166.960 218.062 1.00 57.92  ? 2869 ARG A CA    1 
ATOM   10544 C  C     . ARG A 1 2869 ? 177.858 166.926 217.889 1.00 61.62  ? 2869 ARG A C     1 
ATOM   10545 O  O     . ARG A 1 2869 ? 177.367 167.485 216.892 1.00 65.44  ? 2869 ARG A O     1 
ATOM   10546 C  CB    . ARG A 1 2869 ? 180.023 165.660 217.580 1.00 61.47  ? 2869 ARG A CB    1 
ATOM   10547 C  CG    . ARG A 1 2869 ? 181.534 165.753 217.406 1.00 73.62  ? 2869 ARG A CG    1 
ATOM   10548 C  CD    . ARG A 1 2869 ? 181.903 166.715 216.278 1.00 71.44  ? 2869 ARG A CD    1 
ATOM   10549 N  NE    . ARG A 1 2869 ? 182.001 168.099 216.729 1.00 67.56  ? 2869 ARG A NE    1 
ATOM   10550 C  CZ    . ARG A 1 2869 ? 182.037 169.151 215.922 1.00 63.73  ? 2869 ARG A CZ    1 
ATOM   10551 N  NH1   . ARG A 1 2869 ? 181.982 169.016 214.607 1.00 64.67  ? 2869 ARG A NH1   1 
ATOM   10552 N  NH2   . ARG A 1 2869 ? 182.127 170.369 216.448 1.00 61.16  ? 2869 ARG A NH2   1 
ATOM   10553 N  N     . PRO A 1 2870 ? 177.062 166.308 218.776 1.00 57.06  ? 2870 PRO A N     1 
ATOM   10554 C  CA    . PRO A 1 2870 ? 175.605 166.372 218.585 1.00 52.28  ? 2870 PRO A CA    1 
ATOM   10555 C  C     . PRO A 1 2870 ? 175.052 167.766 218.841 1.00 48.76  ? 2870 PRO A C     1 
ATOM   10556 O  O     . PRO A 1 2870 ? 174.423 168.012 219.875 1.00 53.37  ? 2870 PRO A O     1 
ATOM   10557 C  CB    . PRO A 1 2870 ? 175.066 165.356 219.602 1.00 52.26  ? 2870 PRO A CB    1 
ATOM   10558 C  CG    . PRO A 1 2870 ? 176.236 164.508 219.970 1.00 56.01  ? 2870 PRO A CG    1 
ATOM   10559 C  CD    . PRO A 1 2870 ? 177.416 165.413 219.891 1.00 53.43  ? 2870 PRO A CD    1 
ATOM   10560 N  N     . ILE A 1 2871 ? 175.280 168.685 217.903 1.00 37.95  ? 2871 ILE A N     1 
ATOM   10561 C  CA    . ILE A 1 2871 ? 174.784 170.055 218.017 1.00 35.80  ? 2871 ILE A CA    1 
ATOM   10562 C  C     . ILE A 1 2871 ? 173.327 170.047 217.565 1.00 34.28  ? 2871 ILE A C     1 
ATOM   10563 O  O     . ILE A 1 2871 ? 173.037 170.089 216.369 1.00 35.79  ? 2871 ILE A O     1 
ATOM   10564 C  CB    . ILE A 1 2871 ? 175.622 171.040 217.198 1.00 33.42  ? 2871 ILE A CB    1 
ATOM   10565 C  CG1   . ILE A 1 2871 ? 177.114 170.782 217.405 1.00 33.62  ? 2871 ILE A CG1   1 
ATOM   10566 C  CG2   . ILE A 1 2871 ? 175.279 172.468 217.584 1.00 26.52  ? 2871 ILE A CG2   1 
ATOM   10567 C  CD1   . ILE A 1 2871 ? 178.008 171.856 216.828 1.00 23.99  ? 2871 ILE A CD1   1 
ATOM   10568 N  N     . LEU A 1 2872 ? 172.406 169.996 218.521 1.00 32.08  ? 2872 LEU A N     1 
ATOM   10569 C  CA    . LEU A 1 2872 ? 170.980 169.962 218.236 1.00 28.94  ? 2872 LEU A CA    1 
ATOM   10570 C  C     . LEU A 1 2872 ? 170.285 171.105 218.960 1.00 26.76  ? 2872 LEU A C     1 
ATOM   10571 O  O     . LEU A 1 2872 ? 170.562 171.370 220.134 1.00 32.10  ? 2872 LEU A O     1 
ATOM   10572 C  CB    . LEU A 1 2872 ? 170.365 168.623 218.656 1.00 32.37  ? 2872 LEU A CB    1 
ATOM   10573 C  CG    . LEU A 1 2872 ? 170.835 167.392 217.880 1.00 28.11  ? 2872 LEU A CG    1 
ATOM   10574 C  CD1   . LEU A 1 2872 ? 170.240 166.125 218.471 1.00 30.54  ? 2872 LEU A CD1   1 
ATOM   10575 C  CD2   . LEU A 1 2872 ? 170.486 167.516 216.406 1.00 26.41  ? 2872 LEU A CD2   1 
ATOM   10576 N  N     . TYR A 1 2873 ? 169.383 171.779 218.252 1.00 25.93  ? 2873 TYR A N     1 
ATOM   10577 C  CA    . TYR A 1 2873 ? 168.609 172.883 218.799 1.00 24.53  ? 2873 TYR A CA    1 
ATOM   10578 C  C     . TYR A 1 2873 ? 167.139 172.679 218.471 1.00 26.65  ? 2873 TYR A C     1 
ATOM   10579 O  O     . TYR A 1 2873 ? 166.792 172.320 217.342 1.00 34.28  ? 2873 TYR A O     1 
ATOM   10580 C  CB    . TYR A 1 2873 ? 169.089 174.228 218.244 1.00 25.74  ? 2873 TYR A CB    1 
ATOM   10581 C  CG    . TYR A 1 2873 ? 170.206 174.856 219.041 1.00 23.31  ? 2873 TYR A CG    1 
ATOM   10582 C  CD1   . TYR A 1 2873 ? 171.472 174.292 219.063 1.00 22.36  ? 2873 TYR A CD1   1 
ATOM   10583 C  CD2   . TYR A 1 2873 ? 169.991 176.013 219.774 1.00 24.52  ? 2873 TYR A CD2   1 
ATOM   10584 C  CE1   . TYR A 1 2873 ? 172.493 174.863 219.793 1.00 21.31  ? 2873 TYR A CE1   1 
ATOM   10585 C  CE2   . TYR A 1 2873 ? 171.005 176.592 220.505 1.00 26.23  ? 2873 TYR A CE2   1 
ATOM   10586 C  CZ    . TYR A 1 2873 ? 172.253 176.013 220.512 1.00 24.68  ? 2873 TYR A CZ    1 
ATOM   10587 O  OH    . TYR A 1 2873 ? 173.263 176.588 221.244 1.00 27.39  ? 2873 TYR A OH    1 
ATOM   10588 N  N     . SER A 1 2874 ? 166.279 172.912 219.459 1.00 25.92  ? 2874 SER A N     1 
ATOM   10589 C  CA    . SER A 1 2874 ? 164.850 172.714 219.265 1.00 26.67  ? 2874 SER A CA    1 
ATOM   10590 C  C     . SER A 1 2874 ? 164.082 173.513 220.306 1.00 33.74  ? 2874 SER A C     1 
ATOM   10591 O  O     . SER A 1 2874 ? 164.519 173.650 221.451 1.00 36.60  ? 2874 SER A O     1 
ATOM   10592 C  CB    . SER A 1 2874 ? 164.474 171.232 219.353 1.00 27.81  ? 2874 SER A CB    1 
ATOM   10593 O  OG    . SER A 1 2874 ? 163.098 171.039 219.080 1.00 35.50  ? 2874 SER A OG    1 
ATOM   10594 N  N     . ASN A 1 2875 ? 162.928 174.035 219.890 1.00 35.14  ? 2875 ASN A N     1 
ATOM   10595 C  CA    . ASN A 1 2875 ? 161.995 174.710 220.781 1.00 37.71  ? 2875 ASN A CA    1 
ATOM   10596 C  C     . ASN A 1 2875 ? 160.798 173.823 221.109 1.00 40.62  ? 2875 ASN A C     1 
ATOM   10597 O  O     . ASN A 1 2875 ? 159.703 174.318 221.385 1.00 44.30  ? 2875 ASN A O     1 
ATOM   10598 C  CB    . ASN A 1 2875 ? 161.530 176.034 220.175 1.00 40.42  ? 2875 ASN A CB    1 
ATOM   10599 C  CG    . ASN A 1 2875 ? 160.845 175.855 218.836 1.00 43.19  ? 2875 ASN A CG    1 
ATOM   10600 O  OD1   . ASN A 1 2875 ? 160.869 174.772 218.251 1.00 39.97  ? 2875 ASN A OD1   1 
ATOM   10601 N  ND2   . ASN A 1 2875 ? 160.224 176.920 218.344 1.00 42.80  ? 2875 ASN A ND2   1 
ATOM   10602 N  N     . TRP A 1 2876 ? 160.996 172.505 221.067 1.00 39.95  ? 2876 TRP A N     1 
ATOM   10603 C  CA    . TRP A 1 2876 ? 159.918 171.569 221.362 1.00 34.12  ? 2876 TRP A CA    1 
ATOM   10604 C  C     . TRP A 1 2876 ? 159.828 171.282 222.855 1.00 44.84  ? 2876 TRP A C     1 
ATOM   10605 O  O     . TRP A 1 2876 ? 158.746 171.354 223.447 1.00 51.54  ? 2876 TRP A O     1 
ATOM   10606 C  CB    . TRP A 1 2876 ? 160.131 170.270 220.585 1.00 29.39  ? 2876 TRP A CB    1 
ATOM   10607 C  CG    . TRP A 1 2876 ? 159.699 170.337 219.157 1.00 30.51  ? 2876 TRP A CG    1 
ATOM   10608 C  CD1   . TRP A 1 2876 ? 158.847 171.243 218.598 1.00 31.28  ? 2876 TRP A CD1   1 
ATOM   10609 C  CD2   . TRP A 1 2876 ? 160.102 169.460 218.100 1.00 30.97  ? 2876 TRP A CD2   1 
ATOM   10610 N  NE1   . TRP A 1 2876 ? 158.693 170.984 217.258 1.00 26.55  ? 2876 TRP A NE1   1 
ATOM   10611 C  CE2   . TRP A 1 2876 ? 159.454 169.893 216.928 1.00 26.14  ? 2876 TRP A CE2   1 
ATOM   10612 C  CE3   . TRP A 1 2876 ? 160.948 168.349 218.031 1.00 29.14  ? 2876 TRP A CE3   1 
ATOM   10613 C  CZ2   . TRP A 1 2876 ? 159.624 169.256 215.703 1.00 23.00  ? 2876 TRP A CZ2   1 
ATOM   10614 C  CZ3   . TRP A 1 2876 ? 161.116 167.719 216.815 1.00 24.67  ? 2876 TRP A CZ3   1 
ATOM   10615 C  CH2   . TRP A 1 2876 ? 160.458 168.173 215.667 1.00 23.26  ? 2876 TRP A CH2   1 
ATOM   10616 N  N     . LEU A 1 2877 ? 160.961 170.950 223.478 1.00 45.25  ? 2877 LEU A N     1 
ATOM   10617 C  CA    . LEU A 1 2877 ? 160.962 170.622 224.899 1.00 45.34  ? 2877 LEU A CA    1 
ATOM   10618 C  C     . LEU A 1 2877 ? 160.646 171.843 225.753 1.00 56.58  ? 2877 LEU A C     1 
ATOM   10619 O  O     . LEU A 1 2877 ? 159.926 171.738 226.754 1.00 66.87  ? 2877 LEU A O     1 
ATOM   10620 C  CB    . LEU A 1 2877 ? 162.312 170.025 225.297 1.00 42.77  ? 2877 LEU A CB    1 
ATOM   10621 C  CG    . LEU A 1 2877 ? 162.473 168.509 225.171 1.00 41.89  ? 2877 LEU A CG    1 
ATOM   10622 C  CD1   . LEU A 1 2877 ? 162.534 168.080 223.713 1.00 38.72  ? 2877 LEU A CD1   1 
ATOM   10623 C  CD2   . LEU A 1 2877 ? 163.712 168.050 225.919 1.00 44.06  ? 2877 LEU A CD2   1 
ATOM   10624 N  N     . SER A 1 2878 ? 161.172 173.005 225.379 1.00 54.77  ? 2878 SER A N     1 
ATOM   10625 C  CA    . SER A 1 2878 ? 160.982 174.237 226.131 1.00 57.41  ? 2878 SER A CA    1 
ATOM   10626 C  C     . SER A 1 2878 ? 160.446 175.317 225.200 1.00 56.50  ? 2878 SER A C     1 
ATOM   10627 O  O     . SER A 1 2878 ? 160.353 175.132 223.984 1.00 59.69  ? 2878 SER A O     1 
ATOM   10628 C  CB    . SER A 1 2878 ? 162.291 174.689 226.790 1.00 61.96  ? 2878 SER A CB    1 
ATOM   10629 O  OG    . SER A 1 2878 ? 163.195 175.188 225.821 1.00 59.33  ? 2878 SER A OG    1 
ATOM   10630 N  N     . LYS A 1 2879 ? 160.089 176.461 225.786 1.00 55.22  ? 2879 LYS A N     1 
ATOM   10631 C  CA    . LYS A 1 2879 ? 159.564 177.570 224.998 1.00 57.04  ? 2879 LYS A CA    1 
ATOM   10632 C  C     . LYS A 1 2879 ? 160.646 178.213 224.138 1.00 59.60  ? 2879 LYS A C     1 
ATOM   10633 O  O     . LYS A 1 2879 ? 160.381 178.609 222.998 1.00 54.43  ? 2879 LYS A O     1 
ATOM   10634 C  CB    . LYS A 1 2879 ? 158.929 178.611 225.921 1.00 58.90  ? 2879 LYS A CB    1 
ATOM   10635 C  CG    . LYS A 1 2879 ? 158.061 179.631 225.203 1.00 62.60  ? 2879 LYS A CG    1 
ATOM   10636 C  CD    . LYS A 1 2879 ? 157.714 180.797 226.115 1.00 71.82  ? 2879 LYS A CD    1 
ATOM   10637 C  CE    . LYS A 1 2879 ? 158.964 181.529 226.574 1.00 74.22  ? 2879 LYS A CE    1 
ATOM   10638 N  NZ    . LYS A 1 2879 ? 159.571 182.335 225.479 1.00 65.20  ? 2879 LYS A NZ    1 
ATOM   10639 N  N     . ASP A 1 2880 ? 161.862 178.323 224.661 1.00 61.61  ? 2880 ASP A N     1 
ATOM   10640 C  CA    . ASP A 1 2880 ? 162.951 178.976 223.953 1.00 53.32  ? 2880 ASP A CA    1 
ATOM   10641 C  C     . ASP A 1 2880 ? 163.676 177.994 223.037 1.00 47.19  ? 2880 ASP A C     1 
ATOM   10642 O  O     . ASP A 1 2880 ? 163.560 176.774 223.169 1.00 50.71  ? 2880 ASP A O     1 
ATOM   10643 C  CB    . ASP A 1 2880 ? 163.938 179.599 224.940 1.00 55.87  ? 2880 ASP A CB    1 
ATOM   10644 C  CG    . ASP A 1 2880 ? 163.359 180.796 225.666 1.00 67.43  ? 2880 ASP A CG    1 
ATOM   10645 O  OD1   . ASP A 1 2880 ? 162.227 181.203 225.332 1.00 72.05  ? 2880 ASP A OD1   1 
ATOM   10646 O  OD2   . ASP A 1 2880 ? 164.034 181.329 226.571 1.00 65.54  ? 2880 ASP A OD2   1 
ATOM   10647 N  N     . TYR A 1 2881 ? 164.434 178.555 222.096 1.00 43.13  ? 2881 TYR A N     1 
ATOM   10648 C  CA    . TYR A 1 2881 ? 165.206 177.767 221.134 1.00 34.68  ? 2881 TYR A CA    1 
ATOM   10649 C  C     . TYR A 1 2881 ? 166.576 177.438 221.730 1.00 35.21  ? 2881 TYR A C     1 
ATOM   10650 O  O     . TYR A 1 2881 ? 167.626 177.895 221.276 1.00 37.53  ? 2881 TYR A O     1 
ATOM   10651 C  CB    . TYR A 1 2881 ? 165.322 178.519 219.815 1.00 35.99  ? 2881 TYR A CB    1 
ATOM   10652 C  CG    . TYR A 1 2881 ? 165.844 177.691 218.665 1.00 33.88  ? 2881 TYR A CG    1 
ATOM   10653 C  CD1   . TYR A 1 2881 ? 165.059 176.707 218.081 1.00 30.53  ? 2881 TYR A CD1   1 
ATOM   10654 C  CD2   . TYR A 1 2881 ? 167.115 177.906 218.153 1.00 31.27  ? 2881 TYR A CD2   1 
ATOM   10655 C  CE1   . TYR A 1 2881 ? 165.532 175.952 217.028 1.00 27.06  ? 2881 TYR A CE1   1 
ATOM   10656 C  CE2   . TYR A 1 2881 ? 167.594 177.158 217.099 1.00 26.66  ? 2881 TYR A CE2   1 
ATOM   10657 C  CZ    . TYR A 1 2881 ? 166.799 176.183 216.541 1.00 26.25  ? 2881 TYR A CZ    1 
ATOM   10658 O  OH    . TYR A 1 2881 ? 167.276 175.435 215.492 1.00 27.40  ? 2881 TYR A OH    1 
ATOM   10659 N  N     . ILE A 1 2882 ? 166.541 176.619 222.776 1.00 35.72  ? 2882 ILE A N     1 
ATOM   10660 C  CA    . ILE A 1 2882 ? 167.741 176.235 223.516 1.00 34.23  ? 2882 ILE A CA    1 
ATOM   10661 C  C     . ILE A 1 2882 ? 168.263 174.912 222.966 1.00 32.34  ? 2882 ILE A C     1 
ATOM   10662 O  O     . ILE A 1 2882 ? 167.505 174.174 222.318 1.00 34.38  ? 2882 ILE A O     1 
ATOM   10663 C  CB    . ILE A 1 2882 ? 167.456 176.136 225.023 1.00 36.86  ? 2882 ILE A CB    1 
ATOM   10664 C  CG1   . ILE A 1 2882 ? 166.415 175.051 225.300 1.00 39.59  ? 2882 ILE A CG1   1 
ATOM   10665 C  CG2   . ILE A 1 2882 ? 166.988 177.476 225.565 1.00 44.54  ? 2882 ILE A CG2   1 
ATOM   10666 C  CD1   . ILE A 1 2882 ? 166.250 174.730 226.769 1.00 43.73  ? 2882 ILE A CD1   1 
ATOM   10667 N  N     . PRO A 1 2883 ? 169.537 174.575 223.177 1.00 29.56  ? 2883 PRO A N     1 
ATOM   10668 C  CA    . PRO A 1 2883 ? 170.031 173.268 222.731 1.00 27.35  ? 2883 PRO A CA    1 
ATOM   10669 C  C     . PRO A 1 2883 ? 169.331 172.132 223.459 1.00 32.19  ? 2883 PRO A C     1 
ATOM   10670 O  O     . PRO A 1 2883 ? 168.937 172.255 224.621 1.00 34.25  ? 2883 PRO A O     1 
ATOM   10671 C  CB    . PRO A 1 2883 ? 171.525 173.316 223.072 1.00 22.31  ? 2883 PRO A CB    1 
ATOM   10672 C  CG    . PRO A 1 2883 ? 171.641 174.364 224.126 1.00 24.41  ? 2883 PRO A CG    1 
ATOM   10673 C  CD    . PRO A 1 2883 ? 170.610 175.387 223.775 1.00 28.92  ? 2883 PRO A CD    1 
ATOM   10674 N  N     . VAL A 1 2884 ? 169.179 171.012 222.757 1.00 31.84  ? 2884 VAL A N     1 
ATOM   10675 C  CA    . VAL A 1 2884 ? 168.505 169.833 223.286 1.00 33.34  ? 2884 VAL A CA    1 
ATOM   10676 C  C     . VAL A 1 2884 ? 169.419 168.628 223.111 1.00 38.63  ? 2884 VAL A C     1 
ATOM   10677 O  O     . VAL A 1 2884 ? 170.148 168.526 222.118 1.00 43.22  ? 2884 VAL A O     1 
ATOM   10678 C  CB    . VAL A 1 2884 ? 167.139 169.603 222.600 1.00 28.80  ? 2884 VAL A CB    1 
ATOM   10679 C  CG1   . VAL A 1 2884 ? 167.316 169.239 221.132 1.00 25.74  ? 2884 VAL A CG1   1 
ATOM   10680 C  CG2   . VAL A 1 2884 ? 166.344 168.532 223.331 1.00 37.23  ? 2884 VAL A CG2   1 
ATOM   10681 N  N     . ASP A 1 2885 ? 169.403 167.732 224.093 1.00 39.89  ? 2885 ASP A N     1 
ATOM   10682 C  CA    . ASP A 1 2885 ? 170.193 166.516 224.008 1.00 49.81  ? 2885 ASP A CA    1 
ATOM   10683 C  C     . ASP A 1 2885 ? 169.406 165.434 223.269 1.00 50.58  ? 2885 ASP A C     1 
ATOM   10684 O  O     . ASP A 1 2885 ? 168.185 165.514 223.112 1.00 51.84  ? 2885 ASP A O     1 
ATOM   10685 C  CB    . ASP A 1 2885 ? 170.599 166.042 225.406 1.00 53.98  ? 2885 ASP A CB    1 
ATOM   10686 C  CG    . ASP A 1 2885 ? 171.640 164.936 225.375 1.00 66.03  ? 2885 ASP A CG    1 
ATOM   10687 O  OD1   . ASP A 1 2885 ? 172.046 164.520 224.270 1.00 66.31  ? 2885 ASP A OD1   1 
ATOM   10688 O  OD2   . ASP A 1 2885 ? 172.055 164.484 226.463 1.00 74.13  ? 2885 ASP A OD2   1 
ATOM   10689 N  N     . GLN A 1 2886 ? 170.132 164.413 222.810 1.00 47.85  ? 2886 GLN A N     1 
ATOM   10690 C  CA    . GLN A 1 2886 ? 169.547 163.430 221.904 1.00 41.19  ? 2886 GLN A CA    1 
ATOM   10691 C  C     . GLN A 1 2886 ? 168.487 162.574 222.592 1.00 50.19  ? 2886 GLN A C     1 
ATOM   10692 O  O     . GLN A 1 2886 ? 167.467 162.241 221.981 1.00 50.42  ? 2886 GLN A O     1 
ATOM   10693 C  CB    . GLN A 1 2886 ? 170.650 162.550 221.315 1.00 42.80  ? 2886 GLN A CB    1 
ATOM   10694 C  CG    . GLN A 1 2886 ? 170.285 161.893 219.997 1.00 42.13  ? 2886 GLN A CG    1 
ATOM   10695 C  CD    . GLN A 1 2886 ? 171.463 161.802 219.049 1.00 47.02  ? 2886 GLN A CD    1 
ATOM   10696 O  OE1   . GLN A 1 2886 ? 172.587 161.521 219.463 1.00 51.57  ? 2886 GLN A OE1   1 
ATOM   10697 N  NE2   . GLN A 1 2886 ? 171.211 162.043 217.768 1.00 43.04  ? 2886 GLN A NE2   1 
ATOM   10698 N  N     . GLU A 1 2887 ? 168.710 162.200 223.854 1.00 55.93  ? 2887 GLU A N     1 
ATOM   10699 C  CA    . GLU A 1 2887 ? 167.834 161.228 224.506 1.00 54.21  ? 2887 GLU A CA    1 
ATOM   10700 C  C     . GLU A 1 2887 ? 166.449 161.806 224.783 1.00 51.35  ? 2887 GLU A C     1 
ATOM   10701 O  O     . GLU A 1 2887 ? 165.428 161.177 224.473 1.00 52.26  ? 2887 GLU A O     1 
ATOM   10702 C  CB    . GLU A 1 2887 ? 168.481 160.732 225.799 1.00 55.01  ? 2887 GLU A CB    1 
ATOM   10703 C  CG    . GLU A 1 2887 ? 169.808 160.024 225.588 1.00 62.50  ? 2887 GLU A CG    1 
ATOM   10704 C  CD    . GLU A 1 2887 ? 169.776 159.062 224.416 1.00 66.76  ? 2887 GLU A CD    1 
ATOM   10705 O  OE1   . GLU A 1 2887 ? 168.951 158.124 224.436 1.00 69.14  ? 2887 GLU A OE1   1 
ATOM   10706 O  OE2   . GLU A 1 2887 ? 170.575 159.245 223.474 1.00 60.81  ? 2887 GLU A OE2   1 
ATOM   10707 N  N     . GLU A 1 2888 ? 166.390 162.999 225.380 1.00 49.54  ? 2888 GLU A N     1 
ATOM   10708 C  CA    . GLU A 1 2888 ? 165.096 163.607 225.673 1.00 50.18  ? 2888 GLU A CA    1 
ATOM   10709 C  C     . GLU A 1 2888 ? 164.358 163.968 224.391 1.00 48.28  ? 2888 GLU A C     1 
ATOM   10710 O  O     . GLU A 1 2888 ? 163.130 163.840 224.317 1.00 50.49  ? 2888 GLU A O     1 
ATOM   10711 C  CB    . GLU A 1 2888 ? 165.274 164.840 226.560 1.00 50.77  ? 2888 GLU A CB    1 
ATOM   10712 C  CG    . GLU A 1 2888 ? 166.055 164.589 227.842 1.00 56.97  ? 2888 GLU A CG    1 
ATOM   10713 C  CD    . GLU A 1 2888 ? 167.550 164.722 227.650 1.00 62.89  ? 2888 GLU A CD    1 
ATOM   10714 O  OE1   . GLU A 1 2888 ? 167.991 164.786 226.485 1.00 57.14  ? 2888 GLU A OE1   1 
ATOM   10715 O  OE2   . GLU A 1 2888 ? 168.283 164.763 228.660 1.00 69.79  ? 2888 GLU A OE2   1 
ATOM   10716 N  N     . LEU A 1 2889 ? 165.092 164.420 223.372 1.00 41.85  ? 2889 LEU A N     1 
ATOM   10717 C  CA    . LEU A 1 2889 ? 164.476 164.669 222.075 1.00 39.65  ? 2889 LEU A CA    1 
ATOM   10718 C  C     . LEU A 1 2889 ? 163.886 163.389 221.498 1.00 44.98  ? 2889 LEU A C     1 
ATOM   10719 O  O     . LEU A 1 2889 ? 162.779 163.400 220.951 1.00 44.39  ? 2889 LEU A O     1 
ATOM   10720 C  CB    . LEU A 1 2889 ? 165.501 165.272 221.115 1.00 31.55  ? 2889 LEU A CB    1 
ATOM   10721 C  CG    . LEU A 1 2889 ? 165.060 165.446 219.661 1.00 29.61  ? 2889 LEU A CG    1 
ATOM   10722 C  CD1   . LEU A 1 2889 ? 164.059 166.582 219.535 1.00 31.49  ? 2889 LEU A CD1   1 
ATOM   10723 C  CD2   . LEU A 1 2889 ? 166.262 165.686 218.765 1.00 26.84  ? 2889 LEU A CD2   1 
ATOM   10724 N  N     . ARG A 1 2890 ? 164.610 162.273 221.621 1.00 43.33  ? 2890 ARG A N     1 
ATOM   10725 C  CA    . ARG A 1 2890 ? 164.098 160.997 221.134 1.00 40.03  ? 2890 ARG A CA    1 
ATOM   10726 C  C     . ARG A 1 2890 ? 162.830 160.591 221.872 1.00 41.57  ? 2890 ARG A C     1 
ATOM   10727 O  O     . ARG A 1 2890 ? 161.870 160.124 221.254 1.00 41.35  ? 2890 ARG A O     1 
ATOM   10728 C  CB    . ARG A 1 2890 ? 165.163 159.912 221.276 1.00 40.61  ? 2890 ARG A CB    1 
ATOM   10729 C  CG    . ARG A 1 2890 ? 164.791 158.600 220.609 1.00 45.33  ? 2890 ARG A CG    1 
ATOM   10730 C  CD    . ARG A 1 2890 ? 165.730 157.479 221.023 1.00 50.27  ? 2890 ARG A CD    1 
ATOM   10731 N  NE    . ARG A 1 2890 ? 167.126 157.798 220.749 1.00 52.96  ? 2890 ARG A NE    1 
ATOM   10732 C  CZ    . ARG A 1 2890 ? 167.681 157.758 219.546 1.00 49.41  ? 2890 ARG A CZ    1 
ATOM   10733 N  NH1   . ARG A 1 2890 ? 166.986 157.410 218.475 1.00 41.48  ? 2890 ARG A NH1   1 
ATOM   10734 N  NH2   . ARG A 1 2890 ? 168.967 158.074 219.413 1.00 46.30  ? 2890 ARG A NH2   1 
ATOM   10735 N  N     . ASP A 1 2891 ? 162.810 160.755 223.197 1.00 40.54  ? 2891 ASP A N     1 
ATOM   10736 C  CA    . ASP A 1 2891 ? 161.613 160.402 223.960 1.00 42.51  ? 2891 ASP A CA    1 
ATOM   10737 C  C     . ASP A 1 2891 ? 160.425 161.274 223.562 1.00 42.64  ? 2891 ASP A C     1 
ATOM   10738 O  O     . ASP A 1 2891 ? 159.302 160.775 223.390 1.00 42.04  ? 2891 ASP A O     1 
ATOM   10739 C  CB    . ASP A 1 2891 ? 161.884 160.522 225.460 1.00 50.37  ? 2891 ASP A CB    1 
ATOM   10740 C  CG    . ASP A 1 2891 ? 163.100 159.731 225.899 1.00 52.80  ? 2891 ASP A CG    1 
ATOM   10741 O  OD1   . ASP A 1 2891 ? 163.217 158.551 225.506 1.00 55.92  ? 2891 ASP A OD1   1 
ATOM   10742 O  OD2   . ASP A 1 2891 ? 163.931 160.284 226.648 1.00 51.48  ? 2891 ASP A OD2   1 
ATOM   10743 N  N     . TYR A 1 2892 ? 160.656 162.581 223.411 1.00 39.48  ? 2892 TYR A N     1 
ATOM   10744 C  CA    . TYR A 1 2892 ? 159.581 163.482 223.012 1.00 36.31  ? 2892 TYR A CA    1 
ATOM   10745 C  C     . TYR A 1 2892 ? 159.051 163.128 221.629 1.00 38.07  ? 2892 TYR A C     1 
ATOM   10746 O  O     . TYR A 1 2892 ? 157.834 163.103 221.409 1.00 40.32  ? 2892 TYR A O     1 
ATOM   10747 C  CB    . TYR A 1 2892 ? 160.076 164.928 223.047 1.00 35.60  ? 2892 TYR A CB    1 
ATOM   10748 C  CG    . TYR A 1 2892 ? 159.023 165.954 222.697 1.00 37.43  ? 2892 TYR A CG    1 
ATOM   10749 C  CD1   . TYR A 1 2892 ? 158.090 166.368 223.637 1.00 37.27  ? 2892 TYR A CD1   1 
ATOM   10750 C  CD2   . TYR A 1 2892 ? 158.968 166.515 221.429 1.00 35.03  ? 2892 TYR A CD2   1 
ATOM   10751 C  CE1   . TYR A 1 2892 ? 157.128 167.306 223.321 1.00 44.70  ? 2892 TYR A CE1   1 
ATOM   10752 C  CE2   . TYR A 1 2892 ? 158.011 167.453 221.105 1.00 33.27  ? 2892 TYR A CE2   1 
ATOM   10753 C  CZ    . TYR A 1 2892 ? 157.093 167.846 222.054 1.00 46.32  ? 2892 TYR A CZ    1 
ATOM   10754 O  OH    . TYR A 1 2892 ? 156.137 168.782 221.734 1.00 58.07  ? 2892 TYR A OH    1 
ATOM   10755 N  N     . VAL A 1 2893 ? 159.951 162.839 220.686 1.00 33.76  ? 2893 VAL A N     1 
ATOM   10756 C  CA    . VAL A 1 2893 ? 159.522 162.483 219.338 1.00 33.01  ? 2893 VAL A CA    1 
ATOM   10757 C  C     . VAL A 1 2893 ? 158.794 161.144 219.345 1.00 39.19  ? 2893 VAL A C     1 
ATOM   10758 O  O     . VAL A 1 2893 ? 157.852 160.941 218.579 1.00 39.84  ? 2893 VAL A O     1 
ATOM   10759 C  CB    . VAL A 1 2893 ? 160.721 162.486 218.371 1.00 34.94  ? 2893 VAL A CB    1 
ATOM   10760 C  CG1   . VAL A 1 2893 ? 160.303 161.991 216.999 1.00 32.22  ? 2893 VAL A CG1   1 
ATOM   10761 C  CG2   . VAL A 1 2893 ? 161.295 163.886 218.254 1.00 38.80  ? 2893 VAL A CG2   1 
ATOM   10762 N  N     . LYS A 1 2894 ? 159.204 160.215 220.213 1.00 43.55  ? 2894 LYS A N     1 
ATOM   10763 C  CA    . LYS A 1 2894 ? 158.494 158.944 220.331 1.00 37.03  ? 2894 LYS A CA    1 
ATOM   10764 C  C     . LYS A 1 2894 ? 157.059 159.156 220.800 1.00 35.37  ? 2894 LYS A C     1 
ATOM   10765 O  O     . LYS A 1 2894 ? 156.114 158.592 220.231 1.00 36.97  ? 2894 LYS A O     1 
ATOM   10766 C  CB    . LYS A 1 2894 ? 159.236 158.015 221.294 1.00 38.99  ? 2894 LYS A CB    1 
ATOM   10767 C  CG    . LYS A 1 2894 ? 160.189 157.044 220.623 1.00 43.39  ? 2894 LYS A CG    1 
ATOM   10768 C  CD    . LYS A 1 2894 ? 161.091 156.363 221.637 1.00 47.63  ? 2894 LYS A CD    1 
ATOM   10769 C  CE    . LYS A 1 2894 ? 162.046 155.395 220.958 1.00 52.03  ? 2894 LYS A CE    1 
ATOM   10770 N  NZ    . LYS A 1 2894 ? 163.066 154.862 221.903 1.00 55.72  ? 2894 LYS A NZ    1 
ATOM   10771 N  N     . ALA A 1 2895 ? 156.877 159.967 221.845 1.00 32.84  ? 2895 ALA A N     1 
ATOM   10772 C  CA    . ALA A 1 2895 ? 155.525 160.234 222.332 1.00 33.11  ? 2895 ALA A CA    1 
ATOM   10773 C  C     . ALA A 1 2895 ? 154.687 160.943 221.273 1.00 38.32  ? 2895 ALA A C     1 
ATOM   10774 O  O     . ALA A 1 2895 ? 153.522 160.585 221.036 1.00 43.51  ? 2895 ALA A O     1 
ATOM   10775 C  CB    . ALA A 1 2895 ? 155.582 161.060 223.616 1.00 28.49  ? 2895 ALA A CB    1 
ATOM   10776 N  N     . ARG A 1 2896 ? 155.272 161.943 220.609 1.00 35.07  ? 2896 ARG A N     1 
ATOM   10777 C  CA    . ARG A 1 2896 ? 154.537 162.667 219.581 1.00 32.65  ? 2896 ARG A CA    1 
ATOM   10778 C  C     . ARG A 1 2896 ? 154.233 161.781 218.381 1.00 33.13  ? 2896 ARG A C     1 
ATOM   10779 O  O     . ARG A 1 2896 ? 153.204 161.962 217.730 1.00 36.47  ? 2896 ARG A O     1 
ATOM   10780 C  CB    . ARG A 1 2896 ? 155.317 163.909 219.157 1.00 34.77  ? 2896 ARG A CB    1 
ATOM   10781 C  CG    . ARG A 1 2896 ? 155.513 164.918 220.278 1.00 38.22  ? 2896 ARG A CG    1 
ATOM   10782 C  CD    . ARG A 1 2896 ? 154.254 165.089 221.111 1.00 36.87  ? 2896 ARG A CD    1 
ATOM   10783 N  NE    . ARG A 1 2896 ? 153.216 165.820 220.396 1.00 38.44  ? 2896 ARG A NE    1 
ATOM   10784 C  CZ    . ARG A 1 2896 ? 151.927 165.784 220.706 1.00 44.81  ? 2896 ARG A CZ    1 
ATOM   10785 N  NH1   . ARG A 1 2896 ? 151.480 165.059 221.718 1.00 38.69  ? 2896 ARG A NH1   1 
ATOM   10786 N  NH2   . ARG A 1 2896 ? 151.066 166.493 219.982 1.00 47.48  ? 2896 ARG A NH2   1 
ATOM   10787 N  N     . LEU A 1 2897 ? 155.097 160.807 218.089 1.00 30.88  ? 2897 LEU A N     1 
ATOM   10788 C  CA    . LEU A 1 2897 ? 154.827 159.868 217.007 1.00 28.65  ? 2897 LEU A CA    1 
ATOM   10789 C  C     . LEU A 1 2897 ? 153.710 158.906 217.381 1.00 31.91  ? 2897 LEU A C     1 
ATOM   10790 O  O     . LEU A 1 2897 ? 152.919 158.505 216.523 1.00 35.51  ? 2897 LEU A O     1 
ATOM   10791 C  CB    . LEU A 1 2897 ? 156.099 159.100 216.649 1.00 28.71  ? 2897 LEU A CB    1 
ATOM   10792 C  CG    . LEU A 1 2897 ? 156.920 159.649 215.482 1.00 28.64  ? 2897 LEU A CG    1 
ATOM   10793 C  CD1   . LEU A 1 2897 ? 158.156 158.797 215.254 1.00 27.53  ? 2897 LEU A CD1   1 
ATOM   10794 C  CD2   . LEU A 1 2897 ? 156.076 159.720 214.222 1.00 30.75  ? 2897 LEU A CD2   1 
ATOM   10795 N  N     . LYS A 1 2898 ? 153.634 158.515 218.654 1.00 32.57  ? 2898 LYS A N     1 
ATOM   10796 C  CA    . LYS A 1 2898 ? 152.494 157.721 219.103 1.00 35.34  ? 2898 LYS A CA    1 
ATOM   10797 C  C     . LYS A 1 2898 ? 151.194 158.495 218.917 1.00 36.92  ? 2898 LYS A C     1 
ATOM   10798 O  O     . LYS A 1 2898 ? 150.199 157.959 218.408 1.00 41.77  ? 2898 LYS A O     1 
ATOM   10799 C  CB    . LYS A 1 2898 ? 152.676 157.312 220.565 1.00 39.25  ? 2898 LYS A CB    1 
ATOM   10800 C  CG    . LYS A 1 2898 ? 153.776 156.291 220.796 1.00 43.65  ? 2898 LYS A CG    1 
ATOM   10801 C  CD    . LYS A 1 2898 ? 153.986 156.037 222.279 1.00 50.71  ? 2898 LYS A CD    1 
ATOM   10802 C  CE    . LYS A 1 2898 ? 152.813 155.278 222.877 1.00 57.16  ? 2898 LYS A CE    1 
ATOM   10803 N  NZ    . LYS A 1 2898 ? 153.047 154.919 224.303 1.00 59.00  ? 2898 LYS A NZ    1 
ATOM   10804 N  N     . VAL A 1 2899 ? 151.193 159.773 219.306 1.00 38.03  ? 2899 VAL A N     1 
ATOM   10805 C  CA    . VAL A 1 2899 ? 150.003 160.600 219.099 1.00 37.27  ? 2899 VAL A CA    1 
ATOM   10806 C  C     . VAL A 1 2899 ? 149.710 160.756 217.609 1.00 35.55  ? 2899 VAL A C     1 
ATOM   10807 O  O     . VAL A 1 2899 ? 148.548 160.761 217.184 1.00 40.10  ? 2899 VAL A O     1 
ATOM   10808 C  CB    . VAL A 1 2899 ? 150.168 161.965 219.792 1.00 36.06  ? 2899 VAL A CB    1 
ATOM   10809 C  CG1   . VAL A 1 2899 ? 148.873 162.755 219.714 1.00 38.42  ? 2899 VAL A CG1   1 
ATOM   10810 C  CG2   . VAL A 1 2899 ? 150.580 161.774 221.240 1.00 36.68  ? 2899 VAL A CG2   1 
ATOM   10811 N  N     . PHE A 1 2900 ? 150.761 160.884 216.795 1.00 32.88  ? 2900 PHE A N     1 
ATOM   10812 C  CA    . PHE A 1 2900 ? 150.601 161.016 215.351 1.00 31.30  ? 2900 PHE A CA    1 
ATOM   10813 C  C     . PHE A 1 2900 ? 149.957 159.772 214.753 1.00 34.38  ? 2900 PHE A C     1 
ATOM   10814 O  O     . PHE A 1 2900 ? 149.097 159.870 213.871 1.00 37.63  ? 2900 PHE A O     1 
ATOM   10815 C  CB    . PHE A 1 2900 ? 151.968 161.283 214.717 1.00 26.93  ? 2900 PHE A CB    1 
ATOM   10816 C  CG    . PHE A 1 2900 ? 151.934 161.478 213.229 1.00 23.47  ? 2900 PHE A CG    1 
ATOM   10817 C  CD1   . PHE A 1 2900 ? 151.294 162.571 212.672 1.00 26.88  ? 2900 PHE A CD1   1 
ATOM   10818 C  CD2   . PHE A 1 2900 ? 152.562 160.575 212.388 1.00 24.26  ? 2900 PHE A CD2   1 
ATOM   10819 C  CE1   . PHE A 1 2900 ? 151.273 162.754 211.302 1.00 26.37  ? 2900 PHE A CE1   1 
ATOM   10820 C  CE2   . PHE A 1 2900 ? 152.542 160.752 211.019 1.00 25.48  ? 2900 PHE A CE2   1 
ATOM   10821 C  CZ    . PHE A 1 2900 ? 151.896 161.843 210.476 1.00 22.92  ? 2900 PHE A CZ    1 
ATOM   10822 N  N     . TYR A 1 2901 ? 150.371 158.592 215.216 1.00 36.22  ? 2901 TYR A N     1 
ATOM   10823 C  CA    . TYR A 1 2901 ? 149.728 157.356 214.784 1.00 34.90  ? 2901 TYR A CA    1 
ATOM   10824 C  C     . TYR A 1 2901 ? 148.267 157.327 215.208 1.00 41.01  ? 2901 TYR A C     1 
ATOM   10825 O  O     . TYR A 1 2901 ? 147.394 156.919 214.434 1.00 41.45  ? 2901 TYR A O     1 
ATOM   10826 C  CB    . TYR A 1 2901 ? 150.459 156.141 215.358 1.00 34.70  ? 2901 TYR A CB    1 
ATOM   10827 C  CG    . TYR A 1 2901 ? 151.934 156.064 215.037 1.00 33.38  ? 2901 TYR A CG    1 
ATOM   10828 C  CD1   . TYR A 1 2901 ? 152.451 156.646 213.889 1.00 34.01  ? 2901 TYR A CD1   1 
ATOM   10829 C  CD2   . TYR A 1 2901 ? 152.808 155.398 215.885 1.00 28.76  ? 2901 TYR A CD2   1 
ATOM   10830 C  CE1   . TYR A 1 2901 ? 153.800 156.574 213.600 1.00 33.08  ? 2901 TYR A CE1   1 
ATOM   10831 C  CE2   . TYR A 1 2901 ? 154.156 155.319 215.603 1.00 28.57  ? 2901 TYR A CE2   1 
ATOM   10832 C  CZ    . TYR A 1 2901 ? 154.647 155.907 214.460 1.00 33.05  ? 2901 TYR A CZ    1 
ATOM   10833 O  OH    . TYR A 1 2901 ? 155.991 155.828 214.178 1.00 36.02  ? 2901 TYR A OH    1 
ATOM   10834 N  N     . GLU A 1 2902 ? 147.985 157.751 216.444 1.00 48.04  ? 2902 GLU A N     1 
ATOM   10835 C  CA    . GLU A 1 2902 ? 146.613 157.703 216.942 1.00 45.14  ? 2902 GLU A CA    1 
ATOM   10836 C  C     . GLU A 1 2902 ? 145.687 158.615 216.144 1.00 43.96  ? 2902 GLU A C     1 
ATOM   10837 O  O     . GLU A 1 2902 ? 144.563 158.226 215.807 1.00 44.53  ? 2902 GLU A O     1 
ATOM   10838 C  CB    . GLU A 1 2902 ? 146.577 158.072 218.425 1.00 50.73  ? 2902 GLU A CB    1 
ATOM   10839 C  CG    . GLU A 1 2902 ? 147.259 157.064 219.333 1.00 57.91  ? 2902 GLU A CG    1 
ATOM   10840 C  CD    . GLU A 1 2902 ? 147.300 157.520 220.777 1.00 70.30  ? 2902 GLU A CD    1 
ATOM   10841 O  OE1   . GLU A 1 2902 ? 146.555 158.460 221.126 1.00 61.60  ? 2902 GLU A OE1   1 
ATOM   10842 O  OE2   . GLU A 1 2902 ? 148.077 156.939 221.564 1.00 72.36  ? 2902 GLU A OE2   1 
ATOM   10843 N  N     . GLU A 1 2903 ? 146.137 159.830 215.829 1.00 48.41  ? 2903 GLU A N     1 
ATOM   10844 C  CA    . GLU A 1 2903 ? 145.268 160.823 215.206 1.00 53.52  ? 2903 GLU A CA    1 
ATOM   10845 C  C     . GLU A 1 2903 ? 145.445 160.943 213.699 1.00 47.25  ? 2903 GLU A C     1 
ATOM   10846 O  O     . GLU A 1 2903 ? 144.484 161.284 213.002 1.00 47.91  ? 2903 GLU A O     1 
ATOM   10847 C  CB    . GLU A 1 2903 ? 145.496 162.200 215.840 1.00 56.52  ? 2903 GLU A CB    1 
ATOM   10848 C  CG    . GLU A 1 2903 ? 145.705 162.169 217.344 1.00 59.65  ? 2903 GLU A CG    1 
ATOM   10849 C  CD    . GLU A 1 2903 ? 145.317 163.472 218.012 1.00 74.93  ? 2903 GLU A CD    1 
ATOM   10850 O  OE1   . GLU A 1 2903 ? 144.715 163.424 219.106 1.00 84.29  ? 2903 GLU A OE1   1 
ATOM   10851 O  OE2   . GLU A 1 2903 ? 145.614 164.545 217.445 1.00 72.44  ? 2903 GLU A OE2   1 
ATOM   10852 N  N     . GLU A 1 2904 ? 146.637 160.674 213.180 1.00 46.86  ? 2904 GLU A N     1 
ATOM   10853 C  CA    . GLU A 1 2904 ? 146.940 160.880 211.768 1.00 40.75  ? 2904 GLU A CA    1 
ATOM   10854 C  C     . GLU A 1 2904 ? 147.506 159.579 211.204 1.00 42.90  ? 2904 GLU A C     1 
ATOM   10855 O  O     . GLU A 1 2904 ? 147.376 158.507 211.808 1.00 54.66  ? 2904 GLU A O     1 
ATOM   10856 C  CB    . GLU A 1 2904 ? 147.889 162.070 211.585 1.00 38.49  ? 2904 GLU A CB    1 
ATOM   10857 C  CG    . GLU A 1 2904 ? 147.316 163.400 212.046 1.00 49.27  ? 2904 GLU A CG    1 
ATOM   10858 C  CD    . GLU A 1 2904 ? 146.467 164.071 210.984 1.00 56.05  ? 2904 GLU A CD    1 
ATOM   10859 O  OE1   . GLU A 1 2904 ? 146.976 164.295 209.866 1.00 53.02  ? 2904 GLU A OE1   1 
ATOM   10860 O  OE2   . GLU A 1 2904 ? 145.290 164.378 211.268 1.00 61.22  ? 2904 GLU A OE2   1 
ATOM   10861 N  N     . LEU A 1 2905 ? 148.094 159.671 210.009 1.00 36.75  ? 2905 LEU A N     1 
ATOM   10862 C  CA    . LEU A 1 2905 ? 148.734 158.549 209.326 1.00 43.56  ? 2905 LEU A CA    1 
ATOM   10863 C  C     . LEU A 1 2905 ? 149.443 157.615 210.299 1.00 40.80  ? 2905 LEU A C     1 
ATOM   10864 O  O     . LEU A 1 2905 ? 150.252 158.050 211.122 1.00 37.25  ? 2905 LEU A O     1 
ATOM   10865 C  CB    . LEU A 1 2905 ? 149.733 159.085 208.298 1.00 38.54  ? 2905 LEU A CB    1 
ATOM   10866 C  CG    . LEU A 1 2905 ? 150.822 158.124 207.822 1.00 32.78  ? 2905 LEU A CG    1 
ATOM   10867 C  CD1   . LEU A 1 2905 ? 150.242 157.077 206.900 1.00 38.28  ? 2905 LEU A CD1   1 
ATOM   10868 C  CD2   . LEU A 1 2905 ? 151.942 158.890 207.134 1.00 28.52  ? 2905 LEU A CD2   1 
ATOM   10869 N  N     . ASP A 1 2906 ? 149.129 156.325 210.196 1.00 44.01  ? 2906 ASP A N     1 
ATOM   10870 C  CA    . ASP A 1 2906 ? 149.577 155.306 211.143 1.00 45.57  ? 2906 ASP A CA    1 
ATOM   10871 C  C     . ASP A 1 2906 ? 150.507 154.331 210.426 1.00 50.65  ? 2906 ASP A C     1 
ATOM   10872 O  O     . ASP A 1 2906 ? 150.067 153.299 209.913 1.00 59.61  ? 2906 ASP A O     1 
ATOM   10873 C  CB    . ASP A 1 2906 ? 148.377 154.582 211.761 1.00 47.01  ? 2906 ASP A CB    1 
ATOM   10874 C  CG    . ASP A 1 2906 ? 148.772 153.659 212.901 1.00 54.34  ? 2906 ASP A CG    1 
ATOM   10875 O  OD1   . ASP A 1 2906 ? 149.969 153.614 213.254 1.00 51.82  ? 2906 ASP A OD1   1 
ATOM   10876 O  OD2   . ASP A 1 2906 ? 147.880 152.974 213.444 1.00 59.44  ? 2906 ASP A OD2   1 
ATOM   10877 N  N     . VAL A 1 2907 ? 151.798 154.665 210.396 1.00 45.84  ? 2907 VAL A N     1 
ATOM   10878 C  CA    . VAL A 1 2907 ? 152.837 153.761 209.929 1.00 39.74  ? 2907 VAL A CA    1 
ATOM   10879 C  C     . VAL A 1 2907 ? 153.998 153.825 210.917 1.00 38.52  ? 2907 VAL A C     1 
ATOM   10880 O  O     . VAL A 1 2907 ? 154.545 154.905 211.157 1.00 39.94  ? 2907 VAL A O     1 
ATOM   10881 C  CB    . VAL A 1 2907 ? 153.315 154.083 208.501 1.00 35.83  ? 2907 VAL A CB    1 
ATOM   10882 C  CG1   . VAL A 1 2907 ? 152.224 153.755 207.493 1.00 34.12  ? 2907 VAL A CG1   1 
ATOM   10883 C  CG2   . VAL A 1 2907 ? 153.697 155.547 208.365 1.00 37.08  ? 2907 VAL A CG2   1 
ATOM   10884 N  N     . PRO A 1 2908 ? 154.380 152.716 211.549 1.00 35.87  ? 2908 PRO A N     1 
ATOM   10885 C  CA    . PRO A 1 2908 ? 155.471 152.768 212.530 1.00 35.11  ? 2908 PRO A CA    1 
ATOM   10886 C  C     . PRO A 1 2908 ? 156.777 153.227 211.897 1.00 37.36  ? 2908 PRO A C     1 
ATOM   10887 O  O     . PRO A 1 2908 ? 157.101 152.870 210.763 1.00 38.88  ? 2908 PRO A O     1 
ATOM   10888 C  CB    . PRO A 1 2908 ? 155.563 151.322 213.031 1.00 31.66  ? 2908 PRO A CB    1 
ATOM   10889 C  CG    . PRO A 1 2908 ? 154.205 150.757 212.787 1.00 38.72  ? 2908 PRO A CG    1 
ATOM   10890 C  CD    . PRO A 1 2908 ? 153.729 151.396 211.516 1.00 37.60  ? 2908 PRO A CD    1 
ATOM   10891 N  N     . LEU A 1 2909 ? 157.532 154.021 212.653 1.00 32.30  ? 2909 LEU A N     1 
ATOM   10892 C  CA    . LEU A 1 2909 ? 158.789 154.592 212.195 1.00 26.39  ? 2909 LEU A CA    1 
ATOM   10893 C  C     . LEU A 1 2909 ? 159.901 154.292 213.190 1.00 28.33  ? 2909 LEU A C     1 
ATOM   10894 O  O     . LEU A 1 2909 ? 159.650 154.020 214.368 1.00 32.01  ? 2909 LEU A O     1 
ATOM   10895 C  CB    . LEU A 1 2909 ? 158.674 156.107 211.998 1.00 25.14  ? 2909 LEU A CB    1 
ATOM   10896 C  CG    . LEU A 1 2909 ? 157.645 156.614 210.987 1.00 27.11  ? 2909 LEU A CG    1 
ATOM   10897 C  CD1   . LEU A 1 2909 ? 157.857 158.096 210.730 1.00 22.02  ? 2909 LEU A CD1   1 
ATOM   10898 C  CD2   . LEU A 1 2909 ? 157.728 155.834 209.689 1.00 27.62  ? 2909 LEU A CD2   1 
ATOM   10899 N  N     . VAL A 1 2910 ? 161.136 154.344 212.704 1.00 35.00  ? 2910 VAL A N     1 
ATOM   10900 C  CA    . VAL A 1 2910 ? 162.320 154.119 213.523 1.00 36.20  ? 2910 VAL A CA    1 
ATOM   10901 C  C     . VAL A 1 2910 ? 162.975 155.465 213.786 1.00 36.41  ? 2910 VAL A C     1 
ATOM   10902 O  O     . VAL A 1 2910 ? 163.163 156.263 212.860 1.00 37.37  ? 2910 VAL A O     1 
ATOM   10903 C  CB    . VAL A 1 2910 ? 163.305 153.160 212.839 1.00 34.43  ? 2910 VAL A CB    1 
ATOM   10904 C  CG1   . VAL A 1 2910 ? 164.549 152.961 213.708 1.00 36.65  ? 2910 VAL A CG1   1 
ATOM   10905 C  CG2   . VAL A 1 2910 ? 162.627 151.843 212.522 1.00 32.11  ? 2910 VAL A CG2   1 
ATOM   10906 N  N     . LEU A 1 2911 ? 163.327 155.717 215.042 1.00 30.49  ? 2911 LEU A N     1 
ATOM   10907 C  CA    . LEU A 1 2911 ? 163.970 156.969 215.428 1.00 32.18  ? 2911 LEU A CA    1 
ATOM   10908 C  C     . LEU A 1 2911 ? 165.460 156.718 215.614 1.00 37.99  ? 2911 LEU A C     1 
ATOM   10909 O  O     . LEU A 1 2911 ? 165.911 156.360 216.705 1.00 50.94  ? 2911 LEU A O     1 
ATOM   10910 C  CB    . LEU A 1 2911 ? 163.339 157.530 216.695 1.00 32.70  ? 2911 LEU A CB    1 
ATOM   10911 C  CG    . LEU A 1 2911 ? 161.927 158.090 216.552 1.00 34.07  ? 2911 LEU A CG    1 
ATOM   10912 C  CD1   . LEU A 1 2911 ? 161.502 158.740 217.850 1.00 37.73  ? 2911 LEU A CD1   1 
ATOM   10913 C  CD2   . LEU A 1 2911 ? 161.869 159.080 215.406 1.00 35.48  ? 2911 LEU A CD2   1 
ATOM   10914 N  N     . PHE A 1 2912 ? 166.228 156.894 214.546 1.00 27.17  ? 2912 PHE A N     1 
ATOM   10915 C  CA    . PHE A 1 2912 ? 167.677 156.944 214.638 1.00 28.33  ? 2912 PHE A CA    1 
ATOM   10916 C  C     . PHE A 1 2912 ? 168.132 158.399 214.551 1.00 32.84  ? 2912 PHE A C     1 
ATOM   10917 O  O     . PHE A 1 2912 ? 167.321 159.322 214.431 1.00 35.25  ? 2912 PHE A O     1 
ATOM   10918 C  CB    . PHE A 1 2912 ? 168.346 156.062 213.573 1.00 25.63  ? 2912 PHE A CB    1 
ATOM   10919 C  CG    . PHE A 1 2912 ? 167.778 156.206 212.186 1.00 25.09  ? 2912 PHE A CG    1 
ATOM   10920 C  CD1   . PHE A 1 2912 ? 166.613 155.550 211.824 1.00 25.45  ? 2912 PHE A CD1   1 
ATOM   10921 C  CD2   . PHE A 1 2912 ? 168.422 156.983 211.238 1.00 30.52  ? 2912 PHE A CD2   1 
ATOM   10922 C  CE1   . PHE A 1 2912 ? 166.100 155.670 210.549 1.00 24.84  ? 2912 PHE A CE1   1 
ATOM   10923 C  CE2   . PHE A 1 2912 ? 167.907 157.113 209.963 1.00 25.94  ? 2912 PHE A CE2   1 
ATOM   10924 C  CZ    . PHE A 1 2912 ? 166.749 156.451 209.618 1.00 22.95  ? 2912 PHE A CZ    1 
ATOM   10925 N  N     . ASN A 1 2913 ? 169.450 158.595 214.630 1.00 32.41  ? 2913 ASN A N     1 
ATOM   10926 C  CA    . ASN A 1 2913 ? 170.000 159.943 214.754 1.00 35.07  ? 2913 ASN A CA    1 
ATOM   10927 C  C     . ASN A 1 2913 ? 169.643 160.808 213.550 1.00 31.80  ? 2913 ASN A C     1 
ATOM   10928 O  O     . ASN A 1 2913 ? 169.298 161.989 213.701 1.00 34.46  ? 2913 ASN A O     1 
ATOM   10929 C  CB    . ASN A 1 2913 ? 171.517 159.867 214.929 1.00 47.90  ? 2913 ASN A CB    1 
ATOM   10930 C  CG    . ASN A 1 2913 ? 171.923 158.989 216.096 1.00 45.72  ? 2913 ASN A CG    1 
ATOM   10931 O  OD1   . ASN A 1 2913 ? 171.074 158.425 216.785 1.00 41.17  ? 2913 ASN A OD1   1 
ATOM   10932 N  ND2   . ASN A 1 2913 ? 173.227 158.861 216.319 1.00 42.71  ? 2913 ASN A ND2   1 
ATOM   10933 N  N     . GLU A 1 2914 ? 169.725 160.239 212.345 1.00 27.51  ? 2914 GLU A N     1 
ATOM   10934 C  CA    . GLU A 1 2914 ? 169.419 161.007 211.144 1.00 25.65  ? 2914 GLU A CA    1 
ATOM   10935 C  C     . GLU A 1 2914 ? 167.961 161.444 211.108 1.00 25.96  ? 2914 GLU A C     1 
ATOM   10936 O  O     . GLU A 1 2914 ? 167.661 162.541 210.626 1.00 33.51  ? 2914 GLU A O     1 
ATOM   10937 C  CB    . GLU A 1 2914 ? 169.771 160.195 209.898 1.00 28.87  ? 2914 GLU A CB    1 
ATOM   10938 C  CG    . GLU A 1 2914 ? 171.266 160.016 209.683 1.00 38.11  ? 2914 GLU A CG    1 
ATOM   10939 C  CD    . GLU A 1 2914 ? 171.823 158.798 210.394 1.00 50.55  ? 2914 GLU A CD    1 
ATOM   10940 O  OE1   . GLU A 1 2914 ? 171.696 158.716 211.634 1.00 44.57  ? 2914 GLU A OE1   1 
ATOM   10941 O  OE2   . GLU A 1 2914 ? 172.393 157.922 209.710 1.00 55.24  ? 2914 GLU A OE2   1 
ATOM   10942 N  N     . VAL A 1 2915 ? 167.043 160.615 211.609 1.00 20.62  ? 2915 VAL A N     1 
ATOM   10943 C  CA    . VAL A 1 2915 ? 165.642 161.025 211.670 1.00 18.27  ? 2915 VAL A CA    1 
ATOM   10944 C  C     . VAL A 1 2915 ? 165.478 162.236 212.576 1.00 22.88  ? 2915 VAL A C     1 
ATOM   10945 O  O     . VAL A 1 2915 ? 164.753 163.180 212.245 1.00 30.27  ? 2915 VAL A O     1 
ATOM   10946 C  CB    . VAL A 1 2915 ? 164.747 159.859 212.126 1.00 21.66  ? 2915 VAL A CB    1 
ATOM   10947 C  CG1   . VAL A 1 2915 ? 163.323 160.339 212.324 1.00 22.39  ? 2915 VAL A CG1   1 
ATOM   10948 C  CG2   . VAL A 1 2915 ? 164.762 158.767 211.096 1.00 27.24  ? 2915 VAL A CG2   1 
ATOM   10949 N  N     . LEU A 1 2916 ? 166.140 162.228 213.736 1.00 22.75  ? 2916 LEU A N     1 
ATOM   10950 C  CA    . LEU A 1 2916 ? 166.052 163.372 214.639 1.00 22.24  ? 2916 LEU A CA    1 
ATOM   10951 C  C     . LEU A 1 2916 ? 166.631 164.626 213.997 1.00 21.09  ? 2916 LEU A C     1 
ATOM   10952 O  O     . LEU A 1 2916 ? 166.033 165.709 214.072 1.00 23.05  ? 2916 LEU A O     1 
ATOM   10953 C  CB    . LEU A 1 2916 ? 166.765 163.058 215.953 1.00 25.90  ? 2916 LEU A CB    1 
ATOM   10954 C  CG    . LEU A 1 2916 ? 166.278 161.820 216.708 1.00 24.55  ? 2916 LEU A CG    1 
ATOM   10955 C  CD1   . LEU A 1 2916 ? 166.940 161.732 218.073 1.00 35.33  ? 2916 LEU A CD1   1 
ATOM   10956 C  CD2   . LEU A 1 2916 ? 164.764 161.833 216.845 1.00 25.69  ? 2916 LEU A CD2   1 
ATOM   10957 N  N     . ASP A 1 2917 ? 167.786 164.498 213.339 1.00 20.15  ? 2917 ASP A N     1 
ATOM   10958 C  CA    . ASP A 1 2917 ? 168.377 165.658 212.679 1.00 23.65  ? 2917 ASP A CA    1 
ATOM   10959 C  C     . ASP A 1 2917 ? 167.459 166.202 211.590 1.00 20.92  ? 2917 ASP A C     1 
ATOM   10960 O  O     . ASP A 1 2917 ? 167.247 167.417 211.492 1.00 22.96  ? 2917 ASP A O     1 
ATOM   10961 C  CB    . ASP A 1 2917 ? 169.743 165.290 212.101 1.00 28.32  ? 2917 ASP A CB    1 
ATOM   10962 C  CG    . ASP A 1 2917 ? 170.739 166.429 212.189 1.00 42.75  ? 2917 ASP A CG    1 
ATOM   10963 O  OD1   . ASP A 1 2917 ? 170.426 167.445 212.845 1.00 43.01  ? 2917 ASP A OD1   1 
ATOM   10964 O  OD2   . ASP A 1 2917 ? 171.835 166.309 211.604 1.00 43.75  ? 2917 ASP A OD2   1 
ATOM   10965 N  N     . HIS A 1 2918 ? 166.883 165.313 210.777 1.00 17.11  ? 2918 HIS A N     1 
ATOM   10966 C  CA    . HIS A 1 2918 ? 166.040 165.752 209.670 1.00 15.48  ? 2918 HIS A CA    1 
ATOM   10967 C  C     . HIS A 1 2918 ? 164.733 166.359 210.164 1.00 20.13  ? 2918 HIS A C     1 
ATOM   10968 O  O     . HIS A 1 2918 ? 164.250 167.346 209.595 1.00 26.84  ? 2918 HIS A O     1 
ATOM   10969 C  CB    . HIS A 1 2918 ? 165.774 164.581 208.727 1.00 16.02  ? 2918 HIS A CB    1 
ATOM   10970 C  CG    . HIS A 1 2918 ? 167.009 164.038 208.079 1.00 21.18  ? 2918 HIS A CG    1 
ATOM   10971 N  ND1   . HIS A 1 2918 ? 167.062 162.786 207.505 1.00 25.75  ? 2918 HIS A ND1   1 
ATOM   10972 C  CD2   . HIS A 1 2918 ? 168.241 164.577 207.920 1.00 22.59  ? 2918 HIS A CD2   1 
ATOM   10973 C  CE1   . HIS A 1 2918 ? 168.272 162.579 207.017 1.00 24.00  ? 2918 HIS A CE1   1 
ATOM   10974 N  NE2   . HIS A 1 2918 ? 169.007 163.650 207.256 1.00 20.87  ? 2918 HIS A NE2   1 
ATOM   10975 N  N     . VAL A 1 2919 ? 164.139 165.789 211.215 1.00 18.84  ? 2919 VAL A N     1 
ATOM   10976 C  CA    . VAL A 1 2919 ? 162.903 166.354 211.745 1.00 17.26  ? 2919 VAL A CA    1 
ATOM   10977 C  C     . VAL A 1 2919 ? 163.174 167.722 212.359 1.00 18.22  ? 2919 VAL A C     1 
ATOM   10978 O  O     . VAL A 1 2919 ? 162.361 168.645 212.227 1.00 22.23  ? 2919 VAL A O     1 
ATOM   10979 C  CB    . VAL A 1 2919 ? 162.235 165.382 212.742 1.00 17.76  ? 2919 VAL A CB    1 
ATOM   10980 C  CG1   . VAL A 1 2919 ? 163.056 165.205 213.998 1.00 17.16  ? 2919 VAL A CG1   1 
ATOM   10981 C  CG2   . VAL A 1 2919 ? 160.842 165.847 213.100 1.00 22.81  ? 2919 VAL A CG2   1 
ATOM   10982 N  N     . LEU A 1 2920 ? 164.337 167.892 213.000 1.00 16.48  ? 2920 LEU A N     1 
ATOM   10983 C  CA    . LEU A 1 2920 ? 164.702 169.212 213.507 1.00 16.40  ? 2920 LEU A CA    1 
ATOM   10984 C  C     . LEU A 1 2920 ? 164.892 170.210 212.370 1.00 18.82  ? 2920 LEU A C     1 
ATOM   10985 O  O     . LEU A 1 2920 ? 164.464 171.365 212.476 1.00 23.15  ? 2920 LEU A O     1 
ATOM   10986 C  CB    . LEU A 1 2920 ? 165.964 169.116 214.362 1.00 17.98  ? 2920 LEU A CB    1 
ATOM   10987 C  CG    . LEU A 1 2920 ? 165.777 168.504 215.752 1.00 16.77  ? 2920 LEU A CG    1 
ATOM   10988 C  CD1   . LEU A 1 2920 ? 166.993 168.766 216.623 1.00 19.01  ? 2920 LEU A CD1   1 
ATOM   10989 C  CD2   . LEU A 1 2920 ? 164.518 169.039 216.411 1.00 16.90  ? 2920 LEU A CD2   1 
ATOM   10990 N  N     . ARG A 1 2921 ? 165.529 169.786 211.274 1.00 19.33  ? 2921 ARG A N     1 
ATOM   10991 C  CA    . ARG A 1 2921 ? 165.704 170.680 210.129 1.00 16.62  ? 2921 ARG A CA    1 
ATOM   10992 C  C     . ARG A 1 2921 ? 164.363 171.095 209.533 1.00 17.66  ? 2921 ARG A C     1 
ATOM   10993 O  O     . ARG A 1 2921 ? 164.152 172.271 209.205 1.00 21.76  ? 2921 ARG A O     1 
ATOM   10994 C  CB    . ARG A 1 2921 ? 166.567 170.008 209.063 1.00 17.05  ? 2921 ARG A CB    1 
ATOM   10995 C  CG    . ARG A 1 2921 ? 167.988 169.706 209.492 1.00 19.55  ? 2921 ARG A CG    1 
ATOM   10996 C  CD    . ARG A 1 2921 ? 168.720 168.930 208.413 1.00 22.21  ? 2921 ARG A CD    1 
ATOM   10997 N  NE    . ARG A 1 2921 ? 169.860 168.191 208.942 1.00 25.08  ? 2921 ARG A NE    1 
ATOM   10998 C  CZ    . ARG A 1 2921 ? 170.637 167.398 208.219 1.00 32.91  ? 2921 ARG A CZ    1 
ATOM   10999 N  NH1   . ARG A 1 2921 ? 170.428 167.218 206.926 1.00 33.62  ? 2921 ARG A NH1   1 
ATOM   11000 N  NH2   . ARG A 1 2921 ? 171.651 166.771 208.808 1.00 35.81  ? 2921 ARG A NH2   1 
ATOM   11001 N  N     . ILE A 1 2922 ? 163.447 170.139 209.374 1.00 17.79  ? 2922 ILE A N     1 
ATOM   11002 C  CA    . ILE A 1 2922 ? 162.148 170.452 208.788 1.00 18.57  ? 2922 ILE A CA    1 
ATOM   11003 C  C     . ILE A 1 2922 ? 161.349 171.359 209.717 1.00 18.66  ? 2922 ILE A C     1 
ATOM   11004 O  O     . ILE A 1 2922 ? 160.635 172.260 209.261 1.00 21.70  ? 2922 ILE A O     1 
ATOM   11005 C  CB    . ILE A 1 2922 ? 161.386 169.158 208.449 1.00 19.16  ? 2922 ILE A CB    1 
ATOM   11006 C  CG1   . ILE A 1 2922 ? 162.168 168.337 207.423 1.00 18.48  ? 2922 ILE A CG1   1 
ATOM   11007 C  CG2   . ILE A 1 2922 ? 160.014 169.478 207.888 1.00 16.29  ? 2922 ILE A CG2   1 
ATOM   11008 C  CD1   . ILE A 1 2922 ? 161.587 166.966 207.168 1.00 16.93  ? 2922 ILE A CD1   1 
ATOM   11009 N  N     . ASP A 1 2923 ? 161.461 171.145 211.031 1.00 19.29  ? 2923 ASP A N     1 
ATOM   11010 C  CA    . ASP A 1 2923 ? 160.821 172.046 211.984 1.00 18.87  ? 2923 ASP A CA    1 
ATOM   11011 C  C     . ASP A 1 2923 ? 161.404 173.450 211.884 1.00 22.25  ? 2923 ASP A C     1 
ATOM   11012 O  O     . ASP A 1 2923 ? 160.677 174.446 211.974 1.00 23.44  ? 2923 ASP A O     1 
ATOM   11013 C  CB    . ASP A 1 2923 ? 160.972 171.500 213.403 1.00 23.63  ? 2923 ASP A CB    1 
ATOM   11014 C  CG    . ASP A 1 2923 ? 160.572 172.508 214.460 1.00 37.09  ? 2923 ASP A CG    1 
ATOM   11015 O  OD1   . ASP A 1 2923 ? 161.441 172.903 215.266 1.00 38.47  ? 2923 ASP A OD1   1 
ATOM   11016 O  OD2   . ASP A 1 2923 ? 159.389 172.906 214.484 1.00 41.56  ? 2923 ASP A OD2   1 
ATOM   11017 N  N     . ARG A 1 2924 ? 162.724 173.544 211.709 1.00 24.56  ? 2924 ARG A N     1 
ATOM   11018 C  CA    . ARG A 1 2924 ? 163.364 174.843 211.530 1.00 22.12  ? 2924 ARG A CA    1 
ATOM   11019 C  C     . ARG A 1 2924 ? 162.810 175.561 210.308 1.00 22.87  ? 2924 ARG A C     1 
ATOM   11020 O  O     . ARG A 1 2924 ? 162.513 176.760 210.356 1.00 24.36  ? 2924 ARG A O     1 
ATOM   11021 C  CB    . ARG A 1 2924 ? 164.876 174.665 211.395 1.00 22.51  ? 2924 ARG A CB    1 
ATOM   11022 C  CG    . ARG A 1 2924 ? 165.640 174.672 212.700 1.00 27.60  ? 2924 ARG A CG    1 
ATOM   11023 C  CD    . ARG A 1 2924 ? 167.136 174.656 212.435 1.00 30.05  ? 2924 ARG A CD    1 
ATOM   11024 N  NE    . ARG A 1 2924 ? 167.484 175.427 211.248 1.00 32.29  ? 2924 ARG A NE    1 
ATOM   11025 C  CZ    . ARG A 1 2924 ? 168.078 176.612 211.273 1.00 31.89  ? 2924 ARG A CZ    1 
ATOM   11026 N  NH1   . ARG A 1 2924 ? 168.407 177.197 212.413 1.00 23.59  ? 2924 ARG A NH1   1 
ATOM   11027 N  NH2   . ARG A 1 2924 ? 168.349 177.226 210.125 1.00 37.89  ? 2924 ARG A NH2   1 
ATOM   11028 N  N     . ILE A 1 2925 ? 162.670 174.838 209.197 1.00 26.61  ? 2925 ILE A N     1 
ATOM   11029 C  CA    . ILE A 1 2925 ? 162.201 175.471 207.967 1.00 24.79  ? 2925 ILE A CA    1 
ATOM   11030 C  C     . ILE A 1 2925 ? 160.732 175.864 208.083 1.00 23.75  ? 2925 ILE A C     1 
ATOM   11031 O  O     . ILE A 1 2925 ? 160.324 176.932 207.611 1.00 26.86  ? 2925 ILE A O     1 
ATOM   11032 C  CB    . ILE A 1 2925 ? 162.450 174.554 206.757 1.00 22.89  ? 2925 ILE A CB    1 
ATOM   11033 C  CG1   . ILE A 1 2925 ? 163.938 174.221 206.642 1.00 28.57  ? 2925 ILE A CG1   1 
ATOM   11034 C  CG2   . ILE A 1 2925 ? 161.970 175.225 205.483 1.00 18.81  ? 2925 ILE A CG2   1 
ATOM   11035 C  CD1   . ILE A 1 2925 ? 164.842 175.430 206.746 1.00 26.26  ? 2925 ILE A CD1   1 
ATOM   11036 N  N     . PHE A 1 2926 ? 159.914 175.018 208.714 1.00 24.23  ? 2926 PHE A N     1 
ATOM   11037 C  CA    . PHE A 1 2926 ? 158.483 175.292 208.802 1.00 22.72  ? 2926 PHE A CA    1 
ATOM   11038 C  C     . PHE A 1 2926 ? 158.160 176.476 209.706 1.00 26.83  ? 2926 PHE A C     1 
ATOM   11039 O  O     . PHE A 1 2926 ? 157.025 176.962 209.681 1.00 27.06  ? 2926 PHE A O     1 
ATOM   11040 C  CB    . PHE A 1 2926 ? 157.735 174.053 209.294 1.00 17.34  ? 2926 PHE A CB    1 
ATOM   11041 C  CG    . PHE A 1 2926 ? 157.423 173.062 208.211 1.00 15.34  ? 2926 PHE A CG    1 
ATOM   11042 C  CD1   . PHE A 1 2926 ? 157.610 173.389 206.880 1.00 22.24  ? 2926 PHE A CD1   1 
ATOM   11043 C  CD2   . PHE A 1 2926 ? 156.934 171.808 208.524 1.00 14.72  ? 2926 PHE A CD2   1 
ATOM   11044 C  CE1   . PHE A 1 2926 ? 157.320 172.478 205.883 1.00 24.16  ? 2926 PHE A CE1   1 
ATOM   11045 C  CE2   . PHE A 1 2926 ? 156.644 170.894 207.533 1.00 16.05  ? 2926 PHE A CE2   1 
ATOM   11046 C  CZ    . PHE A 1 2926 ? 156.836 171.229 206.211 1.00 19.79  ? 2926 PHE A CZ    1 
ATOM   11047 N  N     . ARG A 1 2927 ? 159.121 176.948 210.502 1.00 28.68  ? 2927 ARG A N     1 
ATOM   11048 C  CA    . ARG A 1 2927 ? 158.907 178.069 211.408 1.00 26.14  ? 2927 ARG A CA    1 
ATOM   11049 C  C     . ARG A 1 2927 ? 159.345 179.402 210.812 1.00 27.57  ? 2927 ARG A C     1 
ATOM   11050 O  O     . ARG A 1 2927 ? 159.630 180.346 211.560 1.00 30.81  ? 2927 ARG A O     1 
ATOM   11051 C  CB    . ARG A 1 2927 ? 159.630 177.819 212.731 1.00 25.61  ? 2927 ARG A CB    1 
ATOM   11052 C  CG    . ARG A 1 2927 ? 158.913 176.859 213.663 1.00 27.47  ? 2927 ARG A CG    1 
ATOM   11053 C  CD    . ARG A 1 2927 ? 159.637 176.742 214.995 1.00 32.14  ? 2927 ARG A CD    1 
ATOM   11054 N  NE    . ARG A 1 2927 ? 161.003 176.257 214.835 1.00 34.32  ? 2927 ARG A NE    1 
ATOM   11055 C  CZ    . ARG A 1 2927 ? 162.086 177.012 214.954 1.00 35.26  ? 2927 ARG A CZ    1 
ATOM   11056 N  NH1   . ARG A 1 2927 ? 162.002 178.301 215.240 1.00 36.25  ? 2927 ARG A NH1   1 
ATOM   11057 N  NH2   . ARG A 1 2927 ? 163.284 176.461 214.780 1.00 33.77  ? 2927 ARG A NH2   1 
ATOM   11058 N  N     . GLN A 1 2928 ? 159.405 179.506 209.489 1.00 28.41  ? 2928 GLN A N     1 
ATOM   11059 C  CA    . GLN A 1 2928 ? 159.853 180.720 208.828 1.00 29.04  ? 2928 GLN A CA    1 
ATOM   11060 C  C     . GLN A 1 2928 ? 158.810 181.189 207.828 1.00 28.02  ? 2928 GLN A C     1 
ATOM   11061 O  O     . GLN A 1 2928 ? 158.139 180.369 207.191 1.00 28.51  ? 2928 GLN A O     1 
ATOM   11062 C  CB    . GLN A 1 2928 ? 161.186 180.493 208.101 1.00 25.49  ? 2928 GLN A CB    1 
ATOM   11063 C  CG    . GLN A 1 2928 ? 162.411 180.613 208.987 1.00 28.48  ? 2928 GLN A CG    1 
ATOM   11064 C  CD    . GLN A 1 2928 ? 163.583 179.806 208.465 1.00 39.49  ? 2928 GLN A CD    1 
ATOM   11065 O  OE1   . GLN A 1 2928 ? 163.853 179.788 207.264 1.00 38.67  ? 2928 GLN A OE1   1 
ATOM   11066 N  NE2   . GLN A 1 2928 ? 164.286 179.131 209.367 1.00 43.30  ? 2928 GLN A NE2   1 
ATOM   11067 N  N     . PRO A 1 2929 ? 158.650 182.503 207.668 1.00 27.73  ? 2929 PRO A N     1 
ATOM   11068 C  CA    . PRO A 1 2929 ? 157.750 183.011 206.625 1.00 25.24  ? 2929 PRO A CA    1 
ATOM   11069 C  C     . PRO A 1 2929 ? 158.348 182.774 205.247 1.00 26.54  ? 2929 PRO A C     1 
ATOM   11070 O  O     . PRO A 1 2929 ? 159.535 183.019 205.020 1.00 23.36  ? 2929 PRO A O     1 
ATOM   11071 C  CB    . PRO A 1 2929 ? 157.639 184.505 206.949 1.00 28.06  ? 2929 PRO A CB    1 
ATOM   11072 C  CG    . PRO A 1 2929 ? 158.912 184.823 207.657 1.00 31.88  ? 2929 PRO A CG    1 
ATOM   11073 C  CD    . PRO A 1 2929 ? 159.273 183.590 208.443 1.00 30.67  ? 2929 PRO A CD    1 
ATOM   11074 N  N     . GLN A 1 2930 ? 157.510 182.294 204.325 1.00 32.32  ? 2930 GLN A N     1 
ATOM   11075 C  CA    . GLN A 1 2930 ? 157.950 181.901 202.985 1.00 26.92  ? 2930 GLN A CA    1 
ATOM   11076 C  C     . GLN A 1 2930 ? 159.080 180.877 203.059 1.00 21.76  ? 2930 GLN A C     1 
ATOM   11077 O  O     . GLN A 1 2930 ? 160.026 180.909 202.269 1.00 21.06  ? 2930 GLN A O     1 
ATOM   11078 C  CB    . GLN A 1 2930 ? 158.369 183.118 202.156 1.00 24.03  ? 2930 GLN A CB    1 
ATOM   11079 C  CG    . GLN A 1 2930 ? 158.016 183.016 200.683 1.00 23.96  ? 2930 GLN A CG    1 
ATOM   11080 C  CD    . GLN A 1 2930 ? 158.560 184.175 199.874 1.00 28.88  ? 2930 GLN A CD    1 
ATOM   11081 O  OE1   . GLN A 1 2930 ? 159.144 185.110 200.422 1.00 32.26  ? 2930 GLN A OE1   1 
ATOM   11082 N  NE2   . GLN A 1 2930 ? 158.371 184.121 198.561 1.00 29.95  ? 2930 GLN A NE2   1 
ATOM   11083 N  N     . GLY A 1 2931 ? 158.981 179.963 204.020 1.00 21.24  ? 2931 GLY A N     1 
ATOM   11084 C  CA    . GLY A 1 2931 ? 159.992 178.942 204.200 1.00 18.91  ? 2931 GLY A CA    1 
ATOM   11085 C  C     . GLY A 1 2931 ? 159.667 177.666 203.456 1.00 21.00  ? 2931 GLY A C     1 
ATOM   11086 O  O     . GLY A 1 2931 ? 158.877 176.844 203.930 1.00 21.90  ? 2931 GLY A O     1 
ATOM   11087 N  N     . HIS A 1 2932 ? 160.273 177.490 202.290 1.00 22.06  ? 2932 HIS A N     1 
ATOM   11088 C  CA    . HIS A 1 2932 ? 160.036 176.330 201.448 1.00 16.23  ? 2932 HIS A CA    1 
ATOM   11089 C  C     . HIS A 1 2932 ? 161.144 175.301 201.634 1.00 14.76  ? 2932 HIS A C     1 
ATOM   11090 O  O     . HIS A 1 2932 ? 162.224 175.600 202.150 1.00 17.80  ? 2932 HIS A O     1 
ATOM   11091 C  CB    . HIS A 1 2932 ? 159.935 176.745 199.979 1.00 19.13  ? 2932 HIS A CB    1 
ATOM   11092 C  CG    . HIS A 1 2932 ? 158.944 177.838 199.730 1.00 19.21  ? 2932 HIS A CG    1 
ATOM   11093 N  ND1   . HIS A 1 2932 ? 157.619 177.737 200.095 1.00 19.03  ? 2932 HIS A ND1   1 
ATOM   11094 C  CD2   . HIS A 1 2932 ? 159.085 179.056 199.158 1.00 21.99  ? 2932 HIS A CD2   1 
ATOM   11095 C  CE1   . HIS A 1 2932 ? 156.985 178.845 199.754 1.00 19.81  ? 2932 HIS A CE1   1 
ATOM   11096 N  NE2   . HIS A 1 2932 ? 157.852 179.662 199.184 1.00 24.10  ? 2932 HIS A NE2   1 
ATOM   11097 N  N     . LEU A 1 2933 ? 160.862 174.075 201.203 1.00 16.71  ? 2933 LEU A N     1 
ATOM   11098 C  CA    . LEU A 1 2933 ? 161.759 172.951 201.408 1.00 14.21  ? 2933 LEU A CA    1 
ATOM   11099 C  C     . LEU A 1 2933 ? 162.053 172.262 200.085 1.00 16.48  ? 2933 LEU A C     1 
ATOM   11100 O  O     . LEU A 1 2933 ? 161.217 172.234 199.178 1.00 21.80  ? 2933 LEU A O     1 
ATOM   11101 C  CB    . LEU A 1 2933 ? 161.166 171.934 202.388 1.00 15.54  ? 2933 LEU A CB    1 
ATOM   11102 C  CG    . LEU A 1 2933 ? 161.616 172.038 203.843 1.00 16.97  ? 2933 LEU A CG    1 
ATOM   11103 C  CD1   . LEU A 1 2933 ? 160.846 171.060 204.708 1.00 20.38  ? 2933 LEU A CD1   1 
ATOM   11104 C  CD2   . LEU A 1 2933 ? 163.107 171.798 203.951 1.00 15.18  ? 2933 LEU A CD2   1 
ATOM   11105 N  N     . LEU A 1 2934 ? 163.259 171.702 199.986 1.00 16.00  ? 2934 LEU A N     1 
ATOM   11106 C  CA    . LEU A 1 2934 ? 163.664 170.877 198.846 1.00 15.78  ? 2934 LEU A CA    1 
ATOM   11107 C  C     . LEU A 1 2934 ? 164.418 169.678 199.418 1.00 16.48  ? 2934 LEU A C     1 
ATOM   11108 O  O     . LEU A 1 2934 ? 165.631 169.738 199.635 1.00 21.38  ? 2934 LEU A O     1 
ATOM   11109 C  CB    . LEU A 1 2934 ? 164.512 171.659 197.851 1.00 16.92  ? 2934 LEU A CB    1 
ATOM   11110 C  CG    . LEU A 1 2934 ? 165.022 170.863 196.647 1.00 16.74  ? 2934 LEU A CG    1 
ATOM   11111 C  CD1   . LEU A 1 2934 ? 163.872 170.180 195.927 1.00 15.91  ? 2934 LEU A CD1   1 
ATOM   11112 C  CD2   . LEU A 1 2934 ? 165.794 171.756 195.694 1.00 20.41  ? 2934 LEU A CD2   1 
ATOM   11113 N  N     . LEU A 1 2935 ? 163.689 168.595 199.669 1.00 14.54  ? 2935 LEU A N     1 
ATOM   11114 C  CA    . LEU A 1 2935 ? 164.272 167.375 200.211 1.00 14.85  ? 2935 LEU A CA    1 
ATOM   11115 C  C     . LEU A 1 2935 ? 164.710 166.481 199.059 1.00 20.07  ? 2935 LEU A C     1 
ATOM   11116 O  O     . LEU A 1 2935 ? 163.903 166.144 198.187 1.00 24.93  ? 2935 LEU A O     1 
ATOM   11117 C  CB    . LEU A 1 2935 ? 163.271 166.649 201.108 1.00 16.42  ? 2935 LEU A CB    1 
ATOM   11118 C  CG    . LEU A 1 2935 ? 162.618 167.488 202.207 1.00 19.00  ? 2935 LEU A CG    1 
ATOM   11119 C  CD1   . LEU A 1 2935 ? 161.659 166.642 203.025 1.00 18.42  ? 2935 LEU A CD1   1 
ATOM   11120 C  CD2   . LEU A 1 2935 ? 163.676 168.115 203.099 1.00 19.12  ? 2935 LEU A CD2   1 
ATOM   11121 N  N     . ILE A 1 2936 ? 165.984 166.101 199.055 1.00 19.35  ? 2936 ILE A N     1 
ATOM   11122 C  CA    . ILE A 1 2936 ? 166.557 165.270 198.005 1.00 18.86  ? 2936 ILE A CA    1 
ATOM   11123 C  C     . ILE A 1 2936 ? 167.050 163.975 198.633 1.00 20.66  ? 2936 ILE A C     1 
ATOM   11124 O  O     . ILE A 1 2936 ? 167.855 164.000 199.572 1.00 23.33  ? 2936 ILE A O     1 
ATOM   11125 C  CB    . ILE A 1 2936 ? 167.696 165.994 197.265 1.00 19.62  ? 2936 ILE A CB    1 
ATOM   11126 C  CG1   . ILE A 1 2936 ? 167.207 167.340 196.731 1.00 19.37  ? 2936 ILE A CG1   1 
ATOM   11127 C  CG2   . ILE A 1 2936 ? 168.220 165.138 196.130 1.00 22.95  ? 2936 ILE A CG2   1 
ATOM   11128 C  CD1   . ILE A 1 2936 ? 168.275 168.140 196.027 1.00 23.76  ? 2936 ILE A CD1   1 
ATOM   11129 N  N     . GLY A 1 2937 ? 166.568 162.854 198.116 1.00 22.32  ? 2937 GLY A N     1 
ATOM   11130 C  CA    . GLY A 1 2937 ? 166.953 161.556 198.637 1.00 22.12  ? 2937 GLY A CA    1 
ATOM   11131 C  C     . GLY A 1 2937 ? 166.207 160.468 197.899 1.00 23.54  ? 2937 GLY A C     1 
ATOM   11132 O  O     . GLY A 1 2937 ? 165.294 160.732 197.109 1.00 24.12  ? 2937 GLY A O     1 
ATOM   11133 N  N     . VAL A 1 2938 ? 166.615 159.229 198.170 1.00 23.57  ? 2938 VAL A N     1 
ATOM   11134 C  CA    . VAL A 1 2938 ? 165.999 158.084 197.514 1.00 23.28  ? 2938 VAL A CA    1 
ATOM   11135 C  C     . VAL A 1 2938 ? 164.567 157.913 198.006 1.00 25.20  ? 2938 VAL A C     1 
ATOM   11136 O  O     . VAL A 1 2938 ? 164.193 158.381 199.089 1.00 27.61  ? 2938 VAL A O     1 
ATOM   11137 C  CB    . VAL A 1 2938 ? 166.826 156.808 197.758 1.00 19.25  ? 2938 VAL A CB    1 
ATOM   11138 C  CG1   . VAL A 1 2938 ? 168.215 156.957 197.161 1.00 26.95  ? 2938 VAL A CG1   1 
ATOM   11139 C  CG2   . VAL A 1 2938 ? 166.912 156.515 199.244 1.00 17.63  ? 2938 VAL A CG2   1 
ATOM   11140 N  N     . SER A 1 2939 ? 163.752 157.245 197.194 1.00 21.21  ? 2939 SER A N     1 
ATOM   11141 C  CA    . SER A 1 2939 ? 162.373 156.982 197.574 1.00 21.06  ? 2939 SER A CA    1 
ATOM   11142 C  C     . SER A 1 2939 ? 162.319 155.998 198.736 1.00 18.46  ? 2939 SER A C     1 
ATOM   11143 O  O     . SER A 1 2939 ? 163.157 155.102 198.862 1.00 20.28  ? 2939 SER A O     1 
ATOM   11144 C  CB    . SER A 1 2939 ? 161.586 156.435 196.384 1.00 30.91  ? 2939 SER A CB    1 
ATOM   11145 O  OG    . SER A 1 2939 ? 161.544 157.376 195.327 1.00 40.30  ? 2939 SER A OG    1 
ATOM   11146 N  N     . GLY A 1 2940 ? 161.322 156.177 199.597 1.00 19.55  ? 2940 GLY A N     1 
ATOM   11147 C  CA    . GLY A 1 2940 ? 161.190 155.341 200.770 1.00 17.98  ? 2940 GLY A CA    1 
ATOM   11148 C  C     . GLY A 1 2940 ? 162.116 155.690 201.910 1.00 20.73  ? 2940 GLY A C     1 
ATOM   11149 O  O     . GLY A 1 2940 ? 162.223 154.909 202.862 1.00 24.59  ? 2940 GLY A O     1 
ATOM   11150 N  N     . ALA A 1 2941 ? 162.791 156.835 201.848 1.00 18.91  ? 2941 ALA A N     1 
ATOM   11151 C  CA    . ALA A 1 2941 ? 163.713 157.258 202.892 1.00 19.88  ? 2941 ALA A CA    1 
ATOM   11152 C  C     . ALA A 1 2941 ? 163.030 158.040 204.006 1.00 23.83  ? 2941 ALA A C     1 
ATOM   11153 O  O     . ALA A 1 2941 ? 163.696 158.412 204.977 1.00 25.91  ? 2941 ALA A O     1 
ATOM   11154 C  CB    . ALA A 1 2941 ? 164.841 158.100 202.290 1.00 18.50  ? 2941 ALA A CB    1 
ATOM   11155 N  N     . GLY A 1 2942 ? 161.731 158.295 203.894 1.00 22.93  ? 2942 GLY A N     1 
ATOM   11156 C  CA    . GLY A 1 2942 ? 160.997 158.995 204.925 1.00 19.61  ? 2942 GLY A CA    1 
ATOM   11157 C  C     . GLY A 1 2942 ? 160.779 160.473 204.698 1.00 20.51  ? 2942 GLY A C     1 
ATOM   11158 O  O     . GLY A 1 2942 ? 160.345 161.159 205.629 1.00 23.77  ? 2942 GLY A O     1 
ATOM   11159 N  N     . LYS A 1 2943 ? 161.058 160.986 203.499 1.00 17.31  ? 2943 LYS A N     1 
ATOM   11160 C  CA    . LYS A 1 2943 ? 160.945 162.423 203.264 1.00 15.24  ? 2943 LYS A CA    1 
ATOM   11161 C  C     . LYS A 1 2943 ? 159.510 162.906 203.444 1.00 16.70  ? 2943 LYS A C     1 
ATOM   11162 O  O     . LYS A 1 2943 ? 159.246 163.833 204.220 1.00 18.86  ? 2943 LYS A O     1 
ATOM   11163 C  CB    . LYS A 1 2943 ? 161.452 162.759 201.861 1.00 17.58  ? 2943 LYS A CB    1 
ATOM   11164 C  CG    . LYS A 1 2943 ? 162.861 162.267 201.577 1.00 20.24  ? 2943 LYS A CG    1 
ATOM   11165 C  CD    . LYS A 1 2943 ? 163.397 162.839 200.277 1.00 19.66  ? 2943 LYS A CD    1 
ATOM   11166 C  CE    . LYS A 1 2943 ? 162.553 162.404 199.092 1.00 21.94  ? 2943 LYS A CE    1 
ATOM   11167 N  NZ    . LYS A 1 2943 ? 162.653 160.940 198.847 1.00 23.87  ? 2943 LYS A NZ    1 
ATOM   11168 N  N     . THR A 1 2944 ? 158.562 162.270 202.752 1.00 17.62  ? 2944 THR A N     1 
ATOM   11169 C  CA    . THR A 1 2944 ? 157.171 162.705 202.840 1.00 14.16  ? 2944 THR A CA    1 
ATOM   11170 C  C     . THR A 1 2944 ? 156.585 162.412 204.215 1.00 15.38  ? 2944 THR A C     1 
ATOM   11171 O  O     . THR A 1 2944 ? 155.835 163.229 204.761 1.00 20.82  ? 2944 THR A O     1 
ATOM   11172 C  CB    . THR A 1 2944 ? 156.336 162.035 201.749 1.00 18.13  ? 2944 THR A CB    1 
ATOM   11173 O  OG1   . THR A 1 2944 ? 156.926 162.291 200.469 1.00 26.33  ? 2944 THR A OG1   1 
ATOM   11174 C  CG2   . THR A 1 2944 ? 154.914 162.574 201.758 1.00 15.54  ? 2944 THR A CG2   1 
ATOM   11175 N  N     . THR A 1 2945 ? 156.912 161.254 204.791 1.00 17.40  ? 2945 THR A N     1 
ATOM   11176 C  CA    . THR A 1 2945 ? 156.388 160.917 206.110 1.00 17.06  ? 2945 THR A CA    1 
ATOM   11177 C  C     . THR A 1 2945 ? 156.903 161.879 207.173 1.00 15.80  ? 2945 THR A C     1 
ATOM   11178 O  O     . THR A 1 2945 ? 156.133 162.345 208.021 1.00 17.79  ? 2945 THR A O     1 
ATOM   11179 C  CB    . THR A 1 2945 ? 156.750 159.476 206.469 1.00 18.63  ? 2945 THR A CB    1 
ATOM   11180 O  OG1   . THR A 1 2945 ? 156.419 158.614 205.374 1.00 26.68  ? 2945 THR A OG1   1 
ATOM   11181 C  CG2   . THR A 1 2945 ? 155.981 159.030 207.699 1.00 16.25  ? 2945 THR A CG2   1 
ATOM   11182 N  N     . LEU A 1 2946 ? 158.200 162.199 207.139 1.00 13.57  ? 2946 LEU A N     1 
ATOM   11183 C  CA    . LEU A 1 2946 ? 158.742 163.163 208.090 1.00 12.98  ? 2946 LEU A CA    1 
ATOM   11184 C  C     . LEU A 1 2946 ? 158.154 164.551 207.867 1.00 15.82  ? 2946 LEU A C     1 
ATOM   11185 O  O     . LEU A 1 2946 ? 157.877 165.272 208.831 1.00 17.66  ? 2946 LEU A O     1 
ATOM   11186 C  CB    . LEU A 1 2946 ? 160.267 163.205 207.998 1.00 13.05  ? 2946 LEU A CB    1 
ATOM   11187 C  CG    . LEU A 1 2946 ? 161.026 162.028 208.616 1.00 15.67  ? 2946 LEU A CG    1 
ATOM   11188 C  CD1   . LEU A 1 2946 ? 162.502 162.359 208.759 1.00 19.23  ? 2946 LEU A CD1   1 
ATOM   11189 C  CD2   . LEU A 1 2946 ? 160.428 161.642 209.959 1.00 15.73  ? 2946 LEU A CD2   1 
ATOM   11190 N  N     . SER A 1 2947 ? 157.963 164.947 206.605 1.00 15.47  ? 2947 SER A N     1 
ATOM   11191 C  CA    . SER A 1 2947 ? 157.355 166.245 206.332 1.00 13.12  ? 2947 SER A CA    1 
ATOM   11192 C  C     . SER A 1 2947 ? 155.941 166.321 206.897 1.00 14.75  ? 2947 SER A C     1 
ATOM   11193 O  O     . SER A 1 2947 ? 155.562 167.326 207.510 1.00 18.89  ? 2947 SER A O     1 
ATOM   11194 C  CB    . SER A 1 2947 ? 157.349 166.516 204.829 1.00 12.34  ? 2947 SER A CB    1 
ATOM   11195 O  OG    . SER A 1 2947 ? 158.629 166.289 204.267 1.00 15.53  ? 2947 SER A OG    1 
ATOM   11196 N  N     . ARG A 1 2948 ? 155.151 165.261 206.710 1.00 13.84  ? 2948 ARG A N     1 
ATOM   11197 C  CA    . ARG A 1 2948 ? 153.801 165.232 207.264 1.00 13.75  ? 2948 ARG A CA    1 
ATOM   11198 C  C     . ARG A 1 2948 ? 153.829 165.248 208.787 1.00 16.51  ? 2948 ARG A C     1 
ATOM   11199 O  O     . ARG A 1 2948 ? 153.007 165.917 209.425 1.00 18.48  ? 2948 ARG A O     1 
ATOM   11200 C  CB    . ARG A 1 2948 ? 153.050 164.002 206.755 1.00 16.15  ? 2948 ARG A CB    1 
ATOM   11201 C  CG    . ARG A 1 2948 ? 152.795 164.006 205.259 1.00 20.61  ? 2948 ARG A CG    1 
ATOM   11202 C  CD    . ARG A 1 2948 ? 152.066 162.750 204.818 1.00 22.49  ? 2948 ARG A CD    1 
ATOM   11203 N  NE    . ARG A 1 2948 ? 150.671 162.752 205.238 1.00 31.58  ? 2948 ARG A NE    1 
ATOM   11204 C  CZ    . ARG A 1 2948 ? 149.732 161.975 204.717 1.00 45.04  ? 2948 ARG A CZ    1 
ATOM   11205 N  NH1   . ARG A 1 2948 ? 150.005 161.115 203.749 1.00 44.72  ? 2948 ARG A NH1   1 
ATOM   11206 N  NH2   . ARG A 1 2948 ? 148.488 162.062 205.178 1.00 52.76  ? 2948 ARG A NH2   1 
ATOM   11207 N  N     . PHE A 1 2949 ? 154.770 164.515 209.388 1.00 15.68  ? 2949 PHE A N     1 
ATOM   11208 C  CA    . PHE A 1 2949 ? 154.880 164.497 210.843 1.00 16.37  ? 2949 PHE A CA    1 
ATOM   11209 C  C     . PHE A 1 2949 ? 155.206 165.881 211.389 1.00 16.15  ? 2949 PHE A C     1 
ATOM   11210 O  O     . PHE A 1 2949 ? 154.624 166.315 212.389 1.00 18.69  ? 2949 PHE A O     1 
ATOM   11211 C  CB    . PHE A 1 2949 ? 155.940 163.482 211.272 1.00 15.34  ? 2949 PHE A CB    1 
ATOM   11212 C  CG    . PHE A 1 2949 ? 156.293 163.549 212.730 1.00 16.22  ? 2949 PHE A CG    1 
ATOM   11213 C  CD1   . PHE A 1 2949 ? 155.320 163.388 213.700 1.00 18.17  ? 2949 PHE A CD1   1 
ATOM   11214 C  CD2   . PHE A 1 2949 ? 157.600 163.768 213.129 1.00 20.02  ? 2949 PHE A CD2   1 
ATOM   11215 C  CE1   . PHE A 1 2949 ? 155.643 163.447 215.042 1.00 20.27  ? 2949 PHE A CE1   1 
ATOM   11216 C  CE2   . PHE A 1 2949 ? 157.930 163.828 214.469 1.00 19.80  ? 2949 PHE A CE2   1 
ATOM   11217 C  CZ    . PHE A 1 2949 ? 156.950 163.668 215.426 1.00 21.12  ? 2949 PHE A CZ    1 
ATOM   11218 N  N     . VAL A 1 2950 ? 156.129 166.593 210.740 1.00 14.66  ? 2950 VAL A N     1 
ATOM   11219 C  CA    . VAL A 1 2950 ? 156.489 167.929 211.207 1.00 14.94  ? 2950 VAL A CA    1 
ATOM   11220 C  C     . VAL A 1 2950 ? 155.338 168.902 210.989 1.00 18.95  ? 2950 VAL A C     1 
ATOM   11221 O  O     . VAL A 1 2950 ? 155.068 169.763 211.835 1.00 24.18  ? 2950 VAL A O     1 
ATOM   11222 C  CB    . VAL A 1 2950 ? 157.775 168.418 210.518 1.00 15.37  ? 2950 VAL A CB    1 
ATOM   11223 C  CG1   . VAL A 1 2950 ? 158.156 169.785 211.039 1.00 19.77  ? 2950 VAL A CG1   1 
ATOM   11224 C  CG2   . VAL A 1 2950 ? 158.900 167.446 210.748 1.00 14.56  ? 2950 VAL A CG2   1 
ATOM   11225 N  N     . ALA A 1 2951 ? 154.646 168.790 209.851 1.00 16.95  ? 2951 ALA A N     1 
ATOM   11226 C  CA    . ALA A 1 2951 ? 153.505 169.662 209.595 1.00 13.49  ? 2951 ALA A CA    1 
ATOM   11227 C  C     . ALA A 1 2951 ? 152.413 169.455 210.636 1.00 20.83  ? 2951 ALA A C     1 
ATOM   11228 O  O     . ALA A 1 2951 ? 151.782 170.418 211.085 1.00 26.79  ? 2951 ALA A O     1 
ATOM   11229 C  CB    . ALA A 1 2951 ? 152.963 169.419 208.188 1.00 14.72  ? 2951 ALA A CB    1 
ATOM   11230 N  N     . TRP A 1 2952 ? 152.172 168.202 211.026 1.00 21.67  ? 2952 TRP A N     1 
ATOM   11231 C  CA    . TRP A 1 2952 ? 151.242 167.937 212.118 1.00 21.98  ? 2952 TRP A CA    1 
ATOM   11232 C  C     . TRP A 1 2952 ? 151.762 168.507 213.432 1.00 24.00  ? 2952 TRP A C     1 
ATOM   11233 O  O     . TRP A 1 2952 ? 150.984 169.026 214.242 1.00 30.82  ? 2952 TRP A O     1 
ATOM   11234 C  CB    . TRP A 1 2952 ? 150.993 166.434 212.238 1.00 26.31  ? 2952 TRP A CB    1 
ATOM   11235 C  CG    . TRP A 1 2952 ? 150.229 166.041 213.462 1.00 28.87  ? 2952 TRP A CG    1 
ATOM   11236 C  CD1   . TRP A 1 2952 ? 148.875 166.063 213.625 1.00 30.83  ? 2952 TRP A CD1   1 
ATOM   11237 C  CD2   . TRP A 1 2952 ? 150.773 165.554 214.693 1.00 26.05  ? 2952 TRP A CD2   1 
ATOM   11238 N  NE1   . TRP A 1 2952 ? 148.542 165.625 214.883 1.00 30.88  ? 2952 TRP A NE1   1 
ATOM   11239 C  CE2   . TRP A 1 2952 ? 149.690 165.307 215.559 1.00 30.43  ? 2952 TRP A CE2   1 
ATOM   11240 C  CE3   . TRP A 1 2952 ? 152.071 165.306 215.149 1.00 23.76  ? 2952 TRP A CE3   1 
ATOM   11241 C  CZ2   . TRP A 1 2952 ? 149.866 164.823 216.853 1.00 33.84  ? 2952 TRP A CZ2   1 
ATOM   11242 C  CZ3   . TRP A 1 2952 ? 152.243 164.826 216.433 1.00 26.89  ? 2952 TRP A CZ3   1 
ATOM   11243 C  CH2   . TRP A 1 2952 ? 151.147 164.590 217.270 1.00 31.28  ? 2952 TRP A CH2   1 
ATOM   11244 N  N     . MET A 1 2953 ? 153.074 168.411 213.664 1.00 20.86  ? 2953 MET A N     1 
ATOM   11245 C  CA    . MET A 1 2953 ? 153.663 168.968 214.878 1.00 20.35  ? 2953 MET A CA    1 
ATOM   11246 C  C     . MET A 1 2953 ? 153.501 170.482 214.940 1.00 23.43  ? 2953 MET A C     1 
ATOM   11247 O  O     . MET A 1 2953 ? 153.172 171.035 215.996 1.00 25.70  ? 2953 MET A O     1 
ATOM   11248 C  CB    . MET A 1 2953 ? 155.140 168.590 214.962 1.00 19.43  ? 2953 MET A CB    1 
ATOM   11249 C  CG    . MET A 1 2953 ? 155.397 167.186 215.460 1.00 20.32  ? 2953 MET A CG    1 
ATOM   11250 S  SD    . MET A 1 2953 ? 156.893 167.130 216.456 1.00 40.63  ? 2953 MET A SD    1 
ATOM   11251 C  CE    . MET A 1 2953 ? 156.226 167.555 218.058 1.00 35.80  ? 2953 MET A CE    1 
ATOM   11252 N  N     . ASN A 1 2954 ? 153.728 171.169 213.825 1.00 22.82  ? 2954 ASN A N     1 
ATOM   11253 C  CA    . ASN A 1 2954 ? 153.683 172.624 213.784 1.00 24.77  ? 2954 ASN A CA    1 
ATOM   11254 C  C     . ASN A 1 2954 ? 152.300 173.166 213.454 1.00 28.21  ? 2954 ASN A C     1 
ATOM   11255 O  O     . ASN A 1 2954 ? 152.144 174.381 213.301 1.00 34.04  ? 2954 ASN A O     1 
ATOM   11256 C  CB    . ASN A 1 2954 ? 154.704 173.155 212.775 1.00 23.49  ? 2954 ASN A CB    1 
ATOM   11257 C  CG    . ASN A 1 2954 ? 156.124 173.099 213.301 1.00 28.14  ? 2954 ASN A CG    1 
ATOM   11258 O  OD1   . ASN A 1 2954 ? 156.418 173.604 214.383 1.00 35.47  ? 2954 ASN A OD1   1 
ATOM   11259 N  ND2   . ASN A 1 2954 ? 157.015 172.485 212.533 1.00 24.53  ? 2954 ASN A ND2   1 
ATOM   11260 N  N     . GLY A 1 2955 ? 151.298 172.299 213.336 1.00 23.20  ? 2955 GLY A N     1 
ATOM   11261 C  CA    . GLY A 1 2955 ? 149.950 172.733 213.045 1.00 20.57  ? 2955 GLY A CA    1 
ATOM   11262 C  C     . GLY A 1 2955 ? 149.648 172.967 211.583 1.00 23.90  ? 2955 GLY A C     1 
ATOM   11263 O  O     . GLY A 1 2955 ? 148.511 173.329 211.256 1.00 28.44  ? 2955 GLY A O     1 
ATOM   11264 N  N     . LEU A 1 2956 ? 150.620 172.779 210.695 1.00 24.50  ? 2956 LEU A N     1 
ATOM   11265 C  CA    . LEU A 1 2956 ? 150.370 172.943 209.272 1.00 24.03  ? 2956 LEU A CA    1 
ATOM   11266 C  C     . LEU A 1 2956 ? 149.464 171.829 208.762 1.00 25.22  ? 2956 LEU A C     1 
ATOM   11267 O  O     . LEU A 1 2956 ? 149.453 170.714 209.289 1.00 27.97  ? 2956 LEU A O     1 
ATOM   11268 C  CB    . LEU A 1 2956 ? 151.681 172.943 208.485 1.00 21.16  ? 2956 LEU A CB    1 
ATOM   11269 C  CG    . LEU A 1 2956 ? 152.904 173.685 209.032 1.00 20.63  ? 2956 LEU A CG    1 
ATOM   11270 C  CD1   . LEU A 1 2956 ? 153.988 173.736 207.971 1.00 18.78  ? 2956 LEU A CD1   1 
ATOM   11271 C  CD2   . LEU A 1 2956 ? 152.556 175.086 209.499 1.00 28.23  ? 2956 LEU A CD2   1 
ATOM   11272 N  N     . SER A 1 2957 ? 148.695 172.142 207.725 1.00 27.66  ? 2957 SER A N     1 
ATOM   11273 C  CA    . SER A 1 2957 ? 147.810 171.177 207.087 1.00 30.01  ? 2957 SER A CA    1 
ATOM   11274 C  C     . SER A 1 2957 ? 148.494 170.634 205.840 1.00 28.42  ? 2957 SER A C     1 
ATOM   11275 O  O     . SER A 1 2957 ? 148.861 171.402 204.944 1.00 31.23  ? 2957 SER A O     1 
ATOM   11276 C  CB    . SER A 1 2957 ? 146.467 171.815 206.732 1.00 35.73  ? 2957 SER A CB    1 
ATOM   11277 O  OG    . SER A 1 2957 ? 145.933 172.524 207.836 1.00 40.32  ? 2957 SER A OG    1 
ATOM   11278 N  N     . VAL A 1 2958 ? 148.665 169.319 205.786 1.00 26.05  ? 2958 VAL A N     1 
ATOM   11279 C  CA    . VAL A 1 2958 ? 149.345 168.683 204.664 1.00 24.20  ? 2958 VAL A CA    1 
ATOM   11280 C  C     . VAL A 1 2958 ? 148.422 168.683 203.455 1.00 24.75  ? 2958 VAL A C     1 
ATOM   11281 O  O     . VAL A 1 2958 ? 147.263 168.260 203.541 1.00 29.77  ? 2958 VAL A O     1 
ATOM   11282 C  CB    . VAL A 1 2958 ? 149.778 167.255 205.030 1.00 22.76  ? 2958 VAL A CB    1 
ATOM   11283 C  CG1   . VAL A 1 2958 ? 150.375 166.555 203.820 1.00 24.51  ? 2958 VAL A CG1   1 
ATOM   11284 C  CG2   . VAL A 1 2958 ? 150.769 167.280 206.179 1.00 22.27  ? 2958 VAL A CG2   1 
ATOM   11285 N  N     . TYR A 1 2959 ? 148.931 169.164 202.323 1.00 22.83  ? 2959 TYR A N     1 
ATOM   11286 C  CA    . TYR A 1 2959 ? 148.205 169.131 201.062 1.00 26.15  ? 2959 TYR A CA    1 
ATOM   11287 C  C     . TYR A 1 2959 ? 149.088 168.496 200.001 1.00 30.70  ? 2959 TYR A C     1 
ATOM   11288 O  O     . TYR A 1 2959 ? 150.227 168.927 199.796 1.00 33.07  ? 2959 TYR A O     1 
ATOM   11289 C  CB    . TYR A 1 2959 ? 147.776 170.535 200.620 1.00 23.96  ? 2959 TYR A CB    1 
ATOM   11290 C  CG    . TYR A 1 2959 ? 146.820 170.537 199.446 1.00 31.54  ? 2959 TYR A CG    1 
ATOM   11291 C  CD1   . TYR A 1 2959 ? 147.290 170.463 198.141 1.00 32.64  ? 2959 TYR A CD1   1 
ATOM   11292 C  CD2   . TYR A 1 2959 ? 145.448 170.609 199.643 1.00 33.54  ? 2959 TYR A CD2   1 
ATOM   11293 C  CE1   . TYR A 1 2959 ? 146.421 170.461 197.067 1.00 34.15  ? 2959 TYR A CE1   1 
ATOM   11294 C  CE2   . TYR A 1 2959 ? 144.572 170.610 198.575 1.00 32.91  ? 2959 TYR A CE2   1 
ATOM   11295 C  CZ    . TYR A 1 2959 ? 145.064 170.536 197.290 1.00 36.23  ? 2959 TYR A CZ    1 
ATOM   11296 O  OH    . TYR A 1 2959 ? 144.195 170.536 196.223 1.00 45.51  ? 2959 TYR A OH    1 
ATOM   11297 N  N     . GLN A 1 2960 ? 148.562 167.476 199.331 1.00 28.50  ? 2960 GLN A N     1 
ATOM   11298 C  CA    . GLN A 1 2960 ? 149.233 166.835 198.211 1.00 30.78  ? 2960 GLN A CA    1 
ATOM   11299 C  C     . GLN A 1 2960 ? 148.257 166.722 197.051 1.00 38.58  ? 2960 GLN A C     1 
ATOM   11300 O  O     . GLN A 1 2960 ? 147.090 166.368 197.244 1.00 44.37  ? 2960 GLN A O     1 
ATOM   11301 C  CB    . GLN A 1 2960 ? 149.763 165.446 198.586 1.00 30.02  ? 2960 GLN A CB    1 
ATOM   11302 C  CG    . GLN A 1 2960 ? 150.555 165.407 199.881 1.00 27.80  ? 2960 GLN A CG    1 
ATOM   11303 C  CD    . GLN A 1 2960 ? 150.947 164.000 200.278 1.00 31.71  ? 2960 GLN A CD    1 
ATOM   11304 O  OE1   . GLN A 1 2960 ? 150.597 163.528 201.360 1.00 38.03  ? 2960 GLN A OE1   1 
ATOM   11305 N  NE2   . GLN A 1 2960 ? 151.678 163.320 199.403 1.00 26.05  ? 2960 GLN A NE2   1 
ATOM   11306 N  N     . ILE A 1 2961 ? 148.736 167.026 195.846 1.00 37.95  ? 2961 ILE A N     1 
ATOM   11307 C  CA    . ILE A 1 2961 ? 147.887 166.933 194.667 1.00 42.22  ? 2961 ILE A CA    1 
ATOM   11308 C  C     . ILE A 1 2961 ? 147.686 165.469 194.304 1.00 47.24  ? 2961 ILE A C     1 
ATOM   11309 O  O     . ILE A 1 2961 ? 148.638 164.678 194.278 1.00 47.10  ? 2961 ILE A O     1 
ATOM   11310 C  CB    . ILE A 1 2961 ? 148.485 167.736 193.501 1.00 44.38  ? 2961 ILE A CB    1 
ATOM   11311 C  CG1   . ILE A 1 2961 ? 149.896 167.251 193.165 1.00 46.54  ? 2961 ILE A CG1   1 
ATOM   11312 C  CG2   . ILE A 1 2961 ? 148.497 169.222 193.831 1.00 47.88  ? 2961 ILE A CG2   1 
ATOM   11313 C  CD1   . ILE A 1 2961 ? 150.588 168.082 192.108 1.00 54.01  ? 2961 ILE A CD1   1 
ATOM   11314 N  N     . LYS A 1 2962 ? 146.434 165.093 194.047 1.00 55.54  ? 2962 LYS A N     1 
ATOM   11315 C  CA    . LYS A 1 2962 ? 146.089 163.716 193.697 1.00 57.88  ? 2962 LYS A CA    1 
ATOM   11316 C  C     . LYS A 1 2962 ? 146.252 163.564 192.191 1.00 56.64  ? 2962 LYS A C     1 
ATOM   11317 O  O     . LYS A 1 2962 ? 145.340 163.840 191.410 1.00 56.06  ? 2962 LYS A O     1 
ATOM   11318 C  CB    . LYS A 1 2962 ? 144.676 163.381 194.156 1.00 56.48  ? 2962 LYS A CB    1 
ATOM   11319 C  CG    . LYS A 1 2962 ? 144.506 163.347 195.669 1.00 57.28  ? 2962 LYS A CG    1 
ATOM   11320 C  CD    . LYS A 1 2962 ? 145.731 162.765 196.358 1.00 54.84  ? 2962 LYS A CD    1 
ATOM   11321 C  CE    . LYS A 1 2962 ? 145.458 162.479 197.826 1.00 63.19  ? 2962 LYS A CE    1 
ATOM   11322 N  NZ    . LYS A 1 2962 ? 145.030 163.702 198.559 1.00 69.83  ? 2962 LYS A NZ    1 
ATOM   11323 N  N     . VAL A 1 2963 ? 147.434 163.117 191.781 1.00 48.06  ? 2963 VAL A N     1 
ATOM   11324 C  CA    . VAL A 1 2963 ? 147.765 163.005 190.366 1.00 48.35  ? 2963 VAL A CA    1 
ATOM   11325 C  C     . VAL A 1 2963 ? 147.272 161.664 189.839 1.00 53.26  ? 2963 VAL A C     1 
ATOM   11326 O  O     . VAL A 1 2963 ? 147.532 160.613 190.436 1.00 54.49  ? 2963 VAL A O     1 
ATOM   11327 C  CB    . VAL A 1 2963 ? 149.278 163.164 190.150 1.00 45.91  ? 2963 VAL A CB    1 
ATOM   11328 C  CG1   . VAL A 1 2963 ? 149.669 162.723 188.749 1.00 48.18  ? 2963 VAL A CG1   1 
ATOM   11329 C  CG2   . VAL A 1 2963 ? 149.699 164.604 190.398 1.00 48.23  ? 2963 VAL A CG2   1 
ATOM   11330 N  N     . HIS A 1 2964 ? 146.548 161.699 188.720 1.00 52.74  ? 2964 HIS A N     1 
ATOM   11331 C  CA    . HIS A 1 2964 ? 146.136 160.478 188.040 1.00 53.39  ? 2964 HIS A CA    1 
ATOM   11332 C  C     . HIS A 1 2964 ? 146.518 160.548 186.567 1.00 63.34  ? 2964 HIS A C     1 
ATOM   11333 O  O     . HIS A 1 2964 ? 147.229 161.468 186.149 1.00 64.68  ? 2964 HIS A O     1 
ATOM   11334 C  CB    . HIS A 1 2964 ? 144.632 160.243 188.203 1.00 54.10  ? 2964 HIS A CB    1 
ATOM   11335 C  CG    . HIS A 1 2964 ? 143.795 161.452 187.927 1.00 55.86  ? 2964 HIS A CG    1 
ATOM   11336 N  ND1   . HIS A 1 2964 ? 143.571 161.928 186.653 1.00 59.99  ? 2964 HIS A ND1   1 
ATOM   11337 C  CD2   . HIS A 1 2964 ? 143.118 162.277 188.760 1.00 56.43  ? 2964 HIS A CD2   1 
ATOM   11338 C  CE1   . HIS A 1 2964 ? 142.797 162.996 186.714 1.00 62.90  ? 2964 HIS A CE1   1 
ATOM   11339 N  NE2   . HIS A 1 2964 ? 142.508 163.230 187.981 1.00 66.01  ? 2964 HIS A NE2   1 
ATOM   11340 N  N     . ARG A 1 2965 ? 146.064 159.575 185.774 1.00 65.73  ? 2965 ARG A N     1 
ATOM   11341 C  CA    . ARG A 1 2965 ? 146.425 159.540 184.360 1.00 67.35  ? 2965 ARG A CA    1 
ATOM   11342 C  C     . ARG A 1 2965 ? 145.850 160.735 183.609 1.00 64.98  ? 2965 ARG A C     1 
ATOM   11343 O  O     . ARG A 1 2965 ? 146.534 161.349 182.782 1.00 60.06  ? 2965 ARG A O     1 
ATOM   11344 C  CB    . ARG A 1 2965 ? 145.951 158.231 183.732 1.00 75.24  ? 2965 ARG A CB    1 
ATOM   11345 C  CG    . ARG A 1 2965 ? 146.308 158.083 182.262 1.00 79.07  ? 2965 ARG A CG    1 
ATOM   11346 C  CD    . ARG A 1 2965 ? 145.843 156.740 181.737 1.00 73.17  ? 2965 ARG A CD    1 
ATOM   11347 N  NE    . ARG A 1 2965 ? 146.324 155.654 182.580 1.00 74.01  ? 2965 ARG A NE    1 
ATOM   11348 C  CZ    . ARG A 1 2965 ? 145.601 154.599 182.927 1.00 75.10  ? 2965 ARG A CZ    1 
ATOM   11349 N  NH1   . ARG A 1 2965 ? 144.355 154.448 182.510 1.00 74.74  ? 2965 ARG A NH1   1 
ATOM   11350 N  NH2   . ARG A 1 2965 ? 146.141 153.675 183.716 1.00 72.86  ? 2965 ARG A NH2   1 
ATOM   11351 N  N     . LYS A 1 2966 ? 144.594 161.080 183.883 1.00 65.41  ? 2966 LYS A N     1 
ATOM   11352 C  CA    . LYS A 1 2966 ? 143.928 162.179 183.197 1.00 67.48  ? 2966 LYS A CA    1 
ATOM   11353 C  C     . LYS A 1 2966 ? 144.272 163.543 183.784 1.00 66.37  ? 2966 LYS A C     1 
ATOM   11354 O  O     . LYS A 1 2966 ? 143.595 164.526 183.463 1.00 69.57  ? 2966 LYS A O     1 
ATOM   11355 C  CB    . LYS A 1 2966 ? 142.411 161.971 183.222 1.00 75.68  ? 2966 LYS A CB    1 
ATOM   11356 C  CG    . LYS A 1 2966 ? 141.942 160.763 182.427 1.00 75.87  ? 2966 LYS A CG    1 
ATOM   11357 C  CD    . LYS A 1 2966 ? 140.426 160.668 182.408 1.00 76.84  ? 2966 LYS A CD    1 
ATOM   11358 C  CE    . LYS A 1 2966 ? 139.798 161.964 181.920 1.00 76.93  ? 2966 LYS A CE    1 
ATOM   11359 N  NZ    . LYS A 1 2966 ? 139.760 162.036 180.433 1.00 71.08  ? 2966 LYS A NZ    1 
ATOM   11360 N  N     . TYR A 1 2967 ? 145.293 163.624 184.631 1.00 62.74  ? 2967 TYR A N     1 
ATOM   11361 C  CA    . TYR A 1 2967 ? 145.712 164.904 185.184 1.00 59.40  ? 2967 TYR A CA    1 
ATOM   11362 C  C     . TYR A 1 2967 ? 146.282 165.792 184.086 1.00 66.19  ? 2967 TYR A C     1 
ATOM   11363 O  O     . TYR A 1 2967 ? 147.043 165.337 183.227 1.00 67.71  ? 2967 TYR A O     1 
ATOM   11364 C  CB    . TYR A 1 2967 ? 146.752 164.688 186.282 1.00 53.80  ? 2967 TYR A CB    1 
ATOM   11365 C  CG    . TYR A 1 2967 ? 146.692 165.694 187.407 1.00 51.76  ? 2967 TYR A CG    1 
ATOM   11366 C  CD1   . TYR A 1 2967 ? 145.720 165.606 188.392 1.00 53.35  ? 2967 TYR A CD1   1 
ATOM   11367 C  CD2   . TYR A 1 2967 ? 147.616 166.727 187.489 1.00 50.21  ? 2967 TYR A CD2   1 
ATOM   11368 C  CE1   . TYR A 1 2967 ? 145.664 166.522 189.425 1.00 52.72  ? 2967 TYR A CE1   1 
ATOM   11369 C  CE2   . TYR A 1 2967 ? 147.569 167.647 188.518 1.00 48.62  ? 2967 TYR A CE2   1 
ATOM   11370 C  CZ    . TYR A 1 2967 ? 146.592 167.539 189.482 1.00 51.44  ? 2967 TYR A CZ    1 
ATOM   11371 O  OH    . TYR A 1 2967 ? 146.541 168.453 190.508 1.00 55.78  ? 2967 TYR A OH    1 
ATOM   11372 N  N     . THR A 1 2968 ? 145.908 167.070 184.115 1.00 64.21  ? 2968 THR A N     1 
ATOM   11373 C  CA    . THR A 1 2968 ? 146.362 168.036 183.126 1.00 59.83  ? 2968 THR A CA    1 
ATOM   11374 C  C     . THR A 1 2968 ? 146.690 169.346 183.829 1.00 60.57  ? 2968 THR A C     1 
ATOM   11375 O  O     . THR A 1 2968 ? 146.593 169.459 185.055 1.00 57.76  ? 2968 THR A O     1 
ATOM   11376 C  CB    . THR A 1 2968 ? 145.313 168.246 182.027 1.00 60.33  ? 2968 THR A CB    1 
ATOM   11377 O  OG1   . THR A 1 2968 ? 145.854 169.086 181.000 1.00 64.20  ? 2968 THR A OG1   1 
ATOM   11378 C  CG2   . THR A 1 2968 ? 144.063 168.895 182.599 1.00 58.52  ? 2968 THR A CG2   1 
ATOM   11379 N  N     . GLY A 1 2969 ? 147.088 170.344 183.037 1.00 61.86  ? 2969 GLY A N     1 
ATOM   11380 C  CA    . GLY A 1 2969 ? 147.443 171.634 183.602 1.00 59.60  ? 2969 GLY A CA    1 
ATOM   11381 C  C     . GLY A 1 2969 ? 146.284 172.332 184.286 1.00 60.76  ? 2969 GLY A C     1 
ATOM   11382 O  O     . GLY A 1 2969 ? 146.483 173.053 185.267 1.00 64.37  ? 2969 GLY A O     1 
ATOM   11383 N  N     . GLU A 1 2970 ? 145.065 172.142 183.776 1.00 57.87  ? 2970 GLU A N     1 
ATOM   11384 C  CA    . GLU A 1 2970 ? 143.899 172.771 184.389 1.00 58.24  ? 2970 GLU A CA    1 
ATOM   11385 C  C     . GLU A 1 2970 ? 143.649 172.231 185.793 1.00 60.18  ? 2970 GLU A C     1 
ATOM   11386 O  O     . GLU A 1 2970 ? 143.284 172.989 186.699 1.00 63.41  ? 2970 GLU A O     1 
ATOM   11387 C  CB    . GLU A 1 2970 ? 142.670 172.568 183.504 1.00 71.14  ? 2970 GLU A CB    1 
ATOM   11388 C  CG    . GLU A 1 2970 ? 142.941 172.673 182.003 1.00 76.05  ? 2970 GLU A CG    1 
ATOM   11389 C  CD    . GLU A 1 2970 ? 143.142 174.102 181.516 1.00 90.07  ? 2970 GLU A CD    1 
ATOM   11390 O  OE1   . GLU A 1 2970 ? 143.441 174.995 182.336 1.00 89.09  ? 2970 GLU A OE1   1 
ATOM   11391 O  OE2   . GLU A 1 2970 ? 142.999 174.332 180.297 1.00 95.34  ? 2970 GLU A OE2   1 
ATOM   11392 N  N     . ASP A 1 2971 ? 143.833 170.923 185.991 1.00 56.96  ? 2971 ASP A N     1 
ATOM   11393 C  CA    . ASP A 1 2971 ? 143.674 170.351 187.325 1.00 53.33  ? 2971 ASP A CA    1 
ATOM   11394 C  C     . ASP A 1 2971 ? 144.714 170.905 188.289 1.00 52.66  ? 2971 ASP A C     1 
ATOM   11395 O  O     . ASP A 1 2971 ? 144.404 171.196 189.451 1.00 50.60  ? 2971 ASP A O     1 
ATOM   11396 C  CB    . ASP A 1 2971 ? 143.760 168.826 187.257 1.00 59.56  ? 2971 ASP A CB    1 
ATOM   11397 C  CG    . ASP A 1 2971 ? 142.605 168.211 186.494 1.00 69.37  ? 2971 ASP A CG    1 
ATOM   11398 O  OD1   . ASP A 1 2971 ? 141.471 168.225 187.017 1.00 72.73  ? 2971 ASP A OD1   1 
ATOM   11399 O  OD2   . ASP A 1 2971 ? 142.830 167.711 185.372 1.00 68.65  ? 2971 ASP A OD2   1 
ATOM   11400 N  N     . PHE A 1 2972 ? 145.958 171.056 187.827 1.00 52.77  ? 2972 PHE A N     1 
ATOM   11401 C  CA    . PHE A 1 2972 ? 146.990 171.644 188.674 1.00 48.57  ? 2972 PHE A CA    1 
ATOM   11402 C  C     . PHE A 1 2972 ? 146.668 173.094 189.003 1.00 48.33  ? 2972 PHE A C     1 
ATOM   11403 O  O     . PHE A 1 2972 ? 146.901 173.549 190.127 1.00 50.41  ? 2972 PHE A O     1 
ATOM   11404 C  CB    . PHE A 1 2972 ? 148.355 171.542 187.998 1.00 46.62  ? 2972 PHE A CB    1 
ATOM   11405 C  CG    . PHE A 1 2972 ? 149.492 171.988 188.870 1.00 48.97  ? 2972 PHE A CG    1 
ATOM   11406 C  CD1   . PHE A 1 2972 ? 149.703 171.403 190.107 1.00 48.63  ? 2972 PHE A CD1   1 
ATOM   11407 C  CD2   . PHE A 1 2972 ? 150.348 172.995 188.457 1.00 52.24  ? 2972 PHE A CD2   1 
ATOM   11408 C  CE1   . PHE A 1 2972 ? 150.746 171.811 190.914 1.00 43.20  ? 2972 PHE A CE1   1 
ATOM   11409 C  CE2   . PHE A 1 2972 ? 151.393 173.407 189.260 1.00 47.71  ? 2972 PHE A CE2   1 
ATOM   11410 C  CZ    . PHE A 1 2972 ? 151.592 172.814 190.490 1.00 43.26  ? 2972 PHE A CZ    1 
ATOM   11411 N  N     . ASP A 1 2973 ? 146.141 173.840 188.029 1.00 48.56  ? 2973 ASP A N     1 
ATOM   11412 C  CA    . ASP A 1 2973 ? 145.744 175.219 188.289 1.00 41.98  ? 2973 ASP A CA    1 
ATOM   11413 C  C     . ASP A 1 2973 ? 144.625 175.283 189.320 1.00 41.27  ? 2973 ASP A C     1 
ATOM   11414 O  O     . ASP A 1 2973 ? 144.630 176.152 190.199 1.00 46.23  ? 2973 ASP A O     1 
ATOM   11415 C  CB    . ASP A 1 2973 ? 145.316 175.897 186.988 1.00 49.09  ? 2973 ASP A CB    1 
ATOM   11416 C  CG    . ASP A 1 2973 ? 146.476 176.122 186.039 1.00 61.78  ? 2973 ASP A CG    1 
ATOM   11417 O  OD1   . ASP A 1 2973 ? 147.593 175.656 186.345 1.00 59.18  ? 2973 ASP A OD1   1 
ATOM   11418 O  OD2   . ASP A 1 2973 ? 146.271 176.766 184.989 1.00 65.13  ? 2973 ASP A OD2   1 
ATOM   11419 N  N     . GLU A 1 2974 ? 143.655 174.371 189.229 1.00 44.99  ? 2974 GLU A N     1 
ATOM   11420 C  CA    . GLU A 1 2974 ? 142.575 174.339 190.211 1.00 46.61  ? 2974 GLU A CA    1 
ATOM   11421 C  C     . GLU A 1 2974 ? 143.098 173.991 191.601 1.00 46.64  ? 2974 GLU A C     1 
ATOM   11422 O  O     . GLU A 1 2974 ? 142.669 174.583 192.599 1.00 49.34  ? 2974 GLU A O     1 
ATOM   11423 C  CB    . GLU A 1 2974 ? 141.499 173.346 189.776 1.00 48.49  ? 2974 GLU A CB    1 
ATOM   11424 C  CG    . GLU A 1 2974 ? 140.150 173.565 190.441 1.00 59.01  ? 2974 GLU A CG    1 
ATOM   11425 C  CD    . GLU A 1 2974 ? 139.770 175.031 190.521 1.00 65.34  ? 2974 GLU A CD    1 
ATOM   11426 O  OE1   . GLU A 1 2974 ? 139.647 175.674 189.458 1.00 63.65  ? 2974 GLU A OE1   1 
ATOM   11427 O  OE2   . GLU A 1 2974 ? 139.592 175.540 191.648 1.00 68.15  ? 2974 GLU A OE2   1 
ATOM   11428 N  N     . ASP A 1 2975 ? 144.022 173.030 191.686 1.00 50.10  ? 2975 ASP A N     1 
ATOM   11429 C  CA    . ASP A 1 2975 ? 144.614 172.687 192.977 1.00 45.05  ? 2975 ASP A CA    1 
ATOM   11430 C  C     . ASP A 1 2975 ? 145.393 173.864 193.554 1.00 40.45  ? 2975 ASP A C     1 
ATOM   11431 O  O     . ASP A 1 2975 ? 145.322 174.137 194.759 1.00 44.28  ? 2975 ASP A O     1 
ATOM   11432 C  CB    . ASP A 1 2975 ? 145.518 171.464 192.832 1.00 49.28  ? 2975 ASP A CB    1 
ATOM   11433 C  CG    . ASP A 1 2975 ? 144.756 170.220 192.417 1.00 61.45  ? 2975 ASP A CG    1 
ATOM   11434 O  OD1   . ASP A 1 2975 ? 143.549 170.334 192.114 1.00 68.35  ? 2975 ASP A OD1   1 
ATOM   11435 O  OD2   . ASP A 1 2975 ? 145.362 169.129 192.393 1.00 60.54  ? 2975 ASP A OD2   1 
ATOM   11436 N  N     . LEU A 1 2976 ? 146.142 174.571 192.705 1.00 37.72  ? 2976 LEU A N     1 
ATOM   11437 C  CA    . LEU A 1 2976 ? 146.871 175.750 193.158 1.00 31.65  ? 2976 LEU A CA    1 
ATOM   11438 C  C     . LEU A 1 2976 ? 145.917 176.831 193.645 1.00 37.35  ? 2976 LEU A C     1 
ATOM   11439 O  O     . LEU A 1 2976 ? 146.184 177.494 194.652 1.00 41.12  ? 2976 LEU A O     1 
ATOM   11440 C  CB    . LEU A 1 2976 ? 147.755 176.285 192.032 1.00 28.19  ? 2976 LEU A CB    1 
ATOM   11441 C  CG    . LEU A 1 2976 ? 149.168 175.712 191.931 1.00 29.03  ? 2976 LEU A CG    1 
ATOM   11442 C  CD1   . LEU A 1 2976 ? 149.925 176.365 190.786 1.00 29.92  ? 2976 LEU A CD1   1 
ATOM   11443 C  CD2   . LEU A 1 2976 ? 149.913 175.891 193.242 1.00 33.92  ? 2976 LEU A CD2   1 
ATOM   11444 N  N     . ARG A 1 2977 ? 144.803 177.029 192.936 1.00 40.29  ? 2977 ARG A N     1 
ATOM   11445 C  CA    . ARG A 1 2977 ? 143.812 178.007 193.372 1.00 37.11  ? 2977 ARG A CA    1 
ATOM   11446 C  C     . ARG A 1 2977 ? 143.220 177.625 194.721 1.00 37.97  ? 2977 ARG A C     1 
ATOM   11447 O  O     . ARG A 1 2977 ? 143.028 178.485 195.586 1.00 43.19  ? 2977 ARG A O     1 
ATOM   11448 C  CB    . ARG A 1 2977 ? 142.707 178.141 192.324 1.00 38.02  ? 2977 ARG A CB    1 
ATOM   11449 C  CG    . ARG A 1 2977 ? 143.110 178.929 191.093 1.00 39.73  ? 2977 ARG A CG    1 
ATOM   11450 C  CD    . ARG A 1 2977 ? 141.955 179.045 190.115 1.00 46.54  ? 2977 ARG A CD    1 
ATOM   11451 N  NE    . ARG A 1 2977 ? 142.409 179.001 188.731 1.00 45.43  ? 2977 ARG A NE    1 
ATOM   11452 C  CZ    . ARG A 1 2977 ? 141.987 178.123 187.833 1.00 48.52  ? 2977 ARG A CZ    1 
ATOM   11453 N  NH1   . ARG A 1 2977 ? 141.094 177.196 188.139 1.00 52.94  ? 2977 ARG A NH1   1 
ATOM   11454 N  NH2   . ARG A 1 2977 ? 142.473 178.175 186.596 1.00 51.95  ? 2977 ARG A NH2   1 
ATOM   11455 N  N     . THR A 1 2978 ? 142.924 176.338 194.917 1.00 36.25  ? 2978 THR A N     1 
ATOM   11456 C  CA    . THR A 1 2978 ? 142.405 175.890 196.207 1.00 34.73  ? 2978 THR A CA    1 
ATOM   11457 C  C     . THR A 1 2978 ? 143.413 176.138 197.322 1.00 37.27  ? 2978 THR A C     1 
ATOM   11458 O  O     . THR A 1 2978 ? 143.053 176.629 198.400 1.00 38.93  ? 2978 THR A O     1 
ATOM   11459 C  CB    . THR A 1 2978 ? 142.040 174.407 196.140 1.00 36.04  ? 2978 THR A CB    1 
ATOM   11460 O  OG1   . THR A 1 2978 ? 141.265 174.155 194.962 1.00 47.94  ? 2978 THR A OG1   1 
ATOM   11461 C  CG2   . THR A 1 2978 ? 141.237 174.002 197.366 1.00 42.29  ? 2978 THR A CG2   1 
ATOM   11462 N  N     . VAL A 1 2979 ? 144.685 175.813 197.076 1.00 41.19  ? 2979 VAL A N     1 
ATOM   11463 C  CA    . VAL A 1 2979 ? 145.720 176.012 198.089 1.00 33.86  ? 2979 VAL A CA    1 
ATOM   11464 C  C     . VAL A 1 2979 ? 145.864 177.493 198.419 1.00 39.21  ? 2979 VAL A C     1 
ATOM   11465 O  O     . VAL A 1 2979 ? 145.961 177.881 199.589 1.00 41.37  ? 2979 VAL A O     1 
ATOM   11466 C  CB    . VAL A 1 2979 ? 147.055 175.410 197.617 1.00 26.97  ? 2979 VAL A CB    1 
ATOM   11467 C  CG1   . VAL A 1 2979 ? 148.179 175.810 198.554 1.00 33.53  ? 2979 VAL A CG1   1 
ATOM   11468 C  CG2   . VAL A 1 2979 ? 146.950 173.903 197.532 1.00 32.46  ? 2979 VAL A CG2   1 
ATOM   11469 N  N     . LEU A 1 2980 ? 145.889 178.340 197.387 1.00 37.84  ? 2980 LEU A N     1 
ATOM   11470 C  CA    . LEU A 1 2980 ? 146.048 179.774 197.604 1.00 33.49  ? 2980 LEU A CA    1 
ATOM   11471 C  C     . LEU A 1 2980 ? 144.853 180.359 198.344 1.00 39.32  ? 2980 LEU A C     1 
ATOM   11472 O  O     . LEU A 1 2980 ? 145.020 181.218 199.215 1.00 44.17  ? 2980 LEU A O     1 
ATOM   11473 C  CB    . LEU A 1 2980 ? 146.259 180.486 196.268 1.00 35.51  ? 2980 LEU A CB    1 
ATOM   11474 C  CG    . LEU A 1 2980 ? 147.582 180.209 195.550 1.00 33.72  ? 2980 LEU A CG    1 
ATOM   11475 C  CD1   . LEU A 1 2980 ? 147.874 181.287 194.519 1.00 41.76  ? 2980 LEU A CD1   1 
ATOM   11476 C  CD2   . LEU A 1 2980 ? 148.724 180.089 196.544 1.00 34.45  ? 2980 LEU A CD2   1 
ATOM   11477 N  N     . ARG A 1 2981 ? 143.640 179.912 198.012 1.00 37.97  ? 2981 ARG A N     1 
ATOM   11478 C  CA    . ARG A 1 2981 ? 142.461 180.389 198.725 1.00 38.89  ? 2981 ARG A CA    1 
ATOM   11479 C  C     . ARG A 1 2981 ? 142.494 179.965 200.187 1.00 39.77  ? 2981 ARG A C     1 
ATOM   11480 O  O     . ARG A 1 2981 ? 142.162 180.756 201.077 1.00 43.00  ? 2981 ARG A O     1 
ATOM   11481 C  CB    . ARG A 1 2981 ? 141.191 179.873 198.048 1.00 41.33  ? 2981 ARG A CB    1 
ATOM   11482 C  CG    . ARG A 1 2981 ? 140.805 180.631 196.792 1.00 51.34  ? 2981 ARG A CG    1 
ATOM   11483 C  CD    . ARG A 1 2981 ? 139.469 180.153 196.252 1.00 52.32  ? 2981 ARG A CD    1 
ATOM   11484 N  NE    . ARG A 1 2981 ? 139.069 180.892 195.061 1.00 60.60  ? 2981 ARG A NE    1 
ATOM   11485 C  CZ    . ARG A 1 2981 ? 138.869 180.342 193.871 1.00 70.42  ? 2981 ARG A CZ    1 
ATOM   11486 N  NH1   . ARG A 1 2981 ? 139.017 179.042 193.678 1.00 69.57  ? 2981 ARG A NH1   1 
ATOM   11487 N  NH2   . ARG A 1 2981 ? 138.513 181.116 192.850 1.00 73.12  ? 2981 ARG A NH2   1 
ATOM   11488 N  N     . ARG A 1 2982 ? 142.889 178.719 200.455 1.00 41.68  ? 2982 ARG A N     1 
ATOM   11489 C  CA    . ARG A 1 2982 ? 142.922 178.246 201.834 1.00 40.49  ? 2982 ARG A CA    1 
ATOM   11490 C  C     . ARG A 1 2982 ? 143.995 178.960 202.649 1.00 40.62  ? 2982 ARG A C     1 
ATOM   11491 O  O     . ARG A 1 2982 ? 143.769 179.300 203.816 1.00 46.43  ? 2982 ARG A O     1 
ATOM   11492 C  CB    . ARG A 1 2982 ? 143.139 176.734 201.865 1.00 42.51  ? 2982 ARG A CB    1 
ATOM   11493 C  CG    . ARG A 1 2982 ? 141.917 175.918 201.483 1.00 45.12  ? 2982 ARG A CG    1 
ATOM   11494 C  CD    . ARG A 1 2982 ? 142.237 174.432 201.454 1.00 43.68  ? 2982 ARG A CD    1 
ATOM   11495 N  NE    . ARG A 1 2982 ? 142.761 173.964 202.732 1.00 42.81  ? 2982 ARG A NE    1 
ATOM   11496 C  CZ    . ARG A 1 2982 ? 143.370 172.799 202.911 1.00 44.09  ? 2982 ARG A CZ    1 
ATOM   11497 N  NH1   . ARG A 1 2982 ? 143.552 171.954 201.910 1.00 38.21  ? 2982 ARG A NH1   1 
ATOM   11498 N  NH2   . ARG A 1 2982 ? 143.805 172.474 204.124 1.00 46.29  ? 2982 ARG A NH2   1 
ATOM   11499 N  N     . SER A 1 2983 ? 145.166 179.201 202.058 1.00 37.74  ? 2983 SER A N     1 
ATOM   11500 C  CA    . SER A 1 2983 ? 146.294 179.746 202.804 1.00 37.81  ? 2983 SER A CA    1 
ATOM   11501 C  C     . SER A 1 2983 ? 146.399 181.266 202.744 1.00 39.56  ? 2983 SER A C     1 
ATOM   11502 O  O     . SER A 1 2983 ? 147.241 181.836 203.445 1.00 44.33  ? 2983 SER A O     1 
ATOM   11503 C  CB    . SER A 1 2983 ? 147.604 179.134 202.298 1.00 32.44  ? 2983 SER A CB    1 
ATOM   11504 O  OG    . SER A 1 2983 ? 147.802 179.418 200.924 1.00 33.89  ? 2983 SER A OG    1 
ATOM   11505 N  N     . GLY A 1 2984 ? 145.579 181.935 201.939 1.00 41.08  ? 2984 GLY A N     1 
ATOM   11506 C  CA    . GLY A 1 2984 ? 145.680 183.375 201.813 1.00 40.50  ? 2984 GLY A CA    1 
ATOM   11507 C  C     . GLY A 1 2984 ? 144.422 184.111 202.222 1.00 52.84  ? 2984 GLY A C     1 
ATOM   11508 O  O     . GLY A 1 2984 ? 144.482 185.264 202.658 1.00 57.98  ? 2984 GLY A O     1 
ATOM   11509 N  N     . CYS A 1 2985 ? 143.273 183.454 202.082 1.00 48.83  ? 2985 CYS A N     1 
ATOM   11510 C  CA    . CYS A 1 2985 ? 141.992 184.035 202.464 1.00 46.26  ? 2985 CYS A CA    1 
ATOM   11511 C  C     . CYS A 1 2985 ? 141.500 183.542 203.816 1.00 53.41  ? 2985 CYS A C     1 
ATOM   11512 O  O     . CYS A 1 2985 ? 141.062 184.348 204.642 1.00 60.57  ? 2985 CYS A O     1 
ATOM   11513 C  CB    . CYS A 1 2985 ? 140.935 183.736 201.397 1.00 45.43  ? 2985 CYS A CB    1 
ATOM   11514 S  SG    . CYS A 1 2985 ? 141.413 184.208 199.719 1.00 55.41  ? 2985 CYS A SG    1 
ATOM   11515 N  N     . LYS A 1 2986 ? 141.567 182.236 204.063 1.00 49.93  ? 2986 LYS A N     1 
ATOM   11516 C  CA    . LYS A 1 2986 ? 141.118 181.657 205.321 1.00 50.04  ? 2986 LYS A CA    1 
ATOM   11517 C  C     . LYS A 1 2986 ? 142.184 181.695 206.408 1.00 54.47  ? 2986 LYS A C     1 
ATOM   11518 O  O     . LYS A 1 2986 ? 141.894 181.314 207.547 1.00 58.42  ? 2986 LYS A O     1 
ATOM   11519 C  CB    . LYS A 1 2986 ? 140.664 180.211 205.100 1.00 48.50  ? 2986 LYS A CB    1 
ATOM   11520 C  CG    . LYS A 1 2986 ? 139.783 180.017 203.877 1.00 54.90  ? 2986 LYS A CG    1 
ATOM   11521 C  CD    . LYS A 1 2986 ? 138.523 180.861 203.960 1.00 55.34  ? 2986 LYS A CD    1 
ATOM   11522 C  CE    . LYS A 1 2986 ? 138.039 181.263 202.576 1.00 57.60  ? 2986 LYS A CE    1 
ATOM   11523 N  NZ    . LYS A 1 2986 ? 138.139 180.139 201.605 1.00 66.77  ? 2986 LYS A NZ    1 
ATOM   11524 N  N     . ASN A 1 2987 ? 143.399 182.141 206.084 1.00 50.81  ? 2987 ASN A N     1 
ATOM   11525 C  CA    . ASN A 1 2987 ? 144.514 182.206 207.030 1.00 51.95  ? 2987 ASN A CA    1 
ATOM   11526 C  C     . ASN A 1 2987 ? 144.774 180.822 207.631 1.00 58.77  ? 2987 ASN A C     1 
ATOM   11527 O  O     . ASN A 1 2987 ? 144.610 180.585 208.830 1.00 64.00  ? 2987 ASN A O     1 
ATOM   11528 C  CB    . ASN A 1 2987 ? 144.248 183.258 208.116 1.00 55.34  ? 2987 ASN A CB    1 
ATOM   11529 C  CG    . ASN A 1 2987 ? 145.467 183.541 208.986 1.00 57.40  ? 2987 ASN A CG    1 
ATOM   11530 O  OD1   . ASN A 1 2987 ? 146.291 182.665 209.248 1.00 61.96  ? 2987 ASN A OD1   1 
ATOM   11531 N  ND2   . ASN A 1 2987 ? 145.582 184.784 209.440 1.00 60.53  ? 2987 ASN A ND2   1 
ATOM   11532 N  N     . GLU A 1 2988 ? 145.161 179.896 206.758 1.00 51.12  ? 2988 GLU A N     1 
ATOM   11533 C  CA    . GLU A 1 2988 ? 145.410 178.511 207.129 1.00 46.23  ? 2988 GLU A CA    1 
ATOM   11534 C  C     . GLU A 1 2988 ? 146.832 178.135 206.743 1.00 43.19  ? 2988 GLU A C     1 
ATOM   11535 O  O     . GLU A 1 2988 ? 147.228 178.294 205.584 1.00 45.60  ? 2988 GLU A O     1 
ATOM   11536 C  CB    . GLU A 1 2988 ? 144.406 177.577 206.448 1.00 41.65  ? 2988 GLU A CB    1 
ATOM   11537 C  CG    . GLU A 1 2988 ? 144.239 176.229 207.124 1.00 45.35  ? 2988 GLU A CG    1 
ATOM   11538 C  CD    . GLU A 1 2988 ? 143.722 175.168 206.173 1.00 59.17  ? 2988 GLU A CD    1 
ATOM   11539 O  OE1   . GLU A 1 2988 ? 142.704 175.421 205.495 1.00 61.20  ? 2988 GLU A OE1   1 
ATOM   11540 O  OE2   . GLU A 1 2988 ? 144.330 174.082 206.103 1.00 61.02  ? 2988 GLU A OE2   1 
ATOM   11541 N  N     . LYS A 1 2989 ? 147.594 177.637 207.713 1.00 42.03  ? 2989 LYS A N     1 
ATOM   11542 C  CA    . LYS A 1 2989 ? 148.966 177.213 207.464 1.00 33.48  ? 2989 LYS A CA    1 
ATOM   11543 C  C     . LYS A 1 2989 ? 148.954 175.858 206.767 1.00 33.48  ? 2989 LYS A C     1 
ATOM   11544 O  O     . LYS A 1 2989 ? 148.413 174.884 207.300 1.00 36.01  ? 2989 LYS A O     1 
ATOM   11545 C  CB    . LYS A 1 2989 ? 149.746 177.148 208.774 1.00 26.24  ? 2989 LYS A CB    1 
ATOM   11546 C  CG    . LYS A 1 2989 ? 149.859 178.483 209.490 1.00 34.77  ? 2989 LYS A CG    1 
ATOM   11547 C  CD    . LYS A 1 2989 ? 150.806 178.405 210.675 1.00 36.18  ? 2989 LYS A CD    1 
ATOM   11548 C  CE    . LYS A 1 2989 ? 150.331 177.391 211.700 1.00 37.22  ? 2989 LYS A CE    1 
ATOM   11549 N  NZ    . LYS A 1 2989 ? 151.260 177.298 212.861 1.00 40.44  ? 2989 LYS A NZ    1 
ATOM   11550 N  N     . ILE A 1 2990 ? 149.549 175.796 205.578 1.00 29.29  ? 2990 ILE A N     1 
ATOM   11551 C  CA    . ILE A 1 2990 ? 149.496 174.615 204.726 1.00 29.58  ? 2990 ILE A CA    1 
ATOM   11552 C  C     . ILE A 1 2990 ? 150.913 174.210 204.353 1.00 24.63  ? 2990 ILE A C     1 
ATOM   11553 O  O     . ILE A 1 2990 ? 151.724 175.059 203.967 1.00 25.50  ? 2990 ILE A O     1 
ATOM   11554 C  CB    . ILE A 1 2990 ? 148.659 174.865 203.457 1.00 30.34  ? 2990 ILE A CB    1 
ATOM   11555 C  CG1   . ILE A 1 2990 ? 147.207 175.160 203.824 1.00 33.08  ? 2990 ILE A CG1   1 
ATOM   11556 C  CG2   . ILE A 1 2990 ? 148.733 173.674 202.515 1.00 32.35  ? 2990 ILE A CG2   1 
ATOM   11557 C  CD1   . ILE A 1 2990 ? 146.394 175.654 202.664 1.00 42.82  ? 2990 ILE A CD1   1 
ATOM   11558 N  N     . ALA A 1 2991 ? 151.209 172.918 204.471 1.00 22.82  ? 2991 ALA A N     1 
ATOM   11559 C  CA    . ALA A 1 2991 ? 152.478 172.350 204.019 1.00 20.91  ? 2991 ALA A CA    1 
ATOM   11560 C  C     . ALA A 1 2991 ? 152.211 171.652 202.690 1.00 20.83  ? 2991 ALA A C     1 
ATOM   11561 O  O     . ALA A 1 2991 ? 151.892 170.464 202.641 1.00 27.51  ? 2991 ALA A O     1 
ATOM   11562 C  CB    . ALA A 1 2991 ? 153.053 171.395 205.058 1.00 19.03  ? 2991 ALA A CB    1 
ATOM   11563 N  N     . PHE A 1 2992 ? 152.341 172.405 201.601 1.00 18.81  ? 2992 PHE A N     1 
ATOM   11564 C  CA    . PHE A 1 2992 ? 152.079 171.888 200.260 1.00 20.31  ? 2992 PHE A CA    1 
ATOM   11565 C  C     . PHE A 1 2992 ? 153.216 170.956 199.864 1.00 21.54  ? 2992 PHE A C     1 
ATOM   11566 O  O     . PHE A 1 2992 ? 154.256 171.397 199.370 1.00 23.30  ? 2992 PHE A O     1 
ATOM   11567 C  CB    . PHE A 1 2992 ? 151.932 173.038 199.271 1.00 20.92  ? 2992 PHE A CB    1 
ATOM   11568 C  CG    . PHE A 1 2992 ? 151.450 172.618 197.910 1.00 27.65  ? 2992 PHE A CG    1 
ATOM   11569 C  CD1   . PHE A 1 2992 ? 150.764 171.428 197.735 1.00 30.02  ? 2992 PHE A CD1   1 
ATOM   11570 C  CD2   . PHE A 1 2992 ? 151.683 173.418 196.805 1.00 29.82  ? 2992 PHE A CD2   1 
ATOM   11571 C  CE1   . PHE A 1 2992 ? 150.323 171.044 196.484 1.00 31.31  ? 2992 PHE A CE1   1 
ATOM   11572 C  CE2   . PHE A 1 2992 ? 151.243 173.039 195.551 1.00 33.70  ? 2992 PHE A CE2   1 
ATOM   11573 C  CZ    . PHE A 1 2992 ? 150.562 171.851 195.391 1.00 33.42  ? 2992 PHE A CZ    1 
ATOM   11574 N  N     . ILE A 1 2993 ? 153.021 169.659 200.076 1.00 20.64  ? 2993 ILE A N     1 
ATOM   11575 C  CA    . ILE A 1 2993 ? 154.038 168.658 199.778 1.00 20.72  ? 2993 ILE A CA    1 
ATOM   11576 C  C     . ILE A 1 2993 ? 153.884 168.230 198.325 1.00 23.62  ? 2993 ILE A C     1 
ATOM   11577 O  O     . ILE A 1 2993 ? 152.821 167.748 197.918 1.00 30.99  ? 2993 ILE A O     1 
ATOM   11578 C  CB    . ILE A 1 2993 ? 153.926 167.454 200.723 1.00 19.71  ? 2993 ILE A CB    1 
ATOM   11579 C  CG1   . ILE A 1 2993 ? 153.963 167.919 202.179 1.00 18.65  ? 2993 ILE A CG1   1 
ATOM   11580 C  CG2   . ILE A 1 2993 ? 155.043 166.460 200.448 1.00 20.90  ? 2993 ILE A CG2   1 
ATOM   11581 C  CD1   . ILE A 1 2993 ? 154.050 166.793 203.178 1.00 17.94  ? 2993 ILE A CD1   1 
ATOM   11582 N  N     . MET A 1 2994 ? 154.946 168.402 197.543 1.00 25.12  ? 2994 MET A N     1 
ATOM   11583 C  CA    . MET A 1 2994 ? 154.940 168.079 196.125 1.00 29.55  ? 2994 MET A CA    1 
ATOM   11584 C  C     . MET A 1 2994 ? 156.130 167.189 195.803 1.00 33.01  ? 2994 MET A C     1 
ATOM   11585 O  O     . MET A 1 2994 ? 157.220 167.372 196.351 1.00 35.35  ? 2994 MET A O     1 
ATOM   11586 C  CB    . MET A 1 2994 ? 154.985 169.349 195.267 1.00 28.84  ? 2994 MET A CB    1 
ATOM   11587 C  CG    . MET A 1 2994 ? 154.756 169.109 193.786 1.00 40.30  ? 2994 MET A CG    1 
ATOM   11588 S  SD    . MET A 1 2994 ? 153.929 170.491 192.978 1.00 75.69  ? 2994 MET A SD    1 
ATOM   11589 C  CE    . MET A 1 2994 ? 153.914 169.926 191.279 1.00 58.25  ? 2994 MET A CE    1 
ATOM   11590 N  N     . ASP A 1 2995 ? 155.913 166.224 194.916 1.00 37.11  ? 2995 ASP A N     1 
ATOM   11591 C  CA    . ASP A 1 2995 ? 156.948 165.299 194.485 1.00 37.68  ? 2995 ASP A CA    1 
ATOM   11592 C  C     . ASP A 1 2995 ? 157.286 165.542 193.021 1.00 44.76  ? 2995 ASP A C     1 
ATOM   11593 O  O     . ASP A 1 2995 ? 156.471 166.053 192.248 1.00 53.45  ? 2995 ASP A O     1 
ATOM   11594 C  CB    . ASP A 1 2995 ? 156.504 163.846 194.687 1.00 40.90  ? 2995 ASP A CB    1 
ATOM   11595 C  CG    . ASP A 1 2995 ? 156.369 163.475 196.150 1.00 57.50  ? 2995 ASP A CG    1 
ATOM   11596 O  OD1   . ASP A 1 2995 ? 155.274 163.676 196.717 1.00 61.23  ? 2995 ASP A OD1   1 
ATOM   11597 O  OD2   . ASP A 1 2995 ? 157.356 162.981 196.733 1.00 56.00  ? 2995 ASP A OD2   1 
ATOM   11598 N  N     . GLU A 1 2996 ? 158.513 165.172 192.646 1.00 47.81  ? 2996 GLU A N     1 
ATOM   11599 C  CA    . GLU A 1 2996 ? 158.935 165.311 191.258 1.00 50.94  ? 2996 GLU A CA    1 
ATOM   11600 C  C     . GLU A 1 2996 ? 158.116 164.438 190.317 1.00 49.70  ? 2996 GLU A C     1 
ATOM   11601 O  O     . GLU A 1 2996 ? 158.022 164.751 189.126 1.00 52.93  ? 2996 GLU A O     1 
ATOM   11602 C  CB    . GLU A 1 2996 ? 160.421 164.978 191.120 1.00 54.39  ? 2996 GLU A CB    1 
ATOM   11603 C  CG    . GLU A 1 2996 ? 160.785 163.560 191.522 1.00 51.04  ? 2996 GLU A CG    1 
ATOM   11604 C  CD    . GLU A 1 2996 ? 162.037 163.064 190.828 1.00 53.65  ? 2996 GLU A CD    1 
ATOM   11605 O  OE1   . GLU A 1 2996 ? 162.603 163.821 190.011 1.00 58.32  ? 2996 GLU A OE1   1 
ATOM   11606 O  OE2   . GLU A 1 2996 ? 162.455 161.919 191.098 1.00 49.73  ? 2996 GLU A OE2   1 
ATOM   11607 N  N     . SER A 1 2997 ? 157.525 163.352 190.822 1.00 49.60  ? 2997 SER A N     1 
ATOM   11608 C  CA    . SER A 1 2997 ? 156.664 162.518 189.994 1.00 52.16  ? 2997 SER A CA    1 
ATOM   11609 C  C     . SER A 1 2997 ? 155.318 163.174 189.719 1.00 52.63  ? 2997 SER A C     1 
ATOM   11610 O  O     . SER A 1 2997 ? 154.637 162.785 188.765 1.00 50.16  ? 2997 SER A O     1 
ATOM   11611 C  CB    . SER A 1 2997 ? 156.456 161.157 190.659 1.00 51.57  ? 2997 SER A CB    1 
ATOM   11612 O  OG    . SER A 1 2997 ? 155.914 161.304 191.959 1.00 56.72  ? 2997 SER A OG    1 
ATOM   11613 N  N     . ASN A 1 2998 ? 154.922 164.157 190.528 1.00 50.40  ? 2998 ASN A N     1 
ATOM   11614 C  CA    . ASN A 1 2998 ? 153.685 164.890 190.295 1.00 48.68  ? 2998 ASN A CA    1 
ATOM   11615 C  C     . ASN A 1 2998 ? 153.812 165.923 189.185 1.00 54.93  ? 2998 ASN A C     1 
ATOM   11616 O  O     . ASN A 1 2998 ? 152.792 166.473 188.754 1.00 60.03  ? 2998 ASN A O     1 
ATOM   11617 C  CB    . ASN A 1 2998 ? 153.223 165.582 191.581 1.00 43.45  ? 2998 ASN A CB    1 
ATOM   11618 C  CG    . ASN A 1 2998 ? 153.088 164.623 192.750 1.00 49.02  ? 2998 ASN A CG    1 
ATOM   11619 O  OD1   . ASN A 1 2998 ? 152.965 163.414 192.561 1.00 58.43  ? 2998 ASN A OD1   1 
ATOM   11620 N  ND2   . ASN A 1 2998 ? 153.131 165.157 193.965 1.00 42.05  ? 2998 ASN A ND2   1 
ATOM   11621 N  N     . VAL A 1 2999 ? 155.026 166.200 188.715 1.00 55.00  ? 2999 VAL A N     1 
ATOM   11622 C  CA    . VAL A 1 2999 ? 155.253 167.174 187.654 1.00 56.48  ? 2999 VAL A CA    1 
ATOM   11623 C  C     . VAL A 1 2999 ? 155.094 166.441 186.326 1.00 60.39  ? 2999 VAL A C     1 
ATOM   11624 O  O     . VAL A 1 2999 ? 155.962 165.667 185.918 1.00 62.88  ? 2999 VAL A O     1 
ATOM   11625 C  CB    . VAL A 1 2999 ? 156.625 167.836 187.775 1.00 54.14  ? 2999 VAL A CB    1 
ATOM   11626 C  CG1   . VAL A 1 2999 ? 156.890 168.720 186.570 1.00 55.55  ? 2999 VAL A CG1   1 
ATOM   11627 C  CG2   . VAL A 1 2999 ? 156.712 168.641 189.062 1.00 51.61  ? 2999 VAL A CG2   1 
ATOM   11628 N  N     . LEU A 1 3000 ? 153.973 166.682 185.650 1.00 61.44  ? 3000 LEU A N     1 
ATOM   11629 C  CA    . LEU A 1 3000 ? 153.688 166.065 184.363 1.00 64.15  ? 3000 LEU A CA    1 
ATOM   11630 C  C     . LEU A 1 3000 ? 153.862 167.022 183.192 1.00 65.99  ? 3000 LEU A C     1 
ATOM   11631 O  O     . LEU A 1 3000 ? 153.680 166.610 182.042 1.00 66.44  ? 3000 LEU A O     1 
ATOM   11632 C  CB    . LEU A 1 3000 ? 152.265 165.499 184.357 1.00 62.24  ? 3000 LEU A CB    1 
ATOM   11633 C  CG    . LEU A 1 3000 ? 151.851 164.692 185.588 1.00 59.97  ? 3000 LEU A CG    1 
ATOM   11634 C  CD1   . LEU A 1 3000 ? 150.345 164.518 185.622 1.00 57.46  ? 3000 LEU A CD1   1 
ATOM   11635 C  CD2   . LEU A 1 3000 ? 152.550 163.342 185.608 1.00 61.83  ? 3000 LEU A CD2   1 
ATOM   11636 N  N     . ASP A 1 3001 ? 154.208 168.280 183.452 1.00 65.07  ? 3001 ASP A N     1 
ATOM   11637 C  CA    . ASP A 1 3001 ? 154.340 169.268 182.391 1.00 68.24  ? 3001 ASP A CA    1 
ATOM   11638 C  C     . ASP A 1 3001 ? 155.225 170.399 182.896 1.00 63.88  ? 3001 ASP A C     1 
ATOM   11639 O  O     . ASP A 1 3001 ? 155.338 170.631 184.102 1.00 61.83  ? 3001 ASP A O     1 
ATOM   11640 C  CB    . ASP A 1 3001 ? 152.964 169.791 181.951 1.00 70.07  ? 3001 ASP A CB    1 
ATOM   11641 C  CG    . ASP A 1 3001 ? 153.055 170.941 180.964 1.00 76.94  ? 3001 ASP A CG    1 
ATOM   11642 O  OD1   . ASP A 1 3001 ? 154.054 171.015 180.218 1.00 79.63  ? 3001 ASP A OD1   1 
ATOM   11643 O  OD2   . ASP A 1 3001 ? 152.124 171.774 180.936 1.00 76.02  ? 3001 ASP A OD2   1 
ATOM   11644 N  N     . SER A 1 3002 ? 155.862 171.097 181.952 1.00 64.41  ? 3002 SER A N     1 
ATOM   11645 C  CA    . SER A 1 3002 ? 156.692 172.241 182.307 1.00 69.04  ? 3002 SER A CA    1 
ATOM   11646 C  C     . SER A 1 3002 ? 155.870 173.408 182.840 1.00 65.93  ? 3002 SER A C     1 
ATOM   11647 O  O     . SER A 1 3002 ? 156.412 174.254 183.560 1.00 69.33  ? 3002 SER A O     1 
ATOM   11648 C  CB    . SER A 1 3002 ? 157.515 172.690 181.099 1.00 70.13  ? 3002 SER A CB    1 
ATOM   11649 O  OG    . SER A 1 3002 ? 158.386 173.752 181.446 1.00 68.09  ? 3002 SER A OG    1 
ATOM   11650 N  N     . GLY A 1 3003 ? 154.582 173.476 182.497 1.00 57.70  ? 3003 GLY A N     1 
ATOM   11651 C  CA    . GLY A 1 3003 ? 153.728 174.499 183.078 1.00 55.32  ? 3003 GLY A CA    1 
ATOM   11652 C  C     . GLY A 1 3003 ? 153.591 174.347 184.580 1.00 56.80  ? 3003 GLY A C     1 
ATOM   11653 O  O     . GLY A 1 3003 ? 153.492 175.339 185.309 1.00 62.93  ? 3003 GLY A O     1 
ATOM   11654 N  N     . PHE A 1 3004 ? 153.580 173.101 185.062 1.00 49.89  ? 3004 PHE A N     1 
ATOM   11655 C  CA    . PHE A 1 3004 ? 153.599 172.847 186.498 1.00 47.44  ? 3004 PHE A CA    1 
ATOM   11656 C  C     . PHE A 1 3004 ? 154.791 173.538 187.145 1.00 49.30  ? 3004 PHE A C     1 
ATOM   11657 O  O     . PHE A 1 3004 ? 154.646 174.281 188.124 1.00 48.24  ? 3004 PHE A O     1 
ATOM   11658 C  CB    . PHE A 1 3004 ? 153.665 171.339 186.768 1.00 49.14  ? 3004 PHE A CB    1 
ATOM   11659 C  CG    . PHE A 1 3004 ? 152.385 170.596 186.486 1.00 51.22  ? 3004 PHE A CG    1 
ATOM   11660 C  CD1   . PHE A 1 3004 ? 151.763 170.680 185.251 1.00 55.12  ? 3004 PHE A CD1   1 
ATOM   11661 C  CD2   . PHE A 1 3004 ? 151.824 169.780 187.455 1.00 49.80  ? 3004 PHE A CD2   1 
ATOM   11662 C  CE1   . PHE A 1 3004 ? 150.597 169.986 184.996 1.00 55.60  ? 3004 PHE A CE1   1 
ATOM   11663 C  CE2   . PHE A 1 3004 ? 150.659 169.081 187.205 1.00 51.44  ? 3004 PHE A CE2   1 
ATOM   11664 C  CZ    . PHE A 1 3004 ? 150.045 169.185 185.974 1.00 53.13  ? 3004 PHE A CZ    1 
ATOM   11665 N  N     . LEU A 1 3005 ? 155.984 173.308 186.591 1.00 52.18  ? 3005 LEU A N     1 
ATOM   11666 C  CA    . LEU A 1 3005 ? 157.198 173.903 187.136 1.00 45.17  ? 3005 LEU A CA    1 
ATOM   11667 C  C     . LEU A 1 3005 ? 157.195 175.417 187.009 1.00 41.81  ? 3005 LEU A C     1 
ATOM   11668 O  O     . LEU A 1 3005 ? 157.677 176.104 187.910 1.00 45.53  ? 3005 LEU A O     1 
ATOM   11669 C  CB    . LEU A 1 3005 ? 158.428 173.319 186.444 1.00 53.24  ? 3005 LEU A CB    1 
ATOM   11670 C  CG    . LEU A 1 3005 ? 158.686 171.836 186.700 1.00 64.75  ? 3005 LEU A CG    1 
ATOM   11671 C  CD1   . LEU A 1 3005 ? 159.842 171.341 185.851 1.00 72.76  ? 3005 LEU A CD1   1 
ATOM   11672 C  CD2   . LEU A 1 3005 ? 158.957 171.591 188.177 1.00 63.82  ? 3005 LEU A CD2   1 
ATOM   11673 N  N     . GLU A 1 3006 ? 156.674 175.958 185.907 1.00 43.77  ? 3006 GLU A N     1 
ATOM   11674 C  CA    . GLU A 1 3006 ? 156.641 177.410 185.746 1.00 42.11  ? 3006 GLU A CA    1 
ATOM   11675 C  C     . GLU A 1 3006 ? 155.732 178.059 186.787 1.00 41.31  ? 3006 GLU A C     1 
ATOM   11676 O  O     . GLU A 1 3006 ? 156.111 179.048 187.434 1.00 43.96  ? 3006 GLU A O     1 
ATOM   11677 C  CB    . GLU A 1 3006 ? 156.190 177.763 184.328 1.00 42.44  ? 3006 GLU A CB    1 
ATOM   11678 C  CG    . GLU A 1 3006 ? 155.604 179.155 184.177 1.00 55.53  ? 3006 GLU A CG    1 
ATOM   11679 C  CD    . GLU A 1 3006 ? 155.500 179.582 182.726 1.00 67.27  ? 3006 GLU A CD    1 
ATOM   11680 O  OE1   . GLU A 1 3006 ? 155.372 178.697 181.854 1.00 78.30  ? 3006 GLU A OE1   1 
ATOM   11681 O  OE2   . GLU A 1 3006 ? 155.547 180.801 182.457 1.00 56.64  ? 3006 GLU A OE2   1 
ATOM   11682 N  N     . ARG A 1 3007 ? 154.530 177.507 186.970 1.00 41.14  ? 3007 ARG A N     1 
ATOM   11683 C  CA    . ARG A 1 3007 ? 153.614 178.047 187.969 1.00 36.62  ? 3007 ARG A CA    1 
ATOM   11684 C  C     . ARG A 1 3007 ? 154.189 177.908 189.373 1.00 36.72  ? 3007 ARG A C     1 
ATOM   11685 O  O     . ARG A 1 3007 ? 154.082 178.831 190.190 1.00 34.43  ? 3007 ARG A O     1 
ATOM   11686 C  CB    . ARG A 1 3007 ? 152.259 177.348 187.870 1.00 42.40  ? 3007 ARG A CB    1 
ATOM   11687 C  CG    . ARG A 1 3007 ? 151.445 177.746 186.648 1.00 45.63  ? 3007 ARG A CG    1 
ATOM   11688 C  CD    . ARG A 1 3007 ? 149.982 177.965 187.001 1.00 50.89  ? 3007 ARG A CD    1 
ATOM   11689 N  NE    . ARG A 1 3007 ? 149.169 178.282 185.831 1.00 57.09  ? 3007 ARG A NE    1 
ATOM   11690 C  CZ    . ARG A 1 3007 ? 149.210 179.432 185.170 1.00 62.51  ? 3007 ARG A CZ    1 
ATOM   11691 N  NH1   . ARG A 1 3007 ? 150.014 180.415 185.540 1.00 51.30  ? 3007 ARG A NH1   1 
ATOM   11692 N  NH2   . ARG A 1 3007 ? 148.421 179.600 184.113 1.00 68.07  ? 3007 ARG A NH2   1 
ATOM   11693 N  N     . MET A 1 3008 ? 154.815 176.764 189.669 1.00 41.67  ? 3008 MET A N     1 
ATOM   11694 C  CA    . MET A 1 3008 ? 155.421 176.582 190.982 1.00 30.72  ? 3008 MET A CA    1 
ATOM   11695 C  C     . MET A 1 3008 ? 156.598 177.524 191.194 1.00 28.60  ? 3008 MET A C     1 
ATOM   11696 O  O     . MET A 1 3008 ? 156.801 178.009 192.308 1.00 30.99  ? 3008 MET A O     1 
ATOM   11697 C  CB    . MET A 1 3008 ? 155.859 175.130 191.166 1.00 33.60  ? 3008 MET A CB    1 
ATOM   11698 C  CG    . MET A 1 3008 ? 154.716 174.182 191.482 1.00 46.00  ? 3008 MET A CG    1 
ATOM   11699 S  SD    . MET A 1 3008 ? 153.859 174.605 193.010 1.00 47.34  ? 3008 MET A SD    1 
ATOM   11700 C  CE    . MET A 1 3008 ? 155.234 174.721 194.148 1.00 35.17  ? 3008 MET A CE    1 
ATOM   11701 N  N     . ASN A 1 3009 ? 157.384 177.787 190.149 1.00 32.22  ? 3009 ASN A N     1 
ATOM   11702 C  CA    . ASN A 1 3009 ? 158.478 178.746 190.244 1.00 30.14  ? 3009 ASN A CA    1 
ATOM   11703 C  C     . ASN A 1 3009 ? 157.954 180.134 190.581 1.00 34.12  ? 3009 ASN A C     1 
ATOM   11704 O  O     . ASN A 1 3009 ? 158.480 180.813 191.474 1.00 37.92  ? 3009 ASN A O     1 
ATOM   11705 C  CB    . ASN A 1 3009 ? 159.254 178.764 188.926 1.00 30.63  ? 3009 ASN A CB    1 
ATOM   11706 C  CG    . ASN A 1 3009 ? 160.382 179.772 188.920 1.00 37.36  ? 3009 ASN A CG    1 
ATOM   11707 O  OD1   . ASN A 1 3009 ? 161.428 179.553 189.528 1.00 46.05  ? 3009 ASN A OD1   1 
ATOM   11708 N  ND2   . ASN A 1 3009 ? 160.177 180.884 188.226 1.00 36.82  ? 3009 ASN A ND2   1 
ATOM   11709 N  N     . THR A 1 3010 ? 156.903 180.565 189.880 1.00 37.08  ? 3010 THR A N     1 
ATOM   11710 C  CA    . THR A 1 3010 ? 156.314 181.869 190.172 1.00 33.29  ? 3010 THR A CA    1 
ATOM   11711 C  C     . THR A 1 3010 ? 155.777 181.924 191.598 1.00 33.72  ? 3010 THR A C     1 
ATOM   11712 O  O     . THR A 1 3010 ? 155.980 182.917 192.309 1.00 34.09  ? 3010 THR A O     1 
ATOM   11713 C  CB    . THR A 1 3010 ? 155.206 182.185 189.169 1.00 38.56  ? 3010 THR A CB    1 
ATOM   11714 O  OG1   . THR A 1 3010 ? 155.716 182.060 187.836 1.00 35.86  ? 3010 THR A OG1   1 
ATOM   11715 C  CG2   . THR A 1 3010 ? 154.690 183.600 189.376 1.00 44.50  ? 3010 THR A CG2   1 
ATOM   11716 N  N     . LEU A 1 3011 ? 155.097 180.861 192.037 1.00 33.29  ? 3011 LEU A N     1 
ATOM   11717 C  CA    . LEU A 1 3011 ? 154.543 180.839 193.388 1.00 29.67  ? 3011 LEU A CA    1 
ATOM   11718 C  C     . LEU A 1 3011 ? 155.643 180.866 194.444 1.00 30.78  ? 3011 LEU A C     1 
ATOM   11719 O  O     . LEU A 1 3011 ? 155.527 181.569 195.454 1.00 35.45  ? 3011 LEU A O     1 
ATOM   11720 C  CB    . LEU A 1 3011 ? 153.656 179.608 193.569 1.00 27.84  ? 3011 LEU A CB    1 
ATOM   11721 C  CG    . LEU A 1 3011 ? 153.230 179.274 194.999 1.00 25.95  ? 3011 LEU A CG    1 
ATOM   11722 C  CD1   . LEU A 1 3011 ? 152.306 180.348 195.546 1.00 29.64  ? 3011 LEU A CD1   1 
ATOM   11723 C  CD2   . LEU A 1 3011 ? 152.564 177.910 195.055 1.00 26.68  ? 3011 LEU A CD2   1 
ATOM   11724 N  N     . LEU A 1 3012 ? 156.714 180.098 194.235 1.00 30.18  ? 3012 LEU A N     1 
ATOM   11725 C  CA    . LEU A 1 3012 ? 157.811 180.068 195.195 1.00 27.61  ? 3012 LEU A CA    1 
ATOM   11726 C  C     . LEU A 1 3012 ? 158.512 181.416 195.272 1.00 33.27  ? 3012 LEU A C     1 
ATOM   11727 O  O     . LEU A 1 3012 ? 158.897 181.860 196.360 1.00 35.44  ? 3012 LEU A O     1 
ATOM   11728 C  CB    . LEU A 1 3012 ? 158.810 178.974 194.820 1.00 26.72  ? 3012 LEU A CB    1 
ATOM   11729 C  CG    . LEU A 1 3012 ? 158.377 177.517 194.988 1.00 24.83  ? 3012 LEU A CG    1 
ATOM   11730 C  CD1   . LEU A 1 3012 ? 159.464 176.579 194.489 1.00 24.67  ? 3012 LEU A CD1   1 
ATOM   11731 C  CD2   . LEU A 1 3012 ? 158.028 177.219 196.431 1.00 24.38  ? 3012 LEU A CD2   1 
ATOM   11732 N  N     . ALA A 1 3013 ? 158.689 182.081 194.130 1.00 33.30  ? 3013 ALA A N     1 
ATOM   11733 C  CA    . ALA A 1 3013 ? 159.447 183.326 194.123 1.00 28.51  ? 3013 ALA A CA    1 
ATOM   11734 C  C     . ALA A 1 3013 ? 158.624 184.497 194.648 1.00 33.10  ? 3013 ALA A C     1 
ATOM   11735 O  O     . ALA A 1 3013 ? 159.052 185.196 195.573 1.00 31.13  ? 3013 ALA A O     1 
ATOM   11736 C  CB    . ALA A 1 3013 ? 159.958 183.612 192.714 1.00 32.43  ? 3013 ALA A CB    1 
ATOM   11737 N  N     . ASN A 1 3014 ? 157.440 184.731 194.076 1.00 38.81  ? 3014 ASN A N     1 
ATOM   11738 C  CA    . ASN A 1 3014 ? 156.651 185.903 194.437 1.00 33.41  ? 3014 ASN A CA    1 
ATOM   11739 C  C     . ASN A 1 3014 ? 155.610 185.637 195.513 1.00 37.02  ? 3014 ASN A C     1 
ATOM   11740 O  O     . ASN A 1 3014 ? 155.198 186.581 196.196 1.00 45.24  ? 3014 ASN A O     1 
ATOM   11741 C  CB    . ASN A 1 3014 ? 155.937 186.472 193.205 1.00 36.85  ? 3014 ASN A CB    1 
ATOM   11742 C  CG    . ASN A 1 3014 ? 156.898 187.033 192.181 1.00 40.75  ? 3014 ASN A CG    1 
ATOM   11743 O  OD1   . ASN A 1 3014 ? 157.243 186.363 191.211 1.00 37.22  ? 3014 ASN A OD1   1 
ATOM   11744 N  ND2   . ASN A 1 3014 ? 157.339 188.266 192.395 1.00 42.20  ? 3014 ASN A ND2   1 
ATOM   11745 N  N     . GLY A 1 3015 ? 155.176 184.393 195.684 1.00 36.02  ? 3015 GLY A N     1 
ATOM   11746 C  CA    . GLY A 1 3015 ? 154.067 184.095 196.561 1.00 33.78  ? 3015 GLY A CA    1 
ATOM   11747 C  C     . GLY A 1 3015 ? 152.703 184.236 195.925 1.00 42.95  ? 3015 GLY A C     1 
ATOM   11748 O  O     . GLY A 1 3015 ? 151.694 184.089 196.625 1.00 51.72  ? 3015 GLY A O     1 
ATOM   11749 N  N     . GLU A 1 3016 ? 152.637 184.520 194.626 1.00 46.98  ? 3016 GLU A N     1 
ATOM   11750 C  CA    . GLU A 1 3016 ? 151.366 184.630 193.928 1.00 48.93  ? 3016 GLU A CA    1 
ATOM   11751 C  C     . GLU A 1 3016 ? 151.605 184.442 192.438 1.00 55.65  ? 3016 GLU A C     1 
ATOM   11752 O  O     . GLU A 1 3016 ? 152.646 184.847 191.916 1.00 54.63  ? 3016 GLU A O     1 
ATOM   11753 C  CB    . GLU A 1 3016 ? 150.694 185.983 194.199 1.00 46.78  ? 3016 GLU A CB    1 
ATOM   11754 C  CG    . GLU A 1 3016 ? 151.586 187.194 193.962 1.00 51.44  ? 3016 GLU A CG    1 
ATOM   11755 C  CD    . GLU A 1 3016 ? 151.576 187.664 192.521 1.00 60.60  ? 3016 GLU A CD    1 
ATOM   11756 O  OE1   . GLU A 1 3016 ? 150.626 187.319 191.787 1.00 60.80  ? 3016 GLU A OE1   1 
ATOM   11757 O  OE2   . GLU A 1 3016 ? 152.518 188.382 192.124 1.00 61.14  ? 3016 GLU A OE2   1 
ATOM   11758 N  N     . VAL A 1 3017 ? 150.643 183.821 191.768 1.00 54.92  ? 3017 VAL A N     1 
ATOM   11759 C  CA    . VAL A 1 3017 ? 150.675 183.635 190.320 1.00 54.44  ? 3017 VAL A CA    1 
ATOM   11760 C  C     . VAL A 1 3017 ? 149.751 184.675 189.697 1.00 59.34  ? 3017 VAL A C     1 
ATOM   11761 O  O     . VAL A 1 3017 ? 148.559 184.707 190.040 1.00 57.59  ? 3017 VAL A O     1 
ATOM   11762 C  CB    . VAL A 1 3017 ? 150.255 182.213 189.922 1.00 52.91  ? 3017 VAL A CB    1 
ATOM   11763 C  CG1   . VAL A 1 3017 ? 150.216 182.080 188.411 1.00 51.63  ? 3017 VAL A CG1   1 
ATOM   11764 C  CG2   . VAL A 1 3017 ? 151.203 181.192 190.530 1.00 44.44  ? 3017 VAL A CG2   1 
ATOM   11765 N  N     . PRO A 1 3018 ? 150.243 185.536 188.802 1.00 62.70  ? 3018 PRO A N     1 
ATOM   11766 C  CA    . PRO A 1 3018 ? 149.380 186.613 188.287 1.00 65.61  ? 3018 PRO A CA    1 
ATOM   11767 C  C     . PRO A 1 3018 ? 148.224 186.113 187.438 1.00 65.05  ? 3018 PRO A C     1 
ATOM   11768 O  O     . PRO A 1 3018 ? 147.092 186.582 187.610 1.00 64.53  ? 3018 PRO A O     1 
ATOM   11769 C  CB    . PRO A 1 3018 ? 150.354 187.479 187.476 1.00 58.50  ? 3018 PRO A CB    1 
ATOM   11770 C  CG    . PRO A 1 3018 ? 151.441 186.539 187.072 1.00 63.81  ? 3018 PRO A CG    1 
ATOM   11771 C  CD    . PRO A 1 3018 ? 151.591 185.567 188.208 1.00 62.49  ? 3018 PRO A CD    1 
ATOM   11772 N  N     . GLY A 1 3019 ? 148.471 185.177 186.528 1.00 51.67  ? 3019 GLY A N     1 
ATOM   11773 C  CA    . GLY A 1 3019 ? 147.441 184.682 185.642 1.00 49.36  ? 3019 GLY A CA    1 
ATOM   11774 C  C     . GLY A 1 3019 ? 146.599 183.549 186.176 1.00 63.19  ? 3019 GLY A C     1 
ATOM   11775 O  O     . GLY A 1 3019 ? 145.737 183.040 185.454 1.00 77.16  ? 3019 GLY A O     1 
ATOM   11776 N  N     . LEU A 1 3020 ? 146.821 183.130 187.423 1.00 60.72  ? 3020 LEU A N     1 
ATOM   11777 C  CA    . LEU A 1 3020 ? 146.048 182.025 187.981 1.00 54.09  ? 3020 LEU A CA    1 
ATOM   11778 C  C     . LEU A 1 3020 ? 144.592 182.423 188.194 1.00 52.84  ? 3020 LEU A C     1 
ATOM   11779 O  O     . LEU A 1 3020 ? 143.674 181.694 187.803 1.00 55.52  ? 3020 LEU A O     1 
ATOM   11780 C  CB    . LEU A 1 3020 ? 146.677 181.556 189.292 1.00 50.04  ? 3020 LEU A CB    1 
ATOM   11781 C  CG    . LEU A 1 3020 ? 146.339 180.135 189.742 1.00 40.34  ? 3020 LEU A CG    1 
ATOM   11782 C  CD1   . LEU A 1 3020 ? 146.978 179.115 188.816 1.00 39.70  ? 3020 LEU A CD1   1 
ATOM   11783 C  CD2   . LEU A 1 3020 ? 146.780 179.910 191.178 1.00 37.48  ? 3020 LEU A CD2   1 
ATOM   11784 N  N     . PHE A 1 3021 ? 144.363 183.578 188.812 1.00 53.79  ? 3021 PHE A N     1 
ATOM   11785 C  CA    . PHE A 1 3021 ? 143.016 184.069 189.096 1.00 57.55  ? 3021 PHE A CA    1 
ATOM   11786 C  C     . PHE A 1 3021 ? 142.648 185.097 188.031 1.00 70.92  ? 3021 PHE A C     1 
ATOM   11787 O  O     . PHE A 1 3021 ? 143.173 186.213 188.021 1.00 76.52  ? 3021 PHE A O     1 
ATOM   11788 C  CB    . PHE A 1 3021 ? 142.937 184.666 190.497 1.00 53.91  ? 3021 PHE A CB    1 
ATOM   11789 C  CG    . PHE A 1 3021 ? 143.149 183.666 191.598 1.00 46.50  ? 3021 PHE A CG    1 
ATOM   11790 C  CD1   . PHE A 1 3021 ? 144.425 183.353 192.032 1.00 50.56  ? 3021 PHE A CD1   1 
ATOM   11791 C  CD2   . PHE A 1 3021 ? 142.070 183.044 192.202 1.00 51.92  ? 3021 PHE A CD2   1 
ATOM   11792 C  CE1   . PHE A 1 3021 ? 144.622 182.436 193.047 1.00 46.27  ? 3021 PHE A CE1   1 
ATOM   11793 C  CE2   . PHE A 1 3021 ? 142.260 182.126 193.217 1.00 50.73  ? 3021 PHE A CE2   1 
ATOM   11794 C  CZ    . PHE A 1 3021 ? 143.538 181.822 193.639 1.00 44.67  ? 3021 PHE A CZ    1 
ATOM   11795 N  N     . GLU A 1 3022 ? 141.744 184.716 187.132 1.00 75.80  ? 3022 GLU A N     1 
ATOM   11796 C  CA    . GLU A 1 3022 ? 141.245 185.613 186.103 1.00 75.52  ? 3022 GLU A CA    1 
ATOM   11797 C  C     . GLU A 1 3022 ? 139.787 185.283 185.821 1.00 79.21  ? 3022 GLU A C     1 
ATOM   11798 O  O     . GLU A 1 3022 ? 139.353 184.138 185.974 1.00 80.42  ? 3022 GLU A O     1 
ATOM   11799 C  CB    . GLU A 1 3022 ? 142.076 185.516 184.816 1.00 72.76  ? 3022 GLU A CB    1 
ATOM   11800 C  CG    . GLU A 1 3022 ? 142.198 184.110 184.255 1.00 76.93  ? 3022 GLU A CG    1 
ATOM   11801 C  CD    . GLU A 1 3022 ? 143.027 184.060 182.987 1.00 85.78  ? 3022 GLU A CD    1 
ATOM   11802 O  OE1   . GLU A 1 3022 ? 144.135 184.636 182.977 1.00 81.66  ? 3022 GLU A OE1   1 
ATOM   11803 O  OE2   . GLU A 1 3022 ? 142.571 183.445 182.000 1.00 91.15  ? 3022 GLU A OE2   1 
ATOM   11804 N  N     . GLY A 1 3023 ? 139.034 186.299 185.407 1.00 78.41  ? 3023 GLY A N     1 
ATOM   11805 C  CA    . GLY A 1 3023 ? 137.618 186.127 185.149 1.00 79.20  ? 3023 GLY A CA    1 
ATOM   11806 C  C     . GLY A 1 3023 ? 136.791 186.101 186.418 1.00 77.95  ? 3023 GLY A C     1 
ATOM   11807 O  O     . GLY A 1 3023 ? 137.049 186.871 187.348 1.00 71.67  ? 3023 GLY A O     1 
ATOM   11808 N  N     . ASP A 1 3024 ? 135.788 185.220 186.465 1.00 80.48  ? 3024 ASP A N     1 
ATOM   11809 C  CA    . ASP A 1 3024 ? 134.975 185.089 187.671 1.00 79.72  ? 3024 ASP A CA    1 
ATOM   11810 C  C     . ASP A 1 3024 ? 135.799 184.581 188.846 1.00 80.10  ? 3024 ASP A C     1 
ATOM   11811 O  O     . ASP A 1 3024 ? 135.473 184.868 190.006 1.00 81.36  ? 3024 ASP A O     1 
ATOM   11812 C  CB    . ASP A 1 3024 ? 133.792 184.158 187.407 1.00 82.31  ? 3024 ASP A CB    1 
ATOM   11813 C  CG    . ASP A 1 3024 ? 132.539 184.583 188.147 1.00 92.05  ? 3024 ASP A CG    1 
ATOM   11814 O  OD1   . ASP A 1 3024 ? 132.647 184.973 189.329 1.00 91.53  ? 3024 ASP A OD1   1 
ATOM   11815 O  OD2   . ASP A 1 3024 ? 131.445 184.527 187.548 1.00 92.17  ? 3024 ASP A OD2   1 
ATOM   11816 N  N     . GLU A 1 3025 ? 136.865 183.826 188.568 1.00 77.97  ? 3025 GLU A N     1 
ATOM   11817 C  CA    . GLU A 1 3025 ? 137.759 183.383 189.633 1.00 74.45  ? 3025 GLU A CA    1 
ATOM   11818 C  C     . GLU A 1 3025 ? 138.385 184.572 190.346 1.00 73.16  ? 3025 GLU A C     1 
ATOM   11819 O  O     . GLU A 1 3025 ? 138.480 184.587 191.577 1.00 71.85  ? 3025 GLU A O     1 
ATOM   11820 C  CB    . GLU A 1 3025 ? 138.845 182.470 189.063 1.00 74.72  ? 3025 GLU A CB    1 
ATOM   11821 C  CG    . GLU A 1 3025 ? 138.326 181.364 188.160 1.00 80.51  ? 3025 GLU A CG    1 
ATOM   11822 C  CD    . GLU A 1 3025 ? 138.106 180.061 188.903 1.00 86.10  ? 3025 GLU A CD    1 
ATOM   11823 O  OE1   . GLU A 1 3025 ? 138.694 179.891 189.991 1.00 82.88  ? 3025 GLU A OE1   1 
ATOM   11824 O  OE2   . GLU A 1 3025 ? 137.347 179.208 188.397 1.00 87.05  ? 3025 GLU A OE2   1 
ATOM   11825 N  N     . TYR A 1 3026 ? 138.811 185.584 189.587 1.00 72.79  ? 3026 TYR A N     1 
ATOM   11826 C  CA    . TYR A 1 3026 ? 139.386 186.780 190.193 1.00 70.16  ? 3026 TYR A CA    1 
ATOM   11827 C  C     . TYR A 1 3026 ? 138.361 187.509 191.054 1.00 75.33  ? 3026 TYR A C     1 
ATOM   11828 O  O     . TYR A 1 3026 ? 138.682 187.982 192.151 1.00 71.55  ? 3026 TYR A O     1 
ATOM   11829 C  CB    . TYR A 1 3026 ? 139.926 187.698 189.096 1.00 66.87  ? 3026 TYR A CB    1 
ATOM   11830 C  CG    . TYR A 1 3026 ? 140.832 188.807 189.579 1.00 63.76  ? 3026 TYR A CG    1 
ATOM   11831 C  CD1   . TYR A 1 3026 ? 142.161 188.557 189.888 1.00 64.90  ? 3026 TYR A CD1   1 
ATOM   11832 C  CD2   . TYR A 1 3026 ? 140.365 190.109 189.700 1.00 65.82  ? 3026 TYR A CD2   1 
ATOM   11833 C  CE1   . TYR A 1 3026 ? 142.997 189.567 190.319 1.00 66.10  ? 3026 TYR A CE1   1 
ATOM   11834 C  CE2   . TYR A 1 3026 ? 141.195 191.127 190.130 1.00 70.55  ? 3026 TYR A CE2   1 
ATOM   11835 C  CZ    . TYR A 1 3026 ? 142.510 190.850 190.436 1.00 71.84  ? 3026 TYR A CZ    1 
ATOM   11836 O  OH    . TYR A 1 3026 ? 143.342 191.860 190.864 1.00 71.85  ? 3026 TYR A OH    1 
ATOM   11837 N  N     . ALA A 1 3027 ? 137.117 187.604 190.575 1.00 73.18  ? 3027 ALA A N     1 
ATOM   11838 C  CA    . ALA A 1 3027 ? 136.078 188.299 191.330 1.00 63.86  ? 3027 ALA A CA    1 
ATOM   11839 C  C     . ALA A 1 3027 ? 135.765 187.580 192.637 1.00 70.78  ? 3027 ALA A C     1 
ATOM   11840 O  O     . ALA A 1 3027 ? 135.664 188.213 193.697 1.00 76.20  ? 3027 ALA A O     1 
ATOM   11841 C  CB    . ALA A 1 3027 ? 134.818 188.440 190.476 1.00 62.04  ? 3027 ALA A CB    1 
ATOM   11842 N  N     . THR A 1 3028 ? 135.610 186.254 192.588 1.00 70.93  ? 3028 THR A N     1 
ATOM   11843 C  CA    . THR A 1 3028 ? 135.326 185.526 193.820 1.00 72.01  ? 3028 THR A CA    1 
ATOM   11844 C  C     . THR A 1 3028 ? 136.533 185.515 194.752 1.00 69.90  ? 3028 THR A C     1 
ATOM   11845 O  O     . THR A 1 3028 ? 136.366 185.520 195.978 1.00 69.54  ? 3028 THR A O     1 
ATOM   11846 C  CB    . THR A 1 3028 ? 134.850 184.102 193.511 1.00 74.22  ? 3028 THR A CB    1 
ATOM   11847 O  OG1   . THR A 1 3028 ? 134.430 183.463 194.724 1.00 82.46  ? 3028 THR A OG1   1 
ATOM   11848 C  CG2   . THR A 1 3028 ? 135.946 183.275 192.864 1.00 68.49  ? 3028 THR A CG2   1 
ATOM   11849 N  N     . LEU A 1 3029 ? 137.751 185.529 194.199 1.00 67.59  ? 3029 LEU A N     1 
ATOM   11850 C  CA    . LEU A 1 3029 ? 138.939 185.653 195.033 1.00 66.30  ? 3029 LEU A CA    1 
ATOM   11851 C  C     . LEU A 1 3029 ? 138.959 186.989 195.759 1.00 66.60  ? 3029 LEU A C     1 
ATOM   11852 O  O     . LEU A 1 3029 ? 139.280 187.050 196.949 1.00 68.71  ? 3029 LEU A O     1 
ATOM   11853 C  CB    . LEU A 1 3029 ? 140.200 185.489 194.187 1.00 62.26  ? 3029 LEU A CB    1 
ATOM   11854 C  CG    . LEU A 1 3029 ? 141.503 185.910 194.871 1.00 54.42  ? 3029 LEU A CG    1 
ATOM   11855 C  CD1   . LEU A 1 3029 ? 141.976 184.834 195.836 1.00 53.99  ? 3029 LEU A CD1   1 
ATOM   11856 C  CD2   . LEU A 1 3029 ? 142.581 186.239 193.852 1.00 45.30  ? 3029 LEU A CD2   1 
ATOM   11857 N  N     . MET A 1 3030 ? 138.620 188.074 195.058 1.00 63.82  ? 3030 MET A N     1 
ATOM   11858 C  CA    . MET A 1 3030 ? 138.568 189.380 195.708 1.00 63.51  ? 3030 MET A CA    1 
ATOM   11859 C  C     . MET A 1 3030 ? 137.469 189.438 196.760 1.00 68.24  ? 3030 MET A C     1 
ATOM   11860 O  O     . MET A 1 3030 ? 137.653 190.046 197.819 1.00 71.61  ? 3030 MET A O     1 
ATOM   11861 C  CB    . MET A 1 3030 ? 138.392 190.486 194.670 1.00 62.65  ? 3030 MET A CB    1 
ATOM   11862 C  CG    . MET A 1 3030 ? 139.618 190.678 193.809 1.00 66.39  ? 3030 MET A CG    1 
ATOM   11863 S  SD    . MET A 1 3030 ? 141.080 190.666 194.864 1.00 73.02  ? 3030 MET A SD    1 
ATOM   11864 C  CE    . MET A 1 3030 ? 142.291 191.423 193.794 1.00 63.80  ? 3030 MET A CE    1 
ATOM   11865 N  N     . THR A 1 3031 ? 136.322 188.812 196.493 1.00 71.31  ? 3031 THR A N     1 
ATOM   11866 C  CA    . THR A 1 3031 ? 135.272 188.751 197.507 1.00 71.48  ? 3031 THR A CA    1 
ATOM   11867 C  C     . THR A 1 3031 ? 135.766 188.036 198.763 1.00 70.39  ? 3031 THR A C     1 
ATOM   11868 O  O     . THR A 1 3031 ? 135.666 188.568 199.880 1.00 68.95  ? 3031 THR A O     1 
ATOM   11869 C  CB    . THR A 1 3031 ? 134.034 188.055 196.938 1.00 68.83  ? 3031 THR A CB    1 
ATOM   11870 O  OG1   . THR A 1 3031 ? 133.588 188.751 195.768 1.00 69.87  ? 3031 THR A OG1   1 
ATOM   11871 C  CG2   . THR A 1 3031 ? 132.913 188.040 197.962 1.00 69.93  ? 3031 THR A CG2   1 
ATOM   11872 N  N     . GLN A 1 3032 ? 136.324 186.834 198.591 1.00 67.16  ? 3032 GLN A N     1 
ATOM   11873 C  CA    . GLN A 1 3032 ? 136.820 186.070 199.731 1.00 63.43  ? 3032 GLN A CA    1 
ATOM   11874 C  C     . GLN A 1 3032 ? 137.930 186.817 200.457 1.00 65.40  ? 3032 GLN A C     1 
ATOM   11875 O  O     . GLN A 1 3032 ? 138.018 186.764 201.688 1.00 67.35  ? 3032 GLN A O     1 
ATOM   11876 C  CB    . GLN A 1 3032 ? 137.306 184.696 199.272 1.00 65.35  ? 3032 GLN A CB    1 
ATOM   11877 C  CG    . GLN A 1 3032 ? 136.196 183.674 199.093 1.00 72.28  ? 3032 GLN A CG    1 
ATOM   11878 C  CD    . GLN A 1 3032 ? 136.333 182.882 197.809 1.00 77.66  ? 3032 GLN A CD    1 
ATOM   11879 O  OE1   . GLN A 1 3032 ? 137.360 182.947 197.133 1.00 76.68  ? 3032 GLN A OE1   1 
ATOM   11880 N  NE2   . GLN A 1 3032 ? 135.297 182.127 197.465 1.00 80.38  ? 3032 GLN A NE2   1 
ATOM   11881 N  N     . CYS A 1 3033 ? 138.785 187.522 199.713 1.00 66.18  ? 3033 CYS A N     1 
ATOM   11882 C  CA    . CYS A 1 3033 ? 139.824 188.331 200.340 1.00 66.56  ? 3033 CYS A CA    1 
ATOM   11883 C  C     . CYS A 1 3033 ? 139.217 189.475 201.139 1.00 71.97  ? 3033 CYS A C     1 
ATOM   11884 O  O     . CYS A 1 3033 ? 139.751 189.863 202.182 1.00 72.05  ? 3033 CYS A O     1 
ATOM   11885 C  CB    . CYS A 1 3033 ? 140.783 188.867 199.278 1.00 63.06  ? 3033 CYS A CB    1 
ATOM   11886 S  SG    . CYS A 1 3033 ? 141.947 187.645 198.636 1.00 74.46  ? 3033 CYS A SG    1 
ATOM   11887 N  N     . LYS A 1 3034 ? 138.103 190.034 200.660 1.00 75.55  ? 3034 LYS A N     1 
ATOM   11888 C  CA    . LYS A 1 3034 ? 137.429 191.088 201.410 1.00 72.28  ? 3034 LYS A CA    1 
ATOM   11889 C  C     . LYS A 1 3034 ? 136.903 190.563 202.740 1.00 73.75  ? 3034 LYS A C     1 
ATOM   11890 O  O     . LYS A 1 3034 ? 137.115 191.187 203.789 1.00 77.16  ? 3034 LYS A O     1 
ATOM   11891 C  CB    . LYS A 1 3034 ? 136.295 191.685 200.576 1.00 71.11  ? 3034 LYS A CB    1 
ATOM   11892 C  CG    . LYS A 1 3034 ? 135.589 192.872 201.223 1.00 76.10  ? 3034 LYS A CG    1 
ATOM   11893 C  CD    . LYS A 1 3034 ? 136.579 193.831 201.871 1.00 79.51  ? 3034 LYS A CD    1 
ATOM   11894 C  CE    . LYS A 1 3034 ? 135.866 194.997 202.536 1.00 79.31  ? 3034 LYS A CE    1 
ATOM   11895 N  NZ    . LYS A 1 3034 ? 135.594 194.730 203.976 1.00 80.21  ? 3034 LYS A NZ    1 
ATOM   11896 N  N     . GLU A 1 3035 ? 136.226 189.408 202.725 1.00 71.77  ? 3035 GLU A N     1 
ATOM   11897 C  CA    . GLU A 1 3035 ? 135.785 188.836 204.000 1.00 71.23  ? 3035 GLU A CA    1 
ATOM   11898 C  C     . GLU A 1 3035 ? 136.968 188.469 204.892 1.00 78.58  ? 3035 GLU A C     1 
ATOM   11899 O  O     . GLU A 1 3035 ? 136.908 188.655 206.113 1.00 82.35  ? 3035 GLU A O     1 
ATOM   11900 C  CB    . GLU A 1 3035 ? 134.865 187.619 203.826 1.00 70.61  ? 3035 GLU A CB    1 
ATOM   11901 C  CG    . GLU A 1 3035 ? 133.491 187.869 203.198 1.00 77.38  ? 3035 GLU A CG    1 
ATOM   11902 C  CD    . GLU A 1 3035 ? 133.522 188.183 201.729 1.00 79.91  ? 3035 GLU A CD    1 
ATOM   11903 O  OE1   . GLU A 1 3035 ? 133.288 189.351 201.355 1.00 76.19  ? 3035 GLU A OE1   1 
ATOM   11904 O  OE2   . GLU A 1 3035 ? 133.721 187.233 200.945 1.00 81.64  ? 3035 GLU A OE2   1 
ATOM   11905 N  N     . GLY A 1 3036 ? 138.048 187.944 204.311 1.00 75.10  ? 3036 GLY A N     1 
ATOM   11906 C  CA    . GLY A 1 3036 ? 139.211 187.603 205.114 1.00 71.21  ? 3036 GLY A CA    1 
ATOM   11907 C  C     . GLY A 1 3036 ? 139.846 188.813 205.773 1.00 75.12  ? 3036 GLY A C     1 
ATOM   11908 O  O     . GLY A 1 3036 ? 140.220 188.768 206.948 1.00 79.75  ? 3036 GLY A O     1 
ATOM   11909 N  N     . ALA A 1 3037 ? 139.980 189.909 205.025 1.00 72.30  ? 3037 ALA A N     1 
ATOM   11910 C  CA    . ALA A 1 3037 ? 140.526 191.138 205.588 1.00 73.80  ? 3037 ALA A CA    1 
ATOM   11911 C  C     . ALA A 1 3037 ? 139.607 191.708 206.659 1.00 84.44  ? 3037 ALA A C     1 
ATOM   11912 O  O     . ALA A 1 3037 ? 140.080 192.220 207.681 1.00 86.62  ? 3037 ALA A O     1 
ATOM   11913 C  CB    . ALA A 1 3037 ? 140.763 192.163 204.480 1.00 72.61  ? 3037 ALA A CB    1 
ATOM   11914 N  N     . GLN A 1 3038 ? 138.290 191.638 206.442 1.00 85.47  ? 3038 GLN A N     1 
ATOM   11915 C  CA    . GLN A 1 3038 ? 137.355 192.100 207.463 1.00 83.84  ? 3038 GLN A CA    1 
ATOM   11916 C  C     . GLN A 1 3038 ? 137.482 191.274 208.737 1.00 84.07  ? 3038 GLN A C     1 
ATOM   11917 O  O     . GLN A 1 3038 ? 137.438 191.818 209.846 1.00 84.29  ? 3038 GLN A O     1 
ATOM   11918 C  CB    . GLN A 1 3038 ? 135.925 192.049 206.927 1.00 86.90  ? 3038 GLN A CB    1 
ATOM   11919 C  CG    . GLN A 1 3038 ? 134.974 193.017 207.611 1.00 95.02  ? 3038 GLN A CG    1 
ATOM   11920 C  CD    . GLN A 1 3038 ? 133.539 192.845 207.155 1.00 97.71  ? 3038 GLN A CD    1 
ATOM   11921 O  OE1   . GLN A 1 3038 ? 133.279 192.350 206.058 1.00 96.81  ? 3038 GLN A OE1   1 
ATOM   11922 N  NE2   . GLN A 1 3038 ? 132.598 193.256 207.997 1.00 91.85  ? 3038 GLN A NE2   1 
ATOM   11923 N  N     . LYS A 1 3039 ? 137.636 189.955 208.596 1.00 81.88  ? 3039 LYS A N     1 
ATOM   11924 C  CA    . LYS A 1 3039 ? 137.838 189.102 209.763 1.00 78.81  ? 3039 LYS A CA    1 
ATOM   11925 C  C     . LYS A 1 3039 ? 139.146 189.435 210.471 1.00 79.96  ? 3039 LYS A C     1 
ATOM   11926 O  O     . LYS A 1 3039 ? 139.200 189.475 211.706 1.00 81.62  ? 3039 LYS A O     1 
ATOM   11927 C  CB    . LYS A 1 3039 ? 137.813 187.631 209.348 1.00 74.94  ? 3039 LYS A CB    1 
ATOM   11928 C  CG    . LYS A 1 3039 ? 136.444 187.127 208.924 1.00 74.06  ? 3039 LYS A CG    1 
ATOM   11929 C  CD    . LYS A 1 3039 ? 136.379 185.610 208.963 1.00 70.01  ? 3039 LYS A CD    1 
ATOM   11930 C  CE    . LYS A 1 3039 ? 136.405 185.091 210.391 1.00 63.25  ? 3039 LYS A CE    1 
ATOM   11931 N  NZ    . LYS A 1 3039 ? 135.567 183.872 210.552 1.00 59.71  ? 3039 LYS A NZ    1 
ATOM   11932 N  N     . GLU A 1 3040 ? 140.213 189.677 209.706 1.00 82.98  ? 3040 GLU A N     1 
ATOM   11933 C  CA    . GLU A 1 3040 ? 141.500 190.011 210.305 1.00 83.65  ? 3040 GLU A CA    1 
ATOM   11934 C  C     . GLU A 1 3040 ? 141.513 191.410 210.909 1.00 88.85  ? 3040 GLU A C     1 
ATOM   11935 O  O     . GLU A 1 3040 ? 142.434 191.737 211.664 1.00 87.25  ? 3040 GLU A O     1 
ATOM   11936 C  CB    . GLU A 1 3040 ? 142.614 189.879 209.264 1.00 80.79  ? 3040 GLU A CB    1 
ATOM   11937 C  CG    . GLU A 1 3040 ? 144.003 189.688 209.856 1.00 84.52  ? 3040 GLU A CG    1 
ATOM   11938 C  CD    . GLU A 1 3040 ? 145.109 189.940 208.850 1.00 78.48  ? 3040 GLU A CD    1 
ATOM   11939 O  OE1   . GLU A 1 3040 ? 144.886 189.697 207.646 1.00 71.81  ? 3040 GLU A OE1   1 
ATOM   11940 O  OE2   . GLU A 1 3040 ? 146.201 190.383 209.263 1.00 76.50  ? 3040 GLU A OE2   1 
ATOM   11941 N  N     . GLY A 1 3041 ? 140.516 192.234 210.604 1.00 89.17  ? 3041 GLY A N     1 
ATOM   11942 C  CA    . GLY A 1 3041 ? 140.447 193.582 211.126 1.00 85.37  ? 3041 GLY A CA    1 
ATOM   11943 C  C     . GLY A 1 3041 ? 140.962 194.667 210.209 1.00 84.62  ? 3041 GLY A C     1 
ATOM   11944 O  O     . GLY A 1 3041 ? 141.107 195.810 210.656 1.00 82.30  ? 3041 GLY A O     1 
ATOM   11945 N  N     . LEU A 1 3042 ? 141.244 194.352 208.948 1.00 86.63  ? 3042 LEU A N     1 
ATOM   11946 C  CA    . LEU A 1 3042 ? 141.747 195.325 207.988 1.00 83.34  ? 3042 LEU A CA    1 
ATOM   11947 C  C     . LEU A 1 3042 ? 140.636 195.709 207.020 1.00 85.26  ? 3042 LEU A C     1 
ATOM   11948 O  O     . LEU A 1 3042 ? 139.966 194.837 206.457 1.00 83.41  ? 3042 LEU A O     1 
ATOM   11949 C  CB    . LEU A 1 3042 ? 142.945 194.764 207.221 1.00 72.93  ? 3042 LEU A CB    1 
ATOM   11950 C  CG    . LEU A 1 3042 ? 144.150 194.336 208.061 1.00 78.90  ? 3042 LEU A CG    1 
ATOM   11951 C  CD1   . LEU A 1 3042 ? 145.189 193.647 207.192 1.00 80.19  ? 3042 LEU A CD1   1 
ATOM   11952 C  CD2   . LEU A 1 3042 ? 144.756 195.529 208.782 1.00 79.36  ? 3042 LEU A CD2   1 
ATOM   11953 N  N     . MET A 1 3043 ? 140.444 197.013 206.831 1.00 85.26  ? 3043 MET A N     1 
ATOM   11954 C  CA    . MET A 1 3043 ? 139.424 197.537 205.923 1.00 81.98  ? 3043 MET A CA    1 
ATOM   11955 C  C     . MET A 1 3043 ? 140.117 197.960 204.631 1.00 79.12  ? 3043 MET A C     1 
ATOM   11956 O  O     . MET A 1 3043 ? 140.642 199.068 204.517 1.00 76.29  ? 3043 MET A O     1 
ATOM   11957 C  CB    . MET A 1 3043 ? 138.668 198.695 206.565 1.00 78.16  ? 3043 MET A CB    1 
ATOM   11958 C  CG    . MET A 1 3043 ? 137.847 198.301 207.782 1.00 90.82  ? 3043 MET A CG    1 
ATOM   11959 S  SD    . MET A 1 3043 ? 136.520 197.147 207.382 1.00 126.05 ? 3043 MET A SD    1 
ATOM   11960 C  CE    . MET A 1 3043 ? 135.934 196.725 209.021 1.00 107.43 ? 3043 MET A CE    1 
ATOM   11961 N  N     . LEU A 1 3044 ? 140.115 197.063 203.650 1.00 71.36  ? 3044 LEU A N     1 
ATOM   11962 C  CA    . LEU A 1 3044 ? 140.689 197.328 202.340 1.00 67.05  ? 3044 LEU A CA    1 
ATOM   11963 C  C     . LEU A 1 3044 ? 139.573 197.505 201.319 1.00 71.32  ? 3044 LEU A C     1 
ATOM   11964 O  O     . LEU A 1 3044 ? 138.639 196.700 201.259 1.00 73.57  ? 3044 LEU A O     1 
ATOM   11965 C  CB    . LEU A 1 3044 ? 141.622 196.195 201.912 1.00 65.97  ? 3044 LEU A CB    1 
ATOM   11966 C  CG    . LEU A 1 3044 ? 142.738 195.843 202.899 1.00 66.55  ? 3044 LEU A CG    1 
ATOM   11967 C  CD1   . LEU A 1 3044 ? 143.195 194.406 202.706 1.00 56.94  ? 3044 LEU A CD1   1 
ATOM   11968 C  CD2   . LEU A 1 3044 ? 143.906 196.806 202.763 1.00 60.23  ? 3044 LEU A CD2   1 
ATOM   11969 N  N     . ASP A 1 3045 ? 139.674 198.564 200.517 1.00 78.52  ? 3045 ASP A N     1 
ATOM   11970 C  CA    . ASP A 1 3045 ? 138.612 198.943 199.593 1.00 87.98  ? 3045 ASP A CA    1 
ATOM   11971 C  C     . ASP A 1 3045 ? 138.878 198.470 198.169 1.00 84.94  ? 3045 ASP A C     1 
ATOM   11972 O  O     . ASP A 1 3045 ? 138.072 197.724 197.606 1.00 74.05  ? 3045 ASP A O     1 
ATOM   11973 C  CB    . ASP A 1 3045 ? 138.418 200.466 199.621 1.00 88.80  ? 3045 ASP A CB    1 
ATOM   11974 C  CG    . ASP A 1 3045 ? 137.200 200.912 198.837 1.00 87.75  ? 3045 ASP A CG    1 
ATOM   11975 O  OD1   . ASP A 1 3045 ? 136.083 200.869 199.395 1.00 86.99  ? 3045 ASP A OD1   1 
ATOM   11976 O  OD2   . ASP A 1 3045 ? 137.358 201.305 197.662 1.00 82.95  ? 3045 ASP A OD2   1 
ATOM   11977 N  N     . SER A 1 3046 ? 139.991 198.881 197.568 1.00 84.70  ? 3046 SER A N     1 
ATOM   11978 C  CA    . SER A 1 3046 ? 140.235 198.562 196.171 1.00 81.15  ? 3046 SER A CA    1 
ATOM   11979 C  C     . SER A 1 3046 ? 140.908 197.200 196.034 1.00 78.03  ? 3046 SER A C     1 
ATOM   11980 O  O     . SER A 1 3046 ? 141.410 196.620 197.000 1.00 74.07  ? 3046 SER A O     1 
ATOM   11981 C  CB    . SER A 1 3046 ? 141.091 199.641 195.507 1.00 79.28  ? 3046 SER A CB    1 
ATOM   11982 O  OG    . SER A 1 3046 ? 142.408 199.642 196.024 1.00 80.54  ? 3046 SER A OG    1 
ATOM   11983 N  N     . HIS A 1 3047 ? 140.909 196.691 194.799 1.00 77.23  ? 3047 HIS A N     1 
ATOM   11984 C  CA    . HIS A 1 3047 ? 141.440 195.357 194.542 1.00 69.60  ? 3047 HIS A CA    1 
ATOM   11985 C  C     . HIS A 1 3047 ? 142.955 195.302 194.696 1.00 66.47  ? 3047 HIS A C     1 
ATOM   11986 O  O     . HIS A 1 3047 ? 143.506 194.227 194.953 1.00 68.74  ? 3047 HIS A O     1 
ATOM   11987 C  CB    . HIS A 1 3047 ? 141.036 194.896 193.142 1.00 72.21  ? 3047 HIS A CB    1 
ATOM   11988 C  CG    . HIS A 1 3047 ? 139.588 194.536 193.019 1.00 73.75  ? 3047 HIS A CG    1 
ATOM   11989 N  ND1   . HIS A 1 3047 ? 139.033 194.076 191.844 1.00 71.95  ? 3047 HIS A ND1   1 
ATOM   11990 C  CD2   . HIS A 1 3047 ? 138.581 194.569 193.923 1.00 69.93  ? 3047 HIS A CD2   1 
ATOM   11991 C  CE1   . HIS A 1 3047 ? 137.747 193.841 192.030 1.00 69.66  ? 3047 HIS A CE1   1 
ATOM   11992 N  NE2   . HIS A 1 3047 ? 137.447 194.131 193.282 1.00 71.66  ? 3047 HIS A NE2   1 
ATOM   11993 N  N     . GLU A 1 3048 ? 143.644 196.433 194.533 1.00 69.78  ? 3048 GLU A N     1 
ATOM   11994 C  CA    . GLU A 1 3048 ? 145.103 196.423 194.589 1.00 68.53  ? 3048 GLU A CA    1 
ATOM   11995 C  C     . GLU A 1 3048 ? 145.603 196.032 195.975 1.00 68.06  ? 3048 GLU A C     1 
ATOM   11996 O  O     . GLU A 1 3048 ? 146.403 195.098 196.120 1.00 68.98  ? 3048 GLU A O     1 
ATOM   11997 C  CB    . GLU A 1 3048 ? 145.648 197.792 194.183 1.00 74.34  ? 3048 GLU A CB    1 
ATOM   11998 C  CG    . GLU A 1 3048 ? 145.516 198.092 192.699 1.00 93.12  ? 3048 GLU A CG    1 
ATOM   11999 C  CD    . GLU A 1 3048 ? 146.159 199.407 192.308 1.00 106.70 ? 3048 GLU A CD    1 
ATOM   12000 O  OE1   . GLU A 1 3048 ? 146.403 200.242 193.204 1.00 101.42 ? 3048 GLU A OE1   1 
ATOM   12001 O  OE2   . GLU A 1 3048 ? 146.419 199.605 191.103 1.00 100.37 ? 3048 GLU A OE2   1 
ATOM   12002 N  N     . GLU A 1 3049 ? 145.127 196.723 197.013 1.00 65.13  ? 3049 GLU A N     1 
ATOM   12003 C  CA    . GLU A 1 3049 ? 145.553 196.381 198.366 1.00 58.48  ? 3049 GLU A CA    1 
ATOM   12004 C  C     . GLU A 1 3049 ? 145.008 195.027 198.797 1.00 55.10  ? 3049 GLU A C     1 
ATOM   12005 O  O     . GLU A 1 3049 ? 145.653 194.328 199.584 1.00 55.53  ? 3049 GLU A O     1 
ATOM   12006 C  CB    . GLU A 1 3049 ? 145.133 197.468 199.355 1.00 64.12  ? 3049 GLU A CB    1 
ATOM   12007 C  CG    . GLU A 1 3049 ? 145.516 198.877 198.936 1.00 70.19  ? 3049 GLU A CG    1 
ATOM   12008 C  CD    . GLU A 1 3049 ? 144.386 199.608 198.245 1.00 83.02  ? 3049 GLU A CD    1 
ATOM   12009 O  OE1   . GLU A 1 3049 ? 143.368 198.961 197.924 1.00 81.60  ? 3049 GLU A OE1   1 
ATOM   12010 O  OE2   . GLU A 1 3049 ? 144.516 200.831 198.023 1.00 84.53  ? 3049 GLU A OE2   1 
ATOM   12011 N  N     . LEU A 1 3050 ? 143.840 194.634 198.285 1.00 56.56  ? 3050 LEU A N     1 
ATOM   12012 C  CA    . LEU A 1 3050 ? 143.319 193.304 198.579 1.00 56.54  ? 3050 LEU A CA    1 
ATOM   12013 C  C     . LEU A 1 3050 ? 144.255 192.225 198.049 1.00 51.98  ? 3050 LEU A C     1 
ATOM   12014 O  O     . LEU A 1 3050 ? 144.565 191.253 198.749 1.00 51.45  ? 3050 LEU A O     1 
ATOM   12015 C  CB    . LEU A 1 3050 ? 141.920 193.146 197.984 1.00 56.67  ? 3050 LEU A CB    1 
ATOM   12016 C  CG    . LEU A 1 3050 ? 140.750 193.579 198.869 1.00 55.62  ? 3050 LEU A CG    1 
ATOM   12017 C  CD1   . LEU A 1 3050 ? 139.435 193.445 198.119 1.00 65.88  ? 3050 LEU A CD1   1 
ATOM   12018 C  CD2   . LEU A 1 3050 ? 140.723 192.772 200.157 1.00 53.86  ? 3050 LEU A CD2   1 
ATOM   12019 N  N     . TYR A 1 3051 ? 144.736 192.390 196.814 1.00 51.65  ? 3051 TYR A N     1 
ATOM   12020 C  CA    . TYR A 1 3051 ? 145.652 191.407 196.246 1.00 46.76  ? 3051 TYR A CA    1 
ATOM   12021 C  C     . TYR A 1 3051 ? 147.008 191.448 196.938 1.00 53.50  ? 3051 TYR A C     1 
ATOM   12022 O  O     . TYR A 1 3051 ? 147.650 190.407 197.112 1.00 56.01  ? 3051 TYR A O     1 
ATOM   12023 C  CB    . TYR A 1 3051 ? 145.810 191.633 194.744 1.00 44.09  ? 3051 TYR A CB    1 
ATOM   12024 C  CG    . TYR A 1 3051 ? 146.399 190.442 194.022 1.00 50.28  ? 3051 TYR A CG    1 
ATOM   12025 C  CD1   . TYR A 1 3051 ? 145.627 189.320 193.754 1.00 53.81  ? 3051 TYR A CD1   1 
ATOM   12026 C  CD2   . TYR A 1 3051 ? 147.726 190.436 193.618 1.00 50.76  ? 3051 TYR A CD2   1 
ATOM   12027 C  CE1   . TYR A 1 3051 ? 146.159 188.227 193.099 1.00 49.32  ? 3051 TYR A CE1   1 
ATOM   12028 C  CE2   . TYR A 1 3051 ? 148.268 189.347 192.962 1.00 50.22  ? 3051 TYR A CE2   1 
ATOM   12029 C  CZ    . TYR A 1 3051 ? 147.479 188.246 192.705 1.00 54.10  ? 3051 TYR A CZ    1 
ATOM   12030 O  OH    . TYR A 1 3051 ? 148.013 187.159 192.052 1.00 60.73  ? 3051 TYR A OH    1 
ATOM   12031 N  N     . LYS A 1 3052 ? 147.467 192.638 197.335 1.00 48.66  ? 3052 LYS A N     1 
ATOM   12032 C  CA    . LYS A 1 3052 ? 148.717 192.721 198.086 1.00 44.69  ? 3052 LYS A CA    1 
ATOM   12033 C  C     . LYS A 1 3052 ? 148.607 191.992 199.422 1.00 46.06  ? 3052 LYS A C     1 
ATOM   12034 O  O     . LYS A 1 3052 ? 149.524 191.261 199.820 1.00 52.96  ? 3052 LYS A O     1 
ATOM   12035 C  CB    . LYS A 1 3052 ? 149.112 194.182 198.300 1.00 49.82  ? 3052 LYS A CB    1 
ATOM   12036 C  CG    . LYS A 1 3052 ? 150.149 194.701 197.313 1.00 54.99  ? 3052 LYS A CG    1 
ATOM   12037 C  CD    . LYS A 1 3052 ? 149.506 195.171 196.020 1.00 58.70  ? 3052 LYS A CD    1 
ATOM   12038 C  CE    . LYS A 1 3052 ? 150.545 195.447 194.947 1.00 67.00  ? 3052 LYS A CE    1 
ATOM   12039 N  NZ    . LYS A 1 3052 ? 149.964 196.195 193.798 1.00 61.59  ? 3052 LYS A NZ    1 
ATOM   12040 N  N     . TRP A 1 3053 ? 147.487 192.174 200.125 1.00 41.23  ? 3053 TRP A N     1 
ATOM   12041 C  CA    . TRP A 1 3053 ? 147.270 191.469 201.384 1.00 39.27  ? 3053 TRP A CA    1 
ATOM   12042 C  C     . TRP A 1 3053 ? 147.162 189.966 201.164 1.00 41.80  ? 3053 TRP A C     1 
ATOM   12043 O  O     . TRP A 1 3053 ? 147.661 189.177 201.974 1.00 42.60  ? 3053 TRP A O     1 
ATOM   12044 C  CB    . TRP A 1 3053 ? 146.018 192.010 202.073 1.00 41.00  ? 3053 TRP A CB    1 
ATOM   12045 C  CG    . TRP A 1 3053 ? 145.569 191.200 203.248 1.00 44.34  ? 3053 TRP A CG    1 
ATOM   12046 C  CD1   . TRP A 1 3053 ? 145.948 191.362 204.548 1.00 45.64  ? 3053 TRP A CD1   1 
ATOM   12047 C  CD2   . TRP A 1 3053 ? 144.644 190.107 203.233 1.00 46.23  ? 3053 TRP A CD2   1 
ATOM   12048 N  NE1   . TRP A 1 3053 ? 145.321 190.434 205.343 1.00 48.37  ? 3053 TRP A NE1   1 
ATOM   12049 C  CE2   . TRP A 1 3053 ? 144.515 189.651 204.559 1.00 48.30  ? 3053 TRP A CE2   1 
ATOM   12050 C  CE3   . TRP A 1 3053 ? 143.916 189.467 202.226 1.00 49.39  ? 3053 TRP A CE3   1 
ATOM   12051 C  CZ2   . TRP A 1 3053 ? 143.688 188.586 204.904 1.00 53.82  ? 3053 TRP A CZ2   1 
ATOM   12052 C  CZ3   . TRP A 1 3053 ? 143.096 188.410 202.571 1.00 51.18  ? 3053 TRP A CZ3   1 
ATOM   12053 C  CH2   . TRP A 1 3053 ? 142.988 187.980 203.898 1.00 55.11  ? 3053 TRP A CH2   1 
ATOM   12054 N  N     . PHE A 1 3054 ? 146.505 189.551 200.078 1.00 44.74  ? 3054 PHE A N     1 
ATOM   12055 C  CA    . PHE A 1 3054 ? 146.429 188.129 199.754 1.00 39.66  ? 3054 PHE A CA    1 
ATOM   12056 C  C     . PHE A 1 3054 ? 147.815 187.547 199.507 1.00 39.07  ? 3054 PHE A C     1 
ATOM   12057 O  O     . PHE A 1 3054 ? 148.129 186.447 199.976 1.00 45.34  ? 3054 PHE A O     1 
ATOM   12058 C  CB    . PHE A 1 3054 ? 145.532 187.926 198.533 1.00 38.86  ? 3054 PHE A CB    1 
ATOM   12059 C  CG    . PHE A 1 3054 ? 145.526 186.520 198.007 1.00 43.53  ? 3054 PHE A CG    1 
ATOM   12060 C  CD1   . PHE A 1 3054 ? 144.850 185.517 198.680 1.00 45.03  ? 3054 PHE A CD1   1 
ATOM   12061 C  CD2   . PHE A 1 3054 ? 146.189 186.203 196.834 1.00 42.78  ? 3054 PHE A CD2   1 
ATOM   12062 C  CE1   . PHE A 1 3054 ? 144.840 184.225 198.195 1.00 40.39  ? 3054 PHE A CE1   1 
ATOM   12063 C  CE2   . PHE A 1 3054 ? 146.183 184.912 196.345 1.00 39.06  ? 3054 PHE A CE2   1 
ATOM   12064 C  CZ    . PHE A 1 3054 ? 145.508 183.922 197.027 1.00 40.20  ? 3054 PHE A CZ    1 
ATOM   12065 N  N     . THR A 1 3055 ? 148.657 188.276 198.771 1.00 41.48  ? 3055 THR A N     1 
ATOM   12066 C  CA    . THR A 1 3055 ? 150.022 187.821 198.526 1.00 39.90  ? 3055 THR A CA    1 
ATOM   12067 C  C     . THR A 1 3055 ? 150.809 187.717 199.825 1.00 37.39  ? 3055 THR A C     1 
ATOM   12068 O  O     . THR A 1 3055 ? 151.542 186.744 200.040 1.00 38.91  ? 3055 THR A O     1 
ATOM   12069 C  CB    . THR A 1 3055 ? 150.721 188.771 197.553 1.00 43.53  ? 3055 THR A CB    1 
ATOM   12070 O  OG1   . THR A 1 3055 ? 150.029 188.768 196.299 1.00 51.87  ? 3055 THR A OG1   1 
ATOM   12071 C  CG2   . THR A 1 3055 ? 152.166 188.347 197.335 1.00 42.86  ? 3055 THR A CG2   1 
ATOM   12072 N  N     . SER A 1 3056 ? 150.666 188.709 200.707 1.00 40.01  ? 3056 SER A N     1 
ATOM   12073 C  CA    . SER A 1 3056 ? 151.360 188.660 201.990 1.00 39.35  ? 3056 SER A CA    1 
ATOM   12074 C  C     . SER A 1 3056 ? 150.893 187.473 202.825 1.00 39.04  ? 3056 SER A C     1 
ATOM   12075 O  O     . SER A 1 3056 ? 151.706 186.796 203.466 1.00 39.16  ? 3056 SER A O     1 
ATOM   12076 C  CB    . SER A 1 3056 ? 151.150 189.969 202.751 1.00 38.88  ? 3056 SER A CB    1 
ATOM   12077 O  OG    . SER A 1 3056 ? 149.828 190.062 203.251 1.00 45.77  ? 3056 SER A OG    1 
ATOM   12078 N  N     . GLN A 1 3057 ? 149.585 187.204 202.827 1.00 37.12  ? 3057 GLN A N     1 
ATOM   12079 C  CA    . GLN A 1 3057 ? 149.060 186.070 203.580 1.00 35.63  ? 3057 GLN A CA    1 
ATOM   12080 C  C     . GLN A 1 3057 ? 149.569 184.748 203.020 1.00 33.22  ? 3057 GLN A C     1 
ATOM   12081 O  O     . GLN A 1 3057 ? 149.914 183.836 203.782 1.00 32.46  ? 3057 GLN A O     1 
ATOM   12082 C  CB    . GLN A 1 3057 ? 147.532 186.101 203.576 1.00 36.25  ? 3057 GLN A CB    1 
ATOM   12083 C  CG    . GLN A 1 3057 ? 146.934 187.100 204.548 1.00 39.40  ? 3057 GLN A CG    1 
ATOM   12084 C  CD    . GLN A 1 3057 ? 147.075 186.660 205.990 1.00 46.11  ? 3057 GLN A CD    1 
ATOM   12085 O  OE1   . GLN A 1 3057 ? 147.926 187.161 206.724 1.00 48.25  ? 3057 GLN A OE1   1 
ATOM   12086 N  NE2   . GLN A 1 3057 ? 146.237 185.718 206.405 1.00 50.31  ? 3057 GLN A NE2   1 
ATOM   12087 N  N     . VAL A 1 3058 ? 149.616 184.619 201.692 1.00 30.85  ? 3058 VAL A N     1 
ATOM   12088 C  CA    . VAL A 1 3058 ? 150.127 183.391 201.088 1.00 28.50  ? 3058 VAL A CA    1 
ATOM   12089 C  C     . VAL A 1 3058 ? 151.603 183.214 201.416 1.00 29.97  ? 3058 VAL A C     1 
ATOM   12090 O  O     . VAL A 1 3058 ? 152.064 182.100 201.692 1.00 32.85  ? 3058 VAL A O     1 
ATOM   12091 C  CB    . VAL A 1 3058 ? 149.877 183.392 199.568 1.00 28.01  ? 3058 VAL A CB    1 
ATOM   12092 C  CG1   . VAL A 1 3058 ? 150.571 182.208 198.919 1.00 29.21  ? 3058 VAL A CG1   1 
ATOM   12093 C  CG2   . VAL A 1 3058 ? 148.388 183.350 199.277 1.00 35.03  ? 3058 VAL A CG2   1 
ATOM   12094 N  N     . ILE A 1 3059 ? 152.366 184.309 201.396 1.00 33.42  ? 3059 ILE A N     1 
ATOM   12095 C  CA    . ILE A 1 3059 ? 153.782 184.240 201.747 1.00 28.99  ? 3059 ILE A CA    1 
ATOM   12096 C  C     . ILE A 1 3059 ? 153.950 183.792 203.194 1.00 27.66  ? 3059 ILE A C     1 
ATOM   12097 O  O     . ILE A 1 3059 ? 154.798 182.946 203.505 1.00 29.42  ? 3059 ILE A O     1 
ATOM   12098 C  CB    . ILE A 1 3059 ? 154.457 185.600 201.490 1.00 27.23  ? 3059 ILE A CB    1 
ATOM   12099 C  CG1   . ILE A 1 3059 ? 154.768 185.770 200.003 1.00 29.27  ? 3059 ILE A CG1   1 
ATOM   12100 C  CG2   . ILE A 1 3059 ? 155.720 185.747 202.325 1.00 25.03  ? 3059 ILE A CG2   1 
ATOM   12101 C  CD1   . ILE A 1 3059 ? 155.456 187.075 199.670 1.00 31.13  ? 3059 ILE A CD1   1 
ATOM   12102 N  N     . ARG A 1 3060 ? 153.140 184.344 204.098 1.00 28.70  ? 3060 ARG A N     1 
ATOM   12103 C  CA    . ARG A 1 3060 ? 153.289 184.035 205.516 1.00 28.94  ? 3060 ARG A CA    1 
ATOM   12104 C  C     . ARG A 1 3060 ? 152.851 182.608 205.835 1.00 32.16  ? 3060 ARG A C     1 
ATOM   12105 O  O     . ARG A 1 3060 ? 153.480 181.931 206.655 1.00 34.80  ? 3060 ARG A O     1 
ATOM   12106 C  CB    . ARG A 1 3060 ? 152.497 185.042 206.350 1.00 32.93  ? 3060 ARG A CB    1 
ATOM   12107 C  CG    . ARG A 1 3060 ? 152.286 184.637 207.799 1.00 39.95  ? 3060 ARG A CG    1 
ATOM   12108 C  CD    . ARG A 1 3060 ? 151.990 185.847 208.669 1.00 55.92  ? 3060 ARG A CD    1 
ATOM   12109 N  NE    . ARG A 1 3060 ? 150.610 186.297 208.536 1.00 60.74  ? 3060 ARG A NE    1 
ATOM   12110 C  CZ    . ARG A 1 3060 ? 149.570 185.711 209.116 1.00 58.37  ? 3060 ARG A CZ    1 
ATOM   12111 N  NH1   . ARG A 1 3060 ? 149.717 184.646 209.886 1.00 51.74  ? 3060 ARG A NH1   1 
ATOM   12112 N  NH2   . ARG A 1 3060 ? 148.353 186.210 208.920 1.00 57.97  ? 3060 ARG A NH2   1 
ATOM   12113 N  N     . ASN A 1 3061 ? 151.785 182.130 205.193 1.00 32.04  ? 3061 ASN A N     1 
ATOM   12114 C  CA    . ASN A 1 3061 ? 151.153 180.871 205.575 1.00 29.44  ? 3061 ASN A CA    1 
ATOM   12115 C  C     . ASN A 1 3061 ? 151.636 179.669 204.775 1.00 26.62  ? 3061 ASN A C     1 
ATOM   12116 O  O     . ASN A 1 3061 ? 151.929 178.623 205.361 1.00 30.64  ? 3061 ASN A O     1 
ATOM   12117 C  CB    . ASN A 1 3061 ? 149.632 180.984 205.435 1.00 27.85  ? 3061 ASN A CB    1 
ATOM   12118 C  CG    . ASN A 1 3061 ? 149.010 181.857 206.505 1.00 35.44  ? 3061 ASN A CG    1 
ATOM   12119 O  OD1   . ASN A 1 3061 ? 149.397 181.801 207.672 1.00 38.04  ? 3061 ASN A OD1   1 
ATOM   12120 N  ND2   . ASN A 1 3061 ? 148.039 182.671 206.112 1.00 41.82  ? 3061 ASN A ND2   1 
ATOM   12121 N  N     . LEU A 1 3062 ? 151.724 179.783 203.452 1.00 23.80  ? 3062 LEU A N     1 
ATOM   12122 C  CA    . LEU A 1 3062 ? 151.985 178.624 202.609 1.00 21.50  ? 3062 LEU A CA    1 
ATOM   12123 C  C     . LEU A 1 3062 ? 153.442 178.188 202.708 1.00 23.93  ? 3062 LEU A C     1 
ATOM   12124 O  O     . LEU A 1 3062 ? 154.357 179.011 202.604 1.00 28.51  ? 3062 LEU A O     1 
ATOM   12125 C  CB    . LEU A 1 3062 ? 151.629 178.933 201.155 1.00 25.47  ? 3062 LEU A CB    1 
ATOM   12126 C  CG    . LEU A 1 3062 ? 151.778 177.778 200.164 1.00 22.15  ? 3062 LEU A CG    1 
ATOM   12127 C  CD1   . LEU A 1 3062 ? 151.088 176.529 200.686 1.00 22.80  ? 3062 LEU A CD1   1 
ATOM   12128 C  CD2   . LEU A 1 3062 ? 151.229 178.165 198.801 1.00 22.68  ? 3062 LEU A CD2   1 
ATOM   12129 N  N     . HIS A 1 3063 ? 153.649 176.889 202.910 1.00 22.90  ? 3063 HIS A N     1 
ATOM   12130 C  CA    . HIS A 1 3063 ? 154.968 176.271 202.878 1.00 18.44  ? 3063 HIS A CA    1 
ATOM   12131 C  C     . HIS A 1 3063 ? 154.952 175.150 201.849 1.00 18.07  ? 3063 HIS A C     1 
ATOM   12132 O  O     . HIS A 1 3063 ? 154.041 174.317 201.850 1.00 23.81  ? 3063 HIS A O     1 
ATOM   12133 C  CB    . HIS A 1 3063 ? 155.363 175.722 204.251 1.00 14.26  ? 3063 HIS A CB    1 
ATOM   12134 C  CG    . HIS A 1 3063 ? 155.431 176.763 205.324 1.00 17.45  ? 3063 HIS A CG    1 
ATOM   12135 N  ND1   . HIS A 1 3063 ? 154.398 176.990 206.207 1.00 22.17  ? 3063 HIS A ND1   1 
ATOM   12136 C  CD2   . HIS A 1 3063 ? 156.410 177.637 205.658 1.00 20.73  ? 3063 HIS A CD2   1 
ATOM   12137 C  CE1   . HIS A 1 3063 ? 154.736 177.960 207.037 1.00 25.22  ? 3063 HIS A CE1   1 
ATOM   12138 N  NE2   . HIS A 1 3063 ? 155.952 178.370 206.725 1.00 25.19  ? 3063 HIS A NE2   1 
ATOM   12139 N  N     . VAL A 1 3064 ? 155.956 175.131 200.977 1.00 17.21  ? 3064 VAL A N     1 
ATOM   12140 C  CA    . VAL A 1 3064 ? 156.050 174.157 199.897 1.00 15.49  ? 3064 VAL A CA    1 
ATOM   12141 C  C     . VAL A 1 3064 ? 157.225 173.233 200.174 1.00 18.05  ? 3064 VAL A C     1 
ATOM   12142 O  O     . VAL A 1 3064 ? 158.351 173.696 200.394 1.00 20.51  ? 3064 VAL A O     1 
ATOM   12143 C  CB    . VAL A 1 3064 ? 156.205 174.844 198.529 1.00 13.53  ? 3064 VAL A CB    1 
ATOM   12144 C  CG1   . VAL A 1 3064 ? 156.510 173.817 197.453 1.00 13.83  ? 3064 VAL A CG1   1 
ATOM   12145 C  CG2   . VAL A 1 3064 ? 154.949 175.627 198.185 1.00 20.00  ? 3064 VAL A CG2   1 
ATOM   12146 N  N     . VAL A 1 3065 ? 156.964 171.929 200.164 1.00 18.99  ? 3065 VAL A N     1 
ATOM   12147 C  CA    . VAL A 1 3065 ? 157.992 170.909 200.332 1.00 14.96  ? 3065 VAL A CA    1 
ATOM   12148 C  C     . VAL A 1 3065 ? 158.102 170.142 199.023 1.00 17.68  ? 3065 VAL A C     1 
ATOM   12149 O  O     . VAL A 1 3065 ? 157.133 169.515 198.578 1.00 22.17  ? 3065 VAL A O     1 
ATOM   12150 C  CB    . VAL A 1 3065 ? 157.670 169.964 201.499 1.00 14.06  ? 3065 VAL A CB    1 
ATOM   12151 C  CG1   . VAL A 1 3065 ? 158.874 169.096 201.825 1.00 18.50  ? 3065 VAL A CG1   1 
ATOM   12152 C  CG2   . VAL A 1 3065 ? 157.233 170.757 202.715 1.00 12.41  ? 3065 VAL A CG2   1 
ATOM   12153 N  N     . PHE A 1 3066 ? 159.279 170.190 198.407 1.00 16.48  ? 3066 PHE A N     1 
ATOM   12154 C  CA    . PHE A 1 3066 ? 159.540 169.504 197.148 1.00 17.09  ? 3066 PHE A CA    1 
ATOM   12155 C  C     . PHE A 1 3066 ? 160.489 168.344 197.413 1.00 22.23  ? 3066 PHE A C     1 
ATOM   12156 O  O     . PHE A 1 3066 ? 161.627 168.555 197.844 1.00 26.71  ? 3066 PHE A O     1 
ATOM   12157 C  CB    . PHE A 1 3066 ? 160.129 170.463 196.114 1.00 20.18  ? 3066 PHE A CB    1 
ATOM   12158 C  CG    . PHE A 1 3066 ? 159.783 170.110 194.697 1.00 36.62  ? 3066 PHE A CG    1 
ATOM   12159 C  CD1   . PHE A 1 3066 ? 160.549 169.200 193.988 1.00 40.56  ? 3066 PHE A CD1   1 
ATOM   12160 C  CD2   . PHE A 1 3066 ? 158.691 170.690 194.072 1.00 41.60  ? 3066 PHE A CD2   1 
ATOM   12161 C  CE1   . PHE A 1 3066 ? 160.232 168.874 192.683 1.00 42.87  ? 3066 PHE A CE1   1 
ATOM   12162 C  CE2   . PHE A 1 3066 ? 158.369 170.368 192.768 1.00 48.01  ? 3066 PHE A CE2   1 
ATOM   12163 C  CZ    . PHE A 1 3066 ? 159.141 169.459 192.072 1.00 49.02  ? 3066 PHE A CZ    1 
ATOM   12164 N  N     . THR A 1 3067 ? 160.022 167.127 197.155 1.00 24.50  ? 3067 THR A N     1 
ATOM   12165 C  CA    . THR A 1 3067 ? 160.805 165.917 197.367 1.00 23.63  ? 3067 THR A CA    1 
ATOM   12166 C  C     . THR A 1 3067 ? 161.123 165.295 196.014 1.00 29.35  ? 3067 THR A C     1 
ATOM   12167 O  O     . THR A 1 3067 ? 160.213 165.027 195.223 1.00 37.92  ? 3067 THR A O     1 
ATOM   12168 C  CB    . THR A 1 3067 ? 160.053 164.925 198.255 1.00 23.34  ? 3067 THR A CB    1 
ATOM   12169 O  OG1   . THR A 1 3067 ? 158.864 164.488 197.587 1.00 35.35  ? 3067 THR A OG1   1 
ATOM   12170 C  CG2   . THR A 1 3067 ? 159.673 165.575 199.576 1.00 18.90  ? 3067 THR A CG2   1 
ATOM   12171 N  N     . MET A 1 3068 ? 162.408 165.068 195.752 1.00 25.18  ? 3068 MET A N     1 
ATOM   12172 C  CA    . MET A 1 3068 ? 162.846 164.513 194.480 1.00 31.22  ? 3068 MET A CA    1 
ATOM   12173 C  C     . MET A 1 3068 ? 164.019 163.572 194.709 1.00 35.00  ? 3068 MET A C     1 
ATOM   12174 O  O     . MET A 1 3068 ? 164.740 163.671 195.705 1.00 35.80  ? 3068 MET A O     1 
ATOM   12175 C  CB    . MET A 1 3068 ? 163.237 165.618 193.490 1.00 36.83  ? 3068 MET A CB    1 
ATOM   12176 C  CG    . MET A 1 3068 ? 164.028 166.756 194.110 1.00 34.38  ? 3068 MET A CG    1 
ATOM   12177 S  SD    . MET A 1 3068 ? 164.816 167.804 192.874 1.00 72.13  ? 3068 MET A SD    1 
ATOM   12178 C  CE    . MET A 1 3068 ? 165.916 166.630 192.088 1.00 39.39  ? 3068 MET A CE    1 
ATOM   12179 N  N     . ASN A 1 3069 ? 164.200 162.649 193.765 1.00 36.03  ? 3069 ASN A N     1 
ATOM   12180 C  CA    . ASN A 1 3069 ? 165.294 161.695 193.813 1.00 33.29  ? 3069 ASN A CA    1 
ATOM   12181 C  C     . ASN A 1 3069 ? 166.614 162.370 193.441 1.00 36.67  ? 3069 ASN A C     1 
ATOM   12182 O  O     . ASN A 1 3069 ? 166.634 163.322 192.658 1.00 40.97  ? 3069 ASN A O     1 
ATOM   12183 C  CB    . ASN A 1 3069 ? 165.024 160.531 192.865 1.00 37.36  ? 3069 ASN A CB    1 
ATOM   12184 C  CG    . ASN A 1 3069 ? 163.896 159.640 193.346 1.00 36.95  ? 3069 ASN A CG    1 
ATOM   12185 O  OD1   . ASN A 1 3069 ? 163.798 159.330 194.532 1.00 32.33  ? 3069 ASN A OD1   1 
ATOM   12186 N  ND2   . ASN A 1 3069 ? 163.036 159.224 192.424 1.00 40.65  ? 3069 ASN A ND2   1 
ATOM   12187 N  N     . PRO A 1 3070 ? 167.735 161.892 193.991 1.00 37.04  ? 3070 PRO A N     1 
ATOM   12188 C  CA    . PRO A 1 3070 ? 169.043 162.524 193.715 1.00 36.29  ? 3070 PRO A CA    1 
ATOM   12189 C  C     . PRO A 1 3070 ? 169.654 162.104 192.380 1.00 44.95  ? 3070 PRO A C     1 
ATOM   12190 O  O     . PRO A 1 3070 ? 170.548 161.264 192.283 1.00 49.28  ? 3070 PRO A O     1 
ATOM   12191 C  CB    . PRO A 1 3070 ? 169.891 162.061 194.901 1.00 30.28  ? 3070 PRO A CB    1 
ATOM   12192 C  CG    . PRO A 1 3070 ? 169.327 160.733 195.261 1.00 33.17  ? 3070 PRO A CG    1 
ATOM   12193 C  CD    . PRO A 1 3070 ? 167.854 160.773 194.942 1.00 36.86  ? 3070 PRO A CD    1 
ATOM   12194 N  N     . SER A 1 3071 ? 169.157 162.712 191.308 1.00 46.65  ? 3071 SER A N     1 
ATOM   12195 C  CA    . SER A 1 3071 ? 169.684 162.473 189.974 1.00 51.83  ? 3071 SER A CA    1 
ATOM   12196 C  C     . SER A 1 3071 ? 170.740 163.516 189.631 1.00 59.11  ? 3071 SER A C     1 
ATOM   12197 O  O     . SER A 1 3071 ? 170.680 164.662 190.083 1.00 59.13  ? 3071 SER A O     1 
ATOM   12198 C  CB    . SER A 1 3071 ? 168.565 162.500 188.933 1.00 53.02  ? 3071 SER A CB    1 
ATOM   12199 O  OG    . SER A 1 3071 ? 169.074 162.260 187.633 1.00 65.18  ? 3071 SER A OG    1 
ATOM   12200 N  N     . SER A 1 3072 ? 171.718 163.104 188.823 1.00 62.12  ? 3072 SER A N     1 
ATOM   12201 C  CA    . SER A 1 3072 ? 172.806 164.006 188.457 1.00 62.90  ? 3072 SER A CA    1 
ATOM   12202 C  C     . SER A 1 3072 ? 172.338 165.050 187.450 1.00 60.75  ? 3072 SER A C     1 
ATOM   12203 O  O     . SER A 1 3072 ? 172.399 166.257 187.711 1.00 56.18  ? 3072 SER A O     1 
ATOM   12204 C  CB    . SER A 1 3072 ? 173.985 163.205 187.903 1.00 66.66  ? 3072 SER A CB    1 
ATOM   12205 O  OG    . SER A 1 3072 ? 174.432 162.240 188.838 1.00 63.07  ? 3072 SER A OG    1 
ATOM   12206 N  N     . GLU A 1 3073 ? 171.867 164.601 186.284 1.00 66.34  ? 3073 GLU A N     1 
ATOM   12207 C  CA    . GLU A 1 3073 ? 171.404 165.531 185.261 1.00 67.08  ? 3073 GLU A CA    1 
ATOM   12208 C  C     . GLU A 1 3073 ? 170.051 166.143 185.600 1.00 65.90  ? 3073 GLU A C     1 
ATOM   12209 O  O     . GLU A 1 3073 ? 169.765 167.262 185.162 1.00 70.07  ? 3073 GLU A O     1 
ATOM   12210 C  CB    . GLU A 1 3073 ? 171.334 164.824 183.904 1.00 65.24  ? 3073 GLU A CB    1 
ATOM   12211 C  CG    . GLU A 1 3073 ? 172.471 163.834 183.619 1.00 75.54  ? 3073 GLU A CG    1 
ATOM   12212 C  CD    . GLU A 1 3073 ? 173.876 164.423 183.739 1.00 79.74  ? 3073 GLU A CD    1 
ATOM   12213 O  OE1   . GLU A 1 3073 ? 174.029 165.659 183.849 1.00 75.69  ? 3073 GLU A OE1   1 
ATOM   12214 O  OE2   . GLU A 1 3073 ? 174.843 163.632 183.724 1.00 85.81  ? 3073 GLU A OE2   1 
ATOM   12215 N  N     . GLY A 1 3074 ? 169.218 165.436 186.366 1.00 57.75  ? 3074 GLY A N     1 
ATOM   12216 C  CA    . GLY A 1 3074 ? 167.936 165.998 186.759 1.00 56.18  ? 3074 GLY A CA    1 
ATOM   12217 C  C     . GLY A 1 3074 ? 168.083 167.224 187.639 1.00 56.36  ? 3074 GLY A C     1 
ATOM   12218 O  O     . GLY A 1 3074 ? 167.325 168.187 187.511 1.00 52.14  ? 3074 GLY A O     1 
ATOM   12219 N  N     . LEU A 1 3075 ? 169.062 167.203 188.546 1.00 55.54  ? 3075 LEU A N     1 
ATOM   12220 C  CA    . LEU A 1 3075 ? 169.314 168.365 189.392 1.00 49.09  ? 3075 LEU A CA    1 
ATOM   12221 C  C     . LEU A 1 3075 ? 169.739 169.568 188.558 1.00 48.31  ? 3075 LEU A C     1 
ATOM   12222 O  O     . LEU A 1 3075 ? 169.268 170.689 188.786 1.00 48.00  ? 3075 LEU A O     1 
ATOM   12223 C  CB    . LEU A 1 3075 ? 170.381 168.027 190.432 1.00 48.78  ? 3075 LEU A CB    1 
ATOM   12224 C  CG    . LEU A 1 3075 ? 170.415 168.864 191.711 1.00 46.96  ? 3075 LEU A CG    1 
ATOM   12225 C  CD1   . LEU A 1 3075 ? 169.051 168.856 192.379 1.00 43.57  ? 3075 LEU A CD1   1 
ATOM   12226 C  CD2   . LEU A 1 3075 ? 171.483 168.350 192.660 1.00 44.49  ? 3075 LEU A CD2   1 
ATOM   12227 N  N     . LYS A 1 3076 ? 170.621 169.351 187.578 1.00 50.83  ? 3076 LYS A N     1 
ATOM   12228 C  CA    . LYS A 1 3076 ? 171.036 170.438 186.697 1.00 47.17  ? 3076 LYS A CA    1 
ATOM   12229 C  C     . LYS A 1 3076 ? 169.865 170.962 185.876 1.00 52.29  ? 3076 LYS A C     1 
ATOM   12230 O  O     . LYS A 1 3076 ? 169.740 172.173 185.660 1.00 50.43  ? 3076 LYS A O     1 
ATOM   12231 C  CB    . LYS A 1 3076 ? 172.164 169.967 185.779 1.00 44.84  ? 3076 LYS A CB    1 
ATOM   12232 C  CG    . LYS A 1 3076 ? 173.396 169.465 186.512 1.00 48.75  ? 3076 LYS A CG    1 
ATOM   12233 C  CD    . LYS A 1 3076 ? 174.629 169.538 185.626 1.00 51.67  ? 3076 LYS A CD    1 
ATOM   12234 C  CE    . LYS A 1 3076 ? 175.618 168.435 185.964 1.00 56.71  ? 3076 LYS A CE    1 
ATOM   12235 N  NZ    . LYS A 1 3076 ? 176.539 168.828 187.066 1.00 52.68  ? 3076 LYS A NZ    1 
ATOM   12236 N  N     . ASP A 1 3077 ? 169.002 170.061 185.399 1.00 51.37  ? 3077 ASP A N     1 
ATOM   12237 C  CA    . ASP A 1 3077 ? 167.831 170.485 184.639 1.00 48.23  ? 3077 ASP A CA    1 
ATOM   12238 C  C     . ASP A 1 3077 ? 166.904 171.333 185.504 1.00 46.74  ? 3077 ASP A C     1 
ATOM   12239 O  O     . ASP A 1 3077 ? 166.401 172.371 185.058 1.00 50.32  ? 3077 ASP A O     1 
ATOM   12240 C  CB    . ASP A 1 3077 ? 167.102 169.254 184.092 1.00 61.22  ? 3077 ASP A CB    1 
ATOM   12241 C  CG    . ASP A 1 3077 ? 165.877 169.602 183.251 1.00 79.58  ? 3077 ASP A CG    1 
ATOM   12242 O  OD1   . ASP A 1 3077 ? 165.213 168.659 182.773 1.00 96.50  ? 3077 ASP A OD1   1 
ATOM   12243 O  OD2   . ASP A 1 3077 ? 165.592 170.796 183.027 1.00 71.69  ? 3077 ASP A OD2   1 
ATOM   12244 N  N     . ARG A 1 3078 ? 166.679 170.912 186.752 1.00 47.81  ? 3078 ARG A N     1 
ATOM   12245 C  CA    . ARG A 1 3078 ? 165.835 171.685 187.657 1.00 50.34  ? 3078 ARG A CA    1 
ATOM   12246 C  C     . ARG A 1 3078 ? 166.467 173.025 188.008 1.00 45.36  ? 3078 ARG A C     1 
ATOM   12247 O  O     . ARG A 1 3078 ? 165.749 173.999 188.260 1.00 44.16  ? 3078 ARG A O     1 
ATOM   12248 C  CB    . ARG A 1 3078 ? 165.553 170.888 188.930 1.00 55.07  ? 3078 ARG A CB    1 
ATOM   12249 C  CG    . ARG A 1 3078 ? 164.736 169.625 188.718 1.00 55.17  ? 3078 ARG A CG    1 
ATOM   12250 C  CD    . ARG A 1 3078 ? 163.258 169.934 188.553 1.00 60.37  ? 3078 ARG A CD    1 
ATOM   12251 N  NE    . ARG A 1 3078 ? 162.428 168.772 188.847 1.00 72.65  ? 3078 ARG A NE    1 
ATOM   12252 C  CZ    . ARG A 1 3078 ? 161.622 168.186 187.972 1.00 77.99  ? 3078 ARG A CZ    1 
ATOM   12253 N  NH1   . ARG A 1 3078 ? 161.524 168.617 186.726 1.00 80.60  ? 3078 ARG A NH1   1 
ATOM   12254 N  NH2   . ARG A 1 3078 ? 160.901 167.137 188.357 1.00 72.81  ? 3078 ARG A NH2   1 
ATOM   12255 N  N     . ALA A 1 3079 ? 167.801 173.092 188.037 1.00 43.77  ? 3079 ALA A N     1 
ATOM   12256 C  CA    . ALA A 1 3079 ? 168.477 174.347 188.345 1.00 40.72  ? 3079 ALA A CA    1 
ATOM   12257 C  C     . ALA A 1 3079 ? 168.195 175.430 187.314 1.00 42.67  ? 3079 ALA A C     1 
ATOM   12258 O  O     . ALA A 1 3079 ? 168.347 176.617 187.622 1.00 45.71  ? 3079 ALA A O     1 
ATOM   12259 C  CB    . ALA A 1 3079 ? 169.984 174.117 188.460 1.00 43.70  ? 3079 ALA A CB    1 
ATOM   12260 N  N     . ALA A 1 3080 ? 167.792 175.055 186.103 1.00 43.08  ? 3080 ALA A N     1 
ATOM   12261 C  CA    . ALA A 1 3080 ? 167.473 176.009 185.048 1.00 38.19  ? 3080 ALA A CA    1 
ATOM   12262 C  C     . ALA A 1 3080 ? 165.983 176.134 184.777 1.00 36.43  ? 3080 ALA A C     1 
ATOM   12263 O  O     . ALA A 1 3080 ? 165.499 177.239 184.527 1.00 41.44  ? 3080 ALA A O     1 
ATOM   12264 C  CB    . ALA A 1 3080 ? 168.189 175.622 183.750 1.00 34.41  ? 3080 ALA A CB    1 
ATOM   12265 N  N     . THR A 1 3081 ? 165.239 175.026 184.821 1.00 37.13  ? 3081 THR A N     1 
ATOM   12266 C  CA    . THR A 1 3081 ? 163.807 175.095 184.551 1.00 40.47  ? 3081 THR A CA    1 
ATOM   12267 C  C     . THR A 1 3081 ? 163.027 175.618 185.751 1.00 40.12  ? 3081 THR A C     1 
ATOM   12268 O  O     . THR A 1 3081 ? 161.845 175.954 185.620 1.00 43.20  ? 3081 THR A O     1 
ATOM   12269 C  CB    . THR A 1 3081 ? 163.281 173.721 184.135 1.00 52.36  ? 3081 THR A CB    1 
ATOM   12270 O  OG1   . THR A 1 3081 ? 162.008 173.868 183.493 1.00 57.11  ? 3081 THR A OG1   1 
ATOM   12271 C  CG2   . THR A 1 3081 ? 163.131 172.816 185.347 1.00 52.44  ? 3081 THR A CG2   1 
ATOM   12272 N  N     . SER A 1 3082 ? 163.662 175.691 186.919 1.00 40.17  ? 3082 SER A N     1 
ATOM   12273 C  CA    . SER A 1 3082 ? 163.016 176.204 188.128 1.00 38.88  ? 3082 SER A CA    1 
ATOM   12274 C  C     . SER A 1 3082 ? 164.079 176.806 189.033 1.00 40.97  ? 3082 SER A C     1 
ATOM   12275 O  O     . SER A 1 3082 ? 164.530 176.180 190.000 1.00 42.51  ? 3082 SER A O     1 
ATOM   12276 C  CB    . SER A 1 3082 ? 162.239 175.105 188.853 1.00 39.79  ? 3082 SER A CB    1 
ATOM   12277 O  OG    . SER A 1 3082 ? 161.398 175.651 189.854 1.00 37.57  ? 3082 SER A OG    1 
ATOM   12278 N  N     . PRO A 1 3083 ? 164.517 178.032 188.738 1.00 38.56  ? 3083 PRO A N     1 
ATOM   12279 C  CA    . PRO A 1 3083 ? 165.554 178.659 189.575 1.00 34.69  ? 3083 PRO A CA    1 
ATOM   12280 C  C     . PRO A 1 3083 ? 165.121 178.901 191.010 1.00 34.36  ? 3083 PRO A C     1 
ATOM   12281 O  O     . PRO A 1 3083 ? 165.977 178.957 191.901 1.00 41.27  ? 3083 PRO A O     1 
ATOM   12282 C  CB    . PRO A 1 3083 ? 165.843 179.975 188.841 1.00 34.69  ? 3083 PRO A CB    1 
ATOM   12283 C  CG    . PRO A 1 3083 ? 164.597 180.258 188.073 1.00 31.98  ? 3083 PRO A CG    1 
ATOM   12284 C  CD    . PRO A 1 3083 ? 164.067 178.920 187.654 1.00 34.06  ? 3083 PRO A CD    1 
ATOM   12285 N  N     . ALA A 1 3084 ? 163.818 179.053 191.265 1.00 31.46  ? 3084 ALA A N     1 
ATOM   12286 C  CA    . ALA A 1 3084 ? 163.361 179.298 192.629 1.00 30.90  ? 3084 ALA A CA    1 
ATOM   12287 C  C     . ALA A 1 3084 ? 163.556 178.077 193.516 1.00 36.68  ? 3084 ALA A C     1 
ATOM   12288 O  O     . ALA A 1 3084 ? 163.608 178.205 194.744 1.00 40.17  ? 3084 ALA A O     1 
ATOM   12289 C  CB    . ALA A 1 3084 ? 161.893 179.722 192.630 1.00 30.47  ? 3084 ALA A CB    1 
ATOM   12290 N  N     . LEU A 1 3085 ? 163.664 176.888 192.921 1.00 32.95  ? 3085 LEU A N     1 
ATOM   12291 C  CA    . LEU A 1 3085 ? 163.905 175.686 193.709 1.00 28.23  ? 3085 LEU A CA    1 
ATOM   12292 C  C     . LEU A 1 3085 ? 165.277 175.696 194.366 1.00 32.92  ? 3085 LEU A C     1 
ATOM   12293 O  O     . LEU A 1 3085 ? 165.501 174.943 195.319 1.00 42.21  ? 3085 LEU A O     1 
ATOM   12294 C  CB    . LEU A 1 3085 ? 163.762 174.442 192.830 1.00 28.71  ? 3085 LEU A CB    1 
ATOM   12295 C  CG    . LEU A 1 3085 ? 162.399 173.749 192.811 1.00 26.80  ? 3085 LEU A CG    1 
ATOM   12296 C  CD1   . LEU A 1 3085 ? 162.489 172.424 192.071 1.00 28.36  ? 3085 LEU A CD1   1 
ATOM   12297 C  CD2   . LEU A 1 3085 ? 161.879 173.540 194.223 1.00 29.18  ? 3085 LEU A CD2   1 
ATOM   12298 N  N     . PHE A 1 3086 ? 166.196 176.533 193.887 1.00 34.20  ? 3086 PHE A N     1 
ATOM   12299 C  CA    . PHE A 1 3086 ? 167.567 176.529 194.369 1.00 35.11  ? 3086 PHE A CA    1 
ATOM   12300 C  C     . PHE A 1 3086 ? 167.995 177.834 195.024 1.00 36.88  ? 3086 PHE A C     1 
ATOM   12301 O  O     . PHE A 1 3086 ? 169.027 177.850 195.703 1.00 44.80  ? 3086 PHE A O     1 
ATOM   12302 C  CB    . PHE A 1 3086 ? 168.529 176.202 193.217 1.00 31.67  ? 3086 PHE A CB    1 
ATOM   12303 C  CG    . PHE A 1 3086 ? 168.429 174.783 192.737 1.00 36.22  ? 3086 PHE A CG    1 
ATOM   12304 C  CD1   . PHE A 1 3086 ? 167.436 174.411 191.846 1.00 39.30  ? 3086 PHE A CD1   1 
ATOM   12305 C  CD2   . PHE A 1 3086 ? 169.321 173.822 193.177 1.00 38.98  ? 3086 PHE A CD2   1 
ATOM   12306 C  CE1   . PHE A 1 3086 ? 167.334 173.109 191.406 1.00 41.80  ? 3086 PHE A CE1   1 
ATOM   12307 C  CE2   . PHE A 1 3086 ? 169.225 172.518 192.736 1.00 42.30  ? 3086 PHE A CE2   1 
ATOM   12308 C  CZ    . PHE A 1 3086 ? 168.230 172.163 191.848 1.00 46.56  ? 3086 PHE A CZ    1 
ATOM   12309 N  N     . ASN A 1 3087 ? 167.246 178.921 194.844 1.00 30.80  ? 3087 ASN A N     1 
ATOM   12310 C  CA    . ASN A 1 3087 ? 167.534 180.172 195.526 1.00 32.52  ? 3087 ASN A CA    1 
ATOM   12311 C  C     . ASN A 1 3087 ? 166.437 180.620 196.481 1.00 34.83  ? 3087 ASN A C     1 
ATOM   12312 O  O     . ASN A 1 3087 ? 166.665 181.553 197.260 1.00 36.48  ? 3087 ASN A O     1 
ATOM   12313 C  CB    . ASN A 1 3087 ? 167.852 181.278 194.498 1.00 32.93  ? 3087 ASN A CB    1 
ATOM   12314 C  CG    . ASN A 1 3087 ? 166.616 181.829 193.778 1.00 43.72  ? 3087 ASN A CG    1 
ATOM   12315 O  OD1   . ASN A 1 3087 ? 165.534 181.978 194.344 1.00 48.09  ? 3087 ASN A OD1   1 
ATOM   12316 N  ND2   . ASN A 1 3087 ? 166.794 182.139 192.499 1.00 42.44  ? 3087 ASN A ND2   1 
ATOM   12317 N  N     . ARG A 1 3088 ? 165.264 179.987 196.448 1.00 32.55  ? 3088 ARG A N     1 
ATOM   12318 C  CA    . ARG A 1 3088 ? 164.179 180.296 197.365 1.00 33.68  ? 3088 ARG A CA    1 
ATOM   12319 C  C     . ARG A 1 3088 ? 163.845 179.151 198.308 1.00 38.56  ? 3088 ARG A C     1 
ATOM   12320 O  O     . ARG A 1 3088 ? 163.127 179.372 199.290 1.00 42.62  ? 3088 ARG A O     1 
ATOM   12321 C  CB    . ARG A 1 3088 ? 162.910 180.682 196.589 1.00 31.00  ? 3088 ARG A CB    1 
ATOM   12322 C  CG    . ARG A 1 3088 ? 162.832 182.144 196.190 1.00 37.89  ? 3088 ARG A CG    1 
ATOM   12323 C  CD    . ARG A 1 3088 ? 163.112 183.066 197.367 1.00 41.56  ? 3088 ARG A CD    1 
ATOM   12324 N  NE    . ARG A 1 3088 ? 162.530 184.392 197.189 1.00 50.09  ? 3088 ARG A NE    1 
ATOM   12325 C  CZ    . ARG A 1 3088 ? 162.911 185.273 196.273 1.00 52.70  ? 3088 ARG A CZ    1 
ATOM   12326 N  NH1   . ARG A 1 3088 ? 163.903 185.018 195.435 1.00 40.77  ? 3088 ARG A NH1   1 
ATOM   12327 N  NH2   . ARG A 1 3088 ? 162.286 186.445 196.202 1.00 55.07  ? 3088 ARG A NH2   1 
ATOM   12328 N  N     . CYS A 1 3089 ? 164.335 177.944 198.041 1.00 36.90  ? 3089 CYS A N     1 
ATOM   12329 C  CA    . CYS A 1 3089 ? 164.046 176.770 198.849 1.00 28.60  ? 3089 CYS A CA    1 
ATOM   12330 C  C     . CYS A 1 3089 ? 165.302 176.332 199.588 1.00 27.48  ? 3089 CYS A C     1 
ATOM   12331 O  O     . CYS A 1 3089 ? 166.408 176.397 199.043 1.00 33.35  ? 3089 CYS A O     1 
ATOM   12332 C  CB    . CYS A 1 3089 ? 163.529 175.620 197.980 1.00 24.29  ? 3089 CYS A CB    1 
ATOM   12333 S  SG    . CYS A 1 3089 ? 161.938 175.930 197.185 1.00 35.42  ? 3089 CYS A SG    1 
ATOM   12334 N  N     . VAL A 1 3090 ? 165.126 175.888 200.828 1.00 23.51  ? 3090 VAL A N     1 
ATOM   12335 C  CA    . VAL A 1 3090 ? 166.235 175.366 201.619 1.00 19.99  ? 3090 VAL A CA    1 
ATOM   12336 C  C     . VAL A 1 3090 ? 166.458 173.911 201.232 1.00 21.56  ? 3090 VAL A C     1 
ATOM   12337 O  O     . VAL A 1 3090 ? 165.547 173.083 201.337 1.00 26.11  ? 3090 VAL A O     1 
ATOM   12338 C  CB    . VAL A 1 3090 ? 165.960 175.504 203.122 1.00 18.80  ? 3090 VAL A CB    1 
ATOM   12339 C  CG1   . VAL A 1 3090 ? 167.078 174.858 203.923 1.00 23.93  ? 3090 VAL A CG1   1 
ATOM   12340 C  CG2   . VAL A 1 3090 ? 165.807 176.968 203.498 1.00 25.33  ? 3090 VAL A CG2   1 
ATOM   12341 N  N     . LEU A 1 3091 ? 167.669 173.597 200.784 1.00 19.86  ? 3091 LEU A N     1 
ATOM   12342 C  CA    . LEU A 1 3091 ? 168.001 172.275 200.268 1.00 17.21  ? 3091 LEU A CA    1 
ATOM   12343 C  C     . LEU A 1 3091 ? 168.657 171.458 201.375 1.00 19.97  ? 3091 LEU A C     1 
ATOM   12344 O  O     . LEU A 1 3091 ? 169.748 171.798 201.843 1.00 23.43  ? 3091 LEU A O     1 
ATOM   12345 C  CB    . LEU A 1 3091 ? 168.918 172.390 199.052 1.00 17.35  ? 3091 LEU A CB    1 
ATOM   12346 C  CG    . LEU A 1 3091 ? 169.011 171.199 198.096 1.00 19.06  ? 3091 LEU A CG    1 
ATOM   12347 C  CD1   . LEU A 1 3091 ? 169.364 171.676 196.698 1.00 22.40  ? 3091 LEU A CD1   1 
ATOM   12348 C  CD2   . LEU A 1 3091 ? 170.033 170.183 198.579 1.00 20.47  ? 3091 LEU A CD2   1 
ATOM   12349 N  N     . ASN A 1 3092 ? 167.990 170.386 201.792 1.00 19.05  ? 3092 ASN A N     1 
ATOM   12350 C  CA    . ASN A 1 3092 ? 168.566 169.393 202.689 1.00 19.21  ? 3092 ASN A CA    1 
ATOM   12351 C  C     . ASN A 1 3092 ? 168.736 168.095 201.913 1.00 20.76  ? 3092 ASN A C     1 
ATOM   12352 O  O     . ASN A 1 3092 ? 167.769 167.578 201.343 1.00 21.82  ? 3092 ASN A O     1 
ATOM   12353 C  CB    . ASN A 1 3092 ? 167.689 169.175 203.922 1.00 20.25  ? 3092 ASN A CB    1 
ATOM   12354 C  CG    . ASN A 1 3092 ? 167.291 170.472 204.592 1.00 29.65  ? 3092 ASN A CG    1 
ATOM   12355 O  OD1   . ASN A 1 3092 ? 168.138 171.305 204.913 1.00 30.94  ? 3092 ASN A OD1   1 
ATOM   12356 N  ND2   . ASN A 1 3092 ? 165.997 170.647 204.817 1.00 38.68  ? 3092 ASN A ND2   1 
ATOM   12357 N  N     . TRP A 1 3093 ? 169.959 167.575 201.892 1.00 21.00  ? 3093 TRP A N     1 
ATOM   12358 C  CA    . TRP A 1 3093 ? 170.278 166.366 201.139 1.00 17.77  ? 3093 TRP A CA    1 
ATOM   12359 C  C     . TRP A 1 3093 ? 170.126 165.168 202.066 1.00 21.28  ? 3093 TRP A C     1 
ATOM   12360 O  O     . TRP A 1 3093 ? 171.057 164.804 202.789 1.00 25.03  ? 3093 TRP A O     1 
ATOM   12361 C  CB    . TRP A 1 3093 ? 171.685 166.450 200.559 1.00 17.62  ? 3093 TRP A CB    1 
ATOM   12362 C  CG    . TRP A 1 3093 ? 171.937 165.475 199.457 1.00 21.02  ? 3093 TRP A CG    1 
ATOM   12363 C  CD1   . TRP A 1 3093 ? 172.254 164.155 199.586 1.00 21.02  ? 3093 TRP A CD1   1 
ATOM   12364 C  CD2   . TRP A 1 3093 ? 171.892 165.741 198.051 1.00 20.96  ? 3093 TRP A CD2   1 
ATOM   12365 N  NE1   . TRP A 1 3093 ? 172.411 163.583 198.348 1.00 22.02  ? 3093 TRP A NE1   1 
ATOM   12366 C  CE2   . TRP A 1 3093 ? 172.194 164.536 197.389 1.00 20.52  ? 3093 TRP A CE2   1 
ATOM   12367 C  CE3   . TRP A 1 3093 ? 171.626 166.881 197.288 1.00 21.64  ? 3093 TRP A CE3   1 
ATOM   12368 C  CZ2   . TRP A 1 3093 ? 172.238 164.439 196.001 1.00 22.25  ? 3093 TRP A CZ2   1 
ATOM   12369 C  CZ3   . TRP A 1 3093 ? 171.670 166.783 195.911 1.00 23.18  ? 3093 TRP A CZ3   1 
ATOM   12370 C  CH2   . TRP A 1 3093 ? 171.973 165.571 195.281 1.00 22.79  ? 3093 TRP A CH2   1 
ATOM   12371 N  N     . PHE A 1 3094 ? 168.941 164.556 202.053 1.00 19.22  ? 3094 PHE A N     1 
ATOM   12372 C  CA    . PHE A 1 3094 ? 168.723 163.359 202.859 1.00 19.73  ? 3094 PHE A CA    1 
ATOM   12373 C  C     . PHE A 1 3094 ? 169.525 162.184 202.316 1.00 24.70  ? 3094 PHE A C     1 
ATOM   12374 O  O     . PHE A 1 3094 ? 170.228 161.498 203.067 1.00 30.75  ? 3094 PHE A O     1 
ATOM   12375 C  CB    . PHE A 1 3094 ? 167.233 163.017 202.903 1.00 19.89  ? 3094 PHE A CB    1 
ATOM   12376 C  CG    . PHE A 1 3094 ? 166.423 163.922 203.789 1.00 19.61  ? 3094 PHE A CG    1 
ATOM   12377 C  CD1   . PHE A 1 3094 ? 167.017 164.975 204.465 1.00 24.77  ? 3094 PHE A CD1   1 
ATOM   12378 C  CD2   . PHE A 1 3094 ? 165.065 163.714 203.948 1.00 21.29  ? 3094 PHE A CD2   1 
ATOM   12379 C  CE1   . PHE A 1 3094 ? 166.269 165.805 205.277 1.00 25.35  ? 3094 PHE A CE1   1 
ATOM   12380 C  CE2   . PHE A 1 3094 ? 164.313 164.539 204.760 1.00 29.45  ? 3094 PHE A CE2   1 
ATOM   12381 C  CZ    . PHE A 1 3094 ? 164.916 165.586 205.425 1.00 30.09  ? 3094 PHE A CZ    1 
ATOM   12382 N  N     . GLY A 1 3095 ? 169.435 161.941 201.011 1.00 20.99  ? 3095 GLY A N     1 
ATOM   12383 C  CA    . GLY A 1 3095 ? 170.146 160.843 200.395 1.00 20.11  ? 3095 GLY A CA    1 
ATOM   12384 C  C     . GLY A 1 3095 ? 169.627 159.492 200.861 1.00 26.81  ? 3095 GLY A C     1 
ATOM   12385 O  O     . GLY A 1 3095 ? 168.573 159.365 201.486 1.00 32.11  ? 3095 GLY A O     1 
ATOM   12386 N  N     . ASP A 1 3096 ? 170.404 158.465 200.537 1.00 29.14  ? 3096 ASP A N     1 
ATOM   12387 C  CA    . ASP A 1 3096 ? 170.119 157.122 201.016 1.00 28.47  ? 3096 ASP A CA    1 
ATOM   12388 C  C     . ASP A 1 3096 ? 170.527 156.995 202.478 1.00 23.81  ? 3096 ASP A C     1 
ATOM   12389 O  O     . ASP A 1 3096 ? 171.383 157.735 202.971 1.00 25.57  ? 3096 ASP A O     1 
ATOM   12390 C  CB    . ASP A 1 3096 ? 170.856 156.082 200.171 1.00 35.55  ? 3096 ASP A CB    1 
ATOM   12391 C  CG    . ASP A 1 3096 ? 170.238 154.698 200.272 1.00 43.44  ? 3096 ASP A CG    1 
ATOM   12392 O  OD1   . ASP A 1 3096 ? 169.698 154.356 201.344 1.00 38.94  ? 3096 ASP A OD1   1 
ATOM   12393 O  OD2   . ASP A 1 3096 ? 170.296 153.950 199.274 1.00 44.09  ? 3096 ASP A OD2   1 
ATOM   12394 N  N     . TRP A 1 3097 ? 169.893 156.055 203.176 1.00 22.58  ? 3097 TRP A N     1 
ATOM   12395 C  CA    . TRP A 1 3097 ? 170.256 155.795 204.562 1.00 23.11  ? 3097 TRP A CA    1 
ATOM   12396 C  C     . TRP A 1 3097 ? 171.708 155.345 204.644 1.00 25.62  ? 3097 TRP A C     1 
ATOM   12397 O  O     . TRP A 1 3097 ? 172.139 154.455 203.907 1.00 28.48  ? 3097 TRP A O     1 
ATOM   12398 C  CB    . TRP A 1 3097 ? 169.341 154.732 205.167 1.00 22.69  ? 3097 TRP A CB    1 
ATOM   12399 C  CG    . TRP A 1 3097 ? 167.935 155.188 205.398 1.00 23.07  ? 3097 TRP A CG    1 
ATOM   12400 C  CD1   . TRP A 1 3097 ? 167.394 156.390 205.052 1.00 21.17  ? 3097 TRP A CD1   1 
ATOM   12401 C  CD2   . TRP A 1 3097 ? 166.889 154.446 206.037 1.00 25.44  ? 3097 TRP A CD2   1 
ATOM   12402 N  NE1   . TRP A 1 3097 ? 166.074 156.442 205.431 1.00 19.24  ? 3097 TRP A NE1   1 
ATOM   12403 C  CE2   . TRP A 1 3097 ? 165.740 155.261 206.037 1.00 21.42  ? 3097 TRP A CE2   1 
ATOM   12404 C  CE3   . TRP A 1 3097 ? 166.812 153.171 206.605 1.00 21.66  ? 3097 TRP A CE3   1 
ATOM   12405 C  CZ2   . TRP A 1 3097 ? 164.530 154.842 206.585 1.00 21.15  ? 3097 TRP A CZ2   1 
ATOM   12406 C  CZ3   . TRP A 1 3097 ? 165.610 152.758 207.147 1.00 20.48  ? 3097 TRP A CZ3   1 
ATOM   12407 C  CH2   . TRP A 1 3097 ? 164.485 153.591 207.133 1.00 21.69  ? 3097 TRP A CH2   1 
ATOM   12408 N  N     . SER A 1 3098 ? 172.461 155.965 205.547 1.00 25.93  ? 3098 SER A N     1 
ATOM   12409 C  CA    . SER A 1 3098 ? 173.861 155.620 205.711 1.00 25.83  ? 3098 SER A CA    1 
ATOM   12410 C  C     . SER A 1 3098 ? 173.995 154.268 206.406 1.00 30.66  ? 3098 SER A C     1 
ATOM   12411 O  O     . SER A 1 3098 ? 173.017 153.670 206.864 1.00 33.90  ? 3098 SER A O     1 
ATOM   12412 C  CB    . SER A 1 3098 ? 174.589 156.703 206.506 1.00 30.63  ? 3098 SER A CB    1 
ATOM   12413 O  OG    . SER A 1 3098 ? 173.976 156.908 207.767 1.00 36.31  ? 3098 SER A OG    1 
ATOM   12414 N  N     . THR A 1 3099 ? 175.236 153.779 206.469 1.00 33.59  ? 3099 THR A N     1 
ATOM   12415 C  CA    . THR A 1 3099 ? 175.503 152.539 207.190 1.00 27.83  ? 3099 THR A CA    1 
ATOM   12416 C  C     . THR A 1 3099 ? 175.089 152.661 208.651 1.00 29.21  ? 3099 THR A C     1 
ATOM   12417 O  O     . THR A 1 3099 ? 174.571 151.705 209.242 1.00 32.45  ? 3099 THR A O     1 
ATOM   12418 C  CB    . THR A 1 3099 ? 176.984 152.177 207.075 1.00 28.86  ? 3099 THR A CB    1 
ATOM   12419 O  OG1   . THR A 1 3099 ? 177.351 152.099 205.692 1.00 34.51  ? 3099 THR A OG1   1 
ATOM   12420 C  CG2   . THR A 1 3099 ? 177.262 150.842 207.740 1.00 31.82  ? 3099 THR A CG2   1 
ATOM   12421 N  N     . GLU A 1 3100 ? 175.295 153.840 209.243 1.00 30.37  ? 3100 GLU A N     1 
ATOM   12422 C  CA    . GLU A 1 3100 ? 174.836 154.079 210.607 1.00 34.42  ? 3100 GLU A CA    1 
ATOM   12423 C  C     . GLU A 1 3100 ? 173.323 153.934 210.709 1.00 32.97  ? 3100 GLU A C     1 
ATOM   12424 O  O     . GLU A 1 3100 ? 172.816 153.305 211.644 1.00 32.67  ? 3100 GLU A O     1 
ATOM   12425 C  CB    . GLU A 1 3100 ? 175.267 155.473 211.064 1.00 41.82  ? 3100 GLU A CB    1 
ATOM   12426 C  CG    . GLU A 1 3100 ? 176.770 155.659 211.182 1.00 59.46  ? 3100 GLU A CG    1 
ATOM   12427 C  CD    . GLU A 1 3100 ? 177.156 157.058 211.621 1.00 80.08  ? 3100 GLU A CD    1 
ATOM   12428 O  OE1   . GLU A 1 3100 ? 176.260 157.924 211.710 1.00 82.07  ? 3100 GLU A OE1   1 
ATOM   12429 O  OE2   . GLU A 1 3100 ? 178.356 157.292 211.876 1.00 79.47  ? 3100 GLU A OE2   1 
ATOM   12430 N  N     . ALA A 1 3101 ? 172.590 154.508 209.751 1.00 33.30  ? 3101 ALA A N     1 
ATOM   12431 C  CA    . ALA A 1 3101 ? 171.133 154.428 209.777 1.00 29.06  ? 3101 ALA A CA    1 
ATOM   12432 C  C     . ALA A 1 3101 ? 170.651 152.992 209.625 1.00 29.93  ? 3101 ALA A C     1 
ATOM   12433 O  O     . ALA A 1 3101 ? 169.747 152.552 210.346 1.00 32.71  ? 3101 ALA A O     1 
ATOM   12434 C  CB    . ALA A 1 3101 ? 170.545 155.308 208.676 1.00 27.34  ? 3101 ALA A CB    1 
ATOM   12435 N  N     . LEU A 1 3102 ? 171.239 152.248 208.685 1.00 28.03  ? 3102 LEU A N     1 
ATOM   12436 C  CA    . LEU A 1 3102 ? 170.856 150.854 208.495 1.00 20.66  ? 3102 LEU A CA    1 
ATOM   12437 C  C     . LEU A 1 3102 ? 171.137 150.035 209.747 1.00 25.32  ? 3102 LEU A C     1 
ATOM   12438 O  O     . LEU A 1 3102 ? 170.299 149.230 210.174 1.00 27.47  ? 3102 LEU A O     1 
ATOM   12439 C  CB    . LEU A 1 3102 ? 171.599 150.265 207.296 1.00 15.11  ? 3102 LEU A CB    1 
ATOM   12440 C  CG    . LEU A 1 3102 ? 171.362 150.923 205.938 1.00 15.94  ? 3102 LEU A CG    1 
ATOM   12441 C  CD1   . LEU A 1 3102 ? 172.264 150.300 204.887 1.00 18.34  ? 3102 LEU A CD1   1 
ATOM   12442 C  CD2   . LEU A 1 3102 ? 169.903 150.807 205.531 1.00 19.79  ? 3102 LEU A CD2   1 
ATOM   12443 N  N     . TYR A 1 3103 ? 172.309 150.235 210.354 1.00 27.48  ? 3103 TYR A N     1 
ATOM   12444 C  CA    . TYR A 1 3103 ? 172.651 149.500 211.566 1.00 28.96  ? 3103 TYR A CA    1 
ATOM   12445 C  C     . TYR A 1 3103 ? 171.689 149.829 212.700 1.00 30.76  ? 3103 TYR A C     1 
ATOM   12446 O  O     . TYR A 1 3103 ? 171.251 148.935 213.432 1.00 34.56  ? 3103 TYR A O     1 
ATOM   12447 C  CB    . TYR A 1 3103 ? 174.096 149.800 211.969 1.00 34.50  ? 3103 TYR A CB    1 
ATOM   12448 C  CG    . TYR A 1 3103 ? 174.619 148.920 213.084 1.00 38.66  ? 3103 TYR A CG    1 
ATOM   12449 C  CD1   . TYR A 1 3103 ? 174.270 149.161 214.407 1.00 36.66  ? 3103 TYR A CD1   1 
ATOM   12450 C  CD2   . TYR A 1 3103 ? 175.439 147.835 212.812 1.00 39.42  ? 3103 TYR A CD2   1 
ATOM   12451 C  CE1   . TYR A 1 3103 ? 174.735 148.362 215.424 1.00 38.00  ? 3103 TYR A CE1   1 
ATOM   12452 C  CE2   . TYR A 1 3103 ? 175.909 147.026 213.827 1.00 39.19  ? 3103 TYR A CE2   1 
ATOM   12453 C  CZ    . TYR A 1 3103 ? 175.552 147.296 215.131 1.00 43.17  ? 3103 TYR A CZ    1 
ATOM   12454 O  OH    . TYR A 1 3103 ? 176.011 146.501 216.152 1.00 55.76  ? 3103 TYR A OH    1 
ATOM   12455 N  N     . GLN A 1 3104 ? 171.352 151.109 212.867 1.00 27.61  ? 3104 GLN A N     1 
ATOM   12456 C  CA    . GLN A 1 3104 ? 170.454 151.488 213.954 1.00 26.76  ? 3104 GLN A CA    1 
ATOM   12457 C  C     . GLN A 1 3104 ? 169.051 150.934 213.735 1.00 28.71  ? 3104 GLN A C     1 
ATOM   12458 O  O     . GLN A 1 3104 ? 168.412 150.464 214.684 1.00 36.63  ? 3104 GLN A O     1 
ATOM   12459 C  CB    . GLN A 1 3104 ? 170.427 153.007 214.108 1.00 29.07  ? 3104 GLN A CB    1 
ATOM   12460 C  CG    . GLN A 1 3104 ? 171.724 153.580 214.660 1.00 30.21  ? 3104 GLN A CG    1 
ATOM   12461 C  CD    . GLN A 1 3104 ? 171.633 155.061 214.960 1.00 40.60  ? 3104 GLN A CD    1 
ATOM   12462 O  OE1   . GLN A 1 3104 ? 172.376 155.866 214.400 1.00 46.53  ? 3104 GLN A OE1   1 
ATOM   12463 N  NE2   . GLN A 1 3104 ? 170.723 155.428 215.854 1.00 41.83  ? 3104 GLN A NE2   1 
ATOM   12464 N  N     . VAL A 1 3105 ? 168.561 150.963 212.493 1.00 24.77  ? 3105 VAL A N     1 
ATOM   12465 C  CA    . VAL A 1 3105 ? 167.241 150.403 212.201 1.00 26.89  ? 3105 VAL A CA    1 
ATOM   12466 C  C     . VAL A 1 3105 ? 167.229 148.903 212.471 1.00 31.19  ? 3105 VAL A C     1 
ATOM   12467 O  O     . VAL A 1 3105 ? 166.287 148.365 213.073 1.00 36.89  ? 3105 VAL A O     1 
ATOM   12468 C  CB    . VAL A 1 3105 ? 166.834 150.720 210.750 1.00 26.17  ? 3105 VAL A CB    1 
ATOM   12469 C  CG1   . VAL A 1 3105 ? 165.633 149.885 210.338 1.00 32.24  ? 3105 VAL A CG1   1 
ATOM   12470 C  CG2   . VAL A 1 3105 ? 166.529 152.196 210.599 1.00 27.48  ? 3105 VAL A CG2   1 
ATOM   12471 N  N     . GLY A 1 3106 ? 168.276 148.203 212.026 1.00 25.79  ? 3106 GLY A N     1 
ATOM   12472 C  CA    . GLY A 1 3106 ? 168.353 146.775 212.275 1.00 26.33  ? 3106 GLY A CA    1 
ATOM   12473 C  C     . GLY A 1 3106 ? 168.425 146.445 213.753 1.00 33.60  ? 3106 GLY A C     1 
ATOM   12474 O  O     . GLY A 1 3106 ? 167.779 145.506 214.220 1.00 42.68  ? 3106 GLY A O     1 
ATOM   12475 N  N     . LYS A 1 3107 ? 169.204 147.217 214.511 1.00 30.78  ? 3107 LYS A N     1 
ATOM   12476 C  CA    . LYS A 1 3107 ? 169.324 146.965 215.942 1.00 31.67  ? 3107 LYS A CA    1 
ATOM   12477 C  C     . LYS A 1 3107 ? 168.009 147.251 216.657 1.00 36.33  ? 3107 LYS A C     1 
ATOM   12478 O  O     . LYS A 1 3107 ? 167.662 146.580 217.635 1.00 43.26  ? 3107 LYS A O     1 
ATOM   12479 C  CB    . LYS A 1 3107 ? 170.458 147.805 216.529 1.00 31.92  ? 3107 LYS A CB    1 
ATOM   12480 C  CG    . LYS A 1 3107 ? 170.918 147.347 217.902 1.00 46.54  ? 3107 LYS A CG    1 
ATOM   12481 C  CD    . LYS A 1 3107 ? 172.433 147.402 218.016 1.00 43.91  ? 3107 LYS A CD    1 
ATOM   12482 C  CE    . LYS A 1 3107 ? 172.896 147.113 219.433 1.00 50.07  ? 3107 LYS A CE    1 
ATOM   12483 N  NZ    . LYS A 1 3107 ? 172.756 145.669 219.771 1.00 54.27  ? 3107 LYS A NZ    1 
ATOM   12484 N  N     . GLU A 1 3108 ? 167.265 148.254 216.184 1.00 36.20  ? 3108 GLU A N     1 
ATOM   12485 C  CA    . GLU A 1 3108 ? 165.979 148.561 216.801 1.00 38.63  ? 3108 GLU A CA    1 
ATOM   12486 C  C     . GLU A 1 3108 ? 164.958 147.459 216.533 1.00 40.72  ? 3108 GLU A C     1 
ATOM   12487 O  O     . GLU A 1 3108 ? 164.231 147.047 217.444 1.00 42.33  ? 3108 GLU A O     1 
ATOM   12488 C  CB    . GLU A 1 3108 ? 165.466 149.913 216.303 1.00 44.22  ? 3108 GLU A CB    1 
ATOM   12489 C  CG    . GLU A 1 3108 ? 163.992 150.160 216.578 1.00 56.98  ? 3108 GLU A CG    1 
ATOM   12490 C  CD    . GLU A 1 3108 ? 163.732 150.588 218.012 1.00 61.35  ? 3108 GLU A CD    1 
ATOM   12491 O  OE1   . GLU A 1 3108 ? 164.706 150.886 218.734 1.00 57.40  ? 3108 GLU A OE1   1 
ATOM   12492 O  OE2   . GLU A 1 3108 ? 162.552 150.622 218.418 1.00 67.58  ? 3108 GLU A OE2   1 
ATOM   12493 N  N     . PHE A 1 3109 ? 164.883 146.969 215.289 1.00 40.83  ? 3109 PHE A N     1 
ATOM   12494 C  CA    . PHE A 1 3109 ? 163.950 145.877 215.003 1.00 43.81  ? 3109 PHE A CA    1 
ATOM   12495 C  C     . PHE A 1 3109 ? 164.344 144.568 215.679 1.00 44.61  ? 3109 PHE A C     1 
ATOM   12496 O  O     . PHE A 1 3109 ? 163.512 143.952 216.355 1.00 52.31  ? 3109 PHE A O     1 
ATOM   12497 C  CB    . PHE A 1 3109 ? 163.806 145.647 213.499 1.00 38.82  ? 3109 PHE A CB    1 
ATOM   12498 C  CG    . PHE A 1 3109 ? 163.072 146.732 212.774 1.00 39.92  ? 3109 PHE A CG    1 
ATOM   12499 C  CD1   . PHE A 1 3109 ? 162.324 147.661 213.463 1.00 46.83  ? 3109 PHE A CD1   1 
ATOM   12500 C  CD2   . PHE A 1 3109 ? 163.096 146.787 211.391 1.00 48.16  ? 3109 PHE A CD2   1 
ATOM   12501 C  CE1   . PHE A 1 3109 ? 161.630 148.631 212.793 1.00 56.06  ? 3109 PHE A CE1   1 
ATOM   12502 C  CE2   . PHE A 1 3109 ? 162.412 147.766 210.713 1.00 56.35  ? 3109 PHE A CE2   1 
ATOM   12503 C  CZ    . PHE A 1 3109 ? 161.675 148.689 211.416 1.00 58.00  ? 3109 PHE A CZ    1 
ATOM   12504 N  N     . THR A 1 3110 ? 165.589 144.125 215.525 1.00 38.24  ? 3110 THR A N     1 
ATOM   12505 C  CA    . THR A 1 3110 ? 165.994 142.834 216.062 1.00 42.29  ? 3110 THR A CA    1 
ATOM   12506 C  C     . THR A 1 3110 ? 166.236 142.859 217.563 1.00 46.68  ? 3110 THR A C     1 
ATOM   12507 O  O     . THR A 1 3110 ? 166.687 141.854 218.119 1.00 50.62  ? 3110 THR A O     1 
ATOM   12508 C  CB    . THR A 1 3110 ? 167.250 142.319 215.348 1.00 42.55  ? 3110 THR A CB    1 
ATOM   12509 O  OG1   . THR A 1 3110 ? 168.410 142.976 215.871 1.00 44.10  ? 3110 THR A OG1   1 
ATOM   12510 C  CG2   . THR A 1 3110 ? 167.153 142.529 213.841 1.00 32.63  ? 3110 THR A CG2   1 
ATOM   12511 N  N     . SER A 1 3111 ? 165.943 143.976 218.233 1.00 49.72  ? 3111 SER A N     1 
ATOM   12512 C  CA    . SER A 1 3111 ? 166.035 144.004 219.687 1.00 50.65  ? 3111 SER A CA    1 
ATOM   12513 C  C     . SER A 1 3111 ? 165.009 143.078 220.325 1.00 54.76  ? 3111 SER A C     1 
ATOM   12514 O  O     . SER A 1 3111 ? 165.293 142.452 221.352 1.00 49.67  ? 3111 SER A O     1 
ATOM   12515 C  CB    . SER A 1 3111 ? 165.855 145.433 220.198 1.00 43.21  ? 3111 SER A CB    1 
ATOM   12516 O  OG    . SER A 1 3111 ? 164.669 146.013 219.684 1.00 46.27  ? 3111 SER A OG    1 
ATOM   12517 N  N     . LYS A 1 3112 ? 163.816 142.978 219.734 1.00 56.42  ? 3112 LYS A N     1 
ATOM   12518 C  CA    . LYS A 1 3112 ? 162.798 142.073 220.258 1.00 57.77  ? 3112 LYS A CA    1 
ATOM   12519 C  C     . LYS A 1 3112 ? 163.151 140.615 219.994 1.00 57.02  ? 3112 LYS A C     1 
ATOM   12520 O  O     . LYS A 1 3112 ? 162.630 139.720 220.670 1.00 57.27  ? 3112 LYS A O     1 
ATOM   12521 C  CB    . LYS A 1 3112 ? 161.438 142.405 219.643 1.00 61.79  ? 3112 LYS A CB    1 
ATOM   12522 C  CG    . LYS A 1 3112 ? 160.894 143.770 220.031 1.00 63.46  ? 3112 LYS A CG    1 
ATOM   12523 C  CD    . LYS A 1 3112 ? 160.307 143.753 221.431 1.00 66.08  ? 3112 LYS A CD    1 
ATOM   12524 C  CE    . LYS A 1 3112 ? 159.034 142.923 221.484 1.00 64.56  ? 3112 LYS A CE    1 
ATOM   12525 N  NZ    . LYS A 1 3112 ? 158.918 142.164 222.759 1.00 66.55  ? 3112 LYS A NZ    1 
ATOM   12526 N  N     . MET A 1 3113 ? 164.022 140.358 219.024 1.00 55.38  ? 3113 MET A N     1 
ATOM   12527 C  CA    . MET A 1 3113 ? 164.388 139.000 218.657 1.00 49.61  ? 3113 MET A CA    1 
ATOM   12528 C  C     . MET A 1 3113 ? 165.399 138.429 219.649 1.00 54.18  ? 3113 MET A C     1 
ATOM   12529 O  O     . MET A 1 3113 ? 166.075 139.157 220.381 1.00 58.13  ? 3113 MET A O     1 
ATOM   12530 C  CB    . MET A 1 3113 ? 164.955 138.971 217.238 1.00 41.86  ? 3113 MET A CB    1 
ATOM   12531 C  CG    . MET A 1 3113 ? 163.884 138.955 216.159 1.00 43.73  ? 3113 MET A CG    1 
ATOM   12532 S  SD    . MET A 1 3113 ? 164.532 138.951 214.477 1.00 40.61  ? 3113 MET A SD    1 
ATOM   12533 C  CE    . MET A 1 3113 ? 166.097 138.121 214.703 1.00 38.43  ? 3113 MET A CE    1 
ATOM   12534 N  N     . ASP A 1 3114 ? 165.495 137.099 219.664 1.00 53.82  ? 3114 ASP A N     1 
ATOM   12535 C  CA    . ASP A 1 3114 ? 166.377 136.386 220.588 1.00 59.94  ? 3114 ASP A CA    1 
ATOM   12536 C  C     . ASP A 1 3114 ? 167.663 136.025 219.849 1.00 57.03  ? 3114 ASP A C     1 
ATOM   12537 O  O     . ASP A 1 3114 ? 167.832 134.922 219.331 1.00 62.07  ? 3114 ASP A O     1 
ATOM   12538 C  CB    . ASP A 1 3114 ? 165.679 135.151 221.151 1.00 69.57  ? 3114 ASP A CB    1 
ATOM   12539 C  CG    . ASP A 1 3114 ? 164.373 135.486 221.846 1.00 77.14  ? 3114 ASP A CG    1 
ATOM   12540 O  OD1   . ASP A 1 3114 ? 163.367 135.717 221.144 1.00 73.94  ? 3114 ASP A OD1   1 
ATOM   12541 O  OD2   . ASP A 1 3114 ? 164.352 135.515 223.095 1.00 79.30  ? 3114 ASP A OD2   1 
ATOM   12542 N  N     . LEU A 1 3115 ? 168.585 136.985 219.807 1.00 59.34  ? 3115 LEU A N     1 
ATOM   12543 C  CA    . LEU A 1 3115 ? 169.851 136.826 219.105 1.00 53.77  ? 3115 LEU A CA    1 
ATOM   12544 C  C     . LEU A 1 3115 ? 171.044 136.697 220.043 1.00 53.60  ? 3115 LEU A C     1 
ATOM   12545 O  O     . LEU A 1 3115 ? 172.186 136.691 219.574 1.00 47.68  ? 3115 LEU A O     1 
ATOM   12546 C  CB    . LEU A 1 3115 ? 170.069 137.998 218.146 1.00 48.91  ? 3115 LEU A CB    1 
ATOM   12547 C  CG    . LEU A 1 3115 ? 169.057 138.094 217.007 1.00 43.95  ? 3115 LEU A CG    1 
ATOM   12548 C  CD1   . LEU A 1 3115 ? 169.442 139.200 216.041 1.00 36.36  ? 3115 LEU A CD1   1 
ATOM   12549 C  CD2   . LEU A 1 3115 ? 168.969 136.758 216.290 1.00 50.21  ? 3115 LEU A CD2   1 
ATOM   12550 N  N     . GLU A 1 3116 ? 170.813 136.590 221.349 1.00 65.71  ? 3116 GLU A N     1 
ATOM   12551 C  CA    . GLU A 1 3116 ? 171.906 136.441 222.304 1.00 67.61  ? 3116 GLU A CA    1 
ATOM   12552 C  C     . GLU A 1 3116 ? 172.439 135.015 222.225 1.00 69.84  ? 3116 GLU A C     1 
ATOM   12553 O  O     . GLU A 1 3116 ? 171.712 134.054 222.495 1.00 63.79  ? 3116 GLU A O     1 
ATOM   12554 C  CB    . GLU A 1 3116 ? 171.443 136.785 223.717 1.00 64.51  ? 3116 GLU A CB    1 
ATOM   12555 C  CG    . GLU A 1 3116 ? 170.059 136.270 224.076 1.00 68.31  ? 3116 GLU A CG    1 
ATOM   12556 C  CD    . GLU A 1 3116 ? 168.975 137.303 223.844 1.00 68.43  ? 3116 GLU A CD    1 
ATOM   12557 O  OE1   . GLU A 1 3116 ? 169.140 138.148 222.939 1.00 65.81  ? 3116 GLU A OE1   1 
ATOM   12558 O  OE2   . GLU A 1 3116 ? 167.958 137.272 224.568 1.00 72.94  ? 3116 GLU A OE2   1 
ATOM   12559 N  N     . LYS A 1 3117 ? 173.711 134.878 221.849 1.00 75.87  ? 3117 LYS A N     1 
ATOM   12560 C  CA    . LYS A 1 3117 ? 174.380 133.584 221.725 1.00 74.11  ? 3117 LYS A CA    1 
ATOM   12561 C  C     . LYS A 1 3117 ? 175.652 133.640 222.561 1.00 77.51  ? 3117 LYS A C     1 
ATOM   12562 O  O     . LYS A 1 3117 ? 176.712 134.059 222.068 1.00 73.76  ? 3117 LYS A O     1 
ATOM   12563 C  CB    . LYS A 1 3117 ? 174.679 133.257 220.263 1.00 66.36  ? 3117 LYS A CB    1 
ATOM   12564 C  CG    . LYS A 1 3117 ? 175.245 131.868 220.041 1.00 71.27  ? 3117 LYS A CG    1 
ATOM   12565 C  CD    . LYS A 1 3117 ? 175.595 131.632 218.581 1.00 72.38  ? 3117 LYS A CD    1 
ATOM   12566 C  CE    . LYS A 1 3117 ? 174.352 131.333 217.758 1.00 70.01  ? 3117 LYS A CE    1 
ATOM   12567 N  NZ    . LYS A 1 3117 ? 174.688 130.990 216.349 1.00 68.41  ? 3117 LYS A NZ    1 
ATOM   12568 N  N     . PRO A 1 3118 ? 175.589 133.246 223.836 1.00 82.60  ? 3118 PRO A N     1 
ATOM   12569 C  CA    . PRO A 1 3118 ? 176.760 133.399 224.717 1.00 79.70  ? 3118 PRO A CA    1 
ATOM   12570 C  C     . PRO A 1 3118 ? 177.998 132.654 224.247 1.00 79.78  ? 3118 PRO A C     1 
ATOM   12571 O  O     . PRO A 1 3118 ? 179.114 133.113 224.519 1.00 79.60  ? 3118 PRO A O     1 
ATOM   12572 C  CB    . PRO A 1 3118 ? 176.257 132.853 226.060 1.00 81.02  ? 3118 PRO A CB    1 
ATOM   12573 C  CG    . PRO A 1 3118 ? 174.771 133.013 225.998 1.00 79.81  ? 3118 PRO A CG    1 
ATOM   12574 C  CD    . PRO A 1 3118 ? 174.408 132.757 224.565 1.00 78.88  ? 3118 PRO A CD    1 
ATOM   12575 N  N     . ASN A 1 3119 ? 177.846 131.527 223.556 1.00 77.98  ? 3119 ASN A N     1 
ATOM   12576 C  CA    . ASN A 1 3119 ? 178.993 130.759 223.089 1.00 80.20  ? 3119 ASN A CA    1 
ATOM   12577 C  C     . ASN A 1 3119 ? 179.486 131.198 221.715 1.00 82.09  ? 3119 ASN A C     1 
ATOM   12578 O  O     . ASN A 1 3119 ? 180.336 130.516 221.132 1.00 81.65  ? 3119 ASN A O     1 
ATOM   12579 C  CB    . ASN A 1 3119 ? 178.664 129.259 223.087 1.00 81.86  ? 3119 ASN A CB    1 
ATOM   12580 C  CG    . ASN A 1 3119 ? 177.543 128.893 222.126 1.00 87.14  ? 3119 ASN A CG    1 
ATOM   12581 O  OD1   . ASN A 1 3119 ? 177.067 129.720 221.353 1.00 88.87  ? 3119 ASN A OD1   1 
ATOM   12582 N  ND2   . ASN A 1 3119 ? 177.118 127.636 222.175 1.00 87.17  ? 3119 ASN A ND2   1 
ATOM   12583 N  N     . TYR A 1 3120 ? 178.969 132.305 221.186 1.00 78.47  ? 3120 TYR A N     1 
ATOM   12584 C  CA    . TYR A 1 3120 ? 179.472 132.851 219.933 1.00 72.90  ? 3120 TYR A CA    1 
ATOM   12585 C  C     . TYR A 1 3120 ? 180.939 133.236 220.074 1.00 72.34  ? 3120 TYR A C     1 
ATOM   12586 O  O     . TYR A 1 3120 ? 181.341 133.852 221.065 1.00 72.88  ? 3120 TYR A O     1 
ATOM   12587 C  CB    . TYR A 1 3120 ? 178.640 134.065 219.522 1.00 67.87  ? 3120 TYR A CB    1 
ATOM   12588 C  CG    . TYR A 1 3120 ? 179.156 134.796 218.305 1.00 63.31  ? 3120 TYR A CG    1 
ATOM   12589 C  CD1   . TYR A 1 3120 ? 179.048 134.241 217.037 1.00 58.94  ? 3120 TYR A CD1   1 
ATOM   12590 C  CD2   . TYR A 1 3120 ? 179.747 136.047 218.424 1.00 63.71  ? 3120 TYR A CD2   1 
ATOM   12591 C  CE1   . TYR A 1 3120 ? 179.518 134.911 215.923 1.00 61.75  ? 3120 TYR A CE1   1 
ATOM   12592 C  CE2   . TYR A 1 3120 ? 180.219 136.723 217.316 1.00 61.93  ? 3120 TYR A CE2   1 
ATOM   12593 C  CZ    . TYR A 1 3120 ? 180.102 136.150 216.069 1.00 64.86  ? 3120 TYR A CZ    1 
ATOM   12594 O  OH    . TYR A 1 3120 ? 180.571 136.820 214.962 1.00 64.28  ? 3120 TYR A OH    1 
ATOM   12595 N  N     . ILE A 1 3121 ? 181.739 132.872 219.076 1.00 71.72  ? 3121 ILE A N     1 
ATOM   12596 C  CA    . ILE A 1 3121 ? 183.174 133.129 219.073 1.00 75.27  ? 3121 ILE A CA    1 
ATOM   12597 C  C     . ILE A 1 3121 ? 183.464 134.176 218.008 1.00 77.20  ? 3121 ILE A C     1 
ATOM   12598 O  O     . ILE A 1 3121 ? 183.130 133.986 216.832 1.00 78.25  ? 3121 ILE A O     1 
ATOM   12599 C  CB    . ILE A 1 3121 ? 183.979 131.845 218.820 1.00 81.16  ? 3121 ILE A CB    1 
ATOM   12600 C  CG1   . ILE A 1 3121 ? 183.868 130.903 220.020 1.00 80.22  ? 3121 ILE A CG1   1 
ATOM   12601 C  CG2   . ILE A 1 3121 ? 185.436 132.177 218.531 1.00 77.06  ? 3121 ILE A CG2   1 
ATOM   12602 C  CD1   . ILE A 1 3121 ? 183.877 129.437 219.647 1.00 78.79  ? 3121 ILE A CD1   1 
ATOM   12603 N  N     . VAL A 1 3122 ? 184.082 135.275 218.417 1.00 77.31  ? 3122 VAL A N     1 
ATOM   12604 C  CA    . VAL A 1 3122 ? 184.429 136.338 217.468 1.00 79.36  ? 3122 VAL A CA    1 
ATOM   12605 C  C     . VAL A 1 3122 ? 185.593 135.874 216.599 1.00 82.70  ? 3122 VAL A C     1 
ATOM   12606 O  O     . VAL A 1 3122 ? 186.623 135.429 217.136 1.00 82.60  ? 3122 VAL A O     1 
ATOM   12607 C  CB    . VAL A 1 3122 ? 184.779 137.626 218.214 1.00 76.07  ? 3122 VAL A CB    1 
ATOM   12608 C  CG1   . VAL A 1 3122 ? 185.110 138.736 217.229 1.00 73.09  ? 3122 VAL A CG1   1 
ATOM   12609 C  CG2   . VAL A 1 3122 ? 183.633 138.038 219.125 1.00 73.94  ? 3122 VAL A CG2   1 
ATOM   12610 N  N     . PRO A 1 3123 ? 185.485 135.946 215.276 1.00 81.09  ? 3123 PRO A N     1 
ATOM   12611 C  CA    . PRO A 1 3123 ? 186.607 135.550 214.421 1.00 86.51  ? 3123 PRO A CA    1 
ATOM   12612 C  C     . PRO A 1 3123 ? 187.765 136.529 214.536 1.00 91.68  ? 3123 PRO A C     1 
ATOM   12613 O  O     . PRO A 1 3123 ? 187.615 137.671 214.976 1.00 85.35  ? 3123 PRO A O     1 
ATOM   12614 C  CB    . PRO A 1 3123 ? 186.005 135.564 213.013 1.00 77.83  ? 3123 PRO A CB    1 
ATOM   12615 C  CG    . PRO A 1 3123 ? 184.872 136.529 213.104 1.00 74.05  ? 3123 PRO A CG    1 
ATOM   12616 C  CD    . PRO A 1 3123 ? 184.315 136.377 214.492 1.00 71.12  ? 3123 PRO A CD    1 
ATOM   12617 N  N     . ASP A 1 3124 ? 188.946 136.052 214.135 1.00 97.87  ? 3124 ASP A N     1 
ATOM   12618 C  CA    . ASP A 1 3124 ? 190.134 136.900 214.167 1.00 99.74  ? 3124 ASP A CA    1 
ATOM   12619 C  C     . ASP A 1 3124 ? 189.981 138.103 213.243 1.00 100.09 ? 3124 ASP A C     1 
ATOM   12620 O  O     . ASP A 1 3124 ? 190.372 139.221 213.597 1.00 100.42 ? 3124 ASP A O     1 
ATOM   12621 C  CB    . ASP A 1 3124 ? 191.376 136.081 213.807 1.00 104.88 ? 3124 ASP A CB    1 
ATOM   12622 C  CG    . ASP A 1 3124 ? 191.305 135.478 212.413 1.00 111.26 ? 3124 ASP A CG    1 
ATOM   12623 O  OD1   . ASP A 1 3124 ? 190.272 135.642 211.730 1.00 108.46 ? 3124 ASP A OD1   1 
ATOM   12624 O  OD2   . ASP A 1 3124 ? 192.292 134.834 211.998 1.00 114.45 ? 3124 ASP A OD2   1 
ATOM   12625 N  N     . TYR A 1 3125 ? 189.414 137.894 212.059 1.00 95.62  ? 3125 TYR A N     1 
ATOM   12626 C  CA    . TYR A 1 3125 ? 189.110 138.968 211.124 1.00 92.55  ? 3125 TYR A CA    1 
ATOM   12627 C  C     . TYR A 1 3125 ? 187.599 139.143 211.069 1.00 91.81  ? 3125 TYR A C     1 
ATOM   12628 O  O     . TYR A 1 3125 ? 186.872 138.190 210.768 1.00 89.88  ? 3125 TYR A O     1 
ATOM   12629 C  CB    . TYR A 1 3125 ? 189.670 138.667 209.733 1.00 91.40  ? 3125 TYR A CB    1 
ATOM   12630 C  CG    . TYR A 1 3125 ? 188.940 139.379 208.616 1.00 96.91  ? 3125 TYR A CG    1 
ATOM   12631 C  CD1   . TYR A 1 3125 ? 189.062 140.752 208.445 1.00 91.95  ? 3125 TYR A CD1   1 
ATOM   12632 C  CD2   . TYR A 1 3125 ? 188.128 138.678 207.734 1.00 93.56  ? 3125 TYR A CD2   1 
ATOM   12633 C  CE1   . TYR A 1 3125 ? 188.396 141.407 207.426 1.00 92.62  ? 3125 TYR A CE1   1 
ATOM   12634 C  CE2   . TYR A 1 3125 ? 187.458 139.325 206.712 1.00 89.06  ? 3125 TYR A CE2   1 
ATOM   12635 C  CZ    . TYR A 1 3125 ? 187.596 140.689 206.563 1.00 93.68  ? 3125 TYR A CZ    1 
ATOM   12636 O  OH    . TYR A 1 3125 ? 186.931 141.336 205.547 1.00 91.32  ? 3125 TYR A OH    1 
ATOM   12637 N  N     . MET A 1 3126 ? 187.131 140.354 211.361 1.00 88.40  ? 3126 MET A N     1 
ATOM   12638 C  CA    . MET A 1 3126 ? 185.706 140.649 211.384 1.00 85.69  ? 3126 MET A CA    1 
ATOM   12639 C  C     . MET A 1 3126 ? 185.337 141.489 210.172 1.00 82.00  ? 3126 MET A C     1 
ATOM   12640 O  O     . MET A 1 3126 ? 185.869 142.598 210.014 1.00 82.11  ? 3126 MET A O     1 
ATOM   12641 C  CB    . MET A 1 3126 ? 185.326 141.376 212.672 1.00 81.01  ? 3126 MET A CB    1 
ATOM   12642 C  CG    . MET A 1 3126 ? 184.525 140.530 213.648 1.00 81.43  ? 3126 MET A CG    1 
ATOM   12643 S  SD    . MET A 1 3126 ? 183.038 139.826 212.909 1.00 87.06  ? 3126 MET A SD    1 
ATOM   12644 C  CE    . MET A 1 3126 ? 182.004 141.282 212.776 1.00 71.10  ? 3126 MET A CE    1 
ATOM   12645 N  N     . PRO A 1 3127 ? 184.450 141.014 209.295 1.00 76.10  ? 3127 PRO A N     1 
ATOM   12646 C  CA    . PRO A 1 3127 ? 184.028 141.840 208.156 1.00 74.85  ? 3127 PRO A CA    1 
ATOM   12647 C  C     . PRO A 1 3127 ? 183.169 143.007 208.611 1.00 72.01  ? 3127 PRO A C     1 
ATOM   12648 O  O     . PRO A 1 3127 ? 181.945 142.994 208.450 1.00 68.84  ? 3127 PRO A O     1 
ATOM   12649 C  CB    . PRO A 1 3127 ? 183.235 140.863 207.275 1.00 69.15  ? 3127 PRO A CB    1 
ATOM   12650 C  CG    . PRO A 1 3127 ? 183.500 139.494 207.838 1.00 62.94  ? 3127 PRO A CG    1 
ATOM   12651 C  CD    . PRO A 1 3127 ? 183.820 139.686 209.280 1.00 64.82  ? 3127 PRO A CD    1 
ATOM   12652 N  N     . VAL A 1 3128 ? 183.808 144.022 209.183 1.00 74.55  ? 3128 VAL A N     1 
ATOM   12653 C  CA    . VAL A 1 3128 ? 183.094 145.135 209.799 1.00 70.33  ? 3128 VAL A CA    1 
ATOM   12654 C  C     . VAL A 1 3128 ? 182.611 146.082 208.708 1.00 66.83  ? 3128 VAL A C     1 
ATOM   12655 O  O     . VAL A 1 3128 ? 183.414 146.650 207.961 1.00 64.17  ? 3128 VAL A O     1 
ATOM   12656 C  CB    . VAL A 1 3128 ? 183.986 145.865 210.813 1.00 69.35  ? 3128 VAL A CB    1 
ATOM   12657 C  CG1   . VAL A 1 3128 ? 183.373 147.197 211.196 1.00 65.88  ? 3128 VAL A CG1   1 
ATOM   12658 C  CG2   . VAL A 1 3128 ? 184.203 144.999 212.045 1.00 63.71  ? 3128 VAL A CG2   1 
ATOM   12659 N  N     . VAL A 1 3129 ? 181.296 146.250 208.616 1.00 63.22  ? 3129 VAL A N     1 
ATOM   12660 C  CA    . VAL A 1 3129 ? 180.682 147.190 207.685 1.00 56.06  ? 3129 VAL A CA    1 
ATOM   12661 C  C     . VAL A 1 3129 ? 180.346 148.506 208.372 1.00 54.79  ? 3129 VAL A C     1 
ATOM   12662 O  O     . VAL A 1 3129 ? 180.567 149.581 207.816 1.00 59.61  ? 3129 VAL A O     1 
ATOM   12663 C  CB    . VAL A 1 3129 ? 179.430 146.558 207.037 1.00 46.92  ? 3129 VAL A CB    1 
ATOM   12664 C  CG1   . VAL A 1 3129 ? 178.845 147.490 205.993 1.00 45.79  ? 3129 VAL A CG1   1 
ATOM   12665 C  CG2   . VAL A 1 3129 ? 179.774 145.210 206.425 1.00 42.56  ? 3129 VAL A CG2   1 
ATOM   12666 N  N     . TYR A 1 3130 ? 179.811 148.434 209.588 1.00 51.39  ? 3130 TYR A N     1 
ATOM   12667 C  CA    . TYR A 1 3130 ? 179.526 149.615 210.395 1.00 51.34  ? 3130 TYR A CA    1 
ATOM   12668 C  C     . TYR A 1 3130 ? 180.810 150.009 211.116 1.00 62.22  ? 3130 TYR A C     1 
ATOM   12669 O  O     . TYR A 1 3130 ? 181.226 149.337 212.065 1.00 66.62  ? 3130 TYR A O     1 
ATOM   12670 C  CB    . TYR A 1 3130 ? 178.395 149.323 211.378 1.00 47.57  ? 3130 TYR A CB    1 
ATOM   12671 C  CG    . TYR A 1 3130 ? 178.064 150.462 212.314 1.00 50.58  ? 3130 TYR A CG    1 
ATOM   12672 C  CD1   . TYR A 1 3130 ? 178.069 151.775 211.871 1.00 47.45  ? 3130 TYR A CD1   1 
ATOM   12673 C  CD2   . TYR A 1 3130 ? 177.741 150.220 213.643 1.00 54.26  ? 3130 TYR A CD2   1 
ATOM   12674 C  CE1   . TYR A 1 3130 ? 177.766 152.814 212.724 1.00 50.22  ? 3130 TYR A CE1   1 
ATOM   12675 C  CE2   . TYR A 1 3130 ? 177.435 151.255 214.503 1.00 52.22  ? 3130 TYR A CE2   1 
ATOM   12676 C  CZ    . TYR A 1 3130 ? 177.449 152.551 214.037 1.00 54.78  ? 3130 TYR A CZ    1 
ATOM   12677 O  OH    . TYR A 1 3130 ? 177.146 153.589 214.887 1.00 69.79  ? 3130 TYR A OH    1 
ATOM   12678 N  N     . ASP A 1 3131 ? 181.433 151.103 210.670 1.00 62.75  ? 3131 ASP A N     1 
ATOM   12679 C  CA    . ASP A 1 3131 ? 182.771 151.448 211.145 1.00 67.39  ? 3131 ASP A CA    1 
ATOM   12680 C  C     . ASP A 1 3131 ? 182.806 151.699 212.647 1.00 65.84  ? 3131 ASP A C     1 
ATOM   12681 O  O     . ASP A 1 3131 ? 183.850 151.508 213.281 1.00 63.54  ? 3131 ASP A O     1 
ATOM   12682 C  CB    . ASP A 1 3131 ? 183.295 152.670 210.391 1.00 74.08  ? 3131 ASP A CB    1 
ATOM   12683 C  CG    . ASP A 1 3131 ? 183.333 152.455 208.891 1.00 83.71  ? 3131 ASP A CG    1 
ATOM   12684 O  OD1   . ASP A 1 3131 ? 182.787 153.302 208.153 1.00 89.07  ? 3131 ASP A OD1   1 
ATOM   12685 O  OD2   . ASP A 1 3131 ? 183.909 151.439 208.451 1.00 83.67  ? 3131 ASP A OD2   1 
ATOM   12686 N  N     . LYS A 1 3132 ? 181.689 152.122 213.236 1.00 64.31  ? 3132 LYS A N     1 
ATOM   12687 C  CA    . LYS A 1 3132 ? 181.615 152.349 214.672 1.00 58.60  ? 3132 LYS A CA    1 
ATOM   12688 C  C     . LYS A 1 3132 ? 181.176 151.108 215.442 1.00 62.61  ? 3132 LYS A C     1 
ATOM   12689 O  O     . LYS A 1 3132 ? 180.718 151.228 216.584 1.00 69.44  ? 3132 LYS A O     1 
ATOM   12690 C  CB    . LYS A 1 3132 ? 180.678 153.521 214.978 1.00 59.60  ? 3132 LYS A CB    1 
ATOM   12691 C  CG    . LYS A 1 3132 ? 180.576 154.552 213.864 1.00 69.51  ? 3132 LYS A CG    1 
ATOM   12692 C  CD    . LYS A 1 3132 ? 181.879 155.320 213.703 1.00 74.93  ? 3132 LYS A CD    1 
ATOM   12693 C  CE    . LYS A 1 3132 ? 182.018 156.396 214.767 1.00 68.76  ? 3132 LYS A CE    1 
ATOM   12694 N  NZ    . LYS A 1 3132 ? 183.257 157.201 214.584 1.00 65.17  ? 3132 LYS A NZ    1 
ATOM   12695 N  N     . LEU A 1 3133 ? 181.295 149.927 214.842 1.00 60.31  ? 3133 LEU A N     1 
ATOM   12696 C  CA    . LEU A 1 3133 ? 180.978 148.700 215.554 1.00 59.77  ? 3133 LEU A CA    1 
ATOM   12697 C  C     . LEU A 1 3133 ? 181.997 148.464 216.668 1.00 62.91  ? 3133 LEU A C     1 
ATOM   12698 O  O     . LEU A 1 3133 ? 183.197 148.681 216.468 1.00 66.75  ? 3133 LEU A O     1 
ATOM   12699 C  CB    . LEU A 1 3133 ? 180.966 147.510 214.594 1.00 59.86  ? 3133 LEU A CB    1 
ATOM   12700 C  CG    . LEU A 1 3133 ? 180.568 146.140 215.143 1.00 60.95  ? 3133 LEU A CG    1 
ATOM   12701 C  CD1   . LEU A 1 3133 ? 179.060 146.017 215.235 1.00 52.55  ? 3133 LEU A CD1   1 
ATOM   12702 C  CD2   . LEU A 1 3133 ? 181.141 145.029 214.277 1.00 58.50  ? 3133 LEU A CD2   1 
ATOM   12703 N  N     . PRO A 1 3134 ? 181.552 148.039 217.850 1.00 60.49  ? 3134 PRO A N     1 
ATOM   12704 C  CA    . PRO A 1 3134 ? 182.500 147.730 218.927 1.00 70.57  ? 3134 PRO A CA    1 
ATOM   12705 C  C     . PRO A 1 3134 ? 183.476 146.637 218.516 1.00 71.83  ? 3134 PRO A C     1 
ATOM   12706 O  O     . PRO A 1 3134 ? 183.124 145.699 217.797 1.00 69.09  ? 3134 PRO A O     1 
ATOM   12707 C  CB    . PRO A 1 3134 ? 181.593 147.275 220.075 1.00 67.12  ? 3134 PRO A CB    1 
ATOM   12708 C  CG    . PRO A 1 3134 ? 180.295 147.958 219.811 1.00 56.61  ? 3134 PRO A CG    1 
ATOM   12709 C  CD    . PRO A 1 3134 ? 180.157 148.022 218.316 1.00 58.21  ? 3134 PRO A CD    1 
ATOM   12710 N  N     . GLN A 1 3135 ? 184.719 146.779 218.975 1.00 78.94  ? 3135 GLN A N     1 
ATOM   12711 C  CA    . GLN A 1 3135 ? 185.770 145.854 218.561 1.00 88.23  ? 3135 GLN A CA    1 
ATOM   12712 C  C     . GLN A 1 3135 ? 185.512 144.412 218.992 1.00 90.56  ? 3135 GLN A C     1 
ATOM   12713 O  O     . GLN A 1 3135 ? 185.826 143.505 218.202 1.00 90.39  ? 3135 GLN A O     1 
ATOM   12714 C  CB    . GLN A 1 3135 ? 187.132 146.362 219.062 1.00 95.02  ? 3135 GLN A CB    1 
ATOM   12715 C  CG    . GLN A 1 3135 ? 188.318 145.523 218.619 1.00 99.20  ? 3135 GLN A CG    1 
ATOM   12716 C  CD    . GLN A 1 3135 ? 188.545 145.585 217.122 1.00 100.33 ? 3135 GLN A CD    1 
ATOM   12717 O  OE1   . GLN A 1 3135 ? 188.432 146.647 216.508 1.00 99.90  ? 3135 GLN A OE1   1 
ATOM   12718 N  NE2   . GLN A 1 3135 ? 188.869 144.445 216.524 1.00 94.45  ? 3135 GLN A NE2   1 
ATOM   12719 N  N     . PRO A 1 3136 ? 185.046 144.118 220.208 1.00 86.60  ? 3136 PRO A N     1 
ATOM   12720 C  CA    . PRO A 1 3136 ? 184.533 142.763 220.501 1.00 81.46  ? 3136 PRO A CA    1 
ATOM   12721 C  C     . PRO A 1 3136 ? 183.041 142.670 220.231 1.00 84.31  ? 3136 PRO A C     1 
ATOM   12722 O  O     . PRO A 1 3136 ? 182.236 142.781 221.168 1.00 83.26  ? 3136 PRO A O     1 
ATOM   12723 C  CB    . PRO A 1 3136 ? 184.823 142.575 221.999 1.00 81.12  ? 3136 PRO A CB    1 
ATOM   12724 C  CG    . PRO A 1 3136 ? 185.138 143.907 222.536 1.00 81.51  ? 3136 PRO A CG    1 
ATOM   12725 C  CD    . PRO A 1 3136 ? 185.359 144.877 221.433 1.00 81.53  ? 3136 PRO A CD    1 
ATOM   12726 N  N     . PRO A 1 3137 ? 182.619 142.472 218.982 1.00 80.11  ? 3137 PRO A N     1 
ATOM   12727 C  CA    . PRO A 1 3137 ? 181.180 142.491 218.698 1.00 66.46  ? 3137 PRO A CA    1 
ATOM   12728 C  C     . PRO A 1 3137 ? 180.492 141.242 219.231 1.00 65.50  ? 3137 PRO A C     1 
ATOM   12729 O  O     . PRO A 1 3137 ? 181.031 140.135 219.161 1.00 70.53  ? 3137 PRO A O     1 
ATOM   12730 C  CB    . PRO A 1 3137 ? 181.124 142.551 217.170 1.00 59.14  ? 3137 PRO A CB    1 
ATOM   12731 C  CG    . PRO A 1 3137 ? 182.356 141.831 216.731 1.00 67.34  ? 3137 PRO A CG    1 
ATOM   12732 C  CD    . PRO A 1 3137 ? 183.380 141.919 217.848 1.00 77.36  ? 3137 PRO A CD    1 
ATOM   12733 N  N     . SER A 1 3138 ? 179.291 141.430 219.771 1.00 60.21  ? 3138 SER A N     1 
ATOM   12734 C  CA    . SER A 1 3138 ? 178.493 140.305 220.229 1.00 55.70  ? 3138 SER A CA    1 
ATOM   12735 C  C     . SER A 1 3138 ? 177.779 139.660 219.042 1.00 56.66  ? 3138 SER A C     1 
ATOM   12736 O  O     . SER A 1 3138 ? 177.912 140.089 217.893 1.00 62.86  ? 3138 SER A O     1 
ATOM   12737 C  CB    . SER A 1 3138 ? 177.502 140.750 221.302 1.00 55.37  ? 3138 SER A CB    1 
ATOM   12738 O  OG    . SER A 1 3138 ? 176.645 141.768 220.821 1.00 54.30  ? 3138 SER A OG    1 
ATOM   12739 N  N     . HIS A 1 3139 ? 177.015 138.601 219.323 1.00 49.87  ? 3139 HIS A N     1 
ATOM   12740 C  CA    . HIS A 1 3139 ? 176.309 137.899 218.256 1.00 47.97  ? 3139 HIS A CA    1 
ATOM   12741 C  C     . HIS A 1 3139 ? 175.262 138.791 217.599 1.00 49.28  ? 3139 HIS A C     1 
ATOM   12742 O  O     . HIS A 1 3139 ? 175.132 138.805 216.370 1.00 48.90  ? 3139 HIS A O     1 
ATOM   12743 C  CB    . HIS A 1 3139 ? 175.659 136.629 218.804 1.00 52.64  ? 3139 HIS A CB    1 
ATOM   12744 C  CG    . HIS A 1 3139 ? 175.066 135.753 217.746 1.00 51.08  ? 3139 HIS A CG    1 
ATOM   12745 N  ND1   . HIS A 1 3139 ? 173.754 135.332 217.780 1.00 53.98  ? 3139 HIS A ND1   1 
ATOM   12746 C  CD2   . HIS A 1 3139 ? 175.604 135.217 216.626 1.00 50.15  ? 3139 HIS A CD2   1 
ATOM   12747 C  CE1   . HIS A 1 3139 ? 173.510 134.576 216.725 1.00 55.16  ? 3139 HIS A CE1   1 
ATOM   12748 N  NE2   . HIS A 1 3139 ? 174.616 134.489 216.009 1.00 51.55  ? 3139 HIS A NE2   1 
ATOM   12749 N  N     . ARG A 1 3140 ? 174.506 139.541 218.404 1.00 45.06  ? 3140 ARG A N     1 
ATOM   12750 C  CA    . ARG A 1 3140 ? 173.468 140.411 217.858 1.00 41.78  ? 3140 ARG A CA    1 
ATOM   12751 C  C     . ARG A 1 3140 ? 174.067 141.488 216.963 1.00 43.20  ? 3140 ARG A C     1 
ATOM   12752 O  O     . ARG A 1 3140 ? 173.534 141.786 215.885 1.00 47.10  ? 3140 ARG A O     1 
ATOM   12753 C  CB    . ARG A 1 3140 ? 172.677 141.042 219.002 1.00 39.95  ? 3140 ARG A CB    1 
ATOM   12754 C  CG    . ARG A 1 3140 ? 171.404 141.750 218.587 1.00 43.28  ? 3140 ARG A CG    1 
ATOM   12755 C  CD    . ARG A 1 3140 ? 170.787 142.469 219.775 1.00 44.04  ? 3140 ARG A CD    1 
ATOM   12756 N  NE    . ARG A 1 3140 ? 170.208 141.536 220.735 1.00 45.38  ? 3140 ARG A NE    1 
ATOM   12757 C  CZ    . ARG A 1 3140 ? 168.992 141.018 220.639 1.00 45.16  ? 3140 ARG A CZ    1 
ATOM   12758 N  NH1   . ARG A 1 3140 ? 168.192 141.315 219.630 1.00 47.05  ? 3140 ARG A NH1   1 
ATOM   12759 N  NH2   . ARG A 1 3140 ? 168.567 140.180 221.580 1.00 47.33  ? 3140 ARG A NH2   1 
ATOM   12760 N  N     . GLU A 1 3141 ? 175.177 142.086 217.398 1.00 41.35  ? 3141 GLU A N     1 
ATOM   12761 C  CA    . GLU A 1 3141 ? 175.831 143.114 216.598 1.00 37.84  ? 3141 GLU A CA    1 
ATOM   12762 C  C     . GLU A 1 3141 ? 176.384 142.535 215.304 1.00 36.61  ? 3141 GLU A C     1 
ATOM   12763 O  O     . GLU A 1 3141 ? 176.326 143.183 214.252 1.00 36.60  ? 3141 GLU A O     1 
ATOM   12764 C  CB    . GLU A 1 3141 ? 176.936 143.778 217.414 1.00 47.05  ? 3141 GLU A CB    1 
ATOM   12765 C  CG    . GLU A 1 3141 ? 176.486 144.197 218.797 1.00 50.05  ? 3141 GLU A CG    1 
ATOM   12766 C  CD    . GLU A 1 3141 ? 177.124 145.487 219.243 1.00 64.92  ? 3141 GLU A CD    1 
ATOM   12767 O  OE1   . GLU A 1 3141 ? 177.769 146.145 218.405 1.00 65.40  ? 3141 GLU A OE1   1 
ATOM   12768 O  OE2   . GLU A 1 3141 ? 176.979 145.846 220.429 1.00 74.36  ? 3141 GLU A OE2   1 
ATOM   12769 N  N     . ALA A 1 3142 ? 176.926 141.317 215.362 1.00 35.01  ? 3142 ALA A N     1 
ATOM   12770 C  CA    . ALA A 1 3142 ? 177.384 140.652 214.148 1.00 34.79  ? 3142 ALA A CA    1 
ATOM   12771 C  C     . ALA A 1 3142 ? 176.226 140.397 213.191 1.00 36.13  ? 3142 ALA A C     1 
ATOM   12772 O  O     . ALA A 1 3142 ? 176.370 140.557 211.974 1.00 35.86  ? 3142 ALA A O     1 
ATOM   12773 C  CB    . ALA A 1 3142 ? 178.092 139.345 214.501 1.00 39.83  ? 3142 ALA A CB    1 
ATOM   12774 N  N     . ILE A 1 3143 ? 175.068 140.001 213.725 1.00 34.84  ? 3143 ILE A N     1 
ATOM   12775 C  CA    . ILE A 1 3143 ? 173.895 139.775 212.883 1.00 30.99  ? 3143 ILE A CA    1 
ATOM   12776 C  C     . ILE A 1 3143 ? 173.461 141.070 212.207 1.00 32.91  ? 3143 ILE A C     1 
ATOM   12777 O  O     . ILE A 1 3143 ? 173.144 141.089 211.010 1.00 38.41  ? 3143 ILE A O     1 
ATOM   12778 C  CB    . ILE A 1 3143 ? 172.754 139.159 213.713 1.00 32.48  ? 3143 ILE A CB    1 
ATOM   12779 C  CG1   . ILE A 1 3143 ? 173.105 137.730 214.130 1.00 42.47  ? 3143 ILE A CG1   1 
ATOM   12780 C  CG2   . ILE A 1 3143 ? 171.449 139.187 212.934 1.00 32.38  ? 3143 ILE A CG2   1 
ATOM   12781 C  CD1   . ILE A 1 3143 ? 173.017 136.723 213.005 1.00 43.46  ? 3143 ILE A CD1   1 
ATOM   12782 N  N     . VAL A 1 3144 ? 173.437 142.172 212.960 1.00 31.32  ? 3144 VAL A N     1 
ATOM   12783 C  CA    . VAL A 1 3144 ? 173.029 143.450 212.378 1.00 25.71  ? 3144 VAL A CA    1 
ATOM   12784 C  C     . VAL A 1 3144 ? 174.032 143.907 211.322 1.00 28.60  ? 3144 VAL A C     1 
ATOM   12785 O  O     . VAL A 1 3144 ? 173.652 144.441 210.270 1.00 31.59  ? 3144 VAL A O     1 
ATOM   12786 C  CB    . VAL A 1 3144 ? 172.839 144.505 213.482 1.00 28.03  ? 3144 VAL A CB    1 
ATOM   12787 C  CG1   . VAL A 1 3144 ? 172.447 145.841 212.877 1.00 30.64  ? 3144 VAL A CG1   1 
ATOM   12788 C  CG2   . VAL A 1 3144 ? 171.784 144.044 214.474 1.00 26.39  ? 3144 VAL A CG2   1 
ATOM   12789 N  N     . ASN A 1 3145 ? 175.327 143.707 211.581 1.00 30.16  ? 3145 ASN A N     1 
ATOM   12790 C  CA    . ASN A 1 3145 ? 176.342 144.051 210.591 1.00 28.99  ? 3145 ASN A CA    1 
ATOM   12791 C  C     . ASN A 1 3145 ? 176.184 143.213 209.328 1.00 32.68  ? 3145 ASN A C     1 
ATOM   12792 O  O     . ASN A 1 3145 ? 176.362 143.714 208.211 1.00 36.36  ? 3145 ASN A O     1 
ATOM   12793 C  CB    . ASN A 1 3145 ? 177.735 143.868 211.191 1.00 31.63  ? 3145 ASN A CB    1 
ATOM   12794 C  CG    . ASN A 1 3145 ? 178.825 144.460 210.324 1.00 47.37  ? 3145 ASN A CG    1 
ATOM   12795 O  OD1   . ASN A 1 3145 ? 178.893 145.674 210.137 1.00 54.56  ? 3145 ASN A OD1   1 
ATOM   12796 N  ND2   . ASN A 1 3145 ? 179.686 143.604 209.788 1.00 49.14  ? 3145 ASN A ND2   1 
ATOM   12797 N  N     . SER A 1 3146 ? 175.852 141.930 209.487 1.00 33.25  ? 3146 SER A N     1 
ATOM   12798 C  CA    . SER A 1 3146 ? 175.597 141.081 208.329 1.00 29.27  ? 3146 SER A CA    1 
ATOM   12799 C  C     . SER A 1 3146 ? 174.378 141.562 207.554 1.00 29.31  ? 3146 SER A C     1 
ATOM   12800 O  O     . SER A 1 3146 ? 174.356 141.503 206.321 1.00 33.32  ? 3146 SER A O     1 
ATOM   12801 C  CB    . SER A 1 3146 ? 175.416 139.630 208.772 1.00 30.51  ? 3146 SER A CB    1 
ATOM   12802 O  OG    . SER A 1 3146 ? 176.611 139.121 209.338 1.00 34.17  ? 3146 SER A OG    1 
ATOM   12803 N  N     . CYS A 1 3147 ? 173.350 142.036 208.261 1.00 26.00  ? 3147 CYS A N     1 
ATOM   12804 C  CA    . CYS A 1 3147 ? 172.185 142.604 207.584 1.00 21.54  ? 3147 CYS A CA    1 
ATOM   12805 C  C     . CYS A 1 3147 ? 172.567 143.836 206.770 1.00 25.92  ? 3147 CYS A C     1 
ATOM   12806 O  O     . CYS A 1 3147 ? 172.113 144.011 205.630 1.00 32.98  ? 3147 CYS A O     1 
ATOM   12807 C  CB    . CYS A 1 3147 ? 171.105 142.952 208.608 1.00 19.93  ? 3147 CYS A CB    1 
ATOM   12808 S  SG    . CYS A 1 3147 ? 170.361 141.527 209.432 1.00 26.36  ? 3147 CYS A SG    1 
ATOM   12809 N  N     . VAL A 1 3148 ? 173.405 144.702 207.343 1.00 25.82  ? 3148 VAL A N     1 
ATOM   12810 C  CA    . VAL A 1 3148 ? 173.861 145.888 206.619 1.00 22.22  ? 3148 VAL A CA    1 
ATOM   12811 C  C     . VAL A 1 3148 ? 174.657 145.485 205.381 1.00 27.70  ? 3148 VAL A C     1 
ATOM   12812 O  O     . VAL A 1 3148 ? 174.489 146.062 204.297 1.00 32.64  ? 3148 VAL A O     1 
ATOM   12813 C  CB    . VAL A 1 3148 ? 174.681 146.801 207.548 1.00 18.48  ? 3148 VAL A CB    1 
ATOM   12814 C  CG1   . VAL A 1 3148 ? 175.232 147.983 206.774 1.00 22.22  ? 3148 VAL A CG1   1 
ATOM   12815 C  CG2   . VAL A 1 3148 ? 173.827 147.279 208.709 1.00 20.37  ? 3148 VAL A CG2   1 
ATOM   12816 N  N     . PHE A 1 3149 ? 175.537 144.489 205.523 1.00 25.85  ? 3149 PHE A N     1 
ATOM   12817 C  CA    . PHE A 1 3149 ? 176.296 144.013 204.370 1.00 25.78  ? 3149 PHE A CA    1 
ATOM   12818 C  C     . PHE A 1 3149 ? 175.374 143.432 203.309 1.00 26.94  ? 3149 PHE A C     1 
ATOM   12819 O  O     . PHE A 1 3149 ? 175.617 143.595 202.109 1.00 33.99  ? 3149 PHE A O     1 
ATOM   12820 C  CB    . PHE A 1 3149 ? 177.326 142.968 204.793 1.00 29.24  ? 3149 PHE A CB    1 
ATOM   12821 C  CG    . PHE A 1 3149 ? 178.036 142.324 203.634 1.00 31.99  ? 3149 PHE A CG    1 
ATOM   12822 C  CD1   . PHE A 1 3149 ? 179.151 142.922 203.072 1.00 32.77  ? 3149 PHE A CD1   1 
ATOM   12823 C  CD2   . PHE A 1 3149 ? 177.577 141.135 203.090 1.00 29.92  ? 3149 PHE A CD2   1 
ATOM   12824 C  CE1   . PHE A 1 3149 ? 179.803 142.340 202.003 1.00 29.85  ? 3149 PHE A CE1   1 
ATOM   12825 C  CE2   . PHE A 1 3149 ? 178.222 140.551 202.017 1.00 32.52  ? 3149 PHE A CE2   1 
ATOM   12826 C  CZ    . PHE A 1 3149 ? 179.338 141.153 201.475 1.00 34.00  ? 3149 PHE A CZ    1 
ATOM   12827 N  N     . VAL A 1 3150 ? 174.329 142.719 203.733 1.00 25.46  ? 3150 VAL A N     1 
ATOM   12828 C  CA    . VAL A 1 3150 ? 173.362 142.172 202.787 1.00 23.09  ? 3150 VAL A CA    1 
ATOM   12829 C  C     . VAL A 1 3150 ? 172.695 143.296 202.010 1.00 22.32  ? 3150 VAL A C     1 
ATOM   12830 O  O     . VAL A 1 3150 ? 172.496 143.199 200.793 1.00 25.32  ? 3150 VAL A O     1 
ATOM   12831 C  CB    . VAL A 1 3150 ? 172.331 141.297 203.526 1.00 20.02  ? 3150 VAL A CB    1 
ATOM   12832 C  CG1   . VAL A 1 3150 ? 171.071 141.140 202.697 1.00 18.79  ? 3150 VAL A CG1   1 
ATOM   12833 C  CG2   . VAL A 1 3150 ? 172.928 139.939 203.855 1.00 21.42  ? 3150 VAL A CG2   1 
ATOM   12834 N  N     . HIS A 1 3151 ? 172.344 144.384 202.699 1.00 21.78  ? 3151 HIS A N     1 
ATOM   12835 C  CA    . HIS A 1 3151 ? 171.753 145.525 202.005 1.00 20.88  ? 3151 HIS A CA    1 
ATOM   12836 C  C     . HIS A 1 3151 ? 172.726 146.133 200.998 1.00 24.59  ? 3151 HIS A C     1 
ATOM   12837 O  O     . HIS A 1 3151 ? 172.335 146.470 199.875 1.00 25.11  ? 3151 HIS A O     1 
ATOM   12838 C  CB    . HIS A 1 3151 ? 171.295 146.583 203.007 1.00 18.93  ? 3151 HIS A CB    1 
ATOM   12839 C  CG    . HIS A 1 3151 ? 170.506 147.693 202.385 1.00 21.25  ? 3151 HIS A CG    1 
ATOM   12840 N  ND1   . HIS A 1 3151 ? 169.168 147.573 202.075 1.00 19.93  ? 3151 HIS A ND1   1 
ATOM   12841 C  CD2   . HIS A 1 3151 ? 170.869 148.940 202.003 1.00 22.38  ? 3151 HIS A CD2   1 
ATOM   12842 C  CE1   . HIS A 1 3151 ? 168.740 148.700 201.536 1.00 16.59  ? 3151 HIS A CE1   1 
ATOM   12843 N  NE2   . HIS A 1 3151 ? 169.752 149.546 201.481 1.00 21.38  ? 3151 HIS A NE2   1 
ATOM   12844 N  N     . GLN A 1 3152 ? 173.998 146.283 201.380 1.00 26.67  ? 3152 GLN A N     1 
ATOM   12845 C  CA    . GLN A 1 3152 ? 174.968 146.899 200.471 1.00 28.54  ? 3152 GLN A CA    1 
ATOM   12846 C  C     . GLN A 1 3152 ? 175.317 145.986 199.297 1.00 33.35  ? 3152 GLN A C     1 
ATOM   12847 O  O     . GLN A 1 3152 ? 175.723 146.469 198.228 1.00 38.02  ? 3152 GLN A O     1 
ATOM   12848 C  CB    . GLN A 1 3152 ? 176.235 147.287 201.232 1.00 30.48  ? 3152 GLN A CB    1 
ATOM   12849 C  CG    . GLN A 1 3152 ? 175.984 148.135 202.465 1.00 32.13  ? 3152 GLN A CG    1 
ATOM   12850 C  CD    . GLN A 1 3152 ? 177.217 148.890 202.912 1.00 41.42  ? 3152 GLN A CD    1 
ATOM   12851 O  OE1   . GLN A 1 3152 ? 177.134 150.041 203.338 1.00 42.52  ? 3152 GLN A OE1   1 
ATOM   12852 N  NE2   . GLN A 1 3152 ? 178.374 148.246 202.810 1.00 47.02  ? 3152 GLN A NE2   1 
ATOM   12853 N  N     . THR A 1 3153 ? 175.186 144.671 199.484 1.00 31.88  ? 3153 THR A N     1 
ATOM   12854 C  CA    . THR A 1 3153 ? 175.445 143.734 198.398 1.00 28.22  ? 3153 THR A CA    1 
ATOM   12855 C  C     . THR A 1 3153 ? 174.519 143.986 197.218 1.00 29.34  ? 3153 THR A C     1 
ATOM   12856 O  O     . THR A 1 3153 ? 174.919 143.800 196.065 1.00 32.34  ? 3153 THR A O     1 
ATOM   12857 C  CB    . THR A 1 3153 ? 175.292 142.296 198.898 1.00 27.95  ? 3153 THR A CB    1 
ATOM   12858 O  OG1   . THR A 1 3153 ? 176.084 142.112 200.077 1.00 35.14  ? 3153 THR A OG1   1 
ATOM   12859 C  CG2   . THR A 1 3153 ? 175.746 141.306 197.837 1.00 30.56  ? 3153 THR A CG2   1 
ATOM   12860 N  N     . LEU A 1 3154 ? 173.287 144.423 197.483 1.00 28.67  ? 3154 LEU A N     1 
ATOM   12861 C  CA    . LEU A 1 3154 ? 172.361 144.710 196.394 1.00 24.41  ? 3154 LEU A CA    1 
ATOM   12862 C  C     . LEU A 1 3154 ? 172.789 145.946 195.614 1.00 29.06  ? 3154 LEU A C     1 
ATOM   12863 O  O     . LEU A 1 3154 ? 172.648 145.987 194.387 1.00 35.02  ? 3154 LEU A O     1 
ATOM   12864 C  CB    . LEU A 1 3154 ? 170.942 144.875 196.933 1.00 19.90  ? 3154 LEU A CB    1 
ATOM   12865 C  CG    . LEU A 1 3154 ? 170.141 143.582 197.101 1.00 18.28  ? 3154 LEU A CG    1 
ATOM   12866 C  CD1   . LEU A 1 3154 ? 169.938 142.917 195.754 1.00 21.58  ? 3154 LEU A CD1   1 
ATOM   12867 C  CD2   . LEU A 1 3154 ? 170.783 142.617 198.088 1.00 19.85  ? 3154 LEU A CD2   1 
ATOM   12868 N  N     . HIS A 1 3155 ? 173.311 146.964 196.302 1.00 30.28  ? 3155 HIS A N     1 
ATOM   12869 C  CA    . HIS A 1 3155 ? 173.863 148.115 195.595 1.00 32.11  ? 3155 HIS A CA    1 
ATOM   12870 C  C     . HIS A 1 3155 ? 175.042 147.704 194.725 1.00 36.33  ? 3155 HIS A C     1 
ATOM   12871 O  O     . HIS A 1 3155 ? 175.158 148.141 193.573 1.00 37.49  ? 3155 HIS A O     1 
ATOM   12872 C  CB    . HIS A 1 3155 ? 174.285 149.197 196.588 1.00 29.36  ? 3155 HIS A CB    1 
ATOM   12873 C  CG    . HIS A 1 3155 ? 173.140 149.962 197.173 1.00 29.77  ? 3155 HIS A CG    1 
ATOM   12874 N  ND1   . HIS A 1 3155 ? 172.894 150.015 198.527 1.00 33.45  ? 3155 HIS A ND1   1 
ATOM   12875 C  CD2   . HIS A 1 3155 ? 172.174 150.708 196.586 1.00 30.52  ? 3155 HIS A CD2   1 
ATOM   12876 C  CE1   . HIS A 1 3155 ? 171.826 150.760 198.750 1.00 36.73  ? 3155 HIS A CE1   1 
ATOM   12877 N  NE2   . HIS A 1 3155 ? 171.370 151.192 197.588 1.00 35.64  ? 3155 HIS A NE2   1 
ATOM   12878 N  N     . GLN A 1 3156 ? 175.924 146.855 195.259 1.00 38.64  ? 3156 GLN A N     1 
ATOM   12879 C  CA    . GLN A 1 3156 ? 177.055 146.382 194.464 1.00 39.60  ? 3156 GLN A CA    1 
ATOM   12880 C  C     . GLN A 1 3156 ? 176.584 145.592 193.245 1.00 41.70  ? 3156 GLN A C     1 
ATOM   12881 O  O     . GLN A 1 3156 ? 177.109 145.767 192.136 1.00 47.33  ? 3156 GLN A O     1 
ATOM   12882 C  CB    . GLN A 1 3156 ? 177.986 145.533 195.329 1.00 41.68  ? 3156 GLN A CB    1 
ATOM   12883 C  CG    . GLN A 1 3156 ? 178.955 146.344 196.170 1.00 47.33  ? 3156 GLN A CG    1 
ATOM   12884 C  CD    . GLN A 1 3156 ? 179.427 145.596 197.400 1.00 65.87  ? 3156 GLN A CD    1 
ATOM   12885 O  OE1   . GLN A 1 3156 ? 179.467 144.365 197.415 1.00 64.38  ? 3156 GLN A OE1   1 
ATOM   12886 N  NE2   . GLN A 1 3156 ? 179.789 146.337 198.441 1.00 64.96  ? 3156 GLN A NE2   1 
ATOM   12887 N  N     . ALA A 1 3157 ? 175.587 144.725 193.432 1.00 39.88  ? 3157 ALA A N     1 
ATOM   12888 C  CA    . ALA A 1 3157 ? 175.059 143.934 192.326 1.00 38.93  ? 3157 ALA A CA    1 
ATOM   12889 C  C     . ALA A 1 3157 ? 174.412 144.817 191.268 1.00 42.07  ? 3157 ALA A C     1 
ATOM   12890 O  O     . ALA A 1 3157 ? 174.595 144.590 190.068 1.00 53.37  ? 3157 ALA A O     1 
ATOM   12891 C  CB    . ALA A 1 3157 ? 174.057 142.907 192.850 1.00 34.99  ? 3157 ALA A CB    1 
ATOM   12892 N  N     . ASN A 1 3158 ? 173.640 145.820 191.691 1.00 39.11  ? 3158 ASN A N     1 
ATOM   12893 C  CA    . ASN A 1 3158 ? 173.018 146.725 190.731 1.00 41.84  ? 3158 ASN A CA    1 
ATOM   12894 C  C     . ASN A 1 3158 ? 174.065 147.527 189.973 1.00 49.39  ? 3158 ASN A C     1 
ATOM   12895 O  O     . ASN A 1 3158 ? 173.914 147.771 188.771 1.00 52.53  ? 3158 ASN A O     1 
ATOM   12896 C  CB    . ASN A 1 3158 ? 172.033 147.651 191.442 1.00 39.12  ? 3158 ASN A CB    1 
ATOM   12897 C  CG    . ASN A 1 3158 ? 170.649 147.047 191.555 1.00 42.01  ? 3158 ASN A CG    1 
ATOM   12898 O  OD1   . ASN A 1 3158 ? 169.849 147.121 190.623 1.00 50.65  ? 3158 ASN A OD1   1 
ATOM   12899 N  ND2   . ASN A 1 3158 ? 170.364 146.433 192.695 1.00 38.60  ? 3158 ASN A ND2   1 
ATOM   12900 N  N     . ALA A 1 3159 ? 175.136 147.942 190.654 1.00 51.75  ? 3159 ALA A N     1 
ATOM   12901 C  CA    . ALA A 1 3159 ? 176.227 148.619 189.959 1.00 51.28  ? 3159 ALA A CA    1 
ATOM   12902 C  C     . ALA A 1 3159 ? 176.862 147.707 188.917 1.00 52.34  ? 3159 ALA A C     1 
ATOM   12903 O  O     . ALA A 1 3159 ? 177.165 148.143 187.800 1.00 56.45  ? 3159 ALA A O     1 
ATOM   12904 C  CB    . ALA A 1 3159 ? 177.274 149.100 190.963 1.00 45.47  ? 3159 ALA A CB    1 
ATOM   12905 N  N     . ARG A 1 3160 ? 177.073 146.436 189.265 1.00 52.66  ? 3160 ARG A N     1 
ATOM   12906 C  CA    . ARG A 1 3160 ? 177.661 145.501 188.308 1.00 57.91  ? 3160 ARG A CA    1 
ATOM   12907 C  C     . ARG A 1 3160 ? 176.741 145.266 187.111 1.00 58.93  ? 3160 ARG A C     1 
ATOM   12908 O  O     . ARG A 1 3160 ? 177.205 145.212 185.965 1.00 66.85  ? 3160 ARG A O     1 
ATOM   12909 C  CB    . ARG A 1 3160 ? 178.017 144.189 189.011 1.00 63.33  ? 3160 ARG A CB    1 
ATOM   12910 C  CG    . ARG A 1 3160 ? 178.264 143.014 188.082 1.00 73.17  ? 3160 ARG A CG    1 
ATOM   12911 C  CD    . ARG A 1 3160 ? 178.844 141.827 188.837 1.00 73.45  ? 3160 ARG A CD    1 
ATOM   12912 N  NE    . ARG A 1 3160 ? 178.095 141.481 190.039 1.00 75.88  ? 3160 ARG A NE    1 
ATOM   12913 C  CZ    . ARG A 1 3160 ? 178.305 140.385 190.756 1.00 80.46  ? 3160 ARG A CZ    1 
ATOM   12914 N  NH1   . ARG A 1 3160 ? 179.201 139.483 190.393 1.00 77.00  ? 3160 ARG A NH1   1 
ATOM   12915 N  NH2   . ARG A 1 3160 ? 177.605 140.194 191.870 1.00 70.40  ? 3160 ARG A NH2   1 
ATOM   12916 N  N     . LEU A 1 3161 ? 175.434 145.129 187.352 1.00 57.97  ? 3161 LEU A N     1 
ATOM   12917 C  CA    . LEU A 1 3161 ? 174.494 144.981 186.240 1.00 56.57  ? 3161 LEU A CA    1 
ATOM   12918 C  C     . LEU A 1 3161 ? 174.472 146.221 185.356 1.00 62.65  ? 3161 LEU A C     1 
ATOM   12919 O  O     . LEU A 1 3161 ? 174.417 146.112 184.126 1.00 67.41  ? 3161 LEU A O     1 
ATOM   12920 C  CB    . LEU A 1 3161 ? 173.087 144.675 186.752 1.00 55.27  ? 3161 LEU A CB    1 
ATOM   12921 C  CG    . LEU A 1 3161 ? 172.676 143.212 186.915 1.00 52.86  ? 3161 LEU A CG    1 
ATOM   12922 C  CD1   . LEU A 1 3161 ? 173.351 142.586 188.106 1.00 53.04  ? 3161 LEU A CD1   1 
ATOM   12923 C  CD2   . LEU A 1 3161 ? 171.163 143.102 187.033 1.00 50.87  ? 3161 LEU A CD2   1 
ATOM   12924 N  N     . ALA A 1 3162 ? 174.500 147.410 185.962 1.00 64.40  ? 3162 ALA A N     1 
ATOM   12925 C  CA    . ALA A 1 3162 ? 174.533 148.639 185.176 1.00 68.38  ? 3162 ALA A CA    1 
ATOM   12926 C  C     . ALA A 1 3162 ? 175.804 148.722 184.341 1.00 73.00  ? 3162 ALA A C     1 
ATOM   12927 O  O     . ALA A 1 3162 ? 175.772 149.181 183.193 1.00 71.02  ? 3162 ALA A O     1 
ATOM   12928 C  CB    . ALA A 1 3162 ? 174.409 149.855 186.093 1.00 61.08  ? 3162 ALA A CB    1 
ATOM   12929 N  N     . LYS A 1 3163 ? 176.935 148.290 184.906 1.00 76.42  ? 3163 LYS A N     1 
ATOM   12930 C  CA    . LYS A 1 3163 ? 178.176 148.250 184.139 1.00 74.30  ? 3163 LYS A CA    1 
ATOM   12931 C  C     . LYS A 1 3163 ? 178.067 147.283 182.967 1.00 74.08  ? 3163 LYS A C     1 
ATOM   12932 O  O     . LYS A 1 3163 ? 178.517 147.588 181.856 1.00 76.47  ? 3163 LYS A O     1 
ATOM   12933 C  CB    . LYS A 1 3163 ? 179.343 147.863 185.047 1.00 75.10  ? 3163 LYS A CB    1 
ATOM   12934 C  CG    . LYS A 1 3163 ? 180.696 147.892 184.355 1.00 82.71  ? 3163 LYS A CG    1 
ATOM   12935 C  CD    . LYS A 1 3163 ? 181.538 146.686 184.738 1.00 89.21  ? 3163 LYS A CD    1 
ATOM   12936 C  CE    . LYS A 1 3163 ? 182.792 146.597 183.883 1.00 89.89  ? 3163 LYS A CE    1 
ATOM   12937 N  NZ    . LYS A 1 3163 ? 182.471 146.306 182.457 1.00 83.48  ? 3163 LYS A NZ    1 
ATOM   12938 N  N     . ARG A 1 3164 ? 177.472 146.109 183.193 1.00 72.54  ? 3164 ARG A N     1 
ATOM   12939 C  CA    . ARG A 1 3164 ? 177.287 145.156 182.104 1.00 71.87  ? 3164 ARG A CA    1 
ATOM   12940 C  C     . ARG A 1 3164 ? 176.267 145.633 181.078 1.00 73.03  ? 3164 ARG A C     1 
ATOM   12941 O  O     . ARG A 1 3164 ? 176.323 145.203 179.922 1.00 75.22  ? 3164 ARG A O     1 
ATOM   12942 C  CB    . ARG A 1 3164 ? 176.865 143.793 182.652 1.00 69.41  ? 3164 ARG A CB    1 
ATOM   12943 C  CG    . ARG A 1 3164 ? 177.200 142.637 181.722 1.00 72.12  ? 3164 ARG A CG    1 
ATOM   12944 C  CD    . ARG A 1 3164 ? 176.541 141.318 182.144 1.00 83.28  ? 3164 ARG A CD    1 
ATOM   12945 N  NE    . ARG A 1 3164 ? 176.511 141.045 183.581 1.00 94.70  ? 3164 ARG A NE    1 
ATOM   12946 C  CZ    . ARG A 1 3164 ? 177.547 141.105 184.412 1.00 90.87  ? 3164 ARG A CZ    1 
ATOM   12947 N  NH1   . ARG A 1 3164 ? 178.771 141.370 183.985 1.00 92.12  ? 3164 ARG A NH1   1 
ATOM   12948 N  NH2   . ARG A 1 3164 ? 177.353 140.864 185.705 1.00 79.76  ? 3164 ARG A NH2   1 
ATOM   12949 N  N     . GLY A 1 3165 ? 175.342 146.506 181.468 1.00 72.92  ? 3165 GLY A N     1 
ATOM   12950 C  CA    . GLY A 1 3165 ? 174.322 147.000 180.569 1.00 73.12  ? 3165 GLY A CA    1 
ATOM   12951 C  C     . GLY A 1 3165 ? 172.940 146.412 180.762 1.00 75.45  ? 3165 GLY A C     1 
ATOM   12952 O  O     . GLY A 1 3165 ? 172.050 146.695 179.951 1.00 66.34  ? 3165 GLY A O     1 
ATOM   12953 N  N     . GLY A 1 3166 ? 172.728 145.609 181.803 1.00 81.18  ? 3166 GLY A N     1 
ATOM   12954 C  CA    . GLY A 1 3166 ? 171.427 145.039 182.068 1.00 74.13  ? 3166 GLY A CA    1 
ATOM   12955 C  C     . GLY A 1 3166 ? 170.471 146.050 182.670 1.00 68.68  ? 3166 GLY A C     1 
ATOM   12956 O  O     . GLY A 1 3166 ? 170.799 147.213 182.901 1.00 65.79  ? 3166 GLY A O     1 
ATOM   12957 N  N     . ARG A 1 3167 ? 169.252 145.585 182.928 1.00 67.36  ? 3167 ARG A N     1 
ATOM   12958 C  CA    . ARG A 1 3167 ? 168.200 146.444 183.450 1.00 62.26  ? 3167 ARG A CA    1 
ATOM   12959 C  C     . ARG A 1 3167 ? 168.199 146.347 184.971 1.00 57.50  ? 3167 ARG A C     1 
ATOM   12960 O  O     . ARG A 1 3167 ? 168.179 145.245 185.527 1.00 58.67  ? 3167 ARG A O     1 
ATOM   12961 C  CB    . ARG A 1 3167 ? 166.839 146.035 182.888 1.00 62.47  ? 3167 ARG A CB    1 
ATOM   12962 C  CG    . ARG A 1 3167 ? 165.761 147.078 183.079 1.00 63.21  ? 3167 ARG A CG    1 
ATOM   12963 C  CD    . ARG A 1 3167 ? 166.058 148.240 182.144 1.00 74.61  ? 3167 ARG A CD    1 
ATOM   12964 N  NE    . ARG A 1 3167 ? 165.610 147.948 180.787 1.00 77.41  ? 3167 ARG A NE    1 
ATOM   12965 C  CZ    . ARG A 1 3167 ? 165.401 148.857 179.845 1.00 75.88  ? 3167 ARG A CZ    1 
ATOM   12966 N  NH1   . ARG A 1 3167 ? 165.667 150.136 180.047 1.00 74.46  ? 3167 ARG A NH1   1 
ATOM   12967 N  NH2   . ARG A 1 3167 ? 164.930 148.471 178.664 1.00 74.89  ? 3167 ARG A NH2   1 
ATOM   12968 N  N     . THR A 1 3168 ? 168.223 147.497 185.640 1.00 55.64  ? 3168 THR A N     1 
ATOM   12969 C  CA    . THR A 1 3168 ? 168.371 147.549 187.086 1.00 52.74  ? 3168 THR A CA    1 
ATOM   12970 C  C     . THR A 1 3168 ? 167.171 148.232 187.727 1.00 51.97  ? 3168 THR A C     1 
ATOM   12971 O  O     . THR A 1 3168 ? 166.540 149.110 187.131 1.00 54.93  ? 3168 THR A O     1 
ATOM   12972 C  CB    . THR A 1 3168 ? 169.650 148.291 187.491 1.00 57.97  ? 3168 THR A CB    1 
ATOM   12973 O  OG1   . THR A 1 3168 ? 169.734 149.529 186.774 1.00 73.50  ? 3168 THR A OG1   1 
ATOM   12974 C  CG2   . THR A 1 3168 ? 170.874 147.450 187.181 1.00 57.62  ? 3168 THR A CG2   1 
ATOM   12975 N  N     . MET A 1 3169 ? 166.866 147.813 188.952 1.00 49.66  ? 3169 MET A N     1 
ATOM   12976 C  CA    . MET A 1 3169 ? 165.839 148.431 189.775 1.00 45.51  ? 3169 MET A CA    1 
ATOM   12977 C  C     . MET A 1 3169 ? 166.488 149.077 190.991 1.00 44.17  ? 3169 MET A C     1 
ATOM   12978 O  O     . MET A 1 3169 ? 167.433 148.528 191.566 1.00 47.14  ? 3169 MET A O     1 
ATOM   12979 C  CB    . MET A 1 3169 ? 164.792 147.405 190.216 1.00 35.62  ? 3169 MET A CB    1 
ATOM   12980 C  CG    . MET A 1 3169 ? 163.917 146.892 189.085 1.00 37.65  ? 3169 MET A CG    1 
ATOM   12981 S  SD    . MET A 1 3169 ? 163.341 148.219 188.011 1.00 45.89  ? 3169 MET A SD    1 
ATOM   12982 C  CE    . MET A 1 3169 ? 162.971 147.313 186.512 1.00 42.85  ? 3169 MET A CE    1 
ATOM   12983 N  N     . ALA A 1 3170 ? 165.982 150.246 191.373 1.00 41.18  ? 3170 ALA A N     1 
ATOM   12984 C  CA    . ALA A 1 3170 ? 166.576 150.996 192.471 1.00 35.44  ? 3170 ALA A CA    1 
ATOM   12985 C  C     . ALA A 1 3170 ? 166.404 150.257 193.793 1.00 30.72  ? 3170 ALA A C     1 
ATOM   12986 O  O     . ALA A 1 3170 ? 165.361 149.653 194.057 1.00 31.84  ? 3170 ALA A O     1 
ATOM   12987 C  CB    . ALA A 1 3170 ? 165.948 152.385 192.564 1.00 41.27  ? 3170 ALA A CB    1 
ATOM   12988 N  N     . ILE A 1 3171 ? 167.441 150.308 194.624 1.00 29.60  ? 3171 ILE A N     1 
ATOM   12989 C  CA    . ILE A 1 3171 ? 167.415 149.726 195.960 1.00 24.98  ? 3171 ILE A CA    1 
ATOM   12990 C  C     . ILE A 1 3171 ? 167.129 150.844 196.951 1.00 25.18  ? 3171 ILE A C     1 
ATOM   12991 O  O     . ILE A 1 3171 ? 167.880 151.823 197.033 1.00 31.51  ? 3171 ILE A O     1 
ATOM   12992 C  CB    . ILE A 1 3171 ? 168.735 149.013 196.293 1.00 23.26  ? 3171 ILE A CB    1 
ATOM   12993 C  CG1   . ILE A 1 3171 ? 169.019 147.915 195.269 1.00 24.09  ? 3171 ILE A CG1   1 
ATOM   12994 C  CG2   . ILE A 1 3171 ? 168.687 148.433 197.697 1.00 20.86  ? 3171 ILE A CG2   1 
ATOM   12995 C  CD1   . ILE A 1 3171 ? 168.023 146.779 195.299 1.00 22.44  ? 3171 ILE A CD1   1 
ATOM   12996 N  N     . THR A 1 3172 ? 166.048 150.698 197.702 1.00 20.94  ? 3172 THR A N     1 
ATOM   12997 C  CA    . THR A 1 3172 ? 165.566 151.701 198.633 1.00 18.80  ? 3172 THR A CA    1 
ATOM   12998 C  C     . THR A 1 3172 ? 165.625 151.181 200.063 1.00 19.33  ? 3172 THR A C     1 
ATOM   12999 O  O     . THR A 1 3172 ? 165.720 149.971 200.290 1.00 21.50  ? 3172 THR A O     1 
ATOM   13000 C  CB    . THR A 1 3172 ? 164.124 152.099 198.288 1.00 19.38  ? 3172 THR A CB    1 
ATOM   13001 O  OG1   . THR A 1 3172 ? 163.228 151.054 198.685 1.00 20.74  ? 3172 THR A OG1   1 
ATOM   13002 C  CG2   . THR A 1 3172 ? 163.981 152.345 196.795 1.00 22.69  ? 3172 THR A CG2   1 
ATOM   13003 N  N     . PRO A 1 3173 ? 165.589 152.071 201.059 1.00 17.59  ? 3173 PRO A N     1 
ATOM   13004 C  CA    . PRO A 1 3173 ? 165.528 151.601 202.452 1.00 15.44  ? 3173 PRO A CA    1 
ATOM   13005 C  C     . PRO A 1 3173 ? 164.298 150.765 202.755 1.00 18.07  ? 3173 PRO A C     1 
ATOM   13006 O  O     . PRO A 1 3173 ? 164.305 150.014 203.739 1.00 23.51  ? 3173 PRO A O     1 
ATOM   13007 C  CB    . PRO A 1 3173 ? 165.535 152.905 203.259 1.00 14.85  ? 3173 PRO A CB    1 
ATOM   13008 C  CG    . PRO A 1 3173 ? 166.239 153.876 202.378 1.00 16.54  ? 3173 PRO A CG    1 
ATOM   13009 C  CD    . PRO A 1 3173 ? 165.813 153.526 200.983 1.00 17.03  ? 3173 PRO A CD    1 
ATOM   13010 N  N     . ARG A 1 3174 ? 163.241 150.873 201.947 1.00 16.00  ? 3174 ARG A N     1 
ATOM   13011 C  CA    . ARG A 1 3174 ? 162.094 149.988 202.112 1.00 16.52  ? 3174 ARG A CA    1 
ATOM   13012 C  C     . ARG A 1 3174 ? 162.479 148.534 201.874 1.00 18.03  ? 3174 ARG A C     1 
ATOM   13013 O  O     . ARG A 1 3174 ? 161.908 147.631 202.497 1.00 20.96  ? 3174 ARG A O     1 
ATOM   13014 C  CB    . ARG A 1 3174 ? 160.967 150.410 201.170 1.00 15.69  ? 3174 ARG A CB    1 
ATOM   13015 C  CG    . ARG A 1 3174 ? 160.379 151.776 201.490 1.00 18.09  ? 3174 ARG A CG    1 
ATOM   13016 C  CD    . ARG A 1 3174 ? 159.023 151.970 200.833 1.00 19.81  ? 3174 ARG A CD    1 
ATOM   13017 N  NE    . ARG A 1 3174 ? 157.992 151.152 201.458 1.00 18.40  ? 3174 ARG A NE    1 
ATOM   13018 C  CZ    . ARG A 1 3174 ? 156.707 151.191 201.135 1.00 22.60  ? 3174 ARG A CZ    1 
ATOM   13019 N  NH1   . ARG A 1 3174 ? 156.255 152.001 200.192 1.00 23.12  ? 3174 ARG A NH1   1 
ATOM   13020 N  NH2   . ARG A 1 3174 ? 155.853 150.396 201.773 1.00 23.51  ? 3174 ARG A NH2   1 
ATOM   13021 N  N     . HIS A 1 3175 ? 163.450 148.288 200.990 1.00 15.11  ? 3175 HIS A N     1 
ATOM   13022 C  CA    . HIS A 1 3175 ? 163.977 146.937 200.829 1.00 13.34  ? 3175 HIS A CA    1 
ATOM   13023 C  C     . HIS A 1 3175 ? 164.599 146.436 202.125 1.00 17.32  ? 3175 HIS A C     1 
ATOM   13024 O  O     . HIS A 1 3175 ? 164.380 145.287 202.524 1.00 21.85  ? 3175 HIS A O     1 
ATOM   13025 C  CB    . HIS A 1 3175 ? 165.008 146.904 199.700 1.00 13.23  ? 3175 HIS A CB    1 
ATOM   13026 C  CG    . HIS A 1 3175 ? 164.417 147.030 198.332 1.00 16.65  ? 3175 HIS A CG    1 
ATOM   13027 N  ND1   . HIS A 1 3175 ? 163.672 148.120 197.939 1.00 20.46  ? 3175 HIS A ND1   1 
ATOM   13028 C  CD2   . HIS A 1 3175 ? 164.467 146.203 197.261 1.00 18.22  ? 3175 HIS A CD2   1 
ATOM   13029 C  CE1   . HIS A 1 3175 ? 163.285 147.958 196.686 1.00 19.03  ? 3175 HIS A CE1   1 
ATOM   13030 N  NE2   . HIS A 1 3175 ? 163.754 146.803 196.252 1.00 22.67  ? 3175 HIS A NE2   1 
ATOM   13031 N  N     . TYR A 1 3176 ? 165.373 147.288 202.800 1.00 15.24  ? 3176 TYR A N     1 
ATOM   13032 C  CA    . TYR A 1 3176 ? 165.962 146.909 204.081 1.00 13.49  ? 3176 TYR A CA    1 
ATOM   13033 C  C     . TYR A 1 3176 ? 164.887 146.660 205.131 1.00 17.64  ? 3176 TYR A C     1 
ATOM   13034 O  O     . TYR A 1 3176 ? 164.987 145.715 205.925 1.00 25.97  ? 3176 TYR A O     1 
ATOM   13035 C  CB    . TYR A 1 3176 ? 166.927 147.997 204.550 1.00 13.75  ? 3176 TYR A CB    1 
ATOM   13036 C  CG    . TYR A 1 3176 ? 167.723 147.632 205.780 1.00 14.62  ? 3176 TYR A CG    1 
ATOM   13037 C  CD1   . TYR A 1 3176 ? 168.760 146.712 205.711 1.00 15.97  ? 3176 TYR A CD1   1 
ATOM   13038 C  CD2   . TYR A 1 3176 ? 167.439 148.207 207.010 1.00 15.09  ? 3176 TYR A CD2   1 
ATOM   13039 C  CE1   . TYR A 1 3176 ? 169.491 146.376 206.832 1.00 17.37  ? 3176 TYR A CE1   1 
ATOM   13040 C  CE2   . TYR A 1 3176 ? 168.163 147.876 208.136 1.00 19.67  ? 3176 TYR A CE2   1 
ATOM   13041 C  CZ    . TYR A 1 3176 ? 169.189 146.961 208.042 1.00 20.34  ? 3176 TYR A CZ    1 
ATOM   13042 O  OH    . TYR A 1 3176 ? 169.914 146.628 209.162 1.00 26.84  ? 3176 TYR A OH    1 
ATOM   13043 N  N     . LEU A 1 3177 ? 163.856 147.506 205.156 1.00 15.00  ? 3177 LEU A N     1 
ATOM   13044 C  CA    . LEU A 1 3177 ? 162.772 147.321 206.115 1.00 15.38  ? 3177 LEU A CA    1 
ATOM   13045 C  C     . LEU A 1 3177 ? 162.059 145.995 205.886 1.00 20.02  ? 3177 LEU A C     1 
ATOM   13046 O  O     . LEU A 1 3177 ? 161.752 145.272 206.841 1.00 25.48  ? 3177 LEU A O     1 
ATOM   13047 C  CB    . LEU A 1 3177 ? 161.787 148.485 206.022 1.00 18.61  ? 3177 LEU A CB    1 
ATOM   13048 C  CG    . LEU A 1 3177 ? 162.345 149.868 206.361 1.00 16.27  ? 3177 LEU A CG    1 
ATOM   13049 C  CD1   . LEU A 1 3177 ? 161.314 150.943 206.071 1.00 17.87  ? 3177 LEU A CD1   1 
ATOM   13050 C  CD2   . LEU A 1 3177 ? 162.789 149.927 207.810 1.00 17.97  ? 3177 LEU A CD2   1 
ATOM   13051 N  N     . ASP A 1 3178 ? 161.792 145.658 204.622 1.00 19.63  ? 3178 ASP A N     1 
ATOM   13052 C  CA    . ASP A 1 3178 ? 161.167 144.376 204.311 1.00 20.74  ? 3178 ASP A CA    1 
ATOM   13053 C  C     . ASP A 1 3178 ? 162.078 143.215 204.676 1.00 20.90  ? 3178 ASP A C     1 
ATOM   13054 O  O     . ASP A 1 3178 ? 161.610 142.177 205.154 1.00 24.25  ? 3178 ASP A O     1 
ATOM   13055 C  CB    . ASP A 1 3178 ? 160.804 144.310 202.831 1.00 24.65  ? 3178 ASP A CB    1 
ATOM   13056 C  CG    . ASP A 1 3178 ? 159.687 145.254 202.467 1.00 44.36  ? 3178 ASP A CG    1 
ATOM   13057 O  OD1   . ASP A 1 3178 ? 158.840 145.539 203.339 1.00 50.13  ? 3178 ASP A OD1   1 
ATOM   13058 O  OD2   . ASP A 1 3178 ? 159.661 145.706 201.306 1.00 45.84  ? 3178 ASP A OD2   1 
ATOM   13059 N  N     . PHE A 1 3179 ? 163.382 143.366 204.439 1.00 19.02  ? 3179 PHE A N     1 
ATOM   13060 C  CA    . PHE A 1 3179 ? 164.325 142.318 204.806 1.00 17.52  ? 3179 PHE A CA    1 
ATOM   13061 C  C     . PHE A 1 3179 ? 164.284 142.053 206.303 1.00 20.00  ? 3179 PHE A C     1 
ATOM   13062 O  O     . PHE A 1 3179 ? 164.221 140.897 206.735 1.00 26.21  ? 3179 PHE A O     1 
ATOM   13063 C  CB    . PHE A 1 3179 ? 165.733 142.715 204.356 1.00 13.79  ? 3179 PHE A CB    1 
ATOM   13064 C  CG    . PHE A 1 3179 ? 166.836 141.919 204.998 1.00 15.97  ? 3179 PHE A CG    1 
ATOM   13065 C  CD1   . PHE A 1 3179 ? 166.778 140.537 205.056 1.00 20.09  ? 3179 PHE A CD1   1 
ATOM   13066 C  CD2   . PHE A 1 3179 ? 167.944 142.557 205.527 1.00 16.90  ? 3179 PHE A CD2   1 
ATOM   13067 C  CE1   . PHE A 1 3179 ? 167.794 139.810 205.642 1.00 21.28  ? 3179 PHE A CE1   1 
ATOM   13068 C  CE2   . PHE A 1 3179 ? 168.964 141.834 206.110 1.00 18.85  ? 3179 PHE A CE2   1 
ATOM   13069 C  CZ    . PHE A 1 3179 ? 168.889 140.459 206.168 1.00 20.39  ? 3179 PHE A CZ    1 
ATOM   13070 N  N     . ILE A 1 3180 ? 164.286 143.112 207.112 1.00 19.27  ? 3180 ILE A N     1 
ATOM   13071 C  CA    . ILE A 1 3180 ? 164.293 142.912 208.557 1.00 19.68  ? 3180 ILE A CA    1 
ATOM   13072 C  C     . ILE A 1 3180 ? 162.946 142.377 209.038 1.00 22.21  ? 3180 ILE A C     1 
ATOM   13073 O  O     . ILE A 1 3180 ? 162.886 141.549 209.957 1.00 26.38  ? 3180 ILE A O     1 
ATOM   13074 C  CB    . ILE A 1 3180 ? 164.687 144.208 209.283 1.00 20.89  ? 3180 ILE A CB    1 
ATOM   13075 C  CG1   . ILE A 1 3180 ? 166.007 144.743 208.732 1.00 19.58  ? 3180 ILE A CG1   1 
ATOM   13076 C  CG2   . ILE A 1 3180 ? 164.878 143.921 210.747 1.00 31.62  ? 3180 ILE A CG2   1 
ATOM   13077 C  CD1   . ILE A 1 3180 ? 167.213 143.913 209.111 1.00 19.77  ? 3180 ILE A CD1   1 
ATOM   13078 N  N     . ASN A 1 3181 ? 161.844 142.844 208.441 1.00 22.85  ? 3181 ASN A N     1 
ATOM   13079 C  CA    . ASN A 1 3181 ? 160.531 142.311 208.799 1.00 23.73  ? 3181 ASN A CA    1 
ATOM   13080 C  C     . ASN A 1 3181 ? 160.437 140.822 208.488 1.00 29.16  ? 3181 ASN A C     1 
ATOM   13081 O  O     . ASN A 1 3181 ? 159.937 140.036 209.305 1.00 35.28  ? 3181 ASN A O     1 
ATOM   13082 C  CB    . ASN A 1 3181 ? 159.432 143.077 208.062 1.00 28.61  ? 3181 ASN A CB    1 
ATOM   13083 C  CG    . ASN A 1 3181 ? 159.266 144.494 208.571 1.00 42.73  ? 3181 ASN A CG    1 
ATOM   13084 O  OD1   . ASN A 1 3181 ? 159.301 144.741 209.775 1.00 53.42  ? 3181 ASN A OD1   1 
ATOM   13085 N  ND2   . ASN A 1 3181 ? 159.079 145.434 207.652 1.00 46.48  ? 3181 ASN A ND2   1 
ATOM   13086 N  N     . HIS A 1 3182 ? 160.912 140.419 207.307 1.00 24.30  ? 3182 HIS A N     1 
ATOM   13087 C  CA    . HIS A 1 3182 ? 160.934 139.006 206.951 1.00 21.28  ? 3182 HIS A CA    1 
ATOM   13088 C  C     . HIS A 1 3182 ? 161.834 138.225 207.894 1.00 24.58  ? 3182 HIS A C     1 
ATOM   13089 O  O     . HIS A 1 3182 ? 161.518 137.090 208.264 1.00 30.20  ? 3182 HIS A O     1 
ATOM   13090 C  CB    . HIS A 1 3182 ? 161.399 138.837 205.505 1.00 20.47  ? 3182 HIS A CB    1 
ATOM   13091 C  CG    . HIS A 1 3182 ? 160.353 139.173 204.489 1.00 21.97  ? 3182 HIS A CG    1 
ATOM   13092 N  ND1   . HIS A 1 3182 ? 160.628 139.902 203.353 1.00 21.16  ? 3182 HIS A ND1   1 
ATOM   13093 C  CD2   . HIS A 1 3182 ? 159.033 138.878 204.437 1.00 25.01  ? 3182 HIS A CD2   1 
ATOM   13094 C  CE1   . HIS A 1 3182 ? 159.522 140.043 202.644 1.00 23.73  ? 3182 HIS A CE1   1 
ATOM   13095 N  NE2   . HIS A 1 3182 ? 158.540 139.431 203.280 1.00 27.54  ? 3182 HIS A NE2   1 
ATOM   13096 N  N     . TYR A 1 3183 ? 162.962 138.816 208.292 1.00 22.96  ? 3183 TYR A N     1 
ATOM   13097 C  CA    . TYR A 1 3183 ? 163.856 138.156 209.237 1.00 20.95  ? 3183 TYR A CA    1 
ATOM   13098 C  C     . TYR A 1 3183 ? 163.148 137.888 210.557 1.00 23.34  ? 3183 TYR A C     1 
ATOM   13099 O  O     . TYR A 1 3183 ? 163.212 136.777 211.094 1.00 28.60  ? 3183 TYR A O     1 
ATOM   13100 C  CB    . TYR A 1 3183 ? 165.103 139.016 209.451 1.00 17.40  ? 3183 TYR A CB    1 
ATOM   13101 C  CG    . TYR A 1 3183 ? 166.202 138.352 210.248 1.00 22.43  ? 3183 TYR A CG    1 
ATOM   13102 C  CD1   . TYR A 1 3183 ? 166.294 136.970 210.331 1.00 26.39  ? 3183 TYR A CD1   1 
ATOM   13103 C  CD2   . TYR A 1 3183 ? 167.151 139.111 210.917 1.00 28.74  ? 3183 TYR A CD2   1 
ATOM   13104 C  CE1   . TYR A 1 3183 ? 167.298 136.364 211.059 1.00 31.34  ? 3183 TYR A CE1   1 
ATOM   13105 C  CE2   . TYR A 1 3183 ? 168.158 138.514 211.647 1.00 33.08  ? 3183 TYR A CE2   1 
ATOM   13106 C  CZ    . TYR A 1 3183 ? 168.228 137.141 211.715 1.00 33.70  ? 3183 TYR A CZ    1 
ATOM   13107 O  OH    . TYR A 1 3183 ? 169.230 136.543 212.441 1.00 37.86  ? 3183 TYR A OH    1 
ATOM   13108 N  N     . ALA A 1 3184 ? 162.448 138.893 211.085 1.00 20.75  ? 3184 ALA A N     1 
ATOM   13109 C  CA    . ALA A 1 3184 ? 161.741 138.720 212.351 1.00 22.47  ? 3184 ALA A CA    1 
ATOM   13110 C  C     . ALA A 1 3184 ? 160.644 137.669 212.232 1.00 29.64  ? 3184 ALA A C     1 
ATOM   13111 O  O     . ALA A 1 3184 ? 160.520 136.778 213.086 1.00 38.43  ? 3184 ALA A O     1 
ATOM   13112 C  CB    . ALA A 1 3184 ? 161.163 140.057 212.814 1.00 20.42  ? 3184 ALA A CB    1 
ATOM   13113 N  N     . ASN A 1 3185 ? 159.838 137.754 211.169 1.00 27.21  ? 3185 ASN A N     1 
ATOM   13114 C  CA    . ASN A 1 3185 ? 158.739 136.809 210.997 1.00 26.68  ? 3185 ASN A CA    1 
ATOM   13115 C  C     . ASN A 1 3185 ? 159.257 135.384 210.849 1.00 35.84  ? 3185 ASN A C     1 
ATOM   13116 O  O     . ASN A 1 3185 ? 158.738 134.453 211.476 1.00 41.95  ? 3185 ASN A O     1 
ATOM   13117 C  CB    . ASN A 1 3185 ? 157.893 137.203 209.786 1.00 28.61  ? 3185 ASN A CB    1 
ATOM   13118 C  CG    . ASN A 1 3185 ? 157.271 138.575 209.932 1.00 37.52  ? 3185 ASN A CG    1 
ATOM   13119 O  OD1   . ASN A 1 3185 ? 157.297 139.170 211.008 1.00 45.40  ? 3185 ASN A OD1   1 
ATOM   13120 N  ND2   . ASN A 1 3185 ? 156.707 139.087 208.844 1.00 36.98  ? 3185 ASN A ND2   1 
ATOM   13121 N  N     . LEU A 1 3186 ? 160.290 135.197 210.023 1.00 31.19  ? 3186 LEU A N     1 
ATOM   13122 C  CA    . LEU A 1 3186 ? 160.847 133.868 209.811 1.00 31.65  ? 3186 LEU A CA    1 
ATOM   13123 C  C     . LEU A 1 3186 ? 161.481 133.325 211.082 1.00 39.71  ? 3186 LEU A C     1 
ATOM   13124 O  O     . LEU A 1 3186 ? 161.318 132.145 211.405 1.00 50.70  ? 3186 LEU A O     1 
ATOM   13125 C  CB    . LEU A 1 3186 ? 161.865 133.907 208.673 1.00 26.24  ? 3186 LEU A CB    1 
ATOM   13126 C  CG    . LEU A 1 3186 ? 161.270 133.774 207.272 1.00 29.55  ? 3186 LEU A CG    1 
ATOM   13127 C  CD1   . LEU A 1 3186 ? 162.323 134.047 206.217 1.00 26.06  ? 3186 LEU A CD1   1 
ATOM   13128 C  CD2   . LEU A 1 3186 ? 160.665 132.394 207.086 1.00 35.26  ? 3186 LEU A CD2   1 
ATOM   13129 N  N     . PHE A 1 3187 ? 162.208 134.170 211.819 1.00 34.01  ? 3187 PHE A N     1 
ATOM   13130 C  CA    . PHE A 1 3187 ? 162.798 133.735 213.078 1.00 31.84  ? 3187 PHE A CA    1 
ATOM   13131 C  C     . PHE A 1 3187 ? 161.725 133.237 214.035 1.00 39.25  ? 3187 PHE A C     1 
ATOM   13132 O  O     . PHE A 1 3187 ? 161.823 132.127 214.572 1.00 42.83  ? 3187 PHE A O     1 
ATOM   13133 C  CB    . PHE A 1 3187 ? 163.591 134.882 213.704 1.00 34.25  ? 3187 PHE A CB    1 
ATOM   13134 C  CG    . PHE A 1 3187 ? 164.609 134.438 214.714 1.00 40.53  ? 3187 PHE A CG    1 
ATOM   13135 C  CD1   . PHE A 1 3187 ? 165.893 134.103 214.322 1.00 44.29  ? 3187 PHE A CD1   1 
ATOM   13136 C  CD2   . PHE A 1 3187 ? 164.282 134.360 216.057 1.00 40.55  ? 3187 PHE A CD2   1 
ATOM   13137 C  CE1   . PHE A 1 3187 ? 166.832 133.696 215.250 1.00 42.58  ? 3187 PHE A CE1   1 
ATOM   13138 C  CE2   . PHE A 1 3187 ? 165.216 133.954 216.989 1.00 42.22  ? 3187 PHE A CE2   1 
ATOM   13139 C  CZ    . PHE A 1 3187 ? 166.492 133.622 216.585 1.00 45.99  ? 3187 PHE A CZ    1 
ATOM   13140 N  N     . HIS A 1 3188 ? 160.674 134.036 214.238 1.00 40.96  ? 3188 HIS A N     1 
ATOM   13141 C  CA    . HIS A 1 3188 ? 159.627 133.642 215.175 1.00 44.46  ? 3188 HIS A CA    1 
ATOM   13142 C  C     . HIS A 1 3188 ? 158.923 132.370 214.716 1.00 52.45  ? 3188 HIS A C     1 
ATOM   13143 O  O     . HIS A 1 3188 ? 158.702 131.447 215.512 1.00 58.93  ? 3188 HIS A O     1 
ATOM   13144 C  CB    . HIS A 1 3188 ? 158.622 134.780 215.352 1.00 45.79  ? 3188 HIS A CB    1 
ATOM   13145 C  CG    . HIS A 1 3188 ? 157.601 134.519 216.414 1.00 63.51  ? 3188 HIS A CG    1 
ATOM   13146 N  ND1   . HIS A 1 3188 ? 156.427 133.841 216.168 1.00 69.45  ? 3188 HIS A ND1   1 
ATOM   13147 C  CD2   . HIS A 1 3188 ? 157.582 134.838 217.730 1.00 72.23  ? 3188 HIS A CD2   1 
ATOM   13148 C  CE1   . HIS A 1 3188 ? 155.726 133.757 217.285 1.00 74.81  ? 3188 HIS A CE1   1 
ATOM   13149 N  NE2   . HIS A 1 3188 ? 156.405 134.354 218.248 1.00 77.27  ? 3188 HIS A NE2   1 
ATOM   13150 N  N     . GLU A 1 3189 ? 158.574 132.295 213.428 1.00 49.46  ? 3189 GLU A N     1 
ATOM   13151 C  CA    . GLU A 1 3189 ? 157.829 131.146 212.924 1.00 50.34  ? 3189 GLU A CA    1 
ATOM   13152 C  C     . GLU A 1 3189 ? 158.654 129.868 213.016 1.00 50.81  ? 3189 GLU A C     1 
ATOM   13153 O  O     . GLU A 1 3189 ? 158.160 128.827 213.469 1.00 56.47  ? 3189 GLU A O     1 
ATOM   13154 C  CB    . GLU A 1 3189 ? 157.390 131.404 211.483 1.00 50.81  ? 3189 GLU A CB    1 
ATOM   13155 C  CG    . GLU A 1 3189 ? 156.540 130.301 210.879 1.00 66.86  ? 3189 GLU A CG    1 
ATOM   13156 C  CD    . GLU A 1 3189 ? 156.082 130.626 209.471 1.00 69.95  ? 3189 GLU A CD    1 
ATOM   13157 O  OE1   . GLU A 1 3189 ? 156.445 131.707 208.962 1.00 68.32  ? 3189 GLU A OE1   1 
ATOM   13158 O  OE2   . GLU A 1 3189 ? 155.360 129.800 208.872 1.00 68.94  ? 3189 GLU A OE2   1 
ATOM   13159 N  N     . LYS A 1 3190 ? 159.920 129.928 212.594 1.00 42.48  ? 3190 LYS A N     1 
ATOM   13160 C  CA    . LYS A 1 3190 ? 160.771 128.747 212.639 1.00 43.63  ? 3190 LYS A CA    1 
ATOM   13161 C  C     . LYS A 1 3190 ? 161.048 128.321 214.074 1.00 49.79  ? 3190 LYS A C     1 
ATOM   13162 O  O     . LYS A 1 3190 ? 161.062 127.122 214.373 1.00 56.01  ? 3190 LYS A O     1 
ATOM   13163 C  CB    . LYS A 1 3190 ? 162.075 129.010 211.888 1.00 41.09  ? 3190 LYS A CB    1 
ATOM   13164 C  CG    . LYS A 1 3190 ? 161.908 129.141 210.383 1.00 40.37  ? 3190 LYS A CG    1 
ATOM   13165 C  CD    . LYS A 1 3190 ? 161.257 127.905 209.788 1.00 42.62  ? 3190 LYS A CD    1 
ATOM   13166 C  CE    . LYS A 1 3190 ? 161.087 128.039 208.284 1.00 43.61  ? 3190 LYS A CE    1 
ATOM   13167 N  NZ    . LYS A 1 3190 ? 160.607 126.773 207.665 1.00 41.37  ? 3190 LYS A NZ    1 
ATOM   13168 N  N     . ARG A 1 3191 ? 161.264 129.281 214.980 1.00 49.39  ? 3191 ARG A N     1 
ATOM   13169 C  CA    . ARG A 1 3191 ? 161.476 128.928 216.379 1.00 51.48  ? 3191 ARG A CA    1 
ATOM   13170 C  C     . ARG A 1 3191 ? 160.249 128.244 216.966 1.00 55.69  ? 3191 ARG A C     1 
ATOM   13171 O  O     . ARG A 1 3191 ? 160.370 127.229 217.663 1.00 61.38  ? 3191 ARG A O     1 
ATOM   13172 C  CB    . ARG A 1 3191 ? 161.834 130.174 217.188 1.00 53.57  ? 3191 ARG A CB    1 
ATOM   13173 C  CG    . ARG A 1 3191 ? 163.312 130.519 217.172 1.00 54.69  ? 3191 ARG A CG    1 
ATOM   13174 C  CD    . ARG A 1 3191 ? 164.055 129.818 218.295 1.00 58.15  ? 3191 ARG A CD    1 
ATOM   13175 N  NE    . ARG A 1 3191 ? 163.700 130.354 219.604 1.00 66.03  ? 3191 ARG A NE    1 
ATOM   13176 C  CZ    . ARG A 1 3191 ? 164.430 131.235 220.274 1.00 72.82  ? 3191 ARG A CZ    1 
ATOM   13177 N  NH1   . ARG A 1 3191 ? 165.569 131.701 219.788 1.00 71.05  ? 3191 ARG A NH1   1 
ATOM   13178 N  NH2   . ARG A 1 3191 ? 164.007 131.658 221.462 1.00 72.32  ? 3191 ARG A NH2   1 
ATOM   13179 N  N     . SER A 1 3192 ? 159.056 128.778 216.687 1.00 50.98  ? 3192 SER A N     1 
ATOM   13180 C  CA    . SER A 1 3192 ? 157.835 128.170 217.207 1.00 55.19  ? 3192 SER A CA    1 
ATOM   13181 C  C     . SER A 1 3192 ? 157.638 126.765 216.650 1.00 64.71  ? 3192 SER A C     1 
ATOM   13182 O  O     . SER A 1 3192 ? 157.309 125.830 217.391 1.00 74.75  ? 3192 SER A O     1 
ATOM   13183 C  CB    . SER A 1 3192 ? 156.632 129.054 216.882 1.00 56.40  ? 3192 SER A CB    1 
ATOM   13184 O  OG    . SER A 1 3192 ? 156.115 128.758 215.597 1.00 62.17  ? 3192 SER A OG    1 
ATOM   13185 N  N     . GLU A 1 3193 ? 157.841 126.595 215.340 1.00 60.04  ? 3193 GLU A N     1 
ATOM   13186 C  CA    . GLU A 1 3193 ? 157.675 125.278 214.733 1.00 55.91  ? 3193 GLU A CA    1 
ATOM   13187 C  C     . GLU A 1 3193 ? 158.673 124.278 215.303 1.00 61.35  ? 3193 GLU A C     1 
ATOM   13188 O  O     . GLU A 1 3193 ? 158.315 123.131 215.604 1.00 68.95  ? 3193 GLU A O     1 
ATOM   13189 C  CB    . GLU A 1 3193 ? 157.830 125.377 213.216 1.00 53.17  ? 3193 GLU A CB    1 
ATOM   13190 C  CG    . GLU A 1 3193 ? 156.690 126.091 212.515 1.00 62.89  ? 3193 GLU A CG    1 
ATOM   13191 C  CD    . GLU A 1 3193 ? 156.848 126.091 211.007 1.00 65.13  ? 3193 GLU A CD    1 
ATOM   13192 O  OE1   . GLU A 1 3193 ? 157.899 125.626 210.516 1.00 61.30  ? 3193 GLU A OE1   1 
ATOM   13193 O  OE2   . GLU A 1 3193 ? 155.921 126.556 210.312 1.00 69.37  ? 3193 GLU A OE2   1 
ATOM   13194 N  N     . LEU A 1 3194 ? 159.931 124.696 215.459 1.00 58.80  ? 3194 LEU A N     1 
ATOM   13195 C  CA    . LEU A 1 3194 ? 160.956 123.806 215.989 1.00 61.73  ? 3194 LEU A CA    1 
ATOM   13196 C  C     . LEU A 1 3194 ? 160.644 123.409 217.425 1.00 66.91  ? 3194 LEU A C     1 
ATOM   13197 O  O     . LEU A 1 3194 ? 160.766 122.234 217.791 1.00 71.95  ? 3194 LEU A O     1 
ATOM   13198 C  CB    . LEU A 1 3194 ? 162.322 124.485 215.892 1.00 61.32  ? 3194 LEU A CB    1 
ATOM   13199 C  CG    . LEU A 1 3194 ? 163.590 123.741 216.314 1.00 66.94  ? 3194 LEU A CG    1 
ATOM   13200 C  CD1   . LEU A 1 3194 ? 163.818 122.518 215.437 1.00 74.58  ? 3194 LEU A CD1   1 
ATOM   13201 C  CD2   . LEU A 1 3194 ? 164.787 124.672 216.261 1.00 65.19  ? 3194 LEU A CD2   1 
ATOM   13202 N  N     . GLU A 1 3195 ? 160.213 124.371 218.247 1.00 64.15  ? 3195 GLU A N     1 
ATOM   13203 C  CA    . GLU A 1 3195 ? 159.860 124.064 219.629 1.00 64.29  ? 3195 GLU A CA    1 
ATOM   13204 C  C     . GLU A 1 3195 ? 158.684 123.097 219.701 1.00 70.48  ? 3195 GLU A C     1 
ATOM   13205 O  O     . GLU A 1 3195 ? 158.704 122.143 220.489 1.00 75.37  ? 3195 GLU A O     1 
ATOM   13206 C  CB    . GLU A 1 3195 ? 159.540 125.353 220.387 1.00 67.50  ? 3195 GLU A CB    1 
ATOM   13207 C  CG    . GLU A 1 3195 ? 160.762 126.075 220.933 1.00 76.45  ? 3195 GLU A CG    1 
ATOM   13208 C  CD    . GLU A 1 3195 ? 160.432 127.450 221.480 1.00 79.45  ? 3195 GLU A CD    1 
ATOM   13209 O  OE1   . GLU A 1 3195 ? 159.233 127.785 221.573 1.00 74.12  ? 3195 GLU A OE1   1 
ATOM   13210 O  OE2   . GLU A 1 3195 ? 161.375 128.199 221.811 1.00 82.57  ? 3195 GLU A OE2   1 
ATOM   13211 N  N     . GLU A 1 3196 ? 157.648 123.326 218.887 1.00 71.05  ? 3196 GLU A N     1 
ATOM   13212 C  CA    . GLU A 1 3196 ? 156.487 122.441 218.916 1.00 73.65  ? 3196 GLU A CA    1 
ATOM   13213 C  C     . GLU A 1 3196 ? 156.852 121.026 218.483 1.00 73.65  ? 3196 GLU A C     1 
ATOM   13214 O  O     . GLU A 1 3196 ? 156.454 120.047 219.132 1.00 80.76  ? 3196 GLU A O     1 
ATOM   13215 C  CB    . GLU A 1 3196 ? 155.370 123.003 218.034 1.00 76.11  ? 3196 GLU A CB    1 
ATOM   13216 C  CG    . GLU A 1 3196 ? 154.750 124.294 218.552 1.00 80.16  ? 3196 GLU A CG    1 
ATOM   13217 C  CD    . GLU A 1 3196 ? 153.610 124.051 219.524 1.00 93.57  ? 3196 GLU A CD    1 
ATOM   13218 O  OE1   . GLU A 1 3196 ? 153.801 123.292 220.498 1.00 97.05  ? 3196 GLU A OE1   1 
ATOM   13219 O  OE2   . GLU A 1 3196 ? 152.519 124.620 219.314 1.00 101.69 ? 3196 GLU A OE2   1 
ATOM   13220 N  N     . GLN A 1 3197 ? 157.620 120.891 217.395 1.00 70.43  ? 3197 GLN A N     1 
ATOM   13221 C  CA    . GLN A 1 3197 ? 157.957 119.552 216.923 1.00 73.05  ? 3197 GLN A CA    1 
ATOM   13222 C  C     . GLN A 1 3197 ? 158.876 118.851 217.916 1.00 74.79  ? 3197 GLN A C     1 
ATOM   13223 O  O     . GLN A 1 3197 ? 158.770 117.637 218.117 1.00 80.36  ? 3197 GLN A O     1 
ATOM   13224 C  CB    . GLN A 1 3197 ? 158.593 119.606 215.529 1.00 73.75  ? 3197 GLN A CB    1 
ATOM   13225 C  CG    . GLN A 1 3197 ? 159.932 120.318 215.436 1.00 74.96  ? 3197 GLN A CG    1 
ATOM   13226 C  CD    . GLN A 1 3197 ? 161.088 119.398 215.787 1.00 81.20  ? 3197 GLN A CD    1 
ATOM   13227 O  OE1   . GLN A 1 3197 ? 161.017 118.188 215.567 1.00 79.36  ? 3197 GLN A OE1   1 
ATOM   13228 N  NE2   . GLN A 1 3197 ? 162.143 119.958 216.362 1.00 81.52  ? 3197 GLN A NE2   1 
ATOM   13229 N  N     . GLN A 1 3198 ? 159.779 119.602 218.558 1.00 73.85  ? 3198 GLN A N     1 
ATOM   13230 C  CA    . GLN A 1 3198 ? 160.645 119.004 219.567 1.00 75.96  ? 3198 GLN A CA    1 
ATOM   13231 C  C     . GLN A 1 3198 ? 159.844 118.517 220.766 1.00 81.32  ? 3198 GLN A C     1 
ATOM   13232 O  O     . GLN A 1 3198 ? 160.108 117.432 221.293 1.00 85.41  ? 3198 GLN A O     1 
ATOM   13233 C  CB    . GLN A 1 3198 ? 161.716 120.002 220.008 1.00 79.04  ? 3198 GLN A CB    1 
ATOM   13234 C  CG    . GLN A 1 3198 ? 162.620 119.469 221.105 1.00 79.28  ? 3198 GLN A CG    1 
ATOM   13235 C  CD    . GLN A 1 3198 ? 163.786 118.663 220.570 1.00 83.94  ? 3198 GLN A CD    1 
ATOM   13236 O  OE1   . GLN A 1 3198 ? 163.758 118.183 219.436 1.00 87.89  ? 3198 GLN A OE1   1 
ATOM   13237 N  NE2   . GLN A 1 3198 ? 164.813 118.494 221.393 1.00 85.21  ? 3198 GLN A NE2   1 
ATOM   13238 N  N     . MET A 1 3199 ? 158.865 119.306 221.215 1.00 76.96  ? 3199 MET A N     1 
ATOM   13239 C  CA    . MET A 1 3199 ? 158.015 118.858 222.313 1.00 76.15  ? 3199 MET A CA    1 
ATOM   13240 C  C     . MET A 1 3199 ? 157.267 117.587 221.930 1.00 80.84  ? 3199 MET A C     1 
ATOM   13241 O  O     . MET A 1 3199 ? 157.172 116.640 222.724 1.00 88.09  ? 3199 MET A O     1 
ATOM   13242 C  CB    . MET A 1 3199 ? 157.041 119.970 222.709 1.00 75.51  ? 3199 MET A CB    1 
ATOM   13243 C  CG    . MET A 1 3199 ? 155.965 119.549 223.702 1.00 79.33  ? 3199 MET A CG    1 
ATOM   13244 S  SD    . MET A 1 3199 ? 154.414 119.067 222.915 1.00 92.92  ? 3199 MET A SD    1 
ATOM   13245 C  CE    . MET A 1 3199 ? 153.531 120.625 222.926 1.00 74.33  ? 3199 MET A CE    1 
ATOM   13246 N  N     . HIS A 1 3200 ? 156.743 117.544 220.700 1.00 78.70  ? 3200 HIS A N     1 
ATOM   13247 C  CA    . HIS A 1 3200 ? 156.037 116.353 220.237 1.00 80.83  ? 3200 HIS A CA    1 
ATOM   13248 C  C     . HIS A 1 3200 ? 156.955 115.134 220.227 1.00 82.95  ? 3200 HIS A C     1 
ATOM   13249 O  O     . HIS A 1 3200 ? 156.574 114.052 220.695 1.00 85.22  ? 3200 HIS A O     1 
ATOM   13250 C  CB    . HIS A 1 3200 ? 155.464 116.604 218.842 1.00 79.42  ? 3200 HIS A CB    1 
ATOM   13251 C  CG    . HIS A 1 3200 ? 154.231 117.455 218.837 1.00 82.99  ? 3200 HIS A CG    1 
ATOM   13252 N  ND1   . HIS A 1 3200 ? 154.279 118.831 218.885 1.00 86.97  ? 3200 HIS A ND1   1 
ATOM   13253 C  CD2   . HIS A 1 3200 ? 152.919 117.126 218.784 1.00 82.52  ? 3200 HIS A CD2   1 
ATOM   13254 C  CE1   . HIS A 1 3200 ? 153.049 119.314 218.865 1.00 81.88  ? 3200 HIS A CE1   1 
ATOM   13255 N  NE2   . HIS A 1 3200 ? 152.205 118.299 218.804 1.00 76.98  ? 3200 HIS A NE2   1 
ATOM   13256 N  N     . LEU A 1 3201 ? 158.175 115.294 219.709 1.00 82.04  ? 3201 LEU A N     1 
ATOM   13257 C  CA    . LEU A 1 3201 ? 159.110 114.173 219.657 1.00 80.94  ? 3201 LEU A CA    1 
ATOM   13258 C  C     . LEU A 1 3201 ? 159.507 113.710 221.052 1.00 86.98  ? 3201 LEU A C     1 
ATOM   13259 O  O     . LEU A 1 3201 ? 159.586 112.503 221.309 1.00 94.71  ? 3201 LEU A O     1 
ATOM   13260 C  CB    . LEU A 1 3201 ? 160.351 114.549 218.845 1.00 82.32  ? 3201 LEU A CB    1 
ATOM   13261 C  CG    . LEU A 1 3201 ? 160.166 114.975 217.387 1.00 86.80  ? 3201 LEU A CG    1 
ATOM   13262 C  CD1   . LEU A 1 3201 ? 161.451 114.764 216.605 1.00 86.88  ? 3201 LEU A CD1   1 
ATOM   13263 C  CD2   . LEU A 1 3201 ? 159.016 114.222 216.733 1.00 88.22  ? 3201 LEU A CD2   1 
ATOM   13264 N  N     . ASN A 1 3202 ? 159.772 114.648 221.966 1.00 89.49  ? 3202 ASN A N     1 
ATOM   13265 C  CA    . ASN A 1 3202 ? 160.151 114.257 223.320 1.00 93.25  ? 3202 ASN A CA    1 
ATOM   13266 C  C     . ASN A 1 3202 ? 159.027 113.507 224.020 1.00 93.42  ? 3202 ASN A C     1 
ATOM   13267 O  O     . ASN A 1 3202 ? 159.274 112.487 224.675 1.00 97.65  ? 3202 ASN A O     1 
ATOM   13268 C  CB    . ASN A 1 3202 ? 160.572 115.473 224.147 1.00 92.13  ? 3202 ASN A CB    1 
ATOM   13269 C  CG    . ASN A 1 3202 ? 161.871 116.089 223.666 1.00 89.85  ? 3202 ASN A CG    1 
ATOM   13270 O  OD1   . ASN A 1 3202 ? 161.904 117.234 223.223 1.00 84.78  ? 3202 ASN A OD1   1 
ATOM   13271 N  ND2   . ASN A 1 3202 ? 162.953 115.325 223.756 1.00 90.12  ? 3202 ASN A ND2   1 
ATOM   13272 N  N     . VAL A 1 3203 ? 157.785 113.982 223.895 1.00 89.19  ? 3203 VAL A N     1 
ATOM   13273 C  CA    . VAL A 1 3203 ? 156.695 113.287 224.573 1.00 93.40  ? 3203 VAL A CA    1 
ATOM   13274 C  C     . VAL A 1 3203 ? 156.451 111.919 223.939 1.00 95.19  ? 3203 VAL A C     1 
ATOM   13275 O  O     . VAL A 1 3203 ? 156.164 110.943 224.643 1.00 100.27 ? 3203 VAL A O     1 
ATOM   13276 C  CB    . VAL A 1 3203 ? 155.422 114.157 224.612 1.00 91.80  ? 3203 VAL A CB    1 
ATOM   13277 C  CG1   . VAL A 1 3203 ? 154.886 114.419 223.229 1.00 89.53  ? 3203 VAL A CG1   1 
ATOM   13278 C  CG2   . VAL A 1 3203 ? 154.359 113.503 225.483 1.00 91.90  ? 3203 VAL A CG2   1 
ATOM   13279 N  N     . GLY A 1 3204 ? 156.597 111.808 222.614 1.00 92.94  ? 3204 GLY A N     1 
ATOM   13280 C  CA    . GLY A 1 3204 ? 156.457 110.504 221.981 1.00 92.20  ? 3204 GLY A CA    1 
ATOM   13281 C  C     . GLY A 1 3204 ? 157.530 109.519 222.412 1.00 95.70  ? 3204 GLY A C     1 
ATOM   13282 O  O     . GLY A 1 3204 ? 157.244 108.344 222.675 1.00 103.87 ? 3204 GLY A O     1 
ATOM   13283 N  N     . LEU A 1 3205 ? 158.782 109.982 222.483 1.00 96.01  ? 3205 LEU A N     1 
ATOM   13284 C  CA    . LEU A 1 3205 ? 159.864 109.121 222.948 1.00 97.66  ? 3205 LEU A CA    1 
ATOM   13285 C  C     . LEU A 1 3205 ? 159.655 108.713 224.400 1.00 104.83 ? 3205 LEU A C     1 
ATOM   13286 O  O     . LEU A 1 3205 ? 159.924 107.566 224.774 1.00 105.28 ? 3205 LEU A O     1 
ATOM   13287 C  CB    . LEU A 1 3205 ? 161.212 109.820 222.774 1.00 87.80  ? 3205 LEU A CB    1 
ATOM   13288 C  CG    . LEU A 1 3205 ? 161.659 110.088 221.335 1.00 94.50  ? 3205 LEU A CG    1 
ATOM   13289 C  CD1   . LEU A 1 3205 ? 162.939 110.907 221.315 1.00 94.97  ? 3205 LEU A CD1   1 
ATOM   13290 C  CD2   . LEU A 1 3205 ? 161.841 108.783 220.578 1.00 97.61  ? 3205 LEU A CD2   1 
ATOM   13291 N  N     . ARG A 1 3206 ? 159.173 109.637 225.234 1.00 105.61 ? 3206 ARG A N     1 
ATOM   13292 C  CA    . ARG A 1 3206 ? 158.862 109.284 226.614 1.00 106.22 ? 3206 ARG A CA    1 
ATOM   13293 C  C     . ARG A 1 3206 ? 157.777 108.216 226.674 1.00 110.13 ? 3206 ARG A C     1 
ATOM   13294 O  O     . ARG A 1 3206 ? 157.873 107.267 227.461 1.00 115.50 ? 3206 ARG A O     1 
ATOM   13295 C  CB    . ARG A 1 3206 ? 158.437 110.530 227.391 1.00 105.18 ? 3206 ARG A CB    1 
ATOM   13296 C  CG    . ARG A 1 3206 ? 157.578 110.242 228.610 1.00 105.81 ? 3206 ARG A CG    1 
ATOM   13297 C  CD    . ARG A 1 3206 ? 157.570 111.419 229.569 1.00 102.19 ? 3206 ARG A CD    1 
ATOM   13298 N  NE    . ARG A 1 3206 ? 156.803 112.542 229.044 1.00 104.05 ? 3206 ARG A NE    1 
ATOM   13299 C  CZ    . ARG A 1 3206 ? 157.337 113.669 228.593 1.00 107.12 ? 3206 ARG A CZ    1 
ATOM   13300 N  NH1   . ARG A 1 3206 ? 158.646 113.859 228.586 1.00 102.05 ? 3206 ARG A NH1   1 
ATOM   13301 N  NH2   . ARG A 1 3206 ? 156.537 114.629 228.138 1.00 110.54 ? 3206 ARG A NH2   1 
ATOM   13302 N  N     . LYS A 1 3207 ? 156.740 108.351 225.844 1.00 108.16 ? 3207 LYS A N     1 
ATOM   13303 C  CA    . LYS A 1 3207 ? 155.662 107.366 225.845 1.00 110.93 ? 3207 LYS A CA    1 
ATOM   13304 C  C     . LYS A 1 3207 ? 156.161 105.988 225.424 1.00 112.25 ? 3207 LYS A C     1 
ATOM   13305 O  O     . LYS A 1 3207 ? 155.808 104.977 226.042 1.00 112.28 ? 3207 LYS A O     1 
ATOM   13306 C  CB    . LYS A 1 3207 ? 154.525 107.827 224.933 1.00 109.96 ? 3207 LYS A CB    1 
ATOM   13307 C  CG    . LYS A 1 3207 ? 153.787 109.080 225.411 1.00 110.74 ? 3207 LYS A CG    1 
ATOM   13308 C  CD    . LYS A 1 3207 ? 153.139 108.934 226.792 1.00 113.40 ? 3207 LYS A CD    1 
ATOM   13309 C  CE    . LYS A 1 3207 ? 152.454 107.587 226.998 1.00 122.12 ? 3207 LYS A CE    1 
ATOM   13310 N  NZ    . LYS A 1 3207 ? 151.585 107.221 225.849 1.00 123.68 ? 3207 LYS A NZ    1 
ATOM   13311 N  N     . ILE A 1 3208 ? 156.983 105.923 224.375 1.00 109.82 ? 3208 ILE A N     1 
ATOM   13312 C  CA    . ILE A 1 3208 ? 157.473 104.613 223.949 1.00 107.84 ? 3208 ILE A CA    1 
ATOM   13313 C  C     . ILE A 1 3208 ? 158.469 104.046 224.961 1.00 112.94 ? 3208 ILE A C     1 
ATOM   13314 O  O     . ILE A 1 3208 ? 158.576 102.821 225.119 1.00 119.70 ? 3208 ILE A O     1 
ATOM   13315 C  CB    . ILE A 1 3208 ? 158.062 104.681 222.527 1.00 100.45 ? 3208 ILE A CB    1 
ATOM   13316 C  CG1   . ILE A 1 3208 ? 159.266 105.616 222.472 1.00 103.29 ? 3208 ILE A CG1   1 
ATOM   13317 C  CG2   . ILE A 1 3208 ? 156.996 105.124 221.533 1.00 98.23  ? 3208 ILE A CG2   1 
ATOM   13318 C  CD1   . ILE A 1 3208 ? 160.009 105.560 221.164 1.00 100.47 ? 3208 ILE A CD1   1 
ATOM   13319 N  N     . LYS A 1 3209 ? 159.199 104.911 225.673 1.00 110.33 ? 3209 LYS A N     1 
ATOM   13320 C  CA    . LYS A 1 3209 ? 160.051 104.435 226.759 1.00 116.29 ? 3209 LYS A CA    1 
ATOM   13321 C  C     . LYS A 1 3209 ? 159.221 103.825 227.882 1.00 121.19 ? 3209 LYS A C     1 
ATOM   13322 O  O     . LYS A 1 3209 ? 159.585 102.783 228.440 1.00 121.50 ? 3209 LYS A O     1 
ATOM   13323 C  CB    . LYS A 1 3209 ? 160.914 105.579 227.289 1.00 119.34 ? 3209 LYS A CB    1 
ATOM   13324 C  CG    . LYS A 1 3209 ? 162.051 105.131 228.193 1.00 121.50 ? 3209 LYS A CG    1 
ATOM   13325 C  CD    . LYS A 1 3209 ? 163.323 104.878 227.402 1.00 117.00 ? 3209 LYS A CD    1 
ATOM   13326 C  CE    . LYS A 1 3209 ? 164.545 104.883 228.306 1.00 121.53 ? 3209 LYS A CE    1 
ATOM   13327 N  NZ    . LYS A 1 3209 ? 165.647 104.043 227.760 1.00 125.22 ? 3209 LYS A NZ    1 
ATOM   13328 N  N     . GLU A 1 3210 ? 158.102 104.464 228.232 1.00 122.52 ? 3210 GLU A N     1 
ATOM   13329 C  CA    . GLU A 1 3210 ? 157.193 103.861 229.204 1.00 120.45 ? 3210 GLU A CA    1 
ATOM   13330 C  C     . GLU A 1 3210 ? 156.654 102.533 228.689 1.00 120.75 ? 3210 GLU A C     1 
ATOM   13331 O  O     . GLU A 1 3210 ? 156.501 101.577 229.456 1.00 121.04 ? 3210 GLU A O     1 
ATOM   13332 C  CB    . GLU A 1 3210 ? 156.041 104.812 229.538 1.00 112.93 ? 3210 GLU A CB    1 
ATOM   13333 C  CG    . GLU A 1 3210 ? 156.430 106.240 229.936 1.00 118.39 ? 3210 GLU A CG    1 
ATOM   13334 C  CD    . GLU A 1 3210 ? 157.696 106.339 230.780 1.00 119.47 ? 3210 GLU A CD    1 
ATOM   13335 O  OE1   . GLU A 1 3210 ? 158.422 107.344 230.629 1.00 112.82 ? 3210 GLU A OE1   1 
ATOM   13336 O  OE2   . GLU A 1 3210 ? 157.943 105.456 231.630 1.00 119.60 ? 3210 GLU A OE2   1 
ATOM   13337 N  N     . THR A 1 3211 ? 156.368 102.456 227.388 1.00 123.68 ? 3211 THR A N     1 
ATOM   13338 C  CA    . THR A 1 3211 ? 155.874 101.212 226.803 1.00 126.18 ? 3211 THR A CA    1 
ATOM   13339 C  C     . THR A 1 3211 ? 156.887 100.081 226.961 1.00 127.53 ? 3211 THR A C     1 
ATOM   13340 O  O     . THR A 1 3211 ? 156.532 98.966  227.360 1.00 131.91 ? 3211 THR A O     1 
ATOM   13341 C  CB    . THR A 1 3211 ? 155.535 101.428 225.328 1.00 123.83 ? 3211 THR A CB    1 
ATOM   13342 O  OG1   . THR A 1 3211 ? 154.495 102.407 225.212 1.00 123.31 ? 3211 THR A OG1   1 
ATOM   13343 C  CG2   . THR A 1 3211 ? 155.078 100.128 224.685 1.00 118.57 ? 3211 THR A CG2   1 
ATOM   13344 N  N     . VAL A 1 3212 ? 158.159 100.349 226.652 1.00 125.56 ? 3212 VAL A N     1 
ATOM   13345 C  CA    . VAL A 1 3212 ? 159.165 99.290  226.748 1.00 125.61 ? 3212 VAL A CA    1 
ATOM   13346 C  C     . VAL A 1 3212 ? 159.438 98.934  228.209 1.00 127.42 ? 3212 VAL A C     1 
ATOM   13347 O  O     . VAL A 1 3212 ? 159.626 97.756  228.554 1.00 128.00 ? 3212 VAL A O     1 
ATOM   13348 C  CB    . VAL A 1 3212 ? 160.450 99.677  225.986 1.00 120.51 ? 3212 VAL A CB    1 
ATOM   13349 C  CG1   . VAL A 1 3212 ? 161.138 100.876 226.612 1.00 119.82 ? 3212 VAL A CG1   1 
ATOM   13350 C  CG2   . VAL A 1 3212 ? 161.401 98.491  225.913 1.00 115.85 ? 3212 VAL A CG2   1 
ATOM   13351 N  N     . ASP A 1 3213 ? 159.452 99.934  229.097 1.00 129.56 ? 3213 ASP A N     1 
ATOM   13352 C  CA    . ASP A 1 3213 ? 159.625 99.644  230.515 1.00 132.44 ? 3213 ASP A CA    1 
ATOM   13353 C  C     . ASP A 1 3213 ? 158.458 98.830  231.059 1.00 129.33 ? 3213 ASP A C     1 
ATOM   13354 O  O     . ASP A 1 3213 ? 158.631 98.045  231.998 1.00 132.00 ? 3213 ASP A O     1 
ATOM   13355 C  CB    . ASP A 1 3213 ? 159.786 100.945 231.301 1.00 131.59 ? 3213 ASP A CB    1 
ATOM   13356 C  CG    . ASP A 1 3213 ? 161.206 101.477 231.261 1.00 128.63 ? 3213 ASP A CG    1 
ATOM   13357 O  OD1   . ASP A 1 3213 ? 162.148 100.658 231.198 1.00 124.80 ? 3213 ASP A OD1   1 
ATOM   13358 O  OD2   . ASP A 1 3213 ? 161.382 102.713 231.289 1.00 121.77 ? 3213 ASP A OD2   1 
ATOM   13359 N  N     . GLN A 1 3214 ? 157.268 99.004  230.484 1.00 128.39 ? 3214 GLN A N     1 
ATOM   13360 C  CA    . GLN A 1 3214 ? 156.117 98.200  230.874 1.00 131.52 ? 3214 GLN A CA    1 
ATOM   13361 C  C     . GLN A 1 3214 ? 156.208 96.782  230.327 1.00 132.99 ? 3214 GLN A C     1 
ATOM   13362 O  O     . GLN A 1 3214 ? 155.846 95.825  231.019 1.00 133.02 ? 3214 GLN A O     1 
ATOM   13363 C  CB    . GLN A 1 3214 ? 154.827 98.869  230.399 1.00 128.87 ? 3214 GLN A CB    1 
ATOM   13364 C  CG    . GLN A 1 3214 ? 153.562 98.141  230.816 1.00 127.91 ? 3214 GLN A CG    1 
ATOM   13365 C  CD    . GLN A 1 3214 ? 152.305 98.855  230.366 1.00 129.46 ? 3214 GLN A CD    1 
ATOM   13366 O  OE1   . GLN A 1 3214 ? 152.367 99.900  229.718 1.00 132.85 ? 3214 GLN A OE1   1 
ATOM   13367 N  NE2   . GLN A 1 3214 ? 151.153 98.287  230.698 1.00 128.75 ? 3214 GLN A NE2   1 
ATOM   13368 N  N     . VAL A 1 3215 ? 156.673 96.620  229.086 1.00 133.16 ? 3215 VAL A N     1 
ATOM   13369 C  CA    . VAL A 1 3215 ? 156.727 95.273  228.524 1.00 133.82 ? 3215 VAL A CA    1 
ATOM   13370 C  C     . VAL A 1 3215 ? 157.811 94.450  229.208 1.00 136.36 ? 3215 VAL A C     1 
ATOM   13371 O  O     . VAL A 1 3215 ? 157.701 93.221  229.293 1.00 137.48 ? 3215 VAL A O     1 
ATOM   13372 C  CB    . VAL A 1 3215 ? 156.925 95.298  226.996 1.00 128.98 ? 3215 VAL A CB    1 
ATOM   13373 C  CG1   . VAL A 1 3215 ? 155.812 96.086  226.327 1.00 127.10 ? 3215 VAL A CG1   1 
ATOM   13374 C  CG2   . VAL A 1 3215 ? 158.294 95.819  226.622 1.00 124.02 ? 3215 VAL A CG2   1 
ATOM   13375 N  N     . GLU A 1 3216 ? 158.869 95.095  229.708 1.00 137.03 ? 3216 GLU A N     1 
ATOM   13376 C  CA    . GLU A 1 3216 ? 159.869 94.355  230.476 1.00 139.51 ? 3216 GLU A CA    1 
ATOM   13377 C  C     . GLU A 1 3216 ? 159.251 93.737  231.729 1.00 141.50 ? 3216 GLU A C     1 
ATOM   13378 O  O     . GLU A 1 3216 ? 159.416 92.537  232.000 1.00 141.27 ? 3216 GLU A O     1 
ATOM   13379 C  CB    . GLU A 1 3216 ? 161.035 95.274  230.843 1.00 135.53 ? 3216 GLU A CB    1 
ATOM   13380 C  CG    . GLU A 1 3216 ? 162.284 94.541  231.313 1.00 135.76 ? 3216 GLU A CG    1 
ATOM   13381 C  CD    . GLU A 1 3216 ? 162.254 94.217  232.794 1.00 138.52 ? 3216 GLU A CD    1 
ATOM   13382 O  OE1   . GLU A 1 3216 ? 161.583 94.950  233.552 1.00 137.73 ? 3216 GLU A OE1   1 
ATOM   13383 O  OE2   . GLU A 1 3216 ? 162.898 93.227  233.201 1.00 136.99 ? 3216 GLU A OE2   1 
ATOM   13384 N  N     . GLU A 1 3217 ? 158.519 94.543  232.502 1.00 139.56 ? 3217 GLU A N     1 
ATOM   13385 C  CA    . GLU A 1 3217 ? 157.866 94.012  233.693 1.00 139.08 ? 3217 GLU A CA    1 
ATOM   13386 C  C     . GLU A 1 3217 ? 156.755 93.036  233.328 1.00 140.24 ? 3217 GLU A C     1 
ATOM   13387 O  O     . GLU A 1 3217 ? 156.455 92.128  234.107 1.00 141.93 ? 3217 GLU A O     1 
ATOM   13388 C  CB    . GLU A 1 3217 ? 157.326 95.153  234.560 1.00 138.74 ? 3217 GLU A CB    1 
ATOM   13389 C  CG    . GLU A 1 3217 ? 155.972 95.696  234.136 1.00 139.44 ? 3217 GLU A CG    1 
ATOM   13390 C  CD    . GLU A 1 3217 ? 155.502 96.840  235.011 1.00 137.89 ? 3217 GLU A CD    1 
ATOM   13391 O  OE1   . GLU A 1 3217 ? 156.319 97.363  235.797 1.00 143.77 ? 3217 GLU A OE1   1 
ATOM   13392 O  OE2   . GLU A 1 3217 ? 154.314 97.216  234.914 1.00 127.62 ? 3217 GLU A OE2   1 
ATOM   13393 N  N     . LEU A 1 3218 ? 156.151 93.189  232.147 1.00 139.27 ? 3218 LEU A N     1 
ATOM   13394 C  CA    . LEU A 1 3218 ? 155.160 92.215  231.701 1.00 138.79 ? 3218 LEU A CA    1 
ATOM   13395 C  C     . LEU A 1 3218 ? 155.805 90.868  231.403 1.00 139.31 ? 3218 LEU A C     1 
ATOM   13396 O  O     . LEU A 1 3218 ? 155.225 89.822  231.699 1.00 138.44 ? 3218 LEU A O     1 
ATOM   13397 C  CB    . LEU A 1 3218 ? 154.412 92.737  230.476 1.00 137.44 ? 3218 LEU A CB    1 
ATOM   13398 C  CG    . LEU A 1 3218 ? 153.149 93.548  230.776 1.00 134.57 ? 3218 LEU A CG    1 
ATOM   13399 C  CD1   . LEU A 1 3218 ? 152.315 93.719  229.519 1.00 129.85 ? 3218 LEU A CD1   1 
ATOM   13400 C  CD2   . LEU A 1 3218 ? 152.332 92.889  231.878 1.00 126.93 ? 3218 LEU A CD2   1 
ATOM   13401 N  N     . ARG A 1 3219 ? 157.002 90.871  230.812 1.00 139.37 ? 3219 ARG A N     1 
ATOM   13402 C  CA    . ARG A 1 3219 ? 157.731 89.620  230.612 1.00 140.83 ? 3219 ARG A CA    1 
ATOM   13403 C  C     . ARG A 1 3219 ? 158.117 88.991  231.946 1.00 142.80 ? 3219 ARG A C     1 
ATOM   13404 O  O     . ARG A 1 3219 ? 158.032 87.765  232.118 1.00 140.94 ? 3219 ARG A O     1 
ATOM   13405 C  CB    . ARG A 1 3219 ? 158.973 89.868  229.756 1.00 136.67 ? 3219 ARG A CB    1 
ATOM   13406 C  CG    . ARG A 1 3219 ? 158.725 89.790  228.259 1.00 133.93 ? 3219 ARG A CG    1 
ATOM   13407 C  CD    . ARG A 1 3219 ? 160.014 89.522  227.501 1.00 133.56 ? 3219 ARG A CD    1 
ATOM   13408 N  NE    . ARG A 1 3219 ? 161.093 90.403  227.932 1.00 140.38 ? 3219 ARG A NE    1 
ATOM   13409 C  CZ    . ARG A 1 3219 ? 161.627 91.357  227.181 1.00 138.88 ? 3219 ARG A CZ    1 
ATOM   13410 N  NH1   . ARG A 1 3219 ? 161.206 91.582  225.947 1.00 135.10 ? 3219 ARG A NH1   1 
ATOM   13411 N  NH2   . ARG A 1 3219 ? 162.608 92.103  227.680 1.00 136.25 ? 3219 ARG A NH2   1 
ATOM   13412 N  N     . ARG A 1 3220 ? 158.552 89.816  232.902 1.00 142.48 ? 3220 ARG A N     1 
ATOM   13413 C  CA    . ARG A 1 3220 ? 158.868 89.292  234.229 1.00 141.41 ? 3220 ARG A CA    1 
ATOM   13414 C  C     . ARG A 1 3220 ? 157.635 88.675  234.886 1.00 143.89 ? 3220 ARG A C     1 
ATOM   13415 O  O     . ARG A 1 3220 ? 157.709 87.589  235.476 1.00 141.48 ? 3220 ARG A O     1 
ATOM   13416 C  CB    . ARG A 1 3220 ? 159.453 90.401  235.104 1.00 139.29 ? 3220 ARG A CB    1 
ATOM   13417 C  CG    . ARG A 1 3220 ? 159.529 90.057  236.582 1.00 141.98 ? 3220 ARG A CG    1 
ATOM   13418 C  CD    . ARG A 1 3220 ? 159.404 91.304  237.442 1.00 144.05 ? 3220 ARG A CD    1 
ATOM   13419 N  NE    . ARG A 1 3220 ? 158.268 92.128  237.047 1.00 145.95 ? 3220 ARG A NE    1 
ATOM   13420 C  CZ    . ARG A 1 3220 ? 157.022 91.931  237.454 1.00 146.38 ? 3220 ARG A CZ    1 
ATOM   13421 N  NH1   . ARG A 1 3220 ? 156.712 90.943  238.278 1.00 147.08 ? 3220 ARG A NH1   1 
ATOM   13422 N  NH2   . ARG A 1 3220 ? 156.063 92.745  237.024 1.00 144.27 ? 3220 ARG A NH2   1 
ATOM   13423 N  N     . ASP A 1 3221 ? 156.487 89.348  234.778 1.00 146.52 ? 3221 ASP A N     1 
ATOM   13424 C  CA    . ASP A 1 3221 ? 155.243 88.800  235.306 1.00 145.74 ? 3221 ASP A CA    1 
ATOM   13425 C  C     . ASP A 1 3221 ? 154.819 87.545  234.555 1.00 148.49 ? 3221 ASP A C     1 
ATOM   13426 O  O     . ASP A 1 3221 ? 154.211 86.652  235.146 1.00 150.45 ? 3221 ASP A O     1 
ATOM   13427 C  CB    . ASP A 1 3221 ? 154.138 89.855  235.247 1.00 141.93 ? 3221 ASP A CB    1 
ATOM   13428 C  CG    . ASP A 1 3221 ? 152.907 89.454  236.036 1.00 143.39 ? 3221 ASP A CG    1 
ATOM   13429 O  OD1   . ASP A 1 3221 ? 152.032 88.768  235.467 1.00 145.23 ? 3221 ASP A OD1   1 
ATOM   13430 O  OD2   . ASP A 1 3221 ? 152.815 89.824  237.225 1.00 142.10 ? 3221 ASP A OD2   1 
ATOM   13431 N  N     . LEU A 1 3222 ? 155.115 87.467  233.256 1.00 146.95 ? 3222 LEU A N     1 
ATOM   13432 C  CA    . LEU A 1 3222 ? 154.851 86.250  232.496 1.00 143.89 ? 3222 LEU A CA    1 
ATOM   13433 C  C     . LEU A 1 3222 ? 155.643 85.077  233.055 1.00 144.51 ? 3222 LEU A C     1 
ATOM   13434 O  O     . LEU A 1 3222 ? 155.102 83.978  233.237 1.00 144.34 ? 3222 LEU A O     1 
ATOM   13435 C  CB    . LEU A 1 3222 ? 155.196 86.479  231.024 1.00 138.00 ? 3222 LEU A CB    1 
ATOM   13436 C  CG    . LEU A 1 3222 ? 155.338 85.270  230.099 1.00 134.03 ? 3222 LEU A CG    1 
ATOM   13437 C  CD1   . LEU A 1 3222 ? 153.989 84.639  229.817 1.00 135.50 ? 3222 LEU A CD1   1 
ATOM   13438 C  CD2   . LEU A 1 3222 ? 156.029 85.666  228.803 1.00 129.90 ? 3222 LEU A CD2   1 
ATOM   13439 N  N     . ARG A 1 3223 ? 156.927 85.298  233.345 1.00 144.07 ? 3223 ARG A N     1 
ATOM   13440 C  CA    . ARG A 1 3223 ? 157.734 84.246  233.961 1.00 146.96 ? 3223 ARG A CA    1 
ATOM   13441 C  C     . ARG A 1 3223 ? 157.196 83.876  235.340 1.00 147.87 ? 3223 ARG A C     1 
ATOM   13442 O  O     . ARG A 1 3223 ? 157.153 82.692  235.706 1.00 145.99 ? 3223 ARG A O     1 
ATOM   13443 C  CB    . ARG A 1 3223 ? 159.194 84.689  234.052 1.00 145.40 ? 3223 ARG A CB    1 
ATOM   13444 C  CG    . ARG A 1 3223 ? 160.133 83.621  234.595 1.00 140.70 ? 3223 ARG A CG    1 
ATOM   13445 C  CD    . ARG A 1 3223 ? 161.470 84.216  235.006 1.00 138.86 ? 3223 ARG A CD    1 
ATOM   13446 N  NE    . ARG A 1 3223 ? 161.316 85.500  235.678 1.00 146.44 ? 3223 ARG A NE    1 
ATOM   13447 C  CZ    . ARG A 1 3223 ? 161.096 85.645  236.978 1.00 148.66 ? 3223 ARG A CZ    1 
ATOM   13448 N  NH1   . ARG A 1 3223 ? 161.006 84.600  237.784 1.00 146.84 ? 3223 ARG A NH1   1 
ATOM   13449 N  NH2   . ARG A 1 3223 ? 160.966 86.868  237.482 1.00 147.80 ? 3223 ARG A NH2   1 
ATOM   13450 N  N     . ILE A 1 3224 ? 156.779 84.878  236.119 1.00 146.82 ? 3224 ILE A N     1 
ATOM   13451 C  CA    . ILE A 1 3224 ? 156.236 84.615  237.450 1.00 147.34 ? 3224 ILE A CA    1 
ATOM   13452 C  C     . ILE A 1 3224 ? 154.963 83.779  237.358 1.00 147.77 ? 3224 ILE A C     1 
ATOM   13453 O  O     . ILE A 1 3224 ? 154.768 82.829  238.126 1.00 146.27 ? 3224 ILE A O     1 
ATOM   13454 C  CB    . ILE A 1 3224 ? 155.994 85.941  238.197 1.00 149.70 ? 3224 ILE A CB    1 
ATOM   13455 C  CG1   . ILE A 1 3224 ? 157.322 86.526  238.683 1.00 150.22 ? 3224 ILE A CG1   1 
ATOM   13456 C  CG2   . ILE A 1 3224 ? 155.036 85.739  239.363 1.00 145.45 ? 3224 ILE A CG2   1 
ATOM   13457 C  CD1   . ILE A 1 3224 ? 157.174 87.817  239.457 1.00 147.81 ? 3224 ILE A CD1   1 
ATOM   13458 N  N     . LYS A 1 3225 ? 154.078 84.118  236.417 1.00 149.38 ? 3225 LYS A N     1 
ATOM   13459 C  CA    . LYS A 1 3225 ? 152.845 83.357  236.242 1.00 147.69 ? 3225 LYS A CA    1 
ATOM   13460 C  C     . LYS A 1 3225 ? 153.131 81.947  235.746 1.00 148.54 ? 3225 LYS A C     1 
ATOM   13461 O  O     . LYS A 1 3225 ? 152.430 81.001  236.117 1.00 145.14 ? 3225 LYS A O     1 
ATOM   13462 C  CB    . LYS A 1 3225 ? 151.901 84.082  235.282 1.00 144.97 ? 3225 LYS A CB    1 
ATOM   13463 C  CG    . LYS A 1 3225 ? 151.429 85.441  235.771 1.00 147.88 ? 3225 LYS A CG    1 
ATOM   13464 C  CD    . LYS A 1 3225 ? 150.631 85.319  237.059 1.00 150.38 ? 3225 LYS A CD    1 
ATOM   13465 C  CE    . LYS A 1 3225 ? 149.314 84.598  236.824 1.00 146.90 ? 3225 LYS A CE    1 
ATOM   13466 N  NZ    . LYS A 1 3225 ? 148.414 85.368  235.922 1.00 141.80 ? 3225 LYS A NZ    1 
ATOM   13467 N  N     . SER A 1 3226 ? 154.150 81.784  234.898 1.00 150.02 ? 3226 SER A N     1 
ATOM   13468 C  CA    . SER A 1 3226 ? 154.534 80.442  234.470 1.00 146.45 ? 3226 SER A CA    1 
ATOM   13469 C  C     . SER A 1 3226 ? 155.003 79.603  235.654 1.00 147.56 ? 3226 SER A C     1 
ATOM   13470 O  O     . SER A 1 3226 ? 154.615 78.435  235.793 1.00 144.77 ? 3226 SER A O     1 
ATOM   13471 C  CB    . SER A 1 3226 ? 155.624 80.522  233.403 1.00 142.00 ? 3226 SER A CB    1 
ATOM   13472 O  OG    . SER A 1 3226 ? 156.851 80.960  233.960 1.00 143.56 ? 3226 SER A OG    1 
ATOM   13473 N  N     . GLN A 1 3227 ? 155.829 80.187  236.525 1.00 148.73 ? 3227 GLN A N     1 
ATOM   13474 C  CA    . GLN A 1 3227 ? 156.277 79.467  237.715 1.00 150.45 ? 3227 GLN A CA    1 
ATOM   13475 C  C     . GLN A 1 3227 ? 155.105 79.132  238.633 1.00 151.20 ? 3227 GLN A C     1 
ATOM   13476 O  O     . GLN A 1 3227 ? 155.035 78.029  239.192 1.00 148.58 ? 3227 GLN A O     1 
ATOM   13477 C  CB    . GLN A 1 3227 ? 157.327 80.290  238.461 1.00 148.76 ? 3227 GLN A CB    1 
ATOM   13478 C  CG    . GLN A 1 3227 ? 157.884 79.613  239.704 1.00 144.82 ? 3227 GLN A CG    1 
ATOM   13479 C  CD    . GLN A 1 3227 ? 157.239 80.117  240.981 1.00 145.24 ? 3227 GLN A CD    1 
ATOM   13480 O  OE1   . GLN A 1 3227 ? 156.453 81.064  240.961 1.00 148.35 ? 3227 GLN A OE1   1 
ATOM   13481 N  NE2   . GLN A 1 3227 ? 157.569 79.483  242.100 1.00 142.14 ? 3227 GLN A NE2   1 
ATOM   13482 N  N     . GLU A 1 3228 ? 154.177 80.077  238.804 1.00 152.06 ? 3228 GLU A N     1 
ATOM   13483 C  CA    . GLU A 1 3228 ? 153.017 79.835  239.656 1.00 148.33 ? 3228 GLU A CA    1 
ATOM   13484 C  C     . GLU A 1 3228 ? 152.132 78.733  239.084 1.00 148.42 ? 3228 GLU A C     1 
ATOM   13485 O  O     . GLU A 1 3228 ? 151.607 77.899  239.829 1.00 147.63 ? 3228 GLU A O     1 
ATOM   13486 C  CB    . GLU A 1 3228 ? 152.225 81.129  239.840 1.00 146.61 ? 3228 GLU A CB    1 
ATOM   13487 C  CG    . GLU A 1 3228 ? 150.945 80.974  240.644 1.00 142.34 ? 3228 GLU A CG    1 
ATOM   13488 C  CD    . GLU A 1 3228 ? 149.978 82.120  240.422 1.00 144.68 ? 3228 GLU A CD    1 
ATOM   13489 O  OE1   . GLU A 1 3228 ? 150.246 82.962  239.539 1.00 144.94 ? 3228 GLU A OE1   1 
ATOM   13490 O  OE2   . GLU A 1 3228 ? 148.951 82.180  241.130 1.00 143.65 ? 3228 GLU A OE2   1 
ATOM   13491 N  N     . LEU A 1 3229 ? 151.953 78.717  237.761 1.00 149.09 ? 3229 LEU A N     1 
ATOM   13492 C  CA    . LEU A 1 3229 ? 151.195 77.647  237.123 1.00 150.00 ? 3229 LEU A CA    1 
ATOM   13493 C  C     . LEU A 1 3229 ? 151.883 76.303  237.308 1.00 150.66 ? 3229 LEU A C     1 
ATOM   13494 O  O     . LEU A 1 3229 ? 151.220 75.285  237.542 1.00 152.36 ? 3229 LEU A O     1 
ATOM   13495 C  CB    . LEU A 1 3229 ? 151.006 77.950  235.636 1.00 145.41 ? 3229 LEU A CB    1 
ATOM   13496 C  CG    . LEU A 1 3229 ? 150.352 76.845  234.803 1.00 139.35 ? 3229 LEU A CG    1 
ATOM   13497 C  CD1   . LEU A 1 3229 ? 148.999 76.461  235.386 1.00 143.23 ? 3229 LEU A CD1   1 
ATOM   13498 C  CD2   . LEU A 1 3229 ? 150.215 77.270  233.351 1.00 131.78 ? 3229 LEU A CD2   1 
ATOM   13499 N  N     . GLU A 1 3230 ? 153.213 76.276  237.191 1.00 148.75 ? 3230 GLU A N     1 
ATOM   13500 C  CA    . GLU A 1 3230 ? 153.951 75.042  237.440 1.00 149.35 ? 3230 GLU A CA    1 
ATOM   13501 C  C     . GLU A 1 3230 ? 153.708 74.543  238.859 1.00 152.85 ? 3230 GLU A C     1 
ATOM   13502 O  O     . GLU A 1 3230 ? 153.428 73.357  239.076 1.00 152.73 ? 3230 GLU A O     1 
ATOM   13503 C  CB    . GLU A 1 3230 ? 155.444 75.266  237.199 1.00 146.40 ? 3230 GLU A CB    1 
ATOM   13504 C  CG    . GLU A 1 3230 ? 155.842 75.348  235.735 1.00 143.63 ? 3230 GLU A CG    1 
ATOM   13505 C  CD    . GLU A 1 3230 ? 157.328 75.590  235.552 1.00 141.85 ? 3230 GLU A CD    1 
ATOM   13506 O  OE1   . GLU A 1 3230 ? 158.052 75.649  236.568 1.00 138.53 ? 3230 GLU A OE1   1 
ATOM   13507 O  OE2   . GLU A 1 3230 ? 157.772 75.723  234.392 1.00 142.29 ? 3230 GLU A OE2   1 
ATOM   13508 N  N     . VAL A 1 3231 ? 153.791 75.446  239.837 1.00 154.29 ? 3231 VAL A N     1 
ATOM   13509 C  CA    . VAL A 1 3231 ? 153.583 75.059  241.231 1.00 154.28 ? 3231 VAL A CA    1 
ATOM   13510 C  C     . VAL A 1 3231 ? 152.163 74.540  241.432 1.00 155.04 ? 3231 VAL A C     1 
ATOM   13511 O  O     . VAL A 1 3231 ? 151.944 73.507  242.078 1.00 154.37 ? 3231 VAL A O     1 
ATOM   13512 C  CB    . VAL A 1 3231 ? 153.890 76.242  242.168 1.00 148.72 ? 3231 VAL A CB    1 
ATOM   13513 C  CG1   . VAL A 1 3231 ? 153.378 75.960  243.573 1.00 140.67 ? 3231 VAL A CG1   1 
ATOM   13514 C  CG2   . VAL A 1 3231 ? 155.383 76.529  242.185 1.00 143.52 ? 3231 VAL A CG2   1 
ATOM   13515 N  N     . LYS A 1 3232 ? 151.177 75.246  240.871 1.00 154.03 ? 3232 LYS A N     1 
ATOM   13516 C  CA    . LYS A 1 3232 ? 149.782 74.856  241.052 1.00 152.44 ? 3232 LYS A CA    1 
ATOM   13517 C  C     . LYS A 1 3232 ? 149.490 73.499  240.423 1.00 156.05 ? 3232 LYS A C     1 
ATOM   13518 O  O     . LYS A 1 3232 ? 148.821 72.659  241.036 1.00 158.66 ? 3232 LYS A O     1 
ATOM   13519 C  CB    . LYS A 1 3232 ? 148.857 75.925  240.470 1.00 148.69 ? 3232 LYS A CB    1 
ATOM   13520 C  CG    . LYS A 1 3232 ? 148.788 77.204  241.289 1.00 141.16 ? 3232 LYS A CG    1 
ATOM   13521 C  CD    . LYS A 1 3232 ? 147.740 77.100  242.385 1.00 132.37 ? 3232 LYS A CD    1 
ATOM   13522 C  CE    . LYS A 1 3232 ? 147.334 78.473  242.892 1.00 131.36 ? 3232 LYS A CE    1 
ATOM   13523 N  NZ    . LYS A 1 3232 ? 146.147 78.405  243.789 1.00 134.61 ? 3232 LYS A NZ    1 
ATOM   13524 N  N     . ASN A 1 3233 ? 149.981 73.260  239.203 1.00 156.06 ? 3233 ASN A N     1 
ATOM   13525 C  CA    . ASN A 1 3233 ? 149.704 71.981  238.561 1.00 157.41 ? 3233 ASN A CA    1 
ATOM   13526 C  C     . ASN A 1 3233 ? 150.455 70.841  239.237 1.00 159.39 ? 3233 ASN A C     1 
ATOM   13527 O  O     . ASN A 1 3233 ? 149.925 69.729  239.333 1.00 156.99 ? 3233 ASN A O     1 
ATOM   13528 C  CB    . ASN A 1 3233 ? 150.013 72.050  237.058 1.00 157.20 ? 3233 ASN A CB    1 
ATOM   13529 C  CG    . ASN A 1 3233 ? 151.491 72.254  236.751 1.00 159.64 ? 3233 ASN A CG    1 
ATOM   13530 O  OD1   . ASN A 1 3233 ? 152.365 71.600  237.320 1.00 159.70 ? 3233 ASN A OD1   1 
ATOM   13531 N  ND2   . ASN A 1 3233 ? 151.772 73.167  235.828 1.00 155.65 ? 3233 ASN A ND2   1 
ATOM   13532 N  N     . ALA A 1 3234 ? 151.673 71.094  239.728 1.00 159.74 ? 3234 ALA A N     1 
ATOM   13533 C  CA    . ALA A 1 3234 ? 152.377 70.071  240.493 1.00 157.11 ? 3234 ALA A CA    1 
ATOM   13534 C  C     . ALA A 1 3234 ? 151.621 69.724  241.770 1.00 159.48 ? 3234 ALA A C     1 
ATOM   13535 O  O     . ALA A 1 3234 ? 151.490 68.546  242.123 1.00 158.57 ? 3234 ALA A O     1 
ATOM   13536 C  CB    . ALA A 1 3234 ? 153.796 70.537  240.815 1.00 149.75 ? 3234 ALA A CB    1 
ATOM   13537 N  N     . ALA A 1 3235 ? 151.110 70.740  242.472 1.00 159.82 ? 3235 ALA A N     1 
ATOM   13538 C  CA    . ALA A 1 3235 ? 150.334 70.487  243.681 1.00 156.83 ? 3235 ALA A CA    1 
ATOM   13539 C  C     . ALA A 1 3235 ? 149.061 69.710  243.367 1.00 158.41 ? 3235 ALA A C     1 
ATOM   13540 O  O     . ALA A 1 3235 ? 148.690 68.789  244.104 1.00 158.51 ? 3235 ALA A O     1 
ATOM   13541 C  CB    . ALA A 1 3235 ? 150.001 71.805  244.378 1.00 151.66 ? 3235 ALA A CB    1 
ATOM   13542 N  N     . ALA A 1 3236 ? 148.376 70.072  242.280 1.00 159.62 ? 3236 ALA A N     1 
ATOM   13543 C  CA    . ALA A 1 3236 ? 147.162 69.358  241.898 1.00 158.07 ? 3236 ALA A CA    1 
ATOM   13544 C  C     . ALA A 1 3236 ? 147.459 67.903  241.554 1.00 158.23 ? 3236 ALA A C     1 
ATOM   13545 O  O     . ALA A 1 3236 ? 146.717 66.999  241.956 1.00 156.88 ? 3236 ALA A O     1 
ATOM   13546 C  CB    . ALA A 1 3236 ? 146.486 70.062  240.721 1.00 156.07 ? 3236 ALA A CB    1 
ATOM   13547 N  N     . ASN A 1 3237 ? 148.541 67.658  240.810 1.00 158.72 ? 3237 ASN A N     1 
ATOM   13548 C  CA    . ASN A 1 3237 ? 148.909 66.288  240.466 1.00 157.45 ? 3237 ASN A CA    1 
ATOM   13549 C  C     . ASN A 1 3237 ? 149.266 65.484  241.709 1.00 156.28 ? 3237 ASN A C     1 
ATOM   13550 O  O     . ASN A 1 3237 ? 148.889 64.312  241.828 1.00 151.84 ? 3237 ASN A O     1 
ATOM   13551 C  CB    . ASN A 1 3237 ? 150.075 66.290  239.477 1.00 151.55 ? 3237 ASN A CB    1 
ATOM   13552 C  CG    . ASN A 1 3237 ? 149.694 66.864  238.127 1.00 150.28 ? 3237 ASN A CG    1 
ATOM   13553 O  OD1   . ASN A 1 3237 ? 148.627 67.460  237.972 1.00 152.70 ? 3237 ASN A OD1   1 
ATOM   13554 N  ND2   . ASN A 1 3237 ? 150.565 66.687  237.142 1.00 144.27 ? 3237 ASN A ND2   1 
ATOM   13555 N  N     . ASP A 1 3238 ? 149.999 66.093  242.645 1.00 158.51 ? 3238 ASP A N     1 
ATOM   13556 C  CA    . ASP A 1 3238 ? 150.371 65.385  243.866 1.00 157.98 ? 3238 ASP A CA    1 
ATOM   13557 C  C     . ASP A 1 3238 ? 149.151 65.077  244.727 1.00 157.02 ? 3238 ASP A C     1 
ATOM   13558 O  O     . ASP A 1 3238 ? 149.048 63.984  245.297 1.00 153.95 ? 3238 ASP A O     1 
ATOM   13559 C  CB    . ASP A 1 3238 ? 151.394 66.203  244.654 1.00 155.08 ? 3238 ASP A CB    1 
ATOM   13560 C  CG    . ASP A 1 3238 ? 152.782 66.138  244.048 1.00 156.62 ? 3238 ASP A CG    1 
ATOM   13561 O  OD1   . ASP A 1 3238 ? 152.959 65.420  243.042 1.00 156.59 ? 3238 ASP A OD1   1 
ATOM   13562 O  OD2   . ASP A 1 3238 ? 153.696 66.804  244.579 1.00 155.48 ? 3238 ASP A OD2   1 
ATOM   13563 N  N     . LYS A 1 3239 ? 148.216 66.023  244.834 1.00 157.11 ? 3239 LYS A N     1 
ATOM   13564 C  CA    . LYS A 1 3239 ? 147.045 65.820  245.679 1.00 153.61 ? 3239 LYS A CA    1 
ATOM   13565 C  C     . LYS A 1 3239 ? 146.038 64.864  245.052 1.00 152.93 ? 3239 LYS A C     1 
ATOM   13566 O  O     . LYS A 1 3239 ? 145.322 64.166  245.779 1.00 151.37 ? 3239 LYS A O     1 
ATOM   13567 C  CB    . LYS A 1 3239 ? 146.380 67.163  245.983 1.00 151.44 ? 3239 LYS A CB    1 
ATOM   13568 C  CG    . LYS A 1 3239 ? 147.080 67.961  247.073 1.00 144.48 ? 3239 LYS A CG    1 
ATOM   13569 C  CD    . LYS A 1 3239 ? 146.164 69.016  247.668 1.00 142.08 ? 3239 LYS A CD    1 
ATOM   13570 C  CE    . LYS A 1 3239 ? 146.882 69.831  248.732 1.00 132.72 ? 3239 LYS A CE    1 
ATOM   13571 N  NZ    . LYS A 1 3239 ? 146.001 70.875  249.326 1.00 125.02 ? 3239 LYS A NZ    1 
ATOM   13572 N  N     . LEU A 1 3240 ? 145.963 64.818  243.719 1.00 153.12 ? 3240 LEU A N     1 
ATOM   13573 C  CA    . LEU A 1 3240 ? 145.043 63.894  243.063 1.00 152.49 ? 3240 LEU A CA    1 
ATOM   13574 C  C     . LEU A 1 3240 ? 145.421 62.442  243.323 1.00 153.00 ? 3240 LEU A C     1 
ATOM   13575 O  O     . LEU A 1 3240 ? 144.550 61.565  243.326 1.00 150.10 ? 3240 LEU A O     1 
ATOM   13576 C  CB    . LEU A 1 3240 ? 145.004 64.168  241.559 1.00 152.56 ? 3240 LEU A CB    1 
ATOM   13577 C  CG    . LEU A 1 3240 ? 144.012 65.227  241.076 1.00 148.10 ? 3240 LEU A CG    1 
ATOM   13578 C  CD1   . LEU A 1 3240 ? 144.335 65.651  239.653 1.00 141.30 ? 3240 LEU A CD1   1 
ATOM   13579 C  CD2   . LEU A 1 3240 ? 142.589 64.700  241.169 1.00 145.80 ? 3240 LEU A CD2   1 
ATOM   13580 N  N     . LYS A 1 3241 ? 146.708 62.168  243.543 1.00 153.69 ? 3241 LYS A N     1 
ATOM   13581 C  CA    . LYS A 1 3241 ? 147.168 60.803  243.765 1.00 151.74 ? 3241 LYS A CA    1 
ATOM   13582 C  C     . LYS A 1 3241 ? 146.738 60.241  245.114 1.00 150.73 ? 3241 LYS A C     1 
ATOM   13583 O  O     . LYS A 1 3241 ? 146.876 59.033  245.332 1.00 146.14 ? 3241 LYS A O     1 
ATOM   13584 C  CB    . LYS A 1 3241 ? 148.691 60.742  243.638 1.00 146.59 ? 3241 LYS A CB    1 
ATOM   13585 C  CG    . LYS A 1 3241 ? 149.189 60.780  242.203 1.00 143.29 ? 3241 LYS A CG    1 
ATOM   13586 C  CD    . LYS A 1 3241 ? 150.578 61.388  242.110 1.00 143.26 ? 3241 LYS A CD    1 
ATOM   13587 C  CE    . LYS A 1 3241 ? 150.909 61.785  240.680 1.00 138.88 ? 3241 LYS A CE    1 
ATOM   13588 N  NZ    . LYS A 1 3241 ? 152.200 62.522  240.590 1.00 134.21 ? 3241 LYS A NZ    1 
ATOM   13589 N  N     . LYS A 1 3242 ? 146.227 61.074  246.015 1.00 149.98 ? 3242 LYS A N     1 
ATOM   13590 C  CA    . LYS A 1 3242 ? 145.766 60.604  247.316 1.00 142.48 ? 3242 LYS A CA    1 
ATOM   13591 C  C     . LYS A 1 3242 ? 144.377 59.984  247.211 1.00 137.65 ? 3242 LYS A C     1 
ATOM   13592 O  O     . LYS A 1 3242 ? 143.640 60.238  246.258 0.00 142.56 ? 3242 LYS A O     1 
ATOM   13593 C  CB    . LYS A 1 3242 ? 145.757 61.749  248.331 1.00 135.59 ? 3242 LYS A CB    1 
ATOM   13594 C  CG    . LYS A 1 3242 ? 147.117 62.054  248.937 1.00 129.23 ? 3242 LYS A CG    1 
ATOM   13595 C  CD    . LYS A 1 3242 ? 147.038 63.218  249.911 1.00 123.38 ? 3242 LYS A CD    1 
ATOM   13596 C  CE    . LYS A 1 3242 ? 148.401 63.535  250.505 1.00 106.36 ? 3242 LYS A CE    1 
ATOM   13597 N  NZ    . LYS A 1 3242 ? 148.395 64.822  251.253 1.00 83.81  ? 3242 LYS A NZ    1 
ATOM   13598 N  N     . GLU A 1 3449 ? 135.850 67.191  245.431 1.00 153.59 ? 3449 GLU A N     1 
ATOM   13599 C  CA    . GLU A 1 3449 ? 135.497 68.528  245.893 1.00 158.19 ? 3449 GLU A CA    1 
ATOM   13600 C  C     . GLU A 1 3449 ? 136.700 69.462  245.834 1.00 161.08 ? 3449 GLU A C     1 
ATOM   13601 O  O     . GLU A 1 3449 ? 136.724 70.411  245.051 1.00 161.44 ? 3449 GLU A O     1 
ATOM   13602 C  CB    . GLU A 1 3449 ? 134.942 68.475  247.318 1.00 156.63 ? 3449 GLU A CB    1 
ATOM   13603 C  CG    . GLU A 1 3449 ? 133.914 67.379  247.547 1.00 149.80 ? 3449 GLU A CG    1 
ATOM   13604 C  CD    . GLU A 1 3449 ? 133.473 67.290  248.994 1.00 145.97 ? 3449 GLU A CD    1 
ATOM   13605 O  OE1   . GLU A 1 3449 ? 133.890 68.150  249.799 1.00 141.87 ? 3449 GLU A OE1   1 
ATOM   13606 O  OE2   . GLU A 1 3449 ? 132.708 66.361  249.328 1.00 147.44 ? 3449 GLU A OE2   1 
ATOM   13607 N  N     . GLU A 1 3450 ? 137.696 69.185  246.680 1.00 158.50 ? 3450 GLU A N     1 
ATOM   13608 C  CA    . GLU A 1 3450 ? 138.902 70.006  246.704 1.00 157.29 ? 3450 GLU A CA    1 
ATOM   13609 C  C     . GLU A 1 3450 ? 139.657 69.920  245.383 1.00 158.29 ? 3450 GLU A C     1 
ATOM   13610 O  O     . GLU A 1 3450 ? 140.026 70.948  244.801 1.00 157.91 ? 3450 GLU A O     1 
ATOM   13611 C  CB    . GLU A 1 3450 ? 139.798 69.575  247.865 1.00 154.37 ? 3450 GLU A CB    1 
ATOM   13612 C  CG    . GLU A 1 3450 ? 140.910 70.553  248.204 1.00 158.35 ? 3450 GLU A CG    1 
ATOM   13613 C  CD    . GLU A 1 3450 ? 141.661 70.165  249.465 1.00 154.40 ? 3450 GLU A CD    1 
ATOM   13614 O  OE1   . GLU A 1 3450 ? 141.304 69.137  250.078 1.00 149.17 ? 3450 GLU A OE1   1 
ATOM   13615 O  OE2   . GLU A 1 3450 ? 142.607 70.888  249.843 1.00 154.00 ? 3450 GLU A OE2   1 
ATOM   13616 N  N     . TYR A 1 3451 ? 139.880 68.700  244.887 1.00 158.02 ? 3451 TYR A N     1 
ATOM   13617 C  CA    . TYR A 1 3451 ? 140.646 68.524  243.657 1.00 156.51 ? 3451 TYR A CA    1 
ATOM   13618 C  C     . TYR A 1 3451 ? 139.963 69.198  242.475 1.00 157.11 ? 3451 TYR A C     1 
ATOM   13619 O  O     . TYR A 1 3451 ? 140.636 69.696  241.565 1.00 157.80 ? 3451 TYR A O     1 
ATOM   13620 C  CB    . TYR A 1 3451 ? 140.862 67.035  243.385 1.00 150.93 ? 3451 TYR A CB    1 
ATOM   13621 C  CG    . TYR A 1 3451 ? 141.334 66.260  244.596 1.00 151.64 ? 3451 TYR A CG    1 
ATOM   13622 C  CD1   . TYR A 1 3451 ? 142.397 66.717  245.365 1.00 151.77 ? 3451 TYR A CD1   1 
ATOM   13623 C  CD2   . TYR A 1 3451 ? 140.719 65.072  244.969 1.00 146.60 ? 3451 TYR A CD2   1 
ATOM   13624 C  CE1   . TYR A 1 3451 ? 142.833 66.014  246.472 1.00 150.31 ? 3451 TYR A CE1   1 
ATOM   13625 C  CE2   . TYR A 1 3451 ? 141.148 64.362  246.075 1.00 146.78 ? 3451 TYR A CE2   1 
ATOM   13626 C  CZ    . TYR A 1 3451 ? 142.205 64.837  246.822 1.00 148.93 ? 3451 TYR A CZ    1 
ATOM   13627 O  OH    . TYR A 1 3451 ? 142.636 64.134  247.924 1.00 139.05 ? 3451 TYR A OH    1 
ATOM   13628 N  N     . ALA A 1 3452 ? 138.628 69.230  242.470 1.00 159.39 ? 3452 ALA A N     1 
ATOM   13629 C  CA    . ALA A 1 3452 ? 137.914 69.962  241.430 1.00 160.48 ? 3452 ALA A CA    1 
ATOM   13630 C  C     . ALA A 1 3452 ? 138.240 71.450  241.486 1.00 165.58 ? 3452 ALA A C     1 
ATOM   13631 O  O     . ALA A 1 3452 ? 138.461 72.086  240.448 1.00 166.24 ? 3452 ALA A O     1 
ATOM   13632 C  CB    . ALA A 1 3452 ? 136.409 69.734  241.564 1.00 153.44 ? 3452 ALA A CB    1 
ATOM   13633 N  N     . VAL A 1 3453 ? 138.287 72.019  242.692 1.00 165.18 ? 3453 VAL A N     1 
ATOM   13634 C  CA    . VAL A 1 3453 ? 138.641 73.429  242.836 1.00 161.65 ? 3453 VAL A CA    1 
ATOM   13635 C  C     . VAL A 1 3453 ? 140.066 73.672  242.357 1.00 161.91 ? 3453 VAL A C     1 
ATOM   13636 O  O     . VAL A 1 3453 ? 140.343 74.655  241.656 1.00 162.82 ? 3453 VAL A O     1 
ATOM   13637 C  CB    . VAL A 1 3453 ? 138.446 73.881  244.295 1.00 156.44 ? 3453 VAL A CB    1 
ATOM   13638 C  CG1   . VAL A 1 3453 ? 138.945 75.306  244.485 1.00 151.40 ? 3453 VAL A CG1   1 
ATOM   13639 C  CG2   . VAL A 1 3453 ? 136.983 73.763  244.693 1.00 153.20 ? 3453 VAL A CG2   1 
ATOM   13640 N  N     . LEU A 1 3454 ? 140.994 72.783  242.725 1.00 160.28 ? 3454 LEU A N     1 
ATOM   13641 C  CA    . LEU A 1 3454 ? 142.383 72.952  242.303 1.00 158.47 ? 3454 LEU A CA    1 
ATOM   13642 C  C     . LEU A 1 3454 ? 142.526 72.872  240.786 1.00 159.44 ? 3454 LEU A C     1 
ATOM   13643 O  O     . LEU A 1 3454 ? 143.245 73.674  240.183 1.00 158.20 ? 3454 LEU A O     1 
ATOM   13644 C  CB    . LEU A 1 3454 ? 143.287 71.925  242.989 1.00 154.96 ? 3454 LEU A CB    1 
ATOM   13645 C  CG    . LEU A 1 3454 ? 143.812 72.262  244.391 1.00 151.81 ? 3454 LEU A CG    1 
ATOM   13646 C  CD1   . LEU A 1 3454 ? 142.740 72.209  245.464 1.00 151.46 ? 3454 LEU A CD1   1 
ATOM   13647 C  CD2   . LEU A 1 3454 ? 144.976 71.346  244.753 1.00 146.52 ? 3454 LEU A CD2   1 
ATOM   13648 N  N     . ILE A 1 3455 ? 141.849 71.914  240.146 1.00 161.41 ? 3455 ILE A N     1 
ATOM   13649 C  CA    . ILE A 1 3455 ? 141.979 71.812  238.693 1.00 162.91 ? 3455 ILE A CA    1 
ATOM   13650 C  C     . ILE A 1 3455 ? 141.305 72.994  238.001 1.00 161.86 ? 3455 ILE A C     1 
ATOM   13651 O  O     . ILE A 1 3455 ? 141.804 73.487  236.979 1.00 160.74 ? 3455 ILE A O     1 
ATOM   13652 C  CB    . ILE A 1 3455 ? 141.446 70.460  238.174 1.00 163.21 ? 3455 ILE A CB    1 
ATOM   13653 C  CG1   . ILE A 1 3455 ? 139.947 70.308  238.437 1.00 160.38 ? 3455 ILE A CG1   1 
ATOM   13654 C  CG2   . ILE A 1 3455 ? 142.233 69.305  238.785 1.00 158.87 ? 3455 ILE A CG2   1 
ATOM   13655 C  CD1   . ILE A 1 3455 ? 139.406 68.928  238.132 1.00 157.78 ? 3455 ILE A CD1   1 
ATOM   13656 N  N     . SER A 1 3456 ? 140.177 73.476  238.534 1.00 163.25 ? 3456 SER A N     1 
ATOM   13657 C  CA    . SER A 1 3456 ? 139.533 74.650  237.952 1.00 163.86 ? 3456 SER A CA    1 
ATOM   13658 C  C     . SER A 1 3456 ? 140.435 75.875  238.053 1.00 161.90 ? 3456 SER A C     1 
ATOM   13659 O  O     . SER A 1 3456 ? 140.573 76.642  237.091 1.00 158.61 ? 3456 SER A O     1 
ATOM   13660 C  CB    . SER A 1 3456 ? 138.192 74.907  238.641 1.00 162.02 ? 3456 SER A CB    1 
ATOM   13661 O  OG    . SER A 1 3456 ? 138.380 75.412  239.952 1.00 159.22 ? 3456 SER A OG    1 
ATOM   13662 N  N     . GLU A 1 3457 ? 141.071 76.069  239.211 1.00 162.04 ? 3457 GLU A N     1 
ATOM   13663 C  CA    . GLU A 1 3457 ? 141.971 77.206  239.362 1.00 159.10 ? 3457 GLU A CA    1 
ATOM   13664 C  C     . GLU A 1 3457 ? 143.223 77.043  238.508 1.00 160.12 ? 3457 GLU A C     1 
ATOM   13665 O  O     . GLU A 1 3457 ? 143.763 78.037  238.013 1.00 156.82 ? 3457 GLU A O     1 
ATOM   13666 C  CB    . GLU A 1 3457 ? 142.326 77.407  240.839 1.00 155.65 ? 3457 GLU A CB    1 
ATOM   13667 C  CG    . GLU A 1 3457 ? 143.522 76.616  241.341 1.00 152.60 ? 3457 GLU A CG    1 
ATOM   13668 C  CD    . GLU A 1 3457 ? 143.646 76.646  242.851 1.00 145.35 ? 3457 GLU A CD    1 
ATOM   13669 O  OE1   . GLU A 1 3457 ? 142.792 77.280  243.506 1.00 141.39 ? 3457 GLU A OE1   1 
ATOM   13670 O  OE2   . GLU A 1 3457 ? 144.596 76.036  243.384 1.00 143.70 ? 3457 GLU A OE2   1 
ATOM   13671 N  N     . ALA A 1 3458 ? 143.683 75.806  238.299 1.00 161.26 ? 3458 ALA A N     1 
ATOM   13672 C  CA    . ALA A 1 3458 ? 144.810 75.579  237.400 1.00 157.73 ? 3458 ALA A CA    1 
ATOM   13673 C  C     . ALA A 1 3458 ? 144.450 75.943  235.965 1.00 157.34 ? 3458 ALA A C     1 
ATOM   13674 O  O     . ALA A 1 3458 ? 145.253 76.559  235.255 1.00 156.09 ? 3458 ALA A O     1 
ATOM   13675 C  CB    . ALA A 1 3458 ? 145.269 74.124  237.489 1.00 153.20 ? 3458 ALA A CB    1 
ATOM   13676 N  N     . GLN A 1 3459 ? 143.247 75.571  235.521 1.00 159.40 ? 3459 GLN A N     1 
ATOM   13677 C  CA    . GLN A 1 3459 ? 142.808 75.951  234.181 1.00 155.19 ? 3459 GLN A CA    1 
ATOM   13678 C  C     . GLN A 1 3459 ? 142.652 77.464  234.060 1.00 154.50 ? 3459 GLN A C     1 
ATOM   13679 O  O     . GLN A 1 3459 ? 142.976 78.049  233.017 1.00 153.66 ? 3459 GLN A O     1 
ATOM   13680 C  CB    . GLN A 1 3459 ? 141.499 75.242  233.835 1.00 155.81 ? 3459 GLN A CB    1 
ATOM   13681 C  CG    . GLN A 1 3459 ? 141.143 75.286  232.357 1.00 150.64 ? 3459 GLN A CG    1 
ATOM   13682 C  CD    . GLN A 1 3459 ? 139.875 74.518  232.040 1.00 149.88 ? 3459 GLN A CD    1 
ATOM   13683 O  OE1   . GLN A 1 3459 ? 139.742 73.345  232.389 1.00 149.55 ? 3459 GLN A OE1   1 
ATOM   13684 N  NE2   . GLN A 1 3459 ? 138.934 75.179  231.375 1.00 144.80 ? 3459 GLN A NE2   1 
ATOM   13685 N  N     . ALA A 1 3460 ? 142.154 78.113  235.116 1.00 155.81 ? 3460 ALA A N     1 
ATOM   13686 C  CA    . ALA A 1 3460 ? 142.056 79.570  235.105 1.00 153.22 ? 3460 ALA A CA    1 
ATOM   13687 C  C     . ALA A 1 3460 ? 143.433 80.215  235.001 1.00 151.58 ? 3460 ALA A C     1 
ATOM   13688 O  O     . ALA A 1 3460 ? 143.617 81.196  234.269 1.00 150.78 ? 3460 ALA A O     1 
ATOM   13689 C  CB    . ALA A 1 3460 ? 141.327 80.057  236.358 1.00 150.51 ? 3460 ALA A CB    1 
ATOM   13690 N  N     . ILE A 1 3461 ? 144.415 79.677  235.728 1.00 151.51 ? 3461 ILE A N     1 
ATOM   13691 C  CA    . ILE A 1 3461 ? 145.779 80.193  235.643 1.00 151.16 ? 3461 ILE A CA    1 
ATOM   13692 C  C     . ILE A 1 3461 ? 146.348 79.964  234.248 1.00 149.84 ? 3461 ILE A C     1 
ATOM   13693 O  O     . ILE A 1 3461 ? 147.079 80.807  233.716 1.00 148.47 ? 3461 ILE A O     1 
ATOM   13694 C  CB    . ILE A 1 3461 ? 146.661 79.556  236.734 1.00 147.90 ? 3461 ILE A CB    1 
ATOM   13695 C  CG1   . ILE A 1 3461 ? 146.210 80.015  238.122 1.00 144.15 ? 3461 ILE A CG1   1 
ATOM   13696 C  CG2   . ILE A 1 3461 ? 148.121 79.917  236.527 1.00 146.22 ? 3461 ILE A CG2   1 
ATOM   13697 C  CD1   . ILE A 1 3461 ? 146.229 81.516  238.305 1.00 140.74 ? 3461 ILE A CD1   1 
ATOM   13698 N  N     . LYS A 1 3462 ? 146.024 78.824  233.634 1.00 150.63 ? 3462 LYS A N     1 
ATOM   13699 C  CA    . LYS A 1 3462 ? 146.469 78.564  232.267 1.00 147.63 ? 3462 LYS A CA    1 
ATOM   13700 C  C     . LYS A 1 3462 ? 145.900 79.596  231.299 1.00 148.20 ? 3462 LYS A C     1 
ATOM   13701 O  O     . LYS A 1 3462 ? 146.615 80.117  230.434 1.00 145.61 ? 3462 LYS A O     1 
ATOM   13702 C  CB    . LYS A 1 3462 ? 146.063 77.152  231.840 1.00 145.61 ? 3462 LYS A CB    1 
ATOM   13703 C  CG    . LYS A 1 3462 ? 146.886 76.042  232.468 1.00 146.52 ? 3462 LYS A CG    1 
ATOM   13704 C  CD    . LYS A 1 3462 ? 146.222 74.688  232.280 1.00 144.22 ? 3462 LYS A CD    1 
ATOM   13705 C  CE    . LYS A 1 3462 ? 146.957 73.601  233.047 1.00 146.21 ? 3462 LYS A CE    1 
ATOM   13706 N  NZ    . LYS A 1 3462 ? 146.918 73.834  234.517 1.00 149.98 ? 3462 LYS A NZ    1 
ATOM   13707 N  N     . ALA A 1 3463 ? 144.606 79.898  231.430 1.00 151.95 ? 3463 ALA A N     1 
ATOM   13708 C  CA    . ALA A 1 3463 ? 143.990 80.903  230.566 1.00 149.06 ? 3463 ALA A CA    1 
ATOM   13709 C  C     . ALA A 1 3463 ? 144.605 82.280  230.792 1.00 150.79 ? 3463 ALA A C     1 
ATOM   13710 O  O     . ALA A 1 3463 ? 144.857 83.027  229.835 1.00 150.00 ? 3463 ALA A O     1 
ATOM   13711 C  CB    . ALA A 1 3463 ? 142.480 80.942  230.800 1.00 137.36 ? 3463 ALA A CB    1 
ATOM   13712 N  N     . ASP A 1 3464 ? 144.853 82.633  232.056 1.00 148.71 ? 3464 ASP A N     1 
ATOM   13713 C  CA    . ASP A 1 3464 ? 145.480 83.916  232.357 1.00 148.12 ? 3464 ASP A CA    1 
ATOM   13714 C  C     . ASP A 1 3464 ? 146.882 83.994  231.766 1.00 148.21 ? 3464 ASP A C     1 
ATOM   13715 O  O     . ASP A 1 3464 ? 147.282 85.034  231.232 1.00 146.47 ? 3464 ASP A O     1 
ATOM   13716 C  CB    . ASP A 1 3464 ? 145.518 84.139  233.869 1.00 146.55 ? 3464 ASP A CB    1 
ATOM   13717 C  CG    . ASP A 1 3464 ? 145.704 85.597  234.239 1.00 143.69 ? 3464 ASP A CG    1 
ATOM   13718 O  OD1   . ASP A 1 3464 ? 145.609 86.458  233.339 1.00 143.55 ? 3464 ASP A OD1   1 
ATOM   13719 O  OD2   . ASP A 1 3464 ? 145.946 85.883  235.431 1.00 138.74 ? 3464 ASP A OD2   1 
ATOM   13720 N  N     . LEU A 1 3465 ? 147.643 82.900  231.851 1.00 147.09 ? 3465 LEU A N     1 
ATOM   13721 C  CA    . LEU A 1 3465 ? 148.981 82.869  231.270 1.00 145.17 ? 3465 LEU A CA    1 
ATOM   13722 C  C     . LEU A 1 3465 ? 148.925 82.998  229.754 1.00 146.55 ? 3465 LEU A C     1 
ATOM   13723 O  O     . LEU A 1 3465 ? 149.776 83.662  229.149 1.00 143.88 ? 3465 LEU A O     1 
ATOM   13724 C  CB    . LEU A 1 3465 ? 149.693 81.577  231.671 1.00 140.83 ? 3465 LEU A CB    1 
ATOM   13725 C  CG    . LEU A 1 3465 ? 151.142 81.435  231.207 1.00 137.15 ? 3465 LEU A CG    1 
ATOM   13726 C  CD1   . LEU A 1 3465 ? 151.998 82.508  231.853 1.00 142.20 ? 3465 LEU A CD1   1 
ATOM   13727 C  CD2   . LEU A 1 3465 ? 151.687 80.051  231.515 1.00 133.17 ? 3465 LEU A CD2   1 
ATOM   13728 N  N     . ALA A 1 3466 ? 147.941 82.354  229.122 1.00 147.70 ? 3466 ALA A N     1 
ATOM   13729 C  CA    . ALA A 1 3466 ? 147.777 82.484  227.678 1.00 143.35 ? 3466 ALA A CA    1 
ATOM   13730 C  C     . ALA A 1 3466 ? 147.493 83.930  227.291 1.00 142.60 ? 3466 ALA A C     1 
ATOM   13731 O  O     . ALA A 1 3466 ? 148.083 84.459  226.341 1.00 139.63 ? 3466 ALA A O     1 
ATOM   13732 C  CB    . ALA A 1 3466 ? 146.658 81.563  227.192 1.00 135.08 ? 3466 ALA A CB    1 
ATOM   13733 N  N     . ALA A 1 3467 ? 146.599 84.591  228.030 1.00 142.79 ? 3467 ALA A N     1 
ATOM   13734 C  CA    . ALA A 1 3467 ? 146.317 85.998  227.754 1.00 139.38 ? 3467 ALA A CA    1 
ATOM   13735 C  C     . ALA A 1 3467 ? 147.553 86.864  227.974 1.00 140.31 ? 3467 ALA A C     1 
ATOM   13736 O  O     . ALA A 1 3467 ? 147.819 87.797  227.202 1.00 136.77 ? 3467 ALA A O     1 
ATOM   13737 C  CB    . ALA A 1 3467 ? 145.158 86.482  228.624 1.00 134.83 ? 3467 ALA A CB    1 
ATOM   13738 N  N     . VAL A 1 3468 ? 148.320 86.568  229.026 1.00 143.36 ? 3468 VAL A N     1 
ATOM   13739 C  CA    . VAL A 1 3468 ? 149.514 87.351  229.332 1.00 141.73 ? 3468 VAL A CA    1 
ATOM   13740 C  C     . VAL A 1 3468 ? 150.535 87.226  228.209 1.00 138.20 ? 3468 VAL A C     1 
ATOM   13741 O  O     . VAL A 1 3468 ? 151.087 88.225  227.738 1.00 135.89 ? 3468 VAL A O     1 
ATOM   13742 C  CB    . VAL A 1 3468 ? 150.106 86.922  230.687 1.00 139.33 ? 3468 VAL A CB    1 
ATOM   13743 C  CG1   . VAL A 1 3468 ? 151.560 87.356  230.796 1.00 135.73 ? 3468 VAL A CG1   1 
ATOM   13744 C  CG2   . VAL A 1 3468 ? 149.288 87.505  231.828 1.00 139.52 ? 3468 VAL A CG2   1 
ATOM   13745 N  N     . GLU A 1 3469 ? 150.798 85.998  227.754 1.00 138.07 ? 3469 GLU A N     1 
ATOM   13746 C  CA    . GLU A 1 3469 ? 151.760 85.829  226.670 1.00 137.31 ? 3469 GLU A CA    1 
ATOM   13747 C  C     . GLU A 1 3469 ? 151.241 86.425  225.367 1.00 136.02 ? 3469 GLU A C     1 
ATOM   13748 O  O     . GLU A 1 3469 ? 152.030 86.956  224.573 1.00 134.89 ? 3469 GLU A O     1 
ATOM   13749 C  CB    . GLU A 1 3469 ? 152.122 84.351  226.492 1.00 140.10 ? 3469 GLU A CB    1 
ATOM   13750 C  CG    . GLU A 1 3469 ? 151.005 83.460  225.981 1.00 142.76 ? 3469 GLU A CG    1 
ATOM   13751 C  CD    . GLU A 1 3469 ? 151.357 81.987  226.056 1.00 142.40 ? 3469 GLU A CD    1 
ATOM   13752 O  OE1   . GLU A 1 3469 ? 152.392 81.593  225.479 1.00 145.06 ? 3469 GLU A OE1   1 
ATOM   13753 O  OE2   . GLU A 1 3469 ? 150.602 81.223  226.692 1.00 138.81 ? 3469 GLU A OE2   1 
ATOM   13754 N  N     . ALA A 1 3470 ? 149.923 86.377  225.142 1.00 136.32 ? 3470 ALA A N     1 
ATOM   13755 C  CA    . ALA A 1 3470 ? 149.351 87.011  223.960 1.00 134.97 ? 3470 ALA A CA    1 
ATOM   13756 C  C     . ALA A 1 3470 ? 149.630 88.508  223.956 1.00 132.77 ? 3470 ALA A C     1 
ATOM   13757 O  O     . ALA A 1 3470 ? 150.126 89.059  222.963 1.00 129.91 ? 3470 ALA A O     1 
ATOM   13758 C  CB    . ALA A 1 3470 ? 147.848 86.738  223.893 1.00 129.58 ? 3470 ALA A CB    1 
ATOM   13759 N  N     . LYS A 1 3471 ? 149.334 89.184  225.070 1.00 132.69 ? 3471 LYS A N     1 
ATOM   13760 C  CA    . LYS A 1 3471 ? 149.584 90.621  225.120 1.00 132.71 ? 3471 LYS A CA    1 
ATOM   13761 C  C     . LYS A 1 3471 ? 151.073 90.948  225.110 1.00 131.30 ? 3471 LYS A C     1 
ATOM   13762 O  O     . LYS A 1 3471 ? 151.459 91.978  224.546 1.00 131.32 ? 3471 LYS A O     1 
ATOM   13763 C  CB    . LYS A 1 3471 ? 148.904 91.254  226.340 1.00 131.71 ? 3471 LYS A CB    1 
ATOM   13764 C  CG    . LYS A 1 3471 ? 149.427 90.809  227.691 1.00 132.44 ? 3471 LYS A CG    1 
ATOM   13765 C  CD    . LYS A 1 3471 ? 148.734 91.561  228.819 1.00 130.48 ? 3471 LYS A CD    1 
ATOM   13766 C  CE    . LYS A 1 3471 ? 147.287 91.123  228.980 1.00 130.34 ? 3471 LYS A CE    1 
ATOM   13767 N  NZ    . LYS A 1 3471 ? 147.170 89.712  229.438 1.00 133.38 ? 3471 LYS A NZ    1 
ATOM   13768 N  N     . VAL A 1 3472 ? 151.920 90.091  225.689 1.00 130.74 ? 3472 VAL A N     1 
ATOM   13769 C  CA    . VAL A 1 3472 ? 153.362 90.329  225.642 1.00 129.00 ? 3472 VAL A CA    1 
ATOM   13770 C  C     . VAL A 1 3472 ? 153.867 90.283  224.205 1.00 126.63 ? 3472 VAL A C     1 
ATOM   13771 O  O     . VAL A 1 3472 ? 154.629 91.155  223.773 1.00 123.05 ? 3472 VAL A O     1 
ATOM   13772 C  CB    . VAL A 1 3472 ? 154.112 89.326  226.537 1.00 128.26 ? 3472 VAL A CB    1 
ATOM   13773 C  CG1   . VAL A 1 3472 ? 155.608 89.457  226.327 1.00 122.75 ? 3472 VAL A CG1   1 
ATOM   13774 C  CG2   . VAL A 1 3472 ? 153.793 89.588  227.997 1.00 132.31 ? 3472 VAL A CG2   1 
ATOM   13775 N  N     . ASN A 1 3473 ? 153.450 89.271  223.437 1.00 130.35 ? 3473 ASN A N     1 
ATOM   13776 C  CA    . ASN A 1 3473 ? 153.921 89.204  222.056 1.00 128.36 ? 3473 ASN A CA    1 
ATOM   13777 C  C     . ASN A 1 3473 ? 153.310 90.310  221.201 1.00 125.80 ? 3473 ASN A C     1 
ATOM   13778 O  O     . ASN A 1 3473 ? 153.973 90.820  220.290 1.00 120.12 ? 3473 ASN A O     1 
ATOM   13779 C  CB    . ASN A 1 3473 ? 153.656 87.820  221.450 1.00 126.88 ? 3473 ASN A CB    1 
ATOM   13780 C  CG    . ASN A 1 3473 ? 152.193 87.569  221.137 1.00 125.55 ? 3473 ASN A CG    1 
ATOM   13781 O  OD1   . ASN A 1 3473 ? 151.601 88.213  220.270 1.00 124.96 ? 3473 ASN A OD1   1 
ATOM   13782 N  ND2   . ASN A 1 3473 ? 151.614 86.591  221.818 1.00 124.98 ? 3473 ASN A ND2   1 
ATOM   13783 N  N     . ARG A 1 3474 ? 152.067 90.712  221.486 1.00 127.63 ? 3474 ARG A N     1 
ATOM   13784 C  CA    . ARG A 1 3474 ? 151.486 91.844  220.771 1.00 124.32 ? 3474 ARG A CA    1 
ATOM   13785 C  C     . ARG A 1 3474 ? 152.279 93.122  221.026 1.00 126.64 ? 3474 ARG A C     1 
ATOM   13786 O  O     . ARG A 1 3474 ? 152.582 93.877  220.092 1.00 126.10 ? 3474 ARG A O     1 
ATOM   13787 C  CB    . ARG A 1 3474 ? 150.025 92.026  221.183 1.00 114.95 ? 3474 ARG A CB    1 
ATOM   13788 C  CG    . ARG A 1 3474 ? 149.182 92.793  220.180 1.00 114.15 ? 3474 ARG A CG    1 
ATOM   13789 C  CD    . ARG A 1 3474 ? 147.795 93.077  220.735 1.00 111.04 ? 3474 ARG A CD    1 
ATOM   13790 N  NE    . ARG A 1 3474 ? 146.982 93.855  219.807 1.00 109.09 ? 3474 ARG A NE    1 
ATOM   13791 C  CZ    . ARG A 1 3474 ? 146.335 93.345  218.769 1.00 109.43 ? 3474 ARG A CZ    1 
ATOM   13792 N  NH1   . ARG A 1 3474 ? 146.377 92.051  218.495 1.00 106.16 ? 3474 ARG A NH1   1 
ATOM   13793 N  NH2   . ARG A 1 3474 ? 145.626 94.153  217.985 1.00 111.85 ? 3474 ARG A NH2   1 
ATOM   13794 N  N     . SER A 1 3475 ? 152.642 93.370  222.286 1.00 127.27 ? 3475 SER A N     1 
ATOM   13795 C  CA    . SER A 1 3475 ? 153.420 94.560  222.613 1.00 123.70 ? 3475 SER A CA    1 
ATOM   13796 C  C     . SER A 1 3475 ? 154.825 94.483  222.027 1.00 122.18 ? 3475 SER A C     1 
ATOM   13797 O  O     . SER A 1 3475 ? 155.393 95.506  221.628 1.00 121.56 ? 3475 SER A O     1 
ATOM   13798 C  CB    . SER A 1 3475 ? 153.471 94.744  224.127 1.00 127.73 ? 3475 SER A CB    1 
ATOM   13799 O  OG    . SER A 1 3475 ? 153.856 93.544  224.774 1.00 131.80 ? 3475 SER A OG    1 
ATOM   13800 N  N     . THR A 1 3476 ? 155.407 93.282  221.975 1.00 120.44 ? 3476 THR A N     1 
ATOM   13801 C  CA    . THR A 1 3476 ? 156.708 93.123  221.333 1.00 123.72 ? 3476 THR A CA    1 
ATOM   13802 C  C     . THR A 1 3476 ? 156.630 93.442  219.845 1.00 123.73 ? 3476 THR A C     1 
ATOM   13803 O  O     . THR A 1 3476 ? 157.528 94.090  219.291 1.00 123.14 ? 3476 THR A O     1 
ATOM   13804 C  CB    . THR A 1 3476 ? 157.233 91.703  221.548 1.00 123.81 ? 3476 THR A CB    1 
ATOM   13805 O  OG1   . THR A 1 3476 ? 157.045 91.323  222.917 1.00 125.13 ? 3476 THR A OG1   1 
ATOM   13806 C  CG2   . THR A 1 3476 ? 158.713 91.625  221.204 1.00 117.52 ? 3476 THR A CG2   1 
ATOM   13807 N  N     . ALA A 1 3477 ? 155.564 92.989  219.179 1.00 122.13 ? 3477 ALA A N     1 
ATOM   13808 C  CA    . ALA A 1 3477 ? 155.365 93.338  217.776 1.00 119.66 ? 3477 ALA A CA    1 
ATOM   13809 C  C     . ALA A 1 3477 ? 155.214 94.844  217.605 1.00 118.94 ? 3477 ALA A C     1 
ATOM   13810 O  O     . ALA A 1 3477 ? 155.756 95.428  216.660 1.00 117.46 ? 3477 ALA A O     1 
ATOM   13811 C  CB    . ALA A 1 3477 ? 154.144 92.606  217.220 1.00 119.05 ? 3477 ALA A CB    1 
ATOM   13812 N  N     . LEU A 1 3478 ? 154.483 95.488  218.518 1.00 119.45 ? 3478 LEU A N     1 
ATOM   13813 C  CA    . LEU A 1 3478 ? 154.366 96.944  218.482 1.00 114.18 ? 3478 LEU A CA    1 
ATOM   13814 C  C     . LEU A 1 3478 ? 155.727 97.616  218.620 1.00 113.29 ? 3478 LEU A C     1 
ATOM   13815 O  O     . LEU A 1 3478 ? 156.027 98.581  217.907 1.00 116.05 ? 3478 LEU A O     1 
ATOM   13816 C  CB    . LEU A 1 3478 ? 153.431 97.417  219.592 1.00 116.57 ? 3478 LEU A CB    1 
ATOM   13817 C  CG    . LEU A 1 3478 ? 151.970 97.005  219.464 1.00 120.66 ? 3478 LEU A CG    1 
ATOM   13818 C  CD1   . LEU A 1 3478 ? 151.223 97.415  220.703 1.00 117.89 ? 3478 LEU A CD1   1 
ATOM   13819 C  CD2   . LEU A 1 3478 ? 151.360 97.668  218.246 1.00 121.64 ? 3478 LEU A CD2   1 
ATOM   13820 N  N     . LEU A 1 3479 ? 156.558 97.127  219.543 1.00 114.42 ? 3479 LEU A N     1 
ATOM   13821 C  CA    . LEU A 1 3479 ? 157.876 97.722  219.741 1.00 114.59 ? 3479 LEU A CA    1 
ATOM   13822 C  C     . LEU A 1 3479 ? 158.754 97.554  218.508 1.00 113.08 ? 3479 LEU A C     1 
ATOM   13823 O  O     . LEU A 1 3479 ? 159.453 98.490  218.104 1.00 107.95 ? 3479 LEU A O     1 
ATOM   13824 C  CB    . LEU A 1 3479 ? 158.556 97.114  220.965 1.00 116.21 ? 3479 LEU A CB    1 
ATOM   13825 C  CG    . LEU A 1 3479 ? 158.017 97.546  222.327 1.00 119.50 ? 3479 LEU A CG    1 
ATOM   13826 C  CD1   . LEU A 1 3479 ? 158.976 97.112  223.412 1.00 121.73 ? 3479 LEU A CD1   1 
ATOM   13827 C  CD2   . LEU A 1 3479 ? 157.800 99.049  222.374 1.00 114.10 ? 3479 LEU A CD2   1 
ATOM   13828 N  N     . LYS A 1 3480 ? 158.739 96.366  217.900 1.00 116.10 ? 3480 LYS A N     1 
ATOM   13829 C  CA    . LYS A 1 3480 ? 159.526 96.167  216.687 1.00 116.15 ? 3480 LYS A CA    1 
ATOM   13830 C  C     . LYS A 1 3480 ? 158.984 96.966  215.511 1.00 114.03 ? 3480 LYS A C     1 
ATOM   13831 O  O     . LYS A 1 3480 ? 159.755 97.322  214.613 1.00 111.74 ? 3480 LYS A O     1 
ATOM   13832 C  CB    . LYS A 1 3480 ? 159.603 94.679  216.323 1.00 119.01 ? 3480 LYS A CB    1 
ATOM   13833 C  CG    . LYS A 1 3480 ? 159.985 93.726  217.465 1.00 119.76 ? 3480 LYS A CG    1 
ATOM   13834 C  CD    . LYS A 1 3480 ? 161.127 94.224  218.365 1.00 114.18 ? 3480 LYS A CD    1 
ATOM   13835 C  CE    . LYS A 1 3480 ? 162.385 94.606  217.582 1.00 107.49 ? 3480 LYS A CE    1 
ATOM   13836 N  NZ    . LYS A 1 3480 ? 163.035 93.422  216.955 1.00 99.96  ? 3480 LYS A NZ    1 
ATOM   13837 N  N     . SER A 1 3481 ? 157.682 97.256  215.492 1.00 113.52 ? 3481 SER A N     1 
ATOM   13838 C  CA    . SER A 1 3481 ? 157.141 98.128  214.454 1.00 110.02 ? 3481 SER A CA    1 
ATOM   13839 C  C     . SER A 1 3481 ? 157.560 99.576  214.679 1.00 109.22 ? 3481 SER A C     1 
ATOM   13840 O  O     . SER A 1 3481 ? 157.827 100.308 213.719 1.00 106.02 ? 3481 SER A O     1 
ATOM   13841 C  CB    . SER A 1 3481 ? 155.618 98.009  214.411 1.00 106.39 ? 3481 SER A CB    1 
ATOM   13842 O  OG    . SER A 1 3481 ? 155.214 96.654  214.312 1.00 110.28 ? 3481 SER A OG    1 
ATOM   13843 N  N     . LEU A 1 3482 ? 157.623 100.003 215.937 1.00 110.74 ? 3482 LEU A N     1 
ATOM   13844 C  CA    . LEU A 1 3482 ? 157.974 101.374 216.284 1.00 103.95 ? 3482 LEU A CA    1 
ATOM   13845 C  C     . LEU A 1 3482 ? 159.476 101.596 216.414 1.00 106.02 ? 3482 LEU A C     1 
ATOM   13846 O  O     . LEU A 1 3482 ? 159.897 102.727 216.678 1.00 105.51 ? 3482 LEU A O     1 
ATOM   13847 C  CB    . LEU A 1 3482 ? 157.287 101.775 217.595 1.00 99.58  ? 3482 LEU A CB    1 
ATOM   13848 C  CG    . LEU A 1 3482 ? 155.763 101.912 217.571 1.00 95.35  ? 3482 LEU A CG    1 
ATOM   13849 C  CD1   . LEU A 1 3482 ? 155.224 102.141 218.975 1.00 83.74  ? 3482 LEU A CD1   1 
ATOM   13850 C  CD2   . LEU A 1 3482 ? 155.333 103.032 216.640 1.00 99.64  ? 3482 LEU A CD2   1 
ATOM   13851 N  N     . SER A 1 3483 ? 160.289 100.549 216.247 1.00 111.25 ? 3483 SER A N     1 
ATOM   13852 C  CA    . SER A 1 3483 ? 161.729 100.683 216.456 1.00 111.90 ? 3483 SER A CA    1 
ATOM   13853 C  C     . SER A 1 3483 ? 162.355 101.664 215.472 1.00 112.79 ? 3483 SER A C     1 
ATOM   13854 O  O     . SER A 1 3483 ? 163.200 102.482 215.856 1.00 113.13 ? 3483 SER A O     1 
ATOM   13855 C  CB    . SER A 1 3483 ? 162.402 99.316  216.348 1.00 112.22 ? 3483 SER A CB    1 
ATOM   13856 O  OG    . SER A 1 3483 ? 163.809 99.432  216.472 1.00 111.34 ? 3483 SER A OG    1 
ATOM   13857 N  N     . ALA A 1 3484 ? 161.966 101.592 214.196 1.00 112.01 ? 3484 ALA A N     1 
ATOM   13858 C  CA    . ALA A 1 3484 ? 162.526 102.505 213.203 1.00 108.99 ? 3484 ALA A CA    1 
ATOM   13859 C  C     . ALA A 1 3484 ? 162.158 103.951 213.514 1.00 106.57 ? 3484 ALA A C     1 
ATOM   13860 O  O     . ALA A 1 3484 ? 163.000 104.853 213.413 1.00 102.58 ? 3484 ALA A O     1 
ATOM   13861 C  CB    . ALA A 1 3484 ? 162.049 102.117 211.804 1.00 104.47 ? 3484 ALA A CB    1 
ATOM   13862 N  N     . GLU A 1 3485 ? 160.901 104.189 213.896 1.00 104.55 ? 3485 GLU A N     1 
ATOM   13863 C  CA    . GLU A 1 3485 ? 160.485 105.535 214.273 1.00 97.39  ? 3485 GLU A CA    1 
ATOM   13864 C  C     . GLU A 1 3485 ? 161.238 106.013 215.506 1.00 100.33 ? 3485 GLU A C     1 
ATOM   13865 O  O     . GLU A 1 3485 ? 161.582 107.195 215.610 1.00 104.66 ? 3485 GLU A O     1 
ATOM   13866 C  CB    . GLU A 1 3485 ? 158.977 105.572 214.512 1.00 95.16  ? 3485 GLU A CB    1 
ATOM   13867 C  CG    . GLU A 1 3485 ? 158.152 105.347 213.257 1.00 105.31 ? 3485 GLU A CG    1 
ATOM   13868 C  CD    . GLU A 1 3485 ? 156.663 105.378 213.528 1.00 108.53 ? 3485 GLU A CD    1 
ATOM   13869 O  OE1   . GLU A 1 3485 ? 156.277 105.451 214.713 1.00 107.98 ? 3485 GLU A OE1   1 
ATOM   13870 O  OE2   . GLU A 1 3485 ? 155.879 105.333 212.557 1.00 107.10 ? 3485 GLU A OE2   1 
ATOM   13871 N  N     . ARG A 1 3486 ? 161.500 105.109 216.452 1.00 103.05 ? 3486 ARG A N     1 
ATOM   13872 C  CA    . ARG A 1 3486 ? 162.306 105.458 217.618 1.00 102.83 ? 3486 ARG A CA    1 
ATOM   13873 C  C     . ARG A 1 3486 ? 163.678 105.974 217.203 1.00 100.42 ? 3486 ARG A C     1 
ATOM   13874 O  O     . ARG A 1 3486 ? 164.119 107.039 217.653 1.00 103.09 ? 3486 ARG A O     1 
ATOM   13875 C  CB    . ARG A 1 3486 ? 162.446 104.241 218.533 1.00 101.32 ? 3486 ARG A CB    1 
ATOM   13876 C  CG    . ARG A 1 3486 ? 163.139 104.517 219.855 1.00 96.74  ? 3486 ARG A CG    1 
ATOM   13877 C  CD    . ARG A 1 3486 ? 163.000 103.329 220.793 1.00 94.46  ? 3486 ARG A CD    1 
ATOM   13878 N  NE    . ARG A 1 3486 ? 162.946 103.732 222.193 1.00 100.13 ? 3486 ARG A NE    1 
ATOM   13879 C  CZ    . ARG A 1 3486 ? 163.016 102.891 223.215 1.00 107.12 ? 3486 ARG A CZ    1 
ATOM   13880 N  NH1   . ARG A 1 3486 ? 163.141 101.587 223.031 1.00 107.37 ? 3486 ARG A NH1   1 
ATOM   13881 N  NH2   . ARG A 1 3486 ? 162.958 103.371 224.455 1.00 108.24 ? 3486 ARG A NH2   1 
ATOM   13882 N  N     . GLU A 1 3487 ? 164.366 105.227 216.337 1.00 99.84  ? 3487 GLU A N     1 
ATOM   13883 C  CA    . GLU A 1 3487 ? 165.703 105.622 215.906 1.00 100.45 ? 3487 GLU A CA    1 
ATOM   13884 C  C     . GLU A 1 3487 ? 165.669 106.939 215.143 1.00 99.60  ? 3487 GLU A C     1 
ATOM   13885 O  O     . GLU A 1 3487 ? 166.521 107.812 215.350 1.00 100.17 ? 3487 GLU A O     1 
ATOM   13886 C  CB    . GLU A 1 3487 ? 166.323 104.518 215.049 1.00 102.68 ? 3487 GLU A CB    1 
ATOM   13887 C  CG    . GLU A 1 3487 ? 166.500 103.194 215.775 1.00 105.60 ? 3487 GLU A CG    1 
ATOM   13888 C  CD    . GLU A 1 3487 ? 167.228 103.346 217.096 1.00 108.20 ? 3487 GLU A CD    1 
ATOM   13889 O  OE1   . GLU A 1 3487 ? 168.456 103.570 217.077 1.00 110.32 ? 3487 GLU A OE1   1 
ATOM   13890 O  OE2   . GLU A 1 3487 ? 166.571 103.240 218.154 1.00 103.69 ? 3487 GLU A OE2   1 
ATOM   13891 N  N     . ARG A 1 3488 ? 164.688 107.104 214.252 1.00 97.06  ? 3488 ARG A N     1 
ATOM   13892 C  CA    . ARG A 1 3488 ? 164.618 108.332 213.465 1.00 96.33  ? 3488 ARG A CA    1 
ATOM   13893 C  C     . ARG A 1 3488 ? 164.314 109.543 214.341 1.00 97.99  ? 3488 ARG A C     1 
ATOM   13894 O  O     . ARG A 1 3488 ? 164.909 110.613 214.156 1.00 97.40  ? 3488 ARG A O     1 
ATOM   13895 C  CB    . ARG A 1 3488 ? 163.579 108.183 212.354 1.00 93.62  ? 3488 ARG A CB    1 
ATOM   13896 C  CG    . ARG A 1 3488 ? 163.511 109.372 211.411 1.00 93.02  ? 3488 ARG A CG    1 
ATOM   13897 C  CD    . ARG A 1 3488 ? 162.493 109.143 210.307 1.00 95.54  ? 3488 ARG A CD    1 
ATOM   13898 N  NE    . ARG A 1 3488 ? 162.881 108.035 209.443 1.00 111.61 ? 3488 ARG A NE    1 
ATOM   13899 C  CZ    . ARG A 1 3488 ? 162.231 106.882 209.360 1.00 114.38 ? 3488 ARG A CZ    1 
ATOM   13900 N  NH1   . ARG A 1 3488 ? 161.142 106.650 210.074 1.00 110.34 ? 3488 ARG A NH1   1 
ATOM   13901 N  NH2   . ARG A 1 3488 ? 162.685 105.939 208.539 1.00 122.44 ? 3488 ARG A NH2   1 
ATOM   13902 N  N     . TRP A 1 3489 ? 163.399 109.399 215.303 1.00 97.22  ? 3489 TRP A N     1 
ATOM   13903 C  CA    . TRP A 1 3489 ? 163.096 110.503 216.208 1.00 90.63  ? 3489 TRP A CA    1 
ATOM   13904 C  C     . TRP A 1 3489 ? 164.290 110.839 217.090 1.00 94.29  ? 3489 TRP A C     1 
ATOM   13905 O  O     . TRP A 1 3489 ? 164.557 112.017 217.356 1.00 101.12 ? 3489 TRP A O     1 
ATOM   13906 C  CB    . TRP A 1 3489 ? 161.873 110.168 217.061 1.00 85.90  ? 3489 TRP A CB    1 
ATOM   13907 C  CG    . TRP A 1 3489 ? 160.617 110.005 216.264 1.00 89.59  ? 3489 TRP A CG    1 
ATOM   13908 C  CD1   . TRP A 1 3489 ? 160.376 110.481 215.008 1.00 89.20  ? 3489 TRP A CD1   1 
ATOM   13909 C  CD2   . TRP A 1 3489 ? 159.425 109.321 216.669 1.00 97.79  ? 3489 TRP A CD2   1 
ATOM   13910 N  NE1   . TRP A 1 3489 ? 159.110 110.133 214.605 1.00 96.02  ? 3489 TRP A NE1   1 
ATOM   13911 C  CE2   . TRP A 1 3489 ? 158.505 109.421 215.607 1.00 98.67  ? 3489 TRP A CE2   1 
ATOM   13912 C  CE3   . TRP A 1 3489 ? 159.048 108.633 217.826 1.00 99.63  ? 3489 TRP A CE3   1 
ATOM   13913 C  CZ2   . TRP A 1 3489 ? 157.232 108.860 215.668 1.00 97.64  ? 3489 TRP A CZ2   1 
ATOM   13914 C  CZ3   . TRP A 1 3489 ? 157.783 108.076 217.884 1.00 97.27  ? 3489 TRP A CZ3   1 
ATOM   13915 C  CH2   . TRP A 1 3489 ? 156.891 108.193 216.812 1.00 96.18  ? 3489 TRP A CH2   1 
ATOM   13916 N  N     . GLU A 1 3490 ? 165.019 109.823 217.559 1.00 93.85  ? 3490 GLU A N     1 
ATOM   13917 C  CA    . GLU A 1 3490 ? 166.211 110.088 218.357 1.00 95.01  ? 3490 GLU A CA    1 
ATOM   13918 C  C     . GLU A 1 3490 ? 167.277 110.798 217.533 1.00 95.49  ? 3490 GLU A C     1 
ATOM   13919 O  O     . GLU A 1 3490 ? 167.968 111.692 218.035 1.00 93.52  ? 3490 GLU A O     1 
ATOM   13920 C  CB    . GLU A 1 3490 ? 166.753 108.785 218.943 1.00 103.34 ? 3490 GLU A CB    1 
ATOM   13921 C  CG    . GLU A 1 3490 ? 165.981 108.293 220.158 1.00 102.83 ? 3490 GLU A CG    1 
ATOM   13922 C  CD    . GLU A 1 3490 ? 166.471 106.948 220.656 1.00 113.94 ? 3490 GLU A CD    1 
ATOM   13923 O  OE1   . GLU A 1 3490 ? 166.655 106.035 219.823 1.00 117.67 ? 3490 GLU A OE1   1 
ATOM   13924 O  OE2   . GLU A 1 3490 ? 166.668 106.802 221.880 1.00 113.99 ? 3490 GLU A OE2   1 
ATOM   13925 N  N     . LYS A 1 3491 ? 167.431 110.409 216.264 1.00 97.75  ? 3491 LYS A N     1 
ATOM   13926 C  CA    . LYS A 1 3491 ? 168.382 111.091 215.393 1.00 97.75  ? 3491 LYS A CA    1 
ATOM   13927 C  C     . LYS A 1 3491 ? 167.980 112.543 215.163 1.00 100.44 ? 3491 LYS A C     1 
ATOM   13928 O  O     . LYS A 1 3491 ? 168.829 113.442 215.195 1.00 103.04 ? 3491 LYS A O     1 
ATOM   13929 C  CB    . LYS A 1 3491 ? 168.501 110.351 214.060 1.00 97.65  ? 3491 LYS A CB    1 
ATOM   13930 C  CG    . LYS A 1 3491 ? 169.298 109.058 214.133 1.00 105.11 ? 3491 LYS A CG    1 
ATOM   13931 C  CD    . LYS A 1 3491 ? 170.664 109.285 214.759 1.00 110.08 ? 3491 LYS A CD    1 
ATOM   13932 C  CE    . LYS A 1 3491 ? 171.251 107.987 215.291 1.00 106.23 ? 3491 LYS A CE    1 
ATOM   13933 N  NZ    . LYS A 1 3491 ? 170.458 107.445 216.428 1.00 101.57 ? 3491 LYS A NZ    1 
ATOM   13934 N  N     . THR A 1 3492 ? 166.689 112.793 214.923 1.00 101.41 ? 3492 THR A N     1 
ATOM   13935 C  CA    . THR A 1 3492 ? 166.232 114.166 214.732 1.00 96.21  ? 3492 THR A CA    1 
ATOM   13936 C  C     . THR A 1 3492 ? 166.356 114.976 216.017 1.00 95.15  ? 3492 THR A C     1 
ATOM   13937 O  O     . THR A 1 3492 ? 166.751 116.148 215.983 1.00 97.52  ? 3492 THR A O     1 
ATOM   13938 C  CB    . THR A 1 3492 ? 164.788 114.182 214.230 1.00 86.51  ? 3492 THR A CB    1 
ATOM   13939 O  OG1   . THR A 1 3492 ? 163.980 113.345 215.065 1.00 93.96  ? 3492 THR A OG1   1 
ATOM   13940 C  CG2   . THR A 1 3492 ? 164.718 113.678 212.796 1.00 81.56  ? 3492 THR A CG2   1 
ATOM   13941 N  N     . SER A 1 3493 ? 166.022 114.371 217.160 1.00 90.36  ? 3493 SER A N     1 
ATOM   13942 C  CA    . SER A 1 3493 ? 166.149 115.075 218.432 1.00 89.63  ? 3493 SER A CA    1 
ATOM   13943 C  C     . SER A 1 3493 ? 167.608 115.329 218.790 1.00 94.44  ? 3493 SER A C     1 
ATOM   13944 O  O     . SER A 1 3493 ? 167.917 116.321 219.459 1.00 93.40  ? 3493 SER A O     1 
ATOM   13945 C  CB    . SER A 1 3493 ? 165.459 114.285 219.544 1.00 91.47  ? 3493 SER A CB    1 
ATOM   13946 O  OG    . SER A 1 3493 ? 165.661 114.898 220.806 1.00 91.57  ? 3493 SER A OG    1 
ATOM   13947 N  N     . GLU A 1 3494 ? 168.512 114.444 218.363 1.00 98.77  ? 3494 GLU A N     1 
ATOM   13948 C  CA    . GLU A 1 3494 ? 169.936 114.653 218.594 1.00 102.36 ? 3494 GLU A CA    1 
ATOM   13949 C  C     . GLU A 1 3494 ? 170.454 115.901 217.890 1.00 100.63 ? 3494 GLU A C     1 
ATOM   13950 O  O     . GLU A 1 3494 ? 171.454 116.480 218.330 1.00 98.43  ? 3494 GLU A O     1 
ATOM   13951 C  CB    . GLU A 1 3494 ? 170.721 113.421 218.134 1.00 107.08 ? 3494 GLU A CB    1 
ATOM   13952 C  CG    . GLU A 1 3494 ? 172.198 113.431 218.494 1.00 110.41 ? 3494 GLU A CG    1 
ATOM   13953 C  CD    . GLU A 1 3494 ? 173.083 113.730 217.299 1.00 117.70 ? 3494 GLU A CD    1 
ATOM   13954 O  OE1   . GLU A 1 3494 ? 172.592 113.630 216.155 1.00 111.12 ? 3494 GLU A OE1   1 
ATOM   13955 O  OE2   . GLU A 1 3494 ? 174.270 114.063 217.503 1.00 124.77 ? 3494 GLU A OE2   1 
ATOM   13956 N  N     . THR A 1 3495 ? 169.793 116.332 216.818 1.00 98.83  ? 3495 THR A N     1 
ATOM   13957 C  CA    . THR A 1 3495 ? 170.205 117.501 216.056 1.00 98.60  ? 3495 THR A CA    1 
ATOM   13958 C  C     . THR A 1 3495 ? 169.414 118.753 216.417 1.00 96.22  ? 3495 THR A C     1 
ATOM   13959 O  O     . THR A 1 3495 ? 169.553 119.773 215.737 1.00 95.18  ? 3495 THR A O     1 
ATOM   13960 C  CB    . THR A 1 3495 ? 170.076 117.225 214.556 1.00 96.13  ? 3495 THR A CB    1 
ATOM   13961 O  OG1   . THR A 1 3495 ? 168.694 117.070 214.214 1.00 93.62  ? 3495 THR A OG1   1 
ATOM   13962 C  CG2   . THR A 1 3495 ? 170.829 115.957 214.183 1.00 91.71  ? 3495 THR A CG2   1 
ATOM   13963 N  N     . PHE A 1 3496 ? 168.588 118.700 217.466 1.00 94.32  ? 3496 PHE A N     1 
ATOM   13964 C  CA    . PHE A 1 3496 ? 167.771 119.858 217.824 1.00 91.30  ? 3496 PHE A CA    1 
ATOM   13965 C  C     . PHE A 1 3496 ? 168.638 121.063 218.164 1.00 89.71  ? 3496 PHE A C     1 
ATOM   13966 O  O     . PHE A 1 3496 ? 168.327 122.195 217.769 1.00 89.70  ? 3496 PHE A O     1 
ATOM   13967 C  CB    . PHE A 1 3496 ? 166.850 119.508 218.993 1.00 89.68  ? 3496 PHE A CB    1 
ATOM   13968 C  CG    . PHE A 1 3496 ? 166.249 120.705 219.675 1.00 89.93  ? 3496 PHE A CG    1 
ATOM   13969 C  CD1   . PHE A 1 3496 ? 165.146 121.345 219.134 1.00 87.27  ? 3496 PHE A CD1   1 
ATOM   13970 C  CD2   . PHE A 1 3496 ? 166.775 121.180 220.866 1.00 90.03  ? 3496 PHE A CD2   1 
ATOM   13971 C  CE1   . PHE A 1 3496 ? 164.587 122.443 219.761 1.00 84.25  ? 3496 PHE A CE1   1 
ATOM   13972 C  CE2   . PHE A 1 3496 ? 166.220 122.278 221.496 1.00 86.99  ? 3496 PHE A CE2   1 
ATOM   13973 C  CZ    . PHE A 1 3496 ? 165.124 122.909 220.944 1.00 84.97  ? 3496 PHE A CZ    1 
ATOM   13974 N  N     . LYS A 1 3497 ? 169.726 120.840 218.905 1.00 85.29  ? 3497 LYS A N     1 
ATOM   13975 C  CA    . LYS A 1 3497 ? 170.664 121.921 219.185 1.00 83.89  ? 3497 LYS A CA    1 
ATOM   13976 C  C     . LYS A 1 3497 ? 171.251 122.483 217.896 1.00 83.46  ? 3497 LYS A C     1 
ATOM   13977 O  O     . LYS A 1 3497 ? 171.523 123.685 217.800 1.00 81.22  ? 3497 LYS A O     1 
ATOM   13978 C  CB    . LYS A 1 3497 ? 171.768 121.420 220.119 1.00 88.65  ? 3497 LYS A CB    1 
ATOM   13979 C  CG    . LYS A 1 3497 ? 172.996 122.312 220.192 1.00 93.39  ? 3497 LYS A CG    1 
ATOM   13980 C  CD    . LYS A 1 3497 ? 174.212 121.532 220.665 1.00 88.95  ? 3497 LYS A CD    1 
ATOM   13981 C  CE    . LYS A 1 3497 ? 174.550 120.399 219.709 1.00 83.73  ? 3497 LYS A CE    1 
ATOM   13982 N  NZ    . LYS A 1 3497 ? 174.687 120.876 218.306 1.00 78.44  ? 3497 LYS A NZ    1 
ATOM   13983 N  N     . ASN A 1 3498 ? 171.441 121.628 216.887 1.00 83.46  ? 3498 ASN A N     1 
ATOM   13984 C  CA    . ASN A 1 3498 ? 171.967 122.101 215.610 1.00 81.55  ? 3498 ASN A CA    1 
ATOM   13985 C  C     . ASN A 1 3498 ? 170.986 123.041 214.918 1.00 83.13  ? 3498 ASN A C     1 
ATOM   13986 O  O     . ASN A 1 3498 ? 171.390 124.076 214.374 1.00 84.30  ? 3498 ASN A O     1 
ATOM   13987 C  CB    . ASN A 1 3498 ? 172.308 120.915 214.708 1.00 83.78  ? 3498 ASN A CB    1 
ATOM   13988 C  CG    . ASN A 1 3498 ? 172.714 121.344 213.312 1.00 85.74  ? 3498 ASN A CG    1 
ATOM   13989 O  OD1   . ASN A 1 3498 ? 172.086 120.963 212.325 1.00 79.69  ? 3498 ASN A OD1   1 
ATOM   13990 N  ND2   . ASN A 1 3498 ? 173.772 122.141 213.224 1.00 90.29  ? 3498 ASN A ND2   1 
ATOM   13991 N  N     . GLN A 1 3499 ? 169.693 122.699 214.918 1.00 85.96  ? 3499 GLN A N     1 
ATOM   13992 C  CA    . GLN A 1 3499 ? 168.704 123.610 214.346 1.00 82.51  ? 3499 GLN A CA    1 
ATOM   13993 C  C     . GLN A 1 3499 ? 168.612 124.901 215.150 1.00 77.03  ? 3499 GLN A C     1 
ATOM   13994 O  O     . GLN A 1 3499 ? 168.474 125.986 214.575 1.00 73.74  ? 3499 GLN A O     1 
ATOM   13995 C  CB    . GLN A 1 3499 ? 167.325 122.949 214.256 1.00 83.53  ? 3499 GLN A CB    1 
ATOM   13996 C  CG    . GLN A 1 3499 ? 167.167 121.901 213.161 1.00 82.89  ? 3499 GLN A CG    1 
ATOM   13997 C  CD    . GLN A 1 3499 ? 167.839 120.588 213.492 1.00 88.96  ? 3499 GLN A CD    1 
ATOM   13998 O  OE1   . GLN A 1 3499 ? 168.766 120.157 212.809 1.00 94.49  ? 3499 GLN A OE1   1 
ATOM   13999 N  NE2   . GLN A 1 3499 ? 167.353 119.928 214.534 1.00 85.17  ? 3499 GLN A NE2   1 
ATOM   14000 N  N     . MET A 1 3500 ? 168.676 124.802 216.480 1.00 76.05  ? 3500 MET A N     1 
ATOM   14001 C  CA    . MET A 1 3500 ? 168.607 126.000 217.313 1.00 72.02  ? 3500 MET A CA    1 
ATOM   14002 C  C     . MET A 1 3500 ? 169.789 126.929 217.060 1.00 68.18  ? 3500 MET A C     1 
ATOM   14003 O  O     . MET A 1 3500 ? 169.630 128.154 217.048 1.00 70.88  ? 3500 MET A O     1 
ATOM   14004 C  CB    . MET A 1 3500 ? 168.537 125.609 218.789 1.00 75.92  ? 3500 MET A CB    1 
ATOM   14005 C  CG    . MET A 1 3500 ? 167.125 125.417 219.316 1.00 77.68  ? 3500 MET A CG    1 
ATOM   14006 S  SD    . MET A 1 3500 ? 166.018 126.740 218.791 1.00 86.10  ? 3500 MET A SD    1 
ATOM   14007 C  CE    . MET A 1 3500 ? 164.550 126.354 219.740 1.00 73.29  ? 3500 MET A CE    1 
ATOM   14008 N  N     . SER A 1 3501 ? 170.983 126.367 216.866 1.00 68.73  ? 3501 SER A N     1 
ATOM   14009 C  CA    . SER A 1 3501 ? 172.169 127.198 216.685 1.00 72.05  ? 3501 SER A CA    1 
ATOM   14010 C  C     . SER A 1 3501 ? 172.159 127.910 215.337 1.00 69.29  ? 3501 SER A C     1 
ATOM   14011 O  O     . SER A 1 3501 ? 172.509 129.092 215.251 1.00 68.27  ? 3501 SER A O     1 
ATOM   14012 C  CB    . SER A 1 3501 ? 173.430 126.348 216.833 1.00 75.15  ? 3501 SER A CB    1 
ATOM   14013 O  OG    . SER A 1 3501 ? 174.556 127.006 216.277 1.00 74.95  ? 3501 SER A OG    1 
ATOM   14014 N  N     . THR A 1 3502 ? 171.760 127.212 214.275 1.00 67.96  ? 3502 THR A N     1 
ATOM   14015 C  CA    . THR A 1 3502 ? 171.861 127.725 212.916 1.00 61.20  ? 3502 THR A CA    1 
ATOM   14016 C  C     . THR A 1 3502 ? 170.594 128.425 212.443 1.00 57.70  ? 3502 THR A C     1 
ATOM   14017 O  O     . THR A 1 3502 ? 170.522 128.826 211.277 1.00 56.80  ? 3502 THR A O     1 
ATOM   14018 C  CB    . THR A 1 3502 ? 172.211 126.592 211.950 1.00 56.51  ? 3502 THR A CB    1 
ATOM   14019 O  OG1   . THR A 1 3502 ? 171.171 125.607 211.970 1.00 56.60  ? 3502 THR A OG1   1 
ATOM   14020 C  CG2   . THR A 1 3502 ? 173.525 125.940 212.348 1.00 62.46  ? 3502 THR A CG2   1 
ATOM   14021 N  N     . ILE A 1 3503 ? 169.594 128.582 213.313 1.00 56.86  ? 3503 ILE A N     1 
ATOM   14022 C  CA    . ILE A 1 3503 ? 168.328 129.163 212.878 1.00 48.21  ? 3503 ILE A CA    1 
ATOM   14023 C  C     . ILE A 1 3503 ? 168.497 130.628 212.490 1.00 42.05  ? 3503 ILE A C     1 
ATOM   14024 O  O     . ILE A 1 3503 ? 167.840 131.107 211.557 1.00 47.10  ? 3503 ILE A O     1 
ATOM   14025 C  CB    . ILE A 1 3503 ? 167.250 128.974 213.964 1.00 44.77  ? 3503 ILE A CB    1 
ATOM   14026 C  CG1   . ILE A 1 3503 ? 165.869 129.338 213.420 1.00 39.09  ? 3503 ILE A CG1   1 
ATOM   14027 C  CG2   . ILE A 1 3503 ? 167.567 129.790 215.210 1.00 51.42  ? 3503 ILE A CG2   1 
ATOM   14028 C  CD1   . ILE A 1 3503 ? 164.739 128.874 214.301 1.00 42.35  ? 3503 ILE A CD1   1 
ATOM   14029 N  N     . ALA A 1 3504 ? 169.378 131.360 213.178 1.00 44.66  ? 3504 ALA A N     1 
ATOM   14030 C  CA    . ALA A 1 3504 ? 169.547 132.782 212.895 1.00 39.47  ? 3504 ALA A CA    1 
ATOM   14031 C  C     . ALA A 1 3504 ? 170.088 133.006 211.488 1.00 37.68  ? 3504 ALA A C     1 
ATOM   14032 O  O     . ALA A 1 3504 ? 169.552 133.822 210.729 1.00 36.72  ? 3504 ALA A O     1 
ATOM   14033 C  CB    . ALA A 1 3504 ? 170.469 133.417 213.936 1.00 37.24  ? 3504 ALA A CB    1 
ATOM   14034 N  N     . GLY A 1 3505 ? 171.149 132.285 211.119 1.00 37.19  ? 3505 GLY A N     1 
ATOM   14035 C  CA    . GLY A 1 3505 ? 171.716 132.449 209.791 1.00 32.64  ? 3505 GLY A CA    1 
ATOM   14036 C  C     . GLY A 1 3505 ? 170.774 132.005 208.688 1.00 35.93  ? 3505 GLY A C     1 
ATOM   14037 O  O     . GLY A 1 3505 ? 170.672 132.659 207.645 1.00 36.86  ? 3505 GLY A O     1 
ATOM   14038 N  N     . ASP A 1 3506 ? 170.079 130.884 208.898 1.00 37.19  ? 3506 ASP A N     1 
ATOM   14039 C  CA    . ASP A 1 3506 ? 169.127 130.409 207.900 1.00 36.81  ? 3506 ASP A CA    1 
ATOM   14040 C  C     . ASP A 1 3506 ? 167.994 131.406 207.702 1.00 34.75  ? 3506 ASP A C     1 
ATOM   14041 O  O     . ASP A 1 3506 ? 167.597 131.690 206.566 1.00 35.47  ? 3506 ASP A O     1 
ATOM   14042 C  CB    . ASP A 1 3506 ? 168.572 129.045 208.308 1.00 43.00  ? 3506 ASP A CB    1 
ATOM   14043 C  CG    . ASP A 1 3506 ? 169.653 127.992 208.440 1.00 60.41  ? 3506 ASP A CG    1 
ATOM   14044 O  OD1   . ASP A 1 3506 ? 170.672 128.093 207.725 1.00 65.04  ? 3506 ASP A OD1   1 
ATOM   14045 O  OD2   . ASP A 1 3506 ? 169.483 127.064 209.258 1.00 62.78  ? 3506 ASP A OD2   1 
ATOM   14046 N  N     . CYS A 1 3507 ? 167.464 131.954 208.799 1.00 31.49  ? 3507 CYS A N     1 
ATOM   14047 C  CA    . CYS A 1 3507 ? 166.400 132.945 208.685 1.00 27.61  ? 3507 CYS A CA    1 
ATOM   14048 C  C     . CYS A 1 3507 ? 166.902 134.218 208.017 1.00 30.86  ? 3507 CYS A C     1 
ATOM   14049 O  O     . CYS A 1 3507 ? 166.185 134.823 207.213 1.00 32.35  ? 3507 CYS A O     1 
ATOM   14050 C  CB    . CYS A 1 3507 ? 165.817 133.247 210.064 1.00 28.86  ? 3507 CYS A CB    1 
ATOM   14051 S  SG    . CYS A 1 3507 ? 164.795 131.915 210.730 1.00 50.53  ? 3507 CYS A SG    1 
ATOM   14052 N  N     . LEU A 1 3508 ? 168.131 134.635 208.330 1.00 29.61  ? 3508 LEU A N     1 
ATOM   14053 C  CA    . LEU A 1 3508 ? 168.706 135.810 207.680 1.00 26.29  ? 3508 LEU A CA    1 
ATOM   14054 C  C     . LEU A 1 3508 ? 168.813 135.604 206.175 1.00 25.29  ? 3508 LEU A C     1 
ATOM   14055 O  O     . LEU A 1 3508 ? 168.411 136.469 205.386 1.00 26.10  ? 3508 LEU A O     1 
ATOM   14056 C  CB    . LEU A 1 3508 ? 170.078 136.115 208.284 1.00 24.96  ? 3508 LEU A CB    1 
ATOM   14057 C  CG    . LEU A 1 3508 ? 170.711 137.480 208.004 1.00 26.42  ? 3508 LEU A CG    1 
ATOM   14058 C  CD1   . LEU A 1 3508 ? 171.452 137.978 209.233 1.00 29.16  ? 3508 LEU A CD1   1 
ATOM   14059 C  CD2   . LEU A 1 3508 ? 171.650 137.410 206.811 1.00 25.22  ? 3508 LEU A CD2   1 
ATOM   14060 N  N     . LEU A 1 3509 ? 169.348 134.453 205.757 1.00 26.32  ? 3509 LEU A N     1 
ATOM   14061 C  CA    . LEU A 1 3509 ? 169.483 134.171 204.331 1.00 23.87  ? 3509 LEU A CA    1 
ATOM   14062 C  C     . LEU A 1 3509 ? 168.125 134.101 203.645 1.00 22.90  ? 3509 LEU A C     1 
ATOM   14063 O  O     . LEU A 1 3509 ? 167.946 134.651 202.551 1.00 24.63  ? 3509 LEU A O     1 
ATOM   14064 C  CB    . LEU A 1 3509 ? 170.252 132.867 204.123 1.00 27.51  ? 3509 LEU A CB    1 
ATOM   14065 C  CG    . LEU A 1 3509 ? 171.737 132.911 204.469 1.00 26.80  ? 3509 LEU A CG    1 
ATOM   14066 C  CD1   . LEU A 1 3509 ? 172.426 131.619 204.072 1.00 31.25  ? 3509 LEU A CD1   1 
ATOM   14067 C  CD2   . LEU A 1 3509 ? 172.375 134.089 203.766 1.00 22.24  ? 3509 LEU A CD2   1 
ATOM   14068 N  N     . SER A 1 3510 ? 167.157 133.429 204.271 1.00 19.52  ? 3510 SER A N     1 
ATOM   14069 C  CA    . SER A 1 3510 ? 165.836 133.306 203.665 1.00 20.08  ? 3510 SER A CA    1 
ATOM   14070 C  C     . SER A 1 3510 ? 165.163 134.665 203.526 1.00 21.40  ? 3510 SER A C     1 
ATOM   14071 O  O     . SER A 1 3510 ? 164.573 134.969 202.482 1.00 22.89  ? 3510 SER A O     1 
ATOM   14072 C  CB    . SER A 1 3510 ? 164.973 132.355 204.491 1.00 23.66  ? 3510 SER A CB    1 
ATOM   14073 O  OG    . SER A 1 3510 ? 165.671 131.156 204.779 1.00 28.15  ? 3510 SER A OG    1 
ATOM   14074 N  N     . ALA A 1 3511 ? 165.248 135.501 204.564 1.00 21.65  ? 3511 ALA A N     1 
ATOM   14075 C  CA    . ALA A 1 3511 ? 164.650 136.829 204.500 1.00 19.67  ? 3511 ALA A CA    1 
ATOM   14076 C  C     . ALA A 1 3511 ? 165.321 137.689 203.440 1.00 20.46  ? 3511 ALA A C     1 
ATOM   14077 O  O     . ALA A 1 3511 ? 164.645 138.413 202.698 1.00 21.01  ? 3511 ALA A O     1 
ATOM   14078 C  CB    . ALA A 1 3511 ? 164.737 137.505 205.865 1.00 17.16  ? 3511 ALA A CB    1 
ATOM   14079 N  N     . ALA A 1 3512 ? 166.653 137.632 203.361 1.00 20.10  ? 3512 ALA A N     1 
ATOM   14080 C  CA    . ALA A 1 3512 ? 167.362 138.404 202.348 1.00 16.04  ? 3512 ALA A CA    1 
ATOM   14081 C  C     . ALA A 1 3512 ? 166.962 137.964 200.948 1.00 17.44  ? 3512 ALA A C     1 
ATOM   14082 O  O     . ALA A 1 3512 ? 166.741 138.801 200.065 1.00 18.59  ? 3512 ALA A O     1 
ATOM   14083 C  CB    . ALA A 1 3512 ? 168.870 138.267 202.547 1.00 18.29  ? 3512 ALA A CB    1 
ATOM   14084 N  N     . PHE A 1 3513 ? 166.848 136.652 200.730 1.00 19.60  ? 3513 PHE A N     1 
ATOM   14085 C  CA    . PHE A 1 3513 ? 166.436 136.156 199.423 1.00 19.39  ? 3513 PHE A CA    1 
ATOM   14086 C  C     . PHE A 1 3513 ? 165.014 136.588 199.087 1.00 18.30  ? 3513 PHE A C     1 
ATOM   14087 O  O     . PHE A 1 3513 ? 164.729 136.976 197.949 1.00 22.46  ? 3513 PHE A O     1 
ATOM   14088 C  CB    . PHE A 1 3513 ? 166.559 134.635 199.376 1.00 21.53  ? 3513 PHE A CB    1 
ATOM   14089 C  CG    . PHE A 1 3513 ? 166.384 134.060 198.004 1.00 26.78  ? 3513 PHE A CG    1 
ATOM   14090 C  CD1   . PHE A 1 3513 ? 167.441 134.035 197.111 1.00 26.73  ? 3513 PHE A CD1   1 
ATOM   14091 C  CD2   . PHE A 1 3513 ? 165.162 133.546 197.604 1.00 23.50  ? 3513 PHE A CD2   1 
ATOM   14092 C  CE1   . PHE A 1 3513 ? 167.283 133.509 195.848 1.00 28.82  ? 3513 PHE A CE1   1 
ATOM   14093 C  CE2   . PHE A 1 3513 ? 164.999 133.019 196.342 1.00 23.75  ? 3513 PHE A CE2   1 
ATOM   14094 C  CZ    . PHE A 1 3513 ? 166.061 133.000 195.463 1.00 28.69  ? 3513 PHE A CZ    1 
ATOM   14095 N  N     . ILE A 1 3514 ? 164.106 136.523 200.063 1.00 17.21  ? 3514 ILE A N     1 
ATOM   14096 C  CA    . ILE A 1 3514 ? 162.716 136.892 199.806 1.00 16.88  ? 3514 ILE A CA    1 
ATOM   14097 C  C     . ILE A 1 3514 ? 162.608 138.374 199.469 1.00 20.56  ? 3514 ILE A C     1 
ATOM   14098 O  O     . ILE A 1 3514 ? 161.930 138.764 198.511 1.00 24.23  ? 3514 ILE A O     1 
ATOM   14099 C  CB    . ILE A 1 3514 ? 161.828 136.525 201.009 1.00 16.05  ? 3514 ILE A CB    1 
ATOM   14100 C  CG1   . ILE A 1 3514 ? 161.710 135.009 201.152 1.00 18.16  ? 3514 ILE A CG1   1 
ATOM   14101 C  CG2   . ILE A 1 3514 ? 160.451 137.142 200.861 1.00 18.03  ? 3514 ILE A CG2   1 
ATOM   14102 C  CD1   . ILE A 1 3514 ? 160.972 134.581 202.397 1.00 18.54  ? 3514 ILE A CD1   1 
ATOM   14103 N  N     . ALA A 1 3515 ? 163.280 139.223 200.244 1.00 18.45  ? 3515 ALA A N     1 
ATOM   14104 C  CA    . ALA A 1 3515 ? 163.097 140.662 200.119 1.00 13.52  ? 3515 ALA A CA    1 
ATOM   14105 C  C     . ALA A 1 3515 ? 164.001 141.314 199.082 1.00 15.45  ? 3515 ALA A C     1 
ATOM   14106 O  O     . ALA A 1 3515 ? 163.759 142.471 198.722 1.00 19.27  ? 3515 ALA A O     1 
ATOM   14107 C  CB    . ALA A 1 3515 ? 163.320 141.339 201.473 1.00 15.16  ? 3515 ALA A CB    1 
ATOM   14108 N  N     . TYR A 1 3516 ? 165.024 140.622 198.590 1.00 15.38  ? 3516 TYR A N     1 
ATOM   14109 C  CA    . TYR A 1 3516 ? 165.979 141.251 197.686 1.00 12.97  ? 3516 TYR A CA    1 
ATOM   14110 C  C     . TYR A 1 3516 ? 166.062 140.594 196.318 1.00 16.94  ? 3516 TYR A C     1 
ATOM   14111 O  O     . TYR A 1 3516 ? 166.057 141.295 195.304 1.00 22.56  ? 3516 TYR A O     1 
ATOM   14112 C  CB    . TYR A 1 3516 ? 167.376 141.257 198.320 1.00 15.38  ? 3516 TYR A CB    1 
ATOM   14113 C  CG    . TYR A 1 3516 ? 167.568 142.301 199.396 1.00 17.85  ? 3516 TYR A CG    1 
ATOM   14114 C  CD1   . TYR A 1 3516 ? 167.406 143.650 199.118 1.00 15.35  ? 3516 TYR A CD1   1 
ATOM   14115 C  CD2   . TYR A 1 3516 ? 167.931 141.937 200.684 1.00 16.91  ? 3516 TYR A CD2   1 
ATOM   14116 C  CE1   . TYR A 1 3516 ? 167.591 144.605 200.094 1.00 13.36  ? 3516 TYR A CE1   1 
ATOM   14117 C  CE2   . TYR A 1 3516 ? 168.115 142.887 201.667 1.00 15.35  ? 3516 TYR A CE2   1 
ATOM   14118 C  CZ    . TYR A 1 3516 ? 167.944 144.218 201.366 1.00 14.73  ? 3516 TYR A CZ    1 
ATOM   14119 O  OH    . TYR A 1 3516 ? 168.128 145.168 202.343 1.00 23.47  ? 3516 TYR A OH    1 
ATOM   14120 N  N     . ALA A 1 3517 ? 166.137 139.265 196.258 1.00 17.41  ? 3517 ALA A N     1 
ATOM   14121 C  CA    . ALA A 1 3517 ? 166.446 138.552 195.027 1.00 16.36  ? 3517 ALA A CA    1 
ATOM   14122 C  C     . ALA A 1 3517 ? 165.219 138.288 194.161 1.00 19.90  ? 3517 ALA A C     1 
ATOM   14123 O  O     . ALA A 1 3517 ? 165.258 137.396 193.307 1.00 28.58  ? 3517 ALA A O     1 
ATOM   14124 C  CB    . ALA A 1 3517 ? 167.151 137.233 195.349 1.00 20.04  ? 3517 ALA A CB    1 
ATOM   14125 N  N     . GLY A 1 3518 ? 164.133 139.034 194.364 1.00 21.41  ? 3518 GLY A N     1 
ATOM   14126 C  CA    . GLY A 1 3518 ? 162.938 138.807 193.569 1.00 20.97  ? 3518 GLY A CA    1 
ATOM   14127 C  C     . GLY A 1 3518 ? 163.111 139.164 192.105 1.00 21.37  ? 3518 GLY A C     1 
ATOM   14128 O  O     . GLY A 1 3518 ? 162.677 138.420 191.221 1.00 24.65  ? 3518 GLY A O     1 
ATOM   14129 N  N     . TYR A 1 3519 ? 163.744 140.304 191.826 1.00 22.50  ? 3519 TYR A N     1 
ATOM   14130 C  CA    . TYR A 1 3519 ? 163.836 140.797 190.456 1.00 20.97  ? 3519 TYR A CA    1 
ATOM   14131 C  C     . TYR A 1 3519 ? 164.879 140.053 189.632 1.00 24.12  ? 3519 TYR A C     1 
ATOM   14132 O  O     . TYR A 1 3519 ? 164.737 139.954 188.408 1.00 28.28  ? 3519 TYR A O     1 
ATOM   14133 C  CB    . TYR A 1 3519 ? 164.151 142.294 190.461 1.00 21.94  ? 3519 TYR A CB    1 
ATOM   14134 C  CG    . TYR A 1 3519 ? 164.224 142.910 189.084 1.00 23.01  ? 3519 TYR A CG    1 
ATOM   14135 C  CD1   . TYR A 1 3519 ? 163.071 143.189 188.365 1.00 24.67  ? 3519 TYR A CD1   1 
ATOM   14136 C  CD2   . TYR A 1 3519 ? 165.448 143.213 188.502 1.00 24.80  ? 3519 TYR A CD2   1 
ATOM   14137 C  CE1   . TYR A 1 3519 ? 163.133 143.751 187.106 1.00 30.36  ? 3519 TYR A CE1   1 
ATOM   14138 C  CE2   . TYR A 1 3519 ? 165.520 143.776 187.244 1.00 27.69  ? 3519 TYR A CE2   1 
ATOM   14139 C  CZ    . TYR A 1 3519 ? 164.360 144.042 186.550 1.00 33.00  ? 3519 TYR A CZ    1 
ATOM   14140 O  OH    . TYR A 1 3519 ? 164.427 144.603 185.296 1.00 43.93  ? 3519 TYR A OH    1 
ATOM   14141 N  N     . PHE A 1 3520 ? 165.920 139.530 190.269 1.00 23.66  ? 3520 PHE A N     1 
ATOM   14142 C  CA    . PHE A 1 3520 ? 167.054 138.985 189.541 1.00 25.07  ? 3520 PHE A CA    1 
ATOM   14143 C  C     . PHE A 1 3520 ? 166.752 137.585 189.012 1.00 26.19  ? 3520 PHE A C     1 
ATOM   14144 O  O     . PHE A 1 3520 ? 165.829 136.903 189.464 1.00 32.08  ? 3520 PHE A O     1 
ATOM   14145 C  CB    . PHE A 1 3520 ? 168.291 138.957 190.437 1.00 25.75  ? 3520 PHE A CB    1 
ATOM   14146 C  CG    . PHE A 1 3520 ? 168.632 140.292 191.030 1.00 23.91  ? 3520 PHE A CG    1 
ATOM   14147 C  CD1   . PHE A 1 3520 ? 169.454 141.177 190.356 1.00 25.39  ? 3520 PHE A CD1   1 
ATOM   14148 C  CD2   . PHE A 1 3520 ? 168.123 140.664 192.262 1.00 24.22  ? 3520 PHE A CD2   1 
ATOM   14149 C  CE1   . PHE A 1 3520 ? 169.765 142.407 190.901 1.00 28.63  ? 3520 PHE A CE1   1 
ATOM   14150 C  CE2   . PHE A 1 3520 ? 168.429 141.891 192.809 1.00 27.88  ? 3520 PHE A CE2   1 
ATOM   14151 C  CZ    . PHE A 1 3520 ? 169.252 142.764 192.130 1.00 29.32  ? 3520 PHE A CZ    1 
ATOM   14152 N  N     . ASP A 1 3521 ? 167.549 137.165 188.031 1.00 27.65  ? 3521 ASP A N     1 
ATOM   14153 C  CA    . ASP A 1 3521 ? 167.416 135.842 187.443 1.00 27.53  ? 3521 ASP A CA    1 
ATOM   14154 C  C     . ASP A 1 3521 ? 168.120 134.804 188.316 1.00 29.06  ? 3521 ASP A C     1 
ATOM   14155 O  O     . ASP A 1 3521 ? 168.653 135.110 189.385 1.00 34.57  ? 3521 ASP A O     1 
ATOM   14156 C  CB    . ASP A 1 3521 ? 167.966 135.835 186.019 1.00 30.29  ? 3521 ASP A CB    1 
ATOM   14157 C  CG    . ASP A 1 3521 ? 169.291 136.562 185.902 1.00 47.20  ? 3521 ASP A CG    1 
ATOM   14158 O  OD1   . ASP A 1 3521 ? 169.745 137.139 186.911 1.00 45.98  ? 3521 ASP A OD1   1 
ATOM   14159 O  OD2   . ASP A 1 3521 ? 169.878 136.556 184.800 1.00 57.02  ? 3521 ASP A OD2   1 
ATOM   14160 N  N     . GLN A 1 3522 ? 168.126 133.553 187.845 1.00 28.56  ? 3522 GLN A N     1 
ATOM   14161 C  CA    . GLN A 1 3522 ? 168.644 132.451 188.653 1.00 29.67  ? 3522 GLN A CA    1 
ATOM   14162 C  C     . GLN A 1 3522 ? 170.120 132.634 188.984 1.00 34.05  ? 3522 GLN A C     1 
ATOM   14163 O  O     . GLN A 1 3522 ? 170.534 132.443 190.134 1.00 35.91  ? 3522 GLN A O     1 
ATOM   14164 C  CB    . GLN A 1 3522 ? 168.427 131.125 187.926 1.00 29.74  ? 3522 GLN A CB    1 
ATOM   14165 C  CG    . GLN A 1 3522 ? 168.854 129.907 188.725 1.00 38.09  ? 3522 GLN A CG    1 
ATOM   14166 C  CD    . GLN A 1 3522 ? 168.577 128.607 187.999 1.00 42.68  ? 3522 GLN A CD    1 
ATOM   14167 O  OE1   . GLN A 1 3522 ? 168.094 128.605 186.868 1.00 46.93  ? 3522 GLN A OE1   1 
ATOM   14168 N  NE2   . GLN A 1 3522 ? 168.884 127.490 188.648 1.00 49.96  ? 3522 GLN A NE2   1 
ATOM   14169 N  N     . GLN A 1 3523 ? 170.931 132.999 187.987 1.00 36.08  ? 3523 GLN A N     1 
ATOM   14170 C  CA    . GLN A 1 3523 ? 172.366 133.143 188.216 1.00 36.71  ? 3523 GLN A CA    1 
ATOM   14171 C  C     . GLN A 1 3523 ? 172.658 134.254 189.217 1.00 33.15  ? 3523 GLN A C     1 
ATOM   14172 O  O     . GLN A 1 3523 ? 173.505 134.096 190.104 1.00 38.47  ? 3523 GLN A O     1 
ATOM   14173 C  CB    . GLN A 1 3523 ? 173.088 133.390 186.888 1.00 49.13  ? 3523 GLN A CB    1 
ATOM   14174 C  CG    . GLN A 1 3523 ? 172.733 134.695 186.183 1.00 64.16  ? 3523 GLN A CG    1 
ATOM   14175 C  CD    . GLN A 1 3523 ? 173.437 134.847 184.847 1.00 84.96  ? 3523 GLN A CD    1 
ATOM   14176 O  OE1   . GLN A 1 3523 ? 174.239 134.000 184.456 1.00 93.84  ? 3523 GLN A OE1   1 
ATOM   14177 N  NE2   . GLN A 1 3523 ? 173.132 135.926 184.136 1.00 85.64  ? 3523 GLN A NE2   1 
ATOM   14178 N  N     . MET A 1 3524 ? 171.949 135.379 189.109 1.00 31.97  ? 3524 MET A N     1 
ATOM   14179 C  CA    . MET A 1 3524 ? 172.194 136.486 190.022 1.00 31.34  ? 3524 MET A CA    1 
ATOM   14180 C  C     . MET A 1 3524 ? 171.659 136.194 191.417 1.00 27.41  ? 3524 MET A C     1 
ATOM   14181 O  O     . MET A 1 3524 ? 172.263 136.613 192.411 1.00 30.34  ? 3524 MET A O     1 
ATOM   14182 C  CB    . MET A 1 3524 ? 171.583 137.767 189.467 1.00 30.18  ? 3524 MET A CB    1 
ATOM   14183 C  CG    . MET A 1 3524 ? 172.124 139.001 190.128 1.00 35.38  ? 3524 MET A CG    1 
ATOM   14184 S  SD    . MET A 1 3524 ? 173.700 139.442 189.387 1.00 50.64  ? 3524 MET A SD    1 
ATOM   14185 C  CE    . MET A 1 3524 ? 174.601 139.948 190.842 1.00 44.80  ? 3524 MET A CE    1 
ATOM   14186 N  N     . ARG A 1 3525 ? 170.534 135.483 191.511 1.00 25.18  ? 3525 ARG A N     1 
ATOM   14187 C  CA    . ARG A 1 3525 ? 170.047 135.043 192.813 1.00 21.83  ? 3525 ARG A CA    1 
ATOM   14188 C  C     . ARG A 1 3525 ? 171.065 134.135 193.491 1.00 29.03  ? 3525 ARG A C     1 
ATOM   14189 O  O     . ARG A 1 3525 ? 171.342 134.279 194.690 1.00 34.04  ? 3525 ARG A O     1 
ATOM   14190 C  CB    . ARG A 1 3525 ? 168.710 134.321 192.652 1.00 21.07  ? 3525 ARG A CB    1 
ATOM   14191 C  CG    . ARG A 1 3525 ? 167.541 135.227 192.313 1.00 17.78  ? 3525 ARG A CG    1 
ATOM   14192 C  CD    . ARG A 1 3525 ? 166.240 134.444 192.264 1.00 16.70  ? 3525 ARG A CD    1 
ATOM   14193 N  NE    . ARG A 1 3525 ? 165.189 135.173 191.564 1.00 18.31  ? 3525 ARG A NE    1 
ATOM   14194 C  CZ    . ARG A 1 3525 ? 163.908 134.831 191.572 1.00 18.05  ? 3525 ARG A CZ    1 
ATOM   14195 N  NH1   . ARG A 1 3525 ? 163.479 133.773 192.240 1.00 17.82  ? 3525 ARG A NH1   1 
ATOM   14196 N  NH2   . ARG A 1 3525 ? 163.036 135.570 190.893 1.00 22.98  ? 3525 ARG A NH2   1 
ATOM   14197 N  N     . GLN A 1 3526 ? 171.644 133.202 192.731 1.00 28.47  ? 3526 GLN A N     1 
ATOM   14198 C  CA    . GLN A 1 3526 ? 172.668 132.325 193.288 1.00 26.96  ? 3526 GLN A CA    1 
ATOM   14199 C  C     . GLN A 1 3526 ? 173.904 133.111 193.704 1.00 30.21  ? 3526 GLN A C     1 
ATOM   14200 O  O     . GLN A 1 3526 ? 174.500 132.827 194.749 1.00 35.69  ? 3526 GLN A O     1 
ATOM   14201 C  CB    . GLN A 1 3526 ? 173.036 131.238 192.280 1.00 26.60  ? 3526 GLN A CB    1 
ATOM   14202 C  CG    . GLN A 1 3526 ? 173.891 130.126 192.862 1.00 31.90  ? 3526 GLN A CG    1 
ATOM   14203 C  CD    . GLN A 1 3526 ? 173.434 129.703 194.243 1.00 33.68  ? 3526 GLN A CD    1 
ATOM   14204 O  OE1   . GLN A 1 3526 ? 172.325 129.198 194.416 1.00 33.87  ? 3526 GLN A OE1   1 
ATOM   14205 N  NE2   . GLN A 1 3526 ? 174.289 129.910 195.238 1.00 31.23  ? 3526 GLN A NE2   1 
ATOM   14206 N  N     . ASN A 1 3527 ? 174.305 134.101 192.903 1.00 27.49  ? 3527 ASN A N     1 
ATOM   14207 C  CA    . ASN A 1 3527 ? 175.462 134.920 193.256 1.00 27.73  ? 3527 ASN A CA    1 
ATOM   14208 C  C     . ASN A 1 3527 ? 175.220 135.683 194.554 1.00 27.41  ? 3527 ASN A C     1 
ATOM   14209 O  O     . ASN A 1 3527 ? 176.091 135.736 195.431 1.00 34.24  ? 3527 ASN A O     1 
ATOM   14210 C  CB    . ASN A 1 3527 ? 175.788 135.890 192.119 1.00 28.87  ? 3527 ASN A CB    1 
ATOM   14211 C  CG    . ASN A 1 3527 ? 176.379 135.198 190.905 1.00 42.11  ? 3527 ASN A CG    1 
ATOM   14212 O  OD1   . ASN A 1 3527 ? 176.408 133.969 190.834 1.00 52.63  ? 3527 ASN A OD1   1 
ATOM   14213 N  ND2   . ASN A 1 3527 ? 176.844 135.981 189.939 1.00 40.69  ? 3527 ASN A ND2   1 
ATOM   14214 N  N     . LEU A 1 3528 ? 174.034 136.282 194.693 1.00 22.18  ? 3528 LEU A N     1 
ATOM   14215 C  CA    . LEU A 1 3528 ? 173.712 137.018 195.911 1.00 18.27  ? 3528 LEU A CA    1 
ATOM   14216 C  C     . LEU A 1 3528 ? 173.692 136.097 197.124 1.00 19.75  ? 3528 LEU A C     1 
ATOM   14217 O  O     . LEU A 1 3528 ? 174.228 136.441 198.186 1.00 27.29  ? 3528 LEU A O     1 
ATOM   14218 C  CB    . LEU A 1 3528 ? 172.366 137.725 195.756 1.00 21.43  ? 3528 LEU A CB    1 
ATOM   14219 C  CG    . LEU A 1 3528 ? 172.321 138.950 194.841 1.00 22.95  ? 3528 LEU A CG    1 
ATOM   14220 C  CD1   . LEU A 1 3528 ? 170.892 139.444 194.684 1.00 18.94  ? 3528 LEU A CD1   1 
ATOM   14221 C  CD2   . LEU A 1 3528 ? 173.216 140.054 195.375 1.00 24.23  ? 3528 LEU A CD2   1 
ATOM   14222 N  N     . PHE A 1 3529 ? 173.074 134.920 196.986 1.00 18.00  ? 3529 PHE A N     1 
ATOM   14223 C  CA    . PHE A 1 3529 ? 173.030 133.981 198.102 1.00 21.34  ? 3529 PHE A CA    1 
ATOM   14224 C  C     . PHE A 1 3529 ? 174.428 133.512 198.483 1.00 27.23  ? 3529 PHE A C     1 
ATOM   14225 O  O     . PHE A 1 3529 ? 174.744 133.381 199.672 1.00 29.44  ? 3529 PHE A O     1 
ATOM   14226 C  CB    . PHE A 1 3529 ? 172.137 132.793 197.752 1.00 25.45  ? 3529 PHE A CB    1 
ATOM   14227 C  CG    . PHE A 1 3529 ? 171.562 132.097 198.950 1.00 24.36  ? 3529 PHE A CG    1 
ATOM   14228 C  CD1   . PHE A 1 3529 ? 170.397 132.554 199.540 1.00 23.39  ? 3529 PHE A CD1   1 
ATOM   14229 C  CD2   . PHE A 1 3529 ? 172.186 130.984 199.485 1.00 26.09  ? 3529 PHE A CD2   1 
ATOM   14230 C  CE1   . PHE A 1 3529 ? 169.866 131.917 200.642 1.00 24.50  ? 3529 PHE A CE1   1 
ATOM   14231 C  CE2   . PHE A 1 3529 ? 171.659 130.341 200.587 1.00 24.75  ? 3529 PHE A CE2   1 
ATOM   14232 C  CZ    . PHE A 1 3529 ? 170.497 130.808 201.166 1.00 24.21  ? 3529 PHE A CZ    1 
ATOM   14233 N  N     . THR A 1 3530 ? 175.279 133.253 197.487 1.00 30.93  ? 3530 THR A N     1 
ATOM   14234 C  CA    . THR A 1 3530 ? 176.651 132.844 197.769 1.00 31.50  ? 3530 THR A CA    1 
ATOM   14235 C  C     . THR A 1 3530 ? 177.418 133.946 198.487 1.00 30.72  ? 3530 THR A C     1 
ATOM   14236 O  O     . THR A 1 3530 ? 178.177 133.672 199.422 1.00 32.92  ? 3530 THR A O     1 
ATOM   14237 C  CB    . THR A 1 3530 ? 177.360 132.456 196.471 1.00 35.28  ? 3530 THR A CB    1 
ATOM   14238 O  OG1   . THR A 1 3530 ? 176.596 131.453 195.790 1.00 40.23  ? 3530 THR A OG1   1 
ATOM   14239 C  CG2   . THR A 1 3530 ? 178.750 131.912 196.764 1.00 36.95  ? 3530 THR A CG2   1 
ATOM   14240 N  N     . THR A 1 3531 ? 177.233 135.199 198.066 1.00 28.27  ? 3531 THR A N     1 
ATOM   14241 C  CA    . THR A 1 3531 ? 177.910 136.310 198.731 1.00 26.04  ? 3531 THR A CA    1 
ATOM   14242 C  C     . THR A 1 3531 ? 177.458 136.439 200.182 1.00 29.94  ? 3531 THR A C     1 
ATOM   14243 O  O     . THR A 1 3531 ? 178.278 136.643 201.088 1.00 39.39  ? 3531 THR A O     1 
ATOM   14244 C  CB    . THR A 1 3531 ? 177.652 137.611 197.971 1.00 23.37  ? 3531 THR A CB    1 
ATOM   14245 O  OG1   . THR A 1 3531 ? 177.962 137.426 196.584 1.00 28.44  ? 3531 THR A OG1   1 
ATOM   14246 C  CG2   . THR A 1 3531 ? 178.511 138.733 198.530 1.00 25.97  ? 3531 THR A CG2   1 
ATOM   14247 N  N     . TRP A 1 3532 ? 176.150 136.319 200.422 1.00 26.36  ? 3532 TRP A N     1 
ATOM   14248 C  CA    . TRP A 1 3532 ? 175.644 136.416 201.788 1.00 25.61  ? 3532 TRP A CA    1 
ATOM   14249 C  C     . TRP A 1 3532 ? 176.154 135.268 202.655 1.00 31.85  ? 3532 TRP A C     1 
ATOM   14250 O  O     . TRP A 1 3532 ? 176.529 135.478 203.816 1.00 38.94  ? 3532 TRP A O     1 
ATOM   14251 C  CB    . TRP A 1 3532 ? 174.117 136.454 201.781 1.00 20.44  ? 3532 TRP A CB    1 
ATOM   14252 C  CG    . TRP A 1 3532 ? 173.546 137.545 200.928 1.00 20.48  ? 3532 TRP A CG    1 
ATOM   14253 C  CD1   . TRP A 1 3532 ? 174.145 138.725 200.598 1.00 21.94  ? 3532 TRP A CD1   1 
ATOM   14254 C  CD2   . TRP A 1 3532 ? 172.263 137.555 200.291 1.00 17.40  ? 3532 TRP A CD2   1 
ATOM   14255 N  NE1   . TRP A 1 3532 ? 173.314 139.470 199.797 1.00 22.59  ? 3532 TRP A NE1   1 
ATOM   14256 C  CE2   . TRP A 1 3532 ? 172.152 138.773 199.594 1.00 20.08  ? 3532 TRP A CE2   1 
ATOM   14257 C  CE3   . TRP A 1 3532 ? 171.197 136.651 200.243 1.00 15.90  ? 3532 TRP A CE3   1 
ATOM   14258 C  CZ2   . TRP A 1 3532 ? 171.019 139.111 198.859 1.00 18.62  ? 3532 TRP A CZ2   1 
ATOM   14259 C  CZ3   . TRP A 1 3532 ? 170.075 136.988 199.511 1.00 17.04  ? 3532 TRP A CZ3   1 
ATOM   14260 C  CH2   . TRP A 1 3532 ? 169.994 138.208 198.830 1.00 18.59  ? 3532 TRP A CH2   1 
ATOM   14261 N  N     . SER A 1 3533 ? 176.177 134.048 202.110 1.00 34.11  ? 3533 SER A N     1 
ATOM   14262 C  CA    . SER A 1 3533 ? 176.704 132.911 202.860 1.00 35.70  ? 3533 SER A CA    1 
ATOM   14263 C  C     . SER A 1 3533 ? 178.188 133.089 203.159 1.00 37.62  ? 3533 SER A C     1 
ATOM   14264 O  O     . SER A 1 3533 ? 178.657 132.747 204.253 1.00 40.42  ? 3533 SER A O     1 
ATOM   14265 C  CB    . SER A 1 3533 ? 176.462 131.616 202.086 1.00 35.87  ? 3533 SER A CB    1 
ATOM   14266 O  OG    . SER A 1 3533 ? 175.108 131.508 201.684 1.00 36.50  ? 3533 SER A OG    1 
ATOM   14267 N  N     . HIS A 1 3534 ? 178.943 133.615 202.191 1.00 37.41  ? 3534 HIS A N     1 
ATOM   14268 C  CA    . HIS A 1 3534 ? 180.351 133.913 202.421 1.00 40.13  ? 3534 HIS A CA    1 
ATOM   14269 C  C     . HIS A 1 3534 ? 180.516 134.896 203.569 1.00 45.30  ? 3534 HIS A C     1 
ATOM   14270 O  O     . HIS A 1 3534 ? 181.322 134.671 204.479 1.00 54.62  ? 3534 HIS A O     1 
ATOM   14271 C  CB    . HIS A 1 3534 ? 180.978 134.474 201.144 1.00 42.41  ? 3534 HIS A CB    1 
ATOM   14272 C  CG    . HIS A 1 3534 ? 181.619 133.437 200.275 1.00 58.05  ? 3534 HIS A CG    1 
ATOM   14273 N  ND1   . HIS A 1 3534 ? 182.682 132.667 200.695 1.00 63.90  ? 3534 HIS A ND1   1 
ATOM   14274 C  CD2   . HIS A 1 3534 ? 181.347 133.043 199.009 1.00 58.79  ? 3534 HIS A CD2   1 
ATOM   14275 C  CE1   . HIS A 1 3534 ? 183.037 131.843 199.726 1.00 66.93  ? 3534 HIS A CE1   1 
ATOM   14276 N  NE2   . HIS A 1 3534 ? 182.243 132.051 198.691 1.00 63.95  ? 3534 HIS A NE2   1 
ATOM   14277 N  N     . HIS A 1 3535 ? 179.741 135.983 203.557 1.00 40.91  ? 3535 HIS A N     1 
ATOM   14278 C  CA    . HIS A 1 3535 ? 179.847 136.962 204.634 1.00 39.29  ? 3535 HIS A CA    1 
ATOM   14279 C  C     . HIS A 1 3535 ? 179.494 136.346 205.980 1.00 39.92  ? 3535 HIS A C     1 
ATOM   14280 O  O     . HIS A 1 3535 ? 180.144 136.636 206.991 1.00 48.22  ? 3535 HIS A O     1 
ATOM   14281 C  CB    . HIS A 1 3535 ? 178.954 138.167 204.357 1.00 35.41  ? 3535 HIS A CB    1 
ATOM   14282 C  CG    . HIS A 1 3535 ? 179.076 139.250 205.385 1.00 39.01  ? 3535 HIS A CG    1 
ATOM   14283 N  ND1   . HIS A 1 3535 ? 179.928 140.323 205.238 1.00 38.37  ? 3535 HIS A ND1   1 
ATOM   14284 C  CD2   . HIS A 1 3535 ? 178.457 139.422 206.577 1.00 37.77  ? 3535 HIS A CD2   1 
ATOM   14285 C  CE1   . HIS A 1 3535 ? 179.829 141.109 206.294 1.00 40.64  ? 3535 HIS A CE1   1 
ATOM   14286 N  NE2   . HIS A 1 3535 ? 178.942 140.586 207.121 1.00 39.12  ? 3535 HIS A NE2   1 
ATOM   14287 N  N     . LEU A 1 3536 ? 178.462 135.501 206.018 1.00 37.40  ? 3536 LEU A N     1 
ATOM   14288 C  CA    . LEU A 1 3536 ? 178.091 134.873 207.281 1.00 42.07  ? 3536 LEU A CA    1 
ATOM   14289 C  C     . LEU A 1 3536 ? 179.191 133.950 207.791 1.00 46.34  ? 3536 LEU A C     1 
ATOM   14290 O  O     . LEU A 1 3536 ? 179.456 133.904 208.998 1.00 50.88  ? 3536 LEU A O     1 
ATOM   14291 C  CB    . LEU A 1 3536 ? 176.776 134.110 207.144 1.00 40.25  ? 3536 LEU A CB    1 
ATOM   14292 C  CG    . LEU A 1 3536 ? 175.525 134.951 206.901 1.00 31.29  ? 3536 LEU A CG    1 
ATOM   14293 C  CD1   . LEU A 1 3536 ? 174.332 134.043 206.721 1.00 35.69  ? 3536 LEU A CD1   1 
ATOM   14294 C  CD2   . LEU A 1 3536 ? 175.297 135.922 208.044 1.00 33.31  ? 3536 LEU A CD2   1 
ATOM   14295 N  N     . GLN A 1 3537 ? 179.842 133.201 206.896 1.00 46.18  ? 3537 GLN A N     1 
ATOM   14296 C  CA    . GLN A 1 3537 ? 180.874 132.286 207.375 1.00 48.02  ? 3537 GLN A CA    1 
ATOM   14297 C  C     . GLN A 1 3537 ? 182.139 133.029 207.791 1.00 52.96  ? 3537 GLN A C     1 
ATOM   14298 O  O     . GLN A 1 3537 ? 182.838 132.579 208.705 1.00 57.78  ? 3537 GLN A O     1 
ATOM   14299 C  CB    . GLN A 1 3537 ? 181.196 131.211 206.335 1.00 46.06  ? 3537 GLN A CB    1 
ATOM   14300 C  CG    . GLN A 1 3537 ? 181.863 131.688 205.066 1.00 50.20  ? 3537 GLN A CG    1 
ATOM   14301 C  CD    . GLN A 1 3537 ? 182.124 130.549 204.101 1.00 53.88  ? 3537 GLN A CD    1 
ATOM   14302 O  OE1   . GLN A 1 3537 ? 181.849 129.389 204.406 1.00 52.14  ? 3537 GLN A OE1   1 
ATOM   14303 N  NE2   . GLN A 1 3537 ? 182.671 130.872 202.938 1.00 56.60  ? 3537 GLN A NE2   1 
ATOM   14304 N  N     . GLN A 1 3538 ? 182.458 134.157 207.145 1.00 48.45  ? 3538 GLN A N     1 
ATOM   14305 C  CA    . GLN A 1 3538 ? 183.541 134.989 207.663 1.00 47.40  ? 3538 GLN A CA    1 
ATOM   14306 C  C     . GLN A 1 3538 ? 183.182 135.665 208.979 1.00 52.08  ? 3538 GLN A C     1 
ATOM   14307 O  O     . GLN A 1 3538 ? 184.086 136.036 209.735 1.00 62.41  ? 3538 GLN A O     1 
ATOM   14308 C  CB    . GLN A 1 3538 ? 183.962 136.059 206.650 1.00 48.42  ? 3538 GLN A CB    1 
ATOM   14309 C  CG    . GLN A 1 3538 ? 184.040 135.599 205.211 1.00 53.70  ? 3538 GLN A CG    1 
ATOM   14310 C  CD    . GLN A 1 3538 ? 184.092 136.757 204.235 1.00 63.95  ? 3538 GLN A CD    1 
ATOM   14311 O  OE1   . GLN A 1 3538 ? 184.087 137.922 204.635 1.00 62.90  ? 3538 GLN A OE1   1 
ATOM   14312 N  NE2   . GLN A 1 3538 ? 184.139 136.444 202.946 1.00 67.47  ? 3538 GLN A NE2   1 
ATOM   14313 N  N     . ALA A 1 3539 ? 181.895 135.831 209.268 1.00 49.97  ? 3539 ALA A N     1 
ATOM   14314 C  CA    . ALA A 1 3539 ? 181.443 136.411 210.525 1.00 52.43  ? 3539 ALA A CA    1 
ATOM   14315 C  C     . ALA A 1 3539 ? 181.201 135.364 211.603 1.00 52.62  ? 3539 ALA A C     1 
ATOM   14316 O  O     . ALA A 1 3539 ? 180.726 135.714 212.688 1.00 55.57  ? 3539 ALA A O     1 
ATOM   14317 C  CB    . ALA A 1 3539 ? 180.166 137.227 210.303 1.00 46.35  ? 3539 ALA A CB    1 
ATOM   14318 N  N     . ASN A 1 3540 ? 181.513 134.096 211.324 1.00 47.69  ? 3540 ASN A N     1 
ATOM   14319 C  CA    . ASN A 1 3540 ? 181.321 132.995 212.270 1.00 49.95  ? 3540 ASN A CA    1 
ATOM   14320 C  C     . ASN A 1 3540 ? 179.863 132.883 212.710 1.00 54.74  ? 3540 ASN A C     1 
ATOM   14321 O  O     . ASN A 1 3540 ? 179.565 132.561 213.861 1.00 55.41  ? 3540 ASN A O     1 
ATOM   14322 C  CB    . ASN A 1 3540 ? 182.246 133.135 213.481 1.00 57.34  ? 3540 ASN A CB    1 
ATOM   14323 C  CG    . ASN A 1 3540 ? 183.574 132.433 213.282 1.00 66.46  ? 3540 ASN A CG    1 
ATOM   14324 O  OD1   . ASN A 1 3540 ? 184.077 132.336 212.162 1.00 64.11  ? 3540 ASN A OD1   1 
ATOM   14325 N  ND2   . ASN A 1 3540 ? 184.149 131.935 214.370 1.00 76.14  ? 3540 ASN A ND2   1 
ATOM   14326 N  N     . ILE A 1 3541 ? 178.946 133.143 211.783 1.00 53.66  ? 3541 ILE A N     1 
ATOM   14327 C  CA    . ILE A 1 3541 ? 177.517 132.981 212.019 1.00 51.11  ? 3541 ILE A CA    1 
ATOM   14328 C  C     . ILE A 1 3541 ? 177.098 131.646 211.422 1.00 52.78  ? 3541 ILE A C     1 
ATOM   14329 O  O     . ILE A 1 3541 ? 177.201 131.440 210.207 1.00 49.98  ? 3541 ILE A O     1 
ATOM   14330 C  CB    . ILE A 1 3541 ? 176.710 134.141 211.416 1.00 45.47  ? 3541 ILE A CB    1 
ATOM   14331 C  CG1   . ILE A 1 3541 ? 177.072 135.454 212.110 1.00 43.99  ? 3541 ILE A CG1   1 
ATOM   14332 C  CG2   . ILE A 1 3541 ? 175.219 133.870 211.531 1.00 44.59  ? 3541 ILE A CG2   1 
ATOM   14333 C  CD1   . ILE A 1 3541 ? 176.432 136.669 211.487 1.00 40.57  ? 3541 ILE A CD1   1 
ATOM   14334 N  N     . GLN A 1 3542 ? 176.630 130.739 212.274 1.00 56.04  ? 3542 GLN A N     1 
ATOM   14335 C  CA    . GLN A 1 3542 ? 176.334 129.379 211.848 1.00 58.15  ? 3542 GLN A CA    1 
ATOM   14336 C  C     . GLN A 1 3542 ? 175.029 129.335 211.065 1.00 58.11  ? 3542 GLN A C     1 
ATOM   14337 O  O     . GLN A 1 3542 ? 174.011 129.881 211.503 1.00 58.61  ? 3542 GLN A O     1 
ATOM   14338 C  CB    . GLN A 1 3542 ? 176.259 128.448 213.060 1.00 60.56  ? 3542 GLN A CB    1 
ATOM   14339 C  CG    . GLN A 1 3542 ? 177.491 128.444 213.978 1.00 64.08  ? 3542 GLN A CG    1 
ATOM   14340 C  CD    . GLN A 1 3542 ? 178.779 127.951 213.316 1.00 69.63  ? 3542 GLN A CD    1 
ATOM   14341 O  OE1   . GLN A 1 3542 ? 179.088 128.283 212.172 1.00 64.41  ? 3542 GLN A OE1   1 
ATOM   14342 N  NE2   . GLN A 1 3542 ? 179.540 127.152 214.054 1.00 70.46  ? 3542 GLN A NE2   1 
ATOM   14343 N  N     . PHE A 1 3543 ? 175.063 128.685 209.904 1.00 55.76  ? 3543 PHE A N     1 
ATOM   14344 C  CA    . PHE A 1 3543 ? 173.884 128.495 209.074 1.00 51.00  ? 3543 PHE A CA    1 
ATOM   14345 C  C     . PHE A 1 3543 ? 173.998 127.162 208.353 1.00 60.65  ? 3543 PHE A C     1 
ATOM   14346 O  O     . PHE A 1 3543 ? 175.093 126.756 207.954 1.00 63.13  ? 3543 PHE A O     1 
ATOM   14347 C  CB    . PHE A 1 3543 ? 173.714 129.637 208.060 1.00 45.56  ? 3543 PHE A CB    1 
ATOM   14348 C  CG    . PHE A 1 3543 ? 174.818 129.719 207.044 1.00 49.53  ? 3543 PHE A CG    1 
ATOM   14349 C  CD1   . PHE A 1 3543 ? 175.985 130.410 207.323 1.00 51.85  ? 3543 PHE A CD1   1 
ATOM   14350 C  CD2   . PHE A 1 3543 ? 174.685 129.115 205.804 1.00 50.61  ? 3543 PHE A CD2   1 
ATOM   14351 C  CE1   . PHE A 1 3543 ? 177.000 130.490 206.390 1.00 45.98  ? 3543 PHE A CE1   1 
ATOM   14352 C  CE2   . PHE A 1 3543 ? 175.698 129.191 204.868 1.00 50.28  ? 3543 PHE A CE2   1 
ATOM   14353 C  CZ    . PHE A 1 3543 ? 176.857 129.880 205.162 1.00 44.29  ? 3543 PHE A CZ    1 
ATOM   14354 N  N     . ARG A 1 3544 ? 172.866 126.482 208.195 1.00 66.83  ? 3544 ARG A N     1 
ATOM   14355 C  CA    . ARG A 1 3544 ? 172.860 125.194 207.517 1.00 65.36  ? 3544 ARG A CA    1 
ATOM   14356 C  C     . ARG A 1 3544 ? 173.061 125.376 206.017 1.00 70.25  ? 3544 ARG A C     1 
ATOM   14357 O  O     . ARG A 1 3544 ? 172.529 126.309 205.409 1.00 72.98  ? 3544 ARG A O     1 
ATOM   14358 C  CB    . ARG A 1 3544 ? 171.553 124.455 207.798 1.00 62.34  ? 3544 ARG A CB    1 
ATOM   14359 C  CG    . ARG A 1 3544 ? 171.470 123.093 207.143 1.00 79.49  ? 3544 ARG A CG    1 
ATOM   14360 C  CD    . ARG A 1 3544 ? 170.223 122.347 207.566 1.00 84.56  ? 3544 ARG A CD    1 
ATOM   14361 N  NE    . ARG A 1 3544 ? 170.304 121.941 208.962 1.00 87.83  ? 3544 ARG A NE    1 
ATOM   14362 C  CZ    . ARG A 1 3544 ? 169.303 121.414 209.651 1.00 92.69  ? 3544 ARG A CZ    1 
ATOM   14363 N  NH1   . ARG A 1 3544 ? 168.113 121.223 209.105 1.00 92.25  ? 3544 ARG A NH1   1 
ATOM   14364 N  NH2   . ARG A 1 3544 ? 169.501 121.068 210.918 1.00 94.55  ? 3544 ARG A NH2   1 
ATOM   14365 N  N     . THR A 1 3545 ? 173.836 124.471 205.419 1.00 73.03  ? 3545 THR A N     1 
ATOM   14366 C  CA    . THR A 1 3545 ? 174.241 124.590 204.025 1.00 78.89  ? 3545 THR A CA    1 
ATOM   14367 C  C     . THR A 1 3545 ? 173.549 123.612 203.088 1.00 81.35  ? 3545 THR A C     1 
ATOM   14368 O  O     . THR A 1 3545 ? 173.171 124.006 201.982 1.00 78.79  ? 3545 THR A O     1 
ATOM   14369 C  CB    . THR A 1 3545 ? 175.758 124.398 203.896 1.00 72.79  ? 3545 THR A CB    1 
ATOM   14370 O  OG1   . THR A 1 3545 ? 176.424 125.150 204.918 1.00 65.56  ? 3545 THR A OG1   1 
ATOM   14371 C  CG2   . THR A 1 3545 ? 176.243 124.869 202.535 1.00 73.06  ? 3545 THR A CG2   1 
ATOM   14372 N  N     . ASP A 1 3546 ? 173.370 122.352 203.494 1.00 82.17  ? 3546 ASP A N     1 
ATOM   14373 C  CA    . ASP A 1 3546 ? 172.835 121.354 202.572 1.00 84.60  ? 3546 ASP A CA    1 
ATOM   14374 C  C     . ASP A 1 3546 ? 171.373 121.616 202.230 1.00 85.53  ? 3546 ASP A C     1 
ATOM   14375 O  O     . ASP A 1 3546 ? 170.927 121.268 201.131 1.00 90.61  ? 3546 ASP A O     1 
ATOM   14376 C  CB    . ASP A 1 3546 ? 173.003 119.949 203.154 1.00 89.20  ? 3546 ASP A CB    1 
ATOM   14377 C  CG    . ASP A 1 3546 ? 172.382 119.803 204.528 1.00 87.93  ? 3546 ASP A CG    1 
ATOM   14378 O  OD1   . ASP A 1 3546 ? 171.890 120.812 205.072 1.00 81.89  ? 3546 ASP A OD1   1 
ATOM   14379 O  OD2   . ASP A 1 3546 ? 172.386 118.676 205.066 1.00 91.14  ? 3546 ASP A OD2   1 
ATOM   14380 N  N     . ILE A 1 3547 ? 170.614 122.220 203.148 1.00 82.19  ? 3547 ILE A N     1 
ATOM   14381 C  CA    . ILE A 1 3547 ? 169.210 122.499 202.866 1.00 78.21  ? 3547 ILE A CA    1 
ATOM   14382 C  C     . ILE A 1 3547 ? 169.100 123.605 201.819 1.00 78.22  ? 3547 ILE A C     1 
ATOM   14383 O  O     . ILE A 1 3547 ? 169.913 124.536 201.755 1.00 75.50  ? 3547 ILE A O     1 
ATOM   14384 C  CB    . ILE A 1 3547 ? 168.452 122.866 204.153 1.00 80.27  ? 3547 ILE A CB    1 
ATOM   14385 C  CG1   . ILE A 1 3547 ? 166.942 122.890 203.902 1.00 76.18  ? 3547 ILE A CG1   1 
ATOM   14386 C  CG2   . ILE A 1 3547 ? 168.923 124.207 204.700 1.00 75.49  ? 3547 ILE A CG2   1 
ATOM   14387 C  CD1   . ILE A 1 3547 ? 166.112 122.910 205.165 1.00 74.76  ? 3547 ILE A CD1   1 
ATOM   14388 N  N     . ALA A 1 3548 ? 168.085 123.485 200.968 1.00 70.63  ? 3548 ALA A N     1 
ATOM   14389 C  CA    . ALA A 1 3548 ? 167.852 124.430 199.889 1.00 65.91  ? 3548 ALA A CA    1 
ATOM   14390 C  C     . ALA A 1 3548 ? 166.756 125.415 200.274 1.00 57.72  ? 3548 ALA A C     1 
ATOM   14391 O  O     . ALA A 1 3548 ? 166.001 125.195 201.225 1.00 55.29  ? 3548 ALA A O     1 
ATOM   14392 C  CB    . ALA A 1 3548 ? 167.478 123.708 198.592 1.00 60.01  ? 3548 ALA A CB    1 
ATOM   14393 N  N     . ARG A 1 3549 ? 166.686 126.513 199.518 1.00 52.77  ? 3549 ARG A N     1 
ATOM   14394 C  CA    . ARG A 1 3549 ? 165.769 127.600 199.849 1.00 45.79  ? 3549 ARG A CA    1 
ATOM   14395 C  C     . ARG A 1 3549 ? 164.312 127.163 199.753 1.00 45.57  ? 3549 ARG A C     1 
ATOM   14396 O  O     . ARG A 1 3549 ? 163.500 127.490 200.627 1.00 50.93  ? 3549 ARG A O     1 
ATOM   14397 C  CB    . ARG A 1 3549 ? 166.033 128.788 198.926 1.00 38.33  ? 3549 ARG A CB    1 
ATOM   14398 C  CG    . ARG A 1 3549 ? 167.366 129.466 199.170 1.00 34.76  ? 3549 ARG A CG    1 
ATOM   14399 C  CD    . ARG A 1 3549 ? 167.505 130.723 198.336 1.00 34.87  ? 3549 ARG A CD    1 
ATOM   14400 N  NE    . ARG A 1 3549 ? 167.550 130.426 196.909 1.00 32.86  ? 3549 ARG A NE    1 
ATOM   14401 C  CZ    . ARG A 1 3549 ? 168.661 130.153 196.237 1.00 30.99  ? 3549 ARG A CZ    1 
ATOM   14402 N  NH1   . ARG A 1 3549 ? 169.840 130.125 196.835 1.00 28.79  ? 3549 ARG A NH1   1 
ATOM   14403 N  NH2   . ARG A 1 3549 ? 168.586 129.904 194.934 1.00 34.81  ? 3549 ARG A NH2   1 
ATOM   14404 N  N     . THR A 1 3550 ? 163.960 126.433 198.692 1.00 45.03  ? 3550 THR A N     1 
ATOM   14405 C  CA    . THR A 1 3550 ? 162.558 126.100 198.453 1.00 42.25  ? 3550 THR A CA    1 
ATOM   14406 C  C     . THR A 1 3550 ? 161.999 125.196 199.546 1.00 45.26  ? 3550 THR A C     1 
ATOM   14407 O  O     . THR A 1 3550 ? 160.876 125.405 200.018 1.00 46.62  ? 3550 THR A O     1 
ATOM   14408 C  CB    . THR A 1 3550 ? 162.402 125.441 197.082 1.00 45.28  ? 3550 THR A CB    1 
ATOM   14409 O  OG1   . THR A 1 3550 ? 163.170 124.232 197.040 1.00 57.38  ? 3550 THR A OG1   1 
ATOM   14410 C  CG2   . THR A 1 3550 ? 162.882 126.378 195.986 1.00 35.24  ? 3550 THR A CG2   1 
ATOM   14411 N  N     . GLU A 1 3551 ? 162.765 124.186 199.961 1.00 44.03  ? 3551 GLU A N     1 
ATOM   14412 C  CA    . GLU A 1 3551 ? 162.279 123.275 200.993 1.00 43.48  ? 3551 GLU A CA    1 
ATOM   14413 C  C     . GLU A 1 3551 ? 162.295 123.930 202.369 1.00 49.65  ? 3551 GLU A C     1 
ATOM   14414 O  O     . GLU A 1 3551 ? 161.504 123.562 203.245 1.00 55.86  ? 3551 GLU A O     1 
ATOM   14415 C  CB    . GLU A 1 3551 ? 163.106 121.989 200.999 1.00 48.75  ? 3551 GLU A CB    1 
ATOM   14416 C  CG    . GLU A 1 3551 ? 162.935 121.124 199.757 1.00 58.15  ? 3551 GLU A CG    1 
ATOM   14417 C  CD    . GLU A 1 3551 ? 163.796 121.578 198.597 1.00 66.59  ? 3551 GLU A CD    1 
ATOM   14418 O  OE1   . GLU A 1 3551 ? 164.577 122.534 198.776 1.00 68.44  ? 3551 GLU A OE1   1 
ATOM   14419 O  OE2   . GLU A 1 3551 ? 163.692 120.979 197.506 1.00 64.33  ? 3551 GLU A OE2   1 
ATOM   14420 N  N     . TYR A 1 3552 ? 163.193 124.892 202.587 1.00 48.24  ? 3552 TYR A N     1 
ATOM   14421 C  CA    . TYR A 1 3552 ? 163.238 125.562 203.882 1.00 43.73  ? 3552 TYR A CA    1 
ATOM   14422 C  C     . TYR A 1 3552 ? 162.105 126.570 204.028 1.00 40.89  ? 3552 TYR A C     1 
ATOM   14423 O  O     . TYR A 1 3552 ? 161.541 126.723 205.117 1.00 42.71  ? 3552 TYR A O     1 
ATOM   14424 C  CB    . TYR A 1 3552 ? 164.589 126.247 204.080 1.00 44.71  ? 3552 TYR A CB    1 
ATOM   14425 C  CG    . TYR A 1 3552 ? 164.783 126.793 205.477 1.00 43.07  ? 3552 TYR A CG    1 
ATOM   14426 C  CD1   . TYR A 1 3552 ? 164.756 125.952 206.581 1.00 50.83  ? 3552 TYR A CD1   1 
ATOM   14427 C  CD2   . TYR A 1 3552 ? 164.986 128.149 205.692 1.00 39.25  ? 3552 TYR A CD2   1 
ATOM   14428 C  CE1   . TYR A 1 3552 ? 164.929 126.444 207.859 1.00 51.85  ? 3552 TYR A CE1   1 
ATOM   14429 C  CE2   . TYR A 1 3552 ? 165.160 128.651 206.968 1.00 44.34  ? 3552 TYR A CE2   1 
ATOM   14430 C  CZ    . TYR A 1 3552 ? 165.131 127.794 208.047 1.00 50.88  ? 3552 TYR A CZ    1 
ATOM   14431 O  OH    . TYR A 1 3552 ? 165.304 128.288 209.320 1.00 50.43  ? 3552 TYR A OH    1 
ATOM   14432 N  N     . LEU A 1 3553 ? 161.757 127.264 202.948 1.00 38.92  ? 3553 LEU A N     1 
ATOM   14433 C  CA    . LEU A 1 3553 ? 160.747 128.312 202.998 1.00 37.11  ? 3553 LEU A CA    1 
ATOM   14434 C  C     . LEU A 1 3553 ? 159.347 127.819 202.660 1.00 39.42  ? 3553 LEU A C     1 
ATOM   14435 O  O     . LEU A 1 3553 ? 158.415 128.630 202.622 1.00 41.42  ? 3553 LEU A O     1 
ATOM   14436 C  CB    . LEU A 1 3553 ? 161.131 129.455 202.054 1.00 33.84  ? 3553 LEU A CB    1 
ATOM   14437 C  CG    . LEU A 1 3553 ? 162.205 130.404 202.584 1.00 24.13  ? 3553 LEU A CG    1 
ATOM   14438 C  CD1   . LEU A 1 3553 ? 162.733 131.300 201.477 1.00 20.05  ? 3553 LEU A CD1   1 
ATOM   14439 C  CD2   . LEU A 1 3553 ? 161.643 131.229 203.727 1.00 25.03  ? 3553 LEU A CD2   1 
ATOM   14440 N  N     . SER A 1 3554 ? 159.172 126.524 202.414 1.00 38.24  ? 3554 SER A N     1 
ATOM   14441 C  CA    . SER A 1 3554 ? 157.860 125.984 202.091 1.00 39.38  ? 3554 SER A CA    1 
ATOM   14442 C  C     . SER A 1 3554 ? 157.820 124.511 202.467 1.00 45.55  ? 3554 SER A C     1 
ATOM   14443 O  O     . SER A 1 3554 ? 158.850 123.833 202.510 1.00 50.62  ? 3554 SER A O     1 
ATOM   14444 C  CB    . SER A 1 3554 ? 157.529 126.167 200.605 1.00 39.82  ? 3554 SER A CB    1 
ATOM   14445 O  OG    . SER A 1 3554 ? 158.484 125.515 199.787 1.00 43.68  ? 3554 SER A OG    1 
ATOM   14446 N  N     . ASN A 1 3555 ? 156.616 124.021 202.736 1.00 46.20  ? 3555 ASN A N     1 
ATOM   14447 C  CA    . ASN A 1 3555 ? 156.402 122.610 203.016 1.00 50.68  ? 3555 ASN A CA    1 
ATOM   14448 C  C     . ASN A 1 3555 ? 155.777 121.919 201.807 1.00 50.88  ? 3555 ASN A C     1 
ATOM   14449 O  O     . ASN A 1 3555 ? 155.319 122.559 200.858 1.00 49.92  ? 3555 ASN A O     1 
ATOM   14450 C  CB    . ASN A 1 3555 ? 155.542 122.428 204.276 1.00 49.43  ? 3555 ASN A CB    1 
ATOM   14451 C  CG    . ASN A 1 3555 ? 154.153 123.029 204.146 1.00 51.31  ? 3555 ASN A CG    1 
ATOM   14452 O  OD1   . ASN A 1 3555 ? 153.754 123.495 203.083 1.00 48.69  ? 3555 ASN A OD1   1 
ATOM   14453 N  ND2   . ASN A 1 3555 ? 153.406 123.020 205.244 1.00 51.54  ? 3555 ASN A ND2   1 
ATOM   14454 N  N     . ALA A 1 3556 ? 155.773 120.586 201.852 1.00 49.52  ? 3556 ALA A N     1 
ATOM   14455 C  CA    . ALA A 1 3556 ? 155.365 119.805 200.688 1.00 49.52  ? 3556 ALA A CA    1 
ATOM   14456 C  C     . ALA A 1 3556 ? 153.894 120.017 200.350 1.00 53.65  ? 3556 ALA A C     1 
ATOM   14457 O  O     . ALA A 1 3556 ? 153.504 119.925 199.180 1.00 55.90  ? 3556 ALA A O     1 
ATOM   14458 C  CB    . ALA A 1 3556 ? 155.652 118.323 200.926 1.00 51.14  ? 3556 ALA A CB    1 
ATOM   14459 N  N     . ASP A 1 3557 ? 153.062 120.300 201.355 1.00 53.07  ? 3557 ASP A N     1 
ATOM   14460 C  CA    . ASP A 1 3557 ? 151.628 120.421 201.110 1.00 51.18  ? 3557 ASP A CA    1 
ATOM   14461 C  C     . ASP A 1 3557 ? 151.306 121.626 200.233 1.00 49.20  ? 3557 ASP A C     1 
ATOM   14462 O  O     . ASP A 1 3557 ? 150.595 121.499 199.228 1.00 51.31  ? 3557 ASP A O     1 
ATOM   14463 C  CB    . ASP A 1 3557 ? 150.876 120.504 202.438 1.00 56.56  ? 3557 ASP A CB    1 
ATOM   14464 C  CG    . ASP A 1 3557 ? 151.150 119.314 203.335 1.00 71.98  ? 3557 ASP A CG    1 
ATOM   14465 O  OD1   . ASP A 1 3557 ? 152.233 119.273 203.957 1.00 69.89  ? 3557 ASP A OD1   1 
ATOM   14466 O  OD2   . ASP A 1 3557 ? 150.284 118.417 203.417 1.00 80.43  ? 3557 ASP A OD2   1 
ATOM   14467 N  N     . GLU A 1 3558 ? 151.828 122.805 200.583 1.00 46.93  ? 3558 GLU A N     1 
ATOM   14468 C  CA    . GLU A 1 3558 ? 151.540 123.978 199.764 1.00 45.09  ? 3558 GLU A CA    1 
ATOM   14469 C  C     . GLU A 1 3558 ? 152.291 123.929 198.442 1.00 41.10  ? 3558 GLU A C     1 
ATOM   14470 O  O     . GLU A 1 3558 ? 151.846 124.531 197.459 1.00 41.98  ? 3558 GLU A O     1 
ATOM   14471 C  CB    . GLU A 1 3558 ? 151.867 125.265 200.522 1.00 47.21  ? 3558 GLU A CB    1 
ATOM   14472 C  CG    . GLU A 1 3558 ? 153.340 125.500 200.792 1.00 47.78  ? 3558 GLU A CG    1 
ATOM   14473 C  CD    . GLU A 1 3558 ? 153.577 126.752 201.613 1.00 54.45  ? 3558 GLU A CD    1 
ATOM   14474 O  OE1   . GLU A 1 3558 ? 152.587 127.416 201.983 1.00 60.11  ? 3558 GLU A OE1   1 
ATOM   14475 O  OE2   . GLU A 1 3558 ? 154.750 127.072 201.892 1.00 55.07  ? 3558 GLU A OE2   1 
ATOM   14476 N  N     . ARG A 1 3559 ? 153.421 123.220 198.392 1.00 39.62  ? 3559 ARG A N     1 
ATOM   14477 C  CA    . ARG A 1 3559 ? 154.086 122.998 197.112 1.00 35.15  ? 3559 ARG A CA    1 
ATOM   14478 C  C     . ARG A 1 3559 ? 153.206 122.179 196.177 1.00 39.79  ? 3559 ARG A C     1 
ATOM   14479 O  O     . ARG A 1 3559 ? 153.065 122.512 194.995 1.00 43.89  ? 3559 ARG A O     1 
ATOM   14480 C  CB    . ARG A 1 3559 ? 155.431 122.305 197.323 1.00 37.77  ? 3559 ARG A CB    1 
ATOM   14481 C  CG    . ARG A 1 3559 ? 156.609 123.258 197.438 1.00 39.57  ? 3559 ARG A CG    1 
ATOM   14482 C  CD    . ARG A 1 3559 ? 157.926 122.503 197.479 1.00 37.80  ? 3559 ARG A CD    1 
ATOM   14483 N  NE    . ARG A 1 3559 ? 158.475 122.429 198.826 1.00 40.61  ? 3559 ARG A NE    1 
ATOM   14484 C  CZ    . ARG A 1 3559 ? 158.871 121.307 199.412 1.00 48.33  ? 3559 ARG A CZ    1 
ATOM   14485 N  NH1   . ARG A 1 3559 ? 158.796 120.141 198.793 1.00 53.67  ? 3559 ARG A NH1   1 
ATOM   14486 N  NH2   . ARG A 1 3559 ? 159.353 121.356 200.650 1.00 50.11  ? 3559 ARG A NH2   1 
ATOM   14487 N  N     . LEU A 1 3560 ? 152.598 121.107 196.693 1.00 43.10  ? 3560 LEU A N     1 
ATOM   14488 C  CA    . LEU A 1 3560 ? 151.668 120.320 195.890 1.00 43.37  ? 3560 LEU A CA    1 
ATOM   14489 C  C     . LEU A 1 3560 ? 150.444 121.141 195.507 1.00 44.33  ? 3560 LEU A C     1 
ATOM   14490 O  O     . LEU A 1 3560 ? 149.913 121.002 194.399 1.00 45.47  ? 3560 LEU A O     1 
ATOM   14491 C  CB    . LEU A 1 3560 ? 151.251 119.060 196.649 1.00 44.48  ? 3560 LEU A CB    1 
ATOM   14492 C  CG    . LEU A 1 3560 ? 152.000 117.762 196.338 1.00 52.00  ? 3560 LEU A CG    1 
ATOM   14493 C  CD1   . LEU A 1 3560 ? 153.507 117.974 196.340 1.00 48.33  ? 3560 LEU A CD1   1 
ATOM   14494 C  CD2   . LEU A 1 3560 ? 151.607 116.673 197.325 1.00 58.71  ? 3560 LEU A CD2   1 
ATOM   14495 N  N     . ARG A 1 3561 ? 149.976 121.995 196.420 1.00 40.35  ? 3561 ARG A N     1 
ATOM   14496 C  CA    . ARG A 1 3561 ? 148.860 122.881 196.105 1.00 39.54  ? 3561 ARG A CA    1 
ATOM   14497 C  C     . ARG A 1 3561 ? 149.210 123.821 194.957 1.00 43.50  ? 3561 ARG A C     1 
ATOM   14498 O  O     . ARG A 1 3561 ? 148.374 124.091 194.087 1.00 47.01  ? 3561 ARG A O     1 
ATOM   14499 C  CB    . ARG A 1 3561 ? 148.457 123.675 197.347 1.00 44.71  ? 3561 ARG A CB    1 
ATOM   14500 C  CG    . ARG A 1 3561 ? 147.320 124.654 197.122 1.00 47.76  ? 3561 ARG A CG    1 
ATOM   14501 C  CD    . ARG A 1 3561 ? 146.606 124.974 198.427 1.00 54.59  ? 3561 ARG A CD    1 
ATOM   14502 N  NE    . ARG A 1 3561 ? 147.507 125.513 199.439 1.00 57.10  ? 3561 ARG A NE    1 
ATOM   14503 C  CZ    . ARG A 1 3561 ? 148.107 126.695 199.369 1.00 62.29  ? 3561 ARG A CZ    1 
ATOM   14504 N  NH1   . ARG A 1 3561 ? 147.907 127.514 198.349 1.00 57.75  ? 3561 ARG A NH1   1 
ATOM   14505 N  NH2   . ARG A 1 3561 ? 148.923 127.067 200.351 1.00 61.75  ? 3561 ARG A NH2   1 
ATOM   14506 N  N     . TRP A 1 3562 ? 150.442 124.335 194.945 1.00 43.79  ? 3562 TRP A N     1 
ATOM   14507 C  CA    . TRP A 1 3562 ? 150.868 125.226 193.870 1.00 37.45  ? 3562 TRP A CA    1 
ATOM   14508 C  C     . TRP A 1 3562 ? 150.890 124.506 192.527 1.00 39.45  ? 3562 TRP A C     1 
ATOM   14509 O  O     . TRP A 1 3562 ? 150.496 125.078 191.504 1.00 43.52  ? 3562 TRP A O     1 
ATOM   14510 C  CB    . TRP A 1 3562 ? 152.243 125.811 194.191 1.00 34.42  ? 3562 TRP A CB    1 
ATOM   14511 C  CG    . TRP A 1 3562 ? 152.240 126.743 195.364 1.00 32.62  ? 3562 TRP A CG    1 
ATOM   14512 C  CD1   . TRP A 1 3562 ? 151.168 127.416 195.872 1.00 33.76  ? 3562 TRP A CD1   1 
ATOM   14513 C  CD2   . TRP A 1 3562 ? 153.361 127.099 196.181 1.00 33.72  ? 3562 TRP A CD2   1 
ATOM   14514 N  NE1   . TRP A 1 3562 ? 151.553 128.172 196.952 1.00 31.84  ? 3562 TRP A NE1   1 
ATOM   14515 C  CE2   . TRP A 1 3562 ? 152.895 127.995 197.163 1.00 32.89  ? 3562 TRP A CE2   1 
ATOM   14516 C  CE3   . TRP A 1 3562 ? 154.715 126.748 196.177 1.00 30.01  ? 3562 TRP A CE3   1 
ATOM   14517 C  CZ2   . TRP A 1 3562 ? 153.732 128.544 198.130 1.00 32.08  ? 3562 TRP A CZ2   1 
ATOM   14518 C  CZ3   . TRP A 1 3562 ? 155.544 127.294 197.138 1.00 24.59  ? 3562 TRP A CZ3   1 
ATOM   14519 C  CH2   . TRP A 1 3562 ? 155.050 128.182 198.101 1.00 28.54  ? 3562 TRP A CH2   1 
ATOM   14520 N  N     . GLN A 1 3563 ? 151.351 123.252 192.508 1.00 39.82  ? 3563 GLN A N     1 
ATOM   14521 C  CA    . GLN A 1 3563 ? 151.345 122.483 191.266 1.00 45.81  ? 3563 GLN A CA    1 
ATOM   14522 C  C     . GLN A 1 3563 ? 149.928 122.305 190.737 1.00 45.32  ? 3563 GLN A C     1 
ATOM   14523 O  O     . GLN A 1 3563 ? 149.694 122.386 189.525 1.00 41.99  ? 3563 GLN A O     1 
ATOM   14524 C  CB    . GLN A 1 3563 ? 152.012 121.122 191.477 1.00 44.85  ? 3563 GLN A CB    1 
ATOM   14525 C  CG    . GLN A 1 3563 ? 153.347 121.168 192.208 1.00 47.70  ? 3563 GLN A CG    1 
ATOM   14526 C  CD    . GLN A 1 3563 ? 154.445 121.852 191.413 1.00 52.42  ? 3563 GLN A CD    1 
ATOM   14527 O  OE1   . GLN A 1 3563 ? 154.289 122.132 190.225 1.00 50.77  ? 3563 GLN A OE1   1 
ATOM   14528 N  NE2   . GLN A 1 3563 ? 155.566 122.123 192.070 1.00 53.82  ? 3563 GLN A NE2   1 
ATOM   14529 N  N     . ALA A 1 3564 ? 148.968 122.058 191.631 1.00 43.85  ? 3564 ALA A N     1 
ATOM   14530 C  CA    . ALA A 1 3564 ? 147.571 121.974 191.221 1.00 42.38  ? 3564 ALA A CA    1 
ATOM   14531 C  C     . ALA A 1 3564 ? 147.041 123.304 190.703 1.00 45.00  ? 3564 ALA A C     1 
ATOM   14532 O  O     . ALA A 1 3564 ? 146.006 123.323 190.029 1.00 47.42  ? 3564 ALA A O     1 
ATOM   14533 C  CB    . ALA A 1 3564 ? 146.709 121.487 192.386 1.00 44.43  ? 3564 ALA A CB    1 
ATOM   14534 N  N     . SER A 1 3565 ? 147.722 124.411 191.003 1.00 46.02  ? 3565 SER A N     1 
ATOM   14535 C  CA    . SER A 1 3565 ? 147.351 125.731 190.509 1.00 41.87  ? 3565 SER A CA    1 
ATOM   14536 C  C     . SER A 1 3565 ? 148.134 126.118 189.259 1.00 39.73  ? 3565 SER A C     1 
ATOM   14537 O  O     . SER A 1 3565 ? 148.345 127.309 189.003 1.00 43.90  ? 3565 SER A O     1 
ATOM   14538 C  CB    . SER A 1 3565 ? 147.544 126.780 191.604 1.00 40.55  ? 3565 SER A CB    1 
ATOM   14539 O  OG    . SER A 1 3565 ? 146.683 126.535 192.702 1.00 43.40  ? 3565 SER A OG    1 
ATOM   14540 N  N     . SER A 1 3566 ? 148.572 125.126 188.480 1.00 39.79  ? 3566 SER A N     1 
ATOM   14541 C  CA    . SER A 1 3566 ? 149.288 125.347 187.222 1.00 42.78  ? 3566 SER A CA    1 
ATOM   14542 C  C     . SER A 1 3566 ? 150.575 126.143 187.432 1.00 42.15  ? 3566 SER A C     1 
ATOM   14543 O  O     . SER A 1 3566 ? 150.952 126.976 186.605 1.00 45.41  ? 3566 SER A O     1 
ATOM   14544 C  CB    . SER A 1 3566 ? 148.391 126.030 186.187 1.00 50.26  ? 3566 SER A CB    1 
ATOM   14545 O  OG    . SER A 1 3566 ? 148.349 127.431 186.396 1.00 45.05  ? 3566 SER A OG    1 
ATOM   14546 N  N     . LEU A 1 3567 ? 151.257 125.887 188.547 1.00 40.55  ? 3567 LEU A N     1 
ATOM   14547 C  CA    . LEU A 1 3567 ? 152.571 126.492 188.737 1.00 39.10  ? 3567 LEU A CA    1 
ATOM   14548 C  C     . LEU A 1 3567 ? 153.651 125.542 188.235 1.00 43.83  ? 3567 LEU A C     1 
ATOM   14549 O  O     . LEU A 1 3567 ? 153.672 124.374 188.639 1.00 48.98  ? 3567 LEU A O     1 
ATOM   14550 C  CB    . LEU A 1 3567 ? 152.823 126.823 190.200 1.00 36.73  ? 3567 LEU A CB    1 
ATOM   14551 C  CG    . LEU A 1 3567 ? 154.152 127.528 190.484 1.00 34.64  ? 3567 LEU A CG    1 
ATOM   14552 C  CD1   . LEU A 1 3567 ? 154.014 129.031 190.300 1.00 32.20  ? 3567 LEU A CD1   1 
ATOM   14553 C  CD2   . LEU A 1 3567 ? 154.668 127.199 191.875 1.00 31.71  ? 3567 LEU A CD2   1 
ATOM   14554 N  N     . PRO A 1 3568 ? 154.541 125.993 187.352 1.00 40.29  ? 3568 PRO A N     1 
ATOM   14555 C  CA    . PRO A 1 3568 ? 155.596 125.103 186.851 1.00 39.45  ? 3568 PRO A CA    1 
ATOM   14556 C  C     . PRO A 1 3568 ? 156.496 124.613 187.976 1.00 43.14  ? 3568 PRO A C     1 
ATOM   14557 O  O     . PRO A 1 3568 ? 156.727 125.307 188.968 1.00 49.83  ? 3568 PRO A O     1 
ATOM   14558 C  CB    . PRO A 1 3568 ? 156.369 125.982 185.858 1.00 41.86  ? 3568 PRO A CB    1 
ATOM   14559 C  CG    . PRO A 1 3568 ? 155.916 127.383 186.112 1.00 41.05  ? 3568 PRO A CG    1 
ATOM   14560 C  CD    . PRO A 1 3568 ? 154.548 127.306 186.689 1.00 40.17  ? 3568 PRO A CD    1 
ATOM   14561 N  N     . ALA A 1 3569 ? 157.005 123.394 187.807 1.00 40.67  ? 3569 ALA A N     1 
ATOM   14562 C  CA    . ALA A 1 3569 ? 157.839 122.725 188.805 1.00 46.86  ? 3569 ALA A CA    1 
ATOM   14563 C  C     . ALA A 1 3569 ? 159.251 123.289 188.890 1.00 52.35  ? 3569 ALA A C     1 
ATOM   14564 O  O     . ALA A 1 3569 ? 160.083 122.685 189.581 1.00 56.00  ? 3569 ALA A O     1 
ATOM   14565 C  CB    . ALA A 1 3569 ? 157.897 121.225 188.510 1.00 41.58  ? 3569 ALA A CB    1 
ATOM   14566 N  N     . ASP A 1 3570 ? 159.549 124.398 188.220 1.00 48.59  ? 3570 ASP A N     1 
ATOM   14567 C  CA    . ASP A 1 3570 ? 160.878 124.988 188.286 1.00 42.37  ? 3570 ASP A CA    1 
ATOM   14568 C  C     . ASP A 1 3570 ? 161.170 125.489 189.697 1.00 41.21  ? 3570 ASP A C     1 
ATOM   14569 O  O     . ASP A 1 3570 ? 160.276 125.935 190.421 1.00 41.67  ? 3570 ASP A O     1 
ATOM   14570 C  CB    . ASP A 1 3570 ? 160.995 126.136 187.282 1.00 38.24  ? 3570 ASP A CB    1 
ATOM   14571 C  CG    . ASP A 1 3570 ? 162.402 126.699 187.191 1.00 44.07  ? 3570 ASP A CG    1 
ATOM   14572 O  OD1   . ASP A 1 3570 ? 163.320 126.149 187.835 1.00 49.86  ? 3570 ASP A OD1   1 
ATOM   14573 O  OD2   . ASP A 1 3570 ? 162.590 127.702 186.471 1.00 39.80  ? 3570 ASP A OD2   1 
ATOM   14574 N  N     . ASP A 1 3571 ? 162.444 125.401 190.087 1.00 43.65  ? 3571 ASP A N     1 
ATOM   14575 C  CA    . ASP A 1 3571 ? 162.850 125.893 191.400 1.00 37.19  ? 3571 ASP A CA    1 
ATOM   14576 C  C     . ASP A 1 3571 ? 162.720 127.408 191.487 1.00 31.72  ? 3571 ASP A C     1 
ATOM   14577 O  O     . ASP A 1 3571 ? 162.328 127.944 192.531 1.00 32.90  ? 3571 ASP A O     1 
ATOM   14578 C  CB    . ASP A 1 3571 ? 164.283 125.457 191.705 1.00 46.53  ? 3571 ASP A CB    1 
ATOM   14579 C  CG    . ASP A 1 3571 ? 164.349 124.091 192.358 1.00 63.20  ? 3571 ASP A CG    1 
ATOM   14580 O  OD1   . ASP A 1 3571 ? 163.445 123.266 192.106 1.00 65.53  ? 3571 ASP A OD1   1 
ATOM   14581 O  OD2   . ASP A 1 3571 ? 165.302 123.841 193.125 1.00 70.19  ? 3571 ASP A OD2   1 
ATOM   14582 N  N     . LEU A 1 3572 ? 163.051 128.117 190.405 1.00 29.89  ? 3572 LEU A N     1 
ATOM   14583 C  CA    . LEU A 1 3572 ? 162.876 129.565 190.390 1.00 27.74  ? 3572 LEU A CA    1 
ATOM   14584 C  C     . LEU A 1 3572 ? 161.407 129.939 190.536 1.00 28.51  ? 3572 LEU A C     1 
ATOM   14585 O  O     . LEU A 1 3572 ? 161.067 130.889 191.250 1.00 33.44  ? 3572 LEU A O     1 
ATOM   14586 C  CB    . LEU A 1 3572 ? 163.461 130.151 189.104 1.00 29.56  ? 3572 LEU A CB    1 
ATOM   14587 C  CG    . LEU A 1 3572 ? 163.404 131.670 188.924 1.00 22.86  ? 3572 LEU A CG    1 
ATOM   14588 C  CD1   . LEU A 1 3572 ? 164.711 132.182 188.344 1.00 22.82  ? 3572 LEU A CD1   1 
ATOM   14589 C  CD2   . LEU A 1 3572 ? 162.237 132.073 188.035 1.00 24.85  ? 3572 LEU A CD2   1 
ATOM   14590 N  N     . CYS A 1 3573 ? 160.520 129.199 189.869 1.00 29.18  ? 3573 CYS A N     1 
ATOM   14591 C  CA    . CYS A 1 3573 ? 159.092 129.451 190.021 1.00 26.14  ? 3573 CYS A CA    1 
ATOM   14592 C  C     . CYS A 1 3573 ? 158.609 129.115 191.426 1.00 28.10  ? 3573 CYS A C     1 
ATOM   14593 O  O     . CYS A 1 3573 ? 157.715 129.789 191.947 1.00 33.71  ? 3573 CYS A O     1 
ATOM   14594 C  CB    . CYS A 1 3573 ? 158.307 128.662 188.976 1.00 30.10  ? 3573 CYS A CB    1 
ATOM   14595 S  SG    . CYS A 1 3573 ? 158.814 129.009 187.278 1.00 63.15  ? 3573 CYS A SG    1 
ATOM   14596 N  N     . THR A 1 3574 ? 159.186 128.088 192.056 1.00 25.07  ? 3574 THR A N     1 
ATOM   14597 C  CA    . THR A 1 3574 ? 158.846 127.795 193.445 1.00 21.07  ? 3574 THR A CA    1 
ATOM   14598 C  C     . THR A 1 3574 ? 159.271 128.934 194.365 1.00 22.47  ? 3574 THR A C     1 
ATOM   14599 O  O     . THR A 1 3574 ? 158.526 129.323 195.272 1.00 26.90  ? 3574 THR A O     1 
ATOM   14600 C  CB    . THR A 1 3574 ? 159.498 126.483 193.882 1.00 25.30  ? 3574 THR A CB    1 
ATOM   14601 O  OG1   . THR A 1 3574 ? 159.113 125.435 192.983 1.00 32.85  ? 3574 THR A OG1   1 
ATOM   14602 C  CG2   . THR A 1 3574 ? 159.064 126.116 195.291 1.00 23.39  ? 3574 THR A CG2   1 
ATOM   14603 N  N     . GLU A 1 3575 ? 160.464 129.488 194.138 1.00 23.09  ? 3575 GLU A N     1 
ATOM   14604 C  CA    . GLU A 1 3575 ? 160.909 130.638 194.920 1.00 19.68  ? 3575 GLU A CA    1 
ATOM   14605 C  C     . GLU A 1 3575 ? 159.998 131.838 194.697 1.00 19.10  ? 3575 GLU A C     1 
ATOM   14606 O  O     . GLU A 1 3575 ? 159.664 132.560 195.644 1.00 21.10  ? 3575 GLU A O     1 
ATOM   14607 C  CB    . GLU A 1 3575 ? 162.352 130.987 194.562 1.00 19.82  ? 3575 GLU A CB    1 
ATOM   14608 C  CG    . GLU A 1 3575 ? 163.364 129.927 194.960 1.00 26.53  ? 3575 GLU A CG    1 
ATOM   14609 C  CD    . GLU A 1 3575 ? 164.695 130.101 194.258 1.00 32.95  ? 3575 GLU A CD    1 
ATOM   14610 O  OE1   . GLU A 1 3575 ? 164.802 131.000 193.398 1.00 32.70  ? 3575 GLU A OE1   1 
ATOM   14611 O  OE2   . GLU A 1 3575 ? 165.635 129.339 194.565 1.00 34.38  ? 3575 GLU A OE2   1 
ATOM   14612 N  N     . ASN A 1 3576 ? 159.587 132.067 193.448 1.00 19.70  ? 3576 ASN A N     1 
ATOM   14613 C  CA    . ASN A 1 3576 ? 158.678 133.169 193.151 1.00 18.08  ? 3576 ASN A CA    1 
ATOM   14614 C  C     . ASN A 1 3576 ? 157.335 132.982 193.845 1.00 18.50  ? 3576 ASN A C     1 
ATOM   14615 O  O     . ASN A 1 3576 ? 156.761 133.942 194.372 1.00 23.34  ? 3576 ASN A O     1 
ATOM   14616 C  CB    . ASN A 1 3576 ? 158.491 133.296 191.640 1.00 17.20  ? 3576 ASN A CB    1 
ATOM   14617 C  CG    . ASN A 1 3576 ? 159.718 133.848 190.946 1.00 20.58  ? 3576 ASN A CG    1 
ATOM   14618 O  OD1   . ASN A 1 3576 ? 160.719 134.163 191.589 1.00 22.28  ? 3576 ASN A OD1   1 
ATOM   14619 N  ND2   . ASN A 1 3576 ? 159.648 133.969 189.627 1.00 23.21  ? 3576 ASN A ND2   1 
ATOM   14620 N  N     . ALA A 1 3577 ? 156.814 131.753 193.852 1.00 16.25  ? 3577 ALA A N     1 
ATOM   14621 C  CA    . ALA A 1 3577 ? 155.573 131.472 194.564 1.00 14.97  ? 3577 ALA A CA    1 
ATOM   14622 C  C     . ALA A 1 3577 ? 155.736 131.667 196.065 1.00 17.70  ? 3577 ALA A C     1 
ATOM   14623 O  O     . ALA A 1 3577 ? 154.793 132.098 196.739 1.00 20.87  ? 3577 ALA A O     1 
ATOM   14624 C  CB    . ALA A 1 3577 ? 155.100 130.052 194.260 1.00 20.23  ? 3577 ALA A CB    1 
ATOM   14625 N  N     . ILE A 1 3578 ? 156.913 131.344 196.604 1.00 18.54  ? 3578 ILE A N     1 
ATOM   14626 C  CA    . ILE A 1 3578 ? 157.193 131.632 198.008 1.00 19.88  ? 3578 ILE A CA    1 
ATOM   14627 C  C     . ILE A 1 3578 ? 157.146 133.133 198.257 1.00 21.70  ? 3578 ILE A C     1 
ATOM   14628 O  O     . ILE A 1 3578 ? 156.584 133.597 199.257 1.00 26.08  ? 3578 ILE A O     1 
ATOM   14629 C  CB    . ILE A 1 3578 ? 158.552 131.030 198.413 1.00 17.72  ? 3578 ILE A CB    1 
ATOM   14630 C  CG1   . ILE A 1 3578 ? 158.429 129.519 198.606 1.00 21.24  ? 3578 ILE A CG1   1 
ATOM   14631 C  CG2   . ILE A 1 3578 ? 159.077 131.688 199.679 1.00 16.36  ? 3578 ILE A CG2   1 
ATOM   14632 C  CD1   . ILE A 1 3578 ? 159.759 128.807 198.682 1.00 23.52  ? 3578 ILE A CD1   1 
ATOM   14633 N  N     . MET A 1 3579 ? 157.729 133.917 197.347 1.00 20.43  ? 3579 MET A N     1 
ATOM   14634 C  CA    . MET A 1 3579 ? 157.684 135.370 197.474 1.00 13.99  ? 3579 MET A CA    1 
ATOM   14635 C  C     . MET A 1 3579 ? 156.262 135.903 197.357 1.00 15.85  ? 3579 MET A C     1 
ATOM   14636 O  O     . MET A 1 3579 ? 155.905 136.870 198.038 1.00 17.14  ? 3579 MET A O     1 
ATOM   14637 C  CB    . MET A 1 3579 ? 158.578 136.015 196.417 1.00 13.95  ? 3579 MET A CB    1 
ATOM   14638 C  CG    . MET A 1 3579 ? 160.033 135.602 196.510 1.00 15.79  ? 3579 MET A CG    1 
ATOM   14639 S  SD    . MET A 1 3579 ? 161.060 136.450 195.303 1.00 20.36  ? 3579 MET A SD    1 
ATOM   14640 C  CE    . MET A 1 3579 ? 162.621 135.606 195.538 1.00 22.74  ? 3579 MET A CE    1 
ATOM   14641 N  N     . LEU A 1 3580 ? 155.439 135.294 196.500 1.00 19.13  ? 3580 LEU A N     1 
ATOM   14642 C  CA    . LEU A 1 3580 ? 154.055 135.724 196.341 1.00 16.70  ? 3580 LEU A CA    1 
ATOM   14643 C  C     . LEU A 1 3580 ? 153.200 135.430 197.565 1.00 20.65  ? 3580 LEU A C     1 
ATOM   14644 O  O     . LEU A 1 3580 ? 152.071 135.925 197.643 1.00 26.21  ? 3580 LEU A O     1 
ATOM   14645 C  CB    . LEU A 1 3580 ? 153.436 135.062 195.109 1.00 12.91  ? 3580 LEU A CB    1 
ATOM   14646 C  CG    . LEU A 1 3580 ? 153.932 135.569 193.755 1.00 13.68  ? 3580 LEU A CG    1 
ATOM   14647 C  CD1   . LEU A 1 3580 ? 153.379 134.715 192.626 1.00 18.28  ? 3580 LEU A CD1   1 
ATOM   14648 C  CD2   . LEU A 1 3580 ? 153.553 137.026 193.563 1.00 14.56  ? 3580 LEU A CD2   1 
ATOM   14649 N  N     . LYS A 1 3581 ? 153.699 134.636 198.508 1.00 18.24  ? 3581 LYS A N     1 
ATOM   14650 C  CA    . LYS A 1 3581 ? 153.010 134.359 199.762 1.00 19.90  ? 3581 LYS A CA    1 
ATOM   14651 C  C     . LYS A 1 3581 ? 153.613 135.097 200.946 1.00 21.56  ? 3581 LYS A C     1 
ATOM   14652 O  O     . LYS A 1 3581 ? 152.875 135.636 201.773 1.00 22.85  ? 3581 LYS A O     1 
ATOM   14653 C  CB    . LYS A 1 3581 ? 153.016 132.851 200.041 1.00 22.68  ? 3581 LYS A CB    1 
ATOM   14654 C  CG    . LYS A 1 3581 ? 152.784 132.471 201.492 1.00 25.07  ? 3581 LYS A CG    1 
ATOM   14655 C  CD    . LYS A 1 3581 ? 153.535 131.199 201.852 1.00 31.86  ? 3581 LYS A CD    1 
ATOM   14656 C  CE    . LYS A 1 3581 ? 153.133 130.690 203.225 1.00 44.08  ? 3581 LYS A CE    1 
ATOM   14657 N  NZ    . LYS A 1 3581 ? 153.800 129.400 203.553 1.00 46.33  ? 3581 LYS A NZ    1 
ATOM   14658 N  N     . ARG A 1 3582 ? 154.942 135.143 201.041 1.00 23.43  ? 3582 ARG A N     1 
ATOM   14659 C  CA    . ARG A 1 3582 ? 155.634 135.864 202.108 1.00 19.40  ? 3582 ARG A CA    1 
ATOM   14660 C  C     . ARG A 1 3582 ? 156.108 137.204 201.551 1.00 24.27  ? 3582 ARG A C     1 
ATOM   14661 O  O     . ARG A 1 3582 ? 157.257 137.369 201.143 1.00 33.39  ? 3582 ARG A O     1 
ATOM   14662 C  CB    . ARG A 1 3582 ? 156.800 135.040 202.645 1.00 17.17  ? 3582 ARG A CB    1 
ATOM   14663 C  CG    . ARG A 1 3582 ? 156.424 133.671 203.176 1.00 23.00  ? 3582 ARG A CG    1 
ATOM   14664 C  CD    . ARG A 1 3582 ? 157.671 132.884 203.544 1.00 27.63  ? 3582 ARG A CD    1 
ATOM   14665 N  NE    . ARG A 1 3582 ? 157.358 131.573 204.098 1.00 36.10  ? 3582 ARG A NE    1 
ATOM   14666 C  CZ    . ARG A 1 3582 ? 157.162 131.332 205.386 1.00 39.77  ? 3582 ARG A CZ    1 
ATOM   14667 N  NH1   . ARG A 1 3582 ? 157.239 132.296 206.289 1.00 33.85  ? 3582 ARG A NH1   1 
ATOM   14668 N  NH2   . ARG A 1 3582 ? 156.883 130.093 205.779 1.00 45.37  ? 3582 ARG A NH2   1 
ATOM   14669 N  N     . PHE A 1 3583 ? 155.201 138.177 201.533 1.00 23.46  ? 3583 PHE A N     1 
ATOM   14670 C  CA    . PHE A 1 3583 ? 155.521 139.512 201.048 1.00 24.68  ? 3583 PHE A CA    1 
ATOM   14671 C  C     . PHE A 1 3583 ? 154.984 140.559 202.012 1.00 29.81  ? 3583 PHE A C     1 
ATOM   14672 O  O     . PHE A 1 3583 ? 153.912 140.386 202.598 1.00 33.87  ? 3583 PHE A O     1 
ATOM   14673 C  CB    . PHE A 1 3583 ? 154.954 139.750 199.637 1.00 23.19  ? 3583 PHE A CB    1 
ATOM   14674 C  CG    . PHE A 1 3583 ? 153.452 139.736 199.567 1.00 26.35  ? 3583 PHE A CG    1 
ATOM   14675 C  CD1   . PHE A 1 3583 ? 152.769 138.557 199.329 1.00 25.88  ? 3583 PHE A CD1   1 
ATOM   14676 C  CD2   . PHE A 1 3583 ? 152.725 140.906 199.716 1.00 30.16  ? 3583 PHE A CD2   1 
ATOM   14677 C  CE1   . PHE A 1 3583 ? 151.390 138.542 199.259 1.00 28.54  ? 3583 PHE A CE1   1 
ATOM   14678 C  CE2   . PHE A 1 3583 ? 151.347 140.896 199.647 1.00 30.05  ? 3583 PHE A CE2   1 
ATOM   14679 C  CZ    . PHE A 1 3583 ? 150.679 139.712 199.417 1.00 33.13  ? 3583 PHE A CZ    1 
ATOM   14680 N  N     . ASN A 1 3584 ? 155.742 141.643 202.174 1.00 32.06  ? 3584 ASN A N     1 
ATOM   14681 C  CA    . ASN A 1 3584 ? 155.304 142.804 202.939 1.00 34.80  ? 3584 ASN A CA    1 
ATOM   14682 C  C     . ASN A 1 3584 ? 154.730 143.892 202.041 1.00 35.15  ? 3584 ASN A C     1 
ATOM   14683 O  O     . ASN A 1 3584 ? 153.629 144.388 202.294 1.00 42.62  ? 3584 ASN A O     1 
ATOM   14684 C  CB    . ASN A 1 3584 ? 156.464 143.362 203.770 1.00 37.03  ? 3584 ASN A CB    1 
ATOM   14685 C  CG    . ASN A 1 3584 ? 156.958 142.380 204.813 1.00 46.64  ? 3584 ASN A CG    1 
ATOM   14686 O  OD1   . ASN A 1 3584 ? 158.093 141.909 204.748 1.00 43.61  ? 3584 ASN A OD1   1 
ATOM   14687 N  ND2   . ASN A 1 3584 ? 156.106 142.064 205.781 1.00 54.89  ? 3584 ASN A ND2   1 
ATOM   14688 N  N     . ARG A 1 3585 ? 155.455 144.275 200.994 1.00 28.27  ? 3585 ARG A N     1 
ATOM   14689 C  CA    . ARG A 1 3585 ? 154.908 145.144 199.966 1.00 25.10  ? 3585 ARG A CA    1 
ATOM   14690 C  C     . ARG A 1 3585 ? 154.221 144.310 198.893 1.00 23.76  ? 3585 ARG A C     1 
ATOM   14691 O  O     . ARG A 1 3585 ? 154.618 143.176 198.612 1.00 25.03  ? 3585 ARG A O     1 
ATOM   14692 C  CB    . ARG A 1 3585 ? 155.994 146.014 199.332 1.00 20.57  ? 3585 ARG A CB    1 
ATOM   14693 C  CG    . ARG A 1 3585 ? 156.637 147.002 200.283 1.00 19.89  ? 3585 ARG A CG    1 
ATOM   14694 C  CD    . ARG A 1 3585 ? 157.893 147.603 199.680 1.00 18.27  ? 3585 ARG A CD    1 
ATOM   14695 N  NE    . ARG A 1 3585 ? 158.885 146.587 199.347 1.00 16.09  ? 3585 ARG A NE    1 
ATOM   14696 C  CZ    . ARG A 1 3585 ? 159.883 146.763 198.492 1.00 16.01  ? 3585 ARG A CZ    1 
ATOM   14697 N  NH1   . ARG A 1 3585 ? 160.058 147.911 197.861 1.00 17.32  ? 3585 ARG A NH1   1 
ATOM   14698 N  NH2   . ARG A 1 3585 ? 160.727 145.760 198.266 1.00 15.65  ? 3585 ARG A NH2   1 
ATOM   14699 N  N     . TYR A 1 3586 ? 153.183 144.885 198.300 1.00 23.47  ? 3586 TYR A N     1 
ATOM   14700 C  CA    . TYR A 1 3586 ? 152.381 144.159 197.329 1.00 21.47  ? 3586 TYR A CA    1 
ATOM   14701 C  C     . TYR A 1 3586 ? 153.229 143.803 196.111 1.00 21.37  ? 3586 TYR A C     1 
ATOM   14702 O  O     . TYR A 1 3586 ? 153.922 144.674 195.568 1.00 25.08  ? 3586 TYR A O     1 
ATOM   14703 C  CB    . TYR A 1 3586 ? 151.172 144.996 196.920 1.00 24.77  ? 3586 TYR A CB    1 
ATOM   14704 C  CG    . TYR A 1 3586 ? 150.175 145.174 198.043 1.00 26.38  ? 3586 TYR A CG    1 
ATOM   14705 C  CD1   . TYR A 1 3586 ? 149.582 144.075 198.649 1.00 27.50  ? 3586 TYR A CD1   1 
ATOM   14706 C  CD2   . TYR A 1 3586 ? 149.841 146.438 198.508 1.00 26.63  ? 3586 TYR A CD2   1 
ATOM   14707 C  CE1   . TYR A 1 3586 ? 148.675 144.231 199.679 1.00 30.51  ? 3586 TYR A CE1   1 
ATOM   14708 C  CE2   . TYR A 1 3586 ? 148.935 146.604 199.537 1.00 28.86  ? 3586 TYR A CE2   1 
ATOM   14709 C  CZ    . TYR A 1 3586 ? 148.355 145.497 200.119 1.00 34.76  ? 3586 TYR A CZ    1 
ATOM   14710 O  OH    . TYR A 1 3586 ? 147.453 145.654 201.145 1.00 39.10  ? 3586 TYR A OH    1 
ATOM   14711 N  N     . PRO A 1 3587 ? 153.211 142.550 195.662 1.00 19.24  ? 3587 PRO A N     1 
ATOM   14712 C  CA    . PRO A 1 3587 ? 154.146 142.127 194.615 1.00 16.04  ? 3587 PRO A CA    1 
ATOM   14713 C  C     . PRO A 1 3587 ? 153.838 142.759 193.268 1.00 19.28  ? 3587 PRO A C     1 
ATOM   14714 O  O     . PRO A 1 3587 ? 152.693 143.088 192.950 1.00 23.74  ? 3587 PRO A O     1 
ATOM   14715 C  CB    . PRO A 1 3587 ? 153.964 140.603 194.563 1.00 13.76  ? 3587 PRO A CB    1 
ATOM   14716 C  CG    . PRO A 1 3587 ? 153.101 140.247 195.743 1.00 20.07  ? 3587 PRO A CG    1 
ATOM   14717 C  CD    . PRO A 1 3587 ? 152.310 141.464 196.070 1.00 22.52  ? 3587 PRO A CD    1 
ATOM   14718 N  N     . LEU A 1 3588 ? 154.892 142.927 192.472 1.00 19.31  ? 3588 LEU A N     1 
ATOM   14719 C  CA    . LEU A 1 3588 ? 154.785 143.324 191.073 1.00 19.48  ? 3588 LEU A CA    1 
ATOM   14720 C  C     . LEU A 1 3588 ? 155.352 142.178 190.246 1.00 23.07  ? 3588 LEU A C     1 
ATOM   14721 O  O     . LEU A 1 3588 ? 156.569 141.967 190.223 1.00 27.17  ? 3588 LEU A O     1 
ATOM   14722 C  CB    . LEU A 1 3588 ? 155.525 144.636 190.806 1.00 18.79  ? 3588 LEU A CB    1 
ATOM   14723 C  CG    . LEU A 1 3588 ? 155.335 145.315 189.444 1.00 20.98  ? 3588 LEU A CG    1 
ATOM   14724 C  CD1   . LEU A 1 3588 ? 155.532 146.814 189.578 1.00 28.16  ? 3588 LEU A CD1   1 
ATOM   14725 C  CD2   . LEU A 1 3588 ? 156.281 144.760 188.390 1.00 24.47  ? 3588 LEU A CD2   1 
ATOM   14726 N  N     . ILE A 1 3589 ? 154.476 141.444 189.571 1.00 24.71  ? 3589 ILE A N     1 
ATOM   14727 C  CA    . ILE A 1 3589 ? 154.854 140.220 188.876 1.00 24.93  ? 3589 ILE A CA    1 
ATOM   14728 C  C     . ILE A 1 3589 ? 155.260 140.559 187.449 1.00 27.10  ? 3589 ILE A C     1 
ATOM   14729 O  O     . ILE A 1 3589 ? 154.530 141.251 186.732 1.00 29.46  ? 3589 ILE A O     1 
ATOM   14730 C  CB    . ILE A 1 3589 ? 153.702 139.202 188.894 1.00 21.25  ? 3589 ILE A CB    1 
ATOM   14731 C  CG1   . ILE A 1 3589 ? 153.174 139.023 190.318 1.00 21.24  ? 3589 ILE A CG1   1 
ATOM   14732 C  CG2   . ILE A 1 3589 ? 154.165 137.871 188.341 1.00 25.36  ? 3589 ILE A CG2   1 
ATOM   14733 C  CD1   . ILE A 1 3589 ? 151.773 138.461 190.380 1.00 20.40  ? 3589 ILE A CD1   1 
ATOM   14734 N  N     . ILE A 1 3590 ? 156.430 140.077 187.036 1.00 26.56  ? 3590 ILE A N     1 
ATOM   14735 C  CA    . ILE A 1 3590 ? 156.907 140.292 185.675 1.00 26.30  ? 3590 ILE A CA    1 
ATOM   14736 C  C     . ILE A 1 3590 ? 156.974 138.955 184.951 1.00 28.69  ? 3590 ILE A C     1 
ATOM   14737 O  O     . ILE A 1 3590 ? 157.983 138.246 185.027 1.00 33.65  ? 3590 ILE A O     1 
ATOM   14738 C  CB    . ILE A 1 3590 ? 158.277 140.992 185.664 1.00 25.46  ? 3590 ILE A CB    1 
ATOM   14739 C  CG1   . ILE A 1 3590 ? 158.286 142.162 186.648 1.00 25.69  ? 3590 ILE A CG1   1 
ATOM   14740 C  CG2   . ILE A 1 3590 ? 158.619 141.468 184.261 1.00 26.93  ? 3590 ILE A CG2   1 
ATOM   14741 C  CD1   . ILE A 1 3590 ? 159.624 142.856 186.756 1.00 23.31  ? 3590 ILE A CD1   1 
ATOM   14742 N  N     . ASP A 1 3591 ? 155.903 138.601 184.244 1.00 33.63  ? 3591 ASP A N     1 
ATOM   14743 C  CA    . ASP A 1 3591 ? 155.845 137.352 183.497 1.00 37.00  ? 3591 ASP A CA    1 
ATOM   14744 C  C     . ASP A 1 3591 ? 155.495 137.638 182.043 1.00 39.53  ? 3591 ASP A C     1 
ATOM   14745 O  O     . ASP A 1 3591 ? 154.431 138.218 181.767 1.00 41.48  ? 3591 ASP A O     1 
ATOM   14746 C  CB    . ASP A 1 3591 ? 154.834 136.382 184.124 1.00 37.85  ? 3591 ASP A CB    1 
ATOM   14747 C  CG    . ASP A 1 3591 ? 153.443 136.980 184.260 1.00 47.14  ? 3591 ASP A CG    1 
ATOM   14748 O  OD1   . ASP A 1 3591 ? 152.676 136.954 183.277 1.00 45.14  ? 3591 ASP A OD1   1 
ATOM   14749 O  OD2   . ASP A 1 3591 ? 153.115 137.480 185.355 1.00 53.55  ? 3591 ASP A OD2   1 
ATOM   14750 N  N     . PRO A 1 3592 ? 156.356 137.296 181.087 1.00 35.64  ? 3592 PRO A N     1 
ATOM   14751 C  CA    . PRO A 1 3592 ? 155.979 137.442 179.676 1.00 38.05  ? 3592 PRO A CA    1 
ATOM   14752 C  C     . PRO A 1 3592 ? 155.179 136.250 179.178 1.00 44.72  ? 3592 PRO A C     1 
ATOM   14753 O  O     . PRO A 1 3592 ? 154.400 136.364 178.227 1.00 50.01  ? 3592 PRO A O     1 
ATOM   14754 C  CB    . PRO A 1 3592 ? 157.332 137.554 178.965 1.00 37.07  ? 3592 PRO A CB    1 
ATOM   14755 C  CG    . PRO A 1 3592 ? 158.267 136.789 179.837 1.00 41.67  ? 3592 PRO A CG    1 
ATOM   14756 C  CD    . PRO A 1 3592 ? 157.776 136.942 181.253 1.00 32.33  ? 3592 PRO A CD    1 
ATOM   14757 N  N     . SER A 1 3593 ? 155.366 135.096 179.824 1.00 45.67  ? 3593 SER A N     1 
ATOM   14758 C  CA    . SER A 1 3593 ? 154.665 133.887 179.405 1.00 45.63  ? 3593 SER A CA    1 
ATOM   14759 C  C     . SER A 1 3593 ? 153.192 133.926 179.788 1.00 46.16  ? 3593 SER A C     1 
ATOM   14760 O  O     . SER A 1 3593 ? 152.360 133.319 179.104 1.00 57.19  ? 3593 SER A O     1 
ATOM   14761 C  CB    . SER A 1 3593 ? 155.337 132.656 180.012 1.00 49.18  ? 3593 SER A CB    1 
ATOM   14762 O  OG    . SER A 1 3593 ? 156.660 132.508 179.529 1.00 53.02  ? 3593 SER A OG    1 
ATOM   14763 N  N     . GLY A 1 3594 ? 152.850 134.625 180.867 1.00 45.22  ? 3594 GLY A N     1 
ATOM   14764 C  CA    . GLY A 1 3594 ? 151.481 134.701 181.327 1.00 47.25  ? 3594 GLY A CA    1 
ATOM   14765 C  C     . GLY A 1 3594 ? 151.048 133.591 182.258 1.00 45.70  ? 3594 GLY A C     1 
ATOM   14766 O  O     . GLY A 1 3594 ? 149.885 133.583 182.683 1.00 48.51  ? 3594 GLY A O     1 
ATOM   14767 N  N     . GLN A 1 3595 ? 151.937 132.654 182.590 1.00 46.09  ? 3595 GLN A N     1 
ATOM   14768 C  CA    . GLN A 1 3595 ? 151.570 131.569 183.492 1.00 45.55  ? 3595 GLN A CA    1 
ATOM   14769 C  C     . GLN A 1 3595 ? 151.476 132.032 184.941 1.00 44.12  ? 3595 GLN A C     1 
ATOM   14770 O  O     . GLN A 1 3595 ? 150.708 131.455 185.719 1.00 46.79  ? 3595 GLN A O     1 
ATOM   14771 C  CB    . GLN A 1 3595 ? 152.573 130.420 183.370 1.00 45.04  ? 3595 GLN A CB    1 
ATOM   14772 C  CG    . GLN A 1 3595 ? 153.994 130.781 183.772 1.00 51.78  ? 3595 GLN A CG    1 
ATOM   14773 C  CD    . GLN A 1 3595 ? 155.034 130.044 182.954 1.00 63.80  ? 3595 GLN A CD    1 
ATOM   14774 O  OE1   . GLN A 1 3595 ? 154.701 129.247 182.078 1.00 64.59  ? 3595 GLN A OE1   1 
ATOM   14775 N  NE2   . GLN A 1 3595 ? 156.305 130.307 183.238 1.00 66.87  ? 3595 GLN A NE2   1 
ATOM   14776 N  N     . ALA A 1 3596 ? 152.244 133.056 185.322 1.00 38.39  ? 3596 ALA A N     1 
ATOM   14777 C  CA    . ALA A 1 3596 ? 152.183 133.558 186.691 1.00 30.40  ? 3596 ALA A CA    1 
ATOM   14778 C  C     . ALA A 1 3596 ? 150.821 134.168 186.999 1.00 38.32  ? 3596 ALA A C     1 
ATOM   14779 O  O     . ALA A 1 3596 ? 150.284 133.979 188.097 1.00 42.32  ? 3596 ALA A O     1 
ATOM   14780 C  CB    . ALA A 1 3596 ? 153.294 134.577 186.927 1.00 28.78  ? 3596 ALA A CB    1 
ATOM   14781 N  N     . THR A 1 3597 ? 150.251 134.911 186.048 1.00 42.10  ? 3597 THR A N     1 
ATOM   14782 C  CA    . THR A 1 3597 ? 148.919 135.471 186.251 1.00 39.63  ? 3597 THR A CA    1 
ATOM   14783 C  C     . THR A 1 3597 ? 147.876 134.371 186.394 1.00 42.08  ? 3597 THR A C     1 
ATOM   14784 O  O     . THR A 1 3597 ? 146.976 134.465 187.235 1.00 43.53  ? 3597 THR A O     1 
ATOM   14785 C  CB    . THR A 1 3597 ? 148.555 136.405 185.098 1.00 46.98  ? 3597 THR A CB    1 
ATOM   14786 O  OG1   . THR A 1 3597 ? 148.101 135.633 183.980 1.00 56.06  ? 3597 THR A OG1   1 
ATOM   14787 C  CG2   . THR A 1 3597 ? 149.760 137.233 184.682 1.00 43.80  ? 3597 THR A CG2   1 
ATOM   14788 N  N     . GLU A 1 3598 ? 147.978 133.320 185.576 1.00 41.25  ? 3598 GLU A N     1 
ATOM   14789 C  CA    . GLU A 1 3598 ? 147.056 132.196 185.700 1.00 41.22  ? 3598 GLU A CA    1 
ATOM   14790 C  C     . GLU A 1 3598 ? 147.205 131.511 187.052 1.00 41.51  ? 3598 GLU A C     1 
ATOM   14791 O  O     . GLU A 1 3598 ? 146.210 131.119 187.672 1.00 45.68  ? 3598 GLU A O     1 
ATOM   14792 C  CB    . GLU A 1 3598 ? 147.286 131.200 184.564 1.00 46.19  ? 3598 GLU A CB    1 
ATOM   14793 C  CG    . GLU A 1 3598 ? 146.529 131.526 183.288 1.00 64.43  ? 3598 GLU A CG    1 
ATOM   14794 C  CD    . GLU A 1 3598 ? 146.612 130.414 182.260 1.00 83.25  ? 3598 GLU A CD    1 
ATOM   14795 O  OE1   . GLU A 1 3598 ? 145.845 129.436 182.376 1.00 89.80  ? 3598 GLU A OE1   1 
ATOM   14796 O  OE2   . GLU A 1 3598 ? 147.447 130.519 181.337 1.00 75.85  ? 3598 GLU A OE2   1 
ATOM   14797 N  N     . PHE A 1 3599 ? 148.444 131.357 187.524 1.00 39.15  ? 3599 PHE A N     1 
ATOM   14798 C  CA    . PHE A 1 3599 ? 148.676 130.767 188.838 1.00 34.84  ? 3599 PHE A CA    1 
ATOM   14799 C  C     . PHE A 1 3599 ? 148.064 131.623 189.940 1.00 34.79  ? 3599 PHE A C     1 
ATOM   14800 O  O     . PHE A 1 3599 ? 147.470 131.097 190.890 1.00 36.76  ? 3599 PHE A O     1 
ATOM   14801 C  CB    . PHE A 1 3599 ? 150.179 130.583 189.059 1.00 31.92  ? 3599 PHE A CB    1 
ATOM   14802 C  CG    . PHE A 1 3599 ? 150.584 130.501 190.503 1.00 29.65  ? 3599 PHE A CG    1 
ATOM   14803 C  CD1   . PHE A 1 3599 ? 150.389 129.336 191.225 1.00 34.29  ? 3599 PHE A CD1   1 
ATOM   14804 C  CD2   . PHE A 1 3599 ? 151.174 131.583 191.134 1.00 27.30  ? 3599 PHE A CD2   1 
ATOM   14805 C  CE1   . PHE A 1 3599 ? 150.768 129.255 192.551 1.00 32.53  ? 3599 PHE A CE1   1 
ATOM   14806 C  CE2   . PHE A 1 3599 ? 151.553 131.508 192.461 1.00 24.71  ? 3599 PHE A CE2   1 
ATOM   14807 C  CZ    . PHE A 1 3599 ? 151.349 130.343 193.169 1.00 27.82  ? 3599 PHE A CZ    1 
ATOM   14808 N  N     . ILE A 1 3600 ? 148.196 132.946 189.828 1.00 38.69  ? 3600 ILE A N     1 
ATOM   14809 C  CA    . ILE A 1 3600 ? 147.613 133.847 190.820 1.00 37.86  ? 3600 ILE A CA    1 
ATOM   14810 C  C     . ILE A 1 3600 ? 146.092 133.746 190.809 1.00 41.78  ? 3600 ILE A C     1 
ATOM   14811 O  O     . ILE A 1 3600 ? 145.451 133.689 191.866 1.00 43.63  ? 3600 ILE A O     1 
ATOM   14812 C  CB    . ILE A 1 3600 ? 148.089 135.291 190.575 1.00 31.75  ? 3600 ILE A CB    1 
ATOM   14813 C  CG1   . ILE A 1 3600 ? 149.525 135.467 191.070 1.00 24.28  ? 3600 ILE A CG1   1 
ATOM   14814 C  CG2   . ILE A 1 3600 ? 147.166 136.288 191.258 1.00 32.57  ? 3600 ILE A CG2   1 
ATOM   14815 C  CD1   . ILE A 1 3600 ? 149.688 135.236 192.555 1.00 24.11  ? 3600 ILE A CD1   1 
ATOM   14816 N  N     . MET A 1 3601 ? 145.491 133.719 189.616 1.00 39.17  ? 3601 MET A N     1 
ATOM   14817 C  CA    . MET A 1 3601 ? 144.039 133.594 189.520 1.00 37.56  ? 3601 MET A CA    1 
ATOM   14818 C  C     . MET A 1 3601 ? 143.555 132.268 190.095 1.00 45.73  ? 3601 MET A C     1 
ATOM   14819 O  O     . MET A 1 3601 ? 142.516 132.218 190.762 1.00 50.38  ? 3601 MET A O     1 
ATOM   14820 C  CB    . MET A 1 3601 ? 143.588 133.746 188.067 1.00 41.21  ? 3601 MET A CB    1 
ATOM   14821 C  CG    . MET A 1 3601 ? 143.951 135.079 187.432 1.00 48.96  ? 3601 MET A CG    1 
ATOM   14822 S  SD    . MET A 1 3601 ? 142.904 136.439 187.983 1.00 59.41  ? 3601 MET A SD    1 
ATOM   14823 C  CE    . MET A 1 3601 ? 141.292 135.661 187.937 1.00 46.53  ? 3601 MET A CE    1 
ATOM   14824 N  N     . ASN A 1 3602 ? 144.289 131.182 189.840 1.00 44.69  ? 3602 ASN A N     1 
ATOM   14825 C  CA    . ASN A 1 3602 ? 143.905 129.885 190.387 1.00 42.22  ? 3602 ASN A CA    1 
ATOM   14826 C  C     . ASN A 1 3602 ? 144.036 129.859 191.905 1.00 44.24  ? 3602 ASN A C     1 
ATOM   14827 O  O     . ASN A 1 3602 ? 143.191 129.278 192.596 1.00 51.15  ? 3602 ASN A O     1 
ATOM   14828 C  CB    . ASN A 1 3602 ? 144.748 128.777 189.757 1.00 39.10  ? 3602 ASN A CB    1 
ATOM   14829 C  CG    . ASN A 1 3602 ? 144.482 128.614 188.275 1.00 42.92  ? 3602 ASN A CG    1 
ATOM   14830 O  OD1   . ASN A 1 3602 ? 143.357 128.795 187.812 1.00 53.46  ? 3602 ASN A OD1   1 
ATOM   14831 N  ND2   . ASN A 1 3602 ? 145.519 128.268 187.522 1.00 40.34  ? 3602 ASN A ND2   1 
ATOM   14832 N  N     . GLU A 1 3603 ? 145.092 130.476 192.443 1.00 42.61  ? 3603 GLU A N     1 
ATOM   14833 C  CA    . GLU A 1 3603 ? 145.304 130.462 193.888 1.00 44.48  ? 3603 GLU A CA    1 
ATOM   14834 C  C     . GLU A 1 3603 ? 144.193 131.204 194.620 1.00 48.37  ? 3603 GLU A C     1 
ATOM   14835 O  O     . GLU A 1 3603 ? 143.679 130.728 195.639 1.00 50.79  ? 3603 GLU A O     1 
ATOM   14836 C  CB    . GLU A 1 3603 ? 146.665 131.072 194.224 1.00 39.05  ? 3603 GLU A CB    1 
ATOM   14837 C  CG    . GLU A 1 3603 ? 147.832 130.105 194.134 1.00 40.60  ? 3603 GLU A CG    1 
ATOM   14838 C  CD    . GLU A 1 3603 ? 147.683 128.910 195.056 1.00 50.82  ? 3603 GLU A CD    1 
ATOM   14839 O  OE1   . GLU A 1 3603 ? 147.005 127.933 194.673 1.00 53.43  ? 3603 GLU A OE1   1 
ATOM   14840 O  OE2   . GLU A 1 3603 ? 148.245 128.948 196.170 1.00 55.80  ? 3603 GLU A OE2   1 
ATOM   14841 N  N     . TYR A 1 3604 ? 143.807 132.374 194.114 1.00 50.23  ? 3604 TYR A N     1 
ATOM   14842 C  CA    . TYR A 1 3604 ? 142.797 133.205 194.752 1.00 51.46  ? 3604 TYR A CA    1 
ATOM   14843 C  C     . TYR A 1 3604 ? 141.424 133.043 194.111 1.00 54.52  ? 3604 TYR A C     1 
ATOM   14844 O  O     . TYR A 1 3604 ? 140.580 133.938 194.229 1.00 54.15  ? 3604 TYR A O     1 
ATOM   14845 C  CB    . TYR A 1 3604 ? 143.230 134.671 194.728 1.00 47.42  ? 3604 TYR A CB    1 
ATOM   14846 C  CG    . TYR A 1 3604 ? 144.413 134.964 195.624 1.00 44.43  ? 3604 TYR A CG    1 
ATOM   14847 C  CD1   . TYR A 1 3604 ? 145.708 134.676 195.213 1.00 43.19  ? 3604 TYR A CD1   1 
ATOM   14848 C  CD2   . TYR A 1 3604 ? 144.235 135.522 196.882 1.00 47.13  ? 3604 TYR A CD2   1 
ATOM   14849 C  CE1   . TYR A 1 3604 ? 146.791 134.938 196.028 1.00 42.11  ? 3604 TYR A CE1   1 
ATOM   14850 C  CE2   . TYR A 1 3604 ? 145.312 135.788 197.704 1.00 47.46  ? 3604 TYR A CE2   1 
ATOM   14851 C  CZ    . TYR A 1 3604 ? 146.587 135.494 197.272 1.00 49.07  ? 3604 TYR A CZ    1 
ATOM   14852 O  OH    . TYR A 1 3604 ? 147.664 135.757 198.088 1.00 51.64  ? 3604 TYR A OH    1 
ATOM   14853 N  N     . LYS A 1 3605 ? 141.187 131.918 193.432 1.00 56.32  ? 3605 LYS A N     1 
ATOM   14854 C  CA    . LYS A 1 3605 ? 139.876 131.665 192.845 1.00 57.48  ? 3605 LYS A CA    1 
ATOM   14855 C  C     . LYS A 1 3605 ? 138.806 131.540 193.923 1.00 58.32  ? 3605 LYS A C     1 
ATOM   14856 O  O     . LYS A 1 3605 ? 137.689 132.046 193.762 1.00 55.33  ? 3605 LYS A O     1 
ATOM   14857 C  CB    . LYS A 1 3605 ? 139.925 130.402 191.986 1.00 56.55  ? 3605 LYS A CB    1 
ATOM   14858 C  CG    . LYS A 1 3605 ? 138.649 130.118 191.215 1.00 61.15  ? 3605 LYS A CG    1 
ATOM   14859 C  CD    . LYS A 1 3605 ? 138.762 128.813 190.444 1.00 68.77  ? 3605 LYS A CD    1 
ATOM   14860 C  CE    . LYS A 1 3605 ? 139.683 128.961 189.244 1.00 67.15  ? 3605 LYS A CE    1 
ATOM   14861 N  NZ    . LYS A 1 3605 ? 139.720 127.723 188.416 1.00 77.70  ? 3605 LYS A NZ    1 
ATOM   14862 N  N     . ASP A 1 3606 ? 139.130 130.868 195.030 1.00 60.00  ? 3606 ASP A N     1 
ATOM   14863 C  CA    . ASP A 1 3606 ? 138.173 130.717 196.120 1.00 62.78  ? 3606 ASP A CA    1 
ATOM   14864 C  C     . ASP A 1 3606 ? 137.914 132.025 196.857 1.00 61.58  ? 3606 ASP A C     1 
ATOM   14865 O  O     . ASP A 1 3606 ? 136.908 132.131 197.566 1.00 58.52  ? 3606 ASP A O     1 
ATOM   14866 C  CB    . ASP A 1 3606 ? 138.657 129.641 197.096 1.00 66.29  ? 3606 ASP A CB    1 
ATOM   14867 C  CG    . ASP A 1 3606 ? 140.006 129.969 197.715 1.00 71.34  ? 3606 ASP A CG    1 
ATOM   14868 O  OD1   . ASP A 1 3606 ? 140.609 130.999 197.345 1.00 69.78  ? 3606 ASP A OD1   1 
ATOM   14869 O  OD2   . ASP A 1 3606 ? 140.466 129.189 198.575 1.00 71.61  ? 3606 ASP A OD2   1 
ATOM   14870 N  N     . ARG A 1 3607 ? 138.791 133.016 196.710 1.00 59.68  ? 3607 ARG A N     1 
ATOM   14871 C  CA    . ARG A 1 3607 ? 138.574 134.342 197.272 1.00 55.12  ? 3607 ARG A CA    1 
ATOM   14872 C  C     . ARG A 1 3607 ? 138.037 135.330 196.245 1.00 55.10  ? 3607 ARG A C     1 
ATOM   14873 O  O     . ARG A 1 3607 ? 138.222 136.539 196.412 1.00 57.33  ? 3607 ARG A O     1 
ATOM   14874 C  CB    . ARG A 1 3607 ? 139.866 134.878 197.896 1.00 52.67  ? 3607 ARG A CB    1 
ATOM   14875 C  CG    . ARG A 1 3607 ? 139.946 134.670 199.402 1.00 61.01  ? 3607 ARG A CG    1 
ATOM   14876 C  CD    . ARG A 1 3607 ? 141.378 134.547 199.899 1.00 63.62  ? 3607 ARG A CD    1 
ATOM   14877 N  NE    . ARG A 1 3607 ? 142.092 133.434 199.285 1.00 61.14  ? 3607 ARG A NE    1 
ATOM   14878 C  CZ    . ARG A 1 3607 ? 143.394 133.218 199.420 1.00 61.25  ? 3607 ARG A CZ    1 
ATOM   14879 N  NH1   . ARG A 1 3607 ? 144.156 134.017 200.148 1.00 57.10  ? 3607 ARG A NH1   1 
ATOM   14880 N  NH2   . ARG A 1 3607 ? 143.944 132.170 198.811 1.00 61.24  ? 3607 ARG A NH2   1 
ATOM   14881 N  N     . LYS A 1 3608 ? 137.348 134.837 195.210 1.00 56.43  ? 3608 LYS A N     1 
ATOM   14882 C  CA    . LYS A 1 3608 ? 136.756 135.637 194.130 1.00 59.61  ? 3608 LYS A CA    1 
ATOM   14883 C  C     . LYS A 1 3608 ? 137.670 136.790 193.704 1.00 57.15  ? 3608 LYS A C     1 
ATOM   14884 O  O     . LYS A 1 3608 ? 137.305 137.966 193.757 1.00 55.25  ? 3608 LYS A O     1 
ATOM   14885 C  CB    . LYS A 1 3608 ? 135.355 136.153 194.500 1.00 61.07  ? 3608 LYS A CB    1 
ATOM   14886 C  CG    . LYS A 1 3608 ? 135.040 136.282 195.985 1.00 62.74  ? 3608 LYS A CG    1 
ATOM   14887 C  CD    . LYS A 1 3608 ? 133.557 136.509 196.221 1.00 66.79  ? 3608 LYS A CD    1 
ATOM   14888 C  CE    . LYS A 1 3608 ? 133.216 136.418 197.699 1.00 62.44  ? 3608 LYS A CE    1 
ATOM   14889 N  NZ    . LYS A 1 3608 ? 131.756 136.570 197.944 1.00 62.72  ? 3608 LYS A NZ    1 
ATOM   14890 N  N     . ILE A 1 3609 ? 138.880 136.427 193.277 1.00 55.52  ? 3609 ILE A N     1 
ATOM   14891 C  CA    . ILE A 1 3609 ? 139.790 137.408 192.700 1.00 49.57  ? 3609 ILE A CA    1 
ATOM   14892 C  C     . ILE A 1 3609 ? 139.247 137.871 191.355 1.00 55.19  ? 3609 ILE A C     1 
ATOM   14893 O  O     . ILE A 1 3609 ? 138.641 137.093 190.605 1.00 57.33  ? 3609 ILE A O     1 
ATOM   14894 C  CB    . ILE A 1 3609 ? 141.208 136.823 192.569 1.00 45.62  ? 3609 ILE A CB    1 
ATOM   14895 C  CG1   . ILE A 1 3609 ? 142.208 137.914 192.174 1.00 39.50  ? 3609 ILE A CG1   1 
ATOM   14896 C  CG2   . ILE A 1 3609 ? 141.236 135.672 191.575 1.00 47.55  ? 3609 ILE A CG2   1 
ATOM   14897 C  CD1   . ILE A 1 3609 ? 143.653 137.501 192.323 1.00 44.15  ? 3609 ILE A CD1   1 
ATOM   14898 N  N     . THR A 1 3610 ? 139.439 139.151 191.052 1.00 52.98  ? 3610 THR A N     1 
ATOM   14899 C  CA    . THR A 1 3610 ? 138.984 139.739 189.800 1.00 51.64  ? 3610 THR A CA    1 
ATOM   14900 C  C     . THR A 1 3610 ? 140.174 140.319 189.047 1.00 48.21  ? 3610 THR A C     1 
ATOM   14901 O  O     . THR A 1 3610 ? 141.116 140.833 189.661 1.00 45.39  ? 3610 THR A O     1 
ATOM   14902 C  CB    . THR A 1 3610 ? 137.920 140.814 190.050 1.00 54.92  ? 3610 THR A CB    1 
ATOM   14903 O  OG1   . THR A 1 3610 ? 137.377 141.257 188.799 1.00 65.59  ? 3610 THR A OG1   1 
ATOM   14904 C  CG2   . THR A 1 3610 ? 138.496 142.001 190.807 1.00 50.82  ? 3610 THR A CG2   1 
ATOM   14905 N  N     . ARG A 1 3611 ? 140.140 140.209 187.722 1.00 53.79  ? 3611 ARG A N     1 
ATOM   14906 C  CA    . ARG A 1 3611 ? 141.215 140.725 186.889 1.00 49.54  ? 3611 ARG A CA    1 
ATOM   14907 C  C     . ARG A 1 3611 ? 140.898 142.144 186.438 1.00 48.89  ? 3611 ARG A C     1 
ATOM   14908 O  O     . ARG A 1 3611 ? 139.758 142.462 186.087 1.00 55.49  ? 3611 ARG A O     1 
ATOM   14909 C  CB    . ARG A 1 3611 ? 141.431 139.821 185.676 1.00 53.56  ? 3611 ARG A CB    1 
ATOM   14910 C  CG    . ARG A 1 3611 ? 142.879 139.709 185.232 1.00 44.65  ? 3611 ARG A CG    1 
ATOM   14911 C  CD    . ARG A 1 3611 ? 142.985 139.019 183.884 1.00 53.98  ? 3611 ARG A CD    1 
ATOM   14912 N  NE    . ARG A 1 3611 ? 144.359 138.662 183.556 1.00 61.66  ? 3611 ARG A NE    1 
ATOM   14913 C  CZ    . ARG A 1 3611 ? 144.776 137.424 183.324 1.00 59.70  ? 3611 ARG A CZ    1 
ATOM   14914 N  NH1   . ARG A 1 3611 ? 143.949 136.394 183.387 1.00 56.24  ? 3611 ARG A NH1   1 
ATOM   14915 N  NH2   . ARG A 1 3611 ? 146.053 137.216 183.020 1.00 55.26  ? 3611 ARG A NH2   1 
ATOM   14916 N  N     . THR A 1 3612 ? 141.918 142.998 186.449 1.00 42.54  ? 3612 THR A N     1 
ATOM   14917 C  CA    . THR A 1 3612 ? 141.745 144.412 186.152 1.00 45.36  ? 3612 THR A CA    1 
ATOM   14918 C  C     . THR A 1 3612 ? 143.011 144.899 185.457 1.00 48.01  ? 3612 THR A C     1 
ATOM   14919 O  O     . THR A 1 3612 ? 144.060 144.255 185.518 1.00 55.55  ? 3612 THR A O     1 
ATOM   14920 C  CB    . THR A 1 3612 ? 141.443 145.201 187.439 1.00 47.87  ? 3612 THR A CB    1 
ATOM   14921 O  OG1   . THR A 1 3612 ? 140.284 144.646 188.071 1.00 53.54  ? 3612 THR A OG1   1 
ATOM   14922 C  CG2   . THR A 1 3612 ? 141.152 146.666 187.144 1.00 53.24  ? 3612 THR A CG2   1 
ATOM   14923 N  N     . SER A 1 3613 ? 142.897 146.026 184.757 1.00 46.10  ? 3613 SER A N     1 
ATOM   14924 C  CA    . SER A 1 3613 ? 144.038 146.658 184.113 1.00 51.63  ? 3613 SER A CA    1 
ATOM   14925 C  C     . SER A 1 3613 ? 144.030 148.146 184.430 1.00 55.90  ? 3613 SER A C     1 
ATOM   14926 O  O     . SER A 1 3613 ? 142.970 148.748 184.613 1.00 61.99  ? 3613 SER A O     1 
ATOM   14927 C  CB    . SER A 1 3613 ? 144.018 146.446 182.594 1.00 56.95  ? 3613 SER A CB    1 
ATOM   14928 O  OG    . SER A 1 3613 ? 145.028 147.208 181.959 1.00 61.33  ? 3613 SER A OG    1 
ATOM   14929 N  N     . PHE A 1 3614 ? 145.228 148.736 184.499 1.00 49.10  ? 3614 PHE A N     1 
ATOM   14930 C  CA    . PHE A 1 3614 ? 145.318 150.182 184.679 1.00 48.00  ? 3614 PHE A CA    1 
ATOM   14931 C  C     . PHE A 1 3614 ? 144.674 150.929 183.520 1.00 56.89  ? 3614 PHE A C     1 
ATOM   14932 O  O     . PHE A 1 3614 ? 144.062 151.983 183.724 1.00 61.86  ? 3614 PHE A O     1 
ATOM   14933 C  CB    . PHE A 1 3614 ? 146.777 150.622 184.831 1.00 47.75  ? 3614 PHE A CB    1 
ATOM   14934 C  CG    . PHE A 1 3614 ? 147.309 150.509 186.233 1.00 50.44  ? 3614 PHE A CG    1 
ATOM   14935 C  CD1   . PHE A 1 3614 ? 146.772 151.271 187.255 1.00 54.69  ? 3614 PHE A CD1   1 
ATOM   14936 C  CD2   . PHE A 1 3614 ? 148.374 149.675 186.520 1.00 42.81  ? 3614 PHE A CD2   1 
ATOM   14937 C  CE1   . PHE A 1 3614 ? 147.268 151.175 188.539 1.00 50.01  ? 3614 PHE A CE1   1 
ATOM   14938 C  CE2   . PHE A 1 3614 ? 148.871 149.575 187.800 1.00 36.85  ? 3614 PHE A CE2   1 
ATOM   14939 C  CZ    . PHE A 1 3614 ? 148.318 150.325 188.810 1.00 41.78  ? 3614 PHE A CZ    1 
ATOM   14940 N  N     . LEU A 1 3615 ? 144.800 150.402 182.300 1.00 57.07  ? 3615 LEU A N     1 
ATOM   14941 C  CA    . LEU A 1 3615 ? 144.234 151.066 181.133 1.00 56.22  ? 3615 LEU A CA    1 
ATOM   14942 C  C     . LEU A 1 3615 ? 142.712 151.026 181.117 1.00 63.72  ? 3615 LEU A C     1 
ATOM   14943 O  O     . LEU A 1 3615 ? 142.095 151.789 180.366 1.00 72.21  ? 3615 LEU A O     1 
ATOM   14944 C  CB    . LEU A 1 3615 ? 144.784 150.433 179.855 1.00 55.33  ? 3615 LEU A CB    1 
ATOM   14945 C  CG    . LEU A 1 3615 ? 146.292 150.566 179.639 1.00 61.44  ? 3615 LEU A CG    1 
ATOM   14946 C  CD1   . LEU A 1 3615 ? 146.717 149.857 178.364 1.00 63.17  ? 3615 LEU A CD1   1 
ATOM   14947 C  CD2   . LEU A 1 3615 ? 146.692 152.030 179.597 1.00 57.05  ? 3615 LEU A CD2   1 
ATOM   14948 N  N     . ASP A 1 3616 ? 142.097 150.160 181.917 1.00 60.85  ? 3616 ASP A N     1 
ATOM   14949 C  CA    . ASP A 1 3616 ? 140.644 150.098 181.972 1.00 61.98  ? 3616 ASP A CA    1 
ATOM   14950 C  C     . ASP A 1 3616 ? 140.079 151.355 182.621 1.00 69.35  ? 3616 ASP A C     1 
ATOM   14951 O  O     . ASP A 1 3616 ? 140.617 151.859 183.611 1.00 71.16  ? 3616 ASP A O     1 
ATOM   14952 C  CB    . ASP A 1 3616 ? 140.192 148.860 182.746 1.00 59.46  ? 3616 ASP A CB    1 
ATOM   14953 C  CG    . ASP A 1 3616 ? 140.135 147.619 181.878 1.00 76.69  ? 3616 ASP A CG    1 
ATOM   14954 O  OD1   . ASP A 1 3616 ? 140.517 147.703 180.692 1.00 79.72  ? 3616 ASP A OD1   1 
ATOM   14955 O  OD2   . ASP A 1 3616 ? 139.706 146.558 182.381 1.00 80.96  ? 3616 ASP A OD2   1 
ATOM   14956 N  N     . ASP A 1 3617 ? 138.985 151.865 182.052 1.00 70.69  ? 3617 ASP A N     1 
ATOM   14957 C  CA    . ASP A 1 3617 ? 138.336 153.039 182.627 1.00 71.16  ? 3617 ASP A CA    1 
ATOM   14958 C  C     . ASP A 1 3617 ? 137.610 152.701 183.922 1.00 69.09  ? 3617 ASP A C     1 
ATOM   14959 O  O     . ASP A 1 3617 ? 137.365 153.591 184.745 1.00 65.71  ? 3617 ASP A O     1 
ATOM   14960 C  CB    . ASP A 1 3617 ? 137.369 153.655 181.615 1.00 79.86  ? 3617 ASP A CB    1 
ATOM   14961 C  CG    . ASP A 1 3617 ? 136.246 152.710 181.226 1.00 88.06  ? 3617 ASP A CG    1 
ATOM   14962 O  OD1   . ASP A 1 3617 ? 136.345 151.501 181.525 1.00 85.74  ? 3617 ASP A OD1   1 
ATOM   14963 O  OD2   . ASP A 1 3617 ? 135.260 153.179 180.618 1.00 93.84  ? 3617 ASP A OD2   1 
ATOM   14964 N  N     . ALA A 1 3618 ? 137.262 151.433 184.120 1.00 67.90  ? 3618 ALA A N     1 
ATOM   14965 C  CA    . ALA A 1 3618 ? 136.587 150.981 185.327 1.00 64.50  ? 3618 ALA A CA    1 
ATOM   14966 C  C     . ALA A 1 3618 ? 137.554 150.507 186.403 1.00 63.24  ? 3618 ALA A C     1 
ATOM   14967 O  O     . ALA A 1 3618 ? 137.106 149.975 187.424 1.00 63.73  ? 3618 ALA A O     1 
ATOM   14968 C  CB    . ALA A 1 3618 ? 135.600 149.858 184.992 1.00 56.86  ? 3618 ALA A CB    1 
ATOM   14969 N  N     . PHE A 1 3619 ? 138.862 150.686 186.199 1.00 62.04  ? 3619 PHE A N     1 
ATOM   14970 C  CA    . PHE A 1 3619 ? 139.843 150.205 187.167 1.00 59.28  ? 3619 PHE A CA    1 
ATOM   14971 C  C     . PHE A 1 3619 ? 139.648 150.855 188.529 1.00 62.05  ? 3619 PHE A C     1 
ATOM   14972 O  O     . PHE A 1 3619 ? 139.814 150.203 189.567 1.00 60.27  ? 3619 PHE A O     1 
ATOM   14973 C  CB    . PHE A 1 3619 ? 141.260 150.467 186.654 1.00 57.20  ? 3619 PHE A CB    1 
ATOM   14974 C  CG    . PHE A 1 3619 ? 142.280 150.633 187.746 1.00 58.40  ? 3619 PHE A CG    1 
ATOM   14975 C  CD1   . PHE A 1 3619 ? 142.696 149.546 188.497 1.00 57.72  ? 3619 PHE A CD1   1 
ATOM   14976 C  CD2   . PHE A 1 3619 ? 142.821 151.878 188.022 1.00 54.34  ? 3619 PHE A CD2   1 
ATOM   14977 C  CE1   . PHE A 1 3619 ? 143.630 149.697 189.502 1.00 51.82  ? 3619 PHE A CE1   1 
ATOM   14978 C  CE2   . PHE A 1 3619 ? 143.756 152.034 189.026 1.00 49.65  ? 3619 PHE A CE2   1 
ATOM   14979 C  CZ    . PHE A 1 3619 ? 144.159 150.942 189.768 1.00 48.39  ? 3619 PHE A CZ    1 
ATOM   14980 N  N     . ARG A 1 3620 ? 139.304 152.144 188.547 1.00 65.29  ? 3620 ARG A N     1 
ATOM   14981 C  CA    . ARG A 1 3620 ? 139.092 152.832 189.816 1.00 59.97  ? 3620 ARG A CA    1 
ATOM   14982 C  C     . ARG A 1 3620 ? 137.937 152.211 190.592 1.00 57.56  ? 3620 ARG A C     1 
ATOM   14983 O  O     . ARG A 1 3620 ? 138.041 151.993 191.804 1.00 58.64  ? 3620 ARG A O     1 
ATOM   14984 C  CB    . ARG A 1 3620 ? 138.840 154.319 189.568 1.00 59.13  ? 3620 ARG A CB    1 
ATOM   14985 C  CG    . ARG A 1 3620 ? 140.108 155.140 189.402 1.00 54.75  ? 3620 ARG A CG    1 
ATOM   14986 C  CD    . ARG A 1 3620 ? 140.782 155.391 190.739 1.00 61.09  ? 3620 ARG A CD    1 
ATOM   14987 N  NE    . ARG A 1 3620 ? 139.811 155.566 191.813 1.00 71.79  ? 3620 ARG A NE    1 
ATOM   14988 C  CZ    . ARG A 1 3620 ? 139.336 156.739 192.207 1.00 71.08  ? 3620 ARG A CZ    1 
ATOM   14989 N  NH1   . ARG A 1 3620 ? 139.726 157.869 191.640 1.00 58.71  ? 3620 ARG A NH1   1 
ATOM   14990 N  NH2   . ARG A 1 3620 ? 138.448 156.780 193.196 1.00 72.86  ? 3620 ARG A NH2   1 
ATOM   14991 N  N     . LYS A 1 3621 ? 136.833 151.906 189.906 1.00 57.58  ? 3621 LYS A N     1 
ATOM   14992 C  CA    . LYS A 1 3621 ? 135.689 151.295 190.575 1.00 57.04  ? 3621 LYS A CA    1 
ATOM   14993 C  C     . LYS A 1 3621 ? 136.024 149.900 191.092 1.00 59.83  ? 3621 LYS A C     1 
ATOM   14994 O  O     . LYS A 1 3621 ? 135.631 149.537 192.207 1.00 59.89  ? 3621 LYS A O     1 
ATOM   14995 C  CB    . LYS A 1 3621 ? 134.492 151.244 189.627 1.00 56.62  ? 3621 LYS A CB    1 
ATOM   14996 C  CG    . LYS A 1 3621 ? 134.249 152.540 188.872 1.00 64.48  ? 3621 LYS A CG    1 
ATOM   14997 C  CD    . LYS A 1 3621 ? 132.768 152.758 188.609 1.00 71.99  ? 3621 LYS A CD    1 
ATOM   14998 C  CE    . LYS A 1 3621 ? 132.507 154.148 188.052 1.00 76.13  ? 3621 LYS A CE    1 
ATOM   14999 N  NZ    . LYS A 1 3621 ? 131.428 154.142 187.027 1.00 75.74  ? 3621 LYS A NZ    1 
ATOM   15000 N  N     . ASN A 1 3622 ? 136.743 149.103 190.296 1.00 59.52  ? 3622 ASN A N     1 
ATOM   15001 C  CA    . ASN A 1 3622 ? 137.120 147.765 190.743 1.00 54.67  ? 3622 ASN A CA    1 
ATOM   15002 C  C     . ASN A 1 3622 ? 138.046 147.825 191.951 1.00 57.35  ? 3622 ASN A C     1 
ATOM   15003 O  O     . ASN A 1 3622 ? 137.879 147.057 192.905 1.00 57.41  ? 3622 ASN A O     1 
ATOM   15004 C  CB    . ASN A 1 3622 ? 137.776 146.988 189.602 1.00 52.17  ? 3622 ASN A CB    1 
ATOM   15005 C  CG    . ASN A 1 3622 ? 136.826 146.730 188.451 1.00 54.93  ? 3622 ASN A CG    1 
ATOM   15006 O  OD1   . ASN A 1 3622 ? 137.027 147.223 187.342 1.00 53.84  ? 3622 ASN A OD1   1 
ATOM   15007 N  ND2   . ASN A 1 3622 ? 135.781 145.953 188.710 1.00 60.03  ? 3622 ASN A ND2   1 
ATOM   15008 N  N     . LEU A 1 3623 ? 139.025 148.732 191.930 1.00 56.02  ? 3623 LEU A N     1 
ATOM   15009 C  CA    . LEU A 1 3623 ? 139.925 148.874 193.070 1.00 54.92  ? 3623 LEU A CA    1 
ATOM   15010 C  C     . LEU A 1 3623 ? 139.173 149.345 194.308 1.00 56.96  ? 3623 LEU A C     1 
ATOM   15011 O  O     . LEU A 1 3623 ? 139.429 148.867 195.419 1.00 60.02  ? 3623 LEU A O     1 
ATOM   15012 C  CB    . LEU A 1 3623 ? 141.060 149.837 192.723 1.00 53.33  ? 3623 LEU A CB    1 
ATOM   15013 C  CG    . LEU A 1 3623 ? 141.808 150.493 193.885 1.00 51.23  ? 3623 LEU A CG    1 
ATOM   15014 C  CD1   . LEU A 1 3623 ? 142.691 149.480 194.594 1.00 47.47  ? 3623 LEU A CD1   1 
ATOM   15015 C  CD2   . LEU A 1 3623 ? 142.631 151.671 193.391 1.00 47.33  ? 3623 LEU A CD2   1 
ATOM   15016 N  N     . GLU A 1 3624 ? 138.236 150.280 194.134 1.00 58.03  ? 3624 GLU A N     1 
ATOM   15017 C  CA    . GLU A 1 3624 ? 137.442 150.759 195.260 1.00 57.89  ? 3624 GLU A CA    1 
ATOM   15018 C  C     . GLU A 1 3624 ? 136.593 149.642 195.858 1.00 60.32  ? 3624 GLU A C     1 
ATOM   15019 O  O     . GLU A 1 3624 ? 136.500 149.509 197.085 1.00 62.07  ? 3624 GLU A O     1 
ATOM   15020 C  CB    . GLU A 1 3624 ? 136.564 151.923 194.805 1.00 60.35  ? 3624 GLU A CB    1 
ATOM   15021 C  CG    . GLU A 1 3624 ? 135.718 152.533 195.897 1.00 70.30  ? 3624 GLU A CG    1 
ATOM   15022 C  CD    . GLU A 1 3624 ? 135.330 153.967 195.596 1.00 76.95  ? 3624 GLU A CD    1 
ATOM   15023 O  OE1   . GLU A 1 3624 ? 135.992 154.597 194.744 1.00 77.82  ? 3624 GLU A OE1   1 
ATOM   15024 O  OE2   . GLU A 1 3624 ? 134.361 154.461 196.208 1.00 76.81  ? 3624 GLU A OE2   1 
ATOM   15025 N  N     . SER A 1 3625 ? 135.966 148.829 195.004 1.00 56.15  ? 3625 SER A N     1 
ATOM   15026 C  CA    . SER A 1 3625 ? 135.165 147.715 195.500 1.00 55.14  ? 3625 SER A CA    1 
ATOM   15027 C  C     . SER A 1 3625 ? 136.036 146.673 196.189 1.00 59.65  ? 3625 SER A C     1 
ATOM   15028 O  O     . SER A 1 3625 ? 135.626 146.081 197.194 1.00 61.25  ? 3625 SER A O     1 
ATOM   15029 C  CB    . SER A 1 3625 ? 134.373 147.084 194.356 1.00 58.81  ? 3625 SER A CB    1 
ATOM   15030 O  OG    . SER A 1 3625 ? 135.182 146.920 193.205 1.00 62.40  ? 3625 SER A OG    1 
ATOM   15031 N  N     . ALA A 1 3626 ? 137.238 146.429 195.660 1.00 57.90  ? 3626 ALA A N     1 
ATOM   15032 C  CA    . ALA A 1 3626 ? 138.158 145.503 196.311 1.00 53.73  ? 3626 ALA A CA    1 
ATOM   15033 C  C     . ALA A 1 3626 ? 138.577 146.016 197.682 1.00 56.29  ? 3626 ALA A C     1 
ATOM   15034 O  O     . ALA A 1 3626 ? 138.687 145.237 198.635 1.00 56.79  ? 3626 ALA A O     1 
ATOM   15035 C  CB    . ALA A 1 3626 ? 139.381 145.267 195.426 1.00 52.85  ? 3626 ALA A CB    1 
ATOM   15036 N  N     . LEU A 1 3627 ? 138.829 147.322 197.797 1.00 56.27  ? 3627 LEU A N     1 
ATOM   15037 C  CA    . LEU A 1 3627 ? 139.171 147.896 199.096 1.00 49.76  ? 3627 LEU A CA    1 
ATOM   15038 C  C     . LEU A 1 3627 ? 138.012 147.783 200.078 1.00 60.03  ? 3627 LEU A C     1 
ATOM   15039 O  O     . LEU A 1 3627 ? 138.215 147.422 201.244 1.00 59.31  ? 3627 LEU A O     1 
ATOM   15040 C  CB    . LEU A 1 3627 ? 139.591 149.356 198.938 1.00 46.63  ? 3627 LEU A CB    1 
ATOM   15041 C  CG    . LEU A 1 3627 ? 140.880 149.633 198.167 1.00 48.54  ? 3627 LEU A CG    1 
ATOM   15042 C  CD1   . LEU A 1 3627 ? 141.073 151.122 197.985 1.00 58.00  ? 3627 LEU A CD1   1 
ATOM   15043 C  CD2   . LEU A 1 3627 ? 142.063 149.036 198.895 1.00 53.41  ? 3627 LEU A CD2   1 
ATOM   15044 N  N     . ARG A 1 3628 ? 136.792 148.092 199.633 1.00 62.37  ? 3628 ARG A N     1 
ATOM   15045 C  CA    . ARG A 1 3628 ? 135.648 148.044 200.541 1.00 63.31  ? 3628 ARG A CA    1 
ATOM   15046 C  C     . ARG A 1 3628 ? 135.345 146.618 200.986 1.00 62.35  ? 3628 ARG A C     1 
ATOM   15047 O  O     . ARG A 1 3628 ? 135.211 146.346 202.185 1.00 61.15  ? 3628 ARG A O     1 
ATOM   15048 C  CB    . ARG A 1 3628 ? 134.415 148.672 199.888 1.00 60.64  ? 3628 ARG A CB    1 
ATOM   15049 C  CG    . ARG A 1 3628 ? 133.640 149.584 200.830 1.00 66.09  ? 3628 ARG A CG    1 
ATOM   15050 C  CD    . ARG A 1 3628 ? 132.396 150.177 200.184 1.00 73.20  ? 3628 ARG A CD    1 
ATOM   15051 N  NE    . ARG A 1 3628 ? 132.678 150.983 199.002 1.00 78.19  ? 3628 ARG A NE    1 
ATOM   15052 C  CZ    . ARG A 1 3628 ? 133.110 152.236 199.040 1.00 71.47  ? 3628 ARG A CZ    1 
ATOM   15053 N  NH1   . ARG A 1 3628 ? 133.354 152.849 200.187 1.00 68.90  ? 3628 ARG A NH1   1 
ATOM   15054 N  NH2   . ARG A 1 3628 ? 133.293 152.894 197.900 1.00 65.89  ? 3628 ARG A NH2   1 
ATOM   15055 N  N     . PHE A 1 3629 ? 135.235 145.691 200.037 1.00 58.78  ? 3629 PHE A N     1 
ATOM   15056 C  CA    . PHE A 1 3629 ? 134.814 144.330 200.342 1.00 59.77  ? 3629 PHE A CA    1 
ATOM   15057 C  C     . PHE A 1 3629 ? 135.970 143.399 200.682 1.00 59.30  ? 3629 PHE A C     1 
ATOM   15058 O  O     . PHE A 1 3629 ? 135.724 142.243 201.044 1.00 58.36  ? 3629 PHE A O     1 
ATOM   15059 C  CB    . PHE A 1 3629 ? 134.021 143.750 199.166 1.00 63.59  ? 3629 PHE A CB    1 
ATOM   15060 C  CG    . PHE A 1 3629 ? 132.843 144.587 198.759 1.00 66.12  ? 3629 PHE A CG    1 
ATOM   15061 C  CD1   . PHE A 1 3629 ? 132.061 145.216 199.714 1.00 63.89  ? 3629 PHE A CD1   1 
ATOM   15062 C  CD2   . PHE A 1 3629 ? 132.519 144.749 197.423 1.00 68.09  ? 3629 PHE A CD2   1 
ATOM   15063 C  CE1   . PHE A 1 3629 ? 130.977 145.989 199.344 1.00 69.37  ? 3629 PHE A CE1   1 
ATOM   15064 C  CE2   . PHE A 1 3629 ? 131.436 145.520 197.047 1.00 67.79  ? 3629 PHE A CE2   1 
ATOM   15065 C  CZ    . PHE A 1 3629 ? 130.665 146.141 198.009 1.00 72.58  ? 3629 PHE A CZ    1 
ATOM   15066 N  N     . GLY A 1 3630 ? 137.209 143.865 200.582 1.00 58.85  ? 3630 GLY A N     1 
ATOM   15067 C  CA    . GLY A 1 3630 ? 138.353 143.028 200.899 1.00 59.56  ? 3630 GLY A CA    1 
ATOM   15068 C  C     . GLY A 1 3630 ? 138.566 141.867 199.953 1.00 55.40  ? 3630 GLY A C     1 
ATOM   15069 O  O     . GLY A 1 3630 ? 138.928 140.770 200.396 1.00 55.22  ? 3630 GLY A O     1 
ATOM   15070 N  N     . ASN A 1 3631 ? 138.352 142.078 198.661 1.00 53.48  ? 3631 ASN A N     1 
ATOM   15071 C  CA    . ASN A 1 3631 ? 138.608 141.002 197.720 1.00 52.29  ? 3631 ASN A CA    1 
ATOM   15072 C  C     . ASN A 1 3631 ? 139.964 141.189 197.051 1.00 51.01  ? 3631 ASN A C     1 
ATOM   15073 O  O     . ASN A 1 3631 ? 140.390 142.321 196.803 1.00 53.25  ? 3631 ASN A O     1 
ATOM   15074 C  CB    . ASN A 1 3631 ? 137.518 140.946 196.646 1.00 55.75  ? 3631 ASN A CB    1 
ATOM   15075 C  CG    . ASN A 1 3631 ? 136.141 140.700 197.225 1.00 61.70  ? 3631 ASN A CG    1 
ATOM   15076 O  OD1   . ASN A 1 3631 ? 135.992 140.001 198.228 1.00 65.65  ? 3631 ASN A OD1   1 
ATOM   15077 N  ND2   . ASN A 1 3631 ? 135.122 141.272 196.594 1.00 64.20  ? 3631 ASN A ND2   1 
ATOM   15078 N  N     . PRO A 1 3632 ? 140.668 140.095 196.761 1.00 44.16  ? 3632 PRO A N     1 
ATOM   15079 C  CA    . PRO A 1 3632 ? 141.938 140.211 196.038 1.00 39.03  ? 3632 PRO A CA    1 
ATOM   15080 C  C     . PRO A 1 3632 ? 141.742 140.828 194.662 1.00 42.27  ? 3632 PRO A C     1 
ATOM   15081 O  O     . PRO A 1 3632 ? 140.735 140.599 193.987 1.00 44.88  ? 3632 PRO A O     1 
ATOM   15082 C  CB    . PRO A 1 3632 ? 142.429 138.761 195.939 1.00 33.64  ? 3632 PRO A CB    1 
ATOM   15083 C  CG    . PRO A 1 3632 ? 141.223 137.919 196.206 1.00 45.17  ? 3632 PRO A CG    1 
ATOM   15084 C  CD    . PRO A 1 3632 ? 140.384 138.708 197.157 1.00 46.19  ? 3632 PRO A CD    1 
ATOM   15085 N  N     . LEU A 1 3633 ? 142.725 141.625 194.252 1.00 36.20  ? 3633 LEU A N     1 
ATOM   15086 C  CA    . LEU A 1 3633 ? 142.692 142.335 192.982 1.00 32.57  ? 3633 LEU A CA    1 
ATOM   15087 C  C     . LEU A 1 3633 ? 143.993 142.090 192.233 1.00 30.16  ? 3633 LEU A C     1 
ATOM   15088 O  O     . LEU A 1 3633 ? 145.074 142.113 192.827 1.00 34.33  ? 3633 LEU A O     1 
ATOM   15089 C  CB    . LEU A 1 3633 ? 142.483 143.840 193.197 1.00 33.28  ? 3633 LEU A CB    1 
ATOM   15090 C  CG    . LEU A 1 3633 ? 142.361 144.728 191.958 1.00 37.63  ? 3633 LEU A CG    1 
ATOM   15091 C  CD1   . LEU A 1 3633 ? 140.994 144.582 191.319 1.00 45.60  ? 3633 LEU A CD1   1 
ATOM   15092 C  CD2   . LEU A 1 3633 ? 142.633 146.181 192.316 1.00 37.56  ? 3633 LEU A CD2   1 
ATOM   15093 N  N     . LEU A 1 3634 ? 143.884 141.850 190.929 1.00 28.40  ? 3634 LEU A N     1 
ATOM   15094 C  CA    . LEU A 1 3634 ? 145.046 141.654 190.071 1.00 29.07  ? 3634 LEU A CA    1 
ATOM   15095 C  C     . LEU A 1 3634 ? 144.991 142.672 188.944 1.00 35.72  ? 3634 LEU A C     1 
ATOM   15096 O  O     . LEU A 1 3634 ? 144.013 142.714 188.191 1.00 47.52  ? 3634 LEU A O     1 
ATOM   15097 C  CB    . LEU A 1 3634 ? 145.092 140.229 189.511 1.00 33.66  ? 3634 LEU A CB    1 
ATOM   15098 C  CG    . LEU A 1 3634 ? 146.111 139.979 188.397 1.00 33.18  ? 3634 LEU A CG    1 
ATOM   15099 C  CD1   . LEU A 1 3634 ? 147.501 139.775 188.976 1.00 28.63  ? 3634 LEU A CD1   1 
ATOM   15100 C  CD2   . LEU A 1 3634 ? 145.701 138.783 187.556 1.00 45.43  ? 3634 LEU A CD2   1 
ATOM   15101 N  N     . VAL A 1 3635 ? 146.035 143.486 188.830 1.00 31.38  ? 3635 VAL A N     1 
ATOM   15102 C  CA    . VAL A 1 3635 ? 146.127 144.508 187.795 1.00 31.54  ? 3635 VAL A CA    1 
ATOM   15103 C  C     . VAL A 1 3635 ? 147.186 144.065 186.795 1.00 37.55  ? 3635 VAL A C     1 
ATOM   15104 O  O     . VAL A 1 3635 ? 148.337 143.811 187.170 1.00 40.17  ? 3635 VAL A O     1 
ATOM   15105 C  CB    . VAL A 1 3635 ? 146.457 145.884 188.390 1.00 32.58  ? 3635 VAL A CB    1 
ATOM   15106 C  CG1   . VAL A 1 3635 ? 146.639 146.890 187.282 1.00 46.56  ? 3635 VAL A CG1   1 
ATOM   15107 C  CG2   . VAL A 1 3635 ? 145.357 146.325 189.343 1.00 31.33  ? 3635 VAL A CG2   1 
ATOM   15108 N  N     . GLN A 1 3636 ? 146.803 143.979 185.520 1.00 40.47  ? 3636 GLN A N     1 
ATOM   15109 C  CA    . GLN A 1 3636 ? 147.595 143.265 184.527 1.00 47.47  ? 3636 GLN A CA    1 
ATOM   15110 C  C     . GLN A 1 3636 ? 148.477 144.158 183.661 1.00 51.65  ? 3636 GLN A C     1 
ATOM   15111 O  O     . GLN A 1 3636 ? 149.309 143.629 182.917 1.00 59.58  ? 3636 GLN A O     1 
ATOM   15112 C  CB    . GLN A 1 3636 ? 146.675 142.438 183.619 1.00 52.01  ? 3636 GLN A CB    1 
ATOM   15113 C  CG    . GLN A 1 3636 ? 145.741 143.267 182.758 1.00 57.74  ? 3636 GLN A CG    1 
ATOM   15114 C  CD    . GLN A 1 3636 ? 144.817 142.413 181.914 1.00 64.24  ? 3636 GLN A CD    1 
ATOM   15115 O  OE1   . GLN A 1 3636 ? 144.899 141.185 181.933 1.00 71.23  ? 3636 GLN A OE1   1 
ATOM   15116 N  NE2   . GLN A 1 3636 ? 143.931 143.060 181.167 1.00 64.85  ? 3636 GLN A NE2   1 
ATOM   15117 N  N     . ASP A 1 3637 ? 148.328 145.480 183.726 1.00 44.69  ? 3637 ASP A N     1 
ATOM   15118 C  CA    . ASP A 1 3637 ? 149.133 146.391 182.907 1.00 50.33  ? 3637 ASP A CA    1 
ATOM   15119 C  C     . ASP A 1 3637 ? 149.715 147.478 183.805 1.00 47.17  ? 3637 ASP A C     1 
ATOM   15120 O  O     . ASP A 1 3637 ? 149.154 148.572 183.900 1.00 53.76  ? 3637 ASP A O     1 
ATOM   15121 C  CB    . ASP A 1 3637 ? 148.297 146.988 181.777 1.00 56.91  ? 3637 ASP A CB    1 
ATOM   15122 C  CG    . ASP A 1 3637 ? 147.825 145.943 180.786 1.00 70.44  ? 3637 ASP A CG    1 
ATOM   15123 O  OD1   . ASP A 1 3637 ? 148.674 145.191 180.264 1.00 74.14  ? 3637 ASP A OD1   1 
ATOM   15124 O  OD2   . ASP A 1 3637 ? 146.604 145.875 180.529 1.00 70.58  ? 3637 ASP A OD2   1 
ATOM   15125 N  N     . VAL A 1 3638 ? 150.860 147.191 184.433 1.00 43.04  ? 3638 VAL A N     1 
ATOM   15126 C  CA    . VAL A 1 3638 ? 151.469 148.142 185.361 1.00 37.94  ? 3638 VAL A CA    1 
ATOM   15127 C  C     . VAL A 1 3638 ? 152.390 149.127 184.650 1.00 42.15  ? 3638 VAL A C     1 
ATOM   15128 O  O     . VAL A 1 3638 ? 152.834 150.107 185.268 1.00 47.16  ? 3638 VAL A O     1 
ATOM   15129 C  CB    . VAL A 1 3638 ? 152.222 147.385 186.477 1.00 36.01  ? 3638 VAL A CB    1 
ATOM   15130 C  CG1   . VAL A 1 3638 ? 153.405 146.625 185.912 1.00 37.98  ? 3638 VAL A CG1   1 
ATOM   15131 C  CG2   . VAL A 1 3638 ? 152.628 148.309 187.627 1.00 36.69  ? 3638 VAL A CG2   1 
ATOM   15132 N  N     . GLU A 1 3639 ? 152.668 148.921 183.359 1.00 46.54  ? 3639 GLU A N     1 
ATOM   15133 C  CA    . GLU A 1 3639 ? 153.454 149.894 182.607 1.00 43.75  ? 3639 GLU A CA    1 
ATOM   15134 C  C     . GLU A 1 3639 ? 152.750 151.240 182.516 1.00 40.87  ? 3639 GLU A C     1 
ATOM   15135 O  O     . GLU A 1 3639 ? 153.394 152.247 182.201 1.00 41.60  ? 3639 GLU A O     1 
ATOM   15136 C  CB    . GLU A 1 3639 ? 153.749 149.372 181.200 1.00 46.93  ? 3639 GLU A CB    1 
ATOM   15137 C  CG    . GLU A 1 3639 ? 154.271 147.947 181.152 1.00 51.22  ? 3639 GLU A CG    1 
ATOM   15138 C  CD    . GLU A 1 3639 ? 153.172 146.937 180.891 1.00 55.68  ? 3639 GLU A CD    1 
ATOM   15139 O  OE1   . GLU A 1 3639 ? 152.230 146.858 181.706 1.00 58.17  ? 3639 GLU A OE1   1 
ATOM   15140 O  OE2   . GLU A 1 3639 ? 153.248 146.224 179.868 1.00 55.57  ? 3639 GLU A OE2   1 
ATOM   15141 N  N     . SER A 1 3640 ? 151.447 151.276 182.784 1.00 43.26  ? 3640 SER A N     1 
ATOM   15142 C  CA    . SER A 1 3640 ? 150.684 152.514 182.833 1.00 45.58  ? 3640 SER A CA    1 
ATOM   15143 C  C     . SER A 1 3640 ? 150.198 152.746 184.257 1.00 43.09  ? 3640 SER A C     1 
ATOM   15144 O  O     . SER A 1 3640 ? 149.025 153.066 184.476 1.00 47.54  ? 3640 SER A O     1 
ATOM   15145 C  CB    . SER A 1 3640 ? 149.507 152.467 181.859 1.00 52.46  ? 3640 SER A CB    1 
ATOM   15146 O  OG    . SER A 1 3640 ? 149.954 152.276 180.528 1.00 59.81  ? 3640 SER A OG    1 
ATOM   15147 N  N     . TYR A 1 3641 ? 151.097 152.558 185.223 1.00 41.36  ? 3641 TYR A N     1 
ATOM   15148 C  CA    . TYR A 1 3641 ? 150.750 152.681 186.634 1.00 41.32  ? 3641 TYR A CA    1 
ATOM   15149 C  C     . TYR A 1 3641 ? 150.114 154.034 186.922 1.00 46.52  ? 3641 TYR A C     1 
ATOM   15150 O  O     . TYR A 1 3641 ? 150.638 155.079 186.527 1.00 50.14  ? 3641 TYR A O     1 
ATOM   15151 C  CB    . TYR A 1 3641 ? 152.004 152.492 187.490 1.00 38.96  ? 3641 TYR A CB    1 
ATOM   15152 C  CG    . TYR A 1 3641 ? 151.811 152.772 188.964 1.00 41.09  ? 3641 TYR A CG    1 
ATOM   15153 C  CD1   . TYR A 1 3641 ? 151.115 151.888 189.775 1.00 39.14  ? 3641 TYR A CD1   1 
ATOM   15154 C  CD2   . TYR A 1 3641 ? 152.330 153.921 189.545 1.00 40.63  ? 3641 TYR A CD2   1 
ATOM   15155 C  CE1   . TYR A 1 3641 ? 150.938 152.139 191.121 1.00 37.59  ? 3641 TYR A CE1   1 
ATOM   15156 C  CE2   . TYR A 1 3641 ? 152.159 154.182 190.890 1.00 41.01  ? 3641 TYR A CE2   1 
ATOM   15157 C  CZ    . TYR A 1 3641 ? 151.462 153.288 191.673 1.00 41.06  ? 3641 TYR A CZ    1 
ATOM   15158 O  OH    . TYR A 1 3641 ? 151.290 153.543 193.013 1.00 41.46  ? 3641 TYR A OH    1 
ATOM   15159 N  N     . ASP A 1 3642 ? 148.975 154.008 187.614 1.00 46.68  ? 3642 ASP A N     1 
ATOM   15160 C  CA    . ASP A 1 3642 ? 148.253 155.226 187.943 1.00 49.24  ? 3642 ASP A CA    1 
ATOM   15161 C  C     . ASP A 1 3642 ? 148.527 155.583 189.394 1.00 50.89  ? 3642 ASP A C     1 
ATOM   15162 O  O     . ASP A 1 3642 ? 148.348 154.727 190.274 1.00 46.64  ? 3642 ASP A O     1 
ATOM   15163 C  CB    . ASP A 1 3642 ? 146.758 155.046 187.712 1.00 55.16  ? 3642 ASP A CB    1 
ATOM   15164 C  CG    . ASP A 1 3642 ? 145.988 156.346 187.843 1.00 64.55  ? 3642 ASP A CG    1 
ATOM   15165 O  OD1   . ASP A 1 3642 ? 146.087 157.188 186.926 1.00 64.92  ? 3642 ASP A OD1   1 
ATOM   15166 O  OD2   . ASP A 1 3642 ? 145.283 156.528 188.854 1.00 62.69  ? 3642 ASP A OD2   1 
ATOM   15167 N  N     . PRO A 1 3643 ? 148.956 156.812 189.693 1.00 52.73  ? 3643 PRO A N     1 
ATOM   15168 C  CA    . PRO A 1 3643 ? 149.421 157.134 191.051 1.00 43.11  ? 3643 PRO A CA    1 
ATOM   15169 C  C     . PRO A 1 3643 ? 148.343 157.083 192.126 1.00 43.88  ? 3643 PRO A C     1 
ATOM   15170 O  O     . PRO A 1 3643 ? 148.618 157.414 193.284 1.00 42.05  ? 3643 PRO A O     1 
ATOM   15171 C  CB    . PRO A 1 3643 ? 149.977 158.557 190.899 1.00 40.85  ? 3643 PRO A CB    1 
ATOM   15172 C  CG    . PRO A 1 3643 ? 150.247 158.715 189.436 1.00 40.69  ? 3643 PRO A CG    1 
ATOM   15173 C  CD    . PRO A 1 3643 ? 149.185 157.920 188.752 1.00 48.78  ? 3643 PRO A CD    1 
ATOM   15174 N  N     . VAL A 1 3644 ? 147.118 156.684 191.771 1.00 46.10  ? 3644 VAL A N     1 
ATOM   15175 C  CA    . VAL A 1 3644 ? 146.064 156.561 192.772 1.00 48.68  ? 3644 VAL A CA    1 
ATOM   15176 C  C     . VAL A 1 3644 ? 146.395 155.484 193.798 1.00 52.07  ? 3644 VAL A C     1 
ATOM   15177 O  O     . VAL A 1 3644 ? 145.900 155.535 194.931 1.00 55.90  ? 3644 VAL A O     1 
ATOM   15178 C  CB    . VAL A 1 3644 ? 144.708 156.272 192.098 1.00 47.66  ? 3644 VAL A CB    1 
ATOM   15179 C  CG1   . VAL A 1 3644 ? 144.703 154.888 191.463 1.00 48.80  ? 3644 VAL A CG1   1 
ATOM   15180 C  CG2   . VAL A 1 3644 ? 143.561 156.426 193.090 1.00 54.86  ? 3644 VAL A CG2   1 
ATOM   15181 N  N     . LEU A 1 3645 ? 147.236 154.517 193.438 1.00 44.99  ? 3645 LEU A N     1 
ATOM   15182 C  CA    . LEU A 1 3645 ? 147.567 153.395 194.304 1.00 40.02  ? 3645 LEU A CA    1 
ATOM   15183 C  C     . LEU A 1 3645 ? 148.668 153.715 195.306 1.00 37.99  ? 3645 LEU A C     1 
ATOM   15184 O  O     . LEU A 1 3645 ? 149.017 152.847 196.113 1.00 37.26  ? 3645 LEU A O     1 
ATOM   15185 C  CB    . LEU A 1 3645 ? 147.984 152.188 193.459 1.00 33.54  ? 3645 LEU A CB    1 
ATOM   15186 C  CG    . LEU A 1 3645 ? 146.881 151.204 193.071 1.00 33.42  ? 3645 LEU A CG    1 
ATOM   15187 C  CD1   . LEU A 1 3645 ? 147.440 150.119 192.174 1.00 31.47  ? 3645 LEU A CD1   1 
ATOM   15188 C  CD2   . LEU A 1 3645 ? 146.236 150.600 194.304 1.00 38.08  ? 3645 LEU A CD2   1 
ATOM   15189 N  N     . ASN A 1 3646 ? 149.226 154.926 195.270 1.00 38.37  ? 3646 ASN A N     1 
ATOM   15190 C  CA    . ASN A 1 3646 ? 150.316 155.269 196.182 1.00 33.69  ? 3646 ASN A CA    1 
ATOM   15191 C  C     . ASN A 1 3646 ? 149.930 155.130 197.651 1.00 35.68  ? 3646 ASN A C     1 
ATOM   15192 O  O     . ASN A 1 3646 ? 150.711 154.532 198.411 1.00 43.01  ? 3646 ASN A O     1 
ATOM   15193 C  CB    . ASN A 1 3646 ? 150.827 156.678 195.865 1.00 34.55  ? 3646 ASN A CB    1 
ATOM   15194 C  CG    . ASN A 1 3646 ? 151.584 156.742 194.555 1.00 37.52  ? 3646 ASN A CG    1 
ATOM   15195 O  OD1   . ASN A 1 3646 ? 151.704 155.744 193.846 1.00 40.64  ? 3646 ASN A OD1   1 
ATOM   15196 N  ND2   . ASN A 1 3646 ? 152.101 157.919 194.227 1.00 40.67  ? 3646 ASN A ND2   1 
ATOM   15197 N  N     . PRO A 1 3647 ? 148.790 155.649 198.125 1.00 33.28  ? 3647 PRO A N     1 
ATOM   15198 C  CA    . PRO A 1 3647 ? 148.409 155.371 199.520 1.00 32.19  ? 3647 PRO A CA    1 
ATOM   15199 C  C     . PRO A 1 3647 ? 148.190 153.895 199.802 1.00 37.19  ? 3647 PRO A C     1 
ATOM   15200 O  O     . PRO A 1 3647 ? 148.473 153.438 200.917 1.00 36.43  ? 3647 PRO A O     1 
ATOM   15201 C  CB    . PRO A 1 3647 ? 147.117 156.180 199.700 1.00 36.53  ? 3647 PRO A CB    1 
ATOM   15202 C  CG    . PRO A 1 3647 ? 146.598 156.381 198.325 1.00 40.42  ? 3647 PRO A CG    1 
ATOM   15203 C  CD    . PRO A 1 3647 ? 147.811 156.534 197.470 1.00 37.11  ? 3647 PRO A CD    1 
ATOM   15204 N  N     . VAL A 1 3648 ? 147.691 153.135 198.826 1.00 41.24  ? 3648 VAL A N     1 
ATOM   15205 C  CA    . VAL A 1 3648 ? 147.456 151.710 199.037 1.00 34.52  ? 3648 VAL A CA    1 
ATOM   15206 C  C     . VAL A 1 3648 ? 148.776 150.959 199.148 1.00 32.92  ? 3648 VAL A C     1 
ATOM   15207 O  O     . VAL A 1 3648 ? 148.952 150.112 200.032 1.00 35.65  ? 3648 VAL A O     1 
ATOM   15208 C  CB    . VAL A 1 3648 ? 146.579 151.142 197.908 1.00 33.09  ? 3648 VAL A CB    1 
ATOM   15209 C  CG1   . VAL A 1 3648 ? 146.335 149.658 198.122 1.00 34.17  ? 3648 VAL A CG1   1 
ATOM   15210 C  CG2   . VAL A 1 3648 ? 145.266 151.898 197.823 1.00 43.49  ? 3648 VAL A CG2   1 
ATOM   15211 N  N     . LEU A 1 3649 ? 149.723 151.253 198.254 1.00 31.80  ? 3649 LEU A N     1 
ATOM   15212 C  CA    . LEU A 1 3649 ? 151.001 150.549 198.269 1.00 30.06  ? 3649 LEU A CA    1 
ATOM   15213 C  C     . LEU A 1 3649 ? 151.822 150.895 199.504 1.00 32.47  ? 3649 LEU A C     1 
ATOM   15214 O  O     . LEU A 1 3649 ? 152.546 150.039 200.023 1.00 37.09  ? 3649 LEU A O     1 
ATOM   15215 C  CB    . LEU A 1 3649 ? 151.787 150.866 196.997 1.00 29.58  ? 3649 LEU A CB    1 
ATOM   15216 C  CG    . LEU A 1 3649 ? 151.169 150.389 195.681 1.00 24.39  ? 3649 LEU A CG    1 
ATOM   15217 C  CD1   . LEU A 1 3649 ? 152.186 150.460 194.554 1.00 25.69  ? 3649 LEU A CD1   1 
ATOM   15218 C  CD2   . LEU A 1 3649 ? 150.620 148.978 195.820 1.00 21.23  ? 3649 LEU A CD2   1 
ATOM   15219 N  N     . ASN A 1 3650 ? 151.726 152.134 199.986 1.00 29.16  ? 3650 ASN A N     1 
ATOM   15220 C  CA    . ASN A 1 3650 ? 152.416 152.533 201.204 1.00 26.29  ? 3650 ASN A CA    1 
ATOM   15221 C  C     . ASN A 1 3650 ? 151.673 152.118 202.466 1.00 31.44  ? 3650 ASN A C     1 
ATOM   15222 O  O     . ASN A 1 3650 ? 152.201 152.318 203.565 1.00 34.44  ? 3650 ASN A O     1 
ATOM   15223 C  CB    . ASN A 1 3650 ? 152.631 154.048 201.223 1.00 29.15  ? 3650 ASN A CB    1 
ATOM   15224 C  CG    . ASN A 1 3650 ? 153.437 154.536 200.041 1.00 38.76  ? 3650 ASN A CG    1 
ATOM   15225 O  OD1   . ASN A 1 3650 ? 154.555 154.080 199.804 1.00 43.45  ? 3650 ASN A OD1   1 
ATOM   15226 N  ND2   . ASN A 1 3650 ? 152.873 155.474 199.290 1.00 43.65  ? 3650 ASN A ND2   1 
ATOM   15227 N  N     . ARG A 1 3651 ? 150.472 151.552 202.330 1.00 35.49  ? 3651 ARG A N     1 
ATOM   15228 C  CA    . ARG A 1 3651 ? 149.638 151.170 203.471 1.00 36.37  ? 3651 ARG A CA    1 
ATOM   15229 C  C     . ARG A 1 3651 ? 149.372 152.366 204.382 1.00 40.80  ? 3651 ARG A C     1 
ATOM   15230 O  O     . ARG A 1 3651 ? 149.394 152.255 205.610 1.00 48.15  ? 3651 ARG A O     1 
ATOM   15231 C  CB    . ARG A 1 3651 ? 150.262 150.011 204.251 1.00 31.80  ? 3651 ARG A CB    1 
ATOM   15232 C  CG    . ARG A 1 3651 ? 150.488 148.762 203.414 1.00 31.45  ? 3651 ARG A CG    1 
ATOM   15233 C  CD    . ARG A 1 3651 ? 151.447 147.801 204.095 1.00 34.23  ? 3651 ARG A CD    1 
ATOM   15234 N  NE    . ARG A 1 3651 ? 151.703 146.616 203.285 1.00 36.51  ? 3651 ARG A NE    1 
ATOM   15235 C  CZ    . ARG A 1 3651 ? 150.860 145.600 203.153 1.00 41.47  ? 3651 ARG A CZ    1 
ATOM   15236 N  NH1   . ARG A 1 3651 ? 149.692 145.585 203.775 1.00 39.74  ? 3651 ARG A NH1   1 
ATOM   15237 N  NH2   . ARG A 1 3651 ? 151.199 144.573 202.380 1.00 37.32  ? 3651 ARG A NH2   1 
ATOM   15238 N  N     . GLU A 1 3652 ? 149.117 153.524 203.771 1.00 38.94  ? 3652 GLU A N     1 
ATOM   15239 C  CA    . GLU A 1 3652 ? 148.847 154.759 204.506 1.00 41.94  ? 3652 GLU A CA    1 
ATOM   15240 C  C     . GLU A 1 3652 ? 147.405 154.721 205.002 1.00 48.33  ? 3652 GLU A C     1 
ATOM   15241 O  O     . GLU A 1 3652 ? 146.477 155.241 204.378 1.00 52.43  ? 3652 GLU A O     1 
ATOM   15242 C  CB    . GLU A 1 3652 ? 149.107 155.975 203.627 1.00 42.01  ? 3652 GLU A CB    1 
ATOM   15243 C  CG    . GLU A 1 3652 ? 150.575 156.235 203.342 1.00 40.31  ? 3652 GLU A CG    1 
ATOM   15244 C  CD    . GLU A 1 3652 ? 150.780 157.248 202.235 1.00 43.91  ? 3652 GLU A CD    1 
ATOM   15245 O  OE1   . GLU A 1 3652 ? 149.788 157.878 201.813 1.00 42.44  ? 3652 GLU A OE1   1 
ATOM   15246 O  OE2   . GLU A 1 3652 ? 151.933 157.415 201.786 1.00 55.42  ? 3652 GLU A OE2   1 
ATOM   15247 N  N     . VAL A 1 3653 ? 147.221 154.092 206.159 1.00 47.53  ? 3653 VAL A N     1 
ATOM   15248 C  CA    . VAL A 1 3653 ? 145.905 153.892 206.751 1.00 54.61  ? 3653 VAL A CA    1 
ATOM   15249 C  C     . VAL A 1 3653 ? 145.837 154.632 208.079 1.00 61.14  ? 3653 VAL A C     1 
ATOM   15250 O  O     . VAL A 1 3653 ? 146.801 154.638 208.854 1.00 63.40  ? 3653 VAL A O     1 
ATOM   15251 C  CB    . VAL A 1 3653 ? 145.590 152.394 206.933 1.00 51.33  ? 3653 VAL A CB    1 
ATOM   15252 C  CG1   . VAL A 1 3653 ? 145.496 151.713 205.581 1.00 51.43  ? 3653 VAL A CG1   1 
ATOM   15253 C  CG2   . VAL A 1 3653 ? 146.649 151.720 207.792 1.00 50.98  ? 3653 VAL A CG2   1 
ATOM   15254 N  N     . ARG A 1 3654 ? 144.701 155.276 208.329 1.00 62.72  ? 3654 ARG A N     1 
ATOM   15255 C  CA    . ARG A 1 3654 ? 144.422 155.940 209.595 1.00 62.61  ? 3654 ARG A CA    1 
ATOM   15256 C  C     . ARG A 1 3654 ? 143.316 155.170 210.303 1.00 65.94  ? 3654 ARG A C     1 
ATOM   15257 O  O     . ARG A 1 3654 ? 142.256 154.922 209.718 1.00 72.66  ? 3654 ARG A O     1 
ATOM   15258 C  CB    . ARG A 1 3654 ? 144.015 157.397 209.379 1.00 61.65  ? 3654 ARG A CB    1 
ATOM   15259 C  CG    . ARG A 1 3654 ? 143.257 157.647 208.087 1.00 64.70  ? 3654 ARG A CG    1 
ATOM   15260 C  CD    . ARG A 1 3654 ? 142.926 159.120 207.919 1.00 74.17  ? 3654 ARG A CD    1 
ATOM   15261 N  NE    . ARG A 1 3654 ? 142.319 159.683 209.120 1.00 77.27  ? 3654 ARG A NE    1 
ATOM   15262 C  CZ    . ARG A 1 3654 ? 142.413 160.955 209.482 1.00 76.23  ? 3654 ARG A CZ    1 
ATOM   15263 N  NH1   . ARG A 1 3654 ? 143.086 161.832 208.757 1.00 65.73  ? 3654 ARG A NH1   1 
ATOM   15264 N  NH2   . ARG A 1 3654 ? 141.816 161.356 210.601 1.00 73.09  ? 3654 ARG A NH2   1 
ATOM   15265 N  N     . ARG A 1 3655 ? 143.563 154.792 211.554 1.00 60.49  ? 3655 ARG A N     1 
ATOM   15266 C  CA    . ARG A 1 3655 ? 142.624 153.985 212.331 1.00 68.99  ? 3655 ARG A CA    1 
ATOM   15267 C  C     . ARG A 1 3655 ? 141.868 154.914 213.276 1.00 80.10  ? 3655 ARG A C     1 
ATOM   15268 O  O     . ARG A 1 3655 ? 142.282 155.151 214.411 1.00 79.85  ? 3655 ARG A O     1 
ATOM   15269 C  CB    . ARG A 1 3655 ? 143.358 152.880 213.082 1.00 67.19  ? 3655 ARG A CB    1 
ATOM   15270 C  CG    . ARG A 1 3655 ? 144.042 151.877 212.168 1.00 71.65  ? 3655 ARG A CG    1 
ATOM   15271 C  CD    . ARG A 1 3655 ? 145.013 150.991 212.932 1.00 63.45  ? 3655 ARG A CD    1 
ATOM   15272 N  NE    . ARG A 1 3655 ? 145.917 150.280 212.036 1.00 64.51  ? 3655 ARG A NE    1 
ATOM   15273 C  CZ    . ARG A 1 3655 ? 145.578 149.225 211.306 1.00 66.01  ? 3655 ARG A CZ    1 
ATOM   15274 N  NH1   . ARG A 1 3655 ? 144.359 148.713 211.356 1.00 62.00  ? 3655 ARG A NH1   1 
ATOM   15275 N  NH2   . ARG A 1 3655 ? 146.485 148.669 210.509 1.00 65.88  ? 3655 ARG A NH2   1 
ATOM   15276 N  N     . THR A 1 3656 ? 140.745 155.441 212.796 1.00 88.62  ? 3656 THR A N     1 
ATOM   15277 C  CA    . THR A 1 3656 ? 139.880 156.308 213.584 1.00 90.29  ? 3656 THR A CA    1 
ATOM   15278 C  C     . THR A 1 3656 ? 138.779 155.461 214.209 1.00 96.09  ? 3656 THR A C     1 
ATOM   15279 O  O     . THR A 1 3656 ? 137.951 154.887 213.493 1.00 92.04  ? 3656 THR A O     1 
ATOM   15280 C  CB    . THR A 1 3656 ? 139.280 157.418 212.720 1.00 90.80  ? 3656 THR A CB    1 
ATOM   15281 O  OG1   . THR A 1 3656 ? 140.304 158.354 212.360 1.00 79.56  ? 3656 THR A OG1   1 
ATOM   15282 C  CG2   . THR A 1 3656 ? 138.179 158.148 213.477 1.00 87.94  ? 3656 THR A CG2   1 
ATOM   15283 N  N     . GLY A 1 3657 ? 138.768 155.395 215.538 1.00 100.56 ? 3657 GLY A N     1 
ATOM   15284 C  CA    . GLY A 1 3657 ? 137.796 154.555 216.221 1.00 105.52 ? 3657 GLY A CA    1 
ATOM   15285 C  C     . GLY A 1 3657 ? 137.970 153.100 215.833 1.00 105.16 ? 3657 GLY A C     1 
ATOM   15286 O  O     . GLY A 1 3657 ? 139.083 152.561 215.829 1.00 97.62  ? 3657 GLY A O     1 
ATOM   15287 N  N     . GLY A 1 3658 ? 136.860 152.450 215.503 1.00 104.73 ? 3658 GLY A N     1 
ATOM   15288 C  CA    . GLY A 1 3658 ? 136.860 151.074 215.060 1.00 101.88 ? 3658 GLY A CA    1 
ATOM   15289 C  C     . GLY A 1 3658 ? 136.988 150.881 213.565 1.00 101.99 ? 3658 GLY A C     1 
ATOM   15290 O  O     . GLY A 1 3658 ? 136.857 149.751 213.086 1.00 101.74 ? 3658 GLY A O     1 
ATOM   15291 N  N     . ARG A 1 3659 ? 137.239 151.948 212.812 1.00 98.36  ? 3659 ARG A N     1 
ATOM   15292 C  CA    . ARG A 1 3659 ? 137.327 151.890 211.361 1.00 91.25  ? 3659 ARG A CA    1 
ATOM   15293 C  C     . ARG A 1 3659 ? 138.751 152.183 210.906 1.00 88.48  ? 3659 ARG A C     1 
ATOM   15294 O  O     . ARG A 1 3659 ? 139.422 153.060 211.460 1.00 90.86  ? 3659 ARG A O     1 
ATOM   15295 C  CB    . ARG A 1 3659 ? 136.367 152.890 210.712 1.00 89.48  ? 3659 ARG A CB    1 
ATOM   15296 C  CG    . ARG A 1 3659 ? 134.922 152.771 211.162 1.00 93.90  ? 3659 ARG A CG    1 
ATOM   15297 C  CD    . ARG A 1 3659 ? 134.160 154.052 210.862 1.00 91.53  ? 3659 ARG A CD    1 
ATOM   15298 N  NE    . ARG A 1 3659 ? 134.266 154.432 209.459 1.00 86.80  ? 3659 ARG A NE    1 
ATOM   15299 C  CZ    . ARG A 1 3659 ? 134.111 155.668 209.002 1.00 87.10  ? 3659 ARG A CZ    1 
ATOM   15300 N  NH1   . ARG A 1 3659 ? 133.847 156.677 209.816 1.00 88.02  ? 3659 ARG A NH1   1 
ATOM   15301 N  NH2   . ARG A 1 3659 ? 134.225 155.897 207.697 1.00 84.43  ? 3659 ARG A NH2   1 
ATOM   15302 N  N     . VAL A 1 3660 ? 139.204 151.446 209.898 1.00 83.46  ? 3660 VAL A N     1 
ATOM   15303 C  CA    . VAL A 1 3660 ? 140.492 151.683 209.256 1.00 72.07  ? 3660 VAL A CA    1 
ATOM   15304 C  C     . VAL A 1 3660 ? 140.227 152.428 207.957 1.00 69.80  ? 3660 VAL A C     1 
ATOM   15305 O  O     . VAL A 1 3660 ? 139.515 151.926 207.080 1.00 71.77  ? 3660 VAL A O     1 
ATOM   15306 C  CB    . VAL A 1 3660 ? 141.243 150.368 209.000 1.00 61.16  ? 3660 VAL A CB    1 
ATOM   15307 C  CG1   . VAL A 1 3660 ? 142.623 150.647 208.428 1.00 57.27  ? 3660 VAL A CG1   1 
ATOM   15308 C  CG2   . VAL A 1 3660 ? 141.338 149.556 210.281 1.00 60.67  ? 3660 VAL A CG2   1 
ATOM   15309 N  N     . LEU A 1 3661 ? 140.799 153.621 207.825 1.00 68.02  ? 3661 LEU A N     1 
ATOM   15310 C  CA    . LEU A 1 3661 ? 140.451 154.543 206.752 1.00 65.91  ? 3661 LEU A CA    1 
ATOM   15311 C  C     . LEU A 1 3661 ? 141.607 154.659 205.770 1.00 65.25  ? 3661 LEU A C     1 
ATOM   15312 O  O     . LEU A 1 3661 ? 142.758 154.847 206.177 1.00 70.62  ? 3661 LEU A O     1 
ATOM   15313 C  CB    . LEU A 1 3661 ? 140.100 155.926 207.310 1.00 69.05  ? 3661 LEU A CB    1 
ATOM   15314 C  CG    . LEU A 1 3661 ? 138.711 156.172 207.915 1.00 72.43  ? 3661 LEU A CG    1 
ATOM   15315 C  CD1   . LEU A 1 3661 ? 137.600 155.959 206.895 1.00 72.34  ? 3661 LEU A CD1   1 
ATOM   15316 C  CD2   . LEU A 1 3661 ? 138.473 155.335 209.165 1.00 71.80  ? 3661 LEU A CD2   1 
ATOM   15317 N  N     . ILE A 1 3662 ? 141.297 154.548 204.480 1.00 63.54  ? 3662 ILE A N     1 
ATOM   15318 C  CA    . ILE A 1 3662 ? 142.256 154.778 203.406 1.00 59.31  ? 3662 ILE A CA    1 
ATOM   15319 C  C     . ILE A 1 3662 ? 141.608 155.707 202.388 1.00 61.64  ? 3662 ILE A C     1 
ATOM   15320 O  O     . ILE A 1 3662 ? 140.397 155.636 202.153 1.00 68.10  ? 3662 ILE A O     1 
ATOM   15321 C  CB    . ILE A 1 3662 ? 142.720 153.457 202.752 1.00 58.46  ? 3662 ILE A CB    1 
ATOM   15322 C  CG1   . ILE A 1 3662 ? 143.906 153.705 201.818 1.00 52.92  ? 3662 ILE A CG1   1 
ATOM   15323 C  CG2   . ILE A 1 3662 ? 141.577 152.774 202.013 1.00 64.30  ? 3662 ILE A CG2   1 
ATOM   15324 C  CD1   . ILE A 1 3662 ? 144.622 152.444 201.400 1.00 51.14  ? 3662 ILE A CD1   1 
ATOM   15325 N  N     . THR A 1 3663 ? 142.406 156.596 201.803 1.00 58.91  ? 3663 THR A N     1 
ATOM   15326 C  CA    . THR A 1 3663 ? 141.899 157.650 200.934 1.00 64.67  ? 3663 THR A CA    1 
ATOM   15327 C  C     . THR A 1 3663 ? 142.445 157.488 199.522 1.00 69.29  ? 3663 THR A C     1 
ATOM   15328 O  O     . THR A 1 3663 ? 143.652 157.303 199.336 1.00 74.33  ? 3663 THR A O     1 
ATOM   15329 C  CB    . THR A 1 3663 ? 142.274 159.032 201.476 1.00 67.96  ? 3663 THR A CB    1 
ATOM   15330 O  OG1   . THR A 1 3663 ? 143.666 159.277 201.239 1.00 70.18  ? 3663 THR A OG1   1 
ATOM   15331 C  CG2   . THR A 1 3663 ? 141.998 159.115 202.969 1.00 69.87  ? 3663 THR A CG2   1 
ATOM   15332 N  N     . LEU A 1 3664 ? 141.554 157.559 198.535 1.00 69.33  ? 3664 LEU A N     1 
ATOM   15333 C  CA    . LEU A 1 3664 ? 141.928 157.663 197.130 1.00 68.62  ? 3664 LEU A CA    1 
ATOM   15334 C  C     . LEU A 1 3664 ? 141.319 158.938 196.569 1.00 75.44  ? 3664 LEU A C     1 
ATOM   15335 O  O     . LEU A 1 3664 ? 140.096 159.114 196.614 1.00 82.70  ? 3664 LEU A O     1 
ATOM   15336 C  CB    . LEU A 1 3664 ? 141.455 156.454 196.322 1.00 72.01  ? 3664 LEU A CB    1 
ATOM   15337 C  CG    . LEU A 1 3664 ? 141.524 155.059 196.938 1.00 68.83  ? 3664 LEU A CG    1 
ATOM   15338 C  CD1   . LEU A 1 3664 ? 140.874 154.065 195.993 1.00 61.16  ? 3664 LEU A CD1   1 
ATOM   15339 C  CD2   . LEU A 1 3664 ? 142.962 154.672 197.229 1.00 65.21  ? 3664 LEU A CD2   1 
ATOM   15340 N  N     . GLY A 1 3665 ? 142.162 159.809 196.029 1.00 76.46  ? 3665 GLY A N     1 
ATOM   15341 C  CA    . GLY A 1 3665 ? 141.673 161.069 195.495 1.00 81.33  ? 3665 GLY A CA    1 
ATOM   15342 C  C     . GLY A 1 3665 ? 140.991 161.886 196.575 1.00 83.81  ? 3665 GLY A C     1 
ATOM   15343 O  O     . GLY A 1 3665 ? 141.528 162.083 197.672 1.00 81.29  ? 3665 GLY A O     1 
ATOM   15344 N  N     . ASP A 1 3666 ? 139.787 162.370 196.272 1.00 91.46  ? 3666 ASP A N     1 
ATOM   15345 C  CA    . ASP A 1 3666 ? 138.996 163.165 197.204 1.00 97.89  ? 3666 ASP A CA    1 
ATOM   15346 C  C     . ASP A 1 3666 ? 137.963 162.325 197.949 1.00 98.63  ? 3666 ASP A C     1 
ATOM   15347 O  O     . ASP A 1 3666 ? 136.935 162.851 198.389 1.00 102.49 ? 3666 ASP A O     1 
ATOM   15348 C  CB    . ASP A 1 3666 ? 138.315 164.319 196.469 1.00 96.73  ? 3666 ASP A CB    1 
ATOM   15349 C  CG    . ASP A 1 3666 ? 137.478 163.850 195.295 1.00 94.85  ? 3666 ASP A CG    1 
ATOM   15350 O  OD1   . ASP A 1 3666 ? 137.639 162.686 194.873 1.00 92.99  ? 3666 ASP A OD1   1 
ATOM   15351 O  OD2   . ASP A 1 3666 ? 136.658 164.648 194.792 1.00 91.58  ? 3666 ASP A OD2   1 
ATOM   15352 N  N     . GLN A 1 3667 ? 138.215 161.027 198.096 1.00 88.42  ? 3667 GLN A N     1 
ATOM   15353 C  CA    . GLN A 1 3667 ? 137.311 160.120 198.784 1.00 82.18  ? 3667 GLN A CA    1 
ATOM   15354 C  C     . GLN A 1 3667 ? 138.087 159.289 199.797 1.00 79.35  ? 3667 GLN A C     1 
ATOM   15355 O  O     . GLN A 1 3667 ? 139.244 158.925 199.569 1.00 84.05  ? 3667 GLN A O     1 
ATOM   15356 C  CB    . GLN A 1 3667 ? 136.591 159.197 197.791 1.00 80.57  ? 3667 GLN A CB    1 
ATOM   15357 C  CG    . GLN A 1 3667 ? 135.534 158.302 198.418 1.00 78.77  ? 3667 GLN A CG    1 
ATOM   15358 C  CD    . GLN A 1 3667 ? 135.089 157.191 197.491 1.00 83.17  ? 3667 GLN A CD    1 
ATOM   15359 O  OE1   . GLN A 1 3667 ? 135.593 157.060 196.376 1.00 85.84  ? 3667 GLN A OE1   1 
ATOM   15360 N  NE2   . GLN A 1 3667 ? 134.141 156.381 197.949 1.00 79.89  ? 3667 GLN A NE2   1 
ATOM   15361 N  N     . ASP A 1 3668 ? 137.439 158.993 200.921 1.00 77.52  ? 3668 ASP A N     1 
ATOM   15362 C  CA    . ASP A 1 3668 ? 138.022 158.177 201.978 1.00 74.88  ? 3668 ASP A CA    1 
ATOM   15363 C  C     . ASP A 1 3668 ? 137.253 156.865 202.039 1.00 75.11  ? 3668 ASP A C     1 
ATOM   15364 O  O     . ASP A 1 3668 ? 136.018 156.863 201.996 1.00 72.57  ? 3668 ASP A O     1 
ATOM   15365 C  CB    . ASP A 1 3668 ? 137.971 158.905 203.327 1.00 70.19  ? 3668 ASP A CB    1 
ATOM   15366 C  CG    . ASP A 1 3668 ? 138.759 158.191 204.413 1.00 77.01  ? 3668 ASP A CG    1 
ATOM   15367 O  OD1   . ASP A 1 3668 ? 139.016 156.977 204.284 1.00 78.82  ? 3668 ASP A OD1   1 
ATOM   15368 O  OD2   . ASP A 1 3668 ? 139.124 158.854 205.407 1.00 82.01  ? 3668 ASP A OD2   1 
ATOM   15369 N  N     . ILE A 1 3669 ? 137.982 155.755 202.140 1.00 72.92  ? 3669 ILE A N     1 
ATOM   15370 C  CA    . ILE A 1 3669 ? 137.411 154.419 202.030 1.00 66.87  ? 3669 ILE A CA    1 
ATOM   15371 C  C     . ILE A 1 3669 ? 137.817 153.602 203.249 1.00 65.67  ? 3669 ILE A C     1 
ATOM   15372 O  O     . ILE A 1 3669 ? 138.954 153.699 203.722 1.00 72.79  ? 3669 ILE A O     1 
ATOM   15373 C  CB    . ILE A 1 3669 ? 137.866 153.724 200.729 1.00 62.86  ? 3669 ILE A CB    1 
ATOM   15374 C  CG1   . ILE A 1 3669 ? 137.381 154.512 199.513 1.00 70.31  ? 3669 ILE A CG1   1 
ATOM   15375 C  CG2   . ILE A 1 3669 ? 137.352 152.295 200.662 1.00 64.95  ? 3669 ILE A CG2   1 
ATOM   15376 C  CD1   . ILE A 1 3669 ? 138.023 154.087 198.220 1.00 69.23  ? 3669 ILE A CD1   1 
ATOM   15377 N  N     . ASP A 1 3670 ? 136.883 152.801 203.759 1.00 65.28  ? 3670 ASP A N     1 
ATOM   15378 C  CA    . ASP A 1 3670 ? 137.151 151.912 204.884 1.00 66.24  ? 3670 ASP A CA    1 
ATOM   15379 C  C     . ASP A 1 3670 ? 137.866 150.667 204.371 1.00 66.60  ? 3670 ASP A C     1 
ATOM   15380 O  O     . ASP A 1 3670 ? 137.256 149.818 203.714 1.00 64.27  ? 3670 ASP A O     1 
ATOM   15381 C  CB    . ASP A 1 3670 ? 135.851 151.546 205.593 1.00 69.64  ? 3670 ASP A CB    1 
ATOM   15382 C  CG    . ASP A 1 3670 ? 136.058 151.214 207.057 1.00 78.36  ? 3670 ASP A CG    1 
ATOM   15383 O  OD1   . ASP A 1 3670 ? 136.958 150.405 207.365 1.00 77.09  ? 3670 ASP A OD1   1 
ATOM   15384 O  OD2   . ASP A 1 3670 ? 135.314 151.758 207.900 1.00 78.02  ? 3670 ASP A OD2   1 
ATOM   15385 N  N     . LEU A 1 3671 ? 139.158 150.557 204.670 1.00 69.36  ? 3671 LEU A N     1 
ATOM   15386 C  CA    . LEU A 1 3671 ? 139.941 149.418 204.211 1.00 64.49  ? 3671 LEU A CA    1 
ATOM   15387 C  C     . LEU A 1 3671 ? 139.537 148.148 204.951 1.00 66.31  ? 3671 LEU A C     1 
ATOM   15388 O  O     . LEU A 1 3671 ? 139.229 148.176 206.146 1.00 65.75  ? 3671 LEU A O     1 
ATOM   15389 C  CB    . LEU A 1 3671 ? 141.433 149.685 204.410 1.00 59.86  ? 3671 LEU A CB    1 
ATOM   15390 C  CG    . LEU A 1 3671 ? 142.391 148.574 203.972 1.00 54.72  ? 3671 LEU A CG    1 
ATOM   15391 C  CD1   . LEU A 1 3671 ? 142.611 148.613 202.470 1.00 56.54  ? 3671 LEU A CD1   1 
ATOM   15392 C  CD2   . LEU A 1 3671 ? 143.713 148.666 204.714 1.00 52.15  ? 3671 LEU A CD2   1 
ATOM   15393 N  N     . SER A 1 3672 ? 139.540 147.025 204.227 1.00 67.02  ? 3672 SER A N     1 
ATOM   15394 C  CA    . SER A 1 3672 ? 139.257 145.719 204.797 1.00 65.12  ? 3672 SER A CA    1 
ATOM   15395 C  C     . SER A 1 3672 ? 140.546 144.923 204.963 1.00 61.55  ? 3672 SER A C     1 
ATOM   15396 O  O     . SER A 1 3672 ? 141.414 144.961 204.083 1.00 62.92  ? 3672 SER A O     1 
ATOM   15397 C  CB    . SER A 1 3672 ? 138.282 144.932 203.914 1.00 66.40  ? 3672 SER A CB    1 
ATOM   15398 O  OG    . SER A 1 3672 ? 137.936 143.693 204.508 1.00 70.63  ? 3672 SER A OG    1 
ATOM   15399 N  N     . PRO A 1 3673 ? 140.703 144.202 206.076 1.00 62.87  ? 3673 PRO A N     1 
ATOM   15400 C  CA    . PRO A 1 3673 ? 141.975 143.500 206.324 1.00 64.71  ? 3673 PRO A CA    1 
ATOM   15401 C  C     . PRO A 1 3673 ? 142.289 142.405 205.318 1.00 65.65  ? 3673 PRO A C     1 
ATOM   15402 O  O     . PRO A 1 3673 ? 143.461 142.033 205.183 1.00 70.35  ? 3673 PRO A O     1 
ATOM   15403 C  CB    . PRO A 1 3673 ? 141.788 142.923 207.734 1.00 68.02  ? 3673 PRO A CB    1 
ATOM   15404 C  CG    . PRO A 1 3673 ? 140.308 142.843 207.920 1.00 72.97  ? 3673 PRO A CG    1 
ATOM   15405 C  CD    . PRO A 1 3673 ? 139.739 144.009 207.171 1.00 67.38  ? 3673 PRO A CD    1 
ATOM   15406 N  N     . SER A 1 3674 ? 141.294 141.878 204.611 1.00 58.85  ? 3674 SER A N     1 
ATOM   15407 C  CA    . SER A 1 3674 ? 141.506 140.780 203.678 1.00 58.60  ? 3674 SER A CA    1 
ATOM   15408 C  C     . SER A 1 3674 ? 141.905 141.246 202.284 1.00 52.79  ? 3674 SER A C     1 
ATOM   15409 O  O     . SER A 1 3674 ? 142.116 140.405 201.404 1.00 52.06  ? 3674 SER A O     1 
ATOM   15410 C  CB    . SER A 1 3674 ? 140.245 139.914 203.590 1.00 62.58  ? 3674 SER A CB    1 
ATOM   15411 O  OG    . SER A 1 3674 ? 139.350 140.414 202.612 1.00 62.91  ? 3674 SER A OG    1 
ATOM   15412 N  N     . PHE A 1 3675 ? 142.012 142.552 202.061 1.00 49.97  ? 3675 PHE A N     1 
ATOM   15413 C  CA    . PHE A 1 3675 ? 142.364 143.061 200.743 1.00 43.37  ? 3675 PHE A CA    1 
ATOM   15414 C  C     . PHE A 1 3675 ? 143.820 142.753 200.413 1.00 40.78  ? 3675 PHE A C     1 
ATOM   15415 O  O     . PHE A 1 3675 ? 144.699 142.823 201.276 1.00 47.94  ? 3675 PHE A O     1 
ATOM   15416 C  CB    . PHE A 1 3675 ? 142.123 144.569 200.675 1.00 40.44  ? 3675 PHE A CB    1 
ATOM   15417 C  CG    . PHE A 1 3675 ? 142.789 145.237 199.507 1.00 38.61  ? 3675 PHE A CG    1 
ATOM   15418 C  CD1   . PHE A 1 3675 ? 142.285 145.086 198.226 1.00 42.75  ? 3675 PHE A CD1   1 
ATOM   15419 C  CD2   . PHE A 1 3675 ? 143.926 146.007 199.687 1.00 38.30  ? 3675 PHE A CD2   1 
ATOM   15420 C  CE1   . PHE A 1 3675 ? 142.896 145.697 197.149 1.00 38.48  ? 3675 PHE A CE1   1 
ATOM   15421 C  CE2   . PHE A 1 3675 ? 144.543 146.617 198.613 1.00 36.52  ? 3675 PHE A CE2   1 
ATOM   15422 C  CZ    . PHE A 1 3675 ? 144.026 146.463 197.343 1.00 33.17  ? 3675 PHE A CZ    1 
ATOM   15423 N  N     . VAL A 1 3676 ? 144.068 142.409 199.152 1.00 35.15  ? 3676 VAL A N     1 
ATOM   15424 C  CA    . VAL A 1 3676 ? 145.419 142.185 198.648 1.00 32.44  ? 3676 VAL A CA    1 
ATOM   15425 C  C     . VAL A 1 3676 ? 145.409 142.456 197.150 1.00 31.20  ? 3676 VAL A C     1 
ATOM   15426 O  O     . VAL A 1 3676 ? 144.461 142.094 196.449 1.00 35.24  ? 3676 VAL A O     1 
ATOM   15427 C  CB    . VAL A 1 3676 ? 145.918 140.759 198.976 1.00 27.93  ? 3676 VAL A CB    1 
ATOM   15428 C  CG1   . VAL A 1 3676 ? 144.964 139.711 198.423 1.00 34.83  ? 3676 VAL A CG1   1 
ATOM   15429 C  CG2   . VAL A 1 3676 ? 147.326 140.545 198.443 1.00 28.93  ? 3676 VAL A CG2   1 
ATOM   15430 N  N     . ILE A 1 3677 ? 146.458 143.112 196.660 1.00 29.20  ? 3677 ILE A N     1 
ATOM   15431 C  CA    . ILE A 1 3677 ? 146.540 143.516 195.262 1.00 27.47  ? 3677 ILE A CA    1 
ATOM   15432 C  C     . ILE A 1 3677 ? 147.847 143.005 194.672 1.00 29.37  ? 3677 ILE A C     1 
ATOM   15433 O  O     . ILE A 1 3677 ? 148.910 143.140 195.289 1.00 28.52  ? 3677 ILE A O     1 
ATOM   15434 C  CB    . ILE A 1 3677 ? 146.425 145.045 195.099 1.00 24.87  ? 3677 ILE A CB    1 
ATOM   15435 C  CG1   . ILE A 1 3677 ? 146.695 145.455 193.650 1.00 24.57  ? 3677 ILE A CG1   1 
ATOM   15436 C  CG2   . ILE A 1 3677 ? 147.359 145.768 196.055 1.00 27.16  ? 3677 ILE A CG2   1 
ATOM   15437 C  CD1   . ILE A 1 3677 ? 146.276 146.867 193.332 1.00 31.30  ? 3677 ILE A CD1   1 
ATOM   15438 N  N     . PHE A 1 3678 ? 147.763 142.405 193.487 1.00 29.63  ? 3678 PHE A N     1 
ATOM   15439 C  CA    . PHE A 1 3678 ? 148.924 141.947 192.739 1.00 21.11  ? 3678 PHE A CA    1 
ATOM   15440 C  C     . PHE A 1 3678 ? 149.033 142.745 191.448 1.00 21.45  ? 3678 PHE A C     1 
ATOM   15441 O  O     . PHE A 1 3678 ? 148.058 142.855 190.697 1.00 29.11  ? 3678 PHE A O     1 
ATOM   15442 C  CB    . PHE A 1 3678 ? 148.826 140.453 192.420 1.00 22.99  ? 3678 PHE A CB    1 
ATOM   15443 C  CG    . PHE A 1 3678 ? 148.728 139.576 193.634 1.00 23.42  ? 3678 PHE A CG    1 
ATOM   15444 C  CD1   . PHE A 1 3678 ? 147.495 139.261 194.180 1.00 22.68  ? 3678 PHE A CD1   1 
ATOM   15445 C  CD2   . PHE A 1 3678 ? 149.868 139.057 194.222 1.00 24.40  ? 3678 PHE A CD2   1 
ATOM   15446 C  CE1   . PHE A 1 3678 ? 147.404 138.452 195.294 1.00 29.88  ? 3678 PHE A CE1   1 
ATOM   15447 C  CE2   . PHE A 1 3678 ? 149.782 138.247 195.335 1.00 24.53  ? 3678 PHE A CE2   1 
ATOM   15448 C  CZ    . PHE A 1 3678 ? 148.549 137.944 195.872 1.00 29.08  ? 3678 PHE A CZ    1 
ATOM   15449 N  N     . LEU A 1 3679 ? 150.213 143.300 191.195 1.00 21.11  ? 3679 LEU A N     1 
ATOM   15450 C  CA    . LEU A 1 3679 ? 150.496 144.005 189.954 1.00 24.27  ? 3679 LEU A CA    1 
ATOM   15451 C  C     . LEU A 1 3679 ? 151.293 143.094 189.032 1.00 26.97  ? 3679 LEU A C     1 
ATOM   15452 O  O     . LEU A 1 3679 ? 152.215 142.404 189.473 1.00 34.85  ? 3679 LEU A O     1 
ATOM   15453 C  CB    . LEU A 1 3679 ? 151.272 145.296 190.221 1.00 24.48  ? 3679 LEU A CB    1 
ATOM   15454 C  CG    . LEU A 1 3679 ? 150.753 146.186 191.352 1.00 22.86  ? 3679 LEU A CG    1 
ATOM   15455 C  CD1   . LEU A 1 3679 ? 151.665 147.385 191.550 1.00 26.62  ? 3679 LEU A CD1   1 
ATOM   15456 C  CD2   . LEU A 1 3679 ? 149.329 146.635 191.074 1.00 24.12  ? 3679 LEU A CD2   1 
ATOM   15457 N  N     . SER A 1 3680 ? 150.926 143.081 187.753 1.00 24.92  ? 3680 SER A N     1 
ATOM   15458 C  CA    . SER A 1 3680 ? 151.576 142.199 186.797 1.00 30.12  ? 3680 SER A CA    1 
ATOM   15459 C  C     . SER A 1 3680 ? 151.839 142.941 185.495 1.00 31.57  ? 3680 SER A C     1 
ATOM   15460 O  O     . SER A 1 3680 ? 151.178 143.930 185.171 1.00 36.67  ? 3680 SER A O     1 
ATOM   15461 C  CB    . SER A 1 3680 ? 150.743 140.936 186.536 1.00 36.89  ? 3680 SER A CB    1 
ATOM   15462 O  OG    . SER A 1 3680 ? 149.437 141.262 186.104 1.00 42.19  ? 3680 SER A OG    1 
ATOM   15463 N  N     . THR A 1 3681 ? 152.829 142.447 184.755 1.00 30.95  ? 3681 THR A N     1 
ATOM   15464 C  CA    . THR A 1 3681 ? 153.186 142.991 183.454 1.00 34.22  ? 3681 THR A CA    1 
ATOM   15465 C  C     . THR A 1 3681 ? 153.742 141.871 182.588 1.00 38.90  ? 3681 THR A C     1 
ATOM   15466 O  O     . THR A 1 3681 ? 154.205 140.847 183.096 1.00 40.25  ? 3681 THR A O     1 
ATOM   15467 C  CB    . THR A 1 3681 ? 154.216 144.121 183.565 1.00 31.73  ? 3681 THR A CB    1 
ATOM   15468 O  OG1   . THR A 1 3681 ? 154.573 144.577 182.254 1.00 42.15  ? 3681 THR A OG1   1 
ATOM   15469 C  CG2   . THR A 1 3681 ? 155.464 143.639 184.284 1.00 32.08  ? 3681 THR A CG2   1 
ATOM   15470 N  N     . ARG A 1 3682 ? 153.689 142.076 181.275 1.00 37.96  ? 3682 ARG A N     1 
ATOM   15471 C  CA    . ARG A 1 3682 ? 154.203 141.109 180.316 1.00 31.36  ? 3682 ARG A CA    1 
ATOM   15472 C  C     . ARG A 1 3682 ? 155.498 141.558 179.654 1.00 34.24  ? 3682 ARG A C     1 
ATOM   15473 O  O     . ARG A 1 3682 ? 156.048 140.815 178.836 1.00 44.56  ? 3682 ARG A O     1 
ATOM   15474 C  CB    . ARG A 1 3682 ? 153.150 140.820 179.242 1.00 31.82  ? 3682 ARG A CB    1 
ATOM   15475 C  CG    . ARG A 1 3682 ? 151.982 139.978 179.727 1.00 33.19  ? 3682 ARG A CG    1 
ATOM   15476 C  CD    . ARG A 1 3682 ? 150.945 139.792 178.632 1.00 33.48  ? 3682 ARG A CD    1 
ATOM   15477 N  NE    . ARG A 1 3682 ? 150.363 141.059 178.207 1.00 44.24  ? 3682 ARG A NE    1 
ATOM   15478 C  CZ    . ARG A 1 3682 ? 150.640 141.664 177.060 1.00 42.89  ? 3682 ARG A CZ    1 
ATOM   15479 N  NH1   . ARG A 1 3682 ? 151.492 141.143 176.192 1.00 35.57  ? 3682 ARG A NH1   1 
ATOM   15480 N  NH2   . ARG A 1 3682 ? 150.049 142.821 176.777 1.00 43.12  ? 3682 ARG A NH2   1 
ATOM   15481 N  N     . ASP A 1 3683 ? 155.996 142.746 179.984 1.00 30.80  ? 3683 ASP A N     1 
ATOM   15482 C  CA    . ASP A 1 3683 ? 157.210 143.270 179.371 1.00 39.17  ? 3683 ASP A CA    1 
ATOM   15483 C  C     . ASP A 1 3683 ? 158.373 143.137 180.342 1.00 42.03  ? 3683 ASP A C     1 
ATOM   15484 O  O     . ASP A 1 3683 ? 158.393 143.828 181.373 1.00 45.69  ? 3683 ASP A O     1 
ATOM   15485 C  CB    . ASP A 1 3683 ? 157.019 144.732 178.965 1.00 40.81  ? 3683 ASP A CB    1 
ATOM   15486 C  CG    . ASP A 1 3683 ? 157.983 145.167 177.879 1.00 52.34  ? 3683 ASP A CG    1 
ATOM   15487 O  OD1   . ASP A 1 3683 ? 158.743 144.312 177.378 1.00 58.58  ? 3683 ASP A OD1   1 
ATOM   15488 O  OD2   . ASP A 1 3683 ? 157.980 146.364 177.525 1.00 48.45  ? 3683 ASP A OD2   1 
ATOM   15489 N  N     . PRO A 1 3684 ? 159.355 142.272 180.073 1.00 41.47  ? 3684 PRO A N     1 
ATOM   15490 C  CA    . PRO A 1 3684 ? 160.500 142.147 180.984 1.00 42.02  ? 3684 PRO A CA    1 
ATOM   15491 C  C     . PRO A 1 3684 ? 161.521 143.264 180.857 1.00 49.47  ? 3684 PRO A C     1 
ATOM   15492 O  O     . PRO A 1 3684 ? 162.424 143.349 181.701 1.00 57.28  ? 3684 PRO A O     1 
ATOM   15493 C  CB    . PRO A 1 3684 ? 161.113 140.800 180.583 1.00 44.26  ? 3684 PRO A CB    1 
ATOM   15494 C  CG    . PRO A 1 3684 ? 160.767 140.657 179.141 1.00 42.26  ? 3684 PRO A CG    1 
ATOM   15495 C  CD    . PRO A 1 3684 ? 159.426 141.317 178.953 1.00 39.53  ? 3684 PRO A CD    1 
ATOM   15496 N  N     . THR A 1 3685 ? 161.414 144.118 179.840 1.00 48.88  ? 3685 THR A N     1 
ATOM   15497 C  CA    . THR A 1 3685 ? 162.374 145.188 179.609 1.00 50.61  ? 3685 THR A CA    1 
ATOM   15498 C  C     . THR A 1 3685 ? 161.844 146.559 180.012 1.00 53.34  ? 3685 THR A C     1 
ATOM   15499 O  O     . THR A 1 3685 ? 162.484 147.571 179.712 1.00 64.63  ? 3685 THR A O     1 
ATOM   15500 C  CB    . THR A 1 3685 ? 162.796 145.209 178.137 1.00 58.16  ? 3685 THR A CB    1 
ATOM   15501 O  OG1   . THR A 1 3685 ? 161.645 145.020 177.304 1.00 51.00  ? 3685 THR A OG1   1 
ATOM   15502 C  CG2   . THR A 1 3685 ? 163.806 144.106 177.856 1.00 61.28  ? 3685 THR A CG2   1 
ATOM   15503 N  N     . VAL A 1 3686 ? 160.693 146.617 180.682 1.00 54.51  ? 3686 VAL A N     1 
ATOM   15504 C  CA    . VAL A 1 3686 ? 160.104 147.899 181.049 1.00 56.02  ? 3686 VAL A CA    1 
ATOM   15505 C  C     . VAL A 1 3686 ? 160.868 148.501 182.222 1.00 53.37  ? 3686 VAL A C     1 
ATOM   15506 O  O     . VAL A 1 3686 ? 161.367 147.785 183.101 1.00 54.90  ? 3686 VAL A O     1 
ATOM   15507 C  CB    . VAL A 1 3686 ? 158.610 147.727 181.376 1.00 52.51  ? 3686 VAL A CB    1 
ATOM   15508 C  CG1   . VAL A 1 3686 ? 158.421 146.802 182.567 1.00 48.55  ? 3686 VAL A CG1   1 
ATOM   15509 C  CG2   . VAL A 1 3686 ? 157.949 149.075 181.630 1.00 50.29  ? 3686 VAL A CG2   1 
ATOM   15510 N  N     . GLU A 1 3687 ? 160.981 149.826 182.230 1.00 56.37  ? 3687 GLU A N     1 
ATOM   15511 C  CA    . GLU A 1 3687 ? 161.604 150.557 183.323 1.00 54.36  ? 3687 GLU A CA    1 
ATOM   15512 C  C     . GLU A 1 3687 ? 160.541 151.061 184.287 1.00 48.50  ? 3687 GLU A C     1 
ATOM   15513 O  O     . GLU A 1 3687 ? 159.490 151.556 183.870 1.00 51.77  ? 3687 GLU A O     1 
ATOM   15514 C  CB    . GLU A 1 3687 ? 162.427 151.737 182.803 1.00 62.44  ? 3687 GLU A CB    1 
ATOM   15515 C  CG    . GLU A 1 3687 ? 163.755 151.351 182.187 1.00 70.36  ? 3687 GLU A CG    1 
ATOM   15516 C  CD    . GLU A 1 3687 ? 164.933 151.719 183.069 1.00 81.17  ? 3687 GLU A CD    1 
ATOM   15517 O  OE1   . GLU A 1 3687 ? 164.709 152.077 184.244 1.00 80.38  ? 3687 GLU A OE1   1 
ATOM   15518 O  OE2   . GLU A 1 3687 ? 166.084 151.654 182.587 1.00 85.55  ? 3687 GLU A OE2   1 
ATOM   15519 N  N     . PHE A 1 3688 ? 160.822 150.932 185.581 1.00 39.77  ? 3688 PHE A N     1 
ATOM   15520 C  CA    . PHE A 1 3688 ? 159.947 151.463 186.603 1.00 40.87  ? 3688 PHE A CA    1 
ATOM   15521 C  C     . PHE A 1 3688 ? 160.655 152.576 187.365 1.00 47.26  ? 3688 PHE A C     1 
ATOM   15522 O  O     . PHE A 1 3688 ? 161.826 152.428 187.729 1.00 49.42  ? 3688 PHE A O     1 
ATOM   15523 C  CB    . PHE A 1 3688 ? 159.508 150.367 187.585 1.00 41.70  ? 3688 PHE A CB    1 
ATOM   15524 C  CG    . PHE A 1 3688 ? 158.650 149.304 186.963 1.00 43.12  ? 3688 PHE A CG    1 
ATOM   15525 C  CD1   . PHE A 1 3688 ? 157.339 149.572 186.612 1.00 41.12  ? 3688 PHE A CD1   1 
ATOM   15526 C  CD2   . PHE A 1 3688 ? 159.153 148.034 186.736 1.00 37.35  ? 3688 PHE A CD2   1 
ATOM   15527 C  CE1   . PHE A 1 3688 ? 156.546 148.597 186.041 1.00 38.67  ? 3688 PHE A CE1   1 
ATOM   15528 C  CE2   . PHE A 1 3688 ? 158.365 147.054 186.167 1.00 35.21  ? 3688 PHE A CE2   1 
ATOM   15529 C  CZ    . PHE A 1 3688 ? 157.060 147.337 185.819 1.00 38.04  ? 3688 PHE A CZ    1 
ATOM   15530 N  N     . PRO A 1 3689 ? 159.980 153.701 187.606 1.00 48.31  ? 3689 PRO A N     1 
ATOM   15531 C  CA    . PRO A 1 3689 ? 160.612 154.776 188.365 1.00 44.59  ? 3689 PRO A CA    1 
ATOM   15532 C  C     . PRO A 1 3689 ? 160.893 154.336 189.789 1.00 41.46  ? 3689 PRO A C     1 
ATOM   15533 O  O     . PRO A 1 3689 ? 160.194 153.463 190.333 1.00 39.42  ? 3689 PRO A O     1 
ATOM   15534 C  CB    . PRO A 1 3689 ? 159.565 155.904 188.317 1.00 43.73  ? 3689 PRO A CB    1 
ATOM   15535 C  CG    . PRO A 1 3689 ? 158.270 155.206 188.069 1.00 39.98  ? 3689 PRO A CG    1 
ATOM   15536 C  CD    . PRO A 1 3689 ? 158.604 154.033 187.201 1.00 43.13  ? 3689 PRO A CD    1 
ATOM   15537 N  N     . PRO A 1 3690 ? 161.919 154.901 190.432 1.00 41.62  ? 3690 PRO A N     1 
ATOM   15538 C  CA    . PRO A 1 3690 ? 162.285 154.436 191.782 1.00 40.63  ? 3690 PRO A CA    1 
ATOM   15539 C  C     . PRO A 1 3690 ? 161.166 154.562 192.799 1.00 38.87  ? 3690 PRO A C     1 
ATOM   15540 O  O     . PRO A 1 3690 ? 161.112 153.764 193.743 1.00 37.73  ? 3690 PRO A O     1 
ATOM   15541 C  CB    . PRO A 1 3690 ? 163.481 155.328 192.146 1.00 41.62  ? 3690 PRO A CB    1 
ATOM   15542 C  CG    . PRO A 1 3690 ? 164.017 155.807 190.838 1.00 42.44  ? 3690 PRO A CG    1 
ATOM   15543 C  CD    . PRO A 1 3690 ? 162.828 155.949 189.941 1.00 43.21  ? 3690 PRO A CD    1 
ATOM   15544 N  N     . ASP A 1 3691 ? 160.268 155.538 192.638 1.00 40.63  ? 3691 ASP A N     1 
ATOM   15545 C  CA    . ASP A 1 3691 ? 159.147 155.657 193.563 1.00 40.08  ? 3691 ASP A CA    1 
ATOM   15546 C  C     . ASP A 1 3691 ? 158.251 154.425 193.503 1.00 36.95  ? 3691 ASP A C     1 
ATOM   15547 O  O     . ASP A 1 3691 ? 157.788 153.935 194.538 1.00 35.52  ? 3691 ASP A O     1 
ATOM   15548 C  CB    . ASP A 1 3691 ? 158.353 156.934 193.274 1.00 41.82  ? 3691 ASP A CB    1 
ATOM   15549 C  CG    . ASP A 1 3691 ? 157.741 156.951 191.883 1.00 50.28  ? 3691 ASP A CG    1 
ATOM   15550 O  OD1   . ASP A 1 3691 ? 157.964 155.996 191.111 1.00 54.41  ? 3691 ASP A OD1   1 
ATOM   15551 O  OD2   . ASP A 1 3691 ? 157.032 157.926 191.560 1.00 51.12  ? 3691 ASP A OD2   1 
ATOM   15552 N  N     . LEU A 1 3692 ? 158.000 153.906 192.298 1.00 36.97  ? 3692 LEU A N     1 
ATOM   15553 C  CA    . LEU A 1 3692 ? 157.225 152.677 192.169 1.00 31.24  ? 3692 LEU A CA    1 
ATOM   15554 C  C     . LEU A 1 3692 ? 158.041 151.458 192.580 1.00 27.56  ? 3692 LEU A C     1 
ATOM   15555 O  O     . LEU A 1 3692 ? 157.495 150.508 193.151 1.00 28.53  ? 3692 LEU A O     1 
ATOM   15556 C  CB    . LEU A 1 3692 ? 156.716 152.520 190.736 1.00 35.41  ? 3692 LEU A CB    1 
ATOM   15557 C  CG    . LEU A 1 3692 ? 155.850 151.289 190.460 1.00 33.73  ? 3692 LEU A CG    1 
ATOM   15558 C  CD1   . LEU A 1 3692 ? 154.696 151.210 191.446 1.00 30.44  ? 3692 LEU A CD1   1 
ATOM   15559 C  CD2   . LEU A 1 3692 ? 155.334 151.302 189.032 1.00 38.27  ? 3692 LEU A CD2   1 
ATOM   15560 N  N     . CYS A 1 3693 ? 159.346 151.467 192.298 1.00 28.21  ? 3693 CYS A N     1 
ATOM   15561 C  CA    . CYS A 1 3693 ? 160.199 150.356 192.707 1.00 24.39  ? 3693 CYS A CA    1 
ATOM   15562 C  C     . CYS A 1 3693 ? 160.253 150.221 194.221 1.00 26.35  ? 3693 CYS A C     1 
ATOM   15563 O  O     . CYS A 1 3693 ? 160.473 149.121 194.740 1.00 30.13  ? 3693 CYS A O     1 
ATOM   15564 C  CB    . CYS A 1 3693 ? 161.610 150.540 192.148 1.00 27.18  ? 3693 CYS A CB    1 
ATOM   15565 S  SG    . CYS A 1 3693 ? 161.724 150.475 190.350 1.00 43.16  ? 3693 CYS A SG    1 
ATOM   15566 N  N     . SER A 1 3694 ? 160.062 151.325 194.944 1.00 26.90  ? 3694 SER A N     1 
ATOM   15567 C  CA    . SER A 1 3694 ? 160.123 151.282 196.399 1.00 22.52  ? 3694 SER A CA    1 
ATOM   15568 C  C     . SER A 1 3694 ? 158.876 150.666 197.019 1.00 21.74  ? 3694 SER A C     1 
ATOM   15569 O  O     . SER A 1 3694 ? 158.962 150.068 198.096 1.00 22.52  ? 3694 SER A O     1 
ATOM   15570 C  CB    . SER A 1 3694 ? 160.337 152.690 196.956 1.00 22.75  ? 3694 SER A CB    1 
ATOM   15571 O  OG    . SER A 1 3694 ? 159.322 153.573 196.511 1.00 28.58  ? 3694 SER A OG    1 
ATOM   15572 N  N     . ARG A 1 3695 ? 157.718 150.797 196.372 1.00 21.68  ? 3695 ARG A N     1 
ATOM   15573 C  CA    . ARG A 1 3695 ? 156.456 150.388 196.975 1.00 19.50  ? 3695 ARG A CA    1 
ATOM   15574 C  C     . ARG A 1 3695 ? 156.078 148.938 196.699 1.00 20.60  ? 3695 ARG A C     1 
ATOM   15575 O  O     . ARG A 1 3695 ? 155.116 148.447 197.298 1.00 25.13  ? 3695 ARG A O     1 
ATOM   15576 C  CB    . ARG A 1 3695 ? 155.319 151.291 196.485 1.00 18.70  ? 3695 ARG A CB    1 
ATOM   15577 C  CG    . ARG A 1 3695 ? 155.649 152.768 196.475 1.00 25.28  ? 3695 ARG A CG    1 
ATOM   15578 C  CD    . ARG A 1 3695 ? 154.645 153.545 195.637 1.00 30.07  ? 3695 ARG A CD    1 
ATOM   15579 N  NE    . ARG A 1 3695 ? 155.134 154.863 195.248 1.00 37.04  ? 3695 ARG A NE    1 
ATOM   15580 C  CZ    . ARG A 1 3695 ? 155.346 155.872 196.083 1.00 35.30  ? 3695 ARG A CZ    1 
ATOM   15581 N  NH1   . ARG A 1 3695 ? 155.105 155.763 197.379 1.00 32.27  ? 3695 ARG A NH1   1 
ATOM   15582 N  NH2   . ARG A 1 3695 ? 155.807 157.024 195.603 1.00 37.62  ? 3695 ARG A NH2   1 
ATOM   15583 N  N     . VAL A 1 3696 ? 156.795 148.240 195.818 1.00 19.22  ? 3696 VAL A N     1 
ATOM   15584 C  CA    . VAL A 1 3696 ? 156.417 146.892 195.417 1.00 16.20  ? 3696 VAL A CA    1 
ATOM   15585 C  C     . VAL A 1 3696 ? 157.621 145.968 195.521 1.00 18.47  ? 3696 VAL A C     1 
ATOM   15586 O  O     . VAL A 1 3696 ? 158.776 146.400 195.493 1.00 22.44  ? 3696 VAL A O     1 
ATOM   15587 C  CB    . VAL A 1 3696 ? 155.842 146.847 193.984 1.00 17.86  ? 3696 VAL A CB    1 
ATOM   15588 C  CG1   . VAL A 1 3696 ? 154.568 147.670 193.891 1.00 19.28  ? 3696 VAL A CG1   1 
ATOM   15589 C  CG2   . VAL A 1 3696 ? 156.876 147.335 192.985 1.00 20.87  ? 3696 VAL A CG2   1 
ATOM   15590 N  N     . THR A 1 3697 ? 157.332 144.675 195.645 1.00 16.12  ? 3697 THR A N     1 
ATOM   15591 C  CA    . THR A 1 3697 ? 158.346 143.631 195.616 1.00 18.56  ? 3697 THR A CA    1 
ATOM   15592 C  C     . THR A 1 3697 ? 158.304 142.959 194.250 1.00 18.22  ? 3697 THR A C     1 
ATOM   15593 O  O     . THR A 1 3697 ? 157.310 142.312 193.903 1.00 20.20  ? 3697 THR A O     1 
ATOM   15594 C  CB    . THR A 1 3697 ? 158.119 142.603 196.724 1.00 18.55  ? 3697 THR A CB    1 
ATOM   15595 O  OG1   . THR A 1 3697 ? 156.849 141.967 196.536 1.00 18.93  ? 3697 THR A OG1   1 
ATOM   15596 C  CG2   . THR A 1 3697 ? 158.147 143.271 198.087 1.00 23.85  ? 3697 THR A CG2   1 
ATOM   15597 N  N     . PHE A 1 3698 ? 159.378 143.112 193.481 1.00 19.66  ? 3698 PHE A N     1 
ATOM   15598 C  CA    . PHE A 1 3698 ? 159.422 142.540 192.143 1.00 17.40  ? 3698 PHE A CA    1 
ATOM   15599 C  C     . PHE A 1 3698 ? 159.519 141.023 192.217 1.00 23.99  ? 3698 PHE A C     1 
ATOM   15600 O  O     . PHE A 1 3698 ? 160.318 140.477 192.983 1.00 29.70  ? 3698 PHE A O     1 
ATOM   15601 C  CB    . PHE A 1 3698 ? 160.604 143.111 191.363 1.00 21.76  ? 3698 PHE A CB    1 
ATOM   15602 C  CG    . PHE A 1 3698 ? 160.462 144.568 191.035 1.00 26.22  ? 3698 PHE A CG    1 
ATOM   15603 C  CD1   . PHE A 1 3698 ? 159.494 144.999 190.145 1.00 26.85  ? 3698 PHE A CD1   1 
ATOM   15604 C  CD2   . PHE A 1 3698 ? 161.292 145.508 191.621 1.00 27.75  ? 3698 PHE A CD2   1 
ATOM   15605 C  CE1   . PHE A 1 3698 ? 159.358 146.338 189.841 1.00 26.97  ? 3698 PHE A CE1   1 
ATOM   15606 C  CE2   . PHE A 1 3698 ? 161.161 146.848 191.322 1.00 32.90  ? 3698 PHE A CE2   1 
ATOM   15607 C  CZ    . PHE A 1 3698 ? 160.193 147.264 190.431 1.00 34.15  ? 3698 PHE A CZ    1 
ATOM   15608 N  N     . VAL A 1 3699 ? 158.696 140.346 191.428 1.00 25.77  ? 3699 VAL A N     1 
ATOM   15609 C  CA    . VAL A 1 3699 ? 158.700 138.888 191.333 1.00 21.39  ? 3699 VAL A CA    1 
ATOM   15610 C  C     . VAL A 1 3699 ? 158.853 138.562 189.852 1.00 22.76  ? 3699 VAL A C     1 
ATOM   15611 O  O     . VAL A 1 3699 ? 157.875 138.508 189.102 1.00 24.30  ? 3699 VAL A O     1 
ATOM   15612 C  CB    . VAL A 1 3699 ? 157.437 138.258 191.924 1.00 15.29  ? 3699 VAL A CB    1 
ATOM   15613 C  CG1   . VAL A 1 3699 ? 157.562 136.749 191.946 1.00 17.40  ? 3699 VAL A CG1   1 
ATOM   15614 C  CG2   . VAL A 1 3699 ? 157.183 138.787 193.326 1.00 14.34  ? 3699 VAL A CG2   1 
ATOM   15615 N  N     . ASN A 1 3700 ? 160.092 138.340 189.421 1.00 19.82  ? 3700 ASN A N     1 
ATOM   15616 C  CA    . ASN A 1 3700 ? 160.410 138.167 188.008 1.00 22.23  ? 3700 ASN A CA    1 
ATOM   15617 C  C     . ASN A 1 3700 ? 160.315 136.688 187.650 1.00 25.48  ? 3700 ASN A C     1 
ATOM   15618 O  O     . ASN A 1 3700 ? 161.084 135.867 188.161 1.00 27.64  ? 3700 ASN A O     1 
ATOM   15619 C  CB    . ASN A 1 3700 ? 161.800 138.718 187.704 1.00 21.12  ? 3700 ASN A CB    1 
ATOM   15620 C  CG    . ASN A 1 3700 ? 161.959 139.134 186.256 1.00 21.94  ? 3700 ASN A CG    1 
ATOM   15621 O  OD1   . ASN A 1 3700 ? 161.049 138.963 185.446 1.00 27.98  ? 3700 ASN A OD1   1 
ATOM   15622 N  ND2   . ASN A 1 3700 ? 163.119 139.685 185.924 1.00 22.11  ? 3700 ASN A ND2   1 
ATOM   15623 N  N     . PHE A 1 3701 ? 159.374 136.351 186.769 1.00 23.34  ? 3701 PHE A N     1 
ATOM   15624 C  CA    . PHE A 1 3701 ? 159.213 134.983 186.277 1.00 22.14  ? 3701 PHE A CA    1 
ATOM   15625 C  C     . PHE A 1 3701 ? 160.017 134.845 184.991 1.00 25.56  ? 3701 PHE A C     1 
ATOM   15626 O  O     . PHE A 1 3701 ? 159.498 135.014 183.886 1.00 30.85  ? 3701 PHE A O     1 
ATOM   15627 C  CB    . PHE A 1 3701 ? 157.743 134.654 186.054 1.00 23.80  ? 3701 PHE A CB    1 
ATOM   15628 C  CG    . PHE A 1 3701 ? 157.002 134.290 187.307 1.00 21.78  ? 3701 PHE A CG    1 
ATOM   15629 C  CD1   . PHE A 1 3701 ? 156.615 135.265 188.209 1.00 21.18  ? 3701 PHE A CD1   1 
ATOM   15630 C  CD2   . PHE A 1 3701 ? 156.685 132.970 187.579 1.00 22.48  ? 3701 PHE A CD2   1 
ATOM   15631 C  CE1   . PHE A 1 3701 ? 155.930 134.929 189.361 1.00 22.58  ? 3701 PHE A CE1   1 
ATOM   15632 C  CE2   . PHE A 1 3701 ? 156.001 132.629 188.728 1.00 21.40  ? 3701 PHE A CE2   1 
ATOM   15633 C  CZ    . PHE A 1 3701 ? 155.622 133.610 189.619 1.00 23.10  ? 3701 PHE A CZ    1 
ATOM   15634 N  N     . THR A 1 3702 ? 161.299 134.533 185.134 1.00 25.58  ? 3702 THR A N     1 
ATOM   15635 C  CA    . THR A 1 3702 ? 162.168 134.333 183.986 1.00 22.14  ? 3702 THR A CA    1 
ATOM   15636 C  C     . THR A 1 3702 ? 162.166 132.866 183.566 1.00 23.60  ? 3702 THR A C     1 
ATOM   15637 O  O     . THR A 1 3702 ? 161.677 131.985 184.276 1.00 26.17  ? 3702 THR A O     1 
ATOM   15638 C  CB    . THR A 1 3702 ? 163.592 134.794 184.298 1.00 23.38  ? 3702 THR A CB    1 
ATOM   15639 O  OG1   . THR A 1 3702 ? 164.144 133.981 185.340 1.00 34.25  ? 3702 THR A OG1   1 
ATOM   15640 C  CG2   . THR A 1 3702 ? 163.597 136.249 184.739 1.00 25.55  ? 3702 THR A CG2   1 
ATOM   15641 N  N     . VAL A 1 3703 ? 162.723 132.610 182.387 1.00 24.05  ? 3703 VAL A N     1 
ATOM   15642 C  CA    . VAL A 1 3703 ? 162.822 131.264 181.835 1.00 29.49  ? 3703 VAL A CA    1 
ATOM   15643 C  C     . VAL A 1 3703 ? 164.239 130.763 182.069 1.00 30.53  ? 3703 VAL A C     1 
ATOM   15644 O  O     . VAL A 1 3703 ? 165.209 131.382 181.614 1.00 32.40  ? 3703 VAL A O     1 
ATOM   15645 C  CB    . VAL A 1 3703 ? 162.465 131.241 180.341 1.00 27.30  ? 3703 VAL A CB    1 
ATOM   15646 C  CG1   . VAL A 1 3703 ? 162.535 129.822 179.801 1.00 22.10  ? 3703 VAL A CG1   1 
ATOM   15647 C  CG2   . VAL A 1 3703 ? 161.085 131.837 180.118 1.00 31.55  ? 3703 VAL A CG2   1 
ATOM   15648 N  N     . THR A 1 3704 ? 164.362 129.647 182.777 1.00 27.88  ? 3704 THR A N     1 
ATOM   15649 C  CA    . THR A 1 3704 ? 165.653 129.062 183.100 1.00 29.05  ? 3704 THR A CA    1 
ATOM   15650 C  C     . THR A 1 3704 ? 165.956 127.894 182.168 1.00 34.50  ? 3704 THR A C     1 
ATOM   15651 O  O     . THR A 1 3704 ? 165.064 127.325 181.535 1.00 37.24  ? 3704 THR A O     1 
ATOM   15652 C  CB    . THR A 1 3704 ? 165.688 128.594 184.557 1.00 34.63  ? 3704 THR A CB    1 
ATOM   15653 O  OG1   . THR A 1 3704 ? 164.712 127.566 184.755 1.00 40.72  ? 3704 THR A OG1   1 
ATOM   15654 C  CG2   . THR A 1 3704 ? 165.384 129.754 185.491 1.00 32.40  ? 3704 THR A CG2   1 
ATOM   15655 N  N     . ARG A 1 3705 ? 167.243 127.548 182.087 1.00 32.29  ? 3705 ARG A N     1 
ATOM   15656 C  CA    . ARG A 1 3705 ? 167.662 126.467 181.202 1.00 26.65  ? 3705 ARG A CA    1 
ATOM   15657 C  C     . ARG A 1 3705 ? 167.083 125.128 181.643 1.00 28.31  ? 3705 ARG A C     1 
ATOM   15658 O  O     . ARG A 1 3705 ? 166.631 124.338 180.808 1.00 31.34  ? 3705 ARG A O     1 
ATOM   15659 C  CB    . ARG A 1 3705 ? 169.187 126.398 181.141 1.00 29.67  ? 3705 ARG A CB    1 
ATOM   15660 C  CG    . ARG A 1 3705 ? 169.843 127.660 180.612 1.00 31.43  ? 3705 ARG A CG    1 
ATOM   15661 C  CD    . ARG A 1 3705 ? 171.245 127.378 180.096 1.00 33.65  ? 3705 ARG A CD    1 
ATOM   15662 N  NE    . ARG A 1 3705 ? 171.814 128.531 179.407 1.00 37.69  ? 3705 ARG A NE    1 
ATOM   15663 C  CZ    . ARG A 1 3705 ? 172.187 128.533 178.135 1.00 41.81  ? 3705 ARG A CZ    1 
ATOM   15664 N  NH1   . ARG A 1 3705 ? 172.070 127.455 177.378 1.00 33.36  ? 3705 ARG A NH1   1 
ATOM   15665 N  NH2   . ARG A 1 3705 ? 172.690 129.646 177.609 1.00 35.71  ? 3705 ARG A NH2   1 
ATOM   15666 N  N     . SER A 1 3706 ? 167.093 124.853 182.949 1.00 29.24  ? 3706 SER A N     1 
ATOM   15667 C  CA    . SER A 1 3706 ? 166.576 123.579 183.441 1.00 30.14  ? 3706 SER A CA    1 
ATOM   15668 C  C     . SER A 1 3706 ? 165.077 123.451 183.196 1.00 30.02  ? 3706 SER A C     1 
ATOM   15669 O  O     . SER A 1 3706 ? 164.599 122.391 182.772 1.00 29.80  ? 3706 SER A O     1 
ATOM   15670 C  CB    . SER A 1 3706 ? 166.891 123.427 184.928 1.00 38.88  ? 3706 SER A CB    1 
ATOM   15671 O  OG    . SER A 1 3706 ? 166.195 124.392 185.697 1.00 40.14  ? 3706 SER A OG    1 
ATOM   15672 N  N     . SER A 1 3707 ? 164.320 124.519 183.459 1.00 26.91  ? 3707 SER A N     1 
ATOM   15673 C  CA    . SER A 1 3707 ? 162.877 124.475 183.242 1.00 26.51  ? 3707 SER A CA    1 
ATOM   15674 C  C     . SER A 1 3707 ? 162.547 124.271 181.771 1.00 30.84  ? 3707 SER A C     1 
ATOM   15675 O  O     . SER A 1 3707 ? 161.655 123.486 181.429 1.00 37.36  ? 3707 SER A O     1 
ATOM   15676 C  CB    . SER A 1 3707 ? 162.228 125.755 183.765 1.00 28.95  ? 3707 SER A CB    1 
ATOM   15677 O  OG    . SER A 1 3707 ? 160.951 125.953 183.184 1.00 39.59  ? 3707 SER A OG    1 
ATOM   15678 N  N     . LEU A 1 3708 ? 163.257 124.969 180.883 1.00 26.95  ? 3708 LEU A N     1 
ATOM   15679 C  CA    . LEU A 1 3708 ? 163.012 124.805 179.454 1.00 24.89  ? 3708 LEU A CA    1 
ATOM   15680 C  C     . LEU A 1 3708 ? 163.411 123.415 178.978 1.00 27.49  ? 3708 LEU A C     1 
ATOM   15681 O  O     . LEU A 1 3708 ? 162.735 122.830 178.125 1.00 36.35  ? 3708 LEU A O     1 
ATOM   15682 C  CB    . LEU A 1 3708 ? 163.756 125.876 178.663 1.00 25.21  ? 3708 LEU A CB    1 
ATOM   15683 C  CG    . LEU A 1 3708 ? 163.341 125.953 177.195 1.00 24.98  ? 3708 LEU A CG    1 
ATOM   15684 C  CD1   . LEU A 1 3708 ? 161.902 126.419 177.070 1.00 20.38  ? 3708 LEU A CD1   1 
ATOM   15685 C  CD2   . LEU A 1 3708 ? 164.270 126.868 176.437 1.00 22.08  ? 3708 LEU A CD2   1 
ATOM   15686 N  N     . GLN A 1 3709 ? 164.510 122.873 179.508 1.00 24.37  ? 3709 GLN A N     1 
ATOM   15687 C  CA    . GLN A 1 3709 ? 164.897 121.510 179.160 1.00 22.01  ? 3709 GLN A CA    1 
ATOM   15688 C  C     . GLN A 1 3709 ? 163.825 120.516 179.581 1.00 27.07  ? 3709 GLN A C     1 
ATOM   15689 O  O     . GLN A 1 3709 ? 163.468 119.615 178.814 1.00 33.64  ? 3709 GLN A O     1 
ATOM   15690 C  CB    . GLN A 1 3709 ? 166.235 121.157 179.807 1.00 22.46  ? 3709 GLN A CB    1 
ATOM   15691 C  CG    . GLN A 1 3709 ? 167.447 121.712 179.085 1.00 25.64  ? 3709 GLN A CG    1 
ATOM   15692 C  CD    . GLN A 1 3709 ? 168.718 121.579 179.897 1.00 32.29  ? 3709 GLN A CD    1 
ATOM   15693 O  OE1   . GLN A 1 3709 ? 168.751 120.874 180.906 1.00 34.37  ? 3709 GLN A OE1   1 
ATOM   15694 N  NE2   . GLN A 1 3709 ? 169.773 122.258 179.464 1.00 33.77  ? 3709 GLN A NE2   1 
ATOM   15695 N  N     . SER A 1 3710 ? 163.294 120.670 180.796 1.00 25.45  ? 3710 SER A N     1 
ATOM   15696 C  CA    . SER A 1 3710 ? 162.230 119.781 181.253 1.00 28.26  ? 3710 SER A CA    1 
ATOM   15697 C  C     . SER A 1 3710 ? 160.984 119.921 180.386 1.00 31.54  ? 3710 SER A C     1 
ATOM   15698 O  O     . SER A 1 3710 ? 160.352 118.920 180.025 1.00 38.21  ? 3710 SER A O     1 
ATOM   15699 C  CB    . SER A 1 3710 ? 161.902 120.068 182.717 1.00 28.91  ? 3710 SER A CB    1 
ATOM   15700 O  OG    . SER A 1 3710 ? 162.928 119.593 183.570 1.00 32.45  ? 3710 SER A OG    1 
ATOM   15701 N  N     . GLN A 1 3711 ? 160.618 121.157 180.039 1.00 27.36  ? 3711 GLN A N     1 
ATOM   15702 C  CA    . GLN A 1 3711 ? 159.437 121.387 179.213 1.00 29.57  ? 3711 GLN A CA    1 
ATOM   15703 C  C     . GLN A 1 3711 ? 159.594 120.750 177.837 1.00 31.76  ? 3711 GLN A C     1 
ATOM   15704 O  O     . GLN A 1 3711 ? 158.675 120.092 177.334 1.00 34.53  ? 3711 GLN A O     1 
ATOM   15705 C  CB    . GLN A 1 3711 ? 159.179 122.889 179.090 1.00 30.71  ? 3711 GLN A CB    1 
ATOM   15706 C  CG    . GLN A 1 3711 ? 157.879 123.253 178.398 1.00 47.82  ? 3711 GLN A CG    1 
ATOM   15707 C  CD    . GLN A 1 3711 ? 157.569 124.734 178.494 1.00 47.09  ? 3711 GLN A CD    1 
ATOM   15708 O  OE1   . GLN A 1 3711 ? 158.385 125.521 178.974 1.00 36.42  ? 3711 GLN A OE1   1 
ATOM   15709 N  NE2   . GLN A 1 3711 ? 156.385 125.122 178.036 1.00 49.42  ? 3711 GLN A NE2   1 
ATOM   15710 N  N     . CYS A 1 3712 ? 160.763 120.926 177.217 1.00 29.83  ? 3712 CYS A N     1 
ATOM   15711 C  CA    . CYS A 1 3712 ? 160.995 120.357 175.894 1.00 27.01  ? 3712 CYS A CA    1 
ATOM   15712 C  C     . CYS A 1 3712 ? 161.053 118.836 175.946 1.00 29.35  ? 3712 CYS A C     1 
ATOM   15713 O  O     . CYS A 1 3712 ? 160.570 118.161 175.030 1.00 36.18  ? 3712 CYS A O     1 
ATOM   15714 C  CB    . CYS A 1 3712 ? 162.281 120.927 175.297 1.00 25.84  ? 3712 CYS A CB    1 
ATOM   15715 S  SG    . CYS A 1 3712 ? 162.208 122.697 174.938 1.00 42.60  ? 3712 CYS A SG    1 
ATOM   15716 N  N     . LEU A 1 3713 ? 161.643 118.276 177.006 1.00 28.41  ? 3713 LEU A N     1 
ATOM   15717 C  CA    . LEU A 1 3713 ? 161.668 116.825 177.154 1.00 29.60  ? 3713 LEU A CA    1 
ATOM   15718 C  C     . LEU A 1 3713 ? 160.260 116.266 177.304 1.00 33.53  ? 3713 LEU A C     1 
ATOM   15719 O  O     . LEU A 1 3713 ? 159.920 115.247 176.690 1.00 37.09  ? 3713 LEU A O     1 
ATOM   15720 C  CB    . LEU A 1 3713 ? 162.535 116.437 178.351 1.00 29.86  ? 3713 LEU A CB    1 
ATOM   15721 C  CG    . LEU A 1 3713 ? 162.661 114.945 178.659 1.00 34.25  ? 3713 LEU A CG    1 
ATOM   15722 C  CD1   . LEU A 1 3713 ? 163.067 114.176 177.416 1.00 32.48  ? 3713 LEU A CD1   1 
ATOM   15723 C  CD2   . LEU A 1 3713 ? 163.660 114.717 179.781 1.00 40.17  ? 3713 LEU A CD2   1 
ATOM   15724 N  N     . ASN A 1 3714 ? 159.421 116.924 178.107 1.00 32.85  ? 3714 ASN A N     1 
ATOM   15725 C  CA    . ASN A 1 3714 ? 158.036 116.482 178.242 1.00 31.64  ? 3714 ASN A CA    1 
ATOM   15726 C  C     . ASN A 1 3714 ? 157.295 116.589 176.915 1.00 33.94  ? 3714 ASN A C     1 
ATOM   15727 O  O     . ASN A 1 3714 ? 156.523 115.693 176.551 1.00 40.85  ? 3714 ASN A O     1 
ATOM   15728 C  CB    . ASN A 1 3714 ? 157.327 117.299 179.321 1.00 37.86  ? 3714 ASN A CB    1 
ATOM   15729 C  CG    . ASN A 1 3714 ? 157.954 117.125 180.690 1.00 42.80  ? 3714 ASN A CG    1 
ATOM   15730 O  OD1   . ASN A 1 3714 ? 158.931 116.394 180.849 1.00 45.11  ? 3714 ASN A OD1   1 
ATOM   15731 N  ND2   . ASN A 1 3714 ? 157.395 117.799 181.687 1.00 44.93  ? 3714 ASN A ND2   1 
ATOM   15732 N  N     . GLU A 1 3715 ? 157.522 117.679 176.176 1.00 33.13  ? 3715 GLU A N     1 
ATOM   15733 C  CA    . GLU A 1 3715 ? 156.850 117.860 174.893 1.00 33.67  ? 3715 GLU A CA    1 
ATOM   15734 C  C     . GLU A 1 3715 ? 157.248 116.773 173.902 1.00 35.70  ? 3715 GLU A C     1 
ATOM   15735 O  O     . GLU A 1 3715 ? 156.394 116.202 173.215 1.00 41.46  ? 3715 GLU A O     1 
ATOM   15736 C  CB    . GLU A 1 3715 ? 157.167 119.246 174.330 1.00 36.24  ? 3715 GLU A CB    1 
ATOM   15737 C  CG    . GLU A 1 3715 ? 156.052 119.848 173.493 1.00 47.10  ? 3715 GLU A CG    1 
ATOM   15738 C  CD    . GLU A 1 3715 ? 156.237 121.335 173.261 1.00 61.18  ? 3715 GLU A CD    1 
ATOM   15739 O  OE1   . GLU A 1 3715 ? 156.649 122.040 174.206 1.00 57.58  ? 3715 GLU A OE1   1 
ATOM   15740 O  OE2   . GLU A 1 3715 ? 155.971 121.800 172.132 1.00 58.97  ? 3715 GLU A OE2   1 
ATOM   15741 N  N     . VAL A 1 3716 ? 158.546 116.466 173.817 1.00 34.21  ? 3716 VAL A N     1 
ATOM   15742 C  CA    . VAL A 1 3716 ? 158.987 115.450 172.866 1.00 30.45  ? 3716 VAL A CA    1 
ATOM   15743 C  C     . VAL A 1 3716 ? 158.536 114.062 173.306 1.00 37.11  ? 3716 VAL A C     1 
ATOM   15744 O  O     . VAL A 1 3716 ? 158.235 113.209 172.463 1.00 45.82  ? 3716 VAL A O     1 
ATOM   15745 C  CB    . VAL A 1 3716 ? 160.512 115.516 172.649 1.00 29.62  ? 3716 VAL A CB    1 
ATOM   15746 C  CG1   . VAL A 1 3716 ? 161.273 115.045 173.876 1.00 31.12  ? 3716 VAL A CG1   1 
ATOM   15747 C  CG2   . VAL A 1 3716 ? 160.906 114.702 171.426 1.00 31.06  ? 3716 VAL A CG2   1 
ATOM   15748 N  N     . LEU A 1 3717 ? 158.475 113.805 174.616 1.00 36.92  ? 3717 LEU A N     1 
ATOM   15749 C  CA    . LEU A 1 3717 ? 157.957 112.524 175.082 1.00 33.84  ? 3717 LEU A CA    1 
ATOM   15750 C  C     . LEU A 1 3717 ? 156.485 112.368 174.724 1.00 40.12  ? 3717 LEU A C     1 
ATOM   15751 O  O     . LEU A 1 3717 ? 156.055 111.293 174.293 1.00 51.19  ? 3717 LEU A O     1 
ATOM   15752 C  CB    . LEU A 1 3717 ? 158.164 112.388 176.589 1.00 38.28  ? 3717 LEU A CB    1 
ATOM   15753 C  CG    . LEU A 1 3717 ? 159.408 111.610 177.017 1.00 40.98  ? 3717 LEU A CG    1 
ATOM   15754 C  CD1   . LEU A 1 3717 ? 159.489 111.516 178.531 1.00 50.47  ? 3717 LEU A CD1   1 
ATOM   15755 C  CD2   . LEU A 1 3717 ? 159.415 110.226 176.388 1.00 44.80  ? 3717 LEU A CD2   1 
ATOM   15756 N  N     . LYS A 1 3718 ? 155.697 113.433 174.893 1.00 40.61  ? 3718 LYS A N     1 
ATOM   15757 C  CA    . LYS A 1 3718 ? 154.290 113.374 174.510 1.00 45.12  ? 3718 LYS A CA    1 
ATOM   15758 C  C     . LYS A 1 3718 ? 154.135 113.197 173.004 1.00 48.10  ? 3718 LYS A C     1 
ATOM   15759 O  O     . LYS A 1 3718 ? 153.260 112.453 172.545 1.00 52.04  ? 3718 LYS A O     1 
ATOM   15760 C  CB    . LYS A 1 3718 ? 153.565 114.634 174.984 1.00 51.32  ? 3718 LYS A CB    1 
ATOM   15761 C  CG    . LYS A 1 3718 ? 152.157 114.792 174.434 1.00 57.62  ? 3718 LYS A CG    1 
ATOM   15762 C  CD    . LYS A 1 3718 ? 151.397 115.884 175.170 1.00 66.47  ? 3718 LYS A CD    1 
ATOM   15763 C  CE    . LYS A 1 3718 ? 152.121 117.217 175.086 1.00 73.96  ? 3718 LYS A CE    1 
ATOM   15764 N  NZ    . LYS A 1 3718 ? 151.978 118.005 176.341 1.00 71.02  ? 3718 LYS A NZ    1 
ATOM   15765 N  N     . ALA A 1 3719 ? 154.978 113.873 172.220 1.00 43.27  ? 3719 ALA A N     1 
ATOM   15766 C  CA    . ALA A 1 3719 ? 154.861 113.799 170.767 1.00 39.69  ? 3719 ALA A CA    1 
ATOM   15767 C  C     . ALA A 1 3719 ? 155.244 112.422 170.238 1.00 44.34  ? 3719 ALA A C     1 
ATOM   15768 O  O     . ALA A 1 3719 ? 154.544 111.862 169.388 1.00 53.76  ? 3719 ALA A O     1 
ATOM   15769 C  CB    . ALA A 1 3719 ? 155.725 114.879 170.119 1.00 37.73  ? 3719 ALA A CB    1 
ATOM   15770 N  N     . GLU A 1 3720 ? 156.349 111.860 170.727 1.00 42.55  ? 3720 GLU A N     1 
ATOM   15771 C  CA    . GLU A 1 3720 ? 156.876 110.618 170.173 1.00 45.67  ? 3720 GLU A CA    1 
ATOM   15772 C  C     . GLU A 1 3720 ? 156.353 109.379 170.890 1.00 49.91  ? 3720 GLU A C     1 
ATOM   15773 O  O     . GLU A 1 3720 ? 156.026 108.382 170.237 1.00 61.55  ? 3720 GLU A O     1 
ATOM   15774 C  CB    . GLU A 1 3720 ? 158.405 110.633 170.217 1.00 46.32  ? 3720 GLU A CB    1 
ATOM   15775 C  CG    . GLU A 1 3720 ? 159.044 111.585 169.221 1.00 49.97  ? 3720 GLU A CG    1 
ATOM   15776 C  CD    . GLU A 1 3720 ? 158.638 111.291 167.791 1.00 57.96  ? 3720 GLU A CD    1 
ATOM   15777 O  OE1   . GLU A 1 3720 ? 158.963 110.192 167.294 1.00 57.98  ? 3720 GLU A OE1   1 
ATOM   15778 O  OE2   . GLU A 1 3720 ? 157.992 112.157 167.164 1.00 52.90  ? 3720 GLU A OE2   1 
ATOM   15779 N  N     . ARG A 1 3721 ? 156.264 109.417 172.217 1.00 47.86  ? 3721 ARG A N     1 
ATOM   15780 C  CA    . ARG A 1 3721 ? 155.873 108.261 173.023 1.00 49.42  ? 3721 ARG A CA    1 
ATOM   15781 C  C     . ARG A 1 3721 ? 154.709 108.653 173.924 1.00 55.92  ? 3721 ARG A C     1 
ATOM   15782 O  O     . ARG A 1 3721 ? 154.881 108.851 175.133 1.00 59.70  ? 3721 ARG A O     1 
ATOM   15783 C  CB    . ARG A 1 3721 ? 157.053 107.747 173.848 1.00 45.20  ? 3721 ARG A CB    1 
ATOM   15784 C  CG    . ARG A 1 3721 ? 158.326 107.522 173.049 1.00 43.45  ? 3721 ARG A CG    1 
ATOM   15785 C  CD    . ARG A 1 3721 ? 158.282 106.208 172.290 1.00 49.95  ? 3721 ARG A CD    1 
ATOM   15786 N  NE    . ARG A 1 3721 ? 158.895 105.121 173.044 1.00 50.69  ? 3721 ARG A NE    1 
ATOM   15787 C  CZ    . ARG A 1 3721 ? 160.202 104.937 173.170 1.00 52.90  ? 3721 ARG A CZ    1 
ATOM   15788 N  NH1   . ARG A 1 3721 ? 161.073 105.755 172.601 1.00 50.44  ? 3721 ARG A NH1   1 
ATOM   15789 N  NH2   . ARG A 1 3721 ? 160.647 103.907 173.883 1.00 54.14  ? 3721 ARG A NH2   1 
ATOM   15790 N  N     . PRO A 1 3722 ? 153.504 108.785 173.360 1.00 56.60  ? 3722 PRO A N     1 
ATOM   15791 C  CA    . PRO A 1 3722 ? 152.358 109.200 174.188 1.00 57.89  ? 3722 PRO A CA    1 
ATOM   15792 C  C     . PRO A 1 3722 ? 152.064 108.250 175.335 1.00 65.17  ? 3722 PRO A C     1 
ATOM   15793 O  O     . PRO A 1 3722 ? 151.702 108.701 176.429 1.00 67.64  ? 3722 PRO A O     1 
ATOM   15794 C  CB    . PRO A 1 3722 ? 151.203 109.254 173.177 1.00 58.87  ? 3722 PRO A CB    1 
ATOM   15795 C  CG    . PRO A 1 3722 ? 151.620 108.340 172.075 1.00 59.05  ? 3722 PRO A CG    1 
ATOM   15796 C  CD    . PRO A 1 3722 ? 153.109 108.475 171.976 1.00 53.78  ? 3722 PRO A CD    1 
ATOM   15797 N  N     . ASP A 1 3723 ? 152.219 106.942 175.119 1.00 67.07  ? 3723 ASP A N     1 
ATOM   15798 C  CA    . ASP A 1 3723 ? 151.987 105.984 176.195 1.00 67.02  ? 3723 ASP A CA    1 
ATOM   15799 C  C     . ASP A 1 3723 ? 153.015 106.140 177.310 1.00 65.07  ? 3723 ASP A C     1 
ATOM   15800 O  O     . ASP A 1 3723 ? 152.666 106.085 178.496 1.00 70.04  ? 3723 ASP A O     1 
ATOM   15801 C  CB    . ASP A 1 3723 ? 151.986 104.559 175.638 1.00 79.77  ? 3723 ASP A CB    1 
ATOM   15802 C  CG    . ASP A 1 3723 ? 153.298 104.184 174.968 1.00 77.39  ? 3723 ASP A CG    1 
ATOM   15803 O  OD1   . ASP A 1 3723 ? 154.199 105.043 174.877 1.00 69.66  ? 3723 ASP A OD1   1 
ATOM   15804 O  OD2   . ASP A 1 3723 ? 153.427 103.021 174.530 1.00 79.81  ? 3723 ASP A OD2   1 
ATOM   15805 N  N     . VAL A 1 3724 ? 154.284 106.346 176.950 1.00 62.09  ? 3724 VAL A N     1 
ATOM   15806 C  CA    . VAL A 1 3724 ? 155.325 106.527 177.958 1.00 57.68  ? 3724 VAL A CA    1 
ATOM   15807 C  C     . VAL A 1 3724 ? 155.081 107.802 178.756 1.00 62.55  ? 3724 VAL A C     1 
ATOM   15808 O  O     . VAL A 1 3724 ? 155.233 107.821 179.982 1.00 65.97  ? 3724 VAL A O     1 
ATOM   15809 C  CB    . VAL A 1 3724 ? 156.717 106.526 177.299 1.00 52.76  ? 3724 VAL A CB    1 
ATOM   15810 C  CG1   . VAL A 1 3724 ? 157.793 106.825 178.328 1.00 47.43  ? 3724 VAL A CG1   1 
ATOM   15811 C  CG2   . VAL A 1 3724 ? 156.981 105.189 176.625 1.00 52.55  ? 3724 VAL A CG2   1 
ATOM   15812 N  N     . ASP A 1 3725 ? 154.702 108.887 178.076 1.00 60.30  ? 3725 ASP A N     1 
ATOM   15813 C  CA    . ASP A 1 3725 ? 154.431 110.139 178.777 1.00 61.76  ? 3725 ASP A CA    1 
ATOM   15814 C  C     . ASP A 1 3725 ? 153.218 110.006 179.693 1.00 71.08  ? 3725 ASP A C     1 
ATOM   15815 O  O     . ASP A 1 3725 ? 153.223 110.524 180.816 1.00 78.04  ? 3725 ASP A O     1 
ATOM   15816 C  CB    . ASP A 1 3725 ? 154.234 111.270 177.765 1.00 60.10  ? 3725 ASP A CB    1 
ATOM   15817 C  CG    . ASP A 1 3725 ? 154.321 112.654 178.397 1.00 73.02  ? 3725 ASP A CG    1 
ATOM   15818 O  OD1   . ASP A 1 3725 ? 153.921 112.825 179.567 1.00 78.31  ? 3725 ASP A OD1   1 
ATOM   15819 O  OD2   . ASP A 1 3725 ? 154.808 113.581 177.718 1.00 69.87  ? 3725 ASP A OD2   1 
ATOM   15820 N  N     . GLU A 1 3726 ? 152.169 109.321 179.231 1.00 70.04  ? 3726 GLU A N     1 
ATOM   15821 C  CA    . GLU A 1 3726 ? 150.999 109.106 180.077 1.00 69.44  ? 3726 GLU A CA    1 
ATOM   15822 C  C     . GLU A 1 3726 ? 151.356 108.280 181.307 1.00 69.52  ? 3726 GLU A C     1 
ATOM   15823 O  O     . GLU A 1 3726 ? 150.921 108.591 182.425 1.00 73.33  ? 3726 GLU A O     1 
ATOM   15824 C  CB    . GLU A 1 3726 ? 149.891 108.431 179.268 1.00 68.32  ? 3726 GLU A CB    1 
ATOM   15825 C  CG    . GLU A 1 3726 ? 148.594 108.209 180.028 1.00 73.82  ? 3726 GLU A CG    1 
ATOM   15826 C  CD    . GLU A 1 3726 ? 148.373 106.753 180.390 1.00 85.18  ? 3726 GLU A CD    1 
ATOM   15827 O  OE1   . GLU A 1 3726 ? 149.000 105.880 179.755 1.00 82.44  ? 3726 GLU A OE1   1 
ATOM   15828 O  OE2   . GLU A 1 3726 ? 147.564 106.481 181.302 1.00 86.56  ? 3726 GLU A OE2   1 
ATOM   15829 N  N     . LYS A 1 3727 ? 152.161 107.231 181.123 1.00 64.30  ? 3727 LYS A N     1 
ATOM   15830 C  CA    . LYS A 1 3727 ? 152.599 106.426 182.258 1.00 67.82  ? 3727 LYS A CA    1 
ATOM   15831 C  C     . LYS A 1 3727 ? 153.450 107.247 183.219 1.00 68.63  ? 3727 LYS A C     1 
ATOM   15832 O  O     . LYS A 1 3727 ? 153.325 107.108 184.439 1.00 72.21  ? 3727 LYS A O     1 
ATOM   15833 C  CB    . LYS A 1 3727 ? 153.363 105.197 181.762 1.00 70.35  ? 3727 LYS A CB    1 
ATOM   15834 C  CG    . LYS A 1 3727 ? 154.357 104.623 182.758 1.00 70.68  ? 3727 LYS A CG    1 
ATOM   15835 C  CD    . LYS A 1 3727 ? 155.271 103.601 182.101 1.00 62.50  ? 3727 LYS A CD    1 
ATOM   15836 C  CE    . LYS A 1 3727 ? 154.482 102.449 181.506 1.00 67.64  ? 3727 LYS A CE    1 
ATOM   15837 N  NZ    . LYS A 1 3727 ? 155.316 101.224 181.367 1.00 66.65  ? 3727 LYS A NZ    1 
ATOM   15838 N  N     . ARG A 1 3728 ? 154.316 108.113 182.688 1.00 65.39  ? 3728 ARG A N     1 
ATOM   15839 C  CA    . ARG A 1 3728 ? 155.136 108.972 183.538 1.00 65.59  ? 3728 ARG A CA    1 
ATOM   15840 C  C     . ARG A 1 3728 ? 154.281 109.941 184.347 1.00 70.56  ? 3728 ARG A C     1 
ATOM   15841 O  O     . ARG A 1 3728 ? 154.540 110.164 185.536 1.00 74.86  ? 3728 ARG A O     1 
ATOM   15842 C  CB    . ARG A 1 3728 ? 156.149 109.732 182.681 1.00 71.67  ? 3728 ARG A CB    1 
ATOM   15843 C  CG    . ARG A 1 3728 ? 157.068 110.660 183.458 1.00 73.86  ? 3728 ARG A CG    1 
ATOM   15844 C  CD    . ARG A 1 3728 ? 157.746 111.652 182.525 1.00 73.27  ? 3728 ARG A CD    1 
ATOM   15845 N  NE    . ARG A 1 3728 ? 156.973 112.878 182.364 1.00 67.02  ? 3728 ARG A NE    1 
ATOM   15846 C  CZ    . ARG A 1 3728 ? 157.087 113.944 183.144 1.00 67.63  ? 3728 ARG A CZ    1 
ATOM   15847 N  NH1   . ARG A 1 3728 ? 157.944 113.975 184.151 1.00 64.50  ? 3728 ARG A NH1   1 
ATOM   15848 N  NH2   . ARG A 1 3728 ? 156.325 115.008 182.904 1.00 66.27  ? 3728 ARG A NH2   1 
ATOM   15849 N  N     . SER A 1 3729 ? 153.265 110.535 183.717 1.00 70.21  ? 3729 SER A N     1 
ATOM   15850 C  CA    . SER A 1 3729 ? 152.367 111.430 184.442 1.00 71.35  ? 3729 SER A CA    1 
ATOM   15851 C  C     . SER A 1 3729 ? 151.613 110.680 185.533 1.00 71.98  ? 3729 SER A C     1 
ATOM   15852 O  O     . SER A 1 3729 ? 151.447 111.188 186.652 1.00 71.19  ? 3729 SER A O     1 
ATOM   15853 C  CB    . SER A 1 3729 ? 151.392 112.095 183.472 1.00 71.68  ? 3729 SER A CB    1 
ATOM   15854 O  OG    . SER A 1 3729 ? 152.079 112.687 182.384 1.00 76.50  ? 3729 SER A OG    1 
ATOM   15855 N  N     . ASP A 1 3730 ? 151.151 109.464 185.226 1.00 70.50  ? 3730 ASP A N     1 
ATOM   15856 C  CA    . ASP A 1 3730 ? 150.498 108.648 186.243 1.00 70.03  ? 3730 ASP A CA    1 
ATOM   15857 C  C     . ASP A 1 3730 ? 151.449 108.335 187.391 1.00 66.97  ? 3730 ASP A C     1 
ATOM   15858 O  O     . ASP A 1 3730 ? 151.051 108.359 188.561 1.00 70.35  ? 3730 ASP A O     1 
ATOM   15859 C  CB    . ASP A 1 3730 ? 149.966 107.357 185.621 1.00 72.51  ? 3730 ASP A CB    1 
ATOM   15860 C  CG    . ASP A 1 3730 ? 148.784 107.596 184.706 1.00 82.71  ? 3730 ASP A CG    1 
ATOM   15861 O  OD1   . ASP A 1 3730 ? 148.405 106.661 183.971 1.00 88.29  ? 3730 ASP A OD1   1 
ATOM   15862 O  OD2   . ASP A 1 3730 ? 148.234 108.718 184.721 1.00 81.45  ? 3730 ASP A OD2   1 
ATOM   15863 N  N     . LEU A 1 3731 ? 152.711 108.034 187.075 1.00 64.58  ? 3731 LEU A N     1 
ATOM   15864 C  CA    . LEU A 1 3731 ? 153.692 107.763 188.119 1.00 63.96  ? 3731 LEU A CA    1 
ATOM   15865 C  C     . LEU A 1 3731 ? 153.911 108.983 189.001 1.00 69.07  ? 3731 LEU A C     1 
ATOM   15866 O  O     . LEU A 1 3731 ? 154.010 108.855 190.223 1.00 76.21  ? 3731 LEU A O     1 
ATOM   15867 C  CB    . LEU A 1 3731 ? 155.016 107.315 187.506 1.00 65.55  ? 3731 LEU A CB    1 
ATOM   15868 C  CG    . LEU A 1 3731 ? 155.047 105.968 186.790 1.00 69.06  ? 3731 LEU A CG    1 
ATOM   15869 C  CD1   . LEU A 1 3731 ? 156.404 105.769 186.144 1.00 71.06  ? 3731 LEU A CD1   1 
ATOM   15870 C  CD2   . LEU A 1 3731 ? 154.726 104.836 187.749 1.00 64.11  ? 3731 LEU A CD2   1 
ATOM   15871 N  N     . LEU A 1 3732 ? 153.999 110.171 188.400 1.00 68.53  ? 3732 LEU A N     1 
ATOM   15872 C  CA    . LEU A 1 3732 ? 154.164 111.384 189.197 1.00 70.22  ? 3732 LEU A CA    1 
ATOM   15873 C  C     . LEU A 1 3732 ? 152.967 111.603 190.115 1.00 69.46  ? 3732 LEU A C     1 
ATOM   15874 O  O     . LEU A 1 3732 ? 153.127 111.924 191.300 1.00 70.81  ? 3732 LEU A O     1 
ATOM   15875 C  CB    . LEU A 1 3732 ? 154.374 112.596 188.288 1.00 71.80  ? 3732 LEU A CB    1 
ATOM   15876 C  CG    . LEU A 1 3732 ? 155.566 112.573 187.332 1.00 70.14  ? 3732 LEU A CG    1 
ATOM   15877 C  CD1   . LEU A 1 3732 ? 155.805 113.958 186.753 1.00 71.33  ? 3732 LEU A CD1   1 
ATOM   15878 C  CD2   . LEU A 1 3732 ? 156.814 112.061 188.035 1.00 66.91  ? 3732 LEU A CD2   1 
ATOM   15879 N  N     . LYS A 1 3733 ? 151.755 111.421 189.584 1.00 68.24  ? 3733 LYS A N     1 
ATOM   15880 C  CA    . LYS A 1 3733 ? 150.556 111.609 190.397 1.00 66.47  ? 3733 LYS A CA    1 
ATOM   15881 C  C     . LYS A 1 3733 ? 150.517 110.621 191.559 1.00 66.04  ? 3733 LYS A C     1 
ATOM   15882 O  O     . LYS A 1 3733 ? 150.256 111.002 192.709 1.00 68.09  ? 3733 LYS A O     1 
ATOM   15883 C  CB    . LYS A 1 3733 ? 149.309 111.468 189.522 1.00 71.40  ? 3733 LYS A CB    1 
ATOM   15884 C  CG    . LYS A 1 3733 ? 147.999 111.696 190.257 1.00 71.91  ? 3733 LYS A CG    1 
ATOM   15885 C  CD    . LYS A 1 3733 ? 146.823 111.690 189.293 1.00 66.33  ? 3733 LYS A CD    1 
ATOM   15886 C  CE    . LYS A 1 3733 ? 146.535 110.289 188.778 1.00 71.58  ? 3733 LYS A CE    1 
ATOM   15887 N  NZ    . LYS A 1 3733 ? 146.010 109.395 189.847 1.00 69.36  ? 3733 LYS A NZ    1 
ATOM   15888 N  N     . LEU A 1 3734 ? 150.789 109.344 191.278 1.00 66.69  ? 3734 LEU A N     1 
ATOM   15889 C  CA    . LEU A 1 3734 ? 150.757 108.332 192.329 1.00 70.92  ? 3734 LEU A CA    1 
ATOM   15890 C  C     . LEU A 1 3734 ? 151.868 108.546 193.351 1.00 71.70  ? 3734 LEU A C     1 
ATOM   15891 O  O     . LEU A 1 3734 ? 151.658 108.327 194.546 1.00 77.14  ? 3734 LEU A O     1 
ATOM   15892 C  CB    . LEU A 1 3734 ? 150.837 106.927 191.727 1.00 72.67  ? 3734 LEU A CB    1 
ATOM   15893 C  CG    . LEU A 1 3734 ? 149.540 106.259 191.249 1.00 77.76  ? 3734 LEU A CG    1 
ATOM   15894 C  CD1   . LEU A 1 3734 ? 148.649 105.944 192.444 1.00 74.60  ? 3734 LEU A CD1   1 
ATOM   15895 C  CD2   . LEU A 1 3734 ? 148.773 107.088 190.229 1.00 72.72  ? 3734 LEU A CD2   1 
ATOM   15896 N  N     . GLN A 1 3735 ? 153.054 108.971 192.908 1.00 70.42  ? 3735 GLN A N     1 
ATOM   15897 C  CA    . GLN A 1 3735 ? 154.133 109.248 193.851 1.00 69.20  ? 3735 GLN A CA    1 
ATOM   15898 C  C     . GLN A 1 3735 ? 153.782 110.415 194.763 1.00 67.68  ? 3735 GLN A C     1 
ATOM   15899 O  O     . GLN A 1 3735 ? 154.031 110.363 195.973 1.00 68.09  ? 3735 GLN A O     1 
ATOM   15900 C  CB    . GLN A 1 3735 ? 155.435 109.529 193.101 1.00 70.04  ? 3735 GLN A CB    1 
ATOM   15901 C  CG    . GLN A 1 3735 ? 156.124 108.287 192.569 1.00 76.83  ? 3735 GLN A CG    1 
ATOM   15902 C  CD    . GLN A 1 3735 ? 157.634 108.397 192.598 1.00 82.94  ? 3735 GLN A CD    1 
ATOM   15903 O  OE1   . GLN A 1 3735 ? 158.282 108.496 191.555 1.00 83.06  ? 3735 GLN A OE1   1 
ATOM   15904 N  NE2   . GLN A 1 3735 ? 158.205 108.378 193.796 1.00 82.78  ? 3735 GLN A NE2   1 
ATOM   15905 N  N     . GLY A 1 3736 ? 153.205 111.480 194.201 1.00 69.02  ? 3736 GLY A N     1 
ATOM   15906 C  CA    . GLY A 1 3736 ? 152.771 112.588 195.035 1.00 65.41  ? 3736 GLY A CA    1 
ATOM   15907 C  C     . GLY A 1 3736 ? 151.718 112.171 196.043 1.00 69.50  ? 3736 GLY A C     1 
ATOM   15908 O  O     . GLY A 1 3736 ? 151.793 112.532 197.222 1.00 70.39  ? 3736 GLY A O     1 
ATOM   15909 N  N     . GLU A 1 3737 ? 150.735 111.382 195.598 1.00 70.44  ? 3737 GLU A N     1 
ATOM   15910 C  CA    . GLU A 1 3737 ? 149.704 110.904 196.513 1.00 66.64  ? 3737 GLU A CA    1 
ATOM   15911 C  C     . GLU A 1 3737 ? 150.297 110.020 197.604 1.00 67.00  ? 3737 GLU A C     1 
ATOM   15912 O  O     . GLU A 1 3737 ? 149.906 110.118 198.772 1.00 73.36  ? 3737 GLU A O     1 
ATOM   15913 C  CB    . GLU A 1 3737 ? 148.623 110.150 195.738 1.00 71.08  ? 3737 GLU A CB    1 
ATOM   15914 C  CG    . GLU A 1 3737 ? 147.660 111.052 194.982 1.00 74.96  ? 3737 GLU A CG    1 
ATOM   15915 C  CD    . GLU A 1 3737 ? 146.761 110.281 194.035 1.00 78.61  ? 3737 GLU A CD    1 
ATOM   15916 O  OE1   . GLU A 1 3737 ? 146.949 109.054 193.900 1.00 79.58  ? 3737 GLU A OE1   1 
ATOM   15917 O  OE2   . GLU A 1 3737 ? 145.865 110.902 193.426 1.00 75.74  ? 3737 GLU A OE2   1 
ATOM   15918 N  N     . PHE A 1 3738 ? 151.247 109.154 197.244 1.00 66.32  ? 3738 PHE A N     1 
ATOM   15919 C  CA    . PHE A 1 3738 ? 151.849 108.255 198.223 1.00 67.95  ? 3738 PHE A CA    1 
ATOM   15920 C  C     . PHE A 1 3738 ? 152.676 109.018 199.250 1.00 70.25  ? 3738 PHE A C     1 
ATOM   15921 O  O     . PHE A 1 3738 ? 152.636 108.700 200.443 1.00 73.52  ? 3738 PHE A O     1 
ATOM   15922 C  CB    . PHE A 1 3738 ? 152.707 107.209 197.513 1.00 69.08  ? 3738 PHE A CB    1 
ATOM   15923 C  CG    . PHE A 1 3738 ? 151.911 106.153 196.803 1.00 79.52  ? 3738 PHE A CG    1 
ATOM   15924 C  CD1   . PHE A 1 3738 ? 150.645 105.806 197.242 1.00 78.51  ? 3738 PHE A CD1   1 
ATOM   15925 C  CD2   . PHE A 1 3738 ? 152.432 105.503 195.696 1.00 83.41  ? 3738 PHE A CD2   1 
ATOM   15926 C  CE1   . PHE A 1 3738 ? 149.911 104.835 196.589 1.00 80.50  ? 3738 PHE A CE1   1 
ATOM   15927 C  CE2   . PHE A 1 3738 ? 151.703 104.531 195.039 1.00 80.76  ? 3738 PHE A CE2   1 
ATOM   15928 C  CZ    . PHE A 1 3738 ? 150.442 104.196 195.486 1.00 77.58  ? 3738 PHE A CZ    1 
ATOM   15929 N  N     . GLN A 1 3739 ? 153.441 110.021 198.810 1.00 70.96  ? 3739 GLN A N     1 
ATOM   15930 C  CA    . GLN A 1 3739 ? 154.210 110.818 199.761 1.00 65.89  ? 3739 GLN A CA    1 
ATOM   15931 C  C     . GLN A 1 3739 ? 153.294 111.630 200.668 1.00 67.69  ? 3739 GLN A C     1 
ATOM   15932 O  O     . GLN A 1 3739 ? 153.560 111.765 201.870 1.00 67.21  ? 3739 GLN A O     1 
ATOM   15933 C  CB    . GLN A 1 3739 ? 155.191 111.729 199.022 1.00 64.11  ? 3739 GLN A CB    1 
ATOM   15934 C  CG    . GLN A 1 3739 ? 156.186 110.990 198.135 1.00 69.58  ? 3739 GLN A CG    1 
ATOM   15935 C  CD    . GLN A 1 3739 ? 157.270 110.269 198.918 1.00 73.12  ? 3739 GLN A CD    1 
ATOM   15936 O  OE1   . GLN A 1 3739 ? 157.262 110.251 200.149 1.00 71.07  ? 3739 GLN A OE1   1 
ATOM   15937 N  NE2   . GLN A 1 3739 ? 158.209 109.664 198.201 1.00 74.66  ? 3739 GLN A NE2   1 
ATOM   15938 N  N     . LEU A 1 3740 ? 152.206 112.175 200.114 1.00 67.63  ? 3740 LEU A N     1 
ATOM   15939 C  CA    . LEU A 1 3740 ? 151.232 112.876 200.944 1.00 63.79  ? 3740 LEU A CA    1 
ATOM   15940 C  C     . LEU A 1 3740 ? 150.618 111.938 201.976 1.00 69.90  ? 3740 LEU A C     1 
ATOM   15941 O  O     . LEU A 1 3740 ? 150.435 112.315 203.140 1.00 73.74  ? 3740 LEU A O     1 
ATOM   15942 C  CB    . LEU A 1 3740 ? 150.150 113.495 200.060 1.00 68.69  ? 3740 LEU A CB    1 
ATOM   15943 C  CG    . LEU A 1 3740 ? 148.930 114.098 200.755 1.00 74.09  ? 3740 LEU A CG    1 
ATOM   15944 C  CD1   . LEU A 1 3740 ? 149.288 115.413 201.428 1.00 75.69  ? 3740 LEU A CD1   1 
ATOM   15945 C  CD2   . LEU A 1 3740 ? 147.792 114.292 199.764 1.00 67.20  ? 3740 LEU A CD2   1 
ATOM   15946 N  N     . ARG A 1 3741 ? 150.301 110.707 201.566 1.00 72.12  ? 3741 ARG A N     1 
ATOM   15947 C  CA    . ARG A 1 3741 ? 149.749 109.730 202.498 1.00 71.95  ? 3741 ARG A CA    1 
ATOM   15948 C  C     . ARG A 1 3741 ? 150.759 109.368 203.580 1.00 74.43  ? 3741 ARG A C     1 
ATOM   15949 O  O     . ARG A 1 3741 ? 150.392 109.211 204.748 1.00 80.50  ? 3741 ARG A O     1 
ATOM   15950 C  CB    . ARG A 1 3741 ? 149.296 108.481 201.743 1.00 69.04  ? 3741 ARG A CB    1 
ATOM   15951 C  CG    . ARG A 1 3741 ? 148.586 107.445 202.607 1.00 78.16  ? 3741 ARG A CG    1 
ATOM   15952 C  CD    . ARG A 1 3741 ? 147.614 108.099 203.579 1.00 90.98  ? 3741 ARG A CD    1 
ATOM   15953 N  NE    . ARG A 1 3741 ? 146.378 107.339 203.723 1.00 100.61 ? 3741 ARG A NE    1 
ATOM   15954 C  CZ    . ARG A 1 3741 ? 145.447 107.591 204.633 1.00 100.80 ? 3741 ARG A CZ    1 
ATOM   15955 N  NH1   . ARG A 1 3741 ? 145.580 108.580 205.501 1.00 97.85  ? 3741 ARG A NH1   1 
ATOM   15956 N  NH2   . ARG A 1 3741 ? 144.357 106.830 204.674 1.00 99.15  ? 3741 ARG A NH2   1 
ATOM   15957 N  N     . LEU A 1 3742 ? 152.034 109.219 203.211 1.00 69.03  ? 3742 LEU A N     1 
ATOM   15958 C  CA    . LEU A 1 3742 ? 153.060 108.930 204.210 1.00 64.56  ? 3742 LEU A CA    1 
ATOM   15959 C  C     . LEU A 1 3742 ? 153.177 110.060 205.223 1.00 72.06  ? 3742 LEU A C     1 
ATOM   15960 O  O     . LEU A 1 3742 ? 153.273 109.815 206.432 1.00 79.76  ? 3742 LEU A O     1 
ATOM   15961 C  CB    . LEU A 1 3742 ? 154.409 108.687 203.532 1.00 66.31  ? 3742 LEU A CB    1 
ATOM   15962 C  CG    . LEU A 1 3742 ? 154.639 107.318 202.897 1.00 66.72  ? 3742 LEU A CG    1 
ATOM   15963 C  CD1   . LEU A 1 3742 ? 155.949 107.294 202.125 1.00 65.61  ? 3742 LEU A CD1   1 
ATOM   15964 C  CD2   . LEU A 1 3742 ? 154.619 106.229 203.958 1.00 65.66  ? 3742 LEU A CD2   1 
ATOM   15965 N  N     . ARG A 1 3743 ? 153.168 111.307 204.747 1.00 71.44  ? 3743 ARG A N     1 
ATOM   15966 C  CA    . ARG A 1 3743 ? 153.230 112.444 205.660 1.00 71.39  ? 3743 ARG A CA    1 
ATOM   15967 C  C     . ARG A 1 3743 ? 152.020 112.466 206.588 1.00 75.65  ? 3743 ARG A C     1 
ATOM   15968 O  O     . ARG A 1 3743 ? 152.155 112.677 207.801 1.00 82.87  ? 3743 ARG A O     1 
ATOM   15969 C  CB    . ARG A 1 3743 ? 153.328 113.749 204.869 1.00 71.96  ? 3743 ARG A CB    1 
ATOM   15970 C  CG    . ARG A 1 3743 ? 154.733 114.091 204.405 1.00 68.30  ? 3743 ARG A CG    1 
ATOM   15971 C  CD    . ARG A 1 3743 ? 154.783 115.472 203.775 1.00 59.29  ? 3743 ARG A CD    1 
ATOM   15972 N  NE    . ARG A 1 3743 ? 154.536 115.426 202.339 1.00 64.46  ? 3743 ARG A NE    1 
ATOM   15973 C  CZ    . ARG A 1 3743 ? 153.391 115.771 201.766 1.00 63.94  ? 3743 ARG A CZ    1 
ATOM   15974 N  NH1   . ARG A 1 3743 ? 152.363 116.199 202.479 1.00 64.34  ? 3743 ARG A NH1   1 
ATOM   15975 N  NH2   . ARG A 1 3743 ? 153.275 115.686 200.443 1.00 59.47  ? 3743 ARG A NH2   1 
ATOM   15976 N  N     . GLN A 1 3744 ? 150.826 112.241 206.031 1.00 72.03  ? 3744 GLN A N     1 
ATOM   15977 C  CA    . GLN A 1 3744 ? 149.619 112.239 206.852 1.00 71.46  ? 3744 GLN A CA    1 
ATOM   15978 C  C     . GLN A 1 3744 ? 149.654 111.123 207.886 1.00 77.08  ? 3744 GLN A C     1 
ATOM   15979 O  O     . GLN A 1 3744 ? 149.246 111.324 209.034 1.00 80.23  ? 3744 GLN A O     1 
ATOM   15980 C  CB    . GLN A 1 3744 ? 148.374 112.114 205.975 1.00 73.82  ? 3744 GLN A CB    1 
ATOM   15981 C  CG    . GLN A 1 3744 ? 147.953 113.408 205.302 1.00 75.26  ? 3744 GLN A CG    1 
ATOM   15982 C  CD    . GLN A 1 3744 ? 147.028 113.178 204.125 1.00 78.19  ? 3744 GLN A CD    1 
ATOM   15983 O  OE1   . GLN A 1 3744 ? 146.915 114.019 203.235 1.00 78.21  ? 3744 GLN A OE1   1 
ATOM   15984 N  NE2   . GLN A 1 3744 ? 146.357 112.032 204.116 1.00 78.92  ? 3744 GLN A NE2   1 
ATOM   15985 N  N     . LEU A 1 3745 ? 150.129 109.937 207.499 1.00 80.71  ? 3745 LEU A N     1 
ATOM   15986 C  CA    . LEU A 1 3745 ? 150.229 108.835 208.452 1.00 83.54  ? 3745 LEU A CA    1 
ATOM   15987 C  C     . LEU A 1 3745 ? 151.226 109.150 209.557 1.00 83.17  ? 3745 LEU A C     1 
ATOM   15988 O  O     . LEU A 1 3745 ? 150.984 108.832 210.726 1.00 88.51  ? 3745 LEU A O     1 
ATOM   15989 C  CB    . LEU A 1 3745 ? 150.612 107.540 207.734 1.00 83.16  ? 3745 LEU A CB    1 
ATOM   15990 C  CG    . LEU A 1 3745 ? 149.575 106.947 206.779 1.00 87.77  ? 3745 LEU A CG    1 
ATOM   15991 C  CD1   . LEU A 1 3745 ? 150.151 105.750 206.040 1.00 91.26  ? 3745 LEU A CD1   1 
ATOM   15992 C  CD2   . LEU A 1 3745 ? 148.312 106.561 207.530 1.00 88.45  ? 3745 LEU A CD2   1 
ATOM   15993 N  N     . GLU A 1 3746 ? 152.353 109.776 209.211 1.00 81.75  ? 3746 GLU A N     1 
ATOM   15994 C  CA    . GLU A 1 3746 ? 153.330 110.146 210.232 1.00 86.87  ? 3746 GLU A CA    1 
ATOM   15995 C  C     . GLU A 1 3746 ? 152.735 111.135 211.228 1.00 89.56  ? 3746 GLU A C     1 
ATOM   15996 O  O     . GLU A 1 3746 ? 152.848 110.953 212.449 1.00 92.76  ? 3746 GLU A O     1 
ATOM   15997 C  CB    . GLU A 1 3746 ? 154.582 110.726 209.574 1.00 88.49  ? 3746 GLU A CB    1 
ATOM   15998 C  CG    . GLU A 1 3746 ? 155.762 110.899 210.518 1.00 92.62  ? 3746 GLU A CG    1 
ATOM   15999 C  CD    . GLU A 1 3746 ? 155.924 109.733 211.474 1.00 96.64  ? 3746 GLU A CD    1 
ATOM   16000 O  OE1   . GLU A 1 3746 ? 156.427 108.674 211.044 1.00 96.92  ? 3746 GLU A OE1   1 
ATOM   16001 O  OE2   . GLU A 1 3746 ? 155.552 109.878 212.658 1.00 98.56  ? 3746 GLU A OE2   1 
ATOM   16002 N  N     . LYS A 1 3747 ? 152.082 112.188 210.724 1.00 88.83  ? 3747 LYS A N     1 
ATOM   16003 C  CA    . LYS A 1 3747 ? 151.478 113.169 211.624 1.00 84.49  ? 3747 LYS A CA    1 
ATOM   16004 C  C     . LYS A 1 3747 ? 150.361 112.552 212.458 1.00 88.70  ? 3747 LYS A C     1 
ATOM   16005 O  O     . LYS A 1 3747 ? 150.235 112.853 213.650 1.00 90.29  ? 3747 LYS A O     1 
ATOM   16006 C  CB    . LYS A 1 3747 ? 150.959 114.376 210.841 1.00 77.76  ? 3747 LYS A CB    1 
ATOM   16007 C  CG    . LYS A 1 3747 ? 151.928 114.923 209.810 1.00 81.50  ? 3747 LYS A CG    1 
ATOM   16008 C  CD    . LYS A 1 3747 ? 151.364 116.152 209.117 1.00 84.77  ? 3747 LYS A CD    1 
ATOM   16009 C  CE    . LYS A 1 3747 ? 152.201 116.538 207.909 1.00 75.64  ? 3747 LYS A CE    1 
ATOM   16010 N  NZ    . LYS A 1 3747 ? 151.390 116.576 206.660 1.00 67.15  ? 3747 LYS A NZ    1 
ATOM   16011 N  N     . SER A 1 3748 ? 149.539 111.691 211.853 1.00 89.96  ? 3748 SER A N     1 
ATOM   16012 C  CA    . SER A 1 3748 ? 148.451 111.060 212.590 1.00 89.17  ? 3748 SER A CA    1 
ATOM   16013 C  C     . SER A 1 3748 ? 148.981 110.139 213.681 1.00 92.61  ? 3748 SER A C     1 
ATOM   16014 O  O     . SER A 1 3748 ? 148.440 110.113 214.790 1.00 97.51  ? 3748 SER A O     1 
ATOM   16015 C  CB    . SER A 1 3748 ? 147.544 110.289 211.632 1.00 84.51  ? 3748 SER A CB    1 
ATOM   16016 O  OG    . SER A 1 3748 ? 148.228 109.193 211.051 1.00 88.46  ? 3748 SER A OG    1 
ATOM   16017 N  N     . LEU A 1 3749 ? 150.034 109.374 213.386 1.00 92.21  ? 3749 LEU A N     1 
ATOM   16018 C  CA    . LEU A 1 3749 ? 150.629 108.511 214.400 1.00 96.35  ? 3749 LEU A CA    1 
ATOM   16019 C  C     . LEU A 1 3749 ? 151.223 109.332 215.535 1.00 99.72  ? 3749 LEU A C     1 
ATOM   16020 O  O     . LEU A 1 3749 ? 151.062 108.984 216.711 1.00 101.95 ? 3749 LEU A O     1 
ATOM   16021 C  CB    . LEU A 1 3749 ? 151.685 107.607 213.759 1.00 90.66  ? 3749 LEU A CB    1 
ATOM   16022 C  CG    . LEU A 1 3749 ? 152.327 106.487 214.585 1.00 94.61  ? 3749 LEU A CG    1 
ATOM   16023 C  CD1   . LEU A 1 3749 ? 152.783 105.369 213.664 1.00 99.40  ? 3749 LEU A CD1   1 
ATOM   16024 C  CD2   . LEU A 1 3749 ? 153.505 106.990 215.408 1.00 89.48  ? 3749 LEU A CD2   1 
ATOM   16025 N  N     . LEU A 1 3750 ? 151.912 110.428 215.203 1.00 100.47 ? 3750 LEU A N     1 
ATOM   16026 C  CA    . LEU A 1 3750 ? 152.470 111.280 216.248 1.00 98.99  ? 3750 LEU A CA    1 
ATOM   16027 C  C     . LEU A 1 3750 ? 151.368 111.871 217.121 1.00 98.78  ? 3750 LEU A C     1 
ATOM   16028 O  O     . LEU A 1 3750 ? 151.479 111.880 218.352 1.00 98.74  ? 3750 LEU A O     1 
ATOM   16029 C  CB    . LEU A 1 3750 ? 153.319 112.387 215.625 1.00 100.41 ? 3750 LEU A CB    1 
ATOM   16030 C  CG    . LEU A 1 3750 ? 154.039 113.315 216.603 1.00 99.40  ? 3750 LEU A CG    1 
ATOM   16031 C  CD1   . LEU A 1 3750 ? 155.042 112.532 217.435 1.00 93.13  ? 3750 LEU A CD1   1 
ATOM   16032 C  CD2   . LEU A 1 3750 ? 154.724 114.449 215.859 1.00 98.46  ? 3750 LEU A CD2   1 
ATOM   16033 N  N     . GLN A 1 3751 ? 150.285 112.347 216.502 1.00 99.31  ? 3751 GLN A N     1 
ATOM   16034 C  CA    . GLN A 1 3751 ? 149.182 112.921 217.267 1.00 98.01  ? 3751 GLN A CA    1 
ATOM   16035 C  C     . GLN A 1 3751 ? 148.494 111.870 218.131 1.00 103.13 ? 3751 GLN A C     1 
ATOM   16036 O  O     . GLN A 1 3751 ? 148.104 112.153 219.270 1.00 106.78 ? 3751 GLN A O     1 
ATOM   16037 C  CB    . GLN A 1 3751 ? 148.179 113.582 216.322 1.00 99.91  ? 3751 GLN A CB    1 
ATOM   16038 C  CG    . GLN A 1 3751 ? 147.164 114.474 217.016 1.00 106.42 ? 3751 GLN A CG    1 
ATOM   16039 C  CD    . GLN A 1 3751 ? 145.810 114.451 216.337 1.00 108.11 ? 3751 GLN A CD    1 
ATOM   16040 O  OE1   . GLN A 1 3751 ? 145.695 114.084 215.168 1.00 102.50 ? 3751 GLN A OE1   1 
ATOM   16041 N  NE2   . GLN A 1 3751 ? 144.774 114.846 217.069 1.00 106.55 ? 3751 GLN A NE2   1 
ATOM   16042 N  N     . ALA A 1 3752 ? 148.323 110.655 217.603 1.00 103.65 ? 3752 ALA A N     1 
ATOM   16043 C  CA    . ALA A 1 3752 ? 147.712 109.583 218.381 1.00 106.16 ? 3752 ALA A CA    1 
ATOM   16044 C  C     . ALA A 1 3752 ? 148.575 109.210 219.578 1.00 108.52 ? 3752 ALA A C     1 
ATOM   16045 O  O     . ALA A 1 3752 ? 148.055 108.971 220.674 1.00 112.87 ? 3752 ALA A O     1 
ATOM   16046 C  CB    . ALA A 1 3752 ? 147.464 108.364 217.494 1.00 102.07 ? 3752 ALA A CB    1 
ATOM   16047 N  N     . LEU A 1 3753 ? 149.895 109.151 219.388 1.00 105.29 ? 3753 LEU A N     1 
ATOM   16048 C  CA    . LEU A 1 3753 ? 150.790 108.917 220.516 1.00 102.87 ? 3753 LEU A CA    1 
ATOM   16049 C  C     . LEU A 1 3753 ? 150.697 110.050 221.529 1.00 106.77 ? 3753 LEU A C     1 
ATOM   16050 O  O     . LEU A 1 3753 ? 150.751 109.819 222.742 1.00 110.96 ? 3753 LEU A O     1 
ATOM   16051 C  CB    . LEU A 1 3753 ? 152.228 108.753 220.023 1.00 101.30 ? 3753 LEU A CB    1 
ATOM   16052 C  CG    . LEU A 1 3753 ? 152.684 107.334 219.679 1.00 106.64 ? 3753 LEU A CG    1 
ATOM   16053 C  CD1   . LEU A 1 3753 ? 154.199 107.275 219.559 1.00 104.60 ? 3753 LEU A CD1   1 
ATOM   16054 C  CD2   . LEU A 1 3753 ? 152.186 106.341 220.716 1.00 111.50 ? 3753 LEU A CD2   1 
ATOM   16055 N  N     . ASN A 1 3754 ? 150.562 111.286 221.044 1.00 108.59 ? 3754 ASN A N     1 
ATOM   16056 C  CA    . ASN A 1 3754 ? 150.456 112.437 221.935 1.00 108.05 ? 3754 ASN A CA    1 
ATOM   16057 C  C     . ASN A 1 3754 ? 149.190 112.371 222.780 1.00 110.62 ? 3754 ASN A C     1 
ATOM   16058 O  O     . ASN A 1 3754 ? 149.221 112.662 223.982 1.00 112.99 ? 3754 ASN A O     1 
ATOM   16059 C  CB    . ASN A 1 3754 ? 150.473 113.724 221.114 1.00 106.80 ? 3754 ASN A CB    1 
ATOM   16060 C  CG    . ASN A 1 3754 ? 151.802 113.962 220.435 1.00 101.34 ? 3754 ASN A CG    1 
ATOM   16061 O  OD1   . ASN A 1 3754 ? 152.859 113.750 221.021 1.00 92.81  ? 3754 ASN A OD1   1 
ATOM   16062 N  ND2   . ASN A 1 3754 ? 151.753 114.381 219.178 1.00 104.38 ? 3754 ASN A ND2   1 
ATOM   16063 N  N     . GLU A 1 3755 ? 148.067 111.989 222.167 1.00 109.86 ? 3755 GLU A N     1 
ATOM   16064 C  CA    . GLU A 1 3755 ? 146.775 112.027 222.844 1.00 113.57 ? 3755 GLU A CA    1 
ATOM   16065 C  C     . GLU A 1 3755 ? 146.647 110.957 223.923 1.00 119.50 ? 3755 GLU A C     1 
ATOM   16066 O  O     . GLU A 1 3755 ? 145.820 111.107 224.828 1.00 125.37 ? 3755 GLU A O     1 
ATOM   16067 C  CB    . GLU A 1 3755 ? 145.657 111.894 221.800 1.00 110.73 ? 3755 GLU A CB    1 
ATOM   16068 C  CG    . GLU A 1 3755 ? 144.227 111.856 222.337 1.00 117.41 ? 3755 GLU A CG    1 
ATOM   16069 C  CD    . GLU A 1 3755 ? 143.765 110.456 222.704 1.00 120.64 ? 3755 GLU A CD    1 
ATOM   16070 O  OE1   . GLU A 1 3755 ? 144.460 109.483 222.342 1.00 121.75 ? 3755 GLU A OE1   1 
ATOM   16071 O  OE2   . GLU A 1 3755 ? 142.708 110.331 223.358 1.00 116.34 ? 3755 GLU A OE2   1 
ATOM   16072 N  N     . VAL A 1 3756 ? 147.461 109.898 223.861 1.00 117.58 ? 3756 VAL A N     1 
ATOM   16073 C  CA    . VAL A 1 3756 ? 147.312 108.780 224.785 1.00 120.89 ? 3756 VAL A CA    1 
ATOM   16074 C  C     . VAL A 1 3756 ? 147.465 109.269 226.220 1.00 129.00 ? 3756 VAL A C     1 
ATOM   16075 O  O     . VAL A 1 3756 ? 148.294 110.138 226.520 1.00 127.18 ? 3756 VAL A O     1 
ATOM   16076 C  CB    . VAL A 1 3756 ? 148.334 107.679 224.453 1.00 120.43 ? 3756 VAL A CB    1 
ATOM   16077 C  CG1   . VAL A 1 3756 ? 148.465 106.685 225.600 1.00 123.19 ? 3756 VAL A CG1   1 
ATOM   16078 C  CG2   . VAL A 1 3756 ? 147.949 106.973 223.170 1.00 124.72 ? 3756 VAL A CG2   1 
ATOM   16079 N  N     . LYS A 1 3757 ? 146.658 108.704 227.121 1.00 133.36 ? 3757 LYS A N     1 
ATOM   16080 C  CA    . LYS A 1 3757 ? 146.583 109.143 228.508 1.00 129.58 ? 3757 LYS A CA    1 
ATOM   16081 C  C     . LYS A 1 3757 ? 147.678 108.546 229.387 1.00 128.85 ? 3757 LYS A C     1 
ATOM   16082 O  O     . LYS A 1 3757 ? 147.517 108.509 230.613 1.00 125.71 ? 3757 LYS A O     1 
ATOM   16083 C  CB    . LYS A 1 3757 ? 145.208 108.804 229.089 1.00 124.37 ? 3757 LYS A CB    1 
ATOM   16084 C  CG    . LYS A 1 3757 ? 144.042 109.124 228.164 1.00 118.02 ? 3757 LYS A CG    1 
ATOM   16085 C  CD    . LYS A 1 3757 ? 144.037 110.586 227.747 1.00 118.68 ? 3757 LYS A CD    1 
ATOM   16086 C  CE    . LYS A 1 3757 ? 143.794 111.501 228.935 1.00 126.79 ? 3757 LYS A CE    1 
ATOM   16087 N  NZ    . LYS A 1 3757 ? 143.820 112.935 228.538 1.00 133.28 ? 3757 LYS A NZ    1 
ATOM   16088 N  N     . GLY A 1 3758 ? 148.779 108.080 228.800 1.00 132.24 ? 3758 GLY A N     1 
ATOM   16089 C  CA    . GLY A 1 3758 ? 149.901 107.578 229.562 1.00 134.12 ? 3758 GLY A CA    1 
ATOM   16090 C  C     . GLY A 1 3758 ? 149.983 106.074 229.703 1.00 137.43 ? 3758 GLY A C     1 
ATOM   16091 O  O     . GLY A 1 3758 ? 150.950 105.578 230.295 1.00 135.79 ? 3758 GLY A O     1 
ATOM   16092 N  N     . ARG A 1 3759 ? 149.006 105.329 229.181 1.00 138.92 ? 3759 ARG A N     1 
ATOM   16093 C  CA    . ARG A 1 3759 ? 149.001 103.865 229.266 1.00 139.45 ? 3759 ARG A CA    1 
ATOM   16094 C  C     . ARG A 1 3759 ? 148.579 103.333 227.897 1.00 139.50 ? 3759 ARG A C     1 
ATOM   16095 O  O     . ARG A 1 3759 ? 147.388 103.152 227.628 1.00 141.55 ? 3759 ARG A O     1 
ATOM   16096 C  CB    . ARG A 1 3759 ? 148.078 103.381 230.377 1.00 141.13 ? 3759 ARG A CB    1 
ATOM   16097 C  CG    . ARG A 1 3759 ? 148.592 103.683 231.778 1.00 140.65 ? 3759 ARG A CG    1 
ATOM   16098 C  CD    . ARG A 1 3759 ? 149.763 102.790 232.160 1.00 141.33 ? 3759 ARG A CD    1 
ATOM   16099 N  NE    . ARG A 1 3759 ? 149.501 101.386 231.865 1.00 148.09 ? 3759 ARG A NE    1 
ATOM   16100 C  CZ    . ARG A 1 3759 ? 149.200 100.476 232.781 1.00 144.65 ? 3759 ARG A CZ    1 
ATOM   16101 N  NH1   . ARG A 1 3759 ? 149.129 100.785 234.066 1.00 138.73 ? 3759 ARG A NH1   1 
ATOM   16102 N  NH2   . ARG A 1 3759 ? 148.962 99.224  232.400 1.00 141.14 ? 3759 ARG A NH2   1 
ATOM   16103 N  N     . ILE A 1 3760 ? 149.567 103.088 227.033 1.00 137.58 ? 3760 ILE A N     1 
ATOM   16104 C  CA    . ILE A 1 3760 ? 149.277 102.625 225.680 1.00 139.30 ? 3760 ILE A CA    1 
ATOM   16105 C  C     . ILE A 1 3760 ? 148.710 101.211 225.704 1.00 139.78 ? 3760 ILE A C     1 
ATOM   16106 O  O     . ILE A 1 3760 ? 147.718 100.914 225.027 1.00 140.42 ? 3760 ILE A O     1 
ATOM   16107 C  CB    . ILE A 1 3760 ? 150.540 102.714 224.804 1.00 131.49 ? 3760 ILE A CB    1 
ATOM   16108 C  CG1   . ILE A 1 3760 ? 151.036 104.157 224.729 1.00 129.85 ? 3760 ILE A CG1   1 
ATOM   16109 C  CG2   . ILE A 1 3760 ? 150.262 102.183 223.409 1.00 128.58 ? 3760 ILE A CG2   1 
ATOM   16110 C  CD1   . ILE A 1 3760 ? 152.239 104.343 223.833 1.00 120.97 ? 3760 ILE A CD1   1 
ATOM   16111 N  N     . LEU A 1 3761 ? 149.326 100.317 226.481 1.00 135.62 ? 3761 LEU A N     1 
ATOM   16112 C  CA    . LEU A 1 3761 ? 148.889 98.926  226.516 1.00 135.04 ? 3761 LEU A CA    1 
ATOM   16113 C  C     . LEU A 1 3761 ? 147.509 98.763  227.140 1.00 138.48 ? 3761 LEU A C     1 
ATOM   16114 O  O     . LEU A 1 3761 ? 146.837 97.762  226.869 1.00 137.70 ? 3761 LEU A O     1 
ATOM   16115 C  CB    . LEU A 1 3761 ? 149.904 98.068  227.276 1.00 136.08 ? 3761 LEU A CB    1 
ATOM   16116 C  CG    . LEU A 1 3761 ? 151.187 97.657  226.544 1.00 132.09 ? 3761 LEU A CG    1 
ATOM   16117 C  CD1   . LEU A 1 3761 ? 152.140 98.830  226.369 1.00 126.91 ? 3761 LEU A CD1   1 
ATOM   16118 C  CD2   . LEU A 1 3761 ? 151.875 96.517  227.273 1.00 126.42 ? 3761 LEU A CD2   1 
ATOM   16119 N  N     . ASP A 1 3762 ? 147.075 99.714  227.971 1.00 141.61 ? 3762 ASP A N     1 
ATOM   16120 C  CA    . ASP A 1 3762 ? 145.756 99.611  228.585 1.00 142.28 ? 3762 ASP A CA    1 
ATOM   16121 C  C     . ASP A 1 3762 ? 144.646 99.780  227.554 1.00 139.68 ? 3762 ASP A C     1 
ATOM   16122 O  O     . ASP A 1 3762 ? 143.666 99.025  227.559 1.00 135.43 ? 3762 ASP A O     1 
ATOM   16123 C  CB    . ASP A 1 3762 ? 145.612 100.648 229.698 1.00 140.08 ? 3762 ASP A CB    1 
ATOM   16124 C  CG    . ASP A 1 3762 ? 146.335 100.245 230.967 1.00 142.78 ? 3762 ASP A CG    1 
ATOM   16125 O  OD1   . ASP A 1 3762 ? 146.930 99.147  230.991 1.00 138.56 ? 3762 ASP A OD1   1 
ATOM   16126 O  OD2   . ASP A 1 3762 ? 146.307 101.026 231.941 1.00 147.61 ? 3762 ASP A OD2   1 
ATOM   16127 N  N     . ASP A 1 3763 ? 144.782 100.759 226.663 1.00 137.85 ? 3763 ASP A N     1 
ATOM   16128 C  CA    . ASP A 1 3763 ? 143.740 101.084 225.697 1.00 134.23 ? 3763 ASP A CA    1 
ATOM   16129 C  C     . ASP A 1 3763 ? 143.915 100.230 224.447 1.00 135.52 ? 3763 ASP A C     1 
ATOM   16130 O  O     . ASP A 1 3763 ? 144.953 100.301 223.781 1.00 134.90 ? 3763 ASP A O     1 
ATOM   16131 C  CB    . ASP A 1 3763 ? 143.781 102.570 225.346 1.00 131.61 ? 3763 ASP A CB    1 
ATOM   16132 C  CG    . ASP A 1 3763 ? 142.439 103.093 224.875 1.00 131.64 ? 3763 ASP A CG    1 
ATOM   16133 O  OD1   . ASP A 1 3763 ? 141.512 103.189 225.706 1.00 131.14 ? 3763 ASP A OD1   1 
ATOM   16134 O  OD2   . ASP A 1 3763 ? 142.312 103.410 223.674 1.00 131.31 ? 3763 ASP A OD2   1 
ATOM   16135 N  N     . ASP A 1 3764 ? 142.897 99.427  224.130 1.00 133.66 ? 3764 ASP A N     1 
ATOM   16136 C  CA    . ASP A 1 3764 ? 142.943 98.596  222.932 1.00 130.09 ? 3764 ASP A CA    1 
ATOM   16137 C  C     . ASP A 1 3764 ? 142.692 99.405  221.665 1.00 125.76 ? 3764 ASP A C     1 
ATOM   16138 O  O     . ASP A 1 3764 ? 143.214 99.055  220.599 1.00 126.19 ? 3764 ASP A O     1 
ATOM   16139 C  CB    . ASP A 1 3764 ? 141.924 97.462  223.040 1.00 133.00 ? 3764 ASP A CB    1 
ATOM   16140 C  CG    . ASP A 1 3764 ? 142.462 96.267  223.801 1.00 132.21 ? 3764 ASP A CG    1 
ATOM   16141 O  OD1   . ASP A 1 3764 ? 143.623 95.878  223.556 1.00 129.45 ? 3764 ASP A OD1   1 
ATOM   16142 O  OD2   . ASP A 1 3764 ? 141.724 95.717  224.646 1.00 128.05 ? 3764 ASP A OD2   1 
ATOM   16143 N  N     . THR A 1 3765 ? 141.897 100.474 221.758 1.00 127.69 ? 3765 THR A N     1 
ATOM   16144 C  CA    . THR A 1 3765 ? 141.647 101.316 220.592 1.00 131.77 ? 3765 THR A CA    1 
ATOM   16145 C  C     . THR A 1 3765 ? 142.936 101.954 220.091 1.00 127.58 ? 3765 THR A C     1 
ATOM   16146 O  O     . THR A 1 3765 ? 143.189 101.996 218.880 1.00 127.39 ? 3765 THR A O     1 
ATOM   16147 C  CB    . THR A 1 3765 ? 140.615 102.392 220.933 1.00 132.01 ? 3765 THR A CB    1 
ATOM   16148 O  OG1   . THR A 1 3765 ? 139.443 101.776 221.484 1.00 128.08 ? 3765 THR A OG1   1 
ATOM   16149 C  CG2   . THR A 1 3765 ? 140.230 103.176 219.687 1.00 131.59 ? 3765 THR A CG2   1 
ATOM   16150 N  N     . ILE A 1 3766 ? 143.768 102.447 221.012 1.00 126.19 ? 3766 ILE A N     1 
ATOM   16151 C  CA    . ILE A 1 3766 ? 145.061 103.006 220.632 1.00 127.58 ? 3766 ILE A CA    1 
ATOM   16152 C  C     . ILE A 1 3766 ? 145.924 101.944 219.966 1.00 126.43 ? 3766 ILE A C     1 
ATOM   16153 O  O     . ILE A 1 3766 ? 146.599 102.206 218.961 1.00 124.55 ? 3766 ILE A O     1 
ATOM   16154 C  CB    . ILE A 1 3766 ? 145.761 103.613 221.862 1.00 123.49 ? 3766 ILE A CB    1 
ATOM   16155 C  CG1   . ILE A 1 3766 ? 145.031 104.877 222.322 1.00 121.74 ? 3766 ILE A CG1   1 
ATOM   16156 C  CG2   . ILE A 1 3766 ? 147.224 103.894 221.560 1.00 122.09 ? 3766 ILE A CG2   1 
ATOM   16157 C  CD1   . ILE A 1 3766 ? 144.927 105.943 221.254 1.00 118.81 ? 3766 ILE A CD1   1 
ATOM   16158 N  N     . ILE A 1 3767 ? 145.919 100.730 220.517 1.00 125.01 ? 3767 ILE A N     1 
ATOM   16159 C  CA    . ILE A 1 3767 ? 146.742 99.656  219.970 1.00 122.22 ? 3767 ILE A CA    1 
ATOM   16160 C  C     . ILE A 1 3767 ? 146.323 99.358  218.536 1.00 119.80 ? 3767 ILE A C     1 
ATOM   16161 O  O     . ILE A 1 3767 ? 147.160 99.239  217.629 1.00 117.13 ? 3767 ILE A O     1 
ATOM   16162 C  CB    . ILE A 1 3767 ? 146.632 98.403  220.857 1.00 127.30 ? 3767 ILE A CB    1 
ATOM   16163 C  CG1   . ILE A 1 3767 ? 147.244 98.666  222.235 1.00 128.17 ? 3767 ILE A CG1   1 
ATOM   16164 C  CG2   . ILE A 1 3767 ? 147.308 97.215  220.189 1.00 123.45 ? 3767 ILE A CG2   1 
ATOM   16165 C  CD1   . ILE A 1 3767 ? 148.654 99.169  222.202 1.00 124.21 ? 3767 ILE A CD1   1 
ATOM   16166 N  N     . THR A 1 3768 ? 145.011 99.250  218.310 1.00 124.68 ? 3768 THR A N     1 
ATOM   16167 C  CA    . THR A 1 3768 ? 144.502 98.968  216.972 1.00 122.03 ? 3768 THR A CA    1 
ATOM   16168 C  C     . THR A 1 3768 ? 144.816 100.104 216.006 1.00 117.81 ? 3768 THR A C     1 
ATOM   16169 O  O     . THR A 1 3768 ? 145.178 99.855  214.850 1.00 117.49 ? 3768 THR A O     1 
ATOM   16170 C  CB    . THR A 1 3768 ? 142.997 98.713  217.025 1.00 124.39 ? 3768 THR A CB    1 
ATOM   16171 O  OG1   . THR A 1 3768 ? 142.354 99.780  217.734 1.00 125.22 ? 3768 THR A OG1   1 
ATOM   16172 C  CG2   . THR A 1 3768 ? 142.707 97.396  217.729 1.00 122.25 ? 3768 THR A CG2   1 
ATOM   16173 N  N     . THR A 1 3769 ? 144.675 101.355 216.452 1.00 117.10 ? 3769 THR A N     1 
ATOM   16174 C  CA    . THR A 1 3769 ? 144.972 102.483 215.572 1.00 114.08 ? 3769 THR A CA    1 
ATOM   16175 C  C     . THR A 1 3769 ? 146.442 102.494 215.172 1.00 116.83 ? 3769 THR A C     1 
ATOM   16176 O  O     . THR A 1 3769 ? 146.776 102.718 214.003 1.00 120.59 ? 3769 THR A O     1 
ATOM   16177 C  CB    . THR A 1 3769 ? 144.589 103.802 216.246 1.00 107.58 ? 3769 THR A CB    1 
ATOM   16178 O  OG1   . THR A 1 3769 ? 145.154 103.854 217.560 1.00 113.24 ? 3769 THR A OG1   1 
ATOM   16179 C  CG2   . THR A 1 3769 ? 143.076 103.938 216.335 1.00 108.92 ? 3769 THR A CG2   1 
ATOM   16180 N  N     . LEU A 1 3770 ? 147.338 102.250 216.133 1.00 113.16 ? 3770 LEU A N     1 
ATOM   16181 C  CA    . LEU A 1 3770 ? 148.763 102.204 215.811 1.00 110.43 ? 3770 LEU A CA    1 
ATOM   16182 C  C     . LEU A 1 3770 ? 149.080 101.062 214.853 1.00 111.32 ? 3770 LEU A C     1 
ATOM   16183 O  O     . LEU A 1 3770 ? 149.869 101.233 213.915 1.00 114.03 ? 3770 LEU A O     1 
ATOM   16184 C  CB    . LEU A 1 3770 ? 149.599 102.092 217.088 1.00 110.47 ? 3770 LEU A CB    1 
ATOM   16185 C  CG    . LEU A 1 3770 ? 149.979 103.376 217.841 1.00 110.54 ? 3770 LEU A CG    1 
ATOM   16186 C  CD1   . LEU A 1 3770 ? 148.788 104.274 218.142 1.00 115.34 ? 3770 LEU A CD1   1 
ATOM   16187 C  CD2   . LEU A 1 3770 ? 150.728 103.034 219.125 1.00 108.91 ? 3770 LEU A CD2   1 
ATOM   16188 N  N     . GLU A 1 3771 ? 148.475 99.888  215.068 1.00 108.75 ? 3771 GLU A N     1 
ATOM   16189 C  CA    . GLU A 1 3771 ? 148.687 98.777  214.143 1.00 104.77 ? 3771 GLU A CA    1 
ATOM   16190 C  C     . GLU A 1 3771 ? 148.217 99.127  212.736 1.00 104.45 ? 3771 GLU A C     1 
ATOM   16191 O  O     . GLU A 1 3771 ? 148.918 98.852  211.752 1.00 107.49 ? 3771 GLU A O     1 
ATOM   16192 C  CB    . GLU A 1 3771 ? 147.971 97.521  214.648 1.00 110.31 ? 3771 GLU A CB    1 
ATOM   16193 C  CG    . GLU A 1 3771 ? 148.682 96.708  215.746 1.00 119.45 ? 3771 GLU A CG    1 
ATOM   16194 C  CD    . GLU A 1 3771 ? 150.095 96.226  215.394 1.00 120.84 ? 3771 GLU A CD    1 
ATOM   16195 O  OE1   . GLU A 1 3771 ? 150.674 96.641  214.367 1.00 113.42 ? 3771 GLU A OE1   1 
ATOM   16196 O  OE2   . GLU A 1 3771 ? 150.632 95.402  216.164 1.00 122.02 ? 3771 GLU A OE2   1 
ATOM   16197 N  N     . ASN A 1 3772 ? 147.034 99.735  212.620 1.00 105.91 ? 3772 ASN A N     1 
ATOM   16198 C  CA    . ASN A 1 3772 ? 146.509 100.101 211.308 1.00 106.48 ? 3772 ASN A CA    1 
ATOM   16199 C  C     . ASN A 1 3772 ? 147.413 101.115 210.619 1.00 102.60 ? 3772 ASN A C     1 
ATOM   16200 O  O     . ASN A 1 3772 ? 147.702 100.995 209.422 1.00 103.60 ? 3772 ASN A O     1 
ATOM   16201 C  CB    . ASN A 1 3772 ? 145.088 100.650 211.444 1.00 103.01 ? 3772 ASN A CB    1 
ATOM   16202 C  CG    . ASN A 1 3772 ? 144.118 99.628  212.005 1.00 108.98 ? 3772 ASN A CG    1 
ATOM   16203 O  OD1   . ASN A 1 3772 ? 144.518 98.550  212.443 1.00 115.30 ? 3772 ASN A OD1   1 
ATOM   16204 N  ND2   . ASN A 1 3772 ? 142.834 99.965  211.994 1.00 104.94 ? 3772 ASN A ND2   1 
ATOM   16205 N  N     . LEU A 1 3773 ? 147.870 102.126 211.363 1.00 99.95  ? 3773 LEU A N     1 
ATOM   16206 C  CA    . LEU A 1 3773 ? 148.745 103.134 210.773 1.00 100.50 ? 3773 LEU A CA    1 
ATOM   16207 C  C     . LEU A 1 3773 ? 150.061 102.523 210.309 1.00 103.30 ? 3773 LEU A C     1 
ATOM   16208 O  O     . LEU A 1 3773 ? 150.545 102.837 209.216 1.00 107.72 ? 3773 LEU A O     1 
ATOM   16209 C  CB    . LEU A 1 3773 ? 148.994 104.268 211.768 1.00 95.33  ? 3773 LEU A CB    1 
ATOM   16210 C  CG    . LEU A 1 3773 ? 147.763 105.072 212.191 1.00 94.55  ? 3773 LEU A CG    1 
ATOM   16211 C  CD1   . LEU A 1 3773 ? 148.134 106.128 213.218 1.00 87.80  ? 3773 LEU A CD1   1 
ATOM   16212 C  CD2   . LEU A 1 3773 ? 147.087 105.707 210.984 1.00 91.98  ? 3773 LEU A CD2   1 
ATOM   16213 N  N     . LYS A 1 3774 ? 150.652 101.639 211.120 1.00 99.95  ? 3774 LYS A N     1 
ATOM   16214 C  CA    . LYS A 1 3774 ? 151.915 101.019 210.729 1.00 98.08  ? 3774 LYS A CA    1 
ATOM   16215 C  C     . LYS A 1 3774 ? 151.743 100.138 209.496 1.00 97.62  ? 3774 LYS A C     1 
ATOM   16216 O  O     . LYS A 1 3774 ? 152.582 100.159 208.585 1.00 98.56  ? 3774 LYS A O     1 
ATOM   16217 C  CB    . LYS A 1 3774 ? 152.486 100.212 211.894 1.00 99.01  ? 3774 LYS A CB    1 
ATOM   16218 C  CG    . LYS A 1 3774 ? 153.466 100.987 212.762 1.00 96.74  ? 3774 LYS A CG    1 
ATOM   16219 C  CD    . LYS A 1 3774 ? 154.737 101.334 212.002 1.00 97.83  ? 3774 LYS A CD    1 
ATOM   16220 C  CE    . LYS A 1 3774 ? 155.397 100.095 211.422 1.00 98.82  ? 3774 LYS A CE    1 
ATOM   16221 N  NZ    . LYS A 1 3774 ? 156.758 100.390 210.895 1.00 103.46 ? 3774 LYS A NZ    1 
ATOM   16222 N  N     . ARG A 1 3775 ? 150.661 99.355  209.447 1.00 95.46  ? 3775 ARG A N     1 
ATOM   16223 C  CA    . ARG A 1 3775 ? 150.417 98.501  208.287 1.00 96.65  ? 3775 ARG A CA    1 
ATOM   16224 C  C     . ARG A 1 3775 ? 150.193 99.329  207.026 1.00 99.47  ? 3775 ARG A C     1 
ATOM   16225 O  O     . ARG A 1 3775 ? 150.713 98.995  205.950 1.00 98.11  ? 3775 ARG A O     1 
ATOM   16226 C  CB    . ARG A 1 3775 ? 149.218 97.593  208.558 1.00 98.70  ? 3775 ARG A CB    1 
ATOM   16227 C  CG    . ARG A 1 3775 ? 148.940 96.572  207.471 1.00 101.83 ? 3775 ARG A CG    1 
ATOM   16228 C  CD    . ARG A 1 3775 ? 147.783 95.669  207.863 1.00 103.73 ? 3775 ARG A CD    1 
ATOM   16229 N  NE    . ARG A 1 3775 ? 146.534 96.410  207.990 1.00 107.88 ? 3775 ARG A NE    1 
ATOM   16230 C  CZ    . ARG A 1 3775 ? 145.882 96.591  209.131 1.00 109.18 ? 3775 ARG A CZ    1 
ATOM   16231 N  NH1   . ARG A 1 3775 ? 146.334 96.095  210.272 1.00 101.73 ? 3775 ARG A NH1   1 
ATOM   16232 N  NH2   . ARG A 1 3775 ? 144.749 97.287  209.127 1.00 109.46 ? 3775 ARG A NH2   1 
ATOM   16233 N  N     . GLU A 1 3776 ? 149.419 100.413 207.137 1.00 96.93  ? 3776 GLU A N     1 
ATOM   16234 C  CA    . GLU A 1 3776 ? 149.201 101.282 205.987 1.00 94.66  ? 3776 GLU A CA    1 
ATOM   16235 C  C     . GLU A 1 3776 ? 150.504 101.920 205.528 1.00 92.07  ? 3776 GLU A C     1 
ATOM   16236 O  O     . GLU A 1 3776 ? 150.754 102.038 204.323 1.00 93.21  ? 3776 GLU A O     1 
ATOM   16237 C  CB    . GLU A 1 3776 ? 148.167 102.355 206.327 1.00 94.50  ? 3776 GLU A CB    1 
ATOM   16238 C  CG    . GLU A 1 3776 ? 147.562 103.031 205.110 1.00 102.78 ? 3776 GLU A CG    1 
ATOM   16239 C  CD    . GLU A 1 3776 ? 146.399 103.935 205.463 1.00 107.04 ? 3776 GLU A CD    1 
ATOM   16240 O  OE1   . GLU A 1 3776 ? 146.053 104.020 206.660 1.00 108.35 ? 3776 GLU A OE1   1 
ATOM   16241 O  OE2   . GLU A 1 3776 ? 145.830 104.558 204.543 1.00 104.46 ? 3776 GLU A OE2   1 
ATOM   16242 N  N     . ALA A 1 3777 ? 151.349 102.333 206.476 1.00 90.60  ? 3777 ALA A N     1 
ATOM   16243 C  CA    . ALA A 1 3777 ? 152.644 102.899 206.115 1.00 89.63  ? 3777 ALA A CA    1 
ATOM   16244 C  C     . ALA A 1 3777 ? 153.502 101.881 205.377 1.00 94.51  ? 3777 ALA A C     1 
ATOM   16245 O  O     . ALA A 1 3777 ? 154.160 102.216 204.387 1.00 97.12  ? 3777 ALA A O     1 
ATOM   16246 C  CB    . ALA A 1 3777 ? 153.363 103.404 207.366 1.00 81.36  ? 3777 ALA A CB    1 
ATOM   16247 N  N     . ALA A 1 3778 ? 153.504 100.628 205.841 1.00 95.85  ? 3778 ALA A N     1 
ATOM   16248 C  CA    . ALA A 1 3778 ? 154.294 99.597  205.172 1.00 91.33  ? 3778 ALA A CA    1 
ATOM   16249 C  C     . ALA A 1 3778 ? 153.797 99.345  203.752 1.00 91.15  ? 3778 ALA A C     1 
ATOM   16250 O  O     . ALA A 1 3778 ? 154.599 99.232  202.812 1.00 91.40  ? 3778 ALA A O     1 
ATOM   16251 C  CB    . ALA A 1 3778 ? 154.267 98.304  205.987 1.00 84.89  ? 3778 ALA A CB    1 
ATOM   16252 N  N     . GLU A 1 3779 ? 152.476 99.251  203.572 1.00 90.97  ? 3779 GLU A N     1 
ATOM   16253 C  CA    . GLU A 1 3779 ? 151.946 99.001  202.233 1.00 91.52  ? 3779 GLU A CA    1 
ATOM   16254 C  C     . GLU A 1 3779 ? 152.207 100.186 201.306 1.00 89.00  ? 3779 GLU A C     1 
ATOM   16255 O  O     . GLU A 1 3779 ? 152.536 100.003 200.126 1.00 89.00  ? 3779 GLU A O     1 
ATOM   16256 C  CB    . GLU A 1 3779 ? 150.454 98.656  202.306 1.00 89.76  ? 3779 GLU A CB    1 
ATOM   16257 C  CG    . GLU A 1 3779 ? 149.488 99.826  202.205 1.00 94.68  ? 3779 GLU A CG    1 
ATOM   16258 C  CD    . GLU A 1 3779 ? 148.038 99.386  202.251 1.00 104.87 ? 3779 GLU A CD    1 
ATOM   16259 O  OE1   . GLU A 1 3779 ? 147.787 98.163  202.277 1.00 104.26 ? 3779 GLU A OE1   1 
ATOM   16260 O  OE2   . GLU A 1 3779 ? 147.149 100.263 202.259 1.00 108.08 ? 3779 GLU A OE2   1 
ATOM   16261 N  N     . VAL A 1 3780 ? 152.099 101.410 201.828 1.00 86.70  ? 3780 VAL A N     1 
ATOM   16262 C  CA    . VAL A 1 3780 ? 152.391 102.578 201.007 1.00 81.74  ? 3780 VAL A CA    1 
ATOM   16263 C  C     . VAL A 1 3780 ? 153.873 102.619 200.656 1.00 82.89  ? 3780 VAL A C     1 
ATOM   16264 O  O     . VAL A 1 3780 ? 154.243 103.030 199.552 1.00 87.41  ? 3780 VAL A O     1 
ATOM   16265 C  CB    . VAL A 1 3780 ? 151.927 103.860 201.723 1.00 79.31  ? 3780 VAL A CB    1 
ATOM   16266 C  CG1   . VAL A 1 3780 ? 152.550 105.089 201.088 1.00 76.06  ? 3780 VAL A CG1   1 
ATOM   16267 C  CG2   . VAL A 1 3780 ? 150.409 103.958 201.698 1.00 80.28  ? 3780 VAL A CG2   1 
ATOM   16268 N  N     . THR A 1 3781 ? 154.743 102.180 201.570 1.00 78.29  ? 3781 THR A N     1 
ATOM   16269 C  CA    . THR A 1 3781 ? 156.170 102.126 201.271 1.00 75.16  ? 3781 THR A CA    1 
ATOM   16270 C  C     . THR A 1 3781 ? 156.471 101.124 200.161 1.00 83.98  ? 3781 THR A C     1 
ATOM   16271 O  O     . THR A 1 3781 ? 157.289 101.396 199.274 1.00 91.56  ? 3781 THR A O     1 
ATOM   16272 C  CB    . THR A 1 3781 ? 156.958 101.777 202.533 1.00 73.10  ? 3781 THR A CB    1 
ATOM   16273 O  OG1   . THR A 1 3781 ? 156.524 102.610 203.615 1.00 85.80  ? 3781 THR A OG1   1 
ATOM   16274 C  CG2   . THR A 1 3781 ? 158.447 101.989 202.305 1.00 75.73  ? 3781 THR A CG2   1 
ATOM   16275 N  N     . ARG A 1 3782 ? 155.831 99.951  200.198 1.00 84.93  ? 3782 ARG A N     1 
ATOM   16276 C  CA    . ARG A 1 3782 ? 156.059 98.978  199.128 1.00 84.77  ? 3782 ARG A CA    1 
ATOM   16277 C  C     . ARG A 1 3782 ? 155.538 99.505  197.791 1.00 86.63  ? 3782 ARG A C     1 
ATOM   16278 O  O     . ARG A 1 3782 ? 156.173 99.309  196.740 1.00 87.89  ? 3782 ARG A O     1 
ATOM   16279 C  CB    . ARG A 1 3782 ? 155.430 97.625  199.486 1.00 86.45  ? 3782 ARG A CB    1 
ATOM   16280 C  CG    . ARG A 1 3782 ? 153.951 97.469  199.169 1.00 86.71  ? 3782 ARG A CG    1 
ATOM   16281 C  CD    . ARG A 1 3782 ? 153.477 96.037  199.356 1.00 91.06  ? 3782 ARG A CD    1 
ATOM   16282 N  NE    . ARG A 1 3782 ? 154.200 95.101  198.503 1.00 104.82 ? 3782 ARG A NE    1 
ATOM   16283 C  CZ    . ARG A 1 3782 ? 154.911 94.076  198.951 1.00 104.20 ? 3782 ARG A CZ    1 
ATOM   16284 N  NH1   . ARG A 1 3782 ? 155.016 93.821  200.245 1.00 101.44 ? 3782 ARG A NH1   1 
ATOM   16285 N  NH2   . ARG A 1 3782 ? 155.531 93.286  198.079 1.00 98.18  ? 3782 ARG A NH2   1 
ATOM   16286 N  N     . LYS A 1 3783 ? 154.394 100.199 197.813 1.00 86.96  ? 3783 LYS A N     1 
ATOM   16287 C  CA    . LYS A 1 3783 ? 153.893 100.828 196.594 1.00 84.88  ? 3783 LYS A CA    1 
ATOM   16288 C  C     . LYS A 1 3783 ? 154.865 101.887 196.088 1.00 86.71  ? 3783 LYS A C     1 
ATOM   16289 O  O     . LYS A 1 3783 ? 155.084 102.016 194.878 1.00 90.01  ? 3783 LYS A O     1 
ATOM   16290 C  CB    . LYS A 1 3783 ? 152.512 101.433 196.844 1.00 77.32  ? 3783 LYS A CB    1 
ATOM   16291 C  CG    . LYS A 1 3783 ? 151.418 100.403 197.077 1.00 78.13  ? 3783 LYS A CG    1 
ATOM   16292 C  CD    . LYS A 1 3783 ? 150.324 100.950 197.981 1.00 84.34  ? 3783 LYS A CD    1 
ATOM   16293 C  CE    . LYS A 1 3783 ? 149.110 101.392 197.181 1.00 82.77  ? 3783 LYS A CE    1 
ATOM   16294 N  NZ    . LYS A 1 3783 ? 147.842 101.162 197.927 1.00 83.02  ? 3783 LYS A NZ    1 
ATOM   16295 N  N     . VAL A 1 3784 ? 155.463 102.650 197.004 1.00 83.97  ? 3784 VAL A N     1 
ATOM   16296 C  CA    . VAL A 1 3784 ? 156.451 103.656 196.624 1.00 82.57  ? 3784 VAL A CA    1 
ATOM   16297 C  C     . VAL A 1 3784 ? 157.657 102.995 195.971 1.00 84.94  ? 3784 VAL A C     1 
ATOM   16298 O  O     . VAL A 1 3784 ? 158.193 103.497 194.978 1.00 91.98  ? 3784 VAL A O     1 
ATOM   16299 C  CB    . VAL A 1 3784 ? 156.858 104.492 197.853 1.00 79.52  ? 3784 VAL A CB    1 
ATOM   16300 C  CG1   . VAL A 1 3784 ? 158.210 105.155 197.634 1.00 82.11  ? 3784 VAL A CG1   1 
ATOM   16301 C  CG2   . VAL A 1 3784 ? 155.798 105.534 198.158 1.00 75.65  ? 3784 VAL A CG2   1 
ATOM   16302 N  N     . GLU A 1 3785 ? 158.104 101.865 196.519 1.00 82.96  ? 3785 GLU A N     1 
ATOM   16303 C  CA    . GLU A 1 3785 ? 159.262 101.175 195.955 1.00 86.42  ? 3785 GLU A CA    1 
ATOM   16304 C  C     . GLU A 1 3785 ? 158.982 100.691 194.534 1.00 87.28  ? 3785 GLU A C     1 
ATOM   16305 O  O     . GLU A 1 3785 ? 159.798 100.889 193.621 1.00 88.90  ? 3785 GLU A O     1 
ATOM   16306 C  CB    . GLU A 1 3785 ? 159.663 100.006 196.854 1.00 90.58  ? 3785 GLU A CB    1 
ATOM   16307 C  CG    . GLU A 1 3785 ? 160.250 100.422 198.195 1.00 96.89  ? 3785 GLU A CG    1 
ATOM   16308 C  CD    . GLU A 1 3785 ? 161.059 101.702 198.109 1.00 94.67  ? 3785 GLU A CD    1 
ATOM   16309 O  OE1   . GLU A 1 3785 ? 162.223 101.642 197.659 1.00 94.04  ? 3785 GLU A OE1   1 
ATOM   16310 O  OE2   . GLU A 1 3785 ? 160.534 102.768 198.496 1.00 85.86  ? 3785 GLU A OE2   1 
ATOM   16311 N  N     . GLU A 1 3786 ? 157.824 100.056 194.323 1.00 86.98  ? 3786 GLU A N     1 
ATOM   16312 C  CA    . GLU A 1 3786 ? 157.516 99.578  192.975 1.00 83.67  ? 3786 GLU A CA    1 
ATOM   16313 C  C     . GLU A 1 3786 ? 157.323 100.745 192.006 1.00 84.10  ? 3786 GLU A C     1 
ATOM   16314 O  O     . GLU A 1 3786 ? 157.740 100.672 190.839 1.00 86.60  ? 3786 GLU A O     1 
ATOM   16315 C  CB    . GLU A 1 3786 ? 156.291 98.660  192.994 1.00 87.29  ? 3786 GLU A CB    1 
ATOM   16316 C  CG    . GLU A 1 3786 ? 154.989 99.310  193.418 1.00 90.93  ? 3786 GLU A CG    1 
ATOM   16317 C  CD    . GLU A 1 3786 ? 153.907 98.296  193.731 1.00 97.05  ? 3786 GLU A CD    1 
ATOM   16318 O  OE1   . GLU A 1 3786 ? 154.228 97.093  193.834 1.00 101.82 ? 3786 GLU A OE1   1 
ATOM   16319 O  OE2   . GLU A 1 3786 ? 152.734 98.700  193.875 1.00 92.41  ? 3786 GLU A OE2   1 
ATOM   16320 N  N     . THR A 1 3787 ? 156.721 101.841 192.478 1.00 81.80  ? 3787 THR A N     1 
ATOM   16321 C  CA    . THR A 1 3787 ? 156.565 103.020 191.635 1.00 78.37  ? 3787 THR A CA    1 
ATOM   16322 C  C     . THR A 1 3787 ? 157.918 103.620 191.274 1.00 76.26  ? 3787 THR A C     1 
ATOM   16323 O  O     . THR A 1 3787 ? 158.109 104.105 190.155 1.00 79.37  ? 3787 THR A O     1 
ATOM   16324 C  CB    . THR A 1 3787 ? 155.688 104.054 192.338 1.00 81.34  ? 3787 THR A CB    1 
ATOM   16325 O  OG1   . THR A 1 3787 ? 154.569 103.398 192.945 1.00 89.96  ? 3787 THR A OG1   1 
ATOM   16326 C  CG2   . THR A 1 3787 ? 155.177 105.076 191.342 1.00 81.94  ? 3787 THR A CG2   1 
ATOM   16327 N  N     . ASP A 1 3788 ? 158.869 103.601 192.211 1.00 75.49  ? 3788 ASP A N     1 
ATOM   16328 C  CA    . ASP A 1 3788 ? 160.212 104.091 191.919 1.00 76.17  ? 3788 ASP A CA    1 
ATOM   16329 C  C     . ASP A 1 3788 ? 160.902 103.218 190.880 1.00 80.38  ? 3788 ASP A C     1 
ATOM   16330 O  O     . ASP A 1 3788 ? 161.625 103.724 190.013 1.00 85.57  ? 3788 ASP A O     1 
ATOM   16331 C  CB    . ASP A 1 3788 ? 161.042 104.154 193.200 1.00 82.32  ? 3788 ASP A CB    1 
ATOM   16332 C  CG    . ASP A 1 3788 ? 160.558 105.224 194.157 1.00 92.80  ? 3788 ASP A CG    1 
ATOM   16333 O  OD1   . ASP A 1 3788 ? 159.781 106.102 193.726 1.00 93.98  ? 3788 ASP A OD1   1 
ATOM   16334 O  OD2   . ASP A 1 3788 ? 160.955 105.188 195.341 1.00 94.49  ? 3788 ASP A OD2   1 
ATOM   16335 N  N     . ILE A 1 3789 ? 160.704 101.900 190.959 1.00 80.29  ? 3789 ILE A N     1 
ATOM   16336 C  CA    . ILE A 1 3789 ? 161.272 101.012 189.943 1.00 77.17  ? 3789 ILE A CA    1 
ATOM   16337 C  C     . ILE A 1 3789 ? 160.706 101.351 188.566 1.00 73.47  ? 3789 ILE A C     1 
ATOM   16338 O  O     . ILE A 1 3789 ? 161.442 101.467 187.574 1.00 71.96  ? 3789 ILE A O     1 
ATOM   16339 C  CB    . ILE A 1 3789 ? 161.018 99.539  190.314 1.00 75.45  ? 3789 ILE A CB    1 
ATOM   16340 C  CG1   . ILE A 1 3789 ? 161.870 99.139  191.520 1.00 75.19  ? 3789 ILE A CG1   1 
ATOM   16341 C  CG2   . ILE A 1 3789 ? 161.305 98.630  189.128 1.00 71.84  ? 3789 ILE A CG2   1 
ATOM   16342 C  CD1   . ILE A 1 3789 ? 161.781 97.670  191.871 1.00 77.46  ? 3789 ILE A CD1   1 
ATOM   16343 N  N     . VAL A 1 3790 ? 159.385 101.535 188.490 1.00 72.01  ? 3790 VAL A N     1 
ATOM   16344 C  CA    . VAL A 1 3790 ? 158.774 101.869 187.204 1.00 69.44  ? 3790 VAL A CA    1 
ATOM   16345 C  C     . VAL A 1 3790 ? 159.241 103.244 186.722 1.00 69.28  ? 3790 VAL A C     1 
ATOM   16346 O  O     . VAL A 1 3790 ? 159.420 103.464 185.515 1.00 67.86  ? 3790 VAL A O     1 
ATOM   16347 C  CB    . VAL A 1 3790 ? 157.240 101.784 187.310 1.00 67.03  ? 3790 VAL A CB    1 
ATOM   16348 C  CG1   . VAL A 1 3790 ? 156.585 102.218 186.010 1.00 66.23  ? 3790 VAL A CG1   1 
ATOM   16349 C  CG2   . VAL A 1 3790 ? 156.814 100.371 187.679 1.00 61.86  ? 3790 VAL A CG2   1 
ATOM   16350 N  N     . MET A 1 3791 ? 159.455 104.184 187.645 1.00 72.56  ? 3791 MET A N     1 
ATOM   16351 C  CA    . MET A 1 3791 ? 159.938 105.508 187.265 1.00 71.67  ? 3791 MET A CA    1 
ATOM   16352 C  C     . MET A 1 3791 ? 161.363 105.445 186.727 1.00 72.27  ? 3791 MET A C     1 
ATOM   16353 O  O     . MET A 1 3791 ? 161.717 106.188 185.805 1.00 72.10  ? 3791 MET A O     1 
ATOM   16354 C  CB    . MET A 1 3791 ? 159.854 106.458 188.459 1.00 73.06  ? 3791 MET A CB    1 
ATOM   16355 C  CG    . MET A 1 3791 ? 160.185 107.902 188.123 1.00 84.76  ? 3791 MET A CG    1 
ATOM   16356 S  SD    . MET A 1 3791 ? 158.978 108.641 187.007 1.00 95.09  ? 3791 MET A SD    1 
ATOM   16357 C  CE    . MET A 1 3791 ? 159.955 109.946 186.267 1.00 79.88  ? 3791 MET A CE    1 
ATOM   16358 N  N     . GLN A 1 3792 ? 162.201 104.579 187.300 1.00 71.90  ? 3792 GLN A N     1 
ATOM   16359 C  CA    . GLN A 1 3792 ? 163.526 104.355 186.729 1.00 71.63  ? 3792 GLN A CA    1 
ATOM   16360 C  C     . GLN A 1 3792 ? 163.419 103.774 185.325 1.00 67.61  ? 3792 GLN A C     1 
ATOM   16361 O  O     . GLN A 1 3792 ? 164.176 104.158 184.421 1.00 69.67  ? 3792 GLN A O     1 
ATOM   16362 C  CB    . GLN A 1 3792 ? 164.346 103.429 187.627 1.00 77.54  ? 3792 GLN A CB    1 
ATOM   16363 C  CG    . GLN A 1 3792 ? 164.715 104.022 188.975 1.00 89.09  ? 3792 GLN A CG    1 
ATOM   16364 C  CD    . GLN A 1 3792 ? 165.515 103.058 189.830 1.00 94.89  ? 3792 GLN A CD    1 
ATOM   16365 O  OE1   . GLN A 1 3792 ? 165.743 101.911 189.444 1.00 90.95  ? 3792 GLN A OE1   1 
ATOM   16366 N  NE2   . GLN A 1 3792 ? 165.948 103.520 190.997 1.00 98.69  ? 3792 GLN A NE2   1 
ATOM   16367 N  N     . GLU A 1 3793 ? 162.480 102.845 185.128 1.00 68.65  ? 3793 GLU A N     1 
ATOM   16368 C  CA    . GLU A 1 3793 ? 162.247 102.311 183.788 1.00 66.42  ? 3793 GLU A CA    1 
ATOM   16369 C  C     . GLU A 1 3793 ? 161.874 103.421 182.809 1.00 63.86  ? 3793 GLU A C     1 
ATOM   16370 O  O     . GLU A 1 3793 ? 162.326 103.423 181.658 1.00 62.84  ? 3793 GLU A O     1 
ATOM   16371 C  CB    . GLU A 1 3793 ? 161.156 101.240 183.836 1.00 64.54  ? 3793 GLU A CB    1 
ATOM   16372 C  CG    . GLU A 1 3793 ? 160.900 100.535 182.512 1.00 66.88  ? 3793 GLU A CG    1 
ATOM   16373 C  CD    . GLU A 1 3793 ? 159.800 101.193 181.698 1.00 75.38  ? 3793 GLU A CD    1 
ATOM   16374 O  OE1   . GLU A 1 3793 ? 159.143 102.118 182.222 1.00 77.95  ? 3793 GLU A OE1   1 
ATOM   16375 O  OE2   . GLU A 1 3793 ? 159.592 100.786 180.536 1.00 68.33  ? 3793 GLU A OE2   1 
ATOM   16376 N  N     . VAL A 1 3794 ? 161.047 104.370 183.251 1.00 65.82  ? 3794 VAL A N     1 
ATOM   16377 C  CA    . VAL A 1 3794 ? 160.645 105.479 182.384 1.00 62.50  ? 3794 VAL A CA    1 
ATOM   16378 C  C     . VAL A 1 3794 ? 161.822 106.411 182.108 1.00 61.58  ? 3794 VAL A C     1 
ATOM   16379 O  O     . VAL A 1 3794 ? 161.998 106.900 180.982 1.00 62.94  ? 3794 VAL A O     1 
ATOM   16380 C  CB    . VAL A 1 3794 ? 159.459 106.236 183.009 1.00 65.66  ? 3794 VAL A CB    1 
ATOM   16381 C  CG1   . VAL A 1 3794 ? 159.177 107.519 182.243 1.00 60.79  ? 3794 VAL A CG1   1 
ATOM   16382 C  CG2   . VAL A 1 3794 ? 158.231 105.352 183.034 1.00 68.16  ? 3794 VAL A CG2   1 
ATOM   16383 N  N     . GLU A 1 3795 ? 162.632 106.690 183.132 1.00 62.42  ? 3795 GLU A N     1 
ATOM   16384 C  CA    . GLU A 1 3795 ? 163.800 107.546 182.952 1.00 62.42  ? 3795 GLU A CA    1 
ATOM   16385 C  C     . GLU A 1 3795 ? 164.786 106.939 181.965 1.00 63.90  ? 3795 GLU A C     1 
ATOM   16386 O  O     . GLU A 1 3795 ? 165.462 107.669 181.229 1.00 66.77  ? 3795 GLU A O     1 
ATOM   16387 C  CB    . GLU A 1 3795 ? 164.477 107.796 184.301 1.00 64.01  ? 3795 GLU A CB    1 
ATOM   16388 C  CG    . GLU A 1 3795 ? 165.819 108.506 184.213 1.00 65.48  ? 3795 GLU A CG    1 
ATOM   16389 C  CD    . GLU A 1 3795 ? 166.723 108.192 185.387 1.00 73.40  ? 3795 GLU A CD    1 
ATOM   16390 O  OE1   . GLU A 1 3795 ? 167.774 108.853 185.522 1.00 79.22  ? 3795 GLU A OE1   1 
ATOM   16391 O  OE2   . GLU A 1 3795 ? 166.386 107.282 186.173 1.00 75.21  ? 3795 GLU A OE2   1 
ATOM   16392 N  N     . THR A 1 3796 ? 164.878 105.607 181.934 1.00 64.45  ? 3796 THR A N     1 
ATOM   16393 C  CA    . THR A 1 3796 ? 165.721 104.951 180.939 1.00 64.21  ? 3796 THR A CA    1 
ATOM   16394 C  C     . THR A 1 3796 ? 165.307 105.346 179.524 1.00 61.93  ? 3796 THR A C     1 
ATOM   16395 O  O     . THR A 1 3796 ? 166.161 105.626 178.674 1.00 62.99  ? 3796 THR A O     1 
ATOM   16396 C  CB    . THR A 1 3796 ? 165.660 103.433 181.116 1.00 67.14  ? 3796 THR A CB    1 
ATOM   16397 O  OG1   . THR A 1 3796 ? 166.366 103.061 182.307 1.00 69.85  ? 3796 THR A OG1   1 
ATOM   16398 C  CG2   . THR A 1 3796 ? 166.287 102.724 179.924 1.00 58.56  ? 3796 THR A CG2   1 
ATOM   16399 N  N     . VAL A 1 3797 ? 164.000 105.388 179.258 1.00 60.20  ? 3797 VAL A N     1 
ATOM   16400 C  CA    . VAL A 1 3797 ? 163.520 105.799 177.942 1.00 59.26  ? 3797 VAL A CA    1 
ATOM   16401 C  C     . VAL A 1 3797 ? 163.753 107.290 177.723 1.00 59.71  ? 3797 VAL A C     1 
ATOM   16402 O  O     . VAL A 1 3797 ? 164.185 107.713 176.644 1.00 62.14  ? 3797 VAL A O     1 
ATOM   16403 C  CB    . VAL A 1 3797 ? 162.034 105.430 177.780 1.00 54.75  ? 3797 VAL A CB    1 
ATOM   16404 C  CG1   . VAL A 1 3797 ? 161.497 105.949 176.456 1.00 53.83  ? 3797 VAL A CG1   1 
ATOM   16405 C  CG2   . VAL A 1 3797 ? 161.848 103.926 177.883 1.00 59.76  ? 3797 VAL A CG2   1 
ATOM   16406 N  N     . SER A 1 3798 ? 163.470 108.110 178.740 1.00 59.80  ? 3798 SER A N     1 
ATOM   16407 C  CA    . SER A 1 3798 ? 163.598 109.559 178.593 1.00 52.56  ? 3798 SER A CA    1 
ATOM   16408 C  C     . SER A 1 3798 ? 165.039 110.002 178.355 1.00 53.51  ? 3798 SER A C     1 
ATOM   16409 O  O     . SER A 1 3798 ? 165.261 111.069 177.763 1.00 55.25  ? 3798 SER A O     1 
ATOM   16410 C  CB    . SER A 1 3798 ? 163.035 110.263 179.827 1.00 55.53  ? 3798 SER A CB    1 
ATOM   16411 O  OG    . SER A 1 3798 ? 161.777 109.724 180.191 1.00 61.38  ? 3798 SER A OG    1 
ATOM   16412 N  N     . GLN A 1 3799 ? 166.016 109.212 178.806 1.00 52.44  ? 3799 GLN A N     1 
ATOM   16413 C  CA    . GLN A 1 3799 ? 167.416 109.547 178.563 1.00 50.93  ? 3799 GLN A CA    1 
ATOM   16414 C  C     . GLN A 1 3799 ? 167.698 109.674 177.069 1.00 49.21  ? 3799 GLN A C     1 
ATOM   16415 O  O     . GLN A 1 3799 ? 168.503 110.518 176.659 1.00 47.91  ? 3799 GLN A O     1 
ATOM   16416 C  CB    . GLN A 1 3799 ? 168.308 108.487 179.222 1.00 57.72  ? 3799 GLN A CB    1 
ATOM   16417 C  CG    . GLN A 1 3799 ? 169.747 108.899 179.578 1.00 63.55  ? 3799 GLN A CG    1 
ATOM   16418 C  CD    . GLN A 1 3799 ? 170.573 109.404 178.407 1.00 67.64  ? 3799 GLN A CD    1 
ATOM   16419 O  OE1   . GLN A 1 3799 ? 170.511 108.860 177.304 1.00 66.62  ? 3799 GLN A OE1   1 
ATOM   16420 N  NE2   . GLN A 1 3799 ? 171.351 110.453 178.644 1.00 65.74  ? 3799 GLN A NE2   1 
ATOM   16421 N  N     . GLN A 1 3800 ? 167.020 108.874 176.242 1.00 52.12  ? 3800 GLN A N     1 
ATOM   16422 C  CA    . GLN A 1 3800 ? 167.218 108.950 174.798 1.00 48.95  ? 3800 GLN A CA    1 
ATOM   16423 C  C     . GLN A 1 3800 ? 166.858 110.329 174.257 1.00 43.55  ? 3800 GLN A C     1 
ATOM   16424 O  O     . GLN A 1 3800 ? 167.582 110.886 173.423 1.00 45.11  ? 3800 GLN A O     1 
ATOM   16425 C  CB    . GLN A 1 3800 ? 166.391 107.869 174.101 1.00 50.67  ? 3800 GLN A CB    1 
ATOM   16426 C  CG    . GLN A 1 3800 ? 166.248 108.064 172.602 1.00 56.00  ? 3800 GLN A CG    1 
ATOM   16427 C  CD    . GLN A 1 3800 ? 166.103 106.754 171.853 1.00 70.61  ? 3800 GLN A CD    1 
ATOM   16428 O  OE1   . GLN A 1 3800 ? 165.171 105.987 172.096 1.00 71.87  ? 3800 GLN A OE1   1 
ATOM   16429 N  NE2   . GLN A 1 3800 ? 167.026 106.492 170.936 1.00 66.43  ? 3800 GLN A NE2   1 
ATOM   16430 N  N     . TYR A 1 3801 ? 165.745 110.896 174.716 1.00 43.76  ? 3801 TYR A N     1 
ATOM   16431 C  CA    . TYR A 1 3801 ? 165.316 112.214 174.271 1.00 38.36  ? 3801 TYR A CA    1 
ATOM   16432 C  C     . TYR A 1 3801 ? 165.953 113.351 175.058 1.00 36.10  ? 3801 TYR A C     1 
ATOM   16433 O  O     . TYR A 1 3801 ? 165.722 114.517 174.722 1.00 35.53  ? 3801 TYR A O     1 
ATOM   16434 C  CB    . TYR A 1 3801 ? 163.791 112.333 174.359 1.00 35.83  ? 3801 TYR A CB    1 
ATOM   16435 C  CG    . TYR A 1 3801 ? 163.050 111.380 173.452 1.00 38.30  ? 3801 TYR A CG    1 
ATOM   16436 C  CD1   . TYR A 1 3801 ? 162.860 111.675 172.110 1.00 39.91  ? 3801 TYR A CD1   1 
ATOM   16437 C  CD2   . TYR A 1 3801 ? 162.540 110.185 173.938 1.00 41.78  ? 3801 TYR A CD2   1 
ATOM   16438 C  CE1   . TYR A 1 3801 ? 162.184 110.808 171.277 1.00 37.84  ? 3801 TYR A CE1   1 
ATOM   16439 C  CE2   . TYR A 1 3801 ? 161.862 109.311 173.113 1.00 47.90  ? 3801 TYR A CE2   1 
ATOM   16440 C  CZ    . TYR A 1 3801 ? 161.687 109.627 171.783 1.00 46.74  ? 3801 TYR A CZ    1 
ATOM   16441 O  OH    . TYR A 1 3801 ? 161.013 108.759 170.957 1.00 56.57  ? 3801 TYR A OH    1 
ATOM   16442 N  N     . LEU A 1 3802 ? 166.731 113.044 176.096 1.00 40.97  ? 3802 LEU A N     1 
ATOM   16443 C  CA    . LEU A 1 3802 ? 167.396 114.090 176.876 1.00 37.84  ? 3802 LEU A CA    1 
ATOM   16444 C  C     . LEU A 1 3802 ? 168.256 115.044 176.048 1.00 34.77  ? 3802 LEU A C     1 
ATOM   16445 O  O     . LEU A 1 3802 ? 168.140 116.263 176.250 1.00 34.95  ? 3802 LEU A O     1 
ATOM   16446 C  CB    . LEU A 1 3802 ? 168.229 113.440 177.989 1.00 43.94  ? 3802 LEU A CB    1 
ATOM   16447 C  CG    . LEU A 1 3802 ? 168.943 114.404 178.938 1.00 38.16  ? 3802 LEU A CG    1 
ATOM   16448 C  CD1   . LEU A 1 3802 ? 167.936 115.251 179.698 1.00 44.51  ? 3802 LEU A CD1   1 
ATOM   16449 C  CD2   . LEU A 1 3802 ? 169.846 113.646 179.897 1.00 39.39  ? 3802 LEU A CD2   1 
ATOM   16450 N  N     . PRO A 1 3803 ? 169.130 114.589 175.137 1.00 37.91  ? 3803 PRO A N     1 
ATOM   16451 C  CA    . PRO A 1 3803 ? 169.967 115.556 174.397 1.00 33.41  ? 3803 PRO A CA    1 
ATOM   16452 C  C     . PRO A 1 3803 ? 169.177 116.553 173.564 1.00 34.70  ? 3803 PRO A C     1 
ATOM   16453 O  O     . PRO A 1 3803 ? 169.612 117.704 173.413 1.00 33.77  ? 3803 PRO A O     1 
ATOM   16454 C  CB    . PRO A 1 3803 ? 170.840 114.656 173.511 1.00 27.23  ? 3803 PRO A CB    1 
ATOM   16455 C  CG    . PRO A 1 3803 ? 170.854 113.344 174.201 1.00 34.28  ? 3803 PRO A CG    1 
ATOM   16456 C  CD    . PRO A 1 3803 ? 169.490 113.201 174.795 1.00 39.58  ? 3803 PRO A CD    1 
ATOM   16457 N  N     . LEU A 1 3804 ? 168.032 116.146 173.011 1.00 34.81  ? 3804 LEU A N     1 
ATOM   16458 C  CA    . LEU A 1 3804 ? 167.236 117.063 172.202 1.00 24.04  ? 3804 LEU A CA    1 
ATOM   16459 C  C     . LEU A 1 3804 ? 166.729 118.233 173.036 1.00 25.94  ? 3804 LEU A C     1 
ATOM   16460 O  O     . LEU A 1 3804 ? 166.673 119.369 172.554 1.00 29.26  ? 3804 LEU A O     1 
ATOM   16461 C  CB    . LEU A 1 3804 ? 166.071 116.319 171.551 1.00 25.47  ? 3804 LEU A CB    1 
ATOM   16462 C  CG    . LEU A 1 3804 ? 165.085 117.175 170.755 1.00 26.10  ? 3804 LEU A CG    1 
ATOM   16463 C  CD1   . LEU A 1 3804 ? 165.797 117.909 169.630 1.00 24.28  ? 3804 LEU A CD1   1 
ATOM   16464 C  CD2   . LEU A 1 3804 ? 163.955 116.324 170.206 1.00 30.50  ? 3804 LEU A CD2   1 
ATOM   16465 N  N     . SER A 1 3805 ? 166.355 117.974 174.291 1.00 22.53  ? 3805 SER A N     1 
ATOM   16466 C  CA    . SER A 1 3805 ? 165.915 119.054 175.169 1.00 19.22  ? 3805 SER A CA    1 
ATOM   16467 C  C     . SER A 1 3805 ? 167.043 120.043 175.437 1.00 21.11  ? 3805 SER A C     1 
ATOM   16468 O  O     . SER A 1 3805 ? 166.820 121.260 175.467 1.00 27.41  ? 3805 SER A O     1 
ATOM   16469 C  CB    . SER A 1 3805 ? 165.382 118.476 176.478 1.00 24.18  ? 3805 SER A CB    1 
ATOM   16470 O  OG    . SER A 1 3805 ? 166.403 117.792 177.183 1.00 36.62  ? 3805 SER A OG    1 
ATOM   16471 N  N     . THR A 1 3806 ? 168.262 119.539 175.645 1.00 20.13  ? 3806 THR A N     1 
ATOM   16472 C  CA    . THR A 1 3806 ? 169.405 120.425 175.839 1.00 21.94  ? 3806 THR A CA    1 
ATOM   16473 C  C     . THR A 1 3806 ? 169.663 121.267 174.595 1.00 20.47  ? 3806 THR A C     1 
ATOM   16474 O  O     . THR A 1 3806 ? 169.934 122.471 174.694 1.00 24.02  ? 3806 THR A O     1 
ATOM   16475 C  CB    . THR A 1 3806 ? 170.647 119.610 176.201 1.00 27.11  ? 3806 THR A CB    1 
ATOM   16476 O  OG1   . THR A 1 3806 ? 170.417 118.906 177.428 1.00 27.41  ? 3806 THR A OG1   1 
ATOM   16477 C  CG2   . THR A 1 3806 ? 171.854 120.519 176.367 1.00 24.97  ? 3806 THR A CG2   1 
ATOM   16478 N  N     . ALA A 1 3807 ? 169.574 120.651 173.414 1.00 20.25  ? 3807 ALA A N     1 
ATOM   16479 C  CA    . ALA A 1 3807 ? 169.748 121.406 172.176 1.00 19.28  ? 3807 ALA A CA    1 
ATOM   16480 C  C     . ALA A 1 3807 ? 168.673 122.476 172.031 1.00 19.21  ? 3807 ALA A C     1 
ATOM   16481 O  O     . ALA A 1 3807 ? 168.959 123.599 171.602 1.00 20.93  ? 3807 ALA A O     1 
ATOM   16482 C  CB    . ALA A 1 3807 ? 169.731 120.460 170.976 1.00 19.38  ? 3807 ALA A CB    1 
ATOM   16483 N  N     . CYS A 1 3808 ? 167.430 122.142 172.383 1.00 20.53  ? 3808 CYS A N     1 
ATOM   16484 C  CA    . CYS A 1 3808 ? 166.342 123.113 172.307 1.00 17.35  ? 3808 CYS A CA    1 
ATOM   16485 C  C     . CYS A 1 3808 ? 166.578 124.287 173.249 1.00 16.62  ? 3808 CYS A C     1 
ATOM   16486 O  O     . CYS A 1 3808 ? 166.371 125.448 172.873 1.00 19.17  ? 3808 CYS A O     1 
ATOM   16487 C  CB    . CYS A 1 3808 ? 165.016 122.429 172.633 1.00 14.74  ? 3808 CYS A CB    1 
ATOM   16488 S  SG    . CYS A 1 3808 ? 164.447 121.283 171.370 1.00 32.31  ? 3808 CYS A SG    1 
ATOM   16489 N  N     . SER A 1 3809 ? 167.002 124.002 174.482 1.00 16.58  ? 3809 SER A N     1 
ATOM   16490 C  CA    . SER A 1 3809 ? 167.278 125.076 175.430 1.00 17.74  ? 3809 SER A CA    1 
ATOM   16491 C  C     . SER A 1 3809 ? 168.415 125.962 174.939 1.00 22.03  ? 3809 SER A C     1 
ATOM   16492 O  O     . SER A 1 3809 ? 168.342 127.194 175.040 1.00 26.27  ? 3809 SER A O     1 
ATOM   16493 C  CB    . SER A 1 3809 ? 167.604 124.495 176.805 1.00 19.55  ? 3809 SER A CB    1 
ATOM   16494 O  OG    . SER A 1 3809 ? 168.986 124.211 176.923 1.00 22.13  ? 3809 SER A OG    1 
ATOM   16495 N  N     . SER A 1 3810 ? 169.473 125.352 174.399 1.00 19.48  ? 3810 SER A N     1 
ATOM   16496 C  CA    . SER A 1 3810 ? 170.583 126.136 173.868 1.00 15.81  ? 3810 SER A CA    1 
ATOM   16497 C  C     . SER A 1 3810 ? 170.133 127.011 172.706 1.00 16.72  ? 3810 SER A C     1 
ATOM   16498 O  O     . SER A 1 3810 ? 170.529 128.179 172.610 1.00 17.63  ? 3810 SER A O     1 
ATOM   16499 C  CB    . SER A 1 3810 ? 171.720 125.211 173.436 1.00 18.98  ? 3810 SER A CB    1 
ATOM   16500 O  OG    . SER A 1 3810 ? 172.099 124.342 174.490 1.00 23.45  ? 3810 SER A OG    1 
ATOM   16501 N  N     . ILE A 1 3811 ? 169.296 126.469 171.819 1.00 15.67  ? 3811 ILE A N     1 
ATOM   16502 C  CA    . ILE A 1 3811 ? 168.809 127.244 170.681 1.00 14.67  ? 3811 ILE A CA    1 
ATOM   16503 C  C     . ILE A 1 3811 ? 167.970 128.423 171.155 1.00 14.93  ? 3811 ILE A C     1 
ATOM   16504 O  O     . ILE A 1 3811 ? 168.130 129.552 170.672 1.00 20.75  ? 3811 ILE A O     1 
ATOM   16505 C  CB    . ILE A 1 3811 ? 168.021 126.339 169.715 1.00 12.83  ? 3811 ILE A CB    1 
ATOM   16506 C  CG1   . ILE A 1 3811 ? 168.973 125.438 168.929 1.00 14.08  ? 3811 ILE A CG1   1 
ATOM   16507 C  CG2   . ILE A 1 3811 ? 167.178 127.172 168.764 1.00 13.57  ? 3811 ILE A CG2   1 
ATOM   16508 C  CD1   . ILE A 1 3811 ? 168.274 124.524 167.955 1.00 12.73  ? 3811 ILE A CD1   1 
ATOM   16509 N  N     . TYR A 1 3812 ? 167.068 128.188 172.111 1.00 12.94  ? 3812 TYR A N     1 
ATOM   16510 C  CA    . TYR A 1 3812 ? 166.230 129.282 172.593 1.00 14.33  ? 3812 TYR A CA    1 
ATOM   16511 C  C     . TYR A 1 3812 ? 167.059 130.355 173.283 1.00 16.26  ? 3812 TYR A C     1 
ATOM   16512 O  O     . TYR A 1 3812 ? 166.801 131.551 173.111 1.00 19.98  ? 3812 TYR A O     1 
ATOM   16513 C  CB    . TYR A 1 3812 ? 165.152 128.774 173.546 1.00 16.13  ? 3812 TYR A CB    1 
ATOM   16514 C  CG    . TYR A 1 3812 ? 164.443 129.908 174.256 1.00 19.70  ? 3812 TYR A CG    1 
ATOM   16515 C  CD1   . TYR A 1 3812 ? 163.562 130.734 173.572 1.00 24.32  ? 3812 TYR A CD1   1 
ATOM   16516 C  CD2   . TYR A 1 3812 ? 164.678 130.174 175.598 1.00 23.60  ? 3812 TYR A CD2   1 
ATOM   16517 C  CE1   . TYR A 1 3812 ? 162.921 131.779 174.208 1.00 28.68  ? 3812 TYR A CE1   1 
ATOM   16518 C  CE2   . TYR A 1 3812 ? 164.040 131.216 176.243 1.00 28.68  ? 3812 TYR A CE2   1 
ATOM   16519 C  CZ    . TYR A 1 3812 ? 163.163 132.015 175.543 1.00 31.56  ? 3812 TYR A CZ    1 
ATOM   16520 O  OH    . TYR A 1 3812 ? 162.526 133.055 176.180 1.00 31.21  ? 3812 TYR A OH    1 
ATOM   16521 N  N     . PHE A 1 3813 ? 168.049 129.954 174.084 1.00 16.25  ? 3813 PHE A N     1 
ATOM   16522 C  CA    . PHE A 1 3813 ? 168.844 130.953 174.788 1.00 15.74  ? 3813 PHE A CA    1 
ATOM   16523 C  C     . PHE A 1 3813 ? 169.789 131.686 173.845 1.00 17.29  ? 3813 PHE A C     1 
ATOM   16524 O  O     . PHE A 1 3813 ? 170.174 132.828 174.123 1.00 22.25  ? 3813 PHE A O     1 
ATOM   16525 C  CB    . PHE A 1 3813 ? 169.605 130.303 175.940 1.00 18.77  ? 3813 PHE A CB    1 
ATOM   16526 C  CG    . PHE A 1 3813 ? 168.809 130.223 177.210 1.00 22.72  ? 3813 PHE A CG    1 
ATOM   16527 C  CD1   . PHE A 1 3813 ? 167.916 129.187 177.419 1.00 22.82  ? 3813 PHE A CD1   1 
ATOM   16528 C  CD2   . PHE A 1 3813 ? 168.938 131.195 178.187 1.00 28.83  ? 3813 PHE A CD2   1 
ATOM   16529 C  CE1   . PHE A 1 3813 ? 167.176 129.115 178.581 1.00 25.59  ? 3813 PHE A CE1   1 
ATOM   16530 C  CE2   . PHE A 1 3813 ? 168.201 131.128 179.352 1.00 27.09  ? 3813 PHE A CE2   1 
ATOM   16531 C  CZ    . PHE A 1 3813 ? 167.319 130.086 179.549 1.00 25.12  ? 3813 PHE A CZ    1 
ATOM   16532 N  N     . THR A 1 3814 ? 170.177 131.056 172.734 1.00 16.62  ? 3814 THR A N     1 
ATOM   16533 C  CA    . THR A 1 3814 ? 170.872 131.787 171.680 1.00 15.38  ? 3814 THR A CA    1 
ATOM   16534 C  C     . THR A 1 3814 ? 169.943 132.798 171.020 1.00 17.48  ? 3814 THR A C     1 
ATOM   16535 O  O     . THR A 1 3814 ? 170.357 133.917 170.693 1.00 19.28  ? 3814 THR A O     1 
ATOM   16536 C  CB    . THR A 1 3814 ? 171.433 130.810 170.647 1.00 14.23  ? 3814 THR A CB    1 
ATOM   16537 O  OG1   . THR A 1 3814 ? 172.396 129.955 171.274 1.00 18.79  ? 3814 THR A OG1   1 
ATOM   16538 C  CG2   . THR A 1 3814 ? 172.101 131.558 169.505 1.00 16.62  ? 3814 THR A CG2   1 
ATOM   16539 N  N     . MET A 1 3815 ? 168.678 132.419 170.820 1.00 16.03  ? 3815 MET A N     1 
ATOM   16540 C  CA    . MET A 1 3815 ? 167.699 133.350 170.266 1.00 14.88  ? 3815 MET A CA    1 
ATOM   16541 C  C     . MET A 1 3815 ? 167.493 134.545 171.186 1.00 19.56  ? 3815 MET A C     1 
ATOM   16542 O  O     . MET A 1 3815 ? 167.379 135.686 170.723 1.00 21.68  ? 3815 MET A O     1 
ATOM   16543 C  CB    . MET A 1 3815 ? 166.368 132.637 170.036 1.00 14.56  ? 3815 MET A CB    1 
ATOM   16544 C  CG    . MET A 1 3815 ? 166.378 131.595 168.940 1.00 17.36  ? 3815 MET A CG    1 
ATOM   16545 S  SD    . MET A 1 3815 ? 164.736 131.395 168.234 1.00 34.07  ? 3815 MET A SD    1 
ATOM   16546 C  CE    . MET A 1 3815 ? 163.728 131.489 169.707 1.00 28.70  ? 3815 MET A CE    1 
ATOM   16547 N  N     . GLU A 1 3816 ? 167.426 134.298 172.496 1.00 22.50  ? 3816 GLU A N     1 
ATOM   16548 C  CA    . GLU A 1 3816 ? 167.198 135.377 173.451 1.00 21.19  ? 3816 GLU A CA    1 
ATOM   16549 C  C     . GLU A 1 3816 ? 168.370 136.351 173.470 1.00 24.31  ? 3816 GLU A C     1 
ATOM   16550 O  O     . GLU A 1 3816 ? 168.185 137.555 173.681 1.00 31.67  ? 3816 GLU A O     1 
ATOM   16551 C  CB    . GLU A 1 3816 ? 166.956 134.793 174.843 1.00 21.35  ? 3816 GLU A CB    1 
ATOM   16552 C  CG    . GLU A 1 3816 ? 166.626 135.816 175.918 1.00 38.98  ? 3816 GLU A CG    1 
ATOM   16553 C  CD    . GLU A 1 3816 ? 165.292 136.501 175.688 1.00 51.32  ? 3816 GLU A CD    1 
ATOM   16554 O  OE1   . GLU A 1 3816 ? 164.418 135.903 175.025 1.00 51.08  ? 3816 GLU A OE1   1 
ATOM   16555 O  OE2   . GLU A 1 3816 ? 165.114 137.636 176.177 1.00 48.47  ? 3816 GLU A OE2   1 
ATOM   16556 N  N     . SER A 1 3817 ? 169.585 135.848 173.247 1.00 21.70  ? 3817 SER A N     1 
ATOM   16557 C  CA    . SER A 1 3817 ? 170.766 136.700 173.215 1.00 21.02  ? 3817 SER A CA    1 
ATOM   16558 C  C     . SER A 1 3817 ? 170.934 137.425 171.888 1.00 22.83  ? 3817 SER A C     1 
ATOM   16559 O  O     . SER A 1 3817 ? 171.845 138.250 171.766 1.00 25.19  ? 3817 SER A O     1 
ATOM   16560 C  CB    . SER A 1 3817 ? 172.017 135.871 173.511 1.00 24.18  ? 3817 SER A CB    1 
ATOM   16561 O  OG    . SER A 1 3817 ? 172.150 135.623 174.900 1.00 34.35  ? 3817 SER A OG    1 
ATOM   16562 N  N     . LEU A 1 3818 ? 170.090 137.136 170.894 1.00 22.45  ? 3818 LEU A N     1 
ATOM   16563 C  CA    . LEU A 1 3818 ? 170.212 137.789 169.596 1.00 16.26  ? 3818 LEU A CA    1 
ATOM   16564 C  C     . LEU A 1 3818 ? 169.885 139.274 169.660 1.00 16.28  ? 3818 LEU A C     1 
ATOM   16565 O  O     . LEU A 1 3818 ? 170.271 140.021 168.756 1.00 21.93  ? 3818 LEU A O     1 
ATOM   16566 C  CB    . LEU A 1 3818 ? 169.305 137.103 168.574 1.00 14.41  ? 3818 LEU A CB    1 
ATOM   16567 C  CG    . LEU A 1 3818 ? 169.937 135.986 167.744 1.00 12.42  ? 3818 LEU A CG    1 
ATOM   16568 C  CD1   . LEU A 1 3818 ? 168.874 135.258 166.944 1.00 12.05  ? 3818 LEU A CD1   1 
ATOM   16569 C  CD2   . LEU A 1 3818 ? 171.017 136.537 166.830 1.00 18.71  ? 3818 LEU A CD2   1 
ATOM   16570 N  N     . LYS A 1 3819 ? 169.181 139.719 170.702 1.00 16.33  ? 3819 LYS A N     1 
ATOM   16571 C  CA    . LYS A 1 3819 ? 168.857 141.132 170.846 1.00 16.04  ? 3819 LYS A CA    1 
ATOM   16572 C  C     . LYS A 1 3819 ? 170.075 141.988 171.165 1.00 20.83  ? 3819 LYS A C     1 
ATOM   16573 O  O     . LYS A 1 3819 ? 169.978 143.218 171.101 1.00 24.88  ? 3819 LYS A O     1 
ATOM   16574 C  CB    . LYS A 1 3819 ? 167.801 141.319 171.935 1.00 17.68  ? 3819 LYS A CB    1 
ATOM   16575 C  CG    . LYS A 1 3819 ? 168.335 141.158 173.347 1.00 19.98  ? 3819 LYS A CG    1 
ATOM   16576 C  CD    . LYS A 1 3819 ? 167.271 141.480 174.380 1.00 23.21  ? 3819 LYS A CD    1 
ATOM   16577 C  CE    . LYS A 1 3819 ? 166.518 140.231 174.800 1.00 23.67  ? 3819 LYS A CE    1 
ATOM   16578 N  NZ    . LYS A 1 3819 ? 167.307 139.408 175.756 1.00 27.00  ? 3819 LYS A NZ    1 
ATOM   16579 N  N     . GLN A 1 3820 ? 171.210 141.374 171.508 1.00 23.52  ? 3820 GLN A N     1 
ATOM   16580 C  CA    . GLN A 1 3820 ? 172.403 142.149 171.827 1.00 25.45  ? 3820 GLN A CA    1 
ATOM   16581 C  C     . GLN A 1 3820 ? 173.025 142.769 170.583 1.00 26.44  ? 3820 GLN A C     1 
ATOM   16582 O  O     . GLN A 1 3820 ? 173.624 143.848 170.664 1.00 33.05  ? 3820 GLN A O     1 
ATOM   16583 C  CB    . GLN A 1 3820 ? 173.424 141.268 172.546 1.00 29.50  ? 3820 GLN A CB    1 
ATOM   16584 C  CG    . GLN A 1 3820 ? 172.889 140.590 173.796 1.00 29.02  ? 3820 GLN A CG    1 
ATOM   16585 C  CD    . GLN A 1 3820 ? 172.463 141.580 174.860 1.00 38.06  ? 3820 GLN A CD    1 
ATOM   16586 O  OE1   . GLN A 1 3820 ? 171.344 141.521 175.367 1.00 40.38  ? 3820 GLN A OE1   1 
ATOM   16587 N  NE2   . GLN A 1 3820 ? 173.357 142.499 175.204 1.00 47.43  ? 3820 GLN A NE2   1 
ATOM   16588 N  N     . ILE A 1 3821 ? 172.898 142.110 169.427 1.00 21.75  ? 3821 ILE A N     1 
ATOM   16589 C  CA    . ILE A 1 3821 ? 173.507 142.615 168.198 1.00 24.94  ? 3821 ILE A CA    1 
ATOM   16590 C  C     . ILE A 1 3821 ? 172.575 143.500 167.385 1.00 24.46  ? 3821 ILE A C     1 
ATOM   16591 O  O     . ILE A 1 3821 ? 173.030 144.138 166.423 1.00 27.24  ? 3821 ILE A O     1 
ATOM   16592 C  CB    . ILE A 1 3821 ? 174.006 141.455 167.314 1.00 23.49  ? 3821 ILE A CB    1 
ATOM   16593 C  CG1   . ILE A 1 3821 ? 172.828 140.627 166.799 1.00 16.05  ? 3821 ILE A CG1   1 
ATOM   16594 C  CG2   . ILE A 1 3821 ? 174.989 140.593 168.080 1.00 25.72  ? 3821 ILE A CG2   1 
ATOM   16595 C  CD1   . ILE A 1 3821 ? 173.227 139.531 165.839 1.00 15.16  ? 3821 ILE A CD1   1 
ATOM   16596 N  N     . HIS A 1 3822 ? 171.292 143.566 167.736 1.00 19.30  ? 3822 HIS A N     1 
ATOM   16597 C  CA    . HIS A 1 3822 ? 170.350 144.431 167.041 1.00 16.30  ? 3822 HIS A CA    1 
ATOM   16598 C  C     . HIS A 1 3822 ? 169.092 144.557 167.883 1.00 16.87  ? 3822 HIS A C     1 
ATOM   16599 O  O     . HIS A 1 3822 ? 168.656 143.584 168.501 1.00 23.18  ? 3822 HIS A O     1 
ATOM   16600 C  CB    . HIS A 1 3822 ? 170.006 143.882 165.651 1.00 14.87  ? 3822 HIS A CB    1 
ATOM   16601 C  CG    . HIS A 1 3822 ? 169.638 144.938 164.656 1.00 15.62  ? 3822 HIS A CG    1 
ATOM   16602 N  ND1   . HIS A 1 3822 ? 168.373 145.478 164.576 1.00 17.92  ? 3822 HIS A ND1   1 
ATOM   16603 C  CD2   . HIS A 1 3822 ? 170.370 145.550 163.695 1.00 16.71  ? 3822 HIS A CD2   1 
ATOM   16604 C  CE1   . HIS A 1 3822 ? 168.342 146.379 163.611 1.00 17.54  ? 3822 HIS A CE1   1 
ATOM   16605 N  NE2   . HIS A 1 3822 ? 169.541 146.442 163.061 1.00 18.59  ? 3822 HIS A NE2   1 
ATOM   16606 N  N     . PHE A 1 3823 ? 168.515 145.761 167.900 1.00 16.46  ? 3823 PHE A N     1 
ATOM   16607 C  CA    . PHE A 1 3823 ? 167.303 145.999 168.674 1.00 17.88  ? 3823 PHE A CA    1 
ATOM   16608 C  C     . PHE A 1 3823 ? 166.099 145.254 168.115 1.00 16.27  ? 3823 PHE A C     1 
ATOM   16609 O  O     . PHE A 1 3823 ? 165.160 144.968 168.864 1.00 20.09  ? 3823 PHE A O     1 
ATOM   16610 C  CB    . PHE A 1 3823 ? 167.002 147.499 168.731 1.00 16.51  ? 3823 PHE A CB    1 
ATOM   16611 C  CG    . PHE A 1 3823 ? 166.861 148.143 167.379 1.00 17.13  ? 3823 PHE A CG    1 
ATOM   16612 C  CD1   . PHE A 1 3823 ? 165.634 148.177 166.736 1.00 17.55  ? 3823 PHE A CD1   1 
ATOM   16613 C  CD2   . PHE A 1 3823 ? 167.954 148.716 166.752 1.00 17.32  ? 3823 PHE A CD2   1 
ATOM   16614 C  CE1   . PHE A 1 3823 ? 165.502 148.766 165.496 1.00 16.95  ? 3823 PHE A CE1   1 
ATOM   16615 C  CE2   . PHE A 1 3823 ? 167.827 149.307 165.511 1.00 15.61  ? 3823 PHE A CE2   1 
ATOM   16616 C  CZ    . PHE A 1 3823 ? 166.599 149.332 164.883 1.00 17.56  ? 3823 PHE A CZ    1 
ATOM   16617 N  N     . LEU A 1 3824 ? 166.105 144.936 166.821 1.00 13.54  ? 3824 LEU A N     1 
ATOM   16618 C  CA    . LEU A 1 3824 ? 164.956 144.317 166.174 1.00 13.44  ? 3824 LEU A CA    1 
ATOM   16619 C  C     . LEU A 1 3824 ? 164.842 142.824 166.448 1.00 17.35  ? 3824 LEU A C     1 
ATOM   16620 O  O     . LEU A 1 3824 ? 163.804 142.234 166.133 1.00 20.49  ? 3824 LEU A O     1 
ATOM   16621 C  CB    . LEU A 1 3824 ? 165.021 144.554 164.663 1.00 12.93  ? 3824 LEU A CB    1 
ATOM   16622 C  CG    . LEU A 1 3824 ? 163.700 144.547 163.894 1.00 13.40  ? 3824 LEU A CG    1 
ATOM   16623 C  CD1   . LEU A 1 3824 ? 162.970 145.869 164.063 1.00 16.83  ? 3824 LEU A CD1   1 
ATOM   16624 C  CD2   . LEU A 1 3824 ? 163.943 144.250 162.425 1.00 14.43  ? 3824 LEU A CD2   1 
ATOM   16625 N  N     . TYR A 1 3825 ? 165.865 142.201 167.027 1.00 17.22  ? 3825 TYR A N     1 
ATOM   16626 C  CA    . TYR A 1 3825 ? 165.874 140.748 167.202 1.00 14.76  ? 3825 TYR A CA    1 
ATOM   16627 C  C     . TYR A 1 3825 ? 165.223 140.367 168.533 1.00 17.52  ? 3825 TYR A C     1 
ATOM   16628 O  O     . TYR A 1 3825 ? 165.844 139.805 169.435 1.00 20.56  ? 3825 TYR A O     1 
ATOM   16629 C  CB    . TYR A 1 3825 ? 167.296 140.209 167.100 1.00 13.28  ? 3825 TYR A CB    1 
ATOM   16630 C  CG    . TYR A 1 3825 ? 167.994 140.523 165.791 1.00 13.34  ? 3825 TYR A CG    1 
ATOM   16631 C  CD1   . TYR A 1 3825 ? 167.282 140.975 164.687 1.00 15.65  ? 3825 TYR A CD1   1 
ATOM   16632 C  CD2   . TYR A 1 3825 ? 169.365 140.356 165.658 1.00 14.00  ? 3825 TYR A CD2   1 
ATOM   16633 C  CE1   . TYR A 1 3825 ? 167.915 141.266 163.498 1.00 13.46  ? 3825 TYR A CE1   1 
ATOM   16634 C  CE2   . TYR A 1 3825 ? 170.006 140.638 164.468 1.00 13.92  ? 3825 TYR A CE2   1 
ATOM   16635 C  CZ    . TYR A 1 3825 ? 169.276 141.093 163.393 1.00 14.24  ? 3825 TYR A CZ    1 
ATOM   16636 O  OH    . TYR A 1 3825 ? 169.907 141.378 162.206 1.00 21.22  ? 3825 TYR A OH    1 
ATOM   16637 N  N     . GLN A 1 3826 ? 163.936 140.687 168.639 1.00 16.80  ? 3826 GLN A N     1 
ATOM   16638 C  CA    . GLN A 1 3826 ? 163.143 140.396 169.828 1.00 17.09  ? 3826 GLN A CA    1 
ATOM   16639 C  C     . GLN A 1 3826 ? 162.298 139.157 169.555 1.00 19.98  ? 3826 GLN A C     1 
ATOM   16640 O  O     . GLN A 1 3826 ? 161.369 139.198 168.743 1.00 18.79  ? 3826 GLN A O     1 
ATOM   16641 C  CB    . GLN A 1 3826 ? 162.265 141.588 170.202 1.00 16.44  ? 3826 GLN A CB    1 
ATOM   16642 C  CG    . GLN A 1 3826 ? 163.014 142.904 170.309 1.00 16.58  ? 3826 GLN A CG    1 
ATOM   16643 C  CD    . GLN A 1 3826 ? 163.992 142.925 171.464 1.00 19.19  ? 3826 GLN A CD    1 
ATOM   16644 O  OE1   . GLN A 1 3826 ? 163.751 142.319 172.507 1.00 25.18  ? 3826 GLN A OE1   1 
ATOM   16645 N  NE2   . GLN A 1 3826 ? 165.105 143.626 171.284 1.00 14.63  ? 3826 GLN A NE2   1 
ATOM   16646 N  N     . TYR A 1 3827 ? 162.622 138.060 170.234 1.00 21.89  ? 3827 TYR A N     1 
ATOM   16647 C  CA    . TYR A 1 3827 ? 161.913 136.798 170.084 1.00 21.52  ? 3827 TYR A CA    1 
ATOM   16648 C  C     . TYR A 1 3827 ? 161.429 136.334 171.449 1.00 27.76  ? 3827 TYR A C     1 
ATOM   16649 O  O     . TYR A 1 3827 ? 162.189 136.360 172.423 1.00 32.01  ? 3827 TYR A O     1 
ATOM   16650 C  CB    . TYR A 1 3827 ? 162.809 135.735 169.444 1.00 19.71  ? 3827 TYR A CB    1 
ATOM   16651 C  CG    . TYR A 1 3827 ? 163.441 136.181 168.147 1.00 19.57  ? 3827 TYR A CG    1 
ATOM   16652 C  CD1   . TYR A 1 3827 ? 162.675 136.360 167.005 1.00 21.29  ? 3827 TYR A CD1   1 
ATOM   16653 C  CD2   . TYR A 1 3827 ? 164.804 136.430 168.066 1.00 17.85  ? 3827 TYR A CD2   1 
ATOM   16654 C  CE1   . TYR A 1 3827 ? 163.247 136.771 165.818 1.00 21.46  ? 3827 TYR A CE1   1 
ATOM   16655 C  CE2   . TYR A 1 3827 ? 165.385 136.842 166.884 1.00 16.44  ? 3827 TYR A CE2   1 
ATOM   16656 C  CZ    . TYR A 1 3827 ? 164.602 137.011 165.763 1.00 20.39  ? 3827 TYR A CZ    1 
ATOM   16657 O  OH    . TYR A 1 3827 ? 165.176 137.421 164.583 1.00 22.85  ? 3827 TYR A OH    1 
ATOM   16658 N  N     . SER A 1 3828 ? 160.172 135.913 171.516 1.00 27.39  ? 3828 SER A N     1 
ATOM   16659 C  CA    . SER A 1 3828 ? 159.581 135.450 172.759 1.00 26.99  ? 3828 SER A CA    1 
ATOM   16660 C  C     . SER A 1 3828 ? 159.728 133.937 172.892 1.00 27.71  ? 3828 SER A C     1 
ATOM   16661 O  O     . SER A 1 3828 ? 160.168 133.242 171.974 1.00 36.63  ? 3828 SER A O     1 
ATOM   16662 C  CB    . SER A 1 3828 ? 158.108 135.851 172.831 1.00 31.24  ? 3828 SER A CB    1 
ATOM   16663 O  OG    . SER A 1 3828 ? 157.418 135.463 171.656 1.00 31.34  ? 3828 SER A OG    1 
ATOM   16664 N  N     . LEU A 1 3829 ? 159.356 133.427 174.068 1.00 29.18  ? 3829 LEU A N     1 
ATOM   16665 C  CA    . LEU A 1 3829 ? 159.364 131.984 174.281 1.00 24.85  ? 3829 LEU A CA    1 
ATOM   16666 C  C     . LEU A 1 3829 ? 158.337 131.295 173.393 1.00 26.69  ? 3829 LEU A C     1 
ATOM   16667 O  O     . LEU A 1 3829 ? 158.561 130.168 172.934 1.00 35.85  ? 3829 LEU A O     1 
ATOM   16668 C  CB    . LEU A 1 3829 ? 159.101 131.669 175.753 1.00 24.81  ? 3829 LEU A CB    1 
ATOM   16669 C  CG    . LEU A 1 3829 ? 159.149 130.192 176.147 1.00 18.90  ? 3829 LEU A CG    1 
ATOM   16670 C  CD1   . LEU A 1 3829 ? 160.560 129.652 176.004 1.00 19.91  ? 3829 LEU A CD1   1 
ATOM   16671 C  CD2   . LEU A 1 3829 ? 158.638 129.996 177.563 1.00 23.75  ? 3829 LEU A CD2   1 
ATOM   16672 N  N     . GLN A 1 3830 ? 157.205 131.957 173.140 1.00 21.83  ? 3830 GLN A N     1 
ATOM   16673 C  CA    . GLN A 1 3830 ? 156.175 131.363 172.297 1.00 25.43  ? 3830 GLN A CA    1 
ATOM   16674 C  C     . GLN A 1 3830 ? 156.660 131.164 170.868 1.00 27.96  ? 3830 GLN A C     1 
ATOM   16675 O  O     . GLN A 1 3830 ? 156.219 130.231 170.194 1.00 33.99  ? 3830 GLN A O     1 
ATOM   16676 C  CB    . GLN A 1 3830 ? 154.914 132.225 172.316 1.00 30.02  ? 3830 GLN A CB    1 
ATOM   16677 C  CG    . GLN A 1 3830 ? 153.668 131.498 171.835 1.00 34.01  ? 3830 GLN A CG    1 
ATOM   16678 C  CD    . GLN A 1 3830 ? 153.657 130.035 172.234 1.00 40.75  ? 3830 GLN A CD    1 
ATOM   16679 O  OE1   . GLN A 1 3830 ? 153.620 129.701 173.419 1.00 38.30  ? 3830 GLN A OE1   1 
ATOM   16680 N  NE2   . GLN A 1 3830 ? 153.694 129.152 171.243 1.00 40.49  ? 3830 GLN A NE2   1 
ATOM   16681 N  N     . PHE A 1 3831 ? 157.565 132.019 170.391 1.00 24.88  ? 3831 PHE A N     1 
ATOM   16682 C  CA    . PHE A 1 3831 ? 158.135 131.829 169.059 1.00 22.71  ? 3831 PHE A CA    1 
ATOM   16683 C  C     . PHE A 1 3831 ? 158.906 130.515 168.978 1.00 24.91  ? 3831 PHE A C     1 
ATOM   16684 O  O     . PHE A 1 3831 ? 158.723 129.723 168.043 1.00 31.79  ? 3831 PHE A O     1 
ATOM   16685 C  CB    . PHE A 1 3831 ? 159.038 133.016 168.717 1.00 23.60  ? 3831 PHE A CB    1 
ATOM   16686 C  CG    . PHE A 1 3831 ? 159.543 133.013 167.304 1.00 27.94  ? 3831 PHE A CG    1 
ATOM   16687 C  CD1   . PHE A 1 3831 ? 158.662 133.008 166.237 1.00 29.89  ? 3831 PHE A CD1   1 
ATOM   16688 C  CD2   . PHE A 1 3831 ? 160.903 133.033 167.042 1.00 23.49  ? 3831 PHE A CD2   1 
ATOM   16689 C  CE1   . PHE A 1 3831 ? 159.127 133.012 164.936 1.00 29.44  ? 3831 PHE A CE1   1 
ATOM   16690 C  CE2   . PHE A 1 3831 ? 161.374 133.037 165.745 1.00 21.34  ? 3831 PHE A CE2   1 
ATOM   16691 C  CZ    . PHE A 1 3831 ? 160.485 133.026 164.691 1.00 25.23  ? 3831 PHE A CZ    1 
ATOM   16692 N  N     . PHE A 1 3832 ? 159.760 130.256 169.970 1.00 22.32  ? 3832 PHE A N     1 
ATOM   16693 C  CA    . PHE A 1 3832 ? 160.508 129.005 169.982 1.00 21.75  ? 3832 PHE A CA    1 
ATOM   16694 C  C     . PHE A 1 3832 ? 159.586 127.814 170.193 1.00 23.33  ? 3832 PHE A C     1 
ATOM   16695 O  O     . PHE A 1 3832 ? 159.817 126.738 169.632 1.00 25.90  ? 3832 PHE A O     1 
ATOM   16696 C  CB    . PHE A 1 3832 ? 161.585 129.033 171.062 1.00 17.86  ? 3832 PHE A CB    1 
ATOM   16697 C  CG    . PHE A 1 3832 ? 162.312 127.733 171.206 1.00 20.25  ? 3832 PHE A CG    1 
ATOM   16698 C  CD1   . PHE A 1 3832 ? 163.205 127.320 170.233 1.00 19.21  ? 3832 PHE A CD1   1 
ATOM   16699 C  CD2   . PHE A 1 3832 ? 162.089 126.913 172.297 1.00 21.71  ? 3832 PHE A CD2   1 
ATOM   16700 C  CE1   . PHE A 1 3832 ? 163.871 126.123 170.350 1.00 17.56  ? 3832 PHE A CE1   1 
ATOM   16701 C  CE2   . PHE A 1 3832 ? 162.754 125.712 172.419 1.00 22.90  ? 3832 PHE A CE2   1 
ATOM   16702 C  CZ    . PHE A 1 3832 ? 163.644 125.318 171.443 1.00 20.01  ? 3832 PHE A CZ    1 
ATOM   16703 N  N     . LEU A 1 3833 ? 158.546 127.976 171.014 1.00 22.96  ? 3833 LEU A N     1 
ATOM   16704 C  CA    . LEU A 1 3833 ? 157.594 126.888 171.207 1.00 19.76  ? 3833 LEU A CA    1 
ATOM   16705 C  C     . LEU A 1 3833 ? 156.844 126.577 169.918 1.00 25.70  ? 3833 LEU A C     1 
ATOM   16706 O  O     . LEU A 1 3833 ? 156.559 125.412 169.627 1.00 35.60  ? 3833 LEU A O     1 
ATOM   16707 C  CB    . LEU A 1 3833 ? 156.623 127.230 172.335 1.00 25.29  ? 3833 LEU A CB    1 
ATOM   16708 C  CG    . LEU A 1 3833 ? 157.240 127.313 173.733 1.00 25.24  ? 3833 LEU A CG    1 
ATOM   16709 C  CD1   . LEU A 1 3833 ? 156.158 127.405 174.796 1.00 33.50  ? 3833 LEU A CD1   1 
ATOM   16710 C  CD2   . LEU A 1 3833 ? 158.151 126.123 173.992 1.00 23.40  ? 3833 LEU A CD2   1 
ATOM   16711 N  N     . ASP A 1 3834 ? 156.517 127.606 169.133 1.00 25.25  ? 3834 ASP A N     1 
ATOM   16712 C  CA    . ASP A 1 3834 ? 155.898 127.384 167.830 1.00 25.19  ? 3834 ASP A CA    1 
ATOM   16713 C  C     . ASP A 1 3834 ? 156.849 126.663 166.886 1.00 27.06  ? 3834 ASP A C     1 
ATOM   16714 O  O     . ASP A 1 3834 ? 156.433 125.772 166.135 1.00 29.11  ? 3834 ASP A O     1 
ATOM   16715 C  CB    . ASP A 1 3834 ? 155.453 128.716 167.228 1.00 29.08  ? 3834 ASP A CB    1 
ATOM   16716 C  CG    . ASP A 1 3834 ? 154.277 129.324 167.964 1.00 40.23  ? 3834 ASP A CG    1 
ATOM   16717 O  OD1   . ASP A 1 3834 ? 153.721 128.651 168.858 1.00 35.55  ? 3834 ASP A OD1   1 
ATOM   16718 O  OD2   . ASP A 1 3834 ? 153.910 130.476 167.652 1.00 41.24  ? 3834 ASP A OD2   1 
ATOM   16719 N  N     . ILE A 1 3835 ? 158.130 127.038 166.904 1.00 26.26  ? 3835 ILE A N     1 
ATOM   16720 C  CA    . ILE A 1 3835 ? 159.122 126.332 166.092 1.00 22.13  ? 3835 ILE A CA    1 
ATOM   16721 C  C     . ILE A 1 3835 ? 159.188 124.863 166.498 1.00 24.50  ? 3835 ILE A C     1 
ATOM   16722 O  O     . ILE A 1 3835 ? 159.207 123.959 165.653 1.00 29.65  ? 3835 ILE A O     1 
ATOM   16723 C  CB    . ILE A 1 3835 ? 160.498 127.012 166.215 1.00 19.31  ? 3835 ILE A CB    1 
ATOM   16724 C  CG1   . ILE A 1 3835 ? 160.505 128.349 165.474 1.00 20.52  ? 3835 ILE A CG1   1 
ATOM   16725 C  CG2   . ILE A 1 3835 ? 161.597 126.102 165.691 1.00 17.59  ? 3835 ILE A CG2   1 
ATOM   16726 C  CD1   . ILE A 1 3835 ? 161.782 129.137 165.659 1.00 16.55  ? 3835 ILE A CD1   1 
ATOM   16727 N  N     . TYR A 1 3836 ? 159.214 124.608 167.806 1.00 26.34  ? 3836 TYR A N     1 
ATOM   16728 C  CA    . TYR A 1 3836 ? 159.301 123.242 168.310 1.00 23.99  ? 3836 TYR A CA    1 
ATOM   16729 C  C     . TYR A 1 3836 ? 158.056 122.438 167.955 1.00 27.96  ? 3836 TYR A C     1 
ATOM   16730 O  O     . TYR A 1 3836 ? 158.145 121.246 167.642 1.00 34.96  ? 3836 TYR A O     1 
ATOM   16731 C  CB    . TYR A 1 3836 ? 159.521 123.274 169.822 1.00 25.78  ? 3836 TYR A CB    1 
ATOM   16732 C  CG    . TYR A 1 3836 ? 160.015 121.978 170.413 1.00 28.45  ? 3836 TYR A CG    1 
ATOM   16733 C  CD1   . TYR A 1 3836 ? 161.028 121.258 169.800 1.00 31.27  ? 3836 TYR A CD1   1 
ATOM   16734 C  CD2   . TYR A 1 3836 ? 159.493 121.493 171.603 1.00 32.94  ? 3836 TYR A CD2   1 
ATOM   16735 C  CE1   . TYR A 1 3836 ? 161.488 120.078 170.339 1.00 31.06  ? 3836 TYR A CE1   1 
ATOM   16736 C  CE2   . TYR A 1 3836 ? 159.952 120.316 172.154 1.00 31.59  ? 3836 TYR A CE2   1 
ATOM   16737 C  CZ    . TYR A 1 3836 ? 160.950 119.614 171.517 1.00 28.02  ? 3836 TYR A CZ    1 
ATOM   16738 O  OH    . TYR A 1 3836 ? 161.414 118.442 172.059 1.00 32.50  ? 3836 TYR A OH    1 
ATOM   16739 N  N     . HIS A 1 3837 ? 156.883 123.072 168.015 1.00 27.61  ? 3837 HIS A N     1 
ATOM   16740 C  CA    . HIS A 1 3837 ? 155.647 122.409 167.612 1.00 31.70  ? 3837 HIS A CA    1 
ATOM   16741 C  C     . HIS A 1 3837 ? 155.659 122.079 166.125 1.00 37.03  ? 3837 HIS A C     1 
ATOM   16742 O  O     . HIS A 1 3837 ? 155.248 120.986 165.720 1.00 39.65  ? 3837 HIS A O     1 
ATOM   16743 C  CB    . HIS A 1 3837 ? 154.451 123.297 167.957 1.00 37.02  ? 3837 HIS A CB    1 
ATOM   16744 C  CG    . HIS A 1 3837 ? 153.138 122.579 167.952 1.00 48.76  ? 3837 HIS A CG    1 
ATOM   16745 N  ND1   . HIS A 1 3837 ? 152.320 122.532 166.843 1.00 52.66  ? 3837 HIS A ND1   1 
ATOM   16746 C  CD2   . HIS A 1 3837 ? 152.490 121.896 168.925 1.00 50.44  ? 3837 HIS A CD2   1 
ATOM   16747 C  CE1   . HIS A 1 3837 ? 151.231 121.842 167.130 1.00 53.51  ? 3837 HIS A CE1   1 
ATOM   16748 N  NE2   . HIS A 1 3837 ? 151.309 121.446 168.388 1.00 51.63  ? 3837 HIS A NE2   1 
ATOM   16749 N  N     . ASN A 1 3838 ? 156.125 123.016 165.295 1.00 37.62  ? 3838 ASN A N     1 
ATOM   16750 C  CA    . ASN A 1 3838 ? 156.224 122.774 163.861 1.00 37.37  ? 3838 ASN A CA    1 
ATOM   16751 C  C     . ASN A 1 3838 ? 157.267 121.718 163.526 1.00 36.22  ? 3838 ASN A C     1 
ATOM   16752 O  O     . ASN A 1 3838 ? 157.210 121.128 162.443 1.00 46.67  ? 3838 ASN A O     1 
ATOM   16753 C  CB    . ASN A 1 3838 ? 156.551 124.077 163.132 1.00 36.88  ? 3838 ASN A CB    1 
ATOM   16754 C  CG    . ASN A 1 3838 ? 156.437 123.949 161.627 1.00 41.90  ? 3838 ASN A CG    1 
ATOM   16755 O  OD1   . ASN A 1 3838 ? 157.441 123.840 160.924 1.00 37.38  ? 3838 ASN A OD1   1 
ATOM   16756 N  ND2   . ASN A 1 3838 ? 155.209 123.964 161.123 1.00 51.13  ? 3838 ASN A ND2   1 
ATOM   16757 N  N     . VAL A 1 3839 ? 158.230 121.488 164.415 1.00 30.94  ? 3839 VAL A N     1 
ATOM   16758 C  CA    . VAL A 1 3839 ? 159.214 120.437 164.175 1.00 29.09  ? 3839 VAL A CA    1 
ATOM   16759 C  C     . VAL A 1 3839 ? 158.673 119.079 164.612 1.00 32.53  ? 3839 VAL A C     1 
ATOM   16760 O  O     . VAL A 1 3839 ? 158.731 118.101 163.858 1.00 37.84  ? 3839 VAL A O     1 
ATOM   16761 C  CB    . VAL A 1 3839 ? 160.538 120.776 164.883 1.00 26.90  ? 3839 VAL A CB    1 
ATOM   16762 C  CG1   . VAL A 1 3839 ? 161.411 119.539 165.000 1.00 27.95  ? 3839 VAL A CG1   1 
ATOM   16763 C  CG2   . VAL A 1 3839 ? 161.263 121.876 164.131 1.00 24.61  ? 3839 VAL A CG2   1 
ATOM   16764 N  N     . LEU A 1 3840 ? 158.143 118.996 165.835 1.00 33.57  ? 3840 LEU A N     1 
ATOM   16765 C  CA    . LEU A 1 3840 ? 157.618 117.728 166.338 1.00 27.93  ? 3840 LEU A CA    1 
ATOM   16766 C  C     . LEU A 1 3840 ? 156.409 117.270 165.532 1.00 35.73  ? 3840 LEU A C     1 
ATOM   16767 O  O     . LEU A 1 3840 ? 156.367 116.134 165.046 1.00 37.89  ? 3840 LEU A O     1 
ATOM   16768 C  CB    . LEU A 1 3840 ? 157.250 117.863 167.815 1.00 25.62  ? 3840 LEU A CB    1 
ATOM   16769 C  CG    . LEU A 1 3840 ? 158.391 118.064 168.811 1.00 23.53  ? 3840 LEU A CG    1 
ATOM   16770 C  CD1   . LEU A 1 3840 ? 157.833 118.235 170.212 1.00 30.43  ? 3840 LEU A CD1   1 
ATOM   16771 C  CD2   . LEU A 1 3840 ? 159.360 116.898 168.757 1.00 28.25  ? 3840 LEU A CD2   1 
ATOM   16772 N  N     . TYR A 1 3841 ? 155.418 118.141 165.381 1.00 40.06  ? 3841 TYR A N     1 
ATOM   16773 C  CA    . TYR A 1 3841 ? 154.229 117.869 164.590 1.00 39.15  ? 3841 TYR A CA    1 
ATOM   16774 C  C     . TYR A 1 3841 ? 154.333 118.588 163.252 1.00 47.67  ? 3841 TYR A C     1 
ATOM   16775 O  O     . TYR A 1 3841 ? 155.269 119.353 163.012 1.00 53.81  ? 3841 TYR A O     1 
ATOM   16776 C  CB    . TYR A 1 3841 ? 152.963 118.307 165.331 1.00 41.52  ? 3841 TYR A CB    1 
ATOM   16777 C  CG    . TYR A 1 3841 ? 152.885 117.805 166.755 1.00 46.49  ? 3841 TYR A CG    1 
ATOM   16778 C  CD1   . TYR A 1 3841 ? 152.974 116.450 167.039 1.00 49.49  ? 3841 TYR A CD1   1 
ATOM   16779 C  CD2   . TYR A 1 3841 ? 152.737 118.687 167.815 1.00 42.78  ? 3841 TYR A CD2   1 
ATOM   16780 C  CE1   . TYR A 1 3841 ? 152.905 115.987 168.338 1.00 48.51  ? 3841 TYR A CE1   1 
ATOM   16781 C  CE2   . TYR A 1 3841 ? 152.670 118.234 169.117 1.00 45.23  ? 3841 TYR A CE2   1 
ATOM   16782 C  CZ    . TYR A 1 3841 ? 152.755 116.884 169.373 1.00 51.36  ? 3841 TYR A CZ    1 
ATOM   16783 O  OH    . TYR A 1 3841 ? 152.688 116.431 170.670 1.00 56.62  ? 3841 TYR A OH    1 
ATOM   16784 N  N     . GLU A 1 3842 ? 153.348 118.328 162.386 1.00 51.31  ? 3842 GLU A N     1 
ATOM   16785 C  CA    . GLU A 1 3842 ? 153.282 118.868 161.020 1.00 56.49  ? 3842 GLU A CA    1 
ATOM   16786 C  C     . GLU A 1 3842 ? 154.652 118.898 160.344 1.00 55.60  ? 3842 GLU A C     1 
ATOM   16787 O  O     . GLU A 1 3842 ? 155.012 119.876 159.685 1.00 58.41  ? 3842 GLU A O     1 
ATOM   16788 C  CB    . GLU A 1 3842 ? 152.627 120.258 160.979 1.00 54.54  ? 3842 GLU A CB    1 
ATOM   16789 C  CG    . GLU A 1 3842 ? 153.181 121.307 161.935 1.00 50.91  ? 3842 GLU A CG    1 
ATOM   16790 C  CD    . GLU A 1 3842 ? 152.255 122.495 162.099 1.00 62.55  ? 3842 GLU A CD    1 
ATOM   16791 O  OE1   . GLU A 1 3842 ? 152.255 123.104 163.190 1.00 54.08  ? 3842 GLU A OE1   1 
ATOM   16792 O  OE2   . GLU A 1 3842 ? 151.528 122.822 161.139 1.00 79.42  ? 3842 GLU A OE2   1 
ATOM   16793 N  N     . ASN A 1 3843 ? 155.427 117.824 160.505 1.00 49.61  ? 3843 ASN A N     1 
ATOM   16794 C  CA    . ASN A 1 3843 ? 156.736 117.712 159.883 1.00 49.16  ? 3843 ASN A CA    1 
ATOM   16795 C  C     . ASN A 1 3843 ? 156.628 116.812 158.663 1.00 53.98  ? 3843 ASN A C     1 
ATOM   16796 O  O     . ASN A 1 3843 ? 156.288 115.628 158.809 1.00 60.66  ? 3843 ASN A O     1 
ATOM   16797 C  CB    . ASN A 1 3843 ? 157.758 117.153 160.870 1.00 44.41  ? 3843 ASN A CB    1 
ATOM   16798 C  CG    . ASN A 1 3843 ? 159.167 117.632 160.584 1.00 42.60  ? 3843 ASN A CG    1 
ATOM   16799 O  OD1   . ASN A 1 3843 ? 159.388 118.450 159.692 1.00 46.82  ? 3843 ASN A OD1   1 
ATOM   16800 N  ND2   . ASN A 1 3843 ? 160.130 117.123 161.343 1.00 39.19  ? 3843 ASN A ND2   1 
ATOM   16801 N  N     . PRO A 1 3844 ? 156.887 117.315 157.453 1.00 51.29  ? 3844 PRO A N     1 
ATOM   16802 C  CA    . PRO A 1 3844 ? 156.767 116.456 156.263 1.00 56.47  ? 3844 PRO A CA    1 
ATOM   16803 C  C     . PRO A 1 3844 ? 157.692 115.252 156.281 1.00 54.27  ? 3844 PRO A C     1 
ATOM   16804 O  O     . PRO A 1 3844 ? 157.330 114.198 155.744 1.00 59.01  ? 3844 PRO A O     1 
ATOM   16805 C  CB    . PRO A 1 3844 ? 157.108 117.409 155.107 1.00 63.67  ? 3844 PRO A CB    1 
ATOM   16806 C  CG    . PRO A 1 3844 ? 156.906 118.785 155.663 1.00 55.82  ? 3844 PRO A CG    1 
ATOM   16807 C  CD    . PRO A 1 3844 ? 157.268 118.693 157.109 1.00 52.51  ? 3844 PRO A CD    1 
ATOM   16808 N  N     . ASN A 1 3845 ? 158.877 115.372 156.883 1.00 48.03  ? 3845 ASN A N     1 
ATOM   16809 C  CA    . ASN A 1 3845 ? 159.840 114.278 156.887 1.00 46.62  ? 3845 ASN A CA    1 
ATOM   16810 C  C     . ASN A 1 3845 ? 159.422 113.115 157.777 1.00 53.40  ? 3845 ASN A C     1 
ATOM   16811 O  O     . ASN A 1 3845 ? 160.044 112.050 157.702 1.00 60.62  ? 3845 ASN A O     1 
ATOM   16812 C  CB    . ASN A 1 3845 ? 161.212 114.793 157.326 1.00 48.00  ? 3845 ASN A CB    1 
ATOM   16813 C  CG    . ASN A 1 3845 ? 161.668 115.993 156.521 1.00 58.38  ? 3845 ASN A CG    1 
ATOM   16814 O  OD1   . ASN A 1 3845 ? 160.976 117.009 156.453 1.00 59.76  ? 3845 ASN A OD1   1 
ATOM   16815 N  ND2   . ASN A 1 3845 ? 162.840 115.883 155.907 1.00 61.05  ? 3845 ASN A ND2   1 
ATOM   16816 N  N     . LEU A 1 3846 ? 158.398 113.286 158.610 1.00 52.18  ? 3846 LEU A N     1 
ATOM   16817 C  CA    . LEU A 1 3846 ? 157.934 112.240 159.511 1.00 52.39  ? 3846 LEU A CA    1 
ATOM   16818 C  C     . LEU A 1 3846 ? 156.653 111.573 159.025 1.00 60.36  ? 3846 LEU A C     1 
ATOM   16819 O  O     . LEU A 1 3846 ? 155.946 110.956 159.828 1.00 66.24  ? 3846 LEU A O     1 
ATOM   16820 C  CB    . LEU A 1 3846 ? 157.722 112.813 160.913 1.00 47.45  ? 3846 LEU A CB    1 
ATOM   16821 C  CG    . LEU A 1 3846 ? 158.964 113.326 161.642 1.00 42.83  ? 3846 LEU A CG    1 
ATOM   16822 C  CD1   . LEU A 1 3846 ? 158.580 113.938 162.979 1.00 36.20  ? 3846 LEU A CD1   1 
ATOM   16823 C  CD2   . LEU A 1 3846 ? 159.977 112.210 161.831 1.00 42.39  ? 3846 LEU A CD2   1 
ATOM   16824 N  N     . LYS A 1 3847 ? 156.336 111.689 157.734 1.00 61.60  ? 3847 LYS A N     1 
ATOM   16825 C  CA    . LYS A 1 3847 ? 155.064 111.179 157.232 1.00 68.84  ? 3847 LYS A CA    1 
ATOM   16826 C  C     . LYS A 1 3847 ? 154.994 109.658 157.309 1.00 75.13  ? 3847 LYS A C     1 
ATOM   16827 O  O     . LYS A 1 3847 ? 153.979 109.098 157.739 1.00 78.77  ? 3847 LYS A O     1 
ATOM   16828 C  CB    . LYS A 1 3847 ? 154.842 111.653 155.796 1.00 72.55  ? 3847 LYS A CB    1 
ATOM   16829 C  CG    . LYS A 1 3847 ? 153.494 111.260 155.216 1.00 79.56  ? 3847 LYS A CG    1 
ATOM   16830 C  CD    . LYS A 1 3847 ? 153.046 112.245 154.151 1.00 86.36  ? 3847 LYS A CD    1 
ATOM   16831 C  CE    . LYS A 1 3847 ? 152.257 113.391 154.761 1.00 82.90  ? 3847 LYS A CE    1 
ATOM   16832 N  NZ    . LYS A 1 3847 ? 151.237 112.903 155.730 1.00 83.05  ? 3847 LYS A NZ    1 
ATOM   16833 N  N     . GLY A 1 3848 ? 156.059 108.972 156.899 1.00 65.60  ? 3848 GLY A N     1 
ATOM   16834 C  CA    . GLY A 1 3848 ? 156.031 107.523 156.842 1.00 61.26  ? 3848 GLY A CA    1 
ATOM   16835 C  C     . GLY A 1 3848 ? 157.195 106.849 157.537 1.00 63.45  ? 3848 GLY A C     1 
ATOM   16836 O  O     . GLY A 1 3848 ? 157.551 105.714 157.204 1.00 64.00  ? 3848 GLY A O     1 
ATOM   16837 N  N     . VAL A 1 3849 ? 157.797 107.534 158.503 1.00 64.94  ? 3849 VAL A N     1 
ATOM   16838 C  CA    . VAL A 1 3849 ? 158.944 107.018 159.241 1.00 60.29  ? 3849 VAL A CA    1 
ATOM   16839 C  C     . VAL A 1 3849 ? 158.465 106.536 160.603 1.00 60.20  ? 3849 VAL A C     1 
ATOM   16840 O  O     . VAL A 1 3849 ? 157.798 107.280 161.334 1.00 57.80  ? 3849 VAL A O     1 
ATOM   16841 C  CB    . VAL A 1 3849 ? 160.038 108.089 159.384 1.00 51.79  ? 3849 VAL A CB    1 
ATOM   16842 C  CG1   . VAL A 1 3849 ? 161.146 107.588 160.277 1.00 50.30  ? 3849 VAL A CG1   1 
ATOM   16843 C  CG2   . VAL A 1 3849 ? 160.583 108.474 158.018 1.00 53.83  ? 3849 VAL A CG2   1 
ATOM   16844 N  N     . THR A 1 3850 ? 158.802 105.290 160.947 1.00 62.28  ? 3850 THR A N     1 
ATOM   16845 C  CA    . THR A 1 3850 ? 158.320 104.670 162.173 1.00 61.24  ? 3850 THR A CA    1 
ATOM   16846 C  C     . THR A 1 3850 ? 159.403 104.372 163.202 1.00 64.16  ? 3850 THR A C     1 
ATOM   16847 O  O     . THR A 1 3850 ? 159.077 104.262 164.388 1.00 62.99  ? 3850 THR A O     1 
ATOM   16848 C  CB    . THR A 1 3850 ? 157.581 103.358 161.859 1.00 61.76  ? 3850 THR A CB    1 
ATOM   16849 O  OG1   . THR A 1 3850 ? 158.533 102.330 161.558 1.00 65.79  ? 3850 THR A OG1   1 
ATOM   16850 C  CG2   . THR A 1 3850 ? 156.647 103.541 160.674 1.00 59.40  ? 3850 THR A CG2   1 
ATOM   16851 N  N     . ASP A 1 3851 ? 160.662 104.233 162.794 1.00 64.16  ? 3851 ASP A N     1 
ATOM   16852 C  CA    . ASP A 1 3851 ? 161.726 103.943 163.747 1.00 62.69  ? 3851 ASP A CA    1 
ATOM   16853 C  C     . ASP A 1 3851 ? 161.941 105.132 164.674 1.00 60.81  ? 3851 ASP A C     1 
ATOM   16854 O  O     . ASP A 1 3851 ? 162.030 106.277 164.222 1.00 61.21  ? 3851 ASP A O     1 
ATOM   16855 C  CB    . ASP A 1 3851 ? 163.020 103.600 163.012 1.00 64.64  ? 3851 ASP A CB    1 
ATOM   16856 C  CG    . ASP A 1 3851 ? 164.065 102.988 163.925 1.00 69.52  ? 3851 ASP A CG    1 
ATOM   16857 O  OD1   . ASP A 1 3851 ? 163.723 102.642 165.076 1.00 68.39  ? 3851 ASP A OD1   1 
ATOM   16858 O  OD2   . ASP A 1 3851 ? 165.229 102.853 163.494 1.00 69.55  ? 3851 ASP A OD2   1 
ATOM   16859 N  N     . HIS A 1 3852 ? 162.030 104.857 165.978 1.00 58.55  ? 3852 HIS A N     1 
ATOM   16860 C  CA    . HIS A 1 3852 ? 162.111 105.935 166.960 1.00 57.04  ? 3852 HIS A CA    1 
ATOM   16861 C  C     . HIS A 1 3852 ? 163.440 106.678 166.878 1.00 50.12  ? 3852 HIS A C     1 
ATOM   16862 O  O     . HIS A 1 3852 ? 163.472 107.909 166.985 1.00 49.02  ? 3852 HIS A O     1 
ATOM   16863 C  CB    . HIS A 1 3852 ? 161.893 105.377 168.367 1.00 61.83  ? 3852 HIS A CB    1 
ATOM   16864 C  CG    . HIS A 1 3852 ? 160.469 105.022 168.661 1.00 58.95  ? 3852 HIS A CG    1 
ATOM   16865 N  ND1   . HIS A 1 3852 ? 160.094 103.786 169.141 1.00 52.80  ? 3852 HIS A ND1   1 
ATOM   16866 C  CD2   . HIS A 1 3852 ? 159.328 105.741 168.543 1.00 58.11  ? 3852 HIS A CD2   1 
ATOM   16867 C  CE1   . HIS A 1 3852 ? 158.783 103.759 169.306 1.00 54.93  ? 3852 HIS A CE1   1 
ATOM   16868 N  NE2   . HIS A 1 3852 ? 158.294 104.933 168.950 1.00 59.46  ? 3852 HIS A NE2   1 
ATOM   16869 N  N     . THR A 1 3853 ? 164.546 105.954 166.696 1.00 50.76  ? 3853 THR A N     1 
ATOM   16870 C  CA    . THR A 1 3853 ? 165.859 106.594 166.687 1.00 51.17  ? 3853 THR A CA    1 
ATOM   16871 C  C     . THR A 1 3853 ? 166.024 107.509 165.478 1.00 46.40  ? 3853 THR A C     1 
ATOM   16872 O  O     . THR A 1 3853 ? 166.477 108.655 165.607 1.00 43.79  ? 3853 THR A O     1 
ATOM   16873 C  CB    . THR A 1 3853 ? 166.960 105.532 166.710 1.00 54.54  ? 3853 THR A CB    1 
ATOM   16874 O  OG1   . THR A 1 3853 ? 166.836 104.739 167.898 1.00 57.15  ? 3853 THR A OG1   1 
ATOM   16875 C  CG2   . THR A 1 3853 ? 168.332 106.186 166.687 1.00 52.01  ? 3853 THR A CG2   1 
ATOM   16876 N  N     . GLN A 1 3854 ? 165.659 107.024 164.291 1.00 47.36  ? 3854 GLN A N     1 
ATOM   16877 C  CA    . GLN A 1 3854 ? 165.791 107.859 163.103 1.00 48.02  ? 3854 GLN A CA    1 
ATOM   16878 C  C     . GLN A 1 3854 ? 164.752 108.974 163.088 1.00 45.72  ? 3854 GLN A C     1 
ATOM   16879 O  O     . GLN A 1 3854 ? 165.018 110.054 162.550 1.00 47.23  ? 3854 GLN A O     1 
ATOM   16880 C  CB    . GLN A 1 3854 ? 165.711 106.998 161.841 1.00 47.22  ? 3854 GLN A CB    1 
ATOM   16881 C  CG    . GLN A 1 3854 ? 164.317 106.589 161.424 1.00 50.95  ? 3854 GLN A CG    1 
ATOM   16882 C  CD    . GLN A 1 3854 ? 164.270 106.063 160.003 1.00 63.04  ? 3854 GLN A CD    1 
ATOM   16883 O  OE1   . GLN A 1 3854 ? 164.779 106.696 159.078 1.00 63.23  ? 3854 GLN A OE1   1 
ATOM   16884 N  NE2   . GLN A 1 3854 ? 163.658 104.899 159.822 1.00 63.41  ? 3854 GLN A NE2   1 
ATOM   16885 N  N     . ARG A 1 3855 ? 163.583 108.751 163.697 1.00 41.46  ? 3855 ARG A N     1 
ATOM   16886 C  CA    . ARG A 1 3855 ? 162.637 109.847 163.887 1.00 36.78  ? 3855 ARG A CA    1 
ATOM   16887 C  C     . ARG A 1 3855 ? 163.232 110.929 164.777 1.00 35.46  ? 3855 ARG A C     1 
ATOM   16888 O  O     . ARG A 1 3855 ? 163.072 112.124 164.506 1.00 36.29  ? 3855 ARG A O     1 
ATOM   16889 C  CB    . ARG A 1 3855 ? 161.330 109.329 164.489 1.00 40.24  ? 3855 ARG A CB    1 
ATOM   16890 C  CG    . ARG A 1 3855 ? 160.297 108.899 163.466 1.00 48.72  ? 3855 ARG A CG    1 
ATOM   16891 C  CD    . ARG A 1 3855 ? 158.974 108.549 164.126 1.00 45.20  ? 3855 ARG A CD    1 
ATOM   16892 N  NE    . ARG A 1 3855 ? 158.340 109.714 164.731 1.00 39.66  ? 3855 ARG A NE    1 
ATOM   16893 C  CZ    . ARG A 1 3855 ? 157.275 110.328 164.235 1.00 47.06  ? 3855 ARG A CZ    1 
ATOM   16894 N  NH1   . ARG A 1 3855 ? 156.699 109.917 163.117 1.00 45.79  ? 3855 ARG A NH1   1 
ATOM   16895 N  NH2   . ARG A 1 3855 ? 156.776 111.381 164.876 1.00 47.40  ? 3855 ARG A NH2   1 
ATOM   16896 N  N     . LEU A 1 3856 ? 163.921 110.527 165.847 1.00 38.18  ? 3856 LEU A N     1 
ATOM   16897 C  CA    . LEU A 1 3856 ? 164.575 111.495 166.719 1.00 35.50  ? 3856 LEU A CA    1 
ATOM   16898 C  C     . LEU A 1 3856 ? 165.662 112.261 165.977 1.00 35.87  ? 3856 LEU A C     1 
ATOM   16899 O  O     . LEU A 1 3856 ? 165.799 113.478 166.145 1.00 35.97  ? 3856 LEU A O     1 
ATOM   16900 C  CB    . LEU A 1 3856 ? 165.159 110.788 167.942 1.00 36.15  ? 3856 LEU A CB    1 
ATOM   16901 C  CG    . LEU A 1 3856 ? 165.837 111.679 168.983 1.00 38.30  ? 3856 LEU A CG    1 
ATOM   16902 C  CD1   . LEU A 1 3856 ? 164.925 112.825 169.386 1.00 30.63  ? 3856 LEU A CD1   1 
ATOM   16903 C  CD2   . LEU A 1 3856 ? 166.250 110.863 170.195 1.00 40.82  ? 3856 LEU A CD2   1 
ATOM   16904 N  N     . SER A 1 3857 ? 166.452 111.563 165.159 1.00 36.46  ? 3857 SER A N     1 
ATOM   16905 C  CA    . SER A 1 3857 ? 167.489 112.239 164.381 1.00 37.03  ? 3857 SER A CA    1 
ATOM   16906 C  C     . SER A 1 3857 ? 166.882 113.231 163.394 1.00 33.49  ? 3857 SER A C     1 
ATOM   16907 O  O     . SER A 1 3857 ? 167.385 114.352 163.231 1.00 37.24  ? 3857 SER A O     1 
ATOM   16908 C  CB    . SER A 1 3857 ? 168.351 111.213 163.648 1.00 35.77  ? 3857 SER A CB    1 
ATOM   16909 O  OG    . SER A 1 3857 ? 167.647 110.640 162.560 1.00 41.52  ? 3857 SER A OG    1 
ATOM   16910 N  N     . ILE A 1 3858 ? 165.793 112.837 162.729 1.00 31.14  ? 3858 ILE A N     1 
ATOM   16911 C  CA    . ILE A 1 3858 ? 165.116 113.727 161.792 1.00 32.78  ? 3858 ILE A CA    1 
ATOM   16912 C  C     . ILE A 1 3858 ? 164.574 114.952 162.519 1.00 31.71  ? 3858 ILE A C     1 
ATOM   16913 O  O     . ILE A 1 3858 ? 164.691 116.084 162.033 1.00 35.20  ? 3858 ILE A O     1 
ATOM   16914 C  CB    . ILE A 1 3858 ? 164.004 112.961 161.050 1.00 31.54  ? 3858 ILE A CB    1 
ATOM   16915 C  CG1   . ILE A 1 3858 ? 164.605 112.068 159.964 1.00 36.85  ? 3858 ILE A CG1   1 
ATOM   16916 C  CG2   . ILE A 1 3858 ? 162.992 113.915 160.448 1.00 32.37  ? 3858 ILE A CG2   1 
ATOM   16917 C  CD1   . ILE A 1 3858 ? 163.585 111.217 159.244 1.00 43.04  ? 3858 ILE A CD1   1 
ATOM   16918 N  N     . ILE A 1 3859 ? 163.975 114.745 163.694 1.00 32.14  ? 3859 ILE A N     1 
ATOM   16919 C  CA    . ILE A 1 3859 ? 163.451 115.859 164.478 1.00 27.56  ? 3859 ILE A CA    1 
ATOM   16920 C  C     . ILE A 1 3859 ? 164.578 116.794 164.894 1.00 26.71  ? 3859 ILE A C     1 
ATOM   16921 O  O     . ILE A 1 3859 ? 164.436 118.021 164.843 1.00 30.39  ? 3859 ILE A O     1 
ATOM   16922 C  CB    . ILE A 1 3859 ? 162.669 115.333 165.696 1.00 26.31  ? 3859 ILE A CB    1 
ATOM   16923 C  CG1   . ILE A 1 3859 ? 161.320 114.763 165.259 1.00 24.14  ? 3859 ILE A CG1   1 
ATOM   16924 C  CG2   . ILE A 1 3859 ? 162.469 116.430 166.728 1.00 29.73  ? 3859 ILE A CG2   1 
ATOM   16925 C  CD1   . ILE A 1 3859 ? 160.574 114.056 166.364 1.00 23.69  ? 3859 ILE A CD1   1 
ATOM   16926 N  N     . THR A 1 3860 ? 165.716 116.233 165.308 1.00 25.76  ? 3860 THR A N     1 
ATOM   16927 C  CA    . THR A 1 3860 ? 166.851 117.061 165.703 1.00 26.14  ? 3860 THR A CA    1 
ATOM   16928 C  C     . THR A 1 3860 ? 167.362 117.894 164.535 1.00 26.07  ? 3860 THR A C     1 
ATOM   16929 O  O     . THR A 1 3860 ? 167.707 119.069 164.705 1.00 28.28  ? 3860 THR A O     1 
ATOM   16930 C  CB    . THR A 1 3860 ? 167.973 116.185 166.262 1.00 28.08  ? 3860 THR A CB    1 
ATOM   16931 O  OG1   . THR A 1 3860 ? 167.426 115.238 167.188 1.00 38.00  ? 3860 THR A OG1   1 
ATOM   16932 C  CG2   . THR A 1 3860 ? 169.011 117.038 166.973 1.00 27.80  ? 3860 THR A CG2   1 
ATOM   16933 N  N     . LYS A 1 3861 ? 167.426 117.301 163.341 1.00 25.65  ? 3861 LYS A N     1 
ATOM   16934 C  CA    . LYS A 1 3861 ? 167.873 118.050 162.168 1.00 22.96  ? 3861 LYS A CA    1 
ATOM   16935 C  C     . LYS A 1 3861 ? 166.895 119.170 161.820 1.00 26.84  ? 3861 LYS A C     1 
ATOM   16936 O  O     . LYS A 1 3861 ? 167.296 120.331 161.632 1.00 29.26  ? 3861 LYS A O     1 
ATOM   16937 C  CB    . LYS A 1 3861 ? 168.053 117.099 160.985 1.00 27.13  ? 3861 LYS A CB    1 
ATOM   16938 C  CG    . LYS A 1 3861 ? 168.688 117.733 159.760 1.00 40.68  ? 3861 LYS A CG    1 
ATOM   16939 C  CD    . LYS A 1 3861 ? 168.985 116.695 158.686 1.00 38.39  ? 3861 LYS A CD    1 
ATOM   16940 C  CE    . LYS A 1 3861 ? 167.857 115.682 158.555 1.00 43.32  ? 3861 LYS A CE    1 
ATOM   16941 N  NZ    . LYS A 1 3861 ? 166.595 116.308 158.071 1.00 40.26  ? 3861 LYS A NZ    1 
ATOM   16942 N  N     . ASP A 1 3862 ? 165.602 118.843 161.736 1.00 26.91  ? 3862 ASP A N     1 
ATOM   16943 C  CA    . ASP A 1 3862 ? 164.620 119.864 161.395 1.00 25.09  ? 3862 ASP A CA    1 
ATOM   16944 C  C     . ASP A 1 3862 ? 164.485 120.926 162.473 1.00 23.27  ? 3862 ASP A C     1 
ATOM   16945 O  O     . ASP A 1 3862 ? 164.062 122.038 162.160 1.00 23.56  ? 3862 ASP A O     1 
ATOM   16946 C  CB    . ASP A 1 3862 ? 163.245 119.255 161.110 1.00 30.62  ? 3862 ASP A CB    1 
ATOM   16947 C  CG    . ASP A 1 3862 ? 163.308 118.070 160.175 1.00 46.09  ? 3862 ASP A CG    1 
ATOM   16948 O  OD1   . ASP A 1 3862 ? 163.915 118.196 159.090 1.00 44.94  ? 3862 ASP A OD1   1 
ATOM   16949 O  OD2   . ASP A 1 3862 ? 162.708 117.028 160.501 1.00 51.10  ? 3862 ASP A OD2   1 
ATOM   16950 N  N     . LEU A 1 3863 ? 164.846 120.629 163.721 1.00 21.18  ? 3863 LEU A N     1 
ATOM   16951 C  CA    . LEU A 1 3863 ? 164.817 121.664 164.748 1.00 17.24  ? 3863 LEU A CA    1 
ATOM   16952 C  C     . LEU A 1 3863 ? 165.760 122.803 164.391 1.00 16.78  ? 3863 LEU A C     1 
ATOM   16953 O  O     . LEU A 1 3863 ? 165.351 123.969 164.327 1.00 17.40  ? 3863 LEU A O     1 
ATOM   16954 C  CB    . LEU A 1 3863 ? 165.182 121.062 166.106 1.00 15.85  ? 3863 LEU A CB    1 
ATOM   16955 C  CG    . LEU A 1 3863 ? 165.502 122.056 167.222 1.00 17.45  ? 3863 LEU A CG    1 
ATOM   16956 C  CD1   . LEU A 1 3863 ? 164.226 122.647 167.799 1.00 15.56  ? 3863 LEU A CD1   1 
ATOM   16957 C  CD2   . LEU A 1 3863 ? 166.329 121.385 168.305 1.00 15.97  ? 3863 LEU A CD2   1 
ATOM   16958 N  N     . PHE A 1 3864 ? 167.024 122.474 164.111 1.00 17.13  ? 3864 PHE A N     1 
ATOM   16959 C  CA    . PHE A 1 3864 ? 167.984 123.492 163.702 1.00 15.49  ? 3864 PHE A CA    1 
ATOM   16960 C  C     . PHE A 1 3864 ? 167.566 124.144 162.391 1.00 16.32  ? 3864 PHE A C     1 
ATOM   16961 O  O     . PHE A 1 3864 ? 167.648 125.371 162.245 1.00 17.69  ? 3864 PHE A O     1 
ATOM   16962 C  CB    . PHE A 1 3864 ? 169.377 122.876 163.568 1.00 14.25  ? 3864 PHE A CB    1 
ATOM   16963 C  CG    . PHE A 1 3864 ? 170.018 122.530 164.881 1.00 15.13  ? 3864 PHE A CG    1 
ATOM   16964 C  CD1   . PHE A 1 3864 ? 170.805 123.452 165.547 1.00 16.57  ? 3864 PHE A CD1   1 
ATOM   16965 C  CD2   . PHE A 1 3864 ? 169.839 121.279 165.444 1.00 16.67  ? 3864 PHE A CD2   1 
ATOM   16966 C  CE1   . PHE A 1 3864 ? 171.398 123.134 166.753 1.00 16.82  ? 3864 PHE A CE1   1 
ATOM   16967 C  CE2   . PHE A 1 3864 ? 170.429 120.955 166.650 1.00 18.83  ? 3864 PHE A CE2   1 
ATOM   16968 C  CZ    . PHE A 1 3864 ? 171.210 121.884 167.305 1.00 17.75  ? 3864 PHE A CZ    1 
ATOM   16969 N  N     . GLN A 1 3865 ? 167.109 123.338 161.426 1.00 19.28  ? 3865 GLN A N     1 
ATOM   16970 C  CA    . GLN A 1 3865 ? 166.751 123.894 160.123 1.00 18.43  ? 3865 GLN A CA    1 
ATOM   16971 C  C     . GLN A 1 3865 ? 165.615 124.905 160.241 1.00 17.96  ? 3865 GLN A C     1 
ATOM   16972 O  O     . GLN A 1 3865 ? 165.702 126.019 159.710 1.00 18.71  ? 3865 GLN A O     1 
ATOM   16973 C  CB    . GLN A 1 3865 ? 166.377 122.770 159.158 1.00 21.88  ? 3865 GLN A CB    1 
ATOM   16974 C  CG    . GLN A 1 3865 ? 166.155 123.237 157.731 1.00 25.08  ? 3865 GLN A CG    1 
ATOM   16975 C  CD    . GLN A 1 3865 ? 167.376 123.918 157.146 1.00 26.77  ? 3865 GLN A CD    1 
ATOM   16976 O  OE1   . GLN A 1 3865 ? 168.346 123.262 156.769 1.00 29.29  ? 3865 GLN A OE1   1 
ATOM   16977 N  NE2   . GLN A 1 3865 ? 167.334 125.243 157.067 1.00 26.45  ? 3865 GLN A NE2   1 
ATOM   16978 N  N     . VAL A 1 3866 ? 164.544 124.540 160.950 1.00 17.70  ? 3866 VAL A N     1 
ATOM   16979 C  CA    . VAL A 1 3866 ? 163.388 125.417 161.087 1.00 13.41  ? 3866 VAL A CA    1 
ATOM   16980 C  C     . VAL A 1 3866 ? 163.730 126.630 161.940 1.00 13.77  ? 3866 VAL A C     1 
ATOM   16981 O  O     . VAL A 1 3866 ? 163.265 127.742 161.667 1.00 18.99  ? 3866 VAL A O     1 
ATOM   16982 C  CB    . VAL A 1 3866 ? 162.193 124.632 161.660 1.00 13.28  ? 3866 VAL A CB    1 
ATOM   16983 C  CG1   . VAL A 1 3866 ? 161.062 125.572 162.041 1.00 18.95  ? 3866 VAL A CG1   1 
ATOM   16984 C  CG2   . VAL A 1 3866 ? 161.708 123.604 160.652 1.00 22.22  ? 3866 VAL A CG2   1 
ATOM   16985 N  N     . ALA A 1 3867 ? 164.545 126.447 162.984 1.00 14.06  ? 3867 ALA A N     1 
ATOM   16986 C  CA    . ALA A 1 3867 ? 164.959 127.590 163.789 1.00 12.58  ? 3867 ALA A CA    1 
ATOM   16987 C  C     . ALA A 1 3867 ? 165.696 128.613 162.936 1.00 15.94  ? 3867 ALA A C     1 
ATOM   16988 O  O     . ALA A 1 3867 ? 165.388 129.812 162.977 1.00 19.41  ? 3867 ALA A O     1 
ATOM   16989 C  CB    . ALA A 1 3867 ? 165.832 127.125 164.955 1.00 10.70  ? 3867 ALA A CB    1 
ATOM   16990 N  N     . PHE A 1 3868 ? 166.655 128.154 162.129 1.00 14.77  ? 3868 PHE A N     1 
ATOM   16991 C  CA    . PHE A 1 3868 ? 167.386 129.077 161.268 1.00 11.02  ? 3868 PHE A CA    1 
ATOM   16992 C  C     . PHE A 1 3868 ? 166.464 129.718 160.239 1.00 12.86  ? 3868 PHE A C     1 
ATOM   16993 O  O     . PHE A 1 3868 ? 166.544 130.924 159.986 1.00 16.42  ? 3868 PHE A O     1 
ATOM   16994 C  CB    . PHE A 1 3868 ? 168.542 128.361 160.574 1.00 10.98  ? 3868 PHE A CB    1 
ATOM   16995 C  CG    . PHE A 1 3868 ? 169.296 129.233 159.613 1.00 15.58  ? 3868 PHE A CG    1 
ATOM   16996 C  CD1   . PHE A 1 3868 ? 170.222 130.153 160.075 1.00 18.00  ? 3868 PHE A CD1   1 
ATOM   16997 C  CD2   . PHE A 1 3868 ? 169.071 129.145 158.250 1.00 17.66  ? 3868 PHE A CD2   1 
ATOM   16998 C  CE1   . PHE A 1 3868 ? 170.913 130.962 159.196 1.00 15.62  ? 3868 PHE A CE1   1 
ATOM   16999 C  CE2   . PHE A 1 3868 ? 169.759 129.953 157.367 1.00 19.65  ? 3868 PHE A CE2   1 
ATOM   17000 C  CZ    . PHE A 1 3868 ? 170.681 130.862 157.841 1.00 17.21  ? 3868 PHE A CZ    1 
ATOM   17001 N  N     . ASN A 1 3869 ? 165.577 128.925 159.634 1.00 13.45  ? 3869 ASN A N     1 
ATOM   17002 C  CA    . ASN A 1 3869 ? 164.700 129.456 158.594 1.00 11.48  ? 3869 ASN A CA    1 
ATOM   17003 C  C     . ASN A 1 3869 ? 163.776 130.533 159.148 1.00 15.04  ? 3869 ASN A C     1 
ATOM   17004 O  O     . ASN A 1 3869 ? 163.570 131.575 158.516 1.00 20.19  ? 3869 ASN A O     1 
ATOM   17005 C  CB    . ASN A 1 3869 ? 163.890 128.324 157.963 1.00 9.98   ? 3869 ASN A CB    1 
ATOM   17006 C  CG    . ASN A 1 3869 ? 164.735 127.415 157.095 1.00 19.82  ? 3869 ASN A CG    1 
ATOM   17007 O  OD1   . ASN A 1 3869 ? 165.929 127.649 156.910 1.00 25.87  ? 3869 ASN A OD1   1 
ATOM   17008 N  ND2   . ASN A 1 3869 ? 164.118 126.371 156.556 1.00 22.25  ? 3869 ASN A ND2   1 
ATOM   17009 N  N     . ARG A 1 3870 ? 163.208 130.298 160.332 1.00 15.75  ? 3870 ARG A N     1 
ATOM   17010 C  CA    . ARG A 1 3870 ? 162.254 131.249 160.892 1.00 14.47  ? 3870 ARG A CA    1 
ATOM   17011 C  C     . ARG A 1 3870 ? 162.951 132.491 161.431 1.00 15.36  ? 3870 ARG A C     1 
ATOM   17012 O  O     . ARG A 1 3870 ? 162.475 133.613 161.227 1.00 21.26  ? 3870 ARG A O     1 
ATOM   17013 C  CB    . ARG A 1 3870 ? 161.430 130.576 161.989 1.00 13.84  ? 3870 ARG A CB    1 
ATOM   17014 C  CG    . ARG A 1 3870 ? 160.487 129.503 161.475 1.00 18.34  ? 3870 ARG A CG    1 
ATOM   17015 C  CD    . ARG A 1 3870 ? 159.178 129.503 162.241 1.00 26.10  ? 3870 ARG A CD    1 
ATOM   17016 N  NE    . ARG A 1 3870 ? 158.300 128.421 161.813 1.00 27.99  ? 3870 ARG A NE    1 
ATOM   17017 C  CZ    . ARG A 1 3870 ? 157.110 128.171 162.340 1.00 35.82  ? 3870 ARG A CZ    1 
ATOM   17018 N  NH1   . ARG A 1 3870 ? 156.622 128.905 163.326 1.00 43.01  ? 3870 ARG A NH1   1 
ATOM   17019 N  NH2   . ARG A 1 3870 ? 156.390 127.159 161.865 1.00 37.83  ? 3870 ARG A NH2   1 
ATOM   17020 N  N     . VAL A 1 3871 ? 164.077 132.316 162.125 1.00 15.31  ? 3871 VAL A N     1 
ATOM   17021 C  CA    . VAL A 1 3871 ? 164.727 133.461 162.759 1.00 13.42  ? 3871 VAL A CA    1 
ATOM   17022 C  C     . VAL A 1 3871 ? 165.423 134.333 161.720 1.00 17.00  ? 3871 VAL A C     1 
ATOM   17023 O  O     . VAL A 1 3871 ? 165.314 135.564 161.751 1.00 18.63  ? 3871 VAL A O     1 
ATOM   17024 C  CB    . VAL A 1 3871 ? 165.703 132.988 163.848 1.00 13.07  ? 3871 VAL A CB    1 
ATOM   17025 C  CG1   . VAL A 1 3871 ? 166.430 134.171 164.453 1.00 13.99  ? 3871 VAL A CG1   1 
ATOM   17026 C  CG2   . VAL A 1 3871 ? 164.949 132.237 164.917 1.00 16.27  ? 3871 VAL A CG2   1 
ATOM   17027 N  N     . ALA A 1 3872 ? 166.147 133.713 160.785 1.00 17.61  ? 3872 ALA A N     1 
ATOM   17028 C  CA    . ALA A 1 3872 ? 166.885 134.486 159.792 1.00 14.06  ? 3872 ALA A CA    1 
ATOM   17029 C  C     . ALA A 1 3872 ? 165.970 135.235 158.834 1.00 16.87  ? 3872 ALA A C     1 
ATOM   17030 O  O     . ALA A 1 3872 ? 166.424 136.178 158.178 1.00 20.80  ? 3872 ALA A O     1 
ATOM   17031 C  CB    . ALA A 1 3872 ? 167.828 133.579 159.002 1.00 13.32  ? 3872 ALA A CB    1 
ATOM   17032 N  N     . ARG A 1 3873 ? 164.699 134.838 158.733 1.00 18.81  ? 3873 ARG A N     1 
ATOM   17033 C  CA    . ARG A 1 3873 ? 163.760 135.567 157.889 1.00 16.16  ? 3873 ARG A CA    1 
ATOM   17034 C  C     . ARG A 1 3873 ? 163.532 136.988 158.382 1.00 16.84  ? 3873 ARG A C     1 
ATOM   17035 O  O     . ARG A 1 3873 ? 163.271 137.881 157.568 1.00 18.44  ? 3873 ARG A O     1 
ATOM   17036 C  CB    . ARG A 1 3873 ? 162.427 134.821 157.818 1.00 15.99  ? 3873 ARG A CB    1 
ATOM   17037 C  CG    . ARG A 1 3873 ? 162.303 133.884 156.630 1.00 23.08  ? 3873 ARG A CG    1 
ATOM   17038 C  CD    . ARG A 1 3873 ? 162.764 134.553 155.347 1.00 28.09  ? 3873 ARG A CD    1 
ATOM   17039 N  NE    . ARG A 1 3873 ? 162.724 133.641 154.211 1.00 31.25  ? 3873 ARG A NE    1 
ATOM   17040 C  CZ    . ARG A 1 3873 ? 163.374 133.834 153.072 1.00 32.12  ? 3873 ARG A CZ    1 
ATOM   17041 N  NH1   . ARG A 1 3873 ? 164.129 134.904 152.880 1.00 27.28  ? 3873 ARG A NH1   1 
ATOM   17042 N  NH2   . ARG A 1 3873 ? 163.265 132.932 152.101 1.00 34.89  ? 3873 ARG A NH2   1 
ATOM   17043 N  N     . GLY A 1 3874 ? 163.625 137.218 159.688 1.00 15.89  ? 3874 GLY A N     1 
ATOM   17044 C  CA    . GLY A 1 3874 ? 163.481 138.549 160.239 1.00 16.21  ? 3874 GLY A CA    1 
ATOM   17045 C  C     . GLY A 1 3874 ? 164.796 139.089 160.754 1.00 17.04  ? 3874 GLY A C     1 
ATOM   17046 O  O     . GLY A 1 3874 ? 164.842 139.776 161.779 1.00 17.63  ? 3874 GLY A O     1 
ATOM   17047 N  N     . MET A 1 3875 ? 165.876 138.777 160.045 1.00 18.10  ? 3875 MET A N     1 
ATOM   17048 C  CA    . MET A 1 3875 ? 167.217 139.184 160.427 1.00 16.73  ? 3875 MET A CA    1 
ATOM   17049 C  C     . MET A 1 3875 ? 167.940 139.738 159.209 1.00 18.58  ? 3875 MET A C     1 
ATOM   17050 O  O     . MET A 1 3875 ? 167.699 139.308 158.078 1.00 21.41  ? 3875 MET A O     1 
ATOM   17051 C  CB    . MET A 1 3875 ? 168.001 138.004 161.018 1.00 13.69  ? 3875 MET A CB    1 
ATOM   17052 C  CG    . MET A 1 3875 ? 168.025 137.973 162.535 1.00 20.37  ? 3875 MET A CG    1 
ATOM   17053 S  SD    . MET A 1 3875 ? 168.830 136.507 163.198 1.00 22.53  ? 3875 MET A SD    1 
ATOM   17054 C  CE    . MET A 1 3875 ? 170.320 136.474 162.216 1.00 20.09  ? 3875 MET A CE    1 
ATOM   17055 N  N     . LEU A 1 3876 ? 168.824 140.704 159.447 1.00 18.09  ? 3876 LEU A N     1 
ATOM   17056 C  CA    . LEU A 1 3876 ? 169.641 141.236 158.366 1.00 18.04  ? 3876 LEU A CA    1 
ATOM   17057 C  C     . LEU A 1 3876 ? 170.582 140.158 157.842 1.00 24.13  ? 3876 LEU A C     1 
ATOM   17058 O  O     . LEU A 1 3876 ? 171.043 139.290 158.587 1.00 29.30  ? 3876 LEU A O     1 
ATOM   17059 C  CB    . LEU A 1 3876 ? 170.437 142.452 158.841 1.00 14.89  ? 3876 LEU A CB    1 
ATOM   17060 C  CG    . LEU A 1 3876 ? 169.638 143.615 159.433 1.00 12.74  ? 3876 LEU A CG    1 
ATOM   17061 C  CD1   . LEU A 1 3876 ? 170.559 144.585 160.153 1.00 18.87  ? 3876 LEU A CD1   1 
ATOM   17062 C  CD2   . LEU A 1 3876 ? 168.851 144.331 158.350 1.00 12.49  ? 3876 LEU A CD2   1 
ATOM   17063 N  N     . HIS A 1 3877 ? 170.861 140.217 156.538 1.00 20.22  ? 3877 HIS A N     1 
ATOM   17064 C  CA    . HIS A 1 3877 ? 171.665 139.179 155.900 1.00 19.20  ? 3877 HIS A CA    1 
ATOM   17065 C  C     . HIS A 1 3877 ? 173.082 139.117 156.453 1.00 23.27  ? 3877 HIS A C     1 
ATOM   17066 O  O     . HIS A 1 3877 ? 173.745 138.084 156.312 1.00 28.96  ? 3877 HIS A O     1 
ATOM   17067 C  CB    . HIS A 1 3877 ? 171.706 139.403 154.388 1.00 21.59  ? 3877 HIS A CB    1 
ATOM   17068 C  CG    . HIS A 1 3877 ? 172.196 138.218 153.616 1.00 26.99  ? 3877 HIS A CG    1 
ATOM   17069 N  ND1   . HIS A 1 3877 ? 173.523 138.039 153.290 1.00 28.42  ? 3877 HIS A ND1   1 
ATOM   17070 C  CD2   . HIS A 1 3877 ? 171.536 137.153 153.105 1.00 24.46  ? 3877 HIS A CD2   1 
ATOM   17071 C  CE1   . HIS A 1 3877 ? 173.659 136.914 152.612 1.00 27.13  ? 3877 HIS A CE1   1 
ATOM   17072 N  NE2   . HIS A 1 3877 ? 172.468 136.357 152.486 1.00 31.29  ? 3877 HIS A NE2   1 
ATOM   17073 N  N     . GLN A 1 3878 ? 173.562 140.193 157.079 1.00 21.47  ? 3878 GLN A N     1 
ATOM   17074 C  CA    . GLN A 1 3878 ? 174.911 140.182 157.631 1.00 24.45  ? 3878 GLN A CA    1 
ATOM   17075 C  C     . GLN A 1 3878 ? 174.988 139.388 158.931 1.00 27.98  ? 3878 GLN A C     1 
ATOM   17076 O  O     . GLN A 1 3878 ? 176.077 138.956 159.326 1.00 32.86  ? 3878 GLN A O     1 
ATOM   17077 C  CB    . GLN A 1 3878 ? 175.397 141.616 157.843 1.00 25.06  ? 3878 GLN A CB    1 
ATOM   17078 C  CG    . GLN A 1 3878 ? 174.608 142.396 158.878 1.00 28.95  ? 3878 GLN A CG    1 
ATOM   17079 C  CD    . GLN A 1 3878 ? 175.082 143.829 159.009 1.00 38.52  ? 3878 GLN A CD    1 
ATOM   17080 O  OE1   . GLN A 1 3878 ? 176.043 144.238 158.358 1.00 42.74  ? 3878 GLN A OE1   1 
ATOM   17081 N  NE2   . GLN A 1 3878 ? 174.407 144.601 159.851 1.00 44.29  ? 3878 GLN A NE2   1 
ATOM   17082 N  N     . ASP A 1 3879 ? 173.859 139.188 159.607 1.00 21.18  ? 3879 ASP A N     1 
ATOM   17083 C  CA    . ASP A 1 3879 ? 173.814 138.418 160.843 1.00 19.89  ? 3879 ASP A CA    1 
ATOM   17084 C  C     . ASP A 1 3879 ? 173.406 136.966 160.623 1.00 22.50  ? 3879 ASP A C     1 
ATOM   17085 O  O     . ASP A 1 3879 ? 173.421 136.177 161.580 1.00 27.87  ? 3879 ASP A O     1 
ATOM   17086 C  CB    . ASP A 1 3879 ? 172.857 139.082 161.836 1.00 21.08  ? 3879 ASP A CB    1 
ATOM   17087 C  CG    . ASP A 1 3879 ? 173.099 140.572 161.965 1.00 25.39  ? 3879 ASP A CG    1 
ATOM   17088 O  OD1   . ASP A 1 3879 ? 174.271 140.993 161.881 1.00 33.67  ? 3879 ASP A OD1   1 
ATOM   17089 O  OD2   . ASP A 1 3879 ? 172.121 141.324 162.149 1.00 23.60  ? 3879 ASP A OD2   1 
ATOM   17090 N  N     . HIS A 1 3880 ? 173.046 136.599 159.391 1.00 20.65  ? 3880 HIS A N     1 
ATOM   17091 C  CA    . HIS A 1 3880 ? 172.711 135.211 159.097 1.00 19.28  ? 3880 HIS A CA    1 
ATOM   17092 C  C     . HIS A 1 3880 ? 173.898 134.298 159.363 1.00 19.44  ? 3880 HIS A C     1 
ATOM   17093 O  O     . HIS A 1 3880 ? 173.739 133.205 159.919 1.00 22.49  ? 3880 HIS A O     1 
ATOM   17094 C  CB    . HIS A 1 3880 ? 172.257 135.074 157.643 1.00 19.11  ? 3880 HIS A CB    1 
ATOM   17095 C  CG    . HIS A 1 3880 ? 170.888 135.616 157.380 1.00 17.00  ? 3880 HIS A CG    1 
ATOM   17096 N  ND1   . HIS A 1 3880 ? 170.233 135.429 156.183 1.00 17.54  ? 3880 HIS A ND1   1 
ATOM   17097 C  CD2   . HIS A 1 3880 ? 170.052 136.345 158.156 1.00 19.67  ? 3880 HIS A CD2   1 
ATOM   17098 C  CE1   . HIS A 1 3880 ? 169.051 136.016 156.233 1.00 19.62  ? 3880 HIS A CE1   1 
ATOM   17099 N  NE2   . HIS A 1 3880 ? 168.916 136.579 157.420 1.00 22.24  ? 3880 HIS A NE2   1 
ATOM   17100 N  N     . ILE A 1 3881 ? 175.098 134.734 158.976 1.00 21.27  ? 3881 ILE A N     1 
ATOM   17101 C  CA    . ILE A 1 3881 ? 176.289 133.924 159.200 1.00 20.03  ? 3881 ILE A CA    1 
ATOM   17102 C  C     . ILE A 1 3881 ? 176.574 133.791 160.691 1.00 17.46  ? 3881 ILE A C     1 
ATOM   17103 O  O     . ILE A 1 3881 ? 176.984 132.725 161.160 1.00 22.01  ? 3881 ILE A O     1 
ATOM   17104 C  CB    . ILE A 1 3881 ? 177.489 134.511 158.431 1.00 24.57  ? 3881 ILE A CB    1 
ATOM   17105 C  CG1   . ILE A 1 3881 ? 178.742 133.664 158.662 1.00 21.96  ? 3881 ILE A CG1   1 
ATOM   17106 C  CG2   . ILE A 1 3881 ? 177.729 135.966 158.812 1.00 23.50  ? 3881 ILE A CG2   1 
ATOM   17107 C  CD1   . ILE A 1 3881 ? 178.582 132.221 158.243 1.00 21.41  ? 3881 ILE A CD1   1 
ATOM   17108 N  N     . THR A 1 3882 ? 176.343 134.855 161.463 1.00 16.22  ? 3882 THR A N     1 
ATOM   17109 C  CA    . THR A 1 3882 ? 176.542 134.781 162.908 1.00 17.07  ? 3882 THR A CA    1 
ATOM   17110 C  C     . THR A 1 3882 ? 175.592 133.771 163.541 1.00 18.14  ? 3882 THR A C     1 
ATOM   17111 O  O     . THR A 1 3882 ? 176.006 132.918 164.341 1.00 25.21  ? 3882 THR A O     1 
ATOM   17112 C  CB    . THR A 1 3882 ? 176.348 136.165 163.532 1.00 18.21  ? 3882 THR A CB    1 
ATOM   17113 O  OG1   . THR A 1 3882 ? 177.324 137.073 163.005 1.00 27.40  ? 3882 THR A OG1   1 
ATOM   17114 C  CG2   . THR A 1 3882 ? 176.486 136.100 165.044 1.00 18.67  ? 3882 THR A CG2   1 
ATOM   17115 N  N     . PHE A 1 3883 ? 174.308 133.845 163.184 1.00 13.77  ? 3883 PHE A N     1 
ATOM   17116 C  CA    . PHE A 1 3883 ? 173.338 132.921 163.762 1.00 11.79  ? 3883 PHE A CA    1 
ATOM   17117 C  C     . PHE A 1 3883 ? 173.626 131.484 163.339 1.00 15.64  ? 3883 PHE A C     1 
ATOM   17118 O  O     . PHE A 1 3883 ? 173.501 130.554 164.145 1.00 21.60  ? 3883 PHE A O     1 
ATOM   17119 C  CB    . PHE A 1 3883 ? 171.917 133.324 163.372 1.00 15.14  ? 3883 PHE A CB    1 
ATOM   17120 C  CG    . PHE A 1 3883 ? 170.854 132.579 164.125 1.00 15.07  ? 3883 PHE A CG    1 
ATOM   17121 C  CD1   . PHE A 1 3883 ? 170.967 132.384 165.491 1.00 13.92  ? 3883 PHE A CD1   1 
ATOM   17122 C  CD2   . PHE A 1 3883 ? 169.749 132.065 163.470 1.00 12.97  ? 3883 PHE A CD2   1 
ATOM   17123 C  CE1   . PHE A 1 3883 ? 169.997 131.696 166.190 1.00 14.17  ? 3883 PHE A CE1   1 
ATOM   17124 C  CE2   . PHE A 1 3883 ? 168.776 131.375 164.165 1.00 12.76  ? 3883 PHE A CE2   1 
ATOM   17125 C  CZ    . PHE A 1 3883 ? 168.899 131.192 165.527 1.00 14.34  ? 3883 PHE A CZ    1 
ATOM   17126 N  N     . ALA A 1 3884 ? 174.015 131.282 162.076 1.00 15.80  ? 3884 ALA A N     1 
ATOM   17127 C  CA    . ALA A 1 3884 ? 174.351 129.942 161.608 1.00 13.10  ? 3884 ALA A CA    1 
ATOM   17128 C  C     . ALA A 1 3884 ? 175.589 129.404 162.313 1.00 16.86  ? 3884 ALA A C     1 
ATOM   17129 O  O     . ALA A 1 3884 ? 175.659 128.213 162.630 1.00 22.64  ? 3884 ALA A O     1 
ATOM   17130 C  CB    . ALA A 1 3884 ? 174.554 129.950 160.094 1.00 18.26  ? 3884 ALA A CB    1 
ATOM   17131 N  N     . MET A 1 3885 ? 176.575 130.266 162.567 1.00 17.17  ? 3885 MET A N     1 
ATOM   17132 C  CA    . MET A 1 3885 ? 177.763 129.847 163.301 1.00 15.88  ? 3885 MET A CA    1 
ATOM   17133 C  C     . MET A 1 3885 ? 177.402 129.409 164.713 1.00 18.26  ? 3885 MET A C     1 
ATOM   17134 O  O     . MET A 1 3885 ? 177.905 128.392 165.207 1.00 26.19  ? 3885 MET A O     1 
ATOM   17135 C  CB    . MET A 1 3885 ? 178.774 130.992 163.342 1.00 16.61  ? 3885 MET A CB    1 
ATOM   17136 C  CG    . MET A 1 3885 ? 179.726 131.043 162.161 1.00 20.25  ? 3885 MET A CG    1 
ATOM   17137 S  SD    . MET A 1 3885 ? 180.998 129.777 162.235 1.00 42.19  ? 3885 MET A SD    1 
ATOM   17138 C  CE    . MET A 1 3885 ? 182.301 130.662 163.080 1.00 31.64  ? 3885 MET A CE    1 
ATOM   17139 N  N     . LEU A 1 3886 ? 176.529 130.169 165.380 1.00 16.95  ? 3886 LEU A N     1 
ATOM   17140 C  CA    . LEU A 1 3886 ? 176.108 129.796 166.729 1.00 16.24  ? 3886 LEU A CA    1 
ATOM   17141 C  C     . LEU A 1 3886 ? 175.326 128.488 166.728 1.00 18.32  ? 3886 LEU A C     1 
ATOM   17142 O  O     . LEU A 1 3886 ? 175.502 127.652 167.623 1.00 24.36  ? 3886 LEU A O     1 
ATOM   17143 C  CB    . LEU A 1 3886 ? 175.283 130.921 167.351 1.00 15.14  ? 3886 LEU A CB    1 
ATOM   17144 C  CG    . LEU A 1 3886 ? 176.060 132.225 167.539 1.00 13.92  ? 3886 LEU A CG    1 
ATOM   17145 C  CD1   . LEU A 1 3886 ? 175.225 133.294 168.219 1.00 12.24  ? 3886 LEU A CD1   1 
ATOM   17146 C  CD2   . LEU A 1 3886 ? 177.345 131.961 168.313 1.00 13.94  ? 3886 LEU A CD2   1 
ATOM   17147 N  N     . LEU A 1 3887 ? 174.454 128.291 165.737 1.00 15.52  ? 3887 LEU A N     1 
ATOM   17148 C  CA    . LEU A 1 3887 ? 173.720 127.031 165.648 1.00 14.28  ? 3887 LEU A CA    1 
ATOM   17149 C  C     . LEU A 1 3887 ? 174.663 125.861 165.387 1.00 16.24  ? 3887 LEU A C     1 
ATOM   17150 O  O     . LEU A 1 3887 ? 174.478 124.766 165.933 1.00 20.40  ? 3887 LEU A O     1 
ATOM   17151 C  CB    . LEU A 1 3887 ? 172.652 127.121 164.560 1.00 16.58  ? 3887 LEU A CB    1 
ATOM   17152 C  CG    . LEU A 1 3887 ? 171.432 127.981 164.890 1.00 13.38  ? 3887 LEU A CG    1 
ATOM   17153 C  CD1   . LEU A 1 3887 ? 170.437 127.962 163.743 1.00 13.58  ? 3887 LEU A CD1   1 
ATOM   17154 C  CD2   . LEU A 1 3887 ? 170.781 127.512 166.177 1.00 12.27  ? 3887 LEU A CD2   1 
ATOM   17155 N  N     . ALA A 1 3888 ? 175.679 126.074 164.548 1.00 18.49  ? 3888 ALA A N     1 
ATOM   17156 C  CA    . ALA A 1 3888 ? 176.671 125.033 164.302 1.00 20.31  ? 3888 ALA A CA    1 
ATOM   17157 C  C     . ALA A 1 3888 ? 177.441 124.700 165.572 1.00 22.72  ? 3888 ALA A C     1 
ATOM   17158 O  O     . ALA A 1 3888 ? 177.731 123.530 165.841 1.00 29.01  ? 3888 ALA A O     1 
ATOM   17159 C  CB    . ALA A 1 3888 ? 177.623 125.469 163.190 1.00 19.70  ? 3888 ALA A CB    1 
ATOM   17160 N  N     . ARG A 1 3889 ? 177.783 125.718 166.366 1.00 20.10  ? 3889 ARG A N     1 
ATOM   17161 C  CA    . ARG A 1 3889 ? 178.434 125.464 167.648 1.00 22.80  ? 3889 ARG A CA    1 
ATOM   17162 C  C     . ARG A 1 3889 ? 177.524 124.671 168.580 1.00 25.99  ? 3889 ARG A C     1 
ATOM   17163 O  O     . ARG A 1 3889 ? 177.981 123.762 169.285 1.00 28.00  ? 3889 ARG A O     1 
ATOM   17164 C  CB    . ARG A 1 3889 ? 178.848 126.783 168.300 1.00 23.90  ? 3889 ARG A CB    1 
ATOM   17165 C  CG    . ARG A 1 3889 ? 179.946 127.527 167.563 1.00 29.44  ? 3889 ARG A CG    1 
ATOM   17166 C  CD    . ARG A 1 3889 ? 180.774 128.362 168.522 1.00 36.39  ? 3889 ARG A CD    1 
ATOM   17167 N  NE    . ARG A 1 3889 ? 181.347 127.555 169.593 1.00 41.77  ? 3889 ARG A NE    1 
ATOM   17168 C  CZ    . ARG A 1 3889 ? 182.072 128.040 170.591 1.00 45.73  ? 3889 ARG A CZ    1 
ATOM   17169 N  NH1   . ARG A 1 3889 ? 182.329 129.334 170.692 1.00 46.78  ? 3889 ARG A NH1   1 
ATOM   17170 N  NH2   . ARG A 1 3889 ? 182.551 127.207 171.510 1.00 46.48  ? 3889 ARG A NH2   1 
ATOM   17171 N  N     . ILE A 1 3890 ? 176.231 125.005 168.595 1.00 23.54  ? 3890 ILE A N     1 
ATOM   17172 C  CA    . ILE A 1 3890 ? 175.280 124.273 169.429 1.00 22.37  ? 3890 ILE A CA    1 
ATOM   17173 C  C     . ILE A 1 3890 ? 175.228 122.807 169.019 1.00 24.17  ? 3890 ILE A C     1 
ATOM   17174 O  O     . ILE A 1 3890 ? 175.238 121.909 169.870 1.00 27.79  ? 3890 ILE A O     1 
ATOM   17175 C  CB    . ILE A 1 3890 ? 173.888 124.927 169.360 1.00 17.49  ? 3890 ILE A CB    1 
ATOM   17176 C  CG1   . ILE A 1 3890 ? 173.904 126.298 170.034 1.00 16.54  ? 3890 ILE A CG1   1 
ATOM   17177 C  CG2   . ILE A 1 3890 ? 172.843 124.034 170.009 1.00 17.91  ? 3890 ILE A CG2   1 
ATOM   17178 C  CD1   . ILE A 1 3890 ? 172.654 127.106 169.782 1.00 15.39  ? 3890 ILE A CD1   1 
ATOM   17179 N  N     . LYS A 1 3891 ? 175.170 122.540 167.712 1.00 23.68  ? 3891 LYS A N     1 
ATOM   17180 C  CA    . LYS A 1 3891 ? 175.168 121.154 167.251 1.00 22.87  ? 3891 LYS A CA    1 
ATOM   17181 C  C     . LYS A 1 3891 ? 176.478 120.454 167.590 1.00 31.55  ? 3891 LYS A C     1 
ATOM   17182 O  O     . LYS A 1 3891 ? 176.482 119.273 167.958 1.00 35.43  ? 3891 LYS A O     1 
ATOM   17183 C  CB    . LYS A 1 3891 ? 174.909 121.080 165.747 1.00 17.74  ? 3891 LYS A CB    1 
ATOM   17184 C  CG    . LYS A 1 3891 ? 174.611 119.664 165.274 1.00 21.60  ? 3891 LYS A CG    1 
ATOM   17185 C  CD    . LYS A 1 3891 ? 174.517 119.570 163.764 1.00 26.75  ? 3891 LYS A CD    1 
ATOM   17186 C  CE    . LYS A 1 3891 ? 173.984 118.215 163.330 1.00 31.60  ? 3891 LYS A CE    1 
ATOM   17187 N  NZ    . LYS A 1 3891 ? 172.673 117.907 163.966 1.00 36.43  ? 3891 LYS A NZ    1 
ATOM   17188 N  N     . LEU A 1 3892 ? 177.601 121.163 167.463 1.00 33.50  ? 3892 LEU A N     1 
ATOM   17189 C  CA    . LEU A 1 3892 ? 178.898 120.567 167.763 1.00 34.45  ? 3892 LEU A CA    1 
ATOM   17190 C  C     . LEU A 1 3892 ? 178.997 120.173 169.231 1.00 44.45  ? 3892 LEU A C     1 
ATOM   17191 O  O     . LEU A 1 3892 ? 179.593 119.143 169.565 1.00 48.18  ? 3892 LEU A O     1 
ATOM   17192 C  CB    . LEU A 1 3892 ? 180.017 121.537 167.387 1.00 28.90  ? 3892 LEU A CB    1 
ATOM   17193 C  CG    . LEU A 1 3892 ? 181.451 121.019 167.506 1.00 37.76  ? 3892 LEU A CG    1 
ATOM   17194 C  CD1   . LEU A 1 3892 ? 181.602 119.689 166.787 1.00 46.18  ? 3892 LEU A CD1   1 
ATOM   17195 C  CD2   . LEU A 1 3892 ? 182.433 122.042 166.960 1.00 42.58  ? 3892 LEU A CD2   1 
ATOM   17196 N  N     . LYS A 1 3893 ? 178.425 120.986 170.124 1.00 45.73  ? 3893 LYS A N     1 
ATOM   17197 C  CA    . LYS A 1 3893 ? 178.401 120.615 171.536 1.00 43.69  ? 3893 LYS A CA    1 
ATOM   17198 C  C     . LYS A 1 3893 ? 177.564 119.365 171.774 1.00 48.54  ? 3893 LYS A C     1 
ATOM   17199 O  O     . LYS A 1 3893 ? 177.809 118.629 172.737 1.00 60.44  ? 3893 LYS A O     1 
ATOM   17200 C  CB    . LYS A 1 3893 ? 177.866 121.770 172.381 1.00 37.28  ? 3893 LYS A CB    1 
ATOM   17201 C  CG    . LYS A 1 3893 ? 178.769 122.989 172.427 1.00 42.88  ? 3893 LYS A CG    1 
ATOM   17202 C  CD    . LYS A 1 3893 ? 178.246 124.015 173.417 1.00 46.15  ? 3893 LYS A CD    1 
ATOM   17203 C  CE    . LYS A 1 3893 ? 177.014 124.724 172.879 1.00 44.63  ? 3893 LYS A CE    1 
ATOM   17204 N  NZ    . LYS A 1 3893 ? 176.548 125.805 173.790 1.00 49.91  ? 3893 LYS A NZ    1 
ATOM   17205 N  N     . GLY A 1 3894 ? 176.579 119.108 170.917 1.00 44.21  ? 3894 GLY A N     1 
ATOM   17206 C  CA    . GLY A 1 3894 ? 175.676 117.989 171.085 1.00 50.15  ? 3894 GLY A CA    1 
ATOM   17207 C  C     . GLY A 1 3894 ? 176.123 116.672 170.496 1.00 61.04  ? 3894 GLY A C     1 
ATOM   17208 O  O     . GLY A 1 3894 ? 175.376 115.693 170.576 1.00 68.32  ? 3894 GLY A O     1 
ATOM   17209 N  N     . THR A 1 3895 ? 177.312 116.606 169.904 1.00 63.33  ? 3895 THR A N     1 
ATOM   17210 C  CA    . THR A 1 3895 ? 177.816 115.380 169.298 1.00 72.48  ? 3895 THR A CA    1 
ATOM   17211 C  C     . THR A 1 3895 ? 178.823 114.737 170.245 1.00 77.78  ? 3895 THR A C     1 
ATOM   17212 O  O     . THR A 1 3895 ? 179.793 115.382 170.658 1.00 73.61  ? 3895 THR A O     1 
ATOM   17213 C  CB    . THR A 1 3895 ? 178.458 115.659 167.940 1.00 68.06  ? 3895 THR A CB    1 
ATOM   17214 O  OG1   . THR A 1 3895 ? 177.436 115.951 166.979 1.00 54.09  ? 3895 THR A OG1   1 
ATOM   17215 C  CG2   . THR A 1 3895 ? 179.241 114.445 167.469 1.00 71.86  ? 3895 THR A CG2   1 
ATOM   17216 N  N     . VAL A 1 3896 ? 178.588 113.468 170.587 1.00 85.96  ? 3896 VAL A N     1 
ATOM   17217 C  CA    . VAL A 1 3896 ? 179.457 112.777 171.534 1.00 92.38  ? 3896 VAL A CA    1 
ATOM   17218 C  C     . VAL A 1 3896 ? 180.821 112.500 170.914 1.00 87.24  ? 3896 VAL A C     1 
ATOM   17219 O  O     . VAL A 1 3896 ? 181.860 112.683 171.560 1.00 82.10  ? 3896 VAL A O     1 
ATOM   17220 C  CB    . VAL A 1 3896 ? 178.786 111.482 172.024 1.00 89.41  ? 3896 VAL A CB    1 
ATOM   17221 C  CG1   . VAL A 1 3896 ? 179.571 110.883 173.181 1.00 85.61  ? 3896 VAL A CG1   1 
ATOM   17222 C  CG2   . VAL A 1 3896 ? 177.346 111.753 172.430 1.00 85.75  ? 3896 VAL A CG2   1 
ATOM   17223 N  N     . GLY A 1 3897 ? 180.845 112.057 169.660 1.00 81.44  ? 3897 GLY A N     1 
ATOM   17224 C  CA    . GLY A 1 3897 ? 182.090 111.684 169.016 1.00 79.32  ? 3897 GLY A CA    1 
ATOM   17225 C  C     . GLY A 1 3897 ? 182.861 112.849 168.432 1.00 79.55  ? 3897 GLY A C     1 
ATOM   17226 O  O     . GLY A 1 3897 ? 183.421 112.742 167.337 1.00 82.67  ? 3897 GLY A O     1 
ATOM   17227 N  N     . GLU A 1 3898 ? 182.900 113.970 169.153 1.00 76.07  ? 3898 GLU A N     1 
ATOM   17228 C  CA    . GLU A 1 3898 ? 183.622 115.152 168.716 1.00 67.84  ? 3898 GLU A CA    1 
ATOM   17229 C  C     . GLU A 1 3898 ? 184.394 115.740 169.888 1.00 61.95  ? 3898 GLU A C     1 
ATOM   17230 O  O     . GLU A 1 3898 ? 183.907 115.713 171.028 1.00 65.03  ? 3898 GLU A O     1 
ATOM   17231 C  CB    . GLU A 1 3898 ? 182.672 116.215 168.147 1.00 69.02  ? 3898 GLU A CB    1 
ATOM   17232 C  CG    . GLU A 1 3898 ? 182.335 116.043 166.677 1.00 71.14  ? 3898 GLU A CG    1 
ATOM   17233 C  CD    . GLU A 1 3898 ? 183.545 116.177 165.778 1.00 75.99  ? 3898 GLU A CD    1 
ATOM   17234 O  OE1   . GLU A 1 3898 ? 184.373 117.080 166.021 1.00 76.54  ? 3898 GLU A OE1   1 
ATOM   17235 O  OE2   . GLU A 1 3898 ? 183.661 115.383 164.823 1.00 74.46  ? 3898 GLU A OE2   1 
ATOM   17236 N  N     . PRO A 1 3899 ? 185.589 116.269 169.645 1.00 62.23  ? 3899 PRO A N     1 
ATOM   17237 C  CA    . PRO A 1 3899 ? 186.287 117.021 170.691 1.00 60.94  ? 3899 PRO A CA    1 
ATOM   17238 C  C     . PRO A 1 3899 ? 185.552 118.312 171.014 1.00 59.92  ? 3899 PRO A C     1 
ATOM   17239 O  O     . PRO A 1 3899 ? 184.779 118.841 170.212 1.00 61.72  ? 3899 PRO A O     1 
ATOM   17240 C  CB    . PRO A 1 3899 ? 187.664 117.303 170.077 1.00 58.08  ? 3899 PRO A CB    1 
ATOM   17241 C  CG    . PRO A 1 3899 ? 187.810 116.302 168.975 1.00 62.16  ? 3899 PRO A CG    1 
ATOM   17242 C  CD    . PRO A 1 3899 ? 186.427 116.072 168.451 1.00 69.03  ? 3899 PRO A CD    1 
ATOM   17243 N  N     . THR A 1 3900 ? 185.800 118.814 172.226 1.00 61.23  ? 3900 THR A N     1 
ATOM   17244 C  CA    . THR A 1 3900 ? 185.141 120.041 172.663 1.00 64.77  ? 3900 THR A CA    1 
ATOM   17245 C  C     . THR A 1 3900 ? 185.529 121.221 171.780 1.00 63.85  ? 3900 THR A C     1 
ATOM   17246 O  O     . THR A 1 3900 ? 184.690 122.076 171.473 1.00 66.06  ? 3900 THR A O     1 
ATOM   17247 C  CB    . THR A 1 3900 ? 185.484 120.334 174.124 1.00 71.17  ? 3900 THR A CB    1 
ATOM   17248 O  OG1   . THR A 1 3900 ? 186.809 120.874 174.207 1.00 73.70  ? 3900 THR A OG1   1 
ATOM   17249 C  CG2   . THR A 1 3900 ? 185.406 119.063 174.954 1.00 73.19  ? 3900 THR A CG2   1 
ATOM   17250 N  N     . TYR A 1 3901 ? 186.796 121.281 171.364 1.00 65.00  ? 3901 TYR A N     1 
ATOM   17251 C  CA    . TYR A 1 3901 ? 187.317 122.377 170.544 1.00 60.00  ? 3901 TYR A CA    1 
ATOM   17252 C  C     . TYR A 1 3901 ? 187.115 123.722 171.236 1.00 58.86  ? 3901 TYR A C     1 
ATOM   17253 O  O     . TYR A 1 3901 ? 186.858 124.742 170.594 1.00 60.79  ? 3901 TYR A O     1 
ATOM   17254 C  CB    . TYR A 1 3901 ? 186.684 122.381 169.150 1.00 56.40  ? 3901 TYR A CB    1 
ATOM   17255 C  CG    . TYR A 1 3901 ? 187.126 121.226 168.281 1.00 61.30  ? 3901 TYR A CG    1 
ATOM   17256 C  CD1   . TYR A 1 3901 ? 188.470 121.017 168.003 1.00 59.31  ? 3901 TYR A CD1   1 
ATOM   17257 C  CD2   . TYR A 1 3901 ? 186.200 120.344 167.742 1.00 58.12  ? 3901 TYR A CD2   1 
ATOM   17258 C  CE1   . TYR A 1 3901 ? 188.879 119.961 167.213 1.00 59.68  ? 3901 TYR A CE1   1 
ATOM   17259 C  CE2   . TYR A 1 3901 ? 186.599 119.286 166.950 1.00 57.56  ? 3901 TYR A CE2   1 
ATOM   17260 C  CZ    . TYR A 1 3901 ? 187.940 119.099 166.689 1.00 61.61  ? 3901 TYR A CZ    1 
ATOM   17261 O  OH    . TYR A 1 3901 ? 188.343 118.045 165.902 1.00 66.93  ? 3901 TYR A OH    1 
ATOM   17262 N  N     . ASP A 1 3902 ? 187.234 123.722 172.566 1.00 62.65  ? 3902 ASP A N     1 
ATOM   17263 C  CA    . ASP A 1 3902 ? 187.027 124.949 173.326 1.00 63.13  ? 3902 ASP A CA    1 
ATOM   17264 C  C     . ASP A 1 3902 ? 188.153 125.946 173.088 1.00 58.50  ? 3902 ASP A C     1 
ATOM   17265 O  O     . ASP A 1 3902 ? 187.896 127.128 172.834 1.00 59.26  ? 3902 ASP A O     1 
ATOM   17266 C  CB    . ASP A 1 3902 ? 186.900 124.628 174.814 1.00 73.24  ? 3902 ASP A CB    1 
ATOM   17267 C  CG    . ASP A 1 3902 ? 185.621 123.884 175.143 1.00 76.24  ? 3902 ASP A CG    1 
ATOM   17268 O  OD1   . ASP A 1 3902 ? 184.616 124.083 174.429 1.00 74.95  ? 3902 ASP A OD1   1 
ATOM   17269 O  OD2   . ASP A 1 3902 ? 185.621 123.099 176.114 1.00 75.53  ? 3902 ASP A OD2   1 
ATOM   17270 N  N     . ALA A 1 3903 ? 189.405 125.487 173.155 1.00 56.03  ? 3903 ALA A N     1 
ATOM   17271 C  CA    . ALA A 1 3903 ? 190.539 126.393 172.996 1.00 53.10  ? 3903 ALA A CA    1 
ATOM   17272 C  C     . ALA A 1 3903 ? 190.567 127.007 171.603 1.00 57.33  ? 3903 ALA A C     1 
ATOM   17273 O  O     . ALA A 1 3903 ? 190.897 128.189 171.442 1.00 55.83  ? 3903 ALA A O     1 
ATOM   17274 C  CB    . ALA A 1 3903 ? 191.846 125.655 173.284 1.00 50.92  ? 3903 ALA A CB    1 
ATOM   17275 N  N     . GLU A 1 3904 ? 190.228 126.217 170.581 1.00 58.06  ? 3904 GLU A N     1 
ATOM   17276 C  CA    . GLU A 1 3904 ? 190.211 126.738 169.219 1.00 49.71  ? 3904 GLU A CA    1 
ATOM   17277 C  C     . GLU A 1 3904 ? 189.193 127.862 169.072 1.00 47.12  ? 3904 GLU A C     1 
ATOM   17278 O  O     . GLU A 1 3904 ? 189.487 128.899 168.467 1.00 53.16  ? 3904 GLU A O     1 
ATOM   17279 C  CB    . GLU A 1 3904 ? 189.914 125.610 168.232 1.00 47.81  ? 3904 GLU A CB    1 
ATOM   17280 C  CG    . GLU A 1 3904 ? 191.149 124.869 167.749 1.00 57.91  ? 3904 GLU A CG    1 
ATOM   17281 C  CD    . GLU A 1 3904 ? 191.564 123.754 168.688 1.00 69.64  ? 3904 GLU A CD    1 
ATOM   17282 O  OE1   . GLU A 1 3904 ? 192.782 123.576 168.901 1.00 68.39  ? 3904 GLU A OE1   1 
ATOM   17283 O  OE2   . GLU A 1 3904 ? 190.673 123.055 169.213 1.00 72.64  ? 3904 GLU A OE2   1 
ATOM   17284 N  N     . PHE A 1 3905 ? 187.997 127.688 169.638 1.00 41.61  ? 3905 PHE A N     1 
ATOM   17285 C  CA    . PHE A 1 3905 ? 186.986 128.735 169.540 1.00 40.38  ? 3905 PHE A CA    1 
ATOM   17286 C  C     . PHE A 1 3905 ? 187.335 129.944 170.401 1.00 46.70  ? 3905 PHE A C     1 
ATOM   17287 O  O     . PHE A 1 3905 ? 187.031 131.080 170.018 1.00 46.87  ? 3905 PHE A O     1 
ATOM   17288 C  CB    . PHE A 1 3905 ? 185.614 128.179 169.918 1.00 43.62  ? 3905 PHE A CB    1 
ATOM   17289 C  CG    . PHE A 1 3905 ? 184.927 127.459 168.792 1.00 46.73  ? 3905 PHE A CG    1 
ATOM   17290 C  CD1   . PHE A 1 3905 ? 184.655 128.113 167.602 1.00 42.38  ? 3905 PHE A CD1   1 
ATOM   17291 C  CD2   . PHE A 1 3905 ? 184.558 126.131 168.921 1.00 49.43  ? 3905 PHE A CD2   1 
ATOM   17292 C  CE1   . PHE A 1 3905 ? 184.026 127.457 166.562 1.00 44.17  ? 3905 PHE A CE1   1 
ATOM   17293 C  CE2   . PHE A 1 3905 ? 183.929 125.469 167.884 1.00 45.85  ? 3905 PHE A CE2   1 
ATOM   17294 C  CZ    . PHE A 1 3905 ? 183.662 126.133 166.704 1.00 46.66  ? 3905 PHE A CZ    1 
ATOM   17295 N  N     . GLN A 1 3906 ? 187.972 129.730 171.555 1.00 54.81  ? 3906 GLN A N     1 
ATOM   17296 C  CA    . GLN A 1 3906 ? 188.429 130.864 172.355 1.00 52.82  ? 3906 GLN A CA    1 
ATOM   17297 C  C     . GLN A 1 3906 ? 189.475 131.679 171.607 1.00 52.09  ? 3906 GLN A C     1 
ATOM   17298 O  O     . GLN A 1 3906 ? 189.464 132.914 171.663 1.00 57.29  ? 3906 GLN A O     1 
ATOM   17299 C  CB    . GLN A 1 3906 ? 188.979 130.391 173.701 1.00 52.00  ? 3906 GLN A CB    1 
ATOM   17300 C  CG    . GLN A 1 3906 ? 187.982 129.632 174.560 1.00 60.72  ? 3906 GLN A CG    1 
ATOM   17301 C  CD    . GLN A 1 3906 ? 186.572 130.178 174.445 1.00 70.54  ? 3906 GLN A CD    1 
ATOM   17302 O  OE1   . GLN A 1 3906 ? 186.315 131.340 174.761 1.00 73.67  ? 3906 GLN A OE1   1 
ATOM   17303 N  NE2   . GLN A 1 3906 ? 185.648 129.339 173.990 1.00 66.19  ? 3906 GLN A NE2   1 
ATOM   17304 N  N     . HIS A 1 3907 ? 190.392 131.011 170.904 1.00 48.26  ? 3907 HIS A N     1 
ATOM   17305 C  CA    . HIS A 1 3907 ? 191.364 131.750 170.104 1.00 52.16  ? 3907 HIS A CA    1 
ATOM   17306 C  C     . HIS A 1 3907 ? 190.714 132.392 168.886 1.00 51.29  ? 3907 HIS A C     1 
ATOM   17307 O  O     . HIS A 1 3907 ? 191.171 133.441 168.421 1.00 55.17  ? 3907 HIS A O     1 
ATOM   17308 C  CB    . HIS A 1 3907 ? 192.508 130.838 169.668 1.00 56.78  ? 3907 HIS A CB    1 
ATOM   17309 C  CG    . HIS A 1 3907 ? 193.658 131.576 169.056 1.00 63.02  ? 3907 HIS A CG    1 
ATOM   17310 N  ND1   . HIS A 1 3907 ? 193.807 131.727 167.695 1.00 59.47  ? 3907 HIS A ND1   1 
ATOM   17311 C  CD2   . HIS A 1 3907 ? 194.711 132.212 169.622 1.00 63.30  ? 3907 HIS A CD2   1 
ATOM   17312 C  CE1   . HIS A 1 3907 ? 194.902 132.424 167.448 1.00 59.94  ? 3907 HIS A CE1   1 
ATOM   17313 N  NE2   . HIS A 1 3907 ? 195.470 132.729 168.601 1.00 64.35  ? 3907 HIS A NE2   1 
ATOM   17314 N  N     . PHE A 1 3908 ? 189.663 131.774 168.347 1.00 49.14  ? 3908 PHE A N     1 
ATOM   17315 C  CA    . PHE A 1 3908 ? 188.943 132.372 167.229 1.00 42.24  ? 3908 PHE A CA    1 
ATOM   17316 C  C     . PHE A 1 3908 ? 188.228 133.649 167.655 1.00 43.07  ? 3908 PHE A C     1 
ATOM   17317 O  O     . PHE A 1 3908 ? 188.162 134.617 166.888 1.00 43.27  ? 3908 PHE A O     1 
ATOM   17318 C  CB    . PHE A 1 3908 ? 187.949 131.362 166.657 1.00 38.47  ? 3908 PHE A CB    1 
ATOM   17319 C  CG    . PHE A 1 3908 ? 187.275 131.816 165.396 1.00 36.01  ? 3908 PHE A CG    1 
ATOM   17320 C  CD1   . PHE A 1 3908 ? 188.021 132.215 164.301 1.00 36.20  ? 3908 PHE A CD1   1 
ATOM   17321 C  CD2   . PHE A 1 3908 ? 185.894 131.838 165.303 1.00 36.89  ? 3908 PHE A CD2   1 
ATOM   17322 C  CE1   . PHE A 1 3908 ? 187.403 132.631 163.139 1.00 34.37  ? 3908 PHE A CE1   1 
ATOM   17323 C  CE2   . PHE A 1 3908 ? 185.271 132.252 164.144 1.00 33.22  ? 3908 PHE A CE2   1 
ATOM   17324 C  CZ    . PHE A 1 3908 ? 186.027 132.648 163.060 1.00 35.21  ? 3908 PHE A CZ    1 
ATOM   17325 N  N     . LEU A 1 3909 ? 187.687 133.670 168.874 1.00 45.09  ? 3909 LEU A N     1 
ATOM   17326 C  CA    . LEU A 1 3909 ? 186.915 134.821 169.332 1.00 44.84  ? 3909 LEU A CA    1 
ATOM   17327 C  C     . LEU A 1 3909 ? 187.809 135.903 169.930 1.00 52.45  ? 3909 LEU A C     1 
ATOM   17328 O  O     . LEU A 1 3909 ? 187.825 137.043 169.453 1.00 58.98  ? 3909 LEU A O     1 
ATOM   17329 C  CB    . LEU A 1 3909 ? 185.861 134.370 170.346 1.00 47.21  ? 3909 LEU A CB    1 
ATOM   17330 C  CG    . LEU A 1 3909 ? 184.658 133.625 169.766 1.00 48.88  ? 3909 LEU A CG    1 
ATOM   17331 C  CD1   . LEU A 1 3909 ? 183.676 133.254 170.864 1.00 52.76  ? 3909 LEU A CD1   1 
ATOM   17332 C  CD2   . LEU A 1 3909 ? 183.976 134.457 168.691 1.00 41.60  ? 3909 LEU A CD2   1 
ATOM   17333 N  N     . ARG A 1 3910 ? 188.562 135.567 170.976 1.00 55.94  ? 3910 ARG A N     1 
ATOM   17334 C  CA    . ARG A 1 3910 ? 189.396 136.524 171.698 1.00 62.07  ? 3910 ARG A CA    1 
ATOM   17335 C  C     . ARG A 1 3910 ? 190.869 136.390 171.320 1.00 66.86  ? 3910 ARG A C     1 
ATOM   17336 O  O     . ARG A 1 3910 ? 191.757 136.548 172.160 1.00 72.57  ? 3910 ARG A O     1 
ATOM   17337 C  CB    . ARG A 1 3910 ? 189.232 136.361 173.206 1.00 61.92  ? 3910 ARG A CB    1 
ATOM   17338 C  CG    . ARG A 1 3910 ? 187.797 136.234 173.681 1.00 64.56  ? 3910 ARG A CG    1 
ATOM   17339 C  CD    . ARG A 1 3910 ? 187.635 136.824 175.078 1.00 64.51  ? 3910 ARG A CD    1 
ATOM   17340 N  NE    . ARG A 1 3910 ? 186.348 136.513 175.691 1.00 67.06  ? 3910 ARG A NE    1 
ATOM   17341 C  CZ    . ARG A 1 3910 ? 185.905 135.290 175.961 1.00 72.40  ? 3910 ARG A CZ    1 
ATOM   17342 N  NH1   . ARG A 1 3910 ? 186.644 134.216 175.730 1.00 67.20  ? 3910 ARG A NH1   1 
ATOM   17343 N  NH2   . ARG A 1 3910 ? 184.695 135.143 176.491 1.00 73.50  ? 3910 ARG A NH2   1 
ATOM   17344 N  N     . GLY A 1 3911 ? 191.144 136.088 170.051 1.00 65.44  ? 3911 GLY A N     1 
ATOM   17345 C  CA    . GLY A 1 3911 ? 192.525 135.940 169.623 1.00 64.71  ? 3911 GLY A CA    1 
ATOM   17346 C  C     . GLY A 1 3911 ? 193.305 137.239 169.673 1.00 74.74  ? 3911 GLY A C     1 
ATOM   17347 O  O     . GLY A 1 3911 ? 194.456 137.264 170.117 1.00 76.81  ? 3911 GLY A O     1 
ATOM   17348 N  N     . ASN A 1 3912 ? 192.688 138.337 169.234 1.00 78.58  ? 3912 ASN A N     1 
ATOM   17349 C  CA    . ASN A 1 3912 ? 193.369 139.623 169.136 1.00 78.34  ? 3912 ASN A CA    1 
ATOM   17350 C  C     . ASN A 1 3912 ? 193.695 140.238 170.490 1.00 80.57  ? 3912 ASN A C     1 
ATOM   17351 O  O     . ASN A 1 3912 ? 194.298 141.317 170.524 1.00 85.31  ? 3912 ASN A O     1 
ATOM   17352 C  CB    . ASN A 1 3912 ? 192.520 140.598 168.318 1.00 77.98  ? 3912 ASN A CB    1 
ATOM   17353 C  CG    . ASN A 1 3912 ? 191.079 140.652 168.788 1.00 81.12  ? 3912 ASN A CG    1 
ATOM   17354 O  OD1   . ASN A 1 3912 ? 190.421 139.621 168.929 1.00 78.32  ? 3912 ASN A OD1   1 
ATOM   17355 N  ND2   . ASN A 1 3912 ? 190.582 141.858 169.034 1.00 80.41  ? 3912 ASN A ND2   1 
ATOM   17356 N  N     . GLU A 1 3913 ? 193.323 139.597 171.595 1.00 78.52  ? 3913 GLU A N     1 
ATOM   17357 C  CA    . GLU A 1 3913 ? 193.595 140.116 172.928 1.00 80.69  ? 3913 GLU A CA    1 
ATOM   17358 C  C     . GLU A 1 3913 ? 194.903 139.596 173.512 1.00 89.96  ? 3913 GLU A C     1 
ATOM   17359 O  O     . GLU A 1 3913 ? 195.209 139.892 174.672 1.00 94.85  ? 3913 GLU A O     1 
ATOM   17360 C  CB    . GLU A 1 3913 ? 192.434 139.783 173.868 1.00 77.49  ? 3913 GLU A CB    1 
ATOM   17361 C  CG    . GLU A 1 3913 ? 191.152 140.534 173.552 1.00 79.01  ? 3913 GLU A CG    1 
ATOM   17362 C  CD    . GLU A 1 3913 ? 189.994 140.107 174.431 1.00 87.21  ? 3913 GLU A CD    1 
ATOM   17363 O  OE1   . GLU A 1 3913 ? 188.909 139.815 173.886 1.00 84.97  ? 3913 GLU A OE1   1 
ATOM   17364 O  OE2   . GLU A 1 3913 ? 190.169 140.064 175.667 1.00 86.33  ? 3913 GLU A OE2   1 
ATOM   17365 N  N     . ILE A 1 3914 ? 195.675 138.833 172.745 1.00 89.06  ? 3914 ILE A N     1 
ATOM   17366 C  CA    . ILE A 1 3914 ? 196.966 138.335 173.211 1.00 90.91  ? 3914 ILE A CA    1 
ATOM   17367 C  C     . ILE A 1 3914 ? 198.008 139.428 173.009 1.00 96.25  ? 3914 ILE A C     1 
ATOM   17368 O  O     . ILE A 1 3914 ? 198.200 139.920 171.892 1.00 88.89  ? 3914 ILE A O     1 
ATOM   17369 C  CB    . ILE A 1 3914 ? 197.362 137.048 172.475 1.00 83.91  ? 3914 ILE A CB    1 
ATOM   17370 C  CG1   . ILE A 1 3914 ? 196.492 135.878 172.941 1.00 73.05  ? 3914 ILE A CG1   1 
ATOM   17371 C  CG2   . ILE A 1 3914 ? 198.836 136.739 172.693 1.00 88.39  ? 3914 ILE A CG2   1 
ATOM   17372 C  CD1   . ILE A 1 3914 ? 196.745 134.592 172.188 1.00 72.45  ? 3914 ILE A CD1   1 
ATOM   17373 N  N     . VAL A 1 3915 ? 198.683 139.807 174.090 1.00 101.85 ? 3915 VAL A N     1 
ATOM   17374 C  CA    . VAL A 1 3915 ? 199.664 140.887 174.045 1.00 103.07 ? 3915 VAL A CA    1 
ATOM   17375 C  C     . VAL A 1 3915 ? 200.944 140.377 173.397 1.00 106.06 ? 3915 VAL A C     1 
ATOM   17376 O  O     . VAL A 1 3915 ? 201.446 139.301 173.745 1.00 101.31 ? 3915 VAL A O     1 
ATOM   17377 C  CB    . VAL A 1 3915 ? 199.934 141.433 175.455 1.00 106.43 ? 3915 VAL A CB    1 
ATOM   17378 C  CG1   . VAL A 1 3915 ? 200.792 142.687 175.383 1.00 110.71 ? 3915 VAL A CG1   1 
ATOM   17379 C  CG2   . VAL A 1 3915 ? 198.624 141.715 176.173 1.00 104.76 ? 3915 VAL A CG2   1 
ATOM   17380 N  N     . LEU A 1 3916 ? 201.475 141.149 172.457 1.00 108.32 ? 3916 LEU A N     1 
ATOM   17381 C  CA    . LEU A 1 3916 ? 202.692 140.808 171.734 1.00 111.80 ? 3916 LEU A CA    1 
ATOM   17382 C  C     . LEU A 1 3916 ? 203.731 141.908 171.931 1.00 119.86 ? 3916 LEU A C     1 
ATOM   17383 O  O     . LEU A 1 3916 ? 203.517 142.873 172.669 1.00 122.69 ? 3916 LEU A O     1 
ATOM   17384 C  CB    . LEU A 1 3916 ? 202.397 140.589 170.247 1.00 112.99 ? 3916 LEU A CB    1 
ATOM   17385 C  CG    . LEU A 1 3916 ? 201.635 139.310 169.894 1.00 102.06 ? 3916 LEU A CG    1 
ATOM   17386 C  CD1   . LEU A 1 3916 ? 201.613 139.094 168.389 1.00 91.18  ? 3916 LEU A CD1   1 
ATOM   17387 C  CD2   . LEU A 1 3916 ? 202.237 138.107 170.605 1.00 95.93  ? 3916 LEU A CD2   1 
ATOM   17388 N  N     . SER A 1 3917 ? 204.868 141.753 171.258 1.00 124.92 ? 3917 SER A N     1 
ATOM   17389 C  CA    . SER A 1 3917 ? 205.970 142.696 171.370 1.00 131.00 ? 3917 SER A CA    1 
ATOM   17390 C  C     . SER A 1 3917 ? 206.574 142.935 169.994 1.00 138.00 ? 3917 SER A C     1 
ATOM   17391 O  O     . SER A 1 3917 ? 206.350 142.171 169.052 1.00 135.31 ? 3917 SER A O     1 
ATOM   17392 C  CB    . SER A 1 3917 ? 207.048 142.195 172.342 1.00 123.40 ? 3917 SER A CB    1 
ATOM   17393 O  OG    . SER A 1 3917 ? 206.509 141.978 173.635 1.00 114.40 ? 3917 SER A OG    1 
ATOM   17394 N  N     . ALA A 1 3918 ? 207.342 144.023 169.889 1.00 139.74 ? 3918 ALA A N     1 
ATOM   17395 C  CA    . ALA A 1 3918 ? 208.002 144.346 168.628 1.00 137.76 ? 3918 ALA A CA    1 
ATOM   17396 C  C     . ALA A 1 3918 ? 209.004 143.267 168.236 1.00 138.13 ? 3918 ALA A C     1 
ATOM   17397 O  O     . ALA A 1 3918 ? 209.102 142.898 167.059 1.00 132.86 ? 3918 ALA A O     1 
ATOM   17398 C  CB    . ALA A 1 3918 ? 208.688 145.707 168.727 1.00 124.26 ? 3918 ALA A CB    1 
ATOM   17399 N  N     . GLY A 1 3919 ? 209.757 142.750 169.206 1.00 137.62 ? 3919 GLY A N     1 
ATOM   17400 C  CA    . GLY A 1 3919 ? 210.711 141.692 168.933 1.00 136.40 ? 3919 GLY A CA    1 
ATOM   17401 C  C     . GLY A 1 3919 ? 210.109 140.322 168.722 1.00 132.59 ? 3919 GLY A C     1 
ATOM   17402 O  O     . GLY A 1 3919 ? 210.817 139.410 168.283 1.00 128.67 ? 3919 GLY A O     1 
ATOM   17403 N  N     . SER A 1 3920 ? 208.820 140.152 169.025 1.00 130.72 ? 3920 SER A N     1 
ATOM   17404 C  CA    . SER A 1 3920 ? 208.172 138.864 168.802 1.00 128.05 ? 3920 SER A CA    1 
ATOM   17405 C  C     . SER A 1 3920 ? 207.985 138.590 167.315 1.00 122.81 ? 3920 SER A C     1 
ATOM   17406 O  O     . SER A 1 3920 ? 208.013 137.431 166.883 1.00 113.21 ? 3920 SER A O     1 
ATOM   17407 C  CB    . SER A 1 3920 ? 206.830 138.818 169.531 1.00 122.91 ? 3920 SER A CB    1 
ATOM   17408 O  OG    . SER A 1 3920 ? 207.012 138.842 170.936 1.00 122.15 ? 3920 SER A OG    1 
ATOM   17409 N  N     . THR A 1 3921 ? 207.790 139.634 166.522 1.00 122.06 ? 3921 THR A N     1 
ATOM   17410 C  CA    . THR A 1 3921 ? 207.615 139.471 165.084 1.00 113.53 ? 3921 THR A CA    1 
ATOM   17411 C  C     . THR A 1 3921 ? 208.950 139.136 164.430 1.00 115.25 ? 3921 THR A C     1 
ATOM   17412 O  O     . THR A 1 3921 ? 209.901 139.920 164.548 1.00 118.03 ? 3921 THR A O     1 
ATOM   17413 C  CB    . THR A 1 3921 ? 207.032 140.743 164.475 1.00 111.82 ? 3921 THR A CB    1 
ATOM   17414 O  OG1   . THR A 1 3921 ? 205.768 141.031 165.085 1.00 108.45 ? 3921 THR A OG1   1 
ATOM   17415 C  CG2   . THR A 1 3921 ? 206.842 140.577 162.975 1.00 108.08 ? 3921 THR A CG2   1 
ATOM   17416 N  N     . PRO A 1 3922 ? 209.072 138.003 163.742 1.00 112.05 ? 3922 PRO A N     1 
ATOM   17417 C  CA    . PRO A 1 3922 ? 210.341 137.638 163.097 1.00 111.48 ? 3922 PRO A CA    1 
ATOM   17418 C  C     . PRO A 1 3922 ? 210.471 138.050 161.637 1.00 110.41 ? 3922 PRO A C     1 
ATOM   17419 O  O     . PRO A 1 3922 ? 211.424 137.613 160.985 1.00 110.93 ? 3922 PRO A O     1 
ATOM   17420 C  CB    . PRO A 1 3922 ? 210.338 136.108 163.221 1.00 107.89 ? 3922 PRO A CB    1 
ATOM   17421 C  CG    . PRO A 1 3922 ? 208.885 135.728 163.211 1.00 105.06 ? 3922 PRO A CG    1 
ATOM   17422 C  CD    . PRO A 1 3922 ? 208.069 136.931 163.629 1.00 108.63 ? 3922 PRO A CD    1 
ATOM   17423 N  N     . ARG A 1 3923 ? 209.552 138.865 161.112 1.00 103.45 ? 3923 ARG A N     1 
ATOM   17424 C  CA    . ARG A 1 3923 ? 209.617 139.380 159.742 1.00 100.47 ? 3923 ARG A CA    1 
ATOM   17425 C  C     . ARG A 1 3923 ? 209.648 138.229 158.729 1.00 100.13 ? 3923 ARG A C     1 
ATOM   17426 O  O     . ARG A 1 3923 ? 210.636 137.981 158.034 1.00 102.50 ? 3923 ARG A O     1 
ATOM   17427 C  CB    . ARG A 1 3923 ? 210.816 140.324 159.573 1.00 98.85  ? 3923 ARG A CB    1 
ATOM   17428 C  CG    . ARG A 1 3923 ? 210.926 141.001 158.206 1.00 98.53  ? 3923 ARG A CG    1 
ATOM   17429 C  CD    . ARG A 1 3923 ? 209.572 141.458 157.682 1.00 100.70 ? 3923 ARG A CD    1 
ATOM   17430 N  NE    . ARG A 1 3923 ? 209.256 142.822 158.084 1.00 100.67 ? 3923 ARG A NE    1 
ATOM   17431 C  CZ    . ARG A 1 3923 ? 208.056 143.227 158.478 1.00 95.71  ? 3923 ARG A CZ    1 
ATOM   17432 N  NH1   . ARG A 1 3923 ? 207.031 142.392 158.539 1.00 94.43  ? 3923 ARG A NH1   1 
ATOM   17433 N  NH2   . ARG A 1 3923 ? 207.880 144.500 158.819 1.00 87.02  ? 3923 ARG A NH2   1 
ATOM   17434 N  N     . ILE A 1 3924 ? 208.530 137.503 158.694 1.00 95.29  ? 3924 ILE A N     1 
ATOM   17435 C  CA    . ILE A 1 3924 ? 208.356 136.442 157.709 1.00 93.63  ? 3924 ILE A CA    1 
ATOM   17436 C  C     . ILE A 1 3924 ? 208.316 137.053 156.316 1.00 95.47  ? 3924 ILE A C     1 
ATOM   17437 O  O     . ILE A 1 3924 ? 207.582 138.018 156.065 1.00 92.84  ? 3924 ILE A O     1 
ATOM   17438 C  CB    . ILE A 1 3924 ? 207.075 135.639 157.991 1.00 92.78  ? 3924 ILE A CB    1 
ATOM   17439 C  CG1   . ILE A 1 3924 ? 207.142 134.932 159.348 1.00 84.33  ? 3924 ILE A CG1   1 
ATOM   17440 C  CG2   . ILE A 1 3924 ? 206.808 134.642 156.873 1.00 92.06  ? 3924 ILE A CG2   1 
ATOM   17441 C  CD1   . ILE A 1 3924 ? 206.572 135.741 160.493 1.00 81.37  ? 3924 ILE A CD1   1 
ATOM   17442 N  N     . GLN A 1 3925 ? 209.108 136.499 155.402 1.00 98.17  ? 3925 GLN A N     1 
ATOM   17443 C  CA    . GLN A 1 3925 ? 209.088 136.970 154.026 1.00 99.00  ? 3925 GLN A CA    1 
ATOM   17444 C  C     . GLN A 1 3925 ? 207.786 136.557 153.345 1.00 98.52  ? 3925 GLN A C     1 
ATOM   17445 O  O     . GLN A 1 3925 ? 207.224 135.491 153.615 1.00 91.29  ? 3925 GLN A O     1 
ATOM   17446 C  CB    . GLN A 1 3925 ? 210.298 136.435 153.255 1.00 96.49  ? 3925 GLN A CB    1 
ATOM   17447 C  CG    . GLN A 1 3925 ? 210.054 135.152 152.475 1.00 104.12 ? 3925 GLN A CG    1 
ATOM   17448 C  CD    . GLN A 1 3925 ? 210.487 133.915 153.236 1.00 103.72 ? 3925 GLN A CD    1 
ATOM   17449 O  OE1   . GLN A 1 3925 ? 210.644 133.947 154.456 1.00 107.08 ? 3925 GLN A OE1   1 
ATOM   17450 N  NE2   . GLN A 1 3925 ? 210.681 132.816 152.517 1.00 96.15  ? 3925 GLN A NE2   1 
ATOM   17451 N  N     . GLY A 1 3926 ? 207.290 137.433 152.475 1.00 97.67  ? 3926 GLY A N     1 
ATOM   17452 C  CA    . GLY A 1 3926 ? 206.035 137.201 151.795 1.00 91.04  ? 3926 GLY A CA    1 
ATOM   17453 C  C     . GLY A 1 3926 ? 204.800 137.481 152.621 1.00 91.21  ? 3926 GLY A C     1 
ATOM   17454 O  O     . GLY A 1 3926 ? 203.684 137.293 152.119 1.00 85.25  ? 3926 GLY A O     1 
ATOM   17455 N  N     . LEU A 1 3927 ? 204.959 137.926 153.865 1.00 88.52  ? 3927 LEU A N     1 
ATOM   17456 C  CA    . LEU A 1 3927 ? 203.847 138.211 154.759 1.00 77.48  ? 3927 LEU A CA    1 
ATOM   17457 C  C     . LEU A 1 3927 ? 203.937 139.655 155.225 1.00 80.00  ? 3927 LEU A C     1 
ATOM   17458 O  O     . LEU A 1 3927 ? 205.034 140.175 155.450 1.00 86.37  ? 3927 LEU A O     1 
ATOM   17459 C  CB    . LEU A 1 3927 ? 203.849 137.275 155.975 1.00 75.49  ? 3927 LEU A CB    1 
ATOM   17460 C  CG    . LEU A 1 3927 ? 202.917 136.063 155.954 1.00 76.51  ? 3927 LEU A CG    1 
ATOM   17461 C  CD1   . LEU A 1 3927 ? 203.127 135.233 154.698 1.00 78.39  ? 3927 LEU A CD1   1 
ATOM   17462 C  CD2   . LEU A 1 3927 ? 203.117 135.215 157.199 1.00 73.17  ? 3927 LEU A CD2   1 
ATOM   17463 N  N     . THR A 1 3928 ? 202.782 140.299 155.370 1.00 78.15  ? 3928 THR A N     1 
ATOM   17464 C  CA    . THR A 1 3928 ? 202.745 141.665 155.864 1.00 77.26  ? 3928 THR A CA    1 
ATOM   17465 C  C     . THR A 1 3928 ? 202.987 141.681 157.372 1.00 72.13  ? 3928 THR A C     1 
ATOM   17466 O  O     . THR A 1 3928 ? 203.178 140.642 158.012 1.00 71.70  ? 3928 THR A O     1 
ATOM   17467 C  CB    . THR A 1 3928 ? 201.415 142.328 155.514 1.00 78.60  ? 3928 THR A CB    1 
ATOM   17468 O  OG1   . THR A 1 3928 ? 200.344 141.623 156.151 1.00 79.56  ? 3928 THR A OG1   1 
ATOM   17469 C  CG2   . THR A 1 3928 ? 201.195 142.316 154.009 1.00 70.28  ? 3928 THR A CG2   1 
ATOM   17470 N  N     . VAL A 1 3929 ? 202.986 142.882 157.951 1.00 76.18  ? 3929 VAL A N     1 
ATOM   17471 C  CA    . VAL A 1 3929 ? 203.242 143.015 159.382 1.00 80.31  ? 3929 VAL A CA    1 
ATOM   17472 C  C     . VAL A 1 3929 ? 202.085 142.431 160.187 1.00 78.36  ? 3929 VAL A C     1 
ATOM   17473 O  O     . VAL A 1 3929 ? 202.291 141.664 161.136 1.00 83.15  ? 3929 VAL A O     1 
ATOM   17474 C  CB    . VAL A 1 3929 ? 203.501 144.489 159.743 1.00 80.50  ? 3929 VAL A CB    1 
ATOM   17475 C  CG1   . VAL A 1 3929 ? 204.005 144.608 161.171 1.00 79.49  ? 3929 VAL A CG1   1 
ATOM   17476 C  CG2   . VAL A 1 3929 ? 204.494 145.106 158.769 1.00 79.59  ? 3929 VAL A CG2   1 
ATOM   17477 N  N     . GLU A 1 3930 ? 200.850 142.780 159.814 1.00 76.11  ? 3930 GLU A N     1 
ATOM   17478 C  CA    . GLU A 1 3930 ? 199.684 142.265 160.525 1.00 79.03  ? 3930 GLU A CA    1 
ATOM   17479 C  C     . GLU A 1 3930 ? 199.566 140.754 160.372 1.00 71.77  ? 3930 GLU A C     1 
ATOM   17480 O  O     . GLU A 1 3930 ? 199.199 140.055 161.325 1.00 74.07  ? 3930 GLU A O     1 
ATOM   17481 C  CB    . GLU A 1 3930 ? 198.413 142.958 160.025 1.00 79.17  ? 3930 GLU A CB    1 
ATOM   17482 C  CG    . GLU A 1 3930 ? 198.152 144.372 160.577 1.00 86.34  ? 3930 GLU A CG    1 
ATOM   17483 C  CD    . GLU A 1 3930 ? 198.118 144.479 162.105 1.00 92.67  ? 3930 GLU A CD    1 
ATOM   17484 O  OE1   . GLU A 1 3930 ? 198.280 143.462 162.813 1.00 94.91  ? 3930 GLU A OE1   1 
ATOM   17485 O  OE2   . GLU A 1 3930 ? 197.925 145.609 162.603 1.00 86.27  ? 3930 GLU A OE2   1 
ATOM   17486 N  N     . GLN A 1 3931 ? 199.866 140.233 159.181 1.00 65.38  ? 3931 GLN A N     1 
ATOM   17487 C  CA    . GLN A 1 3931 ? 199.870 138.787 158.994 1.00 61.94  ? 3931 GLN A CA    1 
ATOM   17488 C  C     . GLN A 1 3931 ? 200.914 138.125 159.884 1.00 67.25  ? 3931 GLN A C     1 
ATOM   17489 O  O     . GLN A 1 3931 ? 200.666 137.055 160.449 1.00 68.43  ? 3931 GLN A O     1 
ATOM   17490 C  CB    . GLN A 1 3931 ? 200.117 138.442 157.525 1.00 62.24  ? 3931 GLN A CB    1 
ATOM   17491 C  CG    . GLN A 1 3931 ? 198.961 138.794 156.604 1.00 59.96  ? 3931 GLN A CG    1 
ATOM   17492 C  CD    . GLN A 1 3931 ? 199.075 138.131 155.246 1.00 63.52  ? 3931 GLN A CD    1 
ATOM   17493 O  OE1   . GLN A 1 3931 ? 200.023 137.395 154.980 1.00 70.63  ? 3931 GLN A OE1   1 
ATOM   17494 N  NE2   . GLN A 1 3931 ? 198.103 138.387 154.380 1.00 67.23  ? 3931 GLN A NE2   1 
ATOM   17495 N  N     . ALA A 1 3932 ? 202.087 138.747 160.022 1.00 74.66  ? 3932 ALA A N     1 
ATOM   17496 C  CA    . ALA A 1 3932 ? 203.115 138.201 160.902 1.00 74.63  ? 3932 ALA A CA    1 
ATOM   17497 C  C     . ALA A 1 3932 ? 202.660 138.201 162.358 1.00 71.45  ? 3932 ALA A C     1 
ATOM   17498 O  O     . ALA A 1 3932 ? 202.901 137.230 163.089 1.00 72.39  ? 3932 ALA A O     1 
ATOM   17499 C  CB    . ALA A 1 3932 ? 204.414 138.989 160.743 1.00 84.31  ? 3932 ALA A CB    1 
ATOM   17500 N  N     . GLU A 1 3933 ? 202.006 139.279 162.799 1.00 71.02  ? 3933 GLU A N     1 
ATOM   17501 C  CA    . GLU A 1 3933 ? 201.477 139.303 164.160 1.00 69.80  ? 3933 GLU A CA    1 
ATOM   17502 C  C     . GLU A 1 3933 ? 200.422 138.224 164.357 1.00 74.45  ? 3933 GLU A C     1 
ATOM   17503 O  O     . GLU A 1 3933 ? 200.356 137.599 165.421 1.00 77.30  ? 3933 GLU A O     1 
ATOM   17504 C  CB    . GLU A 1 3933 ? 200.893 140.676 164.499 1.00 70.63  ? 3933 GLU A CB    1 
ATOM   17505 C  CG    . GLU A 1 3933 ? 201.908 141.798 164.630 1.00 84.34  ? 3933 GLU A CG    1 
ATOM   17506 C  CD    . GLU A 1 3933 ? 201.361 143.132 164.160 1.00 90.26  ? 3933 GLU A CD    1 
ATOM   17507 O  OE1   . GLU A 1 3933 ? 200.617 143.774 164.930 1.00 92.83  ? 3933 GLU A OE1   1 
ATOM   17508 O  OE2   . GLU A 1 3933 ? 201.670 143.541 163.024 1.00 87.54  ? 3933 GLU A OE2   1 
ATOM   17509 N  N     . ALA A 1 3934 ? 199.576 138.002 163.349 1.00 72.09  ? 3934 ALA A N     1 
ATOM   17510 C  CA    . ALA A 1 3934 ? 198.569 136.950 163.448 1.00 61.20  ? 3934 ALA A CA    1 
ATOM   17511 C  C     . ALA A 1 3934 ? 199.212 135.569 163.521 1.00 63.09  ? 3934 ALA A C     1 
ATOM   17512 O  O     . ALA A 1 3934 ? 198.749 134.700 164.268 1.00 66.46  ? 3934 ALA A O     1 
ATOM   17513 C  CB    . ALA A 1 3934 ? 197.604 137.034 162.266 1.00 56.68  ? 3934 ALA A CB    1 
ATOM   17514 N  N     . VAL A 1 3935 ? 200.274 135.346 162.743 1.00 61.53  ? 3935 VAL A N     1 
ATOM   17515 C  CA    . VAL A 1 3935 ? 200.981 134.066 162.788 1.00 61.40  ? 3935 VAL A CA    1 
ATOM   17516 C  C     . VAL A 1 3935 ? 201.588 133.845 164.166 1.00 68.57  ? 3935 VAL A C     1 
ATOM   17517 O  O     . VAL A 1 3935 ? 201.498 132.751 164.737 1.00 68.41  ? 3935 VAL A O     1 
ATOM   17518 C  CB    . VAL A 1 3935 ? 202.056 134.000 161.688 1.00 66.17  ? 3935 VAL A CB    1 
ATOM   17519 C  CG1   . VAL A 1 3935 ? 202.858 132.716 161.814 1.00 70.12  ? 3935 VAL A CG1   1 
ATOM   17520 C  CG2   . VAL A 1 3935 ? 201.419 134.079 160.323 1.00 72.40  ? 3935 VAL A CG2   1 
ATOM   17521 N  N     . VAL A 1 3936 ? 202.221 134.881 164.719 1.00 70.00  ? 3936 VAL A N     1 
ATOM   17522 C  CA    . VAL A 1 3936 ? 202.810 134.764 166.050 1.00 69.20  ? 3936 VAL A CA    1 
ATOM   17523 C  C     . VAL A 1 3936 ? 201.727 134.492 167.087 1.00 72.02  ? 3936 VAL A C     1 
ATOM   17524 O  O     . VAL A 1 3936 ? 201.892 133.649 167.978 1.00 70.15  ? 3936 VAL A O     1 
ATOM   17525 C  CB    . VAL A 1 3936 ? 203.620 136.030 166.387 1.00 74.69  ? 3936 VAL A CB    1 
ATOM   17526 C  CG1   . VAL A 1 3936 ? 203.837 136.149 167.888 1.00 79.19  ? 3936 VAL A CG1   1 
ATOM   17527 C  CG2   . VAL A 1 3936 ? 204.950 136.019 165.649 1.00 86.67  ? 3936 VAL A CG2   1 
ATOM   17528 N  N     . ARG A 1 3937 ? 200.599 135.197 166.980 1.00 73.82  ? 3937 ARG A N     1 
ATOM   17529 C  CA    . ARG A 1 3937 ? 199.493 135.002 167.912 1.00 67.69  ? 3937 ARG A CA    1 
ATOM   17530 C  C     . ARG A 1 3937 ? 198.915 133.596 167.798 1.00 66.40  ? 3937 ARG A C     1 
ATOM   17531 O  O     . ARG A 1 3937 ? 198.619 132.949 168.809 1.00 67.74  ? 3937 ARG A O     1 
ATOM   17532 C  CB    . ARG A 1 3937 ? 198.414 136.051 167.650 1.00 67.38  ? 3937 ARG A CB    1 
ATOM   17533 C  CG    . ARG A 1 3937 ? 197.752 136.594 168.897 1.00 79.99  ? 3937 ARG A CG    1 
ATOM   17534 C  CD    . ARG A 1 3937 ? 197.120 137.950 168.630 1.00 83.01  ? 3937 ARG A CD    1 
ATOM   17535 N  NE    . ARG A 1 3937 ? 198.103 138.955 168.248 1.00 81.84  ? 3937 ARG A NE    1 
ATOM   17536 C  CZ    . ARG A 1 3937 ? 197.894 139.899 167.341 1.00 84.69  ? 3937 ARG A CZ    1 
ATOM   17537 N  NH1   . ARG A 1 3937 ? 196.746 139.988 166.689 1.00 82.92  ? 3937 ARG A NH1   1 
ATOM   17538 N  NH2   . ARG A 1 3937 ? 198.859 140.777 167.083 1.00 87.54  ? 3937 ARG A NH2   1 
ATOM   17539 N  N     . LEU A 1 3938 ? 198.744 133.106 166.567 1.00 65.32  ? 3938 LEU A N     1 
ATOM   17540 C  CA    . LEU A 1 3938 ? 198.179 131.778 166.359 1.00 60.49  ? 3938 LEU A CA    1 
ATOM   17541 C  C     . LEU A 1 3938 ? 199.119 130.670 166.817 1.00 66.31  ? 3938 LEU A C     1 
ATOM   17542 O  O     . LEU A 1 3938 ? 198.654 129.569 167.130 1.00 66.96  ? 3938 LEU A O     1 
ATOM   17543 C  CB    . LEU A 1 3938 ? 197.819 131.591 164.882 1.00 54.97  ? 3938 LEU A CB    1 
ATOM   17544 C  CG    . LEU A 1 3938 ? 197.178 130.271 164.446 1.00 51.05  ? 3938 LEU A CG    1 
ATOM   17545 C  CD1   . LEU A 1 3938 ? 195.894 130.011 165.213 1.00 48.96  ? 3938 LEU A CD1   1 
ATOM   17546 C  CD2   . LEU A 1 3938 ? 196.915 130.269 162.950 1.00 50.59  ? 3938 LEU A CD2   1 
ATOM   17547 N  N     . SER A 1 3939 ? 200.425 130.941 166.879 1.00 71.26  ? 3939 SER A N     1 
ATOM   17548 C  CA    . SER A 1 3939 ? 201.380 129.922 167.299 1.00 74.05  ? 3939 SER A CA    1 
ATOM   17549 C  C     . SER A 1 3939 ? 201.229 129.552 168.769 1.00 72.44  ? 3939 SER A C     1 
ATOM   17550 O  O     . SER A 1 3939 ? 201.807 128.551 169.206 1.00 66.80  ? 3939 SER A O     1 
ATOM   17551 C  CB    . SER A 1 3939 ? 202.808 130.397 167.027 1.00 72.22  ? 3939 SER A CB    1 
ATOM   17552 O  OG    . SER A 1 3939 ? 203.067 130.459 165.635 1.00 73.96  ? 3939 SER A OG    1 
ATOM   17553 N  N     . CYS A 1 3940 ? 200.471 130.335 169.540 1.00 76.51  ? 3940 CYS A N     1 
ATOM   17554 C  CA    . CYS A 1 3940 ? 200.276 130.017 170.951 1.00 80.13  ? 3940 CYS A CA    1 
ATOM   17555 C  C     . CYS A 1 3940 ? 199.491 128.725 171.137 1.00 78.14  ? 3940 CYS A C     1 
ATOM   17556 O  O     . CYS A 1 3940 ? 199.603 128.080 172.186 1.00 78.51  ? 3940 CYS A O     1 
ATOM   17557 C  CB    . CYS A 1 3940 ? 199.568 131.175 171.655 1.00 80.33  ? 3940 CYS A CB    1 
ATOM   17558 S  SG    . CYS A 1 3940 ? 200.674 132.480 172.238 1.00 94.02  ? 3940 CYS A SG    1 
ATOM   17559 N  N     . LEU A 1 3941 ? 198.694 128.337 170.147 1.00 71.93  ? 3941 LEU A N     1 
ATOM   17560 C  CA    . LEU A 1 3941 ? 197.961 127.084 170.238 1.00 74.68  ? 3941 LEU A CA    1 
ATOM   17561 C  C     . LEU A 1 3941 ? 198.922 125.903 170.121 1.00 79.49  ? 3941 LEU A C     1 
ATOM   17562 O  O     . LEU A 1 3941 ? 199.878 125.954 169.340 1.00 83.43  ? 3941 LEU A O     1 
ATOM   17563 C  CB    . LEU A 1 3941 ? 196.897 126.998 169.144 1.00 70.74  ? 3941 LEU A CB    1 
ATOM   17564 C  CG    . LEU A 1 3941 ? 195.465 127.371 169.537 1.00 71.81  ? 3941 LEU A CG    1 
ATOM   17565 C  CD1   . LEU A 1 3941 ? 195.425 128.709 170.257 1.00 67.06  ? 3941 LEU A CD1   1 
ATOM   17566 C  CD2   . LEU A 1 3941 ? 194.563 127.390 168.312 1.00 61.03  ? 3941 LEU A CD2   1 
ATOM   17567 N  N     . PRO A 1 3942 ? 198.703 124.832 170.888 1.00 78.32  ? 3942 PRO A N     1 
ATOM   17568 C  CA    . PRO A 1 3942 ? 199.570 123.649 170.752 1.00 77.72  ? 3942 PRO A CA    1 
ATOM   17569 C  C     . PRO A 1 3942 ? 199.518 123.018 169.373 1.00 78.96  ? 3942 PRO A C     1 
ATOM   17570 O  O     . PRO A 1 3942 ? 200.486 122.367 168.962 1.00 83.80  ? 3942 PRO A O     1 
ATOM   17571 C  CB    . PRO A 1 3942 ? 199.043 122.692 171.832 1.00 77.03  ? 3942 PRO A CB    1 
ATOM   17572 C  CG    . PRO A 1 3942 ? 197.695 123.203 172.207 1.00 75.18  ? 3942 PRO A CG    1 
ATOM   17573 C  CD    . PRO A 1 3942 ? 197.678 124.670 171.931 1.00 75.20  ? 3942 PRO A CD    1 
ATOM   17574 N  N     . ALA A 1 3943 ? 198.411 123.181 168.644 1.00 76.18  ? 3943 ALA A N     1 
ATOM   17575 C  CA    . ALA A 1 3943 ? 198.308 122.603 167.310 1.00 78.64  ? 3943 ALA A CA    1 
ATOM   17576 C  C     . ALA A 1 3943 ? 199.126 123.366 166.277 1.00 77.65  ? 3943 ALA A C     1 
ATOM   17577 O  O     . ALA A 1 3943 ? 199.525 122.778 165.266 1.00 74.95  ? 3943 ALA A O     1 
ATOM   17578 C  CB    . ALA A 1 3943 ? 196.843 122.548 166.873 1.00 74.57  ? 3943 ALA A CB    1 
ATOM   17579 N  N     . PHE A 1 3944 ? 199.387 124.653 166.505 1.00 77.03  ? 3944 PHE A N     1 
ATOM   17580 C  CA    . PHE A 1 3944 ? 200.115 125.492 165.560 1.00 74.17  ? 3944 PHE A CA    1 
ATOM   17581 C  C     . PHE A 1 3944 ? 201.473 125.924 166.105 1.00 78.12  ? 3944 PHE A C     1 
ATOM   17582 O  O     . PHE A 1 3944 ? 201.926 127.040 165.839 1.00 76.18  ? 3944 PHE A O     1 
ATOM   17583 C  CB    . PHE A 1 3944 ? 199.285 126.718 165.185 1.00 65.04  ? 3944 PHE A CB    1 
ATOM   17584 C  CG    . PHE A 1 3944 ? 198.042 126.398 164.407 1.00 64.41  ? 3944 PHE A CG    1 
ATOM   17585 C  CD1   . PHE A 1 3944 ? 198.102 126.164 163.044 1.00 64.64  ? 3944 PHE A CD1   1 
ATOM   17586 C  CD2   . PHE A 1 3944 ? 196.811 126.337 165.037 1.00 62.20  ? 3944 PHE A CD2   1 
ATOM   17587 C  CE1   . PHE A 1 3944 ? 196.959 125.872 162.325 1.00 59.39  ? 3944 PHE A CE1   1 
ATOM   17588 C  CE2   . PHE A 1 3944 ? 195.664 126.045 164.324 1.00 59.79  ? 3944 PHE A CE2   1 
ATOM   17589 C  CZ    . PHE A 1 3944 ? 195.739 125.812 162.966 1.00 57.35  ? 3944 PHE A CZ    1 
ATOM   17590 N  N     . LYS A 1 3945 ? 202.132 125.053 166.874 1.00 81.00  ? 3945 LYS A N     1 
ATOM   17591 C  CA    . LYS A 1 3945 ? 203.437 125.403 167.428 1.00 82.89  ? 3945 LYS A CA    1 
ATOM   17592 C  C     . LYS A 1 3945 ? 204.472 125.595 166.327 1.00 82.43  ? 3945 LYS A C     1 
ATOM   17593 O  O     . LYS A 1 3945 ? 205.252 126.554 166.358 1.00 80.99  ? 3945 LYS A O     1 
ATOM   17594 C  CB    . LYS A 1 3945 ? 203.898 124.330 168.414 1.00 82.13  ? 3945 LYS A CB    1 
ATOM   17595 C  CG    . LYS A 1 3945 ? 203.484 122.919 168.037 1.00 85.98  ? 3945 LYS A CG    1 
ATOM   17596 C  CD    . LYS A 1 3945 ? 203.706 121.958 169.192 1.00 92.25  ? 3945 LYS A CD    1 
ATOM   17597 C  CE    . LYS A 1 3945 ? 203.319 120.538 168.813 1.00 93.07  ? 3945 LYS A CE    1 
ATOM   17598 N  NZ    . LYS A 1 3945 ? 201.844 120.347 168.827 1.00 80.18  ? 3945 LYS A NZ    1 
ATOM   17599 N  N     . ASP A 1 3946 ? 204.499 124.694 165.350 1.00 84.29  ? 3946 ASP A N     1 
ATOM   17600 C  CA    . ASP A 1 3946 ? 205.434 124.792 164.230 1.00 85.82  ? 3946 ASP A CA    1 
ATOM   17601 C  C     . ASP A 1 3946 ? 204.747 125.411 163.015 1.00 82.43  ? 3946 ASP A C     1 
ATOM   17602 O  O     . ASP A 1 3946 ? 204.676 124.821 161.938 1.00 84.70  ? 3946 ASP A O     1 
ATOM   17603 C  CB    . ASP A 1 3946 ? 206.004 123.416 163.897 1.00 92.20  ? 3946 ASP A CB    1 
ATOM   17604 C  CG    . ASP A 1 3946 ? 206.466 122.664 165.127 1.00 97.61  ? 3946 ASP A CG    1 
ATOM   17605 O  OD1   . ASP A 1 3946 ? 206.042 121.503 165.300 1.00 94.66  ? 3946 ASP A OD1   1 
ATOM   17606 O  OD2   . ASP A 1 3946 ? 207.253 123.228 165.916 1.00 93.66  ? 3946 ASP A OD2   1 
ATOM   17607 N  N     . LEU A 1 3947 ? 204.254 126.636 163.192 1.00 77.65  ? 3947 LEU A N     1 
ATOM   17608 C  CA    . LEU A 1 3947 ? 203.540 127.330 162.127 1.00 79.13  ? 3947 LEU A CA    1 
ATOM   17609 C  C     . LEU A 1 3947 ? 204.465 128.184 161.270 1.00 81.50  ? 3947 LEU A C     1 
ATOM   17610 O  O     . LEU A 1 3947 ? 204.378 128.146 160.040 1.00 83.94  ? 3947 LEU A O     1 
ATOM   17611 C  CB    . LEU A 1 3947 ? 202.419 128.197 162.711 1.00 78.77  ? 3947 LEU A CB    1 
ATOM   17612 C  CG    . LEU A 1 3947 ? 201.571 128.923 161.664 1.00 67.38  ? 3947 LEU A CG    1 
ATOM   17613 C  CD1   . LEU A 1 3947 ? 200.953 127.925 160.695 1.00 59.60  ? 3947 LEU A CD1   1 
ATOM   17614 C  CD2   . LEU A 1 3947 ? 200.503 129.781 162.323 1.00 66.96  ? 3947 LEU A CD2   1 
ATOM   17615 N  N     . ILE A 1 3948 ? 205.355 128.954 161.899 1.00 77.38  ? 3948 ILE A N     1 
ATOM   17616 C  CA    . ILE A 1 3948 ? 206.316 129.751 161.143 1.00 72.50  ? 3948 ILE A CA    1 
ATOM   17617 C  C     . ILE A 1 3948 ? 207.208 128.845 160.305 1.00 77.11  ? 3948 ILE A C     1 
ATOM   17618 O  O     . ILE A 1 3948 ? 207.511 129.145 159.143 1.00 80.38  ? 3948 ILE A O     1 
ATOM   17619 C  CB    . ILE A 1 3948 ? 207.138 130.633 162.098 1.00 70.88  ? 3948 ILE A CB    1 
ATOM   17620 C  CG1   . ILE A 1 3948 ? 206.224 131.624 162.821 1.00 72.19  ? 3948 ILE A CG1   1 
ATOM   17621 C  CG2   . ILE A 1 3948 ? 208.231 131.371 161.342 1.00 74.12  ? 3948 ILE A CG2   1 
ATOM   17622 C  CD1   . ILE A 1 3948 ? 206.893 132.349 163.963 1.00 75.81  ? 3948 ILE A CD1   1 
ATOM   17623 N  N     . ALA A 1 3949 ? 207.636 127.719 160.881 1.00 80.15  ? 3949 ALA A N     1 
ATOM   17624 C  CA    . ALA A 1 3949 ? 208.488 126.785 160.153 1.00 80.44  ? 3949 ALA A CA    1 
ATOM   17625 C  C     . ALA A 1 3949 ? 207.773 126.206 158.937 1.00 83.32  ? 3949 ALA A C     1 
ATOM   17626 O  O     . ALA A 1 3949 ? 208.374 126.068 157.866 1.00 81.00  ? 3949 ALA A O     1 
ATOM   17627 C  CB    . ALA A 1 3949 ? 208.956 125.669 161.086 1.00 74.25  ? 3949 ALA A CB    1 
ATOM   17628 N  N     . LYS A 1 3950 ? 206.490 125.858 159.079 1.00 83.59  ? 3950 LYS A N     1 
ATOM   17629 C  CA    . LYS A 1 3950 ? 205.755 125.322 157.936 1.00 84.70  ? 3950 LYS A CA    1 
ATOM   17630 C  C     . LYS A 1 3950 ? 205.512 126.382 156.870 1.00 86.07  ? 3950 LYS A C     1 
ATOM   17631 O  O     . LYS A 1 3950 ? 205.500 126.064 155.675 1.00 88.37  ? 3950 LYS A O     1 
ATOM   17632 C  CB    . LYS A 1 3950 ? 204.426 124.711 158.382 1.00 79.86  ? 3950 LYS A CB    1 
ATOM   17633 C  CG    . LYS A 1 3950 ? 204.525 123.264 158.826 1.00 82.64  ? 3950 LYS A CG    1 
ATOM   17634 C  CD    . LYS A 1 3950 ? 203.442 122.919 159.831 1.00 78.11  ? 3950 LYS A CD    1 
ATOM   17635 C  CE    . LYS A 1 3950 ? 203.560 121.474 160.292 1.00 80.29  ? 3950 LYS A CE    1 
ATOM   17636 N  NZ    . LYS A 1 3950 ? 203.043 120.508 159.279 1.00 73.70  ? 3950 LYS A NZ    1 
ATOM   17637 N  N     . VAL A 1 3951 ? 205.300 127.636 157.275 1.00 84.10  ? 3951 VAL A N     1 
ATOM   17638 C  CA    . VAL A 1 3951 ? 205.157 128.713 156.299 1.00 82.71  ? 3951 VAL A CA    1 
ATOM   17639 C  C     . VAL A 1 3951 ? 206.458 128.907 155.530 1.00 91.08  ? 3951 VAL A C     1 
ATOM   17640 O  O     . VAL A 1 3951 ? 206.458 129.069 154.304 1.00 93.33  ? 3951 VAL A O     1 
ATOM   17641 C  CB    . VAL A 1 3951 ? 204.710 130.013 156.992 1.00 74.33  ? 3951 VAL A CB    1 
ATOM   17642 C  CG1   . VAL A 1 3951 ? 204.704 131.163 156.003 1.00 71.27  ? 3951 VAL A CG1   1 
ATOM   17643 C  CG2   . VAL A 1 3951 ? 203.328 129.839 157.594 1.00 73.80  ? 3951 VAL A CG2   1 
ATOM   17644 N  N     . GLN A 1 3952 ? 207.587 128.895 156.242 1.00 89.44  ? 3952 GLN A N     1 
ATOM   17645 C  CA    . GLN A 1 3952 ? 208.879 129.054 155.579 1.00 86.80  ? 3952 GLN A CA    1 
ATOM   17646 C  C     . GLN A 1 3952 ? 209.177 127.887 154.645 1.00 85.74  ? 3952 GLN A C     1 
ATOM   17647 O  O     . GLN A 1 3952 ? 209.675 128.089 153.531 1.00 86.08  ? 3952 GLN A O     1 
ATOM   17648 C  CB    . GLN A 1 3952 ? 209.989 129.199 156.619 1.00 90.62  ? 3952 GLN A CB    1 
ATOM   17649 C  CG    . GLN A 1 3952 ? 209.906 130.464 157.452 1.00 87.38  ? 3952 GLN A CG    1 
ATOM   17650 C  CD    . GLN A 1 3952 ? 210.052 131.719 156.617 1.00 94.68  ? 3952 GLN A CD    1 
ATOM   17651 O  OE1   . GLN A 1 3952 ? 209.092 132.461 156.420 1.00 95.13  ? 3952 GLN A OE1   1 
ATOM   17652 N  NE2   . GLN A 1 3952 ? 211.259 131.962 156.119 1.00 104.79 ? 3952 GLN A NE2   1 
ATOM   17653 N  N     . ALA A 1 3953 ? 208.885 126.660 155.083 1.00 86.76  ? 3953 ALA A N     1 
ATOM   17654 C  CA    . ALA A 1 3953 ? 209.248 125.482 154.301 1.00 93.64  ? 3953 ALA A CA    1 
ATOM   17655 C  C     . ALA A 1 3953 ? 208.467 125.409 152.994 1.00 94.86  ? 3953 ALA A C     1 
ATOM   17656 O  O     . ALA A 1 3953 ? 209.033 125.078 151.946 1.00 93.35  ? 3953 ALA A O     1 
ATOM   17657 C  CB    . ALA A 1 3953 ? 209.028 124.217 155.130 1.00 82.57  ? 3953 ALA A CB    1 
ATOM   17658 N  N     . ASP A 1 3954 ? 207.171 125.709 153.034 1.00 92.92  ? 3954 ASP A N     1 
ATOM   17659 C  CA    . ASP A 1 3954 ? 206.338 125.582 151.846 1.00 93.89  ? 3954 ASP A CA    1 
ATOM   17660 C  C     . ASP A 1 3954 ? 206.709 126.643 150.818 1.00 96.01  ? 3954 ASP A C     1 
ATOM   17661 O  O     . ASP A 1 3954 ? 206.808 127.831 151.141 1.00 94.27  ? 3954 ASP A O     1 
ATOM   17662 C  CB    . ASP A 1 3954 ? 204.861 125.700 152.221 1.00 95.24  ? 3954 ASP A CB    1 
ATOM   17663 C  CG    . ASP A 1 3954 ? 203.938 125.219 151.117 1.00 93.71  ? 3954 ASP A CG    1 
ATOM   17664 O  OD1   . ASP A 1 3954 ? 204.441 124.668 150.115 1.00 94.44  ? 3954 ASP A OD1   1 
ATOM   17665 O  OD2   . ASP A 1 3954 ? 202.709 125.391 151.252 1.00 85.24  ? 3954 ASP A OD2   1 
ATOM   17666 N  N     . GLU A 1 3955 ? 206.913 126.210 149.574 1.00 100.14 ? 3955 GLU A N     1 
ATOM   17667 C  CA    . GLU A 1 3955 ? 207.203 127.128 148.480 1.00 101.49 ? 3955 GLU A CA    1 
ATOM   17668 C  C     . GLU A 1 3955 ? 205.955 127.555 147.723 1.00 99.71  ? 3955 GLU A C     1 
ATOM   17669 O  O     . GLU A 1 3955 ? 205.967 128.610 147.078 1.00 94.56  ? 3955 GLU A O     1 
ATOM   17670 C  CB    . GLU A 1 3955 ? 208.199 126.494 147.503 1.00 104.26 ? 3955 GLU A CB    1 
ATOM   17671 C  CG    . GLU A 1 3955 ? 207.731 125.181 146.895 1.00 106.29 ? 3955 GLU A CG    1 
ATOM   17672 C  CD    . GLU A 1 3955 ? 208.165 123.975 147.705 1.00 110.49 ? 3955 GLU A CD    1 
ATOM   17673 O  OE1   . GLU A 1 3955 ? 208.868 124.161 148.721 1.00 117.39 ? 3955 GLU A OE1   1 
ATOM   17674 O  OE2   . GLU A 1 3955 ? 207.804 122.841 147.325 1.00 103.24 ? 3955 GLU A OE2   1 
ATOM   17675 N  N     . GLN A 1 3956 ? 204.884 126.765 147.786 1.00 96.92  ? 3956 GLN A N     1 
ATOM   17676 C  CA    . GLN A 1 3956 ? 203.617 127.114 147.157 1.00 91.37  ? 3956 GLN A CA    1 
ATOM   17677 C  C     . GLN A 1 3956 ? 202.748 127.999 148.039 1.00 83.68  ? 3956 GLN A C     1 
ATOM   17678 O  O     . GLN A 1 3956 ? 201.641 128.361 147.626 1.00 82.24  ? 3956 GLN A O     1 
ATOM   17679 C  CB    . GLN A 1 3956 ? 202.847 125.844 146.785 1.00 87.38  ? 3956 GLN A CB    1 
ATOM   17680 C  CG    . GLN A 1 3956 ? 203.590 124.873 145.866 1.00 92.68  ? 3956 GLN A CG    1 
ATOM   17681 C  CD    . GLN A 1 3956 ? 204.257 125.548 144.678 1.00 96.31  ? 3956 GLN A CD    1 
ATOM   17682 O  OE1   . GLN A 1 3956 ? 205.339 126.125 144.796 1.00 93.04  ? 3956 GLN A OE1   1 
ATOM   17683 N  NE2   . GLN A 1 3956 ? 203.610 125.475 143.521 1.00 94.99  ? 3956 GLN A NE2   1 
ATOM   17684 N  N     . PHE A 1 3957 ? 203.219 128.346 149.240 1.00 83.82  ? 3957 PHE A N     1 
ATOM   17685 C  CA    . PHE A 1 3957 ? 202.424 129.172 150.143 1.00 82.00  ? 3957 PHE A CA    1 
ATOM   17686 C  C     . PHE A 1 3957 ? 202.186 130.560 149.562 1.00 78.81  ? 3957 PHE A C     1 
ATOM   17687 O  O     . PHE A 1 3957 ? 201.109 131.139 149.743 1.00 80.22  ? 3957 PHE A O     1 
ATOM   17688 C  CB    . PHE A 1 3957 ? 203.112 129.270 151.503 1.00 79.34  ? 3957 PHE A CB    1 
ATOM   17689 C  CG    . PHE A 1 3957 ? 202.311 130.011 152.531 1.00 69.92  ? 3957 PHE A CG    1 
ATOM   17690 C  CD1   . PHE A 1 3957 ? 201.238 129.405 153.159 1.00 62.71  ? 3957 PHE A CD1   1 
ATOM   17691 C  CD2   . PHE A 1 3957 ? 202.630 131.316 152.868 1.00 72.69  ? 3957 PHE A CD2   1 
ATOM   17692 C  CE1   . PHE A 1 3957 ? 200.498 130.085 154.104 1.00 63.51  ? 3957 PHE A CE1   1 
ATOM   17693 C  CE2   . PHE A 1 3957 ? 201.894 132.001 153.813 1.00 73.60  ? 3957 PHE A CE2   1 
ATOM   17694 C  CZ    . PHE A 1 3957 ? 200.826 131.384 154.432 1.00 70.64  ? 3957 PHE A CZ    1 
ATOM   17695 N  N     . GLY A 1 3958 ? 203.186 131.117 148.876 1.00 75.16  ? 3958 GLY A N     1 
ATOM   17696 C  CA    . GLY A 1 3958 ? 203.007 132.418 148.254 1.00 73.24  ? 3958 GLY A CA    1 
ATOM   17697 C  C     . GLY A 1 3958 ? 201.935 132.420 147.183 1.00 76.86  ? 3958 GLY A C     1 
ATOM   17698 O  O     . GLY A 1 3958 ? 201.207 133.404 147.030 1.00 74.72  ? 3958 GLY A O     1 
ATOM   17699 N  N     . ILE A 1 3959 ? 201.825 131.326 146.427 1.00 77.32  ? 3959 ILE A N     1 
ATOM   17700 C  CA    . ILE A 1 3959 ? 200.769 131.214 145.425 1.00 74.34  ? 3959 ILE A CA    1 
ATOM   17701 C  C     . ILE A 1 3959 ? 199.403 131.150 146.096 1.00 71.94  ? 3959 ILE A C     1 
ATOM   17702 O  O     . ILE A 1 3959 ? 198.442 131.786 145.646 1.00 72.44  ? 3959 ILE A O     1 
ATOM   17703 C  CB    . ILE A 1 3959 ? 201.018 129.991 144.524 1.00 72.24  ? 3959 ILE A CB    1 
ATOM   17704 C  CG1   . ILE A 1 3959 ? 202.360 130.127 143.802 1.00 72.40  ? 3959 ILE A CG1   1 
ATOM   17705 C  CG2   . ILE A 1 3959 ? 199.886 129.821 143.524 1.00 68.51  ? 3959 ILE A CG2   1 
ATOM   17706 C  CD1   . ILE A 1 3959 ? 203.137 128.835 143.707 1.00 80.84  ? 3959 ILE A CD1   1 
ATOM   17707 N  N     . TRP A 1 3960 ? 199.296 130.379 147.181 1.00 66.09  ? 3960 TRP A N     1 
ATOM   17708 C  CA    . TRP A 1 3960 ? 198.021 130.246 147.878 1.00 59.48  ? 3960 TRP A CA    1 
ATOM   17709 C  C     . TRP A 1 3960 ? 197.590 131.559 148.519 1.00 58.82  ? 3960 TRP A C     1 
ATOM   17710 O  O     . TRP A 1 3960 ? 196.398 131.889 148.528 1.00 57.20  ? 3960 TRP A O     1 
ATOM   17711 C  CB    . TRP A 1 3960 ? 198.111 129.147 148.934 1.00 55.79  ? 3960 TRP A CB    1 
ATOM   17712 C  CG    . TRP A 1 3960 ? 196.886 129.056 149.784 1.00 54.36  ? 3960 TRP A CG    1 
ATOM   17713 C  CD1   . TRP A 1 3960 ? 195.712 128.446 149.462 1.00 53.12  ? 3960 TRP A CD1   1 
ATOM   17714 C  CD2   . TRP A 1 3960 ? 196.710 129.600 151.097 1.00 53.52  ? 3960 TRP A CD2   1 
ATOM   17715 N  NE1   . TRP A 1 3960 ? 194.814 128.572 150.495 1.00 50.79  ? 3960 TRP A NE1   1 
ATOM   17716 C  CE2   . TRP A 1 3960 ? 195.403 129.277 151.510 1.00 48.21  ? 3960 TRP A CE2   1 
ATOM   17717 C  CE3   . TRP A 1 3960 ? 197.530 130.327 151.963 1.00 57.17  ? 3960 TRP A CE3   1 
ATOM   17718 C  CZ2   . TRP A 1 3960 ? 194.898 129.656 152.752 1.00 44.81  ? 3960 TRP A CZ2   1 
ATOM   17719 C  CZ3   . TRP A 1 3960 ? 197.027 130.702 153.194 1.00 51.61  ? 3960 TRP A CZ3   1 
ATOM   17720 C  CH2   . TRP A 1 3960 ? 195.724 130.366 153.577 1.00 43.02  ? 3960 TRP A CH2   1 
ATOM   17721 N  N     . LEU A 1 3961 ? 198.541 132.316 149.071 1.00 60.65  ? 3961 LEU A N     1 
ATOM   17722 C  CA    . LEU A 1 3961 ? 198.196 133.547 149.775 1.00 60.33  ? 3961 LEU A CA    1 
ATOM   17723 C  C     . LEU A 1 3961 ? 197.547 134.561 148.842 1.00 64.74  ? 3961 LEU A C     1 
ATOM   17724 O  O     . LEU A 1 3961 ? 196.646 135.303 149.250 1.00 62.10  ? 3961 LEU A O     1 
ATOM   17725 C  CB    . LEU A 1 3961 ? 199.441 134.143 150.429 1.00 63.23  ? 3961 LEU A CB    1 
ATOM   17726 C  CG    . LEU A 1 3961 ? 199.210 134.914 151.729 1.00 68.22  ? 3961 LEU A CG    1 
ATOM   17727 C  CD1   . LEU A 1 3961 ? 198.663 133.996 152.810 1.00 62.90  ? 3961 LEU A CD1   1 
ATOM   17728 C  CD2   . LEU A 1 3961 ? 200.492 135.587 152.187 1.00 70.04  ? 3961 LEU A CD2   1 
ATOM   17729 N  N     . ASP A 1 3962 ? 197.990 134.610 147.589 1.00 69.12  ? 3962 ASP A N     1 
ATOM   17730 C  CA    . ASP A 1 3962 ? 197.471 135.554 146.611 1.00 68.40  ? 3962 ASP A CA    1 
ATOM   17731 C  C     . ASP A 1 3962 ? 196.352 134.970 145.757 1.00 67.57  ? 3962 ASP A C     1 
ATOM   17732 O  O     . ASP A 1 3962 ? 195.893 135.635 144.822 1.00 69.51  ? 3962 ASP A O     1 
ATOM   17733 C  CB    . ASP A 1 3962 ? 198.605 136.054 145.713 1.00 74.58  ? 3962 ASP A CB    1 
ATOM   17734 C  CG    . ASP A 1 3962 ? 199.730 136.695 146.501 1.00 85.73  ? 3962 ASP A CG    1 
ATOM   17735 O  OD1   . ASP A 1 3962 ? 199.448 137.299 147.557 1.00 84.41  ? 3962 ASP A OD1   1 
ATOM   17736 O  OD2   . ASP A 1 3962 ? 200.897 136.594 146.066 1.00 92.60  ? 3962 ASP A OD2   1 
ATOM   17737 N  N     . SER A 1 3963 ? 195.907 133.752 146.051 1.00 61.74  ? 3963 SER A N     1 
ATOM   17738 C  CA    . SER A 1 3963 ? 194.837 133.138 145.279 1.00 53.25  ? 3963 SER A CA    1 
ATOM   17739 C  C     . SER A 1 3963 ? 193.515 133.862 145.514 1.00 52.75  ? 3963 SER A C     1 
ATOM   17740 O  O     . SER A 1 3963 ? 193.304 134.499 146.549 1.00 51.09  ? 3963 SER A O     1 
ATOM   17741 C  CB    . SER A 1 3963 ? 194.699 131.659 145.640 1.00 51.68  ? 3963 SER A CB    1 
ATOM   17742 O  OG    . SER A 1 3963 ? 194.274 131.500 146.981 1.00 51.43  ? 3963 SER A OG    1 
ATOM   17743 N  N     . SER A 1 3964 ? 192.623 133.763 144.525 1.00 52.45  ? 3964 SER A N     1 
ATOM   17744 C  CA    . SER A 1 3964 ? 191.346 134.468 144.601 1.00 51.73  ? 3964 SER A CA    1 
ATOM   17745 C  C     . SER A 1 3964 ? 190.498 133.966 145.763 1.00 51.21  ? 3964 SER A C     1 
ATOM   17746 O  O     . SER A 1 3964 ? 189.892 134.763 146.488 1.00 46.95  ? 3964 SER A O     1 
ATOM   17747 C  CB    . SER A 1 3964 ? 190.588 134.320 143.282 1.00 54.97  ? 3964 SER A CB    1 
ATOM   17748 O  OG    . SER A 1 3964 ? 190.623 132.981 142.821 1.00 51.03  ? 3964 SER A OG    1 
ATOM   17749 N  N     . SER A 1 3965 ? 190.440 132.650 145.956 1.00 54.21  ? 3965 SER A N     1 
ATOM   17750 C  CA    . SER A 1 3965 ? 189.659 132.033 147.028 1.00 47.67  ? 3965 SER A CA    1 
ATOM   17751 C  C     . SER A 1 3965 ? 190.557 131.065 147.784 1.00 46.78  ? 3965 SER A C     1 
ATOM   17752 O  O     . SER A 1 3965 ? 190.491 129.845 147.578 1.00 45.02  ? 3965 SER A O     1 
ATOM   17753 C  CB    . SER A 1 3965 ? 188.420 131.328 146.476 1.00 42.46  ? 3965 SER A CB    1 
ATOM   17754 O  OG    . SER A 1 3965 ? 188.780 130.312 145.557 1.00 54.71  ? 3965 SER A OG    1 
ATOM   17755 N  N     . PRO A 1 3966 ? 191.420 131.576 148.666 1.00 45.57  ? 3966 PRO A N     1 
ATOM   17756 C  CA    . PRO A 1 3966 ? 192.306 130.682 149.428 1.00 42.19  ? 3966 PRO A CA    1 
ATOM   17757 C  C     . PRO A 1 3966 ? 191.568 129.754 150.373 1.00 44.30  ? 3966 PRO A C     1 
ATOM   17758 O  O     . PRO A 1 3966 ? 192.129 128.725 150.769 1.00 51.28  ? 3966 PRO A O     1 
ATOM   17759 C  CB    . PRO A 1 3966 ? 193.210 131.657 150.193 1.00 45.71  ? 3966 PRO A CB    1 
ATOM   17760 C  CG    . PRO A 1 3966 ? 192.388 132.893 150.325 1.00 42.84  ? 3966 PRO A CG    1 
ATOM   17761 C  CD    . PRO A 1 3966 ? 191.586 132.986 149.058 1.00 44.77  ? 3966 PRO A CD    1 
ATOM   17762 N  N     . GLU A 1 3967 ? 190.332 130.083 150.752 1.00 44.09  ? 3967 GLU A N     1 
ATOM   17763 C  CA    . GLU A 1 3967 ? 189.581 129.243 151.676 1.00 41.86  ? 3967 GLU A CA    1 
ATOM   17764 C  C     . GLU A 1 3967 ? 189.218 127.892 151.074 1.00 43.99  ? 3967 GLU A C     1 
ATOM   17765 O  O     . GLU A 1 3967 ? 188.971 126.943 151.825 1.00 45.79  ? 3967 GLU A O     1 
ATOM   17766 C  CB    . GLU A 1 3967 ? 188.315 129.973 152.132 1.00 37.99  ? 3967 GLU A CB    1 
ATOM   17767 C  CG    . GLU A 1 3967 ? 187.103 129.730 151.250 1.00 40.09  ? 3967 GLU A CG    1 
ATOM   17768 C  CD    . GLU A 1 3967 ? 186.928 130.801 150.192 1.00 48.55  ? 3967 GLU A CD    1 
ATOM   17769 O  OE1   . GLU A 1 3967 ? 185.873 130.813 149.525 1.00 51.49  ? 3967 GLU A OE1   1 
ATOM   17770 O  OE2   . GLU A 1 3967 ? 187.844 131.634 150.030 1.00 53.25  ? 3967 GLU A OE2   1 
ATOM   17771 N  N     . GLN A 1 3968 ? 189.182 127.782 149.744 1.00 47.71  ? 3968 GLN A N     1 
ATOM   17772 C  CA    . GLN A 1 3968 ? 188.786 126.524 149.118 1.00 49.64  ? 3968 GLN A CA    1 
ATOM   17773 C  C     . GLN A 1 3968 ? 189.818 125.430 149.361 1.00 52.80  ? 3968 GLN A C     1 
ATOM   17774 O  O     . GLN A 1 3968 ? 189.460 124.283 149.653 1.00 59.47  ? 3968 GLN A O     1 
ATOM   17775 C  CB    . GLN A 1 3968 ? 188.564 126.731 147.620 1.00 51.10  ? 3968 GLN A CB    1 
ATOM   17776 C  CG    . GLN A 1 3968 ? 187.156 127.177 147.256 1.00 46.60  ? 3968 GLN A CG    1 
ATOM   17777 C  CD    . GLN A 1 3968 ? 186.092 126.197 147.716 1.00 58.37  ? 3968 GLN A CD    1 
ATOM   17778 O  OE1   . GLN A 1 3968 ? 186.329 124.991 147.788 1.00 63.71  ? 3968 GLN A OE1   1 
ATOM   17779 N  NE2   . GLN A 1 3968 ? 184.911 126.714 148.033 1.00 59.14  ? 3968 GLN A NE2   1 
ATOM   17780 N  N     . THR A 1 3969 ? 191.104 125.761 149.245 1.00 55.10  ? 3969 THR A N     1 
ATOM   17781 C  CA    . THR A 1 3969 ? 192.192 124.796 149.407 1.00 58.29  ? 3969 THR A CA    1 
ATOM   17782 C  C     . THR A 1 3969 ? 193.203 125.376 150.392 1.00 53.17  ? 3969 THR A C     1 
ATOM   17783 O  O     . THR A 1 3969 ? 194.175 126.017 149.989 1.00 54.92  ? 3969 THR A O     1 
ATOM   17784 C  CB    . THR A 1 3969 ? 192.840 124.472 148.063 1.00 64.95  ? 3969 THR A CB    1 
ATOM   17785 O  OG1   . THR A 1 3969 ? 193.074 125.687 147.340 1.00 61.22  ? 3969 THR A OG1   1 
ATOM   17786 C  CG2   . THR A 1 3969 ? 191.935 123.567 147.240 1.00 59.02  ? 3969 THR A CG2   1 
ATOM   17787 N  N     . VAL A 1 3970 ? 192.976 125.142 151.680 1.00 49.72  ? 3970 VAL A N     1 
ATOM   17788 C  CA    . VAL A 1 3970 ? 193.864 125.635 152.730 1.00 49.45  ? 3970 VAL A CA    1 
ATOM   17789 C  C     . VAL A 1 3970 ? 194.953 124.600 152.988 1.00 51.76  ? 3970 VAL A C     1 
ATOM   17790 O  O     . VAL A 1 3970 ? 194.647 123.411 153.157 1.00 53.10  ? 3970 VAL A O     1 
ATOM   17791 C  CB    . VAL A 1 3970 ? 193.084 125.954 154.016 1.00 47.55  ? 3970 VAL A CB    1 
ATOM   17792 C  CG1   . VAL A 1 3970 ? 193.987 126.632 155.033 1.00 45.22  ? 3970 VAL A CG1   1 
ATOM   17793 C  CG2   . VAL A 1 3970 ? 191.878 126.824 153.701 1.00 40.97  ? 3970 VAL A CG2   1 
ATOM   17794 N  N     . PRO A 1 3971 ? 196.223 124.996 153.015 1.00 51.83  ? 3971 PRO A N     1 
ATOM   17795 C  CA    . PRO A 1 3971 ? 197.296 124.029 153.265 1.00 55.43  ? 3971 PRO A CA    1 
ATOM   17796 C  C     . PRO A 1 3971 ? 197.206 123.427 154.659 1.00 59.76  ? 3971 PRO A C     1 
ATOM   17797 O  O     . PRO A 1 3971 ? 196.695 124.032 155.604 1.00 59.70  ? 3971 PRO A O     1 
ATOM   17798 C  CB    . PRO A 1 3971 ? 198.569 124.868 153.104 1.00 53.76  ? 3971 PRO A CB    1 
ATOM   17799 C  CG    . PRO A 1 3971 ? 198.147 126.001 152.219 1.00 53.78  ? 3971 PRO A CG    1 
ATOM   17800 C  CD    . PRO A 1 3971 ? 196.766 126.328 152.703 1.00 53.90  ? 3971 PRO A CD    1 
ATOM   17801 N  N     . TYR A 1 3972 ? 197.722 122.202 154.772 1.00 57.50  ? 3972 TYR A N     1 
ATOM   17802 C  CA    . TYR A 1 3972 ? 197.719 121.453 156.030 1.00 56.30  ? 3972 TYR A CA    1 
ATOM   17803 C  C     . TYR A 1 3972 ? 198.836 121.976 156.935 1.00 60.67  ? 3972 TYR A C     1 
ATOM   17804 O  O     . TYR A 1 3972 ? 199.835 121.308 157.210 1.00 69.63  ? 3972 TYR A O     1 
ATOM   17805 C  CB    . TYR A 1 3972 ? 197.872 119.964 155.753 1.00 60.90  ? 3972 TYR A CB    1 
ATOM   17806 C  CG    . TYR A 1 3972 ? 197.249 119.067 156.797 1.00 66.35  ? 3972 TYR A CG    1 
ATOM   17807 C  CD1   . TYR A 1 3972 ? 197.932 118.747 157.962 1.00 66.74  ? 3972 TYR A CD1   1 
ATOM   17808 C  CD2   . TYR A 1 3972 ? 195.982 118.533 156.612 1.00 67.16  ? 3972 TYR A CD2   1 
ATOM   17809 C  CE1   . TYR A 1 3972 ? 197.368 117.924 158.916 1.00 67.06  ? 3972 TYR A CE1   1 
ATOM   17810 C  CE2   . TYR A 1 3972 ? 195.409 117.710 157.561 1.00 70.73  ? 3972 TYR A CE2   1 
ATOM   17811 C  CZ    . TYR A 1 3972 ? 196.107 117.409 158.711 1.00 72.87  ? 3972 TYR A CZ    1 
ATOM   17812 O  OH    . TYR A 1 3972 ? 195.540 116.589 159.657 1.00 80.87  ? 3972 TYR A OH    1 
ATOM   17813 N  N     . LEU A 1 3973 ? 198.648 123.206 157.403 1.00 60.11  ? 3973 LEU A N     1 
ATOM   17814 C  CA    . LEU A 1 3973 ? 199.661 123.896 158.202 1.00 62.21  ? 3973 LEU A CA    1 
ATOM   17815 C  C     . LEU A 1 3973 ? 199.441 123.704 159.701 1.00 68.62  ? 3973 LEU A C     1 
ATOM   17816 O  O     . LEU A 1 3973 ? 199.388 124.666 160.466 1.00 72.16  ? 3973 LEU A O     1 
ATOM   17817 C  CB    . LEU A 1 3973 ? 199.681 125.375 157.839 1.00 56.15  ? 3973 LEU A CB    1 
ATOM   17818 C  CG    . LEU A 1 3973 ? 200.133 125.699 156.415 1.00 60.48  ? 3973 LEU A CG    1 
ATOM   17819 C  CD1   . LEU A 1 3973 ? 199.978 127.182 156.130 1.00 64.01  ? 3973 LEU A CD1   1 
ATOM   17820 C  CD2   . LEU A 1 3973 ? 201.567 125.252 156.186 1.00 70.64  ? 3973 LEU A CD2   1 
ATOM   17821 N  N     . TRP A 1 3974 ? 199.315 122.452 160.134 1.00 68.93  ? 3974 TRP A N     1 
ATOM   17822 C  CA    . TRP A 1 3974 ? 199.232 122.147 161.555 1.00 73.38  ? 3974 TRP A CA    1 
ATOM   17823 C  C     . TRP A 1 3974 ? 199.647 120.701 161.773 1.00 81.51  ? 3974 TRP A C     1 
ATOM   17824 O  O     . TRP A 1 3974 ? 199.519 119.857 160.882 1.00 78.31  ? 3974 TRP A O     1 
ATOM   17825 C  CB    . TRP A 1 3974 ? 197.827 122.407 162.116 1.00 69.51  ? 3974 TRP A CB    1 
ATOM   17826 C  CG    . TRP A 1 3974 ? 196.754 121.519 161.560 1.00 66.89  ? 3974 TRP A CG    1 
ATOM   17827 C  CD1   . TRP A 1 3974 ? 196.406 120.277 162.004 1.00 71.04  ? 3974 TRP A CD1   1 
ATOM   17828 C  CD2   . TRP A 1 3974 ? 195.872 121.817 160.471 1.00 62.83  ? 3974 TRP A CD2   1 
ATOM   17829 N  NE1   . TRP A 1 3974 ? 195.371 119.778 161.252 1.00 68.14  ? 3974 TRP A NE1   1 
ATOM   17830 C  CE2   . TRP A 1 3974 ? 195.024 120.705 160.305 1.00 60.50  ? 3974 TRP A CE2   1 
ATOM   17831 C  CE3   . TRP A 1 3974 ? 195.721 122.914 159.618 1.00 61.98  ? 3974 TRP A CE3   1 
ATOM   17832 C  CZ2   . TRP A 1 3974 ? 194.040 120.658 159.320 1.00 55.50  ? 3974 TRP A CZ2   1 
ATOM   17833 C  CZ3   . TRP A 1 3974 ? 194.743 122.865 158.641 1.00 58.07  ? 3974 TRP A CZ3   1 
ATOM   17834 C  CH2   . TRP A 1 3974 ? 193.916 121.745 158.501 1.00 55.80  ? 3974 TRP A CH2   1 
ATOM   17835 N  N     . SER A 1 3975 ? 200.149 120.428 162.975 1.00 88.14  ? 3975 SER A N     1 
ATOM   17836 C  CA    . SER A 1 3975 ? 200.637 119.108 163.352 1.00 90.61  ? 3975 SER A CA    1 
ATOM   17837 C  C     . SER A 1 3975 ? 199.696 118.499 164.379 1.00 87.91  ? 3975 SER A C     1 
ATOM   17838 O  O     . SER A 1 3975 ? 199.338 119.154 165.364 1.00 82.74  ? 3975 SER A O     1 
ATOM   17839 C  CB    . SER A 1 3975 ? 202.059 119.186 163.914 1.00 95.14  ? 3975 SER A CB    1 
ATOM   17840 O  OG    . SER A 1 3975 ? 202.124 120.083 165.009 1.00 97.90  ? 3975 SER A OG    1 
ATOM   17841 N  N     . GLU A 1 3976 ? 199.299 117.250 164.148 1.00 89.67  ? 3976 GLU A N     1 
ATOM   17842 C  CA    . GLU A 1 3976 ? 198.386 116.547 165.036 1.00 94.11  ? 3976 GLU A CA    1 
ATOM   17843 C  C     . GLU A 1 3976 ? 198.845 115.107 165.208 1.00 100.56 ? 3976 GLU A C     1 
ATOM   17844 O  O     . GLU A 1 3976 ? 199.422 114.516 164.290 1.00 100.89 ? 3976 GLU A O     1 
ATOM   17845 C  CB    . GLU A 1 3976 ? 196.951 116.592 164.499 1.00 88.74  ? 3976 GLU A CB    1 
ATOM   17846 C  CG    . GLU A 1 3976 ? 196.758 115.869 163.178 1.00 92.71  ? 3976 GLU A CG    1 
ATOM   17847 C  CD    . GLU A 1 3976 ? 195.348 116.009 162.646 1.00 95.22  ? 3976 GLU A CD    1 
ATOM   17848 O  OE1   . GLU A 1 3976 ? 194.536 116.695 163.299 1.00 95.12  ? 3976 GLU A OE1   1 
ATOM   17849 O  OE2   . GLU A 1 3976 ? 195.052 115.433 161.578 1.00 92.10  ? 3976 GLU A OE2   1 
ATOM   17850 N  N     . GLU A 1 3977 ? 198.592 114.551 166.395 1.00 101.14 ? 3977 GLU A N     1 
ATOM   17851 C  CA    . GLU A 1 3977 ? 198.995 113.175 166.668 1.00 101.40 ? 3977 GLU A CA    1 
ATOM   17852 C  C     . GLU A 1 3977 ? 198.097 112.179 165.945 1.00 100.93 ? 3977 GLU A C     1 
ATOM   17853 O  O     . GLU A 1 3977 ? 198.580 111.176 165.407 1.00 98.77  ? 3977 GLU A O     1 
ATOM   17854 C  CB    . GLU A 1 3977 ? 198.980 112.914 168.174 1.00 101.68 ? 3977 GLU A CB    1 
ATOM   17855 C  CG    . GLU A 1 3977 ? 199.696 113.974 168.995 1.00 107.16 ? 3977 GLU A CG    1 
ATOM   17856 C  CD    . GLU A 1 3977 ? 198.735 114.885 169.733 1.00 110.19 ? 3977 GLU A CD    1 
ATOM   17857 O  OE1   . GLU A 1 3977 ? 197.923 115.560 169.066 1.00 108.81 ? 3977 GLU A OE1   1 
ATOM   17858 O  OE2   . GLU A 1 3977 ? 198.791 114.926 170.980 1.00 109.05 ? 3977 GLU A OE2   1 
ATOM   17859 N  N     . THR A 1 3978 ? 196.792 112.439 165.919 1.00 104.60 ? 3978 THR A N     1 
ATOM   17860 C  CA    . THR A 1 3978 ? 195.821 111.566 165.284 1.00 104.72 ? 3978 THR A CA    1 
ATOM   17861 C  C     . THR A 1 3978 ? 195.010 112.349 164.258 1.00 102.90 ? 3978 THR A C     1 
ATOM   17862 O  O     . THR A 1 3978 ? 194.841 113.565 164.398 1.00 102.02 ? 3978 THR A O     1 
ATOM   17863 C  CB    . THR A 1 3978 ? 194.869 110.946 166.317 1.00 101.97 ? 3978 THR A CB    1 
ATOM   17864 O  OG1   . THR A 1 3978 ? 194.118 111.983 166.961 1.00 99.84  ? 3978 THR A OG1   1 
ATOM   17865 C  CG2   . THR A 1 3978 ? 195.648 110.164 167.363 1.00 101.06 ? 3978 THR A CG2   1 
ATOM   17866 N  N     . PRO A 1 3979 ? 194.506 111.688 163.215 1.00 101.18 ? 3979 PRO A N     1 
ATOM   17867 C  CA    . PRO A 1 3979 ? 193.724 112.405 162.200 1.00 98.94  ? 3979 PRO A CA    1 
ATOM   17868 C  C     . PRO A 1 3979 ? 192.499 113.073 162.810 1.00 102.87 ? 3979 PRO A C     1 
ATOM   17869 O  O     . PRO A 1 3979 ? 191.854 112.530 163.709 1.00 103.20 ? 3979 PRO A O     1 
ATOM   17870 C  CB    . PRO A 1 3979 ? 193.330 111.304 161.210 1.00 96.39  ? 3979 PRO A CB    1 
ATOM   17871 C  CG    . PRO A 1 3979 ? 194.351 110.237 161.402 1.00 97.17  ? 3979 PRO A CG    1 
ATOM   17872 C  CD    . PRO A 1 3979 ? 194.714 110.275 162.855 1.00 101.65 ? 3979 PRO A CD    1 
ATOM   17873 N  N     . ALA A 1 3980 ? 192.187 114.263 162.309 1.00 99.62  ? 3980 ALA A N     1 
ATOM   17874 C  CA    . ALA A 1 3980 ? 191.075 115.046 162.822 1.00 86.99  ? 3980 ALA A CA    1 
ATOM   17875 C  C     . ALA A 1 3980 ? 189.809 114.778 162.022 1.00 77.70  ? 3980 ALA A C     1 
ATOM   17876 O  O     . ALA A 1 3980 ? 189.855 114.356 160.863 1.00 76.79  ? 3980 ALA A O     1 
ATOM   17877 C  CB    . ALA A 1 3980 ? 191.400 116.540 162.786 1.00 76.59  ? 3980 ALA A CB    1 
ATOM   17878 N  N     . THR A 1 3981 ? 188.670 115.028 162.660 1.00 78.55  ? 3981 THR A N     1 
ATOM   17879 C  CA    . THR A 1 3981 ? 187.389 114.919 161.992 1.00 76.94  ? 3981 THR A CA    1 
ATOM   17880 C  C     . THR A 1 3981 ? 187.223 116.065 160.996 1.00 69.66  ? 3981 THR A C     1 
ATOM   17881 O  O     . THR A 1 3981 ? 187.922 117.078 161.081 1.00 66.74  ? 3981 THR A O     1 
ATOM   17882 C  CB    . THR A 1 3981 ? 186.258 114.935 163.017 1.00 74.23  ? 3981 THR A CB    1 
ATOM   17883 O  OG1   . THR A 1 3981 ? 186.363 116.111 163.830 1.00 73.16  ? 3981 THR A OG1   1 
ATOM   17884 C  CG2   . THR A 1 3981 ? 186.332 113.704 163.907 1.00 75.77  ? 3981 THR A CG2   1 
ATOM   17885 N  N     . PRO A 1 3982 ? 186.315 115.921 160.023 1.00 64.09  ? 3982 PRO A N     1 
ATOM   17886 C  CA    . PRO A 1 3982 ? 186.088 117.030 159.080 1.00 60.98  ? 3982 PRO A CA    1 
ATOM   17887 C  C     . PRO A 1 3982 ? 185.699 118.330 159.763 1.00 56.02  ? 3982 PRO A C     1 
ATOM   17888 O  O     . PRO A 1 3982 ? 186.070 119.409 159.285 1.00 53.41  ? 3982 PRO A O     1 
ATOM   17889 C  CB    . PRO A 1 3982 ? 184.965 116.500 158.173 1.00 55.80  ? 3982 PRO A CB    1 
ATOM   17890 C  CG    . PRO A 1 3982 ? 184.422 115.282 158.867 1.00 61.48  ? 3982 PRO A CG    1 
ATOM   17891 C  CD    . PRO A 1 3982 ? 185.565 114.716 159.636 1.00 61.39  ? 3982 PRO A CD    1 
ATOM   17892 N  N     . ILE A 1 3983 ? 184.961 118.260 160.872 1.00 56.85  ? 3983 ILE A N     1 
ATOM   17893 C  CA    . ILE A 1 3983 ? 184.642 119.468 161.628 1.00 51.32  ? 3983 ILE A CA    1 
ATOM   17894 C  C     . ILE A 1 3983 ? 185.909 120.082 162.214 1.00 51.47  ? 3983 ILE A C     1 
ATOM   17895 O  O     . ILE A 1 3983 ? 186.084 121.307 162.204 1.00 53.82  ? 3983 ILE A O     1 
ATOM   17896 C  CB    . ILE A 1 3983 ? 183.601 119.157 162.718 1.00 47.22  ? 3983 ILE A CB    1 
ATOM   17897 C  CG1   . ILE A 1 3983 ? 182.305 118.646 162.085 1.00 45.18  ? 3983 ILE A CG1   1 
ATOM   17898 C  CG2   . ILE A 1 3983 ? 183.325 120.390 163.560 1.00 46.38  ? 3983 ILE A CG2   1 
ATOM   17899 C  CD1   . ILE A 1 3983 ? 182.107 117.152 162.214 1.00 56.88  ? 3983 ILE A CD1   1 
ATOM   17900 N  N     . GLY A 1 3984 ? 186.809 119.248 162.738 1.00 53.02  ? 3984 GLY A N     1 
ATOM   17901 C  CA    . GLY A 1 3984 ? 188.071 119.764 163.243 1.00 52.92  ? 3984 GLY A CA    1 
ATOM   17902 C  C     . GLY A 1 3984 ? 188.934 120.365 162.151 1.00 52.46  ? 3984 GLY A C     1 
ATOM   17903 O  O     . GLY A 1 3984 ? 189.591 121.391 162.359 1.00 52.65  ? 3984 GLY A O     1 
ATOM   17904 N  N     . GLN A 1 3985 ? 188.949 119.734 160.974 1.00 52.50  ? 3985 GLN A N     1 
ATOM   17905 C  CA    . GLN A 1 3985 ? 189.654 120.314 159.837 1.00 49.71  ? 3985 GLN A CA    1 
ATOM   17906 C  C     . GLN A 1 3985 ? 189.060 121.664 159.463 1.00 46.45  ? 3985 GLN A C     1 
ATOM   17907 O  O     . GLN A 1 3985 ? 189.794 122.610 159.159 1.00 49.18  ? 3985 GLN A O     1 
ATOM   17908 C  CB    . GLN A 1 3985 ? 189.608 119.361 158.643 1.00 53.13  ? 3985 GLN A CB    1 
ATOM   17909 C  CG    . GLN A 1 3985 ? 190.571 118.192 158.736 1.00 66.82  ? 3985 GLN A CG    1 
ATOM   17910 C  CD    . GLN A 1 3985 ? 190.238 117.087 157.752 1.00 76.76  ? 3985 GLN A CD    1 
ATOM   17911 O  OE1   . GLN A 1 3985 ? 189.695 117.342 156.676 1.00 69.34  ? 3985 GLN A OE1   1 
ATOM   17912 N  NE2   . GLN A 1 3985 ? 190.561 115.852 158.116 1.00 79.93  ? 3985 GLN A NE2   1 
ATOM   17913 N  N     . ALA A 1 3986 ? 187.729 121.771 159.483 1.00 46.84  ? 3986 ALA A N     1 
ATOM   17914 C  CA    . ALA A 1 3986 ? 187.081 123.044 159.189 1.00 39.12  ? 3986 ALA A CA    1 
ATOM   17915 C  C     . ALA A 1 3986 ? 187.459 124.105 160.214 1.00 38.91  ? 3986 ALA A C     1 
ATOM   17916 O  O     . ALA A 1 3986 ? 187.702 125.260 159.856 1.00 45.46  ? 3986 ALA A O     1 
ATOM   17917 C  CB    . ALA A 1 3986 ? 185.565 122.863 159.136 1.00 34.81  ? 3986 ALA A CB    1 
ATOM   17918 N  N     . ILE A 1 3987 ? 187.516 123.731 161.494 1.00 41.18  ? 3987 ILE A N     1 
ATOM   17919 C  CA    . ILE A 1 3987 ? 187.885 124.689 162.535 1.00 39.40  ? 3987 ILE A CA    1 
ATOM   17920 C  C     . ILE A 1 3987 ? 189.322 125.165 162.349 1.00 37.46  ? 3987 ILE A C     1 
ATOM   17921 O  O     . ILE A 1 3987 ? 189.616 126.366 162.449 1.00 44.02  ? 3987 ILE A O     1 
ATOM   17922 C  CB    . ILE A 1 3987 ? 187.673 124.070 163.929 1.00 42.13  ? 3987 ILE A CB    1 
ATOM   17923 C  CG1   . ILE A 1 3987 ? 186.185 123.853 164.200 1.00 44.76  ? 3987 ILE A CG1   1 
ATOM   17924 C  CG2   . ILE A 1 3987 ? 188.281 124.953 165.005 1.00 42.24  ? 3987 ILE A CG2   1 
ATOM   17925 C  CD1   . ILE A 1 3987 ? 185.895 123.244 165.551 1.00 51.26  ? 3987 ILE A CD1   1 
ATOM   17926 N  N     . HIS A 1 3988 ? 190.242 124.235 162.086 1.00 37.32  ? 3988 HIS A N     1 
ATOM   17927 C  CA    . HIS A 1 3988 ? 191.640 124.617 161.912 1.00 40.11  ? 3988 HIS A CA    1 
ATOM   17928 C  C     . HIS A 1 3988 ? 191.829 125.471 160.664 1.00 40.88  ? 3988 HIS A C     1 
ATOM   17929 O  O     . HIS A 1 3988 ? 192.599 126.440 160.678 1.00 42.38  ? 3988 HIS A O     1 
ATOM   17930 C  CB    . HIS A 1 3988 ? 192.521 123.370 161.866 1.00 45.62  ? 3988 HIS A CB    1 
ATOM   17931 C  CG    . HIS A 1 3988 ? 192.725 122.732 163.204 1.00 52.79  ? 3988 HIS A CG    1 
ATOM   17932 N  ND1   . HIS A 1 3988 ? 192.145 121.531 163.554 1.00 53.36  ? 3988 HIS A ND1   1 
ATOM   17933 C  CD2   . HIS A 1 3988 ? 193.436 123.134 164.284 1.00 52.49  ? 3988 HIS A CD2   1 
ATOM   17934 C  CE1   . HIS A 1 3988 ? 192.494 121.219 164.789 1.00 52.31  ? 3988 HIS A CE1   1 
ATOM   17935 N  NE2   . HIS A 1 3988 ? 193.277 122.175 165.255 1.00 51.75  ? 3988 HIS A NE2   1 
ATOM   17936 N  N     . ARG A 1 3989 ? 191.126 125.138 159.578 1.00 39.84  ? 3989 ARG A N     1 
ATOM   17937 C  CA    . ARG A 1 3989 ? 191.172 125.974 158.385 1.00 34.35  ? 3989 ARG A CA    1 
ATOM   17938 C  C     . ARG A 1 3989 ? 190.564 127.346 158.642 1.00 32.38  ? 3989 ARG A C     1 
ATOM   17939 O  O     . ARG A 1 3989 ? 191.033 128.342 158.088 1.00 36.13  ? 3989 ARG A O     1 
ATOM   17940 C  CB    . ARG A 1 3989 ? 190.452 125.280 157.229 1.00 32.61  ? 3989 ARG A CB    1 
ATOM   17941 C  CG    . ARG A 1 3989 ? 191.175 124.062 156.680 1.00 35.70  ? 3989 ARG A CG    1 
ATOM   17942 C  CD    . ARG A 1 3989 ? 190.608 123.651 155.331 1.00 41.68  ? 3989 ARG A CD    1 
ATOM   17943 N  NE    . ARG A 1 3989 ? 190.211 122.249 155.307 1.00 47.27  ? 3989 ARG A NE    1 
ATOM   17944 C  CZ    . ARG A 1 3989 ? 191.041 121.239 155.086 1.00 56.51  ? 3989 ARG A CZ    1 
ATOM   17945 N  NH1   . ARG A 1 3989 ? 192.330 121.439 154.867 1.00 54.20  ? 3989 ARG A NH1   1 
ATOM   17946 N  NH2   . ARG A 1 3989 ? 190.565 119.997 155.084 1.00 59.71  ? 3989 ARG A NH2   1 
ATOM   17947 N  N     . LEU A 1 3990 ? 189.519 127.417 159.470 1.00 31.34  ? 3990 LEU A N     1 
ATOM   17948 C  CA    . LEU A 1 3990 ? 188.945 128.705 159.843 1.00 30.13  ? 3990 LEU A CA    1 
ATOM   17949 C  C     . LEU A 1 3990 ? 189.962 129.564 160.579 1.00 35.80  ? 3990 LEU A C     1 
ATOM   17950 O  O     . LEU A 1 3990 ? 190.107 130.758 160.291 1.00 42.30  ? 3990 LEU A O     1 
ATOM   17951 C  CB    . LEU A 1 3990 ? 187.701 128.482 160.704 1.00 26.48  ? 3990 LEU A CB    1 
ATOM   17952 C  CG    . LEU A 1 3990 ? 186.838 129.680 161.098 1.00 28.50  ? 3990 LEU A CG    1 
ATOM   17953 C  CD1   . LEU A 1 3990 ? 186.456 130.500 159.883 1.00 31.98  ? 3990 LEU A CD1   1 
ATOM   17954 C  CD2   . LEU A 1 3990 ? 185.598 129.208 161.838 1.00 28.87  ? 3990 LEU A CD2   1 
ATOM   17955 N  N     . LEU A 1 3991 ? 190.684 128.964 161.527 1.00 39.45  ? 3991 LEU A N     1 
ATOM   17956 C  CA    . LEU A 1 3991 ? 191.732 129.698 162.230 1.00 38.31  ? 3991 LEU A CA    1 
ATOM   17957 C  C     . LEU A 1 3991 ? 192.826 130.149 161.268 1.00 39.93  ? 3991 LEU A C     1 
ATOM   17958 O  O     . LEU A 1 3991 ? 193.313 131.284 161.352 1.00 41.86  ? 3991 LEU A O     1 
ATOM   17959 C  CB    . LEU A 1 3991 ? 192.319 128.835 163.345 1.00 37.11  ? 3991 LEU A CB    1 
ATOM   17960 C  CG    . LEU A 1 3991 ? 191.466 128.685 164.604 1.00 39.32  ? 3991 LEU A CG    1 
ATOM   17961 C  CD1   . LEU A 1 3991 ? 192.066 127.644 165.531 1.00 42.91  ? 3991 LEU A CD1   1 
ATOM   17962 C  CD2   . LEU A 1 3991 ? 191.320 130.020 165.315 1.00 45.84  ? 3991 LEU A CD2   1 
ATOM   17963 N  N     . LEU A 1 3992 ? 193.219 129.270 160.342 1.00 37.23  ? 3992 LEU A N     1 
ATOM   17964 C  CA    . LEU A 1 3992 ? 194.261 129.616 159.380 1.00 37.61  ? 3992 LEU A CA    1 
ATOM   17965 C  C     . LEU A 1 3992 ? 193.829 130.768 158.479 1.00 38.10  ? 3992 LEU A C     1 
ATOM   17966 O  O     . LEU A 1 3992 ? 194.623 131.670 158.194 1.00 41.10  ? 3992 LEU A O     1 
ATOM   17967 C  CB    . LEU A 1 3992 ? 194.629 128.392 158.543 1.00 38.36  ? 3992 LEU A CB    1 
ATOM   17968 C  CG    . LEU A 1 3992 ? 195.676 127.457 159.150 1.00 43.50  ? 3992 LEU A CG    1 
ATOM   17969 C  CD1   . LEU A 1 3992 ? 195.941 126.281 158.227 1.00 49.52  ? 3992 LEU A CD1   1 
ATOM   17970 C  CD2   . LEU A 1 3992 ? 196.961 128.212 159.444 1.00 47.64  ? 3992 LEU A CD2   1 
ATOM   17971 N  N     . ILE A 1 3993 ? 192.579 130.748 158.011 1.00 36.17  ? 3993 ILE A N     1 
ATOM   17972 C  CA    . ILE A 1 3993 ? 192.076 131.835 157.174 1.00 32.74  ? 3993 ILE A CA    1 
ATOM   17973 C  C     . ILE A 1 3993 ? 192.006 133.134 157.965 1.00 33.62  ? 3993 ILE A C     1 
ATOM   17974 O  O     . ILE A 1 3993 ? 192.377 134.201 157.463 1.00 41.57  ? 3993 ILE A O     1 
ATOM   17975 C  CB    . ILE A 1 3993 ? 190.709 131.466 156.568 1.00 33.36  ? 3993 ILE A CB    1 
ATOM   17976 C  CG1   . ILE A 1 3993 ? 190.841 130.249 155.652 1.00 39.80  ? 3993 ILE A CG1   1 
ATOM   17977 C  CG2   . ILE A 1 3993 ? 190.124 132.640 155.804 1.00 32.07  ? 3993 ILE A CG2   1 
ATOM   17978 C  CD1   . ILE A 1 3993 ? 191.762 130.474 154.476 1.00 41.24  ? 3993 ILE A CD1   1 
ATOM   17979 N  N     . GLN A 1 3994 ? 191.535 133.069 159.213 1.00 33.15  ? 3994 GLN A N     1 
ATOM   17980 C  CA    . GLN A 1 3994 ? 191.457 134.278 160.026 1.00 33.44  ? 3994 GLN A CA    1 
ATOM   17981 C  C     . GLN A 1 3994 ? 192.838 134.881 160.249 1.00 37.32  ? 3994 GLN A C     1 
ATOM   17982 O  O     . GLN A 1 3994 ? 192.999 136.107 160.230 1.00 37.29  ? 3994 GLN A O     1 
ATOM   17983 C  CB    . GLN A 1 3994 ? 190.786 133.976 161.365 1.00 33.54  ? 3994 GLN A CB    1 
ATOM   17984 C  CG    . GLN A 1 3994 ? 190.431 135.219 162.163 1.00 32.72  ? 3994 GLN A CG    1 
ATOM   17985 C  CD    . GLN A 1 3994 ? 190.249 134.935 163.638 1.00 37.95  ? 3994 GLN A CD    1 
ATOM   17986 O  OE1   . GLN A 1 3994 ? 190.659 133.887 164.135 1.00 42.50  ? 3994 GLN A OE1   1 
ATOM   17987 N  NE2   . GLN A 1 3994 ? 189.633 135.871 164.349 1.00 38.90  ? 3994 GLN A NE2   1 
ATOM   17988 N  N     . ALA A 1 3995 ? 193.848 134.036 160.464 1.00 40.25  ? 3995 ALA A N     1 
ATOM   17989 C  CA    . ALA A 1 3995 ? 195.199 134.548 160.676 1.00 39.00  ? 3995 ALA A CA    1 
ATOM   17990 C  C     . ALA A 1 3995 ? 195.817 135.064 159.380 1.00 39.19  ? 3995 ALA A C     1 
ATOM   17991 O  O     . ALA A 1 3995 ? 196.525 136.077 159.384 1.00 40.29  ? 3995 ALA A O     1 
ATOM   17992 C  CB    . ALA A 1 3995 ? 196.080 133.464 161.294 1.00 42.35  ? 3995 ALA A CB    1 
ATOM   17993 N  N     . PHE A 1 3996 ? 195.558 134.386 158.262 1.00 44.93  ? 3996 PHE A N     1 
ATOM   17994 C  CA    . PHE A 1 3996 ? 196.242 134.667 157.003 1.00 45.70  ? 3996 PHE A CA    1 
ATOM   17995 C  C     . PHE A 1 3996 ? 195.472 135.660 156.136 1.00 45.06  ? 3996 PHE A C     1 
ATOM   17996 O  O     . PHE A 1 3996 ? 195.989 136.726 155.790 1.00 54.47  ? 3996 PHE A O     1 
ATOM   17997 C  CB    . PHE A 1 3996 ? 196.466 133.359 156.237 1.00 46.48  ? 3996 PHE A CB    1 
ATOM   17998 C  CG    . PHE A 1 3996 ? 197.588 132.522 156.778 1.00 50.85  ? 3996 PHE A CG    1 
ATOM   17999 C  CD1   . PHE A 1 3996 ? 197.660 131.171 156.489 1.00 55.57  ? 3996 PHE A CD1   1 
ATOM   18000 C  CD2   . PHE A 1 3996 ? 198.576 133.087 157.563 1.00 46.99  ? 3996 PHE A CD2   1 
ATOM   18001 C  CE1   . PHE A 1 3996 ? 198.690 130.396 156.984 1.00 57.30  ? 3996 PHE A CE1   1 
ATOM   18002 C  CE2   . PHE A 1 3996 ? 199.609 132.316 158.056 1.00 49.95  ? 3996 PHE A CE2   1 
ATOM   18003 C  CZ    . PHE A 1 3996 ? 199.666 130.971 157.766 1.00 58.51  ? 3996 PHE A CZ    1 
ATOM   18004 N  N     . ARG A 1 3997 ? 194.232 135.319 155.778 1.00 38.35  ? 3997 ARG A N     1 
ATOM   18005 C  CA    . ARG A 1 3997 ? 193.422 136.095 154.842 1.00 34.31  ? 3997 ARG A CA    1 
ATOM   18006 C  C     . ARG A 1 3997 ? 192.097 136.434 155.515 1.00 34.32  ? 3997 ARG A C     1 
ATOM   18007 O  O     . ARG A 1 3997 ? 191.083 135.757 155.289 1.00 37.77  ? 3997 ARG A O     1 
ATOM   18008 C  CB    . ARG A 1 3997 ? 193.197 135.329 153.540 1.00 36.84  ? 3997 ARG A CB    1 
ATOM   18009 C  CG    . ARG A 1 3997 ? 194.455 135.125 152.711 1.00 42.62  ? 3997 ARG A CG    1 
ATOM   18010 C  CD    . ARG A 1 3997 ? 194.843 136.399 151.981 1.00 48.31  ? 3997 ARG A CD    1 
ATOM   18011 N  NE    . ARG A 1 3997 ? 193.739 136.927 151.189 1.00 48.07  ? 3997 ARG A NE    1 
ATOM   18012 C  CZ    . ARG A 1 3997 ? 193.423 136.509 149.971 1.00 46.17  ? 3997 ARG A CZ    1 
ATOM   18013 N  NH1   . ARG A 1 3997 ? 194.120 135.564 149.362 1.00 46.73  ? 3997 ARG A NH1   1 
ATOM   18014 N  NH2   . ARG A 1 3997 ? 192.384 137.056 149.347 1.00 49.59  ? 3997 ARG A NH2   1 
ATOM   18015 N  N     . PRO A 1 3998 ? 192.069 137.472 156.354 1.00 33.21  ? 3998 PRO A N     1 
ATOM   18016 C  CA    . PRO A 1 3998 ? 190.816 137.825 157.041 1.00 32.09  ? 3998 PRO A CA    1 
ATOM   18017 C  C     . PRO A 1 3998 ? 189.701 138.242 156.100 1.00 36.78  ? 3998 PRO A C     1 
ATOM   18018 O  O     . PRO A 1 3998 ? 188.531 138.209 156.500 1.00 40.81  ? 3998 PRO A O     1 
ATOM   18019 C  CB    . PRO A 1 3998 ? 191.232 138.978 157.966 1.00 33.11  ? 3998 PRO A CB    1 
ATOM   18020 C  CG    . PRO A 1 3998 ? 192.482 139.524 157.362 1.00 31.41  ? 3998 PRO A CG    1 
ATOM   18021 C  CD    . PRO A 1 3998 ? 193.179 138.365 156.722 1.00 35.02  ? 3998 PRO A CD    1 
ATOM   18022 N  N     . ASP A 1 3999 ? 190.021 138.639 154.866 1.00 35.76  ? 3999 ASP A N     1 
ATOM   18023 C  CA    . ASP A 1 3999 ? 188.984 138.994 153.904 1.00 32.95  ? 3999 ASP A CA    1 
ATOM   18024 C  C     . ASP A 1 3999 ? 188.140 137.795 153.495 1.00 40.17  ? 3999 ASP A C     1 
ATOM   18025 O  O     . ASP A 1 3999 ? 186.996 137.977 153.066 1.00 44.22  ? 3999 ASP A O     1 
ATOM   18026 C  CB    . ASP A 1 3999 ? 189.612 139.636 152.667 1.00 39.53  ? 3999 ASP A CB    1 
ATOM   18027 C  CG    . ASP A 1 3999 ? 190.765 138.825 152.110 1.00 45.88  ? 3999 ASP A CG    1 
ATOM   18028 O  OD1   . ASP A 1 3999 ? 191.847 138.822 152.734 1.00 43.16  ? 3999 ASP A OD1   1 
ATOM   18029 O  OD2   . ASP A 1 3999 ? 190.592 138.193 151.048 1.00 48.23  ? 3999 ASP A OD2   1 
ATOM   18030 N  N     . ARG A 1 4000 ? 188.672 136.580 153.619 1.00 38.19  ? 4000 ARG A N     1 
ATOM   18031 C  CA    . ARG A 1 4000 ? 187.939 135.362 153.301 1.00 31.72  ? 4000 ARG A CA    1 
ATOM   18032 C  C     . ARG A 1 4000 ? 187.371 134.688 154.544 1.00 33.06  ? 4000 ARG A C     1 
ATOM   18033 O  O     . ARG A 1 4000 ? 187.040 133.499 154.502 1.00 38.90  ? 4000 ARG A O     1 
ATOM   18034 C  CB    . ARG A 1 4000 ? 188.837 134.391 152.536 1.00 30.72  ? 4000 ARG A CB    1 
ATOM   18035 C  CG    . ARG A 1 4000 ? 189.580 135.023 151.374 1.00 35.98  ? 4000 ARG A CG    1 
ATOM   18036 C  CD    . ARG A 1 4000 ? 188.614 135.591 150.349 1.00 39.24  ? 4000 ARG A CD    1 
ATOM   18037 N  NE    . ARG A 1 4000 ? 187.724 134.568 149.814 1.00 41.92  ? 4000 ARG A NE    1 
ATOM   18038 C  CZ    . ARG A 1 4000 ? 186.674 134.818 149.044 1.00 44.35  ? 4000 ARG A CZ    1 
ATOM   18039 N  NH1   . ARG A 1 4000 ? 186.351 136.053 148.697 1.00 49.74  ? 4000 ARG A NH1   1 
ATOM   18040 N  NH2   . ARG A 1 4000 ? 185.930 133.804 148.612 1.00 40.51  ? 4000 ARG A NH2   1 
ATOM   18041 N  N     . LEU A 1 4001 ? 187.261 135.425 155.652 1.00 30.46  ? 4001 LEU A N     1 
ATOM   18042 C  CA    . LEU A 1 4001 ? 186.737 134.843 156.883 1.00 26.18  ? 4001 LEU A CA    1 
ATOM   18043 C  C     . LEU A 1 4001 ? 185.277 134.437 156.730 1.00 28.30  ? 4001 LEU A C     1 
ATOM   18044 O  O     . LEU A 1 4001 ? 184.860 133.397 157.252 1.00 39.78  ? 4001 LEU A O     1 
ATOM   18045 C  CB    . LEU A 1 4001 ? 186.900 135.830 158.039 1.00 25.21  ? 4001 LEU A CB    1 
ATOM   18046 C  CG    . LEU A 1 4001 ? 186.622 135.289 159.442 1.00 25.02  ? 4001 LEU A CG    1 
ATOM   18047 C  CD1   . LEU A 1 4001 ? 187.392 134.003 159.676 1.00 30.88  ? 4001 LEU A CD1   1 
ATOM   18048 C  CD2   . LEU A 1 4001 ? 186.973 136.324 160.496 1.00 30.81  ? 4001 LEU A CD2   1 
ATOM   18049 N  N     . LEU A 1 4002 ? 184.483 135.249 156.029 1.00 24.67  ? 4002 LEU A N     1 
ATOM   18050 C  CA    . LEU A 1 4002 ? 183.064 134.944 155.872 1.00 25.30  ? 4002 LEU A CA    1 
ATOM   18051 C  C     . LEU A 1 4002 ? 182.849 133.673 155.060 1.00 25.92  ? 4002 LEU A C     1 
ATOM   18052 O  O     . LEU A 1 4002 ? 181.990 132.852 155.398 1.00 31.86  ? 4002 LEU A O     1 
ATOM   18053 C  CB    . LEU A 1 4002 ? 182.344 136.124 155.223 1.00 31.00  ? 4002 LEU A CB    1 
ATOM   18054 C  CG    . LEU A 1 4002 ? 182.023 137.299 156.147 1.00 25.80  ? 4002 LEU A CG    1 
ATOM   18055 C  CD1   . LEU A 1 4002 ? 181.129 138.299 155.439 1.00 27.37  ? 4002 LEU A CD1   1 
ATOM   18056 C  CD2   . LEU A 1 4002 ? 181.377 136.814 157.434 1.00 23.71  ? 4002 LEU A CD2   1 
ATOM   18057 N  N     . ALA A 1 4003 ? 183.616 133.493 153.982 1.00 23.02  ? 4003 ALA A N     1 
ATOM   18058 C  CA    . ALA A 1 4003 ? 183.474 132.288 153.169 1.00 26.56  ? 4003 ALA A CA    1 
ATOM   18059 C  C     . ALA A 1 4003 ? 183.872 131.042 153.950 1.00 30.60  ? 4003 ALA A C     1 
ATOM   18060 O  O     . ALA A 1 4003 ? 183.215 129.998 153.847 1.00 33.70  ? 4003 ALA A O     1 
ATOM   18061 C  CB    . ALA A 1 4003 ? 184.307 132.416 151.895 1.00 29.51  ? 4003 ALA A CB    1 
ATOM   18062 N  N     . MET A 1 4004 ? 184.942 131.130 154.742 1.00 27.31  ? 4004 MET A N     1 
ATOM   18063 C  CA    . MET A 1 4004 ? 185.349 129.988 155.551 1.00 26.26  ? 4004 MET A CA    1 
ATOM   18064 C  C     . MET A 1 4004 ? 184.339 129.699 156.655 1.00 28.93  ? 4004 MET A C     1 
ATOM   18065 O  O     . MET A 1 4004 ? 184.107 128.536 157.000 1.00 35.07  ? 4004 MET A O     1 
ATOM   18066 C  CB    . MET A 1 4004 ? 186.741 130.222 156.131 1.00 25.28  ? 4004 MET A CB    1 
ATOM   18067 C  CG    . MET A 1 4004 ? 187.339 128.982 156.756 1.00 33.05  ? 4004 MET A CG    1 
ATOM   18068 S  SD    . MET A 1 4004 ? 187.924 127.767 155.566 1.00 45.22  ? 4004 MET A SD    1 
ATOM   18069 C  CE    . MET A 1 4004 ? 187.185 126.286 156.248 1.00 30.60  ? 4004 MET A CE    1 
ATOM   18070 N  N     . ALA A 1 4005 ? 183.726 130.741 157.221 1.00 24.67  ? 4005 ALA A N     1 
ATOM   18071 C  CA    . ALA A 1 4005 ? 182.647 130.526 158.179 1.00 21.11  ? 4005 ALA A CA    1 
ATOM   18072 C  C     . ALA A 1 4005 ? 181.460 129.835 157.517 1.00 23.82  ? 4005 ALA A C     1 
ATOM   18073 O  O     . ALA A 1 4005 ? 180.839 128.944 158.109 1.00 32.81  ? 4005 ALA A O     1 
ATOM   18074 C  CB    . ALA A 1 4005 ? 182.223 131.856 158.799 1.00 20.27  ? 4005 ALA A CB    1 
ATOM   18075 N  N     . HIS A 1 4006 ? 181.134 130.235 156.286 1.00 21.83  ? 4006 HIS A N     1 
ATOM   18076 C  CA    . HIS A 1 4006 ? 180.065 129.573 155.547 1.00 22.14  ? 4006 HIS A CA    1 
ATOM   18077 C  C     . HIS A 1 4006 ? 180.388 128.104 155.313 1.00 23.98  ? 4006 HIS A C     1 
ATOM   18078 O  O     . HIS A 1 4006 ? 179.514 127.239 155.443 1.00 26.87  ? 4006 HIS A O     1 
ATOM   18079 C  CB    . HIS A 1 4006 ? 179.830 130.282 154.213 1.00 23.25  ? 4006 HIS A CB    1 
ATOM   18080 C  CG    . HIS A 1 4006 ? 178.854 131.412 154.292 1.00 30.39  ? 4006 HIS A CG    1 
ATOM   18081 N  ND1   . HIS A 1 4006 ? 179.189 132.652 154.792 1.00 33.47  ? 4006 HIS A ND1   1 
ATOM   18082 C  CD2   . HIS A 1 4006 ? 177.551 131.491 153.934 1.00 30.62  ? 4006 HIS A CD2   1 
ATOM   18083 C  CE1   . HIS A 1 4006 ? 178.134 133.445 154.740 1.00 33.70  ? 4006 HIS A CE1   1 
ATOM   18084 N  NE2   . HIS A 1 4006 ? 177.127 132.765 154.223 1.00 34.30  ? 4006 HIS A NE2   1 
ATOM   18085 N  N     . MET A 1 4007 ? 181.640 127.800 154.965 1.00 24.23  ? 4007 MET A N     1 
ATOM   18086 C  CA    . MET A 1 4007 ? 182.003 126.404 154.738 1.00 25.59  ? 4007 MET A CA    1 
ATOM   18087 C  C     . MET A 1 4007 ? 182.016 125.605 156.037 1.00 28.10  ? 4007 MET A C     1 
ATOM   18088 O  O     . MET A 1 4007 ? 181.686 124.416 156.028 1.00 37.26  ? 4007 MET A O     1 
ATOM   18089 C  CB    . MET A 1 4007 ? 183.351 126.305 154.026 1.00 27.76  ? 4007 MET A CB    1 
ATOM   18090 C  CG    . MET A 1 4007 ? 183.376 127.016 152.679 1.00 34.98  ? 4007 MET A CG    1 
ATOM   18091 S  SD    . MET A 1 4007 ? 184.769 126.543 151.635 1.00 54.29  ? 4007 MET A SD    1 
ATOM   18092 C  CE    . MET A 1 4007 ? 186.023 126.205 152.863 1.00 38.46  ? 4007 MET A CE    1 
ATOM   18093 N  N     . PHE A 1 4008 ? 182.379 126.232 157.158 1.00 24.92  ? 4008 PHE A N     1 
ATOM   18094 C  CA    . PHE A 1 4008 ? 182.262 125.559 158.449 1.00 24.19  ? 4008 PHE A CA    1 
ATOM   18095 C  C     . PHE A 1 4008 ? 180.806 125.255 158.781 1.00 25.02  ? 4008 PHE A C     1 
ATOM   18096 O  O     . PHE A 1 4008 ? 180.484 124.169 159.285 1.00 28.46  ? 4008 PHE A O     1 
ATOM   18097 C  CB    . PHE A 1 4008 ? 182.893 126.416 159.545 1.00 24.28  ? 4008 PHE A CB    1 
ATOM   18098 C  CG    . PHE A 1 4008 ? 182.641 125.906 160.934 1.00 30.25  ? 4008 PHE A CG    1 
ATOM   18099 C  CD1   . PHE A 1 4008 ? 183.346 124.825 161.431 1.00 38.30  ? 4008 PHE A CD1   1 
ATOM   18100 C  CD2   . PHE A 1 4008 ? 181.697 126.512 161.745 1.00 30.42  ? 4008 PHE A CD2   1 
ATOM   18101 C  CE1   . PHE A 1 4008 ? 183.112 124.358 162.709 1.00 38.33  ? 4008 PHE A CE1   1 
ATOM   18102 C  CE2   . PHE A 1 4008 ? 181.461 126.052 163.024 1.00 30.43  ? 4008 PHE A CE2   1 
ATOM   18103 C  CZ    . PHE A 1 4008 ? 182.169 124.974 163.507 1.00 35.36  ? 4008 PHE A CZ    1 
ATOM   18104 N  N     . VAL A 1 4009 ? 179.911 126.208 158.511 1.00 27.40  ? 4009 VAL A N     1 
ATOM   18105 C  CA    . VAL A 1 4009 ? 178.486 125.978 158.730 1.00 23.42  ? 4009 VAL A CA    1 
ATOM   18106 C  C     . VAL A 1 4009 ? 177.988 124.849 157.837 1.00 25.93  ? 4009 VAL A C     1 
ATOM   18107 O  O     . VAL A 1 4009 ? 177.171 124.023 158.255 1.00 30.19  ? 4009 VAL A O     1 
ATOM   18108 C  CB    . VAL A 1 4009 ? 177.692 127.277 158.502 1.00 20.46  ? 4009 VAL A CB    1 
ATOM   18109 C  CG1   . VAL A 1 4009 ? 176.197 127.004 158.552 1.00 21.75  ? 4009 VAL A CG1   1 
ATOM   18110 C  CG2   . VAL A 1 4009 ? 178.072 128.316 159.542 1.00 21.53  ? 4009 VAL A CG2   1 
ATOM   18111 N  N     . SER A 1 4010 ? 178.470 124.796 156.594 1.00 24.86  ? 4010 SER A N     1 
ATOM   18112 C  CA    . SER A 1 4010 ? 178.080 123.709 155.700 1.00 27.77  ? 4010 SER A CA    1 
ATOM   18113 C  C     . SER A 1 4010 ? 178.604 122.368 156.201 1.00 30.86  ? 4010 SER A C     1 
ATOM   18114 O  O     . SER A 1 4010 ? 177.916 121.345 156.101 1.00 32.33  ? 4010 SER A O     1 
ATOM   18115 C  CB    . SER A 1 4010 ? 178.582 123.982 154.283 1.00 30.23  ? 4010 SER A CB    1 
ATOM   18116 O  OG    . SER A 1 4010 ? 179.995 123.941 154.228 1.00 38.39  ? 4010 SER A OG    1 
ATOM   18117 N  N     . THR A 1 4011 ? 179.828 122.351 156.732 1.00 30.10  ? 4011 THR A N     1 
ATOM   18118 C  CA    . THR A 1 4011 ? 180.396 121.114 157.259 1.00 29.79  ? 4011 THR A CA    1 
ATOM   18119 C  C     . THR A 1 4011 ? 179.603 120.608 158.457 1.00 32.83  ? 4011 THR A C     1 
ATOM   18120 O  O     . THR A 1 4011 ? 179.343 119.405 158.576 1.00 35.03  ? 4011 THR A O     1 
ATOM   18121 C  CB    . THR A 1 4011 ? 181.860 121.331 157.643 1.00 29.40  ? 4011 THR A CB    1 
ATOM   18122 O  OG1   . THR A 1 4011 ? 182.584 121.839 156.515 1.00 34.63  ? 4011 THR A OG1   1 
ATOM   18123 C  CG2   . THR A 1 4011 ? 182.493 120.026 158.098 1.00 36.19  ? 4011 THR A CG2   1 
ATOM   18124 N  N     . ASN A 1 4012 ? 179.208 121.512 159.354 1.00 32.40  ? 4012 ASN A N     1 
ATOM   18125 C  CA    . ASN A 1 4012 ? 178.498 121.091 160.559 1.00 27.87  ? 4012 ASN A CA    1 
ATOM   18126 C  C     . ASN A 1 4012 ? 177.034 120.768 160.272 1.00 29.12  ? 4012 ASN A C     1 
ATOM   18127 O  O     . ASN A 1 4012 ? 176.567 119.655 160.540 1.00 31.38  ? 4012 ASN A O     1 
ATOM   18128 C  CB    . ASN A 1 4012 ? 178.604 122.172 161.638 1.00 22.57  ? 4012 ASN A CB    1 
ATOM   18129 C  CG    . ASN A 1 4012 ? 180.009 122.317 162.179 1.00 28.68  ? 4012 ASN A CG    1 
ATOM   18130 O  OD1   . ASN A 1 4012 ? 180.982 122.291 161.428 1.00 35.51  ? 4012 ASN A OD1   1 
ATOM   18131 N  ND2   . ASN A 1 4012 ? 180.123 122.466 163.493 1.00 33.25  ? 4012 ASN A ND2   1 
ATOM   18132 N  N     . LEU A 1 4013 ? 176.297 121.731 159.727 1.00 27.37  ? 4013 LEU A N     1 
ATOM   18133 C  CA    . LEU A 1 4013 ? 174.848 121.661 159.606 1.00 24.90  ? 4013 LEU A CA    1 
ATOM   18134 C  C     . LEU A 1 4013 ? 174.369 121.184 158.240 1.00 30.53  ? 4013 LEU A C     1 
ATOM   18135 O  O     . LEU A 1 4013 ? 173.175 120.914 158.081 1.00 34.82  ? 4013 LEU A O     1 
ATOM   18136 C  CB    . LEU A 1 4013 ? 174.250 123.038 159.911 1.00 22.58  ? 4013 LEU A CB    1 
ATOM   18137 C  CG    . LEU A 1 4013 ? 174.445 123.511 161.352 1.00 21.20  ? 4013 LEU A CG    1 
ATOM   18138 C  CD1   . LEU A 1 4013 ? 174.028 124.955 161.514 1.00 19.40  ? 4013 LEU A CD1   1 
ATOM   18139 C  CD2   . LEU A 1 4013 ? 173.643 122.637 162.289 1.00 23.12  ? 4013 LEU A CD2   1 
ATOM   18140 N  N     . GLY A 1 4014 ? 175.251 121.069 157.265 1.00 31.69  ? 4014 GLY A N     1 
ATOM   18141 C  CA    . GLY A 1 4014 ? 174.840 120.651 155.941 1.00 34.22  ? 4014 GLY A CA    1 
ATOM   18142 C  C     . GLY A 1 4014 ? 175.069 121.743 154.909 1.00 38.77  ? 4014 GLY A C     1 
ATOM   18143 O  O     . GLY A 1 4014 ? 175.012 122.944 155.206 1.00 43.28  ? 4014 GLY A O     1 
ATOM   18144 N  N     . GLU A 1 4015 ? 175.325 121.317 153.669 1.00 41.41  ? 4015 GLU A N     1 
ATOM   18145 C  CA    . GLU A 1 4015 ? 175.660 122.265 152.609 1.00 44.78  ? 4015 GLU A CA    1 
ATOM   18146 C  C     . GLU A 1 4015 ? 174.492 123.180 152.266 1.00 40.98  ? 4015 GLU A C     1 
ATOM   18147 O  O     . GLU A 1 4015 ? 174.703 124.356 151.948 1.00 41.12  ? 4015 GLU A O     1 
ATOM   18148 C  CB    . GLU A 1 4015 ? 176.126 121.515 151.361 1.00 50.63  ? 4015 GLU A CB    1 
ATOM   18149 C  CG    . GLU A 1 4015 ? 177.471 120.824 151.512 1.00 56.48  ? 4015 GLU A CG    1 
ATOM   18150 C  CD    . GLU A 1 4015 ? 177.344 119.318 151.644 1.00 76.15  ? 4015 GLU A CD    1 
ATOM   18151 O  OE1   . GLU A 1 4015 ? 176.546 118.858 152.487 1.00 77.27  ? 4015 GLU A OE1   1 
ATOM   18152 O  OE2   . GLU A 1 4015 ? 178.043 118.595 150.904 1.00 83.79  ? 4015 GLU A OE2   1 
ATOM   18153 N  N     . SER A 1 4016 ? 173.262 122.669 152.319 1.00 40.58  ? 4016 SER A N     1 
ATOM   18154 C  CA    . SER A 1 4016 ? 172.079 123.440 151.965 1.00 38.85  ? 4016 SER A CA    1 
ATOM   18155 C  C     . SER A 1 4016 ? 171.377 124.027 153.185 1.00 39.09  ? 4016 SER A C     1 
ATOM   18156 O  O     . SER A 1 4016 ? 170.166 124.265 153.139 1.00 39.41  ? 4016 SER A O     1 
ATOM   18157 C  CB    . SER A 1 4016 ? 171.106 122.573 151.166 1.00 43.26  ? 4016 SER A CB    1 
ATOM   18158 O  OG    . SER A 1 4016 ? 170.777 121.391 151.875 1.00 41.86  ? 4016 SER A OG    1 
ATOM   18159 N  N     . PHE A 1 4017 ? 172.112 124.261 154.274 1.00 34.26  ? 4017 PHE A N     1 
ATOM   18160 C  CA    . PHE A 1 4017 ? 171.493 124.798 155.482 1.00 28.13  ? 4017 PHE A CA    1 
ATOM   18161 C  C     . PHE A 1 4017 ? 171.002 126.224 155.266 1.00 33.58  ? 4017 PHE A C     1 
ATOM   18162 O  O     . PHE A 1 4017 ? 169.859 126.556 155.603 1.00 34.60  ? 4017 PHE A O     1 
ATOM   18163 C  CB    . PHE A 1 4017 ? 172.481 124.747 156.646 1.00 24.03  ? 4017 PHE A CB    1 
ATOM   18164 C  CG    . PHE A 1 4017 ? 171.861 125.065 157.974 1.00 24.32  ? 4017 PHE A CG    1 
ATOM   18165 C  CD1   . PHE A 1 4017 ? 170.999 124.169 158.582 1.00 23.11  ? 4017 PHE A CD1   1 
ATOM   18166 C  CD2   . PHE A 1 4017 ? 172.119 126.270 158.604 1.00 22.28  ? 4017 PHE A CD2   1 
ATOM   18167 C  CE1   . PHE A 1 4017 ? 170.422 124.459 159.800 1.00 19.90  ? 4017 PHE A CE1   1 
ATOM   18168 C  CE2   . PHE A 1 4017 ? 171.539 126.568 159.819 1.00 21.52  ? 4017 PHE A CE2   1 
ATOM   18169 C  CZ    . PHE A 1 4017 ? 170.693 125.659 160.419 1.00 20.14  ? 4017 PHE A CZ    1 
ATOM   18170 N  N     . MET A 1 4018 ? 171.850 127.081 154.703 1.00 33.03  ? 4018 MET A N     1 
ATOM   18171 C  CA    . MET A 1 4018 ? 171.530 128.487 154.502 1.00 27.47  ? 4018 MET A CA    1 
ATOM   18172 C  C     . MET A 1 4018 ? 171.019 128.777 153.097 1.00 35.68  ? 4018 MET A C     1 
ATOM   18173 O  O     . MET A 1 4018 ? 170.857 129.946 152.736 1.00 36.89  ? 4018 MET A O     1 
ATOM   18174 C  CB    . MET A 1 4018 ? 172.757 129.351 154.801 1.00 23.33  ? 4018 MET A CB    1 
ATOM   18175 C  CG    . MET A 1 4018 ? 173.311 129.173 156.204 1.00 21.55  ? 4018 MET A CG    1 
ATOM   18176 S  SD    . MET A 1 4018 ? 174.972 129.844 156.394 1.00 42.60  ? 4018 MET A SD    1 
ATOM   18177 C  CE    . MET A 1 4018 ? 174.615 131.592 156.535 1.00 19.99  ? 4018 MET A CE    1 
ATOM   18178 N  N     . SER A 1 4019 ? 170.762 127.740 152.297 1.00 38.85  ? 4019 SER A N     1 
ATOM   18179 C  CA    . SER A 1 4019 ? 170.313 127.928 150.924 1.00 41.99  ? 4019 SER A CA    1 
ATOM   18180 C  C     . SER A 1 4019 ? 168.902 128.494 150.830 1.00 45.22  ? 4019 SER A C     1 
ATOM   18181 O  O     . SER A 1 4019 ? 168.509 128.960 149.756 1.00 48.75  ? 4019 SER A O     1 
ATOM   18182 C  CB    . SER A 1 4019 ? 170.382 126.601 150.165 1.00 47.89  ? 4019 SER A CB    1 
ATOM   18183 O  OG    . SER A 1 4019 ? 169.613 126.654 148.976 1.00 61.45  ? 4019 SER A OG    1 
ATOM   18184 N  N     . ILE A 1 4020 ? 168.128 128.452 151.915 1.00 42.11  ? 4020 ILE A N     1 
ATOM   18185 C  CA    . ILE A 1 4020 ? 166.775 128.997 151.877 1.00 42.05  ? 4020 ILE A CA    1 
ATOM   18186 C  C     . ILE A 1 4020 ? 166.811 130.519 151.792 1.00 40.58  ? 4020 ILE A C     1 
ATOM   18187 O  O     . ILE A 1 4020 ? 166.010 131.134 151.078 1.00 44.27  ? 4020 ILE A O     1 
ATOM   18188 C  CB    . ILE A 1 4020 ? 165.972 128.513 153.098 1.00 46.36  ? 4020 ILE A CB    1 
ATOM   18189 C  CG1   . ILE A 1 4020 ? 165.905 126.985 153.116 1.00 45.26  ? 4020 ILE A CG1   1 
ATOM   18190 C  CG2   . ILE A 1 4020 ? 164.572 129.105 153.088 1.00 35.84  ? 4020 ILE A CG2   1 
ATOM   18191 C  CD1   . ILE A 1 4020 ? 165.221 126.391 151.904 1.00 42.21  ? 4020 ILE A CD1   1 
ATOM   18192 N  N     . MET A 1 4021 ? 167.742 131.150 152.511 1.00 40.76  ? 4021 MET A N     1 
ATOM   18193 C  CA    . MET A 1 4021 ? 167.787 132.605 152.595 1.00 41.40  ? 4021 MET A CA    1 
ATOM   18194 C  C     . MET A 1 4021 ? 168.152 133.276 151.277 1.00 41.90  ? 4021 MET A C     1 
ATOM   18195 O  O     . MET A 1 4021 ? 167.927 134.483 151.140 1.00 48.45  ? 4021 MET A O     1 
ATOM   18196 C  CB    . MET A 1 4021 ? 168.775 133.034 153.680 1.00 38.98  ? 4021 MET A CB    1 
ATOM   18197 C  CG    . MET A 1 4021 ? 168.332 132.698 155.096 1.00 34.52  ? 4021 MET A CG    1 
ATOM   18198 S  SD    . MET A 1 4021 ? 166.701 133.351 155.500 1.00 39.76  ? 4021 MET A SD    1 
ATOM   18199 C  CE    . MET A 1 4021 ? 165.725 131.850 155.525 1.00 27.37  ? 4021 MET A CE    1 
ATOM   18200 N  N     . GLU A 1 4022 ? 168.703 132.543 150.314 1.00 41.90  ? 4022 GLU A N     1 
ATOM   18201 C  CA    . GLU A 1 4022 ? 169.045 133.115 149.018 1.00 40.44  ? 4022 GLU A CA    1 
ATOM   18202 C  C     . GLU A 1 4022 ? 167.914 132.998 148.005 1.00 39.61  ? 4022 GLU A C     1 
ATOM   18203 O  O     . GLU A 1 4022 ? 168.087 133.410 146.854 1.00 37.37  ? 4022 GLU A O     1 
ATOM   18204 C  CB    . GLU A 1 4022 ? 170.311 132.454 148.462 1.00 43.15  ? 4022 GLU A CB    1 
ATOM   18205 C  CG    . GLU A 1 4022 ? 170.127 131.012 148.030 1.00 48.22  ? 4022 GLU A CG    1 
ATOM   18206 C  CD    . GLU A 1 4022 ? 171.444 130.308 147.770 1.00 57.03  ? 4022 GLU A CD    1 
ATOM   18207 O  OE1   . GLU A 1 4022 ? 172.278 130.244 148.697 1.00 59.90  ? 4022 GLU A OE1   1 
ATOM   18208 O  OE2   . GLU A 1 4022 ? 171.644 129.817 146.639 1.00 60.27  ? 4022 GLU A OE2   1 
ATOM   18209 N  N     . GLN A 1 4023 ? 166.762 132.446 148.405 1.00 43.28  ? 4023 GLN A N     1 
ATOM   18210 C  CA    . GLN A 1 4023 ? 165.564 132.336 147.591 1.00 40.84  ? 4023 GLN A CA    1 
ATOM   18211 C  C     . GLN A 1 4023 ? 164.585 133.452 147.934 1.00 44.66  ? 4023 GLN A C     1 
ATOM   18212 O  O     . GLN A 1 4023 ? 164.559 133.935 149.070 1.00 47.33  ? 4023 GLN A O     1 
ATOM   18213 C  CB    . GLN A 1 4023 ? 164.883 130.980 147.809 1.00 39.30  ? 4023 GLN A CB    1 
ATOM   18214 C  CG    . GLN A 1 4023 ? 165.770 129.782 147.520 1.00 46.50  ? 4023 GLN A CG    1 
ATOM   18215 C  CD    . GLN A 1 4023 ? 166.335 129.801 146.113 1.00 59.73  ? 4023 GLN A CD    1 
ATOM   18216 O  OE1   . GLN A 1 4023 ? 165.602 129.977 145.140 1.00 60.88  ? 4023 GLN A OE1   1 
ATOM   18217 N  NE2   . GLN A 1 4023 ? 167.645 129.618 145.999 1.00 63.13  ? 4023 GLN A NE2   1 
ATOM   18218 N  N     . PRO A 1 4024 ? 163.778 133.895 146.970 1.00 45.66  ? 4024 PRO A N     1 
ATOM   18219 C  CA    . PRO A 1 4024 ? 162.788 134.937 147.265 1.00 41.64  ? 4024 PRO A CA    1 
ATOM   18220 C  C     . PRO A 1 4024 ? 161.802 134.476 148.329 1.00 45.62  ? 4024 PRO A C     1 
ATOM   18221 O  O     . PRO A 1 4024 ? 161.405 133.310 148.372 1.00 46.64  ? 4024 PRO A O     1 
ATOM   18222 C  CB    . PRO A 1 4024 ? 162.096 135.168 145.916 1.00 35.22  ? 4024 PRO A CB    1 
ATOM   18223 C  CG    . PRO A 1 4024 ? 162.421 133.962 145.094 1.00 36.16  ? 4024 PRO A CG    1 
ATOM   18224 C  CD    . PRO A 1 4024 ? 163.769 133.510 145.550 1.00 41.31  ? 4024 PRO A CD    1 
ATOM   18225 N  N     . LEU A 1 4025 ? 161.414 135.409 149.194 1.00 42.34  ? 4025 LEU A N     1 
ATOM   18226 C  CA    . LEU A 1 4025 ? 160.517 135.083 150.293 1.00 36.48  ? 4025 LEU A CA    1 
ATOM   18227 C  C     . LEU A 1 4025 ? 159.135 134.716 149.769 1.00 45.18  ? 4025 LEU A C     1 
ATOM   18228 O  O     . LEU A 1 4025 ? 158.567 135.411 148.922 1.00 52.23  ? 4025 LEU A O     1 
ATOM   18229 C  CB    . LEU A 1 4025 ? 160.421 136.261 151.262 1.00 29.60  ? 4025 LEU A CB    1 
ATOM   18230 C  CG    . LEU A 1 4025 ? 159.360 136.168 152.359 1.00 24.84  ? 4025 LEU A CG    1 
ATOM   18231 C  CD1   . LEU A 1 4025 ? 159.735 135.107 153.374 1.00 27.94  ? 4025 LEU A CD1   1 
ATOM   18232 C  CD2   . LEU A 1 4025 ? 159.179 137.514 153.036 1.00 24.88  ? 4025 LEU A CD2   1 
ATOM   18233 N  N     . ASP A 1 4026 ? 158.594 133.615 150.280 1.00 46.06  ? 4026 ASP A N     1 
ATOM   18234 C  CA    . ASP A 1 4026 ? 157.279 133.113 149.891 1.00 42.66  ? 4026 ASP A CA    1 
ATOM   18235 C  C     . ASP A 1 4026 ? 156.316 133.414 151.036 1.00 42.76  ? 4026 ASP A C     1 
ATOM   18236 O  O     . ASP A 1 4026 ? 156.202 132.646 151.992 1.00 45.09  ? 4026 ASP A O     1 
ATOM   18237 C  CB    . ASP A 1 4026 ? 157.333 131.621 149.574 1.00 46.30  ? 4026 ASP A CB    1 
ATOM   18238 C  CG    . ASP A 1 4026 ? 155.968 131.039 149.275 1.00 50.48  ? 4026 ASP A CG    1 
ATOM   18239 O  OD1   . ASP A 1 4026 ? 155.304 131.527 148.336 1.00 51.83  ? 4026 ASP A OD1   1 
ATOM   18240 O  OD2   . ASP A 1 4026 ? 155.558 130.091 149.976 1.00 48.78  ? 4026 ASP A OD2   1 
ATOM   18241 N  N     . LEU A 1 4027 ? 155.620 134.548 150.929 1.00 39.01  ? 4027 LEU A N     1 
ATOM   18242 C  CA    . LEU A 1 4027 ? 154.716 134.969 151.991 1.00 35.21  ? 4027 LEU A CA    1 
ATOM   18243 C  C     . LEU A 1 4027 ? 153.416 134.176 152.006 1.00 42.08  ? 4027 LEU A C     1 
ATOM   18244 O  O     . LEU A 1 4027 ? 152.722 134.179 153.025 1.00 46.80  ? 4027 LEU A O     1 
ATOM   18245 C  CB    . LEU A 1 4027 ? 154.408 136.460 151.860 1.00 35.84  ? 4027 LEU A CB    1 
ATOM   18246 C  CG    . LEU A 1 4027 ? 155.458 137.421 152.417 1.00 38.87  ? 4027 LEU A CG    1 
ATOM   18247 C  CD1   . LEU A 1 4027 ? 155.118 138.855 152.049 1.00 37.82  ? 4027 LEU A CD1   1 
ATOM   18248 C  CD2   . LEU A 1 4027 ? 155.578 137.266 153.925 1.00 32.79  ? 4027 LEU A CD2   1 
ATOM   18249 N  N     . THR A 1 4028 ? 153.070 133.500 150.908 1.00 44.44  ? 4028 THR A N     1 
ATOM   18250 C  CA    . THR A 1 4028 ? 151.809 132.764 150.862 1.00 44.46  ? 4028 THR A CA    1 
ATOM   18251 C  C     . THR A 1 4028 ? 151.786 131.642 151.893 1.00 45.86  ? 4028 THR A C     1 
ATOM   18252 O  O     . THR A 1 4028 ? 150.862 131.550 152.710 1.00 47.43  ? 4028 THR A O     1 
ATOM   18253 C  CB    . THR A 1 4028 ? 151.580 132.204 149.458 1.00 46.30  ? 4028 THR A CB    1 
ATOM   18254 O  OG1   . THR A 1 4028 ? 151.711 133.255 148.493 1.00 42.26  ? 4028 THR A OG1   1 
ATOM   18255 C  CG2   . THR A 1 4028 ? 150.194 131.589 149.349 1.00 45.48  ? 4028 THR A CG2   1 
ATOM   18256 N  N     . HIS A 1 4029 ? 152.808 130.783 151.877 1.00 43.63  ? 4029 HIS A N     1 
ATOM   18257 C  CA    . HIS A 1 4029 ? 152.866 129.676 152.825 1.00 47.02  ? 4029 HIS A CA    1 
ATOM   18258 C  C     . HIS A 1 4029 ? 153.060 130.177 154.250 1.00 47.14  ? 4029 HIS A C     1 
ATOM   18259 O  O     . HIS A 1 4029 ? 152.455 129.648 155.189 1.00 49.21  ? 4029 HIS A O     1 
ATOM   18260 C  CB    . HIS A 1 4029 ? 153.990 128.716 152.436 1.00 49.24  ? 4029 HIS A CB    1 
ATOM   18261 C  CG    . HIS A 1 4029 ? 154.247 127.640 153.445 1.00 59.86  ? 4029 HIS A CG    1 
ATOM   18262 N  ND1   . HIS A 1 4029 ? 155.514 127.188 153.742 1.00 58.92  ? 4029 HIS A ND1   1 
ATOM   18263 C  CD2   . HIS A 1 4029 ? 153.400 126.919 154.218 1.00 57.52  ? 4029 HIS A CD2   1 
ATOM   18264 C  CE1   . HIS A 1 4029 ? 155.438 126.241 154.660 1.00 59.59  ? 4029 HIS A CE1   1 
ATOM   18265 N  NE2   . HIS A 1 4029 ? 154.166 126.059 154.966 1.00 57.59  ? 4029 HIS A NE2   1 
ATOM   18266 N  N     . ILE A 1 4030 ? 153.896 131.202 154.429 1.00 43.26  ? 4030 ILE A N     1 
ATOM   18267 C  CA    . ILE A 1 4030 ? 154.226 131.687 155.767 1.00 40.80  ? 4030 ILE A CA    1 
ATOM   18268 C  C     . ILE A 1 4030 ? 153.107 132.521 156.373 1.00 39.87  ? 4030 ILE A C     1 
ATOM   18269 O  O     . ILE A 1 4030 ? 153.099 132.745 157.589 1.00 44.33  ? 4030 ILE A O     1 
ATOM   18270 C  CB    . ILE A 1 4030 ? 155.559 132.455 155.682 1.00 38.82  ? 4030 ILE A CB    1 
ATOM   18271 C  CG1   . ILE A 1 4030 ? 156.656 131.530 155.159 1.00 41.98  ? 4030 ILE A CG1   1 
ATOM   18272 C  CG2   . ILE A 1 4030 ? 155.999 132.951 157.041 1.00 39.47  ? 4030 ILE A CG2   1 
ATOM   18273 C  CD1   . ILE A 1 4030 ? 157.935 132.246 154.799 1.00 37.13  ? 4030 ILE A CD1   1 
ATOM   18274 N  N     . VAL A 1 4031 ? 152.147 132.968 155.571 1.00 43.71  ? 4031 VAL A N     1 
ATOM   18275 C  CA    . VAL A 1 4031 ? 150.988 133.693 156.073 1.00 36.88  ? 4031 VAL A CA    1 
ATOM   18276 C  C     . VAL A 1 4031 ? 149.787 132.772 156.254 1.00 41.13  ? 4031 VAL A C     1 
ATOM   18277 O  O     . VAL A 1 4031 ? 149.087 132.858 157.264 1.00 41.53  ? 4031 VAL A O     1 
ATOM   18278 C  CB    . VAL A 1 4031 ? 150.652 134.876 155.139 1.00 33.39  ? 4031 VAL A CB    1 
ATOM   18279 C  CG1   . VAL A 1 4031 ? 149.208 135.315 155.319 1.00 31.73  ? 4031 VAL A CG1   1 
ATOM   18280 C  CG2   . VAL A 1 4031 ? 151.594 136.039 155.406 1.00 30.12  ? 4031 VAL A CG2   1 
ATOM   18281 N  N     . GLY A 1 4032 ? 149.542 131.878 155.293 1.00 44.77  ? 4032 GLY A N     1 
ATOM   18282 C  CA    . GLY A 1 4032 ? 148.443 130.937 155.439 1.00 44.21  ? 4032 GLY A CA    1 
ATOM   18283 C  C     . GLY A 1 4032 ? 148.621 130.016 156.631 1.00 49.95  ? 4032 GLY A C     1 
ATOM   18284 O  O     . GLY A 1 4032 ? 147.653 129.671 157.313 1.00 52.05  ? 4032 GLY A O     1 
ATOM   18285 N  N     . THR A 1 4033 ? 149.858 129.605 156.896 1.00 51.11  ? 4033 THR A N     1 
ATOM   18286 C  CA    . THR A 1 4033 ? 150.201 128.808 158.062 1.00 52.72  ? 4033 THR A CA    1 
ATOM   18287 C  C     . THR A 1 4033 ? 151.364 129.473 158.785 1.00 53.89  ? 4033 THR A C     1 
ATOM   18288 O  O     . THR A 1 4033 ? 151.908 130.481 158.331 1.00 53.90  ? 4033 THR A O     1 
ATOM   18289 C  CB    . THR A 1 4033 ? 150.564 127.368 157.676 1.00 51.37  ? 4033 THR A CB    1 
ATOM   18290 O  OG1   . THR A 1 4033 ? 151.393 127.380 156.508 1.00 47.33  ? 4033 THR A OG1   1 
ATOM   18291 C  CG2   . THR A 1 4033 ? 149.308 126.561 157.391 1.00 55.15  ? 4033 THR A CG2   1 
ATOM   18292 N  N     . GLU A 1 4034 ? 151.733 128.905 159.933 1.00 50.92  ? 4034 GLU A N     1 
ATOM   18293 C  CA    . GLU A 1 4034 ? 152.849 129.325 160.778 1.00 49.17  ? 4034 GLU A CA    1 
ATOM   18294 C  C     . GLU A 1 4034 ? 152.637 130.686 161.432 1.00 51.74  ? 4034 GLU A C     1 
ATOM   18295 O  O     . GLU A 1 4034 ? 153.509 131.130 162.189 1.00 55.30  ? 4034 GLU A O     1 
ATOM   18296 C  CB    . GLU A 1 4034 ? 154.185 129.356 160.017 1.00 45.24  ? 4034 GLU A CB    1 
ATOM   18297 C  CG    . GLU A 1 4034 ? 154.471 128.113 159.191 1.00 54.15  ? 4034 GLU A CG    1 
ATOM   18298 C  CD    . GLU A 1 4034 ? 155.745 128.236 158.380 1.00 53.81  ? 4034 GLU A CD    1 
ATOM   18299 O  OE1   . GLU A 1 4034 ? 156.372 129.316 158.415 1.00 46.08  ? 4034 GLU A OE1   1 
ATOM   18300 O  OE2   . GLU A 1 4034 ? 156.120 127.254 157.706 1.00 56.68  ? 4034 GLU A OE2   1 
ATOM   18301 N  N     . VAL A 1 4035 ? 151.522 131.365 161.172 1.00 49.16  ? 4035 VAL A N     1 
ATOM   18302 C  CA    . VAL A 1 4035 ? 151.212 132.645 161.801 1.00 43.97  ? 4035 VAL A CA    1 
ATOM   18303 C  C     . VAL A 1 4035 ? 149.791 132.583 162.340 1.00 43.12  ? 4035 VAL A C     1 
ATOM   18304 O  O     . VAL A 1 4035 ? 148.848 132.318 161.586 1.00 45.04  ? 4035 VAL A O     1 
ATOM   18305 C  CB    . VAL A 1 4035 ? 151.370 133.828 160.830 1.00 37.27  ? 4035 VAL A CB    1 
ATOM   18306 C  CG1   . VAL A 1 4035 ? 150.867 135.107 161.474 1.00 34.90  ? 4035 VAL A CG1   1 
ATOM   18307 C  CG2   . VAL A 1 4035 ? 152.825 133.993 160.438 1.00 38.93  ? 4035 VAL A CG2   1 
ATOM   18308 N  N     . LYS A 1 4036 ? 149.641 132.825 163.639 1.00 40.59  ? 4036 LYS A N     1 
ATOM   18309 C  CA    . LYS A 1 4036 ? 148.330 132.873 164.261 1.00 40.04  ? 4036 LYS A CA    1 
ATOM   18310 C  C     . LYS A 1 4036 ? 147.621 134.178 163.905 1.00 36.02  ? 4036 LYS A C     1 
ATOM   18311 O  O     . LYS A 1 4036 ? 148.271 135.185 163.613 1.00 35.58  ? 4036 LYS A O     1 
ATOM   18312 C  CB    . LYS A 1 4036 ? 148.457 132.745 165.776 1.00 44.15  ? 4036 LYS A CB    1 
ATOM   18313 C  CG    . LYS A 1 4036 ? 148.733 131.329 166.258 1.00 48.51  ? 4036 LYS A CG    1 
ATOM   18314 C  CD    . LYS A 1 4036 ? 147.954 130.304 165.448 1.00 47.06  ? 4036 LYS A CD    1 
ATOM   18315 C  CE    . LYS A 1 4036 ? 148.540 128.911 165.605 1.00 49.24  ? 4036 LYS A CE    1 
ATOM   18316 N  NZ    . LYS A 1 4036 ? 149.779 128.736 164.798 1.00 45.96  ? 4036 LYS A NZ    1 
ATOM   18317 N  N     . PRO A 1 4037 ? 146.284 134.181 163.908 1.00 36.51  ? 4037 PRO A N     1 
ATOM   18318 C  CA    . PRO A 1 4037 ? 145.562 135.422 163.578 1.00 37.11  ? 4037 PRO A CA    1 
ATOM   18319 C  C     . PRO A 1 4037 ? 145.869 136.574 164.518 1.00 43.04  ? 4037 PRO A C     1 
ATOM   18320 O  O     . PRO A 1 4037 ? 145.871 137.734 164.087 1.00 44.78  ? 4037 PRO A O     1 
ATOM   18321 C  CB    . PRO A 1 4037 ? 144.087 135.000 163.658 1.00 37.12  ? 4037 PRO A CB    1 
ATOM   18322 C  CG    . PRO A 1 4037 ? 144.082 133.724 164.441 1.00 42.42  ? 4037 PRO A CG    1 
ATOM   18323 C  CD    . PRO A 1 4037 ? 145.368 133.048 164.111 1.00 40.90  ? 4037 PRO A CD    1 
ATOM   18324 N  N     . ASN A 1 4038 ? 146.133 136.291 165.792 1.00 45.31  ? 4038 ASN A N     1 
ATOM   18325 C  CA    . ASN A 1 4038 ? 146.442 137.337 166.758 1.00 40.20  ? 4038 ASN A CA    1 
ATOM   18326 C  C     . ASN A 1 4038 ? 147.903 137.764 166.723 1.00 39.50  ? 4038 ASN A C     1 
ATOM   18327 O  O     . ASN A 1 4038 ? 148.285 138.666 167.476 1.00 38.41  ? 4038 ASN A O     1 
ATOM   18328 C  CB    . ASN A 1 4038 ? 146.071 136.877 168.171 1.00 44.90  ? 4038 ASN A CB    1 
ATOM   18329 C  CG    . ASN A 1 4038 ? 146.492 135.448 168.448 1.00 60.59  ? 4038 ASN A CG    1 
ATOM   18330 O  OD1   . ASN A 1 4038 ? 147.667 135.101 168.330 1.00 54.18  ? 4038 ASN A OD1   1 
ATOM   18331 N  ND2   . ASN A 1 4038 ? 145.531 134.610 168.817 1.00 63.66  ? 4038 ASN A ND2   1 
ATOM   18332 N  N     . THR A 1 4039 ? 148.723 137.142 165.877 1.00 40.99  ? 4039 THR A N     1 
ATOM   18333 C  CA    . THR A 1 4039 ? 150.121 137.521 165.746 1.00 29.18  ? 4039 THR A CA    1 
ATOM   18334 C  C     . THR A 1 4039 ? 150.271 138.449 164.551 1.00 27.02  ? 4039 THR A C     1 
ATOM   18335 O  O     . THR A 1 4039 ? 150.100 138.000 163.407 1.00 33.08  ? 4039 THR A O     1 
ATOM   18336 C  CB    . THR A 1 4039 ? 151.000 136.284 165.573 1.00 26.24  ? 4039 THR A CB    1 
ATOM   18337 O  OG1   . THR A 1 4039 ? 151.006 135.526 166.789 1.00 38.88  ? 4039 THR A OG1   1 
ATOM   18338 C  CG2   . THR A 1 4039 ? 152.425 136.682 165.226 1.00 20.40  ? 4039 THR A CG2   1 
ATOM   18339 N  N     . PRO A 1 4040 ? 150.571 139.730 164.753 1.00 20.38  ? 4040 PRO A N     1 
ATOM   18340 C  CA    . PRO A 1 4040 ? 150.751 140.631 163.611 1.00 18.66  ? 4040 PRO A CA    1 
ATOM   18341 C  C     . PRO A 1 4040 ? 151.987 140.273 162.803 1.00 20.03  ? 4040 PRO A C     1 
ATOM   18342 O  O     . PRO A 1 4040 ? 152.962 139.725 163.320 1.00 22.61  ? 4040 PRO A O     1 
ATOM   18343 C  CB    . PRO A 1 4040 ? 150.894 142.010 164.265 1.00 13.61  ? 4040 PRO A CB    1 
ATOM   18344 C  CG    . PRO A 1 4040 ? 151.370 141.723 165.647 1.00 15.35  ? 4040 PRO A CG    1 
ATOM   18345 C  CD    . PRO A 1 4040 ? 150.728 140.426 166.040 1.00 17.74  ? 4040 PRO A CD    1 
ATOM   18346 N  N     . VAL A 1 4041 ? 151.933 140.588 161.514 1.00 17.66  ? 4041 VAL A N     1 
ATOM   18347 C  CA    . VAL A 1 4041 ? 153.043 140.354 160.599 1.00 13.85  ? 4041 VAL A CA    1 
ATOM   18348 C  C     . VAL A 1 4041 ? 153.791 141.671 160.445 1.00 16.09  ? 4041 VAL A C     1 
ATOM   18349 O  O     . VAL A 1 4041 ? 153.330 142.582 159.750 1.00 22.92  ? 4041 VAL A O     1 
ATOM   18350 C  CB    . VAL A 1 4041 ? 152.558 139.822 159.245 1.00 14.41  ? 4041 VAL A CB    1 
ATOM   18351 C  CG1   . VAL A 1 4041 ? 153.742 139.485 158.355 1.00 16.89  ? 4041 VAL A CG1   1 
ATOM   18352 C  CG2   . VAL A 1 4041 ? 151.667 138.606 159.442 1.00 15.85  ? 4041 VAL A CG2   1 
ATOM   18353 N  N     . LEU A 1 4042 ? 154.950 141.774 161.091 1.00 14.24  ? 4042 LEU A N     1 
ATOM   18354 C  CA    . LEU A 1 4042 ? 155.760 142.986 161.052 1.00 13.28  ? 4042 LEU A CA    1 
ATOM   18355 C  C     . LEU A 1 4042 ? 156.624 142.950 159.798 1.00 16.22  ? 4042 LEU A C     1 
ATOM   18356 O  O     . LEU A 1 4042 ? 157.555 142.146 159.698 1.00 20.68  ? 4042 LEU A O     1 
ATOM   18357 C  CB    . LEU A 1 4042 ? 156.616 143.103 162.309 1.00 14.54  ? 4042 LEU A CB    1 
ATOM   18358 C  CG    . LEU A 1 4042 ? 155.903 142.847 163.637 1.00 15.42  ? 4042 LEU A CG    1 
ATOM   18359 C  CD1   . LEU A 1 4042 ? 156.857 143.051 164.795 1.00 17.48  ? 4042 LEU A CD1   1 
ATOM   18360 C  CD2   . LEU A 1 4042 ? 154.694 143.750 163.779 1.00 14.29  ? 4042 LEU A CD2   1 
ATOM   18361 N  N     . MET A 1 4043 ? 156.314 143.820 158.843 1.00 17.77  ? 4043 MET A N     1 
ATOM   18362 C  CA    . MET A 1 4043 ? 157.014 143.850 157.560 1.00 16.15  ? 4043 MET A CA    1 
ATOM   18363 C  C     . MET A 1 4043 ? 158.093 144.932 157.571 1.00 19.57  ? 4043 MET A C     1 
ATOM   18364 O  O     . MET A 1 4043 ? 158.047 145.911 156.826 1.00 23.76  ? 4043 MET A O     1 
ATOM   18365 C  CB    . MET A 1 4043 ? 156.015 144.065 156.427 1.00 16.63  ? 4043 MET A CB    1 
ATOM   18366 C  CG    . MET A 1 4043 ? 154.865 143.067 156.435 1.00 22.15  ? 4043 MET A CG    1 
ATOM   18367 S  SD    . MET A 1 4043 ? 155.224 141.509 155.604 1.00 54.73  ? 4043 MET A SD    1 
ATOM   18368 C  CE    . MET A 1 4043 ? 155.510 142.078 153.934 1.00 34.16  ? 4043 MET A CE    1 
ATOM   18369 N  N     . CYS A 1 4044 ? 159.078 144.738 158.445 1.00 19.70  ? 4044 CYS A N     1 
ATOM   18370 C  CA    . CYS A 1 4044 ? 160.149 145.712 158.603 1.00 17.94  ? 4044 CYS A CA    1 
ATOM   18371 C  C     . CYS A 1 4044 ? 161.027 145.756 157.359 1.00 18.34  ? 4044 CYS A C     1 
ATOM   18372 O  O     . CYS A 1 4044 ? 161.343 144.724 156.764 1.00 23.61  ? 4044 CYS A O     1 
ATOM   18373 C  CB    . CYS A 1 4044 ? 160.995 145.375 159.831 1.00 16.93  ? 4044 CYS A CB    1 
ATOM   18374 S  SG    . CYS A 1 4044 ? 160.039 145.060 161.332 1.00 31.45  ? 4044 CYS A SG    1 
ATOM   18375 N  N     . SER A 1 4045 ? 161.421 146.963 156.964 1.00 20.30  ? 4045 SER A N     1 
ATOM   18376 C  CA    . SER A 1 4045 ? 162.220 147.147 155.764 1.00 20.88  ? 4045 SER A CA    1 
ATOM   18377 C  C     . SER A 1 4045 ? 163.267 148.225 155.997 1.00 28.56  ? 4045 SER A C     1 
ATOM   18378 O  O     . SER A 1 4045 ? 163.068 149.148 156.792 1.00 33.46  ? 4045 SER A O     1 
ATOM   18379 C  CB    . SER A 1 4045 ? 161.347 147.521 154.560 1.00 24.35  ? 4045 SER A CB    1 
ATOM   18380 O  OG    . SER A 1 4045 ? 160.613 148.706 154.813 1.00 26.95  ? 4045 SER A OG    1 
ATOM   18381 N  N     . VAL A 1 4046 ? 164.386 148.094 155.294 1.00 31.30  ? 4046 VAL A N     1 
ATOM   18382 C  CA    . VAL A 1 4046 ? 165.449 149.095 155.299 1.00 33.46  ? 4046 VAL A CA    1 
ATOM   18383 C  C     . VAL A 1 4046 ? 164.957 150.295 154.497 1.00 44.05  ? 4046 VAL A C     1 
ATOM   18384 O  O     . VAL A 1 4046 ? 164.021 150.149 153.697 1.00 43.99  ? 4046 VAL A O     1 
ATOM   18385 C  CB    . VAL A 1 4046 ? 166.753 148.518 154.724 1.00 28.69  ? 4046 VAL A CB    1 
ATOM   18386 C  CG1   . VAL A 1 4046 ? 167.233 147.351 155.571 1.00 23.76  ? 4046 VAL A CG1   1 
ATOM   18387 C  CG2   . VAL A 1 4046 ? 166.550 148.091 153.282 1.00 31.99  ? 4046 VAL A CG2   1 
ATOM   18388 N  N     . PRO A 1 4047 ? 165.522 151.491 154.679 1.00 45.22  ? 4047 PRO A N     1 
ATOM   18389 C  CA    . PRO A 1 4047 ? 165.072 152.635 153.877 1.00 40.85  ? 4047 PRO A CA    1 
ATOM   18390 C  C     . PRO A 1 4047 ? 165.298 152.396 152.391 1.00 45.57  ? 4047 PRO A C     1 
ATOM   18391 O  O     . PRO A 1 4047 ? 166.306 151.817 151.980 1.00 44.63  ? 4047 PRO A O     1 
ATOM   18392 C  CB    . PRO A 1 4047 ? 165.920 153.796 154.406 1.00 42.10  ? 4047 PRO A CB    1 
ATOM   18393 C  CG    . PRO A 1 4047 ? 167.135 153.152 154.961 1.00 38.97  ? 4047 PRO A CG    1 
ATOM   18394 C  CD    . PRO A 1 4047 ? 166.672 151.842 155.532 1.00 43.90  ? 4047 PRO A CD    1 
ATOM   18395 N  N     . GLY A 1 4048 ? 164.342 152.853 151.585 1.00 48.71  ? 4048 GLY A N     1 
ATOM   18396 C  CA    . GLY A 1 4048 ? 164.342 152.594 150.163 1.00 46.67  ? 4048 GLY A CA    1 
ATOM   18397 C  C     . GLY A 1 4048 ? 163.593 151.348 149.744 1.00 39.74  ? 4048 GLY A C     1 
ATOM   18398 O  O     . GLY A 1 4048 ? 163.414 151.129 148.539 1.00 40.09  ? 4048 GLY A O     1 
ATOM   18399 N  N     . TYR A 1 4049 ? 163.152 150.527 150.693 1.00 40.58  ? 4049 TYR A N     1 
ATOM   18400 C  CA    . TYR A 1 4049 ? 162.397 149.314 150.410 1.00 47.13  ? 4049 TYR A CA    1 
ATOM   18401 C  C     . TYR A 1 4049 ? 161.030 149.407 151.070 1.00 51.92  ? 4049 TYR A C     1 
ATOM   18402 O  O     . TYR A 1 4049 ? 160.928 149.761 152.250 1.00 55.43  ? 4049 TYR A O     1 
ATOM   18403 C  CB    . TYR A 1 4049 ? 163.144 148.072 150.903 1.00 36.95  ? 4049 TYR A CB    1 
ATOM   18404 C  CG    . TYR A 1 4049 ? 163.924 147.368 149.818 1.00 41.88  ? 4049 TYR A CG    1 
ATOM   18405 C  CD1   . TYR A 1 4049 ? 163.344 146.354 149.068 1.00 40.41  ? 4049 TYR A CD1   1 
ATOM   18406 C  CD2   . TYR A 1 4049 ? 165.233 147.727 149.532 1.00 40.36  ? 4049 TYR A CD2   1 
ATOM   18407 C  CE1   . TYR A 1 4049 ? 164.050 145.710 148.072 1.00 44.77  ? 4049 TYR A CE1   1 
ATOM   18408 C  CE2   . TYR A 1 4049 ? 165.946 147.091 148.535 1.00 36.46  ? 4049 TYR A CE2   1 
ATOM   18409 C  CZ    . TYR A 1 4049 ? 165.350 146.082 147.810 1.00 46.19  ? 4049 TYR A CZ    1 
ATOM   18410 O  OH    . TYR A 1 4049 ? 166.057 145.444 146.817 1.00 51.06  ? 4049 TYR A OH    1 
ATOM   18411 N  N     . ASP A 1 4050 ? 159.986 149.094 150.308 1.00 43.00  ? 4050 ASP A N     1 
ATOM   18412 C  CA    . ASP A 1 4050 ? 158.613 149.114 150.797 1.00 42.06  ? 4050 ASP A CA    1 
ATOM   18413 C  C     . ASP A 1 4050 ? 158.010 147.732 150.601 1.00 44.81  ? 4050 ASP A C     1 
ATOM   18414 O  O     . ASP A 1 4050 ? 157.976 147.220 149.477 1.00 45.65  ? 4050 ASP A O     1 
ATOM   18415 C  CB    . ASP A 1 4050 ? 157.786 150.176 150.068 1.00 45.26  ? 4050 ASP A CB    1 
ATOM   18416 C  CG    . ASP A 1 4050 ? 156.345 150.212 150.532 1.00 46.09  ? 4050 ASP A CG    1 
ATOM   18417 O  OD1   . ASP A 1 4050 ? 156.114 150.380 151.748 1.00 45.53  ? 4050 ASP A OD1   1 
ATOM   18418 O  OD2   . ASP A 1 4050 ? 155.442 150.077 149.679 1.00 41.43  ? 4050 ASP A OD2   1 
ATOM   18419 N  N     . ALA A 1 4051 ? 157.539 147.132 151.692 1.00 37.77  ? 4051 ALA A N     1 
ATOM   18420 C  CA    . ALA A 1 4051 ? 156.954 145.801 151.659 1.00 31.72  ? 4051 ALA A CA    1 
ATOM   18421 C  C     . ALA A 1 4051 ? 155.436 145.819 151.570 1.00 35.02  ? 4051 ALA A C     1 
ATOM   18422 O  O     . ALA A 1 4051 ? 154.816 144.751 151.581 1.00 42.72  ? 4051 ALA A O     1 
ATOM   18423 C  CB    . ALA A 1 4051 ? 157.389 145.006 152.893 1.00 31.76  ? 4051 ALA A CB    1 
ATOM   18424 N  N     . SER A 1 4052 ? 154.822 147.002 151.488 1.00 31.45  ? 4052 SER A N     1 
ATOM   18425 C  CA    . SER A 1 4052 ? 153.370 147.075 151.359 1.00 26.92  ? 4052 SER A CA    1 
ATOM   18426 C  C     . SER A 1 4052 ? 152.904 146.480 150.036 1.00 31.90  ? 4052 SER A C     1 
ATOM   18427 O  O     . SER A 1 4052 ? 151.873 145.799 149.981 1.00 33.85  ? 4052 SER A O     1 
ATOM   18428 C  CB    . SER A 1 4052 ? 152.904 148.524 151.492 1.00 27.80  ? 4052 SER A CB    1 
ATOM   18429 O  OG    . SER A 1 4052 ? 152.912 149.179 150.236 1.00 38.83  ? 4052 SER A OG    1 
ATOM   18430 N  N     . GLY A 1 4053 ? 153.654 146.729 148.960 1.00 37.33  ? 4053 GLY A N     1 
ATOM   18431 C  CA    . GLY A 1 4053 ? 153.287 146.170 147.669 1.00 38.02  ? 4053 GLY A CA    1 
ATOM   18432 C  C     . GLY A 1 4053 ? 153.276 144.654 147.673 1.00 39.14  ? 4053 GLY A C     1 
ATOM   18433 O  O     . GLY A 1 4053 ? 152.450 144.029 147.005 1.00 42.69  ? 4053 GLY A O     1 
ATOM   18434 N  N     . HIS A 1 4054 ? 154.192 144.043 148.429 1.00 38.40  ? 4054 HIS A N     1 
ATOM   18435 C  CA    . HIS A 1 4054 ? 154.185 142.591 148.565 1.00 36.71  ? 4054 HIS A CA    1 
ATOM   18436 C  C     . HIS A 1 4054 ? 152.886 142.107 149.194 1.00 37.03  ? 4054 HIS A C     1 
ATOM   18437 O  O     . HIS A 1 4054 ? 152.296 141.122 148.739 1.00 40.75  ? 4054 HIS A O     1 
ATOM   18438 C  CB    . HIS A 1 4054 ? 155.382 142.125 149.395 1.00 37.44  ? 4054 HIS A CB    1 
ATOM   18439 C  CG    . HIS A 1 4054 ? 156.713 142.503 148.820 1.00 42.80  ? 4054 HIS A CG    1 
ATOM   18440 N  ND1   . HIS A 1 4054 ? 157.858 141.777 149.068 1.00 45.96  ? 4054 HIS A ND1   1 
ATOM   18441 C  CD2   . HIS A 1 4054 ? 157.084 143.526 148.014 1.00 48.52  ? 4054 HIS A CD2   1 
ATOM   18442 C  CE1   . HIS A 1 4054 ? 158.877 142.336 148.439 1.00 51.19  ? 4054 HIS A CE1   1 
ATOM   18443 N  NE2   . HIS A 1 4054 ? 158.434 143.399 147.792 1.00 57.12  ? 4054 HIS A NE2   1 
ATOM   18444 N  N     . VAL A 1 4055 ? 152.418 142.797 150.238 1.00 38.06  ? 4055 VAL A N     1 
ATOM   18445 C  CA    . VAL A 1 4055 ? 151.173 142.405 150.890 1.00 35.25  ? 4055 VAL A CA    1 
ATOM   18446 C  C     . VAL A 1 4055 ? 149.990 142.598 149.951 1.00 36.69  ? 4055 VAL A C     1 
ATOM   18447 O  O     . VAL A 1 4055 ? 149.076 141.766 149.906 1.00 38.31  ? 4055 VAL A O     1 
ATOM   18448 C  CB    . VAL A 1 4055 ? 150.983 143.188 152.201 1.00 29.32  ? 4055 VAL A CB    1 
ATOM   18449 C  CG1   . VAL A 1 4055 ? 149.841 142.596 153.008 1.00 25.86  ? 4055 VAL A CG1   1 
ATOM   18450 C  CG2   . VAL A 1 4055 ? 152.263 143.188 153.009 1.00 29.61  ? 4055 VAL A CG2   1 
ATOM   18451 N  N     . GLU A 1 4056 ? 149.976 143.701 149.199 1.00 37.01  ? 4056 GLU A N     1 
ATOM   18452 C  CA    . GLU A 1 4056 ? 148.884 143.928 148.255 1.00 42.39  ? 4056 GLU A CA    1 
ATOM   18453 C  C     . GLU A 1 4056 ? 148.850 142.848 147.180 1.00 47.41  ? 4056 GLU A C     1 
ATOM   18454 O  O     . GLU A 1 4056 ? 147.778 142.332 146.839 1.00 54.35  ? 4056 GLU A O     1 
ATOM   18455 C  CB    . GLU A 1 4056 ? 149.008 145.313 147.622 1.00 47.08  ? 4056 GLU A CB    1 
ATOM   18456 C  CG    . GLU A 1 4056 ? 149.152 146.448 148.620 1.00 50.59  ? 4056 GLU A CG    1 
ATOM   18457 C  CD    . GLU A 1 4056 ? 147.833 147.122 148.935 1.00 62.88  ? 4056 GLU A CD    1 
ATOM   18458 O  OE1   . GLU A 1 4056 ? 146.775 146.500 148.700 1.00 63.86  ? 4056 GLU A OE1   1 
ATOM   18459 O  OE2   . GLU A 1 4056 ? 147.853 148.274 149.416 1.00 60.68  ? 4056 GLU A OE2   1 
ATOM   18460 N  N     . ASP A 1 4057 ? 150.017 142.487 146.638 1.00 44.88  ? 4057 ASP A N     1 
ATOM   18461 C  CA    . ASP A 1 4057 ? 150.070 141.435 145.629 1.00 45.64  ? 4057 ASP A CA    1 
ATOM   18462 C  C     . ASP A 1 4057 ? 149.661 140.087 146.210 1.00 45.81  ? 4057 ASP A C     1 
ATOM   18463 O  O     . ASP A 1 4057 ? 148.978 139.301 145.545 1.00 52.91  ? 4057 ASP A O     1 
ATOM   18464 C  CB    . ASP A 1 4057 ? 151.471 141.359 145.023 1.00 51.84  ? 4057 ASP A CB    1 
ATOM   18465 C  CG    . ASP A 1 4057 ? 151.859 142.630 144.293 1.00 58.56  ? 4057 ASP A CG    1 
ATOM   18466 O  OD1   . ASP A 1 4057 ? 150.956 143.314 143.766 1.00 56.44  ? 4057 ASP A OD1   1 
ATOM   18467 O  OD2   . ASP A 1 4057 ? 153.066 142.946 144.246 1.00 59.13  ? 4057 ASP A OD2   1 
ATOM   18468 N  N     . LEU A 1 4058 ? 150.077 139.798 147.446 1.00 43.98  ? 4058 LEU A N     1 
ATOM   18469 C  CA    . LEU A 1 4058 ? 149.684 138.549 148.090 1.00 42.56  ? 4058 LEU A CA    1 
ATOM   18470 C  C     . LEU A 1 4058 ? 148.176 138.483 148.295 1.00 44.23  ? 4058 LEU A C     1 
ATOM   18471 O  O     . LEU A 1 4058 ? 147.556 137.439 148.067 1.00 52.47  ? 4058 LEU A O     1 
ATOM   18472 C  CB    . LEU A 1 4058 ? 150.415 138.402 149.424 1.00 40.41  ? 4058 LEU A CB    1 
ATOM   18473 C  CG    . LEU A 1 4058 ? 149.986 137.250 150.333 1.00 39.69  ? 4058 LEU A CG    1 
ATOM   18474 C  CD1   . LEU A 1 4058 ? 150.217 135.914 149.650 1.00 44.26  ? 4058 LEU A CD1   1 
ATOM   18475 C  CD2   . LEU A 1 4058 ? 150.726 137.313 151.659 1.00 33.36  ? 4058 LEU A CD2   1 
ATOM   18476 N  N     . ALA A 1 4059 ? 147.570 139.589 148.733 1.00 43.04  ? 4059 ALA A N     1 
ATOM   18477 C  CA    . ALA A 1 4059 ? 146.124 139.617 148.919 1.00 45.84  ? 4059 ALA A CA    1 
ATOM   18478 C  C     . ALA A 1 4059 ? 145.391 139.472 147.592 1.00 54.66  ? 4059 ALA A C     1 
ATOM   18479 O  O     . ALA A 1 4059 ? 144.372 138.775 147.513 1.00 58.75  ? 4059 ALA A O     1 
ATOM   18480 C  CB    . ALA A 1 4059 ? 145.711 140.908 149.624 1.00 40.05  ? 4059 ALA A CB    1 
ATOM   18481 N  N     . ALA A 1 4060 ? 145.887 140.129 146.540 1.00 52.28  ? 4060 ALA A N     1 
ATOM   18482 C  CA    . ALA A 1 4060 ? 145.257 140.006 145.230 1.00 52.92  ? 4060 ALA A CA    1 
ATOM   18483 C  C     . ALA A 1 4060 ? 145.360 138.582 144.697 1.00 58.28  ? 4060 ALA A C     1 
ATOM   18484 O  O     . ALA A 1 4060 ? 144.407 138.062 144.104 1.00 64.13  ? 4060 ALA A O     1 
ATOM   18485 C  CB    . ALA A 1 4060 ? 145.886 140.995 144.249 1.00 49.10  ? 4060 ALA A CB    1 
ATOM   18486 N  N     . GLU A 1 4061 ? 146.514 137.938 144.892 1.00 56.16  ? 4061 GLU A N     1 
ATOM   18487 C  CA    . GLU A 1 4061 ? 146.698 136.572 144.410 1.00 58.84  ? 4061 GLU A CA    1 
ATOM   18488 C  C     . GLU A 1 4061 ? 145.747 135.605 145.105 1.00 62.31  ? 4061 GLU A C     1 
ATOM   18489 O  O     . GLU A 1 4061 ? 145.188 134.706 144.467 1.00 67.82  ? 4061 GLU A O     1 
ATOM   18490 C  CB    . GLU A 1 4061 ? 148.152 136.142 144.609 1.00 57.41  ? 4061 GLU A CB    1 
ATOM   18491 C  CG    . GLU A 1 4061 ? 148.545 134.866 143.875 1.00 70.75  ? 4061 GLU A CG    1 
ATOM   18492 C  CD    . GLU A 1 4061 ? 148.200 133.608 144.650 1.00 81.89  ? 4061 GLU A CD    1 
ATOM   18493 O  OE1   . GLU A 1 4061 ? 147.998 133.701 145.879 1.00 76.07  ? 4061 GLU A OE1   1 
ATOM   18494 O  OE2   . GLU A 1 4061 ? 148.129 132.527 144.028 1.00 84.48  ? 4061 GLU A OE2   1 
ATOM   18495 N  N     . GLN A 1 4062 ? 145.553 135.772 146.411 1.00 60.19  ? 4062 GLN A N     1 
ATOM   18496 C  CA    . GLN A 1 4062 ? 144.678 134.896 147.179 1.00 60.03  ? 4062 GLN A CA    1 
ATOM   18497 C  C     . GLN A 1 4062 ? 143.209 135.282 147.076 1.00 62.76  ? 4062 GLN A C     1 
ATOM   18498 O  O     . GLN A 1 4062 ? 142.366 134.584 147.651 1.00 65.38  ? 4062 GLN A O     1 
ATOM   18499 C  CB    . GLN A 1 4062 ? 145.099 134.889 148.651 1.00 58.79  ? 4062 GLN A CB    1 
ATOM   18500 C  CG    . GLN A 1 4062 ? 146.436 134.224 148.920 1.00 58.45  ? 4062 GLN A CG    1 
ATOM   18501 C  CD    . GLN A 1 4062 ? 146.472 133.525 150.264 1.00 65.22  ? 4062 GLN A CD    1 
ATOM   18502 O  OE1   . GLN A 1 4062 ? 145.431 133.205 150.837 1.00 68.04  ? 4062 GLN A OE1   1 
ATOM   18503 N  NE2   . GLN A 1 4062 ? 147.673 133.288 150.776 1.00 63.39  ? 4062 GLN A NE2   1 
ATOM   18504 N  N     . ASN A 1 4063 ? 142.889 136.367 146.368 1.00 61.62  ? 4063 ASN A N     1 
ATOM   18505 C  CA    . ASN A 1 4063 ? 141.519 136.874 146.262 1.00 66.53  ? 4063 ASN A CA    1 
ATOM   18506 C  C     . ASN A 1 4063 ? 140.932 137.162 147.642 1.00 69.60  ? 4063 ASN A C     1 
ATOM   18507 O  O     . ASN A 1 4063 ? 139.753 136.916 147.902 1.00 72.59  ? 4063 ASN A O     1 
ATOM   18508 C  CB    . ASN A 1 4063 ? 140.625 135.908 145.480 1.00 67.91  ? 4063 ASN A CB    1 
ATOM   18509 C  CG    . ASN A 1 4063 ? 141.168 135.602 144.099 1.00 69.92  ? 4063 ASN A CG    1 
ATOM   18510 O  OD1   . ASN A 1 4063 ? 141.455 136.508 143.317 1.00 68.48  ? 4063 ASN A OD1   1 
ATOM   18511 N  ND2   . ASN A 1 4063 ? 141.312 134.318 143.792 1.00 67.42  ? 4063 ASN A ND2   1 
ATOM   18512 N  N     . THR A 1 4064 ? 141.766 137.688 148.534 1.00 62.47  ? 4064 THR A N     1 
ATOM   18513 C  CA    . THR A 1 4064 ? 141.365 138.039 149.888 1.00 56.45  ? 4064 THR A CA    1 
ATOM   18514 C  C     . THR A 1 4064 ? 141.287 139.553 150.008 1.00 58.15  ? 4064 THR A C     1 
ATOM   18515 O  O     . THR A 1 4064 ? 142.234 140.258 149.641 1.00 61.17  ? 4064 THR A O     1 
ATOM   18516 C  CB    . THR A 1 4064 ? 142.348 137.478 150.919 1.00 49.23  ? 4064 THR A CB    1 
ATOM   18517 O  OG1   . THR A 1 4064 ? 142.615 136.101 150.629 1.00 58.48  ? 4064 THR A OG1   1 
ATOM   18518 C  CG2   . THR A 1 4064 ? 141.771 137.592 152.320 1.00 43.80  ? 4064 THR A CG2   1 
ATOM   18519 N  N     . GLN A 1 4065 ? 140.163 140.049 150.515 1.00 53.78  ? 4065 GLN A N     1 
ATOM   18520 C  CA    . GLN A 1 4065 ? 139.996 141.484 150.691 1.00 55.53  ? 4065 GLN A CA    1 
ATOM   18521 C  C     . GLN A 1 4065 ? 140.924 141.994 151.785 1.00 45.68  ? 4065 GLN A C     1 
ATOM   18522 O  O     . GLN A 1 4065 ? 141.033 141.398 152.859 1.00 42.83  ? 4065 GLN A O     1 
ATOM   18523 C  CB    . GLN A 1 4065 ? 138.543 141.812 151.032 1.00 59.91  ? 4065 GLN A CB    1 
ATOM   18524 C  CG    . GLN A 1 4065 ? 137.595 141.771 149.841 1.00 66.33  ? 4065 GLN A CG    1 
ATOM   18525 C  CD    . GLN A 1 4065 ? 138.139 142.500 148.625 1.00 67.42  ? 4065 GLN A CD    1 
ATOM   18526 O  OE1   . GLN A 1 4065 ? 138.159 141.957 147.520 1.00 68.14  ? 4065 GLN A OE1   1 
ATOM   18527 N  NE2   . GLN A 1 4065 ? 138.567 143.743 148.819 1.00 60.43  ? 4065 GLN A NE2   1 
ATOM   18528 N  N     . ILE A 1 4066 ? 141.597 143.107 151.505 1.00 40.66  ? 4066 ILE A N     1 
ATOM   18529 C  CA    . ILE A 1 4066 ? 142.556 143.702 152.426 1.00 35.53  ? 4066 ILE A CA    1 
ATOM   18530 C  C     . ILE A 1 4066 ? 142.252 145.187 152.558 1.00 39.29  ? 4066 ILE A C     1 
ATOM   18531 O  O     . ILE A 1 4066 ? 141.911 145.853 151.573 1.00 48.45  ? 4066 ILE A O     1 
ATOM   18532 C  CB    . ILE A 1 4066 ? 144.011 143.474 151.962 1.00 32.73  ? 4066 ILE A CB    1 
ATOM   18533 C  CG1   . ILE A 1 4066 ? 144.999 144.049 152.979 1.00 27.75  ? 4066 ILE A CG1   1 
ATOM   18534 C  CG2   . ILE A 1 4066 ? 144.243 144.072 150.582 1.00 39.97  ? 4066 ILE A CG2   1 
ATOM   18535 C  CD1   . ILE A 1 4066 ? 146.444 143.907 152.573 1.00 29.64  ? 4066 ILE A CD1   1 
ATOM   18536 N  N     . THR A 1 4067 ? 142.351 145.700 153.780 1.00 33.39  ? 4067 THR A N     1 
ATOM   18537 C  CA    . THR A 1 4067 ? 142.161 147.117 154.063 1.00 28.62  ? 4067 THR A CA    1 
ATOM   18538 C  C     . THR A 1 4067 ? 143.521 147.737 154.353 1.00 26.84  ? 4067 THR A C     1 
ATOM   18539 O  O     . THR A 1 4067 ? 144.209 147.319 155.290 1.00 30.08  ? 4067 THR A O     1 
ATOM   18540 C  CB    . THR A 1 4067 ? 141.213 147.321 155.243 1.00 33.43  ? 4067 THR A CB    1 
ATOM   18541 O  OG1   . THR A 1 4067 ? 139.902 146.864 154.889 1.00 39.61  ? 4067 THR A OG1   1 
ATOM   18542 C  CG2   . THR A 1 4067 ? 141.142 148.790 155.617 1.00 30.08  ? 4067 THR A CG2   1 
ATOM   18543 N  N     . SER A 1 4068 ? 143.902 148.727 153.552 1.00 26.58  ? 4068 SER A N     1 
ATOM   18544 C  CA    . SER A 1 4068 ? 145.191 149.393 153.675 1.00 22.16  ? 4068 SER A CA    1 
ATOM   18545 C  C     . SER A 1 4068 ? 144.990 150.766 154.299 1.00 26.33  ? 4068 SER A C     1 
ATOM   18546 O  O     . SER A 1 4068 ? 144.166 151.554 153.824 1.00 32.34  ? 4068 SER A O     1 
ATOM   18547 C  CB    . SER A 1 4068 ? 145.870 149.523 152.311 1.00 27.26  ? 4068 SER A CB    1 
ATOM   18548 O  OG    . SER A 1 4068 ? 145.849 148.290 151.613 1.00 35.35  ? 4068 SER A OG    1 
ATOM   18549 N  N     . ILE A 1 4069 ? 145.742 151.046 155.361 1.00 20.95  ? 4069 ILE A N     1 
ATOM   18550 C  CA    . ILE A 1 4069 ? 145.620 152.288 156.112 1.00 21.68  ? 4069 ILE A CA    1 
ATOM   18551 C  C     . ILE A 1 4069 ? 147.014 152.851 156.342 1.00 21.76  ? 4069 ILE A C     1 
ATOM   18552 O  O     . ILE A 1 4069 ? 147.926 152.117 156.737 1.00 22.65  ? 4069 ILE A O     1 
ATOM   18553 C  CB    . ILE A 1 4069 ? 144.894 152.072 157.453 1.00 21.39  ? 4069 ILE A CB    1 
ATOM   18554 C  CG1   . ILE A 1 4069 ? 143.461 151.603 157.205 1.00 23.83  ? 4069 ILE A CG1   1 
ATOM   18555 C  CG2   . ILE A 1 4069 ? 144.900 153.346 158.281 1.00 23.22  ? 4069 ILE A CG2   1 
ATOM   18556 C  CD1   . ILE A 1 4069 ? 142.959 150.619 158.224 1.00 25.98  ? 4069 ILE A CD1   1 
ATOM   18557 N  N     . ALA A 1 4070 ? 147.179 154.146 156.093 1.00 22.01  ? 4070 ALA A N     1 
ATOM   18558 C  CA    . ALA A 1 4070 ? 148.440 154.836 156.319 1.00 18.67  ? 4070 ALA A CA    1 
ATOM   18559 C  C     . ALA A 1 4070 ? 148.386 155.530 157.674 1.00 25.20  ? 4070 ALA A C     1 
ATOM   18560 O  O     . ALA A 1 4070 ? 147.499 156.354 157.920 1.00 35.49  ? 4070 ALA A O     1 
ATOM   18561 C  CB    . ALA A 1 4070 ? 148.719 155.842 155.204 1.00 17.08  ? 4070 ALA A CB    1 
ATOM   18562 N  N     . ILE A 1 4071 ? 149.333 155.199 158.542 1.00 21.07  ? 4071 ILE A N     1 
ATOM   18563 C  CA    . ILE A 1 4071 ? 149.331 155.686 159.916 1.00 25.58  ? 4071 ILE A CA    1 
ATOM   18564 C  C     . ILE A 1 4071 ? 149.939 157.081 159.965 1.00 29.21  ? 4071 ILE A C     1 
ATOM   18565 O  O     . ILE A 1 4071 ? 150.889 157.388 159.234 1.00 27.51  ? 4071 ILE A O     1 
ATOM   18566 C  CB    . ILE A 1 4071 ? 150.089 154.700 160.825 1.00 22.07  ? 4071 ILE A CB    1 
ATOM   18567 C  CG1   . ILE A 1 4071 ? 149.344 153.367 160.890 1.00 18.10  ? 4071 ILE A CG1   1 
ATOM   18568 C  CG2   . ILE A 1 4071 ? 150.278 155.266 162.224 1.00 25.99  ? 4071 ILE A CG2   1 
ATOM   18569 C  CD1   . ILE A 1 4071 ? 147.908 153.494 161.343 1.00 17.45  ? 4071 ILE A CD1   1 
ATOM   18570 N  N     . GLY A 1 4072 ? 149.393 157.933 160.832 1.00 30.35  ? 4072 GLY A N     1 
ATOM   18571 C  CA    . GLY A 1 4072 ? 149.923 159.270 161.005 1.00 28.58  ? 4072 GLY A CA    1 
ATOM   18572 C  C     . GLY A 1 4072 ? 148.895 160.335 161.327 1.00 34.26  ? 4072 GLY A C     1 
ATOM   18573 O  O     . GLY A 1 4072 ? 149.248 161.408 161.824 1.00 37.71  ? 4072 GLY A O     1 
ATOM   18574 N  N     . SER A 1 4073 ? 147.623 160.057 161.058 1.00 38.54  ? 4073 SER A N     1 
ATOM   18575 C  CA    . SER A 1 4073 ? 146.548 161.002 161.313 1.00 37.26  ? 4073 SER A CA    1 
ATOM   18576 C  C     . SER A 1 4073 ? 145.549 160.407 162.297 1.00 41.69  ? 4073 SER A C     1 
ATOM   18577 O  O     . SER A 1 4073 ? 145.429 159.186 162.432 1.00 46.08  ? 4073 SER A O     1 
ATOM   18578 C  CB    . SER A 1 4073 ? 145.835 161.397 160.014 1.00 35.38  ? 4073 SER A CB    1 
ATOM   18579 O  OG    . SER A 1 4073 ? 145.335 160.255 159.339 1.00 37.01  ? 4073 SER A OG    1 
ATOM   18580 N  N     . ALA A 1 4074 ? 144.835 161.293 162.998 1.00 37.45  ? 4074 ALA A N     1 
ATOM   18581 C  CA    . ALA A 1 4074 ? 143.820 160.844 163.946 1.00 37.86  ? 4074 ALA A CA    1 
ATOM   18582 C  C     . ALA A 1 4074 ? 142.709 160.078 163.240 1.00 40.25  ? 4074 ALA A C     1 
ATOM   18583 O  O     . ALA A 1 4074 ? 142.249 159.037 163.729 1.00 43.09  ? 4074 ALA A O     1 
ATOM   18584 C  CB    . ALA A 1 4074 ? 143.248 162.038 164.709 1.00 34.88  ? 4074 ALA A CB    1 
ATOM   18585 N  N     . GLU A 1 4075 ? 142.262 160.582 162.086 1.00 39.94  ? 4075 GLU A N     1 
ATOM   18586 C  CA    . GLU A 1 4075 ? 141.334 159.817 161.264 1.00 41.39  ? 4075 GLU A CA    1 
ATOM   18587 C  C     . GLU A 1 4075 ? 141.941 158.484 160.856 1.00 42.30  ? 4075 GLU A C     1 
ATOM   18588 O  O     . GLU A 1 4075 ? 141.229 157.479 160.770 1.00 45.78  ? 4075 GLU A O     1 
ATOM   18589 C  CB    . GLU A 1 4075 ? 140.932 160.620 160.027 1.00 47.09  ? 4075 GLU A CB    1 
ATOM   18590 C  CG    . GLU A 1 4075 ? 140.495 162.045 160.321 1.00 57.45  ? 4075 GLU A CG    1 
ATOM   18591 C  CD    . GLU A 1 4075 ? 141.615 163.049 160.137 1.00 56.84  ? 4075 GLU A CD    1 
ATOM   18592 O  OE1   . GLU A 1 4075 ? 142.691 162.655 159.639 1.00 53.92  ? 4075 GLU A OE1   1 
ATOM   18593 O  OE2   . GLU A 1 4075 ? 141.421 164.231 160.489 1.00 56.37  ? 4075 GLU A OE2   1 
ATOM   18594 N  N     . GLY A 1 4076 ? 143.253 158.455 160.616 1.00 42.18  ? 4076 GLY A N     1 
ATOM   18595 C  CA    . GLY A 1 4076 ? 143.915 157.194 160.331 1.00 37.16  ? 4076 GLY A CA    1 
ATOM   18596 C  C     . GLY A 1 4076 ? 143.833 156.219 161.488 1.00 35.26  ? 4076 GLY A C     1 
ATOM   18597 O  O     . GLY A 1 4076 ? 143.579 155.030 161.290 1.00 36.86  ? 4076 GLY A O     1 
ATOM   18598 N  N     . PHE A 1 4077 ? 144.038 156.708 162.714 1.00 36.68  ? 4077 PHE A N     1 
ATOM   18599 C  CA    . PHE A 1 4077 ? 143.925 155.843 163.886 1.00 33.29  ? 4077 PHE A CA    1 
ATOM   18600 C  C     . PHE A 1 4077 ? 142.505 155.316 164.053 1.00 33.57  ? 4077 PHE A C     1 
ATOM   18601 O  O     . PHE A 1 4077 ? 142.305 154.125 164.327 1.00 34.48  ? 4077 PHE A O     1 
ATOM   18602 C  CB    . PHE A 1 4077 ? 144.361 156.596 165.142 1.00 28.46  ? 4077 PHE A CB    1 
ATOM   18603 C  CG    . PHE A 1 4077 ? 145.812 156.976 165.150 1.00 30.03  ? 4077 PHE A CG    1 
ATOM   18604 C  CD1   . PHE A 1 4077 ? 146.782 156.068 164.765 1.00 29.62  ? 4077 PHE A CD1   1 
ATOM   18605 C  CD2   . PHE A 1 4077 ? 146.206 158.242 165.548 1.00 33.15  ? 4077 PHE A CD2   1 
ATOM   18606 C  CE1   . PHE A 1 4077 ? 148.117 156.417 164.774 1.00 28.05  ? 4077 PHE A CE1   1 
ATOM   18607 C  CE2   . PHE A 1 4077 ? 147.540 158.595 165.559 1.00 32.28  ? 4077 PHE A CE2   1 
ATOM   18608 C  CZ    . PHE A 1 4077 ? 148.497 157.681 165.171 1.00 30.50  ? 4077 PHE A CZ    1 
ATOM   18609 N  N     . ASN A 1 4078 ? 141.506 156.190 163.897 1.00 35.37  ? 4078 ASN A N     1 
ATOM   18610 C  CA    . ASN A 1 4078 ? 140.120 155.751 164.027 1.00 36.09  ? 4078 ASN A CA    1 
ATOM   18611 C  C     . ASN A 1 4078 ? 139.767 154.721 162.962 1.00 35.64  ? 4078 ASN A C     1 
ATOM   18612 O  O     . ASN A 1 4078 ? 139.118 153.707 163.254 1.00 40.96  ? 4078 ASN A O     1 
ATOM   18613 C  CB    . ASN A 1 4078 ? 139.179 156.952 163.943 1.00 36.00  ? 4078 ASN A CB    1 
ATOM   18614 C  CG    . ASN A 1 4078 ? 139.275 157.855 165.156 1.00 49.70  ? 4078 ASN A CG    1 
ATOM   18615 O  OD1   . ASN A 1 4078 ? 139.360 157.383 166.289 1.00 61.03  ? 4078 ASN A OD1   1 
ATOM   18616 N  ND2   . ASN A 1 4078 ? 139.263 159.162 164.923 1.00 46.03  ? 4078 ASN A ND2   1 
ATOM   18617 N  N     . GLN A 1 4079 ? 140.196 154.960 161.721 1.00 34.50  ? 4079 GLN A N     1 
ATOM   18618 C  CA    . GLN A 1 4079 ? 139.908 154.029 160.638 1.00 32.67  ? 4079 GLN A CA    1 
ATOM   18619 C  C     . GLN A 1 4079 ? 140.621 152.701 160.853 1.00 27.63  ? 4079 GLN A C     1 
ATOM   18620 O  O     . GLN A 1 4079 ? 140.063 151.638 160.563 1.00 32.15  ? 4079 GLN A O     1 
ATOM   18621 C  CB    . GLN A 1 4079 ? 140.302 154.661 159.302 1.00 34.82  ? 4079 GLN A CB    1 
ATOM   18622 C  CG    . GLN A 1 4079 ? 140.661 153.682 158.201 1.00 39.69  ? 4079 GLN A CG    1 
ATOM   18623 C  CD    . GLN A 1 4079 ? 141.128 154.385 156.941 1.00 45.09  ? 4079 GLN A CD    1 
ATOM   18624 O  OE1   . GLN A 1 4079 ? 141.361 155.593 156.942 1.00 38.39  ? 4079 GLN A OE1   1 
ATOM   18625 N  NE2   . GLN A 1 4079 ? 141.259 153.632 155.856 1.00 51.13  ? 4079 GLN A NE2   1 
ATOM   18626 N  N     . ALA A 1 4080 ? 141.851 152.738 161.373 1.00 26.05  ? 4080 ALA A N     1 
ATOM   18627 C  CA    . ALA A 1 4080 ? 142.568 151.502 161.668 1.00 26.61  ? 4080 ALA A CA    1 
ATOM   18628 C  C     . ALA A 1 4080 ? 141.866 150.701 162.755 1.00 29.05  ? 4080 ALA A C     1 
ATOM   18629 O  O     . ALA A 1 4080 ? 141.731 149.477 162.644 1.00 29.49  ? 4080 ALA A O     1 
ATOM   18630 C  CB    . ALA A 1 4080 ? 144.007 151.815 162.078 1.00 25.83  ? 4080 ALA A CB    1 
ATOM   18631 N  N     . ASP A 1 4081 ? 141.410 151.375 163.814 1.00 33.22  ? 4081 ASP A N     1 
ATOM   18632 C  CA    . ASP A 1 4081 ? 140.688 150.677 164.874 1.00 28.40  ? 4081 ASP A CA    1 
ATOM   18633 C  C     . ASP A 1 4081 ? 139.400 150.061 164.342 1.00 29.85  ? 4081 ASP A C     1 
ATOM   18634 O  O     . ASP A 1 4081 ? 139.078 148.904 164.644 1.00 33.31  ? 4081 ASP A O     1 
ATOM   18635 C  CB    . ASP A 1 4081 ? 140.393 151.637 166.026 1.00 33.07  ? 4081 ASP A CB    1 
ATOM   18636 C  CG    . ASP A 1 4081 ? 141.646 152.057 166.770 1.00 48.40  ? 4081 ASP A CG    1 
ATOM   18637 O  OD1   . ASP A 1 4081 ? 142.734 151.536 166.446 1.00 46.55  ? 4081 ASP A OD1   1 
ATOM   18638 O  OD2   . ASP A 1 4081 ? 141.544 152.909 167.677 1.00 62.72  ? 4081 ASP A OD2   1 
ATOM   18639 N  N     . LYS A 1 4082 ? 138.653 150.820 163.534 1.00 27.16  ? 4082 LYS A N     1 
ATOM   18640 C  CA    . LYS A 1 4082 ? 137.415 150.298 162.964 1.00 26.33  ? 4082 LYS A CA    1 
ATOM   18641 C  C     . LYS A 1 4082 ? 137.683 149.106 162.053 1.00 28.39  ? 4082 LYS A C     1 
ATOM   18642 O  O     . LYS A 1 4082 ? 136.959 148.104 162.100 1.00 34.93  ? 4082 LYS A O     1 
ATOM   18643 C  CB    . LYS A 1 4082 ? 136.685 151.401 162.199 1.00 32.71  ? 4082 LYS A CB    1 
ATOM   18644 C  CG    . LYS A 1 4082 ? 135.819 152.296 163.067 1.00 40.83  ? 4082 LYS A CG    1 
ATOM   18645 C  CD    . LYS A 1 4082 ? 134.900 153.159 162.219 1.00 45.94  ? 4082 LYS A CD    1 
ATOM   18646 C  CE    . LYS A 1 4082 ? 135.672 154.271 161.528 1.00 44.49  ? 4082 LYS A CE    1 
ATOM   18647 N  NZ    . LYS A 1 4082 ? 134.926 155.559 161.538 1.00 55.41  ? 4082 LYS A NZ    1 
ATOM   18648 N  N     . ALA A 1 4083 ? 138.721 149.196 161.218 1.00 26.47  ? 4083 ALA A N     1 
ATOM   18649 C  CA    . ALA A 1 4083 ? 139.044 148.106 160.307 1.00 22.97  ? 4083 ALA A CA    1 
ATOM   18650 C  C     . ALA A 1 4083 ? 139.468 146.856 161.064 1.00 25.15  ? 4083 ALA A C     1 
ATOM   18651 O  O     . ALA A 1 4083 ? 139.085 145.744 160.691 1.00 29.64  ? 4083 ALA A O     1 
ATOM   18652 C  CB    . ALA A 1 4083 ? 140.139 148.541 159.335 1.00 23.91  ? 4083 ALA A CB    1 
ATOM   18653 N  N     . ILE A 1 4084 ? 140.262 147.015 162.125 1.00 23.36  ? 4084 ILE A N     1 
ATOM   18654 C  CA    . ILE A 1 4084 ? 140.666 145.859 162.918 1.00 22.64  ? 4084 ILE A CA    1 
ATOM   18655 C  C     . ILE A 1 4084 ? 139.457 145.224 163.594 1.00 25.18  ? 4084 ILE A C     1 
ATOM   18656 O  O     . ILE A 1 4084 ? 139.309 143.994 163.602 1.00 29.52  ? 4084 ILE A O     1 
ATOM   18657 C  CB    . ILE A 1 4084 ? 141.743 146.264 163.941 1.00 20.05  ? 4084 ILE A CB    1 
ATOM   18658 C  CG1   . ILE A 1 4084 ? 143.048 146.613 163.225 1.00 18.22  ? 4084 ILE A CG1   1 
ATOM   18659 C  CG2   . ILE A 1 4084 ? 141.973 145.149 164.947 1.00 19.28  ? 4084 ILE A CG2   1 
ATOM   18660 C  CD1   . ILE A 1 4084 ? 144.078 147.256 164.119 1.00 15.99  ? 4084 ILE A CD1   1 
ATOM   18661 N  N     . ASN A 1 4085 ? 138.572 146.046 164.165 1.00 23.97  ? 4085 ASN A N     1 
ATOM   18662 C  CA    . ASN A 1 4085 ? 137.386 145.508 164.825 1.00 24.12  ? 4085 ASN A CA    1 
ATOM   18663 C  C     . ASN A 1 4085 ? 136.480 144.786 163.836 1.00 26.54  ? 4085 ASN A C     1 
ATOM   18664 O  O     . ASN A 1 4085 ? 135.854 143.776 164.178 1.00 32.05  ? 4085 ASN A O     1 
ATOM   18665 C  CB    . ASN A 1 4085 ? 136.626 146.628 165.534 1.00 27.05  ? 4085 ASN A CB    1 
ATOM   18666 C  CG    . ASN A 1 4085 ? 137.334 147.110 166.783 1.00 34.70  ? 4085 ASN A CG    1 
ATOM   18667 O  OD1   . ASN A 1 4085 ? 138.328 146.524 167.212 1.00 34.88  ? 4085 ASN A OD1   1 
ATOM   18668 N  ND2   . ASN A 1 4085 ? 136.826 148.184 167.375 1.00 42.06  ? 4085 ASN A ND2   1 
ATOM   18669 N  N     . THR A 1 4086 ? 136.384 145.297 162.607 1.00 26.18  ? 4086 THR A N     1 
ATOM   18670 C  CA    . THR A 1 4086 ? 135.576 144.625 161.594 1.00 27.75  ? 4086 THR A CA    1 
ATOM   18671 C  C     . THR A 1 4086 ? 136.231 143.328 161.129 1.00 32.60  ? 4086 THR A C     1 
ATOM   18672 O  O     . THR A 1 4086 ? 135.547 142.316 160.937 1.00 37.61  ? 4086 THR A O     1 
ATOM   18673 C  CB    . THR A 1 4086 ? 135.340 145.560 160.408 1.00 32.60  ? 4086 THR A CB    1 
ATOM   18674 O  OG1   . THR A 1 4086 ? 134.740 146.777 160.869 1.00 43.43  ? 4086 THR A OG1   1 
ATOM   18675 C  CG2   . THR A 1 4086 ? 134.424 144.907 159.385 1.00 34.54  ? 4086 THR A CG2   1 
ATOM   18676 N  N     . ALA A 1 4087 ? 137.553 143.338 160.948 1.00 32.05  ? 4087 ALA A N     1 
ATOM   18677 C  CA    . ALA A 1 4087 ? 138.249 142.187 160.390 1.00 27.93  ? 4087 ALA A CA    1 
ATOM   18678 C  C     . ALA A 1 4087 ? 138.356 141.032 161.375 1.00 31.53  ? 4087 ALA A C     1 
ATOM   18679 O  O     . ALA A 1 4087 ? 138.299 139.870 160.960 1.00 36.76  ? 4087 ALA A O     1 
ATOM   18680 C  CB    . ALA A 1 4087 ? 139.643 142.595 159.915 1.00 25.38  ? 4087 ALA A CB    1 
ATOM   18681 N  N     . VAL A 1 4088 ? 138.515 141.314 162.671 1.00 29.57  ? 4088 VAL A N     1 
ATOM   18682 C  CA    . VAL A 1 4088 ? 138.574 140.238 163.651 1.00 29.47  ? 4088 VAL A CA    1 
ATOM   18683 C  C     . VAL A 1 4088 ? 137.272 139.456 163.726 1.00 41.63  ? 4088 VAL A C     1 
ATOM   18684 O  O     . VAL A 1 4088 ? 137.247 138.358 164.289 1.00 47.54  ? 4088 VAL A O     1 
ATOM   18685 C  CB    . VAL A 1 4088 ? 138.953 140.778 165.046 1.00 29.13  ? 4088 VAL A CB    1 
ATOM   18686 C  CG1   . VAL A 1 4088 ? 140.332 141.409 165.010 1.00 27.40  ? 4088 VAL A CG1   1 
ATOM   18687 C  CG2   . VAL A 1 4088 ? 137.913 141.766 165.540 1.00 37.28  ? 4088 VAL A CG2   1 
ATOM   18688 N  N     . LYS A 1 4089 ? 136.187 139.996 163.172 1.00 42.13  ? 4089 LYS A N     1 
ATOM   18689 C  CA    . LYS A 1 4089 ? 134.916 139.292 163.061 1.00 39.21  ? 4089 LYS A CA    1 
ATOM   18690 C  C     . LYS A 1 4089 ? 134.706 138.699 161.673 1.00 40.79  ? 4089 LYS A C     1 
ATOM   18691 O  O     . LYS A 1 4089 ? 134.351 137.524 161.547 1.00 47.12  ? 4089 LYS A O     1 
ATOM   18692 C  CB    . LYS A 1 4089 ? 133.761 140.240 163.402 1.00 35.53  ? 4089 LYS A CB    1 
ATOM   18693 C  CG    . LYS A 1 4089 ? 133.753 140.721 164.842 1.00 43.62  ? 4089 LYS A CG    1 
ATOM   18694 C  CD    . LYS A 1 4089 ? 132.576 141.644 165.104 1.00 51.50  ? 4089 LYS A CD    1 
ATOM   18695 C  CE    . LYS A 1 4089 ? 132.521 142.066 166.562 1.00 59.67  ? 4089 LYS A CE    1 
ATOM   18696 N  NZ    . LYS A 1 4089 ? 133.679 142.928 166.929 1.00 64.47  ? 4089 LYS A NZ    1 
ATOM   18697 N  N     . SER A 1 4090 ? 134.921 139.496 160.624 1.00 41.20  ? 4090 SER A N     1 
ATOM   18698 C  CA    . SER A 1 4090 ? 134.700 139.024 159.261 1.00 43.87  ? 4090 SER A CA    1 
ATOM   18699 C  C     . SER A 1 4090 ? 135.808 138.096 158.780 1.00 42.18  ? 4090 SER A C     1 
ATOM   18700 O  O     . SER A 1 4090 ? 135.547 137.195 157.975 1.00 47.16  ? 4090 SER A O     1 
ATOM   18701 C  CB    . SER A 1 4090 ? 134.566 140.213 158.309 1.00 48.71  ? 4090 SER A CB    1 
ATOM   18702 O  OG    . SER A 1 4090 ? 133.719 141.210 158.855 1.00 54.63  ? 4090 SER A OG    1 
ATOM   18703 N  N     . GLY A 1 4091 ? 137.036 138.294 159.249 1.00 43.43  ? 4091 GLY A N     1 
ATOM   18704 C  CA    . GLY A 1 4091 ? 138.156 137.484 158.823 1.00 39.81  ? 4091 GLY A CA    1 
ATOM   18705 C  C     . GLY A 1 4091 ? 138.986 138.050 157.693 1.00 42.86  ? 4091 GLY A C     1 
ATOM   18706 O  O     . GLY A 1 4091 ? 139.797 137.315 157.120 1.00 43.17  ? 4091 GLY A O     1 
ATOM   18707 N  N     . ARG A 1 4092 ? 138.811 139.324 157.351 1.00 43.84  ? 4092 ARG A N     1 
ATOM   18708 C  CA    . ARG A 1 4092 ? 139.574 139.940 156.278 1.00 35.96  ? 4092 ARG A CA    1 
ATOM   18709 C  C     . ARG A 1 4092 ? 140.989 140.268 156.748 1.00 33.34  ? 4092 ARG A C     1 
ATOM   18710 O  O     . ARG A 1 4092 ? 141.375 140.006 157.891 1.00 34.09  ? 4092 ARG A O     1 
ATOM   18711 C  CB    . ARG A 1 4092 ? 138.868 141.197 155.775 1.00 41.08  ? 4092 ARG A CB    1 
ATOM   18712 C  CG    . ARG A 1 4092 ? 137.445 140.976 155.297 1.00 48.34  ? 4092 ARG A CG    1 
ATOM   18713 C  CD    . ARG A 1 4092 ? 136.669 142.285 155.248 1.00 51.72  ? 4092 ARG A CD    1 
ATOM   18714 N  NE    . ARG A 1 4092 ? 136.939 143.046 154.033 1.00 57.17  ? 4092 ARG A NE    1 
ATOM   18715 C  CZ    . ARG A 1 4092 ? 137.861 143.994 153.928 1.00 53.98  ? 4092 ARG A CZ    1 
ATOM   18716 N  NH1   . ARG A 1 4092 ? 138.622 144.335 154.955 1.00 50.15  ? 4092 ARG A NH1   1 
ATOM   18717 N  NH2   . ARG A 1 4092 ? 138.019 144.619 152.765 1.00 48.82  ? 4092 ARG A NH2   1 
ATOM   18718 N  N     . TRP A 1 4093 ? 141.774 140.853 155.850 1.00 31.46  ? 4093 TRP A N     1 
ATOM   18719 C  CA    . TRP A 1 4093 ? 143.133 141.276 156.146 1.00 30.11  ? 4093 TRP A CA    1 
ATOM   18720 C  C     . TRP A 1 4093 ? 143.184 142.787 156.337 1.00 30.98  ? 4093 TRP A C     1 
ATOM   18721 O  O     . TRP A 1 4093 ? 142.446 143.538 155.694 1.00 34.99  ? 4093 TRP A O     1 
ATOM   18722 C  CB    . TRP A 1 4093 ? 144.091 140.866 155.026 1.00 30.04  ? 4093 TRP A CB    1 
ATOM   18723 C  CG    . TRP A 1 4093 ? 144.358 139.395 154.958 1.00 24.60  ? 4093 TRP A CG    1 
ATOM   18724 C  CD1   . TRP A 1 4093 ? 143.746 138.415 155.682 1.00 24.43  ? 4093 TRP A CD1   1 
ATOM   18725 C  CD2   . TRP A 1 4093 ? 145.312 138.736 154.117 1.00 22.99  ? 4093 TRP A CD2   1 
ATOM   18726 N  NE1   . TRP A 1 4093 ? 144.259 137.187 155.344 1.00 23.85  ? 4093 TRP A NE1   1 
ATOM   18727 C  CE2   . TRP A 1 4093 ? 145.222 137.357 154.385 1.00 24.56  ? 4093 TRP A CE2   1 
ATOM   18728 C  CE3   . TRP A 1 4093 ? 146.233 139.180 153.163 1.00 27.69  ? 4093 TRP A CE3   1 
ATOM   18729 C  CZ2   . TRP A 1 4093 ? 146.018 136.418 153.735 1.00 30.75  ? 4093 TRP A CZ2   1 
ATOM   18730 C  CZ3   . TRP A 1 4093 ? 147.022 138.246 152.519 1.00 31.25  ? 4093 TRP A CZ3   1 
ATOM   18731 C  CH2   . TRP A 1 4093 ? 146.910 136.881 152.807 1.00 33.74  ? 4093 TRP A CH2   1 
ATOM   18732 N  N     . VAL A 1 4094 ? 144.061 143.225 157.235 1.00 24.78  ? 4094 VAL A N     1 
ATOM   18733 C  CA    . VAL A 1 4094 ? 144.275 144.642 157.505 1.00 23.35  ? 4094 VAL A CA    1 
ATOM   18734 C  C     . VAL A 1 4094 ? 145.769 144.919 157.448 1.00 22.64  ? 4094 VAL A C     1 
ATOM   18735 O  O     . VAL A 1 4094 ? 146.561 144.208 158.077 1.00 26.62  ? 4094 VAL A O     1 
ATOM   18736 C  CB    . VAL A 1 4094 ? 143.699 145.061 158.872 1.00 20.99  ? 4094 VAL A CB    1 
ATOM   18737 C  CG1   . VAL A 1 4094 ? 144.078 146.498 159.190 1.00 17.73  ? 4094 VAL A CG1   1 
ATOM   18738 C  CG2   . VAL A 1 4094 ? 142.193 144.900 158.882 1.00 25.06  ? 4094 VAL A CG2   1 
ATOM   18739 N  N     . MET A 1 4095 ? 146.154 145.945 156.694 1.00 19.09  ? 4095 MET A N     1 
ATOM   18740 C  CA    . MET A 1 4095 ? 147.540 146.379 156.602 1.00 18.73  ? 4095 MET A CA    1 
ATOM   18741 C  C     . MET A 1 4095 ? 147.641 147.832 157.040 1.00 17.00  ? 4095 MET A C     1 
ATOM   18742 O  O     . MET A 1 4095 ? 146.891 148.685 156.553 1.00 21.86  ? 4095 MET A O     1 
ATOM   18743 C  CB    . MET A 1 4095 ? 148.086 146.219 155.181 1.00 22.43  ? 4095 MET A CB    1 
ATOM   18744 C  CG    . MET A 1 4095 ? 149.585 146.448 155.078 1.00 20.16  ? 4095 MET A CG    1 
ATOM   18745 S  SD    . MET A 1 4095 ? 150.190 146.454 153.382 1.00 36.48  ? 4095 MET A SD    1 
ATOM   18746 C  CE    . MET A 1 4095 ? 148.844 147.283 152.545 1.00 34.49  ? 4095 MET A CE    1 
ATOM   18747 N  N     . LEU A 1 4096 ? 148.564 148.107 157.957 1.00 14.17  ? 4096 LEU A N     1 
ATOM   18748 C  CA    . LEU A 1 4096 ? 148.822 149.454 158.446 1.00 15.94  ? 4096 LEU A CA    1 
ATOM   18749 C  C     . LEU A 1 4096 ? 150.241 149.838 158.056 1.00 16.02  ? 4096 LEU A C     1 
ATOM   18750 O  O     . LEU A 1 4096 ? 151.197 149.151 158.432 1.00 18.09  ? 4096 LEU A O     1 
ATOM   18751 C  CB    . LEU A 1 4096 ? 148.629 149.533 159.961 1.00 15.49  ? 4096 LEU A CB    1 
ATOM   18752 C  CG    . LEU A 1 4096 ? 147.343 148.904 160.499 1.00 13.26  ? 4096 LEU A CG    1 
ATOM   18753 C  CD1   . LEU A 1 4096 ? 147.296 148.983 162.012 1.00 13.18  ? 4096 LEU A CD1   1 
ATOM   18754 C  CD2   . LEU A 1 4096 ? 146.125 149.575 159.892 1.00 15.32  ? 4096 LEU A CD2   1 
ATOM   18755 N  N     . LYS A 1 4097 ? 150.376 150.928 157.310 1.00 15.89  ? 4097 LYS A N     1 
ATOM   18756 C  CA    . LYS A 1 4097 ? 151.656 151.343 156.759 1.00 14.87  ? 4097 LYS A CA    1 
ATOM   18757 C  C     . LYS A 1 4097 ? 152.293 152.425 157.621 1.00 16.37  ? 4097 LYS A C     1 
ATOM   18758 O  O     . LYS A 1 4097 ? 151.604 153.260 158.213 1.00 19.74  ? 4097 LYS A O     1 
ATOM   18759 C  CB    . LYS A 1 4097 ? 151.491 151.859 155.328 1.00 16.65  ? 4097 LYS A CB    1 
ATOM   18760 C  CG    . LYS A 1 4097 ? 150.626 150.982 154.443 1.00 14.39  ? 4097 LYS A CG    1 
ATOM   18761 C  CD    . LYS A 1 4097 ? 150.264 151.704 153.159 1.00 21.49  ? 4097 LYS A CD    1 
ATOM   18762 C  CE    . LYS A 1 4097 ? 149.205 150.947 152.381 1.00 29.63  ? 4097 LYS A CE    1 
ATOM   18763 N  NZ    . LYS A 1 4097 ? 148.755 151.703 151.181 1.00 33.10  ? 4097 LYS A NZ    1 
ATOM   18764 N  N     . ASN A 1 4098 ? 153.626 152.400 157.675 1.00 17.62  ? 4098 ASN A N     1 
ATOM   18765 C  CA    . ASN A 1 4098 ? 154.418 153.395 158.399 1.00 17.48  ? 4098 ASN A CA    1 
ATOM   18766 C  C     . ASN A 1 4098 ? 153.991 153.494 159.862 1.00 20.00  ? 4098 ASN A C     1 
ATOM   18767 O  O     . ASN A 1 4098 ? 153.837 154.583 160.418 1.00 24.46  ? 4098 ASN A O     1 
ATOM   18768 C  CB    . ASN A 1 4098 ? 154.340 154.761 157.713 1.00 20.19  ? 4098 ASN A CB    1 
ATOM   18769 C  CG    . ASN A 1 4098 ? 154.476 154.666 156.207 1.00 20.97  ? 4098 ASN A CG    1 
ATOM   18770 O  OD1   . ASN A 1 4098 ? 153.652 155.199 155.464 1.00 20.68  ? 4098 ASN A OD1   1 
ATOM   18771 N  ND2   . ASN A 1 4098 ? 155.519 153.984 155.749 1.00 21.06  ? 4098 ASN A ND2   1 
ATOM   18772 N  N     . VAL A 1 4099 ? 153.798 152.332 160.493 1.00 18.34  ? 4099 VAL A N     1 
ATOM   18773 C  CA    . VAL A 1 4099 ? 153.415 152.302 161.900 1.00 16.77  ? 4099 VAL A CA    1 
ATOM   18774 C  C     . VAL A 1 4099 ? 154.532 152.766 162.820 1.00 21.07  ? 4099 VAL A C     1 
ATOM   18775 O  O     . VAL A 1 4099 ? 154.278 153.034 164.000 1.00 25.99  ? 4099 VAL A O     1 
ATOM   18776 C  CB    . VAL A 1 4099 ? 152.957 150.890 162.318 1.00 15.13  ? 4099 VAL A CB    1 
ATOM   18777 C  CG1   . VAL A 1 4099 ? 151.757 150.461 161.496 1.00 15.00  ? 4099 VAL A CG1   1 
ATOM   18778 C  CG2   . VAL A 1 4099 ? 154.092 149.896 162.171 1.00 16.38  ? 4099 VAL A CG2   1 
ATOM   18779 N  N     . HIS A 1 4100 ? 155.762 152.872 162.314 1.00 20.78  ? 4100 HIS A N     1 
ATOM   18780 C  CA    . HIS A 1 4100 ? 156.864 153.386 163.115 1.00 21.87  ? 4100 HIS A CA    1 
ATOM   18781 C  C     . HIS A 1 4100 ? 156.740 154.878 163.393 1.00 25.01  ? 4100 HIS A C     1 
ATOM   18782 O  O     . HIS A 1 4100 ? 157.462 155.391 164.254 1.00 31.11  ? 4100 HIS A O     1 
ATOM   18783 C  CB    . HIS A 1 4100 ? 158.197 153.098 162.421 1.00 20.12  ? 4100 HIS A CB    1 
ATOM   18784 C  CG    . HIS A 1 4100 ? 158.374 153.826 161.125 1.00 22.28  ? 4100 HIS A CG    1 
ATOM   18785 N  ND1   . HIS A 1 4100 ? 157.823 153.385 159.941 1.00 24.39  ? 4100 HIS A ND1   1 
ATOM   18786 C  CD2   . HIS A 1 4100 ? 159.045 154.963 160.826 1.00 25.05  ? 4100 HIS A CD2   1 
ATOM   18787 C  CE1   . HIS A 1 4100 ? 158.145 154.220 158.970 1.00 21.77  ? 4100 HIS A CE1   1 
ATOM   18788 N  NE2   . HIS A 1 4100 ? 158.886 155.186 159.480 1.00 23.76  ? 4100 HIS A NE2   1 
ATOM   18789 N  N     . LEU A 1 4101 ? 155.850 155.581 162.692 1.00 23.07  ? 4101 LEU A N     1 
ATOM   18790 C  CA    . LEU A 1 4101 ? 155.632 157.000 162.933 1.00 22.25  ? 4101 LEU A CA    1 
ATOM   18791 C  C     . LEU A 1 4101 ? 154.728 157.265 164.129 1.00 26.62  ? 4101 LEU A C     1 
ATOM   18792 O  O     . LEU A 1 4101 ? 154.587 158.424 164.533 1.00 35.78  ? 4101 LEU A O     1 
ATOM   18793 C  CB    . LEU A 1 4101 ? 155.039 157.662 161.687 1.00 17.17  ? 4101 LEU A CB    1 
ATOM   18794 C  CG    . LEU A 1 4101 ? 155.854 157.520 160.401 1.00 18.13  ? 4101 LEU A CG    1 
ATOM   18795 C  CD1   . LEU A 1 4101 ? 155.089 158.080 159.216 1.00 17.35  ? 4101 LEU A CD1   1 
ATOM   18796 C  CD2   . LEU A 1 4101 ? 157.202 158.206 160.545 1.00 19.51  ? 4101 LEU A CD2   1 
ATOM   18797 N  N     . ALA A 1 4102 ? 154.116 156.230 164.698 1.00 26.60  ? 4102 ALA A N     1 
ATOM   18798 C  CA    . ALA A 1 4102 ? 153.279 156.352 165.892 1.00 27.48  ? 4102 ALA A CA    1 
ATOM   18799 C  C     . ALA A 1 4102 ? 153.711 155.303 166.907 1.00 29.58  ? 4102 ALA A C     1 
ATOM   18800 O  O     . ALA A 1 4102 ? 152.995 154.325 167.154 1.00 31.20  ? 4102 ALA A O     1 
ATOM   18801 C  CB    . ALA A 1 4102 ? 151.798 156.205 165.542 1.00 22.39  ? 4102 ALA A CB    1 
ATOM   18802 N  N     . PRO A 1 4103 ? 154.893 155.469 167.509 1.00 29.08  ? 4103 PRO A N     1 
ATOM   18803 C  CA    . PRO A 1 4103 ? 155.352 154.481 168.498 1.00 27.56  ? 4103 PRO A CA    1 
ATOM   18804 C  C     . PRO A 1 4103 ? 154.454 154.378 169.717 1.00 29.29  ? 4103 PRO A C     1 
ATOM   18805 O  O     . PRO A 1 4103 ? 154.318 153.286 170.284 1.00 31.15  ? 4103 PRO A O     1 
ATOM   18806 C  CB    . PRO A 1 4103 ? 156.754 154.984 168.868 1.00 29.30  ? 4103 PRO A CB    1 
ATOM   18807 C  CG    . PRO A 1 4103 ? 156.723 156.441 168.568 1.00 31.81  ? 4103 PRO A CG    1 
ATOM   18808 C  CD    . PRO A 1 4103 ? 155.830 156.597 167.376 1.00 28.49  ? 4103 PRO A CD    1 
ATOM   18809 N  N     . GLY A 1 4104 ? 153.840 155.483 170.144 1.00 28.43  ? 4104 GLY A N     1 
ATOM   18810 C  CA    . GLY A 1 4104 ? 152.966 155.430 171.304 1.00 29.89  ? 4104 GLY A CA    1 
ATOM   18811 C  C     . GLY A 1 4104 ? 151.712 154.613 171.056 1.00 30.32  ? 4104 GLY A C     1 
ATOM   18812 O  O     . GLY A 1 4104 ? 151.255 153.879 171.936 1.00 34.37  ? 4104 GLY A O     1 
ATOM   18813 N  N     . TRP A 1 4105 ? 151.139 154.730 169.859 1.00 29.18  ? 4105 TRP A N     1 
ATOM   18814 C  CA    . TRP A 1 4105 ? 149.942 153.976 169.511 1.00 28.55  ? 4105 TRP A CA    1 
ATOM   18815 C  C     . TRP A 1 4105 ? 150.227 152.495 169.295 1.00 30.04  ? 4105 TRP A C     1 
ATOM   18816 O  O     . TRP A 1 4105 ? 149.311 151.674 169.428 1.00 32.38  ? 4105 TRP A O     1 
ATOM   18817 C  CB    . TRP A 1 4105 ? 149.303 154.577 168.257 1.00 24.01  ? 4105 TRP A CB    1 
ATOM   18818 C  CG    . TRP A 1 4105 ? 148.082 153.858 167.785 1.00 26.27  ? 4105 TRP A CG    1 
ATOM   18819 C  CD1   . TRP A 1 4105 ? 146.827 153.941 168.311 1.00 30.57  ? 4105 TRP A CD1   1 
ATOM   18820 C  CD2   . TRP A 1 4105 ? 147.996 152.950 166.682 1.00 28.99  ? 4105 TRP A CD2   1 
ATOM   18821 N  NE1   . TRP A 1 4105 ? 145.964 153.138 167.607 1.00 32.92  ? 4105 TRP A NE1   1 
ATOM   18822 C  CE2   . TRP A 1 4105 ? 146.658 152.518 166.601 1.00 29.73  ? 4105 TRP A CE2   1 
ATOM   18823 C  CE3   . TRP A 1 4105 ? 148.921 152.458 165.756 1.00 28.51  ? 4105 TRP A CE3   1 
ATOM   18824 C  CZ2   . TRP A 1 4105 ? 146.223 151.620 165.632 1.00 31.19  ? 4105 TRP A CZ2   1 
ATOM   18825 C  CZ3   . TRP A 1 4105 ? 148.487 151.567 164.796 1.00 28.63  ? 4105 TRP A CZ3   1 
ATOM   18826 C  CH2   . TRP A 1 4105 ? 147.150 151.157 164.741 1.00 31.96  ? 4105 TRP A CH2   1 
ATOM   18827 N  N     . LEU A 1 4106 ? 151.473 152.136 168.977 1.00 29.28  ? 4106 LEU A N     1 
ATOM   18828 C  CA    . LEU A 1 4106 ? 151.808 150.733 168.760 1.00 28.89  ? 4106 LEU A CA    1 
ATOM   18829 C  C     . LEU A 1 4106 ? 151.680 149.927 170.046 1.00 35.57  ? 4106 LEU A C     1 
ATOM   18830 O  O     . LEU A 1 4106 ? 151.280 148.759 170.014 1.00 36.71  ? 4106 LEU A O     1 
ATOM   18831 C  CB    . LEU A 1 4106 ? 153.219 150.614 168.186 1.00 27.05  ? 4106 LEU A CB    1 
ATOM   18832 C  CG    . LEU A 1 4106 ? 153.330 150.770 166.668 1.00 25.65  ? 4106 LEU A CG    1 
ATOM   18833 C  CD1   . LEU A 1 4106 ? 154.774 150.632 166.216 1.00 21.92  ? 4106 LEU A CD1   1 
ATOM   18834 C  CD2   . LEU A 1 4106 ? 152.442 149.761 165.958 1.00 23.23  ? 4106 LEU A CD2   1 
ATOM   18835 N  N     . MET A 1 4107 ? 152.017 150.529 171.189 1.00 38.00  ? 4107 MET A N     1 
ATOM   18836 C  CA    . MET A 1 4107 ? 151.852 149.839 172.464 1.00 36.63  ? 4107 MET A CA    1 
ATOM   18837 C  C     . MET A 1 4107 ? 150.382 149.536 172.735 1.00 36.50  ? 4107 MET A C     1 
ATOM   18838 O  O     . MET A 1 4107 ? 150.029 148.421 173.138 1.00 42.69  ? 4107 MET A O     1 
ATOM   18839 C  CB    . MET A 1 4107 ? 152.448 150.679 173.594 1.00 34.80  ? 4107 MET A CB    1 
ATOM   18840 C  CG    . MET A 1 4107 ? 153.961 150.793 173.550 1.00 42.03  ? 4107 MET A CG    1 
ATOM   18841 S  SD    . MET A 1 4107 ? 154.703 150.828 175.192 1.00 83.54  ? 4107 MET A SD    1 
ATOM   18842 C  CE    . MET A 1 4107 ? 156.408 151.195 174.786 1.00 54.89  ? 4107 MET A CE    1 
ATOM   18843 N  N     . GLN A 1 4108 ? 149.509 150.521 172.509 1.00 33.85  ? 4108 GLN A N     1 
ATOM   18844 C  CA    . GLN A 1 4108 ? 148.078 150.298 172.691 1.00 34.75  ? 4108 GLN A CA    1 
ATOM   18845 C  C     . GLN A 1 4108 ? 147.561 149.246 171.721 1.00 34.09  ? 4108 GLN A C     1 
ATOM   18846 O  O     . GLN A 1 4108 ? 146.716 148.418 172.082 1.00 35.41  ? 4108 GLN A O     1 
ATOM   18847 C  CB    . GLN A 1 4108 ? 147.314 151.610 172.516 1.00 42.60  ? 4108 GLN A CB    1 
ATOM   18848 C  CG    . GLN A 1 4108 ? 147.921 152.790 173.254 1.00 52.64  ? 4108 GLN A CG    1 
ATOM   18849 C  CD    . GLN A 1 4108 ? 147.237 154.099 172.913 1.00 63.99  ? 4108 GLN A CD    1 
ATOM   18850 O  OE1   . GLN A 1 4108 ? 146.181 154.115 172.280 1.00 64.26  ? 4108 GLN A OE1   1 
ATOM   18851 N  NE2   . GLN A 1 4108 ? 147.837 155.207 173.332 1.00 63.78  ? 4108 GLN A NE2   1 
ATOM   18852 N  N     . LEU A 1 4109 ? 148.055 149.265 170.481 1.00 34.38  ? 4109 LEU A N     1 
ATOM   18853 C  CA    . LEU A 1 4109 ? 147.660 148.247 169.513 1.00 31.67  ? 4109 LEU A CA    1 
ATOM   18854 C  C     . LEU A 1 4109 ? 148.087 146.858 169.971 1.00 35.23  ? 4109 LEU A C     1 
ATOM   18855 O  O     . LEU A 1 4109 ? 147.339 145.888 169.812 1.00 39.78  ? 4109 LEU A O     1 
ATOM   18856 C  CB    . LEU A 1 4109 ? 148.252 148.570 168.141 1.00 29.02  ? 4109 LEU A CB    1 
ATOM   18857 C  CG    . LEU A 1 4109 ? 148.157 147.473 167.080 1.00 30.18  ? 4109 LEU A CG    1 
ATOM   18858 C  CD1   . LEU A 1 4109 ? 146.712 147.255 166.668 1.00 26.16  ? 4109 LEU A CD1   1 
ATOM   18859 C  CD2   . LEU A 1 4109 ? 149.015 147.817 165.874 1.00 29.44  ? 4109 LEU A CD2   1 
ATOM   18860 N  N     . GLU A 1 4110 ? 149.288 146.744 170.542 1.00 32.58  ? 4110 GLU A N     1 
ATOM   18861 C  CA    . GLU A 1 4110 ? 149.748 145.454 171.049 1.00 33.32  ? 4110 GLU A CA    1 
ATOM   18862 C  C     . GLU A 1 4110 ? 148.884 144.974 172.210 1.00 37.85  ? 4110 GLU A C     1 
ATOM   18863 O  O     . GLU A 1 4110 ? 148.533 143.790 172.281 1.00 41.79  ? 4110 GLU A O     1 
ATOM   18864 C  CB    . GLU A 1 4110 ? 151.213 145.549 171.472 1.00 34.89  ? 4110 GLU A CB    1 
ATOM   18865 C  CG    . GLU A 1 4110 ? 151.907 144.203 171.611 1.00 35.78  ? 4110 GLU A CG    1 
ATOM   18866 C  CD    . GLU A 1 4110 ? 151.727 143.589 172.984 1.00 43.56  ? 4110 GLU A CD    1 
ATOM   18867 O  OE1   . GLU A 1 4110 ? 151.946 144.299 173.988 1.00 47.59  ? 4110 GLU A OE1   1 
ATOM   18868 O  OE2   . GLU A 1 4110 ? 151.366 142.396 173.060 1.00 42.58  ? 4110 GLU A OE2   1 
ATOM   18869 N  N     . LYS A 1 4111 ? 148.538 145.877 173.134 1.00 40.95  ? 4111 LYS A N     1 
ATOM   18870 C  CA    . LYS A 1 4111 ? 147.662 145.490 174.238 1.00 38.65  ? 4111 LYS A CA    1 
ATOM   18871 C  C     . LYS A 1 4111 ? 146.294 145.051 173.729 1.00 38.54  ? 4111 LYS A C     1 
ATOM   18872 O  O     . LYS A 1 4111 ? 145.710 144.092 174.245 1.00 44.80  ? 4111 LYS A O     1 
ATOM   18873 C  CB    . LYS A 1 4111 ? 147.512 146.633 175.244 1.00 41.44  ? 4111 LYS A CB    1 
ATOM   18874 C  CG    . LYS A 1 4111 ? 148.810 147.297 175.655 1.00 44.75  ? 4111 LYS A CG    1 
ATOM   18875 C  CD    . LYS A 1 4111 ? 149.685 146.362 176.469 1.00 43.94  ? 4111 LYS A CD    1 
ATOM   18876 C  CE    . LYS A 1 4111 ? 150.847 147.112 177.097 1.00 52.33  ? 4111 LYS A CE    1 
ATOM   18877 N  NZ    . LYS A 1 4111 ? 150.478 148.512 177.447 1.00 56.67  ? 4111 LYS A NZ    1 
ATOM   18878 N  N     . LYS A 1 4112 ? 145.766 145.748 172.721 1.00 36.61  ? 4112 LYS A N     1 
ATOM   18879 C  CA    . LYS A 1 4112 ? 144.491 145.350 172.131 1.00 35.60  ? 4112 LYS A CA    1 
ATOM   18880 C  C     . LYS A 1 4112 ? 144.595 143.985 171.461 1.00 39.24  ? 4112 LYS A C     1 
ATOM   18881 O  O     . LYS A 1 4112 ? 143.673 143.166 171.558 1.00 45.75  ? 4112 LYS A O     1 
ATOM   18882 C  CB    . LYS A 1 4112 ? 144.029 146.413 171.134 1.00 32.61  ? 4112 LYS A CB    1 
ATOM   18883 C  CG    . LYS A 1 4112 ? 143.049 145.921 170.083 1.00 35.69  ? 4112 LYS A CG    1 
ATOM   18884 C  CD    . LYS A 1 4112 ? 142.770 147.004 169.052 1.00 38.72  ? 4112 LYS A CD    1 
ATOM   18885 C  CE    . LYS A 1 4112 ? 141.474 146.744 168.304 1.00 33.26  ? 4112 LYS A CE    1 
ATOM   18886 N  NZ    . LYS A 1 4112 ? 140.378 146.327 169.221 1.00 35.76  ? 4112 LYS A NZ    1 
ATOM   18887 N  N     . LEU A 1 4113 ? 145.712 143.722 170.780 1.00 38.81  ? 4113 LEU A N     1 
ATOM   18888 C  CA    . LEU A 1 4113 ? 145.886 142.451 170.085 1.00 40.67  ? 4113 LEU A CA    1 
ATOM   18889 C  C     . LEU A 1 4113 ? 146.023 141.291 171.063 1.00 44.87  ? 4113 LEU A C     1 
ATOM   18890 O  O     . LEU A 1 4113 ? 145.536 140.187 170.793 1.00 49.04  ? 4113 LEU A O     1 
ATOM   18891 C  CB    . LEU A 1 4113 ? 147.108 142.518 169.170 1.00 35.92  ? 4113 LEU A CB    1 
ATOM   18892 C  CG    . LEU A 1 4113 ? 146.947 143.260 167.844 1.00 32.43  ? 4113 LEU A CG    1 
ATOM   18893 C  CD1   . LEU A 1 4113 ? 148.307 143.526 167.225 1.00 30.15  ? 4113 LEU A CD1   1 
ATOM   18894 C  CD2   . LEU A 1 4113 ? 146.064 142.471 166.892 1.00 35.08  ? 4113 LEU A CD2   1 
ATOM   18895 N  N     . HIS A 1 4114 ? 146.695 141.515 172.196 1.00 45.93  ? 4114 HIS A N     1 
ATOM   18896 C  CA    . HIS A 1 4114 ? 146.917 140.428 173.146 1.00 43.41  ? 4114 HIS A CA    1 
ATOM   18897 C  C     . HIS A 1 4114 ? 145.602 139.890 173.697 1.00 45.25  ? 4114 HIS A C     1 
ATOM   18898 O  O     . HIS A 1 4114 ? 145.411 138.671 173.787 1.00 44.37  ? 4114 HIS A O     1 
ATOM   18899 C  CB    . HIS A 1 4114 ? 147.819 140.900 174.286 1.00 41.88  ? 4114 HIS A CB    1 
ATOM   18900 C  CG    . HIS A 1 4114 ? 148.024 139.872 175.354 1.00 42.25  ? 4114 HIS A CG    1 
ATOM   18901 N  ND1   . HIS A 1 4114 ? 148.679 138.681 175.125 1.00 39.81  ? 4114 HIS A ND1   1 
ATOM   18902 C  CD2   . HIS A 1 4114 ? 147.656 139.853 176.657 1.00 38.15  ? 4114 HIS A CD2   1 
ATOM   18903 C  CE1   . HIS A 1 4114 ? 148.708 137.975 176.241 1.00 35.94  ? 4114 HIS A CE1   1 
ATOM   18904 N  NE2   . HIS A 1 4114 ? 148.094 138.663 177.186 1.00 36.27  ? 4114 HIS A NE2   1 
ATOM   18905 N  N     . SER A 1 4115 ? 144.684 140.779 174.070 1.00 47.16  ? 4115 SER A N     1 
ATOM   18906 C  CA    . SER A 1 4115 ? 143.374 140.373 174.581 1.00 50.47  ? 4115 SER A CA    1 
ATOM   18907 C  C     . SER A 1 4115 ? 142.374 140.334 173.425 1.00 54.03  ? 4115 SER A C     1 
ATOM   18908 O  O     . SER A 1 4115 ? 141.471 141.164 173.301 1.00 56.61  ? 4115 SER A O     1 
ATOM   18909 C  CB    . SER A 1 4115 ? 142.920 141.314 175.689 1.00 50.56  ? 4115 SER A CB    1 
ATOM   18910 O  OG    . SER A 1 4115 ? 142.713 142.624 175.191 1.00 50.51  ? 4115 SER A OG    1 
ATOM   18911 N  N     . LEU A 1 4116 ? 142.555 139.334 172.566 1.00 50.93  ? 4116 LEU A N     1 
ATOM   18912 C  CA    . LEU A 1 4116 ? 141.754 139.231 171.356 1.00 52.29  ? 4116 LEU A CA    1 
ATOM   18913 C  C     . LEU A 1 4116 ? 141.780 137.796 170.852 1.00 56.91  ? 4116 LEU A C     1 
ATOM   18914 O  O     . LEU A 1 4116 ? 142.820 137.135 170.898 1.00 59.23  ? 4116 LEU A O     1 
ATOM   18915 C  CB    . LEU A 1 4116 ? 142.274 140.188 170.279 1.00 46.77  ? 4116 LEU A CB    1 
ATOM   18916 C  CG    . LEU A 1 4116 ? 141.514 140.277 168.958 1.00 52.10  ? 4116 LEU A CG    1 
ATOM   18917 C  CD1   . LEU A 1 4116 ? 140.101 140.786 169.184 1.00 46.18  ? 4116 LEU A CD1   1 
ATOM   18918 C  CD2   . LEU A 1 4116 ? 142.267 141.181 168.000 1.00 48.74  ? 4116 LEU A CD2   1 
ATOM   18919 N  N     . GLN A 1 4117 ? 140.628 137.324 170.374 1.00 56.19  ? 4117 GLN A N     1 
ATOM   18920 C  CA    . GLN A 1 4117 ? 140.489 135.999 169.770 1.00 56.28  ? 4117 GLN A CA    1 
ATOM   18921 C  C     . GLN A 1 4117 ? 139.792 136.185 168.429 1.00 54.95  ? 4117 GLN A C     1 
ATOM   18922 O  O     . GLN A 1 4117 ? 138.573 135.998 168.313 1.00 55.45  ? 4117 GLN A O     1 
ATOM   18923 C  CB    . GLN A 1 4117 ? 139.718 135.047 170.686 1.00 57.29  ? 4117 GLN A CB    1 
ATOM   18924 C  CG    . GLN A 1 4117 ? 139.600 133.626 170.157 1.00 68.86  ? 4117 GLN A CG    1 
ATOM   18925 C  CD    . GLN A 1 4117 ? 140.948 132.951 169.993 1.00 74.91  ? 4117 GLN A CD    1 
ATOM   18926 O  OE1   . GLN A 1 4117 ? 141.447 132.799 168.878 1.00 77.13  ? 4117 GLN A OE1   1 
ATOM   18927 N  NE2   . GLN A 1 4117 ? 141.544 132.542 171.107 1.00 73.07  ? 4117 GLN A NE2   1 
ATOM   18928 N  N     . PRO A 1 4118 ? 140.533 136.562 167.396 1.00 51.95  ? 4118 PRO A N     1 
ATOM   18929 C  CA    . PRO A 1 4118 ? 139.922 136.936 166.118 1.00 45.11  ? 4118 PRO A CA    1 
ATOM   18930 C  C     . PRO A 1 4118 ? 139.563 135.711 165.281 1.00 42.21  ? 4118 PRO A C     1 
ATOM   18931 O  O     . PRO A 1 4118 ? 139.702 134.566 165.705 1.00 48.29  ? 4118 PRO A O     1 
ATOM   18932 C  CB    . PRO A 1 4118 ? 141.017 137.766 165.448 1.00 40.10  ? 4118 PRO A CB    1 
ATOM   18933 C  CG    . PRO A 1 4118 ? 142.283 137.187 165.972 1.00 41.90  ? 4118 PRO A CG    1 
ATOM   18934 C  CD    . PRO A 1 4118 ? 142.000 136.705 167.372 1.00 50.50  ? 4118 PRO A CD    1 
ATOM   18935 N  N     . HIS A 1 4119 ? 139.091 135.985 164.067 1.00 39.53  ? 4119 HIS A N     1 
ATOM   18936 C  CA    . HIS A 1 4119 ? 138.725 134.933 163.131 1.00 39.65  ? 4119 HIS A CA    1 
ATOM   18937 C  C     . HIS A 1 4119 ? 139.963 134.165 162.678 1.00 41.47  ? 4119 HIS A C     1 
ATOM   18938 O  O     . HIS A 1 4119 ? 141.096 134.642 162.778 1.00 50.04  ? 4119 HIS A O     1 
ATOM   18939 C  CB    . HIS A 1 4119 ? 138.003 135.531 161.922 1.00 43.95  ? 4119 HIS A CB    1 
ATOM   18940 C  CG    . HIS A 1 4119 ? 137.226 134.532 161.123 1.00 51.12  ? 4119 HIS A CG    1 
ATOM   18941 N  ND1   . HIS A 1 4119 ? 137.515 134.246 159.807 1.00 47.46  ? 4119 HIS A ND1   1 
ATOM   18942 C  CD2   . HIS A 1 4119 ? 136.166 133.757 161.452 1.00 57.33  ? 4119 HIS A CD2   1 
ATOM   18943 C  CE1   . HIS A 1 4119 ? 136.668 133.336 159.359 1.00 49.18  ? 4119 HIS A CE1   1 
ATOM   18944 N  NE2   . HIS A 1 4119 ? 135.839 133.022 160.338 1.00 57.83  ? 4119 HIS A NE2   1 
ATOM   18945 N  N     . ALA A 1 4120 ? 139.733 132.952 162.173 1.00 38.64  ? 4120 ALA A N     1 
ATOM   18946 C  CA    . ALA A 1 4120 ? 140.842 132.107 161.743 1.00 40.55  ? 4120 ALA A CA    1 
ATOM   18947 C  C     . ALA A 1 4120 ? 141.562 132.683 160.531 1.00 45.10  ? 4120 ALA A C     1 
ATOM   18948 O  O     . ALA A 1 4120 ? 142.773 132.485 160.382 1.00 47.17  ? 4120 ALA A O     1 
ATOM   18949 C  CB    . ALA A 1 4120 ? 140.341 130.696 161.440 1.00 43.82  ? 4120 ALA A CB    1 
ATOM   18950 N  N     . CYS A 1 4121 ? 140.846 133.390 159.659 1.00 40.43  ? 4121 CYS A N     1 
ATOM   18951 C  CA    . CYS A 1 4121 ? 141.423 133.944 158.442 1.00 35.55  ? 4121 CYS A CA    1 
ATOM   18952 C  C     . CYS A 1 4121 ? 141.917 135.375 158.609 1.00 37.15  ? 4121 CYS A C     1 
ATOM   18953 O  O     . CYS A 1 4121 ? 142.382 135.970 157.633 1.00 39.27  ? 4121 CYS A O     1 
ATOM   18954 C  CB    . CYS A 1 4121 ? 140.401 133.885 157.302 1.00 39.32  ? 4121 CYS A CB    1 
ATOM   18955 S  SG    . CYS A 1 4121 ? 139.919 132.213 156.815 1.00 73.08  ? 4121 CYS A SG    1 
ATOM   18956 N  N     . PHE A 1 4122 ? 141.829 135.940 159.810 1.00 34.08  ? 4122 PHE A N     1 
ATOM   18957 C  CA    . PHE A 1 4122 ? 142.257 137.314 160.034 1.00 28.97  ? 4122 PHE A CA    1 
ATOM   18958 C  C     . PHE A 1 4122 ? 143.777 137.393 160.089 1.00 31.93  ? 4122 PHE A C     1 
ATOM   18959 O  O     . PHE A 1 4122 ? 144.426 136.595 160.771 1.00 36.88  ? 4122 PHE A O     1 
ATOM   18960 C  CB    . PHE A 1 4122 ? 141.656 137.857 161.330 1.00 27.91  ? 4122 PHE A CB    1 
ATOM   18961 C  CG    . PHE A 1 4122 ? 142.283 139.140 161.797 1.00 27.35  ? 4122 PHE A CG    1 
ATOM   18962 C  CD1   . PHE A 1 4122 ? 142.109 140.312 161.081 1.00 26.11  ? 4122 PHE A CD1   1 
ATOM   18963 C  CD2   . PHE A 1 4122 ? 143.047 139.174 162.950 1.00 28.09  ? 4122 PHE A CD2   1 
ATOM   18964 C  CE1   . PHE A 1 4122 ? 142.684 141.493 161.508 1.00 21.46  ? 4122 PHE A CE1   1 
ATOM   18965 C  CE2   . PHE A 1 4122 ? 143.623 140.353 163.382 1.00 26.62  ? 4122 PHE A CE2   1 
ATOM   18966 C  CZ    . PHE A 1 4122 ? 143.441 141.513 162.660 1.00 19.30  ? 4122 PHE A CZ    1 
ATOM   18967 N  N     . ARG A 1 4123 ? 144.341 138.357 159.364 1.00 29.02  ? 4123 ARG A N     1 
ATOM   18968 C  CA    . ARG A 1 4123 ? 145.775 138.614 159.382 1.00 23.32  ? 4123 ARG A CA    1 
ATOM   18969 C  C     . ARG A 1 4123 ? 146.000 140.115 159.460 1.00 21.22  ? 4123 ARG A C     1 
ATOM   18970 O  O     . ARG A 1 4123 ? 145.351 140.878 158.739 1.00 22.52  ? 4123 ARG A O     1 
ATOM   18971 C  CB    . ARG A 1 4123 ? 146.465 138.041 158.138 1.00 24.53  ? 4123 ARG A CB    1 
ATOM   18972 C  CG    . ARG A 1 4123 ? 146.425 136.526 158.035 1.00 22.14  ? 4123 ARG A CG    1 
ATOM   18973 C  CD    . ARG A 1 4123 ? 147.219 135.873 159.152 1.00 24.34  ? 4123 ARG A CD    1 
ATOM   18974 N  NE    . ARG A 1 4123 ? 147.275 134.424 159.005 1.00 32.71  ? 4123 ARG A NE    1 
ATOM   18975 C  CZ    . ARG A 1 4123 ? 146.295 133.597 159.339 1.00 35.61  ? 4123 ARG A CZ    1 
ATOM   18976 N  NH1   . ARG A 1 4123 ? 145.160 134.042 159.853 1.00 36.04  ? 4123 ARG A NH1   1 
ATOM   18977 N  NH2   . ARG A 1 4123 ? 146.457 132.290 159.154 1.00 43.27  ? 4123 ARG A NH2   1 
ATOM   18978 N  N     . LEU A 1 4124 ? 146.913 140.534 160.329 1.00 18.16  ? 4124 LEU A N     1 
ATOM   18979 C  CA    . LEU A 1 4124 ? 147.253 141.940 160.499 1.00 16.17  ? 4124 LEU A CA    1 
ATOM   18980 C  C     . LEU A 1 4124 ? 148.696 142.154 160.062 1.00 18.34  ? 4124 LEU A C     1 
ATOM   18981 O  O     . LEU A 1 4124 ? 149.608 141.501 160.579 1.00 19.31  ? 4124 LEU A O     1 
ATOM   18982 C  CB    . LEU A 1 4124 ? 147.056 142.384 161.948 1.00 15.64  ? 4124 LEU A CB    1 
ATOM   18983 C  CG    . LEU A 1 4124 ? 147.393 143.844 162.253 1.00 14.01  ? 4124 LEU A CG    1 
ATOM   18984 C  CD1   . LEU A 1 4124 ? 146.456 144.778 161.508 1.00 15.05  ? 4124 LEU A CD1   1 
ATOM   18985 C  CD2   . LEU A 1 4124 ? 147.329 144.103 163.746 1.00 13.83  ? 4124 LEU A CD2   1 
ATOM   18986 N  N     . PHE A 1 4125 ? 148.896 143.064 159.115 1.00 15.98  ? 4125 PHE A N     1 
ATOM   18987 C  CA    . PHE A 1 4125 ? 150.215 143.392 158.594 1.00 12.90  ? 4125 PHE A CA    1 
ATOM   18988 C  C     . PHE A 1 4125 ? 150.587 144.802 159.029 1.00 14.09  ? 4125 PHE A C     1 
ATOM   18989 O  O     . PHE A 1 4125 ? 149.806 145.740 158.840 1.00 18.46  ? 4125 PHE A O     1 
ATOM   18990 C  CB    . PHE A 1 4125 ? 150.247 143.284 157.068 1.00 15.93  ? 4125 PHE A CB    1 
ATOM   18991 C  CG    . PHE A 1 4125 ? 149.882 141.923 156.547 1.00 16.63  ? 4125 PHE A CG    1 
ATOM   18992 C  CD1   . PHE A 1 4125 ? 148.560 141.587 156.312 1.00 16.86  ? 4125 PHE A CD1   1 
ATOM   18993 C  CD2   . PHE A 1 4125 ? 150.863 140.982 156.288 1.00 18.66  ? 4125 PHE A CD2   1 
ATOM   18994 C  CE1   . PHE A 1 4125 ? 148.224 140.338 155.833 1.00 17.74  ? 4125 PHE A CE1   1 
ATOM   18995 C  CE2   . PHE A 1 4125 ? 150.532 139.730 155.809 1.00 19.02  ? 4125 PHE A CE2   1 
ATOM   18996 C  CZ    . PHE A 1 4125 ? 149.211 139.408 155.581 1.00 19.45  ? 4125 PHE A CZ    1 
ATOM   18997 N  N     . LEU A 1 4126 ? 151.773 144.947 159.611 1.00 11.61  ? 4126 LEU A N     1 
ATOM   18998 C  CA    . LEU A 1 4126 ? 152.273 146.239 160.074 1.00 12.64  ? 4126 LEU A CA    1 
ATOM   18999 C  C     . LEU A 1 4126 ? 153.559 146.547 159.316 1.00 15.60  ? 4126 LEU A C     1 
ATOM   19000 O  O     . LEU A 1 4126 ? 154.621 146.003 159.632 1.00 20.01  ? 4126 LEU A O     1 
ATOM   19001 C  CB    . LEU A 1 4126 ? 152.498 146.231 161.584 1.00 13.63  ? 4126 LEU A CB    1 
ATOM   19002 C  CG    . LEU A 1 4126 ? 151.327 145.741 162.436 1.00 13.05  ? 4126 LEU A CG    1 
ATOM   19003 C  CD1   . LEU A 1 4126 ? 151.678 145.783 163.913 1.00 13.92  ? 4126 LEU A CD1   1 
ATOM   19004 C  CD2   . LEU A 1 4126 ? 150.083 146.565 162.158 1.00 14.31  ? 4126 LEU A CD2   1 
ATOM   19005 N  N     . THR A 1 4127 ? 153.460 147.417 158.315 1.00 16.74  ? 4127 THR A N     1 
ATOM   19006 C  CA    . THR A 1 4127 ? 154.615 147.842 157.538 1.00 16.41  ? 4127 THR A CA    1 
ATOM   19007 C  C     . THR A 1 4127 ? 155.329 148.970 158.269 1.00 15.40  ? 4127 THR A C     1 
ATOM   19008 O  O     . THR A 1 4127 ? 154.694 149.939 158.698 1.00 18.05  ? 4127 THR A O     1 
ATOM   19009 C  CB    . THR A 1 4127 ? 154.191 148.299 156.142 1.00 19.43  ? 4127 THR A CB    1 
ATOM   19010 O  OG1   . THR A 1 4127 ? 153.270 147.352 155.586 1.00 22.04  ? 4127 THR A OG1   1 
ATOM   19011 C  CG2   . THR A 1 4127 ? 155.401 148.416 155.230 1.00 26.31  ? 4127 THR A CG2   1 
ATOM   19012 N  N     . MET A 1 4128 ? 156.645 148.843 158.411 1.00 18.30  ? 4128 MET A N     1 
ATOM   19013 C  CA    . MET A 1 4128 ? 157.415 149.836 159.145 1.00 19.18  ? 4128 MET A CA    1 
ATOM   19014 C  C     . MET A 1 4128 ? 158.861 149.801 158.678 1.00 18.75  ? 4128 MET A C     1 
ATOM   19015 O  O     . MET A 1 4128 ? 159.317 148.829 158.071 1.00 20.78  ? 4128 MET A O     1 
ATOM   19016 C  CB    . MET A 1 4128 ? 157.339 149.599 160.656 1.00 20.48  ? 4128 MET A CB    1 
ATOM   19017 C  CG    . MET A 1 4128 ? 158.307 148.546 161.167 1.00 21.27  ? 4128 MET A CG    1 
ATOM   19018 S  SD    . MET A 1 4128 ? 157.808 147.849 162.751 1.00 41.60  ? 4128 MET A SD    1 
ATOM   19019 C  CE    . MET A 1 4128 ? 156.369 146.902 162.266 1.00 16.86  ? 4128 MET A CE    1 
ATOM   19020 N  N     . GLU A 1 4129 ? 159.571 150.885 158.968 1.00 22.12  ? 4129 GLU A N     1 
ATOM   19021 C  CA    . GLU A 1 4129 ? 161.002 150.972 158.732 1.00 21.21  ? 4129 GLU A CA    1 
ATOM   19022 C  C     . GLU A 1 4129 ? 161.752 150.529 159.983 1.00 27.36  ? 4129 GLU A C     1 
ATOM   19023 O  O     . GLU A 1 4129 ? 161.243 150.630 161.102 1.00 33.93  ? 4129 GLU A O     1 
ATOM   19024 C  CB    . GLU A 1 4129 ? 161.396 152.401 158.351 1.00 28.31  ? 4129 GLU A CB    1 
ATOM   19025 C  CG    . GLU A 1 4129 ? 162.810 152.553 157.815 1.00 46.62  ? 4129 GLU A CG    1 
ATOM   19026 C  CD    . GLU A 1 4129 ? 163.455 153.858 158.241 1.00 59.56  ? 4129 GLU A CD    1 
ATOM   19027 O  OE1   . GLU A 1 4129 ? 164.677 154.015 158.034 1.00 64.36  ? 4129 GLU A OE1   1 
ATOM   19028 O  OE2   . GLU A 1 4129 ? 162.740 154.727 158.782 1.00 57.50  ? 4129 GLU A OE2   1 
ATOM   19029 N  N     . ILE A 1 4130 ? 162.970 150.031 159.785 1.00 27.31  ? 4130 ILE A N     1 
ATOM   19030 C  CA    . ILE A 1 4130 ? 163.769 149.531 160.898 1.00 26.88  ? 4130 ILE A CA    1 
ATOM   19031 C  C     . ILE A 1 4130 ? 164.335 150.708 161.680 1.00 31.56  ? 4130 ILE A C     1 
ATOM   19032 O  O     . ILE A 1 4130 ? 165.367 151.280 161.309 1.00 34.36  ? 4130 ILE A O     1 
ATOM   19033 C  CB    . ILE A 1 4130 ? 164.893 148.601 160.407 1.00 21.01  ? 4130 ILE A CB    1 
ATOM   19034 C  CG1   . ILE A 1 4130 ? 164.314 147.465 159.564 1.00 19.74  ? 4130 ILE A CG1   1 
ATOM   19035 C  CG2   . ILE A 1 4130 ? 165.676 148.044 161.585 1.00 19.74  ? 4130 ILE A CG2   1 
ATOM   19036 C  CD1   . ILE A 1 4130 ? 165.338 146.438 159.139 1.00 20.72  ? 4130 ILE A CD1   1 
ATOM   19037 N  N     . ASN A 1 4131 ? 163.660 151.079 162.763 1.00 27.73  ? 4131 ASN A N     1 
ATOM   19038 C  CA    . ASN A 1 4131 ? 164.096 152.143 163.653 1.00 30.99  ? 4131 ASN A CA    1 
ATOM   19039 C  C     . ASN A 1 4131 ? 163.810 151.733 165.089 1.00 29.62  ? 4131 ASN A C     1 
ATOM   19040 O  O     . ASN A 1 4131 ? 162.872 150.967 165.342 1.00 32.09  ? 4131 ASN A O     1 
ATOM   19041 C  CB    . ASN A 1 4131 ? 163.395 153.473 163.330 1.00 35.77  ? 4131 ASN A CB    1 
ATOM   19042 C  CG    . ASN A 1 4131 ? 161.907 153.430 163.603 1.00 40.15  ? 4131 ASN A CG    1 
ATOM   19043 O  OD1   . ASN A 1 4131 ? 161.261 152.398 163.425 1.00 39.78  ? 4131 ASN A OD1   1 
ATOM   19044 N  ND2   . ASN A 1 4131 ? 161.353 154.556 164.032 1.00 38.39  ? 4131 ASN A ND2   1 
ATOM   19045 N  N     . PRO A 1 4132 ? 164.600 152.223 166.050 1.00 25.15  ? 4132 PRO A N     1 
ATOM   19046 C  CA    . PRO A 1 4132 ? 164.431 151.774 167.443 1.00 26.77  ? 4132 PRO A CA    1 
ATOM   19047 C  C     . PRO A 1 4132 ? 163.164 152.278 168.115 1.00 33.79  ? 4132 PRO A C     1 
ATOM   19048 O  O     . PRO A 1 4132 ? 162.867 151.833 169.231 1.00 40.53  ? 4132 PRO A O     1 
ATOM   19049 C  CB    . PRO A 1 4132 ? 165.679 152.324 168.143 1.00 21.57  ? 4132 PRO A CB    1 
ATOM   19050 C  CG    . PRO A 1 4132 ? 166.104 153.477 167.306 1.00 21.96  ? 4132 PRO A CG    1 
ATOM   19051 C  CD    . PRO A 1 4132 ? 165.766 153.109 165.894 1.00 21.54  ? 4132 PRO A CD    1 
ATOM   19052 N  N     . LYS A 1 4133 ? 162.411 153.184 167.487 1.00 35.66  ? 4133 LYS A N     1 
ATOM   19053 C  CA    . LYS A 1 4133 ? 161.202 153.703 168.116 1.00 38.26  ? 4133 LYS A CA    1 
ATOM   19054 C  C     . LYS A 1 4133 ? 160.101 152.655 168.220 1.00 42.83  ? 4133 LYS A C     1 
ATOM   19055 O  O     . LYS A 1 4133 ? 159.172 152.832 169.015 1.00 46.23  ? 4133 LYS A O     1 
ATOM   19056 C  CB    . LYS A 1 4133 ? 160.687 154.923 167.350 1.00 39.77  ? 4133 LYS A CB    1 
ATOM   19057 C  CG    . LYS A 1 4133 ? 161.484 156.195 167.603 1.00 46.45  ? 4133 LYS A CG    1 
ATOM   19058 C  CD    . LYS A 1 4133 ? 160.833 157.419 166.967 1.00 55.43  ? 4133 LYS A CD    1 
ATOM   19059 C  CE    . LYS A 1 4133 ? 160.038 157.062 165.719 1.00 54.93  ? 4133 LYS A CE    1 
ATOM   19060 N  NZ    . LYS A 1 4133 ? 159.693 158.265 164.914 1.00 49.56  ? 4133 LYS A NZ    1 
ATOM   19061 N  N     . VAL A 1 4134 ? 160.179 151.582 167.444 1.00 36.67  ? 4134 VAL A N     1 
ATOM   19062 C  CA    . VAL A 1 4134 ? 159.164 150.524 167.513 1.00 31.56  ? 4134 VAL A CA    1 
ATOM   19063 C  C     . VAL A 1 4134 ? 159.255 149.829 168.868 1.00 32.53  ? 4134 VAL A C     1 
ATOM   19064 O  O     . VAL A 1 4134 ? 160.362 149.450 169.292 1.00 33.71  ? 4134 VAL A O     1 
ATOM   19065 C  CB    . VAL A 1 4134 ? 159.355 149.528 166.368 1.00 31.11  ? 4134 VAL A CB    1 
ATOM   19066 C  CG1   . VAL A 1 4134 ? 158.258 148.477 166.388 1.00 30.76  ? 4134 VAL A CG1   1 
ATOM   19067 C  CG2   . VAL A 1 4134 ? 159.372 150.257 165.035 1.00 28.20  ? 4134 VAL A CG2   1 
ATOM   19068 N  N     . PRO A 1 4135 ? 158.143 149.649 169.581 1.00 28.99  ? 4135 PRO A N     1 
ATOM   19069 C  CA    . PRO A 1 4135 ? 158.209 149.029 170.909 1.00 29.46  ? 4135 PRO A CA    1 
ATOM   19070 C  C     . PRO A 1 4135 ? 158.716 147.595 170.849 1.00 28.99  ? 4135 PRO A C     1 
ATOM   19071 O  O     . PRO A 1 4135 ? 158.482 146.865 169.884 1.00 31.97  ? 4135 PRO A O     1 
ATOM   19072 C  CB    . PRO A 1 4135 ? 156.757 149.086 171.399 1.00 29.87  ? 4135 PRO A CB    1 
ATOM   19073 C  CG    . PRO A 1 4135 ? 156.126 150.173 170.600 1.00 31.96  ? 4135 PRO A CG    1 
ATOM   19074 C  CD    . PRO A 1 4135 ? 156.789 150.128 169.260 1.00 32.02  ? 4135 PRO A CD    1 
ATOM   19075 N  N     . VAL A 1 4136 ? 159.426 147.201 171.908 1.00 26.77  ? 4136 VAL A N     1 
ATOM   19076 C  CA    . VAL A 1 4136 ? 159.959 145.845 171.995 1.00 20.67  ? 4136 VAL A CA    1 
ATOM   19077 C  C     . VAL A 1 4136 ? 158.832 144.834 172.171 1.00 22.02  ? 4136 VAL A C     1 
ATOM   19078 O  O     . VAL A 1 4136 ? 158.880 143.727 171.620 1.00 26.96  ? 4136 VAL A O     1 
ATOM   19079 C  CB    . VAL A 1 4136 ? 160.991 145.759 173.136 1.00 22.32  ? 4136 VAL A CB    1 
ATOM   19080 C  CG1   . VAL A 1 4136 ? 161.286 144.311 173.496 1.00 31.73  ? 4136 VAL A CG1   1 
ATOM   19081 C  CG2   . VAL A 1 4136 ? 162.268 146.487 172.748 1.00 23.57  ? 4136 VAL A CG2   1 
ATOM   19082 N  N     . ASN A 1 4137 ? 157.800 145.196 172.938 1.00 24.40  ? 4137 ASN A N     1 
ATOM   19083 C  CA    . ASN A 1 4137 ? 156.696 144.271 173.174 1.00 29.24  ? 4137 ASN A CA    1 
ATOM   19084 C  C     . ASN A 1 4137 ? 155.952 143.948 171.883 1.00 28.36  ? 4137 ASN A C     1 
ATOM   19085 O  O     . ASN A 1 4137 ? 155.520 142.808 171.677 1.00 28.20  ? 4137 ASN A O     1 
ATOM   19086 C  CB    . ASN A 1 4137 ? 155.749 144.840 174.236 1.00 33.21  ? 4137 ASN A CB    1 
ATOM   19087 C  CG    . ASN A 1 4137 ? 155.079 146.136 173.807 1.00 45.38  ? 4137 ASN A CG    1 
ATOM   19088 O  OD1   . ASN A 1 4137 ? 155.209 146.580 172.668 1.00 50.92  ? 4137 ASN A OD1   1 
ATOM   19089 N  ND2   . ASN A 1 4137 ? 154.352 146.751 174.733 1.00 45.41  ? 4137 ASN A ND2   1 
ATOM   19090 N  N     . LEU A 1 4138 ? 155.791 144.938 171.002 1.00 25.67  ? 4138 LEU A N     1 
ATOM   19091 C  CA    . LEU A 1 4138 ? 155.184 144.673 169.702 1.00 24.14  ? 4138 LEU A CA    1 
ATOM   19092 C  C     . LEU A 1 4138 ? 156.053 143.739 168.870 1.00 23.11  ? 4138 LEU A C     1 
ATOM   19093 O  O     . LEU A 1 4138 ? 155.538 142.852 168.179 1.00 26.32  ? 4138 LEU A O     1 
ATOM   19094 C  CB    . LEU A 1 4138 ? 154.942 145.983 168.954 1.00 27.85  ? 4138 LEU A CB    1 
ATOM   19095 C  CG    . LEU A 1 4138 ? 154.392 145.824 167.535 1.00 22.65  ? 4138 LEU A CG    1 
ATOM   19096 C  CD1   . LEU A 1 4138 ? 152.876 145.703 167.554 1.00 16.22  ? 4138 LEU A CD1   1 
ATOM   19097 C  CD2   . LEU A 1 4138 ? 154.835 146.976 166.651 1.00 27.59  ? 4138 LEU A CD2   1 
ATOM   19098 N  N     . LEU A 1 4139 ? 157.374 143.928 168.919 1.00 20.59  ? 4139 LEU A N     1 
ATOM   19099 C  CA    . LEU A 1 4139 ? 158.276 143.047 168.184 1.00 16.42  ? 4139 LEU A CA    1 
ATOM   19100 C  C     . LEU A 1 4139 ? 158.174 141.613 168.686 1.00 18.51  ? 4139 LEU A C     1 
ATOM   19101 O  O     . LEU A 1 4139 ? 158.181 140.666 167.891 1.00 19.76  ? 4139 LEU A O     1 
ATOM   19102 C  CB    . LEU A 1 4139 ? 159.713 143.555 168.297 1.00 13.50  ? 4139 LEU A CB    1 
ATOM   19103 C  CG    . LEU A 1 4139 ? 160.028 144.893 167.626 1.00 16.98  ? 4139 LEU A CG    1 
ATOM   19104 C  CD1   . LEU A 1 4139 ? 161.453 145.321 167.932 1.00 18.96  ? 4139 LEU A CD1   1 
ATOM   19105 C  CD2   . LEU A 1 4139 ? 159.805 144.809 166.127 1.00 18.72  ? 4139 LEU A CD2   1 
ATOM   19106 N  N     . ARG A 1 4140 ? 158.080 141.433 170.005 1.00 19.50  ? 4140 ARG A N     1 
ATOM   19107 C  CA    . ARG A 1 4140 ? 157.939 140.088 170.554 1.00 17.70  ? 4140 ARG A CA    1 
ATOM   19108 C  C     . ARG A 1 4140 ? 156.570 139.493 170.250 1.00 20.94  ? 4140 ARG A C     1 
ATOM   19109 O  O     . ARG A 1 4140 ? 156.451 138.275 170.078 1.00 20.06  ? 4140 ARG A O     1 
ATOM   19110 C  CB    . ARG A 1 4140 ? 158.183 140.105 172.063 1.00 19.17  ? 4140 ARG A CB    1 
ATOM   19111 C  CG    . ARG A 1 4140 ? 159.557 140.608 172.466 1.00 23.96  ? 4140 ARG A CG    1 
ATOM   19112 C  CD    . ARG A 1 4140 ? 159.747 140.548 173.972 1.00 33.54  ? 4140 ARG A CD    1 
ATOM   19113 N  NE    . ARG A 1 4140 ? 158.988 139.458 174.574 1.00 43.59  ? 4140 ARG A NE    1 
ATOM   19114 C  CZ    . ARG A 1 4140 ? 159.527 138.461 175.263 1.00 45.97  ? 4140 ARG A CZ    1 
ATOM   19115 N  NH1   . ARG A 1 4140 ? 160.833 138.382 175.458 1.00 50.14  ? 4140 ARG A NH1   1 
ATOM   19116 N  NH2   . ARG A 1 4140 ? 158.736 137.520 175.769 1.00 36.15  ? 4140 ARG A NH2   1 
ATOM   19117 N  N     . ALA A 1 4141 ? 155.531 140.328 170.182 1.00 22.86  ? 4141 ALA A N     1 
ATOM   19118 C  CA    . ALA A 1 4141 ? 154.181 139.826 169.951 1.00 20.56  ? 4141 ALA A CA    1 
ATOM   19119 C  C     . ALA A 1 4141 ? 153.989 139.299 168.535 1.00 17.96  ? 4141 ALA A C     1 
ATOM   19120 O  O     . ALA A 1 4141 ? 153.294 138.296 168.344 1.00 21.99  ? 4141 ALA A O     1 
ATOM   19121 C  CB    . ALA A 1 4141 ? 153.156 140.924 170.240 1.00 20.21  ? 4141 ALA A CB    1 
ATOM   19122 N  N     . GLY A 1 4142 ? 154.585 139.953 167.538 1.00 16.79  ? 4142 GLY A N     1 
ATOM   19123 C  CA    . GLY A 1 4142 ? 154.410 139.585 166.153 1.00 17.18  ? 4142 GLY A CA    1 
ATOM   19124 C  C     . GLY A 1 4142 ? 155.627 138.891 165.560 1.00 18.56  ? 4142 GLY A C     1 
ATOM   19125 O  O     . GLY A 1 4142 ? 156.644 138.667 166.211 1.00 27.81  ? 4142 GLY A O     1 
ATOM   19126 N  N     . ARG A 1 4143 ? 155.493 138.551 164.282 1.00 17.60  ? 4143 ARG A N     1 
ATOM   19127 C  CA    . ARG A 1 4143 ? 156.561 137.918 163.521 1.00 17.38  ? 4143 ARG A CA    1 
ATOM   19128 C  C     . ARG A 1 4143 ? 157.215 138.956 162.620 1.00 17.62  ? 4143 ARG A C     1 
ATOM   19129 O  O     . ARG A 1 4143 ? 156.524 139.686 161.902 1.00 21.45  ? 4143 ARG A O     1 
ATOM   19130 C  CB    . ARG A 1 4143 ? 156.031 136.748 162.690 1.00 17.87  ? 4143 ARG A CB    1 
ATOM   19131 C  CG    . ARG A 1 4143 ? 157.117 135.984 161.952 1.00 27.97  ? 4143 ARG A CG    1 
ATOM   19132 C  CD    . ARG A 1 4143 ? 156.762 134.516 161.795 1.00 37.78  ? 4143 ARG A CD    1 
ATOM   19133 N  NE    . ARG A 1 4143 ? 157.696 133.823 160.916 1.00 42.67  ? 4143 ARG A NE    1 
ATOM   19134 C  CZ    . ARG A 1 4143 ? 157.512 132.597 160.446 1.00 48.99  ? 4143 ARG A CZ    1 
ATOM   19135 N  NH1   . ARG A 1 4143 ? 156.436 131.893 160.753 1.00 46.93  ? 4143 ARG A NH1   1 
ATOM   19136 N  NH2   . ARG A 1 4143 ? 158.432 132.066 159.645 1.00 46.76  ? 4143 ARG A NH2   1 
ATOM   19137 N  N     . ILE A 1 4144 ? 158.542 139.012 162.656 1.00 14.60  ? 4144 ILE A N     1 
ATOM   19138 C  CA    . ILE A 1 4144 ? 159.310 140.061 161.998 1.00 12.35  ? 4144 ILE A CA    1 
ATOM   19139 C  C     . ILE A 1 4144 ? 159.838 139.533 160.673 1.00 15.84  ? 4144 ILE A C     1 
ATOM   19140 O  O     . ILE A 1 4144 ? 160.345 138.407 160.600 1.00 18.53  ? 4144 ILE A O     1 
ATOM   19141 C  CB    . ILE A 1 4144 ? 160.459 140.547 162.897 1.00 13.61  ? 4144 ILE A CB    1 
ATOM   19142 C  CG1   . ILE A 1 4144 ? 159.910 140.981 164.256 1.00 16.04  ? 4144 ILE A CG1   1 
ATOM   19143 C  CG2   . ILE A 1 4144 ? 161.210 141.688 162.235 1.00 16.34  ? 4144 ILE A CG2   1 
ATOM   19144 C  CD1   . ILE A 1 4144 ? 160.956 141.071 165.336 1.00 17.87  ? 4144 ILE A CD1   1 
ATOM   19145 N  N     . PHE A 1 4145 ? 159.705 140.341 159.623 1.00 18.58  ? 4145 PHE A N     1 
ATOM   19146 C  CA    . PHE A 1 4145 ? 160.225 140.019 158.298 1.00 15.47  ? 4145 PHE A CA    1 
ATOM   19147 C  C     . PHE A 1 4145 ? 161.033 141.214 157.814 1.00 17.46  ? 4145 PHE A C     1 
ATOM   19148 O  O     . PHE A 1 4145 ? 160.470 142.284 157.566 1.00 20.67  ? 4145 PHE A O     1 
ATOM   19149 C  CB    . PHE A 1 4145 ? 159.095 139.698 157.322 1.00 14.45  ? 4145 PHE A CB    1 
ATOM   19150 C  CG    . PHE A 1 4145 ? 158.434 138.382 157.581 1.00 18.10  ? 4145 PHE A CG    1 
ATOM   19151 C  CD1   . PHE A 1 4145 ? 159.103 137.197 157.339 1.00 22.17  ? 4145 PHE A CD1   1 
ATOM   19152 C  CD2   . PHE A 1 4145 ? 157.145 138.331 158.078 1.00 19.23  ? 4145 PHE A CD2   1 
ATOM   19153 C  CE1   . PHE A 1 4145 ? 158.495 135.985 157.583 1.00 25.57  ? 4145 PHE A CE1   1 
ATOM   19154 C  CE2   . PHE A 1 4145 ? 156.532 137.123 158.323 1.00 20.26  ? 4145 PHE A CE2   1 
ATOM   19155 C  CZ    . PHE A 1 4145 ? 157.208 135.950 158.077 1.00 25.89  ? 4145 PHE A CZ    1 
ATOM   19156 N  N     . VAL A 1 4146 ? 162.342 141.036 157.681 1.00 14.56  ? 4146 VAL A N     1 
ATOM   19157 C  CA    . VAL A 1 4146 ? 163.231 142.108 157.250 1.00 15.50  ? 4146 VAL A CA    1 
ATOM   19158 C  C     . VAL A 1 4146 ? 163.325 142.094 155.732 1.00 19.68  ? 4146 VAL A C     1 
ATOM   19159 O  O     . VAL A 1 4146 ? 163.652 141.065 155.129 1.00 24.05  ? 4146 VAL A O     1 
ATOM   19160 C  CB    . VAL A 1 4146 ? 164.620 141.963 157.891 1.00 14.31  ? 4146 VAL A CB    1 
ATOM   19161 C  CG1   . VAL A 1 4146 ? 165.610 142.898 157.219 1.00 15.43  ? 4146 VAL A CG1   1 
ATOM   19162 C  CG2   . VAL A 1 4146 ? 164.545 142.253 159.378 1.00 15.93  ? 4146 VAL A CG2   1 
ATOM   19163 N  N     . PHE A 1 4147 ? 163.036 143.235 155.114 1.00 20.99  ? 4147 PHE A N     1 
ATOM   19164 C  CA    . PHE A 1 4147 ? 163.128 143.398 153.671 1.00 19.38  ? 4147 PHE A CA    1 
ATOM   19165 C  C     . PHE A 1 4147 ? 164.288 144.326 153.343 1.00 24.24  ? 4147 PHE A C     1 
ATOM   19166 O  O     . PHE A 1 4147 ? 164.408 145.410 153.923 1.00 31.05  ? 4147 PHE A O     1 
ATOM   19167 C  CB    . PHE A 1 4147 ? 161.818 143.938 153.095 1.00 19.04  ? 4147 PHE A CB    1 
ATOM   19168 C  CG    . PHE A 1 4147 ? 160.712 142.927 153.084 1.00 19.43  ? 4147 PHE A CG    1 
ATOM   19169 C  CD1   . PHE A 1 4147 ? 159.993 142.654 154.233 1.00 17.81  ? 4147 PHE A CD1   1 
ATOM   19170 C  CD2   . PHE A 1 4147 ? 160.405 142.233 151.926 1.00 31.11  ? 4147 PHE A CD2   1 
ATOM   19171 C  CE1   . PHE A 1 4147 ? 158.982 141.717 154.225 1.00 21.32  ? 4147 PHE A CE1   1 
ATOM   19172 C  CE2   . PHE A 1 4147 ? 159.395 141.296 151.913 1.00 33.46  ? 4147 PHE A CE2   1 
ATOM   19173 C  CZ    . PHE A 1 4147 ? 158.684 141.037 153.063 1.00 26.04  ? 4147 PHE A CZ    1 
ATOM   19174 N  N     . GLU A 1 4148 ? 165.132 143.894 152.415 1.00 25.46  ? 4148 GLU A N     1 
ATOM   19175 C  CA    . GLU A 1 4148 ? 166.401 144.555 152.144 1.00 29.55  ? 4148 GLU A CA    1 
ATOM   19176 C  C     . GLU A 1 4148 ? 166.879 144.104 150.771 1.00 37.57  ? 4148 GLU A C     1 
ATOM   19177 O  O     . GLU A 1 4148 ? 166.301 143.180 150.181 1.00 37.70  ? 4148 GLU A O     1 
ATOM   19178 C  CB    . GLU A 1 4148 ? 167.434 144.228 153.238 1.00 29.12  ? 4148 GLU A CB    1 
ATOM   19179 C  CG    . GLU A 1 4148 ? 167.836 142.770 153.295 1.00 36.37  ? 4148 GLU A CG    1 
ATOM   19180 C  CD    . GLU A 1 4148 ? 168.799 142.485 154.424 1.00 43.34  ? 4148 GLU A CD    1 
ATOM   19181 O  OE1   . GLU A 1 4148 ? 169.134 143.426 155.172 1.00 43.19  ? 4148 GLU A OE1   1 
ATOM   19182 O  OE2   . GLU A 1 4148 ? 169.212 141.317 154.571 1.00 43.11  ? 4148 GLU A OE2   1 
ATOM   19183 N  N     . PRO A 1 4149 ? 167.909 144.747 150.221 1.00 38.03  ? 4149 PRO A N     1 
ATOM   19184 C  CA    . PRO A 1 4149 ? 168.420 144.337 148.907 1.00 35.09  ? 4149 PRO A CA    1 
ATOM   19185 C  C     . PRO A 1 4149 ? 168.839 142.879 148.908 1.00 35.92  ? 4149 PRO A C     1 
ATOM   19186 O  O     . PRO A 1 4149 ? 169.349 142.369 149.917 1.00 37.36  ? 4149 PRO A O     1 
ATOM   19187 C  CB    . PRO A 1 4149 ? 169.627 145.261 148.696 1.00 35.26  ? 4149 PRO A CB    1 
ATOM   19188 C  CG    . PRO A 1 4149 ? 169.285 146.479 149.455 1.00 37.83  ? 4149 PRO A CG    1 
ATOM   19189 C  CD    . PRO A 1 4149 ? 168.516 146.019 150.662 1.00 35.17  ? 4149 PRO A CD    1 
ATOM   19190 N  N     . PRO A 1 4150 ? 168.619 142.171 147.801 1.00 32.83  ? 4150 PRO A N     1 
ATOM   19191 C  CA    . PRO A 1 4150 ? 168.993 140.763 147.751 1.00 34.20  ? 4150 PRO A CA    1 
ATOM   19192 C  C     . PRO A 1 4150 ? 170.489 140.599 147.919 1.00 36.66  ? 4150 PRO A C     1 
ATOM   19193 O  O     . PRO A 1 4150 ? 171.276 141.485 147.537 1.00 37.59  ? 4150 PRO A O     1 
ATOM   19194 C  CB    . PRO A 1 4150 ? 168.528 140.324 146.355 1.00 29.98  ? 4150 PRO A CB    1 
ATOM   19195 C  CG    . PRO A 1 4150 ? 167.463 141.301 145.990 1.00 32.57  ? 4150 PRO A CG    1 
ATOM   19196 C  CD    . PRO A 1 4150 ? 167.906 142.599 146.587 1.00 35.07  ? 4150 PRO A CD    1 
ATOM   19197 N  N     . PRO A 1 4151 ? 170.930 139.478 148.497 1.00 29.71  ? 4151 PRO A N     1 
ATOM   19198 C  CA    . PRO A 1 4151 ? 172.362 139.323 148.807 1.00 30.15  ? 4151 PRO A CA    1 
ATOM   19199 C  C     . PRO A 1 4151 ? 173.276 139.407 147.597 1.00 34.38  ? 4151 PRO A C     1 
ATOM   19200 O  O     . PRO A 1 4151 ? 174.405 139.896 147.724 1.00 40.50  ? 4151 PRO A O     1 
ATOM   19201 C  CB    . PRO A 1 4151 ? 172.428 137.937 149.465 1.00 30.59  ? 4151 PRO A CB    1 
ATOM   19202 C  CG    . PRO A 1 4151 ? 171.176 137.239 149.033 1.00 29.67  ? 4151 PRO A CG    1 
ATOM   19203 C  CD    . PRO A 1 4151 ? 170.142 138.308 148.914 1.00 28.44  ? 4151 PRO A CD    1 
ATOM   19204 N  N     . GLY A 1 4152 ? 172.833 138.950 146.429 1.00 26.04  ? 4152 GLY A N     1 
ATOM   19205 C  CA    . GLY A 1 4152 ? 173.703 138.945 145.269 1.00 26.46  ? 4152 GLY A CA    1 
ATOM   19206 C  C     . GLY A 1 4152 ? 172.991 139.139 143.947 1.00 24.91  ? 4152 GLY A C     1 
ATOM   19207 O  O     . GLY A 1 4152 ? 171.781 139.381 143.912 1.00 29.73  ? 4152 GLY A O     1 
ATOM   19208 N  N     . VAL A 1 4153 ? 173.744 139.044 142.849 1.00 22.72  ? 4153 VAL A N     1 
ATOM   19209 C  CA    . VAL A 1 4153 ? 173.154 139.199 141.523 1.00 19.84  ? 4153 VAL A CA    1 
ATOM   19210 C  C     . VAL A 1 4153 ? 172.163 138.077 141.243 1.00 20.22  ? 4153 VAL A C     1 
ATOM   19211 O  O     . VAL A 1 4153 ? 171.069 138.315 140.719 1.00 22.16  ? 4153 VAL A O     1 
ATOM   19212 C  CB    . VAL A 1 4153 ? 174.259 139.259 140.453 1.00 20.65  ? 4153 VAL A CB    1 
ATOM   19213 C  CG1   . VAL A 1 4153 ? 173.651 139.275 139.060 1.00 20.44  ? 4153 VAL A CG1   1 
ATOM   19214 C  CG2   . VAL A 1 4153 ? 175.140 140.479 140.667 1.00 19.40  ? 4153 VAL A CG2   1 
ATOM   19215 N  N     . LYS A 1 4154 ? 172.527 136.839 141.585 1.00 21.09  ? 4154 LYS A N     1 
ATOM   19216 C  CA    . LYS A 1 4154 ? 171.642 135.704 141.340 1.00 19.63  ? 4154 LYS A CA    1 
ATOM   19217 C  C     . LYS A 1 4154 ? 170.337 135.847 142.113 1.00 17.84  ? 4154 LYS A C     1 
ATOM   19218 O  O     . LYS A 1 4154 ? 169.247 135.650 141.561 1.00 19.26  ? 4154 LYS A O     1 
ATOM   19219 C  CB    . LYS A 1 4154 ? 172.353 134.404 141.715 1.00 20.24  ? 4154 LYS A CB    1 
ATOM   19220 C  CG    . LYS A 1 4154 ? 171.499 133.157 141.583 1.00 25.42  ? 4154 LYS A CG    1 
ATOM   19221 C  CD    . LYS A 1 4154 ? 172.272 131.926 142.021 1.00 25.82  ? 4154 LYS A CD    1 
ATOM   19222 C  CE    . LYS A 1 4154 ? 171.373 130.707 142.107 1.00 30.24  ? 4154 LYS A CE    1 
ATOM   19223 N  NZ    . LYS A 1 4154 ? 172.124 129.501 142.552 1.00 36.12  ? 4154 LYS A NZ    1 
ATOM   19224 N  N     . ALA A 1 4155 ? 170.430 136.200 143.397 1.00 17.60  ? 4155 ALA A N     1 
ATOM   19225 C  CA    . ALA A 1 4155 ? 169.228 136.381 144.204 1.00 17.40  ? 4155 ALA A CA    1 
ATOM   19226 C  C     . ALA A 1 4155 ? 168.394 137.548 143.695 1.00 19.84  ? 4155 ALA A C     1 
ATOM   19227 O  O     . ALA A 1 4155 ? 167.160 137.483 143.693 1.00 26.23  ? 4155 ALA A O     1 
ATOM   19228 C  CB    . ALA A 1 4155 ? 169.606 136.589 145.670 1.00 20.81  ? 4155 ALA A CB    1 
ATOM   19229 N  N     . ASN A 1 4156 ? 169.050 138.626 143.261 1.00 18.52  ? 4156 ASN A N     1 
ATOM   19230 C  CA    . ASN A 1 4156 ? 168.324 139.777 142.734 1.00 17.93  ? 4156 ASN A CA    1 
ATOM   19231 C  C     . ASN A 1 4156 ? 167.555 139.409 141.471 1.00 19.56  ? 4156 ASN A C     1 
ATOM   19232 O  O     . ASN A 1 4156 ? 166.385 139.777 141.313 1.00 23.74  ? 4156 ASN A O     1 
ATOM   19233 C  CB    . ASN A 1 4156 ? 169.295 140.926 142.465 1.00 18.80  ? 4156 ASN A CB    1 
ATOM   19234 C  CG    . ASN A 1 4156 ? 168.619 142.279 142.497 1.00 22.68  ? 4156 ASN A CG    1 
ATOM   19235 O  OD1   . ASN A 1 4156 ? 167.395 142.373 142.571 1.00 30.21  ? 4156 ASN A OD1   1 
ATOM   19236 N  ND2   . ASN A 1 4156 ? 169.416 143.339 142.451 1.00 21.03  ? 4156 ASN A ND2   1 
ATOM   19237 N  N     . MET A 1 4157 ? 168.197 138.675 140.558 1.00 19.00  ? 4157 MET A N     1 
ATOM   19238 C  CA    . MET A 1 4157 ? 167.515 138.256 139.338 1.00 15.59  ? 4157 MET A CA    1 
ATOM   19239 C  C     . MET A 1 4157 ? 166.377 137.291 139.643 1.00 15.92  ? 4157 MET A C     1 
ATOM   19240 O  O     . MET A 1 4157 ? 165.311 137.362 139.020 1.00 16.02  ? 4157 MET A O     1 
ATOM   19241 C  CB    . MET A 1 4157 ? 168.508 137.625 138.362 1.00 14.72  ? 4157 MET A CB    1 
ATOM   19242 C  CG    . MET A 1 4157 ? 169.645 138.542 137.953 1.00 12.42  ? 4157 MET A CG    1 
ATOM   19243 S  SD    . MET A 1 4157 ? 170.340 138.108 136.350 1.00 19.33  ? 4157 MET A SD    1 
ATOM   19244 C  CE    . MET A 1 4157 ? 168.849 137.931 135.377 1.00 17.05  ? 4157 MET A CE    1 
ATOM   19245 N  N     . LEU A 1 4158 ? 166.583 136.376 140.594 1.00 20.76  ? 4158 LEU A N     1 
ATOM   19246 C  CA    . LEU A 1 4158 ? 165.514 135.457 140.971 1.00 20.19  ? 4158 LEU A CA    1 
ATOM   19247 C  C     . LEU A 1 4158 ? 164.323 136.208 141.553 1.00 22.27  ? 4158 LEU A C     1 
ATOM   19248 O  O     . LEU A 1 4158 ? 163.169 135.907 141.226 1.00 28.91  ? 4158 LEU A O     1 
ATOM   19249 C  CB    . LEU A 1 4158 ? 166.037 134.422 141.965 1.00 19.34  ? 4158 LEU A CB    1 
ATOM   19250 C  CG    . LEU A 1 4158 ? 166.908 133.308 141.382 1.00 19.52  ? 4158 LEU A CG    1 
ATOM   19251 C  CD1   . LEU A 1 4158 ? 167.304 132.315 142.462 1.00 27.67  ? 4158 LEU A CD1   1 
ATOM   19252 C  CD2   . LEU A 1 4158 ? 166.185 132.606 140.244 1.00 25.08  ? 4158 LEU A CD2   1 
ATOM   19253 N  N     . ARG A 1 4159 ? 164.585 137.195 142.414 1.00 19.43  ? 4159 ARG A N     1 
ATOM   19254 C  CA    . ARG A 1 4159 ? 163.506 137.995 142.983 1.00 21.22  ? 4159 ARG A CA    1 
ATOM   19255 C  C     . ARG A 1 4159 ? 162.782 138.789 141.905 1.00 24.32  ? 4159 ARG A C     1 
ATOM   19256 O  O     . ARG A 1 4159 ? 161.550 138.898 141.925 1.00 28.93  ? 4159 ARG A O     1 
ATOM   19257 C  CB    . ARG A 1 4159 ? 164.061 138.930 144.057 1.00 25.66  ? 4159 ARG A CB    1 
ATOM   19258 C  CG    . ARG A 1 4159 ? 163.001 139.650 144.869 1.00 31.34  ? 4159 ARG A CG    1 
ATOM   19259 C  CD    . ARG A 1 4159 ? 163.605 140.275 146.114 1.00 42.10  ? 4159 ARG A CD    1 
ATOM   19260 N  NE    . ARG A 1 4159 ? 164.442 139.329 146.843 1.00 52.63  ? 4159 ARG A NE    1 
ATOM   19261 C  CZ    . ARG A 1 4159 ? 165.072 139.605 147.976 1.00 54.51  ? 4159 ARG A CZ    1 
ATOM   19262 N  NH1   . ARG A 1 4159 ? 164.983 140.796 148.545 1.00 45.91  ? 4159 ARG A NH1   1 
ATOM   19263 N  NH2   . ARG A 1 4159 ? 165.811 138.661 148.553 1.00 47.25  ? 4159 ARG A NH2   1 
ATOM   19264 N  N     . THR A 1 4160 ? 163.532 139.356 140.956 1.00 24.73  ? 4160 THR A N     1 
ATOM   19265 C  CA    . THR A 1 4160 ? 162.911 140.103 139.867 1.00 18.80  ? 4160 THR A CA    1 
ATOM   19266 C  C     . THR A 1 4160 ? 162.021 139.205 139.019 1.00 18.81  ? 4160 THR A C     1 
ATOM   19267 O  O     . THR A 1 4160 ? 160.900 139.587 138.661 1.00 22.79  ? 4160 THR A O     1 
ATOM   19268 C  CB    . THR A 1 4160 ? 163.989 140.759 139.003 1.00 17.87  ? 4160 THR A CB    1 
ATOM   19269 O  OG1   . THR A 1 4160 ? 164.621 141.812 139.741 1.00 16.80  ? 4160 THR A OG1   1 
ATOM   19270 C  CG2   . THR A 1 4160 ? 163.385 141.329 137.728 1.00 15.34  ? 4160 THR A CG2   1 
ATOM   19271 N  N     . PHE A 1 4161 ? 162.496 138.001 138.697 1.00 19.23  ? 4161 PHE A N     1 
ATOM   19272 C  CA    . PHE A 1 4161 ? 161.705 137.093 137.873 1.00 18.98  ? 4161 PHE A CA    1 
ATOM   19273 C  C     . PHE A 1 4161 ? 160.474 136.594 138.620 1.00 25.33  ? 4161 PHE A C     1 
ATOM   19274 O  O     . PHE A 1 4161 ? 159.405 136.428 138.021 1.00 35.77  ? 4161 PHE A O     1 
ATOM   19275 C  CB    . PHE A 1 4161 ? 162.567 135.921 137.406 1.00 20.60  ? 4161 PHE A CB    1 
ATOM   19276 C  CG    . PHE A 1 4161 ? 163.340 136.205 136.150 1.00 23.53  ? 4161 PHE A CG    1 
ATOM   19277 C  CD1   . PHE A 1 4161 ? 162.681 136.497 134.968 1.00 23.75  ? 4161 PHE A CD1   1 
ATOM   19278 C  CD2   . PHE A 1 4161 ? 164.724 136.185 136.153 1.00 23.89  ? 4161 PHE A CD2   1 
ATOM   19279 C  CE1   . PHE A 1 4161 ? 163.388 136.761 133.812 1.00 26.81  ? 4161 PHE A CE1   1 
ATOM   19280 C  CE2   . PHE A 1 4161 ? 165.436 136.449 135.000 1.00 27.44  ? 4161 PHE A CE2   1 
ATOM   19281 C  CZ    . PHE A 1 4161 ? 164.767 136.737 133.828 1.00 32.14  ? 4161 PHE A CZ    1 
ATOM   19282 N  N     . SER A 1 4162 ? 160.603 136.343 139.925 1.00 23.50  ? 4162 SER A N     1 
ATOM   19283 C  CA    . SER A 1 4162 ? 159.448 135.915 140.707 1.00 22.96  ? 4162 SER A CA    1 
ATOM   19284 C  C     . SER A 1 4162 ? 158.414 137.028 140.827 1.00 25.58  ? 4162 SER A C     1 
ATOM   19285 O  O     . SER A 1 4162 ? 157.207 136.770 140.761 1.00 33.08  ? 4162 SER A O     1 
ATOM   19286 C  CB    . SER A 1 4162 ? 159.895 135.447 142.091 1.00 22.77  ? 4162 SER A CB    1 
ATOM   19287 O  OG    . SER A 1 4162 ? 160.042 136.542 142.977 1.00 31.44  ? 4162 SER A OG    1 
ATOM   19288 N  N     . SER A 1 4163 ? 158.868 138.272 141.009 1.00 22.84  ? 4163 SER A N     1 
ATOM   19289 C  CA    . SER A 1 4163 ? 157.938 139.386 141.162 1.00 24.47  ? 4163 SER A CA    1 
ATOM   19290 C  C     . SER A 1 4163 ? 157.130 139.621 139.891 1.00 27.59  ? 4163 SER A C     1 
ATOM   19291 O  O     . SER A 1 4163 ? 155.918 139.854 139.955 1.00 31.40  ? 4163 SER A O     1 
ATOM   19292 C  CB    . SER A 1 4163 ? 158.698 140.652 141.556 1.00 26.46  ? 4163 SER A CB    1 
ATOM   19293 O  OG    . SER A 1 4163 ? 159.304 141.254 140.426 1.00 32.00  ? 4163 SER A OG    1 
ATOM   19294 N  N     . ILE A 1 4164 ? 157.779 139.568 138.736 1.00 26.90  ? 4164 ILE A N     1 
ATOM   19295 C  CA    . ILE A 1 4164 ? 157.070 139.784 137.469 1.00 29.14  ? 4164 ILE A CA    1 
ATOM   19296 C  C     . ILE A 1 4164 ? 156.204 138.566 137.166 1.00 34.04  ? 4164 ILE A C     1 
ATOM   19297 O  O     . ILE A 1 4164 ? 156.699 137.427 137.233 1.00 33.57  ? 4164 ILE A O     1 
ATOM   19298 C  CB    . ILE A 1 4164 ? 158.065 140.048 136.339 1.00 31.64  ? 4164 ILE A CB    1 
ATOM   19299 C  CG1   . ILE A 1 4164 ? 158.960 141.239 136.682 1.00 31.12  ? 4164 ILE A CG1   1 
ATOM   19300 C  CG2   . ILE A 1 4164 ? 157.331 140.301 135.032 1.00 30.04  ? 4164 ILE A CG2   1 
ATOM   19301 C  CD1   . ILE A 1 4164 ? 160.038 141.504 135.656 1.00 29.18  ? 4164 ILE A CD1   1 
ATOM   19302 N  N     . PRO A 1 4165 ? 154.923 138.745 136.841 1.00 40.29  ? 4165 PRO A N     1 
ATOM   19303 C  CA    . PRO A 1 4165 ? 154.078 137.591 136.515 1.00 37.34  ? 4165 PRO A CA    1 
ATOM   19304 C  C     . PRO A 1 4165 ? 154.580 136.862 135.277 1.00 39.95  ? 4165 PRO A C     1 
ATOM   19305 O  O     . PRO A 1 4165 ? 155.166 137.457 134.371 1.00 42.93  ? 4165 PRO A O     1 
ATOM   19306 C  CB    . PRO A 1 4165 ? 152.698 138.215 136.275 1.00 31.37  ? 4165 PRO A CB    1 
ATOM   19307 C  CG    . PRO A 1 4165 ? 152.745 139.533 136.976 1.00 33.11  ? 4165 PRO A CG    1 
ATOM   19308 C  CD    . PRO A 1 4165 ? 154.160 140.003 136.856 1.00 37.32  ? 4165 PRO A CD    1 
ATOM   19309 N  N     . VAL A 1 4166 ? 154.346 135.548 135.256 1.00 41.28  ? 4166 VAL A N     1 
ATOM   19310 C  CA    . VAL A 1 4166 ? 154.789 134.727 134.133 1.00 41.96  ? 4166 VAL A CA    1 
ATOM   19311 C  C     . VAL A 1 4166 ? 154.065 135.131 132.855 1.00 46.56  ? 4166 VAL A C     1 
ATOM   19312 O  O     . VAL A 1 4166 ? 154.666 135.195 131.776 1.00 45.10  ? 4166 VAL A O     1 
ATOM   19313 C  CB    . VAL A 1 4166 ? 154.585 133.234 134.450 1.00 41.05  ? 4166 VAL A CB    1 
ATOM   19314 C  CG1   . VAL A 1 4166 ? 155.160 132.370 133.339 1.00 37.26  ? 4166 VAL A CG1   1 
ATOM   19315 C  CG2   . VAL A 1 4166 ? 155.220 132.886 135.788 1.00 40.65  ? 4166 VAL A CG2   1 
ATOM   19316 N  N     . SER A 1 4167 ? 152.762 135.406 132.955 1.00 49.50  ? 4167 SER A N     1 
ATOM   19317 C  CA    . SER A 1 4167 ? 151.982 135.774 131.779 1.00 48.26  ? 4167 SER A CA    1 
ATOM   19318 C  C     . SER A 1 4167 ? 152.434 137.094 131.170 1.00 49.55  ? 4167 SER A C     1 
ATOM   19319 O  O     . SER A 1 4167 ? 152.227 137.313 129.972 1.00 51.96  ? 4167 SER A O     1 
ATOM   19320 C  CB    . SER A 1 4167 ? 150.497 135.850 132.139 1.00 45.32  ? 4167 SER A CB    1 
ATOM   19321 O  OG    . SER A 1 4167 ? 150.262 136.847 133.118 1.00 52.43  ? 4167 SER A OG    1 
ATOM   19322 N  N     . ARG A 1 4168 ? 153.038 137.980 131.964 1.00 46.00  ? 4168 ARG A N     1 
ATOM   19323 C  CA    . ARG A 1 4168 ? 153.511 139.251 131.424 1.00 42.91  ? 4168 ARG A CA    1 
ATOM   19324 C  C     . ARG A 1 4168 ? 154.717 139.052 130.513 1.00 45.33  ? 4168 ARG A C     1 
ATOM   19325 O  O     . ARG A 1 4168 ? 154.796 139.658 129.438 1.00 47.91  ? 4168 ARG A O     1 
ATOM   19326 C  CB    . ARG A 1 4168 ? 153.850 140.211 132.564 1.00 38.29  ? 4168 ARG A CB    1 
ATOM   19327 C  CG    . ARG A 1 4168 ? 154.502 141.504 132.109 1.00 39.07  ? 4168 ARG A CG    1 
ATOM   19328 C  CD    . ARG A 1 4168 ? 154.601 142.507 133.246 1.00 42.13  ? 4168 ARG A CD    1 
ATOM   19329 N  NE    . ARG A 1 4168 ? 154.417 143.875 132.778 1.00 40.73  ? 4168 ARG A NE    1 
ATOM   19330 C  CZ    . ARG A 1 4168 ? 154.615 144.955 133.521 1.00 41.41  ? 4168 ARG A CZ    1 
ATOM   19331 N  NH1   . ARG A 1 4168 ? 155.010 144.864 134.780 1.00 40.10  ? 4168 ARG A NH1   1 
ATOM   19332 N  NH2   . ARG A 1 4168 ? 154.412 146.156 132.988 1.00 39.15  ? 4168 ARG A NH2   1 
ATOM   19333 N  N     . ILE A 1 4169 ? 155.666 138.210 130.926 1.00 44.23  ? 4169 ILE A N     1 
ATOM   19334 C  CA    . ILE A 1 4169 ? 156.861 137.984 130.121 1.00 40.67  ? 4169 ILE A CA    1 
ATOM   19335 C  C     . ILE A 1 4169 ? 156.519 137.201 128.859 1.00 49.01  ? 4169 ILE A C     1 
ATOM   19336 O  O     . ILE A 1 4169 ? 157.051 137.478 127.777 1.00 48.10  ? 4169 ILE A O     1 
ATOM   19337 C  CB    . ILE A 1 4169 ? 157.939 137.273 130.957 1.00 35.63  ? 4169 ILE A CB    1 
ATOM   19338 C  CG1   . ILE A 1 4169 ? 158.099 137.964 132.312 1.00 34.17  ? 4169 ILE A CG1   1 
ATOM   19339 C  CG2   . ILE A 1 4169 ? 159.262 137.250 130.213 1.00 32.79  ? 4169 ILE A CG2   1 
ATOM   19340 C  CD1   . ILE A 1 4169 ? 159.258 137.443 133.131 1.00 34.39  ? 4169 ILE A CD1   1 
ATOM   19341 N  N     . CYS A 1 4170 ? 155.633 136.216 128.973 1.00 50.85  ? 4170 CYS A N     1 
ATOM   19342 C  CA    . CYS A 1 4170 ? 155.222 135.396 127.835 1.00 56.66  ? 4170 CYS A CA    1 
ATOM   19343 C  C     . CYS A 1 4170 ? 154.074 136.105 127.128 1.00 57.68  ? 4170 CYS A C     1 
ATOM   19344 O  O     . CYS A 1 4170 ? 152.916 136.006 127.541 1.00 61.97  ? 4170 CYS A O     1 
ATOM   19345 C  CB    . CYS A 1 4170 ? 154.819 133.999 128.295 1.00 59.77  ? 4170 CYS A CB    1 
ATOM   19346 S  SG    . CYS A 1 4170 ? 156.173 133.026 128.994 1.00 99.15  ? 4170 CYS A SG    1 
ATOM   19347 N  N     . LYS A 1 4171 ? 154.392 136.819 126.051 1.00 55.47  ? 4171 LYS A N     1 
ATOM   19348 C  CA    . LYS A 1 4171 ? 153.407 137.604 125.319 1.00 57.26  ? 4171 LYS A CA    1 
ATOM   19349 C  C     . LYS A 1 4171 ? 153.616 137.372 123.826 1.00 62.70  ? 4171 LYS A C     1 
ATOM   19350 O  O     . LYS A 1 4171 ? 154.333 136.454 123.415 1.00 64.18  ? 4171 LYS A O     1 
ATOM   19351 C  CB    . LYS A 1 4171 ? 153.501 139.087 125.701 1.00 56.15  ? 4171 LYS A CB    1 
ATOM   19352 C  CG    . LYS A 1 4171 ? 152.661 139.464 126.909 1.00 53.13  ? 4171 LYS A CG    1 
ATOM   19353 C  CD    . LYS A 1 4171 ? 151.188 139.545 126.550 1.00 54.05  ? 4171 LYS A CD    1 
ATOM   19354 C  CE    . LYS A 1 4171 ? 150.941 140.577 125.464 1.00 51.89  ? 4171 LYS A CE    1 
ATOM   19355 N  NZ    . LYS A 1 4171 ? 151.421 141.927 125.865 1.00 47.08  ? 4171 LYS A NZ    1 
ATOM   19356 N  N     . SER A 1 4172 ? 152.971 138.210 123.013 1.00 63.53  ? 4172 SER A N     1 
ATOM   19357 C  CA    . SER A 1 4172 ? 152.978 138.006 121.565 1.00 65.81  ? 4172 SER A CA    1 
ATOM   19358 C  C     . SER A 1 4172 ? 154.379 137.987 120.963 1.00 65.34  ? 4172 SER A C     1 
ATOM   19359 O  O     . SER A 1 4172 ? 154.681 137.053 120.200 1.00 70.56  ? 4172 SER A O     1 
ATOM   19360 C  CB    . SER A 1 4172 ? 152.094 139.064 120.894 1.00 70.58  ? 4172 SER A CB    1 
ATOM   19361 O  OG    . SER A 1 4172 ? 150.773 139.024 121.406 1.00 84.52  ? 4172 SER A OG    1 
ATOM   19362 N  N     . PRO A 1 4173 ? 155.278 138.949 121.245 1.00 61.60  ? 4173 PRO A N     1 
ATOM   19363 C  CA    . PRO A 1 4173 ? 156.631 138.838 120.685 1.00 57.40  ? 4173 PRO A CA    1 
ATOM   19364 C  C     . PRO A 1 4173 ? 157.536 137.973 121.548 1.00 56.21  ? 4173 PRO A C     1 
ATOM   19365 O  O     . PRO A 1 4173 ? 157.649 138.192 122.758 1.00 57.99  ? 4173 PRO A O     1 
ATOM   19366 C  CB    . PRO A 1 4173 ? 157.110 140.292 120.633 1.00 43.58  ? 4173 PRO A CB    1 
ATOM   19367 C  CG    . PRO A 1 4173 ? 156.381 140.968 121.738 1.00 54.52  ? 4173 PRO A CG    1 
ATOM   19368 C  CD    . PRO A 1 4173 ? 155.116 140.192 122.023 1.00 57.28  ? 4173 PRO A CD    1 
ATOM   19369 N  N     . ASN A 1 4174 ? 158.181 136.979 120.932 1.00 53.27  ? 4174 ASN A N     1 
ATOM   19370 C  CA    . ASN A 1 4174 ? 159.070 136.094 121.676 1.00 49.83  ? 4174 ASN A CA    1 
ATOM   19371 C  C     . ASN A 1 4174 ? 160.306 136.816 122.192 1.00 49.03  ? 4174 ASN A C     1 
ATOM   19372 O  O     . ASN A 1 4174 ? 160.942 136.335 123.136 1.00 53.22  ? 4174 ASN A O     1 
ATOM   19373 C  CB    . ASN A 1 4174 ? 159.486 134.910 120.803 1.00 55.70  ? 4174 ASN A CB    1 
ATOM   19374 C  CG    . ASN A 1 4174 ? 158.320 134.012 120.444 1.00 60.88  ? 4174 ASN A CG    1 
ATOM   19375 O  OD1   . ASN A 1 4174 ? 157.194 134.230 120.891 1.00 58.95  ? 4174 ASN A OD1   1 
ATOM   19376 N  ND2   . ASN A 1 4174 ? 158.584 132.994 119.634 1.00 64.02  ? 4174 ASN A ND2   1 
ATOM   19377 N  N     . GLU A 1 4175 ? 160.658 137.956 121.597 1.00 46.21  ? 4175 GLU A N     1 
ATOM   19378 C  CA    . GLU A 1 4175 ? 161.811 138.730 122.038 1.00 39.01  ? 4175 GLU A CA    1 
ATOM   19379 C  C     . GLU A 1 4175 ? 161.564 139.455 123.353 1.00 32.34  ? 4175 GLU A C     1 
ATOM   19380 O  O     . GLU A 1 4175 ? 162.510 140.013 123.919 1.00 35.53  ? 4175 GLU A O     1 
ATOM   19381 C  CB    . GLU A 1 4175 ? 162.208 139.735 120.954 1.00 38.39  ? 4175 GLU A CB    1 
ATOM   19382 C  CG    . GLU A 1 4175 ? 162.857 139.108 119.725 1.00 45.96  ? 4175 GLU A CG    1 
ATOM   19383 C  CD    . GLU A 1 4175 ? 161.873 138.354 118.850 1.00 53.21  ? 4175 GLU A CD    1 
ATOM   19384 O  OE1   . GLU A 1 4175 ? 160.651 138.492 119.065 1.00 58.10  ? 4175 GLU A OE1   1 
ATOM   19385 O  OE2   . GLU A 1 4175 ? 162.324 137.615 117.950 1.00 49.74  ? 4175 GLU A OE2   1 
ATOM   19386 N  N     . ARG A 1 4176 ? 160.322 139.466 123.845 1.00 30.82  ? 4176 ARG A N     1 
ATOM   19387 C  CA    . ARG A 1 4176 ? 160.029 140.123 125.114 1.00 28.28  ? 4176 ARG A CA    1 
ATOM   19388 C  C     . ARG A 1 4176 ? 160.726 139.434 126.279 1.00 26.63  ? 4176 ARG A C     1 
ATOM   19389 O  O     . ARG A 1 4176 ? 161.171 140.102 127.219 1.00 27.04  ? 4176 ARG A O     1 
ATOM   19390 C  CB    . ARG A 1 4176 ? 158.517 140.164 125.341 1.00 35.49  ? 4176 ARG A CB    1 
ATOM   19391 C  CG    . ARG A 1 4176 ? 158.095 140.804 126.652 1.00 40.29  ? 4176 ARG A CG    1 
ATOM   19392 C  CD    . ARG A 1 4176 ? 156.583 140.860 126.768 1.00 40.83  ? 4176 ARG A CD    1 
ATOM   19393 N  NE    . ARG A 1 4176 ? 155.964 141.345 125.541 1.00 45.64  ? 4176 ARG A NE    1 
ATOM   19394 C  CZ    . ARG A 1 4176 ? 155.202 142.427 125.462 1.00 42.84  ? 4176 ARG A CZ    1 
ATOM   19395 N  NH1   . ARG A 1 4176 ? 154.934 143.163 126.529 1.00 39.31  ? 4176 ARG A NH1   1 
ATOM   19396 N  NH2   . ARG A 1 4176 ? 154.695 142.780 124.285 1.00 44.75  ? 4176 ARG A NH2   1 
ATOM   19397 N  N     . ALA A 1 4177 ? 160.828 138.103 126.239 1.00 30.65  ? 4177 ALA A N     1 
ATOM   19398 C  CA    . ALA A 1 4177 ? 161.492 137.378 127.317 1.00 27.10  ? 4177 ALA A CA    1 
ATOM   19399 C  C     . ALA A 1 4177 ? 162.962 137.763 127.422 1.00 26.96  ? 4177 ALA A C     1 
ATOM   19400 O  O     . ALA A 1 4177 ? 163.487 137.943 128.527 1.00 30.74  ? 4177 ALA A O     1 
ATOM   19401 C  CB    . ALA A 1 4177 ? 161.345 135.872 127.107 1.00 34.22  ? 4177 ALA A CB    1 
ATOM   19402 N  N     . ARG A 1 4178 ? 163.645 137.893 126.282 1.00 25.55  ? 4178 ARG A N     1 
ATOM   19403 C  CA    . ARG A 1 4178 ? 165.046 138.300 126.310 1.00 22.71  ? 4178 ARG A CA    1 
ATOM   19404 C  C     . ARG A 1 4178 ? 165.194 139.736 126.795 1.00 21.04  ? 4178 ARG A C     1 
ATOM   19405 O  O     . ARG A 1 4178 ? 166.144 140.056 127.519 1.00 22.76  ? 4178 ARG A O     1 
ATOM   19406 C  CB    . ARG A 1 4178 ? 165.673 138.133 124.927 1.00 28.79  ? 4178 ARG A CB    1 
ATOM   19407 C  CG    . ARG A 1 4178 ? 167.185 138.006 124.953 1.00 30.50  ? 4178 ARG A CG    1 
ATOM   19408 C  CD    . ARG A 1 4178 ? 167.683 137.207 123.765 1.00 36.78  ? 4178 ARG A CD    1 
ATOM   19409 N  NE    . ARG A 1 4178 ? 169.080 136.819 123.909 1.00 41.17  ? 4178 ARG A NE    1 
ATOM   19410 C  CZ    . ARG A 1 4178 ? 169.531 135.583 123.749 1.00 50.46  ? 4178 ARG A CZ    1 
ATOM   19411 N  NH1   . ARG A 1 4178 ? 168.719 134.586 123.439 1.00 46.68  ? 4178 ARG A NH1   1 
ATOM   19412 N  NH2   . ARG A 1 4178 ? 170.830 135.341 123.902 1.00 55.98  ? 4178 ARG A NH2   1 
ATOM   19413 N  N     . LEU A 1 4179 ? 164.270 140.616 126.403 1.00 24.17  ? 4179 LEU A N     1 
ATOM   19414 C  CA    . LEU A 1 4179 ? 164.303 141.988 126.901 1.00 18.07  ? 4179 LEU A CA    1 
ATOM   19415 C  C     . LEU A 1 4179 ? 164.098 142.029 128.409 1.00 15.73  ? 4179 LEU A C     1 
ATOM   19416 O  O     . LEU A 1 4179 ? 164.777 142.783 129.115 1.00 20.19  ? 4179 LEU A O     1 
ATOM   19417 C  CB    . LEU A 1 4179 ? 163.242 142.830 126.192 1.00 18.24  ? 4179 LEU A CB    1 
ATOM   19418 C  CG    . LEU A 1 4179 ? 163.505 143.157 124.722 1.00 19.68  ? 4179 LEU A CG    1 
ATOM   19419 C  CD1   . LEU A 1 4179 ? 162.623 144.305 124.264 1.00 21.41  ? 4179 LEU A CD1   1 
ATOM   19420 C  CD2   . LEU A 1 4179 ? 164.972 143.483 124.501 1.00 20.56  ? 4179 LEU A CD2   1 
ATOM   19421 N  N     . TYR A 1 4180 ? 163.170 141.219 128.922 1.00 18.49  ? 4180 TYR A N     1 
ATOM   19422 C  CA    . TYR A 1 4180 ? 162.957 141.160 130.364 1.00 19.28  ? 4180 TYR A CA    1 
ATOM   19423 C  C     . TYR A 1 4180 ? 164.174 140.594 131.084 1.00 19.91  ? 4180 TYR A C     1 
ATOM   19424 O  O     . TYR A 1 4180 ? 164.518 141.049 132.179 1.00 21.16  ? 4180 TYR A O     1 
ATOM   19425 C  CB    . TYR A 1 4180 ? 161.711 140.336 130.679 1.00 22.51  ? 4180 TYR A CB    1 
ATOM   19426 C  CG    . TYR A 1 4180 ? 160.455 141.164 130.799 1.00 25.09  ? 4180 TYR A CG    1 
ATOM   19427 C  CD1   . TYR A 1 4180 ? 159.874 141.746 129.683 1.00 23.89  ? 4180 TYR A CD1   1 
ATOM   19428 C  CD2   . TYR A 1 4180 ? 159.854 141.369 132.032 1.00 32.64  ? 4180 TYR A CD2   1 
ATOM   19429 C  CE1   . TYR A 1 4180 ? 158.727 142.505 129.791 1.00 26.44  ? 4180 TYR A CE1   1 
ATOM   19430 C  CE2   . TYR A 1 4180 ? 158.708 142.126 132.150 1.00 32.00  ? 4180 TYR A CE2   1 
ATOM   19431 C  CZ    . TYR A 1 4180 ? 158.149 142.692 131.028 1.00 31.89  ? 4180 TYR A CZ    1 
ATOM   19432 O  OH    . TYR A 1 4180 ? 157.007 143.446 131.147 1.00 38.45  ? 4180 TYR A OH    1 
ATOM   19433 N  N     . PHE A 1 4181 ? 164.834 139.595 130.494 1.00 19.35  ? 4181 PHE A N     1 
ATOM   19434 C  CA    . PHE A 1 4181 ? 166.052 139.065 131.100 1.00 18.10  ? 4181 PHE A CA    1 
ATOM   19435 C  C     . PHE A 1 4181 ? 167.159 140.112 131.127 1.00 20.28  ? 4181 PHE A C     1 
ATOM   19436 O  O     . PHE A 1 4181 ? 167.882 140.233 132.124 1.00 22.73  ? 4181 PHE A O     1 
ATOM   19437 C  CB    . PHE A 1 4181 ? 166.520 137.818 130.353 1.00 21.70  ? 4181 PHE A CB    1 
ATOM   19438 C  CG    . PHE A 1 4181 ? 167.874 137.333 130.784 1.00 23.94  ? 4181 PHE A CG    1 
ATOM   19439 C  CD1   . PHE A 1 4181 ? 168.012 136.535 131.907 1.00 24.40  ? 4181 PHE A CD1   1 
ATOM   19440 C  CD2   . PHE A 1 4181 ? 169.009 137.679 130.071 1.00 24.29  ? 4181 PHE A CD2   1 
ATOM   19441 C  CE1   . PHE A 1 4181 ? 169.255 136.093 132.308 1.00 27.25  ? 4181 PHE A CE1   1 
ATOM   19442 C  CE2   . PHE A 1 4181 ? 170.253 137.241 130.469 1.00 24.42  ? 4181 PHE A CE2   1 
ATOM   19443 C  CZ    . PHE A 1 4181 ? 170.376 136.446 131.588 1.00 24.89  ? 4181 PHE A CZ    1 
ATOM   19444 N  N     . LEU A 1 4182 ? 167.319 140.862 130.035 1.00 20.75  ? 4182 LEU A N     1 
ATOM   19445 C  CA    . LEU A 1 4182 ? 168.312 141.930 130.009 1.00 15.79  ? 4182 LEU A CA    1 
ATOM   19446 C  C     . LEU A 1 4182 ? 167.992 142.992 131.049 1.00 16.20  ? 4182 LEU A C     1 
ATOM   19447 O  O     . LEU A 1 4182 ? 168.892 143.508 131.718 1.00 20.76  ? 4182 LEU A O     1 
ATOM   19448 C  CB    . LEU A 1 4182 ? 168.381 142.552 128.616 1.00 15.22  ? 4182 LEU A CB    1 
ATOM   19449 C  CG    . LEU A 1 4182 ? 169.165 141.781 127.555 1.00 20.00  ? 4182 LEU A CG    1 
ATOM   19450 C  CD1   . LEU A 1 4182 ? 168.977 142.427 126.197 1.00 19.97  ? 4182 LEU A CD1   1 
ATOM   19451 C  CD2   . LEU A 1 4182 ? 170.638 141.714 127.922 1.00 25.40  ? 4182 LEU A CD2   1 
ATOM   19452 N  N     . LEU A 1 4183 ? 166.710 143.328 131.197 1.00 14.09  ? 4183 LEU A N     1 
ATOM   19453 C  CA    . LEU A 1 4183 ? 166.301 144.279 132.224 1.00 12.61  ? 4183 LEU A CA    1 
ATOM   19454 C  C     . LEU A 1 4183 ? 166.610 143.762 133.622 1.00 13.58  ? 4183 LEU A C     1 
ATOM   19455 O  O     . LEU A 1 4183 ? 167.082 144.516 134.479 1.00 16.21  ? 4183 LEU A O     1 
ATOM   19456 C  CB    . LEU A 1 4183 ? 164.813 144.585 132.079 1.00 15.09  ? 4183 LEU A CB    1 
ATOM   19457 C  CG    . LEU A 1 4183 ? 164.262 145.569 133.101 1.00 20.05  ? 4183 LEU A CG    1 
ATOM   19458 C  CD1   . LEU A 1 4183 ? 164.990 146.875 132.975 1.00 21.39  ? 4183 LEU A CD1   1 
ATOM   19459 C  CD2   . LEU A 1 4183 ? 162.780 145.765 132.868 1.00 21.10  ? 4183 LEU A CD2   1 
ATOM   19460 N  N     . ALA A 1 4184 ? 166.343 142.480 133.875 1.00 13.33  ? 4184 ALA A N     1 
ATOM   19461 C  CA    . ALA A 1 4184 ? 166.632 141.909 135.185 1.00 14.00  ? 4184 ALA A CA    1 
ATOM   19462 C  C     . ALA A 1 4184 ? 168.127 141.925 135.474 1.00 12.47  ? 4184 ALA A C     1 
ATOM   19463 O  O     . ALA A 1 4184 ? 168.549 142.272 136.584 1.00 13.25  ? 4184 ALA A O     1 
ATOM   19464 C  CB    . ALA A 1 4184 ? 166.083 140.486 135.272 1.00 15.60  ? 4184 ALA A CB    1 
ATOM   19465 N  N     . TRP A 1 4185 ? 168.946 141.560 134.484 1.00 12.15  ? 4185 TRP A N     1 
ATOM   19466 C  CA    . TRP A 1 4185 ? 170.393 141.595 134.673 1.00 11.37  ? 4185 TRP A CA    1 
ATOM   19467 C  C     . TRP A 1 4185 ? 170.885 143.017 134.908 1.00 12.82  ? 4185 TRP A C     1 
ATOM   19468 O  O     . TRP A 1 4185 ? 171.739 143.251 135.770 1.00 14.60  ? 4185 TRP A O     1 
ATOM   19469 C  CB    . TRP A 1 4185 ? 171.099 140.975 133.467 1.00 10.45  ? 4185 TRP A CB    1 
ATOM   19470 C  CG    . TRP A 1 4185 ? 172.591 141.115 133.515 1.00 14.89  ? 4185 TRP A CG    1 
ATOM   19471 C  CD1   . TRP A 1 4185 ? 173.340 142.103 132.947 1.00 16.10  ? 4185 TRP A CD1   1 
ATOM   19472 C  CD2   . TRP A 1 4185 ? 173.516 140.239 134.171 1.00 16.82  ? 4185 TRP A CD2   1 
ATOM   19473 N  NE1   . TRP A 1 4185 ? 174.673 141.897 133.207 1.00 20.09  ? 4185 TRP A NE1   1 
ATOM   19474 C  CE2   . TRP A 1 4185 ? 174.807 140.759 133.957 1.00 20.14  ? 4185 TRP A CE2   1 
ATOM   19475 C  CE3   . TRP A 1 4185 ? 173.377 139.065 134.918 1.00 16.33  ? 4185 TRP A CE3   1 
ATOM   19476 C  CZ2   . TRP A 1 4185 ? 175.951 140.146 134.462 1.00 21.63  ? 4185 TRP A CZ2   1 
ATOM   19477 C  CZ3   . TRP A 1 4185 ? 174.515 138.459 135.418 1.00 17.75  ? 4185 TRP A CZ3   1 
ATOM   19478 C  CH2   . TRP A 1 4185 ? 175.784 139.000 135.188 1.00 21.87  ? 4185 TRP A CH2   1 
ATOM   19479 N  N     . PHE A 1 4186 ? 170.359 143.980 134.147 1.00 12.47  ? 4186 PHE A N     1 
ATOM   19480 C  CA    . PHE A 1 4186 ? 170.750 145.374 134.323 1.00 11.27  ? 4186 PHE A CA    1 
ATOM   19481 C  C     . PHE A 1 4186 ? 170.386 145.874 135.714 1.00 10.86  ? 4186 PHE A C     1 
ATOM   19482 O  O     . PHE A 1 4186 ? 171.189 146.537 136.378 1.00 13.61  ? 4186 PHE A O     1 
ATOM   19483 C  CB    . PHE A 1 4186 ? 170.086 146.233 133.245 1.00 12.16  ? 4186 PHE A CB    1 
ATOM   19484 C  CG    . PHE A 1 4186 ? 170.248 147.711 133.456 1.00 13.35  ? 4186 PHE A CG    1 
ATOM   19485 C  CD1   . PHE A 1 4186 ? 171.449 148.337 133.173 1.00 13.95  ? 4186 PHE A CD1   1 
ATOM   19486 C  CD2   . PHE A 1 4186 ? 169.195 148.475 133.929 1.00 12.39  ? 4186 PHE A CD2   1 
ATOM   19487 C  CE1   . PHE A 1 4186 ? 171.597 149.697 133.362 1.00 13.46  ? 4186 PHE A CE1   1 
ATOM   19488 C  CE2   . PHE A 1 4186 ? 169.338 149.834 134.121 1.00 13.18  ? 4186 PHE A CE2   1 
ATOM   19489 C  CZ    . PHE A 1 4186 ? 170.540 150.446 133.837 1.00 13.62  ? 4186 PHE A CZ    1 
ATOM   19490 N  N     . HIS A 1 4187 ? 169.172 145.561 136.172 1.00 9.32   ? 4187 HIS A N     1 
ATOM   19491 C  CA    . HIS A 1 4187 ? 168.748 145.980 137.503 1.00 7.99   ? 4187 HIS A CA    1 
ATOM   19492 C  C     . HIS A 1 4187 ? 169.601 145.329 138.582 1.00 11.91  ? 4187 HIS A C     1 
ATOM   19493 O  O     . HIS A 1 4187 ? 169.957 145.975 139.574 1.00 13.87  ? 4187 HIS A O     1 
ATOM   19494 C  CB    . HIS A 1 4187 ? 167.271 145.646 137.710 1.00 9.77   ? 4187 HIS A CB    1 
ATOM   19495 C  CG    . HIS A 1 4187 ? 166.689 146.234 138.957 1.00 12.00  ? 4187 HIS A CG    1 
ATOM   19496 N  ND1   . HIS A 1 4187 ? 166.486 147.588 139.118 1.00 14.16  ? 4187 HIS A ND1   1 
ATOM   19497 C  CD2   . HIS A 1 4187 ? 166.266 145.652 140.104 1.00 15.45  ? 4187 HIS A CD2   1 
ATOM   19498 C  CE1   . HIS A 1 4187 ? 165.964 147.814 140.309 1.00 16.05  ? 4187 HIS A CE1   1 
ATOM   19499 N  NE2   . HIS A 1 4187 ? 165.819 146.656 140.928 1.00 16.45  ? 4187 HIS A NE2   1 
ATOM   19500 N  N     . ALA A 1 4188 ? 169.937 144.049 138.408 1.00 12.85  ? 4188 ALA A N     1 
ATOM   19501 C  CA    . ALA A 1 4188 ? 170.792 143.373 139.378 1.00 10.99  ? 4188 ALA A CA    1 
ATOM   19502 C  C     . ALA A 1 4188 ? 172.175 144.007 139.433 1.00 12.32  ? 4188 ALA A C     1 
ATOM   19503 O  O     . ALA A 1 4188 ? 172.724 144.218 140.519 1.00 16.34  ? 4188 ALA A O     1 
ATOM   19504 C  CB    . ALA A 1 4188 ? 170.897 141.887 139.038 1.00 13.07  ? 4188 ALA A CB    1 
ATOM   19505 N  N     . ILE A 1 4189 ? 172.752 144.322 138.272 1.00 11.85  ? 4189 ILE A N     1 
ATOM   19506 C  CA    . ILE A 1 4189 ? 174.083 144.922 138.247 1.00 11.47  ? 4189 ILE A CA    1 
ATOM   19507 C  C     . ILE A 1 4189 ? 174.059 146.311 138.873 1.00 11.74  ? 4189 ILE A C     1 
ATOM   19508 O  O     . ILE A 1 4189 ? 174.935 146.660 139.673 1.00 12.79  ? 4189 ILE A O     1 
ATOM   19509 C  CB    . ILE A 1 4189 ? 174.631 144.957 136.809 1.00 11.55  ? 4189 ILE A CB    1 
ATOM   19510 C  CG1   . ILE A 1 4189 ? 174.802 143.539 136.262 1.00 13.87  ? 4189 ILE A CG1   1 
ATOM   19511 C  CG2   . ILE A 1 4189 ? 175.952 145.706 136.759 1.00 13.16  ? 4189 ILE A CG2   1 
ATOM   19512 C  CD1   . ILE A 1 4189 ? 175.583 142.617 137.166 1.00 15.09  ? 4189 ILE A CD1   1 
ATOM   19513 N  N     . ILE A 1 4190 ? 173.060 147.125 138.523 1.00 11.66  ? 4190 ILE A N     1 
ATOM   19514 C  CA    . ILE A 1 4190 ? 172.983 148.484 139.054 1.00 9.21   ? 4190 ILE A CA    1 
ATOM   19515 C  C     . ILE A 1 4190 ? 172.757 148.464 140.561 1.00 10.77  ? 4190 ILE A C     1 
ATOM   19516 O  O     . ILE A 1 4190 ? 173.401 149.209 141.309 1.00 13.35  ? 4190 ILE A O     1 
ATOM   19517 C  CB    . ILE A 1 4190 ? 171.884 149.280 138.325 1.00 9.62   ? 4190 ILE A CB    1 
ATOM   19518 C  CG1   . ILE A 1 4190 ? 172.214 149.412 136.838 1.00 14.21  ? 4190 ILE A CG1   1 
ATOM   19519 C  CG2   . ILE A 1 4190 ? 171.713 150.647 138.945 1.00 13.74  ? 4190 ILE A CG2   1 
ATOM   19520 C  CD1   . ILE A 1 4190 ? 173.644 149.806 136.563 1.00 18.52  ? 4190 ILE A CD1   1 
ATOM   19521 N  N     . GLN A 1 4191 ? 171.844 147.612 141.031 1.00 12.65  ? 4191 GLN A N     1 
ATOM   19522 C  CA    . GLN A 1 4191 ? 171.507 147.592 142.448 1.00 11.77  ? 4191 GLN A CA    1 
ATOM   19523 C  C     . GLN A 1 4191 ? 172.599 146.953 143.297 1.00 13.00  ? 4191 GLN A C     1 
ATOM   19524 O  O     . GLN A 1 4191 ? 172.782 147.344 144.455 1.00 13.70  ? 4191 GLN A O     1 
ATOM   19525 C  CB    . GLN A 1 4191 ? 170.182 146.859 142.659 1.00 11.34  ? 4191 GLN A CB    1 
ATOM   19526 C  CG    . GLN A 1 4191 ? 169.374 147.372 143.837 1.00 19.39  ? 4191 GLN A CG    1 
ATOM   19527 C  CD    . GLN A 1 4191 ? 167.974 146.797 143.875 1.00 27.11  ? 4191 GLN A CD    1 
ATOM   19528 O  OE1   . GLN A 1 4191 ? 167.621 145.939 143.068 1.00 23.77  ? 4191 GLN A OE1   1 
ATOM   19529 N  NE2   . GLN A 1 4191 ? 167.168 147.268 144.818 1.00 33.02  ? 4191 GLN A NE2   1 
ATOM   19530 N  N     . GLU A 1 4192 ? 173.326 145.974 142.753 1.00 14.58  ? 4192 GLU A N     1 
ATOM   19531 C  CA    . GLU A 1 4192 ? 174.381 145.332 143.529 1.00 14.67  ? 4192 GLU A CA    1 
ATOM   19532 C  C     . GLU A 1 4192 ? 175.609 146.223 143.660 1.00 15.73  ? 4192 GLU A C     1 
ATOM   19533 O  O     . GLU A 1 4192 ? 176.386 146.066 144.608 1.00 21.05  ? 4192 GLU A O     1 
ATOM   19534 C  CB    . GLU A 1 4192 ? 174.764 143.994 142.899 1.00 13.20  ? 4192 GLU A CB    1 
ATOM   19535 C  CG    . GLU A 1 4192 ? 173.794 142.868 143.206 1.00 21.24  ? 4192 GLU A CG    1 
ATOM   19536 C  CD    . GLU A 1 4192 ? 173.568 142.683 144.692 1.00 43.58  ? 4192 GLU A CD    1 
ATOM   19537 O  OE1   . GLU A 1 4192 ? 174.501 142.221 145.383 1.00 42.26  ? 4192 GLU A OE1   1 
ATOM   19538 O  OE2   . GLU A 1 4192 ? 172.458 142.999 145.172 1.00 42.28  ? 4192 GLU A OE2   1 
ATOM   19539 N  N     . ARG A 1 4193 ? 175.806 147.154 142.724 1.00 12.84  ? 4193 ARG A N     1 
ATOM   19540 C  CA    . ARG A 1 4193 ? 176.929 148.079 142.822 1.00 11.91  ? 4193 ARG A CA    1 
ATOM   19541 C  C     . ARG A 1 4193 ? 176.762 149.075 143.961 1.00 16.62  ? 4193 ARG A C     1 
ATOM   19542 O  O     . ARG A 1 4193 ? 177.743 149.712 144.357 1.00 23.40  ? 4193 ARG A O     1 
ATOM   19543 C  CB    . ARG A 1 4193 ? 177.116 148.832 141.504 1.00 11.61  ? 4193 ARG A CB    1 
ATOM   19544 C  CG    . ARG A 1 4193 ? 177.759 148.010 140.403 1.00 12.17  ? 4193 ARG A CG    1 
ATOM   19545 C  CD    . ARG A 1 4193 ? 177.935 148.826 139.134 1.00 13.75  ? 4193 ARG A CD    1 
ATOM   19546 N  NE    . ARG A 1 4193 ? 178.983 149.831 139.271 1.00 13.63  ? 4193 ARG A NE    1 
ATOM   19547 C  CZ    . ARG A 1 4193 ? 180.164 149.767 138.672 1.00 11.91  ? 4193 ARG A CZ    1 
ATOM   19548 N  NH1   . ARG A 1 4193 ? 180.484 148.757 137.881 1.00 14.44  ? 4193 ARG A NH1   1 
ATOM   19549 N  NH2   . ARG A 1 4193 ? 181.046 150.742 138.872 1.00 12.20  ? 4193 ARG A NH2   1 
ATOM   19550 N  N     . LEU A 1 4194 ? 175.546 149.226 144.491 1.00 15.64  ? 4194 LEU A N     1 
ATOM   19551 C  CA    . LEU A 1 4194 ? 175.314 150.165 145.582 1.00 13.23  ? 4194 LEU A CA    1 
ATOM   19552 C  C     . LEU A 1 4194 ? 175.974 149.722 146.881 1.00 19.29  ? 4194 LEU A C     1 
ATOM   19553 O  O     . LEU A 1 4194 ? 176.174 150.555 147.772 1.00 21.55  ? 4194 LEU A O     1 
ATOM   19554 C  CB    . LEU A 1 4194 ? 173.813 150.356 145.798 1.00 13.37  ? 4194 LEU A CB    1 
ATOM   19555 C  CG    . LEU A 1 4194 ? 173.079 151.161 144.725 1.00 13.65  ? 4194 LEU A CG    1 
ATOM   19556 C  CD1   . LEU A 1 4194 ? 171.577 150.963 144.834 1.00 13.50  ? 4194 LEU A CD1   1 
ATOM   19557 C  CD2   . LEU A 1 4194 ? 173.437 152.634 144.824 1.00 18.42  ? 4194 LEU A CD2   1 
ATOM   19558 N  N     . ARG A 1 4195 ? 176.305 148.436 147.016 1.00 18.53  ? 4195 ARG A N     1 
ATOM   19559 C  CA    . ARG A 1 4195 ? 177.027 147.980 148.200 1.00 18.79  ? 4195 ARG A CA    1 
ATOM   19560 C  C     . ARG A 1 4195 ? 178.406 148.620 148.275 1.00 21.11  ? 4195 ARG A C     1 
ATOM   19561 O  O     . ARG A 1 4195 ? 178.853 149.032 149.352 1.00 28.05  ? 4195 ARG A O     1 
ATOM   19562 C  CB    . ARG A 1 4195 ? 177.143 146.457 148.190 1.00 18.29  ? 4195 ARG A CB    1 
ATOM   19563 C  CG    . ARG A 1 4195 ? 175.849 145.741 147.856 1.00 22.26  ? 4195 ARG A CG    1 
ATOM   19564 C  CD    . ARG A 1 4195 ? 175.972 144.244 148.080 1.00 30.87  ? 4195 ARG A CD    1 
ATOM   19565 N  NE    . ARG A 1 4195 ? 174.678 143.576 148.009 1.00 31.84  ? 4195 ARG A NE    1 
ATOM   19566 C  CZ    . ARG A 1 4195 ? 173.774 143.589 148.978 1.00 36.20  ? 4195 ARG A CZ    1 
ATOM   19567 N  NH1   . ARG A 1 4195 ? 173.992 144.221 150.120 1.00 37.53  ? 4195 ARG A NH1   1 
ATOM   19568 N  NH2   . ARG A 1 4195 ? 172.621 142.952 148.798 1.00 38.92  ? 4195 ARG A NH2   1 
ATOM   19569 N  N     . TYR A 1 4196 ? 179.095 148.709 147.140 1.00 16.92  ? 4196 TYR A N     1 
ATOM   19570 C  CA    . TYR A 1 4196 ? 180.374 149.410 147.048 1.00 19.00  ? 4196 TYR A CA    1 
ATOM   19571 C  C     . TYR A 1 4196 ? 180.099 150.866 146.670 1.00 23.44  ? 4196 TYR A C     1 
ATOM   19572 O  O     . TYR A 1 4196 ? 180.318 151.313 145.543 1.00 26.08  ? 4196 TYR A O     1 
ATOM   19573 C  CB    . TYR A 1 4196 ? 181.283 148.710 146.048 1.00 19.27  ? 4196 TYR A CB    1 
ATOM   19574 C  CG    . TYR A 1 4196 ? 181.118 147.207 146.071 1.00 23.57  ? 4196 TYR A CG    1 
ATOM   19575 C  CD1   . TYR A 1 4196 ? 180.515 146.540 145.015 1.00 22.72  ? 4196 TYR A CD1   1 
ATOM   19576 C  CD2   . TYR A 1 4196 ? 181.549 146.457 147.156 1.00 28.14  ? 4196 TYR A CD2   1 
ATOM   19577 C  CE1   . TYR A 1 4196 ? 180.355 145.169 145.034 1.00 19.86  ? 4196 TYR A CE1   1 
ATOM   19578 C  CE2   . TYR A 1 4196 ? 181.393 145.084 147.183 1.00 29.28  ? 4196 TYR A CE2   1 
ATOM   19579 C  CZ    . TYR A 1 4196 ? 180.795 144.446 146.119 1.00 24.08  ? 4196 TYR A CZ    1 
ATOM   19580 O  OH    . TYR A 1 4196 ? 180.636 143.080 146.139 1.00 33.37  ? 4196 TYR A OH    1 
ATOM   19581 N  N     . ALA A 1 4197 ? 179.599 151.602 147.663 1.00 25.76  ? 4197 ALA A N     1 
ATOM   19582 C  CA    . ALA A 1 4197 ? 179.024 152.924 147.416 1.00 24.36  ? 4197 ALA A CA    1 
ATOM   19583 C  C     . ALA A 1 4197 ? 179.982 153.907 146.756 1.00 34.02  ? 4197 ALA A C     1 
ATOM   19584 O  O     . ALA A 1 4197 ? 179.577 154.555 145.776 1.00 40.74  ? 4197 ALA A O     1 
ATOM   19585 C  CB    . ALA A 1 4197 ? 178.469 153.490 148.728 1.00 34.24  ? 4197 ALA A CB    1 
ATOM   19586 N  N     . PRO A 1 4198 ? 181.228 154.090 147.216 1.00 34.09  ? 4198 PRO A N     1 
ATOM   19587 C  CA    . PRO A 1 4198 ? 182.079 155.109 146.579 1.00 26.44  ? 4198 PRO A CA    1 
ATOM   19588 C  C     . PRO A 1 4198 ? 182.608 154.705 145.214 1.00 26.90  ? 4198 PRO A C     1 
ATOM   19589 O  O     . PRO A 1 4198 ? 182.918 155.591 144.409 1.00 32.63  ? 4198 PRO A O     1 
ATOM   19590 C  CB    . PRO A 1 4198 ? 183.219 155.295 147.586 1.00 27.32  ? 4198 PRO A CB    1 
ATOM   19591 C  CG    . PRO A 1 4198 ? 183.322 153.990 148.267 1.00 37.93  ? 4198 PRO A CG    1 
ATOM   19592 C  CD    . PRO A 1 4198 ? 181.929 153.420 148.328 1.00 28.39  ? 4198 PRO A CD    1 
ATOM   19593 N  N     . LEU A 1 4199 ? 182.722 153.410 144.921 1.00 25.27  ? 4199 LEU A N     1 
ATOM   19594 C  CA    . LEU A 1 4199 ? 183.255 152.949 143.644 1.00 20.79  ? 4199 LEU A CA    1 
ATOM   19595 C  C     . LEU A 1 4199 ? 182.163 152.544 142.661 1.00 23.93  ? 4199 LEU A C     1 
ATOM   19596 O  O     . LEU A 1 4199 ? 182.195 152.958 141.499 1.00 28.50  ? 4199 LEU A O     1 
ATOM   19597 C  CB    . LEU A 1 4199 ? 184.219 151.778 143.863 1.00 19.15  ? 4199 LEU A CB    1 
ATOM   19598 C  CG    . LEU A 1 4199 ? 185.704 152.132 143.958 1.00 22.41  ? 4199 LEU A CG    1 
ATOM   19599 C  CD1   . LEU A 1 4199 ? 185.986 152.975 145.192 1.00 29.69  ? 4199 LEU A CD1   1 
ATOM   19600 C  CD2   . LEU A 1 4199 ? 186.555 150.872 143.958 1.00 24.38  ? 4199 LEU A CD2   1 
ATOM   19601 N  N     . GLY A 1 4200 ? 181.200 151.732 143.102 1.00 22.92  ? 4200 GLY A N     1 
ATOM   19602 C  CA    . GLY A 1 4200 ? 180.108 151.350 142.222 1.00 17.92  ? 4200 GLY A CA    1 
ATOM   19603 C  C     . GLY A 1 4200 ? 179.288 152.534 141.753 1.00 18.28  ? 4200 GLY A C     1 
ATOM   19604 O  O     . GLY A 1 4200 ? 178.827 152.562 140.610 1.00 20.91  ? 4200 GLY A O     1 
ATOM   19605 N  N     . TRP A 1 4201 ? 179.095 153.520 142.623 1.00 18.70  ? 4201 TRP A N     1 
ATOM   19606 C  CA    . TRP A 1 4201 ? 178.413 154.760 142.284 1.00 20.74  ? 4201 TRP A CA    1 
ATOM   19607 C  C     . TRP A 1 4201 ? 179.143 155.891 142.999 1.00 28.14  ? 4201 TRP A C     1 
ATOM   19608 O  O     . TRP A 1 4201 ? 180.276 155.730 143.459 1.00 32.83  ? 4201 TRP A O     1 
ATOM   19609 C  CB    . TRP A 1 4201 ? 176.926 154.680 142.653 1.00 17.55  ? 4201 TRP A CB    1 
ATOM   19610 C  CG    . TRP A 1 4201 ? 176.140 153.776 141.752 1.00 17.69  ? 4201 TRP A CG    1 
ATOM   19611 C  CD1   . TRP A 1 4201 ? 175.615 152.557 142.069 1.00 15.98  ? 4201 TRP A CD1   1 
ATOM   19612 C  CD2   . TRP A 1 4201 ? 175.797 154.014 140.381 1.00 18.28  ? 4201 TRP A CD2   1 
ATOM   19613 N  NE1   . TRP A 1 4201 ? 174.964 152.024 140.985 1.00 13.52  ? 4201 TRP A NE1   1 
ATOM   19614 C  CE2   . TRP A 1 4201 ? 175.062 152.899 139.935 1.00 14.93  ? 4201 TRP A CE2   1 
ATOM   19615 C  CE3   . TRP A 1 4201 ? 176.039 155.062 139.489 1.00 21.19  ? 4201 TRP A CE3   1 
ATOM   19616 C  CZ2   . TRP A 1 4201 ? 174.567 152.802 138.637 1.00 14.26  ? 4201 TRP A CZ2   1 
ATOM   19617 C  CZ3   . TRP A 1 4201 ? 175.547 154.964 138.201 1.00 17.89  ? 4201 TRP A CZ3   1 
ATOM   19618 C  CH2   . TRP A 1 4201 ? 174.819 153.843 137.788 1.00 14.99  ? 4201 TRP A CH2   1 
ATOM   19619 N  N     . SER A 1 4202 ? 178.507 157.060 143.072 1.00 26.02  ? 4202 SER A N     1 
ATOM   19620 C  CA    . SER A 1 4202 ? 179.022 158.149 143.889 1.00 24.84  ? 4202 SER A CA    1 
ATOM   19621 C  C     . SER A 1 4202 ? 178.224 158.370 145.163 1.00 29.02  ? 4202 SER A C     1 
ATOM   19622 O  O     . SER A 1 4202 ? 178.757 158.951 146.113 1.00 35.15  ? 4202 SER A O     1 
ATOM   19623 C  CB    . SER A 1 4202 ? 179.056 159.458 143.088 1.00 27.26  ? 4202 SER A CB    1 
ATOM   19624 O  OG    . SER A 1 4202 ? 179.964 159.366 142.005 1.00 30.49  ? 4202 SER A OG    1 
ATOM   19625 N  N     . LYS A 1 4203 ? 176.974 157.918 145.207 1.00 26.93  ? 4203 LYS A N     1 
ATOM   19626 C  CA    . LYS A 1 4203 ? 176.152 158.010 146.403 1.00 27.60  ? 4203 LYS A CA    1 
ATOM   19627 C  C     . LYS A 1 4203 ? 175.138 156.877 146.377 1.00 27.41  ? 4203 LYS A C     1 
ATOM   19628 O  O     . LYS A 1 4203 ? 174.890 156.264 145.336 1.00 25.65  ? 4203 LYS A O     1 
ATOM   19629 C  CB    . LYS A 1 4203 ? 175.453 159.370 146.506 1.00 27.06  ? 4203 LYS A CB    1 
ATOM   19630 C  CG    . LYS A 1 4203 ? 174.828 159.844 145.208 1.00 25.93  ? 4203 LYS A CG    1 
ATOM   19631 C  CD    . LYS A 1 4203 ? 174.265 161.247 145.347 1.00 35.29  ? 4203 LYS A CD    1 
ATOM   19632 C  CE    . LYS A 1 4203 ? 175.373 162.264 145.568 1.00 41.27  ? 4203 LYS A CE    1 
ATOM   19633 N  NZ    . LYS A 1 4203 ? 176.305 162.331 144.409 1.00 32.85  ? 4203 LYS A NZ    1 
ATOM   19634 N  N     . LYS A 1 4204 ? 174.553 156.603 147.541 1.00 33.14  ? 4204 LYS A N     1 
ATOM   19635 C  CA    . LYS A 1 4204 ? 173.602 155.506 147.664 1.00 32.33  ? 4204 LYS A CA    1 
ATOM   19636 C  C     . LYS A 1 4204 ? 172.265 155.885 147.040 1.00 31.54  ? 4204 LYS A C     1 
ATOM   19637 O  O     . LYS A 1 4204 ? 171.375 156.400 147.724 1.00 32.54  ? 4204 LYS A O     1 
ATOM   19638 C  CB    . LYS A 1 4204 ? 173.422 155.118 149.133 1.00 34.29  ? 4204 LYS A CB    1 
ATOM   19639 C  CG    . LYS A 1 4204 ? 172.510 153.924 149.362 1.00 34.61  ? 4204 LYS A CG    1 
ATOM   19640 C  CD    . LYS A 1 4204 ? 173.134 152.646 148.827 1.00 30.25  ? 4204 LYS A CD    1 
ATOM   19641 C  CE    . LYS A 1 4204 ? 172.224 151.452 149.053 1.00 31.79  ? 4204 LYS A CE    1 
ATOM   19642 N  NZ    . LYS A 1 4204 ? 172.068 151.143 150.501 1.00 40.12  ? 4204 LYS A NZ    1 
ATOM   19643 N  N     . TYR A 1 4205 ? 172.121 155.646 145.739 1.00 24.98  ? 4205 TYR A N     1 
ATOM   19644 C  CA    . TYR A 1 4205 ? 170.870 155.936 145.055 1.00 22.70  ? 4205 TYR A CA    1 
ATOM   19645 C  C     . TYR A 1 4205 ? 169.789 154.941 145.464 1.00 29.03  ? 4205 TYR A C     1 
ATOM   19646 O  O     . TYR A 1 4205 ? 170.072 153.816 145.883 1.00 32.47  ? 4205 TYR A O     1 
ATOM   19647 C  CB    . TYR A 1 4205 ? 171.063 155.896 143.541 1.00 20.88  ? 4205 TYR A CB    1 
ATOM   19648 C  CG    . TYR A 1 4205 ? 171.975 156.973 143.003 1.00 18.74  ? 4205 TYR A CG    1 
ATOM   19649 C  CD1   . TYR A 1 4205 ? 171.638 158.314 143.116 1.00 23.05  ? 4205 TYR A CD1   1 
ATOM   19650 C  CD2   . TYR A 1 4205 ? 173.170 156.649 142.378 1.00 17.50  ? 4205 TYR A CD2   1 
ATOM   19651 C  CE1   . TYR A 1 4205 ? 172.467 159.302 142.624 1.00 25.20  ? 4205 TYR A CE1   1 
ATOM   19652 C  CE2   . TYR A 1 4205 ? 174.005 157.630 141.883 1.00 18.68  ? 4205 TYR A CE2   1 
ATOM   19653 C  CZ    . TYR A 1 4205 ? 173.649 158.954 142.009 1.00 25.51  ? 4205 TYR A CZ    1 
ATOM   19654 O  OH    . TYR A 1 4205 ? 174.479 159.935 141.518 1.00 29.95  ? 4205 TYR A OH    1 
ATOM   19655 N  N     . GLU A 1 4206 ? 168.536 155.371 145.337 1.00 31.08  ? 4206 GLU A N     1 
ATOM   19656 C  CA    . GLU A 1 4206 ? 167.391 154.542 145.712 1.00 27.57  ? 4206 GLU A CA    1 
ATOM   19657 C  C     . GLU A 1 4206 ? 166.872 153.756 144.506 1.00 26.39  ? 4206 GLU A C     1 
ATOM   19658 O  O     . GLU A 1 4206 ? 165.695 153.797 144.154 1.00 31.99  ? 4206 GLU A O     1 
ATOM   19659 C  CB    . GLU A 1 4206 ? 166.295 155.405 146.325 1.00 32.08  ? 4206 GLU A CB    1 
ATOM   19660 C  CG    . GLU A 1 4206 ? 166.729 156.175 147.559 1.00 38.39  ? 4206 GLU A CG    1 
ATOM   19661 C  CD    . GLU A 1 4206 ? 166.705 157.676 147.346 1.00 57.33  ? 4206 GLU A CD    1 
ATOM   19662 O  OE1   . GLU A 1 4206 ? 166.116 158.388 148.186 1.00 58.75  ? 4206 GLU A OE1   1 
ATOM   19663 O  OE2   . GLU A 1 4206 ? 167.276 158.143 146.338 1.00 56.06  ? 4206 GLU A OE2   1 
ATOM   19664 N  N     . PHE A 1 4207 ? 167.785 153.026 143.871 1.00 24.42  ? 4207 PHE A N     1 
ATOM   19665 C  CA    . PHE A 1 4207 ? 167.423 152.133 142.773 1.00 24.60  ? 4207 PHE A CA    1 
ATOM   19666 C  C     . PHE A 1 4207 ? 166.617 150.976 143.347 1.00 30.42  ? 4207 PHE A C     1 
ATOM   19667 O  O     . PHE A 1 4207 ? 167.167 150.075 143.984 1.00 31.86  ? 4207 PHE A O     1 
ATOM   19668 C  CB    . PHE A 1 4207 ? 168.671 151.634 142.054 1.00 20.65  ? 4207 PHE A CB    1 
ATOM   19669 C  CG    . PHE A 1 4207 ? 169.414 152.705 141.309 1.00 20.75  ? 4207 PHE A CG    1 
ATOM   19670 C  CD1   . PHE A 1 4207 ? 168.743 153.579 140.471 1.00 22.39  ? 4207 PHE A CD1   1 
ATOM   19671 C  CD2   . PHE A 1 4207 ? 170.785 152.838 141.445 1.00 18.08  ? 4207 PHE A CD2   1 
ATOM   19672 C  CE1   . PHE A 1 4207 ? 169.426 154.563 139.783 1.00 20.00  ? 4207 PHE A CE1   1 
ATOM   19673 C  CE2   . PHE A 1 4207 ? 171.473 153.818 140.758 1.00 14.55  ? 4207 PHE A CE2   1 
ATOM   19674 C  CZ    . PHE A 1 4207 ? 170.793 154.682 139.928 1.00 14.38  ? 4207 PHE A CZ    1 
ATOM   19675 N  N     . GLY A 1 4208 ? 165.305 150.994 143.127 1.00 27.09  ? 4208 GLY A N     1 
ATOM   19676 C  CA    . GLY A 1 4208 ? 164.440 150.015 143.754 1.00 26.58  ? 4208 GLY A CA    1 
ATOM   19677 C  C     . GLY A 1 4208 ? 163.413 149.385 142.838 1.00 24.23  ? 4208 GLY A C     1 
ATOM   19678 O  O     . GLY A 1 4208 ? 163.584 149.358 141.616 1.00 23.81  ? 4208 GLY A O     1 
ATOM   19679 N  N     . GLU A 1 4209 ? 162.333 148.872 143.431 1.00 26.71  ? 4209 GLU A N     1 
ATOM   19680 C  CA    . GLU A 1 4209 ? 161.323 148.155 142.660 1.00 27.80  ? 4209 GLU A CA    1 
ATOM   19681 C  C     . GLU A 1 4209 ? 160.518 149.090 141.766 1.00 24.32  ? 4209 GLU A C     1 
ATOM   19682 O  O     . GLU A 1 4209 ? 160.031 148.666 140.713 1.00 26.27  ? 4209 GLU A O     1 
ATOM   19683 C  CB    . GLU A 1 4209 ? 160.395 147.389 143.604 1.00 38.66  ? 4209 GLU A CB    1 
ATOM   19684 C  CG    . GLU A 1 4209 ? 159.430 146.444 142.908 1.00 46.08  ? 4209 GLU A CG    1 
ATOM   19685 C  CD    . GLU A 1 4209 ? 158.117 146.302 143.652 1.00 60.97  ? 4209 GLU A CD    1 
ATOM   19686 O  OE1   . GLU A 1 4209 ? 157.664 145.155 143.849 1.00 66.62  ? 4209 GLU A OE1   1 
ATOM   19687 O  OE2   . GLU A 1 4209 ? 157.537 147.339 144.041 1.00 60.17  ? 4209 GLU A OE2   1 
ATOM   19688 N  N     . SER A 1 4210 ? 160.357 150.354 142.166 1.00 23.52  ? 4210 SER A N     1 
ATOM   19689 C  CA    . SER A 1 4210 ? 159.622 151.301 141.333 1.00 22.14  ? 4210 SER A CA    1 
ATOM   19690 C  C     . SER A 1 4210 ? 160.328 151.529 140.003 1.00 21.10  ? 4210 SER A C     1 
ATOM   19691 O  O     . SER A 1 4210 ? 159.681 151.595 138.950 1.00 22.12  ? 4210 SER A O     1 
ATOM   19692 C  CB    . SER A 1 4210 ? 159.438 152.623 142.078 1.00 24.00  ? 4210 SER A CB    1 
ATOM   19693 O  OG    . SER A 1 4210 ? 160.633 153.011 142.730 1.00 29.47  ? 4210 SER A OG    1 
ATOM   19694 N  N     . ASP A 1 4211 ? 161.657 151.651 140.031 1.00 24.18  ? 4211 ASP A N     1 
ATOM   19695 C  CA    . ASP A 1 4211 ? 162.414 151.814 138.795 1.00 19.09  ? 4211 ASP A CA    1 
ATOM   19696 C  C     . ASP A 1 4211 ? 162.273 150.590 137.901 1.00 17.88  ? 4211 ASP A C     1 
ATOM   19697 O  O     . ASP A 1 4211 ? 162.115 150.717 136.681 1.00 21.37  ? 4211 ASP A O     1 
ATOM   19698 C  CB    . ASP A 1 4211 ? 163.885 152.079 139.112 1.00 23.31  ? 4211 ASP A CB    1 
ATOM   19699 C  CG    . ASP A 1 4211 ? 164.102 153.413 139.793 1.00 27.61  ? 4211 ASP A CG    1 
ATOM   19700 O  OD1   . ASP A 1 4211 ? 163.313 154.347 139.543 1.00 31.08  ? 4211 ASP A OD1   1 
ATOM   19701 O  OD2   . ASP A 1 4211 ? 165.064 153.529 140.581 1.00 28.09  ? 4211 ASP A OD2   1 
ATOM   19702 N  N     . LEU A 1 4212 ? 162.327 149.394 138.490 1.00 16.66  ? 4212 LEU A N     1 
ATOM   19703 C  CA    . LEU A 1 4212 ? 162.162 148.172 137.709 1.00 14.82  ? 4212 LEU A CA    1 
ATOM   19704 C  C     . LEU A 1 4212 ? 160.773 148.095 137.088 1.00 16.23  ? 4212 LEU A C     1 
ATOM   19705 O  O     . LEU A 1 4212 ? 160.629 147.697 135.927 1.00 20.63  ? 4212 LEU A O     1 
ATOM   19706 C  CB    . LEU A 1 4212 ? 162.427 146.951 138.587 1.00 17.13  ? 4212 LEU A CB    1 
ATOM   19707 C  CG    . LEU A 1 4212 ? 162.200 145.582 137.944 1.00 14.76  ? 4212 LEU A CG    1 
ATOM   19708 C  CD1   . LEU A 1 4212 ? 163.317 145.252 136.968 1.00 13.92  ? 4212 LEU A CD1   1 
ATOM   19709 C  CD2   . LEU A 1 4212 ? 162.079 144.510 139.012 1.00 16.96  ? 4212 LEU A CD2   1 
ATOM   19710 N  N     . ARG A 1 4213 ? 159.739 148.468 137.845 1.00 16.86  ? 4213 ARG A N     1 
ATOM   19711 C  CA    . ARG A 1 4213 ? 158.381 148.445 137.310 1.00 16.66  ? 4213 ARG A CA    1 
ATOM   19712 C  C     . ARG A 1 4213 ? 158.216 149.452 136.179 1.00 18.43  ? 4213 ARG A C     1 
ATOM   19713 O  O     . ARG A 1 4213 ? 157.580 149.155 135.159 1.00 22.37  ? 4213 ARG A O     1 
ATOM   19714 C  CB    . ARG A 1 4213 ? 157.375 148.716 138.428 1.00 21.18  ? 4213 ARG A CB    1 
ATOM   19715 C  CG    . ARG A 1 4213 ? 157.147 147.532 139.353 1.00 28.05  ? 4213 ARG A CG    1 
ATOM   19716 C  CD    . ARG A 1 4213 ? 155.953 147.760 140.265 1.00 33.71  ? 4213 ARG A CD    1 
ATOM   19717 N  NE    . ARG A 1 4213 ? 155.748 149.175 140.553 1.00 45.53  ? 4213 ARG A NE    1 
ATOM   19718 C  CZ    . ARG A 1 4213 ? 155.783 149.705 141.768 1.00 52.00  ? 4213 ARG A CZ    1 
ATOM   19719 N  NH1   . ARG A 1 4213 ? 156.014 148.964 142.839 1.00 45.29  ? 4213 ARG A NH1   1 
ATOM   19720 N  NH2   . ARG A 1 4213 ? 155.584 151.012 141.912 1.00 46.91  ? 4213 ARG A NH2   1 
ATOM   19721 N  N     . SER A 1 4214 ? 158.783 150.651 136.338 1.00 16.20  ? 4214 SER A N     1 
ATOM   19722 C  CA    . SER A 1 4214 ? 158.708 151.648 135.275 1.00 14.16  ? 4214 SER A CA    1 
ATOM   19723 C  C     . SER A 1 4214 ? 159.450 151.180 134.029 1.00 16.91  ? 4214 SER A C     1 
ATOM   19724 O  O     . SER A 1 4214 ? 158.987 151.395 132.902 1.00 21.38  ? 4214 SER A O     1 
ATOM   19725 C  CB    . SER A 1 4214 ? 159.267 152.982 135.766 1.00 18.19  ? 4214 SER A CB    1 
ATOM   19726 O  OG    . SER A 1 4214 ? 158.600 153.409 136.941 1.00 24.61  ? 4214 SER A OG    1 
ATOM   19727 N  N     . ALA A 1 4215 ? 160.607 150.540 134.211 1.00 16.72  ? 4215 ALA A N     1 
ATOM   19728 C  CA    . ALA A 1 4215 ? 161.350 150.011 133.073 1.00 14.03  ? 4215 ALA A CA    1 
ATOM   19729 C  C     . ALA A 1 4215 ? 160.576 148.900 132.374 1.00 17.56  ? 4215 ALA A C     1 
ATOM   19730 O  O     . ALA A 1 4215 ? 160.568 148.821 131.140 1.00 21.89  ? 4215 ALA A O     1 
ATOM   19731 C  CB    . ALA A 1 4215 ? 162.716 149.511 133.534 1.00 12.08  ? 4215 ALA A CB    1 
ATOM   19732 N  N     . CYS A 1 4216 ? 159.926 148.027 133.148 1.00 20.36  ? 4216 CYS A N     1 
ATOM   19733 C  CA    . CYS A 1 4216 ? 159.087 146.989 132.556 1.00 18.21  ? 4216 CYS A CA    1 
ATOM   19734 C  C     . CYS A 1 4216 ? 157.947 147.601 131.755 1.00 24.69  ? 4216 CYS A C     1 
ATOM   19735 O  O     . CYS A 1 4216 ? 157.636 147.141 130.650 1.00 28.83  ? 4216 CYS A O     1 
ATOM   19736 C  CB    . CYS A 1 4216 ? 158.533 146.072 133.646 1.00 21.82  ? 4216 CYS A CB    1 
ATOM   19737 S  SG    . CYS A 1 4216 ? 159.740 144.979 134.426 1.00 39.28  ? 4216 CYS A SG    1 
ATOM   19738 N  N     . ASP A 1 4217 ? 157.310 148.640 132.301 1.00 25.21  ? 4217 ASP A N     1 
ATOM   19739 C  CA    . ASP A 1 4217 ? 156.229 149.309 131.584 1.00 23.90  ? 4217 ASP A CA    1 
ATOM   19740 C  C     . ASP A 1 4217 ? 156.730 149.935 130.290 1.00 24.53  ? 4217 ASP A C     1 
ATOM   19741 O  O     . ASP A 1 4217 ? 156.065 149.847 129.251 1.00 27.11  ? 4217 ASP A O     1 
ATOM   19742 C  CB    . ASP A 1 4217 ? 155.585 150.368 132.478 1.00 25.21  ? 4217 ASP A CB    1 
ATOM   19743 C  CG    . ASP A 1 4217 ? 154.787 149.763 133.615 1.00 36.32  ? 4217 ASP A CG    1 
ATOM   19744 O  OD1   . ASP A 1 4217 ? 154.633 148.525 133.643 1.00 39.11  ? 4217 ASP A OD1   1 
ATOM   19745 O  OD2   . ASP A 1 4217 ? 154.314 150.527 134.483 1.00 39.73  ? 4217 ASP A OD2   1 
ATOM   19746 N  N     . THR A 1 4218 ? 157.901 150.575 130.334 1.00 23.05  ? 4218 THR A N     1 
ATOM   19747 C  CA    . THR A 1 4218 ? 158.473 151.174 129.131 1.00 21.36  ? 4218 THR A CA    1 
ATOM   19748 C  C     . THR A 1 4218 ? 158.770 150.115 128.077 1.00 23.40  ? 4218 THR A C     1 
ATOM   19749 O  O     . THR A 1 4218 ? 158.454 150.290 126.891 1.00 31.60  ? 4218 THR A O     1 
ATOM   19750 C  CB    . THR A 1 4218 ? 159.744 151.946 129.491 1.00 19.22  ? 4218 THR A CB    1 
ATOM   19751 O  OG1   . THR A 1 4218 ? 159.396 153.163 130.164 1.00 28.28  ? 4218 THR A OG1   1 
ATOM   19752 C  CG2   . THR A 1 4218 ? 160.553 152.267 128.246 1.00 16.99  ? 4218 THR A CG2   1 
ATOM   19753 N  N     . VAL A 1 4219 ? 159.376 149.001 128.495 1.00 20.65  ? 4219 VAL A N     1 
ATOM   19754 C  CA    . VAL A 1 4219 ? 159.702 147.929 127.560 1.00 20.53  ? 4219 VAL A CA    1 
ATOM   19755 C  C     . VAL A 1 4219 ? 158.431 147.377 126.930 1.00 25.43  ? 4219 VAL A C     1 
ATOM   19756 O  O     . VAL A 1 4219 ? 158.354 147.185 125.711 1.00 30.79  ? 4219 VAL A O     1 
ATOM   19757 C  CB    . VAL A 1 4219 ? 160.509 146.826 128.268 1.00 17.85  ? 4219 VAL A CB    1 
ATOM   19758 C  CG1   . VAL A 1 4219 ? 160.479 145.537 127.462 1.00 17.75  ? 4219 VAL A CG1   1 
ATOM   19759 C  CG2   . VAL A 1 4219 ? 161.942 147.280 128.496 1.00 19.97  ? 4219 VAL A CG2   1 
ATOM   19760 N  N     . ASP A 1 4220 ? 157.406 147.133 127.752 1.00 25.92  ? 4220 ASP A N     1 
ATOM   19761 C  CA    . ASP A 1 4220 ? 156.142 146.620 127.236 1.00 25.22  ? 4220 ASP A CA    1 
ATOM   19762 C  C     . ASP A 1 4220 ? 155.525 147.587 126.236 1.00 27.79  ? 4220 ASP A C     1 
ATOM   19763 O  O     . ASP A 1 4220 ? 155.116 147.186 125.140 1.00 36.67  ? 4220 ASP A O     1 
ATOM   19764 C  CB    . ASP A 1 4220 ? 155.173 146.360 128.389 1.00 29.92  ? 4220 ASP A CB    1 
ATOM   19765 C  CG    . ASP A 1 4220 ? 155.487 145.084 129.138 1.00 42.79  ? 4220 ASP A CG    1 
ATOM   19766 O  OD1   . ASP A 1 4220 ? 156.429 144.373 128.732 1.00 45.33  ? 4220 ASP A OD1   1 
ATOM   19767 O  OD2   . ASP A 1 4220 ? 154.793 144.793 130.135 1.00 44.65  ? 4220 ASP A OD2   1 
ATOM   19768 N  N     . THR A 1 4221 ? 155.463 148.871 126.594 1.00 26.22  ? 4221 THR A N     1 
ATOM   19769 C  CA    . THR A 1 4221 ? 154.826 149.859 125.730 1.00 25.95  ? 4221 THR A CA    1 
ATOM   19770 C  C     . THR A 1 4221 ? 155.537 149.956 124.388 1.00 27.95  ? 4221 THR A C     1 
ATOM   19771 O  O     . THR A 1 4221 ? 154.898 149.924 123.330 1.00 32.90  ? 4221 THR A O     1 
ATOM   19772 C  CB    . THR A 1 4221 ? 154.803 151.222 126.424 1.00 28.05  ? 4221 THR A CB    1 
ATOM   19773 O  OG1   . THR A 1 4221 ? 153.946 151.163 127.571 1.00 34.54  ? 4221 THR A OG1   1 
ATOM   19774 C  CG2   . THR A 1 4221 ? 154.300 152.298 125.474 1.00 29.48  ? 4221 THR A CG2   1 
ATOM   19775 N  N     . TRP A 1 4222 ? 156.868 150.045 124.407 1.00 26.20  ? 4222 TRP A N     1 
ATOM   19776 C  CA    . TRP A 1 4222 ? 157.582 150.242 123.151 1.00 26.54  ? 4222 TRP A CA    1 
ATOM   19777 C  C     . TRP A 1 4222 ? 157.644 148.971 122.313 1.00 32.11  ? 4222 TRP A C     1 
ATOM   19778 O  O     . TRP A 1 4222 ? 157.607 149.053 121.079 1.00 43.61  ? 4222 TRP A O     1 
ATOM   19779 C  CB    . TRP A 1 4222 ? 158.980 150.791 123.426 1.00 23.91  ? 4222 TRP A CB    1 
ATOM   19780 C  CG    . TRP A 1 4222 ? 158.929 152.230 123.825 1.00 23.96  ? 4222 TRP A CG    1 
ATOM   19781 C  CD1   . TRP A 1 4222 ? 158.941 152.729 125.093 1.00 22.88  ? 4222 TRP A CD1   1 
ATOM   19782 C  CD2   . TRP A 1 4222 ? 158.811 153.358 122.951 1.00 24.05  ? 4222 TRP A CD2   1 
ATOM   19783 N  NE1   . TRP A 1 4222 ? 158.858 154.099 125.062 1.00 21.43  ? 4222 TRP A NE1   1 
ATOM   19784 C  CE2   . TRP A 1 4222 ? 158.777 154.510 123.759 1.00 22.95  ? 4222 TRP A CE2   1 
ATOM   19785 C  CE3   . TRP A 1 4222 ? 158.741 153.506 121.562 1.00 29.09  ? 4222 TRP A CE3   1 
ATOM   19786 C  CZ2   . TRP A 1 4222 ? 158.676 155.792 123.226 1.00 27.92  ? 4222 TRP A CZ2   1 
ATOM   19787 C  CZ3   . TRP A 1 4222 ? 158.641 154.780 121.035 1.00 29.39  ? 4222 TRP A CZ3   1 
ATOM   19788 C  CH2   . TRP A 1 4222 ? 158.610 155.907 121.866 1.00 27.23  ? 4222 TRP A CH2   1 
ATOM   19789 N  N     . LEU A 1 4223 ? 157.717 147.796 122.943 1.00 29.28  ? 4223 LEU A N     1 
ATOM   19790 C  CA    . LEU A 1 4223 ? 157.661 146.558 122.176 1.00 29.96  ? 4223 LEU A CA    1 
ATOM   19791 C  C     . LEU A 1 4223 ? 156.288 146.364 121.545 1.00 36.81  ? 4223 LEU A C     1 
ATOM   19792 O  O     . LEU A 1 4223 ? 156.185 145.898 120.405 1.00 44.87  ? 4223 LEU A O     1 
ATOM   19793 C  CB    . LEU A 1 4223 ? 158.021 145.370 123.066 1.00 32.42  ? 4223 LEU A CB    1 
ATOM   19794 C  CG    . LEU A 1 4223 ? 158.708 144.208 122.350 1.00 42.27  ? 4223 LEU A CG    1 
ATOM   19795 C  CD1   . LEU A 1 4223 ? 159.870 144.709 121.508 1.00 40.48  ? 4223 LEU A CD1   1 
ATOM   19796 C  CD2   . LEU A 1 4223 ? 159.180 143.178 123.353 1.00 37.54  ? 4223 LEU A CD2   1 
ATOM   19797 N  N     . ASP A 1 4224 ? 155.220 146.711 122.270 1.00 34.07  ? 4224 ASP A N     1 
ATOM   19798 C  CA    . ASP A 1 4224 ? 153.884 146.644 121.689 1.00 37.85  ? 4224 ASP A CA    1 
ATOM   19799 C  C     . ASP A 1 4224 ? 153.731 147.640 120.547 1.00 43.63  ? 4224 ASP A C     1 
ATOM   19800 O  O     . ASP A 1 4224 ? 153.090 147.337 119.534 1.00 52.71  ? 4224 ASP A O     1 
ATOM   19801 C  CB    . ASP A 1 4224 ? 152.830 146.894 122.767 1.00 41.72  ? 4224 ASP A CB    1 
ATOM   19802 C  CG    . ASP A 1 4224 ? 152.737 145.758 123.765 1.00 52.73  ? 4224 ASP A CG    1 
ATOM   19803 O  OD1   . ASP A 1 4224 ? 153.290 144.673 123.487 1.00 56.86  ? 4224 ASP A OD1   1 
ATOM   19804 O  OD2   . ASP A 1 4224 ? 152.113 145.950 124.830 1.00 45.65  ? 4224 ASP A OD2   1 
ATOM   19805 N  N     . ASP A 1 4225 ? 154.302 148.837 120.698 1.00 43.69  ? 4225 ASP A N     1 
ATOM   19806 C  CA    . ASP A 1 4225 ? 154.237 149.830 119.631 1.00 46.44  ? 4225 ASP A CA    1 
ATOM   19807 C  C     . ASP A 1 4225 ? 154.958 149.343 118.380 1.00 47.11  ? 4225 ASP A C     1 
ATOM   19808 O  O     . ASP A 1 4225 ? 154.432 149.448 117.266 1.00 54.06  ? 4225 ASP A O     1 
ATOM   19809 C  CB    . ASP A 1 4225 ? 154.831 151.153 120.114 1.00 49.11  ? 4225 ASP A CB    1 
ATOM   19810 C  CG    . ASP A 1 4225 ? 154.153 152.358 119.493 1.00 64.77  ? 4225 ASP A CG    1 
ATOM   19811 O  OD1   . ASP A 1 4225 ? 153.248 152.167 118.653 1.00 66.44  ? 4225 ASP A OD1   1 
ATOM   19812 O  OD2   . ASP A 1 4225 ? 154.526 153.497 119.843 1.00 65.64  ? 4225 ASP A OD2   1 
ATOM   19813 N  N     . THR A 1 4226 ? 156.168 148.804 118.544 1.00 43.60  ? 4226 THR A N     1 
ATOM   19814 C  CA    . THR A 1 4226 ? 156.931 148.363 117.380 1.00 46.03  ? 4226 THR A CA    1 
ATOM   19815 C  C     . THR A 1 4226 ? 156.381 147.059 116.811 1.00 47.90  ? 4226 THR A C     1 
ATOM   19816 O  O     . THR A 1 4226 ? 156.256 146.915 115.589 1.00 51.78  ? 4226 THR A O     1 
ATOM   19817 C  CB    . THR A 1 4226 ? 158.406 148.208 117.745 1.00 47.50  ? 4226 THR A CB    1 
ATOM   19818 O  OG1   . THR A 1 4226 ? 158.858 149.391 118.415 1.00 47.47  ? 4226 THR A OG1   1 
ATOM   19819 C  CG2   . THR A 1 4226 ? 159.239 148.004 116.491 1.00 50.62  ? 4226 THR A CG2   1 
ATOM   19820 N  N     . ALA A 1 4227 ? 156.046 146.103 117.674 1.00 50.94  ? 4227 ALA A N     1 
ATOM   19821 C  CA    . ALA A 1 4227 ? 155.536 144.799 117.252 1.00 56.31  ? 4227 ALA A CA    1 
ATOM   19822 C  C     . ALA A 1 4227 ? 154.029 144.779 117.483 1.00 58.87  ? 4227 ALA A C     1 
ATOM   19823 O  O     . ALA A 1 4227 ? 153.564 144.611 118.613 1.00 60.33  ? 4227 ALA A O     1 
ATOM   19824 C  CB    . ALA A 1 4227 ? 156.233 143.672 118.006 1.00 52.03  ? 4227 ALA A CB    1 
ATOM   19825 N  N     . LYS A 1 4228 ? 153.264 144.945 116.403 1.00 59.42  ? 4228 LYS A N     1 
ATOM   19826 C  CA    . LYS A 1 4228 ? 151.804 145.010 116.483 1.00 67.85  ? 4228 LYS A CA    1 
ATOM   19827 C  C     . LYS A 1 4228 ? 151.225 143.594 116.456 1.00 75.05  ? 4228 LYS A C     1 
ATOM   19828 O  O     . LYS A 1 4228 ? 150.579 143.158 115.501 1.00 77.55  ? 4228 LYS A O     1 
ATOM   19829 C  CB    . LYS A 1 4228 ? 151.249 145.865 115.353 1.00 66.85  ? 4228 LYS A CB    1 
ATOM   19830 C  CG    . LYS A 1 4228 ? 151.443 147.358 115.553 1.00 61.80  ? 4228 LYS A CG    1 
ATOM   19831 C  CD    . LYS A 1 4228 ? 152.406 147.929 114.525 1.00 72.58  ? 4228 LYS A CD    1 
ATOM   19832 C  CE    . LYS A 1 4228 ? 152.500 149.441 114.635 1.00 72.57  ? 4228 LYS A CE    1 
ATOM   19833 N  NZ    . LYS A 1 4228 ? 153.608 149.991 113.805 1.00 66.21  ? 4228 LYS A NZ    1 
ATOM   19834 N  N     . GLY A 1 4229 ? 151.473 142.868 117.544 1.00 70.13  ? 4229 GLY A N     1 
ATOM   19835 C  CA    . GLY A 1 4229 ? 150.949 141.529 117.705 1.00 65.54  ? 4229 GLY A CA    1 
ATOM   19836 C  C     . GLY A 1 4229 ? 151.704 140.446 116.969 1.00 67.85  ? 4229 GLY A C     1 
ATOM   19837 O  O     . GLY A 1 4229 ? 151.292 139.280 117.029 1.00 75.22  ? 4229 GLY A O     1 
ATOM   19838 N  N     . ARG A 1 4230 ? 152.786 140.785 116.275 1.00 67.43  ? 4230 ARG A N     1 
ATOM   19839 C  CA    . ARG A 1 4230 ? 153.552 139.789 115.541 1.00 68.54  ? 4230 ARG A CA    1 
ATOM   19840 C  C     . ARG A 1 4230 ? 154.233 138.822 116.501 1.00 72.13  ? 4230 ARG A C     1 
ATOM   19841 O  O     . ARG A 1 4230 ? 154.715 139.214 117.567 1.00 74.47  ? 4230 ARG A O     1 
ATOM   19842 C  CB    . ARG A 1 4230 ? 154.589 140.472 114.651 1.00 64.25  ? 4230 ARG A CB    1 
ATOM   19843 C  CG    . ARG A 1 4230 ? 153.987 141.443 113.649 1.00 64.43  ? 4230 ARG A CG    1 
ATOM   19844 C  CD    . ARG A 1 4230 ? 154.985 141.817 112.567 1.00 69.20  ? 4230 ARG A CD    1 
ATOM   19845 N  NE    . ARG A 1 4230 ? 156.234 142.313 113.131 1.00 84.14  ? 4230 ARG A NE    1 
ATOM   19846 C  CZ    . ARG A 1 4230 ? 156.882 143.382 112.689 1.00 84.73  ? 4230 ARG A CZ    1 
ATOM   19847 N  NH1   . ARG A 1 4230 ? 156.424 144.097 111.675 1.00 78.04  ? 4230 ARG A NH1   1 
ATOM   19848 N  NH2   . ARG A 1 4230 ? 158.018 143.742 113.279 1.00 79.58  ? 4230 ARG A NH2   1 
ATOM   19849 N  N     . GLN A 1 4231 ? 154.264 137.543 116.115 1.00 70.12  ? 4231 GLN A N     1 
ATOM   19850 C  CA    . GLN A 1 4231 ? 154.881 136.528 116.963 1.00 69.93  ? 4231 GLN A CA    1 
ATOM   19851 C  C     . GLN A 1 4231 ? 156.377 136.761 117.125 1.00 66.29  ? 4231 GLN A C     1 
ATOM   19852 O  O     . GLN A 1 4231 ? 156.922 136.553 118.214 1.00 65.02  ? 4231 GLN A O     1 
ATOM   19853 C  CB    . GLN A 1 4231 ? 154.621 135.134 116.391 1.00 74.65  ? 4231 GLN A CB    1 
ATOM   19854 C  CG    . GLN A 1 4231 ? 153.291 134.510 116.801 1.00 80.16  ? 4231 GLN A CG    1 
ATOM   19855 C  CD    . GLN A 1 4231 ? 153.115 134.415 118.306 1.00 82.68  ? 4231 GLN A CD    1 
ATOM   19856 O  OE1   . GLN A 1 4231 ? 152.745 135.387 118.966 1.00 81.10  ? 4231 GLN A OE1   1 
ATOM   19857 N  NE2   . GLN A 1 4231 ? 153.382 133.237 118.857 1.00 82.91  ? 4231 GLN A NE2   1 
ATOM   19858 N  N     . ASN A 1 4232 ? 157.054 137.187 116.062 1.00 61.99  ? 4232 ASN A N     1 
ATOM   19859 C  CA    . ASN A 1 4232 ? 158.490 137.418 116.093 1.00 63.63  ? 4232 ASN A CA    1 
ATOM   19860 C  C     . ASN A 1 4232 ? 158.801 138.810 115.565 1.00 64.68  ? 4232 ASN A C     1 
ATOM   19861 O  O     . ASN A 1 4232 ? 158.132 139.303 114.652 1.00 67.06  ? 4232 ASN A O     1 
ATOM   19862 C  CB    . ASN A 1 4232 ? 159.243 136.370 115.265 1.00 63.98  ? 4232 ASN A CB    1 
ATOM   19863 C  CG    . ASN A 1 4232 ? 159.339 135.032 115.967 1.00 69.10  ? 4232 ASN A CG    1 
ATOM   19864 O  OD1   . ASN A 1 4232 ? 159.488 134.967 117.187 1.00 68.08  ? 4232 ASN A OD1   1 
ATOM   19865 N  ND2   . ASN A 1 4232 ? 159.255 133.953 115.198 1.00 68.38  ? 4232 ASN A ND2   1 
ATOM   19866 N  N     . ILE A 1 4233 ? 159.818 139.438 116.149 1.00 62.65  ? 4233 ILE A N     1 
ATOM   19867 C  CA    . ILE A 1 4233 ? 160.318 140.732 115.703 1.00 54.74  ? 4233 ILE A CA    1 
ATOM   19868 C  C     . ILE A 1 4233 ? 161.827 140.622 115.536 1.00 51.39  ? 4233 ILE A C     1 
ATOM   19869 O  O     . ILE A 1 4233 ? 162.499 139.963 116.337 1.00 54.45  ? 4233 ILE A O     1 
ATOM   19870 C  CB    . ILE A 1 4233 ? 159.946 141.865 116.682 1.00 53.65  ? 4233 ILE A CB    1 
ATOM   19871 C  CG1   . ILE A 1 4233 ? 160.284 143.230 116.078 1.00 56.25  ? 4233 ILE A CG1   1 
ATOM   19872 C  CG2   . ILE A 1 4233 ? 160.620 141.678 118.036 1.00 51.81  ? 4233 ILE A CG2   1 
ATOM   19873 C  CD1   . ILE A 1 4233 ? 159.676 144.392 116.825 1.00 52.97  ? 4233 ILE A CD1   1 
ATOM   19874 N  N     . SER A 1 4234 ? 162.351 141.230 114.479 1.00 45.74  ? 4234 SER A N     1 
ATOM   19875 C  CA    . SER A 1 4234 ? 163.787 141.203 114.260 1.00 48.54  ? 4234 SER A CA    1 
ATOM   19876 C  C     . SER A 1 4234 ? 164.492 141.974 115.373 1.00 53.08  ? 4234 SER A C     1 
ATOM   19877 O  O     . SER A 1 4234 ? 164.022 143.042 115.781 1.00 50.69  ? 4234 SER A O     1 
ATOM   19878 C  CB    . SER A 1 4234 ? 164.136 141.802 112.897 1.00 52.05  ? 4234 SER A CB    1 
ATOM   19879 O  OG    . SER A 1 4234 ? 165.539 141.854 112.707 1.00 56.50  ? 4234 SER A OG    1 
ATOM   19880 N  N     . PRO A 1 4235 ? 165.608 141.458 115.896 1.00 56.00  ? 4235 PRO A N     1 
ATOM   19881 C  CA    . PRO A 1 4235 ? 166.322 142.190 116.955 1.00 48.94  ? 4235 PRO A CA    1 
ATOM   19882 C  C     . PRO A 1 4235 ? 166.777 143.573 116.529 1.00 51.11  ? 4235 PRO A C     1 
ATOM   19883 O  O     . PRO A 1 4235 ? 166.881 144.470 117.375 1.00 54.32  ? 4235 PRO A O     1 
ATOM   19884 C  CB    . PRO A 1 4235 ? 167.512 141.274 117.271 1.00 49.39  ? 4235 PRO A CB    1 
ATOM   19885 C  CG    . PRO A 1 4235 ? 167.079 139.917 116.817 1.00 53.20  ? 4235 PRO A CG    1 
ATOM   19886 C  CD    . PRO A 1 4235 ? 166.221 140.151 115.613 1.00 54.75  ? 4235 PRO A CD    1 
ATOM   19887 N  N     . ASP A 1 4236 ? 167.056 143.775 115.239 1.00 53.98  ? 4236 ASP A N     1 
ATOM   19888 C  CA    . ASP A 1 4236 ? 167.422 145.103 114.763 1.00 55.19  ? 4236 ASP A CA    1 
ATOM   19889 C  C     . ASP A 1 4236 ? 166.232 146.053 114.777 1.00 51.16  ? 4236 ASP A C     1 
ATOM   19890 O  O     . ASP A 1 4236 ? 166.416 147.273 114.855 1.00 54.91  ? 4236 ASP A O     1 
ATOM   19891 C  CB    . ASP A 1 4236 ? 168.013 145.013 113.357 1.00 62.45  ? 4236 ASP A CB    1 
ATOM   19892 C  CG    . ASP A 1 4236 ? 169.352 144.302 113.332 1.00 76.23  ? 4236 ASP A CG    1 
ATOM   19893 O  OD1   . ASP A 1 4236 ? 169.371 143.062 113.481 1.00 75.99  ? 4236 ASP A OD1   1 
ATOM   19894 O  OD2   . ASP A 1 4236 ? 170.385 144.983 113.163 1.00 82.10  ? 4236 ASP A OD2   1 
ATOM   19895 N  N     . LYS A 1 4237 ? 165.011 145.521 114.702 1.00 46.77  ? 4237 LYS A N     1 
ATOM   19896 C  CA    . LYS A 1 4237 ? 163.814 146.351 114.707 1.00 45.95  ? 4237 LYS A CA    1 
ATOM   19897 C  C     . LYS A 1 4237 ? 163.352 146.724 116.109 1.00 44.37  ? 4237 LYS A C     1 
ATOM   19898 O  O     . LYS A 1 4237 ? 162.450 147.558 116.242 1.00 49.33  ? 4237 LYS A O     1 
ATOM   19899 C  CB    . LYS A 1 4237 ? 162.676 145.641 113.969 1.00 49.02  ? 4237 LYS A CB    1 
ATOM   19900 C  CG    . LYS A 1 4237 ? 163.004 145.258 112.535 1.00 53.62  ? 4237 LYS A CG    1 
ATOM   19901 C  CD    . LYS A 1 4237 ? 163.624 146.420 111.777 1.00 50.86  ? 4237 LYS A CD    1 
ATOM   19902 C  CE    . LYS A 1 4237 ? 164.580 145.930 110.703 1.00 55.70  ? 4237 LYS A CE    1 
ATOM   19903 N  NZ    . LYS A 1 4237 ? 165.726 146.861 110.514 1.00 64.16  ? 4237 LYS A NZ    1 
ATOM   19904 N  N     . ILE A 1 4238 ? 163.934 146.133 117.143 1.00 42.82  ? 4238 ILE A N     1 
ATOM   19905 C  CA    . ILE A 1 4238 ? 163.570 146.488 118.520 1.00 38.94  ? 4238 ILE A CA    1 
ATOM   19906 C  C     . ILE A 1 4238 ? 163.978 147.934 118.785 1.00 38.24  ? 4238 ILE A C     1 
ATOM   19907 O  O     . ILE A 1 4238 ? 165.110 148.325 118.449 1.00 39.70  ? 4238 ILE A O     1 
ATOM   19908 C  CB    . ILE A 1 4238 ? 164.241 145.533 119.510 1.00 34.93  ? 4238 ILE A CB    1 
ATOM   19909 C  CG1   . ILE A 1 4238 ? 163.760 144.100 119.273 1.00 40.10  ? 4238 ILE A CG1   1 
ATOM   19910 C  CG2   . ILE A 1 4238 ? 163.964 145.957 120.944 1.00 35.05  ? 4238 ILE A CG2   1 
ATOM   19911 C  CD1   . ILE A 1 4238 ? 164.237 143.116 120.314 1.00 39.17  ? 4238 ILE A CD1   1 
ATOM   19912 N  N     . PRO A 1 4239 ? 163.109 148.763 119.371 1.00 36.69  ? 4239 PRO A N     1 
ATOM   19913 C  CA    . PRO A 1 4239 ? 163.479 150.164 119.615 1.00 33.60  ? 4239 PRO A CA    1 
ATOM   19914 C  C     . PRO A 1 4239 ? 164.536 150.301 120.698 1.00 29.42  ? 4239 PRO A C     1 
ATOM   19915 O  O     . PRO A 1 4239 ? 164.233 150.691 121.829 1.00 30.07  ? 4239 PRO A O     1 
ATOM   19916 C  CB    . PRO A 1 4239 ? 162.153 150.809 120.035 1.00 31.63  ? 4239 PRO A CB    1 
ATOM   19917 C  CG    . PRO A 1 4239 ? 161.349 149.683 120.588 1.00 31.11  ? 4239 PRO A CG    1 
ATOM   19918 C  CD    . PRO A 1 4239 ? 161.721 148.478 119.774 1.00 35.58  ? 4239 PRO A CD    1 
ATOM   19919 N  N     . TRP A 1 4240 ? 165.784 149.976 120.353 1.00 31.98  ? 4240 TRP A N     1 
ATOM   19920 C  CA    . TRP A 1 4240 ? 166.869 150.052 121.326 1.00 28.57  ? 4240 TRP A CA    1 
ATOM   19921 C  C     . TRP A 1 4240 ? 167.106 151.484 121.785 1.00 27.14  ? 4240 TRP A C     1 
ATOM   19922 O  O     . TRP A 1 4240 ? 167.314 151.734 122.978 1.00 27.60  ? 4240 TRP A O     1 
ATOM   19923 C  CB    . TRP A 1 4240 ? 168.148 149.467 120.728 1.00 31.13  ? 4240 TRP A CB    1 
ATOM   19924 C  CG    . TRP A 1 4240 ? 168.053 148.012 120.407 1.00 34.17  ? 4240 TRP A CG    1 
ATOM   19925 C  CD1   . TRP A 1 4240 ? 168.040 147.446 119.167 1.00 38.50  ? 4240 TRP A CD1   1 
ATOM   19926 C  CD2   . TRP A 1 4240 ? 167.969 146.931 121.343 1.00 33.27  ? 4240 TRP A CD2   1 
ATOM   19927 N  NE1   . TRP A 1 4240 ? 167.947 146.080 119.271 1.00 42.94  ? 4240 TRP A NE1   1 
ATOM   19928 C  CE2   . TRP A 1 4240 ? 167.903 145.738 120.597 1.00 38.03  ? 4240 TRP A CE2   1 
ATOM   19929 C  CE3   . TRP A 1 4240 ? 167.941 146.856 122.738 1.00 31.23  ? 4240 TRP A CE3   1 
ATOM   19930 C  CZ2   . TRP A 1 4240 ? 167.811 144.487 121.199 1.00 35.27  ? 4240 TRP A CZ2   1 
ATOM   19931 C  CZ3   . TRP A 1 4240 ? 167.850 145.613 123.334 1.00 31.12  ? 4240 TRP A CZ3   1 
ATOM   19932 C  CH2   . TRP A 1 4240 ? 167.787 144.445 122.565 1.00 31.81  ? 4240 TRP A CH2   1 
ATOM   19933 N  N     . SER A 1 4241 ? 167.087 152.437 120.850 1.00 27.96  ? 4241 SER A N     1 
ATOM   19934 C  CA    . SER A 1 4241 ? 167.363 153.827 121.203 1.00 25.15  ? 4241 SER A CA    1 
ATOM   19935 C  C     . SER A 1 4241 ? 166.315 154.375 122.163 1.00 21.36  ? 4241 SER A C     1 
ATOM   19936 O  O     . SER A 1 4241 ? 166.653 155.062 123.133 1.00 18.65  ? 4241 SER A O     1 
ATOM   19937 C  CB    . SER A 1 4241 ? 167.433 154.684 119.940 1.00 29.65  ? 4241 SER A CB    1 
ATOM   19938 O  OG    . SER A 1 4241 ? 166.204 154.653 119.234 1.00 32.86  ? 4241 SER A OG    1 
ATOM   19939 N  N     . ALA A 1 4242 ? 165.038 154.078 121.910 1.00 24.87  ? 4242 ALA A N     1 
ATOM   19940 C  CA    . ALA A 1 4242 ? 163.973 154.571 122.778 1.00 21.85  ? 4242 ALA A CA    1 
ATOM   19941 C  C     . ALA A 1 4242 ? 164.133 154.042 124.197 1.00 21.18  ? 4242 ALA A C     1 
ATOM   19942 O  O     . ALA A 1 4242 ? 164.079 154.807 125.169 1.00 21.51  ? 4242 ALA A O     1 
ATOM   19943 C  CB    . ALA A 1 4242 ? 162.611 154.177 122.208 1.00 20.55  ? 4242 ALA A CB    1 
ATOM   19944 N  N     . LEU A 1 4243 ? 164.342 152.731 124.333 1.00 21.49  ? 4243 LEU A N     1 
ATOM   19945 C  CA    . LEU A 1 4243 ? 164.506 152.139 125.656 1.00 19.95  ? 4243 LEU A CA    1 
ATOM   19946 C  C     . LEU A 1 4243 ? 165.732 152.703 126.359 1.00 23.14  ? 4243 LEU A C     1 
ATOM   19947 O  O     . LEU A 1 4243 ? 165.666 153.084 127.532 1.00 26.56  ? 4243 LEU A O     1 
ATOM   19948 C  CB    . LEU A 1 4243 ? 164.605 150.616 125.543 1.00 20.10  ? 4243 LEU A CB    1 
ATOM   19949 C  CG    . LEU A 1 4243 ? 163.434 149.885 124.883 1.00 27.78  ? 4243 LEU A CG    1 
ATOM   19950 C  CD1   . LEU A 1 4243 ? 163.704 148.390 124.820 1.00 29.52  ? 4243 LEU A CD1   1 
ATOM   19951 C  CD2   . LEU A 1 4243 ? 162.140 150.167 125.623 1.00 23.27  ? 4243 LEU A CD2   1 
ATOM   19952 N  N     . LYS A 1 4244 ? 166.862 152.774 125.651 1.00 21.51  ? 4244 LYS A N     1 
ATOM   19953 C  CA    . LYS A 1 4244 ? 168.092 153.262 126.265 1.00 15.41  ? 4244 LYS A CA    1 
ATOM   19954 C  C     . LYS A 1 4244 ? 167.932 154.698 126.745 1.00 17.11  ? 4244 LYS A C     1 
ATOM   19955 O  O     . LYS A 1 4244 ? 168.310 155.033 127.874 1.00 18.05  ? 4244 LYS A O     1 
ATOM   19956 C  CB    . LYS A 1 4244 ? 169.250 153.155 125.274 1.00 13.25  ? 4244 LYS A CB    1 
ATOM   19957 C  CG    . LYS A 1 4244 ? 169.798 151.753 125.106 1.00 19.66  ? 4244 LYS A CG    1 
ATOM   19958 C  CD    . LYS A 1 4244 ? 171.101 151.768 124.329 1.00 24.32  ? 4244 LYS A CD    1 
ATOM   19959 C  CE    . LYS A 1 4244 ? 170.899 152.316 122.927 1.00 22.40  ? 4244 LYS A CE    1 
ATOM   19960 N  NZ    . LYS A 1 4244 ? 172.132 152.197 122.102 1.00 30.73  ? 4244 LYS A NZ    1 
ATOM   19961 N  N     . THR A 1 4245 ? 167.361 155.561 125.901 1.00 16.27  ? 4245 THR A N     1 
ATOM   19962 C  CA    . THR A 1 4245 ? 167.182 156.956 126.282 1.00 13.02  ? 4245 THR A CA    1 
ATOM   19963 C  C     . THR A 1 4245 ? 166.221 157.093 127.454 1.00 16.55  ? 4245 THR A C     1 
ATOM   19964 O  O     . THR A 1 4245 ? 166.468 157.881 128.373 1.00 18.97  ? 4245 THR A O     1 
ATOM   19965 C  CB    . THR A 1 4245 ? 166.691 157.768 125.085 1.00 17.70  ? 4245 THR A CB    1 
ATOM   19966 O  OG1   . THR A 1 4245 ? 167.544 157.526 123.960 1.00 26.04  ? 4245 THR A OG1   1 
ATOM   19967 C  CG2   . THR A 1 4245 ? 166.700 159.253 125.410 1.00 20.26  ? 4245 THR A CG2   1 
ATOM   19968 N  N     . LEU A 1 4246 ? 165.118 156.338 127.447 1.00 15.12  ? 4246 LEU A N     1 
ATOM   19969 C  CA    . LEU A 1 4246 ? 164.172 156.447 128.551 1.00 14.32  ? 4246 LEU A CA    1 
ATOM   19970 C  C     . LEU A 1 4246 ? 164.794 155.986 129.863 1.00 16.46  ? 4246 LEU A C     1 
ATOM   19971 O  O     . LEU A 1 4246 ? 164.645 156.657 130.889 1.00 20.10  ? 4246 LEU A O     1 
ATOM   19972 C  CB    . LEU A 1 4246 ? 162.898 155.666 128.239 1.00 16.89  ? 4246 LEU A CB    1 
ATOM   19973 C  CG    . LEU A 1 4246 ? 161.917 156.440 127.355 1.00 15.98  ? 4246 LEU A CG    1 
ATOM   19974 C  CD1   . LEU A 1 4246 ? 160.581 155.734 127.270 1.00 17.47  ? 4246 LEU A CD1   1 
ATOM   19975 C  CD2   . LEU A 1 4246 ? 161.736 157.859 127.869 1.00 13.08  ? 4246 LEU A CD2   1 
ATOM   19976 N  N     . MET A 1 4247 ? 165.526 154.868 129.849 1.00 18.11  ? 4247 MET A N     1 
ATOM   19977 C  CA    . MET A 1 4247 ? 166.210 154.435 131.066 1.00 15.10  ? 4247 MET A CA    1 
ATOM   19978 C  C     . MET A 1 4247 ? 167.241 155.458 131.523 1.00 15.06  ? 4247 MET A C     1 
ATOM   19979 O  O     . MET A 1 4247 ? 167.359 155.731 132.723 1.00 17.78  ? 4247 MET A O     1 
ATOM   19980 C  CB    . MET A 1 4247 ? 166.880 153.079 130.857 1.00 17.11  ? 4247 MET A CB    1 
ATOM   19981 C  CG    . MET A 1 4247 ? 166.007 152.007 130.252 1.00 15.53  ? 4247 MET A CG    1 
ATOM   19982 S  SD    . MET A 1 4247 ? 165.262 150.968 131.508 1.00 30.25  ? 4247 MET A SD    1 
ATOM   19983 C  CE    . MET A 1 4247 ? 166.502 149.683 131.580 1.00 23.70  ? 4247 MET A CE    1 
ATOM   19984 N  N     . ALA A 1 4248 ? 167.999 156.032 130.589 1.00 17.07  ? 4248 ALA A N     1 
ATOM   19985 C  CA    . ALA A 1 4248 ? 169.065 156.951 130.961 1.00 16.23  ? 4248 ALA A CA    1 
ATOM   19986 C  C     . ALA A 1 4248 ? 168.552 158.316 131.399 1.00 23.84  ? 4248 ALA A C     1 
ATOM   19987 O  O     . ALA A 1 4248 ? 169.288 159.047 132.070 1.00 27.74  ? 4248 ALA A O     1 
ATOM   19988 C  CB    . ALA A 1 4248 ? 170.039 157.123 129.794 1.00 13.47  ? 4248 ALA A CB    1 
ATOM   19989 N  N     . GLN A 1 4249 ? 167.321 158.681 131.040 1.00 18.78  ? 4249 GLN A N     1 
ATOM   19990 C  CA    . GLN A 1 4249 ? 166.819 160.012 131.356 1.00 16.01  ? 4249 GLN A CA    1 
ATOM   19991 C  C     . GLN A 1 4249 ? 165.717 160.043 132.404 1.00 19.40  ? 4249 GLN A C     1 
ATOM   19992 O  O     . GLN A 1 4249 ? 165.752 160.913 133.276 1.00 25.03  ? 4249 GLN A O     1 
ATOM   19993 C  CB    . GLN A 1 4249 ? 166.310 160.702 130.083 1.00 16.45  ? 4249 GLN A CB    1 
ATOM   19994 C  CG    . GLN A 1 4249 ? 167.353 160.808 128.981 1.00 23.15  ? 4249 GLN A CG    1 
ATOM   19995 C  CD    . GLN A 1 4249 ? 167.987 162.181 128.904 1.00 34.32  ? 4249 GLN A CD    1 
ATOM   19996 O  OE1   . GLN A 1 4249 ? 167.354 163.147 128.479 1.00 32.21  ? 4249 GLN A OE1   1 
ATOM   19997 N  NE2   . GLN A 1 4249 ? 169.247 162.274 129.312 1.00 36.50  ? 4249 GLN A NE2   1 
ATOM   19998 N  N     . SER A 1 4250 ? 164.743 159.135 132.356 1.00 17.75  ? 4250 SER A N     1 
ATOM   19999 C  CA    . SER A 1 4250 ? 163.579 159.214 133.229 1.00 17.14  ? 4250 SER A CA    1 
ATOM   20000 C  C     . SER A 1 4250 ? 163.525 158.094 134.254 1.00 17.61  ? 4250 SER A C     1 
ATOM   20001 O  O     . SER A 1 4250 ? 163.253 158.355 135.432 1.00 23.94  ? 4250 SER A O     1 
ATOM   20002 C  CB    . SER A 1 4250 ? 162.295 159.208 132.385 1.00 17.53  ? 4250 SER A CB    1 
ATOM   20003 O  OG    . SER A 1 4250 ? 162.411 160.078 131.273 1.00 15.66  ? 4250 SER A OG    1 
ATOM   20004 N  N     . ILE A 1 4251 ? 163.774 156.851 133.845 1.00 16.12  ? 4251 ILE A N     1 
ATOM   20005 C  CA    . ILE A 1 4251 ? 163.581 155.717 134.745 1.00 17.08  ? 4251 ILE A CA    1 
ATOM   20006 C  C     . ILE A 1 4251 ? 164.698 155.646 135.777 1.00 18.80  ? 4251 ILE A C     1 
ATOM   20007 O  O     . ILE A 1 4251 ? 164.460 155.763 136.985 1.00 25.95  ? 4251 ILE A O     1 
ATOM   20008 C  CB    . ILE A 1 4251 ? 163.477 154.406 133.944 1.00 15.73  ? 4251 ILE A CB    1 
ATOM   20009 C  CG1   . ILE A 1 4251 ? 162.605 154.599 132.704 1.00 14.77  ? 4251 ILE A CG1   1 
ATOM   20010 C  CG2   . ILE A 1 4251 ? 162.923 153.296 134.819 1.00 16.75  ? 4251 ILE A CG2   1 
ATOM   20011 C  CD1   . ILE A 1 4251 ? 161.155 154.873 133.015 1.00 12.68  ? 4251 ILE A CD1   1 
ATOM   20012 N  N     . TYR A 1 4252 ? 165.933 155.456 135.319 1.00 18.33  ? 4252 TYR A N     1 
ATOM   20013 C  CA    . TYR A 1 4252 ? 167.069 155.310 136.219 1.00 17.23  ? 4252 TYR A CA    1 
ATOM   20014 C  C     . TYR A 1 4252 ? 167.939 156.555 136.295 1.00 20.07  ? 4252 TYR A C     1 
ATOM   20015 O  O     . TYR A 1 4252 ? 168.574 156.790 137.327 1.00 25.02  ? 4252 TYR A O     1 
ATOM   20016 C  CB    . TYR A 1 4252 ? 167.933 154.118 135.793 1.00 15.23  ? 4252 TYR A CB    1 
ATOM   20017 C  CG    . TYR A 1 4252 ? 167.350 152.776 136.173 1.00 15.23  ? 4252 TYR A CG    1 
ATOM   20018 C  CD1   . TYR A 1 4252 ? 166.381 152.171 135.384 1.00 16.70  ? 4252 TYR A CD1   1 
ATOM   20019 C  CD2   . TYR A 1 4252 ? 167.764 152.116 137.320 1.00 18.63  ? 4252 TYR A CD2   1 
ATOM   20020 C  CE1   . TYR A 1 4252 ? 165.844 150.946 135.725 1.00 14.15  ? 4252 TYR A CE1   1 
ATOM   20021 C  CE2   . TYR A 1 4252 ? 167.231 150.890 137.670 1.00 19.53  ? 4252 TYR A CE2   1 
ATOM   20022 C  CZ    . TYR A 1 4252 ? 166.272 150.310 136.869 1.00 16.21  ? 4252 TYR A CZ    1 
ATOM   20023 O  OH    . TYR A 1 4252 ? 165.739 149.090 137.213 1.00 17.11  ? 4252 TYR A OH    1 
ATOM   20024 N  N     . GLY A 1 4253 ? 167.984 157.354 135.230 1.00 16.36  ? 4253 GLY A N     1 
ATOM   20025 C  CA    . GLY A 1 4253 ? 168.757 158.580 135.245 1.00 14.22  ? 4253 GLY A CA    1 
ATOM   20026 C  C     . GLY A 1 4253 ? 168.109 159.737 135.968 1.00 20.00  ? 4253 GLY A C     1 
ATOM   20027 O  O     . GLY A 1 4253 ? 168.761 160.765 136.171 1.00 28.74  ? 4253 GLY A O     1 
ATOM   20028 N  N     . GLY A 1 4254 ? 166.840 159.599 136.356 1.00 16.94  ? 4254 GLY A N     1 
ATOM   20029 C  CA    . GLY A 1 4254 ? 166.196 160.651 137.123 1.00 12.95  ? 4254 GLY A CA    1 
ATOM   20030 C  C     . GLY A 1 4254 ? 166.802 160.819 138.503 1.00 15.93  ? 4254 GLY A C     1 
ATOM   20031 O  O     . GLY A 1 4254 ? 166.962 161.942 138.988 1.00 21.34  ? 4254 GLY A O     1 
ATOM   20032 N  N     . ARG A 1 4255 ? 167.149 159.706 139.153 1.00 19.09  ? 4255 ARG A N     1 
ATOM   20033 C  CA    . ARG A 1 4255 ? 167.772 159.779 140.469 1.00 18.76  ? 4255 ARG A CA    1 
ATOM   20034 C  C     . ARG A 1 4255 ? 169.201 160.299 140.389 1.00 18.06  ? 4255 ARG A C     1 
ATOM   20035 O  O     . ARG A 1 4255 ? 169.703 160.880 141.357 1.00 25.89  ? 4255 ARG A O     1 
ATOM   20036 C  CB    . ARG A 1 4255 ? 167.757 158.405 141.136 1.00 21.85  ? 4255 ARG A CB    1 
ATOM   20037 C  CG    . ARG A 1 4255 ? 166.413 157.706 141.101 1.00 25.45  ? 4255 ARG A CG    1 
ATOM   20038 C  CD    . ARG A 1 4255 ? 166.453 156.416 141.899 1.00 26.52  ? 4255 ARG A CD    1 
ATOM   20039 N  NE    . ARG A 1 4255 ? 165.126 155.844 142.087 1.00 31.52  ? 4255 ARG A NE    1 
ATOM   20040 C  CZ    . ARG A 1 4255 ? 164.248 156.269 142.985 1.00 34.14  ? 4255 ARG A CZ    1 
ATOM   20041 N  NH1   . ARG A 1 4255 ? 164.524 157.275 143.799 1.00 29.75  ? 4255 ARG A NH1   1 
ATOM   20042 N  NH2   . ARG A 1 4255 ? 163.065 155.669 143.070 1.00 35.35  ? 4255 ARG A NH2   1 
ATOM   20043 N  N     . VAL A 1 4256 ? 169.867 160.101 139.252 1.00 16.15  ? 4256 VAL A N     1 
ATOM   20044 C  CA    . VAL A 1 4256 ? 171.279 160.440 139.138 1.00 17.94  ? 4256 VAL A CA    1 
ATOM   20045 C  C     . VAL A 1 4256 ? 171.440 161.952 139.069 1.00 24.10  ? 4256 VAL A C     1 
ATOM   20046 O  O     . VAL A 1 4256 ? 170.850 162.620 138.210 1.00 27.56  ? 4256 VAL A O     1 
ATOM   20047 C  CB    . VAL A 1 4256 ? 171.894 159.757 137.908 1.00 16.83  ? 4256 VAL A CB    1 
ATOM   20048 C  CG1   . VAL A 1 4256 ? 173.254 160.350 137.599 1.00 22.32  ? 4256 VAL A CG1   1 
ATOM   20049 C  CG2   . VAL A 1 4256 ? 172.000 158.257 138.133 1.00 15.86  ? 4256 VAL A CG2   1 
ATOM   20050 N  N     . ASP A 1 4257 ? 172.248 162.499 139.980 1.00 24.18  ? 4257 ASP A N     1 
ATOM   20051 C  CA    . ASP A 1 4257 ? 172.570 163.921 139.997 1.00 26.55  ? 4257 ASP A CA    1 
ATOM   20052 C  C     . ASP A 1 4257 ? 174.056 164.170 139.767 1.00 30.58  ? 4257 ASP A C     1 
ATOM   20053 O  O     . ASP A 1 4257 ? 174.549 165.269 140.041 1.00 35.35  ? 4257 ASP A O     1 
ATOM   20054 C  CB    . ASP A 1 4257 ? 172.119 164.558 141.314 1.00 27.48  ? 4257 ASP A CB    1 
ATOM   20055 C  CG    . ASP A 1 4257 ? 172.544 163.755 142.529 1.00 36.67  ? 4257 ASP A CG    1 
ATOM   20056 O  OD1   . ASP A 1 4257 ? 173.710 163.313 142.581 1.00 41.08  ? 4257 ASP A OD1   1 
ATOM   20057 O  OD2   . ASP A 1 4257 ? 171.706 163.565 143.436 1.00 43.66  ? 4257 ASP A OD2   1 
ATOM   20058 N  N     . ASN A 1 4258 ? 174.778 163.170 139.268 1.00 28.38  ? 4258 ASN A N     1 
ATOM   20059 C  CA    . ASN A 1 4258 ? 176.208 163.268 139.024 1.00 23.91  ? 4258 ASN A CA    1 
ATOM   20060 C  C     . ASN A 1 4258 ? 176.472 163.009 137.549 1.00 26.04  ? 4258 ASN A C     1 
ATOM   20061 O  O     . ASN A 1 4258 ? 175.864 162.118 136.949 1.00 31.19  ? 4258 ASN A O     1 
ATOM   20062 C  CB    . ASN A 1 4258 ? 176.986 162.267 139.894 1.00 25.41  ? 4258 ASN A CB    1 
ATOM   20063 C  CG    . ASN A 1 4258 ? 178.489 162.492 139.859 1.00 32.93  ? 4258 ASN A CG    1 
ATOM   20064 O  OD1   . ASN A 1 4258 ? 179.063 162.813 138.819 1.00 40.74  ? 4258 ASN A OD1   1 
ATOM   20065 N  ND2   . ASN A 1 4258 ? 179.134 162.316 141.005 1.00 34.46  ? 4258 ASN A ND2   1 
ATOM   20066 N  N     . GLU A 1 4259 ? 177.376 163.799 136.966 1.00 24.46  ? 4259 GLU A N     1 
ATOM   20067 C  CA    . GLU A 1 4259 ? 177.715 163.618 135.559 1.00 22.37  ? 4259 GLU A CA    1 
ATOM   20068 C  C     . GLU A 1 4259 ? 178.366 162.262 135.316 1.00 21.84  ? 4259 GLU A C     1 
ATOM   20069 O  O     . GLU A 1 4259 ? 178.061 161.587 134.325 1.00 25.58  ? 4259 GLU A O     1 
ATOM   20070 C  CB    . GLU A 1 4259 ? 178.634 164.748 135.096 1.00 33.40  ? 4259 GLU A CB    1 
ATOM   20071 C  CG    . GLU A 1 4259 ? 179.408 164.448 133.823 1.00 41.51  ? 4259 GLU A CG    1 
ATOM   20072 C  CD    . GLU A 1 4259 ? 180.566 165.402 133.607 1.00 51.75  ? 4259 GLU A CD    1 
ATOM   20073 O  OE1   . GLU A 1 4259 ? 181.391 165.143 132.706 1.00 53.06  ? 4259 GLU A OE1   1 
ATOM   20074 O  OE2   . GLU A 1 4259 ? 180.651 166.411 134.339 1.00 47.05  ? 4259 GLU A OE2   1 
ATOM   20075 N  N     . PHE A 1 4260 ? 179.255 161.840 136.215 1.00 21.96  ? 4260 PHE A N     1 
ATOM   20076 C  CA    . PHE A 1 4260 ? 179.971 160.583 136.030 1.00 19.25  ? 4260 PHE A CA    1 
ATOM   20077 C  C     . PHE A 1 4260 ? 179.099 159.373 136.339 1.00 22.14  ? 4260 PHE A C     1 
ATOM   20078 O  O     . PHE A 1 4260 ? 179.250 158.328 135.696 1.00 26.96  ? 4260 PHE A O     1 
ATOM   20079 C  CB    . PHE A 1 4260 ? 181.233 160.587 136.890 1.00 19.40  ? 4260 PHE A CB    1 
ATOM   20080 C  CG    . PHE A 1 4260 ? 182.127 161.761 136.623 1.00 25.57  ? 4260 PHE A CG    1 
ATOM   20081 C  CD1   . PHE A 1 4260 ? 183.016 161.743 135.563 1.00 26.80  ? 4260 PHE A CD1   1 
ATOM   20082 C  CD2   . PHE A 1 4260 ? 182.054 162.897 137.410 1.00 28.85  ? 4260 PHE A CD2   1 
ATOM   20083 C  CE1   . PHE A 1 4260 ? 183.830 162.826 135.305 1.00 28.30  ? 4260 PHE A CE1   1 
ATOM   20084 C  CE2   . PHE A 1 4260 ? 182.864 163.984 137.156 1.00 31.56  ? 4260 PHE A CE2   1 
ATOM   20085 C  CZ    . PHE A 1 4260 ? 183.753 163.948 136.102 1.00 31.25  ? 4260 PHE A CZ    1 
ATOM   20086 N  N     . ASP A 1 4261 ? 178.178 159.490 137.298 1.00 21.53  ? 4261 ASP A N     1 
ATOM   20087 C  CA    . ASP A 1 4261 ? 177.196 158.430 137.499 1.00 18.95  ? 4261 ASP A CA    1 
ATOM   20088 C  C     . ASP A 1 4261 ? 176.312 158.269 136.270 1.00 19.12  ? 4261 ASP A C     1 
ATOM   20089 O  O     . ASP A 1 4261 ? 175.995 157.145 135.864 1.00 21.74  ? 4261 ASP A O     1 
ATOM   20090 C  CB    . ASP A 1 4261 ? 176.348 158.724 138.735 1.00 20.02  ? 4261 ASP A CB    1 
ATOM   20091 C  CG    . ASP A 1 4261 ? 177.139 158.626 140.020 1.00 26.71  ? 4261 ASP A CG    1 
ATOM   20092 O  OD1   . ASP A 1 4261 ? 178.251 158.058 139.994 1.00 27.85  ? 4261 ASP A OD1   1 
ATOM   20093 O  OD2   . ASP A 1 4261 ? 176.646 159.116 141.057 1.00 30.97  ? 4261 ASP A OD2   1 
ATOM   20094 N  N     . GLN A 1 4262 ? 175.905 159.387 135.664 1.00 16.96  ? 4262 GLN A N     1 
ATOM   20095 C  CA    . GLN A 1 4262 ? 175.140 159.322 134.424 1.00 14.02  ? 4262 GLN A CA    1 
ATOM   20096 C  C     . GLN A 1 4262 ? 175.963 158.699 133.305 1.00 18.30  ? 4262 GLN A C     1 
ATOM   20097 O  O     . GLN A 1 4262 ? 175.435 157.936 132.489 1.00 24.08  ? 4262 GLN A O     1 
ATOM   20098 C  CB    . GLN A 1 4262 ? 174.660 160.717 134.028 1.00 15.55  ? 4262 GLN A CB    1 
ATOM   20099 C  CG    . GLN A 1 4262 ? 173.779 160.741 132.791 1.00 21.28  ? 4262 GLN A CG    1 
ATOM   20100 C  CD    . GLN A 1 4262 ? 172.403 160.160 133.044 1.00 21.83  ? 4262 GLN A CD    1 
ATOM   20101 O  OE1   . GLN A 1 4262 ? 171.668 160.633 133.909 1.00 22.65  ? 4262 GLN A OE1   1 
ATOM   20102 N  NE2   . GLN A 1 4262 ? 172.048 159.129 132.288 1.00 20.69  ? 4262 GLN A NE2   1 
ATOM   20103 N  N     . ARG A 1 4263 ? 177.258 159.018 133.246 1.00 18.84  ? 4263 ARG A N     1 
ATOM   20104 C  CA    . ARG A 1 4263 ? 178.130 158.402 132.250 1.00 17.87  ? 4263 ARG A CA    1 
ATOM   20105 C  C     . ARG A 1 4263 ? 178.205 156.892 132.440 1.00 18.22  ? 4263 ARG A C     1 
ATOM   20106 O  O     . ARG A 1 4263 ? 178.145 156.131 131.468 1.00 23.28  ? 4263 ARG A O     1 
ATOM   20107 C  CB    . ARG A 1 4263 ? 179.525 159.022 132.328 1.00 19.79  ? 4263 ARG A CB    1 
ATOM   20108 C  CG    . ARG A 1 4263 ? 180.508 158.490 131.302 1.00 25.39  ? 4263 ARG A CG    1 
ATOM   20109 C  CD    . ARG A 1 4263 ? 181.847 159.200 131.412 1.00 29.76  ? 4263 ARG A CD    1 
ATOM   20110 N  NE    . ARG A 1 4263 ? 182.530 158.885 132.661 1.00 33.51  ? 4263 ARG A NE    1 
ATOM   20111 C  CZ    . ARG A 1 4263 ? 183.652 159.461 133.069 1.00 34.76  ? 4263 ARG A CZ    1 
ATOM   20112 N  NH1   . ARG A 1 4263 ? 184.247 160.400 132.352 1.00 35.59  ? 4263 ARG A NH1   1 
ATOM   20113 N  NH2   . ARG A 1 4263 ? 184.193 159.082 134.223 1.00 36.20  ? 4263 ARG A NH2   1 
ATOM   20114 N  N     . LEU A 1 4264 ? 178.334 156.441 133.690 1.00 14.81  ? 4264 LEU A N     1 
ATOM   20115 C  CA    . LEU A 1 4264 ? 178.379 155.008 133.965 1.00 16.88  ? 4264 LEU A CA    1 
ATOM   20116 C  C     . LEU A 1 4264 ? 177.063 154.331 133.598 1.00 18.87  ? 4264 LEU A C     1 
ATOM   20117 O  O     . LEU A 1 4264 ? 177.056 153.230 133.030 1.00 25.07  ? 4264 LEU A O     1 
ATOM   20118 C  CB    . LEU A 1 4264 ? 178.713 154.775 135.438 1.00 14.34  ? 4264 LEU A CB    1 
ATOM   20119 C  CG    . LEU A 1 4264 ? 178.747 153.327 135.921 1.00 13.27  ? 4264 LEU A CG    1 
ATOM   20120 C  CD1   . LEU A 1 4264 ? 179.684 152.507 135.056 1.00 17.28  ? 4264 LEU A CD1   1 
ATOM   20121 C  CD2   . LEU A 1 4264 ? 179.165 153.265 137.379 1.00 14.08  ? 4264 LEU A CD2   1 
ATOM   20122 N  N     . LEU A 1 4265 ? 175.938 154.973 133.921 1.00 17.48  ? 4265 LEU A N     1 
ATOM   20123 C  CA    . LEU A 1 4265 ? 174.637 154.416 133.564 1.00 14.35  ? 4265 LEU A CA    1 
ATOM   20124 C  C     . LEU A 1 4265 ? 174.477 154.320 132.052 1.00 16.14  ? 4265 LEU A C     1 
ATOM   20125 O  O     . LEU A 1 4265 ? 173.968 153.318 131.535 1.00 21.99  ? 4265 LEU A O     1 
ATOM   20126 C  CB    . LEU A 1 4265 ? 173.521 155.265 134.172 1.00 13.14  ? 4265 LEU A CB    1 
ATOM   20127 C  CG    . LEU A 1 4265 ? 172.097 154.726 134.034 1.00 14.43  ? 4265 LEU A CG    1 
ATOM   20128 C  CD1   . LEU A 1 4265 ? 171.831 153.652 135.075 1.00 15.24  ? 4265 LEU A CD1   1 
ATOM   20129 C  CD2   . LEU A 1 4265 ? 171.088 155.854 134.155 1.00 16.79  ? 4265 LEU A CD2   1 
ATOM   20130 N  N     . ASN A 1 4266 ? 174.906 155.356 131.327 1.00 17.29  ? 4266 ASN A N     1 
ATOM   20131 C  CA    . ASN A 1 4266 ? 174.848 155.320 129.870 1.00 18.98  ? 4266 ASN A CA    1 
ATOM   20132 C  C     . ASN A 1 4266 ? 175.734 154.216 129.312 1.00 22.73  ? 4266 ASN A C     1 
ATOM   20133 O  O     . ASN A 1 4266 ? 175.359 153.539 128.350 1.00 26.36  ? 4266 ASN A O     1 
ATOM   20134 C  CB    . ASN A 1 4266 ? 175.256 156.676 129.294 1.00 18.54  ? 4266 ASN A CB    1 
ATOM   20135 C  CG    . ASN A 1 4266 ? 174.290 157.782 129.666 1.00 22.21  ? 4266 ASN A CG    1 
ATOM   20136 O  OD1   . ASN A 1 4266 ? 173.256 157.536 130.283 1.00 25.39  ? 4266 ASN A OD1   1 
ATOM   20137 N  ND2   . ASN A 1 4266 ? 174.625 159.011 129.290 1.00 22.15  ? 4266 ASN A ND2   1 
ATOM   20138 N  N     . THR A 1 4267 ? 176.920 154.029 129.896 1.00 21.36  ? 4267 THR A N     1 
ATOM   20139 C  CA    . THR A 1 4267 ? 177.806 152.953 129.462 1.00 25.19  ? 4267 THR A CA    1 
ATOM   20140 C  C     . THR A 1 4267 ? 177.139 151.595 129.638 1.00 26.28  ? 4267 THR A C     1 
ATOM   20141 O  O     . THR A 1 4267 ? 177.143 150.761 128.722 1.00 28.73  ? 4267 THR A O     1 
ATOM   20142 C  CB    . THR A 1 4267 ? 179.121 153.011 130.242 1.00 25.04  ? 4267 THR A CB    1 
ATOM   20143 O  OG1   . THR A 1 4267 ? 179.890 154.138 129.804 1.00 38.38  ? 4267 THR A OG1   1 
ATOM   20144 C  CG2   . THR A 1 4267 ? 179.928 151.738 130.034 1.00 26.40  ? 4267 THR A CG2   1 
ATOM   20145 N  N     . PHE A 1 4268 ? 176.546 151.362 130.811 1.00 24.94  ? 4268 PHE A N     1 
ATOM   20146 C  CA    . PHE A 1 4268 ? 175.866 150.093 131.052 1.00 20.01  ? 4268 PHE A CA    1 
ATOM   20147 C  C     . PHE A 1 4268 ? 174.710 149.890 130.080 1.00 19.94  ? 4268 PHE A C     1 
ATOM   20148 O  O     . PHE A 1 4268 ? 174.531 148.794 129.533 1.00 24.05  ? 4268 PHE A O     1 
ATOM   20149 C  CB    . PHE A 1 4268 ? 175.367 150.029 132.495 1.00 17.07  ? 4268 PHE A CB    1 
ATOM   20150 C  CG    . PHE A 1 4268 ? 176.399 149.549 133.473 1.00 21.81  ? 4268 PHE A CG    1 
ATOM   20151 C  CD1   . PHE A 1 4268 ? 177.187 148.448 133.183 1.00 28.02  ? 4268 PHE A CD1   1 
ATOM   20152 C  CD2   . PHE A 1 4268 ? 176.581 150.195 134.683 1.00 19.67  ? 4268 PHE A CD2   1 
ATOM   20153 C  CE1   . PHE A 1 4268 ? 178.137 148.003 134.082 1.00 27.54  ? 4268 PHE A CE1   1 
ATOM   20154 C  CE2   . PHE A 1 4268 ? 177.527 149.754 135.585 1.00 19.92  ? 4268 PHE A CE2   1 
ATOM   20155 C  CZ    . PHE A 1 4268 ? 178.307 148.657 135.284 1.00 22.43  ? 4268 PHE A CZ    1 
ATOM   20156 N  N     . LEU A 1 4269 ? 173.919 150.940 129.845 1.00 19.21  ? 4269 LEU A N     1 
ATOM   20157 C  CA    . LEU A 1 4269 ? 172.756 150.807 128.973 1.00 17.21  ? 4269 LEU A CA    1 
ATOM   20158 C  C     . LEU A 1 4269 ? 173.163 150.560 127.525 1.00 22.47  ? 4269 LEU A C     1 
ATOM   20159 O  O     . LEU A 1 4269 ? 172.530 149.758 126.828 1.00 24.01  ? 4269 LEU A O     1 
ATOM   20160 C  CB    . LEU A 1 4269 ? 171.876 152.050 129.082 1.00 15.73  ? 4269 LEU A CB    1 
ATOM   20161 C  CG    . LEU A 1 4269 ? 171.000 152.089 130.333 1.00 14.66  ? 4269 LEU A CG    1 
ATOM   20162 C  CD1   . LEU A 1 4269 ? 170.557 153.508 130.643 1.00 15.12  ? 4269 LEU A CD1   1 
ATOM   20163 C  CD2   . LEU A 1 4269 ? 169.808 151.162 130.174 1.00 17.60  ? 4269 LEU A CD2   1 
ATOM   20164 N  N     . GLU A 1 4270 ? 174.209 151.239 127.047 1.00 25.42  ? 4270 GLU A N     1 
ATOM   20165 C  CA    . GLU A 1 4270 ? 174.645 151.032 125.672 1.00 25.10  ? 4270 GLU A CA    1 
ATOM   20166 C  C     . GLU A 1 4270 ? 175.348 149.694 125.498 1.00 26.93  ? 4270 GLU A C     1 
ATOM   20167 O  O     . GLU A 1 4270 ? 175.340 149.136 124.396 1.00 29.29  ? 4270 GLU A O     1 
ATOM   20168 C  CB    . GLU A 1 4270 ? 175.561 152.172 125.217 1.00 30.01  ? 4270 GLU A CB    1 
ATOM   20169 C  CG    . GLU A 1 4270 ? 176.891 152.252 125.948 1.00 42.57  ? 4270 GLU A CG    1 
ATOM   20170 C  CD    . GLU A 1 4270 ? 177.730 153.437 125.510 1.00 54.17  ? 4270 GLU A CD    1 
ATOM   20171 O  OE1   . GLU A 1 4270 ? 177.263 154.213 124.650 1.00 63.87  ? 4270 GLU A OE1   1 
ATOM   20172 O  OE2   . GLU A 1 4270 ? 178.857 153.593 126.027 1.00 50.91  ? 4270 GLU A OE2   1 
ATOM   20173 N  N     . ARG A 1 4271 ? 175.960 149.165 126.560 1.00 28.39  ? 4271 ARG A N     1 
ATOM   20174 C  CA    . ARG A 1 4271 ? 176.564 147.842 126.461 1.00 30.35  ? 4271 ARG A CA    1 
ATOM   20175 C  C     . ARG A 1 4271 ? 175.512 146.740 126.484 1.00 27.51  ? 4271 ARG A C     1 
ATOM   20176 O  O     . ARG A 1 4271 ? 175.633 145.751 125.753 1.00 30.24  ? 4271 ARG A O     1 
ATOM   20177 C  CB    . ARG A 1 4271 ? 177.568 147.633 127.594 1.00 31.87  ? 4271 ARG A CB    1 
ATOM   20178 C  CG    . ARG A 1 4271 ? 178.725 146.718 127.230 1.00 36.98  ? 4271 ARG A CG    1 
ATOM   20179 C  CD    . ARG A 1 4271 ? 179.747 146.650 128.351 1.00 50.48  ? 4271 ARG A CD    1 
ATOM   20180 N  NE    . ARG A 1 4271 ? 179.112 146.593 129.662 1.00 49.91  ? 4271 ARG A NE    1 
ATOM   20181 C  CZ    . ARG A 1 4271 ? 178.627 145.489 130.213 1.00 47.32  ? 4271 ARG A CZ    1 
ATOM   20182 N  NH1   . ARG A 1 4271 ? 178.684 144.323 129.590 1.00 52.28  ? 4271 ARG A NH1   1 
ATOM   20183 N  NH2   . ARG A 1 4271 ? 178.071 145.555 131.419 1.00 38.07  ? 4271 ARG A NH2   1 
ATOM   20184 N  N     . LEU A 1 4272 ? 174.473 146.893 127.307 1.00 24.54  ? 4272 LEU A N     1 
ATOM   20185 C  CA    . LEU A 1 4272 ? 173.516 145.806 127.489 1.00 24.96  ? 4272 LEU A CA    1 
ATOM   20186 C  C     . LEU A 1 4272 ? 172.407 145.843 126.444 1.00 26.11  ? 4272 LEU A C     1 
ATOM   20187 O  O     . LEU A 1 4272 ? 172.126 144.831 125.793 1.00 28.57  ? 4272 LEU A O     1 
ATOM   20188 C  CB    . LEU A 1 4272 ? 172.927 145.862 128.899 1.00 18.78  ? 4272 LEU A CB    1 
ATOM   20189 C  CG    . LEU A 1 4272 ? 173.712 145.092 129.960 1.00 19.25  ? 4272 LEU A CG    1 
ATOM   20190 C  CD1   . LEU A 1 4272 ? 173.311 145.538 131.356 1.00 21.52  ? 4272 LEU A CD1   1 
ATOM   20191 C  CD2   . LEU A 1 4272 ? 173.508 143.597 129.789 1.00 19.91  ? 4272 LEU A CD2   1 
ATOM   20192 N  N     . PHE A 1 4273 ? 171.765 146.996 126.268 1.00 25.59  ? 4273 PHE A N     1 
ATOM   20193 C  CA    . PHE A 1 4273 ? 170.623 147.115 125.361 1.00 25.62  ? 4273 PHE A CA    1 
ATOM   20194 C  C     . PHE A 1 4273 ? 171.139 147.458 123.970 1.00 31.76  ? 4273 PHE A C     1 
ATOM   20195 O  O     . PHE A 1 4273 ? 171.288 148.625 123.605 1.00 32.69  ? 4273 PHE A O     1 
ATOM   20196 C  CB    . PHE A 1 4273 ? 169.634 148.154 125.876 1.00 22.28  ? 4273 PHE A CB    1 
ATOM   20197 C  CG    . PHE A 1 4273 ? 168.915 147.733 127.124 1.00 27.65  ? 4273 PHE A CG    1 
ATOM   20198 C  CD1   . PHE A 1 4273 ? 169.466 147.971 128.372 1.00 27.12  ? 4273 PHE A CD1   1 
ATOM   20199 C  CD2   . PHE A 1 4273 ? 167.692 147.089 127.050 1.00 28.68  ? 4273 PHE A CD2   1 
ATOM   20200 C  CE1   . PHE A 1 4273 ? 168.809 147.581 129.521 1.00 23.46  ? 4273 PHE A CE1   1 
ATOM   20201 C  CE2   . PHE A 1 4273 ? 167.030 146.696 128.197 1.00 25.68  ? 4273 PHE A CE2   1 
ATOM   20202 C  CZ    . PHE A 1 4273 ? 167.590 146.942 129.434 1.00 28.47  ? 4273 PHE A CZ    1 
ATOM   20203 N  N     . THR A 1 4274 ? 171.411 146.421 123.182 1.00 31.15  ? 4274 THR A N     1 
ATOM   20204 C  CA    . THR A 1 4274 ? 171.910 146.590 121.826 1.00 31.12  ? 4274 THR A CA    1 
ATOM   20205 C  C     . THR A 1 4274 ? 171.478 145.395 120.991 1.00 37.21  ? 4274 THR A C     1 
ATOM   20206 O  O     . THR A 1 4274 ? 171.033 144.373 121.518 1.00 38.84  ? 4274 THR A O     1 
ATOM   20207 C  CB    . THR A 1 4274 ? 173.436 146.739 121.796 1.00 36.66  ? 4274 THR A CB    1 
ATOM   20208 O  OG1   . THR A 1 4274 ? 173.882 146.834 120.438 1.00 42.99  ? 4274 THR A OG1   1 
ATOM   20209 C  CG2   . THR A 1 4274 ? 174.100 145.543 122.460 1.00 34.62  ? 4274 THR A CG2   1 
ATOM   20210 N  N     . THR A 1 4275 ? 171.607 145.542 119.669 1.00 42.10  ? 4275 THR A N     1 
ATOM   20211 C  CA    . THR A 1 4275 ? 171.231 144.458 118.766 1.00 39.88  ? 4275 THR A CA    1 
ATOM   20212 C  C     . THR A 1 4275 ? 172.114 143.233 118.960 1.00 44.43  ? 4275 THR A C     1 
ATOM   20213 O  O     . THR A 1 4275 ? 171.678 142.107 118.696 1.00 47.82  ? 4275 THR A O     1 
ATOM   20214 C  CB    . THR A 1 4275 ? 171.302 144.931 117.315 1.00 47.16  ? 4275 THR A CB    1 
ATOM   20215 O  OG1   . THR A 1 4275 ? 172.672 145.009 116.902 1.00 54.67  ? 4275 THR A OG1   1 
ATOM   20216 C  CG2   . THR A 1 4275 ? 170.659 146.300 117.169 1.00 48.97  ? 4275 THR A CG2   1 
ATOM   20217 N  N     . ARG A 1 4276 ? 173.352 143.428 119.418 1.00 45.44  ? 4276 ARG A N     1 
ATOM   20218 C  CA    . ARG A 1 4276 ? 174.264 142.312 119.637 1.00 46.26  ? 4276 ARG A CA    1 
ATOM   20219 C  C     . ARG A 1 4276 ? 173.881 141.462 120.839 1.00 45.90  ? 4276 ARG A C     1 
ATOM   20220 O  O     . ARG A 1 4276 ? 174.462 140.387 121.024 1.00 55.72  ? 4276 ARG A O     1 
ATOM   20221 C  CB    . ARG A 1 4276 ? 175.693 142.830 119.807 1.00 39.10  ? 4276 ARG A CB    1 
ATOM   20222 C  CG    . ARG A 1 4276 ? 176.084 143.897 118.801 1.00 43.92  ? 4276 ARG A CG    1 
ATOM   20223 C  CD    . ARG A 1 4276 ? 176.837 143.298 117.624 1.00 58.54  ? 4276 ARG A CD    1 
ATOM   20224 N  NE    . ARG A 1 4276 ? 175.942 142.649 116.673 1.00 68.51  ? 4276 ARG A NE    1 
ATOM   20225 C  CZ    . ARG A 1 4276 ? 175.145 143.291 115.829 1.00 67.47  ? 4276 ARG A CZ    1 
ATOM   20226 N  NH1   . ARG A 1 4276 ? 175.110 144.613 115.779 1.00 65.50  ? 4276 ARG A NH1   1 
ATOM   20227 N  NH2   . ARG A 1 4276 ? 174.363 142.589 115.014 1.00 59.34  ? 4276 ARG A NH2   1 
ATOM   20228 N  N     . SER A 1 4277 ? 172.928 141.912 121.657 1.00 38.08  ? 4277 SER A N     1 
ATOM   20229 C  CA    . SER A 1 4277 ? 172.513 141.139 122.821 1.00 38.10  ? 4277 SER A CA    1 
ATOM   20230 C  C     . SER A 1 4277 ? 171.772 139.865 122.440 1.00 43.08  ? 4277 SER A C     1 
ATOM   20231 O  O     . SER A 1 4277 ? 171.671 138.952 123.266 1.00 45.84  ? 4277 SER A O     1 
ATOM   20232 C  CB    . SER A 1 4277 ? 171.635 141.995 123.732 1.00 37.02  ? 4277 SER A CB    1 
ATOM   20233 O  OG    . SER A 1 4277 ? 170.301 142.029 123.258 1.00 44.42  ? 4277 SER A OG    1 
ATOM   20234 N  N     . PHE A 1 4278 ? 171.254 139.781 121.218 1.00 45.55  ? 4278 PHE A N     1 
ATOM   20235 C  CA    . PHE A 1 4278 ? 170.528 138.604 120.763 1.00 47.29  ? 4278 PHE A CA    1 
ATOM   20236 C  C     . PHE A 1 4278 ? 171.422 137.588 120.068 1.00 53.86  ? 4278 PHE A C     1 
ATOM   20237 O  O     . PHE A 1 4278 ? 170.924 136.548 119.622 1.00 56.94  ? 4278 PHE A O     1 
ATOM   20238 C  CB    . PHE A 1 4278 ? 169.386 139.019 119.830 1.00 36.95  ? 4278 PHE A CB    1 
ATOM   20239 C  CG    . PHE A 1 4278 ? 168.156 139.478 120.556 1.00 36.64  ? 4278 PHE A CG    1 
ATOM   20240 C  CD1   . PHE A 1 4278 ? 168.115 140.722 121.160 1.00 38.60  ? 4278 PHE A CD1   1 
ATOM   20241 C  CD2   . PHE A 1 4278 ? 167.043 138.660 120.642 1.00 38.62  ? 4278 PHE A CD2   1 
ATOM   20242 C  CE1   . PHE A 1 4278 ? 166.986 141.143 121.834 1.00 35.48  ? 4278 PHE A CE1   1 
ATOM   20243 C  CE2   . PHE A 1 4278 ? 165.913 139.076 121.315 1.00 36.99  ? 4278 PHE A CE2   1 
ATOM   20244 C  CZ    . PHE A 1 4278 ? 165.884 140.319 121.910 1.00 32.79  ? 4278 PHE A CZ    1 
ATOM   20245 N  N     . ASP A 1 4279 ? 172.718 137.859 119.962 1.00 53.97  ? 4279 ASP A N     1 
ATOM   20246 C  CA    . ASP A 1 4279 ? 173.648 136.885 119.418 1.00 62.45  ? 4279 ASP A CA    1 
ATOM   20247 C  C     . ASP A 1 4279 ? 174.037 135.869 120.488 1.00 67.54  ? 4279 ASP A C     1 
ATOM   20248 O  O     . ASP A 1 4279 ? 173.928 136.119 121.691 1.00 67.35  ? 4279 ASP A O     1 
ATOM   20249 C  CB    . ASP A 1 4279 ? 174.897 137.579 118.871 1.00 58.51  ? 4279 ASP A CB    1 
ATOM   20250 C  CG    . ASP A 1 4279 ? 174.580 138.548 117.750 1.00 61.13  ? 4279 ASP A CG    1 
ATOM   20251 O  OD1   . ASP A 1 4279 ? 173.411 138.595 117.315 1.00 58.67  ? 4279 ASP A OD1   1 
ATOM   20252 O  OD2   . ASP A 1 4279 ? 175.501 139.265 117.304 1.00 60.23  ? 4279 ASP A OD2   1 
ATOM   20253 N  N     . SER A 1 4280 ? 174.493 134.703 120.030 1.00 69.62  ? 4280 SER A N     1 
ATOM   20254 C  CA    . SER A 1 4280 ? 174.927 133.655 120.944 1.00 69.55  ? 4280 SER A CA    1 
ATOM   20255 C  C     . SER A 1 4280 ? 176.261 133.972 121.607 1.00 69.26  ? 4280 SER A C     1 
ATOM   20256 O  O     . SER A 1 4280 ? 176.557 133.417 122.671 1.00 63.79  ? 4280 SER A O     1 
ATOM   20257 C  CB    . SER A 1 4280 ? 175.026 132.320 120.204 1.00 74.97  ? 4280 SER A CB    1 
ATOM   20258 O  OG    . SER A 1 4280 ? 175.739 132.465 118.988 1.00 77.51  ? 4280 SER A OG    1 
ATOM   20259 N  N     . GLU A 1 4281 ? 177.063 134.848 121.006 1.00 68.68  ? 4281 GLU A N     1 
ATOM   20260 C  CA    . GLU A 1 4281 ? 178.388 135.183 121.508 1.00 64.26  ? 4281 GLU A CA    1 
ATOM   20261 C  C     . GLU A 1 4281 ? 178.358 136.278 122.569 1.00 62.96  ? 4281 GLU A C     1 
ATOM   20262 O  O     . GLU A 1 4281 ? 179.369 136.489 123.246 1.00 63.89  ? 4281 GLU A O     1 
ATOM   20263 C  CB    . GLU A 1 4281 ? 179.282 135.586 120.318 1.00 68.33  ? 4281 GLU A CB    1 
ATOM   20264 C  CG    . GLU A 1 4281 ? 180.747 135.932 120.606 1.00 71.22  ? 4281 GLU A CG    1 
ATOM   20265 C  CD    . GLU A 1 4281 ? 180.965 137.394 120.961 1.00 68.40  ? 4281 GLU A CD    1 
ATOM   20266 O  OE1   . GLU A 1 4281 ? 181.471 137.675 122.068 1.00 64.83  ? 4281 GLU A OE1   1 
ATOM   20267 O  OE2   . GLU A 1 4281 ? 180.629 138.262 120.129 1.00 74.65  ? 4281 GLU A OE2   1 
ATOM   20268 N  N     . PHE A 1 4282 ? 177.210 136.926 122.774 1.00 61.39  ? 4282 PHE A N     1 
ATOM   20269 C  CA    . PHE A 1 4282 ? 177.133 138.101 123.636 1.00 54.21  ? 4282 PHE A CA    1 
ATOM   20270 C  C     . PHE A 1 4282 ? 177.647 137.803 125.040 1.00 47.80  ? 4282 PHE A C     1 
ATOM   20271 O  O     . PHE A 1 4282 ? 177.361 136.748 125.612 1.00 51.51  ? 4282 PHE A O     1 
ATOM   20272 C  CB    . PHE A 1 4282 ? 175.692 138.605 123.703 1.00 45.00  ? 4282 PHE A CB    1 
ATOM   20273 C  CG    . PHE A 1 4282 ? 175.552 139.954 124.346 1.00 44.44  ? 4282 PHE A CG    1 
ATOM   20274 C  CD1   . PHE A 1 4282 ? 176.197 141.058 123.815 1.00 43.23  ? 4282 PHE A CD1   1 
ATOM   20275 C  CD2   . PHE A 1 4282 ? 174.777 140.118 125.482 1.00 44.66  ? 4282 PHE A CD2   1 
ATOM   20276 C  CE1   . PHE A 1 4282 ? 176.071 142.300 124.405 1.00 42.86  ? 4282 PHE A CE1   1 
ATOM   20277 C  CE2   . PHE A 1 4282 ? 174.647 141.358 126.076 1.00 38.52  ? 4282 PHE A CE2   1 
ATOM   20278 C  CZ    . PHE A 1 4282 ? 175.295 142.450 125.537 1.00 35.21  ? 4282 PHE A CZ    1 
ATOM   20279 N  N     . LYS A 1 4283 ? 178.415 138.742 125.587 1.00 44.71  ? 4283 LYS A N     1 
ATOM   20280 C  CA    . LYS A 1 4283 ? 179.027 138.612 126.903 1.00 43.15  ? 4283 LYS A CA    1 
ATOM   20281 C  C     . LYS A 1 4283 ? 178.306 139.536 127.875 1.00 44.75  ? 4283 LYS A C     1 
ATOM   20282 O  O     . LYS A 1 4283 ? 178.332 140.760 127.704 1.00 54.46  ? 4283 LYS A O     1 
ATOM   20283 C  CB    . LYS A 1 4283 ? 180.513 138.967 126.851 1.00 50.91  ? 4283 LYS A CB    1 
ATOM   20284 C  CG    . LYS A 1 4283 ? 181.464 137.784 126.884 1.00 54.40  ? 4283 LYS A CG    1 
ATOM   20285 C  CD    . LYS A 1 4283 ? 181.459 137.054 125.553 1.00 58.50  ? 4283 LYS A CD    1 
ATOM   20286 C  CE    . LYS A 1 4283 ? 182.197 135.733 125.633 1.00 57.25  ? 4283 LYS A CE    1 
ATOM   20287 N  NZ    . LYS A 1 4283 ? 181.866 134.839 124.490 1.00 53.05  ? 4283 LYS A NZ    1 
ATOM   20288 N  N     . LEU A 1 4284 ? 177.662 138.955 128.889 1.00 39.10  ? 4284 LEU A N     1 
ATOM   20289 C  CA    . LEU A 1 4284 ? 177.091 139.773 129.955 1.00 34.42  ? 4284 LEU A CA    1 
ATOM   20290 C  C     . LEU A 1 4284 ? 178.186 140.466 130.755 1.00 41.97  ? 4284 LEU A C     1 
ATOM   20291 O  O     . LEU A 1 4284 ? 178.069 141.650 131.091 1.00 50.26  ? 4284 LEU A O     1 
ATOM   20292 C  CB    . LEU A 1 4284 ? 176.215 138.916 130.866 1.00 26.30  ? 4284 LEU A CB    1 
ATOM   20293 C  CG    . LEU A 1 4284 ? 174.893 138.451 130.260 1.00 26.85  ? 4284 LEU A CG    1 
ATOM   20294 C  CD1   . LEU A 1 4284 ? 174.114 137.614 131.257 1.00 30.48  ? 4284 LEU A CD1   1 
ATOM   20295 C  CD2   . LEU A 1 4284 ? 174.077 139.652 129.813 1.00 25.49  ? 4284 LEU A CD2   1 
ATOM   20296 N  N     . ALA A 1 4285 ? 179.256 139.741 131.071 1.00 38.30  ? 4285 ALA A N     1 
ATOM   20297 C  CA    . ALA A 1 4285 ? 180.429 140.303 131.719 1.00 38.30  ? 4285 ALA A CA    1 
ATOM   20298 C  C     . ALA A 1 4285 ? 181.666 139.678 131.096 1.00 50.59  ? 4285 ALA A C     1 
ATOM   20299 O  O     . ALA A 1 4285 ? 181.621 138.552 130.595 1.00 52.67  ? 4285 ALA A O     1 
ATOM   20300 C  CB    . ALA A 1 4285 ? 180.415 140.063 133.234 1.00 36.03  ? 4285 ALA A CB    1 
ATOM   20301 N  N     . CYS A 1 4286 ? 182.771 140.417 131.124 1.00 65.53  ? 4286 CYS A N     1 
ATOM   20302 C  CA    . CYS A 1 4286 ? 184.019 139.985 130.510 1.00 65.85  ? 4286 CYS A CA    1 
ATOM   20303 C  C     . CYS A 1 4286 ? 185.092 139.840 131.577 1.00 65.15  ? 4286 CYS A C     1 
ATOM   20304 O  O     . CYS A 1 4286 ? 185.317 140.764 132.367 1.00 67.03  ? 4286 CYS A O     1 
ATOM   20305 C  CB    . CYS A 1 4286 ? 184.472 140.973 129.432 1.00 72.04  ? 4286 CYS A CB    1 
ATOM   20306 S  SG    . CYS A 1 4286 ? 183.198 141.388 128.218 1.00 85.45  ? 4286 CYS A SG    1 
ATOM   20307 N  N     . LYS A 1 4287 ? 185.749 138.679 131.593 1.00 67.20  ? 4287 LYS A N     1 
ATOM   20308 C  CA    . LYS A 1 4287 ? 186.867 138.397 132.494 1.00 72.09  ? 4287 LYS A CA    1 
ATOM   20309 C  C     . LYS A 1 4287 ? 186.459 138.574 133.958 1.00 71.03  ? 4287 LYS A C     1 
ATOM   20310 O  O     . LYS A 1 4287 ? 186.966 139.440 134.675 1.00 71.73  ? 4287 LYS A O     1 
ATOM   20311 C  CB    . LYS A 1 4287 ? 188.080 139.267 132.147 1.00 76.56  ? 4287 LYS A CB    1 
ATOM   20312 C  CG    . LYS A 1 4287 ? 188.833 138.816 130.904 1.00 80.66  ? 4287 LYS A CG    1 
ATOM   20313 C  CD    . LYS A 1 4287 ? 190.060 139.681 130.647 1.00 72.83  ? 4287 LYS A CD    1 
ATOM   20314 C  CE    . LYS A 1 4287 ? 189.723 141.163 130.711 1.00 65.36  ? 4287 LYS A CE    1 
ATOM   20315 N  NZ    . LYS A 1 4287 ? 188.650 141.535 129.747 1.00 64.11  ? 4287 LYS A NZ    1 
ATOM   20316 N  N     . VAL A 1 4288 ? 185.517 137.734 134.394 1.00 65.80  ? 4288 VAL A N     1 
ATOM   20317 C  CA    . VAL A 1 4288 ? 185.108 137.759 135.796 1.00 62.42  ? 4288 VAL A CA    1 
ATOM   20318 C  C     . VAL A 1 4288 ? 186.265 137.335 136.695 1.00 69.87  ? 4288 VAL A C     1 
ATOM   20319 O  O     . VAL A 1 4288 ? 186.447 137.875 137.793 1.00 67.39  ? 4288 VAL A O     1 
ATOM   20320 C  CB    . VAL A 1 4288 ? 183.850 136.896 136.012 1.00 56.71  ? 4288 VAL A CB    1 
ATOM   20321 C  CG1   . VAL A 1 4288 ? 182.724 137.381 135.115 1.00 49.58  ? 4288 VAL A CG1   1 
ATOM   20322 C  CG2   . VAL A 1 4288 ? 184.135 135.427 135.744 1.00 63.56  ? 4288 VAL A CG2   1 
ATOM   20323 N  N     . ASP A 1 4289 ? 187.065 136.371 136.244 1.00 80.18  ? 4289 ASP A N     1 
ATOM   20324 C  CA    . ASP A 1 4289 ? 188.326 136.022 136.880 1.00 83.12  ? 4289 ASP A CA    1 
ATOM   20325 C  C     . ASP A 1 4289 ? 189.191 135.280 135.869 1.00 90.56  ? 4289 ASP A C     1 
ATOM   20326 O  O     . ASP A 1 4289 ? 188.683 134.495 135.064 1.00 89.60  ? 4289 ASP A O     1 
ATOM   20327 C  CB    . ASP A 1 4289 ? 188.113 135.216 138.177 1.00 78.65  ? 4289 ASP A CB    1 
ATOM   20328 C  CG    . ASP A 1 4289 ? 187.683 133.771 137.939 1.00 88.72  ? 4289 ASP A CG    1 
ATOM   20329 O  OD1   . ASP A 1 4289 ? 187.190 133.433 136.845 1.00 86.66  ? 4289 ASP A OD1   1 
ATOM   20330 O  OD2   . ASP A 1 4289 ? 187.844 132.957 138.872 1.00 93.32  ? 4289 ASP A OD2   1 
ATOM   20331 N  N     . GLY A 1 4290 ? 190.490 135.568 135.887 1.00 93.18  ? 4290 GLY A N     1 
ATOM   20332 C  CA    . GLY A 1 4290 ? 191.388 135.004 134.899 1.00 93.51  ? 4290 GLY A CA    1 
ATOM   20333 C  C     . GLY A 1 4290 ? 190.956 135.352 133.489 1.00 97.76  ? 4290 GLY A C     1 
ATOM   20334 O  O     . GLY A 1 4290 ? 191.090 136.499 133.052 1.00 97.18  ? 4290 GLY A O     1 
ATOM   20335 N  N     . HIS A 1 4291 ? 190.432 134.360 132.770 1.00 99.42  ? 4291 HIS A N     1 
ATOM   20336 C  CA    . HIS A 1 4291 ? 189.855 134.569 131.452 1.00 103.57 ? 4291 HIS A CA    1 
ATOM   20337 C  C     . HIS A 1 4291 ? 188.390 134.165 131.360 1.00 99.98  ? 4291 HIS A C     1 
ATOM   20338 O  O     . HIS A 1 4291 ? 187.764 134.415 130.324 1.00 93.16  ? 4291 HIS A O     1 
ATOM   20339 C  CB    . HIS A 1 4291 ? 190.652 133.801 130.385 1.00 105.75 ? 4291 HIS A CB    1 
ATOM   20340 C  CG    . HIS A 1 4291 ? 190.679 132.319 130.600 1.00 109.03 ? 4291 HIS A CG    1 
ATOM   20341 N  ND1   . HIS A 1 4291 ? 191.240 131.737 131.716 1.00 107.92 ? 4291 HIS A ND1   1 
ATOM   20342 C  CD2   . HIS A 1 4291 ? 190.214 131.300 129.839 1.00 108.68 ? 4291 HIS A CD2   1 
ATOM   20343 C  CE1   . HIS A 1 4291 ? 191.119 130.424 131.634 1.00 105.61 ? 4291 HIS A CE1   1 
ATOM   20344 N  NE2   . HIS A 1 4291 ? 190.499 130.133 130.504 1.00 112.63 ? 4291 HIS A NE2   1 
ATOM   20345 N  N     . LYS A 1 4292 ? 187.830 133.552 132.401 1.00 92.35  ? 4292 LYS A N     1 
ATOM   20346 C  CA    . LYS A 1 4292 ? 186.431 133.147 132.383 1.00 76.04  ? 4292 LYS A CA    1 
ATOM   20347 C  C     . LYS A 1 4292 ? 185.516 134.367 132.381 1.00 74.75  ? 4292 LYS A C     1 
ATOM   20348 O  O     . LYS A 1 4292 ? 185.825 135.405 132.971 1.00 75.73  ? 4292 LYS A O     1 
ATOM   20349 C  CB    . LYS A 1 4292 ? 186.122 132.261 133.591 1.00 73.38  ? 4292 LYS A CB    1 
ATOM   20350 C  CG    . LYS A 1 4292 ? 184.762 131.581 133.545 1.00 66.91  ? 4292 LYS A CG    1 
ATOM   20351 C  CD    . LYS A 1 4292 ? 184.491 130.809 134.826 1.00 67.24  ? 4292 LYS A CD    1 
ATOM   20352 C  CE    . LYS A 1 4292 ? 184.063 131.737 135.951 1.00 70.36  ? 4292 LYS A CE    1 
ATOM   20353 N  NZ    . LYS A 1 4292 ? 182.721 132.332 135.704 1.00 74.07  ? 4292 LYS A NZ    1 
ATOM   20354 N  N     . ASP A 1 4293 ? 184.377 134.232 131.706 1.00 71.64  ? 4293 ASP A N     1 
ATOM   20355 C  CA    . ASP A 1 4293 ? 183.417 135.321 131.605 1.00 59.86  ? 4293 ASP A CA    1 
ATOM   20356 C  C     . ASP A 1 4293 ? 182.008 134.749 131.552 1.00 51.69  ? 4293 ASP A C     1 
ATOM   20357 O  O     . ASP A 1 4293 ? 181.803 133.581 131.212 1.00 55.85  ? 4293 ASP A O     1 
ATOM   20358 C  CB    . ASP A 1 4293 ? 183.699 136.199 130.381 1.00 61.37  ? 4293 ASP A CB    1 
ATOM   20359 C  CG    . ASP A 1 4293 ? 183.974 135.388 129.133 1.00 64.66  ? 4293 ASP A CG    1 
ATOM   20360 O  OD1   . ASP A 1 4293 ? 183.941 134.143 129.210 1.00 71.21  ? 4293 ASP A OD1   1 
ATOM   20361 O  OD2   . ASP A 1 4293 ? 184.235 135.998 128.075 1.00 64.21  ? 4293 ASP A OD2   1 
ATOM   20362 N  N     . ILE A 1 4294 ? 181.037 135.592 131.894 1.00 49.32  ? 4294 ILE A N     1 
ATOM   20363 C  CA    . ILE A 1 4294 ? 179.637 135.189 131.963 1.00 47.38  ? 4294 ILE A CA    1 
ATOM   20364 C  C     . ILE A 1 4294 ? 179.026 135.269 130.571 1.00 47.29  ? 4294 ILE A C     1 
ATOM   20365 O  O     . ILE A 1 4294 ? 179.160 136.285 129.879 1.00 50.76  ? 4294 ILE A O     1 
ATOM   20366 C  CB    . ILE A 1 4294 ? 178.861 136.067 132.958 1.00 36.57  ? 4294 ILE A CB    1 
ATOM   20367 C  CG1   . ILE A 1 4294 ? 179.426 135.897 134.368 1.00 32.48  ? 4294 ILE A CG1   1 
ATOM   20368 C  CG2   . ILE A 1 4294 ? 177.382 135.720 132.939 1.00 34.09  ? 4294 ILE A CG2   1 
ATOM   20369 C  CD1   . ILE A 1 4294 ? 178.899 136.905 135.360 1.00 29.46  ? 4294 ILE A CD1   1 
ATOM   20370 N  N     . GLN A 1 4295 ? 178.352 134.198 130.162 1.00 44.82  ? 4295 GLN A N     1 
ATOM   20371 C  CA    . GLN A 1 4295 ? 177.777 134.084 128.832 1.00 46.50  ? 4295 GLN A CA    1 
ATOM   20372 C  C     . GLN A 1 4295 ? 176.310 134.495 128.839 1.00 46.79  ? 4295 GLN A C     1 
ATOM   20373 O  O     . GLN A 1 4295 ? 175.574 134.225 129.792 1.00 48.66  ? 4295 GLN A O     1 
ATOM   20374 C  CB    . GLN A 1 4295 ? 177.897 132.651 128.309 1.00 60.77  ? 4295 GLN A CB    1 
ATOM   20375 C  CG    . GLN A 1 4295 ? 179.319 132.159 128.125 1.00 65.95  ? 4295 GLN A CG    1 
ATOM   20376 C  CD    . GLN A 1 4295 ? 180.060 132.903 127.035 1.00 64.02  ? 4295 GLN A CD    1 
ATOM   20377 O  OE1   . GLN A 1 4295 ? 181.250 133.182 127.163 1.00 69.95  ? 4295 GLN A OE1   1 
ATOM   20378 N  NE2   . GLN A 1 4295 ? 179.359 133.227 125.955 1.00 53.20  ? 4295 GLN A NE2   1 
ATOM   20379 N  N     . MET A 1 4296 ? 175.893 135.153 127.764 1.00 44.69  ? 4296 MET A N     1 
ATOM   20380 C  CA    . MET A 1 4296 ? 174.477 135.415 127.564 1.00 37.55  ? 4296 MET A CA    1 
ATOM   20381 C  C     . MET A 1 4296 ? 173.755 134.113 127.225 1.00 44.50  ? 4296 MET A C     1 
ATOM   20382 O  O     . MET A 1 4296 ? 174.229 133.341 126.386 1.00 52.85  ? 4296 MET A O     1 
ATOM   20383 C  CB    . MET A 1 4296 ? 174.269 136.438 126.447 1.00 41.86  ? 4296 MET A CB    1 
ATOM   20384 C  CG    . MET A 1 4296 ? 172.814 136.792 126.183 1.00 45.83  ? 4296 MET A CG    1 
ATOM   20385 S  SD    . MET A 1 4296 ? 172.103 137.883 127.427 1.00 49.51  ? 4296 MET A SD    1 
ATOM   20386 C  CE    . MET A 1 4296 ? 170.459 138.128 126.763 1.00 32.40  ? 4296 MET A CE    1 
ATOM   20387 N  N     . PRO A 1 4297 ? 172.621 133.834 127.866 1.00 41.53  ? 4297 PRO A N     1 
ATOM   20388 C  CA    . PRO A 1 4297 ? 171.893 132.596 127.567 1.00 41.80  ? 4297 PRO A CA    1 
ATOM   20389 C  C     . PRO A 1 4297 ? 171.410 132.564 126.126 1.00 47.23  ? 4297 PRO A C     1 
ATOM   20390 O  O     . PRO A 1 4297 ? 171.107 133.596 125.523 1.00 53.85  ? 4297 PRO A O     1 
ATOM   20391 C  CB    . PRO A 1 4297 ? 170.714 132.627 128.547 1.00 37.07  ? 4297 PRO A CB    1 
ATOM   20392 C  CG    . PRO A 1 4297 ? 171.116 133.586 129.610 1.00 37.07  ? 4297 PRO A CG    1 
ATOM   20393 C  CD    . PRO A 1 4297 ? 171.987 134.601 128.949 1.00 37.08  ? 4297 PRO A CD    1 
ATOM   20394 N  N     . ASP A 1 4298 ? 171.342 131.356 125.575 1.00 49.05  ? 4298 ASP A N     1 
ATOM   20395 C  CA    . ASP A 1 4298 ? 170.855 131.142 124.220 1.00 58.64  ? 4298 ASP A CA    1 
ATOM   20396 C  C     . ASP A 1 4298 ? 169.348 130.930 124.165 1.00 58.64  ? 4298 ASP A C     1 
ATOM   20397 O  O     . ASP A 1 4298 ? 168.812 130.677 123.082 1.00 54.64  ? 4298 ASP A O     1 
ATOM   20398 C  CB    . ASP A 1 4298 ? 171.565 129.942 123.587 1.00 61.32  ? 4298 ASP A CB    1 
ATOM   20399 C  CG    . ASP A 1 4298 ? 172.974 130.270 123.138 1.00 72.68  ? 4298 ASP A CG    1 
ATOM   20400 O  OD1   . ASP A 1 4298 ? 173.231 131.443 122.796 1.00 76.54  ? 4298 ASP A OD1   1 
ATOM   20401 O  OD2   . ASP A 1 4298 ? 173.825 129.356 123.128 1.00 77.88  ? 4298 ASP A OD2   1 
ATOM   20402 N  N     . GLY A 1 4299 ? 168.660 131.028 125.297 1.00 54.39  ? 4299 GLY A N     1 
ATOM   20403 C  CA    . GLY A 1 4299 ? 167.240 130.760 125.335 1.00 53.68  ? 4299 GLY A CA    1 
ATOM   20404 C  C     . GLY A 1 4299 ? 166.413 131.848 124.679 1.00 54.42  ? 4299 GLY A C     1 
ATOM   20405 O  O     . GLY A 1 4299 ? 166.873 132.955 124.397 1.00 53.65  ? 4299 GLY A O     1 
ATOM   20406 N  N     . ILE A 1 4300 ? 165.149 131.507 124.425 1.00 55.78  ? 4300 ILE A N     1 
ATOM   20407 C  CA    . ILE A 1 4300 ? 164.201 132.430 123.811 1.00 55.84  ? 4300 ILE A CA    1 
ATOM   20408 C  C     . ILE A 1 4300 ? 162.919 132.462 124.632 1.00 55.33  ? 4300 ILE A C     1 
ATOM   20409 O  O     . ILE A 1 4300 ? 161.935 133.099 124.239 1.00 55.27  ? 4300 ILE A O     1 
ATOM   20410 C  CB    . ILE A 1 4300 ? 163.902 132.042 122.351 1.00 52.37  ? 4300 ILE A CB    1 
ATOM   20411 C  CG1   . ILE A 1 4300 ? 163.130 130.721 122.299 1.00 55.18  ? 4300 ILE A CG1   1 
ATOM   20412 C  CG2   . ILE A 1 4300 ? 165.185 131.958 121.535 1.00 51.87  ? 4300 ILE A CG2   1 
ATOM   20413 C  CD1   . ILE A 1 4300 ? 162.882 130.212 120.896 1.00 58.06  ? 4300 ILE A CD1   1 
ATOM   20414 N  N     . ARG A 1 4301 ? 162.918 131.779 125.774 1.00 54.12  ? 4301 ARG A N     1 
ATOM   20415 C  CA    . ARG A 1 4301 ? 161.722 131.647 126.591 1.00 54.82  ? 4301 ARG A CA    1 
ATOM   20416 C  C     . ARG A 1 4301 ? 162.069 131.901 128.053 1.00 53.55  ? 4301 ARG A C     1 
ATOM   20417 O  O     . ARG A 1 4301 ? 163.219 131.753 128.476 1.00 51.71  ? 4301 ARG A O     1 
ATOM   20418 C  CB    . ARG A 1 4301 ? 161.083 130.262 126.410 1.00 62.91  ? 4301 ARG A CB    1 
ATOM   20419 C  CG    . ARG A 1 4301 ? 159.651 130.153 126.913 1.00 69.34  ? 4301 ARG A CG    1 
ATOM   20420 C  CD    . ARG A 1 4301 ? 158.852 128.981 126.314 1.00 75.70  ? 4301 ARG A CD    1 
ATOM   20421 N  NE    . ARG A 1 4301 ? 158.894 128.881 124.856 1.00 80.42  ? 4301 ARG A NE    1 
ATOM   20422 C  CZ    . ARG A 1 4301 ? 159.844 128.273 124.157 1.00 80.48  ? 4301 ARG A CZ    1 
ATOM   20423 N  NH1   . ARG A 1 4301 ? 160.833 127.624 124.749 1.00 78.27  ? 4301 ARG A NH1   1 
ATOM   20424 N  NH2   . ARG A 1 4301 ? 159.787 128.298 122.829 1.00 84.02  ? 4301 ARG A NH2   1 
ATOM   20425 N  N     . ARG A 1 4302 ? 161.048 132.294 128.821 1.00 53.18  ? 4302 ARG A N     1 
ATOM   20426 C  CA    . ARG A 1 4302 ? 161.267 132.753 130.190 1.00 46.76  ? 4302 ARG A CA    1 
ATOM   20427 C  C     . ARG A 1 4302 ? 161.838 131.653 131.078 1.00 48.24  ? 4302 ARG A C     1 
ATOM   20428 O  O     . ARG A 1 4302 ? 162.751 131.903 131.875 1.00 50.31  ? 4302 ARG A O     1 
ATOM   20429 C  CB    . ARG A 1 4302 ? 159.958 133.283 130.775 1.00 39.08  ? 4302 ARG A CB    1 
ATOM   20430 C  CG    . ARG A 1 4302 ? 160.027 133.610 132.256 1.00 36.06  ? 4302 ARG A CG    1 
ATOM   20431 C  CD    . ARG A 1 4302 ? 158.648 133.591 132.891 1.00 39.22  ? 4302 ARG A CD    1 
ATOM   20432 N  NE    . ARG A 1 4302 ? 158.703 133.839 134.326 1.00 35.72  ? 4302 ARG A NE    1 
ATOM   20433 C  CZ    . ARG A 1 4302 ? 158.987 132.917 135.235 1.00 40.96  ? 4302 ARG A CZ    1 
ATOM   20434 N  NH1   . ARG A 1 4302 ? 159.247 131.665 134.893 1.00 41.05  ? 4302 ARG A NH1   1 
ATOM   20435 N  NH2   . ARG A 1 4302 ? 159.008 133.258 136.521 1.00 39.43  ? 4302 ARG A NH2   1 
ATOM   20436 N  N     . GLU A 1 4303 ? 161.312 130.430 130.964 1.00 50.47  ? 4303 GLU A N     1 
ATOM   20437 C  CA    . GLU A 1 4303 ? 161.752 129.364 131.859 1.00 48.83  ? 4303 GLU A CA    1 
ATOM   20438 C  C     . GLU A 1 4303 ? 163.219 129.022 131.636 1.00 50.44  ? 4303 GLU A C     1 
ATOM   20439 O  O     . GLU A 1 4303 ? 163.939 128.703 132.587 1.00 50.52  ? 4303 GLU A O     1 
ATOM   20440 C  CB    . GLU A 1 4303 ? 160.878 128.120 131.690 1.00 55.40  ? 4303 GLU A CB    1 
ATOM   20441 C  CG    . GLU A 1 4303 ? 160.712 127.629 130.264 1.00 63.91  ? 4303 GLU A CG    1 
ATOM   20442 C  CD    . GLU A 1 4303 ? 159.346 127.951 129.695 1.00 76.54  ? 4303 GLU A CD    1 
ATOM   20443 O  OE1   . GLU A 1 4303 ? 158.756 128.975 130.098 1.00 71.93  ? 4303 GLU A OE1   1 
ATOM   20444 O  OE2   . GLU A 1 4303 ? 158.855 127.166 128.857 1.00 85.42  ? 4303 GLU A OE2   1 
ATOM   20445 N  N     . GLU A 1 4304 ? 163.682 129.084 130.386 1.00 48.69  ? 4304 GLU A N     1 
ATOM   20446 C  CA    . GLU A 1 4304 ? 165.090 128.813 130.111 1.00 50.88  ? 4304 GLU A CA    1 
ATOM   20447 C  C     . GLU A 1 4304 ? 165.989 129.875 130.735 1.00 49.47  ? 4304 GLU A C     1 
ATOM   20448 O  O     . GLU A 1 4304 ? 167.047 129.556 131.291 1.00 52.62  ? 4304 GLU A O     1 
ATOM   20449 C  CB    . GLU A 1 4304 ? 165.312 128.713 128.602 1.00 55.14  ? 4304 GLU A CB    1 
ATOM   20450 C  CG    . GLU A 1 4304 ? 164.618 127.507 127.979 1.00 72.86  ? 4304 GLU A CG    1 
ATOM   20451 C  CD    . GLU A 1 4304 ? 164.809 127.418 126.479 1.00 83.29  ? 4304 GLU A CD    1 
ATOM   20452 O  OE1   . GLU A 1 4304 ? 165.379 128.358 125.892 1.00 71.17  ? 4304 GLU A OE1   1 
ATOM   20453 O  OE2   . GLU A 1 4304 ? 164.384 126.406 125.884 1.00 95.42  ? 4304 GLU A OE2   1 
ATOM   20454 N  N     . PHE A 1 4305 ? 165.577 131.144 130.667 1.00 49.59  ? 4305 PHE A N     1 
ATOM   20455 C  CA    . PHE A 1 4305 ? 166.331 132.203 131.333 1.00 39.69  ? 4305 PHE A CA    1 
ATOM   20456 C  C     . PHE A 1 4305 ? 166.347 132.006 132.844 1.00 38.81  ? 4305 PHE A C     1 
ATOM   20457 O  O     . PHE A 1 4305 ? 167.379 132.215 133.492 1.00 42.40  ? 4305 PHE A O     1 
ATOM   20458 C  CB    . PHE A 1 4305 ? 165.747 133.570 130.978 1.00 37.06  ? 4305 PHE A CB    1 
ATOM   20459 C  CG    . PHE A 1 4305 ? 166.014 133.995 129.564 1.00 36.17  ? 4305 PHE A CG    1 
ATOM   20460 C  CD1   . PHE A 1 4305 ? 167.303 133.993 129.059 1.00 34.18  ? 4305 PHE A CD1   1 
ATOM   20461 C  CD2   . PHE A 1 4305 ? 164.978 134.400 128.741 1.00 32.16  ? 4305 PHE A CD2   1 
ATOM   20462 C  CE1   . PHE A 1 4305 ? 167.552 134.385 127.759 1.00 31.95  ? 4305 PHE A CE1   1 
ATOM   20463 C  CE2   . PHE A 1 4305 ? 165.222 134.792 127.441 1.00 33.02  ? 4305 PHE A CE2   1 
ATOM   20464 C  CZ    . PHE A 1 4305 ? 166.510 134.785 126.950 1.00 34.80  ? 4305 PHE A CZ    1 
ATOM   20465 N  N     . VAL A 1 4306 ? 165.212 131.608 133.423 1.00 39.67  ? 4306 VAL A N     1 
ATOM   20466 C  CA    . VAL A 1 4306 ? 165.159 131.371 134.864 1.00 42.16  ? 4306 VAL A CA    1 
ATOM   20467 C  C     . VAL A 1 4306 ? 166.079 130.218 135.250 1.00 43.81  ? 4306 VAL A C     1 
ATOM   20468 O  O     . VAL A 1 4306 ? 166.776 130.274 136.271 1.00 44.16  ? 4306 VAL A O     1 
ATOM   20469 C  CB    . VAL A 1 4306 ? 163.708 131.118 135.313 1.00 41.70  ? 4306 VAL A CB    1 
ATOM   20470 C  CG1   . VAL A 1 4306 ? 163.665 130.712 136.776 1.00 40.45  ? 4306 VAL A CG1   1 
ATOM   20471 C  CG2   . VAL A 1 4306 ? 162.861 132.357 135.081 1.00 36.59  ? 4306 VAL A CG2   1 
ATOM   20472 N  N     . GLN A 1 4307 ? 166.093 129.155 134.442 1.00 39.65  ? 4307 GLN A N     1 
ATOM   20473 C  CA    . GLN A 1 4307 ? 166.992 128.035 134.703 1.00 39.17  ? 4307 GLN A CA    1 
ATOM   20474 C  C     . GLN A 1 4307 ? 168.450 128.463 134.606 1.00 41.12  ? 4307 GLN A C     1 
ATOM   20475 O  O     . GLN A 1 4307 ? 169.288 128.020 135.400 1.00 49.86  ? 4307 GLN A O     1 
ATOM   20476 C  CB    . GLN A 1 4307 ? 166.701 126.890 133.734 1.00 45.00  ? 4307 GLN A CB    1 
ATOM   20477 C  CG    . GLN A 1 4307 ? 165.350 126.226 133.944 1.00 52.94  ? 4307 GLN A CG    1 
ATOM   20478 C  CD    . GLN A 1 4307 ? 164.959 125.319 132.794 1.00 60.78  ? 4307 GLN A CD    1 
ATOM   20479 O  OE1   . GLN A 1 4307 ? 165.436 125.480 131.671 1.00 61.90  ? 4307 GLN A OE1   1 
ATOM   20480 N  NE2   . GLN A 1 4307 ? 164.082 124.361 133.069 1.00 53.61  ? 4307 GLN A NE2   1 
ATOM   20481 N  N     . TRP A 1 4308 ? 168.775 129.318 133.632 1.00 35.17  ? 4308 TRP A N     1 
ATOM   20482 C  CA    . TRP A 1 4308 ? 170.138 129.833 133.537 1.00 35.46  ? 4308 TRP A CA    1 
ATOM   20483 C  C     . TRP A 1 4308 ? 170.505 130.644 134.773 1.00 33.85  ? 4308 TRP A C     1 
ATOM   20484 O  O     . TRP A 1 4308 ? 171.627 130.542 135.282 1.00 32.25  ? 4308 TRP A O     1 
ATOM   20485 C  CB    . TRP A 1 4308 ? 170.299 130.684 132.277 1.00 35.51  ? 4308 TRP A CB    1 
ATOM   20486 C  CG    . TRP A 1 4308 ? 171.660 131.309 132.148 1.00 35.37  ? 4308 TRP A CG    1 
ATOM   20487 C  CD1   . TRP A 1 4308 ? 172.735 130.797 131.484 1.00 37.89  ? 4308 TRP A CD1   1 
ATOM   20488 C  CD2   . TRP A 1 4308 ? 172.090 132.561 132.700 1.00 32.21  ? 4308 TRP A CD2   1 
ATOM   20489 N  NE1   . TRP A 1 4308 ? 173.806 131.651 131.585 1.00 36.53  ? 4308 TRP A NE1   1 
ATOM   20490 C  CE2   . TRP A 1 4308 ? 173.435 132.742 132.327 1.00 31.84  ? 4308 TRP A CE2   1 
ATOM   20491 C  CE3   . TRP A 1 4308 ? 171.466 133.548 133.471 1.00 29.42  ? 4308 TRP A CE3   1 
ATOM   20492 C  CZ2   . TRP A 1 4308 ? 174.169 133.865 132.699 1.00 29.43  ? 4308 TRP A CZ2   1 
ATOM   20493 C  CZ3   . TRP A 1 4308 ? 172.197 134.661 133.841 1.00 28.06  ? 4308 TRP A CZ3   1 
ATOM   20494 C  CH2   . TRP A 1 4308 ? 173.533 134.811 133.454 1.00 29.17  ? 4308 TRP A CH2   1 
ATOM   20495 N  N     . VAL A 1 4309 ? 169.572 131.464 135.261 1.00 34.11  ? 4309 VAL A N     1 
ATOM   20496 C  CA    . VAL A 1 4309 ? 169.828 132.253 136.465 1.00 34.46  ? 4309 VAL A CA    1 
ATOM   20497 C  C     . VAL A 1 4309 ? 170.054 131.340 137.663 1.00 38.43  ? 4309 VAL A C     1 
ATOM   20498 O  O     . VAL A 1 4309 ? 170.944 131.582 138.488 1.00 43.82  ? 4309 VAL A O     1 
ATOM   20499 C  CB    . VAL A 1 4309 ? 168.673 133.241 136.715 1.00 27.86  ? 4309 VAL A CB    1 
ATOM   20500 C  CG1   . VAL A 1 4309 ? 168.862 133.953 138.042 1.00 26.48  ? 4309 VAL A CG1   1 
ATOM   20501 C  CG2   . VAL A 1 4309 ? 168.588 134.249 135.585 1.00 25.47  ? 4309 VAL A CG2   1 
ATOM   20502 N  N     . GLU A 1 4310 ? 169.255 130.277 137.777 1.00 37.47  ? 4310 GLU A N     1 
ATOM   20503 C  CA    . GLU A 1 4310 ? 169.392 129.359 138.904 1.00 35.93  ? 4310 GLU A CA    1 
ATOM   20504 C  C     . GLU A 1 4310 ? 170.732 128.633 138.888 1.00 40.04  ? 4310 GLU A C     1 
ATOM   20505 O  O     . GLU A 1 4310 ? 171.236 128.247 139.949 1.00 44.45  ? 4310 GLU A O     1 
ATOM   20506 C  CB    . GLU A 1 4310 ? 168.247 128.348 138.899 1.00 38.77  ? 4310 GLU A CB    1 
ATOM   20507 C  CG    . GLU A 1 4310 ? 167.034 128.775 139.707 1.00 46.91  ? 4310 GLU A CG    1 
ATOM   20508 C  CD    . GLU A 1 4310 ? 165.734 128.273 139.111 1.00 57.92  ? 4310 GLU A CD    1 
ATOM   20509 O  OE1   . GLU A 1 4310 ? 165.779 127.331 138.292 1.00 56.74  ? 4310 GLU A OE1   1 
ATOM   20510 O  OE2   . GLU A 1 4310 ? 164.667 128.818 139.462 1.00 58.22  ? 4310 GLU A OE2   1 
ATOM   20511 N  N     . LEU A 1 4311 ? 171.320 128.436 137.709 1.00 37.19  ? 4311 LEU A N     1 
ATOM   20512 C  CA    . LEU A 1 4311 ? 172.573 127.709 137.570 1.00 35.37  ? 4311 LEU A CA    1 
ATOM   20513 C  C     . LEU A 1 4311 ? 173.797 128.616 137.646 1.00 43.42  ? 4311 LEU A C     1 
ATOM   20514 O  O     . LEU A 1 4311 ? 174.865 128.240 137.148 1.00 50.61  ? 4311 LEU A O     1 
ATOM   20515 C  CB    . LEU A 1 4311 ? 172.585 126.925 136.257 1.00 35.61  ? 4311 LEU A CB    1 
ATOM   20516 C  CG    . LEU A 1 4311 ? 171.572 125.786 136.141 1.00 40.06  ? 4311 LEU A CG    1 
ATOM   20517 C  CD1   . LEU A 1 4311 ? 171.597 125.187 134.744 1.00 40.65  ? 4311 LEU A CD1   1 
ATOM   20518 C  CD2   . LEU A 1 4311 ? 171.844 124.719 137.190 1.00 41.68  ? 4311 LEU A CD2   1 
ATOM   20519 N  N     . LEU A 1 4312 ? 173.668 129.794 138.248 1.00 40.72  ? 4312 LEU A N     1 
ATOM   20520 C  CA    . LEU A 1 4312 ? 174.812 130.678 138.392 1.00 35.91  ? 4312 LEU A CA    1 
ATOM   20521 C  C     . LEU A 1 4312 ? 175.831 130.064 139.354 1.00 41.56  ? 4312 LEU A C     1 
ATOM   20522 O  O     . LEU A 1 4312 ? 175.463 129.331 140.275 1.00 47.16  ? 4312 LEU A O     1 
ATOM   20523 C  CB    . LEU A 1 4312 ? 174.369 132.051 138.888 1.00 36.51  ? 4312 LEU A CB    1 
ATOM   20524 C  CG    . LEU A 1 4312 ? 173.899 133.009 137.788 1.00 32.92  ? 4312 LEU A CG    1 
ATOM   20525 C  CD1   . LEU A 1 4312 ? 173.615 134.394 138.344 1.00 30.16  ? 4312 LEU A CD1   1 
ATOM   20526 C  CD2   . LEU A 1 4312 ? 174.917 133.083 136.661 1.00 31.55  ? 4312 LEU A CD2   1 
ATOM   20527 N  N     . PRO A 1 4313 ? 177.122 130.347 139.156 1.00 41.97  ? 4313 PRO A N     1 
ATOM   20528 C  CA    . PRO A 1 4313 ? 178.159 129.635 139.925 1.00 47.68  ? 4313 PRO A CA    1 
ATOM   20529 C  C     . PRO A 1 4313 ? 178.103 129.868 141.425 1.00 51.71  ? 4313 PRO A C     1 
ATOM   20530 O  O     . PRO A 1 4313 ? 178.716 129.093 142.170 1.00 58.16  ? 4313 PRO A O     1 
ATOM   20531 C  CB    . PRO A 1 4313 ? 179.468 130.172 139.329 1.00 47.55  ? 4313 PRO A CB    1 
ATOM   20532 C  CG    . PRO A 1 4313 ? 179.093 130.698 137.985 1.00 48.46  ? 4313 PRO A CG    1 
ATOM   20533 C  CD    . PRO A 1 4313 ? 177.706 131.233 138.136 1.00 44.47  ? 4313 PRO A CD    1 
ATOM   20534 N  N     . ASP A 1 4314 ? 177.406 130.907 141.890 1.00 47.40  ? 4314 ASP A N     1 
ATOM   20535 C  CA    . ASP A 1 4314 ? 177.362 131.265 143.310 1.00 53.31  ? 4314 ASP A CA    1 
ATOM   20536 C  C     . ASP A 1 4314 ? 178.757 131.562 143.854 1.00 48.18  ? 4314 ASP A C     1 
ATOM   20537 O  O     . ASP A 1 4314 ? 179.045 131.326 145.030 1.00 45.19  ? 4314 ASP A O     1 
ATOM   20538 C  CB    . ASP A 1 4314 ? 176.676 130.178 144.145 1.00 57.97  ? 4314 ASP A CB    1 
ATOM   20539 C  CG    . ASP A 1 4314 ? 176.116 130.712 145.450 1.00 69.91  ? 4314 ASP A CG    1 
ATOM   20540 O  OD1   . ASP A 1 4314 ? 175.149 131.502 145.406 1.00 71.25  ? 4314 ASP A OD1   1 
ATOM   20541 O  OD2   . ASP A 1 4314 ? 176.644 130.343 146.520 1.00 66.80  ? 4314 ASP A OD2   1 
ATOM   20542 N  N     . THR A 1 4315 ? 179.630 132.080 142.993 1.00 47.75  ? 4315 THR A N     1 
ATOM   20543 C  CA    . THR A 1 4315 ? 180.960 132.520 143.393 1.00 43.62  ? 4315 THR A CA    1 
ATOM   20544 C  C     . THR A 1 4315 ? 181.143 133.969 142.965 1.00 39.76  ? 4315 THR A C     1 
ATOM   20545 O  O     . THR A 1 4315 ? 182.163 134.327 142.368 1.00 40.98  ? 4315 THR A O     1 
ATOM   20546 C  CB    . THR A 1 4315 ? 182.043 131.635 142.774 1.00 48.56  ? 4315 THR A CB    1 
ATOM   20547 O  OG1   . THR A 1 4315 ? 181.778 131.458 141.377 1.00 48.74  ? 4315 THR A OG1   1 
ATOM   20548 C  CG2   . THR A 1 4315 ? 182.075 130.276 143.455 1.00 53.83  ? 4315 THR A CG2   1 
ATOM   20549 N  N     . GLN A 1 4316 ? 180.147 134.800 143.261 1.00 35.35  ? 4316 GLN A N     1 
ATOM   20550 C  CA    . GLN A 1 4316 ? 180.126 136.166 142.761 1.00 26.93  ? 4316 GLN A CA    1 
ATOM   20551 C  C     . GLN A 1 4316 ? 181.283 136.979 143.325 1.00 32.84  ? 4316 GLN A C     1 
ATOM   20552 O  O     . GLN A 1 4316 ? 181.642 136.858 144.500 1.00 38.12  ? 4316 GLN A O     1 
ATOM   20553 C  CB    . GLN A 1 4316 ? 178.800 136.839 143.112 1.00 24.95  ? 4316 GLN A CB    1 
ATOM   20554 C  CG    . GLN A 1 4316 ? 178.572 138.161 142.401 1.00 23.41  ? 4316 GLN A CG    1 
ATOM   20555 C  CD    . GLN A 1 4316 ? 177.558 139.036 143.107 1.00 25.32  ? 4316 GLN A CD    1 
ATOM   20556 O  OE1   . GLN A 1 4316 ? 176.384 138.683 143.212 1.00 31.50  ? 4316 GLN A OE1   1 
ATOM   20557 N  NE2   . GLN A 1 4316 ? 178.006 140.185 143.596 1.00 29.75  ? 4316 GLN A NE2   1 
ATOM   20558 N  N     . THR A 1 4317 ? 181.863 137.808 142.472 1.00 33.69  ? 4317 THR A N     1 
ATOM   20559 C  CA    . THR A 1 4317 ? 182.912 138.755 142.807 1.00 31.03  ? 4317 THR A CA    1 
ATOM   20560 C  C     . THR A 1 4317 ? 182.516 140.108 142.242 1.00 27.57  ? 4317 THR A C     1 
ATOM   20561 O  O     . THR A 1 4317 ? 181.695 140.184 141.322 1.00 32.09  ? 4317 THR A O     1 
ATOM   20562 C  CB    . THR A 1 4317 ? 184.268 138.316 142.233 1.00 29.54  ? 4317 THR A CB    1 
ATOM   20563 O  OG1   . THR A 1 4317 ? 184.122 137.998 140.844 1.00 31.38  ? 4317 THR A OG1   1 
ATOM   20564 C  CG2   . THR A 1 4317 ? 184.790 137.097 142.975 1.00 34.81  ? 4317 THR A CG2   1 
ATOM   20565 N  N     . PRO A 1 4318 ? 183.068 141.201 142.778 1.00 25.72  ? 4318 PRO A N     1 
ATOM   20566 C  CA    . PRO A 1 4318 ? 182.731 142.529 142.237 1.00 21.90  ? 4318 PRO A CA    1 
ATOM   20567 C  C     . PRO A 1 4318 ? 183.074 142.703 140.764 1.00 20.83  ? 4318 PRO A C     1 
ATOM   20568 O  O     . PRO A 1 4318 ? 182.658 143.707 140.172 1.00 21.29  ? 4318 PRO A O     1 
ATOM   20569 C  CB    . PRO A 1 4318 ? 183.545 143.490 143.117 1.00 23.27  ? 4318 PRO A CB    1 
ATOM   20570 C  CG    . PRO A 1 4318 ? 184.564 142.635 143.802 1.00 31.42  ? 4318 PRO A CG    1 
ATOM   20571 C  CD    . PRO A 1 4318 ? 183.922 141.301 143.971 1.00 32.36  ? 4318 PRO A CD    1 
ATOM   20572 N  N     . SER A 1 4319 ? 183.808 141.770 140.155 1.00 21.40  ? 4319 SER A N     1 
ATOM   20573 C  CA    . SER A 1 4319 ? 184.064 141.836 138.722 1.00 19.23  ? 4319 SER A CA    1 
ATOM   20574 C  C     . SER A 1 4319 ? 182.850 141.449 137.890 1.00 21.22  ? 4319 SER A C     1 
ATOM   20575 O  O     . SER A 1 4319 ? 182.820 141.753 136.693 1.00 23.64  ? 4319 SER A O     1 
ATOM   20576 C  CB    . SER A 1 4319 ? 185.245 140.943 138.349 1.00 28.45  ? 4319 SER A CB    1 
ATOM   20577 O  OG    . SER A 1 4319 ? 185.226 140.641 136.968 1.00 42.26  ? 4319 SER A OG    1 
ATOM   20578 N  N     . TRP A 1 4320 ? 181.862 140.777 138.486 1.00 24.48  ? 4320 TRP A N     1 
ATOM   20579 C  CA    . TRP A 1 4320 ? 180.579 140.605 137.813 1.00 20.67  ? 4320 TRP A CA    1 
ATOM   20580 C  C     . TRP A 1 4320 ? 179.929 141.950 137.532 1.00 19.45  ? 4320 TRP A C     1 
ATOM   20581 O  O     . TRP A 1 4320 ? 179.185 142.094 136.556 1.00 20.02  ? 4320 TRP A O     1 
ATOM   20582 C  CB    . TRP A 1 4320 ? 179.640 139.748 138.664 1.00 17.06  ? 4320 TRP A CB    1 
ATOM   20583 C  CG    . TRP A 1 4320 ? 180.005 138.300 138.753 1.00 23.15  ? 4320 TRP A CG    1 
ATOM   20584 C  CD1   . TRP A 1 4320 ? 181.257 137.761 138.729 1.00 27.54  ? 4320 TRP A CD1   1 
ATOM   20585 C  CD2   . TRP A 1 4320 ? 179.098 137.200 138.891 1.00 29.41  ? 4320 TRP A CD2   1 
ATOM   20586 N  NE1   . TRP A 1 4320 ? 181.186 136.394 138.840 1.00 33.01  ? 4320 TRP A NE1   1 
ATOM   20587 C  CE2   . TRP A 1 4320 ? 179.871 136.025 138.941 1.00 34.23  ? 4320 TRP A CE2   1 
ATOM   20588 C  CE3   . TRP A 1 4320 ? 177.706 137.096 138.975 1.00 24.65  ? 4320 TRP A CE3   1 
ATOM   20589 C  CZ2   . TRP A 1 4320 ? 179.299 134.761 139.071 1.00 34.97  ? 4320 TRP A CZ2   1 
ATOM   20590 C  CZ3   . TRP A 1 4320 ? 177.141 135.843 139.104 1.00 22.78  ? 4320 TRP A CZ3   1 
ATOM   20591 C  CH2   . TRP A 1 4320 ? 177.936 134.692 139.151 1.00 31.55  ? 4320 TRP A CH2   1 
ATOM   20592 N  N     . LEU A 1 4321 ? 180.201 142.939 138.377 1.00 17.63  ? 4321 LEU A N     1 
ATOM   20593 C  CA    . LEU A 1 4321 ? 179.624 144.270 138.279 1.00 13.99  ? 4321 LEU A CA    1 
ATOM   20594 C  C     . LEU A 1 4321 ? 180.468 145.217 137.439 1.00 17.87  ? 4321 LEU A C     1 
ATOM   20595 O  O     . LEU A 1 4321 ? 180.068 146.367 137.236 1.00 22.61  ? 4321 LEU A O     1 
ATOM   20596 C  CB    . LEU A 1 4321 ? 179.448 144.855 139.682 1.00 14.36  ? 4321 LEU A CB    1 
ATOM   20597 C  CG    . LEU A 1 4321 ? 178.512 144.096 140.624 1.00 13.20  ? 4321 LEU A CG    1 
ATOM   20598 C  CD1   . LEU A 1 4321 ? 178.550 144.701 142.016 1.00 15.03  ? 4321 LEU A CD1   1 
ATOM   20599 C  CD2   . LEU A 1 4321 ? 177.099 144.080 140.088 1.00 15.31  ? 4321 LEU A CD2   1 
ATOM   20600 N  N     . GLY A 1 4322 ? 181.622 144.764 136.949 1.00 17.44  ? 4322 GLY A N     1 
ATOM   20601 C  CA    . GLY A 1 4322 ? 182.574 145.626 136.287 1.00 16.53  ? 4322 GLY A CA    1 
ATOM   20602 C  C     . GLY A 1 4322 ? 183.608 146.242 137.202 1.00 17.63  ? 4322 GLY A C     1 
ATOM   20603 O  O     . GLY A 1 4322 ? 184.550 146.875 136.710 1.00 27.73  ? 4322 GLY A O     1 
ATOM   20604 N  N     . LEU A 1 4323 ? 183.461 146.079 138.512 1.00 15.49  ? 4323 LEU A N     1 
ATOM   20605 C  CA    . LEU A 1 4323 ? 184.393 146.617 139.486 1.00 17.99  ? 4323 LEU A CA    1 
ATOM   20606 C  C     . LEU A 1 4323 ? 185.609 145.706 139.629 1.00 22.77  ? 4323 LEU A C     1 
ATOM   20607 O  O     . LEU A 1 4323 ? 185.566 144.534 139.254 1.00 26.17  ? 4323 LEU A O     1 
ATOM   20608 C  CB    . LEU A 1 4323 ? 183.693 146.780 140.832 1.00 16.79  ? 4323 LEU A CB    1 
ATOM   20609 C  CG    . LEU A 1 4323 ? 182.687 147.927 140.920 1.00 15.95  ? 4323 LEU A CG    1 
ATOM   20610 C  CD1   . LEU A 1 4323 ? 181.522 147.547 141.814 1.00 12.38  ? 4323 LEU A CD1   1 
ATOM   20611 C  CD2   . LEU A 1 4323 ? 183.363 149.186 141.426 1.00 21.47  ? 4323 LEU A CD2   1 
ATOM   20612 N  N     . PRO A 1 4324 ? 186.719 146.226 140.155 1.00 23.46  ? 4324 PRO A N     1 
ATOM   20613 C  CA    . PRO A 1 4324 ? 187.874 145.362 140.419 1.00 23.80  ? 4324 PRO A CA    1 
ATOM   20614 C  C     . PRO A 1 4324 ? 187.572 144.349 141.514 1.00 31.01  ? 4324 PRO A C     1 
ATOM   20615 O  O     . PRO A 1 4324 ? 186.729 144.574 142.385 1.00 32.46  ? 4324 PRO A O     1 
ATOM   20616 C  CB    . PRO A 1 4324 ? 188.966 146.347 140.853 1.00 26.60  ? 4324 PRO A CB    1 
ATOM   20617 C  CG    . PRO A 1 4324 ? 188.225 147.560 141.307 1.00 24.70  ? 4324 PRO A CG    1 
ATOM   20618 C  CD    . PRO A 1 4324 ? 187.020 147.641 140.428 1.00 24.87  ? 4324 PRO A CD    1 
ATOM   20619 N  N     . ASN A 1 4325 ? 188.275 143.214 141.456 1.00 33.93  ? 4325 ASN A N     1 
ATOM   20620 C  CA    . ASN A 1 4325 ? 188.088 142.159 142.447 1.00 34.40  ? 4325 ASN A CA    1 
ATOM   20621 C  C     . ASN A 1 4325 ? 188.424 142.613 143.860 1.00 39.94  ? 4325 ASN A C     1 
ATOM   20622 O  O     . ASN A 1 4325 ? 187.879 142.061 144.822 1.00 41.11  ? 4325 ASN A O     1 
ATOM   20623 C  CB    . ASN A 1 4325 ? 188.940 140.940 142.087 1.00 39.27  ? 4325 ASN A CB    1 
ATOM   20624 C  CG    . ASN A 1 4325 ? 188.158 139.882 141.337 1.00 42.87  ? 4325 ASN A CG    1 
ATOM   20625 O  OD1   . ASN A 1 4325 ? 187.179 140.184 140.660 1.00 34.24  ? 4325 ASN A OD1   1 
ATOM   20626 N  ND2   . ASN A 1 4325 ? 188.592 138.633 141.453 1.00 55.46  ? 4325 ASN A ND2   1 
ATOM   20627 N  N     . ASN A 1 4326 ? 189.302 143.601 144.010 1.00 35.83  ? 4326 ASN A N     1 
ATOM   20628 C  CA    . ASN A 1 4326 ? 189.726 144.078 145.318 1.00 38.30  ? 4326 ASN A CA    1 
ATOM   20629 C  C     . ASN A 1 4326 ? 188.783 145.122 145.903 1.00 38.37  ? 4326 ASN A C     1 
ATOM   20630 O  O     . ASN A 1 4326 ? 189.067 145.664 146.975 1.00 44.17  ? 4326 ASN A O     1 
ATOM   20631 C  CB    . ASN A 1 4326 ? 191.145 144.644 145.234 1.00 45.39  ? 4326 ASN A CB    1 
ATOM   20632 C  CG    . ASN A 1 4326 ? 191.295 145.681 144.140 1.00 47.37  ? 4326 ASN A CG    1 
ATOM   20633 O  OD1   . ASN A 1 4326 ? 190.690 146.751 144.192 1.00 44.59  ? 4326 ASN A OD1   1 
ATOM   20634 N  ND2   . ASN A 1 4326 ? 192.103 145.365 143.136 1.00 52.61  ? 4326 ASN A ND2   1 
ATOM   20635 N  N     . ALA A 1 4327 ? 187.672 145.415 145.224 1.00 31.96  ? 4327 ALA A N     1 
ATOM   20636 C  CA    . ALA A 1 4327 ? 186.715 146.386 145.740 1.00 35.23  ? 4327 ALA A CA    1 
ATOM   20637 C  C     . ALA A 1 4327 ? 185.960 145.871 146.958 1.00 42.56  ? 4327 ALA A C     1 
ATOM   20638 O  O     . ALA A 1 4327 ? 185.278 146.656 147.625 1.00 43.92  ? 4327 ALA A O     1 
ATOM   20639 C  CB    . ALA A 1 4327 ? 185.724 146.782 144.646 1.00 25.81  ? 4327 ALA A CB    1 
ATOM   20640 N  N     . GLU A 1 4328 ? 186.061 144.578 147.261 1.00 41.36  ? 4328 GLU A N     1 
ATOM   20641 C  CA    . GLU A 1 4328 ? 185.336 143.974 148.369 1.00 36.35  ? 4328 GLU A CA    1 
ATOM   20642 C  C     . GLU A 1 4328 ? 186.239 143.511 149.503 1.00 39.78  ? 4328 GLU A C     1 
ATOM   20643 O  O     . GLU A 1 4328 ? 185.730 143.003 150.507 1.00 47.81  ? 4328 GLU A O     1 
ATOM   20644 C  CB    . GLU A 1 4328 ? 184.503 142.788 147.868 1.00 33.23  ? 4328 GLU A CB    1 
ATOM   20645 C  CG    . GLU A 1 4328 ? 185.337 141.587 147.451 1.00 41.38  ? 4328 GLU A CG    1 
ATOM   20646 C  CD    . GLU A 1 4328 ? 184.504 140.336 147.248 1.00 53.31  ? 4328 GLU A CD    1 
ATOM   20647 O  OE1   . GLU A 1 4328 ? 183.269 140.407 147.418 1.00 46.39  ? 4328 GLU A OE1   1 
ATOM   20648 O  OE2   . GLU A 1 4328 ? 185.085 139.281 146.917 1.00 53.36  ? 4328 GLU A OE2   1 
ATOM   20649 N  N     . ARG A 1 4329 ? 187.559 143.669 149.377 1.00 40.14  ? 4329 ARG A N     1 
ATOM   20650 C  CA    . ARG A 1 4329 ? 188.467 143.151 150.396 1.00 38.87  ? 4329 ARG A CA    1 
ATOM   20651 C  C     . ARG A 1 4329 ? 188.264 143.856 151.732 1.00 37.35  ? 4329 ARG A C     1 
ATOM   20652 O  O     . ARG A 1 4329 ? 188.131 143.206 152.776 1.00 40.75  ? 4329 ARG A O     1 
ATOM   20653 C  CB    . ARG A 1 4329 ? 189.916 143.292 149.929 1.00 39.22  ? 4329 ARG A CB    1 
ATOM   20654 C  CG    . ARG A 1 4329 ? 190.340 142.262 148.898 1.00 43.18  ? 4329 ARG A CG    1 
ATOM   20655 C  CD    . ARG A 1 4329 ? 191.851 142.124 148.860 1.00 49.39  ? 4329 ARG A CD    1 
ATOM   20656 N  NE    . ARG A 1 4329 ? 192.428 142.157 150.198 1.00 58.57  ? 4329 ARG A NE    1 
ATOM   20657 C  CZ    . ARG A 1 4329 ? 193.548 141.539 150.548 1.00 60.55  ? 4329 ARG A CZ    1 
ATOM   20658 N  NH1   . ARG A 1 4329 ? 194.244 140.826 149.678 1.00 51.92  ? 4329 ARG A NH1   1 
ATOM   20659 N  NH2   . ARG A 1 4329 ? 193.979 141.638 151.802 1.00 60.61  ? 4329 ARG A NH2   1 
ATOM   20660 N  N     . VAL A 1 4330 ? 188.239 145.190 151.719 1.00 36.95  ? 4330 VAL A N     1 
ATOM   20661 C  CA    . VAL A 1 4330 ? 188.047 145.940 152.956 1.00 37.82  ? 4330 VAL A CA    1 
ATOM   20662 C  C     . VAL A 1 4330 ? 186.666 145.668 153.537 1.00 38.32  ? 4330 VAL A C     1 
ATOM   20663 O  O     . VAL A 1 4330 ? 186.513 145.473 154.749 1.00 41.51  ? 4330 VAL A O     1 
ATOM   20664 C  CB    . VAL A 1 4330 ? 188.277 147.442 152.708 1.00 36.14  ? 4330 VAL A CB    1 
ATOM   20665 C  CG1   . VAL A 1 4330 ? 187.643 148.274 153.812 1.00 36.15  ? 4330 VAL A CG1   1 
ATOM   20666 C  CG2   . VAL A 1 4330 ? 189.764 147.738 152.600 1.00 32.77  ? 4330 VAL A CG2   1 
ATOM   20667 N  N     . LEU A 1 4331 ? 185.640 145.646 152.682 1.00 34.85  ? 4331 LEU A N     1 
ATOM   20668 C  CA    . LEU A 1 4331 ? 184.286 145.375 153.153 1.00 35.20  ? 4331 LEU A CA    1 
ATOM   20669 C  C     . LEU A 1 4331 ? 184.181 143.989 153.775 1.00 34.47  ? 4331 LEU A C     1 
ATOM   20670 O  O     . LEU A 1 4331 ? 183.581 143.825 154.842 1.00 40.01  ? 4331 LEU A O     1 
ATOM   20671 C  CB    . LEU A 1 4331 ? 183.293 145.522 152.001 1.00 38.02  ? 4331 LEU A CB    1 
ATOM   20672 C  CG    . LEU A 1 4331 ? 181.809 145.477 152.369 1.00 39.83  ? 4331 LEU A CG    1 
ATOM   20673 C  CD1   . LEU A 1 4331 ? 181.491 146.496 153.451 1.00 40.98  ? 4331 LEU A CD1   1 
ATOM   20674 C  CD2   . LEU A 1 4331 ? 180.946 145.707 151.139 1.00 35.57  ? 4331 LEU A CD2   1 
ATOM   20675 N  N     . LEU A 1 4332 ? 184.766 142.979 153.127 1.00 32.67  ? 4332 LEU A N     1 
ATOM   20676 C  CA    . LEU A 1 4332 ? 184.693 141.621 153.659 1.00 31.64  ? 4332 LEU A CA    1 
ATOM   20677 C  C     . LEU A 1 4332 ? 185.486 141.484 154.954 1.00 34.65  ? 4332 LEU A C     1 
ATOM   20678 O  O     . LEU A 1 4332 ? 185.052 140.790 155.879 1.00 36.39  ? 4332 LEU A O     1 
ATOM   20679 C  CB    . LEU A 1 4332 ? 185.182 140.618 152.616 1.00 35.75  ? 4332 LEU A CB    1 
ATOM   20680 C  CG    . LEU A 1 4332 ? 184.220 140.327 151.462 1.00 30.27  ? 4332 LEU A CG    1 
ATOM   20681 C  CD1   . LEU A 1 4332 ? 184.682 139.116 150.670 1.00 29.56  ? 4332 LEU A CD1   1 
ATOM   20682 C  CD2   . LEU A 1 4332 ? 182.805 140.123 151.980 1.00 33.68  ? 4332 LEU A CD2   1 
ATOM   20683 N  N     . THR A 1 4333 ? 186.652 142.130 155.038 1.00 33.73  ? 4333 THR A N     1 
ATOM   20684 C  CA    . THR A 1 4333 ? 187.424 142.090 156.278 1.00 34.90  ? 4333 THR A CA    1 
ATOM   20685 C  C     . THR A 1 4333 ? 186.660 142.746 157.422 1.00 33.04  ? 4333 THR A C     1 
ATOM   20686 O  O     . THR A 1 4333 ? 186.611 142.211 158.539 1.00 38.47  ? 4333 THR A O     1 
ATOM   20687 C  CB    . THR A 1 4333 ? 188.777 142.772 156.077 1.00 34.55  ? 4333 THR A CB    1 
ATOM   20688 O  OG1   . THR A 1 4333 ? 189.485 142.129 155.010 1.00 33.77  ? 4333 THR A OG1   1 
ATOM   20689 C  CG2   . THR A 1 4333 ? 189.609 142.693 157.347 1.00 37.97  ? 4333 THR A CG2   1 
ATOM   20690 N  N     . THR A 1 4334 ? 186.048 143.904 157.159 1.00 29.46  ? 4334 THR A N     1 
ATOM   20691 C  CA    . THR A 1 4334 ? 185.255 144.573 158.182 1.00 32.70  ? 4334 THR A CA    1 
ATOM   20692 C  C     . THR A 1 4334 ? 184.061 143.721 158.594 1.00 29.68  ? 4334 THR A C     1 
ATOM   20693 O  O     . THR A 1 4334 ? 183.735 143.632 159.782 1.00 27.31  ? 4334 THR A O     1 
ATOM   20694 C  CB    . THR A 1 4334 ? 184.794 145.941 157.675 1.00 39.35  ? 4334 THR A CB    1 
ATOM   20695 O  OG1   . THR A 1 4334 ? 185.929 146.803 157.528 1.00 45.23  ? 4334 THR A OG1   1 
ATOM   20696 C  CG2   . THR A 1 4334 ? 183.812 146.575 158.649 1.00 38.34  ? 4334 THR A CG2   1 
ATOM   20697 N  N     . GLN A 1 4335 ? 183.405 143.076 157.626 1.00 33.12  ? 4335 GLN A N     1 
ATOM   20698 C  CA    . GLN A 1 4335 ? 182.261 142.226 157.939 1.00 28.06  ? 4335 GLN A CA    1 
ATOM   20699 C  C     . GLN A 1 4335 ? 182.675 141.020 158.774 1.00 29.64  ? 4335 GLN A C     1 
ATOM   20700 O  O     . GLN A 1 4335 ? 181.953 140.620 159.693 1.00 36.00  ? 4335 GLN A O     1 
ATOM   20701 C  CB    . GLN A 1 4335 ? 181.575 141.783 156.647 1.00 27.04  ? 4335 GLN A CB    1 
ATOM   20702 C  CG    . GLN A 1 4335 ? 180.520 142.757 156.151 1.00 31.05  ? 4335 GLN A CG    1 
ATOM   20703 C  CD    . GLN A 1 4335 ? 179.813 142.271 154.902 1.00 42.48  ? 4335 GLN A CD    1 
ATOM   20704 O  OE1   . GLN A 1 4335 ? 179.684 141.069 154.676 1.00 47.17  ? 4335 GLN A OE1   1 
ATOM   20705 N  NE2   . GLN A 1 4335 ? 179.351 143.207 154.083 1.00 44.21  ? 4335 GLN A NE2   1 
ATOM   20706 N  N     . GLY A 1 4336 ? 183.831 140.427 158.473 1.00 30.11  ? 4336 GLY A N     1 
ATOM   20707 C  CA    . GLY A 1 4336 ? 184.311 139.316 159.280 1.00 26.76  ? 4336 GLY A CA    1 
ATOM   20708 C  C     . GLY A 1 4336 ? 184.660 139.731 160.696 1.00 28.24  ? 4336 GLY A C     1 
ATOM   20709 O  O     . GLY A 1 4336 ? 184.328 139.032 161.660 1.00 29.85  ? 4336 GLY A O     1 
ATOM   20710 N  N     . VAL A 1 4337 ? 185.332 140.876 160.845 1.00 29.27  ? 4337 VAL A N     1 
ATOM   20711 C  CA    . VAL A 1 4337 ? 185.640 141.387 162.179 1.00 27.14  ? 4337 VAL A CA    1 
ATOM   20712 C  C     . VAL A 1 4337 ? 184.354 141.680 162.943 1.00 30.37  ? 4337 VAL A C     1 
ATOM   20713 O  O     . VAL A 1 4337 ? 184.250 141.411 164.147 1.00 32.21  ? 4337 VAL A O     1 
ATOM   20714 C  CB    . VAL A 1 4337 ? 186.542 142.632 162.076 1.00 29.55  ? 4337 VAL A CB    1 
ATOM   20715 C  CG1   . VAL A 1 4337 ? 186.583 143.379 163.399 1.00 29.55  ? 4337 VAL A CG1   1 
ATOM   20716 C  CG2   . VAL A 1 4337 ? 187.942 142.235 161.637 1.00 29.85  ? 4337 VAL A CG2   1 
ATOM   20717 N  N     . ASP A 1 4338 ? 183.349 142.222 162.252 1.00 33.31  ? 4338 ASP A N     1 
ATOM   20718 C  CA    . ASP A 1 4338 ? 182.079 142.532 162.897 1.00 30.61  ? 4338 ASP A CA    1 
ATOM   20719 C  C     . ASP A 1 4338 ? 181.350 141.257 163.309 1.00 30.11  ? 4338 ASP A C     1 
ATOM   20720 O  O     . ASP A 1 4338 ? 180.709 141.218 164.362 1.00 38.24  ? 4338 ASP A O     1 
ATOM   20721 C  CB    . ASP A 1 4338 ? 181.219 143.377 161.956 1.00 37.22  ? 4338 ASP A CB    1 
ATOM   20722 C  CG    . ASP A 1 4338 ? 179.988 143.953 162.635 1.00 57.65  ? 4338 ASP A CG    1 
ATOM   20723 O  OD1   . ASP A 1 4338 ? 179.776 143.691 163.837 1.00 56.49  ? 4338 ASP A OD1   1 
ATOM   20724 O  OD2   . ASP A 1 4338 ? 179.225 144.675 161.959 1.00 68.51  ? 4338 ASP A OD2   1 
ATOM   20725 N  N     . MET A 1 4339 ? 181.434 140.205 162.491 1.00 27.29  ? 4339 MET A N     1 
ATOM   20726 C  CA    . MET A 1 4339 ? 180.852 138.921 162.873 1.00 28.32  ? 4339 MET A CA    1 
ATOM   20727 C  C     . MET A 1 4339 ? 181.551 138.348 164.100 1.00 30.98  ? 4339 MET A C     1 
ATOM   20728 O  O     . MET A 1 4339 ? 180.899 137.791 164.994 1.00 34.35  ? 4339 MET A O     1 
ATOM   20729 C  CB    . MET A 1 4339 ? 180.927 137.940 161.703 1.00 31.78  ? 4339 MET A CB    1 
ATOM   20730 C  CG    . MET A 1 4339 ? 180.536 136.512 162.055 1.00 27.18  ? 4339 MET A CG    1 
ATOM   20731 S  SD    . MET A 1 4339 ? 181.282 135.281 160.969 1.00 43.63  ? 4339 MET A SD    1 
ATOM   20732 C  CE    . MET A 1 4339 ? 183.023 135.631 161.198 1.00 37.14  ? 4339 MET A CE    1 
ATOM   20733 N  N     . ILE A 1 4340 ? 182.880 138.472 164.157 1.00 36.40  ? 4340 ILE A N     1 
ATOM   20734 C  CA    . ILE A 1 4340 ? 183.620 138.042 165.342 1.00 35.15  ? 4340 ILE A CA    1 
ATOM   20735 C  C     . ILE A 1 4340 ? 183.140 138.805 166.570 1.00 30.66  ? 4340 ILE A C     1 
ATOM   20736 O  O     . ILE A 1 4340 ? 182.896 138.219 167.633 1.00 36.38  ? 4340 ILE A O     1 
ATOM   20737 C  CB    . ILE A 1 4340 ? 185.134 138.227 165.126 1.00 32.27  ? 4340 ILE A CB    1 
ATOM   20738 C  CG1   . ILE A 1 4340 ? 185.664 137.231 164.096 1.00 30.66  ? 4340 ILE A CG1   1 
ATOM   20739 C  CG2   . ILE A 1 4340 ? 185.883 138.076 166.439 1.00 29.95  ? 4340 ILE A CG2   1 
ATOM   20740 C  CD1   . ILE A 1 4340 ? 185.392 135.797 164.451 1.00 34.22  ? 4340 ILE A CD1   1 
ATOM   20741 N  N     . SER A 1 4341 ? 182.991 140.125 166.438 1.00 24.82  ? 4341 SER A N     1 
ATOM   20742 C  CA    . SER A 1 4341 ? 182.540 140.941 167.561 1.00 26.45  ? 4341 SER A CA    1 
ATOM   20743 C  C     . SER A 1 4341 ? 181.126 140.563 167.990 1.00 29.98  ? 4341 SER A C     1 
ATOM   20744 O  O     . SER A 1 4341 ? 180.827 140.513 169.187 1.00 35.73  ? 4341 SER A O     1 
ATOM   20745 C  CB    . SER A 1 4341 ? 182.612 142.423 167.196 1.00 35.14  ? 4341 SER A CB    1 
ATOM   20746 O  OG    . SER A 1 4341 ? 181.488 142.816 166.430 1.00 38.02  ? 4341 SER A OG    1 
ATOM   20747 N  N     . LYS A 1 4342 ? 180.241 140.305 167.025 1.00 30.66  ? 4342 LYS A N     1 
ATOM   20748 C  CA    . LYS A 1 4342 ? 178.870 139.925 167.353 1.00 26.95  ? 4342 LYS A CA    1 
ATOM   20749 C  C     . LYS A 1 4342 ? 178.819 138.584 168.073 1.00 31.35  ? 4342 LYS A C     1 
ATOM   20750 O  O     . LYS A 1 4342 ? 178.078 138.431 169.051 1.00 39.05  ? 4342 LYS A O     1 
ATOM   20751 C  CB    . LYS A 1 4342 ? 178.010 139.882 166.090 1.00 25.64  ? 4342 LYS A CB    1 
ATOM   20752 C  CG    . LYS A 1 4342 ? 177.677 141.243 165.507 1.00 26.81  ? 4342 LYS A CG    1 
ATOM   20753 C  CD    . LYS A 1 4342 ? 177.005 141.105 164.150 1.00 28.32  ? 4342 LYS A CD    1 
ATOM   20754 C  CE    . LYS A 1 4342 ? 176.837 142.453 163.470 1.00 31.58  ? 4342 LYS A CE    1 
ATOM   20755 N  NZ    . LYS A 1 4342 ? 176.211 143.461 164.371 1.00 37.78  ? 4342 LYS A NZ    1 
ATOM   20756 N  N     . MET A 1 4343 ? 179.588 137.597 167.604 1.00 29.62  ? 4343 MET A N     1 
ATOM   20757 C  CA    . MET A 1 4343 ? 179.607 136.312 168.297 1.00 28.92  ? 4343 MET A CA    1 
ATOM   20758 C  C     . MET A 1 4343 ? 180.205 136.437 169.691 1.00 39.62  ? 4343 MET A C     1 
ATOM   20759 O  O     . MET A 1 4343 ? 179.741 135.769 170.622 1.00 47.22  ? 4343 MET A O     1 
ATOM   20760 C  CB    . MET A 1 4343 ? 180.372 135.262 167.490 1.00 29.35  ? 4343 MET A CB    1 
ATOM   20761 C  CG    . MET A 1 4343 ? 179.710 134.871 166.185 1.00 33.64  ? 4343 MET A CG    1 
ATOM   20762 S  SD    . MET A 1 4343 ? 180.617 133.578 165.318 1.00 54.69  ? 4343 MET A SD    1 
ATOM   20763 C  CE    . MET A 1 4343 ? 182.021 134.498 164.705 1.00 45.36  ? 4343 MET A CE    1 
ATOM   20764 N  N     . LEU A 1 4344 ? 181.225 137.281 169.858 1.00 41.72  ? 4344 LEU A N     1 
ATOM   20765 C  CA    . LEU A 1 4344 ? 181.801 137.474 171.185 1.00 40.50  ? 4344 LEU A CA    1 
ATOM   20766 C  C     . LEU A 1 4344 ? 180.832 138.204 172.108 1.00 39.66  ? 4344 LEU A C     1 
ATOM   20767 O  O     . LEU A 1 4344 ? 180.828 137.972 173.323 1.00 47.33  ? 4344 LEU A O     1 
ATOM   20768 C  CB    . LEU A 1 4344 ? 183.120 138.236 171.075 1.00 34.66  ? 4344 LEU A CB    1 
ATOM   20769 C  CG    . LEU A 1 4344 ? 183.887 138.465 172.376 1.00 41.57  ? 4344 LEU A CG    1 
ATOM   20770 C  CD1   . LEU A 1 4344 ? 184.299 137.137 172.985 1.00 45.84  ? 4344 LEU A CD1   1 
ATOM   20771 C  CD2   . LEU A 1 4344 ? 185.099 139.346 172.127 1.00 57.20  ? 4344 LEU A CD2   1 
ATOM   20772 N  N     . LYS A 1 4345 ? 180.002 139.089 171.551 1.00 38.31  ? 4345 LYS A N     1 
ATOM   20773 C  CA    . LYS A 1 4345 ? 179.085 139.874 172.370 1.00 38.70  ? 4345 LYS A CA    1 
ATOM   20774 C  C     . LYS A 1 4345 ? 178.001 139.022 173.016 1.00 42.35  ? 4345 LYS A C     1 
ATOM   20775 O  O     . LYS A 1 4345 ? 177.478 139.402 174.069 1.00 52.20  ? 4345 LYS A O     1 
ATOM   20776 C  CB    . LYS A 1 4345 ? 178.446 140.981 171.529 1.00 38.27  ? 4345 LYS A CB    1 
ATOM   20777 C  CG    . LYS A 1 4345 ? 177.901 142.143 172.347 1.00 33.21  ? 4345 LYS A CG    1 
ATOM   20778 C  CD    . LYS A 1 4345 ? 177.834 143.428 171.532 1.00 39.12  ? 4345 LYS A CD    1 
ATOM   20779 C  CE    . LYS A 1 4345 ? 177.363 143.169 170.109 1.00 43.24  ? 4345 LYS A CE    1 
ATOM   20780 N  NZ    . LYS A 1 4345 ? 177.615 144.330 169.209 1.00 44.45  ? 4345 LYS A NZ    1 
ATOM   20781 N  N     . MET A 1 4346 ? 177.653 137.883 172.421 1.00 39.64  ? 4346 MET A N     1 
ATOM   20782 C  CA    . MET A 1 4346 ? 176.639 136.988 172.970 1.00 43.38  ? 4346 MET A CA    1 
ATOM   20783 C  C     . MET A 1 4346 ? 177.267 135.718 173.535 1.00 50.40  ? 4346 MET A C     1 
ATOM   20784 O  O     . MET A 1 4346 ? 176.718 134.622 173.412 1.00 50.96  ? 4346 MET A O     1 
ATOM   20785 C  CB    . MET A 1 4346 ? 175.582 136.649 171.921 1.00 31.92  ? 4346 MET A CB    1 
ATOM   20786 C  CG    . MET A 1 4346 ? 175.036 137.865 171.191 1.00 38.40  ? 4346 MET A CG    1 
ATOM   20787 S  SD    . MET A 1 4346 ? 174.360 137.479 169.567 1.00 53.72  ? 4346 MET A SD    1 
ATOM   20788 C  CE    . MET A 1 4346 ? 173.577 135.905 169.899 1.00 24.87  ? 4346 MET A CE    1 
ATOM   20789 N  N     . GLN A 1 4347 ? 178.431 135.862 174.160 1.00 51.74  ? 4347 GLN A N     1 
ATOM   20790 C  CA    . GLN A 1 4347 ? 179.115 134.744 174.798 1.00 53.01  ? 4347 GLN A CA    1 
ATOM   20791 C  C     . GLN A 1 4347 ? 178.771 134.675 176.283 1.00 52.02  ? 4347 GLN A C     1 
ATOM   20792 O  O     . GLN A 1 4347 ? 177.617 134.460 176.653 1.00 47.84  ? 4347 GLN A O     1 
ATOM   20793 C  CB    . GLN A 1 4347 ? 180.629 134.865 174.608 1.00 45.73  ? 4347 GLN A CB    1 
ATOM   20794 C  CG    . GLN A 1 4347 ? 181.407 133.611 174.968 1.00 53.93  ? 4347 GLN A CG    1 
ATOM   20795 C  CD    . GLN A 1 4347 ? 181.181 132.480 173.987 1.00 65.79  ? 4347 GLN A CD    1 
ATOM   20796 O  OE1   . GLN A 1 4347 ? 181.075 132.700 172.781 1.00 66.07  ? 4347 GLN A OE1   1 
ATOM   20797 N  NE2   . GLN A 1 4347 ? 181.102 131.259 174.502 1.00 70.75  ? 4347 GLN A NE2   1 
ATOM   20798 N  N     . PRO A 1 4374 ? 190.222 163.995 188.649 1.00 98.66  ? 4374 PRO A N     1 
ATOM   20799 C  CA    . PRO A 1 4374 ? 189.939 162.786 187.869 1.00 103.82 ? 4374 PRO A CA    1 
ATOM   20800 C  C     . PRO A 1 4374 ? 190.984 162.525 186.788 1.00 101.00 ? 4374 PRO A C     1 
ATOM   20801 O  O     . PRO A 1 4374 ? 191.800 163.398 186.496 1.00 98.34  ? 4374 PRO A O     1 
ATOM   20802 C  CB    . PRO A 1 4374 ? 188.572 163.084 187.248 1.00 104.44 ? 4374 PRO A CB    1 
ATOM   20803 C  CG    . PRO A 1 4374 ? 188.520 164.565 187.160 1.00 96.21  ? 4374 PRO A CG    1 
ATOM   20804 C  CD    . PRO A 1 4374 ? 189.276 165.083 188.349 1.00 94.19  ? 4374 PRO A CD    1 
ATOM   20805 N  N     . ALA A 1 4375 ? 190.953 161.325 186.204 1.00 102.62 ? 4375 ALA A N     1 
ATOM   20806 C  CA    . ALA A 1 4375 ? 191.934 160.961 185.189 1.00 107.96 ? 4375 ALA A CA    1 
ATOM   20807 C  C     . ALA A 1 4375 ? 191.676 161.658 183.860 1.00 107.91 ? 4375 ALA A C     1 
ATOM   20808 O  O     . ALA A 1 4375 ? 192.628 161.932 183.114 1.00 104.01 ? 4375 ALA A O     1 
ATOM   20809 C  CB    . ALA A 1 4375 ? 191.946 159.445 184.990 1.00 98.80  ? 4375 ALA A CB    1 
ATOM   20810 N  N     . TRP A 1 4376 ? 190.410 161.946 183.542 1.00 102.02 ? 4376 TRP A N     1 
ATOM   20811 C  CA    . TRP A 1 4376 ? 190.106 162.603 182.276 1.00 93.51  ? 4376 TRP A CA    1 
ATOM   20812 C  C     . TRP A 1 4376 ? 190.730 163.990 182.220 1.00 93.85  ? 4376 TRP A C     1 
ATOM   20813 O  O     . TRP A 1 4376 ? 191.199 164.422 181.164 1.00 94.08  ? 4376 TRP A O     1 
ATOM   20814 C  CB    . TRP A 1 4376 ? 188.592 162.670 182.050 1.00 85.94  ? 4376 TRP A CB    1 
ATOM   20815 C  CG    . TRP A 1 4376 ? 187.858 163.687 182.878 1.00 91.95  ? 4376 TRP A CG    1 
ATOM   20816 C  CD1   . TRP A 1 4376 ? 187.163 163.456 184.029 1.00 95.63  ? 4376 TRP A CD1   1 
ATOM   20817 C  CD2   . TRP A 1 4376 ? 187.718 165.088 182.601 1.00 93.31  ? 4376 TRP A CD2   1 
ATOM   20818 N  NE1   . TRP A 1 4376 ? 186.613 164.627 184.494 1.00 96.83  ? 4376 TRP A NE1   1 
ATOM   20819 C  CE2   . TRP A 1 4376 ? 186.940 165.643 183.635 1.00 95.52  ? 4376 TRP A CE2   1 
ATOM   20820 C  CE3   . TRP A 1 4376 ? 188.184 165.927 181.584 1.00 88.85  ? 4376 TRP A CE3   1 
ATOM   20821 C  CZ2   . TRP A 1 4376 ? 186.615 166.997 183.681 1.00 91.38  ? 4376 TRP A CZ2   1 
ATOM   20822 C  CZ3   . TRP A 1 4376 ? 187.864 167.270 181.633 1.00 84.67  ? 4376 TRP A CZ3   1 
ATOM   20823 C  CH2   . TRP A 1 4376 ? 187.086 167.792 182.673 1.00 87.99  ? 4376 TRP A CH2   1 
ATOM   20824 N  N     . MET A 1 4377 ? 190.764 164.693 183.354 1.00 94.53  ? 4377 MET A N     1 
ATOM   20825 C  CA    . MET A 1 4377 ? 191.397 166.007 183.397 1.00 96.80  ? 4377 MET A CA    1 
ATOM   20826 C  C     . MET A 1 4377 ? 192.875 165.917 183.033 1.00 96.06  ? 4377 MET A C     1 
ATOM   20827 O  O     . MET A 1 4377 ? 193.369 166.686 182.197 1.00 94.54  ? 4377 MET A O     1 
ATOM   20828 C  CB    . MET A 1 4377 ? 191.222 166.612 184.790 1.00 104.00 ? 4377 MET A CB    1 
ATOM   20829 C  CG    . MET A 1 4377 ? 189.841 167.194 185.049 1.00 102.77 ? 4377 MET A CG    1 
ATOM   20830 S  SD    . MET A 1 4377 ? 189.808 168.452 186.342 1.00 124.83 ? 4377 MET A SD    1 
ATOM   20831 C  CE    . MET A 1 4377 ? 190.727 169.775 185.570 1.00 92.86  ? 4377 MET A CE    1 
ATOM   20832 N  N     . ARG A 1 4378 ? 193.591 164.964 183.633 1.00 100.35 ? 4378 ARG A N     1 
ATOM   20833 C  CA    . ARG A 1 4378 ? 195.025 164.839 183.391 1.00 99.44  ? 4378 ARG A CA    1 
ATOM   20834 C  C     . ARG A 1 4378 ? 195.308 164.403 181.958 1.00 99.30  ? 4378 ARG A C     1 
ATOM   20835 O  O     . ARG A 1 4378 ? 196.216 164.933 181.304 1.00 96.37  ? 4378 ARG A O     1 
ATOM   20836 C  CB    . ARG A 1 4378 ? 195.642 163.856 184.389 1.00 100.22 ? 4378 ARG A CB    1 
ATOM   20837 C  CG    . ARG A 1 4378 ? 196.022 164.469 185.735 1.00 99.94  ? 4378 ARG A CG    1 
ATOM   20838 C  CD    . ARG A 1 4378 ? 194.793 164.843 186.553 1.00 105.35 ? 4378 ARG A CD    1 
ATOM   20839 N  NE    . ARG A 1 4378 ? 195.133 165.287 187.899 1.00 107.41 ? 4378 ARG A NE    1 
ATOM   20840 C  CZ    . ARG A 1 4378 ? 194.258 165.769 188.770 1.00 105.38 ? 4378 ARG A CZ    1 
ATOM   20841 N  NH1   . ARG A 1 4378 ? 192.975 165.885 188.468 1.00 95.64  ? 4378 ARG A NH1   1 
ATOM   20842 N  NH2   . ARG A 1 4378 ? 194.680 166.145 189.974 1.00 107.30 ? 4378 ARG A NH2   1 
ATOM   20843 N  N     . THR A 1 4379 ? 194.540 163.434 181.448 1.00 99.57  ? 4379 THR A N     1 
ATOM   20844 C  CA    . THR A 1 4379 ? 194.786 162.981 180.082 1.00 99.34  ? 4379 THR A CA    1 
ATOM   20845 C  C     . THR A 1 4379 ? 194.416 164.061 179.070 1.00 95.47  ? 4379 THR A C     1 
ATOM   20846 O  O     . THR A 1 4379 ? 195.081 164.199 178.037 1.00 88.91  ? 4379 THR A O     1 
ATOM   20847 C  CB    . THR A 1 4379 ? 194.042 161.671 179.799 1.00 95.74  ? 4379 THR A CB    1 
ATOM   20848 O  OG1   . THR A 1 4379 ? 194.444 161.161 178.521 1.00 93.46  ? 4379 THR A OG1   1 
ATOM   20849 C  CG2   . THR A 1 4379 ? 192.539 161.871 179.797 1.00 90.19  ? 4379 THR A CG2   1 
ATOM   20850 N  N     . LEU A 1 4380 ? 193.378 164.855 179.355 1.00 97.40  ? 4380 LEU A N     1 
ATOM   20851 C  CA    . LEU A 1 4380 ? 193.049 165.979 178.488 1.00 90.94  ? 4380 LEU A CA    1 
ATOM   20852 C  C     . LEU A 1 4380 ? 194.158 167.019 178.500 1.00 86.11  ? 4380 LEU A C     1 
ATOM   20853 O  O     . LEU A 1 4380 ? 194.498 167.580 177.454 1.00 88.36  ? 4380 LEU A O     1 
ATOM   20854 C  CB    . LEU A 1 4380 ? 191.725 166.609 178.916 1.00 88.61  ? 4380 LEU A CB    1 
ATOM   20855 C  CG    . LEU A 1 4380 ? 191.171 167.665 177.957 1.00 81.42  ? 4380 LEU A CG    1 
ATOM   20856 C  CD1   . LEU A 1 4380 ? 190.996 167.087 176.560 1.00 75.76  ? 4380 LEU A CD1   1 
ATOM   20857 C  CD2   . LEU A 1 4380 ? 189.865 168.242 178.476 1.00 77.48  ? 4380 LEU A CD2   1 
ATOM   20858 N  N     . HIS A 1 4381 ? 194.732 167.292 179.674 1.00 85.13  ? 4381 HIS A N     1 
ATOM   20859 C  CA    . HIS A 1 4381 ? 195.855 168.222 179.741 1.00 87.49  ? 4381 HIS A CA    1 
ATOM   20860 C  C     . HIS A 1 4381 ? 197.025 167.719 178.907 1.00 90.94  ? 4381 HIS A C     1 
ATOM   20861 O  O     . HIS A 1 4381 ? 197.634 168.478 178.142 1.00 89.04  ? 4381 HIS A O     1 
ATOM   20862 C  CB    . HIS A 1 4381 ? 196.278 168.428 181.197 1.00 88.25  ? 4381 HIS A CB    1 
ATOM   20863 C  CG    . HIS A 1 4381 ? 197.403 169.401 181.369 1.00 89.69  ? 4381 HIS A CG    1 
ATOM   20864 N  ND1   . HIS A 1 4381 ? 198.719 169.071 181.127 1.00 89.99  ? 4381 HIS A ND1   1 
ATOM   20865 C  CD2   . HIS A 1 4381 ? 197.406 170.699 181.757 1.00 90.75  ? 4381 HIS A CD2   1 
ATOM   20866 C  CE1   . HIS A 1 4381 ? 199.485 170.122 181.360 1.00 85.92  ? 4381 HIS A CE1   1 
ATOM   20867 N  NE2   . HIS A 1 4381 ? 198.713 171.123 181.744 1.00 88.16  ? 4381 HIS A NE2   1 
ATOM   20868 N  N     . THR A 1 4382 ? 197.342 166.428 179.033 1.00 95.41  ? 4382 THR A N     1 
ATOM   20869 C  CA    . THR A 1 4382 ? 198.462 165.862 178.285 1.00 92.74  ? 4382 THR A CA    1 
ATOM   20870 C  C     . THR A 1 4382 ? 198.217 165.935 176.781 1.00 90.00  ? 4382 THR A C     1 
ATOM   20871 O  O     . THR A 1 4382 ? 199.095 166.356 176.017 1.00 89.40  ? 4382 THR A O     1 
ATOM   20872 C  CB    . THR A 1 4382 ? 198.707 164.417 178.720 1.00 96.49  ? 4382 THR A CB    1 
ATOM   20873 O  OG1   . THR A 1 4382 ? 198.847 164.362 180.146 1.00 101.80 ? 4382 THR A OG1   1 
ATOM   20874 C  CG2   . THR A 1 4382 ? 199.971 163.873 178.072 1.00 92.64  ? 4382 THR A CG2   1 
ATOM   20875 N  N     . THR A 1 4383 ? 197.020 165.538 176.337 1.00 87.26  ? 4383 THR A N     1 
ATOM   20876 C  CA    . THR A 1 4383 ? 196.721 165.558 174.908 1.00 81.90  ? 4383 THR A CA    1 
ATOM   20877 C  C     . THR A 1 4383 ? 196.679 166.980 174.363 1.00 78.78  ? 4383 THR A C     1 
ATOM   20878 O  O     . THR A 1 4383 ? 197.134 167.230 173.242 1.00 80.98  ? 4383 THR A O     1 
ATOM   20879 C  CB    . THR A 1 4383 ? 195.401 164.837 174.626 1.00 75.31  ? 4383 THR A CB    1 
ATOM   20880 O  OG1   . THR A 1 4383 ? 194.336 165.481 175.336 1.00 85.32  ? 4383 THR A OG1   1 
ATOM   20881 C  CG2   . THR A 1 4383 ? 195.487 163.373 175.035 1.00 73.97  ? 4383 THR A CG2   1 
ATOM   20882 N  N     . ALA A 1 4384 ? 196.132 167.925 175.131 1.00 80.83  ? 4384 ALA A N     1 
ATOM   20883 C  CA    . ALA A 1 4384 ? 196.094 169.311 174.681 1.00 76.63  ? 4384 ALA A CA    1 
ATOM   20884 C  C     . ALA A 1 4384 ? 197.496 169.897 174.570 1.00 81.13  ? 4384 ALA A C     1 
ATOM   20885 O  O     . ALA A 1 4384 ? 197.795 170.620 173.614 1.00 83.07  ? 4384 ALA A O     1 
ATOM   20886 C  CB    . ALA A 1 4384 ? 195.231 170.145 175.625 1.00 82.34  ? 4384 ALA A CB    1 
ATOM   20887 N  N     . SER A 1 4385 ? 198.370 169.600 175.537 1.00 81.90  ? 4385 SER A N     1 
ATOM   20888 C  CA    . SER A 1 4385 ? 199.750 170.065 175.441 1.00 84.35  ? 4385 SER A CA    1 
ATOM   20889 C  C     . SER A 1 4385 ? 200.458 169.439 174.246 1.00 86.78  ? 4385 SER A C     1 
ATOM   20890 O  O     . SER A 1 4385 ? 201.213 170.115 173.534 1.00 87.16  ? 4385 SER A O     1 
ATOM   20891 C  CB    . SER A 1 4385 ? 200.499 169.757 176.737 1.00 89.15  ? 4385 SER A CB    1 
ATOM   20892 O  OG    . SER A 1 4385 ? 199.811 170.284 177.859 1.00 89.30  ? 4385 SER A OG    1 
ATOM   20893 N  N     . ASN A 1 4386 ? 200.221 168.145 174.007 1.00 83.91  ? 4386 ASN A N     1 
ATOM   20894 C  CA    . ASN A 1 4386 ? 200.814 167.484 172.850 1.00 84.93  ? 4386 ASN A CA    1 
ATOM   20895 C  C     . ASN A 1 4386 ? 200.338 168.122 171.550 1.00 87.03  ? 4386 ASN A C     1 
ATOM   20896 O  O     . ASN A 1 4386 ? 201.132 168.334 170.628 1.00 87.99  ? 4386 ASN A O     1 
ATOM   20897 C  CB    . ASN A 1 4386 ? 200.475 165.993 172.874 1.00 80.87  ? 4386 ASN A CB    1 
ATOM   20898 C  CG    . ASN A 1 4386 ? 201.245 165.195 171.837 1.00 93.77  ? 4386 ASN A CG    1 
ATOM   20899 O  OD1   . ASN A 1 4386 ? 202.037 165.743 171.070 1.00 97.48  ? 4386 ASN A OD1   1 
ATOM   20900 N  ND2   . ASN A 1 4386 ? 201.010 163.888 171.807 1.00 97.95  ? 4386 ASN A ND2   1 
ATOM   20901 N  N     . TRP A 1 4387 ? 199.043 168.430 171.459 1.00 84.68  ? 4387 TRP A N     1 
ATOM   20902 C  CA    . TRP A 1 4387 ? 198.506 169.059 170.257 1.00 74.10  ? 4387 TRP A CA    1 
ATOM   20903 C  C     . TRP A 1 4387 ? 199.076 170.460 170.069 1.00 75.87  ? 4387 TRP A C     1 
ATOM   20904 O  O     . TRP A 1 4387 ? 199.406 170.862 168.948 1.00 80.12  ? 4387 TRP A O     1 
ATOM   20905 C  CB    . TRP A 1 4387 ? 196.980 169.097 170.331 1.00 66.47  ? 4387 TRP A CB    1 
ATOM   20906 C  CG    . TRP A 1 4387 ? 196.348 167.774 170.045 1.00 63.91  ? 4387 TRP A CG    1 
ATOM   20907 C  CD1   . TRP A 1 4387 ? 196.903 166.733 169.361 1.00 68.94  ? 4387 TRP A CD1   1 
ATOM   20908 C  CD2   . TRP A 1 4387 ? 195.048 167.336 170.456 1.00 66.70  ? 4387 TRP A CD2   1 
ATOM   20909 N  NE1   . TRP A 1 4387 ? 196.025 165.678 169.309 1.00 70.84  ? 4387 TRP A NE1   1 
ATOM   20910 C  CE2   . TRP A 1 4387 ? 194.879 166.023 169.976 1.00 70.20  ? 4387 TRP A CE2   1 
ATOM   20911 C  CE3   . TRP A 1 4387 ? 194.009 167.929 171.179 1.00 69.14  ? 4387 TRP A CE3   1 
ATOM   20912 C  CZ2   . TRP A 1 4387 ? 193.713 165.293 170.195 1.00 70.71  ? 4387 TRP A CZ2   1 
ATOM   20913 C  CZ3   . TRP A 1 4387 ? 192.853 167.203 171.396 1.00 65.57  ? 4387 TRP A CZ3   1 
ATOM   20914 C  CH2   . TRP A 1 4387 ? 192.715 165.899 170.907 1.00 66.08  ? 4387 TRP A CH2   1 
ATOM   20915 N  N     . LEU A 1 4388 ? 199.198 171.219 171.161 1.00 76.38  ? 4388 LEU A N     1 
ATOM   20916 C  CA    . LEU A 1 4388 ? 199.764 172.560 171.070 1.00 78.93  ? 4388 LEU A CA    1 
ATOM   20917 C  C     . LEU A 1 4388 ? 201.209 172.513 170.593 1.00 82.09  ? 4388 LEU A C     1 
ATOM   20918 O  O     . LEU A 1 4388 ? 201.630 173.343 169.778 1.00 76.67  ? 4388 LEU A O     1 
ATOM   20919 C  CB    . LEU A 1 4388 ? 199.667 173.264 172.424 1.00 79.80  ? 4388 LEU A CB    1 
ATOM   20920 C  CG    . LEU A 1 4388 ? 198.351 173.982 172.726 1.00 73.16  ? 4388 LEU A CG    1 
ATOM   20921 C  CD1   . LEU A 1 4388 ? 198.297 174.417 174.182 1.00 77.32  ? 4388 LEU A CD1   1 
ATOM   20922 C  CD2   . LEU A 1 4388 ? 198.165 175.173 171.800 1.00 66.57  ? 4388 LEU A CD2   1 
ATOM   20923 N  N     . HIS A 1 4389 ? 201.987 171.552 171.096 1.00 87.96  ? 4389 HIS A N     1 
ATOM   20924 C  CA    . HIS A 1 4389 ? 203.353 171.380 170.610 1.00 89.94  ? 4389 HIS A CA    1 
ATOM   20925 C  C     . HIS A 1 4389 ? 203.369 170.958 169.145 1.00 89.37  ? 4389 HIS A C     1 
ATOM   20926 O  O     . HIS A 1 4389 ? 204.203 171.431 168.363 1.00 89.39  ? 4389 HIS A O     1 
ATOM   20927 C  CB    . HIS A 1 4389 ? 204.092 170.357 171.472 1.00 94.60  ? 4389 HIS A CB    1 
ATOM   20928 C  CG    . HIS A 1 4389 ? 205.567 170.312 171.224 1.00 106.83 ? 4389 HIS A CG    1 
ATOM   20929 N  ND1   . HIS A 1 4389 ? 206.224 169.158 170.852 1.00 112.70 ? 4389 HIS A ND1   1 
ATOM   20930 C  CD2   . HIS A 1 4389 ? 206.513 171.278 171.293 1.00 101.64 ? 4389 HIS A CD2   1 
ATOM   20931 C  CE1   . HIS A 1 4389 ? 207.511 169.416 170.704 1.00 111.54 ? 4389 HIS A CE1   1 
ATOM   20932 N  NE2   . HIS A 1 4389 ? 207.713 170.695 170.965 1.00 103.75 ? 4389 HIS A NE2   1 
ATOM   20933 N  N     . LEU A 1 4390 ? 202.454 170.068 168.757 1.00 85.42  ? 4390 LEU A N     1 
ATOM   20934 C  CA    . LEU A 1 4390 ? 202.446 169.544 167.395 1.00 80.56  ? 4390 LEU A CA    1 
ATOM   20935 C  C     . LEU A 1 4390 ? 201.997 170.599 166.391 1.00 75.00  ? 4390 LEU A C     1 
ATOM   20936 O  O     . LEU A 1 4390 ? 202.582 170.722 165.308 1.00 71.44  ? 4390 LEU A O     1 
ATOM   20937 C  CB    . LEU A 1 4390 ? 201.542 168.313 167.322 1.00 82.14  ? 4390 LEU A CB    1 
ATOM   20938 C  CG    . LEU A 1 4390 ? 201.603 167.459 166.055 1.00 85.79  ? 4390 LEU A CG    1 
ATOM   20939 C  CD1   . LEU A 1 4390 ? 202.766 166.480 166.127 1.00 83.28  ? 4390 LEU A CD1   1 
ATOM   20940 C  CD2   . LEU A 1 4390 ? 200.289 166.725 165.844 1.00 71.42  ? 4390 LEU A CD2   1 
ATOM   20941 N  N     . ILE A 1 4391 ? 200.961 171.361 166.727 1.00 73.21  ? 4391 ILE A N     1 
ATOM   20942 C  CA    . ILE A 1 4391 ? 200.442 172.409 165.851 1.00 67.35  ? 4391 ILE A CA    1 
ATOM   20943 C  C     . ILE A 1 4391 ? 201.442 173.560 165.812 1.00 71.80  ? 4391 ILE A C     1 
ATOM   20944 O  O     . ILE A 1 4391 ? 201.985 173.940 166.859 1.00 75.60  ? 4391 ILE A O     1 
ATOM   20945 C  CB    . ILE A 1 4391 ? 199.057 172.884 166.318 1.00 66.00  ? 4391 ILE A CB    1 
ATOM   20946 C  CG1   . ILE A 1 4391 ? 198.044 171.741 166.239 1.00 72.53  ? 4391 ILE A CG1   1 
ATOM   20947 C  CG2   . ILE A 1 4391 ? 198.575 174.047 165.481 1.00 59.87  ? 4391 ILE A CG2   1 
ATOM   20948 C  CD1   . ILE A 1 4391 ? 196.728 172.050 166.919 1.00 62.80  ? 4391 ILE A CD1   1 
ATOM   20949 N  N     . PRO A 1 4392 ? 201.728 174.128 164.639 1.00 72.82  ? 4392 PRO A N     1 
ATOM   20950 C  CA    . PRO A 1 4392 ? 202.644 175.274 164.578 1.00 74.66  ? 4392 PRO A CA    1 
ATOM   20951 C  C     . PRO A 1 4392 ? 202.126 176.449 165.396 1.00 76.00  ? 4392 PRO A C     1 
ATOM   20952 O  O     . PRO A 1 4392 ? 200.922 176.704 165.460 1.00 78.47  ? 4392 PRO A O     1 
ATOM   20953 C  CB    . PRO A 1 4392 ? 202.695 175.605 163.083 1.00 68.55  ? 4392 PRO A CB    1 
ATOM   20954 C  CG    . PRO A 1 4392 ? 202.372 174.315 162.409 1.00 66.62  ? 4392 PRO A CG    1 
ATOM   20955 C  CD    . PRO A 1 4392 ? 201.368 173.638 163.297 1.00 68.19  ? 4392 PRO A CD    1 
ATOM   20956 N  N     . GLN A 1 4393 ? 203.059 177.166 166.026 1.00 79.46  ? 4393 GLN A N     1 
ATOM   20957 C  CA    . GLN A 1 4393 ? 202.683 178.226 166.957 1.00 79.12  ? 4393 GLN A CA    1 
ATOM   20958 C  C     . GLN A 1 4393 ? 202.036 179.404 166.238 1.00 78.93  ? 4393 GLN A C     1 
ATOM   20959 O  O     . GLN A 1 4393 ? 200.977 179.890 166.653 1.00 81.12  ? 4393 GLN A O     1 
ATOM   20960 C  CB    . GLN A 1 4393 ? 203.908 178.687 167.748 1.00 76.86  ? 4393 GLN A CB    1 
ATOM   20961 C  CG    . GLN A 1 4393 ? 204.745 177.554 168.319 1.00 79.24  ? 4393 GLN A CG    1 
ATOM   20962 C  CD    . GLN A 1 4393 ? 205.899 177.166 167.414 1.00 94.89  ? 4393 GLN A CD    1 
ATOM   20963 O  OE1   . GLN A 1 4393 ? 205.715 176.933 166.220 1.00 93.00  ? 4393 GLN A OE1   1 
ATOM   20964 N  NE2   . GLN A 1 4393 ? 207.097 177.096 167.981 1.00 98.70  ? 4393 GLN A NE2   1 
ATOM   20965 N  N     . THR A 1 4394 ? 202.655 179.886 165.163 1.00 76.80  ? 4394 THR A N     1 
ATOM   20966 C  CA    . THR A 1 4394 ? 202.166 181.077 164.486 1.00 81.11  ? 4394 THR A CA    1 
ATOM   20967 C  C     . THR A 1 4394 ? 202.280 180.910 162.978 1.00 82.93  ? 4394 THR A C     1 
ATOM   20968 O  O     . THR A 1 4394 ? 203.171 180.221 162.476 1.00 80.16  ? 4394 THR A O     1 
ATOM   20969 C  CB    . THR A 1 4394 ? 202.931 182.334 164.930 1.00 83.90  ? 4394 THR A CB    1 
ATOM   20970 O  OG1   . THR A 1 4394 ? 202.488 183.462 164.164 1.00 83.52  ? 4394 THR A OG1   1 
ATOM   20971 C  CG2   . THR A 1 4394 ? 204.429 182.149 164.738 1.00 82.16  ? 4394 THR A CG2   1 
ATOM   20972 N  N     . LEU A 1 4395 ? 201.358 181.552 162.264 1.00 78.39  ? 4395 LEU A N     1 
ATOM   20973 C  CA    . LEU A 1 4395 ? 201.359 181.595 160.807 1.00 76.90  ? 4395 LEU A CA    1 
ATOM   20974 C  C     . LEU A 1 4395 ? 201.351 183.052 160.370 1.00 81.94  ? 4395 LEU A C     1 
ATOM   20975 O  O     . LEU A 1 4395 ? 200.429 183.800 160.712 1.00 83.32  ? 4395 LEU A O     1 
ATOM   20976 C  CB    . LEU A 1 4395 ? 200.153 180.851 160.231 1.00 73.87  ? 4395 LEU A CB    1 
ATOM   20977 C  CG    . LEU A 1 4395 ? 199.818 181.105 158.760 1.00 69.83  ? 4395 LEU A CG    1 
ATOM   20978 C  CD1   . LEU A 1 4395 ? 200.901 180.549 157.853 1.00 69.35  ? 4395 LEU A CD1   1 
ATOM   20979 C  CD2   . LEU A 1 4395 ? 198.467 180.505 158.409 1.00 68.66  ? 4395 LEU A CD2   1 
ATOM   20980 N  N     . SER A 1 4396 ? 202.372 183.450 159.618 1.00 86.76  ? 4396 SER A N     1 
ATOM   20981 C  CA    . SER A 1 4396 ? 202.469 184.821 159.148 1.00 86.00  ? 4396 SER A CA    1 
ATOM   20982 C  C     . SER A 1 4396 ? 201.513 185.059 157.983 1.00 89.43  ? 4396 SER A C     1 
ATOM   20983 O  O     . SER A 1 4396 ? 201.156 184.142 157.238 1.00 94.52  ? 4396 SER A O     1 
ATOM   20984 C  CB    . SER A 1 4396 ? 203.901 185.144 158.723 1.00 85.55  ? 4396 SER A CB    1 
ATOM   20985 O  OG    . SER A 1 4396 ? 204.822 184.818 159.749 1.00 88.28  ? 4396 SER A OG    1 
ATOM   20986 N  N     . HIS A 1 4397 ? 201.102 186.313 157.831 1.00 87.42  ? 4397 HIS A N     1 
ATOM   20987 C  CA    . HIS A 1 4397 ? 200.243 186.724 156.735 1.00 91.61  ? 4397 HIS A CA    1 
ATOM   20988 C  C     . HIS A 1 4397 ? 201.099 187.129 155.537 1.00 96.35  ? 4397 HIS A C     1 
ATOM   20989 O  O     . HIS A 1 4397 ? 202.331 187.128 155.588 1.00 97.41  ? 4397 HIS A O     1 
ATOM   20990 C  CB    . HIS A 1 4397 ? 199.320 187.867 157.164 1.00 94.03  ? 4397 HIS A CB    1 
ATOM   20991 C  CG    . HIS A 1 4397 ? 198.556 187.592 158.422 1.00 100.03 ? 4397 HIS A CG    1 
ATOM   20992 N  ND1   . HIS A 1 4397 ? 199.162 187.476 159.655 1.00 101.32 ? 4397 HIS A ND1   1 
ATOM   20993 C  CD2   . HIS A 1 4397 ? 197.231 187.414 158.637 1.00 98.13  ? 4397 HIS A CD2   1 
ATOM   20994 C  CE1   . HIS A 1 4397 ? 198.244 187.236 160.574 1.00 99.81  ? 4397 HIS A CE1   1 
ATOM   20995 N  NE2   . HIS A 1 4397 ? 197.064 187.194 159.983 1.00 100.56 ? 4397 HIS A NE2   1 
ATOM   20996 N  N     . LEU A 1 4398 ? 200.432 187.480 154.443 1.00 98.07  ? 4398 LEU A N     1 
ATOM   20997 C  CA    . LEU A 1 4398 ? 201.104 187.877 153.216 1.00 105.07 ? 4398 LEU A CA    1 
ATOM   20998 C  C     . LEU A 1 4398 ? 200.966 189.381 153.023 1.00 109.52 ? 4398 LEU A C     1 
ATOM   20999 O  O     . LEU A 1 4398 ? 199.877 189.941 153.180 1.00 109.93 ? 4398 LEU A O     1 
ATOM   21000 C  CB    . LEU A 1 4398 ? 200.524 187.137 152.011 1.00 104.92 ? 4398 LEU A CB    1 
ATOM   21001 C  CG    . LEU A 1 4398 ? 200.649 185.613 152.009 1.00 92.78  ? 4398 LEU A CG    1 
ATOM   21002 C  CD1   . LEU A 1 4398 ? 199.934 185.017 150.804 1.00 87.19  ? 4398 LEU A CD1   1 
ATOM   21003 C  CD2   . LEU A 1 4398 ? 202.100 185.184 152.051 1.00 86.47  ? 4398 LEU A CD2   1 
ATOM   21004 N  N     . LYS A 1 4399 ? 202.075 190.031 152.679 1.00 108.44 ? 4399 LYS A N     1 
ATOM   21005 C  CA    . LYS A 1 4399 ? 202.123 191.483 152.568 1.00 108.14 ? 4399 LYS A CA    1 
ATOM   21006 C  C     . LYS A 1 4399 ? 201.493 191.919 151.250 1.00 106.44 ? 4399 LYS A C     1 
ATOM   21007 O  O     . LYS A 1 4399 ? 201.973 191.549 150.173 1.00 106.06 ? 4399 LYS A O     1 
ATOM   21008 C  CB    . LYS A 1 4399 ? 203.565 191.979 152.667 1.00 102.82 ? 4399 LYS A CB    1 
ATOM   21009 C  CG    . LYS A 1 4399 ? 204.129 191.962 154.079 1.00 95.72  ? 4399 LYS A CG    1 
ATOM   21010 C  CD    . LYS A 1 4399 ? 204.854 190.659 154.370 1.00 90.69  ? 4399 LYS A CD    1 
ATOM   21011 C  CE    . LYS A 1 4399 ? 205.599 190.726 155.693 1.00 83.58  ? 4399 LYS A CE    1 
ATOM   21012 N  NZ    . LYS A 1 4399 ? 206.554 189.594 155.849 1.00 78.33  ? 4399 LYS A NZ    1 
ATOM   21013 N  N     . ARG A 1 4400 ? 200.421 192.703 151.339 1.00 103.05 ? 4400 ARG A N     1 
ATOM   21014 C  CA    . ARG A 1 4400 ? 199.762 193.211 150.144 1.00 113.03 ? 4400 ARG A CA    1 
ATOM   21015 C  C     . ARG A 1 4400 ? 200.618 194.273 149.466 1.00 125.14 ? 4400 ARG A C     1 
ATOM   21016 O  O     . ARG A 1 4400 ? 201.402 194.973 150.113 1.00 124.15 ? 4400 ARG A O     1 
ATOM   21017 C  CB    . ARG A 1 4400 ? 198.392 193.790 150.495 1.00 105.87 ? 4400 ARG A CB    1 
ATOM   21018 C  CG    . ARG A 1 4400 ? 197.273 192.765 150.546 1.00 99.07  ? 4400 ARG A CG    1 
ATOM   21019 C  CD    . ARG A 1 4400 ? 195.913 193.443 150.507 1.00 98.33  ? 4400 ARG A CD    1 
ATOM   21020 N  NE    . ARG A 1 4400 ? 194.887 192.581 149.931 1.00 102.63 ? 4400 ARG A NE    1 
ATOM   21021 C  CZ    . ARG A 1 4400 ? 193.650 192.971 149.655 1.00 96.84  ? 4400 ARG A CZ    1 
ATOM   21022 N  NH1   . ARG A 1 4400 ? 193.248 194.210 149.883 1.00 93.11  ? 4400 ARG A NH1   1 
ATOM   21023 N  NH2   . ARG A 1 4400 ? 192.795 192.095 149.135 1.00 87.68  ? 4400 ARG A NH2   1 
ATOM   21024 N  N     . THR A 1 4401 ? 200.462 194.389 148.148 1.00 127.34 ? 4401 THR A N     1 
ATOM   21025 C  CA    . THR A 1 4401 ? 201.184 195.373 147.356 1.00 124.45 ? 4401 THR A CA    1 
ATOM   21026 C  C     . THR A 1 4401 ? 200.297 195.758 146.176 1.00 127.45 ? 4401 THR A C     1 
ATOM   21027 O  O     . THR A 1 4401 ? 199.377 195.023 145.807 1.00 128.90 ? 4401 THR A O     1 
ATOM   21028 C  CB    . THR A 1 4401 ? 202.547 194.820 146.898 1.00 120.50 ? 4401 THR A CB    1 
ATOM   21029 O  OG1   . THR A 1 4401 ? 203.296 194.405 148.046 1.00 121.42 ? 4401 THR A OG1   1 
ATOM   21030 C  CG2   . THR A 1 4401 ? 203.365 195.883 146.185 1.00 117.90 ? 4401 THR A CG2   1 
ATOM   21031 N  N     . VAL A 1 4402 ? 200.570 196.930 145.593 1.00 129.94 ? 4402 VAL A N     1 
ATOM   21032 C  CA    . VAL A 1 4402 ? 199.683 197.486 144.572 1.00 132.69 ? 4402 VAL A CA    1 
ATOM   21033 C  C     . VAL A 1 4402 ? 199.589 196.558 143.363 1.00 127.38 ? 4402 VAL A C     1 
ATOM   21034 O  O     . VAL A 1 4402 ? 198.501 196.330 142.820 1.00 118.24 ? 4402 VAL A O     1 
ATOM   21035 C  CB    . VAL A 1 4402 ? 200.137 198.905 144.176 1.00 137.20 ? 4402 VAL A CB    1 
ATOM   21036 C  CG1   . VAL A 1 4402 ? 200.029 199.840 145.369 1.00 144.25 ? 4402 VAL A CG1   1 
ATOM   21037 C  CG2   . VAL A 1 4402 ? 201.568 198.901 143.654 1.00 131.69 ? 4402 VAL A CG2   1 
ATOM   21038 N  N     . GLU A 1 4403 ? 200.723 196.007 142.919 1.00 128.11 ? 4403 GLU A N     1 
ATOM   21039 C  CA    . GLU A 1 4403 ? 200.679 195.070 141.802 1.00 124.64 ? 4403 GLU A CA    1 
ATOM   21040 C  C     . GLU A 1 4403 ? 200.341 193.656 142.257 1.00 119.17 ? 4403 GLU A C     1 
ATOM   21041 O  O     . GLU A 1 4403 ? 200.023 192.801 141.422 1.00 110.10 ? 4403 GLU A O     1 
ATOM   21042 C  CB    . GLU A 1 4403 ? 202.008 195.073 141.041 1.00 121.49 ? 4403 GLU A CB    1 
ATOM   21043 C  CG    . GLU A 1 4403 ? 203.126 194.282 141.704 1.00 117.73 ? 4403 GLU A CG    1 
ATOM   21044 C  CD    . GLU A 1 4403 ? 203.796 195.045 142.827 1.00 121.76 ? 4403 GLU A CD    1 
ATOM   21045 O  OE1   . GLU A 1 4403 ? 203.454 196.230 143.029 1.00 123.52 ? 4403 GLU A OE1   1 
ATOM   21046 O  OE2   . GLU A 1 4403 ? 204.665 194.461 143.509 1.00 118.51 ? 4403 GLU A OE2   1 
ATOM   21047 N  N     . ASN A 1 4404 ? 200.404 193.392 143.564 1.00 118.06 ? 4404 ASN A N     1 
ATOM   21048 C  CA    . ASN A 1 4404 ? 200.063 192.065 144.065 1.00 104.72 ? 4404 ASN A CA    1 
ATOM   21049 C  C     . ASN A 1 4404 ? 198.560 191.822 144.036 1.00 105.05 ? 4404 ASN A C     1 
ATOM   21050 O  O     . ASN A 1 4404 ? 198.123 190.669 143.950 1.00 106.00 ? 4404 ASN A O     1 
ATOM   21051 C  CB    . ASN A 1 4404 ? 200.598 191.886 145.486 1.00 103.42 ? 4404 ASN A CB    1 
ATOM   21052 C  CG    . ASN A 1 4404 ? 202.059 191.482 145.512 1.00 110.43 ? 4404 ASN A CG    1 
ATOM   21053 O  OD1   . ASN A 1 4404 ? 202.643 191.161 144.478 1.00 113.08 ? 4404 ASN A OD1   1 
ATOM   21054 N  ND2   . ASN A 1 4404 ? 202.654 191.487 146.699 1.00 107.75 ? 4404 ASN A ND2   1 
ATOM   21055 N  N     . ILE A 1 4405 ? 197.760 192.888 144.111 1.00 108.88 ? 4405 ILE A N     1 
ATOM   21056 C  CA    . ILE A 1 4405 ? 196.308 192.735 144.159 1.00 107.69 ? 4405 ILE A CA    1 
ATOM   21057 C  C     . ILE A 1 4405 ? 195.787 192.131 142.861 1.00 103.68 ? 4405 ILE A C     1 
ATOM   21058 O  O     . ILE A 1 4405 ? 194.927 191.242 142.874 1.00 99.51  ? 4405 ILE A O     1 
ATOM   21059 C  CB    . ILE A 1 4405 ? 195.638 194.089 144.462 1.00 110.75 ? 4405 ILE A CB    1 
ATOM   21060 C  CG1   . ILE A 1 4405 ? 196.092 194.625 145.822 1.00 120.53 ? 4405 ILE A CG1   1 
ATOM   21061 C  CG2   . ILE A 1 4405 ? 194.123 193.957 144.423 1.00 91.42  ? 4405 ILE A CG2   1 
ATOM   21062 C  CD1   . ILE A 1 4405 ? 196.186 193.570 146.904 1.00 111.75 ? 4405 ILE A CD1   1 
ATOM   21063 N  N     . LYS A 1 4406 ? 196.298 192.601 141.721 1.00 105.15 ? 4406 LYS A N     1 
ATOM   21064 C  CA    . LYS A 1 4406 ? 195.818 192.116 140.433 1.00 97.61  ? 4406 LYS A CA    1 
ATOM   21065 C  C     . LYS A 1 4406 ? 196.199 190.664 140.175 1.00 96.44  ? 4406 LYS A C     1 
ATOM   21066 O  O     . LYS A 1 4406 ? 195.616 190.033 139.287 1.00 90.14  ? 4406 LYS A O     1 
ATOM   21067 C  CB    . LYS A 1 4406 ? 196.350 193.004 139.307 1.00 91.07  ? 4406 LYS A CB    1 
ATOM   21068 C  CG    . LYS A 1 4406 ? 196.026 194.479 139.483 1.00 97.78  ? 4406 LYS A CG    1 
ATOM   21069 C  CD    . LYS A 1 4406 ? 194.669 194.824 138.892 1.00 92.53  ? 4406 LYS A CD    1 
ATOM   21070 C  CE    . LYS A 1 4406 ? 194.459 196.329 138.833 1.00 88.24  ? 4406 LYS A CE    1 
ATOM   21071 N  NZ    . LYS A 1 4406 ? 195.580 197.024 138.144 1.00 77.49  ? 4406 LYS A NZ    1 
ATOM   21072 N  N     . ASP A 1 4407 ? 197.153 190.124 140.921 1.00 101.26 ? 4407 ASP A N     1 
ATOM   21073 C  CA    . ASP A 1 4407 ? 197.549 188.732 140.745 1.00 92.52  ? 4407 ASP A CA    1 
ATOM   21074 C  C     . ASP A 1 4407 ? 196.489 187.816 141.343 1.00 89.99  ? 4407 ASP A C     1 
ATOM   21075 O  O     . ASP A 1 4407 ? 196.207 187.914 142.545 1.00 91.90  ? 4407 ASP A O     1 
ATOM   21076 C  CB    . ASP A 1 4407 ? 198.904 188.482 141.402 1.00 88.74  ? 4407 ASP A CB    1 
ATOM   21077 C  CG    . ASP A 1 4407 ? 199.637 187.299 140.802 1.00 89.58  ? 4407 ASP A CG    1 
ATOM   21078 O  OD1   . ASP A 1 4407 ? 198.975 186.302 140.443 1.00 82.54  ? 4407 ASP A OD1   1 
ATOM   21079 O  OD2   . ASP A 1 4407 ? 200.879 187.364 140.691 1.00 95.93  ? 4407 ASP A OD2   1 
ATOM   21080 N  N     . PRO A 1 4408 ? 195.880 186.922 140.560 1.00 84.02  ? 4408 PRO A N     1 
ATOM   21081 C  CA    . PRO A 1 4408 ? 194.856 186.036 141.133 1.00 80.39  ? 4408 PRO A CA    1 
ATOM   21082 C  C     . PRO A 1 4408 ? 195.431 184.951 142.024 1.00 76.29  ? 4408 PRO A C     1 
ATOM   21083 O  O     . PRO A 1 4408 ? 194.782 184.565 143.005 1.00 78.81  ? 4408 PRO A O     1 
ATOM   21084 C  CB    . PRO A 1 4408 ? 194.171 185.446 139.894 1.00 72.40  ? 4408 PRO A CB    1 
ATOM   21085 C  CG    . PRO A 1 4408 ? 195.218 185.502 138.839 1.00 73.14  ? 4408 PRO A CG    1 
ATOM   21086 C  CD    . PRO A 1 4408 ? 196.020 186.741 139.106 1.00 78.50  ? 4408 PRO A CD    1 
ATOM   21087 N  N     . LEU A 1 4409 ? 196.626 184.442 141.712 1.00 70.69  ? 4409 LEU A N     1 
ATOM   21088 C  CA    . LEU A 1 4409 ? 197.274 183.489 142.606 1.00 75.07  ? 4409 LEU A CA    1 
ATOM   21089 C  C     . LEU A 1 4409 ? 197.547 184.121 143.963 1.00 82.57  ? 4409 LEU A C     1 
ATOM   21090 O  O     . LEU A 1 4409 ? 197.322 183.496 145.008 1.00 83.12  ? 4409 LEU A O     1 
ATOM   21091 C  CB    . LEU A 1 4409 ? 198.573 182.981 141.981 1.00 67.71  ? 4409 LEU A CB    1 
ATOM   21092 C  CG    . LEU A 1 4409 ? 198.471 181.773 141.050 1.00 66.38  ? 4409 LEU A CG    1 
ATOM   21093 C  CD1   . LEU A 1 4409 ? 199.833 181.437 140.468 1.00 64.49  ? 4409 LEU A CD1   1 
ATOM   21094 C  CD2   . LEU A 1 4409 ? 197.890 180.578 141.786 1.00 62.59  ? 4409 LEU A CD2   1 
ATOM   21095 N  N     . PHE A 1 4410 ? 198.025 185.368 143.964 1.00 85.90  ? 4410 PHE A N     1 
ATOM   21096 C  CA    . PHE A 1 4410 ? 198.254 186.065 145.222 1.00 82.39  ? 4410 PHE A CA    1 
ATOM   21097 C  C     . PHE A 1 4410 ? 196.951 186.312 145.967 1.00 83.88  ? 4410 PHE A C     1 
ATOM   21098 O  O     . PHE A 1 4410 ? 196.930 186.243 147.194 1.00 93.17  ? 4410 PHE A O     1 
ATOM   21099 C  CB    . PHE A 1 4410 ? 198.985 187.385 144.981 1.00 85.62  ? 4410 PHE A CB    1 
ATOM   21100 C  CG    . PHE A 1 4410 ? 199.291 188.144 146.244 1.00 94.78  ? 4410 PHE A CG    1 
ATOM   21101 C  CD1   . PHE A 1 4410 ? 200.438 187.869 146.970 1.00 96.93  ? 4410 PHE A CD1   1 
ATOM   21102 C  CD2   . PHE A 1 4410 ? 198.433 189.129 146.706 1.00 96.31  ? 4410 PHE A CD2   1 
ATOM   21103 C  CE1   . PHE A 1 4410 ? 200.724 188.561 148.131 1.00 97.84  ? 4410 PHE A CE1   1 
ATOM   21104 C  CE2   . PHE A 1 4410 ? 198.713 189.823 147.867 1.00 101.76 ? 4410 PHE A CE2   1 
ATOM   21105 C  CZ    . PHE A 1 4410 ? 199.861 189.539 148.580 1.00 104.01 ? 4410 PHE A CZ    1 
ATOM   21106 N  N     . ARG A 1 4411 ? 195.861 186.603 145.253 1.00 79.16  ? 4411 ARG A N     1 
ATOM   21107 C  CA    . ARG A 1 4411 ? 194.569 186.781 145.912 1.00 84.11  ? 4411 ARG A CA    1 
ATOM   21108 C  C     . ARG A 1 4411 ? 194.103 185.487 146.572 1.00 86.30  ? 4411 ARG A C     1 
ATOM   21109 O  O     . ARG A 1 4411 ? 193.640 185.487 147.723 1.00 91.65  ? 4411 ARG A O     1 
ATOM   21110 C  CB    . ARG A 1 4411 ? 193.535 187.267 144.896 1.00 78.51  ? 4411 ARG A CB    1 
ATOM   21111 C  CG    . ARG A 1 4411 ? 193.647 188.741 144.549 1.00 83.35  ? 4411 ARG A CG    1 
ATOM   21112 C  CD    . ARG A 1 4411 ? 192.364 189.253 143.918 1.00 81.95  ? 4411 ARG A CD    1 
ATOM   21113 N  NE    . ARG A 1 4411 ? 191.992 188.477 142.741 1.00 76.48  ? 4411 ARG A NE    1 
ATOM   21114 C  CZ    . ARG A 1 4411 ? 191.798 188.992 141.535 1.00 82.71  ? 4411 ARG A CZ    1 
ATOM   21115 N  NH1   . ARG A 1 4411 ? 191.932 190.289 141.307 1.00 85.88  ? 4411 ARG A NH1   1 
ATOM   21116 N  NH2   . ARG A 1 4411 ? 191.459 188.187 140.532 1.00 76.70  ? 4411 ARG A NH2   1 
ATOM   21117 N  N     . PHE A 1 4412 ? 194.217 184.369 145.850 1.00 79.00  ? 4412 PHE A N     1 
ATOM   21118 C  CA    . PHE A 1 4412 ? 193.803 183.084 146.401 1.00 76.89  ? 4412 PHE A CA    1 
ATOM   21119 C  C     . PHE A 1 4412 ? 194.633 182.727 147.625 1.00 71.28  ? 4412 PHE A C     1 
ATOM   21120 O  O     . PHE A 1 4412 ? 194.098 182.279 148.646 1.00 70.41  ? 4412 PHE A O     1 
ATOM   21121 C  CB    . PHE A 1 4412 ? 193.906 181.997 145.325 1.00 73.78  ? 4412 PHE A CB    1 
ATOM   21122 C  CG    . PHE A 1 4412 ? 193.975 180.595 145.871 1.00 70.86  ? 4412 PHE A CG    1 
ATOM   21123 C  CD1   . PHE A 1 4412 ? 195.197 179.996 146.140 1.00 69.56  ? 4412 PHE A CD1   1 
ATOM   21124 C  CD2   . PHE A 1 4412 ? 192.817 179.879 146.122 1.00 61.58  ? 4412 PHE A CD2   1 
ATOM   21125 C  CE1   . PHE A 1 4412 ? 195.260 178.712 146.643 1.00 67.72  ? 4412 PHE A CE1   1 
ATOM   21126 C  CE2   . PHE A 1 4412 ? 192.875 178.593 146.625 1.00 61.28  ? 4412 PHE A CE2   1 
ATOM   21127 C  CZ    . PHE A 1 4412 ? 194.098 178.010 146.886 1.00 67.21  ? 4412 PHE A CZ    1 
ATOM   21128 N  N     . PHE A 1 4413 ? 195.949 182.935 147.548 1.00 69.15  ? 4413 PHE A N     1 
ATOM   21129 C  CA    . PHE A 1 4413 ? 196.790 182.622 148.695 1.00 75.31  ? 4413 PHE A CA    1 
ATOM   21130 C  C     . PHE A 1 4413 ? 196.583 183.617 149.832 1.00 80.29  ? 4413 PHE A C     1 
ATOM   21131 O  O     . PHE A 1 4413 ? 196.735 183.252 150.998 1.00 83.25  ? 4413 PHE A O     1 
ATOM   21132 C  CB    . PHE A 1 4413 ? 198.254 182.553 148.266 1.00 73.60  ? 4413 PHE A CB    1 
ATOM   21133 C  CG    . PHE A 1 4413 ? 198.623 181.250 147.612 1.00 78.41  ? 4413 PHE A CG    1 
ATOM   21134 C  CD1   . PHE A 1 4413 ? 198.292 180.045 148.210 1.00 77.65  ? 4413 PHE A CD1   1 
ATOM   21135 C  CD2   . PHE A 1 4413 ? 199.281 181.226 146.394 1.00 78.29  ? 4413 PHE A CD2   1 
ATOM   21136 C  CE1   . PHE A 1 4413 ? 198.621 178.845 147.612 1.00 73.81  ? 4413 PHE A CE1   1 
ATOM   21137 C  CE2   . PHE A 1 4413 ? 199.615 180.027 145.793 1.00 71.54  ? 4413 PHE A CE2   1 
ATOM   21138 C  CZ    . PHE A 1 4413 ? 199.284 178.835 146.403 1.00 70.66  ? 4413 PHE A CZ    1 
ATOM   21139 N  N     . GLU A 1 4414 ? 196.206 184.860 149.519 1.00 82.47  ? 4414 GLU A N     1 
ATOM   21140 C  CA    . GLU A 1 4414 ? 195.799 185.808 150.551 1.00 83.57  ? 4414 GLU A CA    1 
ATOM   21141 C  C     . GLU A 1 4414 ? 194.620 185.268 151.342 1.00 80.21  ? 4414 GLU A C     1 
ATOM   21142 O  O     . GLU A 1 4414 ? 194.644 185.233 152.580 1.00 77.71  ? 4414 GLU A O     1 
ATOM   21143 C  CB    . GLU A 1 4414 ? 195.430 187.148 149.907 1.00 86.50  ? 4414 GLU A CB    1 
ATOM   21144 C  CG    . GLU A 1 4414 ? 195.442 188.356 150.841 1.00 98.00  ? 4414 GLU A CG    1 
ATOM   21145 C  CD    . GLU A 1 4414 ? 196.680 188.436 151.707 1.00 104.39 ? 4414 GLU A CD    1 
ATOM   21146 O  OE1   . GLU A 1 4414 ? 197.780 188.156 151.192 1.00 101.55 ? 4414 GLU A OE1   1 
ATOM   21147 O  OE2   . GLU A 1 4414 ? 196.554 188.778 152.902 1.00 100.79 ? 4414 GLU A OE2   1 
ATOM   21148 N  N     . ARG A 1 4415 ? 193.574 184.837 150.634 1.00 72.94  ? 4415 ARG A N     1 
ATOM   21149 C  CA    . ARG A 1 4415 ? 192.402 184.294 151.315 1.00 73.62  ? 4415 ARG A CA    1 
ATOM   21150 C  C     . ARG A 1 4415 ? 192.761 183.046 152.112 1.00 76.44  ? 4415 ARG A C     1 
ATOM   21151 O  O     . ARG A 1 4415 ? 192.324 182.882 153.261 1.00 77.51  ? 4415 ARG A O     1 
ATOM   21152 C  CB    . ARG A 1 4415 ? 191.299 183.989 150.302 1.00 67.36  ? 4415 ARG A CB    1 
ATOM   21153 C  CG    . ARG A 1 4415 ? 189.977 183.585 150.931 1.00 63.52  ? 4415 ARG A CG    1 
ATOM   21154 C  CD    . ARG A 1 4415 ? 188.810 184.287 150.259 1.00 55.85  ? 4415 ARG A CD    1 
ATOM   21155 N  NE    . ARG A 1 4415 ? 188.403 183.616 149.031 1.00 58.88  ? 4415 ARG A NE    1 
ATOM   21156 C  CZ    . ARG A 1 4415 ? 187.604 182.559 148.985 1.00 62.94  ? 4415 ARG A CZ    1 
ATOM   21157 N  NH1   . ARG A 1 4415 ? 187.102 182.023 150.085 1.00 66.81  ? 4415 ARG A NH1   1 
ATOM   21158 N  NH2   . ARG A 1 4415 ? 187.301 182.026 147.805 1.00 58.24  ? 4415 ARG A NH2   1 
ATOM   21159 N  N     . GLU A 1 4416 ? 193.568 182.160 151.522 1.00 75.00  ? 4416 GLU A N     1 
ATOM   21160 C  CA    . GLU A 1 4416 ? 193.942 180.924 152.202 1.00 71.26  ? 4416 GLU A CA    1 
ATOM   21161 C  C     . GLU A 1 4416 ? 194.722 181.207 153.480 1.00 71.31  ? 4416 GLU A C     1 
ATOM   21162 O  O     . GLU A 1 4416 ? 194.434 180.630 154.533 1.00 76.60  ? 4416 GLU A O     1 
ATOM   21163 C  CB    . GLU A 1 4416 ? 194.756 180.031 151.262 1.00 72.21  ? 4416 GLU A CB    1 
ATOM   21164 C  CG    . GLU A 1 4416 ? 193.975 179.424 150.094 1.00 75.03  ? 4416 GLU A CG    1 
ATOM   21165 C  CD    . GLU A 1 4416 ? 192.571 178.956 150.456 1.00 83.30  ? 4416 GLU A CD    1 
ATOM   21166 O  OE1   . GLU A 1 4416 ? 192.358 178.465 151.585 1.00 83.77  ? 4416 GLU A OE1   1 
ATOM   21167 O  OE2   . GLU A 1 4416 ? 191.671 179.084 149.600 1.00 89.91  ? 4416 GLU A OE2   1 
ATOM   21168 N  N     . VAL A 1 4417 ? 195.710 182.103 153.409 1.00 72.14  ? 4417 VAL A N     1 
ATOM   21169 C  CA    . VAL A 1 4417 ? 196.521 182.415 154.581 1.00 71.32  ? 4417 VAL A CA    1 
ATOM   21170 C  C     . VAL A 1 4417 ? 195.686 183.111 155.646 1.00 72.75  ? 4417 VAL A C     1 
ATOM   21171 O  O     . VAL A 1 4417 ? 195.833 182.830 156.839 1.00 70.11  ? 4417 VAL A O     1 
ATOM   21172 C  CB    . VAL A 1 4417 ? 197.751 183.250 154.180 1.00 72.41  ? 4417 VAL A CB    1 
ATOM   21173 C  CG1   . VAL A 1 4417 ? 198.526 183.671 155.412 1.00 77.29  ? 4417 VAL A CG1   1 
ATOM   21174 C  CG2   . VAL A 1 4417 ? 198.658 182.438 153.270 1.00 74.52  ? 4417 VAL A CG2   1 
ATOM   21175 N  N     . LYS A 1 4418 ? 194.794 184.022 155.245 1.00 71.83  ? 4418 LYS A N     1 
ATOM   21176 C  CA    . LYS A 1 4418 ? 193.950 184.689 156.232 1.00 71.88  ? 4418 LYS A CA    1 
ATOM   21177 C  C     . LYS A 1 4418 ? 193.071 183.686 156.970 1.00 69.96  ? 4418 LYS A C     1 
ATOM   21178 O  O     . LYS A 1 4418 ? 193.024 183.673 158.209 1.00 71.46  ? 4418 LYS A O     1 
ATOM   21179 C  CB    . LYS A 1 4418 ? 193.092 185.762 155.560 1.00 67.59  ? 4418 LYS A CB    1 
ATOM   21180 C  CG    . LYS A 1 4418 ? 193.803 187.090 155.355 1.00 69.66  ? 4418 LYS A CG    1 
ATOM   21181 C  CD    . LYS A 1 4418 ? 192.805 188.230 155.233 1.00 71.21  ? 4418 LYS A CD    1 
ATOM   21182 C  CE    . LYS A 1 4418 ? 192.026 188.153 153.931 1.00 78.76  ? 4418 LYS A CE    1 
ATOM   21183 N  NZ    . LYS A 1 4418 ? 191.133 189.330 153.747 1.00 70.53  ? 4418 LYS A NZ    1 
ATOM   21184 N  N     . MET A 1 4419 ? 192.375 182.823 156.222 1.00 65.63  ? 4419 MET A N     1 
ATOM   21185 C  CA    . MET A 1 4419 ? 191.492 181.850 156.859 1.00 65.46  ? 4419 MET A CA    1 
ATOM   21186 C  C     . MET A 1 4419 ? 192.280 180.865 157.714 1.00 62.29  ? 4419 MET A C     1 
ATOM   21187 O  O     . MET A 1 4419 ? 191.858 180.517 158.826 1.00 60.66  ? 4419 MET A O     1 
ATOM   21188 C  CB    . MET A 1 4419 ? 190.669 181.118 155.799 1.00 68.40  ? 4419 MET A CB    1 
ATOM   21189 C  CG    . MET A 1 4419 ? 189.286 180.699 156.272 1.00 71.77  ? 4419 MET A CG    1 
ATOM   21190 S  SD    . MET A 1 4419 ? 188.622 179.289 155.367 1.00 79.25  ? 4419 MET A SD    1 
ATOM   21191 C  CE    . MET A 1 4419 ? 188.818 179.847 153.677 1.00 71.35  ? 4419 MET A CE    1 
ATOM   21192 N  N     . GLY A 1 4420 ? 193.434 180.412 157.219 1.00 59.48  ? 4420 GLY A N     1 
ATOM   21193 C  CA    . GLY A 1 4420 ? 194.246 179.486 157.987 1.00 59.15  ? 4420 GLY A CA    1 
ATOM   21194 C  C     . GLY A 1 4420 ? 194.780 180.095 159.267 1.00 63.27  ? 4420 GLY A C     1 
ATOM   21195 O  O     . GLY A 1 4420 ? 194.797 179.441 160.309 1.00 67.92  ? 4420 GLY A O     1 
ATOM   21196 N  N     . ALA A 1 4421 ? 195.222 181.354 159.210 1.00 64.24  ? 4421 ALA A N     1 
ATOM   21197 C  CA    . ALA A 1 4421 ? 195.708 182.024 160.410 1.00 64.46  ? 4421 ALA A CA    1 
ATOM   21198 C  C     . ALA A 1 4421 ? 194.587 182.231 161.420 1.00 65.12  ? 4421 ALA A C     1 
ATOM   21199 O  O     . ALA A 1 4421 ? 194.796 182.062 162.628 1.00 66.49  ? 4421 ALA A O     1 
ATOM   21200 C  CB    . ALA A 1 4421 ? 196.354 183.359 160.041 1.00 71.38  ? 4421 ALA A CB    1 
ATOM   21201 N  N     . LYS A 1 4422 ? 193.393 182.600 160.949 1.00 60.13  ? 4422 LYS A N     1 
ATOM   21202 C  CA    . LYS A 1 4422 ? 192.265 182.760 161.862 1.00 60.24  ? 4422 LYS A CA    1 
ATOM   21203 C  C     . LYS A 1 4422 ? 191.923 181.439 162.543 1.00 65.85  ? 4422 LYS A C     1 
ATOM   21204 O  O     . LYS A 1 4422 ? 191.744 181.381 163.769 1.00 64.42  ? 4422 LYS A O     1 
ATOM   21205 C  CB    . LYS A 1 4422 ? 191.056 183.312 161.107 1.00 52.82  ? 4422 LYS A CB    1 
ATOM   21206 C  CG    . LYS A 1 4422 ? 189.716 182.967 161.734 1.00 56.58  ? 4422 LYS A CG    1 
ATOM   21207 C  CD    . LYS A 1 4422 ? 188.669 184.019 161.406 1.00 60.02  ? 4422 LYS A CD    1 
ATOM   21208 C  CE    . LYS A 1 4422 ? 187.415 183.830 162.243 1.00 68.13  ? 4422 LYS A CE    1 
ATOM   21209 N  NZ    . LYS A 1 4422 ? 186.220 184.442 161.599 1.00 56.40  ? 4422 LYS A NZ    1 
ATOM   21210 N  N     . LEU A 1 4423 ? 191.849 180.357 161.763 1.00 66.51  ? 4423 LEU A N     1 
ATOM   21211 C  CA    . LEU A 1 4423 ? 191.556 179.053 162.347 1.00 57.53  ? 4423 LEU A CA    1 
ATOM   21212 C  C     . LEU A 1 4423 ? 192.660 178.621 163.305 1.00 54.37  ? 4423 LEU A C     1 
ATOM   21213 O  O     . LEU A 1 4423 ? 192.383 178.045 164.363 1.00 62.00  ? 4423 LEU A O     1 
ATOM   21214 C  CB    . LEU A 1 4423 ? 191.359 178.014 161.244 1.00 54.20  ? 4423 LEU A CB    1 
ATOM   21215 C  CG    . LEU A 1 4423 ? 190.793 176.661 161.679 1.00 57.57  ? 4423 LEU A CG    1 
ATOM   21216 C  CD1   . LEU A 1 4423 ? 189.675 176.843 162.694 1.00 55.72  ? 4423 LEU A CD1   1 
ATOM   21217 C  CD2   . LEU A 1 4423 ? 190.302 175.875 160.475 1.00 59.27  ? 4423 LEU A CD2   1 
ATOM   21218 N  N     . LEU A 1 4424 ? 193.917 178.897 162.952 1.00 54.54  ? 4424 LEU A N     1 
ATOM   21219 C  CA    . LEU A 1 4424 ? 195.040 178.531 163.805 1.00 56.32  ? 4424 LEU A CA    1 
ATOM   21220 C  C     . LEU A 1 4424 ? 194.972 179.250 165.145 1.00 64.46  ? 4424 LEU A C     1 
ATOM   21221 O  O     . LEU A 1 4424 ? 195.146 178.632 166.201 1.00 66.52  ? 4424 LEU A O     1 
ATOM   21222 C  CB    . LEU A 1 4424 ? 196.355 178.850 163.093 1.00 55.73  ? 4424 LEU A CB    1 
ATOM   21223 C  CG    . LEU A 1 4424 ? 197.644 178.706 163.903 1.00 58.28  ? 4424 LEU A CG    1 
ATOM   21224 C  CD1   . LEU A 1 4424 ? 197.721 177.341 164.554 1.00 59.07  ? 4424 LEU A CD1   1 
ATOM   21225 C  CD2   . LEU A 1 4424 ? 198.861 178.951 163.029 1.00 60.77  ? 4424 LEU A CD2   1 
ATOM   21226 N  N     . GLN A 1 4425 ? 194.723 180.562 165.123 1.00 67.42  ? 4425 GLN A N     1 
ATOM   21227 C  CA    . GLN A 1 4425 ? 194.668 181.301 166.379 1.00 66.61  ? 4425 GLN A CA    1 
ATOM   21228 C  C     . GLN A 1 4425 ? 193.473 180.864 167.216 1.00 64.62  ? 4425 GLN A C     1 
ATOM   21229 O  O     . GLN A 1 4425 ? 193.582 180.744 168.442 1.00 65.48  ? 4425 GLN A O     1 
ATOM   21230 C  CB    . GLN A 1 4425 ? 194.645 182.812 166.123 1.00 67.04  ? 4425 GLN A CB    1 
ATOM   21231 C  CG    . GLN A 1 4425 ? 193.407 183.347 165.430 1.00 68.70  ? 4425 GLN A CG    1 
ATOM   21232 C  CD    . GLN A 1 4425 ? 193.486 184.839 165.167 1.00 80.11  ? 4425 GLN A CD    1 
ATOM   21233 O  OE1   . GLN A 1 4425 ? 194.457 185.496 165.543 1.00 88.01  ? 4425 GLN A OE1   1 
ATOM   21234 N  NE2   . GLN A 1 4425 ? 192.461 185.381 164.521 1.00 83.50  ? 4425 GLN A NE2   1 
ATOM   21235 N  N     . ASP A 1 4426 ? 192.333 180.587 166.574 1.00 62.79  ? 4426 ASP A N     1 
ATOM   21236 C  CA    . ASP A 1 4426 ? 191.171 180.115 167.324 1.00 61.21  ? 4426 ASP A CA    1 
ATOM   21237 C  C     . ASP A 1 4426 ? 191.449 178.767 167.983 1.00 58.44  ? 4426 ASP A C     1 
ATOM   21238 O  O     . ASP A 1 4426 ? 191.148 178.566 169.167 1.00 63.25  ? 4426 ASP A O     1 
ATOM   21239 C  CB    . ASP A 1 4426 ? 189.955 180.027 166.402 1.00 67.68  ? 4426 ASP A CB    1 
ATOM   21240 C  CG    . ASP A 1 4426 ? 189.295 181.373 166.181 1.00 71.97  ? 4426 ASP A CG    1 
ATOM   21241 O  OD1   . ASP A 1 4426 ? 189.387 182.235 167.079 1.00 65.96  ? 4426 ASP A OD1   1 
ATOM   21242 O  OD2   . ASP A 1 4426 ? 188.685 181.569 165.109 1.00 78.75  ? 4426 ASP A OD2   1 
ATOM   21243 N  N     . VAL A 1 4427 ? 192.039 177.834 167.231 1.00 56.39  ? 4427 VAL A N     1 
ATOM   21244 C  CA    . VAL A 1 4427 ? 192.322 176.506 167.770 1.00 50.88  ? 4427 VAL A CA    1 
ATOM   21245 C  C     . VAL A 1 4427 ? 193.344 176.591 168.895 1.00 58.49  ? 4427 VAL A C     1 
ATOM   21246 O  O     . VAL A 1 4427 ? 193.205 175.927 169.930 1.00 64.36  ? 4427 VAL A O     1 
ATOM   21247 C  CB    . VAL A 1 4427 ? 192.791 175.563 166.645 1.00 46.59  ? 4427 VAL A CB    1 
ATOM   21248 C  CG1   . VAL A 1 4427 ? 193.402 174.298 167.226 1.00 47.38  ? 4427 VAL A CG1   1 
ATOM   21249 C  CG2   . VAL A 1 4427 ? 191.630 175.219 165.726 1.00 53.68  ? 4427 VAL A CG2   1 
ATOM   21250 N  N     . ARG A 1 4428 ? 194.389 177.402 168.714 1.00 59.82  ? 4428 ARG A N     1 
ATOM   21251 C  CA    . ARG A 1 4428 ? 195.409 177.527 169.748 1.00 59.76  ? 4428 ARG A CA    1 
ATOM   21252 C  C     . ARG A 1 4428 ? 194.848 178.177 171.006 1.00 65.51  ? 4428 ARG A C     1 
ATOM   21253 O  O     . ARG A 1 4428 ? 195.193 177.772 172.121 1.00 67.19  ? 4428 ARG A O     1 
ATOM   21254 C  CB    . ARG A 1 4428 ? 196.604 178.315 169.215 1.00 63.24  ? 4428 ARG A CB    1 
ATOM   21255 C  CG    . ARG A 1 4428 ? 197.477 177.517 168.262 1.00 63.12  ? 4428 ARG A CG    1 
ATOM   21256 C  CD    . ARG A 1 4428 ? 198.862 178.122 168.138 1.00 66.26  ? 4428 ARG A CD    1 
ATOM   21257 N  NE    . ARG A 1 4428 ? 199.695 177.833 169.298 1.00 71.27  ? 4428 ARG A NE    1 
ATOM   21258 C  CZ    . ARG A 1 4428 ? 200.360 176.700 169.481 1.00 73.62  ? 4428 ARG A CZ    1 
ATOM   21259 N  NH1   . ARG A 1 4428 ? 200.311 175.720 168.594 1.00 71.98  ? 4428 ARG A NH1   1 
ATOM   21260 N  NH2   . ARG A 1 4428 ? 201.092 176.547 170.580 1.00 76.42  ? 4428 ARG A NH2   1 
ATOM   21261 N  N     . GLN A 1 4429 ? 193.980 179.182 170.853 1.00 65.94  ? 4429 GLN A N     1 
ATOM   21262 C  CA    . GLN A 1 4429 ? 193.340 179.781 172.019 1.00 65.76  ? 4429 GLN A CA    1 
ATOM   21263 C  C     . GLN A 1 4429 ? 192.464 178.768 172.746 1.00 66.53  ? 4429 GLN A C     1 
ATOM   21264 O  O     . GLN A 1 4429 ? 192.479 178.697 173.981 1.00 72.01  ? 4429 GLN A O     1 
ATOM   21265 C  CB    . GLN A 1 4429 ? 192.517 180.998 171.597 1.00 64.08  ? 4429 GLN A CB    1 
ATOM   21266 C  CG    . GLN A 1 4429 ? 192.150 181.928 172.741 1.00 73.47  ? 4429 GLN A CG    1 
ATOM   21267 C  CD    . GLN A 1 4429 ? 193.354 182.349 173.559 1.00 80.35  ? 4429 GLN A CD    1 
ATOM   21268 O  OE1   . GLN A 1 4429 ? 193.381 182.180 174.778 1.00 80.08  ? 4429 GLN A OE1   1 
ATOM   21269 N  NE2   . GLN A 1 4429 ? 194.358 182.904 172.891 1.00 85.65  ? 4429 GLN A NE2   1 
ATOM   21270 N  N     . ASP A 1 4430 ? 191.698 177.972 171.995 1.00 58.26  ? 4430 ASP A N     1 
ATOM   21271 C  CA    . ASP A 1 4430 ? 190.857 176.958 172.624 1.00 54.76  ? 4430 ASP A CA    1 
ATOM   21272 C  C     . ASP A 1 4430 ? 191.698 175.931 173.373 1.00 62.49  ? 4430 ASP A C     1 
ATOM   21273 O  O     . ASP A 1 4430 ? 191.362 175.542 174.498 1.00 72.74  ? 4430 ASP A O     1 
ATOM   21274 C  CB    . ASP A 1 4430 ? 189.984 176.275 171.572 1.00 59.99  ? 4430 ASP A CB    1 
ATOM   21275 C  CG    . ASP A 1 4430 ? 188.925 177.199 171.007 1.00 67.74  ? 4430 ASP A CG    1 
ATOM   21276 O  OD1   . ASP A 1 4430 ? 188.873 178.373 171.429 1.00 69.78  ? 4430 ASP A OD1   1 
ATOM   21277 O  OD2   . ASP A 1 4430 ? 188.144 176.752 170.141 1.00 70.55  ? 4430 ASP A OD2   1 
ATOM   21278 N  N     . LEU A 1 4431 ? 192.802 175.487 172.769 1.00 62.48  ? 4431 LEU A N     1 
ATOM   21279 C  CA    . LEU A 1 4431 ? 193.667 174.515 173.431 1.00 65.60  ? 4431 LEU A CA    1 
ATOM   21280 C  C     . LEU A 1 4431 ? 194.330 175.112 174.668 1.00 71.23  ? 4431 LEU A C     1 
ATOM   21281 O  O     . LEU A 1 4431 ? 194.486 174.426 175.684 1.00 69.28  ? 4431 LEU A O     1 
ATOM   21282 C  CB    . LEU A 1 4431 ? 194.718 173.991 172.454 1.00 65.62  ? 4431 LEU A CB    1 
ATOM   21283 C  CG    . LEU A 1 4431 ? 194.196 173.151 171.287 1.00 61.72  ? 4431 LEU A CG    1 
ATOM   21284 C  CD1   . LEU A 1 4431 ? 195.324 172.808 170.328 1.00 64.94  ? 4431 LEU A CD1   1 
ATOM   21285 C  CD2   . LEU A 1 4431 ? 193.516 171.889 171.795 1.00 56.51  ? 4431 LEU A CD2   1 
ATOM   21286 N  N     . ALA A 1 4432 ? 194.736 176.382 174.600 1.00 72.02  ? 4432 ALA A N     1 
ATOM   21287 C  CA    . ALA A 1 4432 ? 195.318 177.035 175.768 1.00 71.16  ? 4432 ALA A CA    1 
ATOM   21288 C  C     . ALA A 1 4432 ? 194.309 177.131 176.904 1.00 75.24  ? 4432 ALA A C     1 
ATOM   21289 O  O     . ALA A 1 4432 ? 194.648 176.885 178.067 1.00 78.43  ? 4432 ALA A O     1 
ATOM   21290 C  CB    . ALA A 1 4432 ? 195.839 178.421 175.391 1.00 63.50  ? 4432 ALA A CB    1 
ATOM   21291 N  N     . ASP A 1 4433 ? 193.062 177.488 176.586 1.00 70.88  ? 4433 ASP A N     1 
ATOM   21292 C  CA    . ASP A 1 4433 ? 192.023 177.525 177.612 1.00 66.87  ? 4433 ASP A CA    1 
ATOM   21293 C  C     . ASP A 1 4433 ? 191.764 176.137 178.187 1.00 66.72  ? 4433 ASP A C     1 
ATOM   21294 O  O     . ASP A 1 4433 ? 191.528 175.990 179.392 1.00 71.18  ? 4433 ASP A O     1 
ATOM   21295 C  CB    . ASP A 1 4433 ? 190.737 178.123 177.043 1.00 68.40  ? 4433 ASP A CB    1 
ATOM   21296 C  CG    . ASP A 1 4433 ? 190.952 179.494 176.436 1.00 80.72  ? 4433 ASP A CG    1 
ATOM   21297 O  OD1   . ASP A 1 4433 ? 189.972 180.083 175.932 1.00 85.16  ? 4433 ASP A OD1   1 
ATOM   21298 O  OD2   . ASP A 1 4433 ? 192.099 179.987 176.468 1.00 77.25  ? 4433 ASP A OD2   1 
ATOM   21299 N  N     . VAL A 1 4434 ? 191.800 175.106 177.339 1.00 64.91  ? 4434 VAL A N     1 
ATOM   21300 C  CA    . VAL A 1 4434 ? 191.623 173.738 177.822 1.00 64.61  ? 4434 VAL A CA    1 
ATOM   21301 C  C     . VAL A 1 4434 ? 192.742 173.364 178.786 1.00 75.69  ? 4434 VAL A C     1 
ATOM   21302 O  O     . VAL A 1 4434 ? 192.501 172.756 179.835 1.00 78.87  ? 4434 VAL A O     1 
ATOM   21303 C  CB    . VAL A 1 4434 ? 191.541 172.759 176.636 1.00 66.04  ? 4434 VAL A CB    1 
ATOM   21304 C  CG1   . VAL A 1 4434 ? 191.811 171.334 177.094 1.00 69.88  ? 4434 VAL A CG1   1 
ATOM   21305 C  CG2   . VAL A 1 4434 ? 190.181 172.853 175.969 1.00 63.21  ? 4434 VAL A CG2   1 
ATOM   21306 N  N     . VAL A 1 4435 ? 193.983 173.721 178.447 1.00 79.27  ? 4435 VAL A N     1 
ATOM   21307 C  CA    . VAL A 1 4435 ? 195.113 173.434 179.330 1.00 81.71  ? 4435 VAL A CA    1 
ATOM   21308 C  C     . VAL A 1 4435 ? 194.954 174.173 180.653 1.00 84.21  ? 4435 VAL A C     1 
ATOM   21309 O  O     . VAL A 1 4435 ? 195.190 173.613 181.731 1.00 85.23  ? 4435 VAL A O     1 
ATOM   21310 C  CB    . VAL A 1 4435 ? 196.443 173.791 178.642 1.00 80.04  ? 4435 VAL A CB    1 
ATOM   21311 C  CG1   . VAL A 1 4435 ? 197.602 173.619 179.610 1.00 83.52  ? 4435 VAL A CG1   1 
ATOM   21312 C  CG2   . VAL A 1 4435 ? 196.656 172.923 177.419 1.00 80.62  ? 4435 VAL A CG2   1 
ATOM   21313 N  N     . GLN A 1 4436 ? 194.552 175.445 180.591 1.00 83.47  ? 4436 GLN A N     1 
ATOM   21314 C  CA    . GLN A 1 4436 ? 194.379 176.228 181.812 1.00 78.76  ? 4436 GLN A CA    1 
ATOM   21315 C  C     . GLN A 1 4436 ? 193.292 175.635 182.701 1.00 81.19  ? 4436 GLN A C     1 
ATOM   21316 O  O     . GLN A 1 4436 ? 193.442 175.588 183.927 1.00 84.91  ? 4436 GLN A O     1 
ATOM   21317 C  CB    . GLN A 1 4436 ? 194.058 177.682 181.467 1.00 76.27  ? 4436 GLN A CB    1 
ATOM   21318 C  CG    . GLN A 1 4436 ? 195.190 178.425 180.773 1.00 80.14  ? 4436 GLN A CG    1 
ATOM   21319 C  CD    . GLN A 1 4436 ? 196.372 178.684 181.687 1.00 94.55  ? 4436 GLN A CD    1 
ATOM   21320 O  OE1   . GLN A 1 4436 ? 196.259 178.600 182.909 1.00 104.45 ? 4436 GLN A OE1   1 
ATOM   21321 N  NE2   . GLN A 1 4436 ? 197.518 179.000 181.094 1.00 86.51  ? 4436 GLN A NE2   1 
ATOM   21322 N  N     . VAL A 1 4437 ? 192.186 175.186 182.102 1.00 79.33  ? 4437 VAL A N     1 
ATOM   21323 C  CA    . VAL A 1 4437 ? 191.138 174.528 182.879 1.00 78.08  ? 4437 VAL A CA    1 
ATOM   21324 C  C     . VAL A 1 4437 ? 191.671 173.244 183.500 1.00 84.32  ? 4437 VAL A C     1 
ATOM   21325 O  O     . VAL A 1 4437 ? 191.453 172.966 184.685 1.00 90.90  ? 4437 VAL A O     1 
ATOM   21326 C  CB    . VAL A 1 4437 ? 189.905 174.255 181.999 1.00 70.38  ? 4437 VAL A CB    1 
ATOM   21327 C  CG1   . VAL A 1 4437 ? 189.020 173.199 182.642 1.00 68.01  ? 4437 VAL A CG1   1 
ATOM   21328 C  CG2   . VAL A 1 4437 ? 189.125 175.533 181.767 1.00 68.73  ? 4437 VAL A CG2   1 
ATOM   21329 N  N     . CYS A 1 4438 ? 192.390 172.447 182.708 1.00 84.52  ? 4438 CYS A N     1 
ATOM   21330 C  CA    . CYS A 1 4438 ? 192.950 171.194 183.195 1.00 90.22  ? 4438 CYS A CA    1 
ATOM   21331 C  C     . CYS A 1 4438 ? 194.066 171.402 184.208 1.00 93.43  ? 4438 CYS A C     1 
ATOM   21332 O  O     . CYS A 1 4438 ? 194.419 170.455 184.918 1.00 87.25  ? 4438 CYS A O     1 
ATOM   21333 C  CB    . CYS A 1 4438 ? 193.458 170.361 182.020 1.00 92.43  ? 4438 CYS A CB    1 
ATOM   21334 S  SG    . CYS A 1 4438 ? 192.153 169.701 180.958 1.00 105.05 ? 4438 CYS A SG    1 
ATOM   21335 N  N     . GLU A 1 4439 ? 194.626 172.606 184.291 1.00 95.66  ? 4439 GLU A N     1 
ATOM   21336 C  CA    . GLU A 1 4439 ? 195.609 172.944 185.309 1.00 90.76  ? 4439 GLU A CA    1 
ATOM   21337 C  C     . GLU A 1 4439 ? 194.969 173.444 186.597 1.00 94.60  ? 4439 GLU A C     1 
ATOM   21338 O  O     . GLU A 1 4439 ? 195.687 173.707 187.567 1.00 100.32 ? 4439 GLU A O     1 
ATOM   21339 C  CB    . GLU A 1 4439 ? 196.579 174.003 184.774 1.00 91.15  ? 4439 GLU A CB    1 
ATOM   21340 C  CG    . GLU A 1 4439 ? 197.800 173.432 184.074 1.00 93.26  ? 4439 GLU A CG    1 
ATOM   21341 C  CD    . GLU A 1 4439 ? 198.801 174.503 183.688 1.00 101.87 ? 4439 GLU A CD    1 
ATOM   21342 O  OE1   . GLU A 1 4439 ? 199.438 175.077 184.596 1.00 108.22 ? 4439 GLU A OE1   1 
ATOM   21343 O  OE2   . GLU A 1 4439 ? 198.950 174.772 182.478 1.00 92.01  ? 4439 GLU A OE2   1 
ATOM   21344 N  N     . GLY A 1 4440 ? 193.646 173.580 186.629 1.00 92.99  ? 4440 GLY A N     1 
ATOM   21345 C  CA    . GLY A 1 4440 ? 192.973 174.077 187.813 1.00 89.77  ? 4440 GLY A CA    1 
ATOM   21346 C  C     . GLY A 1 4440 ? 193.167 175.554 188.065 1.00 94.81  ? 4440 GLY A C     1 
ATOM   21347 O  O     . GLY A 1 4440 ? 193.059 175.999 189.212 1.00 100.53 ? 4440 GLY A O     1 
ATOM   21348 N  N     . LYS A 1 4441 ? 193.451 176.332 187.021 1.00 94.13  ? 4441 LYS A N     1 
ATOM   21349 C  CA    . LYS A 1 4441 ? 193.734 177.755 187.160 1.00 97.20  ? 4441 LYS A CA    1 
ATOM   21350 C  C     . LYS A 1 4441 ? 192.541 178.635 186.807 1.00 93.64  ? 4441 LYS A C     1 
ATOM   21351 O  O     . LYS A 1 4441 ? 192.165 179.510 187.593 1.00 97.66  ? 4441 LYS A O     1 
ATOM   21352 C  CB    . LYS A 1 4441 ? 194.940 178.135 186.293 1.00 96.84  ? 4441 LYS A CB    1 
ATOM   21353 C  CG    . LYS A 1 4441 ? 196.274 177.698 186.875 1.00 95.98  ? 4441 LYS A CG    1 
ATOM   21354 C  CD    . LYS A 1 4441 ? 197.433 178.133 185.997 1.00 104.00 ? 4441 LYS A CD    1 
ATOM   21355 C  CE    . LYS A 1 4441 ? 198.760 177.663 186.570 1.00 112.29 ? 4441 LYS A CE    1 
ATOM   21356 N  NZ    . LYS A 1 4441 ? 199.884 177.866 185.615 1.00 121.55 ? 4441 LYS A NZ    1 
ATOM   21357 N  N     . LYS A 1 4442 ? 191.934 178.425 185.643 1.00 86.12  ? 4442 LYS A N     1 
ATOM   21358 C  CA    . LYS A 1 4442 ? 190.809 179.235 185.201 1.00 83.10  ? 4442 LYS A CA    1 
ATOM   21359 C  C     . LYS A 1 4442 ? 189.504 178.460 185.343 1.00 74.03  ? 4442 LYS A C     1 
ATOM   21360 O  O     . LYS A 1 4442 ? 189.480 177.227 185.303 1.00 70.29  ? 4442 LYS A O     1 
ATOM   21361 C  CB    . LYS A 1 4442 ? 190.998 179.693 183.752 1.00 81.05  ? 4442 LYS A CB    1 
ATOM   21362 C  CG    . LYS A 1 4442 ? 190.563 178.683 182.707 1.00 76.98  ? 4442 LYS A CG    1 
ATOM   21363 C  CD    . LYS A 1 4442 ? 190.717 179.242 181.302 1.00 75.41  ? 4442 LYS A CD    1 
ATOM   21364 C  CE    . LYS A 1 4442 ? 189.797 180.431 181.077 1.00 73.96  ? 4442 LYS A CE    1 
ATOM   21365 N  NZ    . LYS A 1 4442 ? 189.933 180.988 179.703 1.00 71.89  ? 4442 LYS A NZ    1 
ATOM   21366 N  N     . LYS A 1 4443 ? 188.416 179.203 185.523 1.00 75.27  ? 4443 LYS A N     1 
ATOM   21367 C  CA    . LYS A 1 4443 ? 187.107 178.603 185.728 1.00 75.36  ? 4443 LYS A CA    1 
ATOM   21368 C  C     . LYS A 1 4443 ? 186.534 178.089 184.412 1.00 72.89  ? 4443 LYS A C     1 
ATOM   21369 O  O     . LYS A 1 4443 ? 186.782 178.646 183.339 1.00 71.14  ? 4443 LYS A O     1 
ATOM   21370 C  CB    . LYS A 1 4443 ? 186.148 179.614 186.359 1.00 77.58  ? 4443 LYS A CB    1 
ATOM   21371 C  CG    . LYS A 1 4443 ? 185.008 178.985 187.143 1.00 82.75  ? 4443 LYS A CG    1 
ATOM   21372 C  CD    . LYS A 1 4443 ? 183.749 179.832 187.068 1.00 87.22  ? 4443 LYS A CD    1 
ATOM   21373 C  CE    . LYS A 1 4443 ? 182.702 179.353 188.062 1.00 99.54  ? 4443 LYS A CE    1 
ATOM   21374 N  NZ    . LYS A 1 4443 ? 182.524 177.876 188.014 1.00 89.60  ? 4443 LYS A NZ    1 
ATOM   21375 N  N     . GLN A 1 4444 ? 185.759 177.012 184.507 1.00 67.59  ? 4444 GLN A N     1 
ATOM   21376 C  CA    . GLN A 1 4444 ? 185.163 176.393 183.332 1.00 68.03  ? 4444 GLN A CA    1 
ATOM   21377 C  C     . GLN A 1 4444 ? 183.866 177.102 182.962 1.00 68.05  ? 4444 GLN A C     1 
ATOM   21378 O  O     . GLN A 1 4444 ? 182.968 177.248 183.796 1.00 66.12  ? 4444 GLN A O     1 
ATOM   21379 C  CB    . GLN A 1 4444 ? 184.904 174.910 183.592 1.00 68.88  ? 4444 GLN A CB    1 
ATOM   21380 C  CG    . GLN A 1 4444 ? 184.604 174.097 182.346 1.00 63.71  ? 4444 GLN A CG    1 
ATOM   21381 C  CD    . GLN A 1 4444 ? 184.530 172.610 182.629 1.00 71.82  ? 4444 GLN A CD    1 
ATOM   21382 O  OE1   . GLN A 1 4444 ? 185.251 171.814 182.028 1.00 70.69  ? 4444 GLN A OE1   1 
ATOM   21383 N  NE2   . GLN A 1 4444 ? 183.656 172.227 183.553 1.00 77.02  ? 4444 GLN A NE2   1 
ATOM   21384 N  N     . THR A 1 4445 ? 183.772 177.541 181.709 1.00 62.66  ? 4445 THR A N     1 
ATOM   21385 C  CA    . THR A 1 4445 ? 182.602 178.244 181.208 1.00 48.44  ? 4445 THR A CA    1 
ATOM   21386 C  C     . THR A 1 4445 ? 181.734 177.296 180.383 1.00 48.25  ? 4445 THR A C     1 
ATOM   21387 O  O     . THR A 1 4445 ? 182.035 176.111 180.227 1.00 56.20  ? 4445 THR A O     1 
ATOM   21388 C  CB    . THR A 1 4445 ? 183.023 179.463 180.383 1.00 40.12  ? 4445 THR A CB    1 
ATOM   21389 O  OG1   . THR A 1 4445 ? 183.816 179.038 179.269 1.00 42.82  ? 4445 THR A OG1   1 
ATOM   21390 C  CG2   . THR A 1 4445 ? 183.838 180.422 181.235 1.00 42.24  ? 4445 THR A CG2   1 
ATOM   21391 N  N     . ASN A 1 4446 ? 180.633 177.832 179.851 1.00 43.19  ? 4446 ASN A N     1 
ATOM   21392 C  CA    . ASN A 1 4446 ? 179.721 177.020 179.049 1.00 40.84  ? 4446 ASN A CA    1 
ATOM   21393 C  C     . ASN A 1 4446 ? 180.381 176.569 177.751 1.00 46.20  ? 4446 ASN A C     1 
ATOM   21394 O  O     . ASN A 1 4446 ? 180.344 175.382 177.401 1.00 52.49  ? 4446 ASN A O     1 
ATOM   21395 C  CB    . ASN A 1 4446 ? 178.442 177.806 178.758 1.00 35.95  ? 4446 ASN A CB    1 
ATOM   21396 C  CG    . ASN A 1 4446 ? 177.407 177.661 179.855 1.00 34.99  ? 4446 ASN A CG    1 
ATOM   21397 O  OD1   . ASN A 1 4446 ? 177.129 176.556 180.319 1.00 38.86  ? 4446 ASN A OD1   1 
ATOM   21398 N  ND2   . ASN A 1 4446 ? 176.830 178.780 180.275 1.00 25.12  ? 4446 ASN A ND2   1 
ATOM   21399 N  N     . TYR A 1 4447 ? 180.992 177.508 177.022 1.00 48.47  ? 4447 TYR A N     1 
ATOM   21400 C  CA    . TYR A 1 4447 ? 181.722 177.142 175.814 1.00 53.89  ? 4447 TYR A CA    1 
ATOM   21401 C  C     . TYR A 1 4447 ? 182.884 176.217 176.140 1.00 51.36  ? 4447 TYR A C     1 
ATOM   21402 O  O     . TYR A 1 4447 ? 183.148 175.257 175.407 1.00 52.99  ? 4447 TYR A O     1 
ATOM   21403 C  CB    . TYR A 1 4447 ? 182.225 178.394 175.097 1.00 59.44  ? 4447 TYR A CB    1 
ATOM   21404 C  CG    . TYR A 1 4447 ? 183.149 178.089 173.941 1.00 61.52  ? 4447 TYR A CG    1 
ATOM   21405 C  CD1   . TYR A 1 4447 ? 182.667 177.507 172.776 1.00 66.23  ? 4447 TYR A CD1   1 
ATOM   21406 C  CD2   . TYR A 1 4447 ? 184.506 178.374 174.017 1.00 58.66  ? 4447 TYR A CD2   1 
ATOM   21407 C  CE1   . TYR A 1 4447 ? 183.510 177.223 171.718 1.00 69.93  ? 4447 TYR A CE1   1 
ATOM   21408 C  CE2   . TYR A 1 4447 ? 185.356 178.093 172.965 1.00 63.47  ? 4447 TYR A CE2   1 
ATOM   21409 C  CZ    . TYR A 1 4447 ? 184.852 177.518 171.818 1.00 70.06  ? 4447 TYR A CZ    1 
ATOM   21410 O  OH    . TYR A 1 4447 ? 185.694 177.237 170.767 1.00 74.06  ? 4447 TYR A OH    1 
ATOM   21411 N  N     . LEU A 1 4448 ? 183.595 176.496 177.234 1.00 51.61  ? 4448 LEU A N     1 
ATOM   21412 C  CA    . LEU A 1 4448 ? 184.670 175.609 177.659 1.00 52.80  ? 4448 LEU A CA    1 
ATOM   21413 C  C     . LEU A 1 4448 ? 184.131 174.232 178.022 1.00 56.66  ? 4448 LEU A C     1 
ATOM   21414 O  O     . LEU A 1 4448 ? 184.755 173.215 177.705 1.00 62.25  ? 4448 LEU A O     1 
ATOM   21415 C  CB    . LEU A 1 4448 ? 185.426 176.225 178.834 1.00 53.49  ? 4448 LEU A CB    1 
ATOM   21416 C  CG    . LEU A 1 4448 ? 186.552 177.176 178.427 1.00 58.54  ? 4448 LEU A CG    1 
ATOM   21417 C  CD1   . LEU A 1 4448 ? 187.230 177.773 179.647 1.00 62.20  ? 4448 LEU A CD1   1 
ATOM   21418 C  CD2   . LEU A 1 4448 ? 187.557 176.450 177.549 1.00 51.67  ? 4448 LEU A CD2   1 
ATOM   21419 N  N     . ARG A 1 4449 ? 182.970 174.179 178.679 1.00 56.75  ? 4449 ARG A N     1 
ATOM   21420 C  CA    . ARG A 1 4449 ? 182.356 172.893 178.997 1.00 52.53  ? 4449 ARG A CA    1 
ATOM   21421 C  C     . ARG A 1 4449 ? 182.070 172.095 177.732 1.00 53.78  ? 4449 ARG A C     1 
ATOM   21422 O  O     . ARG A 1 4449 ? 182.418 170.911 177.638 1.00 58.99  ? 4449 ARG A O     1 
ATOM   21423 C  CB    . ARG A 1 4449 ? 181.066 173.106 179.792 1.00 52.63  ? 4449 ARG A CB    1 
ATOM   21424 C  CG    . ARG A 1 4449 ? 181.240 173.080 181.300 1.00 54.65  ? 4449 ARG A CG    1 
ATOM   21425 C  CD    . ARG A 1 4449 ? 179.891 173.108 182.003 1.00 50.28  ? 4449 ARG A CD    1 
ATOM   21426 N  NE    . ARG A 1 4449 ? 179.344 174.456 182.092 1.00 48.96  ? 4449 ARG A NE    1 
ATOM   21427 C  CZ    . ARG A 1 4449 ? 179.760 175.382 182.947 1.00 53.40  ? 4449 ARG A CZ    1 
ATOM   21428 N  NH1   . ARG A 1 4449 ? 180.724 175.135 183.819 1.00 63.10  ? 4449 ARG A NH1   1 
ATOM   21429 N  NH2   . ARG A 1 4449 ? 179.193 176.584 182.928 1.00 43.95  ? 4449 ARG A NH2   1 
ATOM   21430 N  N     . THR A 1 4450 ? 181.439 172.732 176.743 1.00 59.70  ? 4450 THR A N     1 
ATOM   21431 C  CA    . THR A 1 4450 ? 181.099 172.032 175.506 1.00 61.56  ? 4450 THR A CA    1 
ATOM   21432 C  C     . THR A 1 4450 ? 182.352 171.576 174.767 1.00 60.05  ? 4450 THR A C     1 
ATOM   21433 O  O     . THR A 1 4450 ? 182.433 170.433 174.297 1.00 60.76  ? 4450 THR A O     1 
ATOM   21434 C  CB    . THR A 1 4450 ? 180.246 172.933 174.613 1.00 55.08  ? 4450 THR A CB    1 
ATOM   21435 O  OG1   . THR A 1 4450 ? 179.109 173.400 175.349 1.00 58.17  ? 4450 THR A OG1   1 
ATOM   21436 C  CG2   . THR A 1 4450 ? 179.770 172.171 173.386 1.00 53.08  ? 4450 THR A CG2   1 
ATOM   21437 N  N     . LEU A 1 4451 ? 183.347 172.461 174.660 1.00 57.46  ? 4451 LEU A N     1 
ATOM   21438 C  CA    . LEU A 1 4451 ? 184.574 172.122 173.947 1.00 55.50  ? 4451 LEU A CA    1 
ATOM   21439 C  C     . LEU A 1 4451 ? 185.319 170.987 174.637 1.00 55.91  ? 4451 LEU A C     1 
ATOM   21440 O  O     . LEU A 1 4451 ? 185.829 170.076 173.975 1.00 64.88  ? 4451 LEU A O     1 
ATOM   21441 C  CB    . LEU A 1 4451 ? 185.460 173.362 173.827 1.00 59.43  ? 4451 LEU A CB    1 
ATOM   21442 C  CG    . LEU A 1 4451 ? 186.934 173.161 173.480 1.00 55.07  ? 4451 LEU A CG    1 
ATOM   21443 C  CD1   . LEU A 1 4451 ? 187.094 172.783 172.021 1.00 55.62  ? 4451 LEU A CD1   1 
ATOM   21444 C  CD2   . LEU A 1 4451 ? 187.721 174.421 173.795 1.00 60.85  ? 4451 LEU A CD2   1 
ATOM   21445 N  N     . ILE A 1 4452 ? 185.380 171.017 175.969 1.00 54.13  ? 4452 ILE A N     1 
ATOM   21446 C  CA    . ILE A 1 4452 ? 186.070 169.970 176.711 1.00 56.55  ? 4452 ILE A CA    1 
ATOM   21447 C  C     . ILE A 1 4452 ? 185.330 168.646 176.581 1.00 59.11  ? 4452 ILE A C     1 
ATOM   21448 O  O     . ILE A 1 4452 ? 185.951 167.587 176.436 1.00 66.22  ? 4452 ILE A O     1 
ATOM   21449 C  CB    . ILE A 1 4452 ? 186.236 170.396 178.181 1.00 58.07  ? 4452 ILE A CB    1 
ATOM   21450 C  CG1   . ILE A 1 4452 ? 187.436 171.333 178.322 1.00 56.51  ? 4452 ILE A CG1   1 
ATOM   21451 C  CG2   . ILE A 1 4452 ? 186.378 169.186 179.087 1.00 59.94  ? 4452 ILE A CG2   1 
ATOM   21452 C  CD1   . ILE A 1 4452 ? 187.434 172.132 179.597 1.00 59.01  ? 4452 ILE A CD1   1 
ATOM   21453 N  N     . ASN A 1 4453 ? 183.996 168.678 176.626 1.00 58.57  ? 4453 ASN A N     1 
ATOM   21454 C  CA    . ASN A 1 4453 ? 183.225 167.453 176.443 1.00 58.66  ? 4453 ASN A CA    1 
ATOM   21455 C  C     . ASN A 1 4453 ? 183.482 166.852 175.067 1.00 62.62  ? 4453 ASN A C     1 
ATOM   21456 O  O     . ASN A 1 4453 ? 183.698 165.641 174.934 1.00 66.85  ? 4453 ASN A O     1 
ATOM   21457 C  CB    . ASN A 1 4453 ? 181.736 167.738 176.641 1.00 63.02  ? 4453 ASN A CB    1 
ATOM   21458 C  CG    . ASN A 1 4453 ? 181.348 167.825 178.103 1.00 70.30  ? 4453 ASN A CG    1 
ATOM   21459 O  OD1   . ASN A 1 4453 ? 181.991 167.226 178.965 1.00 74.95  ? 4453 ASN A OD1   1 
ATOM   21460 N  ND2   . ASN A 1 4453 ? 180.293 168.578 178.391 1.00 73.09  ? 4453 ASN A ND2   1 
ATOM   21461 N  N     . GLU A 1 4454 ? 183.479 167.694 174.029 1.00 61.81  ? 4454 GLU A N     1 
ATOM   21462 C  CA    . GLU A 1 4454 ? 183.741 167.202 172.680 1.00 61.30  ? 4454 GLU A CA    1 
ATOM   21463 C  C     . GLU A 1 4454 ? 185.150 166.634 172.559 1.00 60.84  ? 4454 GLU A C     1 
ATOM   21464 O  O     . GLU A 1 4454 ? 185.353 165.591 171.926 1.00 70.09  ? 4454 GLU A O     1 
ATOM   21465 C  CB    . GLU A 1 4454 ? 183.522 168.319 171.660 1.00 57.84  ? 4454 GLU A CB    1 
ATOM   21466 C  CG    . GLU A 1 4454 ? 182.079 168.777 171.544 1.00 62.63  ? 4454 GLU A CG    1 
ATOM   21467 C  CD    . GLU A 1 4454 ? 181.827 169.600 170.297 1.00 70.83  ? 4454 GLU A CD    1 
ATOM   21468 O  OE1   . GLU A 1 4454 ? 181.494 169.008 169.249 1.00 74.04  ? 4454 GLU A OE1   1 
ATOM   21469 O  OE2   . GLU A 1 4454 ? 181.963 170.839 170.365 1.00 75.30  ? 4454 GLU A OE2   1 
ATOM   21470 N  N     . LEU A 1 4455 ? 186.138 167.308 173.152 1.00 55.98  ? 4455 LEU A N     1 
ATOM   21471 C  CA    . LEU A 1 4455 ? 187.515 166.833 173.056 1.00 53.61  ? 4455 LEU A CA    1 
ATOM   21472 C  C     . LEU A 1 4455 ? 187.709 165.514 173.794 1.00 62.48  ? 4455 LEU A C     1 
ATOM   21473 O  O     . LEU A 1 4455 ? 188.389 164.611 173.291 1.00 68.49  ? 4455 LEU A O     1 
ATOM   21474 C  CB    . LEU A 1 4455 ? 188.474 167.895 173.592 1.00 54.64  ? 4455 LEU A CB    1 
ATOM   21475 C  CG    . LEU A 1 4455 ? 188.697 169.116 172.699 1.00 53.86  ? 4455 LEU A CG    1 
ATOM   21476 C  CD1   . LEU A 1 4455 ? 189.887 169.927 173.185 1.00 55.86  ? 4455 LEU A CD1   1 
ATOM   21477 C  CD2   . LEU A 1 4455 ? 188.890 168.694 171.250 1.00 54.42  ? 4455 LEU A CD2   1 
ATOM   21478 N  N     . VAL A 1 4456 ? 187.128 165.381 174.988 1.00 64.68  ? 4456 VAL A N     1 
ATOM   21479 C  CA    . VAL A 1 4456 ? 187.296 164.156 175.764 1.00 67.17  ? 4456 VAL A CA    1 
ATOM   21480 C  C     . VAL A 1 4456 ? 186.570 162.993 175.100 1.00 68.46  ? 4456 VAL A C     1 
ATOM   21481 O  O     . VAL A 1 4456 ? 187.128 161.900 174.949 1.00 68.74  ? 4456 VAL A O     1 
ATOM   21482 C  CB    . VAL A 1 4456 ? 186.821 164.362 177.214 1.00 62.16  ? 4456 VAL A CB    1 
ATOM   21483 C  CG1   . VAL A 1 4456 ? 186.892 163.054 177.983 1.00 57.85  ? 4456 VAL A CG1   1 
ATOM   21484 C  CG2   . VAL A 1 4456 ? 187.675 165.408 177.902 1.00 70.72  ? 4456 VAL A CG2   1 
ATOM   21485 N  N     . LYS A 1 4457 ? 185.316 163.206 174.691 1.00 67.07  ? 4457 LYS A N     1 
ATOM   21486 C  CA    . LYS A 1 4457 ? 184.546 162.095 174.143 1.00 71.31  ? 4457 LYS A CA    1 
ATOM   21487 C  C     . LYS A 1 4457 ? 185.065 161.672 172.773 1.00 73.07  ? 4457 LYS A C     1 
ATOM   21488 O  O     . LYS A 1 4457 ? 185.082 160.474 172.464 1.00 81.05  ? 4457 LYS A O     1 
ATOM   21489 C  CB    . LYS A 1 4457 ? 183.063 162.463 174.085 1.00 74.30  ? 4457 LYS A CB    1 
ATOM   21490 C  CG    . LYS A 1 4457 ? 182.222 161.544 173.216 1.00 82.71  ? 4457 LYS A CG    1 
ATOM   21491 C  CD    . LYS A 1 4457 ? 180.760 161.530 173.650 1.00 80.39  ? 4457 LYS A CD    1 
ATOM   21492 C  CE    . LYS A 1 4457 ? 180.250 162.920 174.007 1.00 81.79  ? 4457 LYS A CE    1 
ATOM   21493 N  NZ    . LYS A 1 4457 ? 180.389 163.891 172.885 1.00 82.16  ? 4457 LYS A NZ    1 
ATOM   21494 N  N     . GLY A 1 4458 ? 185.508 162.621 171.951 1.00 67.72  ? 4458 GLY A N     1 
ATOM   21495 C  CA    . GLY A 1 4458 ? 186.177 162.273 170.711 1.00 69.65  ? 4458 GLY A CA    1 
ATOM   21496 C  C     . GLY A 1 4458 ? 185.642 162.918 169.448 1.00 76.15  ? 4458 GLY A C     1 
ATOM   21497 O  O     . GLY A 1 4458 ? 186.166 162.668 168.359 1.00 79.23  ? 4458 GLY A O     1 
ATOM   21498 N  N     . ILE A 1 4459 ? 184.609 163.742 169.566 1.00 73.65  ? 4459 ILE A N     1 
ATOM   21499 C  CA    . ILE A 1 4459 ? 184.032 164.427 168.414 1.00 72.90  ? 4459 ILE A CA    1 
ATOM   21500 C  C     . ILE A 1 4459 ? 184.770 165.737 168.183 1.00 73.10  ? 4459 ILE A C     1 
ATOM   21501 O  O     . ILE A 1 4459 ? 185.048 166.488 169.126 1.00 76.22  ? 4459 ILE A O     1 
ATOM   21502 C  CB    . ILE A 1 4459 ? 182.520 164.664 168.603 1.00 70.12  ? 4459 ILE A CB    1 
ATOM   21503 C  CG1   . ILE A 1 4459 ? 181.758 163.336 168.624 1.00 79.83  ? 4459 ILE A CG1   1 
ATOM   21504 C  CG2   . ILE A 1 4459 ? 181.971 165.573 167.511 1.00 68.04  ? 4459 ILE A CG2   1 
ATOM   21505 C  CD1   . ILE A 1 4459 ? 181.599 162.731 169.987 1.00 79.83  ? 4459 ILE A CD1   1 
ATOM   21506 N  N     . LEU A 1 4460 ? 185.100 166.004 166.925 1.00 70.69  ? 4460 LEU A N     1 
ATOM   21507 C  CA    . LEU A 1 4460 ? 185.733 167.266 166.568 1.00 65.85  ? 4460 LEU A CA    1 
ATOM   21508 C  C     . LEU A 1 4460 ? 184.782 168.421 166.862 1.00 67.74  ? 4460 LEU A C     1 
ATOM   21509 O  O     . LEU A 1 4460 ? 183.611 168.368 166.469 1.00 66.77  ? 4460 LEU A O     1 
ATOM   21510 C  CB    . LEU A 1 4460 ? 186.128 167.267 165.094 1.00 60.24  ? 4460 LEU A CB    1 
ATOM   21511 C  CG    . LEU A 1 4460 ? 186.590 168.611 164.533 1.00 57.83  ? 4460 LEU A CG    1 
ATOM   21512 C  CD1   . LEU A 1 4460 ? 188.046 168.847 164.878 1.00 61.12  ? 4460 LEU A CD1   1 
ATOM   21513 C  CD2   . LEU A 1 4460 ? 186.375 168.666 163.029 1.00 51.52  ? 4460 LEU A CD2   1 
ATOM   21514 N  N     . PRO A 1 4461 ? 185.236 169.464 167.556 1.00 59.14  ? 4461 PRO A N     1 
ATOM   21515 C  CA    . PRO A 1 4461 ? 184.340 170.578 167.886 1.00 57.57  ? 4461 PRO A CA    1 
ATOM   21516 C  C     . PRO A 1 4461 ? 183.787 171.244 166.635 1.00 62.97  ? 4461 PRO A C     1 
ATOM   21517 O  O     . PRO A 1 4461 ? 184.476 171.379 165.622 1.00 66.69  ? 4461 PRO A O     1 
ATOM   21518 C  CB    . PRO A 1 4461 ? 185.239 171.532 168.681 1.00 52.78  ? 4461 PRO A CB    1 
ATOM   21519 C  CG    . PRO A 1 4461 ? 186.330 170.662 169.214 1.00 53.24  ? 4461 PRO A CG    1 
ATOM   21520 C  CD    . PRO A 1 4461 ? 186.567 169.625 168.163 1.00 54.71  ? 4461 PRO A CD    1 
ATOM   21521 N  N     . ARG A 1 4462 ? 182.522 171.662 166.718 1.00 66.09  ? 4462 ARG A N     1 
ATOM   21522 C  CA    . ARG A 1 4462 ? 181.860 172.280 165.576 1.00 76.41  ? 4462 ARG A CA    1 
ATOM   21523 C  C     . ARG A 1 4462 ? 182.434 173.649 165.242 1.00 71.30  ? 4462 ARG A C     1 
ATOM   21524 O  O     . ARG A 1 4462 ? 182.232 174.136 164.124 1.00 69.15  ? 4462 ARG A O     1 
ATOM   21525 C  CB    . ARG A 1 4462 ? 180.358 172.395 165.840 1.00 79.25  ? 4462 ARG A CB    1 
ATOM   21526 C  CG    . ARG A 1 4462 ? 179.646 171.057 165.943 1.00 79.99  ? 4462 ARG A CG    1 
ATOM   21527 C  CD    . ARG A 1 4462 ? 178.616 170.886 164.839 1.00 94.20  ? 4462 ARG A CD    1 
ATOM   21528 N  NE    . ARG A 1 4462 ? 178.269 169.485 164.634 1.00 109.70 ? 4462 ARG A NE    1 
ATOM   21529 C  CZ    . ARG A 1 4462 ? 177.910 168.964 163.468 1.00 116.88 ? 4462 ARG A CZ    1 
ATOM   21530 N  NH1   . ARG A 1 4462 ? 177.836 169.704 162.374 1.00 119.90 ? 4462 ARG A NH1   1 
ATOM   21531 N  NH2   . ARG A 1 4462 ? 177.618 167.669 163.399 1.00 119.31 ? 4462 ARG A NH2   1 
ATOM   21532 N  N     . SER A 1 4463 ? 183.140 174.281 166.179 1.00 63.98  ? 4463 SER A N     1 
ATOM   21533 C  CA    . SER A 1 4463 ? 183.748 175.580 165.927 1.00 60.96  ? 4463 SER A CA    1 
ATOM   21534 C  C     . SER A 1 4463 ? 185.110 175.476 165.254 1.00 64.10  ? 4463 SER A C     1 
ATOM   21535 O  O     . SER A 1 4463 ? 185.697 176.511 164.922 1.00 68.60  ? 4463 SER A O     1 
ATOM   21536 C  CB    . SER A 1 4463 ? 183.880 176.361 167.237 1.00 59.51  ? 4463 SER A CB    1 
ATOM   21537 O  OG    . SER A 1 4463 ? 184.724 175.683 168.151 1.00 64.93  ? 4463 SER A OG    1 
ATOM   21538 N  N     . TRP A 1 4464 ? 185.623 174.264 165.045 1.00 59.81  ? 4464 TRP A N     1 
ATOM   21539 C  CA    . TRP A 1 4464 ? 186.906 174.071 164.384 1.00 57.71  ? 4464 TRP A CA    1 
ATOM   21540 C  C     . TRP A 1 4464 ? 186.775 173.665 162.923 1.00 67.53  ? 4464 TRP A C     1 
ATOM   21541 O  O     . TRP A 1 4464 ? 187.716 173.880 162.151 1.00 73.03  ? 4464 TRP A O     1 
ATOM   21542 C  CB    . TRP A 1 4464 ? 187.733 173.010 165.120 1.00 50.17  ? 4464 TRP A CB    1 
ATOM   21543 C  CG    . TRP A 1 4464 ? 188.232 173.449 166.461 1.00 52.98  ? 4464 TRP A CG    1 
ATOM   21544 C  CD1   . TRP A 1 4464 ? 187.973 174.634 167.086 1.00 57.06  ? 4464 TRP A CD1   1 
ATOM   21545 C  CD2   . TRP A 1 4464 ? 189.082 172.708 167.344 1.00 48.94  ? 4464 TRP A CD2   1 
ATOM   21546 N  NE1   . TRP A 1 4464 ? 188.606 174.676 168.303 1.00 55.46  ? 4464 TRP A NE1   1 
ATOM   21547 C  CE2   . TRP A 1 4464 ? 189.295 173.505 168.485 1.00 49.70  ? 4464 TRP A CE2   1 
ATOM   21548 C  CE3   . TRP A 1 4464 ? 189.683 171.448 167.280 1.00 51.44  ? 4464 TRP A CE3   1 
ATOM   21549 C  CZ2   . TRP A 1 4464 ? 190.082 173.083 169.553 1.00 51.66  ? 4464 TRP A CZ2   1 
ATOM   21550 C  CZ3   . TRP A 1 4464 ? 190.465 171.031 168.341 1.00 53.00  ? 4464 TRP A CZ3   1 
ATOM   21551 C  CH2   . TRP A 1 4464 ? 190.657 171.846 169.462 1.00 52.64  ? 4464 TRP A CH2   1 
ATOM   21552 N  N     . SER A 1 4465 ? 185.640 173.090 162.527 1.00 66.89  ? 4465 SER A N     1 
ATOM   21553 C  CA    . SER A 1 4465 ? 185.437 172.620 161.157 1.00 66.65  ? 4465 SER A CA    1 
ATOM   21554 C  C     . SER A 1 4465 ? 185.051 173.809 160.280 1.00 68.36  ? 4465 SER A C     1 
ATOM   21555 O  O     . SER A 1 4465 ? 183.876 174.093 160.032 1.00 70.36  ? 4465 SER A O     1 
ATOM   21556 C  CB    . SER A 1 4465 ? 184.380 171.524 161.117 1.00 67.03  ? 4465 SER A CB    1 
ATOM   21557 O  OG    . SER A 1 4465 ? 183.076 172.076 161.075 1.00 75.38  ? 4465 SER A OG    1 
ATOM   21558 N  N     . HIS A 1 4466 ? 186.072 174.516 159.802 1.00 67.20  ? 4466 HIS A N     1 
ATOM   21559 C  CA    . HIS A 1 4466 ? 185.891 175.655 158.914 1.00 67.84  ? 4466 HIS A CA    1 
ATOM   21560 C  C     . HIS A 1 4466 ? 186.176 175.316 157.457 1.00 72.46  ? 4466 HIS A C     1 
ATOM   21561 O  O     . HIS A 1 4466 ? 186.186 176.217 156.612 1.00 74.00  ? 4466 HIS A O     1 
ATOM   21562 C  CB    . HIS A 1 4466 ? 186.775 176.821 159.362 1.00 69.26  ? 4466 HIS A CB    1 
ATOM   21563 C  CG    . HIS A 1 4466 ? 186.318 177.472 160.630 1.00 72.82  ? 4466 HIS A CG    1 
ATOM   21564 N  ND1   . HIS A 1 4466 ? 186.995 178.520 161.214 1.00 78.78  ? 4466 HIS A ND1   1 
ATOM   21565 C  CD2   . HIS A 1 4466 ? 185.250 177.224 161.424 1.00 69.30  ? 4466 HIS A CD2   1 
ATOM   21566 C  CE1   . HIS A 1 4466 ? 186.365 178.890 162.315 1.00 80.93  ? 4466 HIS A CE1   1 
ATOM   21567 N  NE2   . HIS A 1 4466 ? 185.303 178.119 162.465 1.00 75.94  ? 4466 HIS A NE2   1 
ATOM   21568 N  N     . TYR A 1 4467 ? 186.407 174.043 157.143 1.00 72.72  ? 4467 TYR A N     1 
ATOM   21569 C  CA    . TYR A 1 4467 ? 186.650 173.613 155.775 1.00 64.79  ? 4467 TYR A CA    1 
ATOM   21570 C  C     . TYR A 1 4467 ? 186.041 172.234 155.571 1.00 69.53  ? 4467 TYR A C     1 
ATOM   21571 O  O     . TYR A 1 4467 ? 185.551 171.600 156.509 1.00 74.23  ? 4467 TYR A O     1 
ATOM   21572 C  CB    . TYR A 1 4467 ? 188.148 173.603 155.439 1.00 61.17  ? 4467 TYR A CB    1 
ATOM   21573 C  CG    . TYR A 1 4467 ? 189.012 172.861 156.434 1.00 60.61  ? 4467 TYR A CG    1 
ATOM   21574 C  CD1   . TYR A 1 4467 ? 189.559 173.513 157.531 1.00 63.00  ? 4467 TYR A CD1   1 
ATOM   21575 C  CD2   . TYR A 1 4467 ? 189.287 171.510 156.273 1.00 58.51  ? 4467 TYR A CD2   1 
ATOM   21576 C  CE1   . TYR A 1 4467 ? 190.351 172.840 158.441 1.00 62.53  ? 4467 TYR A CE1   1 
ATOM   21577 C  CE2   . TYR A 1 4467 ? 190.078 170.829 157.178 1.00 61.44  ? 4467 TYR A CE2   1 
ATOM   21578 C  CZ    . TYR A 1 4467 ? 190.607 171.498 158.259 1.00 63.52  ? 4467 TYR A CZ    1 
ATOM   21579 O  OH    . TYR A 1 4467 ? 191.396 170.823 159.162 1.00 61.72  ? 4467 TYR A OH    1 
ATOM   21580 N  N     . THR A 1 4468 ? 186.070 171.780 154.319 1.00 72.20  ? 4468 THR A N     1 
ATOM   21581 C  CA    . THR A 1 4468 ? 185.505 170.482 153.969 1.00 70.82  ? 4468 THR A CA    1 
ATOM   21582 C  C     . THR A 1 4468 ? 186.201 169.365 154.735 1.00 75.06  ? 4468 THR A C     1 
ATOM   21583 O  O     . THR A 1 4468 ? 187.433 169.307 154.796 1.00 76.71  ? 4468 THR A O     1 
ATOM   21584 C  CB    . THR A 1 4468 ? 185.634 170.248 152.467 1.00 71.85  ? 4468 THR A CB    1 
ATOM   21585 O  OG1   . THR A 1 4468 ? 187.020 170.251 152.109 1.00 77.76  ? 4468 THR A OG1   1 
ATOM   21586 C  CG2   . THR A 1 4468 ? 184.912 171.342 151.694 1.00 68.71  ? 4468 THR A CG2   1 
ATOM   21587 N  N     . VAL A 1 4469 ? 185.404 168.472 155.312 1.00 76.93  ? 4469 VAL A N     1 
ATOM   21588 C  CA    . VAL A 1 4469 ? 185.903 167.418 156.191 1.00 78.77  ? 4469 VAL A CA    1 
ATOM   21589 C  C     . VAL A 1 4469 ? 185.087 166.150 155.959 1.00 83.78  ? 4469 VAL A C     1 
ATOM   21590 O  O     . VAL A 1 4469 ? 183.852 166.220 155.875 1.00 85.98  ? 4469 VAL A O     1 
ATOM   21591 C  CB    . VAL A 1 4469 ? 185.847 167.862 157.664 1.00 80.40  ? 4469 VAL A CB    1 
ATOM   21592 C  CG1   . VAL A 1 4469 ? 185.911 166.669 158.596 1.00 76.03  ? 4469 VAL A CG1   1 
ATOM   21593 C  CG2   . VAL A 1 4469 ? 186.980 168.829 157.975 1.00 73.03  ? 4469 VAL A CG2   1 
ATOM   21594 N  N     . PRO A 1 4470 ? 185.723 164.984 155.828 1.00 82.18  ? 4470 PRO A N     1 
ATOM   21595 C  CA    . PRO A 1 4470 ? 184.958 163.732 155.780 1.00 81.95  ? 4470 PRO A CA    1 
ATOM   21596 C  C     . PRO A 1 4470 ? 184.113 163.560 157.034 1.00 88.83  ? 4470 PRO A C     1 
ATOM   21597 O  O     . PRO A 1 4470 ? 184.527 163.915 158.138 1.00 91.34  ? 4470 PRO A O     1 
ATOM   21598 C  CB    . PRO A 1 4470 ? 186.044 162.655 155.678 1.00 67.30  ? 4470 PRO A CB    1 
ATOM   21599 C  CG    . PRO A 1 4470 ? 187.217 163.356 155.093 1.00 66.01  ? 4470 PRO A CG    1 
ATOM   21600 C  CD    . PRO A 1 4470 ? 187.160 164.765 155.601 1.00 75.24  ? 4470 PRO A CD    1 
ATOM   21601 N  N     . ALA A 1 4471 ? 182.917 162.996 156.850 1.00 86.94  ? 4471 ALA A N     1 
ATOM   21602 C  CA    . ALA A 1 4471 ? 181.937 162.955 157.931 1.00 91.32  ? 4471 ALA A CA    1 
ATOM   21603 C  C     . ALA A 1 4471 ? 182.432 162.159 159.132 1.00 94.01  ? 4471 ALA A C     1 
ATOM   21604 O  O     . ALA A 1 4471 ? 181.901 162.318 160.238 1.00 96.89  ? 4471 ALA A O     1 
ATOM   21605 C  CB    . ALA A 1 4471 ? 180.620 162.373 157.418 1.00 93.84  ? 4471 ALA A CB    1 
ATOM   21606 N  N     . GLY A 1 4472 ? 183.435 161.307 158.947 1.00 89.58  ? 4472 GLY A N     1 
ATOM   21607 C  CA    . GLY A 1 4472 ? 183.914 160.439 160.001 1.00 86.66  ? 4472 GLY A CA    1 
ATOM   21608 C  C     . GLY A 1 4472 ? 185.277 160.757 160.579 1.00 87.86  ? 4472 GLY A C     1 
ATOM   21609 O  O     . GLY A 1 4472 ? 185.764 159.985 161.413 1.00 89.07  ? 4472 GLY A O     1 
ATOM   21610 N  N     . MET A 1 4473 ? 185.911 161.857 160.177 1.00 87.32  ? 4473 MET A N     1 
ATOM   21611 C  CA    . MET A 1 4473 ? 187.250 162.154 160.671 1.00 79.32  ? 4473 MET A CA    1 
ATOM   21612 C  C     . MET A 1 4473 ? 187.193 162.601 162.128 1.00 79.54  ? 4473 MET A C     1 
ATOM   21613 O  O     . MET A 1 4473 ? 186.380 163.453 162.498 1.00 82.23  ? 4473 MET A O     1 
ATOM   21614 C  CB    . MET A 1 4473 ? 187.924 163.221 159.805 1.00 74.44  ? 4473 MET A CB    1 
ATOM   21615 C  CG    . MET A 1 4473 ? 189.084 163.912 160.502 1.00 70.46  ? 4473 MET A CG    1 
ATOM   21616 S  SD    . MET A 1 4473 ? 190.283 164.735 159.431 1.00 79.34  ? 4473 MET A SD    1 
ATOM   21617 C  CE    . MET A 1 4473 ? 189.239 165.566 158.252 1.00 69.15  ? 4473 MET A CE    1 
ATOM   21618 N  N     . THR A 1 4474 ? 188.064 162.022 162.954 1.00 75.72  ? 4474 THR A N     1 
ATOM   21619 C  CA    . THR A 1 4474 ? 188.070 162.272 164.387 1.00 73.10  ? 4474 THR A CA    1 
ATOM   21620 C  C     . THR A 1 4474 ? 188.992 163.448 164.711 1.00 70.63  ? 4474 THR A C     1 
ATOM   21621 O  O     . THR A 1 4474 ? 189.490 164.142 163.822 1.00 73.80  ? 4474 THR A O     1 
ATOM   21622 C  CB    . THR A 1 4474 ? 188.477 161.009 165.141 1.00 72.82  ? 4474 THR A CB    1 
ATOM   21623 O  OG1   . THR A 1 4474 ? 189.844 160.694 164.848 1.00 71.12  ? 4474 THR A OG1   1 
ATOM   21624 C  CG2   . THR A 1 4474 ? 187.593 159.840 164.734 1.00 70.40  ? 4474 THR A CG2   1 
ATOM   21625 N  N     . VAL A 1 4475 ? 189.228 163.680 166.005 1.00 67.93  ? 4475 VAL A N     1 
ATOM   21626 C  CA    . VAL A 1 4475 ? 189.950 164.875 166.433 1.00 64.68  ? 4475 VAL A CA    1 
ATOM   21627 C  C     . VAL A 1 4475 ? 191.439 164.762 166.122 1.00 63.48  ? 4475 VAL A C     1 
ATOM   21628 O  O     . VAL A 1 4475 ? 192.061 165.728 165.667 1.00 62.74  ? 4475 VAL A O     1 
ATOM   21629 C  CB    . VAL A 1 4475 ? 189.708 165.136 167.930 1.00 66.12  ? 4475 VAL A CB    1 
ATOM   21630 C  CG1   . VAL A 1 4475 ? 190.402 166.419 168.363 1.00 61.07  ? 4475 VAL A CG1   1 
ATOM   21631 C  CG2   . VAL A 1 4475 ? 188.222 165.198 168.228 1.00 68.66  ? 4475 VAL A CG2   1 
ATOM   21632 N  N     . ILE A 1 4476 ? 192.039 163.598 166.380 1.00 62.91  ? 4476 ILE A N     1 
ATOM   21633 C  CA    . ILE A 1 4476 ? 193.494 163.473 166.291 1.00 63.59  ? 4476 ILE A CA    1 
ATOM   21634 C  C     . ILE A 1 4476 ? 193.964 163.622 164.847 1.00 65.89  ? 4476 ILE A C     1 
ATOM   21635 O  O     . ILE A 1 4476 ? 194.896 164.383 164.551 1.00 65.31  ? 4476 ILE A O     1 
ATOM   21636 C  CB    . ILE A 1 4476 ? 193.962 162.136 166.896 1.00 68.85  ? 4476 ILE A CB    1 
ATOM   21637 C  CG1   . ILE A 1 4476 ? 193.628 162.056 168.390 1.00 73.30  ? 4476 ILE A CG1   1 
ATOM   21638 C  CG2   . ILE A 1 4476 ? 195.455 161.945 166.676 1.00 65.14  ? 4476 ILE A CG2   1 
ATOM   21639 C  CD1   . ILE A 1 4476 ? 192.259 161.479 168.701 1.00 65.32  ? 4476 ILE A CD1   1 
ATOM   21640 N  N     . GLN A 1 4477 ? 193.328 162.899 163.925 1.00 65.45  ? 4477 GLN A N     1 
ATOM   21641 C  CA    . GLN A 1 4477 ? 193.741 162.980 162.530 1.00 63.84  ? 4477 GLN A CA    1 
ATOM   21642 C  C     . GLN A 1 4477 ? 193.359 164.324 161.920 1.00 59.60  ? 4477 GLN A C     1 
ATOM   21643 O  O     . GLN A 1 4477 ? 194.048 164.824 161.024 1.00 62.97  ? 4477 GLN A O     1 
ATOM   21644 C  CB    . GLN A 1 4477 ? 193.152 161.810 161.739 1.00 64.94  ? 4477 GLN A CB    1 
ATOM   21645 C  CG    . GLN A 1 4477 ? 191.665 161.894 161.489 1.00 68.63  ? 4477 GLN A CG    1 
ATOM   21646 C  CD    . GLN A 1 4477 ? 190.994 160.534 161.493 1.00 72.22  ? 4477 GLN A CD    1 
ATOM   21647 O  OE1   . GLN A 1 4477 ? 191.036 159.812 162.489 1.00 75.70  ? 4477 GLN A OE1   1 
ATOM   21648 N  NE2   . GLN A 1 4477 ? 190.367 160.179 160.378 1.00 68.39  ? 4477 GLN A NE2   1 
ATOM   21649 N  N     . TRP A 1 4478 ? 192.281 164.943 162.414 1.00 54.49  ? 4478 TRP A N     1 
ATOM   21650 C  CA    . TRP A 1 4478 ? 191.972 166.307 161.998 1.00 52.78  ? 4478 TRP A CA    1 
ATOM   21651 C  C     . TRP A 1 4478 ? 193.063 167.272 162.435 1.00 57.56  ? 4478 TRP A C     1 
ATOM   21652 O  O     . TRP A 1 4478 ? 193.434 168.179 161.685 1.00 60.27  ? 4478 TRP A O     1 
ATOM   21653 C  CB    . TRP A 1 4478 ? 190.622 166.753 162.559 1.00 54.60  ? 4478 TRP A CB    1 
ATOM   21654 C  CG    . TRP A 1 4478 ? 190.212 168.119 162.088 1.00 51.85  ? 4478 TRP A CG    1 
ATOM   21655 C  CD1   . TRP A 1 4478 ? 189.435 168.413 161.007 1.00 51.96  ? 4478 TRP A CD1   1 
ATOM   21656 C  CD2   . TRP A 1 4478 ? 190.571 169.377 162.677 1.00 55.25  ? 4478 TRP A CD2   1 
ATOM   21657 N  NE1   . TRP A 1 4478 ? 189.280 169.773 160.889 1.00 53.26  ? 4478 TRP A NE1   1 
ATOM   21658 C  CE2   . TRP A 1 4478 ? 189.967 170.387 161.903 1.00 55.35  ? 4478 TRP A CE2   1 
ATOM   21659 C  CE3   . TRP A 1 4478 ? 191.337 169.747 163.787 1.00 56.13  ? 4478 TRP A CE3   1 
ATOM   21660 C  CZ2   . TRP A 1 4478 ? 190.109 171.741 162.200 1.00 56.21  ? 4478 TRP A CZ2   1 
ATOM   21661 C  CZ3   . TRP A 1 4478 ? 191.476 171.091 164.080 1.00 53.05  ? 4478 TRP A CZ3   1 
ATOM   21662 C  CH2   . TRP A 1 4478 ? 190.865 172.071 163.290 1.00 52.83  ? 4478 TRP A CH2   1 
ATOM   21663 N  N     . VAL A 1 4479 ? 193.577 167.102 163.654 1.00 56.78  ? 4479 VAL A N     1 
ATOM   21664 C  CA    . VAL A 1 4479 ? 194.659 167.954 164.133 1.00 56.78  ? 4479 VAL A CA    1 
ATOM   21665 C  C     . VAL A 1 4479 ? 195.909 167.745 163.291 1.00 59.26  ? 4479 VAL A C     1 
ATOM   21666 O  O     . VAL A 1 4479 ? 196.608 168.703 162.944 1.00 63.65  ? 4479 VAL A O     1 
ATOM   21667 C  CB    . VAL A 1 4479 ? 194.922 167.689 165.627 1.00 55.62  ? 4479 VAL A CB    1 
ATOM   21668 C  CG1   . VAL A 1 4479 ? 196.316 168.155 166.020 1.00 60.25  ? 4479 VAL A CG1   1 
ATOM   21669 C  CG2   . VAL A 1 4479 ? 193.867 168.377 166.478 1.00 57.98  ? 4479 VAL A CG2   1 
ATOM   21670 N  N     . SER A 1 4480 ? 196.209 166.491 162.945 1.00 52.53  ? 4480 SER A N     1 
ATOM   21671 C  CA    . SER A 1 4480 ? 197.361 166.222 162.085 1.00 51.25  ? 4480 SER A CA    1 
ATOM   21672 C  C     . SER A 1 4480 ? 197.201 166.881 160.717 1.00 55.27  ? 4480 SER A C     1 
ATOM   21673 O  O     . SER A 1 4480 ? 198.137 167.514 160.207 1.00 60.00  ? 4480 SER A O     1 
ATOM   21674 C  CB    . SER A 1 4480 ? 197.562 164.715 161.935 1.00 50.00  ? 4480 SER A CB    1 
ATOM   21675 O  OG    . SER A 1 4480 ? 197.909 164.121 163.173 1.00 49.90  ? 4480 SER A OG    1 
ATOM   21676 N  N     . ASP A 1 4481 ? 196.018 166.751 160.111 1.00 55.98  ? 4481 ASP A N     1 
ATOM   21677 C  CA    . ASP A 1 4481 ? 195.776 167.365 158.809 1.00 58.31  ? 4481 ASP A CA    1 
ATOM   21678 C  C     . ASP A 1 4481 ? 195.856 168.885 158.892 1.00 58.56  ? 4481 ASP A C     1 
ATOM   21679 O  O     . ASP A 1 4481 ? 196.412 169.534 157.998 1.00 61.22  ? 4481 ASP A O     1 
ATOM   21680 C  CB    . ASP A 1 4481 ? 194.414 166.928 158.270 1.00 62.07  ? 4481 ASP A CB    1 
ATOM   21681 C  CG    . ASP A 1 4481 ? 194.266 167.184 156.785 1.00 72.08  ? 4481 ASP A CG    1 
ATOM   21682 O  OD1   . ASP A 1 4481 ? 195.298 167.240 156.084 1.00 69.50  ? 4481 ASP A OD1   1 
ATOM   21683 O  OD2   . ASP A 1 4481 ? 193.117 167.330 156.318 1.00 73.29  ? 4481 ASP A OD2   1 
ATOM   21684 N  N     . PHE A 1 4482 ? 195.299 169.468 159.955 1.00 54.72  ? 4482 PHE A N     1 
ATOM   21685 C  CA    . PHE A 1 4482 ? 195.356 170.914 160.133 1.00 52.38  ? 4482 PHE A CA    1 
ATOM   21686 C  C     . PHE A 1 4482 ? 196.791 171.390 160.312 1.00 51.52  ? 4482 PHE A C     1 
ATOM   21687 O  O     . PHE A 1 4482 ? 197.171 172.439 159.784 1.00 52.56  ? 4482 PHE A O     1 
ATOM   21688 C  CB    . PHE A 1 4482 ? 194.497 171.325 161.328 1.00 50.43  ? 4482 PHE A CB    1 
ATOM   21689 C  CG    . PHE A 1 4482 ? 194.419 172.808 161.538 1.00 53.76  ? 4482 PHE A CG    1 
ATOM   21690 C  CD1   . PHE A 1 4482 ? 193.907 173.634 160.552 1.00 54.12  ? 4482 PHE A CD1   1 
ATOM   21691 C  CD2   . PHE A 1 4482 ? 194.852 173.376 162.723 1.00 54.91  ? 4482 PHE A CD2   1 
ATOM   21692 C  CE1   . PHE A 1 4482 ? 193.834 174.999 160.742 1.00 52.92  ? 4482 PHE A CE1   1 
ATOM   21693 C  CE2   . PHE A 1 4482 ? 194.780 174.741 162.920 1.00 52.92  ? 4482 PHE A CE2   1 
ATOM   21694 C  CZ    . PHE A 1 4482 ? 194.270 175.553 161.928 1.00 54.76  ? 4482 PHE A CZ    1 
ATOM   21695 N  N     . SER A 1 4483 ? 197.601 170.632 161.055 1.00 52.26  ? 4483 SER A N     1 
ATOM   21696 C  CA    . SER A 1 4483 ? 199.007 170.984 161.210 1.00 53.69  ? 4483 SER A CA    1 
ATOM   21697 C  C     . SER A 1 4483 ? 199.736 170.925 159.875 1.00 55.05  ? 4483 SER A C     1 
ATOM   21698 O  O     . SER A 1 4483 ? 200.564 171.791 159.572 1.00 57.58  ? 4483 SER A O     1 
ATOM   21699 C  CB    . SER A 1 4483 ? 199.670 170.054 162.226 1.00 59.63  ? 4483 SER A CB    1 
ATOM   21700 O  OG    . SER A 1 4483 ? 199.096 170.212 163.511 1.00 63.56  ? 4483 SER A OG    1 
ATOM   21701 N  N     . GLU A 1 4484 ? 199.440 169.908 159.060 1.00 55.43  ? 4484 GLU A N     1 
ATOM   21702 C  CA    . GLU A 1 4484 ? 200.048 169.831 157.734 1.00 55.34  ? 4484 GLU A CA    1 
ATOM   21703 C  C     . GLU A 1 4484 ? 199.642 171.020 156.868 1.00 57.09  ? 4484 GLU A C     1 
ATOM   21704 O  O     . GLU A 1 4484 ? 200.476 171.601 156.161 1.00 60.14  ? 4484 GLU A O     1 
ATOM   21705 C  CB    . GLU A 1 4484 ? 199.666 168.516 157.057 1.00 58.16  ? 4484 GLU A CB    1 
ATOM   21706 C  CG    . GLU A 1 4484 ? 200.657 167.389 157.293 1.00 59.65  ? 4484 GLU A CG    1 
ATOM   21707 C  CD    . GLU A 1 4484 ? 202.081 167.789 156.963 1.00 70.16  ? 4484 GLU A CD    1 
ATOM   21708 O  OE1   . GLU A 1 4484 ? 202.310 168.330 155.861 1.00 70.42  ? 4484 GLU A OE1   1 
ATOM   21709 O  OE2   . GLU A 1 4484 ? 202.974 167.562 157.807 1.00 75.53  ? 4484 GLU A OE2   1 
ATOM   21710 N  N     . ARG A 1 4485 ? 198.361 171.396 156.914 1.00 53.45  ? 4485 ARG A N     1 
ATOM   21711 C  CA    . ARG A 1 4485 ? 197.895 172.547 156.144 1.00 50.15  ? 4485 ARG A CA    1 
ATOM   21712 C  C     . ARG A 1 4485 ? 198.569 173.832 156.610 1.00 59.45  ? 4485 ARG A C     1 
ATOM   21713 O  O     . ARG A 1 4485 ? 198.946 174.679 155.791 1.00 64.04  ? 4485 ARG A O     1 
ATOM   21714 C  CB    . ARG A 1 4485 ? 196.375 172.670 156.255 1.00 45.03  ? 4485 ARG A CB    1 
ATOM   21715 C  CG    . ARG A 1 4485 ? 195.609 171.488 155.687 1.00 49.00  ? 4485 ARG A CG    1 
ATOM   21716 C  CD    . ARG A 1 4485 ? 194.124 171.597 155.988 1.00 51.66  ? 4485 ARG A CD    1 
ATOM   21717 N  NE    . ARG A 1 4485 ? 193.393 170.409 155.567 1.00 55.52  ? 4485 ARG A NE    1 
ATOM   21718 C  CZ    . ARG A 1 4485 ? 192.380 170.415 154.712 1.00 57.75  ? 4485 ARG A CZ    1 
ATOM   21719 N  NH1   . ARG A 1 4485 ? 191.944 171.537 154.165 1.00 61.62  ? 4485 ARG A NH1   1 
ATOM   21720 N  NH2   . ARG A 1 4485 ? 191.789 169.265 154.398 1.00 58.54  ? 4485 ARG A NH2   1 
ATOM   21721 N  N     . ILE A 1 4486 ? 198.726 173.995 157.925 1.00 59.00  ? 4486 ILE A N     1 
ATOM   21722 C  CA    . ILE A 1 4486 ? 199.371 175.191 158.457 1.00 54.86  ? 4486 ILE A CA    1 
ATOM   21723 C  C     . ILE A 1 4486 ? 200.842 175.228 158.061 1.00 55.86  ? 4486 ILE A C     1 
ATOM   21724 O  O     . ILE A 1 4486 ? 201.383 176.294 157.752 1.00 64.08  ? 4486 ILE A O     1 
ATOM   21725 C  CB    . ILE A 1 4486 ? 199.185 175.266 159.984 1.00 55.59  ? 4486 ILE A CB    1 
ATOM   21726 C  CG1   . ILE A 1 4486 ? 197.711 175.481 160.332 1.00 53.14  ? 4486 ILE A CG1   1 
ATOM   21727 C  CG2   . ILE A 1 4486 ? 200.022 176.388 160.574 1.00 62.36  ? 4486 ILE A CG2   1 
ATOM   21728 C  CD1   . ILE A 1 4486 ? 197.039 176.562 159.514 1.00 51.11  ? 4486 ILE A CD1   1 
ATOM   21729 N  N     . LYS A 1 4487 ? 201.513 174.074 158.059 1.00 51.76  ? 4487 LYS A N     1 
ATOM   21730 C  CA    . LYS A 1 4487 ? 202.901 174.037 157.606 1.00 55.03  ? 4487 LYS A CA    1 
ATOM   21731 C  C     . LYS A 1 4487 ? 203.013 174.397 156.129 1.00 62.10  ? 4487 LYS A C     1 
ATOM   21732 O  O     . LYS A 1 4487 ? 203.937 175.116 155.726 1.00 70.72  ? 4487 LYS A O     1 
ATOM   21733 C  CB    . LYS A 1 4487 ? 203.512 172.661 157.873 1.00 51.57  ? 4487 LYS A CB    1 
ATOM   21734 C  CG    . LYS A 1 4487 ? 203.693 172.341 159.347 1.00 57.62  ? 4487 LYS A CG    1 
ATOM   21735 C  CD    . LYS A 1 4487 ? 204.321 170.973 159.543 1.00 59.80  ? 4487 LYS A CD    1 
ATOM   21736 C  CE    . LYS A 1 4487 ? 204.599 170.700 161.012 1.00 60.60  ? 4487 LYS A CE    1 
ATOM   21737 N  NZ    . LYS A 1 4487 ? 203.345 170.579 161.805 1.00 63.60  ? 4487 LYS A NZ    1 
ATOM   21738 N  N     . GLN A 1 4488 ? 202.085 173.904 155.304 1.00 58.50  ? 4488 GLN A N     1 
ATOM   21739 C  CA    . GLN A 1 4488 ? 202.092 174.273 153.891 1.00 59.89  ? 4488 GLN A CA    1 
ATOM   21740 C  C     . GLN A 1 4488 ? 201.874 175.771 153.714 1.00 62.40  ? 4488 GLN A C     1 
ATOM   21741 O  O     . GLN A 1 4488 ? 202.544 176.415 152.895 1.00 66.50  ? 4488 GLN A O     1 
ATOM   21742 C  CB    . GLN A 1 4488 ? 201.027 173.481 153.134 1.00 61.31  ? 4488 GLN A CB    1 
ATOM   21743 C  CG    . GLN A 1 4488 ? 200.867 173.892 151.679 1.00 67.07  ? 4488 GLN A CG    1 
ATOM   21744 C  CD    . GLN A 1 4488 ? 199.588 173.366 151.061 1.00 62.46  ? 4488 GLN A CD    1 
ATOM   21745 O  OE1   . GLN A 1 4488 ? 199.618 172.645 150.064 1.00 59.80  ? 4488 GLN A OE1   1 
ATOM   21746 N  NE2   . GLN A 1 4488 ? 198.454 173.728 151.648 1.00 62.97  ? 4488 GLN A NE2   1 
ATOM   21747 N  N     . LEU A 1 4489 ? 200.943 176.346 154.479 1.00 64.66  ? 4489 LEU A N     1 
ATOM   21748 C  CA    . LEU A 1 4489 ? 200.704 177.784 154.402 1.00 67.26  ? 4489 LEU A CA    1 
ATOM   21749 C  C     . LEU A 1 4489 ? 201.919 178.573 154.878 1.00 69.52  ? 4489 LEU A C     1 
ATOM   21750 O  O     . LEU A 1 4489 ? 202.228 179.638 154.333 1.00 72.06  ? 4489 LEU A O     1 
ATOM   21751 C  CB    . LEU A 1 4489 ? 199.464 178.153 155.214 1.00 68.37  ? 4489 LEU A CB    1 
ATOM   21752 C  CG    . LEU A 1 4489 ? 198.124 177.752 154.592 1.00 63.97  ? 4489 LEU A CG    1 
ATOM   21753 C  CD1   . LEU A 1 4489 ? 196.963 178.267 155.427 1.00 61.76  ? 4489 LEU A CD1   1 
ATOM   21754 C  CD2   . LEU A 1 4489 ? 198.024 178.256 153.161 1.00 61.00  ? 4489 LEU A CD2   1 
ATOM   21755 N  N     . GLN A 1 4490 ? 202.616 178.070 155.900 1.00 68.56  ? 4490 GLN A N     1 
ATOM   21756 C  CA    . GLN A 1 4490 ? 203.840 178.719 156.357 1.00 67.28  ? 4490 GLN A CA    1 
ATOM   21757 C  C     . GLN A 1 4490 ? 204.907 178.704 155.272 1.00 71.94  ? 4490 GLN A C     1 
ATOM   21758 O  O     . GLN A 1 4490 ? 205.593 179.710 155.049 1.00 77.56  ? 4490 GLN A O     1 
ATOM   21759 C  CB    . GLN A 1 4490 ? 204.360 178.030 157.620 1.00 64.37  ? 4490 GLN A CB    1 
ATOM   21760 C  CG    . GLN A 1 4490 ? 203.620 178.397 158.893 1.00 67.21  ? 4490 GLN A CG    1 
ATOM   21761 C  CD    . GLN A 1 4490 ? 204.270 177.811 160.130 1.00 74.89  ? 4490 GLN A CD    1 
ATOM   21762 O  OE1   . GLN A 1 4490 ? 204.571 176.619 160.181 1.00 69.97  ? 4490 GLN A OE1   1 
ATOM   21763 N  NE2   . GLN A 1 4490 ? 204.491 178.649 161.136 1.00 79.36  ? 4490 GLN A NE2   1 
ATOM   21764 N  N     . ASN A 1 4491 ? 205.067 177.567 154.591 1.00 71.28  ? 4491 ASN A N     1 
ATOM   21765 C  CA    . ASN A 1 4491 ? 206.020 177.494 153.488 1.00 72.45  ? 4491 ASN A CA    1 
ATOM   21766 C  C     . ASN A 1 4491 ? 205.643 178.465 152.378 1.00 71.63  ? 4491 ASN A C     1 
ATOM   21767 O  O     . ASN A 1 4491 ? 206.512 179.119 151.789 1.00 76.88  ? 4491 ASN A O     1 
ATOM   21768 C  CB    . ASN A 1 4491 ? 206.096 176.064 152.952 1.00 69.46  ? 4491 ASN A CB    1 
ATOM   21769 C  CG    . ASN A 1 4491 ? 206.921 175.154 153.837 1.00 68.62  ? 4491 ASN A CG    1 
ATOM   21770 O  OD1   . ASN A 1 4491 ? 206.779 175.161 155.060 1.00 64.03  ? 4491 ASN A OD1   1 
ATOM   21771 N  ND2   . ASN A 1 4491 ? 207.791 174.361 153.223 1.00 70.30  ? 4491 ASN A ND2   1 
ATOM   21772 N  N     . ILE A 1 4492 ? 204.346 178.573 152.083 1.00 71.53  ? 4492 ILE A N     1 
ATOM   21773 C  CA    . ILE A 1 4492 ? 203.878 179.535 151.088 1.00 74.33  ? 4492 ILE A CA    1 
ATOM   21774 C  C     . ILE A 1 4492 ? 204.224 180.956 151.517 1.00 84.35  ? 4492 ILE A C     1 
ATOM   21775 O  O     . ILE A 1 4492 ? 204.649 181.782 150.700 1.00 89.97  ? 4492 ILE A O     1 
ATOM   21776 C  CB    . ILE A 1 4492 ? 202.366 179.362 150.858 1.00 73.60  ? 4492 ILE A CB    1 
ATOM   21777 C  CG1   . ILE A 1 4492 ? 202.090 178.052 150.119 1.00 76.55  ? 4492 ILE A CG1   1 
ATOM   21778 C  CG2   . ILE A 1 4492 ? 201.798 180.543 150.087 1.00 69.25  ? 4492 ILE A CG2   1 
ATOM   21779 C  CD1   . ILE A 1 4492 ? 200.646 177.615 150.174 1.00 73.25  ? 4492 ILE A CD1   1 
ATOM   21780 N  N     . SER A 1 4493 ? 204.041 181.263 152.803 1.00 85.98  ? 4493 SER A N     1 
ATOM   21781 C  CA    . SER A 1 4493 ? 204.353 182.598 153.306 1.00 83.18  ? 4493 SER A CA    1 
ATOM   21782 C  C     . SER A 1 4493 ? 205.839 182.911 153.181 1.00 85.51  ? 4493 SER A C     1 
ATOM   21783 O  O     . SER A 1 4493 ? 206.212 184.020 152.780 1.00 89.44  ? 4493 SER A O     1 
ATOM   21784 C  CB    . SER A 1 4493 ? 203.899 182.730 154.760 1.00 77.00  ? 4493 SER A CB    1 
ATOM   21785 O  OG    . SER A 1 4493 ? 202.501 182.942 154.840 1.00 78.41  ? 4493 SER A OG    1 
ATOM   21786 N  N     . LEU A 1 4494 ? 206.703 181.952 153.525 1.00 80.29  ? 4494 LEU A N     1 
ATOM   21787 C  CA    . LEU A 1 4494 ? 208.140 182.176 153.370 1.00 81.20  ? 4494 LEU A CA    1 
ATOM   21788 C  C     . LEU A 1 4494 ? 208.517 182.351 151.903 1.00 92.30  ? 4494 LEU A C     1 
ATOM   21789 O  O     . LEU A 1 4494 ? 209.355 183.197 151.567 1.00 101.01 ? 4494 LEU A O     1 
ATOM   21790 C  CB    . LEU A 1 4494 ? 208.946 181.036 153.995 1.00 76.99  ? 4494 LEU A CB    1 
ATOM   21791 C  CG    . LEU A 1 4494 ? 208.517 180.454 155.342 1.00 78.87  ? 4494 LEU A CG    1 
ATOM   21792 C  CD1   . LEU A 1 4494 ? 209.497 179.385 155.800 1.00 76.63  ? 4494 LEU A CD1   1 
ATOM   21793 C  CD2   . LEU A 1 4494 ? 208.390 181.551 156.388 1.00 74.87  ? 4494 LEU A CD2   1 
ATOM   21794 N  N     . ALA A 1 4495 ? 207.910 181.559 151.015 1.00 91.63  ? 4495 ALA A N     1 
ATOM   21795 C  CA    . ALA A 1 4495 ? 208.182 181.708 149.589 1.00 90.86  ? 4495 ALA A CA    1 
ATOM   21796 C  C     . ALA A 1 4495 ? 207.760 183.084 149.090 1.00 97.99  ? 4495 ALA A C     1 
ATOM   21797 O  O     . ALA A 1 4495 ? 208.460 183.702 148.279 1.00 106.70 ? 4495 ALA A O     1 
ATOM   21798 C  CB    . ALA A 1 4495 ? 207.473 180.608 148.800 1.00 87.15  ? 4495 ALA A CB    1 
ATOM   21799 N  N     . ALA A 1 4496 ? 206.610 183.576 149.556 1.00 90.07  ? 4496 ALA A N     1 
ATOM   21800 C  CA    . ALA A 1 4496 ? 206.170 184.915 149.179 1.00 94.28  ? 4496 ALA A CA    1 
ATOM   21801 C  C     . ALA A 1 4496 ? 207.119 185.979 149.714 1.00 105.49 ? 4496 ALA A C     1 
ATOM   21802 O  O     . ALA A 1 4496 ? 207.439 186.946 149.013 1.00 107.45 ? 4496 ALA A O     1 
ATOM   21803 C  CB    . ALA A 1 4496 ? 204.752 185.166 149.687 1.00 86.44  ? 4496 ALA A CB    1 
ATOM   21804 N  N     . ALA A 1 4497 ? 207.572 185.821 150.960 1.00 104.86 ? 4497 ALA A N     1 
ATOM   21805 C  CA    . ALA A 1 4497 ? 208.486 186.795 151.546 1.00 103.24 ? 4497 ALA A CA    1 
ATOM   21806 C  C     . ALA A 1 4497 ? 209.812 186.826 150.798 1.00 106.03 ? 4497 ALA A C     1 
ATOM   21807 O  O     . ALA A 1 4497 ? 210.425 187.890 150.649 1.00 106.26 ? 4497 ALA A O     1 
ATOM   21808 C  CB    . ALA A 1 4497 ? 208.710 186.483 153.025 1.00 87.76  ? 4497 ALA A CB    1 
ATOM   21809 N  N     . SER A 1 4498 ? 210.274 185.669 150.323 1.00 107.80 ? 4498 SER A N     1 
ATOM   21810 C  CA    . SER A 1 4498 ? 211.561 185.611 149.638 1.00 108.18 ? 4498 SER A CA    1 
ATOM   21811 C  C     . SER A 1 4498 ? 211.480 186.243 148.253 1.00 108.38 ? 4498 SER A C     1 
ATOM   21812 O  O     . SER A 1 4498 ? 212.161 187.235 147.968 1.00 114.35 ? 4498 SER A O     1 
ATOM   21813 C  CB    . SER A 1 4498 ? 212.036 184.159 149.545 1.00 107.39 ? 4498 SER A CB    1 
ATOM   21814 O  OG    . SER A 1 4498 ? 212.086 183.555 150.826 1.00 103.39 ? 4498 SER A OG    1 
ATOM   21815 N  N     . GLY A 1 4499 ? 210.649 185.683 147.377 1.00 106.70 ? 4499 GLY A N     1 
ATOM   21816 C  CA    . GLY A 1 4499 ? 210.590 186.144 146.003 1.00 110.51 ? 4499 GLY A CA    1 
ATOM   21817 C  C     . GLY A 1 4499 ? 209.509 187.164 145.710 1.00 111.18 ? 4499 GLY A C     1 
ATOM   21818 O  O     . GLY A 1 4499 ? 209.790 188.227 145.148 1.00 109.97 ? 4499 GLY A O     1 
ATOM   21819 N  N     . GLY A 1 4500 ? 208.270 186.857 146.086 1.00 111.48 ? 4500 GLY A N     1 
ATOM   21820 C  CA    . GLY A 1 4500 ? 207.154 187.732 145.783 1.00 107.90 ? 4500 GLY A CA    1 
ATOM   21821 C  C     . GLY A 1 4500 ? 206.000 187.008 145.121 1.00 108.21 ? 4500 GLY A C     1 
ATOM   21822 O  O     . GLY A 1 4500 ? 205.906 185.779 145.196 1.00 107.03 ? 4500 GLY A O     1 
ATOM   21823 N  N     . ALA A 1 4501 ? 205.108 187.761 144.470 1.00 110.09 ? 4501 ALA A N     1 
ATOM   21824 C  CA    . ALA A 1 4501 ? 203.966 187.144 143.802 1.00 112.43 ? 4501 ALA A CA    1 
ATOM   21825 C  C     . ALA A 1 4501 ? 204.409 186.276 142.631 1.00 108.42 ? 4501 ALA A C     1 
ATOM   21826 O  O     . ALA A 1 4501 ? 203.752 185.282 142.303 1.00 103.04 ? 4501 ALA A O     1 
ATOM   21827 C  CB    . ALA A 1 4501 ? 202.987 188.218 143.331 1.00 110.39 ? 4501 ALA A CB    1 
ATOM   21828 N  N     . LYS A 1 4502 ? 205.517 186.641 141.982 1.00 105.96 ? 4502 LYS A N     1 
ATOM   21829 C  CA    . LYS A 1 4502 ? 206.043 185.812 140.903 1.00 104.73 ? 4502 LYS A CA    1 
ATOM   21830 C  C     . LYS A 1 4502 ? 206.524 184.464 141.421 1.00 102.85 ? 4502 LYS A C     1 
ATOM   21831 O  O     . LYS A 1 4502 ? 206.515 183.474 140.680 1.00 99.65  ? 4502 LYS A O     1 
ATOM   21832 C  CB    . LYS A 1 4502 ? 207.178 186.543 140.186 1.00 107.46 ? 4502 LYS A CB    1 
ATOM   21833 C  CG    . LYS A 1 4502 ? 208.243 187.091 141.121 1.00 110.15 ? 4502 LYS A CG    1 
ATOM   21834 C  CD    . LYS A 1 4502 ? 209.480 187.530 140.360 1.00 109.93 ? 4502 LYS A CD    1 
ATOM   21835 C  CE    . LYS A 1 4502 ? 210.596 187.925 141.312 1.00 108.56 ? 4502 LYS A CE    1 
ATOM   21836 N  NZ    . LYS A 1 4502 ? 210.908 186.833 142.275 1.00 102.93 ? 4502 LYS A NZ    1 
ATOM   21837 N  N     . GLU A 1 4503 ? 206.947 184.404 142.686 1.00 102.08 ? 4503 GLU A N     1 
ATOM   21838 C  CA    . GLU A 1 4503 ? 207.373 183.135 143.266 1.00 99.46  ? 4503 GLU A CA    1 
ATOM   21839 C  C     . GLU A 1 4503 ? 206.180 182.242 143.582 1.00 91.67  ? 4503 GLU A C     1 
ATOM   21840 O  O     . GLU A 1 4503 ? 206.311 181.012 143.596 1.00 91.40  ? 4503 GLU A O     1 
ATOM   21841 C  CB    . GLU A 1 4503 ? 208.204 183.392 144.525 1.00 103.42 ? 4503 GLU A CB    1 
ATOM   21842 C  CG    . GLU A 1 4503 ? 208.719 182.138 145.211 1.00 99.64  ? 4503 GLU A CG    1 
ATOM   21843 C  CD    . GLU A 1 4503 ? 209.462 181.218 144.261 1.00 98.51  ? 4503 GLU A CD    1 
ATOM   21844 O  OE1   . GLU A 1 4503 ? 210.455 181.665 143.651 1.00 104.19 ? 4503 GLU A OE1   1 
ATOM   21845 O  OE2   . GLU A 1 4503 ? 209.050 180.047 144.120 1.00 90.20  ? 4503 GLU A OE2   1 
ATOM   21846 N  N     . LEU A 1 4504 ? 205.012 182.842 143.824 1.00 86.43  ? 4504 LEU A N     1 
ATOM   21847 C  CA    . LEU A 1 4504 ? 203.814 182.065 144.126 1.00 84.42  ? 4504 LEU A CA    1 
ATOM   21848 C  C     . LEU A 1 4504 ? 203.400 181.186 142.954 1.00 84.62  ? 4504 LEU A C     1 
ATOM   21849 O  O     . LEU A 1 4504 ? 202.696 180.189 143.145 1.00 86.47  ? 4504 LEU A O     1 
ATOM   21850 C  CB    . LEU A 1 4504 ? 202.675 183.008 144.513 1.00 87.17  ? 4504 LEU A CB    1 
ATOM   21851 C  CG    . LEU A 1 4504 ? 202.423 183.160 146.011 1.00 84.46  ? 4504 LEU A CG    1 
ATOM   21852 C  CD1   . LEU A 1 4504 ? 203.652 183.742 146.678 1.00 89.70  ? 4504 LEU A CD1   1 
ATOM   21853 C  CD2   . LEU A 1 4504 ? 201.220 184.055 146.252 1.00 83.56  ? 4504 LEU A CD2   1 
ATOM   21854 N  N     . LYS A 1 4505 ? 203.814 181.544 141.737 1.00 85.11  ? 4505 LYS A N     1 
ATOM   21855 C  CA    . LYS A 1 4505 ? 203.491 180.726 140.573 1.00 78.79  ? 4505 LYS A CA    1 
ATOM   21856 C  C     . LYS A 1 4505 ? 204.283 179.423 140.583 1.00 80.72  ? 4505 LYS A C     1 
ATOM   21857 O  O     . LYS A 1 4505 ? 203.749 178.363 140.235 1.00 78.90  ? 4505 LYS A O     1 
ATOM   21858 C  CB    . LYS A 1 4505 ? 203.736 181.545 139.296 1.00 75.22  ? 4505 LYS A CB    1 
ATOM   21859 C  CG    . LYS A 1 4505 ? 203.538 180.857 137.927 1.00 76.62  ? 4505 LYS A CG    1 
ATOM   21860 C  CD    . LYS A 1 4505 ? 204.632 179.862 137.541 1.00 77.84  ? 4505 LYS A CD    1 
ATOM   21861 C  CE    . LYS A 1 4505 ? 204.366 179.240 136.183 1.00 76.68  ? 4505 LYS A CE    1 
ATOM   21862 N  NZ    . LYS A 1 4505 ? 205.393 178.219 135.837 1.00 78.33  ? 4505 LYS A NZ    1 
ATOM   21863 N  N     . ASN A 1 4506 ? 205.552 179.477 140.989 1.00 81.98  ? 4506 ASN A N     1 
ATOM   21864 C  CA    . ASN A 1 4506 ? 206.466 178.347 140.878 1.00 84.03  ? 4506 ASN A CA    1 
ATOM   21865 C  C     . ASN A 1 4506 ? 206.560 177.541 142.171 1.00 83.72  ? 4506 ASN A C     1 
ATOM   21866 O  O     . ASN A 1 4506 ? 207.624 176.999 142.490 1.00 85.74  ? 4506 ASN A O     1 
ATOM   21867 C  CB    . ASN A 1 4506 ? 207.851 178.835 140.450 1.00 85.23  ? 4506 ASN A CB    1 
ATOM   21868 C  CG    . ASN A 1 4506 ? 208.685 177.741 139.809 1.00 87.94  ? 4506 ASN A CG    1 
ATOM   21869 O  OD1   . ASN A 1 4506 ? 208.265 176.587 139.731 1.00 92.56  ? 4506 ASN A OD1   1 
ATOM   21870 N  ND2   . ASN A 1 4506 ? 209.876 178.102 139.344 1.00 81.57  ? 4506 ASN A ND2   1 
ATOM   21871 N  N     . ILE A 1 4507 ? 205.469 177.451 142.926 1.00 79.18  ? 4507 ILE A N     1 
ATOM   21872 C  CA    . ILE A 1 4507 ? 205.413 176.648 144.141 1.00 76.90  ? 4507 ILE A CA    1 
ATOM   21873 C  C     . ILE A 1 4507 ? 204.528 175.437 143.877 1.00 77.18  ? 4507 ILE A C     1 
ATOM   21874 O  O     . ILE A 1 4507 ? 203.531 175.528 143.150 1.00 76.27  ? 4507 ILE A O     1 
ATOM   21875 C  CB    . ILE A 1 4507 ? 204.906 177.465 145.348 1.00 73.39  ? 4507 ILE A CB    1 
ATOM   21876 C  CG1   . ILE A 1 4507 ? 205.151 176.706 146.654 1.00 75.03  ? 4507 ILE A CG1   1 
ATOM   21877 C  CG2   . ILE A 1 4507 ? 203.433 177.816 145.200 1.00 70.53  ? 4507 ILE A CG2   1 
ATOM   21878 C  CD1   . ILE A 1 4507 ? 206.614 176.523 146.990 1.00 75.47  ? 4507 ILE A CD1   1 
ATOM   21879 N  N     . HIS A 1 4508 ? 204.914 174.295 144.442 1.00 69.57  ? 4508 HIS A N     1 
ATOM   21880 C  CA    . HIS A 1 4508 ? 204.163 173.053 144.303 1.00 60.55  ? 4508 HIS A CA    1 
ATOM   21881 C  C     . HIS A 1 4508 ? 203.234 172.927 145.505 1.00 60.79  ? 4508 HIS A C     1 
ATOM   21882 O  O     . HIS A 1 4508 ? 203.691 172.700 146.630 1.00 64.73  ? 4508 HIS A O     1 
ATOM   21883 C  CB    . HIS A 1 4508 ? 205.104 171.855 144.200 1.00 59.66  ? 4508 HIS A CB    1 
ATOM   21884 C  CG    . HIS A 1 4508 ? 206.139 171.992 143.128 1.00 62.67  ? 4508 HIS A CG    1 
ATOM   21885 N  ND1   . HIS A 1 4508 ? 205.819 172.268 141.816 1.00 68.04  ? 4508 HIS A ND1   1 
ATOM   21886 C  CD2   . HIS A 1 4508 ? 207.488 171.888 143.172 1.00 71.22  ? 4508 HIS A CD2   1 
ATOM   21887 C  CE1   . HIS A 1 4508 ? 206.927 172.330 141.099 1.00 71.77  ? 4508 HIS A CE1   1 
ATOM   21888 N  NE2   . HIS A 1 4508 ? 207.953 172.104 141.898 1.00 77.78  ? 4508 HIS A NE2   1 
ATOM   21889 N  N     . VAL A 1 4509 ? 201.937 173.072 145.265 1.00 55.66  ? 4509 VAL A N     1 
ATOM   21890 C  CA    . VAL A 1 4509 ? 200.945 173.109 146.332 1.00 59.94  ? 4509 VAL A CA    1 
ATOM   21891 C  C     . VAL A 1 4509 ? 200.123 171.829 146.295 1.00 56.39  ? 4509 VAL A C     1 
ATOM   21892 O  O     . VAL A 1 4509 ? 199.856 171.260 145.230 1.00 55.45  ? 4509 VAL A O     1 
ATOM   21893 C  CB    . VAL A 1 4509 ? 200.051 174.363 146.210 1.00 57.58  ? 4509 VAL A CB    1 
ATOM   21894 C  CG1   . VAL A 1 4509 ? 199.211 174.304 144.947 1.00 48.43  ? 4509 VAL A CG1   1 
ATOM   21895 C  CG2   . VAL A 1 4509 ? 199.180 174.530 147.442 1.00 59.84  ? 4509 VAL A CG2   1 
ATOM   21896 N  N     . CYS A 1 4510 ? 199.733 171.360 147.478 1.00 55.46  ? 4510 CYS A N     1 
ATOM   21897 C  CA    . CYS A 1 4510 ? 198.905 170.167 147.616 1.00 53.84  ? 4510 CYS A CA    1 
ATOM   21898 C  C     . CYS A 1 4510 ? 197.440 170.589 147.631 1.00 59.00  ? 4510 CYS A C     1 
ATOM   21899 O  O     . CYS A 1 4510 ? 197.011 171.331 148.520 1.00 61.38  ? 4510 CYS A O     1 
ATOM   21900 C  CB    . CYS A 1 4510 ? 199.272 169.404 148.886 1.00 51.49  ? 4510 CYS A CB    1 
ATOM   21901 S  SG    . CYS A 1 4510 ? 198.355 167.866 149.131 1.00 82.13  ? 4510 CYS A SG    1 
ATOM   21902 N  N     . LEU A 1 4511 ? 196.673 170.119 146.642 1.00 51.44  ? 4511 LEU A N     1 
ATOM   21903 C  CA    . LEU A 1 4511 ? 195.251 170.445 146.596 1.00 49.77  ? 4511 LEU A CA    1 
ATOM   21904 C  C     . LEU A 1 4511 ? 194.504 169.865 147.789 1.00 55.22  ? 4511 LEU A C     1 
ATOM   21905 O  O     . LEU A 1 4511 ? 193.517 170.452 148.247 1.00 57.59  ? 4511 LEU A O     1 
ATOM   21906 C  CB    . LEU A 1 4511 ? 194.632 169.944 145.291 1.00 48.79  ? 4511 LEU A CB    1 
ATOM   21907 C  CG    . LEU A 1 4511 ? 195.091 170.618 143.998 1.00 49.87  ? 4511 LEU A CG    1 
ATOM   21908 C  CD1   . LEU A 1 4511 ? 194.487 169.917 142.791 1.00 45.31  ? 4511 LEU A CD1   1 
ATOM   21909 C  CD2   . LEU A 1 4511 ? 194.734 172.094 143.999 1.00 52.82  ? 4511 LEU A CD2   1 
ATOM   21910 N  N     . GLY A 1 4512 ? 194.950 168.716 148.299 1.00 52.84  ? 4512 GLY A N     1 
ATOM   21911 C  CA    . GLY A 1 4512 ? 194.328 168.150 149.482 1.00 52.34  ? 4512 GLY A CA    1 
ATOM   21912 C  C     . GLY A 1 4512 ? 194.503 169.013 150.714 1.00 56.65  ? 4512 GLY A C     1 
ATOM   21913 O  O     . GLY A 1 4512 ? 193.603 169.087 151.556 1.00 59.19  ? 4512 GLY A O     1 
ATOM   21914 N  N     . GLY A 1 4513 ? 195.652 169.672 150.841 1.00 57.43  ? 4513 GLY A N     1 
ATOM   21915 C  CA    . GLY A 1 4513 ? 195.913 170.559 151.954 1.00 54.63  ? 4513 GLY A CA    1 
ATOM   21916 C  C     . GLY A 1 4513 ? 195.358 171.956 151.820 1.00 54.18  ? 4513 GLY A C     1 
ATOM   21917 O  O     . GLY A 1 4513 ? 195.454 172.743 152.765 1.00 58.45  ? 4513 GLY A O     1 
ATOM   21918 N  N     . LEU A 1 4514 ? 194.781 172.296 150.671 1.00 52.82  ? 4514 LEU A N     1 
ATOM   21919 C  CA    . LEU A 1 4514 ? 194.160 173.598 150.479 1.00 54.08  ? 4514 LEU A CA    1 
ATOM   21920 C  C     . LEU A 1 4514 ? 192.716 173.566 150.955 1.00 59.42  ? 4514 LEU A C     1 
ATOM   21921 O  O     . LEU A 1 4514 ? 192.016 172.563 150.793 1.00 66.81  ? 4514 LEU A O     1 
ATOM   21922 C  CB    . LEU A 1 4514 ? 194.214 174.020 149.011 1.00 54.98  ? 4514 LEU A CB    1 
ATOM   21923 C  CG    . LEU A 1 4514 ? 195.593 174.372 148.457 1.00 54.37  ? 4514 LEU A CG    1 
ATOM   21924 C  CD1   . LEU A 1 4514 ? 195.518 174.615 146.960 1.00 52.27  ? 4514 LEU A CD1   1 
ATOM   21925 C  CD2   . LEU A 1 4514 ? 196.148 175.591 149.174 1.00 60.44  ? 4514 LEU A CD2   1 
ATOM   21926 N  N     . PHE A 1 4515 ? 192.279 174.674 151.555 1.00 59.18  ? 4515 PHE A N     1 
ATOM   21927 C  CA    . PHE A 1 4515 ? 190.900 174.760 152.026 1.00 60.40  ? 4515 PHE A CA    1 
ATOM   21928 C  C     . PHE A 1 4515 ? 189.920 174.705 150.860 1.00 65.55  ? 4515 PHE A C     1 
ATOM   21929 O  O     . PHE A 1 4515 ? 188.892 174.022 150.936 1.00 69.85  ? 4515 PHE A O     1 
ATOM   21930 C  CB    . PHE A 1 4515 ? 190.697 176.037 152.847 1.00 63.74  ? 4515 PHE A CB    1 
ATOM   21931 C  CG    . PHE A 1 4515 ? 191.457 176.064 154.156 1.00 64.78  ? 4515 PHE A CG    1 
ATOM   21932 C  CD1   . PHE A 1 4515 ? 192.414 175.106 154.457 1.00 60.84  ? 4515 PHE A CD1   1 
ATOM   21933 C  CD2   . PHE A 1 4515 ? 191.215 177.064 155.082 1.00 64.09  ? 4515 PHE A CD2   1 
ATOM   21934 C  CE1   . PHE A 1 4515 ? 193.104 175.142 155.654 1.00 56.55  ? 4515 PHE A CE1   1 
ATOM   21935 C  CE2   . PHE A 1 4515 ? 191.902 177.105 156.280 1.00 67.45  ? 4515 PHE A CE2   1 
ATOM   21936 C  CZ    . PHE A 1 4515 ? 192.847 176.143 156.566 1.00 60.42  ? 4515 PHE A CZ    1 
ATOM   21937 N  N     . VAL A 1 4516 ? 190.217 175.417 149.776 1.00 65.06  ? 4516 VAL A N     1 
ATOM   21938 C  CA    . VAL A 1 4516 ? 189.394 175.384 148.568 1.00 67.29  ? 4516 VAL A CA    1 
ATOM   21939 C  C     . VAL A 1 4516 ? 190.298 175.143 147.363 1.00 65.56  ? 4516 VAL A C     1 
ATOM   21940 O  O     . VAL A 1 4516 ? 190.859 176.101 146.811 1.00 69.56  ? 4516 VAL A O     1 
ATOM   21941 C  CB    . VAL A 1 4516 ? 188.584 176.680 148.398 1.00 60.94  ? 4516 VAL A CB    1 
ATOM   21942 C  CG1   . VAL A 1 4516 ? 187.575 176.524 147.273 1.00 59.19  ? 4516 VAL A CG1   1 
ATOM   21943 C  CG2   . VAL A 1 4516 ? 187.885 177.061 149.695 1.00 60.43  ? 4516 VAL A CG2   1 
ATOM   21944 N  N     . PRO A 1 4517 ? 190.473 173.894 146.921 1.00 56.21  ? 4517 PRO A N     1 
ATOM   21945 C  CA    . PRO A 1 4517 ? 191.373 173.644 145.781 1.00 54.73  ? 4517 PRO A CA    1 
ATOM   21946 C  C     . PRO A 1 4517 ? 190.795 174.072 144.442 1.00 59.03  ? 4517 PRO A C     1 
ATOM   21947 O  O     . PRO A 1 4517 ? 191.555 174.471 143.548 1.00 63.63  ? 4517 PRO A O     1 
ATOM   21948 C  CB    . PRO A 1 4517 ? 191.596 172.127 145.841 1.00 57.76  ? 4517 PRO A CB    1 
ATOM   21949 C  CG    . PRO A 1 4517 ? 190.379 171.597 146.517 1.00 57.63  ? 4517 PRO A CG    1 
ATOM   21950 C  CD    . PRO A 1 4517 ? 189.923 172.650 147.486 1.00 52.02  ? 4517 PRO A CD    1 
ATOM   21951 N  N     . GLU A 1 4518 ? 189.473 173.987 144.269 1.00 55.17  ? 4518 GLU A N     1 
ATOM   21952 C  CA    . GLU A 1 4518 ? 188.859 174.490 143.045 1.00 59.58  ? 4518 GLU A CA    1 
ATOM   21953 C  C     . GLU A 1 4518 ? 189.133 175.977 142.864 1.00 61.05  ? 4518 GLU A C     1 
ATOM   21954 O  O     . GLU A 1 4518 ? 189.309 176.446 141.731 1.00 63.47  ? 4518 GLU A O     1 
ATOM   21955 C  CB    . GLU A 1 4518 ? 187.356 174.209 143.064 1.00 51.81  ? 4518 GLU A CB    1 
ATOM   21956 C  CG    . GLU A 1 4518 ? 186.566 174.879 141.952 1.00 60.70  ? 4518 GLU A CG    1 
ATOM   21957 C  CD    . GLU A 1 4518 ? 186.823 174.286 140.577 1.00 64.95  ? 4518 GLU A CD    1 
ATOM   21958 O  OE1   . GLU A 1 4518 ? 187.954 174.410 140.063 1.00 65.77  ? 4518 GLU A OE1   1 
ATOM   21959 O  OE2   . GLU A 1 4518 ? 185.878 173.708 140.000 1.00 59.13  ? 4518 GLU A OE2   1 
ATOM   21960 N  N     . ALA A 1 4519 ? 189.188 176.728 143.966 1.00 56.88  ? 4519 ALA A N     1 
ATOM   21961 C  CA    . ALA A 1 4519 ? 189.625 178.115 143.889 1.00 54.09  ? 4519 ALA A CA    1 
ATOM   21962 C  C     . ALA A 1 4519 ? 191.055 178.217 143.379 1.00 56.63  ? 4519 ALA A C     1 
ATOM   21963 O  O     . ALA A 1 4519 ? 191.381 179.154 142.645 1.00 65.35  ? 4519 ALA A O     1 
ATOM   21964 C  CB    . ALA A 1 4519 ? 189.498 178.790 145.254 1.00 56.61  ? 4519 ALA A CB    1 
ATOM   21965 N  N     . TYR A 1 4520 ? 191.922 177.270 143.748 1.00 53.56  ? 4520 TYR A N     1 
ATOM   21966 C  CA    . TYR A 1 4520 ? 193.279 177.277 143.209 1.00 51.84  ? 4520 TYR A CA    1 
ATOM   21967 C  C     . TYR A 1 4520 ? 193.284 177.024 141.708 1.00 49.60  ? 4520 TYR A C     1 
ATOM   21968 O  O     . TYR A 1 4520 ? 194.056 177.650 140.973 1.00 58.76  ? 4520 TYR A O     1 
ATOM   21969 C  CB    . TYR A 1 4520 ? 194.152 176.242 143.914 1.00 55.11  ? 4520 TYR A CB    1 
ATOM   21970 C  CG    . TYR A 1 4520 ? 195.559 176.200 143.361 1.00 52.13  ? 4520 TYR A CG    1 
ATOM   21971 C  CD1   . TYR A 1 4520 ? 196.469 177.206 143.652 1.00 57.20  ? 4520 TYR A CD1   1 
ATOM   21972 C  CD2   . TYR A 1 4520 ? 195.969 175.165 142.531 1.00 48.12  ? 4520 TYR A CD2   1 
ATOM   21973 C  CE1   . TYR A 1 4520 ? 197.752 177.177 143.141 1.00 56.77  ? 4520 TYR A CE1   1 
ATOM   21974 C  CE2   . TYR A 1 4520 ? 197.249 175.128 142.016 1.00 50.07  ? 4520 TYR A CE2   1 
ATOM   21975 C  CZ    . TYR A 1 4520 ? 198.136 176.137 142.323 1.00 55.95  ? 4520 TYR A CZ    1 
ATOM   21976 O  OH    . TYR A 1 4520 ? 199.414 176.104 141.815 1.00 59.18  ? 4520 TYR A OH    1 
ATOM   21977 N  N     . ILE A 1 4521 ? 192.450 176.095 141.236 1.00 47.60  ? 4521 ILE A N     1 
ATOM   21978 C  CA    . ILE A 1 4521 ? 192.367 175.854 139.795 1.00 49.35  ? 4521 ILE A CA    1 
ATOM   21979 C  C     . ILE A 1 4521 ? 191.897 177.111 139.074 1.00 55.12  ? 4521 ILE A C     1 
ATOM   21980 O  O     . ILE A 1 4521 ? 192.449 177.500 138.032 1.00 56.89  ? 4521 ILE A O     1 
ATOM   21981 C  CB    . ILE A 1 4521 ? 191.447 174.655 139.502 1.00 48.44  ? 4521 ILE A CB    1 
ATOM   21982 C  CG1   . ILE A 1 4521 ? 191.730 173.511 140.477 1.00 49.37  ? 4521 ILE A CG1   1 
ATOM   21983 C  CG2   . ILE A 1 4521 ? 191.616 174.192 138.063 1.00 45.63  ? 4521 ILE A CG2   1 
ATOM   21984 C  CD1   . ILE A 1 4521 ? 193.027 172.782 140.203 1.00 45.85  ? 4521 ILE A CD1   1 
ATOM   21985 N  N     . THR A 1 4522 ? 190.874 177.771 139.623 1.00 56.71  ? 4522 THR A N     1 
ATOM   21986 C  CA    . THR A 1 4522 ? 190.382 179.011 139.032 1.00 51.11  ? 4522 THR A CA    1 
ATOM   21987 C  C     . THR A 1 4522 ? 191.460 180.089 139.035 1.00 50.97  ? 4522 THR A C     1 
ATOM   21988 O  O     . THR A 1 4522 ? 191.605 180.836 138.061 1.00 55.53  ? 4522 THR A O     1 
ATOM   21989 C  CB    . THR A 1 4522 ? 189.138 179.488 139.783 1.00 61.32  ? 4522 THR A CB    1 
ATOM   21990 O  OG1   . THR A 1 4522 ? 188.070 178.554 139.581 1.00 66.78  ? 4522 THR A OG1   1 
ATOM   21991 C  CG2   . THR A 1 4522 ? 188.700 180.859 139.290 1.00 60.87  ? 4522 THR A CG2   1 
ATOM   21992 N  N     . ALA A 1 4523 ? 192.228 180.183 140.123 1.00 53.03  ? 4523 ALA A N     1 
ATOM   21993 C  CA    . ALA A 1 4523 ? 193.294 181.175 140.208 1.00 52.29  ? 4523 ALA A CA    1 
ATOM   21994 C  C     . ALA A 1 4523 ? 194.392 180.904 139.187 1.00 56.07  ? 4523 ALA A C     1 
ATOM   21995 O  O     . ALA A 1 4523 ? 194.931 181.840 138.591 1.00 62.64  ? 4523 ALA A O     1 
ATOM   21996 C  CB    . ALA A 1 4523 ? 193.872 181.203 141.622 1.00 49.22  ? 4523 ALA A CB    1 
ATOM   21997 N  N     . THR A 1 4524 ? 194.748 179.634 138.982 1.00 54.86  ? 4524 THR A N     1 
ATOM   21998 C  CA    . THR A 1 4524 ? 195.745 179.303 137.967 1.00 54.14  ? 4524 THR A CA    1 
ATOM   21999 C  C     . THR A 1 4524 ? 195.251 179.666 136.572 1.00 57.72  ? 4524 THR A C     1 
ATOM   22000 O  O     . THR A 1 4524 ? 196.003 180.224 135.760 1.00 66.51  ? 4524 THR A O     1 
ATOM   22001 C  CB    . THR A 1 4524 ? 196.099 177.818 138.035 1.00 50.89  ? 4524 THR A CB    1 
ATOM   22002 O  OG1   . THR A 1 4524 ? 194.903 177.034 137.936 1.00 50.15  ? 4524 THR A OG1   1 
ATOM   22003 C  CG2   . THR A 1 4524 ? 196.807 177.496 139.339 1.00 50.92  ? 4524 THR A CG2   1 
ATOM   22004 N  N     . ARG A 1 4525 ? 193.985 179.358 136.277 1.00 54.99  ? 4525 ARG A N     1 
ATOM   22005 C  CA    . ARG A 1 4525 ? 193.427 179.721 134.978 1.00 58.31  ? 4525 ARG A CA    1 
ATOM   22006 C  C     . ARG A 1 4525 ? 193.419 181.235 134.789 1.00 62.80  ? 4525 ARG A C     1 
ATOM   22007 O  O     . ARG A 1 4525 ? 193.770 181.740 133.714 1.00 65.74  ? 4525 ARG A O     1 
ATOM   22008 C  CB    . ARG A 1 4525 ? 192.018 179.147 134.842 1.00 55.63  ? 4525 ARG A CB    1 
ATOM   22009 C  CG    . ARG A 1 4525 ? 191.499 179.075 133.420 1.00 60.31  ? 4525 ARG A CG    1 
ATOM   22010 C  CD    . ARG A 1 4525 ? 189.997 178.872 133.415 1.00 59.06  ? 4525 ARG A CD    1 
ATOM   22011 N  NE    . ARG A 1 4525 ? 189.511 178.308 132.162 1.00 66.69  ? 4525 ARG A NE    1 
ATOM   22012 C  CZ    . ARG A 1 4525 ? 188.646 177.306 132.080 1.00 73.12  ? 4525 ARG A CZ    1 
ATOM   22013 N  NH1   . ARG A 1 4525 ? 188.149 176.732 133.163 1.00 70.48  ? 4525 ARG A NH1   1 
ATOM   22014 N  NH2   . ARG A 1 4525 ? 188.267 176.872 130.882 1.00 78.52  ? 4525 ARG A NH2   1 
ATOM   22015 N  N     . GLN A 1 4526 ? 193.033 181.975 135.833 1.00 60.94  ? 4526 GLN A N     1 
ATOM   22016 C  CA    . GLN A 1 4526 ? 193.056 183.432 135.774 1.00 58.29  ? 4526 GLN A CA    1 
ATOM   22017 C  C     . GLN A 1 4526 ? 194.466 183.962 135.563 1.00 64.51  ? 4526 GLN A C     1 
ATOM   22018 O  O     . GLN A 1 4526 ? 194.669 184.914 134.802 1.00 74.47  ? 4526 GLN A O     1 
ATOM   22019 C  CB    . GLN A 1 4526 ? 192.458 184.020 137.053 1.00 63.52  ? 4526 GLN A CB    1 
ATOM   22020 C  CG    . GLN A 1 4526 ? 190.932 184.077 137.137 1.00 65.55  ? 4526 GLN A CG    1 
ATOM   22021 C  CD    . GLN A 1 4526 ? 190.281 184.912 136.039 1.00 68.75  ? 4526 GLN A CD    1 
ATOM   22022 O  OE1   . GLN A 1 4526 ? 190.544 184.738 134.849 1.00 67.52  ? 4526 GLN A OE1   1 
ATOM   22023 N  NE2   . GLN A 1 4526 ? 189.441 185.852 136.450 1.00 69.09  ? 4526 GLN A NE2   1 
ATOM   22024 N  N     . TYR A 1 4527 ? 195.451 183.378 136.248 1.00 64.52  ? 4527 TYR A N     1 
ATOM   22025 C  CA    . TYR A 1 4527 ? 196.827 183.835 136.094 1.00 65.48  ? 4527 TYR A CA    1 
ATOM   22026 C  C     . TYR A 1 4527 ? 197.311 183.622 134.669 1.00 65.80  ? 4527 TYR A C     1 
ATOM   22027 O  O     . TYR A 1 4527 ? 197.946 184.508 134.089 1.00 73.57  ? 4527 TYR A O     1 
ATOM   22028 C  CB    . TYR A 1 4527 ? 197.737 183.120 137.096 1.00 62.72  ? 4527 TYR A CB    1 
ATOM   22029 C  CG    . TYR A 1 4527 ? 199.222 183.250 136.812 1.00 69.05  ? 4527 TYR A CG    1 
ATOM   22030 C  CD1   . TYR A 1 4527 ? 199.874 182.370 135.955 1.00 70.16  ? 4527 TYR A CD1   1 
ATOM   22031 C  CD2   . TYR A 1 4527 ? 199.971 184.261 137.401 1.00 70.42  ? 4527 TYR A CD2   1 
ATOM   22032 C  CE1   . TYR A 1 4527 ? 201.225 182.491 135.696 1.00 72.25  ? 4527 TYR A CE1   1 
ATOM   22033 C  CE2   . TYR A 1 4527 ? 201.324 184.389 137.147 1.00 72.73  ? 4527 TYR A CE2   1 
ATOM   22034 C  CZ    . TYR A 1 4527 ? 201.945 183.502 136.294 1.00 76.33  ? 4527 TYR A CZ    1 
ATOM   22035 O  OH    . TYR A 1 4527 ? 203.291 183.626 136.038 1.00 82.63  ? 4527 TYR A OH    1 
ATOM   22036 N  N     . VAL A 1 4528 ? 197.013 182.459 134.087 1.00 62.41  ? 4528 VAL A N     1 
ATOM   22037 C  CA    . VAL A 1 4528 ? 197.412 182.212 132.703 1.00 65.18  ? 4528 VAL A CA    1 
ATOM   22038 C  C     . VAL A 1 4528 ? 196.737 183.209 131.769 1.00 77.82  ? 4528 VAL A C     1 
ATOM   22039 O  O     . VAL A 1 4528 ? 197.388 183.821 130.908 1.00 83.40  ? 4528 VAL A O     1 
ATOM   22040 C  CB    . VAL A 1 4528 ? 197.097 180.759 132.305 1.00 62.00  ? 4528 VAL A CB    1 
ATOM   22041 C  CG1   . VAL A 1 4528 ? 197.173 180.595 130.795 1.00 68.86  ? 4528 VAL A CG1   1 
ATOM   22042 C  CG2   . VAL A 1 4528 ? 198.053 179.804 132.995 1.00 64.17  ? 4528 VAL A CG2   1 
ATOM   22043 N  N     . ALA A 1 4529 ? 195.426 183.409 131.942 1.00 78.20  ? 4529 ALA A N     1 
ATOM   22044 C  CA    . ALA A 1 4529 ? 194.687 184.303 131.056 1.00 77.37  ? 4529 ALA A CA    1 
ATOM   22045 C  C     . ALA A 1 4529 ? 195.196 185.736 131.156 1.00 82.16  ? 4529 ALA A C     1 
ATOM   22046 O  O     . ALA A 1 4529 ? 195.314 186.431 130.141 1.00 82.96  ? 4529 ALA A O     1 
ATOM   22047 C  CB    . ALA A 1 4529 ? 193.194 184.240 131.374 1.00 73.68  ? 4529 ALA A CB    1 
ATOM   22048 N  N     . GLN A 1 4530 ? 195.499 186.198 132.370 1.00 80.98  ? 4530 GLN A N     1 
ATOM   22049 C  CA    . GLN A 1 4530 ? 195.970 187.568 132.544 1.00 79.16  ? 4530 GLN A CA    1 
ATOM   22050 C  C     . GLN A 1 4530 ? 197.399 187.734 132.042 1.00 84.86  ? 4530 GLN A C     1 
ATOM   22051 O  O     . GLN A 1 4530 ? 197.728 188.749 131.417 1.00 89.47  ? 4530 GLN A O     1 
ATOM   22052 C  CB    . GLN A 1 4530 ? 195.862 187.977 134.013 1.00 77.01  ? 4530 GLN A CB    1 
ATOM   22053 C  CG    . GLN A 1 4530 ? 196.684 189.202 134.382 1.00 86.22  ? 4530 GLN A CG    1 
ATOM   22054 C  CD    . GLN A 1 4530 ? 196.436 189.665 135.804 1.00 88.09  ? 4530 GLN A CD    1 
ATOM   22055 O  OE1   . GLN A 1 4530 ? 196.300 188.853 136.718 1.00 89.13  ? 4530 GLN A OE1   1 
ATOM   22056 N  NE2   . GLN A 1 4530 ? 196.376 190.977 135.997 1.00 85.78  ? 4530 GLN A NE2   1 
ATOM   22057 N  N     . ALA A 1 4531 ? 198.264 186.748 132.300 1.00 83.18  ? 4531 ALA A N     1 
ATOM   22058 C  CA    . ALA A 1 4531 ? 199.647 186.842 131.851 1.00 84.48  ? 4531 ALA A CA    1 
ATOM   22059 C  C     . ALA A 1 4531 ? 199.747 186.839 130.334 1.00 86.32  ? 4531 ALA A C     1 
ATOM   22060 O  O     . ALA A 1 4531 ? 200.552 187.586 129.767 1.00 90.16  ? 4531 ALA A O     1 
ATOM   22061 C  CB    . ALA A 1 4531 ? 200.470 185.696 132.440 1.00 80.30  ? 4531 ALA A CB    1 
ATOM   22062 N  N     . ASN A 1 4532 ? 198.947 186.015 129.658 1.00 83.31  ? 4532 ASN A N     1 
ATOM   22063 C  CA    . ASN A 1 4532 ? 198.987 185.953 128.204 1.00 88.72  ? 4532 ASN A CA    1 
ATOM   22064 C  C     . ASN A 1 4532 ? 197.904 186.787 127.534 1.00 94.59  ? 4532 ASN A C     1 
ATOM   22065 O  O     . ASN A 1 4532 ? 197.789 186.749 126.305 1.00 95.17  ? 4532 ASN A O     1 
ATOM   22066 C  CB    . ASN A 1 4532 ? 198.893 184.498 127.733 1.00 89.13  ? 4532 ASN A CB    1 
ATOM   22067 C  CG    . ASN A 1 4532 ? 200.247 183.816 127.686 1.00 95.46  ? 4532 ASN A CG    1 
ATOM   22068 O  OD1   . ASN A 1 4532 ? 200.439 182.747 128.265 1.00 100.19 ? 4532 ASN A OD1   1 
ATOM   22069 N  ND2   . ASN A 1 4532 ? 201.197 184.437 126.996 1.00 93.40  ? 4532 ASN A ND2   1 
ATOM   22070 N  N     . SER A 1 4533 ? 197.124 187.551 128.304 1.00 96.59  ? 4533 SER A N     1 
ATOM   22071 C  CA    . SER A 1 4533 ? 196.051 188.393 127.766 1.00 96.34  ? 4533 SER A CA    1 
ATOM   22072 C  C     . SER A 1 4533 ? 195.043 187.568 126.967 1.00 93.71  ? 4533 SER A C     1 
ATOM   22073 O  O     . SER A 1 4533 ? 194.526 188.009 125.938 1.00 91.14  ? 4533 SER A O     1 
ATOM   22074 C  CB    . SER A 1 4533 ? 196.613 189.537 126.919 1.00 91.80  ? 4533 SER A CB    1 
ATOM   22075 O  OG    . SER A 1 4533 ? 197.396 190.417 127.707 1.00 89.35  ? 4533 SER A OG    1 
ATOM   22076 N  N     . TRP A 1 4534 ? 194.761 186.360 127.446 1.00 91.74  ? 4534 TRP A N     1 
ATOM   22077 C  CA    . TRP A 1 4534 ? 193.814 185.458 126.813 1.00 89.64  ? 4534 TRP A CA    1 
ATOM   22078 C  C     . TRP A 1 4534 ? 192.454 185.555 127.503 1.00 91.20  ? 4534 TRP A C     1 
ATOM   22079 O  O     . TRP A 1 4534 ? 192.241 186.358 128.414 1.00 92.61  ? 4534 TRP A O     1 
ATOM   22080 C  CB    . TRP A 1 4534 ? 194.349 184.026 126.835 1.00 90.36  ? 4534 TRP A CB    1 
ATOM   22081 C  CG    . TRP A 1 4534 ? 195.539 183.823 125.952 1.00 91.67  ? 4534 TRP A CG    1 
ATOM   22082 C  CD1   . TRP A 1 4534 ? 196.058 184.716 125.062 1.00 91.99  ? 4534 TRP A CD1   1 
ATOM   22083 C  CD2   . TRP A 1 4534 ? 196.372 182.659 125.884 1.00 94.56  ? 4534 TRP A CD2   1 
ATOM   22084 N  NE1   . TRP A 1 4534 ? 197.157 184.178 124.437 1.00 95.52  ? 4534 TRP A NE1   1 
ATOM   22085 C  CE2   . TRP A 1 4534 ? 197.371 182.916 124.925 1.00 94.08  ? 4534 TRP A CE2   1 
ATOM   22086 C  CE3   . TRP A 1 4534 ? 196.367 181.424 126.539 1.00 93.08  ? 4534 TRP A CE3   1 
ATOM   22087 C  CZ2   . TRP A 1 4534 ? 198.354 181.984 124.604 1.00 92.38  ? 4534 TRP A CZ2   1 
ATOM   22088 C  CZ3   . TRP A 1 4534 ? 197.344 180.500 126.219 1.00 92.60  ? 4534 TRP A CZ3   1 
ATOM   22089 C  CH2   . TRP A 1 4534 ? 198.324 180.785 125.260 1.00 95.97  ? 4534 TRP A CH2   1 
ATOM   22090 N  N     . SER A 1 4535 ? 191.522 184.720 127.055 1.00 91.99  ? 4535 SER A N     1 
ATOM   22091 C  CA    . SER A 1 4535 ? 190.161 184.712 127.570 1.00 91.03  ? 4535 SER A CA    1 
ATOM   22092 C  C     . SER A 1 4535 ? 189.953 183.517 128.491 1.00 96.69  ? 4535 SER A C     1 
ATOM   22093 O  O     . SER A 1 4535 ? 190.455 182.420 128.228 1.00 102.29 ? 4535 SER A O     1 
ATOM   22094 C  CB    . SER A 1 4535 ? 189.145 184.676 126.427 1.00 84.36  ? 4535 SER A CB    1 
ATOM   22095 O  OG    . SER A 1 4535 ? 187.832 184.904 126.907 1.00 89.39  ? 4535 SER A OG    1 
ATOM   22096 N  N     . LEU A 1 4536 ? 189.211 183.743 129.577 1.00 89.36  ? 4536 LEU A N     1 
ATOM   22097 C  CA    . LEU A 1 4536 ? 188.965 182.686 130.553 1.00 86.00  ? 4536 LEU A CA    1 
ATOM   22098 C  C     . LEU A 1 4536 ? 188.186 181.531 129.935 1.00 85.32  ? 4536 LEU A C     1 
ATOM   22099 O  O     . LEU A 1 4536 ? 188.540 180.361 130.115 1.00 84.59  ? 4536 LEU A O     1 
ATOM   22100 C  CB    . LEU A 1 4536 ? 188.225 183.270 131.758 1.00 82.86  ? 4536 LEU A CB    1 
ATOM   22101 C  CG    . LEU A 1 4536 ? 188.238 182.579 133.123 1.00 77.39  ? 4536 LEU A CG    1 
ATOM   22102 C  CD1   . LEU A 1 4536 ? 187.600 183.503 134.121 1.00 74.26  ? 4536 LEU A CD1   1 
ATOM   22103 C  CD2   . LEU A 1 4536 ? 187.473 181.268 133.106 1.00 74.27  ? 4536 LEU A CD2   1 
ATOM   22104 N  N     . GLU A 1 4537 ? 187.121 181.841 129.197 1.00 82.19  ? 4537 GLU A N     1 
ATOM   22105 C  CA    . GLU A 1 4537 ? 186.314 180.805 128.567 1.00 90.52  ? 4537 GLU A CA    1 
ATOM   22106 C  C     . GLU A 1 4537 ? 187.007 180.151 127.379 1.00 92.95  ? 4537 GLU A C     1 
ATOM   22107 O  O     . GLU A 1 4537 ? 186.501 179.148 126.862 1.00 93.09  ? 4537 GLU A O     1 
ATOM   22108 C  CB    . GLU A 1 4537 ? 184.963 181.382 128.133 1.00 93.61  ? 4537 GLU A CB    1 
ATOM   22109 C  CG    . GLU A 1 4537 ? 185.013 182.233 126.876 1.00 92.75  ? 4537 GLU A CG    1 
ATOM   22110 C  CD    . GLU A 1 4537 ? 185.042 183.718 127.186 1.00 92.54  ? 4537 GLU A CD    1 
ATOM   22111 O  OE1   . GLU A 1 4537 ? 185.124 184.075 128.380 1.00 86.72  ? 4537 GLU A OE1   1 
ATOM   22112 O  OE2   . GLU A 1 4537 ? 184.981 184.527 126.237 1.00 92.29  ? 4537 GLU A OE2   1 
ATOM   22113 N  N     . GLU A 1 4538 ? 188.142 180.687 126.938 1.00 91.21  ? 4538 GLU A N     1 
ATOM   22114 C  CA    . GLU A 1 4538 ? 188.900 180.130 125.827 1.00 94.70  ? 4538 GLU A CA    1 
ATOM   22115 C  C     . GLU A 1 4538 ? 189.949 179.118 126.277 1.00 92.95  ? 4538 GLU A C     1 
ATOM   22116 O  O     . GLU A 1 4538 ? 190.604 178.504 125.428 1.00 93.54  ? 4538 GLU A O     1 
ATOM   22117 C  CB    . GLU A 1 4538 ? 189.571 181.265 125.042 1.00 94.55  ? 4538 GLU A CB    1 
ATOM   22118 C  CG    . GLU A 1 4538 ? 189.990 180.912 123.623 1.00 100.67 ? 4538 GLU A CG    1 
ATOM   22119 C  CD    . GLU A 1 4538 ? 188.928 180.129 122.879 1.00 106.57 ? 4538 GLU A CD    1 
ATOM   22120 O  OE1   . GLU A 1 4538 ? 187.927 180.740 122.451 1.00 110.48 ? 4538 GLU A OE1   1 
ATOM   22121 O  OE2   . GLU A 1 4538 ? 189.096 178.902 122.718 1.00 104.95 ? 4538 GLU A OE2   1 
ATOM   22122 N  N     . LEU A 1 4539 ? 190.112 178.914 127.581 1.00 88.09  ? 4539 LEU A N     1 
ATOM   22123 C  CA    . LEU A 1 4539 ? 191.183 178.087 128.119 1.00 82.45  ? 4539 LEU A CA    1 
ATOM   22124 C  C     . LEU A 1 4539 ? 190.683 176.687 128.451 1.00 83.95  ? 4539 LEU A C     1 
ATOM   22125 O  O     . LEU A 1 4539 ? 189.538 176.506 128.874 1.00 88.15  ? 4539 LEU A O     1 
ATOM   22126 C  CB    . LEU A 1 4539 ? 191.786 178.728 129.370 1.00 70.97  ? 4539 LEU A CB    1 
ATOM   22127 C  CG    . LEU A 1 4539 ? 192.597 180.006 129.158 1.00 77.21  ? 4539 LEU A CG    1 
ATOM   22128 C  CD1   . LEU A 1 4539 ? 193.398 180.345 130.404 1.00 74.76  ? 4539 LEU A CD1   1 
ATOM   22129 C  CD2   . LEU A 1 4539 ? 193.513 179.860 127.955 1.00 82.95  ? 4539 LEU A CD2   1 
ATOM   22130 N  N     . CYS A 1 4540 ? 191.556 175.700 128.255 1.00 77.26  ? 4540 CYS A N     1 
ATOM   22131 C  CA    . CYS A 1 4540 ? 191.297 174.319 128.634 1.00 68.59  ? 4540 CYS A CA    1 
ATOM   22132 C  C     . CYS A 1 4540 ? 192.515 173.769 129.362 1.00 70.74  ? 4540 CYS A C     1 
ATOM   22133 O  O     . CYS A 1 4540 ? 193.639 174.242 129.169 1.00 77.10  ? 4540 CYS A O     1 
ATOM   22134 C  CB    . CYS A 1 4540 ? 190.967 173.446 127.417 1.00 75.03  ? 4540 CYS A CB    1 
ATOM   22135 S  SG    . CYS A 1 4540 ? 192.270 173.361 126.172 1.00 78.43  ? 4540 CYS A SG    1 
ATOM   22136 N  N     . LEU A 1 4541 ? 192.284 172.763 130.201 1.00 64.60  ? 4541 LEU A N     1 
ATOM   22137 C  CA    . LEU A 1 4541 ? 193.316 172.254 131.093 1.00 57.46  ? 4541 LEU A CA    1 
ATOM   22138 C  C     . LEU A 1 4541 ? 193.958 171.004 130.503 1.00 55.29  ? 4541 LEU A C     1 
ATOM   22139 O  O     . LEU A 1 4541 ? 193.267 170.086 130.053 1.00 56.60  ? 4541 LEU A O     1 
ATOM   22140 C  CB    . LEU A 1 4541 ? 192.718 171.955 132.472 1.00 57.07  ? 4541 LEU A CB    1 
ATOM   22141 C  CG    . LEU A 1 4541 ? 193.574 171.709 133.725 1.00 52.19  ? 4541 LEU A CG    1 
ATOM   22142 C  CD1   . LEU A 1 4541 ? 192.670 171.654 134.946 1.00 52.51  ? 4541 LEU A CD1   1 
ATOM   22143 C  CD2   . LEU A 1 4541 ? 194.408 170.440 133.658 1.00 52.39  ? 4541 LEU A CD2   1 
ATOM   22144 N  N     . GLU A 1 4542 ? 195.290 170.980 130.509 1.00 56.90  ? 4542 GLU A N     1 
ATOM   22145 C  CA    . GLU A 1 4542 ? 196.069 169.825 130.092 1.00 56.04  ? 4542 GLU A CA    1 
ATOM   22146 C  C     . GLU A 1 4542 ? 196.845 169.280 131.284 1.00 54.57  ? 4542 GLU A C     1 
ATOM   22147 O  O     . GLU A 1 4542 ? 197.302 170.037 132.145 1.00 58.72  ? 4542 GLU A O     1 
ATOM   22148 C  CB    . GLU A 1 4542 ? 197.034 170.178 128.955 1.00 60.72  ? 4542 GLU A CB    1 
ATOM   22149 C  CG    . GLU A 1 4542 ? 196.436 170.026 127.567 1.00 68.90  ? 4542 GLU A CG    1 
ATOM   22150 C  CD    . GLU A 1 4542 ? 197.485 169.754 126.508 1.00 79.54  ? 4542 GLU A CD    1 
ATOM   22151 O  OE1   . GLU A 1 4542 ? 198.484 170.500 126.453 1.00 83.59  ? 4542 GLU A OE1   1 
ATOM   22152 O  OE2   . GLU A 1 4542 ? 197.309 168.793 125.730 1.00 82.27  ? 4542 GLU A OE2   1 
ATOM   22153 N  N     . VAL A 1 4543 ? 196.993 167.958 131.325 1.00 57.53  ? 4543 VAL A N     1 
ATOM   22154 C  CA    . VAL A 1 4543 ? 197.577 167.261 132.465 1.00 55.78  ? 4543 VAL A CA    1 
ATOM   22155 C  C     . VAL A 1 4543 ? 198.854 166.564 132.017 1.00 60.02  ? 4543 VAL A C     1 
ATOM   22156 O  O     . VAL A 1 4543 ? 198.863 165.871 130.993 1.00 61.23  ? 4543 VAL A O     1 
ATOM   22157 C  CB    . VAL A 1 4543 ? 196.592 166.248 133.073 1.00 49.50  ? 4543 VAL A CB    1 
ATOM   22158 C  CG1   . VAL A 1 4543 ? 197.159 165.659 134.353 1.00 49.77  ? 4543 VAL A CG1   1 
ATOM   22159 C  CG2   . VAL A 1 4543 ? 195.252 166.909 133.331 1.00 49.02  ? 4543 VAL A CG2   1 
ATOM   22160 N  N     . ASN A 1 4544 ? 199.926 166.750 132.784 1.00 55.35  ? 4544 ASN A N     1 
ATOM   22161 C  CA    . ASN A 1 4544 ? 201.202 166.085 132.532 1.00 59.90  ? 4544 ASN A CA    1 
ATOM   22162 C  C     . ASN A 1 4544 ? 201.742 165.593 133.867 1.00 60.30  ? 4544 ASN A C     1 
ATOM   22163 O  O     . ASN A 1 4544 ? 202.019 166.399 134.760 1.00 64.67  ? 4544 ASN A O     1 
ATOM   22164 C  CB    . ASN A 1 4544 ? 202.194 167.027 131.850 1.00 62.03  ? 4544 ASN A CB    1 
ATOM   22165 C  CG    . ASN A 1 4544 ? 203.567 166.407 131.685 1.00 63.54  ? 4544 ASN A CG    1 
ATOM   22166 O  OD1   . ASN A 1 4544 ? 204.581 167.024 132.008 1.00 67.41  ? 4544 ASN A OD1   1 
ATOM   22167 N  ND2   . ASN A 1 4544 ? 203.606 165.181 131.177 1.00 60.67  ? 4544 ASN A ND2   1 
ATOM   22168 N  N     . VAL A 1 4545 ? 201.889 164.278 134.005 1.00 63.77  ? 4545 VAL A N     1 
ATOM   22169 C  CA    . VAL A 1 4545 ? 202.351 163.659 135.242 1.00 65.44  ? 4545 VAL A CA    1 
ATOM   22170 C  C     . VAL A 1 4545 ? 203.820 163.295 135.075 1.00 73.26  ? 4545 VAL A C     1 
ATOM   22171 O  O     . VAL A 1 4545 ? 204.172 162.476 134.218 1.00 77.27  ? 4545 VAL A O     1 
ATOM   22172 C  CB    . VAL A 1 4545 ? 201.513 162.422 135.598 1.00 60.27  ? 4545 VAL A CB    1 
ATOM   22173 C  CG1   . VAL A 1 4545 ? 202.126 161.689 136.780 1.00 56.79  ? 4545 VAL A CG1   1 
ATOM   22174 C  CG2   . VAL A 1 4545 ? 200.079 162.824 135.901 1.00 62.55  ? 4545 VAL A CG2   1 
ATOM   22175 N  N     . THR A 1 4546 ? 204.677 163.901 135.896 1.00 73.59  ? 4546 THR A N     1 
ATOM   22176 C  CA    . THR A 1 4546 ? 206.114 163.674 135.839 1.00 77.90  ? 4546 THR A CA    1 
ATOM   22177 C  C     . THR A 1 4546 ? 206.664 163.567 137.255 1.00 80.96  ? 4546 THR A C     1 
ATOM   22178 O  O     . THR A 1 4546 ? 205.968 163.826 138.240 1.00 78.66  ? 4546 THR A O     1 
ATOM   22179 C  CB    . THR A 1 4546 ? 206.840 164.792 135.077 1.00 86.57  ? 4546 THR A CB    1 
ATOM   22180 O  OG1   . THR A 1 4546 ? 206.546 166.056 135.685 1.00 85.38  ? 4546 THR A OG1   1 
ATOM   22181 C  CG2   . THR A 1 4546 ? 206.424 164.819 133.613 1.00 80.31  ? 4546 THR A CG2   1 
ATOM   22182 N  N     . THR A 1 4547 ? 207.933 163.175 137.345 1.00 94.12  ? 4547 THR A N     1 
ATOM   22183 C  CA    . THR A 1 4547 ? 208.618 163.115 138.628 1.00 99.87  ? 4547 THR A CA    1 
ATOM   22184 C  C     . THR A 1 4547 ? 208.825 164.524 139.179 1.00 100.30 ? 4547 THR A C     1 
ATOM   22185 O  O     . THR A 1 4547 ? 209.054 165.479 138.432 1.00 102.26 ? 4547 THR A O     1 
ATOM   22186 C  CB    . THR A 1 4547 ? 209.961 162.395 138.476 1.00 107.28 ? 4547 THR A CB    1 
ATOM   22187 O  OG1   . THR A 1 4547 ? 209.737 161.070 137.977 1.00 107.25 ? 4547 THR A OG1   1 
ATOM   22188 C  CG2   . THR A 1 4547 ? 210.687 162.298 139.811 1.00 101.23 ? 4547 THR A CG2   1 
ATOM   22189 N  N     . SER A 1 4548 ? 208.729 164.647 140.506 1.00 95.73  ? 4548 SER A N     1 
ATOM   22190 C  CA    . SER A 1 4548 ? 208.815 165.959 141.144 1.00 99.28  ? 4548 SER A CA    1 
ATOM   22191 C  C     . SER A 1 4548 ? 210.158 166.627 140.871 1.00 109.06 ? 4548 SER A C     1 
ATOM   22192 O  O     . SER A 1 4548 ? 210.214 167.804 140.496 1.00 104.56 ? 4548 SER A O     1 
ATOM   22193 C  CB    . SER A 1 4548 ? 208.577 165.823 142.648 1.00 90.23  ? 4548 SER A CB    1 
ATOM   22194 O  OG    . SER A 1 4548 ? 208.575 167.090 143.281 1.00 88.97  ? 4548 SER A OG    1 
ATOM   22195 N  N     . GLN A 1 4549 ? 211.255 165.891 141.055 1.00 116.16 ? 4549 GLN A N     1 
ATOM   22196 C  CA    . GLN A 1 4549 ? 212.574 166.471 140.822 1.00 115.27 ? 4549 GLN A CA    1 
ATOM   22197 C  C     . GLN A 1 4549 ? 212.870 166.622 139.335 1.00 117.91 ? 4549 GLN A C     1 
ATOM   22198 O  O     . GLN A 1 4549 ? 213.406 167.651 138.909 1.00 122.11 ? 4549 GLN A O     1 
ATOM   22199 C  CB    . GLN A 1 4549 ? 213.652 165.621 141.496 1.00 119.95 ? 4549 GLN A CB    1 
ATOM   22200 C  CG    . GLN A 1 4549 ? 215.013 166.294 141.560 1.00 124.49 ? 4549 GLN A CG    1 
ATOM   22201 C  CD    . GLN A 1 4549 ? 214.931 167.733 142.034 1.00 127.59 ? 4549 GLN A CD    1 
ATOM   22202 O  OE1   . GLN A 1 4549 ? 215.237 168.663 141.288 1.00 130.62 ? 4549 GLN A OE1   1 
ATOM   22203 N  NE2   . GLN A 1 4549 ? 214.515 167.922 143.281 1.00 123.46 ? 4549 GLN A NE2   1 
ATOM   22204 N  N     . GLY A 1 4550 ? 212.532 165.614 138.535 1.00 115.82 ? 4550 GLY A N     1 
ATOM   22205 C  CA    . GLY A 1 4550 ? 212.793 165.666 137.110 1.00 117.40 ? 4550 GLY A CA    1 
ATOM   22206 C  C     . GLY A 1 4550 ? 211.655 166.266 136.312 1.00 118.19 ? 4550 GLY A C     1 
ATOM   22207 O  O     . GLY A 1 4550 ? 210.988 165.563 135.546 1.00 109.58 ? 4550 GLY A O     1 
ATOM   22208 N  N     . ALA A 1 4551 ? 211.421 167.565 136.481 1.00 121.44 ? 4551 ALA A N     1 
ATOM   22209 C  CA    . ALA A 1 4551 ? 210.353 168.242 135.761 1.00 117.57 ? 4551 ALA A CA    1 
ATOM   22210 C  C     . ALA A 1 4551 ? 210.684 169.722 135.651 1.00 120.40 ? 4551 ALA A C     1 
ATOM   22211 O  O     . ALA A 1 4551 ? 211.485 170.259 136.422 1.00 118.04 ? 4551 ALA A O     1 
ATOM   22212 C  CB    . ALA A 1 4551 ? 208.998 168.045 136.448 1.00 109.53 ? 4551 ALA A CB    1 
ATOM   22213 N  N     . THR A 1 4552 ? 210.052 170.373 134.677 1.00 121.40 ? 4552 THR A N     1 
ATOM   22214 C  CA    . THR A 1 4552 ? 210.184 171.806 134.467 1.00 119.69 ? 4552 THR A CA    1 
ATOM   22215 C  C     . THR A 1 4552 ? 208.803 172.413 134.273 1.00 110.74 ? 4552 THR A C     1 
ATOM   22216 O  O     . THR A 1 4552 ? 207.884 171.759 133.772 1.00 106.26 ? 4552 THR A O     1 
ATOM   22217 C  CB    . THR A 1 4552 ? 211.067 172.129 133.250 1.00 122.80 ? 4552 THR A CB    1 
ATOM   22218 O  OG1   . THR A 1 4552 ? 210.589 171.411 132.106 1.00 124.72 ? 4552 THR A OG1   1 
ATOM   22219 C  CG2   . THR A 1 4552 ? 212.514 171.745 133.520 1.00 126.76 ? 4552 THR A CG2   1 
ATOM   22220 N  N     . LEU A 1 4553 ? 208.665 173.673 134.677 1.00 104.14 ? 4553 LEU A N     1 
ATOM   22221 C  CA    . LEU A 1 4553 ? 207.408 174.401 134.573 1.00 92.57  ? 4553 LEU A CA    1 
ATOM   22222 C  C     . LEU A 1 4553 ? 207.603 175.614 133.676 1.00 88.88  ? 4553 LEU A C     1 
ATOM   22223 O  O     . LEU A 1 4553 ? 208.512 176.419 133.905 1.00 92.28  ? 4553 LEU A O     1 
ATOM   22224 C  CB    . LEU A 1 4553 ? 206.903 174.840 135.952 1.00 90.15  ? 4553 LEU A CB    1 
ATOM   22225 C  CG    . LEU A 1 4553 ? 206.091 173.843 136.785 1.00 83.54  ? 4553 LEU A CG    1 
ATOM   22226 C  CD1   . LEU A 1 4553 ? 206.942 172.669 137.247 1.00 83.95  ? 4553 LEU A CD1   1 
ATOM   22227 C  CD2   . LEU A 1 4553 ? 205.451 174.543 137.974 1.00 77.12  ? 4553 LEU A CD2   1 
ATOM   22228 N  N     . ASP A 1 4554 ? 206.754 175.741 132.661 1.00 82.81  ? 4554 ASP A N     1 
ATOM   22229 C  CA    . ASP A 1 4554 ? 206.771 176.905 131.789 1.00 83.55  ? 4554 ASP A CA    1 
ATOM   22230 C  C     . ASP A 1 4554 ? 205.810 177.958 132.340 1.00 77.26  ? 4554 ASP A C     1 
ATOM   22231 O  O     . ASP A 1 4554 ? 205.351 177.873 133.481 1.00 76.70  ? 4554 ASP A O     1 
ATOM   22232 C  CB    . ASP A 1 4554 ? 206.448 176.501 130.349 1.00 88.67  ? 4554 ASP A CB    1 
ATOM   22233 C  CG    . ASP A 1 4554 ? 205.056 175.909 130.193 1.00 89.62  ? 4554 ASP A CG    1 
ATOM   22234 O  OD1   . ASP A 1 4554 ? 204.339 175.756 131.203 1.00 87.66  ? 4554 ASP A OD1   1 
ATOM   22235 O  OD2   . ASP A 1 4554 ? 204.676 175.595 129.046 1.00 87.59  ? 4554 ASP A OD2   1 
ATOM   22236 N  N     . ALA A 1 4555 ? 205.498 178.970 131.530 1.00 76.87  ? 4555 ALA A N     1 
ATOM   22237 C  CA    . ALA A 1 4555 ? 204.620 180.047 131.968 1.00 78.33  ? 4555 ALA A CA    1 
ATOM   22238 C  C     . ALA A 1 4555 ? 203.193 179.586 132.241 1.00 78.77  ? 4555 ALA A C     1 
ATOM   22239 O  O     . ALA A 1 4555 ? 202.436 180.328 132.876 1.00 79.51  ? 4555 ALA A O     1 
ATOM   22240 C  CB    . ALA A 1 4555 ? 204.606 181.167 130.927 1.00 76.92  ? 4555 ALA A CB    1 
ATOM   22241 N  N     . CYS A 1 4556 ? 202.806 178.395 131.783 1.00 77.53  ? 4556 CYS A N     1 
ATOM   22242 C  CA    . CYS A 1 4556 ? 201.442 177.906 131.951 1.00 75.77  ? 4556 CYS A CA    1 
ATOM   22243 C  C     . CYS A 1 4556 ? 201.363 176.619 132.763 1.00 70.92  ? 4556 CYS A C     1 
ATOM   22244 O  O     . CYS A 1 4556 ? 200.291 176.007 132.825 1.00 71.80  ? 4556 CYS A O     1 
ATOM   22245 C  CB    . CYS A 1 4556 ? 200.784 177.697 130.583 1.00 74.20  ? 4556 CYS A CB    1 
ATOM   22246 S  SG    . CYS A 1 4556 ? 200.447 179.221 129.675 1.00 86.70  ? 4556 CYS A SG    1 
ATOM   22247 N  N     . SER A 1 4557 ? 202.456 176.193 133.390 1.00 70.22  ? 4557 SER A N     1 
ATOM   22248 C  CA    . SER A 1 4557 ? 202.495 174.949 134.148 1.00 66.57  ? 4557 SER A CA    1 
ATOM   22249 C  C     . SER A 1 4557 ? 202.461 175.251 135.639 1.00 62.32  ? 4557 SER A C     1 
ATOM   22250 O  O     . SER A 1 4557 ? 203.190 176.127 136.117 1.00 71.00  ? 4557 SER A O     1 
ATOM   22251 C  CB    . SER A 1 4557 ? 203.745 174.135 133.809 1.00 72.28  ? 4557 SER A CB    1 
ATOM   22252 O  OG    . SER A 1 4557 ? 203.697 173.656 132.477 1.00 73.06  ? 4557 SER A OG    1 
ATOM   22253 N  N     . PHE A 1 4558 ? 201.616 174.526 136.366 1.00 54.74  ? 4558 PHE A N     1 
ATOM   22254 C  CA    . PHE A 1 4558 ? 201.514 174.641 137.814 1.00 52.60  ? 4558 PHE A CA    1 
ATOM   22255 C  C     . PHE A 1 4558 ? 201.715 173.266 138.432 1.00 55.44  ? 4558 PHE A C     1 
ATOM   22256 O  O     . PHE A 1 4558 ? 201.066 172.298 138.023 1.00 59.81  ? 4558 PHE A O     1 
ATOM   22257 C  CB    . PHE A 1 4558 ? 200.159 175.217 138.231 1.00 47.78  ? 4558 PHE A CB    1 
ATOM   22258 C  CG    . PHE A 1 4558 ? 199.881 176.578 137.665 1.00 55.22  ? 4558 PHE A CG    1 
ATOM   22259 C  CD1   . PHE A 1 4558 ? 199.287 176.716 136.422 1.00 57.68  ? 4558 PHE A CD1   1 
ATOM   22260 C  CD2   . PHE A 1 4558 ? 200.219 177.719 138.371 1.00 58.53  ? 4558 PHE A CD2   1 
ATOM   22261 C  CE1   . PHE A 1 4558 ? 199.030 177.966 135.898 1.00 57.20  ? 4558 PHE A CE1   1 
ATOM   22262 C  CE2   . PHE A 1 4558 ? 199.965 178.972 137.851 1.00 58.20  ? 4558 PHE A CE2   1 
ATOM   22263 C  CZ    . PHE A 1 4558 ? 199.370 179.094 136.613 1.00 56.62  ? 4558 PHE A CZ    1 
ATOM   22264 N  N     . GLY A 1 4559 ? 202.609 173.183 139.415 1.00 56.29  ? 4559 GLY A N     1 
ATOM   22265 C  CA    . GLY A 1 4559 ? 202.910 171.921 140.064 1.00 52.86  ? 4559 GLY A CA    1 
ATOM   22266 C  C     . GLY A 1 4559 ? 201.917 171.620 141.168 1.00 49.06  ? 4559 GLY A C     1 
ATOM   22267 O  O     . GLY A 1 4559 ? 201.672 172.456 142.041 1.00 58.30  ? 4559 GLY A O     1 
ATOM   22268 N  N     . VAL A 1 4560 ? 201.346 170.419 141.123 1.00 44.60  ? 4560 VAL A N     1 
ATOM   22269 C  CA    . VAL A 1 4560 ? 200.371 169.967 142.108 1.00 44.92  ? 4560 VAL A CA    1 
ATOM   22270 C  C     . VAL A 1 4560 ? 200.820 168.616 142.644 1.00 47.81  ? 4560 VAL A C     1 
ATOM   22271 O  O     . VAL A 1 4560 ? 201.078 167.690 141.867 1.00 55.44  ? 4560 VAL A O     1 
ATOM   22272 C  CB    . VAL A 1 4560 ? 198.955 169.871 141.508 1.00 40.59  ? 4560 VAL A CB    1 
ATOM   22273 C  CG1   . VAL A 1 4560 ? 198.043 169.079 142.427 1.00 44.37  ? 4560 VAL A CG1   1 
ATOM   22274 C  CG2   . VAL A 1 4560 ? 198.391 171.259 141.262 1.00 40.73  ? 4560 VAL A CG2   1 
ATOM   22275 N  N     . THR A 1 4561 ? 200.910 168.504 143.964 1.00 46.23  ? 4561 THR A N     1 
ATOM   22276 C  CA    . THR A 1 4561 ? 201.311 167.276 144.632 1.00 49.59  ? 4561 THR A CA    1 
ATOM   22277 C  C     . THR A 1 4561 ? 200.162 166.736 145.474 1.00 51.00  ? 4561 THR A C     1 
ATOM   22278 O  O     . THR A 1 4561 ? 199.183 167.430 145.761 1.00 52.27  ? 4561 THR A O     1 
ATOM   22279 C  CB    . THR A 1 4561 ? 202.546 167.508 145.510 1.00 54.44  ? 4561 THR A CB    1 
ATOM   22280 O  OG1   . THR A 1 4561 ? 202.211 168.394 146.585 1.00 55.22  ? 4561 THR A OG1   1 
ATOM   22281 C  CG2   . THR A 1 4561 ? 203.676 168.115 144.694 1.00 55.53  ? 4561 THR A CG2   1 
ATOM   22282 N  N     . GLY A 1 4562 ? 200.293 165.470 145.868 1.00 49.38  ? 4562 GLY A N     1 
ATOM   22283 C  CA    . GLY A 1 4562 ? 199.319 164.823 146.717 1.00 47.74  ? 4562 GLY A CA    1 
ATOM   22284 C  C     . GLY A 1 4562 ? 198.183 164.134 145.995 1.00 49.25  ? 4562 GLY A C     1 
ATOM   22285 O  O     . GLY A 1 4562 ? 197.374 163.464 146.649 1.00 54.80  ? 4562 GLY A O     1 
ATOM   22286 N  N     . LEU A 1 4563 ? 198.088 164.278 144.676 1.00 47.98  ? 4563 LEU A N     1 
ATOM   22287 C  CA    . LEU A 1 4563 ? 197.031 163.613 143.928 1.00 40.86  ? 4563 LEU A CA    1 
ATOM   22288 C  C     . LEU A 1 4563 ? 197.232 162.103 143.948 1.00 45.72  ? 4563 LEU A C     1 
ATOM   22289 O  O     . LEU A 1 4563 ? 198.347 161.605 143.777 1.00 52.75  ? 4563 LEU A O     1 
ATOM   22290 C  CB    . LEU A 1 4563 ? 196.996 164.119 142.486 1.00 39.39  ? 4563 LEU A CB    1 
ATOM   22291 C  CG    . LEU A 1 4563 ? 196.568 165.572 142.272 1.00 40.66  ? 4563 LEU A CG    1 
ATOM   22292 C  CD1   . LEU A 1 4563 ? 196.230 165.818 140.812 1.00 39.24  ? 4563 LEU A CD1   1 
ATOM   22293 C  CD2   . LEU A 1 4563 ? 195.387 165.923 143.163 1.00 41.60  ? 4563 LEU A CD2   1 
ATOM   22294 N  N     . LYS A 1 4564 ? 196.140 161.374 144.160 1.00 42.90  ? 4564 LYS A N     1 
ATOM   22295 C  CA    . LYS A 1 4564 ? 196.156 159.920 144.216 1.00 44.54  ? 4564 LYS A CA    1 
ATOM   22296 C  C     . LYS A 1 4564 ? 195.263 159.367 143.115 1.00 37.79  ? 4564 LYS A C     1 
ATOM   22297 O  O     . LYS A 1 4564 ? 194.129 159.825 142.944 1.00 38.24  ? 4564 LYS A O     1 
ATOM   22298 C  CB    . LYS A 1 4564 ? 195.691 159.415 145.584 1.00 45.27  ? 4564 LYS A CB    1 
ATOM   22299 C  CG    . LYS A 1 4564 ? 196.552 159.886 146.744 1.00 47.87  ? 4564 LYS A CG    1 
ATOM   22300 C  CD    . LYS A 1 4564 ? 197.854 159.108 146.809 1.00 51.66  ? 4564 LYS A CD    1 
ATOM   22301 C  CE    . LYS A 1 4564 ? 198.601 159.377 148.105 1.00 64.22  ? 4564 LYS A CE    1 
ATOM   22302 N  NZ    . LYS A 1 4564 ? 199.002 160.806 148.230 1.00 63.08  ? 4564 LYS A NZ    1 
ATOM   22303 N  N     . LEU A 1 4565 ? 195.775 158.387 142.378 1.00 35.96  ? 4565 LEU A N     1 
ATOM   22304 C  CA    . LEU A 1 4565 ? 195.041 157.752 141.292 1.00 34.34  ? 4565 LEU A CA    1 
ATOM   22305 C  C     . LEU A 1 4565 ? 194.438 156.446 141.789 1.00 42.32  ? 4565 LEU A C     1 
ATOM   22306 O  O     . LEU A 1 4565 ? 195.155 155.586 142.311 1.00 50.44  ? 4565 LEU A O     1 
ATOM   22307 C  CB    . LEU A 1 4565 ? 195.958 157.496 140.096 1.00 33.83  ? 4565 LEU A CB    1 
ATOM   22308 C  CG    . LEU A 1 4565 ? 195.289 157.059 138.793 1.00 33.76  ? 4565 LEU A CG    1 
ATOM   22309 C  CD1   . LEU A 1 4565 ? 194.221 158.056 138.378 1.00 32.22  ? 4565 LEU A CD1   1 
ATOM   22310 C  CD2   . LEU A 1 4565 ? 196.328 156.897 137.698 1.00 39.46  ? 4565 LEU A CD2   1 
ATOM   22311 N  N     . GLN A 1 4566 ? 193.127 156.298 141.621 1.00 37.50  ? 4566 GLN A N     1 
ATOM   22312 C  CA    . GLN A 1 4566 ? 192.391 155.156 142.147 1.00 36.56  ? 4566 GLN A CA    1 
ATOM   22313 C  C     . GLN A 1 4566 ? 192.225 154.106 141.056 1.00 37.29  ? 4566 GLN A C     1 
ATOM   22314 O  O     . GLN A 1 4566 ? 191.640 154.384 140.005 1.00 36.69  ? 4566 GLN A O     1 
ATOM   22315 C  CB    . GLN A 1 4566 ? 191.026 155.589 142.679 1.00 31.93  ? 4566 GLN A CB    1 
ATOM   22316 C  CG    . GLN A 1 4566 ? 191.080 156.747 143.657 1.00 35.02  ? 4566 GLN A CG    1 
ATOM   22317 C  CD    . GLN A 1 4566 ? 191.754 156.376 144.962 1.00 44.62  ? 4566 GLN A CD    1 
ATOM   22318 O  OE1   . GLN A 1 4566 ? 192.763 156.969 145.343 1.00 46.04  ? 4566 GLN A OE1   1 
ATOM   22319 N  NE2   . GLN A 1 4566 ? 191.198 155.391 145.656 1.00 50.44  ? 4566 GLN A NE2   1 
ATOM   22320 N  N     . GLY A 1 4567 ? 192.736 152.904 141.311 1.00 37.81  ? 4567 GLY A N     1 
ATOM   22321 C  CA    . GLY A 1 4567 ? 192.533 151.793 140.401 1.00 39.56  ? 4567 GLY A CA    1 
ATOM   22322 C  C     . GLY A 1 4567 ? 193.240 151.914 139.071 1.00 42.39  ? 4567 GLY A C     1 
ATOM   22323 O  O     . GLY A 1 4567 ? 192.806 151.302 138.091 1.00 45.00  ? 4567 GLY A O     1 
ATOM   22324 N  N     . ALA A 1 4568 ? 194.322 152.686 139.007 1.00 39.99  ? 4568 ALA A N     1 
ATOM   22325 C  CA    . ALA A 1 4568 ? 195.059 152.850 137.763 1.00 40.12  ? 4568 ALA A CA    1 
ATOM   22326 C  C     . ALA A 1 4568 ? 196.473 153.308 138.082 1.00 47.05  ? 4568 ALA A C     1 
ATOM   22327 O  O     . ALA A 1 4568 ? 196.761 153.776 139.186 1.00 50.88  ? 4568 ALA A O     1 
ATOM   22328 C  CB    . ALA A 1 4568 ? 194.368 153.846 136.826 1.00 36.41  ? 4568 ALA A CB    1 
ATOM   22329 N  N     . THR A 1 4569 ? 197.353 153.162 137.095 1.00 49.84  ? 4569 THR A N     1 
ATOM   22330 C  CA    . THR A 1 4569 ? 198.730 153.621 137.192 1.00 51.36  ? 4569 THR A CA    1 
ATOM   22331 C  C     . THR A 1 4569 ? 199.056 154.481 135.981 1.00 53.98  ? 4569 THR A C     1 
ATOM   22332 O  O     . THR A 1 4569 ? 198.565 154.236 134.876 1.00 56.85  ? 4569 THR A O     1 
ATOM   22333 C  CB    . THR A 1 4569 ? 199.721 152.451 137.279 1.00 54.70  ? 4569 THR A CB    1 
ATOM   22334 O  OG1   . THR A 1 4569 ? 199.450 151.512 136.231 1.00 59.31  ? 4569 THR A OG1   1 
ATOM   22335 C  CG2   . THR A 1 4569 ? 199.605 151.751 138.624 1.00 50.02  ? 4569 THR A CG2   1 
ATOM   22336 N  N     . CYS A 1 4570 ? 199.889 155.494 136.198 1.00 56.39  ? 4570 CYS A N     1 
ATOM   22337 C  CA    . CYS A 1 4570 ? 200.262 156.445 135.159 1.00 56.74  ? 4570 CYS A CA    1 
ATOM   22338 C  C     . CYS A 1 4570 ? 201.739 156.273 134.831 1.00 65.17  ? 4570 CYS A C     1 
ATOM   22339 O  O     . CYS A 1 4570 ? 202.602 156.562 135.666 1.00 66.31  ? 4570 CYS A O     1 
ATOM   22340 C  CB    . CYS A 1 4570 ? 199.972 157.878 135.602 1.00 56.82  ? 4570 CYS A CB    1 
ATOM   22341 S  SG    . CYS A 1 4570 ? 200.331 159.132 134.353 1.00 82.60  ? 4570 CYS A SG    1 
ATOM   22342 N  N     . ASN A 1 4571 ? 202.023 155.805 133.617 1.00 68.77  ? 4571 ASN A N     1 
ATOM   22343 C  CA    . ASN A 1 4571 ? 203.388 155.646 133.128 1.00 68.76  ? 4571 ASN A CA    1 
ATOM   22344 C  C     . ASN A 1 4571 ? 203.517 156.405 131.817 1.00 68.20  ? 4571 ASN A C     1 
ATOM   22345 O  O     . ASN A 1 4571 ? 202.743 156.168 130.884 1.00 68.06  ? 4571 ASN A O     1 
ATOM   22346 C  CB    . ASN A 1 4571 ? 203.740 154.168 132.933 1.00 68.20  ? 4571 ASN A CB    1 
ATOM   22347 C  CG    . ASN A 1 4571 ? 203.830 153.412 134.244 1.00 75.10  ? 4571 ASN A CG    1 
ATOM   22348 O  OD1   . ASN A 1 4571 ? 203.877 154.012 135.318 1.00 72.27  ? 4571 ASN A OD1   1 
ATOM   22349 N  ND2   . ASN A 1 4571 ? 203.853 152.087 134.163 1.00 72.42  ? 4571 ASN A ND2   1 
ATOM   22350 N  N     . ASN A 1 4572 ? 204.497 157.311 131.750 1.00 70.37  ? 4572 ASN A N     1 
ATOM   22351 C  CA    . ASN A 1 4572 ? 204.713 158.158 130.575 1.00 70.07  ? 4572 ASN A CA    1 
ATOM   22352 C  C     . ASN A 1 4572 ? 203.444 158.923 130.204 1.00 71.72  ? 4572 ASN A C     1 
ATOM   22353 O  O     . ASN A 1 4572 ? 203.096 159.050 129.029 1.00 70.54  ? 4572 ASN A O     1 
ATOM   22354 C  CB    . ASN A 1 4572 ? 205.225 157.342 129.386 1.00 73.48  ? 4572 ASN A CB    1 
ATOM   22355 C  CG    . ASN A 1 4572 ? 206.613 156.775 129.621 1.00 78.18  ? 4572 ASN A CG    1 
ATOM   22356 O  OD1   . ASN A 1 4572 ? 207.308 157.175 130.555 1.00 76.62  ? 4572 ASN A OD1   1 
ATOM   22357 N  ND2   . ASN A 1 4572 ? 207.021 155.836 128.775 1.00 77.87  ? 4572 ASN A ND2   1 
ATOM   22358 N  N     . ASN A 1 4573 ? 202.750 159.433 131.224 1.00 70.42  ? 4573 ASN A N     1 
ATOM   22359 C  CA    . ASN A 1 4573 ? 201.499 160.176 131.051 1.00 68.05  ? 4573 ASN A CA    1 
ATOM   22360 C  C     . ASN A 1 4573 ? 200.449 159.342 130.319 1.00 67.68  ? 4573 ASN A C     1 
ATOM   22361 O  O     . ASN A 1 4573 ? 199.677 159.856 129.507 1.00 69.22  ? 4573 ASN A O     1 
ATOM   22362 C  CB    . ASN A 1 4573 ? 201.739 161.506 130.333 1.00 69.49  ? 4573 ASN A CB    1 
ATOM   22363 C  CG    . ASN A 1 4573 ? 200.777 162.589 130.778 1.00 71.68  ? 4573 ASN A CG    1 
ATOM   22364 O  OD1   . ASN A 1 4573 ? 200.617 162.841 131.972 1.00 72.94  ? 4573 ASN A OD1   1 
ATOM   22365 N  ND2   . ASN A 1 4573 ? 200.129 163.237 129.817 1.00 70.52  ? 4573 ASN A ND2   1 
ATOM   22366 N  N     . LYS A 1 4574 ? 200.420 158.043 130.608 1.00 68.30  ? 4574 LYS A N     1 
ATOM   22367 C  CA    . LYS A 1 4574 ? 199.433 157.139 130.036 1.00 61.08  ? 4574 LYS A CA    1 
ATOM   22368 C  C     . LYS A 1 4574 ? 198.884 156.238 131.131 1.00 60.14  ? 4574 LYS A C     1 
ATOM   22369 O  O     . LYS A 1 4574 ? 199.633 155.764 131.989 1.00 62.57  ? 4574 LYS A O     1 
ATOM   22370 C  CB    . LYS A 1 4574 ? 200.030 156.296 128.903 1.00 65.10  ? 4574 LYS A CB    1 
ATOM   22371 C  CG    . LYS A 1 4574 ? 200.335 157.090 127.644 1.00 69.98  ? 4574 LYS A CG    1 
ATOM   22372 C  CD    . LYS A 1 4574 ? 200.739 156.182 126.496 1.00 73.88  ? 4574 LYS A CD    1 
ATOM   22373 C  CE    . LYS A 1 4574 ? 201.075 156.990 125.254 1.00 72.41  ? 4574 LYS A CE    1 
ATOM   22374 N  NZ    . LYS A 1 4574 ? 200.026 158.005 124.956 1.00 67.89  ? 4574 LYS A NZ    1 
ATOM   22375 N  N     . LEU A 1 4575 ? 197.576 156.001 131.092 1.00 55.57  ? 4575 LEU A N     1 
ATOM   22376 C  CA    . LEU A 1 4575 ? 196.894 155.247 132.133 1.00 50.59  ? 4575 LEU A CA    1 
ATOM   22377 C  C     . LEU A 1 4575 ? 196.835 153.764 131.796 1.00 53.73  ? 4575 LEU A C     1 
ATOM   22378 O  O     . LEU A 1 4575 ? 196.631 153.380 130.641 1.00 63.72  ? 4575 LEU A O     1 
ATOM   22379 C  CB    . LEU A 1 4575 ? 195.476 155.776 132.343 1.00 44.99  ? 4575 LEU A CB    1 
ATOM   22380 C  CG    . LEU A 1 4575 ? 195.332 157.167 132.955 1.00 44.99  ? 4575 LEU A CG    1 
ATOM   22381 C  CD1   . LEU A 1 4575 ? 193.933 157.333 133.506 1.00 38.55  ? 4575 LEU A CD1   1 
ATOM   22382 C  CD2   . LEU A 1 4575 ? 196.370 157.392 134.040 1.00 43.56  ? 4575 LEU A CD2   1 
ATOM   22383 N  N     . SER A 1 4576 ? 197.016 152.934 132.820 1.00 54.21  ? 4576 SER A N     1 
ATOM   22384 C  CA    . SER A 1 4576 ? 196.840 151.494 132.721 1.00 57.47  ? 4576 SER A CA    1 
ATOM   22385 C  C     . SER A 1 4576 ? 196.069 151.011 133.939 1.00 52.22  ? 4576 SER A C     1 
ATOM   22386 O  O     . SER A 1 4576 ? 196.362 151.414 135.068 1.00 52.84  ? 4576 SER A O     1 
ATOM   22387 C  CB    . SER A 1 4576 ? 198.188 150.767 132.627 1.00 58.92  ? 4576 SER A CB    1 
ATOM   22388 O  OG    . SER A 1 4576 ? 198.929 151.210 131.504 1.00 59.53  ? 4576 SER A OG    1 
ATOM   22389 N  N     . LEU A 1 4577 ? 195.078 150.153 133.706 1.00 49.74  ? 4577 LEU A N     1 
ATOM   22390 C  CA    . LEU A 1 4577 ? 194.288 149.621 134.808 1.00 43.88  ? 4577 LEU A CA    1 
ATOM   22391 C  C     . LEU A 1 4577 ? 195.152 148.748 135.708 1.00 45.12  ? 4577 LEU A C     1 
ATOM   22392 O  O     . LEU A 1 4577 ? 195.960 147.944 135.235 1.00 52.87  ? 4577 LEU A O     1 
ATOM   22393 C  CB    . LEU A 1 4577 ? 193.102 148.818 134.276 1.00 40.88  ? 4577 LEU A CB    1 
ATOM   22394 C  CG    . LEU A 1 4577 ? 191.959 149.617 133.651 1.00 35.67  ? 4577 LEU A CG    1 
ATOM   22395 C  CD1   . LEU A 1 4577 ? 190.925 148.677 133.061 1.00 32.87  ? 4577 LEU A CD1   1 
ATOM   22396 C  CD2   . LEU A 1 4577 ? 191.325 150.541 134.675 1.00 33.83  ? 4577 LEU A CD2   1 
ATOM   22397 N  N     . SER A 1 4578 ? 194.977 148.911 137.017 1.00 44.98  ? 4578 SER A N     1 
ATOM   22398 C  CA    . SER A 1 4578 ? 195.744 148.158 137.996 1.00 51.76  ? 4578 SER A CA    1 
ATOM   22399 C  C     . SER A 1 4578 ? 194.825 147.717 139.124 1.00 52.78  ? 4578 SER A C     1 
ATOM   22400 O  O     . SER A 1 4578 ? 193.780 148.321 139.377 1.00 51.97  ? 4578 SER A O     1 
ATOM   22401 C  CB    . SER A 1 4578 ? 196.909 148.983 138.557 1.00 54.90  ? 4578 SER A CB    1 
ATOM   22402 O  OG    . SER A 1 4578 ? 196.458 149.889 139.548 1.00 57.12  ? 4578 SER A OG    1 
ATOM   22403 N  N     . ASN A 1 4579 ? 195.231 146.646 139.802 1.00 56.16  ? 4579 ASN A N     1 
ATOM   22404 C  CA    . ASN A 1 4579 ? 194.489 146.134 140.944 1.00 61.09  ? 4579 ASN A CA    1 
ATOM   22405 C  C     . ASN A 1 4579 ? 194.817 146.863 142.239 1.00 63.55  ? 4579 ASN A C     1 
ATOM   22406 O  O     . ASN A 1 4579 ? 194.183 146.588 143.264 1.00 67.98  ? 4579 ASN A O     1 
ATOM   22407 C  CB    . ASN A 1 4579 ? 194.757 144.635 141.120 1.00 60.73  ? 4579 ASN A CB    1 
ATOM   22408 C  CG    . ASN A 1 4579 ? 194.132 143.801 140.020 1.00 66.42  ? 4579 ASN A CG    1 
ATOM   22409 O  OD1   . ASN A 1 4579 ? 194.817 143.043 139.335 1.00 71.22  ? 4579 ASN A OD1   1 
ATOM   22410 N  ND2   . ASN A 1 4579 ? 192.822 143.936 139.846 1.00 60.93  ? 4579 ASN A ND2   1 
ATOM   22411 N  N     . ALA A 1 4580 ? 195.788 147.774 142.221 1.00 53.40  ? 4580 ALA A N     1 
ATOM   22412 C  CA    . ALA A 1 4580 ? 196.106 148.550 143.411 1.00 52.36  ? 4580 ALA A CA    1 
ATOM   22413 C  C     . ALA A 1 4580 ? 194.944 149.464 143.774 1.00 57.02  ? 4580 ALA A C     1 
ATOM   22414 O  O     . ALA A 1 4580 ? 194.255 149.998 142.901 1.00 61.58  ? 4580 ALA A O     1 
ATOM   22415 C  CB    . ALA A 1 4580 ? 197.375 149.372 143.184 1.00 51.69  ? 4580 ALA A CB    1 
ATOM   22416 N  N     . ILE A 1 4581 ? 194.722 149.633 145.079 1.00 53.84  ? 4581 ILE A N     1 
ATOM   22417 C  CA    . ILE A 1 4581 ? 193.621 150.473 145.543 1.00 54.61  ? 4581 ILE A CA    1 
ATOM   22418 C  C     . ILE A 1 4581 ? 193.845 151.923 145.132 1.00 51.06  ? 4581 ILE A C     1 
ATOM   22419 O  O     . ILE A 1 4581 ? 192.929 152.596 144.646 1.00 51.56  ? 4581 ILE A O     1 
ATOM   22420 C  CB    . ILE A 1 4581 ? 193.448 150.337 147.066 1.00 54.16  ? 4581 ILE A CB    1 
ATOM   22421 C  CG1   . ILE A 1 4581 ? 193.164 148.882 147.441 1.00 53.54  ? 4581 ILE A CG1   1 
ATOM   22422 C  CG2   . ILE A 1 4581 ? 192.331 151.242 147.559 1.00 51.42  ? 4581 ILE A CG2   1 
ATOM   22423 C  CD1   . ILE A 1 4581 ? 191.896 148.334 146.828 1.00 46.94  ? 4581 ILE A CD1   1 
ATOM   22424 N  N     . SER A 1 4582 ? 195.065 152.424 145.315 1.00 49.15  ? 4582 SER A N     1 
ATOM   22425 C  CA    . SER A 1 4582 ? 195.381 153.802 144.972 1.00 49.35  ? 4582 SER A CA    1 
ATOM   22426 C  C     . SER A 1 4582 ? 196.857 153.911 144.625 1.00 55.97  ? 4582 SER A C     1 
ATOM   22427 O  O     . SER A 1 4582 ? 197.705 153.306 145.287 1.00 64.82  ? 4582 SER A O     1 
ATOM   22428 C  CB    . SER A 1 4582 ? 195.038 154.758 146.121 1.00 51.68  ? 4582 SER A CB    1 
ATOM   22429 O  OG    . SER A 1 4582 ? 195.811 154.469 147.272 1.00 62.89  ? 4582 SER A OG    1 
ATOM   22430 N  N     . THR A 1 4583 ? 197.154 154.685 143.584 1.00 51.76  ? 4583 THR A N     1 
ATOM   22431 C  CA    . THR A 1 4583 ? 198.519 154.938 143.144 1.00 46.38  ? 4583 THR A CA    1 
ATOM   22432 C  C     . THR A 1 4583 ? 198.809 156.426 143.275 1.00 51.73  ? 4583 THR A C     1 
ATOM   22433 O  O     . THR A 1 4583 ? 198.054 157.257 142.761 1.00 58.03  ? 4583 THR A O     1 
ATOM   22434 C  CB    . THR A 1 4583 ? 198.730 154.481 141.698 1.00 44.06  ? 4583 THR A CB    1 
ATOM   22435 O  OG1   . THR A 1 4583 ? 198.822 153.051 141.656 1.00 54.98  ? 4583 THR A OG1   1 
ATOM   22436 C  CG2   . THR A 1 4583 ? 200.005 155.080 141.125 1.00 43.04  ? 4583 THR A CG2   1 
ATOM   22437 N  N     . ALA A 1 4584 ? 199.899 156.757 143.962 1.00 54.32  ? 4584 ALA A N     1 
ATOM   22438 C  CA    . ALA A 1 4584 ? 200.248 158.149 144.204 1.00 53.67  ? 4584 ALA A CA    1 
ATOM   22439 C  C     . ALA A 1 4584 ? 200.900 158.757 142.970 1.00 52.55  ? 4584 ALA A C     1 
ATOM   22440 O  O     . ALA A 1 4584 ? 201.846 158.192 142.412 1.00 51.93  ? 4584 ALA A O     1 
ATOM   22441 C  CB    . ALA A 1 4584 ? 201.184 158.262 145.406 1.00 59.30  ? 4584 ALA A CB    1 
ATOM   22442 N  N     . LEU A 1 4585 ? 200.390 159.907 142.544 1.00 48.57  ? 4585 LEU A N     1 
ATOM   22443 C  CA    . LEU A 1 4585 ? 200.997 160.641 141.442 1.00 50.26  ? 4585 LEU A CA    1 
ATOM   22444 C  C     . LEU A 1 4585 ? 202.130 161.507 141.977 1.00 59.58  ? 4585 LEU A C     1 
ATOM   22445 O  O     . LEU A 1 4585 ? 201.898 162.323 142.877 1.00 64.24  ? 4585 LEU A O     1 
ATOM   22446 C  CB    . LEU A 1 4585 ? 199.959 161.502 140.736 1.00 43.02  ? 4585 LEU A CB    1 
ATOM   22447 C  CG    . LEU A 1 4585 ? 198.761 160.758 140.142 1.00 40.61  ? 4585 LEU A CG    1 
ATOM   22448 C  CD1   . LEU A 1 4585 ? 197.748 161.737 139.570 1.00 36.91  ? 4585 LEU A CD1   1 
ATOM   22449 C  CD2   . LEU A 1 4585 ? 199.214 159.771 139.080 1.00 46.72  ? 4585 LEU A CD2   1 
ATOM   22450 N  N     . PRO A 1 4586 ? 203.361 161.358 141.473 1.00 58.60  ? 4586 PRO A N     1 
ATOM   22451 C  CA    . PRO A 1 4586 ? 204.490 162.121 142.027 1.00 58.31  ? 4586 PRO A CA    1 
ATOM   22452 C  C     . PRO A 1 4586 ? 204.304 163.627 141.924 1.00 61.51  ? 4586 PRO A C     1 
ATOM   22453 O  O     . PRO A 1 4586 ? 204.340 164.335 142.936 1.00 59.00  ? 4586 PRO A O     1 
ATOM   22454 C  CB    . PRO A 1 4586 ? 205.683 161.647 141.185 1.00 64.21  ? 4586 PRO A CB    1 
ATOM   22455 C  CG    . PRO A 1 4586 ? 205.084 161.066 139.945 1.00 64.88  ? 4586 PRO A CG    1 
ATOM   22456 C  CD    . PRO A 1 4586 ? 203.766 160.493 140.353 1.00 55.88  ? 4586 PRO A CD    1 
ATOM   22457 N  N     . LEU A 1 4587 ? 204.104 164.126 140.707 1.00 61.69  ? 4587 LEU A N     1 
ATOM   22458 C  CA    . LEU A 1 4587 ? 203.882 165.548 140.484 1.00 56.87  ? 4587 LEU A CA    1 
ATOM   22459 C  C     . LEU A 1 4587 ? 202.989 165.716 139.267 1.00 58.44  ? 4587 LEU A C     1 
ATOM   22460 O  O     . LEU A 1 4587 ? 203.264 165.142 138.210 1.00 68.17  ? 4587 LEU A O     1 
ATOM   22461 C  CB    . LEU A 1 4587 ? 205.205 166.295 140.283 1.00 63.34  ? 4587 LEU A CB    1 
ATOM   22462 C  CG    . LEU A 1 4587 ? 205.094 167.782 139.944 1.00 60.52  ? 4587 LEU A CG    1 
ATOM   22463 C  CD1   . LEU A 1 4587 ? 204.637 168.577 141.155 1.00 56.65  ? 4587 LEU A CD1   1 
ATOM   22464 C  CD2   . LEU A 1 4587 ? 206.417 168.315 139.418 1.00 75.22  ? 4587 LEU A CD2   1 
ATOM   22465 N  N     . THR A 1 4588 ? 201.928 166.501 139.420 1.00 51.75  ? 4588 THR A N     1 
ATOM   22466 C  CA    . THR A 1 4588 ? 200.974 166.758 138.351 1.00 48.13  ? 4588 THR A CA    1 
ATOM   22467 C  C     . THR A 1 4588 ? 201.106 168.204 137.898 1.00 50.17  ? 4588 THR A C     1 
ATOM   22468 O  O     . THR A 1 4588 ? 201.029 169.125 138.718 1.00 55.01  ? 4588 THR A O     1 
ATOM   22469 C  CB    . THR A 1 4588 ? 199.543 166.476 138.814 1.00 48.26  ? 4588 THR A CB    1 
ATOM   22470 O  OG1   . THR A 1 4588 ? 199.492 165.201 139.465 1.00 53.27  ? 4588 THR A OG1   1 
ATOM   22471 C  CG2   . THR A 1 4588 ? 198.593 166.471 137.630 1.00 52.80  ? 4588 THR A CG2   1 
ATOM   22472 N  N     . GLN A 1 4589 ? 201.304 168.399 136.598 1.00 53.43  ? 4589 GLN A N     1 
ATOM   22473 C  CA    . GLN A 1 4589 ? 201.439 169.723 136.007 1.00 54.33  ? 4589 GLN A CA    1 
ATOM   22474 C  C     . GLN A 1 4589 ? 200.137 170.080 135.305 1.00 50.42  ? 4589 GLN A C     1 
ATOM   22475 O  O     . GLN A 1 4589 ? 199.671 169.333 134.438 1.00 59.61  ? 4589 GLN A O     1 
ATOM   22476 C  CB    . GLN A 1 4589 ? 202.610 169.769 135.026 1.00 61.53  ? 4589 GLN A CB    1 
ATOM   22477 C  CG    . GLN A 1 4589 ? 203.976 169.729 135.688 1.00 70.39  ? 4589 GLN A CG    1 
ATOM   22478 C  CD    . GLN A 1 4589 ? 205.109 169.745 134.681 1.00 86.94  ? 4589 GLN A CD    1 
ATOM   22479 O  OE1   . GLN A 1 4589 ? 204.879 169.747 133.472 1.00 82.97  ? 4589 GLN A OE1   1 
ATOM   22480 N  NE2   . GLN A 1 4589 ? 206.340 169.757 135.177 1.00 97.42  ? 4589 GLN A NE2   1 
ATOM   22481 N  N     . LEU A 1 4590 ? 199.557 171.217 135.678 1.00 43.10  ? 4590 LEU A N     1 
ATOM   22482 C  CA    . LEU A 1 4590 ? 198.311 171.699 135.086 1.00 44.18  ? 4590 LEU A CA    1 
ATOM   22483 C  C     . LEU A 1 4590 ? 198.662 172.769 134.059 1.00 52.31  ? 4590 LEU A C     1 
ATOM   22484 O  O     . LEU A 1 4590 ? 198.997 173.901 134.415 1.00 61.81  ? 4590 LEU A O     1 
ATOM   22485 C  CB    . LEU A 1 4590 ? 197.372 172.239 136.158 1.00 46.50  ? 4590 LEU A CB    1 
ATOM   22486 C  CG    . LEU A 1 4590 ? 197.133 171.343 137.374 1.00 47.60  ? 4590 LEU A CG    1 
ATOM   22487 C  CD1   . LEU A 1 4590 ? 196.207 172.029 138.364 1.00 45.72  ? 4590 LEU A CD1   1 
ATOM   22488 C  CD2   . LEU A 1 4590 ? 196.567 169.998 136.947 1.00 43.20  ? 4590 LEU A CD2   1 
ATOM   22489 N  N     . ARG A 1 4591 ? 198.580 172.407 132.783 1.00 56.49  ? 4591 ARG A N     1 
ATOM   22490 C  CA    . ARG A 1 4591 ? 198.882 173.319 131.689 1.00 59.12  ? 4591 ARG A CA    1 
ATOM   22491 C  C     . ARG A 1 4591 ? 197.586 173.886 131.129 1.00 58.87  ? 4591 ARG A C     1 
ATOM   22492 O  O     . ARG A 1 4591 ? 196.641 173.139 130.856 1.00 67.46  ? 4591 ARG A O     1 
ATOM   22493 C  CB    . ARG A 1 4591 ? 199.669 172.612 130.586 1.00 65.69  ? 4591 ARG A CB    1 
ATOM   22494 C  CG    . ARG A 1 4591 ? 201.133 172.378 130.919 1.00 74.56  ? 4591 ARG A CG    1 
ATOM   22495 C  CD    . ARG A 1 4591 ? 201.972 171.935 129.715 1.00 85.22  ? 4591 ARG A CD    1 
ATOM   22496 N  NE    . ARG A 1 4591 ? 202.222 173.003 128.750 1.00 88.07  ? 4591 ARG A NE    1 
ATOM   22497 C  CZ    . ARG A 1 4591 ? 201.398 173.363 127.774 1.00 91.64  ? 4591 ARG A CZ    1 
ATOM   22498 N  NH1   . ARG A 1 4591 ? 200.272 172.708 127.539 1.00 86.09  ? 4591 ARG A NH1   1 
ATOM   22499 N  NH2   . ARG A 1 4591 ? 201.722 174.393 126.999 1.00 91.40  ? 4591 ARG A NH2   1 
ATOM   22500 N  N     . TRP A 1 4592 ? 197.545 175.204 130.961 1.00 57.92  ? 4592 TRP A N     1 
ATOM   22501 C  CA    . TRP A 1 4592 ? 196.384 175.899 130.423 1.00 62.75  ? 4592 TRP A CA    1 
ATOM   22502 C  C     . TRP A 1 4592 ? 196.701 176.350 129.004 1.00 71.76  ? 4592 TRP A C     1 
ATOM   22503 O  O     . TRP A 1 4592 ? 197.673 177.081 128.785 1.00 80.69  ? 4592 TRP A O     1 
ATOM   22504 C  CB    . TRP A 1 4592 ? 196.006 177.091 131.301 1.00 64.28  ? 4592 TRP A CB    1 
ATOM   22505 C  CG    . TRP A 1 4592 ? 195.400 176.695 132.610 1.00 63.05  ? 4592 TRP A CG    1 
ATOM   22506 C  CD1   . TRP A 1 4592 ? 195.989 176.762 133.838 1.00 61.14  ? 4592 TRP A CD1   1 
ATOM   22507 C  CD2   . TRP A 1 4592 ? 194.084 176.174 132.824 1.00 59.54  ? 4592 TRP A CD2   1 
ATOM   22508 N  NE1   . TRP A 1 4592 ? 195.122 176.311 134.803 1.00 56.98  ? 4592 TRP A NE1   1 
ATOM   22509 C  CE2   . TRP A 1 4592 ? 193.945 175.944 134.206 1.00 55.60  ? 4592 TRP A CE2   1 
ATOM   22510 C  CE3   . TRP A 1 4592 ? 193.010 175.877 131.980 1.00 61.90  ? 4592 TRP A CE3   1 
ATOM   22511 C  CZ2   . TRP A 1 4592 ? 192.776 175.433 134.764 1.00 55.23  ? 4592 TRP A CZ2   1 
ATOM   22512 C  CZ3   . TRP A 1 4592 ? 191.850 175.371 132.536 1.00 60.81  ? 4592 TRP A CZ3   1 
ATOM   22513 C  CH2   . TRP A 1 4592 ? 191.743 175.153 133.914 1.00 56.68  ? 4592 TRP A CH2   1 
ATOM   22514 N  N     . VAL A 1 4593 ? 195.883 175.912 128.047 1.00 67.99  ? 4593 VAL A N     1 
ATOM   22515 C  CA    . VAL A 1 4593 ? 196.064 176.250 126.644 1.00 71.83  ? 4593 VAL A CA    1 
ATOM   22516 C  C     . VAL A 1 4593 ? 194.727 176.694 126.071 1.00 83.25  ? 4593 VAL A C     1 
ATOM   22517 O  O     . VAL A 1 4593 ? 193.660 176.397 126.614 1.00 89.26  ? 4593 VAL A O     1 
ATOM   22518 C  CB    . VAL A 1 4593 ? 196.635 175.072 125.825 1.00 69.10  ? 4593 VAL A CB    1 
ATOM   22519 C  CG1   . VAL A 1 4593 ? 198.103 174.860 126.153 1.00 76.08  ? 4593 VAL A CG1   1 
ATOM   22520 C  CG2   . VAL A 1 4593 ? 195.839 173.808 126.094 1.00 66.92  ? 4593 VAL A CG2   1 
ATOM   22521 N  N     . LYS A 1 4594 ? 194.799 177.422 124.961 1.00 87.93  ? 4594 LYS A N     1 
ATOM   22522 C  CA    . LYS A 1 4594 ? 193.593 177.878 124.286 1.00 87.28  ? 4594 LYS A CA    1 
ATOM   22523 C  C     . LYS A 1 4594 ? 192.802 176.689 123.758 1.00 92.55  ? 4594 LYS A C     1 
ATOM   22524 O  O     . LYS A 1 4594 ? 193.370 175.737 123.216 1.00 94.22  ? 4594 LYS A O     1 
ATOM   22525 C  CB    . LYS A 1 4594 ? 193.950 178.827 123.143 1.00 88.32  ? 4594 LYS A CB    1 
ATOM   22526 C  CG    . LYS A 1 4594 ? 194.889 179.953 123.542 1.00 91.04  ? 4594 LYS A CG    1 
ATOM   22527 C  CD    . LYS A 1 4594 ? 194.880 181.075 122.516 1.00 91.71  ? 4594 LYS A CD    1 
ATOM   22528 C  CE    . LYS A 1 4594 ? 193.531 181.773 122.467 1.00 89.18  ? 4594 LYS A CE    1 
ATOM   22529 N  NZ    . LYS A 1 4594 ? 193.186 182.403 123.771 1.00 88.67  ? 4594 LYS A NZ    1 
ATOM   22530 N  N     . GLN A 1 4595 ? 191.483 176.744 123.929 1.00 95.04  ? 4595 GLN A N     1 
ATOM   22531 C  CA    . GLN A 1 4595 ? 190.624 175.659 123.472 1.00 101.42 ? 4595 GLN A CA    1 
ATOM   22532 C  C     . GLN A 1 4595 ? 190.710 175.518 121.959 1.00 109.82 ? 4595 GLN A C     1 
ATOM   22533 O  O     . GLN A 1 4595 ? 190.591 176.501 121.221 1.00 111.70 ? 4595 GLN A O     1 
ATOM   22534 C  CB    . GLN A 1 4595 ? 189.179 175.913 123.901 1.00 104.59 ? 4595 GLN A CB    1 
ATOM   22535 C  CG    . GLN A 1 4595 ? 188.212 174.798 123.534 1.00 112.02 ? 4595 GLN A CG    1 
ATOM   22536 C  CD    . GLN A 1 4595 ? 188.540 173.489 124.223 1.00 112.69 ? 4595 GLN A CD    1 
ATOM   22537 O  OE1   . GLN A 1 4595 ? 189.073 172.566 123.607 1.00 107.20 ? 4595 GLN A OE1   1 
ATOM   22538 N  NE2   . GLN A 1 4595 ? 188.217 173.399 125.507 1.00 105.06 ? 4595 GLN A NE2   1 
ATOM   22539 N  N     . THR A 1 4596 ? 190.918 174.285 121.497 1.00 113.80 ? 4596 THR A N     1 
ATOM   22540 C  CA    . THR A 1 4596 ? 191.021 174.005 120.072 1.00 116.05 ? 4596 THR A CA    1 
ATOM   22541 C  C     . THR A 1 4596 ? 189.716 173.519 119.460 1.00 118.44 ? 4596 THR A C     1 
ATOM   22542 O  O     . THR A 1 4596 ? 189.541 173.643 118.243 1.00 118.05 ? 4596 THR A O     1 
ATOM   22543 C  CB    . THR A 1 4596 ? 192.114 172.961 119.811 1.00 115.57 ? 4596 THR A CB    1 
ATOM   22544 O  OG1   . THR A 1 4596 ? 191.747 171.718 120.425 1.00 117.00 ? 4596 THR A OG1   1 
ATOM   22545 C  CG2   . THR A 1 4596 ? 193.445 173.429 120.380 1.00 107.64 ? 4596 THR A CG2   1 
ATOM   22546 N  N     . ASN A 1 4597 ? 188.806 172.978 120.272 1.00 118.64 ? 4597 ASN A N     1 
ATOM   22547 C  CA    . ASN A 1 4597 ? 187.520 172.462 119.798 1.00 121.24 ? 4597 ASN A CA    1 
ATOM   22548 C  C     . ASN A 1 4597 ? 187.711 171.420 118.698 1.00 119.41 ? 4597 ASN A C     1 
ATOM   22549 O  O     . ASN A 1 4597 ? 186.983 171.397 117.703 1.00 114.68 ? 4597 ASN A O     1 
ATOM   22550 C  CB    . ASN A 1 4597 ? 186.609 173.597 119.326 1.00 123.74 ? 4597 ASN A CB    1 
ATOM   22551 C  CG    . ASN A 1 4597 ? 186.188 174.513 120.457 1.00 124.03 ? 4597 ASN A CG    1 
ATOM   22552 O  OD1   . ASN A 1 4597 ? 186.581 175.679 120.507 1.00 127.96 ? 4597 ASN A OD1   1 
ATOM   22553 N  ND2   . ASN A 1 4597 ? 185.384 173.989 121.375 1.00 120.38 ? 4597 ASN A ND2   1 
ATOM   22554 N  N     . THR A 1 4598 ? 188.701 170.549 118.880 1.00 121.89 ? 4598 THR A N     1 
ATOM   22555 C  CA    . THR A 1 4598 ? 188.990 169.465 117.943 1.00 124.10 ? 4598 THR A CA    1 
ATOM   22556 C  C     . THR A 1 4598 ? 188.474 168.129 118.458 1.00 128.09 ? 4598 THR A C     1 
ATOM   22557 O  O     . THR A 1 4598 ? 189.102 167.087 118.244 1.00 124.07 ? 4598 THR A O     1 
ATOM   22558 C  CB    . THR A 1 4598 ? 190.488 169.388 117.662 1.00 121.77 ? 4598 THR A CB    1 
ATOM   22559 O  OG1   . THR A 1 4598 ? 191.204 169.294 118.899 1.00 123.65 ? 4598 THR A OG1   1 
ATOM   22560 C  CG2   . THR A 1 4598 ? 190.953 170.625 116.907 1.00 114.83 ? 4598 THR A CG2   1 
ATOM   22561 N  N     . GLU A 1 4599 ? 187.336 168.147 119.143 1.00 130.26 ? 4599 GLU A N     1 
ATOM   22562 C  CA    . GLU A 1 4599 ? 186.703 166.951 119.728 1.00 127.19 ? 4599 GLU A CA    1 
ATOM   22563 C  C     . GLU A 1 4599 ? 187.701 166.348 120.722 1.00 127.35 ? 4599 GLU A C     1 
ATOM   22564 O  O     . GLU A 1 4599 ? 188.446 167.092 121.377 1.00 132.14 ? 4599 GLU A O     1 
ATOM   22565 C  CB    . GLU A 1 4599 ? 186.244 166.015 118.627 1.00 126.00 ? 4599 GLU A CB    1 
ATOM   22566 C  CG    . GLU A 1 4599 ? 185.467 166.696 117.513 1.00 128.80 ? 4599 GLU A CG    1 
ATOM   22567 C  CD    . GLU A 1 4599 ? 185.601 165.974 116.187 1.00 130.27 ? 4599 GLU A CD    1 
ATOM   22568 O  OE1   . GLU A 1 4599 ? 185.425 164.738 116.162 1.00 132.37 ? 4599 GLU A OE1   1 
ATOM   22569 O  OE2   . GLU A 1 4599 ? 185.886 166.643 115.171 1.00 125.83 ? 4599 GLU A OE2   1 
ATOM   22570 N  N     . LYS A 1 4600 ? 187.742 165.026 120.863 1.00 120.22 ? 4600 LYS A N     1 
ATOM   22571 C  CA    . LYS A 1 4600 ? 188.734 164.375 121.703 1.00 114.24 ? 4600 LYS A CA    1 
ATOM   22572 C  C     . LYS A 1 4600 ? 189.119 163.050 121.063 1.00 108.41 ? 4600 LYS A C     1 
ATOM   22573 O  O     . LYS A 1 4600 ? 188.351 162.473 120.288 1.00 106.20 ? 4600 LYS A O     1 
ATOM   22574 C  CB    . LYS A 1 4600 ? 188.220 164.150 123.132 1.00 104.10 ? 4600 LYS A CB    1 
ATOM   22575 C  CG    . LYS A 1 4600 ? 187.367 162.904 123.301 1.00 102.51 ? 4600 LYS A CG    1 
ATOM   22576 C  CD    . LYS A 1 4600 ? 187.104 162.607 124.769 1.00 90.78  ? 4600 LYS A CD    1 
ATOM   22577 C  CE    . LYS A 1 4600 ? 186.506 161.221 124.951 1.00 80.93  ? 4600 LYS A CE    1 
ATOM   22578 N  NZ    . LYS A 1 4600 ? 186.230 160.919 126.383 1.00 69.12  ? 4600 LYS A NZ    1 
ATOM   22579 N  N     . LYS A 1 4601 ? 190.320 162.581 121.385 1.00 100.24 ? 4601 LYS A N     1 
ATOM   22580 C  CA    . LYS A 1 4601 ? 190.783 161.307 120.861 1.00 95.24  ? 4601 LYS A CA    1 
ATOM   22581 C  C     . LYS A 1 4601 ? 189.989 160.159 121.472 1.00 85.75  ? 4601 LYS A C     1 
ATOM   22582 O  O     . LYS A 1 4601 ? 189.474 160.254 122.589 1.00 81.11  ? 4601 LYS A O     1 
ATOM   22583 C  CB    . LYS A 1 4601 ? 192.275 161.123 121.141 1.00 89.87  ? 4601 LYS A CB    1 
ATOM   22584 C  CG    . LYS A 1 4601 ? 193.142 162.273 120.657 1.00 90.08  ? 4601 LYS A CG    1 
ATOM   22585 C  CD    . LYS A 1 4601 ? 194.618 161.978 120.863 1.00 88.01  ? 4601 LYS A CD    1 
ATOM   22586 C  CE    . LYS A 1 4601 ? 195.004 160.644 120.246 1.00 87.78  ? 4601 LYS A CE    1 
ATOM   22587 N  NZ    . LYS A 1 4601 ? 196.352 160.694 119.616 1.00 91.64  ? 4601 LYS A NZ    1 
ATOM   22588 N  N     . ALA A 1 4602 ? 189.886 159.063 120.717 1.00 81.98  ? 4602 ALA A N     1 
ATOM   22589 C  CA    . ALA A 1 4602 ? 189.164 157.895 121.210 1.00 78.87  ? 4602 ALA A CA    1 
ATOM   22590 C  C     . ALA A 1 4602 ? 189.859 157.270 122.412 1.00 79.70  ? 4602 ALA A C     1 
ATOM   22591 O  O     . ALA A 1 4602 ? 189.212 156.599 123.224 1.00 78.29  ? 4602 ALA A O     1 
ATOM   22592 C  CB    . ALA A 1 4602 ? 189.004 156.865 120.091 1.00 71.93  ? 4602 ALA A CB    1 
ATOM   22593 N  N     . SER A 1 4603 ? 191.168 157.480 122.546 1.00 76.06  ? 4603 SER A N     1 
ATOM   22594 C  CA    . SER A 1 4603 ? 191.944 156.931 123.648 1.00 73.25  ? 4603 SER A CA    1 
ATOM   22595 C  C     . SER A 1 4603 ? 192.100 157.912 124.802 1.00 71.90  ? 4603 SER A C     1 
ATOM   22596 O  O     . SER A 1 4603 ? 192.944 157.695 125.676 1.00 75.14  ? 4603 SER A O     1 
ATOM   22597 C  CB    . SER A 1 4603 ? 193.321 156.485 123.152 1.00 70.90  ? 4603 SER A CB    1 
ATOM   22598 O  OG    . SER A 1 4603 ? 194.243 157.560 123.171 1.00 73.21  ? 4603 SER A OG    1 
ATOM   22599 N  N     . VAL A 1 4604 ? 191.315 158.985 124.823 1.00 66.83  ? 4604 VAL A N     1 
ATOM   22600 C  CA    . VAL A 1 4604 ? 191.362 159.980 125.888 1.00 61.28  ? 4604 VAL A CA    1 
ATOM   22601 C  C     . VAL A 1 4604 ? 190.202 159.723 126.838 1.00 58.13  ? 4604 VAL A C     1 
ATOM   22602 O  O     . VAL A 1 4604 ? 189.042 159.661 126.412 1.00 66.13  ? 4604 VAL A O     1 
ATOM   22603 C  CB    . VAL A 1 4604 ? 191.305 161.409 125.320 1.00 71.05  ? 4604 VAL A CB    1 
ATOM   22604 C  CG1   . VAL A 1 4604 ? 190.837 162.391 126.386 1.00 64.95  ? 4604 VAL A CG1   1 
ATOM   22605 C  CG2   . VAL A 1 4604 ? 192.661 161.817 124.773 1.00 70.76  ? 4604 VAL A CG2   1 
ATOM   22606 N  N     . VAL A 1 4605 ? 190.512 159.571 128.123 1.00 54.16  ? 4605 VAL A N     1 
ATOM   22607 C  CA    . VAL A 1 4605 ? 189.513 159.318 129.154 1.00 49.60  ? 4605 VAL A CA    1 
ATOM   22608 C  C     . VAL A 1 4605 ? 189.450 160.529 130.074 1.00 48.46  ? 4605 VAL A C     1 
ATOM   22609 O  O     . VAL A 1 4605 ? 190.473 161.165 130.357 1.00 49.32  ? 4605 VAL A O     1 
ATOM   22610 C  CB    . VAL A 1 4605 ? 189.821 158.026 129.940 1.00 44.04  ? 4605 VAL A CB    1 
ATOM   22611 C  CG1   . VAL A 1 4605 ? 190.986 158.227 130.900 1.00 44.60  ? 4605 VAL A CG1   1 
ATOM   22612 C  CG2   . VAL A 1 4605 ? 188.585 157.549 130.685 1.00 46.06  ? 4605 VAL A CG2   1 
ATOM   22613 N  N     . THR A 1 4606 ? 188.241 160.871 130.508 1.00 43.88  ? 4606 THR A N     1 
ATOM   22614 C  CA    . THR A 1 4606 ? 188.021 161.979 131.427 1.00 38.75  ? 4606 THR A CA    1 
ATOM   22615 C  C     . THR A 1 4606 ? 187.803 161.418 132.827 1.00 41.92  ? 4606 THR A C     1 
ATOM   22616 O  O     . THR A 1 4606 ? 186.847 160.671 133.058 1.00 45.75  ? 4606 THR A O     1 
ATOM   22617 C  CB    . THR A 1 4606 ? 186.826 162.827 130.993 1.00 36.64  ? 4606 THR A CB    1 
ATOM   22618 O  OG1   . THR A 1 4606 ? 187.097 163.415 129.715 1.00 43.75  ? 4606 THR A OG1   1 
ATOM   22619 C  CG2   . THR A 1 4606 ? 186.565 163.932 132.004 1.00 36.52  ? 4606 THR A CG2   1 
ATOM   22620 N  N     . LEU A 1 4607 ? 188.687 161.781 133.754 1.00 35.62  ? 4607 LEU A N     1 
ATOM   22621 C  CA    . LEU A 1 4607 ? 188.648 161.254 135.106 1.00 29.74  ? 4607 LEU A CA    1 
ATOM   22622 C  C     . LEU A 1 4607 ? 188.206 162.326 136.085 1.00 33.02  ? 4607 LEU A C     1 
ATOM   22623 O  O     . LEU A 1 4607 ? 188.778 163.424 136.092 1.00 41.29  ? 4607 LEU A O     1 
ATOM   22624 C  CB    . LEU A 1 4607 ? 190.022 160.720 135.518 1.00 26.39  ? 4607 LEU A CB    1 
ATOM   22625 C  CG    . LEU A 1 4607 ? 190.484 159.402 134.901 1.00 29.78  ? 4607 LEU A CG    1 
ATOM   22626 C  CD1   . LEU A 1 4607 ? 191.594 158.813 135.747 1.00 39.35  ? 4607 LEU A CD1   1 
ATOM   22627 C  CD2   . LEU A 1 4607 ? 189.326 158.427 134.775 1.00 30.57  ? 4607 LEU A CD2   1 
ATOM   22628 N  N     . PRO A 1 4608 ? 187.201 162.057 136.912 1.00 28.57  ? 4608 PRO A N     1 
ATOM   22629 C  CA    . PRO A 1 4608 ? 186.850 163.005 137.971 1.00 26.35  ? 4608 PRO A CA    1 
ATOM   22630 C  C     . PRO A 1 4608 ? 187.975 163.137 138.983 1.00 27.26  ? 4608 PRO A C     1 
ATOM   22631 O  O     . PRO A 1 4608 ? 188.704 162.184 139.267 1.00 34.60  ? 4608 PRO A O     1 
ATOM   22632 C  CB    . PRO A 1 4608 ? 185.603 162.383 138.608 1.00 22.13  ? 4608 PRO A CB    1 
ATOM   22633 C  CG    . PRO A 1 4608 ? 185.703 160.931 138.295 1.00 23.01  ? 4608 PRO A CG    1 
ATOM   22634 C  CD    . PRO A 1 4608 ? 186.384 160.833 136.963 1.00 26.74  ? 4608 PRO A CD    1 
ATOM   22635 N  N     . VAL A 1 4609 ? 188.111 164.337 139.529 1.00 25.94  ? 4609 VAL A N     1 
ATOM   22636 C  CA    . VAL A 1 4609 ? 189.101 164.623 140.564 1.00 25.76  ? 4609 VAL A CA    1 
ATOM   22637 C  C     . VAL A 1 4609 ? 188.319 164.963 141.826 1.00 26.96  ? 4609 VAL A C     1 
ATOM   22638 O  O     . VAL A 1 4609 ? 187.931 166.112 142.054 1.00 31.78  ? 4609 VAL A O     1 
ATOM   22639 C  CB    . VAL A 1 4609 ? 190.058 165.750 140.172 1.00 27.02  ? 4609 VAL A CB    1 
ATOM   22640 C  CG1   . VAL A 1 4609 ? 191.100 165.958 141.260 1.00 27.01  ? 4609 VAL A CG1   1 
ATOM   22641 C  CG2   . VAL A 1 4609 ? 190.724 165.435 138.847 1.00 27.80  ? 4609 VAL A CG2   1 
ATOM   22642 N  N     . TYR A 1 4610 ? 188.078 163.955 142.659 1.00 26.84  ? 4610 TYR A N     1 
ATOM   22643 C  CA    . TYR A 1 4610 ? 187.350 164.165 143.896 1.00 28.14  ? 4610 TYR A CA    1 
ATOM   22644 C  C     . TYR A 1 4610 ? 188.291 164.639 144.998 1.00 33.22  ? 4610 TYR A C     1 
ATOM   22645 O  O     . TYR A 1 4610 ? 189.507 164.437 144.949 1.00 36.08  ? 4610 TYR A O     1 
ATOM   22646 C  CB    . TYR A 1 4610 ? 186.634 162.885 144.324 1.00 27.19  ? 4610 TYR A CB    1 
ATOM   22647 C  CG    . TYR A 1 4610 ? 185.556 162.445 143.361 1.00 26.89  ? 4610 TYR A CG    1 
ATOM   22648 C  CD1   . TYR A 1 4610 ? 184.380 163.169 143.228 1.00 26.58  ? 4610 TYR A CD1   1 
ATOM   22649 C  CD2   . TYR A 1 4610 ? 185.716 161.308 142.583 1.00 25.69  ? 4610 TYR A CD2   1 
ATOM   22650 C  CE1   . TYR A 1 4610 ? 183.392 162.773 142.350 1.00 25.83  ? 4610 TYR A CE1   1 
ATOM   22651 C  CE2   . TYR A 1 4610 ? 184.732 160.903 141.703 1.00 31.47  ? 4610 TYR A CE2   1 
ATOM   22652 C  CZ    . TYR A 1 4610 ? 183.573 161.640 141.589 1.00 31.09  ? 4610 TYR A CZ    1 
ATOM   22653 O  OH    . TYR A 1 4610 ? 182.591 161.240 140.713 1.00 31.64  ? 4610 TYR A OH    1 
ATOM   22654 N  N     . LEU A 1 4611 ? 187.705 165.287 146.004 1.00 35.46  ? 4611 LEU A N     1 
ATOM   22655 C  CA    . LEU A 1 4611 ? 188.502 165.861 147.082 1.00 34.04  ? 4611 LEU A CA    1 
ATOM   22656 C  C     . LEU A 1 4611 ? 189.028 164.782 148.021 1.00 38.84  ? 4611 LEU A C     1 
ATOM   22657 O  O     . LEU A 1 4611 ? 190.189 164.824 148.442 1.00 49.82  ? 4611 LEU A O     1 
ATOM   22658 C  CB    . LEU A 1 4611 ? 187.669 166.888 147.846 1.00 36.45  ? 4611 LEU A CB    1 
ATOM   22659 C  CG    . LEU A 1 4611 ? 188.384 167.690 148.929 1.00 39.18  ? 4611 LEU A CG    1 
ATOM   22660 C  CD1   . LEU A 1 4611 ? 189.662 168.302 148.387 1.00 49.18  ? 4611 LEU A CD1   1 
ATOM   22661 C  CD2   . LEU A 1 4611 ? 187.455 168.765 149.438 1.00 46.05  ? 4611 LEU A CD2   1 
ATOM   22662 N  N     . ASN A 1 4612 ? 188.190 163.805 148.358 1.00 36.16  ? 4612 ASN A N     1 
ATOM   22663 C  CA    . ASN A 1 4612 ? 188.547 162.775 149.324 1.00 34.86  ? 4612 ASN A CA    1 
ATOM   22664 C  C     . ASN A 1 4612 ? 187.913 161.457 148.891 1.00 40.63  ? 4612 ASN A C     1 
ATOM   22665 O  O     . ASN A 1 4612 ? 187.261 161.371 147.846 1.00 41.40  ? 4612 ASN A O     1 
ATOM   22666 C  CB    . ASN A 1 4612 ? 188.145 163.217 150.739 1.00 34.04  ? 4612 ASN A CB    1 
ATOM   22667 C  CG    . ASN A 1 4612 ? 186.644 163.402 150.899 1.00 44.18  ? 4612 ASN A CG    1 
ATOM   22668 O  OD1   . ASN A 1 4612 ? 185.860 163.092 150.002 1.00 52.28  ? 4612 ASN A OD1   1 
ATOM   22669 N  ND2   . ASN A 1 4612 ? 186.239 163.923 152.049 1.00 48.67  ? 4612 ASN A ND2   1 
ATOM   22670 N  N     . PHE A 1 4613 ? 188.106 160.417 149.709 1.00 39.14  ? 4613 PHE A N     1 
ATOM   22671 C  CA    . PHE A 1 4613 ? 187.640 159.083 149.347 1.00 35.13  ? 4613 PHE A CA    1 
ATOM   22672 C  C     . PHE A 1 4613 ? 186.122 158.971 149.342 1.00 36.21  ? 4613 PHE A C     1 
ATOM   22673 O  O     . PHE A 1 4613 ? 185.587 158.047 148.720 1.00 45.98  ? 4613 PHE A O     1 
ATOM   22674 C  CB    . PHE A 1 4613 ? 188.246 158.041 150.292 1.00 38.06  ? 4613 PHE A CB    1 
ATOM   22675 C  CG    . PHE A 1 4613 ? 187.698 158.089 151.692 1.00 46.73  ? 4613 PHE A CG    1 
ATOM   22676 C  CD1   . PHE A 1 4613 ? 188.290 158.892 152.652 1.00 49.67  ? 4613 PHE A CD1   1 
ATOM   22677 C  CD2   . PHE A 1 4613 ? 186.611 157.309 152.057 1.00 48.42  ? 4613 PHE A CD2   1 
ATOM   22678 C  CE1   . PHE A 1 4613 ? 187.796 158.935 153.942 1.00 53.06  ? 4613 PHE A CE1   1 
ATOM   22679 C  CE2   . PHE A 1 4613 ? 186.113 157.348 153.346 1.00 50.41  ? 4613 PHE A CE2   1 
ATOM   22680 C  CZ    . PHE A 1 4613 ? 186.708 158.161 154.289 1.00 54.94  ? 4613 PHE A CZ    1 
ATOM   22681 N  N     . THR A 1 4614 ? 185.416 159.880 150.017 1.00 33.77  ? 4614 THR A N     1 
ATOM   22682 C  CA    . THR A 1 4614 ? 183.959 159.835 150.015 1.00 34.30  ? 4614 THR A CA    1 
ATOM   22683 C  C     . THR A 1 4614 ? 183.373 160.182 148.654 1.00 39.10  ? 4614 THR A C     1 
ATOM   22684 O  O     . THR A 1 4614 ? 182.211 159.851 148.393 1.00 43.99  ? 4614 THR A O     1 
ATOM   22685 C  CB    . THR A 1 4614 ? 183.394 160.782 151.075 1.00 40.04  ? 4614 THR A CB    1 
ATOM   22686 O  OG1   . THR A 1 4614 ? 183.806 162.123 150.789 1.00 48.69  ? 4614 THR A OG1   1 
ATOM   22687 C  CG2   . THR A 1 4614 ? 183.890 160.389 152.457 1.00 48.72  ? 4614 THR A CG2   1 
ATOM   22688 N  N     . ARG A 1 4615 ? 184.147 160.843 147.790 1.00 36.24  ? 4615 ARG A N     1 
ATOM   22689 C  CA    . ARG A 1 4615 ? 183.714 161.211 146.441 1.00 31.24  ? 4615 ARG A CA    1 
ATOM   22690 C  C     . ARG A 1 4615 ? 182.446 162.059 146.461 1.00 34.35  ? 4615 ARG A C     1 
ATOM   22691 O  O     . ARG A 1 4615 ? 181.612 161.969 145.558 1.00 39.74  ? 4615 ARG A O     1 
ATOM   22692 C  CB    . ARG A 1 4615 ? 183.516 159.973 145.562 1.00 23.28  ? 4615 ARG A CB    1 
ATOM   22693 C  CG    . ARG A 1 4615 ? 184.741 159.082 145.467 1.00 22.57  ? 4615 ARG A CG    1 
ATOM   22694 C  CD    . ARG A 1 4615 ? 184.726 158.259 144.192 1.00 19.70  ? 4615 ARG A CD    1 
ATOM   22695 N  NE    . ARG A 1 4615 ? 185.800 157.274 144.164 1.00 21.97  ? 4615 ARG A NE    1 
ATOM   22696 C  CZ    . ARG A 1 4615 ? 186.118 156.544 143.105 1.00 23.24  ? 4615 ARG A CZ    1 
ATOM   22697 N  NH1   . ARG A 1 4615 ? 185.463 156.662 141.962 1.00 18.57  ? 4615 ARG A NH1   1 
ATOM   22698 N  NH2   . ARG A 1 4615 ? 187.119 155.672 143.194 1.00 24.67  ? 4615 ARG A NH2   1 
ATOM   22699 N  N     . ALA A 1 4616 ? 182.292 162.890 147.490 1.00 33.10  ? 4616 ALA A N     1 
ATOM   22700 C  CA    . ALA A 1 4616 ? 181.137 163.772 147.588 1.00 38.80  ? 4616 ALA A CA    1 
ATOM   22701 C  C     . ALA A 1 4616 ? 181.386 165.136 146.965 1.00 48.06  ? 4616 ALA A C     1 
ATOM   22702 O  O     . ALA A 1 4616 ? 180.434 165.788 146.518 1.00 50.73  ? 4616 ALA A O     1 
ATOM   22703 C  CB    . ALA A 1 4616 ? 180.727 163.947 149.053 1.00 38.97  ? 4616 ALA A CB    1 
ATOM   22704 N  N     . ASP A 1 4617 ? 182.637 165.582 146.923 1.00 52.74  ? 4617 ASP A N     1 
ATOM   22705 C  CA    . ASP A 1 4617 ? 183.001 166.878 146.368 1.00 49.52  ? 4617 ASP A CA    1 
ATOM   22706 C  C     . ASP A 1 4617 ? 183.876 166.675 145.140 1.00 42.65  ? 4617 ASP A C     1 
ATOM   22707 O  O     . ASP A 1 4617 ? 184.908 166.001 145.212 1.00 47.64  ? 4617 ASP A O     1 
ATOM   22708 C  CB    . ASP A 1 4617 ? 183.734 167.730 147.406 1.00 58.20  ? 4617 ASP A CB    1 
ATOM   22709 C  CG    . ASP A 1 4617 ? 182.834 168.163 148.546 1.00 66.14  ? 4617 ASP A CG    1 
ATOM   22710 O  OD1   . ASP A 1 4617 ? 181.616 168.320 148.316 1.00 67.33  ? 4617 ASP A OD1   1 
ATOM   22711 O  OD2   . ASP A 1 4617 ? 183.342 168.344 149.672 1.00 58.51  ? 4617 ASP A OD2   1 
ATOM   22712 N  N     . LEU A 1 4618 ? 183.464 167.260 144.019 1.00 37.14  ? 4618 LEU A N     1 
ATOM   22713 C  CA    . LEU A 1 4618 ? 184.214 167.189 142.773 1.00 34.84  ? 4618 LEU A CA    1 
ATOM   22714 C  C     . LEU A 1 4618 ? 184.930 168.512 142.539 1.00 38.28  ? 4618 LEU A C     1 
ATOM   22715 O  O     . LEU A 1 4618 ? 184.297 169.573 142.532 1.00 42.07  ? 4618 LEU A O     1 
ATOM   22716 C  CB    . LEU A 1 4618 ? 183.292 166.870 141.596 1.00 31.25  ? 4618 LEU A CB    1 
ATOM   22717 C  CG    . LEU A 1 4618 ? 183.918 166.974 140.205 1.00 32.12  ? 4618 LEU A CG    1 
ATOM   22718 C  CD1   . LEU A 1 4618 ? 184.664 165.699 139.855 1.00 28.74  ? 4618 LEU A CD1   1 
ATOM   22719 C  CD2   . LEU A 1 4618 ? 182.857 167.282 139.161 1.00 37.22  ? 4618 LEU A CD2   1 
ATOM   22720 N  N     . ILE A 1 4619 ? 186.246 168.445 142.349 1.00 37.21  ? 4619 ILE A N     1 
ATOM   22721 C  CA    . ILE A 1 4619 ? 187.051 169.647 142.164 1.00 36.94  ? 4619 ILE A CA    1 
ATOM   22722 C  C     . ILE A 1 4619 ? 187.083 170.017 140.687 1.00 37.97  ? 4619 ILE A C     1 
ATOM   22723 O  O     . ILE A 1 4619 ? 186.614 171.091 140.297 1.00 44.65  ? 4619 ILE A O     1 
ATOM   22724 C  CB    . ILE A 1 4619 ? 188.474 169.455 142.719 1.00 35.56  ? 4619 ILE A CB    1 
ATOM   22725 C  CG1   . ILE A 1 4619 ? 188.421 168.803 144.101 1.00 32.32  ? 4619 ILE A CG1   1 
ATOM   22726 C  CG2   . ILE A 1 4619 ? 189.198 170.788 142.795 1.00 41.00  ? 4619 ILE A CG2   1 
ATOM   22727 C  CD1   . ILE A 1 4619 ? 187.639 169.599 145.124 1.00 33.77  ? 4619 ILE A CD1   1 
ATOM   22728 N  N     . PHE A 1 4620 ? 187.626 169.133 139.857 1.00 32.39  ? 4620 PHE A N     1 
ATOM   22729 C  CA    . PHE A 1 4620 ? 187.712 169.376 138.421 1.00 34.76  ? 4620 PHE A CA    1 
ATOM   22730 C  C     . PHE A 1 4620 ? 187.849 168.030 137.718 1.00 35.83  ? 4620 PHE A C     1 
ATOM   22731 O  O     . PHE A 1 4620 ? 187.698 166.971 138.336 1.00 41.01  ? 4620 PHE A O     1 
ATOM   22732 C  CB    . PHE A 1 4620 ? 188.865 170.333 138.090 1.00 33.67  ? 4620 PHE A CB    1 
ATOM   22733 C  CG    . PHE A 1 4620 ? 190.228 169.801 138.441 1.00 34.91  ? 4620 PHE A CG    1 
ATOM   22734 C  CD1   . PHE A 1 4620 ? 190.653 169.749 139.759 1.00 34.16  ? 4620 PHE A CD1   1 
ATOM   22735 C  CD2   . PHE A 1 4620 ? 191.093 169.372 137.450 1.00 38.20  ? 4620 PHE A CD2   1 
ATOM   22736 C  CE1   . PHE A 1 4620 ? 191.907 169.268 140.081 1.00 36.81  ? 4620 PHE A CE1   1 
ATOM   22737 C  CE2   . PHE A 1 4620 ? 192.349 168.892 137.768 1.00 35.93  ? 4620 PHE A CE2   1 
ATOM   22738 C  CZ    . PHE A 1 4620 ? 192.755 168.839 139.084 1.00 33.97  ? 4620 PHE A CZ    1 
ATOM   22739 N  N     . THR A 1 4621 ? 188.123 168.070 136.416 1.00 32.48  ? 4621 THR A N     1 
ATOM   22740 C  CA    . THR A 1 4621 ? 188.234 166.871 135.599 1.00 33.06  ? 4621 THR A CA    1 
ATOM   22741 C  C     . THR A 1 4621 ? 189.544 166.895 134.827 1.00 39.96  ? 4621 THR A C     1 
ATOM   22742 O  O     . THR A 1 4621 ? 189.993 167.955 134.381 1.00 49.15  ? 4621 THR A O     1 
ATOM   22743 C  CB    . THR A 1 4621 ? 187.062 166.748 134.618 1.00 39.65  ? 4621 THR A CB    1 
ATOM   22744 O  OG1   . THR A 1 4621 ? 187.070 167.864 133.720 1.00 57.32  ? 4621 THR A OG1   1 
ATOM   22745 C  CG2   . THR A 1 4621 ? 185.740 166.721 135.366 1.00 33.65  ? 4621 THR A CG2   1 
ATOM   22746 N  N     . VAL A 1 4622 ? 190.151 165.722 134.670 1.00 35.49  ? 4622 VAL A N     1 
ATOM   22747 C  CA    . VAL A 1 4622 ? 191.399 165.572 133.934 1.00 35.85  ? 4622 VAL A CA    1 
ATOM   22748 C  C     . VAL A 1 4622 ? 191.162 164.660 132.740 1.00 40.29  ? 4622 VAL A C     1 
ATOM   22749 O  O     . VAL A 1 4622 ? 190.388 163.699 132.807 1.00 43.88  ? 4622 VAL A O     1 
ATOM   22750 C  CB    . VAL A 1 4622 ? 192.537 165.025 134.824 1.00 41.46  ? 4622 VAL A CB    1 
ATOM   22751 C  CG1   . VAL A 1 4622 ? 192.835 165.989 135.951 1.00 40.65  ? 4622 VAL A CG1   1 
ATOM   22752 C  CG2   . VAL A 1 4622 ? 192.173 163.661 135.384 1.00 47.47  ? 4622 VAL A CG2   1 
ATOM   22753 N  N     . ASP A 1 4623 ? 191.829 164.975 131.635 1.00 44.15  ? 4623 ASP A N     1 
ATOM   22754 C  CA    . ASP A 1 4623 ? 191.743 164.198 130.402 1.00 46.13  ? 4623 ASP A CA    1 
ATOM   22755 C  C     . ASP A 1 4623 ? 193.052 163.431 130.242 1.00 45.28  ? 4623 ASP A C     1 
ATOM   22756 O  O     . ASP A 1 4623 ? 194.094 164.018 129.940 1.00 50.93  ? 4623 ASP A O     1 
ATOM   22757 C  CB    . ASP A 1 4623 ? 191.472 165.101 129.203 1.00 51.47  ? 4623 ASP A CB    1 
ATOM   22758 C  CG    . ASP A 1 4623 ? 190.081 165.703 129.231 1.00 59.68  ? 4623 ASP A CG    1 
ATOM   22759 O  OD1   . ASP A 1 4623 ? 189.167 165.064 129.791 1.00 63.21  ? 4623 ASP A OD1   1 
ATOM   22760 O  OD2   . ASP A 1 4623 ? 189.902 166.816 128.694 1.00 65.79  ? 4623 ASP A OD2   1 
ATOM   22761 N  N     . PHE A 1 4624 ? 192.991 162.120 130.446 1.00 45.82  ? 4624 PHE A N     1 
ATOM   22762 C  CA    . PHE A 1 4624 ? 194.155 161.253 130.361 1.00 47.63  ? 4624 PHE A CA    1 
ATOM   22763 C  C     . PHE A 1 4624 ? 194.062 160.358 129.132 1.00 54.25  ? 4624 PHE A C     1 
ATOM   22764 O  O     . PHE A 1 4624 ? 192.975 159.947 128.721 1.00 64.81  ? 4624 PHE A O     1 
ATOM   22765 C  CB    . PHE A 1 4624 ? 194.283 160.392 131.618 1.00 47.74  ? 4624 PHE A CB    1 
ATOM   22766 C  CG    . PHE A 1 4624 ? 195.135 161.003 132.691 1.00 51.08  ? 4624 PHE A CG    1 
ATOM   22767 C  CD1   . PHE A 1 4624 ? 196.505 161.120 132.525 1.00 55.28  ? 4624 PHE A CD1   1 
ATOM   22768 C  CD2   . PHE A 1 4624 ? 194.568 161.454 133.871 1.00 45.53  ? 4624 PHE A CD2   1 
ATOM   22769 C  CE1   . PHE A 1 4624 ? 197.292 161.679 133.513 1.00 58.06  ? 4624 PHE A CE1   1 
ATOM   22770 C  CE2   . PHE A 1 4624 ? 195.349 162.014 134.862 1.00 49.27  ? 4624 PHE A CE2   1 
ATOM   22771 C  CZ    . PHE A 1 4624 ? 196.713 162.127 134.683 1.00 56.95  ? 4624 PHE A CZ    1 
ATOM   22772 N  N     . GLU A 1 4625 ? 195.220 160.057 128.550 1.00 53.71  ? 4625 GLU A N     1 
ATOM   22773 C  CA    . GLU A 1 4625 ? 195.313 159.181 127.388 1.00 58.06  ? 4625 GLU A CA    1 
ATOM   22774 C  C     . GLU A 1 4625 ? 195.618 157.769 127.872 1.00 58.67  ? 4625 GLU A C     1 
ATOM   22775 O  O     . GLU A 1 4625 ? 196.730 157.491 128.332 1.00 63.40  ? 4625 GLU A O     1 
ATOM   22776 C  CB    . GLU A 1 4625 ? 196.385 159.669 126.416 1.00 68.37  ? 4625 GLU A CB    1 
ATOM   22777 C  CG    . GLU A 1 4625 ? 196.065 160.991 125.744 1.00 82.59  ? 4625 GLU A CG    1 
ATOM   22778 C  CD    . GLU A 1 4625 ? 197.163 161.445 124.802 1.00 97.79  ? 4625 GLU A CD    1 
ATOM   22779 O  OE1   . GLU A 1 4625 ? 198.226 160.792 124.769 1.00 98.85  ? 4625 GLU A OE1   1 
ATOM   22780 O  OE2   . GLU A 1 4625 ? 196.961 162.454 124.095 1.00 99.98  ? 4625 GLU A OE2   1 
ATOM   22781 N  N     . ILE A 1 4626 ? 194.631 156.879 127.767 1.00 59.97  ? 4626 ILE A N     1 
ATOM   22782 C  CA    . ILE A 1 4626 ? 194.833 155.497 128.180 1.00 59.34  ? 4626 ILE A CA    1 
ATOM   22783 C  C     . ILE A 1 4626 ? 195.755 154.793 127.193 1.00 63.34  ? 4626 ILE A C     1 
ATOM   22784 O  O     . ILE A 1 4626 ? 195.801 155.121 126.000 1.00 63.98  ? 4626 ILE A O     1 
ATOM   22785 C  CB    . ILE A 1 4626 ? 193.488 154.759 128.305 1.00 54.38  ? 4626 ILE A CB    1 
ATOM   22786 C  CG1   . ILE A 1 4626 ? 192.776 154.709 126.953 1.00 63.40  ? 4626 ILE A CG1   1 
ATOM   22787 C  CG2   . ILE A 1 4626 ? 192.608 155.428 129.340 1.00 50.29  ? 4626 ILE A CG2   1 
ATOM   22788 C  CD1   . ILE A 1 4626 ? 191.566 153.807 126.937 1.00 60.32  ? 4626 ILE A CD1   1 
ATOM   22789 N  N     . ALA A 1 4627 ? 196.504 153.817 127.697 1.00 68.23  ? 4627 ALA A N     1 
ATOM   22790 C  CA    . ALA A 1 4627 ? 197.361 153.017 126.841 1.00 75.12  ? 4627 ALA A CA    1 
ATOM   22791 C  C     . ALA A 1 4627 ? 196.516 152.094 125.965 1.00 82.81  ? 4627 ALA A C     1 
ATOM   22792 O  O     . ALA A 1 4627 ? 195.310 151.929 126.166 1.00 84.79  ? 4627 ALA A O     1 
ATOM   22793 C  CB    . ALA A 1 4627 ? 198.349 152.206 127.679 1.00 70.89  ? 4627 ALA A CB    1 
ATOM   22794 N  N     . THR A 1 4628 ? 197.167 151.491 124.974 1.00 86.01  ? 4628 THR A N     1 
ATOM   22795 C  CA    . THR A 1 4628 ? 196.473 150.585 124.074 1.00 86.40  ? 4628 THR A CA    1 
ATOM   22796 C  C     . THR A 1 4628 ? 196.007 149.341 124.829 1.00 88.11  ? 4628 THR A C     1 
ATOM   22797 O  O     . THR A 1 4628 ? 196.448 149.056 125.947 1.00 85.22  ? 4628 THR A O     1 
ATOM   22798 C  CB    . THR A 1 4628 ? 197.374 150.193 122.904 1.00 92.07  ? 4628 THR A CB    1 
ATOM   22799 O  OG1   . THR A 1 4628 ? 198.688 149.890 123.390 1.00 99.24  ? 4628 THR A OG1   1 
ATOM   22800 C  CG2   . THR A 1 4628 ? 197.459 151.329 121.895 1.00 87.03  ? 4628 THR A CG2   1 
ATOM   22801 N  N     . LYS A 1 4629 ? 195.064 148.622 124.210 1.00 85.73  ? 4629 LYS A N     1 
ATOM   22802 C  CA    . LYS A 1 4629 ? 194.485 147.387 124.736 1.00 83.66  ? 4629 LYS A CA    1 
ATOM   22803 C  C     . LYS A 1 4629 ? 193.552 147.699 125.907 1.00 78.80  ? 4629 LYS A C     1 
ATOM   22804 O  O     . LYS A 1 4629 ? 192.842 146.818 126.403 1.00 82.43  ? 4629 LYS A O     1 
ATOM   22805 C  CB    . LYS A 1 4629 ? 195.599 146.399 125.124 1.00 87.92  ? 4629 LYS A CB    1 
ATOM   22806 C  CG    . LYS A 1 4629 ? 195.164 145.098 125.787 1.00 89.24  ? 4629 LYS A CG    1 
ATOM   22807 C  CD    . LYS A 1 4629 ? 196.193 144.001 125.563 1.00 85.31  ? 4629 LYS A CD    1 
ATOM   22808 C  CE    . LYS A 1 4629 ? 195.900 142.780 126.419 1.00 78.28  ? 4629 LYS A CE    1 
ATOM   22809 N  NZ    . LYS A 1 4629 ? 196.418 141.530 125.797 1.00 73.24  ? 4629 LYS A NZ    1 
ATOM   22810 N  N     . GLU A 1 4630 ? 193.505 148.962 126.321 1.00 75.55  ? 4630 GLU A N     1 
ATOM   22811 C  CA    . GLU A 1 4630 ? 192.643 149.404 127.408 1.00 72.62  ? 4630 GLU A CA    1 
ATOM   22812 C  C     . GLU A 1 4630 ? 191.392 150.064 126.844 1.00 69.19  ? 4630 GLU A C     1 
ATOM   22813 O  O     . GLU A 1 4630 ? 191.433 150.693 125.783 1.00 73.47  ? 4630 GLU A O     1 
ATOM   22814 C  CB    . GLU A 1 4630 ? 193.379 150.381 128.329 1.00 72.10  ? 4630 GLU A CB    1 
ATOM   22815 C  CG    . GLU A 1 4630 ? 194.562 149.779 129.081 1.00 77.48  ? 4630 GLU A CG    1 
ATOM   22816 C  CD    . GLU A 1 4630 ? 194.151 148.766 130.137 1.00 76.09  ? 4630 GLU A CD    1 
ATOM   22817 O  OE1   . GLU A 1 4630 ? 192.942 148.651 130.429 1.00 71.21  ? 4630 GLU A OE1   1 
ATOM   22818 O  OE2   . GLU A 1 4630 ? 195.044 148.082 130.679 1.00 67.17  ? 4630 GLU A OE2   1 
ATOM   22819 N  N     . ASP A 1 4631 ? 190.278 149.915 127.561 1.00 63.10  ? 4631 ASP A N     1 
ATOM   22820 C  CA    . ASP A 1 4631 ? 188.993 150.435 127.120 1.00 59.71  ? 4631 ASP A CA    1 
ATOM   22821 C  C     . ASP A 1 4631 ? 188.512 151.534 128.054 1.00 51.31  ? 4631 ASP A C     1 
ATOM   22822 O  O     . ASP A 1 4631 ? 188.529 151.348 129.278 1.00 50.63  ? 4631 ASP A O     1 
ATOM   22823 C  CB    . ASP A 1 4631 ? 187.952 149.312 127.062 1.00 56.73  ? 4631 ASP A CB    1 
ATOM   22824 C  CG    . ASP A 1 4631 ? 186.884 149.560 126.018 1.00 63.05  ? 4631 ASP A CG    1 
ATOM   22825 O  OD1   . ASP A 1 4631 ? 187.211 150.128 124.955 1.00 72.24  ? 4631 ASP A OD1   1 
ATOM   22826 O  OD2   . ASP A 1 4631 ? 185.718 149.187 126.260 1.00 60.67  ? 4631 ASP A OD2   1 
ATOM   22827 N  N     . PRO A 1 4632 ? 188.088 152.684 127.524 1.00 45.98  ? 4632 PRO A N     1 
ATOM   22828 C  CA    . PRO A 1 4632 ? 187.516 153.723 128.398 1.00 44.83  ? 4632 PRO A CA    1 
ATOM   22829 C  C     . PRO A 1 4632 ? 186.254 153.276 129.114 1.00 45.12  ? 4632 PRO A C     1 
ATOM   22830 O  O     . PRO A 1 4632 ? 185.983 153.745 130.228 1.00 46.04  ? 4632 PRO A O     1 
ATOM   22831 C  CB    . PRO A 1 4632 ? 187.240 154.882 127.430 1.00 45.57  ? 4632 PRO A CB    1 
ATOM   22832 C  CG    . PRO A 1 4632 ? 187.127 154.241 126.089 1.00 52.14  ? 4632 PRO A CG    1 
ATOM   22833 C  CD    . PRO A 1 4632 ? 188.067 153.074 126.105 1.00 48.24  ? 4632 PRO A CD    1 
ATOM   22834 N  N     . ARG A 1 4633 ? 185.466 152.389 128.502 1.00 48.25  ? 4633 ARG A N     1 
ATOM   22835 C  CA    . ARG A 1 4633 ? 184.278 151.868 129.171 1.00 41.73  ? 4633 ARG A CA    1 
ATOM   22836 C  C     . ARG A 1 4633 ? 184.656 151.091 130.424 1.00 36.40  ? 4633 ARG A C     1 
ATOM   22837 O  O     . ARG A 1 4633 ? 183.969 151.175 131.449 1.00 36.47  ? 4633 ARG A O     1 
ATOM   22838 C  CB    . ARG A 1 4633 ? 183.480 150.988 128.211 1.00 49.59  ? 4633 ARG A CB    1 
ATOM   22839 C  CG    . ARG A 1 4633 ? 182.685 151.763 127.176 1.00 50.90  ? 4633 ARG A CG    1 
ATOM   22840 C  CD    . ARG A 1 4633 ? 181.718 150.856 126.435 1.00 64.28  ? 4633 ARG A CD    1 
ATOM   22841 N  NE    . ARG A 1 4633 ? 182.242 150.448 125.137 1.00 75.68  ? 4633 ARG A NE    1 
ATOM   22842 C  CZ    . ARG A 1 4633 ? 181.693 149.522 124.363 1.00 78.74  ? 4633 ARG A CZ    1 
ATOM   22843 N  NH1   . ARG A 1 4633 ? 180.594 148.882 124.726 1.00 73.18  ? 4633 ARG A NH1   1 
ATOM   22844 N  NH2   . ARG A 1 4633 ? 182.262 149.230 123.197 1.00 76.82  ? 4633 ARG A NH2   1 
ATOM   22845 N  N     . SER A 1 4634 ? 185.745 150.321 130.358 1.00 39.95  ? 4634 SER A N     1 
ATOM   22846 C  CA    . SER A 1 4634 ? 186.243 149.638 131.546 1.00 37.85  ? 4634 SER A CA    1 
ATOM   22847 C  C     . SER A 1 4634 ? 186.709 150.629 132.604 1.00 35.69  ? 4634 SER A C     1 
ATOM   22848 O  O     . SER A 1 4634 ? 186.547 150.377 133.803 1.00 35.74  ? 4634 SER A O     1 
ATOM   22849 C  CB    . SER A 1 4634 ? 187.376 148.687 131.165 1.00 37.03  ? 4634 SER A CB    1 
ATOM   22850 O  OG    . SER A 1 4634 ? 188.593 149.392 130.998 1.00 42.69  ? 4634 SER A OG    1 
ATOM   22851 N  N     . PHE A 1 4635 ? 187.294 151.754 132.184 1.00 34.07  ? 4635 PHE A N     1 
ATOM   22852 C  CA    . PHE A 1 4635 ? 187.672 152.791 133.139 1.00 30.13  ? 4635 PHE A CA    1 
ATOM   22853 C  C     . PHE A 1 4635 ? 186.447 153.374 133.830 1.00 25.63  ? 4635 PHE A C     1 
ATOM   22854 O  O     . PHE A 1 4635 ? 186.470 153.624 135.041 1.00 26.86  ? 4635 PHE A O     1 
ATOM   22855 C  CB    . PHE A 1 4635 ? 188.463 153.892 132.433 1.00 33.47  ? 4635 PHE A CB    1 
ATOM   22856 C  CG    . PHE A 1 4635 ? 189.937 153.619 132.346 1.00 30.96  ? 4635 PHE A CG    1 
ATOM   22857 C  CD1   . PHE A 1 4635 ? 190.443 152.781 131.369 1.00 34.99  ? 4635 PHE A CD1   1 
ATOM   22858 C  CD2   . PHE A 1 4635 ? 190.816 154.203 133.242 1.00 30.22  ? 4635 PHE A CD2   1 
ATOM   22859 C  CE1   . PHE A 1 4635 ? 191.797 152.528 131.287 1.00 40.71  ? 4635 PHE A CE1   1 
ATOM   22860 C  CE2   . PHE A 1 4635 ? 192.171 153.954 133.164 1.00 36.88  ? 4635 PHE A CE2   1 
ATOM   22861 C  CZ    . PHE A 1 4635 ? 192.662 153.115 132.186 1.00 41.44  ? 4635 PHE A CZ    1 
ATOM   22862 N  N     . TYR A 1 4636 ? 185.371 153.605 133.075 1.00 28.96  ? 4636 TYR A N     1 
ATOM   22863 C  CA    . TYR A 1 4636 ? 184.137 154.104 133.676 1.00 28.50  ? 4636 TYR A CA    1 
ATOM   22864 C  C     . TYR A 1 4636 ? 183.535 153.084 134.635 1.00 27.22  ? 4636 TYR A C     1 
ATOM   22865 O  O     . TYR A 1 4636 ? 183.072 153.444 135.724 1.00 28.25  ? 4636 TYR A O     1 
ATOM   22866 C  CB    . TYR A 1 4636 ? 183.124 154.467 132.589 1.00 28.37  ? 4636 TYR A CB    1 
ATOM   22867 C  CG    . TYR A 1 4636 ? 183.602 155.493 131.585 1.00 32.37  ? 4636 TYR A CG    1 
ATOM   22868 C  CD1   . TYR A 1 4636 ? 184.654 156.351 131.878 1.00 31.49  ? 4636 TYR A CD1   1 
ATOM   22869 C  CD2   . TYR A 1 4636 ? 182.998 155.603 130.340 1.00 36.77  ? 4636 TYR A CD2   1 
ATOM   22870 C  CE1   . TYR A 1 4636 ? 185.088 157.287 130.961 1.00 32.48  ? 4636 TYR A CE1   1 
ATOM   22871 C  CE2   . TYR A 1 4636 ? 183.425 156.536 129.417 1.00 40.09  ? 4636 TYR A CE2   1 
ATOM   22872 C  CZ    . TYR A 1 4636 ? 184.471 157.375 129.733 1.00 40.56  ? 4636 TYR A CZ    1 
ATOM   22873 O  OH    . TYR A 1 4636 ? 184.901 158.306 128.816 1.00 55.80  ? 4636 TYR A OH    1 
ATOM   22874 N  N     . GLU A 1 4637 ? 183.531 151.807 134.246 1.00 26.87  ? 4637 GLU A N     1 
ATOM   22875 C  CA    . GLU A 1 4637 ? 182.883 150.782 135.059 1.00 22.53  ? 4637 GLU A CA    1 
ATOM   22876 C  C     . GLU A 1 4637 ? 183.641 150.530 136.357 1.00 25.30  ? 4637 GLU A C     1 
ATOM   22877 O  O     . GLU A 1 4637 ? 183.028 150.274 137.400 1.00 24.72  ? 4637 GLU A O     1 
ATOM   22878 C  CB    . GLU A 1 4637 ? 182.744 149.489 134.257 1.00 25.97  ? 4637 GLU A CB    1 
ATOM   22879 C  CG    . GLU A 1 4637 ? 181.470 149.411 133.435 1.00 32.20  ? 4637 GLU A CG    1 
ATOM   22880 C  CD    . GLU A 1 4637 ? 181.576 148.431 132.286 1.00 48.37  ? 4637 GLU A CD    1 
ATOM   22881 O  OE1   . GLU A 1 4637 ? 182.560 147.664 132.247 1.00 53.76  ? 4637 GLU A OE1   1 
ATOM   22882 O  OE2   . GLU A 1 4637 ? 180.675 148.427 131.421 1.00 51.90  ? 4637 GLU A OE2   1 
ATOM   22883 N  N     . ARG A 1 4638 ? 184.970 150.597 136.317 1.00 26.42  ? 4638 ARG A N     1 
ATOM   22884 C  CA    . ARG A 1 4638 ? 185.784 150.333 137.496 1.00 22.91  ? 4638 ARG A CA    1 
ATOM   22885 C  C     . ARG A 1 4638 ? 185.845 151.515 138.455 1.00 25.19  ? 4638 ARG A C     1 
ATOM   22886 O  O     . ARG A 1 4638 ? 186.479 151.401 139.509 1.00 31.12  ? 4638 ARG A O     1 
ATOM   22887 C  CB    . ARG A 1 4638 ? 187.200 149.930 137.078 1.00 22.41  ? 4638 ARG A CB    1 
ATOM   22888 C  CG    . ARG A 1 4638 ? 187.272 148.575 136.393 1.00 27.70  ? 4638 ARG A CG    1 
ATOM   22889 C  CD    . ARG A 1 4638 ? 188.692 148.222 135.991 1.00 32.44  ? 4638 ARG A CD    1 
ATOM   22890 N  NE    . ARG A 1 4638 ? 189.583 148.125 137.140 1.00 31.84  ? 4638 ARG A NE    1 
ATOM   22891 C  CZ    . ARG A 1 4638 ? 190.378 147.093 137.383 1.00 36.49  ? 4638 ARG A CZ    1 
ATOM   22892 N  NH1   . ARG A 1 4638 ? 190.414 146.043 136.579 1.00 33.61  ? 4638 ARG A NH1   1 
ATOM   22893 N  NH2   . ARG A 1 4638 ? 191.158 147.114 138.460 1.00 47.53  ? 4638 ARG A NH2   1 
ATOM   22894 N  N     . GLY A 1 4639 ? 185.208 152.633 138.122 1.00 22.79  ? 4639 GLY A N     1 
ATOM   22895 C  CA    . GLY A 1 4639 ? 185.195 153.781 139.016 1.00 22.72  ? 4639 GLY A CA    1 
ATOM   22896 C  C     . GLY A 1 4639 ? 186.549 154.426 139.209 1.00 24.74  ? 4639 GLY A C     1 
ATOM   22897 O  O     . GLY A 1 4639 ? 186.904 154.794 140.336 1.00 28.83  ? 4639 GLY A O     1 
ATOM   22898 N  N     . VAL A 1 4640 ? 187.319 154.570 138.131 1.00 23.22  ? 4640 VAL A N     1 
ATOM   22899 C  CA    . VAL A 1 4640 ? 188.631 155.195 138.225 1.00 24.09  ? 4640 VAL A CA    1 
ATOM   22900 C  C     . VAL A 1 4640 ? 188.462 156.694 138.429 1.00 26.11  ? 4640 VAL A C     1 
ATOM   22901 O  O     . VAL A 1 4640 ? 187.710 157.356 137.703 1.00 27.87  ? 4640 VAL A O     1 
ATOM   22902 C  CB    . VAL A 1 4640 ? 189.462 154.891 136.970 1.00 21.61  ? 4640 VAL A CB    1 
ATOM   22903 C  CG1   . VAL A 1 4640 ? 190.838 155.522 137.078 1.00 23.25  ? 4640 VAL A CG1   1 
ATOM   22904 C  CG2   . VAL A 1 4640 ? 189.576 153.390 136.762 1.00 24.08  ? 4640 VAL A CG2   1 
ATOM   22905 N  N     . ALA A 1 4641 ? 189.160 157.235 139.425 1.00 28.53  ? 4641 ALA A N     1 
ATOM   22906 C  CA    . ALA A 1 4641 ? 189.078 158.653 139.738 1.00 24.15  ? 4641 ALA A CA    1 
ATOM   22907 C  C     . ALA A 1 4641 ? 190.381 159.091 140.390 1.00 30.26  ? 4641 ALA A C     1 
ATOM   22908 O  O     . ALA A 1 4641 ? 191.251 158.275 140.701 1.00 38.36  ? 4641 ALA A O     1 
ATOM   22909 C  CB    . ALA A 1 4641 ? 187.883 158.959 140.647 1.00 20.20  ? 4641 ALA A CB    1 
ATOM   22910 N  N     . VAL A 1 4642 ? 190.506 160.400 140.592 1.00 28.76  ? 4642 VAL A N     1 
ATOM   22911 C  CA    . VAL A 1 4642 ? 191.681 161.004 141.208 1.00 29.09  ? 4642 VAL A CA    1 
ATOM   22912 C  C     . VAL A 1 4642 ? 191.248 161.671 142.505 1.00 28.79  ? 4642 VAL A C     1 
ATOM   22913 O  O     . VAL A 1 4642 ? 190.275 162.432 142.522 1.00 31.89  ? 4642 VAL A O     1 
ATOM   22914 C  CB    . VAL A 1 4642 ? 192.358 162.020 140.269 1.00 26.57  ? 4642 VAL A CB    1 
ATOM   22915 C  CG1   . VAL A 1 4642 ? 193.658 162.520 140.876 1.00 31.31  ? 4642 VAL A CG1   1 
ATOM   22916 C  CG2   . VAL A 1 4642 ? 192.606 161.397 138.905 1.00 25.62  ? 4642 VAL A CG2   1 
ATOM   22917 N  N     . LEU A 1 4643 ? 191.962 161.380 143.588 1.00 30.08  ? 4643 LEU A N     1 
ATOM   22918 C  CA    . LEU A 1 4643 ? 191.661 161.932 144.901 1.00 33.77  ? 4643 LEU A CA    1 
ATOM   22919 C  C     . LEU A 1 4643 ? 192.706 162.975 145.271 1.00 38.84  ? 4643 LEU A C     1 
ATOM   22920 O  O     . LEU A 1 4643 ? 193.909 162.730 145.135 1.00 41.30  ? 4643 LEU A O     1 
ATOM   22921 C  CB    . LEU A 1 4643 ? 191.613 160.832 145.963 1.00 36.77  ? 4643 LEU A CB    1 
ATOM   22922 C  CG    . LEU A 1 4643 ? 190.566 159.737 145.762 1.00 31.85  ? 4643 LEU A CG    1 
ATOM   22923 C  CD1   . LEU A 1 4643 ? 190.463 158.873 147.006 1.00 30.98  ? 4643 LEU A CD1   1 
ATOM   22924 C  CD2   . LEU A 1 4643 ? 189.216 160.337 145.408 1.00 28.19  ? 4643 LEU A CD2   1 
ATOM   22925 N  N     . CYS A 1 4644 ? 192.241 164.137 145.736 1.00 37.21  ? 4644 CYS A N     1 
ATOM   22926 C  CA    . CYS A 1 4644 ? 193.152 165.201 146.137 1.00 40.23  ? 4644 CYS A CA    1 
ATOM   22927 C  C     . CYS A 1 4644 ? 193.932 164.855 147.398 1.00 46.46  ? 4644 CYS A C     1 
ATOM   22928 O  O     . CYS A 1 4644 ? 195.029 165.387 147.597 1.00 50.75  ? 4644 CYS A O     1 
ATOM   22929 C  CB    . CYS A 1 4644 ? 192.379 166.504 146.347 1.00 40.15  ? 4644 CYS A CB    1 
ATOM   22930 S  SG    . CYS A 1 4644 ? 191.796 167.284 144.825 1.00 63.50  ? 4644 CYS A SG    1 
ATOM   22931 N  N     . THR A 1 4645 ? 193.397 163.985 148.248 1.00 49.41  ? 4645 THR A N     1 
ATOM   22932 C  CA    . THR A 1 4645 ? 194.076 163.604 149.480 1.00 52.78  ? 4645 THR A CA    1 
ATOM   22933 C  C     . THR A 1 4645 ? 193.742 162.170 149.876 1.00 52.96  ? 4645 THR A C     1 
ATOM   22934 O  O     . THR A 1 4645 ? 192.851 161.548 149.299 1.00 51.38  ? 4645 THR A O     1 
ATOM   22935 C  CB    . THR A 1 4645 ? 193.708 164.546 150.641 1.00 53.60  ? 4645 THR A CB    1 
ATOM   22936 O  OG1   . THR A 1 4645 ? 194.521 164.243 151.781 1.00 72.30  ? 4645 THR A OG1   1 
ATOM   22937 C  CG2   . THR A 1 4645 ? 192.243 164.385 151.013 1.00 39.01  ? 4645 THR A CG2   1 
HETATM 22938 P  PB    . ADP B 2 .    ? 163.918 176.137 142.167 1.00 17.86  ? 4701 ADP A PB    1 
HETATM 22939 O  O1B   . ADP B 2 .    ? 165.238 175.418 142.057 1.00 17.18  ? 4701 ADP A O1B   1 
HETATM 22940 O  O2B   . ADP B 2 .    ? 162.749 175.275 141.761 1.00 21.32  ? 4701 ADP A O2B   1 
HETATM 22941 O  O3B   . ADP B 2 .    ? 163.720 176.787 143.513 1.00 22.44  ? 4701 ADP A O3B   1 
HETATM 22942 P  PA    . ADP B 2 .    ? 162.852 178.378 140.594 1.00 19.68  ? 4701 ADP A PA    1 
HETATM 22943 O  O1A   . ADP B 2 .    ? 161.792 177.617 139.870 1.00 15.29  ? 4701 ADP A O1A   1 
HETATM 22944 O  O2A   . ADP B 2 .    ? 162.443 179.236 141.745 1.00 21.10  ? 4701 ADP A O2A   1 
HETATM 22945 O  O3A   . ADP B 2 .    ? 163.971 177.344 141.096 1.00 20.86  ? 4701 ADP A O3A   1 
HETATM 22946 O  "O5'" . ADP B 2 .    ? 163.683 179.263 139.546 1.00 19.76  ? 4701 ADP A "O5'" 1 
HETATM 22947 C  "C5'" . ADP B 2 .    ? 164.729 180.130 140.055 1.00 15.56  ? 4701 ADP A "C5'" 1 
HETATM 22948 C  "C4'" . ADP B 2 .    ? 165.031 181.204 139.039 1.00 14.33  ? 4701 ADP A "C4'" 1 
HETATM 22949 O  "O4'" . ADP B 2 .    ? 165.576 180.586 137.843 1.00 17.55  ? 4701 ADP A "O4'" 1 
HETATM 22950 C  "C3'" . ADP B 2 .    ? 163.831 182.032 138.559 1.00 19.50  ? 4701 ADP A "C3'" 1 
HETATM 22951 O  "O3'" . ADP B 2 .    ? 164.214 183.380 138.321 1.00 29.88  ? 4701 ADP A "O3'" 1 
HETATM 22952 C  "C2'" . ADP B 2 .    ? 163.461 181.331 137.250 1.00 17.86  ? 4701 ADP A "C2'" 1 
HETATM 22953 O  "O2'" . ADP B 2 .    ? 162.702 182.134 136.372 1.00 29.85  ? 4701 ADP A "O2'" 1 
HETATM 22954 C  "C1'" . ADP B 2 .    ? 164.855 181.028 136.718 1.00 19.66  ? 4701 ADP A "C1'" 1 
HETATM 22955 N  N9    . ADP B 2 .    ? 164.886 179.976 135.710 1.00 13.43  ? 4701 ADP A N9    1 
HETATM 22956 C  C8    . ADP B 2 .    ? 164.945 178.625 135.943 1.00 11.46  ? 4701 ADP A C8    1 
HETATM 22957 N  N7    . ADP B 2 .    ? 164.964 177.910 134.847 1.00 12.23  ? 4701 ADP A N7    1 
HETATM 22958 C  C5    . ADP B 2 .    ? 164.915 178.847 133.825 1.00 10.88  ? 4701 ADP A C5    1 
HETATM 22959 C  C6    . ADP B 2 .    ? 164.906 178.716 132.423 1.00 11.34  ? 4701 ADP A C6    1 
HETATM 22960 N  N6    . ADP B 2 .    ? 164.949 177.547 131.791 1.00 14.46  ? 4701 ADP A N6    1 
HETATM 22961 N  N1    . ADP B 2 .    ? 164.853 179.853 131.690 1.00 10.77  ? 4701 ADP A N1    1 
HETATM 22962 C  C2    . ADP B 2 .    ? 164.810 181.026 132.335 1.00 12.95  ? 4701 ADP A C2    1 
HETATM 22963 N  N3    . ADP B 2 .    ? 164.813 181.269 133.642 1.00 16.77  ? 4701 ADP A N3    1 
HETATM 22964 C  C4    . ADP B 2 .    ? 164.868 180.126 134.344 1.00 12.52  ? 4701 ADP A C4    1 
HETATM 22965 P  PG    . ATP C 3 .    ? 169.752 197.198 164.904 1.00 20.81  ? 4702 ATP A PG    1 
HETATM 22966 O  O1G   . ATP C 3 .    ? 170.697 196.223 164.249 1.00 21.83  ? 4702 ATP A O1G   1 
HETATM 22967 O  O2G   . ATP C 3 .    ? 168.330 197.045 164.427 1.00 21.82  ? 4702 ATP A O2G   1 
HETATM 22968 O  O3G   . ATP C 3 .    ? 169.866 197.198 166.408 1.00 23.52  ? 4702 ATP A O3G   1 
HETATM 22969 P  PB    . ATP C 3 .    ? 170.506 199.296 162.982 1.00 17.26  ? 4702 ATP A PB    1 
HETATM 22970 O  O1B   . ATP C 3 .    ? 171.782 198.727 162.458 1.00 19.10  ? 4702 ATP A O1B   1 
HETATM 22971 O  O2B   . ATP C 3 .    ? 169.261 199.195 162.165 1.00 18.29  ? 4702 ATP A O2B   1 
HETATM 22972 O  O3B   . ATP C 3 .    ? 170.221 198.664 164.424 1.00 17.65  ? 4702 ATP A O3B   1 
HETATM 22973 P  PA    . ATP C 3 .    ? 169.678 201.989 163.697 1.00 22.02  ? 4702 ATP A PA    1 
HETATM 22974 O  O1A   . ATP C 3 .    ? 168.519 201.382 164.415 1.00 22.04  ? 4702 ATP A O1A   1 
HETATM 22975 O  O2A   . ATP C 3 .    ? 169.417 202.763 162.448 1.00 15.15  ? 4702 ATP A O2A   1 
HETATM 22976 O  O3A   . ATP C 3 .    ? 170.736 200.830 163.374 1.00 17.34  ? 4702 ATP A O3A   1 
HETATM 22977 O  "O5'" . ATP C 3 .    ? 170.515 202.895 164.721 1.00 25.47  ? 4702 ATP A "O5'" 1 
HETATM 22978 C  "C5'" . ATP C 3 .    ? 171.609 203.698 164.215 1.00 17.09  ? 4702 ATP A "C5'" 1 
HETATM 22979 C  "C4'" . ATP C 3 .    ? 172.056 204.652 165.293 1.00 17.57  ? 4702 ATP A "C4'" 1 
HETATM 22980 O  "O4'" . ATP C 3 .    ? 172.820 205.724 164.687 1.00 21.80  ? 4702 ATP A "O4'" 1 
HETATM 22981 C  "C3'" . ATP C 3 .    ? 170.934 205.388 166.027 1.00 19.57  ? 4702 ATP A "C3'" 1 
HETATM 22982 O  "O3'" . ATP C 3 .    ? 171.410 205.971 167.231 1.00 29.69  ? 4702 ATP A "O3'" 1 
HETATM 22983 C  "C2'" . ATP C 3 .    ? 170.594 206.456 164.988 1.00 19.48  ? 4702 ATP A "C2'" 1 
HETATM 22984 O  "O2'" . ATP C 3 .    ? 169.875 207.549 165.518 1.00 26.31  ? 4702 ATP A "O2'" 1 
HETATM 22985 C  "C1'" . ATP C 3 .    ? 171.992 206.855 164.518 1.00 19.40  ? 4702 ATP A "C1'" 1 
HETATM 22986 N  N9    . ATP C 3 .    ? 172.046 207.251 163.119 1.00 20.73  ? 4702 ATP A N9    1 
HETATM 22987 C  C8    . ATP C 3 .    ? 171.428 206.648 162.052 1.00 19.79  ? 4702 ATP A C8    1 
HETATM 22988 N  N7    . ATP C 3 .    ? 171.666 207.263 160.917 1.00 18.83  ? 4702 ATP A N7    1 
HETATM 22989 C  C5    . ATP C 3 .    ? 172.471 208.341 161.264 1.00 19.07  ? 4702 ATP A C5    1 
HETATM 22990 C  C6    . ATP C 3 .    ? 173.058 209.374 160.511 1.00 20.07  ? 4702 ATP A C6    1 
HETATM 22991 N  N6    . ATP C 3 .    ? 172.921 209.501 159.194 1.00 18.56  ? 4702 ATP A N6    1 
HETATM 22992 N  N1    . ATP C 3 .    ? 173.804 210.284 161.181 1.00 22.62  ? 4702 ATP A N1    1 
HETATM 22993 C  C2    . ATP C 3 .    ? 173.937 210.154 162.507 1.00 22.36  ? 4702 ATP A C2    1 
HETATM 22994 N  N3    . ATP C 3 .    ? 173.435 209.227 163.317 1.00 23.08  ? 4702 ATP A N3    1 
HETATM 22995 C  C4    . ATP C 3 .    ? 172.704 208.342 162.622 1.00 21.04  ? 4702 ATP A C4    1 
HETATM 22996 P  PB    . ADP D 2 .    ? 170.896 188.889 194.040 1.00 22.75  ? 4703 ADP A PB    1 
HETATM 22997 O  O1B   . ADP D 2 .    ? 170.101 190.032 193.467 1.00 21.41  ? 4703 ADP A O1B   1 
HETATM 22998 O  O2B   . ADP D 2 .    ? 170.211 187.560 193.871 1.00 47.22  ? 4703 ADP A O2B   1 
HETATM 22999 O  O3B   . ADP D 2 .    ? 172.324 188.874 193.558 1.00 22.40  ? 4703 ADP A O3B   1 
HETATM 23000 P  PA    . ADP D 2 .    ? 169.854 189.583 196.699 1.00 30.42  ? 4703 ADP A PA    1 
HETATM 23001 O  O1A   . ADP D 2 .    ? 169.623 191.053 196.590 1.00 23.50  ? 4703 ADP A O1A   1 
HETATM 23002 O  O2A   . ADP D 2 .    ? 168.680 188.674 196.554 1.00 31.68  ? 4703 ADP A O2A   1 
HETATM 23003 O  O3A   . ADP D 2 .    ? 170.966 189.154 195.628 1.00 24.71  ? 4703 ADP A O3A   1 
HETATM 23004 O  "O5'" . ADP D 2 .    ? 170.609 189.260 198.074 1.00 24.59  ? 4703 ADP A "O5'" 1 
HETATM 23005 C  "C5'" . ADP D 2 .    ? 171.889 189.885 198.327 1.00 16.78  ? 4703 ADP A "C5'" 1 
HETATM 23006 C  "C4'" . ADP D 2 .    ? 172.425 189.388 199.646 1.00 17.43  ? 4703 ADP A "C4'" 1 
HETATM 23007 O  "O4'" . ADP D 2 .    ? 173.602 190.162 199.996 1.00 18.37  ? 4703 ADP A "O4'" 1 
HETATM 23008 C  "C3'" . ADP D 2 .    ? 171.480 189.523 200.845 1.00 22.68  ? 4703 ADP A "C3'" 1 
HETATM 23009 O  "O3'" . ADP D 2 .    ? 171.693 188.471 201.775 1.00 33.80  ? 4703 ADP A "O3'" 1 
HETATM 23010 C  "C2'" . ADP D 2 .    ? 171.916 190.863 201.437 1.00 21.30  ? 4703 ADP A "C2'" 1 
HETATM 23011 O  "O2'" . ADP D 2 .    ? 171.538 191.024 202.786 1.00 31.76  ? 4703 ADP A "O2'" 1 
HETATM 23012 C  "C1'" . ADP D 2 .    ? 173.426 190.752 201.262 1.00 18.36  ? 4703 ADP A "C1'" 1 
HETATM 23013 N  N9    . ADP D 2 .    ? 174.118 192.034 201.263 1.00 16.91  ? 4703 ADP A N9    1 
HETATM 23014 C  C8    . ADP D 2 .    ? 175.177 192.381 200.464 1.00 16.26  ? 4703 ADP A C8    1 
HETATM 23015 N  N7    . ADP D 2 .    ? 175.609 193.598 200.672 1.00 17.30  ? 4703 ADP A N7    1 
HETATM 23016 C  C5    . ADP D 2 .    ? 174.789 194.085 201.680 1.00 16.82  ? 4703 ADP A C5    1 
HETATM 23017 C  C6    . ADP D 2 .    ? 174.746 195.325 202.344 1.00 22.20  ? 4703 ADP A C6    1 
HETATM 23018 N  N6    . ADP D 2 .    ? 175.575 196.332 202.083 1.00 23.11  ? 4703 ADP A N6    1 
HETATM 23019 N  N1    . ADP D 2 .    ? 173.804 195.488 203.302 1.00 24.41  ? 4703 ADP A N1    1 
HETATM 23020 C  C2    . ADP D 2 .    ? 172.974 194.470 203.560 1.00 19.12  ? 4703 ADP A C2    1 
HETATM 23021 N  N3    . ADP D 2 .    ? 172.923 193.265 203.001 1.00 15.42  ? 4703 ADP A N3    1 
HETATM 23022 C  C4    . ADP D 2 .    ? 173.866 193.130 202.056 1.00 15.07  ? 4703 ADP A C4    1 
HETATM 23023 P  PB    . ADP E 2 .    ? 159.913 159.375 200.459 1.00 26.73  ? 4704 ADP A PB    1 
HETATM 23024 O  O1B   . ADP E 2 .    ? 161.070 159.333 201.426 1.00 21.97  ? 4704 ADP A O1B   1 
HETATM 23025 O  O2B   . ADP E 2 .    ? 159.115 160.650 200.561 1.00 21.72  ? 4704 ADP A O2B   1 
HETATM 23026 O  O3B   . ADP E 2 .    ? 160.322 159.055 199.044 1.00 31.77  ? 4704 ADP A O3B   1 
HETATM 23027 P  PA    . ADP E 2 .    ? 157.847 158.044 202.096 1.00 24.04  ? 4704 ADP A PA    1 
HETATM 23028 O  O1A   . ADP E 2 .    ? 158.411 158.647 203.339 1.00 18.77  ? 4704 ADP A O1A   1 
HETATM 23029 O  O2A   . ADP E 2 .    ? 156.518 158.523 201.614 1.00 25.19  ? 4704 ADP A O2A   1 
HETATM 23030 O  O3A   . ADP E 2 .    ? 158.915 158.192 200.909 1.00 29.80  ? 4704 ADP A O3A   1 
HETATM 23031 O  "O5'" . ADP E 2 .    ? 157.815 156.450 202.250 1.00 30.06  ? 4704 ADP A "O5'" 1 
HETATM 23032 C  "C5'" . ADP E 2 .    ? 156.968 155.858 203.265 1.00 30.38  ? 4704 ADP A "C5'" 1 
HETATM 23033 C  "C4'" . ADP E 2 .    ? 157.418 154.441 203.510 1.00 23.33  ? 4704 ADP A "C4'" 1 
HETATM 23034 O  "O4'" . ADP E 2 .    ? 158.774 154.472 204.029 1.00 19.93  ? 4704 ADP A "O4'" 1 
HETATM 23035 C  "C3'" . ADP E 2 .    ? 156.606 153.640 204.536 1.00 25.71  ? 4704 ADP A "C3'" 1 
HETATM 23036 O  "O3'" . ADP E 2 .    ? 156.566 152.264 204.185 1.00 30.55  ? 4704 ADP A "O3'" 1 
HETATM 23037 C  "C2'" . ADP E 2 .    ? 157.418 153.853 205.814 1.00 30.60  ? 4704 ADP A "C2'" 1 
HETATM 23038 O  "O2'" . ADP E 2 .    ? 157.174 152.879 206.805 1.00 33.48  ? 4704 ADP A "O2'" 1 
HETATM 23039 C  "C1'" . ADP E 2 .    ? 158.830 153.769 205.248 1.00 23.45  ? 4704 ADP A "C1'" 1 
HETATM 23040 N  N9    . ADP E 2 .    ? 159.838 154.394 206.095 1.00 22.29  ? 4704 ADP A N9    1 
HETATM 23041 C  C8    . ADP E 2 .    ? 160.701 155.399 205.737 1.00 24.78  ? 4704 ADP A C8    1 
HETATM 23042 N  N7    . ADP E 2 .    ? 161.504 155.763 206.705 1.00 25.55  ? 4704 ADP A N7    1 
HETATM 23043 C  C5    . ADP E 2 .    ? 161.159 154.939 207.767 1.00 21.73  ? 4704 ADP A C5    1 
HETATM 23044 C  C6    . ADP E 2 .    ? 161.653 154.832 209.081 1.00 22.69  ? 4704 ADP A C6    1 
HETATM 23045 N  N6    . ADP E 2 .    ? 162.635 155.586 209.566 1.00 21.67  ? 4704 ADP A N6    1 
HETATM 23046 N  N1    . ADP E 2 .    ? 161.086 153.904 209.887 1.00 25.37  ? 4704 ADP A N1    1 
HETATM 23047 C  C2    . ADP E 2 .    ? 160.098 153.147 209.393 1.00 25.04  ? 4704 ADP A C2    1 
HETATM 23048 N  N3    . ADP E 2 .    ? 159.554 153.160 208.180 1.00 22.04  ? 4704 ADP A N3    1 
HETATM 23049 C  C4    . ADP E 2 .    ? 160.134 154.088 207.402 1.00 21.43  ? 4704 ADP A C4    1 
HETATM 23050 MG MG    . MG  F 4 .    ? 160.598 176.101 144.105 1.00 14.85  ? 4705 MG  A MG    1 
HETATM 23051 MG MG    . MG  G 4 .    ? 166.725 198.676 163.272 1.00 13.85  ? 4706 MG  A MG    1 
# 
